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author guerler
date Fri, 22 Jan 2021 15:50:27 +0000
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HEADER    VIRAL PROTEIN                           25-FEB-20   6VYB              
TITLE     SARS-COV-2 SPIKE ECTODOMAIN STRUCTURE (OPEN STATE)                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SPIKE GLYCOPROTEIN;                                        
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: ECTODOMAIN;                                                
COMPND   5 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN;                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 GENE: S, 2;                                                          
SOURCE   7 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   8 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    CORONAVIRUS, SARS-COV-2, SARS-COV, SPIKE GLYCOPROTEIN, FUSION         
KEYWDS   2 PROTEIN, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR 
KEYWDS   3 INFECTIOUS DISEASE, SSGCID, VIRAL PROTEIN                            
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    A.C.WALLS,Y.J.PARK,M.A.TORTORICI,A.WALL,SEATTLE STRUCTURAL GENOMICS   
AUTHOR   2 CENTER FOR INFECTIOUS DISEASE (SSGCID),A.T.MCGUIRE,D.VEESLER         
REVDAT   6   29-JUL-20 6VYB    1       COMPND REMARK HETNAM LINK                
REVDAT   6 2                   1       SITE   ATOM                              
REVDAT   5   06-MAY-20 6VYB    1       COMPND SOURCE DBREF  SEQADV              
REVDAT   4   29-APR-20 6VYB    1       JRNL                                     
REVDAT   3   01-APR-20 6VYB    1       COMPND                                   
REVDAT   2   25-MAR-20 6VYB    1       JRNL                                     
REVDAT   1   11-MAR-20 6VYB    0                                                
JRNL        AUTH   A.C.WALLS,Y.J.PARK,M.A.TORTORICI,A.WALL,A.T.MCGUIRE,         
JRNL        AUTH 2 D.VEESLER                                                    
JRNL        TITL   STRUCTURE, FUNCTION, AND ANTIGENICITY OF THE SARS-COV-2      
JRNL        TITL 2 SPIKE GLYCOPROTEIN.                                          
JRNL        REF    CELL                          V. 181   281 2020              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   32155444                                                     
JRNL        DOI    10.1016/J.CELL.2020.02.058                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : LEGINON, RELION, RELION                   
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.200                          
REMARK   3   NUMBER OF PARTICLES               : 197005                         
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6VYB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000247307.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : SARS-COV-2 PREFUSION SPIKE        
REMARK 245                                    ECTODOMAIN                        
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : UNSPECIFIED                       
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 8.00                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 70.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N, O                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -18                                                      
REMARK 465     GLY A   -17                                                      
REMARK 465     ILE A   -16                                                      
REMARK 465     LEU A   -15                                                      
REMARK 465     PRO A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     PRO A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     MET A   -10                                                      
REMARK 465     PRO A    -9                                                      
REMARK 465     ALA A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     SER A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     VAL A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     LEU A    -1                                                      
REMARK 465     LEU A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     MET A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     CYS A     7                                                      
REMARK 465     VAL A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     GLU A    10                                                      
REMARK 465     THR A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     GLN A    14                                                      
REMARK 465     CYS A    15                                                      
REMARK 465     VAL A    16                                                      
REMARK 465     ASN A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     THR A    19                                                      
REMARK 465     THR A    20                                                      
REMARK 465     ARG A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     GLN A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     VAL A    70                                                      
REMARK 465     SER A    71                                                      
REMARK 465     GLY A    72                                                      
REMARK 465     THR A    73                                                      
REMARK 465     ASN A    74                                                      
REMARK 465     GLY A    75                                                      
REMARK 465     THR A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     ARG A    78                                                      
REMARK 465     PHE A    79                                                      
REMARK 465     ASP A    80                                                      
REMARK 465     ASN A    81                                                      
REMARK 465     THR A   114                                                      
REMARK 465     GLN A   115                                                      
REMARK 465     TYR A   144                                                      
REMARK 465     TYR A   145                                                      
REMARK 465     HIS A   146                                                      
REMARK 465     LYS A   147                                                      
REMARK 465     ASN A   148                                                      
REMARK 465     ASN A   149                                                      
REMARK 465     LYS A   150                                                      
REMARK 465     SER A   151                                                      
REMARK 465     TRP A   152                                                      
REMARK 465     MET A   153                                                      
REMARK 465     GLU A   154                                                      
REMARK 465     SER A   155                                                      
REMARK 465     GLU A   156                                                      
REMARK 465     PHE A   157                                                      
REMARK 465     ARG A   158                                                      
REMARK 465     VAL A   159                                                      
REMARK 465     TYR A   160                                                      
REMARK 465     SER A   161                                                      
REMARK 465     SER A   162                                                      
REMARK 465     ALA A   163                                                      
REMARK 465     ASN A   164                                                      
REMARK 465     ASN A   165                                                      
REMARK 465     GLN A   173                                                      
REMARK 465     PRO A   174                                                      
REMARK 465     PHE A   175                                                      
REMARK 465     LEU A   176                                                      
REMARK 465     MET A   177                                                      
REMARK 465     ASP A   178                                                      
REMARK 465     LEU A   179                                                      
REMARK 465     GLU A   180                                                      
REMARK 465     GLY A   181                                                      
REMARK 465     LYS A   182                                                      
REMARK 465     GLN A   183                                                      
REMARK 465     GLY A   184                                                      
REMARK 465     ASN A   185                                                      
REMARK 465     ALA A   243                                                      
REMARK 465     LEU A   244                                                      
REMARK 465     HIS A   245                                                      
REMARK 465     ARG A   246                                                      
REMARK 465     SER A   247                                                      
REMARK 465     TYR A   248                                                      
REMARK 465     LEU A   249                                                      
REMARK 465     THR A   250                                                      
REMARK 465     PRO A   251                                                      
REMARK 465     GLY A   252                                                      
REMARK 465     ASP A   253                                                      
REMARK 465     SER A   254                                                      
REMARK 465     SER A   255                                                      
REMARK 465     SER A   256                                                      
REMARK 465     GLY A   257                                                      
REMARK 465     TRP A   258                                                      
REMARK 465     THR A   259                                                      
REMARK 465     ALA A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     SER A   443                                                      
REMARK 465     LYS A   444                                                      
REMARK 465     VAL A   445                                                      
REMARK 465     GLY A   446                                                      
REMARK 465     GLY A   447                                                      
REMARK 465     GLU A   471                                                      
REMARK 465     ILE A   472                                                      
REMARK 465     TYR A   473                                                      
REMARK 465     GLN A   474                                                      
REMARK 465     ALA A   475                                                      
REMARK 465     GLY A   476                                                      
REMARK 465     SER A   477                                                      
REMARK 465     THR A   478                                                      
REMARK 465     PRO A   479                                                      
REMARK 465     CYS A   480                                                      
REMARK 465     ASN A   481                                                      
REMARK 465     GLY A   482                                                      
REMARK 465     VAL A   483                                                      
REMARK 465     GLU A   484                                                      
REMARK 465     GLY A   485                                                      
REMARK 465     PHE A   486                                                      
REMARK 465     ASN A   487                                                      
REMARK 465     CYS A   488                                                      
REMARK 465     TYR A   489                                                      
REMARK 465     GLY A   502                                                      
REMARK 465     PRO A   621                                                      
REMARK 465     VAL A   622                                                      
REMARK 465     ALA A   623                                                      
REMARK 465     ILE A   624                                                      
REMARK 465     HIS A   625                                                      
REMARK 465     ALA A   626                                                      
REMARK 465     ASP A   627                                                      
REMARK 465     GLN A   628                                                      
REMARK 465     LEU A   629                                                      
REMARK 465     THR A   630                                                      
REMARK 465     PRO A   631                                                      
REMARK 465     THR A   632                                                      
REMARK 465     TRP A   633                                                      
REMARK 465     ARG A   634                                                      
REMARK 465     VAL A   635                                                      
REMARK 465     TYR A   636                                                      
REMARK 465     SER A   637                                                      
REMARK 465     THR A   638                                                      
REMARK 465     GLY A   639                                                      
REMARK 465     SER A   640                                                      
REMARK 465     GLN A   677                                                      
REMARK 465     THR A   678                                                      
REMARK 465     ASN A   679                                                      
REMARK 465     SER A   680                                                      
REMARK 465     PRO A   681                                                      
REMARK 465     SER A   682                                                      
REMARK 465     GLY A   683                                                      
REMARK 465     ALA A   684                                                      
REMARK 465     GLY A   685                                                      
REMARK 465     SER A   686                                                      
REMARK 465     VAL A   687                                                      
REMARK 465     ALA A   688                                                      
REMARK 465     SER A   689                                                      
REMARK 465     PRO A   812                                                      
REMARK 465     LEU A   828                                                      
REMARK 465     ALA A   829                                                      
REMARK 465     ASP A   830                                                      
REMARK 465     ALA A   831                                                      
REMARK 465     GLY A   832                                                      
REMARK 465     PHE A   833                                                      
REMARK 465     ILE A   834                                                      
REMARK 465     LYS A   835                                                      
REMARK 465     GLN A   836                                                      
REMARK 465     TYR A   837                                                      
REMARK 465     GLY A   838                                                      
REMARK 465     ASP A   839                                                      
REMARK 465     CYS A   840                                                      
REMARK 465     LEU A   841                                                      
REMARK 465     GLY A   842                                                      
REMARK 465     ASP A   843                                                      
REMARK 465     ILE A   844                                                      
REMARK 465     ALA A   845                                                      
REMARK 465     ALA A   846                                                      
REMARK 465     ARG A   847                                                      
REMARK 465     ASP A   848                                                      
REMARK 465     LEU A   849                                                      
REMARK 465     ILE A   850                                                      
REMARK 465     CYS A   851                                                      
REMARK 465     ALA A   852                                                      
REMARK 465     GLN A   853                                                      
REMARK 465     LYS A   854                                                      
REMARK 465     PHE A  1148                                                      
REMARK 465     LYS A  1149                                                      
REMARK 465     GLU A  1150                                                      
REMARK 465     GLU A  1151                                                      
REMARK 465     LEU A  1152                                                      
REMARK 465     ASP A  1153                                                      
REMARK 465     LYS A  1154                                                      
REMARK 465     TYR A  1155                                                      
REMARK 465     PHE A  1156                                                      
REMARK 465     LYS A  1157                                                      
REMARK 465     ASN A  1158                                                      
REMARK 465     HIS A  1159                                                      
REMARK 465     THR A  1160                                                      
REMARK 465     SER A  1161                                                      
REMARK 465     PRO A  1162                                                      
REMARK 465     ASP A  1163                                                      
REMARK 465     VAL A  1164                                                      
REMARK 465     ASP A  1165                                                      
REMARK 465     LEU A  1166                                                      
REMARK 465     GLY A  1167                                                      
REMARK 465     ASP A  1168                                                      
REMARK 465     ILE A  1169                                                      
REMARK 465     SER A  1170                                                      
REMARK 465     GLY A  1171                                                      
REMARK 465     ILE A  1172                                                      
REMARK 465     ASN A  1173                                                      
REMARK 465     ALA A  1174                                                      
REMARK 465     SER A  1175                                                      
REMARK 465     VAL A  1176                                                      
REMARK 465     VAL A  1177                                                      
REMARK 465     ASN A  1178                                                      
REMARK 465     ILE A  1179                                                      
REMARK 465     GLN A  1180                                                      
REMARK 465     LYS A  1181                                                      
REMARK 465     GLU A  1182                                                      
REMARK 465     ILE A  1183                                                      
REMARK 465     ASP A  1184                                                      
REMARK 465     ARG A  1185                                                      
REMARK 465     LEU A  1186                                                      
REMARK 465     ASN A  1187                                                      
REMARK 465     GLU A  1188                                                      
REMARK 465     VAL A  1189                                                      
REMARK 465     ALA A  1190                                                      
REMARK 465     LYS A  1191                                                      
REMARK 465     ASN A  1192                                                      
REMARK 465     LEU A  1193                                                      
REMARK 465     ASN A  1194                                                      
REMARK 465     GLU A  1195                                                      
REMARK 465     SER A  1196                                                      
REMARK 465     LEU A  1197                                                      
REMARK 465     ILE A  1198                                                      
REMARK 465     ASP A  1199                                                      
REMARK 465     LEU A  1200                                                      
REMARK 465     GLN A  1201                                                      
REMARK 465     GLU A  1202                                                      
REMARK 465     LEU A  1203                                                      
REMARK 465     GLY A  1204                                                      
REMARK 465     LYS A  1205                                                      
REMARK 465     TYR A  1206                                                      
REMARK 465     GLU A  1207                                                      
REMARK 465     GLN A  1208                                                      
REMARK 465     TYR A  1209                                                      
REMARK 465     ILE A  1210                                                      
REMARK 465     LYS A  1211                                                      
REMARK 465     GLY A  1212                                                      
REMARK 465     SER A  1213                                                      
REMARK 465     GLY A  1214                                                      
REMARK 465     ARG A  1215                                                      
REMARK 465     GLU A  1216                                                      
REMARK 465     ASN A  1217                                                      
REMARK 465     LEU A  1218                                                      
REMARK 465     TYR A  1219                                                      
REMARK 465     PHE A  1220                                                      
REMARK 465     GLN A  1221                                                      
REMARK 465     GLY A  1222                                                      
REMARK 465     GLY A  1223                                                      
REMARK 465     GLY A  1224                                                      
REMARK 465     GLY A  1225                                                      
REMARK 465     SER A  1226                                                      
REMARK 465     GLY A  1227                                                      
REMARK 465     TYR A  1228                                                      
REMARK 465     ILE A  1229                                                      
REMARK 465     PRO A  1230                                                      
REMARK 465     GLU A  1231                                                      
REMARK 465     ALA A  1232                                                      
REMARK 465     PRO A  1233                                                      
REMARK 465     ARG A  1234                                                      
REMARK 465     ASP A  1235                                                      
REMARK 465     GLY A  1236                                                      
REMARK 465     GLN A  1237                                                      
REMARK 465     ALA A  1238                                                      
REMARK 465     TYR A  1239                                                      
REMARK 465     VAL A  1240                                                      
REMARK 465     ARG A  1241                                                      
REMARK 465     LYS A  1242                                                      
REMARK 465     ASP A  1243                                                      
REMARK 465     GLY A  1244                                                      
REMARK 465     GLU A  1245                                                      
REMARK 465     TRP A  1246                                                      
REMARK 465     VAL A  1247                                                      
REMARK 465     LEU A  1248                                                      
REMARK 465     LEU A  1249                                                      
REMARK 465     SER A  1250                                                      
REMARK 465     THR A  1251                                                      
REMARK 465     PHE A  1252                                                      
REMARK 465     LEU A  1253                                                      
REMARK 465     GLY A  1254                                                      
REMARK 465     HIS A  1255                                                      
REMARK 465     HIS A  1256                                                      
REMARK 465     HIS A  1257                                                      
REMARK 465     HIS A  1258                                                      
REMARK 465     HIS A  1259                                                      
REMARK 465     HIS A  1260                                                      
REMARK 465     HIS A  1261                                                      
REMARK 465     HIS A  1262                                                      
REMARK 465     MET B   -18                                                      
REMARK 465     GLY B   -17                                                      
REMARK 465     ILE B   -16                                                      
REMARK 465     LEU B   -15                                                      
REMARK 465     PRO B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     PRO B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     MET B   -10                                                      
REMARK 465     PRO B    -9                                                      
REMARK 465     ALA B    -8                                                      
REMARK 465     LEU B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     SER B    -5                                                      
REMARK 465     LEU B    -4                                                      
REMARK 465     VAL B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     LEU B    -1                                                      
REMARK 465     LEU B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     MET B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     CYS B     7                                                      
REMARK 465     VAL B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     GLU B    10                                                      
REMARK 465     THR B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     GLN B    14                                                      
REMARK 465     CYS B    15                                                      
REMARK 465     VAL B    16                                                      
REMARK 465     ASN B    17                                                      
REMARK 465     LEU B    18                                                      
REMARK 465     THR B    19                                                      
REMARK 465     THR B    20                                                      
REMARK 465     ARG B    21                                                      
REMARK 465     THR B    22                                                      
REMARK 465     GLN B    23                                                      
REMARK 465     LEU B    24                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     PRO B    26                                                      
REMARK 465     ALA B    67                                                      
REMARK 465     ILE B    68                                                      
REMARK 465     HIS B    69                                                      
REMARK 465     VAL B    70                                                      
REMARK 465     SER B    71                                                      
REMARK 465     GLY B    72                                                      
REMARK 465     THR B    73                                                      
REMARK 465     ASN B    74                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     THR B    76                                                      
REMARK 465     LYS B    77                                                      
REMARK 465     ARG B    78                                                      
REMARK 465     PHE B    79                                                      
REMARK 465     ASP B    80                                                      
REMARK 465     LEU B   141                                                      
REMARK 465     GLY B   142                                                      
REMARK 465     VAL B   143                                                      
REMARK 465     TYR B   144                                                      
REMARK 465     TYR B   145                                                      
REMARK 465     HIS B   146                                                      
REMARK 465     LYS B   147                                                      
REMARK 465     ASN B   148                                                      
REMARK 465     ASN B   149                                                      
REMARK 465     LYS B   150                                                      
REMARK 465     SER B   151                                                      
REMARK 465     TRP B   152                                                      
REMARK 465     MET B   153                                                      
REMARK 465     GLU B   154                                                      
REMARK 465     SER B   155                                                      
REMARK 465     GLU B   156                                                      
REMARK 465     PHE B   157                                                      
REMARK 465     ARG B   158                                                      
REMARK 465     VAL B   159                                                      
REMARK 465     TYR B   160                                                      
REMARK 465     SER B   161                                                      
REMARK 465     SER B   162                                                      
REMARK 465     ALA B   163                                                      
REMARK 465     GLN B   173                                                      
REMARK 465     PRO B   174                                                      
REMARK 465     PHE B   175                                                      
REMARK 465     LEU B   176                                                      
REMARK 465     MET B   177                                                      
REMARK 465     ASP B   178                                                      
REMARK 465     LEU B   179                                                      
REMARK 465     GLU B   180                                                      
REMARK 465     GLY B   181                                                      
REMARK 465     LYS B   182                                                      
REMARK 465     GLN B   183                                                      
REMARK 465     GLY B   184                                                      
REMARK 465     ASN B   185                                                      
REMARK 465     ILE B   197                                                      
REMARK 465     ASP B   198                                                      
REMARK 465     GLY B   199                                                      
REMARK 465     LEU B   212                                                      
REMARK 465     VAL B   213                                                      
REMARK 465     ARG B   214                                                      
REMARK 465     ALA B   243                                                      
REMARK 465     LEU B   244                                                      
REMARK 465     HIS B   245                                                      
REMARK 465     ARG B   246                                                      
REMARK 465     SER B   247                                                      
REMARK 465     TYR B   248                                                      
REMARK 465     LEU B   249                                                      
REMARK 465     THR B   250                                                      
REMARK 465     PRO B   251                                                      
REMARK 465     GLY B   252                                                      
REMARK 465     ASP B   253                                                      
REMARK 465     SER B   254                                                      
REMARK 465     SER B   255                                                      
REMARK 465     SER B   256                                                      
REMARK 465     GLY B   257                                                      
REMARK 465     TRP B   258                                                      
REMARK 465     THR B   259                                                      
REMARK 465     ALA B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     LEU B   455                                                      
REMARK 465     PHE B   456                                                      
REMARK 465     ARG B   457                                                      
REMARK 465     LYS B   458                                                      
REMARK 465     SER B   459                                                      
REMARK 465     ASN B   460                                                      
REMARK 465     LEU B   461                                                      
REMARK 465     ASP B   467                                                      
REMARK 465     ILE B   468                                                      
REMARK 465     SER B   469                                                      
REMARK 465     THR B   470                                                      
REMARK 465     GLU B   471                                                      
REMARK 465     ILE B   472                                                      
REMARK 465     TYR B   473                                                      
REMARK 465     GLN B   474                                                      
REMARK 465     ALA B   475                                                      
REMARK 465     GLY B   476                                                      
REMARK 465     SER B   477                                                      
REMARK 465     THR B   478                                                      
REMARK 465     PRO B   479                                                      
REMARK 465     CYS B   480                                                      
REMARK 465     ASN B   481                                                      
REMARK 465     GLY B   482                                                      
REMARK 465     VAL B   483                                                      
REMARK 465     GLU B   484                                                      
REMARK 465     GLY B   485                                                      
REMARK 465     PHE B   486                                                      
REMARK 465     ASN B   487                                                      
REMARK 465     CYS B   488                                                      
REMARK 465     TYR B   489                                                      
REMARK 465     PHE B   490                                                      
REMARK 465     GLU B   516                                                      
REMARK 465     LEU B   517                                                      
REMARK 465     LEU B   518                                                      
REMARK 465     HIS B   519                                                      
REMARK 465     ALA B   520                                                      
REMARK 465     PRO B   521                                                      
REMARK 465     PRO B   621                                                      
REMARK 465     VAL B   622                                                      
REMARK 465     ALA B   623                                                      
REMARK 465     ILE B   624                                                      
REMARK 465     HIS B   625                                                      
REMARK 465     ALA B   626                                                      
REMARK 465     ASP B   627                                                      
REMARK 465     GLN B   628                                                      
REMARK 465     LEU B   629                                                      
REMARK 465     THR B   630                                                      
REMARK 465     PRO B   631                                                      
REMARK 465     THR B   632                                                      
REMARK 465     TRP B   633                                                      
REMARK 465     ARG B   634                                                      
REMARK 465     VAL B   635                                                      
REMARK 465     TYR B   636                                                      
REMARK 465     SER B   637                                                      
REMARK 465     THR B   638                                                      
REMARK 465     GLY B   639                                                      
REMARK 465     SER B   640                                                      
REMARK 465     GLN B   677                                                      
REMARK 465     THR B   678                                                      
REMARK 465     ASN B   679                                                      
REMARK 465     SER B   680                                                      
REMARK 465     PRO B   681                                                      
REMARK 465     SER B   682                                                      
REMARK 465     GLY B   683                                                      
REMARK 465     ALA B   684                                                      
REMARK 465     GLY B   685                                                      
REMARK 465     SER B   686                                                      
REMARK 465     VAL B   687                                                      
REMARK 465     ALA B   688                                                      
REMARK 465     PRO B   812                                                      
REMARK 465     LEU B   828                                                      
REMARK 465     ALA B   829                                                      
REMARK 465     ASP B   830                                                      
REMARK 465     ALA B   831                                                      
REMARK 465     GLY B   832                                                      
REMARK 465     PHE B   833                                                      
REMARK 465     ILE B   834                                                      
REMARK 465     LYS B   835                                                      
REMARK 465     GLN B   836                                                      
REMARK 465     TYR B   837                                                      
REMARK 465     GLY B   838                                                      
REMARK 465     ASP B   839                                                      
REMARK 465     CYS B   840                                                      
REMARK 465     LEU B   841                                                      
REMARK 465     GLY B   842                                                      
REMARK 465     ASP B   843                                                      
REMARK 465     ILE B   844                                                      
REMARK 465     ALA B   845                                                      
REMARK 465     ALA B   846                                                      
REMARK 465     ARG B   847                                                      
REMARK 465     ASP B   848                                                      
REMARK 465     LEU B   849                                                      
REMARK 465     ILE B   850                                                      
REMARK 465     CYS B   851                                                      
REMARK 465     ALA B   852                                                      
REMARK 465     GLN B   853                                                      
REMARK 465     PHE B  1148                                                      
REMARK 465     LYS B  1149                                                      
REMARK 465     GLU B  1150                                                      
REMARK 465     GLU B  1151                                                      
REMARK 465     LEU B  1152                                                      
REMARK 465     ASP B  1153                                                      
REMARK 465     LYS B  1154                                                      
REMARK 465     TYR B  1155                                                      
REMARK 465     PHE B  1156                                                      
REMARK 465     LYS B  1157                                                      
REMARK 465     ASN B  1158                                                      
REMARK 465     HIS B  1159                                                      
REMARK 465     THR B  1160                                                      
REMARK 465     SER B  1161                                                      
REMARK 465     PRO B  1162                                                      
REMARK 465     ASP B  1163                                                      
REMARK 465     VAL B  1164                                                      
REMARK 465     ASP B  1165                                                      
REMARK 465     LEU B  1166                                                      
REMARK 465     GLY B  1167                                                      
REMARK 465     ASP B  1168                                                      
REMARK 465     ILE B  1169                                                      
REMARK 465     SER B  1170                                                      
REMARK 465     GLY B  1171                                                      
REMARK 465     ILE B  1172                                                      
REMARK 465     ASN B  1173                                                      
REMARK 465     ALA B  1174                                                      
REMARK 465     SER B  1175                                                      
REMARK 465     VAL B  1176                                                      
REMARK 465     VAL B  1177                                                      
REMARK 465     ASN B  1178                                                      
REMARK 465     ILE B  1179                                                      
REMARK 465     GLN B  1180                                                      
REMARK 465     LYS B  1181                                                      
REMARK 465     GLU B  1182                                                      
REMARK 465     ILE B  1183                                                      
REMARK 465     ASP B  1184                                                      
REMARK 465     ARG B  1185                                                      
REMARK 465     LEU B  1186                                                      
REMARK 465     ASN B  1187                                                      
REMARK 465     GLU B  1188                                                      
REMARK 465     VAL B  1189                                                      
REMARK 465     ALA B  1190                                                      
REMARK 465     LYS B  1191                                                      
REMARK 465     ASN B  1192                                                      
REMARK 465     LEU B  1193                                                      
REMARK 465     ASN B  1194                                                      
REMARK 465     GLU B  1195                                                      
REMARK 465     SER B  1196                                                      
REMARK 465     LEU B  1197                                                      
REMARK 465     ILE B  1198                                                      
REMARK 465     ASP B  1199                                                      
REMARK 465     LEU B  1200                                                      
REMARK 465     GLN B  1201                                                      
REMARK 465     GLU B  1202                                                      
REMARK 465     LEU B  1203                                                      
REMARK 465     GLY B  1204                                                      
REMARK 465     LYS B  1205                                                      
REMARK 465     TYR B  1206                                                      
REMARK 465     GLU B  1207                                                      
REMARK 465     GLN B  1208                                                      
REMARK 465     TYR B  1209                                                      
REMARK 465     ILE B  1210                                                      
REMARK 465     LYS B  1211                                                      
REMARK 465     GLY B  1212                                                      
REMARK 465     SER B  1213                                                      
REMARK 465     GLY B  1214                                                      
REMARK 465     ARG B  1215                                                      
REMARK 465     GLU B  1216                                                      
REMARK 465     ASN B  1217                                                      
REMARK 465     LEU B  1218                                                      
REMARK 465     TYR B  1219                                                      
REMARK 465     PHE B  1220                                                      
REMARK 465     GLN B  1221                                                      
REMARK 465     GLY B  1222                                                      
REMARK 465     GLY B  1223                                                      
REMARK 465     GLY B  1224                                                      
REMARK 465     GLY B  1225                                                      
REMARK 465     SER B  1226                                                      
REMARK 465     GLY B  1227                                                      
REMARK 465     TYR B  1228                                                      
REMARK 465     ILE B  1229                                                      
REMARK 465     PRO B  1230                                                      
REMARK 465     GLU B  1231                                                      
REMARK 465     ALA B  1232                                                      
REMARK 465     PRO B  1233                                                      
REMARK 465     ARG B  1234                                                      
REMARK 465     ASP B  1235                                                      
REMARK 465     GLY B  1236                                                      
REMARK 465     GLN B  1237                                                      
REMARK 465     ALA B  1238                                                      
REMARK 465     TYR B  1239                                                      
REMARK 465     VAL B  1240                                                      
REMARK 465     ARG B  1241                                                      
REMARK 465     LYS B  1242                                                      
REMARK 465     ASP B  1243                                                      
REMARK 465     GLY B  1244                                                      
REMARK 465     GLU B  1245                                                      
REMARK 465     TRP B  1246                                                      
REMARK 465     VAL B  1247                                                      
REMARK 465     LEU B  1248                                                      
REMARK 465     LEU B  1249                                                      
REMARK 465     SER B  1250                                                      
REMARK 465     THR B  1251                                                      
REMARK 465     PHE B  1252                                                      
REMARK 465     LEU B  1253                                                      
REMARK 465     GLY B  1254                                                      
REMARK 465     HIS B  1255                                                      
REMARK 465     HIS B  1256                                                      
REMARK 465     HIS B  1257                                                      
REMARK 465     HIS B  1258                                                      
REMARK 465     HIS B  1259                                                      
REMARK 465     HIS B  1260                                                      
REMARK 465     HIS B  1261                                                      
REMARK 465     HIS B  1262                                                      
REMARK 465     MET C   -18                                                      
REMARK 465     GLY C   -17                                                      
REMARK 465     ILE C   -16                                                      
REMARK 465     LEU C   -15                                                      
REMARK 465     PRO C   -14                                                      
REMARK 465     SER C   -13                                                      
REMARK 465     PRO C   -12                                                      
REMARK 465     GLY C   -11                                                      
REMARK 465     MET C   -10                                                      
REMARK 465     PRO C    -9                                                      
REMARK 465     ALA C    -8                                                      
REMARK 465     LEU C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     SER C    -5                                                      
REMARK 465     LEU C    -4                                                      
REMARK 465     VAL C    -3                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     LEU C    -1                                                      
REMARK 465     LEU C     0                                                      
REMARK 465     SER C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     MET C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     CYS C     7                                                      
REMARK 465     VAL C     8                                                      
REMARK 465     ALA C     9                                                      
REMARK 465     GLU C    10                                                      
REMARK 465     THR C    11                                                      
REMARK 465     GLY C    12                                                      
REMARK 465     THR C    13                                                      
REMARK 465     GLN C    14                                                      
REMARK 465     CYS C    15                                                      
REMARK 465     VAL C    16                                                      
REMARK 465     ASN C    17                                                      
REMARK 465     LEU C    18                                                      
REMARK 465     THR C    19                                                      
REMARK 465     THR C    20                                                      
REMARK 465     ARG C    21                                                      
REMARK 465     THR C    22                                                      
REMARK 465     GLN C    23                                                      
REMARK 465     LEU C    24                                                      
REMARK 465     PRO C    25                                                      
REMARK 465     PRO C    26                                                      
REMARK 465     ALA C    67                                                      
REMARK 465     ILE C    68                                                      
REMARK 465     HIS C    69                                                      
REMARK 465     VAL C    70                                                      
REMARK 465     SER C    71                                                      
REMARK 465     GLY C    72                                                      
REMARK 465     THR C    73                                                      
REMARK 465     ASN C    74                                                      
REMARK 465     GLY C    75                                                      
REMARK 465     THR C    76                                                      
REMARK 465     LYS C    77                                                      
REMARK 465     ARG C    78                                                      
REMARK 465     PHE C    79                                                      
REMARK 465     ASP C    80                                                      
REMARK 465     TYR C   144                                                      
REMARK 465     TYR C   145                                                      
REMARK 465     HIS C   146                                                      
REMARK 465     LYS C   147                                                      
REMARK 465     ASN C   148                                                      
REMARK 465     ASN C   149                                                      
REMARK 465     LYS C   150                                                      
REMARK 465     SER C   151                                                      
REMARK 465     TRP C   152                                                      
REMARK 465     MET C   153                                                      
REMARK 465     GLU C   154                                                      
REMARK 465     SER C   155                                                      
REMARK 465     GLU C   156                                                      
REMARK 465     PHE C   157                                                      
REMARK 465     ARG C   158                                                      
REMARK 465     VAL C   159                                                      
REMARK 465     TYR C   160                                                      
REMARK 465     SER C   161                                                      
REMARK 465     SER C   162                                                      
REMARK 465     ALA C   163                                                      
REMARK 465     ASN C   164                                                      
REMARK 465     GLN C   173                                                      
REMARK 465     PRO C   174                                                      
REMARK 465     PHE C   175                                                      
REMARK 465     LEU C   176                                                      
REMARK 465     MET C   177                                                      
REMARK 465     ASP C   178                                                      
REMARK 465     LEU C   179                                                      
REMARK 465     GLU C   180                                                      
REMARK 465     GLY C   181                                                      
REMARK 465     LYS C   182                                                      
REMARK 465     GLN C   183                                                      
REMARK 465     GLY C   184                                                      
REMARK 465     ASN C   185                                                      
REMARK 465     ALA C   243                                                      
REMARK 465     LEU C   244                                                      
REMARK 465     HIS C   245                                                      
REMARK 465     ARG C   246                                                      
REMARK 465     SER C   247                                                      
REMARK 465     TYR C   248                                                      
REMARK 465     LEU C   249                                                      
REMARK 465     THR C   250                                                      
REMARK 465     PRO C   251                                                      
REMARK 465     GLY C   252                                                      
REMARK 465     ASP C   253                                                      
REMARK 465     SER C   254                                                      
REMARK 465     SER C   255                                                      
REMARK 465     SER C   256                                                      
REMARK 465     GLY C   257                                                      
REMARK 465     TRP C   258                                                      
REMARK 465     THR C   259                                                      
REMARK 465     ALA C   260                                                      
REMARK 465     GLY C   261                                                      
REMARK 465     ALA C   262                                                      
REMARK 465     ALA C   263                                                      
REMARK 465     VAL C   445                                                      
REMARK 465     GLY C   446                                                      
REMARK 465     GLY C   447                                                      
REMARK 465     LEU C   455                                                      
REMARK 465     PHE C   456                                                      
REMARK 465     ARG C   457                                                      
REMARK 465     LYS C   458                                                      
REMARK 465     SER C   459                                                      
REMARK 465     ASN C   460                                                      
REMARK 465     LEU C   461                                                      
REMARK 465     GLU C   471                                                      
REMARK 465     ILE C   472                                                      
REMARK 465     TYR C   473                                                      
REMARK 465     GLN C   474                                                      
REMARK 465     ALA C   475                                                      
REMARK 465     GLY C   476                                                      
REMARK 465     SER C   477                                                      
REMARK 465     THR C   478                                                      
REMARK 465     PRO C   479                                                      
REMARK 465     CYS C   480                                                      
REMARK 465     ASN C   481                                                      
REMARK 465     GLY C   482                                                      
REMARK 465     VAL C   483                                                      
REMARK 465     GLU C   484                                                      
REMARK 465     GLY C   485                                                      
REMARK 465     PHE C   486                                                      
REMARK 465     ASN C   487                                                      
REMARK 465     CYS C   488                                                      
REMARK 465     TYR C   489                                                      
REMARK 465     PHE C   490                                                      
REMARK 465     PRO C   621                                                      
REMARK 465     VAL C   622                                                      
REMARK 465     ALA C   623                                                      
REMARK 465     ILE C   624                                                      
REMARK 465     HIS C   625                                                      
REMARK 465     ALA C   626                                                      
REMARK 465     ASP C   627                                                      
REMARK 465     GLN C   628                                                      
REMARK 465     LEU C   629                                                      
REMARK 465     THR C   630                                                      
REMARK 465     PRO C   631                                                      
REMARK 465     THR C   632                                                      
REMARK 465     TRP C   633                                                      
REMARK 465     ARG C   634                                                      
REMARK 465     VAL C   635                                                      
REMARK 465     TYR C   636                                                      
REMARK 465     SER C   637                                                      
REMARK 465     THR C   638                                                      
REMARK 465     GLY C   639                                                      
REMARK 465     SER C   640                                                      
REMARK 465     GLN C   677                                                      
REMARK 465     THR C   678                                                      
REMARK 465     ASN C   679                                                      
REMARK 465     SER C   680                                                      
REMARK 465     PRO C   681                                                      
REMARK 465     SER C   682                                                      
REMARK 465     GLY C   683                                                      
REMARK 465     ALA C   684                                                      
REMARK 465     GLY C   685                                                      
REMARK 465     SER C   686                                                      
REMARK 465     VAL C   687                                                      
REMARK 465     ALA C   688                                                      
REMARK 465     SER C   689                                                      
REMARK 465     PRO C   812                                                      
REMARK 465     LEU C   828                                                      
REMARK 465     ALA C   829                                                      
REMARK 465     ASP C   830                                                      
REMARK 465     ALA C   831                                                      
REMARK 465     GLY C   832                                                      
REMARK 465     PHE C   833                                                      
REMARK 465     ILE C   834                                                      
REMARK 465     LYS C   835                                                      
REMARK 465     GLN C   836                                                      
REMARK 465     TYR C   837                                                      
REMARK 465     GLY C   838                                                      
REMARK 465     ASP C   839                                                      
REMARK 465     CYS C   840                                                      
REMARK 465     LEU C   841                                                      
REMARK 465     GLY C   842                                                      
REMARK 465     ASP C   843                                                      
REMARK 465     ILE C   844                                                      
REMARK 465     ALA C   845                                                      
REMARK 465     ALA C   846                                                      
REMARK 465     ARG C   847                                                      
REMARK 465     ASP C   848                                                      
REMARK 465     LEU C   849                                                      
REMARK 465     ILE C   850                                                      
REMARK 465     CYS C   851                                                      
REMARK 465     ALA C   852                                                      
REMARK 465     GLN C   853                                                      
REMARK 465     LYS C   854                                                      
REMARK 465     PHE C   855                                                      
REMARK 465     PHE C  1148                                                      
REMARK 465     LYS C  1149                                                      
REMARK 465     GLU C  1150                                                      
REMARK 465     GLU C  1151                                                      
REMARK 465     LEU C  1152                                                      
REMARK 465     ASP C  1153                                                      
REMARK 465     LYS C  1154                                                      
REMARK 465     TYR C  1155                                                      
REMARK 465     PHE C  1156                                                      
REMARK 465     LYS C  1157                                                      
REMARK 465     ASN C  1158                                                      
REMARK 465     HIS C  1159                                                      
REMARK 465     THR C  1160                                                      
REMARK 465     SER C  1161                                                      
REMARK 465     PRO C  1162                                                      
REMARK 465     ASP C  1163                                                      
REMARK 465     VAL C  1164                                                      
REMARK 465     ASP C  1165                                                      
REMARK 465     LEU C  1166                                                      
REMARK 465     GLY C  1167                                                      
REMARK 465     ASP C  1168                                                      
REMARK 465     ILE C  1169                                                      
REMARK 465     SER C  1170                                                      
REMARK 465     GLY C  1171                                                      
REMARK 465     ILE C  1172                                                      
REMARK 465     ASN C  1173                                                      
REMARK 465     ALA C  1174                                                      
REMARK 465     SER C  1175                                                      
REMARK 465     VAL C  1176                                                      
REMARK 465     VAL C  1177                                                      
REMARK 465     ASN C  1178                                                      
REMARK 465     ILE C  1179                                                      
REMARK 465     GLN C  1180                                                      
REMARK 465     LYS C  1181                                                      
REMARK 465     GLU C  1182                                                      
REMARK 465     ILE C  1183                                                      
REMARK 465     ASP C  1184                                                      
REMARK 465     ARG C  1185                                                      
REMARK 465     LEU C  1186                                                      
REMARK 465     ASN C  1187                                                      
REMARK 465     GLU C  1188                                                      
REMARK 465     VAL C  1189                                                      
REMARK 465     ALA C  1190                                                      
REMARK 465     LYS C  1191                                                      
REMARK 465     ASN C  1192                                                      
REMARK 465     LEU C  1193                                                      
REMARK 465     ASN C  1194                                                      
REMARK 465     GLU C  1195                                                      
REMARK 465     SER C  1196                                                      
REMARK 465     LEU C  1197                                                      
REMARK 465     ILE C  1198                                                      
REMARK 465     ASP C  1199                                                      
REMARK 465     LEU C  1200                                                      
REMARK 465     GLN C  1201                                                      
REMARK 465     GLU C  1202                                                      
REMARK 465     LEU C  1203                                                      
REMARK 465     GLY C  1204                                                      
REMARK 465     LYS C  1205                                                      
REMARK 465     TYR C  1206                                                      
REMARK 465     GLU C  1207                                                      
REMARK 465     GLN C  1208                                                      
REMARK 465     TYR C  1209                                                      
REMARK 465     ILE C  1210                                                      
REMARK 465     LYS C  1211                                                      
REMARK 465     GLY C  1212                                                      
REMARK 465     SER C  1213                                                      
REMARK 465     GLY C  1214                                                      
REMARK 465     ARG C  1215                                                      
REMARK 465     GLU C  1216                                                      
REMARK 465     ASN C  1217                                                      
REMARK 465     LEU C  1218                                                      
REMARK 465     TYR C  1219                                                      
REMARK 465     PHE C  1220                                                      
REMARK 465     GLN C  1221                                                      
REMARK 465     GLY C  1222                                                      
REMARK 465     GLY C  1223                                                      
REMARK 465     GLY C  1224                                                      
REMARK 465     GLY C  1225                                                      
REMARK 465     SER C  1226                                                      
REMARK 465     GLY C  1227                                                      
REMARK 465     TYR C  1228                                                      
REMARK 465     ILE C  1229                                                      
REMARK 465     PRO C  1230                                                      
REMARK 465     GLU C  1231                                                      
REMARK 465     ALA C  1232                                                      
REMARK 465     PRO C  1233                                                      
REMARK 465     ARG C  1234                                                      
REMARK 465     ASP C  1235                                                      
REMARK 465     GLY C  1236                                                      
REMARK 465     GLN C  1237                                                      
REMARK 465     ALA C  1238                                                      
REMARK 465     TYR C  1239                                                      
REMARK 465     VAL C  1240                                                      
REMARK 465     ARG C  1241                                                      
REMARK 465     LYS C  1242                                                      
REMARK 465     ASP C  1243                                                      
REMARK 465     GLY C  1244                                                      
REMARK 465     GLU C  1245                                                      
REMARK 465     TRP C  1246                                                      
REMARK 465     VAL C  1247                                                      
REMARK 465     LEU C  1248                                                      
REMARK 465     LEU C  1249                                                      
REMARK 465     SER C  1250                                                      
REMARK 465     THR C  1251                                                      
REMARK 465     PHE C  1252                                                      
REMARK 465     LEU C  1253                                                      
REMARK 465     GLY C  1254                                                      
REMARK 465     HIS C  1255                                                      
REMARK 465     HIS C  1256                                                      
REMARK 465     HIS C  1257                                                      
REMARK 465     HIS C  1258                                                      
REMARK 465     HIS C  1259                                                      
REMARK 465     HIS C  1260                                                      
REMARK 465     HIS C  1261                                                      
REMARK 465     HIS C  1262                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A  99    CG   OD1  ND2                                       
REMARK 470     ASP A 111    CG   OD1  OD2                                       
REMARK 470     THR A 124    OG1  CG2                                            
REMARK 470     LYS A 129    CG   CD   CE   NZ                                   
REMARK 470     PHE A 135    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     CYS A 136    SG                                                  
REMARK 470     ASN A 137    CG   OD1  ND2                                       
REMARK 470     ASN A 188    CG   OD1  ND2                                       
REMARK 470     ASN A 196    CG   OD1  ND2                                       
REMARK 470     LEU A 242    CG   CD1  CD2                                       
REMARK 470     GLU A 281    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 340    CG   CD   OE1  OE2                                  
REMARK 470     THR A 345    OG1  CG2                                            
REMARK 470     ASP A 405    CG   OD1  OD2                                       
REMARK 470     GLU A 406    CG   CD   OE1  OE2                                  
REMARK 470     THR A 415    OG1  CG2                                            
REMARK 470     ASP A 420    CG   OD1  OD2                                       
REMARK 470     ASP A 427    CG   OD1  OD2                                       
REMARK 470     ASN A 440    CG   OD1  ND2                                       
REMARK 470     ASP A 442    CG   OD1  OD2                                       
REMARK 470     LYS A 458    CG   CD   CE   NZ                                   
REMARK 470     GLU A 465    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 505    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 518    CG   CD1  CD2                                       
REMARK 470     HIS A 519    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 528    CG   CD   CE   NZ                                   
REMARK 470     ASP A 568    CG   OD1  OD2                                       
REMARK 470     ASP A 571    CG   OD1  OD2                                       
REMARK 470     LEU A 582    CG   CD1  CD2                                       
REMARK 470     GLU A 583    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 586    CG   OD1  OD2                                       
REMARK 470     ASP A 614    CG   OD1  OD2                                       
REMARK 470     GLU A 619    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 646    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 661    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 745    CG   OD1  OD2                                       
REMARK 470     GLU A 748    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 786    CG   CD   CE   NZ                                   
REMARK 470     LYS A 814    CG   CD   CE   NZ                                   
REMARK 470     PHE A 855    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 921    CG   CD   CE   NZ                                   
REMARK 470     LYS A1045    CG   CD   CE   NZ                                   
REMARK 470     LYS A1073    CG   CD   CE   NZ                                   
REMARK 470     GLU A1092    CG   CD   OE1  OE2                                  
REMARK 470     ASP A1118    CG   OD1  OD2                                       
REMARK 470     GLU A1144    CG   CD   OE1  OE2                                  
REMARK 470     ASP A1146    CG   OD1  OD2                                       
REMARK 470     ASP B  53    CG   OD1  OD2                                       
REMARK 470     ASN B  81    CG   OD1  ND2                                       
REMARK 470     GLU B  96    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 113    CG   CD   CE   NZ                                   
REMARK 470     THR B 124    OG1  CG2                                            
REMARK 470     ASN B 125    CG   OD1  ND2                                       
REMARK 470     GLU B 132    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 134    CG   CD   OE1  NE2                                  
REMARK 470     CYS B 136    SG                                                  
REMARK 470     ASN B 137    CG   OD1  ND2                                       
REMARK 470     ASP B 138    CG   OD1  OD2                                       
REMARK 470     ASN B 164    CG   OD1  ND2                                       
REMARK 470     SER B 172    OG                                                  
REMARK 470     ASP B 215    CG   OD1  OD2                                       
REMARK 470     GLN B 218    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 224    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 239    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 309    CG   CD   OE1  OE2                                  
REMARK 470     THR B 333    OG1  CG2                                            
REMARK 470     ASN B 334    CG   OD1  ND2                                       
REMARK 470     GLU B 340    CG   CD   OE1  OE2                                  
REMARK 470     THR B 345    OG1  CG2                                            
REMARK 470     ARG B 346    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B 347    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER B 349    OG                                                  
REMARK 470     VAL B 350    CG1  CG2                                            
REMARK 470     TYR B 351    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TRP B 353    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 353    CZ3  CH2                                            
REMARK 470     ASN B 354    CG   OD1  ND2                                       
REMARK 470     ARG B 355    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 356    CG   CD   CE   NZ                                   
REMARK 470     ARG B 357    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 358    CG1  CG2  CD1                                       
REMARK 470     SER B 359    OG                                                  
REMARK 470     ASN B 360    CG   OD1  ND2                                       
REMARK 470     VAL B 362    CG1  CG2                                            
REMARK 470     ASP B 364    CG   OD1  OD2                                       
REMARK 470     TYR B 365    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER B 366    OG                                                  
REMARK 470     VAL B 367    CG1  CG2                                            
REMARK 470     LEU B 368    CG   CD1  CD2                                       
REMARK 470     TYR B 369    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN B 370    CG   OD1  ND2                                       
REMARK 470     SER B 371    OG                                                  
REMARK 470     SER B 373    OG                                                  
REMARK 470     PHE B 374    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER B 375    OG                                                  
REMARK 470     THR B 376    OG1  CG2                                            
REMARK 470     PHE B 377    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 378    CG   CD   CE   NZ                                   
REMARK 470     TYR B 380    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL B 382    CG1  CG2                                            
REMARK 470     SER B 383    OG                                                  
REMARK 470     THR B 385    OG1  CG2                                            
REMARK 470     LYS B 386    CG   CD   CE   NZ                                   
REMARK 470     LEU B 387    CG   CD1  CD2                                       
REMARK 470     ASN B 388    CG   OD1  ND2                                       
REMARK 470     ASP B 389    CG   OD1  OD2                                       
REMARK 470     LEU B 390    CG   CD1  CD2                                       
REMARK 470     PHE B 392    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR B 393    OG1  CG2                                            
REMARK 470     ASN B 394    CG   OD1  ND2                                       
REMARK 470     VAL B 395    CG1  CG2                                            
REMARK 470     TYR B 396    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP B 398    CG   OD1  OD2                                       
REMARK 470     SER B 399    OG                                                  
REMARK 470     PHE B 400    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL B 401    CG1  CG2                                            
REMARK 470     ILE B 402    CG1  CG2  CD1                                       
REMARK 470     ARG B 403    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 405    CG   OD1  OD2                                       
REMARK 470     GLU B 406    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 407    CG1  CG2                                            
REMARK 470     ARG B 408    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 409    CG   CD   OE1  NE2                                  
REMARK 470     ILE B 410    CG1  CG2  CD1                                       
REMARK 470     GLN B 414    CG   CD   OE1  NE2                                  
REMARK 470     THR B 415    OG1  CG2                                            
REMARK 470     LYS B 417    CG   CD   CE   NZ                                   
REMARK 470     ILE B 418    CG1  CG2  CD1                                       
REMARK 470     ASP B 420    CG   OD1  OD2                                       
REMARK 470     TYR B 421    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN B 422    CG   OD1  ND2                                       
REMARK 470     TYR B 423    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 424    CG   CD   CE   NZ                                   
REMARK 470     LEU B 425    CG   CD1  CD2                                       
REMARK 470     ASP B 427    CG   OD1  OD2                                       
REMARK 470     ASP B 428    CG   OD1  OD2                                       
REMARK 470     PHE B 429    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR B 430    OG1  CG2                                            
REMARK 470     VAL B 433    CG1  CG2                                            
REMARK 470     ILE B 434    CG1  CG2  CD1                                       
REMARK 470     TRP B 436    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 436    CZ3  CH2                                            
REMARK 470     ASN B 437    CG   OD1  ND2                                       
REMARK 470     SER B 438    OG                                                  
REMARK 470     ASN B 439    CG   OD1  ND2                                       
REMARK 470     ASN B 440    CG   OD1  ND2                                       
REMARK 470     LEU B 441    CG   CD1  CD2                                       
REMARK 470     ASP B 442    CG   OD1  OD2                                       
REMARK 470     SER B 443    OG                                                  
REMARK 470     LYS B 444    CG   CD   CE   NZ                                   
REMARK 470     VAL B 445    CG1  CG2                                            
REMARK 470     ASN B 448    CG   OD1  ND2                                       
REMARK 470     TYR B 449    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN B 450    CG   OD1  ND2                                       
REMARK 470     TYR B 451    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU B 452    CG   CD1  CD2                                       
REMARK 470     TYR B 453    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B 454    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 462    CG   CD   CE   NZ                                   
REMARK 470     PHE B 464    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 465    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 466    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 492    CG   CD1  CD2                                       
REMARK 470     GLN B 493    CG   CD   OE1  NE2                                  
REMARK 470     SER B 494    OG                                                  
REMARK 470     TYR B 495    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE B 497    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN B 498    CG   CD   OE1  NE2                                  
REMARK 470     THR B 500    OG1  CG2                                            
REMARK 470     ASN B 501    CG   OD1  ND2                                       
REMARK 470     VAL B 503    CG1  CG2                                            
REMARK 470     TYR B 505    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN B 506    CG   CD   OE1  NE2                                  
REMARK 470     TYR B 508    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B 509    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 510    CG1  CG2                                            
REMARK 470     VAL B 511    CG1  CG2                                            
REMARK 470     VAL B 512    CG1  CG2                                            
REMARK 470     LEU B 513    CG   CD1  CD2                                       
REMARK 470     SER B 514    OG                                                  
REMARK 470     PHE B 515    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR B 523    OG1  CG2                                            
REMARK 470     VAL B 524    CG1  CG2                                            
REMARK 470     LYS B 528    CG   CD   CE   NZ                                   
REMARK 470     LYS B 529    CG   CD   CE   NZ                                   
REMARK 470     GLU B 554    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 583    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 646    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 661    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 748    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 786    CG   CD   CE   NZ                                   
REMARK 470     ILE B 794    CG1  CG2  CD1                                       
REMARK 470     ASP B 796    CG   OD1  OD2                                       
REMARK 470     LYS B 814    CG   CD   CE   NZ                                   
REMARK 470     LYS B1045    CG   CD   CE   NZ                                   
REMARK 470     GLU B1092    CG   CD   OE1  OE2                                  
REMARK 470     GLN B1142    CG   CD   OE1  NE2                                  
REMARK 470     LEU B1145    CG   CD1  CD2                                       
REMARK 470     ASP B1146    CG   OD1  OD2                                       
REMARK 470     SER C  46    OG                                                  
REMARK 470     ASN C  81    CG   OD1  ND2                                       
REMARK 470     ASP C  88    CG   OD1  OD2                                       
REMARK 470     LYS C  97    CG   CD   CE   NZ                                   
REMARK 470     LEU C 110    CG   CD1  CD2                                       
REMARK 470     SER C 112    OG                                                  
REMARK 470     GLN C 115    CG   CD   OE1  NE2                                  
REMARK 470     THR C 124    OG1  CG2                                            
REMARK 470     ASN C 125    CG   OD1  ND2                                       
REMARK 470     LYS C 129    CG   CD   CE   NZ                                   
REMARK 470     GLU C 132    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 134    CG   CD   OE1  NE2                                  
REMARK 470     CYS C 136    SG                                                  
REMARK 470     ASN C 137    CG   OD1  ND2                                       
REMARK 470     ASP C 138    CG   OD1  OD2                                       
REMARK 470     GLU C 169    CG   CD   OE1  OE2                                  
REMARK 470     SER C 172    OG                                                  
REMARK 470     GLU C 191    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 198    CG   OD1  OD2                                       
REMARK 470     ASN C 211    CG   OD1  ND2                                       
REMARK 470     VAL C 213    CG1  CG2                                            
REMARK 470     ASP C 215    CG   OD1  OD2                                       
REMARK 470     LEU C 242    CG   CD1  CD2                                       
REMARK 470     GLU C 281    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 324    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 340    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 346    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 378    CG   CD   CE   NZ                                   
REMARK 470     ASP C 398    CG   OD1  OD2                                       
REMARK 470     VAL C 401    CG1  CG2                                            
REMARK 470     ILE C 402    CG1  CG2  CD1                                       
REMARK 470     ASP C 405    CG   OD1  OD2                                       
REMARK 470     THR C 415    OG1  CG2                                            
REMARK 470     LYS C 417    CG   CD   CE   NZ                                   
REMARK 470     ILE C 418    CG1  CG2  CD1                                       
REMARK 470     ASP C 420    CG   OD1  OD2                                       
REMARK 470     ASN C 422    CG   OD1  ND2                                       
REMARK 470     ASN C 437    CG   OD1  ND2                                       
REMARK 470     ASN C 440    CG   OD1  ND2                                       
REMARK 470     LEU C 441    CG   CD1  CD2                                       
REMARK 470     ASP C 442    CG   OD1  OD2                                       
REMARK 470     SER C 443    OG                                                  
REMARK 470     LYS C 444    CG   CD   CE   NZ                                   
REMARK 470     TYR C 449    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU C 452    CG   CD1  CD2                                       
REMARK 470     LYS C 462    CG   CD   CE   NZ                                   
REMARK 470     GLU C 465    CG   CD   OE1  OE2                                  
REMARK 470     SER C 469    OG                                                  
REMARK 470     THR C 470    OG1  CG2                                            
REMARK 470     GLN C 498    CG   CD   OE1  NE2                                  
REMARK 470     THR C 500    OG1  CG2                                            
REMARK 470     TYR C 505    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU C 516    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 614    CG   OD1  OD2                                       
REMARK 470     GLU C 661    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 745    CG   OD1  OD2                                       
REMARK 470     GLU C 748    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 786    CG   CD   CE   NZ                                   
REMARK 470     LYS C 811    CG   CD   CE   NZ                                   
REMARK 470     LYS C 814    CG   CD   CE   NZ                                   
REMARK 470     ASP C 867    CG   OD1  OD2                                       
REMARK 470     GLU C 868    CG   CD   OE1  OE2                                  
REMARK 470     SER C 940    OG                                                  
REMARK 470     ASP C 985    CG   OD1  OD2                                       
REMARK 470     GLU C 988    CG   CD   OE1  OE2                                  
REMARK 470     LYS C1045    CG   CD   CE   NZ                                   
REMARK 470     GLU C1092    CG   CD   OE1  OE2                                  
REMARK 470     ASP C1146    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS B   336     SG   CYS B   361              1.67            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASN A 422   CB    ASN A 422   CG     -0.158                       
REMARK 500    TYR B 200   CG    TYR B 200   CD2     0.079                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ALA B1070   CB  -  CA  -  C   ANGL. DEV. = -16.4 DEGREES          
REMARK 500    ALA B1070   N   -  CA  -  C   ANGL. DEV. =  22.6 DEGREES          
REMARK 500    GLN B1071   N   -  CA  -  C   ANGL. DEV. = -19.3 DEGREES          
REMARK 500    TYR C 904   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ALA C1070   CB  -  CA  -  C   ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ALA C1070   N   -  CA  -  C   ANGL. DEV. =  19.0 DEGREES          
REMARK 500    GLN C1071   N   -  CA  -  C   ANGL. DEV. = -18.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  32     -121.71     51.35                                   
REMARK 500    ALA A  67       54.06   -143.91                                   
REMARK 500    ASN A  87     -122.59     52.53                                   
REMARK 500    THR A 108      -74.03   -108.13                                   
REMARK 500    ALA A 123     -108.24     57.16                                   
REMARK 500    ARG A 214      -86.46   -103.37                                   
REMARK 500    ASN A 422      -51.98   -124.44                                   
REMARK 500    LEU A 441      -51.08   -126.45                                   
REMARK 500    ILE A 468       82.74   -153.33                                   
REMARK 500    THR A 618      -81.59   -134.32                                   
REMARK 500    ASP A 663      -77.40   -111.87                                   
REMARK 500    HIS A1083      -77.09   -107.89                                   
REMARK 500    THR A1100      -30.90   -130.94                                   
REMARK 500    GLU A1111       78.41   -154.88                                   
REMARK 500    PHE B  32     -117.75     51.42                                   
REMARK 500    ASN B  87     -123.56     54.92                                   
REMARK 500    THR B 108      -77.21   -116.93                                   
REMARK 500    ASP B 111       82.19   -159.50                                   
REMARK 500    SER B 112     -147.63     47.89                                   
REMARK 500    LYS B 113      -56.18     67.47                                   
REMARK 500    ALA B 123     -112.41     62.50                                   
REMARK 500    ASN B 334       65.91     71.61                                   
REMARK 500    ASN B 422      -58.16   -122.10                                   
REMARK 500    LEU B 441      -56.58   -124.20                                   
REMARK 500    ASN B 544     -110.82     52.83                                   
REMARK 500    ALA B 570       57.29    -90.50                                   
REMARK 500    ASP B 663      -79.23   -111.76                                   
REMARK 500    LEU B1049      -61.69   -109.73                                   
REMARK 500    HIS B1083      -76.15   -118.73                                   
REMARK 500    PHE B1109      116.91   -169.24                                   
REMARK 500    GLU B1111       79.67   -158.75                                   
REMARK 500    PHE C  32     -119.37     51.04                                   
REMARK 500    ASN C  87     -122.81     53.23                                   
REMARK 500    THR C 108      -76.04   -114.34                                   
REMARK 500    ASP C 111       52.27   -150.71                                   
REMARK 500    ALA C 123     -113.43     62.34                                   
REMARK 500    LEU C 441      -56.61   -124.70                                   
REMARK 500    ASP C 663      -78.70   -116.43                                   
REMARK 500    PHE C 797       45.39    -96.55                                   
REMARK 500    LEU C1049      -61.47   -107.05                                   
REMARK 500    ALA C1070      -50.92   -124.59                                   
REMARK 500    HIS C1083      -79.24   -109.43                                   
REMARK 500    GLU C1092       68.22   -155.83                                   
REMARK 500    GLU C1111       77.13   -155.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-21452   RELATED DB: EMDB                             
REMARK 900 SARS-COV-2 SPIKE ECTODOMAIN STRUCTURE (CLOSED STATE)                 
REMARK 900 RELATED ID: EMD-21457   RELATED DB: EMDB                             
REMARK 900 SARS-COV-2 SPIKE ECTODOMAIN STRUCTURE (OPEN STATE)                   
DBREF  6VYB A   14  1211  UNP    P0DTC2   SPIKE_SARS2     14   1211             
DBREF  6VYB B   14  1211  UNP    P0DTC2   SPIKE_SARS2     14   1211             
DBREF  6VYB C   14  1211  UNP    P0DTC2   SPIKE_SARS2     14   1211             
SEQADV 6VYB MET A  -18  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY A  -17  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ILE A  -16  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU A  -15  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PRO A  -14  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER A  -13  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PRO A  -12  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY A  -11  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB MET A  -10  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PRO A   -9  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ALA A   -8  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU A   -7  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU A   -6  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER A   -5  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU A   -4  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB VAL A   -3  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER A   -2  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU A   -1  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU A    0  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER A    1  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB VAL A    2  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU A    3  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU A    4  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB MET A    5  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY A    6  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB CYS A    7  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB VAL A    8  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ALA A    9  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLU A   10  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB THR A   11  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY A   12  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB THR A   13  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLU A  607  UNP  P0DTC2    GLN   607 CONFLICT                       
SEQADV 6VYB SER A  682  UNP  P0DTC2    ARG   682 CONFLICT                       
SEQADV 6VYB GLY A  683  UNP  P0DTC2    ARG   683 CONFLICT                       
SEQADV 6VYB GLY A  685  UNP  P0DTC2    ARG   685 CONFLICT                       
SEQADV 6VYB PRO A  986  UNP  P0DTC2    LYS   986 CONFLICT                       
SEQADV 6VYB PRO A  987  UNP  P0DTC2    VAL   987 CONFLICT                       
SEQADV 6VYB GLY A 1212  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER A 1213  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY A 1214  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ARG A 1215  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLU A 1216  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ASN A 1217  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU A 1218  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB TYR A 1219  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PHE A 1220  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLN A 1221  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY A 1222  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY A 1223  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY A 1224  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY A 1225  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER A 1226  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY A 1227  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB TYR A 1228  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ILE A 1229  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PRO A 1230  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLU A 1231  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ALA A 1232  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PRO A 1233  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ARG A 1234  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ASP A 1235  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY A 1236  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLN A 1237  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ALA A 1238  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB TYR A 1239  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB VAL A 1240  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ARG A 1241  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LYS A 1242  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ASP A 1243  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY A 1244  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLU A 1245  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB TRP A 1246  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB VAL A 1247  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU A 1248  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU A 1249  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER A 1250  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB THR A 1251  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PHE A 1252  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU A 1253  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY A 1254  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS A 1255  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS A 1256  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS A 1257  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS A 1258  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS A 1259  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS A 1260  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS A 1261  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS A 1262  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB MET B  -18  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY B  -17  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ILE B  -16  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU B  -15  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PRO B  -14  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER B  -13  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PRO B  -12  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY B  -11  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB MET B  -10  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PRO B   -9  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ALA B   -8  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU B   -7  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU B   -6  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER B   -5  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU B   -4  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB VAL B   -3  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER B   -2  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU B   -1  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU B    0  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER B    1  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB VAL B    2  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU B    3  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU B    4  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB MET B    5  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY B    6  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB CYS B    7  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB VAL B    8  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ALA B    9  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLU B   10  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB THR B   11  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY B   12  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB THR B   13  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLU B  607  UNP  P0DTC2    GLN   607 CONFLICT                       
SEQADV 6VYB SER B  682  UNP  P0DTC2    ARG   682 CONFLICT                       
SEQADV 6VYB GLY B  683  UNP  P0DTC2    ARG   683 CONFLICT                       
SEQADV 6VYB GLY B  685  UNP  P0DTC2    ARG   685 CONFLICT                       
SEQADV 6VYB PRO B  986  UNP  P0DTC2    LYS   986 CONFLICT                       
SEQADV 6VYB PRO B  987  UNP  P0DTC2    VAL   987 CONFLICT                       
SEQADV 6VYB GLY B 1212  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER B 1213  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY B 1214  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ARG B 1215  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLU B 1216  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ASN B 1217  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU B 1218  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB TYR B 1219  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PHE B 1220  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLN B 1221  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY B 1222  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY B 1223  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY B 1224  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY B 1225  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER B 1226  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY B 1227  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB TYR B 1228  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ILE B 1229  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PRO B 1230  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLU B 1231  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ALA B 1232  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PRO B 1233  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ARG B 1234  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ASP B 1235  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY B 1236  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLN B 1237  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ALA B 1238  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB TYR B 1239  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB VAL B 1240  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ARG B 1241  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LYS B 1242  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ASP B 1243  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY B 1244  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLU B 1245  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB TRP B 1246  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB VAL B 1247  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU B 1248  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU B 1249  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER B 1250  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB THR B 1251  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PHE B 1252  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU B 1253  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY B 1254  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS B 1255  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS B 1256  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS B 1257  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS B 1258  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS B 1259  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS B 1260  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS B 1261  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS B 1262  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB MET C  -18  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY C  -17  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ILE C  -16  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU C  -15  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PRO C  -14  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER C  -13  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PRO C  -12  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY C  -11  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB MET C  -10  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PRO C   -9  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ALA C   -8  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU C   -7  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU C   -6  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER C   -5  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU C   -4  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB VAL C   -3  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER C   -2  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU C   -1  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU C    0  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER C    1  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB VAL C    2  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU C    3  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU C    4  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB MET C    5  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY C    6  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB CYS C    7  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB VAL C    8  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ALA C    9  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLU C   10  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB THR C   11  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY C   12  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB THR C   13  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLU C  607  UNP  P0DTC2    GLN   607 CONFLICT                       
SEQADV 6VYB SER C  682  UNP  P0DTC2    ARG   682 CONFLICT                       
SEQADV 6VYB GLY C  683  UNP  P0DTC2    ARG   683 CONFLICT                       
SEQADV 6VYB GLY C  685  UNP  P0DTC2    ARG   685 CONFLICT                       
SEQADV 6VYB PRO C  986  UNP  P0DTC2    LYS   986 CONFLICT                       
SEQADV 6VYB PRO C  987  UNP  P0DTC2    VAL   987 CONFLICT                       
SEQADV 6VYB GLY C 1212  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER C 1213  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY C 1214  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ARG C 1215  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLU C 1216  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ASN C 1217  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU C 1218  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB TYR C 1219  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PHE C 1220  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLN C 1221  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY C 1222  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY C 1223  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY C 1224  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY C 1225  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER C 1226  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY C 1227  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB TYR C 1228  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ILE C 1229  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PRO C 1230  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLU C 1231  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ALA C 1232  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PRO C 1233  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ARG C 1234  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ASP C 1235  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY C 1236  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLN C 1237  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ALA C 1238  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB TYR C 1239  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB VAL C 1240  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ARG C 1241  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LYS C 1242  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB ASP C 1243  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY C 1244  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLU C 1245  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB TRP C 1246  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB VAL C 1247  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU C 1248  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU C 1249  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB SER C 1250  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB THR C 1251  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB PHE C 1252  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB LEU C 1253  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB GLY C 1254  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS C 1255  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS C 1256  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS C 1257  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS C 1258  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS C 1259  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS C 1260  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS C 1261  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6VYB HIS C 1262  UNP  P0DTC2              EXPRESSION TAG                 
SEQRES   1 A 1281  MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU          
SEQRES   2 A 1281  SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS          
SEQRES   3 A 1281  VAL ALA GLU THR GLY THR GLN CYS VAL ASN LEU THR THR          
SEQRES   4 A 1281  ARG THR GLN LEU PRO PRO ALA TYR THR ASN SER PHE THR          
SEQRES   5 A 1281  ARG GLY VAL TYR TYR PRO ASP LYS VAL PHE ARG SER SER          
SEQRES   6 A 1281  VAL LEU HIS SER THR GLN ASP LEU PHE LEU PRO PHE PHE          
SEQRES   7 A 1281  SER ASN VAL THR TRP PHE HIS ALA ILE HIS VAL SER GLY          
SEQRES   8 A 1281  THR ASN GLY THR LYS ARG PHE ASP ASN PRO VAL LEU PRO          
SEQRES   9 A 1281  PHE ASN ASP GLY VAL TYR PHE ALA SER THR GLU LYS SER          
SEQRES  10 A 1281  ASN ILE ILE ARG GLY TRP ILE PHE GLY THR THR LEU ASP          
SEQRES  11 A 1281  SER LYS THR GLN SER LEU LEU ILE VAL ASN ASN ALA THR          
SEQRES  12 A 1281  ASN VAL VAL ILE LYS VAL CYS GLU PHE GLN PHE CYS ASN          
SEQRES  13 A 1281  ASP PRO PHE LEU GLY VAL TYR TYR HIS LYS ASN ASN LYS          
SEQRES  14 A 1281  SER TRP MET GLU SER GLU PHE ARG VAL TYR SER SER ALA          
SEQRES  15 A 1281  ASN ASN CYS THR PHE GLU TYR VAL SER GLN PRO PHE LEU          
SEQRES  16 A 1281  MET ASP LEU GLU GLY LYS GLN GLY ASN PHE LYS ASN LEU          
SEQRES  17 A 1281  ARG GLU PHE VAL PHE LYS ASN ILE ASP GLY TYR PHE LYS          
SEQRES  18 A 1281  ILE TYR SER LYS HIS THR PRO ILE ASN LEU VAL ARG ASP          
SEQRES  19 A 1281  LEU PRO GLN GLY PHE SER ALA LEU GLU PRO LEU VAL ASP          
SEQRES  20 A 1281  LEU PRO ILE GLY ILE ASN ILE THR ARG PHE GLN THR LEU          
SEQRES  21 A 1281  LEU ALA LEU HIS ARG SER TYR LEU THR PRO GLY ASP SER          
SEQRES  22 A 1281  SER SER GLY TRP THR ALA GLY ALA ALA ALA TYR TYR VAL          
SEQRES  23 A 1281  GLY TYR LEU GLN PRO ARG THR PHE LEU LEU LYS TYR ASN          
SEQRES  24 A 1281  GLU ASN GLY THR ILE THR ASP ALA VAL ASP CYS ALA LEU          
SEQRES  25 A 1281  ASP PRO LEU SER GLU THR LYS CYS THR LEU LYS SER PHE          
SEQRES  26 A 1281  THR VAL GLU LYS GLY ILE TYR GLN THR SER ASN PHE ARG          
SEQRES  27 A 1281  VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN ILE          
SEQRES  28 A 1281  THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR          
SEQRES  29 A 1281  ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE          
SEQRES  30 A 1281  SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER          
SEQRES  31 A 1281  ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO          
SEQRES  32 A 1281  THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA          
SEQRES  33 A 1281  ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE          
SEQRES  34 A 1281  ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR          
SEQRES  35 A 1281  LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP          
SEQRES  36 A 1281  ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR          
SEQRES  37 A 1281  ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS          
SEQRES  38 A 1281  PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA          
SEQRES  39 A 1281  GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS          
SEQRES  40 A 1281  TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN          
SEQRES  41 A 1281  GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER          
SEQRES  42 A 1281  PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO          
SEQRES  43 A 1281  LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL ASN          
SEQRES  44 A 1281  PHE ASN PHE ASN GLY LEU THR GLY THR GLY VAL LEU THR          
SEQRES  45 A 1281  GLU SER ASN LYS LYS PHE LEU PRO PHE GLN GLN PHE GLY          
SEQRES  46 A 1281  ARG ASP ILE ALA ASP THR THR ASP ALA VAL ARG ASP PRO          
SEQRES  47 A 1281  GLN THR LEU GLU ILE LEU ASP ILE THR PRO CYS SER PHE          
SEQRES  48 A 1281  GLY GLY VAL SER VAL ILE THR PRO GLY THR ASN THR SER          
SEQRES  49 A 1281  ASN GLU VAL ALA VAL LEU TYR GLN ASP VAL ASN CYS THR          
SEQRES  50 A 1281  GLU VAL PRO VAL ALA ILE HIS ALA ASP GLN LEU THR PRO          
SEQRES  51 A 1281  THR TRP ARG VAL TYR SER THR GLY SER ASN VAL PHE GLN          
SEQRES  52 A 1281  THR ARG ALA GLY CYS LEU ILE GLY ALA GLU HIS VAL ASN          
SEQRES  53 A 1281  ASN SER TYR GLU CYS ASP ILE PRO ILE GLY ALA GLY ILE          
SEQRES  54 A 1281  CYS ALA SER TYR GLN THR GLN THR ASN SER PRO SER GLY          
SEQRES  55 A 1281  ALA GLY SER VAL ALA SER GLN SER ILE ILE ALA TYR THR          
SEQRES  56 A 1281  MET SER LEU GLY ALA GLU ASN SER VAL ALA TYR SER ASN          
SEQRES  57 A 1281  ASN SER ILE ALA ILE PRO THR ASN PHE THR ILE SER VAL          
SEQRES  58 A 1281  THR THR GLU ILE LEU PRO VAL SER MET THR LYS THR SER          
SEQRES  59 A 1281  VAL ASP CYS THR MET TYR ILE CYS GLY ASP SER THR GLU          
SEQRES  60 A 1281  CYS SER ASN LEU LEU LEU GLN TYR GLY SER PHE CYS THR          
SEQRES  61 A 1281  GLN LEU ASN ARG ALA LEU THR GLY ILE ALA VAL GLU GLN          
SEQRES  62 A 1281  ASP LYS ASN THR GLN GLU VAL PHE ALA GLN VAL LYS GLN          
SEQRES  63 A 1281  ILE TYR LYS THR PRO PRO ILE LYS ASP PHE GLY GLY PHE          
SEQRES  64 A 1281  ASN PHE SER GLN ILE LEU PRO ASP PRO SER LYS PRO SER          
SEQRES  65 A 1281  LYS ARG SER PHE ILE GLU ASP LEU LEU PHE ASN LYS VAL          
SEQRES  66 A 1281  THR LEU ALA ASP ALA GLY PHE ILE LYS GLN TYR GLY ASP          
SEQRES  67 A 1281  CYS LEU GLY ASP ILE ALA ALA ARG ASP LEU ILE CYS ALA          
SEQRES  68 A 1281  GLN LYS PHE ASN GLY LEU THR VAL LEU PRO PRO LEU LEU          
SEQRES  69 A 1281  THR ASP GLU MET ILE ALA GLN TYR THR SER ALA LEU LEU          
SEQRES  70 A 1281  ALA GLY THR ILE THR SER GLY TRP THR PHE GLY ALA GLY          
SEQRES  71 A 1281  ALA ALA LEU GLN ILE PRO PHE ALA MET GLN MET ALA TYR          
SEQRES  72 A 1281  ARG PHE ASN GLY ILE GLY VAL THR GLN ASN VAL LEU TYR          
SEQRES  73 A 1281  GLU ASN GLN LYS LEU ILE ALA ASN GLN PHE ASN SER ALA          
SEQRES  74 A 1281  ILE GLY LYS ILE GLN ASP SER LEU SER SER THR ALA SER          
SEQRES  75 A 1281  ALA LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN ASN ALA          
SEQRES  76 A 1281  GLN ALA LEU ASN THR LEU VAL LYS GLN LEU SER SER ASN          
SEQRES  77 A 1281  PHE GLY ALA ILE SER SER VAL LEU ASN ASP ILE LEU SER          
SEQRES  78 A 1281  ARG LEU ASP PRO PRO GLU ALA GLU VAL GLN ILE ASP ARG          
SEQRES  79 A 1281  LEU ILE THR GLY ARG LEU GLN SER LEU GLN THR TYR VAL          
SEQRES  80 A 1281  THR GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG ALA SER          
SEQRES  81 A 1281  ALA ASN LEU ALA ALA THR LYS MET SER GLU CYS VAL LEU          
SEQRES  82 A 1281  GLY GLN SER LYS ARG VAL ASP PHE CYS GLY LYS GLY TYR          
SEQRES  83 A 1281  HIS LEU MET SER PHE PRO GLN SER ALA PRO HIS GLY VAL          
SEQRES  84 A 1281  VAL PHE LEU HIS VAL THR TYR VAL PRO ALA GLN GLU LYS          
SEQRES  85 A 1281  ASN PHE THR THR ALA PRO ALA ILE CYS HIS ASP GLY LYS          
SEQRES  86 A 1281  ALA HIS PHE PRO ARG GLU GLY VAL PHE VAL SER ASN GLY          
SEQRES  87 A 1281  THR HIS TRP PHE VAL THR GLN ARG ASN PHE TYR GLU PRO          
SEQRES  88 A 1281  GLN ILE ILE THR THR ASP ASN THR PHE VAL SER GLY ASN          
SEQRES  89 A 1281  CYS ASP VAL VAL ILE GLY ILE VAL ASN ASN THR VAL TYR          
SEQRES  90 A 1281  ASP PRO LEU GLN PRO GLU LEU ASP SER PHE LYS GLU GLU          
SEQRES  91 A 1281  LEU ASP LYS TYR PHE LYS ASN HIS THR SER PRO ASP VAL          
SEQRES  92 A 1281  ASP LEU GLY ASP ILE SER GLY ILE ASN ALA SER VAL VAL          
SEQRES  93 A 1281  ASN ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU VAL ALA          
SEQRES  94 A 1281  LYS ASN LEU ASN GLU SER LEU ILE ASP LEU GLN GLU LEU          
SEQRES  95 A 1281  GLY LYS TYR GLU GLN TYR ILE LYS GLY SER GLY ARG GLU          
SEQRES  96 A 1281  ASN LEU TYR PHE GLN GLY GLY GLY GLY SER GLY TYR ILE          
SEQRES  97 A 1281  PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS          
SEQRES  98 A 1281  ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY HIS          
SEQRES  99 A 1281  HIS HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B 1281  MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU          
SEQRES   2 B 1281  SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS          
SEQRES   3 B 1281  VAL ALA GLU THR GLY THR GLN CYS VAL ASN LEU THR THR          
SEQRES   4 B 1281  ARG THR GLN LEU PRO PRO ALA TYR THR ASN SER PHE THR          
SEQRES   5 B 1281  ARG GLY VAL TYR TYR PRO ASP LYS VAL PHE ARG SER SER          
SEQRES   6 B 1281  VAL LEU HIS SER THR GLN ASP LEU PHE LEU PRO PHE PHE          
SEQRES   7 B 1281  SER ASN VAL THR TRP PHE HIS ALA ILE HIS VAL SER GLY          
SEQRES   8 B 1281  THR ASN GLY THR LYS ARG PHE ASP ASN PRO VAL LEU PRO          
SEQRES   9 B 1281  PHE ASN ASP GLY VAL TYR PHE ALA SER THR GLU LYS SER          
SEQRES  10 B 1281  ASN ILE ILE ARG GLY TRP ILE PHE GLY THR THR LEU ASP          
SEQRES  11 B 1281  SER LYS THR GLN SER LEU LEU ILE VAL ASN ASN ALA THR          
SEQRES  12 B 1281  ASN VAL VAL ILE LYS VAL CYS GLU PHE GLN PHE CYS ASN          
SEQRES  13 B 1281  ASP PRO PHE LEU GLY VAL TYR TYR HIS LYS ASN ASN LYS          
SEQRES  14 B 1281  SER TRP MET GLU SER GLU PHE ARG VAL TYR SER SER ALA          
SEQRES  15 B 1281  ASN ASN CYS THR PHE GLU TYR VAL SER GLN PRO PHE LEU          
SEQRES  16 B 1281  MET ASP LEU GLU GLY LYS GLN GLY ASN PHE LYS ASN LEU          
SEQRES  17 B 1281  ARG GLU PHE VAL PHE LYS ASN ILE ASP GLY TYR PHE LYS          
SEQRES  18 B 1281  ILE TYR SER LYS HIS THR PRO ILE ASN LEU VAL ARG ASP          
SEQRES  19 B 1281  LEU PRO GLN GLY PHE SER ALA LEU GLU PRO LEU VAL ASP          
SEQRES  20 B 1281  LEU PRO ILE GLY ILE ASN ILE THR ARG PHE GLN THR LEU          
SEQRES  21 B 1281  LEU ALA LEU HIS ARG SER TYR LEU THR PRO GLY ASP SER          
SEQRES  22 B 1281  SER SER GLY TRP THR ALA GLY ALA ALA ALA TYR TYR VAL          
SEQRES  23 B 1281  GLY TYR LEU GLN PRO ARG THR PHE LEU LEU LYS TYR ASN          
SEQRES  24 B 1281  GLU ASN GLY THR ILE THR ASP ALA VAL ASP CYS ALA LEU          
SEQRES  25 B 1281  ASP PRO LEU SER GLU THR LYS CYS THR LEU LYS SER PHE          
SEQRES  26 B 1281  THR VAL GLU LYS GLY ILE TYR GLN THR SER ASN PHE ARG          
SEQRES  27 B 1281  VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN ILE          
SEQRES  28 B 1281  THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR          
SEQRES  29 B 1281  ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE          
SEQRES  30 B 1281  SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER          
SEQRES  31 B 1281  ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO          
SEQRES  32 B 1281  THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA          
SEQRES  33 B 1281  ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE          
SEQRES  34 B 1281  ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR          
SEQRES  35 B 1281  LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP          
SEQRES  36 B 1281  ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR          
SEQRES  37 B 1281  ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS          
SEQRES  38 B 1281  PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA          
SEQRES  39 B 1281  GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS          
SEQRES  40 B 1281  TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN          
SEQRES  41 B 1281  GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER          
SEQRES  42 B 1281  PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO          
SEQRES  43 B 1281  LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL ASN          
SEQRES  44 B 1281  PHE ASN PHE ASN GLY LEU THR GLY THR GLY VAL LEU THR          
SEQRES  45 B 1281  GLU SER ASN LYS LYS PHE LEU PRO PHE GLN GLN PHE GLY          
SEQRES  46 B 1281  ARG ASP ILE ALA ASP THR THR ASP ALA VAL ARG ASP PRO          
SEQRES  47 B 1281  GLN THR LEU GLU ILE LEU ASP ILE THR PRO CYS SER PHE          
SEQRES  48 B 1281  GLY GLY VAL SER VAL ILE THR PRO GLY THR ASN THR SER          
SEQRES  49 B 1281  ASN GLU VAL ALA VAL LEU TYR GLN ASP VAL ASN CYS THR          
SEQRES  50 B 1281  GLU VAL PRO VAL ALA ILE HIS ALA ASP GLN LEU THR PRO          
SEQRES  51 B 1281  THR TRP ARG VAL TYR SER THR GLY SER ASN VAL PHE GLN          
SEQRES  52 B 1281  THR ARG ALA GLY CYS LEU ILE GLY ALA GLU HIS VAL ASN          
SEQRES  53 B 1281  ASN SER TYR GLU CYS ASP ILE PRO ILE GLY ALA GLY ILE          
SEQRES  54 B 1281  CYS ALA SER TYR GLN THR GLN THR ASN SER PRO SER GLY          
SEQRES  55 B 1281  ALA GLY SER VAL ALA SER GLN SER ILE ILE ALA TYR THR          
SEQRES  56 B 1281  MET SER LEU GLY ALA GLU ASN SER VAL ALA TYR SER ASN          
SEQRES  57 B 1281  ASN SER ILE ALA ILE PRO THR ASN PHE THR ILE SER VAL          
SEQRES  58 B 1281  THR THR GLU ILE LEU PRO VAL SER MET THR LYS THR SER          
SEQRES  59 B 1281  VAL ASP CYS THR MET TYR ILE CYS GLY ASP SER THR GLU          
SEQRES  60 B 1281  CYS SER ASN LEU LEU LEU GLN TYR GLY SER PHE CYS THR          
SEQRES  61 B 1281  GLN LEU ASN ARG ALA LEU THR GLY ILE ALA VAL GLU GLN          
SEQRES  62 B 1281  ASP LYS ASN THR GLN GLU VAL PHE ALA GLN VAL LYS GLN          
SEQRES  63 B 1281  ILE TYR LYS THR PRO PRO ILE LYS ASP PHE GLY GLY PHE          
SEQRES  64 B 1281  ASN PHE SER GLN ILE LEU PRO ASP PRO SER LYS PRO SER          
SEQRES  65 B 1281  LYS ARG SER PHE ILE GLU ASP LEU LEU PHE ASN LYS VAL          
SEQRES  66 B 1281  THR LEU ALA ASP ALA GLY PHE ILE LYS GLN TYR GLY ASP          
SEQRES  67 B 1281  CYS LEU GLY ASP ILE ALA ALA ARG ASP LEU ILE CYS ALA          
SEQRES  68 B 1281  GLN LYS PHE ASN GLY LEU THR VAL LEU PRO PRO LEU LEU          
SEQRES  69 B 1281  THR ASP GLU MET ILE ALA GLN TYR THR SER ALA LEU LEU          
SEQRES  70 B 1281  ALA GLY THR ILE THR SER GLY TRP THR PHE GLY ALA GLY          
SEQRES  71 B 1281  ALA ALA LEU GLN ILE PRO PHE ALA MET GLN MET ALA TYR          
SEQRES  72 B 1281  ARG PHE ASN GLY ILE GLY VAL THR GLN ASN VAL LEU TYR          
SEQRES  73 B 1281  GLU ASN GLN LYS LEU ILE ALA ASN GLN PHE ASN SER ALA          
SEQRES  74 B 1281  ILE GLY LYS ILE GLN ASP SER LEU SER SER THR ALA SER          
SEQRES  75 B 1281  ALA LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN ASN ALA          
SEQRES  76 B 1281  GLN ALA LEU ASN THR LEU VAL LYS GLN LEU SER SER ASN          
SEQRES  77 B 1281  PHE GLY ALA ILE SER SER VAL LEU ASN ASP ILE LEU SER          
SEQRES  78 B 1281  ARG LEU ASP PRO PRO GLU ALA GLU VAL GLN ILE ASP ARG          
SEQRES  79 B 1281  LEU ILE THR GLY ARG LEU GLN SER LEU GLN THR TYR VAL          
SEQRES  80 B 1281  THR GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG ALA SER          
SEQRES  81 B 1281  ALA ASN LEU ALA ALA THR LYS MET SER GLU CYS VAL LEU          
SEQRES  82 B 1281  GLY GLN SER LYS ARG VAL ASP PHE CYS GLY LYS GLY TYR          
SEQRES  83 B 1281  HIS LEU MET SER PHE PRO GLN SER ALA PRO HIS GLY VAL          
SEQRES  84 B 1281  VAL PHE LEU HIS VAL THR TYR VAL PRO ALA GLN GLU LYS          
SEQRES  85 B 1281  ASN PHE THR THR ALA PRO ALA ILE CYS HIS ASP GLY LYS          
SEQRES  86 B 1281  ALA HIS PHE PRO ARG GLU GLY VAL PHE VAL SER ASN GLY          
SEQRES  87 B 1281  THR HIS TRP PHE VAL THR GLN ARG ASN PHE TYR GLU PRO          
SEQRES  88 B 1281  GLN ILE ILE THR THR ASP ASN THR PHE VAL SER GLY ASN          
SEQRES  89 B 1281  CYS ASP VAL VAL ILE GLY ILE VAL ASN ASN THR VAL TYR          
SEQRES  90 B 1281  ASP PRO LEU GLN PRO GLU LEU ASP SER PHE LYS GLU GLU          
SEQRES  91 B 1281  LEU ASP LYS TYR PHE LYS ASN HIS THR SER PRO ASP VAL          
SEQRES  92 B 1281  ASP LEU GLY ASP ILE SER GLY ILE ASN ALA SER VAL VAL          
SEQRES  93 B 1281  ASN ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU VAL ALA          
SEQRES  94 B 1281  LYS ASN LEU ASN GLU SER LEU ILE ASP LEU GLN GLU LEU          
SEQRES  95 B 1281  GLY LYS TYR GLU GLN TYR ILE LYS GLY SER GLY ARG GLU          
SEQRES  96 B 1281  ASN LEU TYR PHE GLN GLY GLY GLY GLY SER GLY TYR ILE          
SEQRES  97 B 1281  PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS          
SEQRES  98 B 1281  ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY HIS          
SEQRES  99 B 1281  HIS HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 C 1281  MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU          
SEQRES   2 C 1281  SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS          
SEQRES   3 C 1281  VAL ALA GLU THR GLY THR GLN CYS VAL ASN LEU THR THR          
SEQRES   4 C 1281  ARG THR GLN LEU PRO PRO ALA TYR THR ASN SER PHE THR          
SEQRES   5 C 1281  ARG GLY VAL TYR TYR PRO ASP LYS VAL PHE ARG SER SER          
SEQRES   6 C 1281  VAL LEU HIS SER THR GLN ASP LEU PHE LEU PRO PHE PHE          
SEQRES   7 C 1281  SER ASN VAL THR TRP PHE HIS ALA ILE HIS VAL SER GLY          
SEQRES   8 C 1281  THR ASN GLY THR LYS ARG PHE ASP ASN PRO VAL LEU PRO          
SEQRES   9 C 1281  PHE ASN ASP GLY VAL TYR PHE ALA SER THR GLU LYS SER          
SEQRES  10 C 1281  ASN ILE ILE ARG GLY TRP ILE PHE GLY THR THR LEU ASP          
SEQRES  11 C 1281  SER LYS THR GLN SER LEU LEU ILE VAL ASN ASN ALA THR          
SEQRES  12 C 1281  ASN VAL VAL ILE LYS VAL CYS GLU PHE GLN PHE CYS ASN          
SEQRES  13 C 1281  ASP PRO PHE LEU GLY VAL TYR TYR HIS LYS ASN ASN LYS          
SEQRES  14 C 1281  SER TRP MET GLU SER GLU PHE ARG VAL TYR SER SER ALA          
SEQRES  15 C 1281  ASN ASN CYS THR PHE GLU TYR VAL SER GLN PRO PHE LEU          
SEQRES  16 C 1281  MET ASP LEU GLU GLY LYS GLN GLY ASN PHE LYS ASN LEU          
SEQRES  17 C 1281  ARG GLU PHE VAL PHE LYS ASN ILE ASP GLY TYR PHE LYS          
SEQRES  18 C 1281  ILE TYR SER LYS HIS THR PRO ILE ASN LEU VAL ARG ASP          
SEQRES  19 C 1281  LEU PRO GLN GLY PHE SER ALA LEU GLU PRO LEU VAL ASP          
SEQRES  20 C 1281  LEU PRO ILE GLY ILE ASN ILE THR ARG PHE GLN THR LEU          
SEQRES  21 C 1281  LEU ALA LEU HIS ARG SER TYR LEU THR PRO GLY ASP SER          
SEQRES  22 C 1281  SER SER GLY TRP THR ALA GLY ALA ALA ALA TYR TYR VAL          
SEQRES  23 C 1281  GLY TYR LEU GLN PRO ARG THR PHE LEU LEU LYS TYR ASN          
SEQRES  24 C 1281  GLU ASN GLY THR ILE THR ASP ALA VAL ASP CYS ALA LEU          
SEQRES  25 C 1281  ASP PRO LEU SER GLU THR LYS CYS THR LEU LYS SER PHE          
SEQRES  26 C 1281  THR VAL GLU LYS GLY ILE TYR GLN THR SER ASN PHE ARG          
SEQRES  27 C 1281  VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN ILE          
SEQRES  28 C 1281  THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR          
SEQRES  29 C 1281  ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE          
SEQRES  30 C 1281  SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER          
SEQRES  31 C 1281  ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO          
SEQRES  32 C 1281  THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA          
SEQRES  33 C 1281  ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE          
SEQRES  34 C 1281  ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR          
SEQRES  35 C 1281  LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP          
SEQRES  36 C 1281  ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR          
SEQRES  37 C 1281  ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS          
SEQRES  38 C 1281  PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA          
SEQRES  39 C 1281  GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS          
SEQRES  40 C 1281  TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN          
SEQRES  41 C 1281  GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER          
SEQRES  42 C 1281  PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO          
SEQRES  43 C 1281  LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL ASN          
SEQRES  44 C 1281  PHE ASN PHE ASN GLY LEU THR GLY THR GLY VAL LEU THR          
SEQRES  45 C 1281  GLU SER ASN LYS LYS PHE LEU PRO PHE GLN GLN PHE GLY          
SEQRES  46 C 1281  ARG ASP ILE ALA ASP THR THR ASP ALA VAL ARG ASP PRO          
SEQRES  47 C 1281  GLN THR LEU GLU ILE LEU ASP ILE THR PRO CYS SER PHE          
SEQRES  48 C 1281  GLY GLY VAL SER VAL ILE THR PRO GLY THR ASN THR SER          
SEQRES  49 C 1281  ASN GLU VAL ALA VAL LEU TYR GLN ASP VAL ASN CYS THR          
SEQRES  50 C 1281  GLU VAL PRO VAL ALA ILE HIS ALA ASP GLN LEU THR PRO          
SEQRES  51 C 1281  THR TRP ARG VAL TYR SER THR GLY SER ASN VAL PHE GLN          
SEQRES  52 C 1281  THR ARG ALA GLY CYS LEU ILE GLY ALA GLU HIS VAL ASN          
SEQRES  53 C 1281  ASN SER TYR GLU CYS ASP ILE PRO ILE GLY ALA GLY ILE          
SEQRES  54 C 1281  CYS ALA SER TYR GLN THR GLN THR ASN SER PRO SER GLY          
SEQRES  55 C 1281  ALA GLY SER VAL ALA SER GLN SER ILE ILE ALA TYR THR          
SEQRES  56 C 1281  MET SER LEU GLY ALA GLU ASN SER VAL ALA TYR SER ASN          
SEQRES  57 C 1281  ASN SER ILE ALA ILE PRO THR ASN PHE THR ILE SER VAL          
SEQRES  58 C 1281  THR THR GLU ILE LEU PRO VAL SER MET THR LYS THR SER          
SEQRES  59 C 1281  VAL ASP CYS THR MET TYR ILE CYS GLY ASP SER THR GLU          
SEQRES  60 C 1281  CYS SER ASN LEU LEU LEU GLN TYR GLY SER PHE CYS THR          
SEQRES  61 C 1281  GLN LEU ASN ARG ALA LEU THR GLY ILE ALA VAL GLU GLN          
SEQRES  62 C 1281  ASP LYS ASN THR GLN GLU VAL PHE ALA GLN VAL LYS GLN          
SEQRES  63 C 1281  ILE TYR LYS THR PRO PRO ILE LYS ASP PHE GLY GLY PHE          
SEQRES  64 C 1281  ASN PHE SER GLN ILE LEU PRO ASP PRO SER LYS PRO SER          
SEQRES  65 C 1281  LYS ARG SER PHE ILE GLU ASP LEU LEU PHE ASN LYS VAL          
SEQRES  66 C 1281  THR LEU ALA ASP ALA GLY PHE ILE LYS GLN TYR GLY ASP          
SEQRES  67 C 1281  CYS LEU GLY ASP ILE ALA ALA ARG ASP LEU ILE CYS ALA          
SEQRES  68 C 1281  GLN LYS PHE ASN GLY LEU THR VAL LEU PRO PRO LEU LEU          
SEQRES  69 C 1281  THR ASP GLU MET ILE ALA GLN TYR THR SER ALA LEU LEU          
SEQRES  70 C 1281  ALA GLY THR ILE THR SER GLY TRP THR PHE GLY ALA GLY          
SEQRES  71 C 1281  ALA ALA LEU GLN ILE PRO PHE ALA MET GLN MET ALA TYR          
SEQRES  72 C 1281  ARG PHE ASN GLY ILE GLY VAL THR GLN ASN VAL LEU TYR          
SEQRES  73 C 1281  GLU ASN GLN LYS LEU ILE ALA ASN GLN PHE ASN SER ALA          
SEQRES  74 C 1281  ILE GLY LYS ILE GLN ASP SER LEU SER SER THR ALA SER          
SEQRES  75 C 1281  ALA LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN ASN ALA          
SEQRES  76 C 1281  GLN ALA LEU ASN THR LEU VAL LYS GLN LEU SER SER ASN          
SEQRES  77 C 1281  PHE GLY ALA ILE SER SER VAL LEU ASN ASP ILE LEU SER          
SEQRES  78 C 1281  ARG LEU ASP PRO PRO GLU ALA GLU VAL GLN ILE ASP ARG          
SEQRES  79 C 1281  LEU ILE THR GLY ARG LEU GLN SER LEU GLN THR TYR VAL          
SEQRES  80 C 1281  THR GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG ALA SER          
SEQRES  81 C 1281  ALA ASN LEU ALA ALA THR LYS MET SER GLU CYS VAL LEU          
SEQRES  82 C 1281  GLY GLN SER LYS ARG VAL ASP PHE CYS GLY LYS GLY TYR          
SEQRES  83 C 1281  HIS LEU MET SER PHE PRO GLN SER ALA PRO HIS GLY VAL          
SEQRES  84 C 1281  VAL PHE LEU HIS VAL THR TYR VAL PRO ALA GLN GLU LYS          
SEQRES  85 C 1281  ASN PHE THR THR ALA PRO ALA ILE CYS HIS ASP GLY LYS          
SEQRES  86 C 1281  ALA HIS PHE PRO ARG GLU GLY VAL PHE VAL SER ASN GLY          
SEQRES  87 C 1281  THR HIS TRP PHE VAL THR GLN ARG ASN PHE TYR GLU PRO          
SEQRES  88 C 1281  GLN ILE ILE THR THR ASP ASN THR PHE VAL SER GLY ASN          
SEQRES  89 C 1281  CYS ASP VAL VAL ILE GLY ILE VAL ASN ASN THR VAL TYR          
SEQRES  90 C 1281  ASP PRO LEU GLN PRO GLU LEU ASP SER PHE LYS GLU GLU          
SEQRES  91 C 1281  LEU ASP LYS TYR PHE LYS ASN HIS THR SER PRO ASP VAL          
SEQRES  92 C 1281  ASP LEU GLY ASP ILE SER GLY ILE ASN ALA SER VAL VAL          
SEQRES  93 C 1281  ASN ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU VAL ALA          
SEQRES  94 C 1281  LYS ASN LEU ASN GLU SER LEU ILE ASP LEU GLN GLU LEU          
SEQRES  95 C 1281  GLY LYS TYR GLU GLN TYR ILE LYS GLY SER GLY ARG GLU          
SEQRES  96 C 1281  ASN LEU TYR PHE GLN GLY GLY GLY GLY SER GLY TYR ILE          
SEQRES  97 C 1281  PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS          
SEQRES  98 C 1281  ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY HIS          
SEQRES  99 C 1281  HIS HIS HIS HIS HIS HIS HIS                                  
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    NAG  I   1      14                                                       
HET    NAG  I   2      14                                                       
HET    NAG  J   1      14                                                       
HET    NAG  J   2      14                                                       
HET    NAG  K   1      14                                                       
HET    NAG  K   2      14                                                       
HET    NAG  L   1      14                                                       
HET    NAG  L   2      14                                                       
HET    NAG  M   1      14                                                       
HET    NAG  M   2      14                                                       
HET    NAG  N   1      14                                                       
HET    NAG  N   2      14                                                       
HET    NAG  O   1      14                                                       
HET    NAG  O   2      14                                                       
HET    NAG  A1301      14                                                       
HET    NAG  A1302      14                                                       
HET    NAG  A1305      14                                                       
HET    NAG  A1306      14                                                       
HET    NAG  A1307      14                                                       
HET    NAG  A1308      14                                                       
HET    NAG  A1309      14                                                       
HET    NAG  A1310      14                                                       
HET    NAG  A1311      14                                                       
HET    NAG  A1316      14                                                       
HET    NAG  B1301      14                                                       
HET    NAG  B1302      14                                                       
HET    NAG  B1303      14                                                       
HET    NAG  B1304      14                                                       
HET    NAG  B1305      14                                                       
HET    NAG  B1306      14                                                       
HET    NAG  B1307      14                                                       
HET    NAG  B1308      14                                                       
HET    NAG  B1309      14                                                       
HET    NAG  B1310      14                                                       
HET    NAG  B1311      14                                                       
HET    NAG  B1314      14                                                       
HET    NAG  B1319      14                                                       
HET    NAG  C1301      14                                                       
HET    NAG  C1302      14                                                       
HET    NAG  C1303      14                                                       
HET    NAG  C1304      14                                                       
HET    NAG  C1305      14                                                       
HET    NAG  C1306      14                                                       
HET    NAG  C1307      14                                                       
HET    NAG  C1308      14                                                       
HET    NAG  C1309      14                                                       
HET    NAG  C1310      14                                                       
HET    NAG  C1315      14                                                       
HET    NAG  C1320      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   4  NAG    59(C8 H15 N O6)                                              
HELIX    1 AA1 ASP A  294  LEU A  303  1                                  10    
HELIX    2 AA2 PHE A  338  ASN A  343  1                                   6    
HELIX    3 AA3 ASP A  364  SER A  371  1                                   8    
HELIX    4 AA4 ASP A  405  ILE A  410  5                                   6    
HELIX    5 AA5 GLY A  416  ASN A  422  1                                   7    
HELIX    6 AA6 ASP A  737  CYS A  743  1                                   7    
HELIX    7 AA7 SER A  746  LEU A  754  1                                   9    
HELIX    8 AA8 GLN A  755  GLY A  757  5                                   3    
HELIX    9 AA9 CYS A  760  ALA A  783  1                                  24    
HELIX   10 AB1 SER A  816  ASN A  824  1                                   9    
HELIX   11 AB2 THR A  866  GLY A  885  1                                  20    
HELIX   12 AB3 TRP A  886  GLY A  891  1                                   6    
HELIX   13 AB4 PRO A  897  GLY A  908  1                                  12    
HELIX   14 AB5 GLN A  913  ASN A  919  1                                   7    
HELIX   15 AB6 ASN A  919  THR A  941  1                                  23    
HELIX   16 AB7 ALA A  942  ALA A  944  5                                   3    
HELIX   17 AB8 LEU A  945  GLN A  965  1                                  21    
HELIX   18 AB9 LEU A  966  SER A  968  5                                   3    
HELIX   19 AC1 VAL A  976  LEU A  984  1                                   9    
HELIX   20 AC2 ASP A  985  VAL A 1033  1                                  49    
HELIX   21 AC3 PRO A 1140  SER A 1147  1                                   8    
HELIX   22 AC4 ASP B  294  LEU B  303  1                                  10    
HELIX   23 AC5 PRO B  337  VAL B  341  5                                   5    
HELIX   24 AC6 TYR B  365  SER B  371  1                                   7    
HELIX   25 AC7 ASP B  405  ILE B  410  5                                   6    
HELIX   26 AC8 GLY B  416  ASN B  422  1                                   7    
HELIX   27 AC9 GLY B  502  TYR B  505  5                                   4    
HELIX   28 AD1 ASP B  737  CYS B  743  1                                   7    
HELIX   29 AD2 SER B  746  LEU B  754  1                                   9    
HELIX   30 AD3 GLN B  755  GLY B  757  5                                   3    
HELIX   31 AD4 SER B  758  ALA B  783  1                                  26    
HELIX   32 AD5 SER B  816  ASN B  824  1                                   9    
HELIX   33 AD6 THR B  866  GLY B  885  1                                  20    
HELIX   34 AD7 TRP B  886  GLY B  891  1                                   6    
HELIX   35 AD8 PRO B  897  GLY B  908  1                                  12    
HELIX   36 AD9 THR B  912  ASN B  919  1                                   8    
HELIX   37 AE1 ASN B  919  THR B  941  1                                  23    
HELIX   38 AE2 ALA B  942  ALA B  944  5                                   3    
HELIX   39 AE3 LEU B  945  GLN B  965  1                                  21    
HELIX   40 AE4 LEU B  966  SER B  968  5                                   3    
HELIX   41 AE5 VAL B  976  SER B  982  1                                   7    
HELIX   42 AE6 ASP B  985  VAL B 1033  1                                  49    
HELIX   43 AE7 PRO B 1140  SER B 1147  1                                   8    
HELIX   44 AE8 ASP C  294  LYS C  304  1                                  11    
HELIX   45 AE9 PHE C  338  ASN C  343  1                                   6    
HELIX   46 AF1 TYR C  351  TRP C  353  5                                   3    
HELIX   47 AF2 TYR C  365  SER C  371  1                                   7    
HELIX   48 AF3 ASP C  405  ILE C  410  5                                   6    
HELIX   49 AF4 GLY C  416  ASN C  422  1                                   7    
HELIX   50 AF5 GLY C  502  TYR C  505  5                                   4    
HELIX   51 AF6 ASP C  737  CYS C  743  1                                   7    
HELIX   52 AF7 SER C  746  LEU C  754  1                                   9    
HELIX   53 AF8 GLN C  755  GLY C  757  5                                   3    
HELIX   54 AF9 SER C  758  ALA C  783  1                                  26    
HELIX   55 AG1 SER C  816  ASN C  824  1                                   9    
HELIX   56 AG2 THR C  866  GLY C  885  1                                  20    
HELIX   57 AG3 TRP C  886  GLY C  891  1                                   6    
HELIX   58 AG4 PRO C  897  GLY C  908  1                                  12    
HELIX   59 AG5 GLN C  913  ASN C  919  1                                   7    
HELIX   60 AG6 ASN C  919  THR C  941  1                                  23    
HELIX   61 AG7 ALA C  942  ALA C  944  5                                   3    
HELIX   62 AG8 LEU C  945  GLN C  965  1                                  21    
HELIX   63 AG9 LEU C  966  SER C  968  5                                   3    
HELIX   64 AH1 VAL C  976  LEU C  984  1                                   9    
HELIX   65 AH2 ASP C  985  VAL C 1033  1                                  49    
HELIX   66 AH3 PRO C 1140  SER C 1147  1                                   8    
SHEET    1 AA1 7 TYR A  28  ASN A  30  0                                        
SHEET    2 AA1 7 ASN A  61  PHE A  65 -1  O  VAL A  62   N  THR A  29           
SHEET    3 AA1 7 TYR A 265  TYR A 269 -1  O  TYR A 265   N  PHE A  65           
SHEET    4 AA1 7 VAL A  90  GLU A  96 -1  N  ALA A  93   O  TYR A 266           
SHEET    5 AA1 7 ASN A 188  ILE A 197 -1  O  PHE A 192   N  PHE A  92           
SHEET    6 AA1 7 TYR A 200  PRO A 209 -1  O  THR A 208   N  LEU A 189           
SHEET    7 AA1 7 GLU A 224  LEU A 229 -1  O  VAL A 227   N  ILE A 203           
SHEET    1 AA2 3 VAL A  47  PHE A  55  0                                        
SHEET    2 AA2 3 GLN A 271  TYR A 279 -1  O  LEU A 277   N  HIS A  49           
SHEET    3 AA2 3 ILE A 285  ASP A 290 -1  O  THR A 286   N  LYS A 278           
SHEET    1 AA3 6 VAL A  83  PRO A  85  0                                        
SHEET    2 AA3 6 ARG A 237  LEU A 241 -1  O  PHE A 238   N  LEU A  84           
SHEET    3 AA3 6 GLY A 103  GLY A 107 -1  N  GLY A 103   O  LEU A 241           
SHEET    4 AA3 6 LEU A 117  ASN A 122 -1  O  LEU A 117   N  PHE A 106           
SHEET    5 AA3 6 ASN A 125  LYS A 129 -1  O  LYS A 129   N  LEU A 118           
SHEET    6 AA3 6 GLU A 169  VAL A 171 -1  O  TYR A 170   N  ILE A 128           
SHEET    1 AA4 5 GLY A 311  ARG A 319  0                                        
SHEET    2 AA4 5 PHE A 592  THR A 599 -1  O  GLY A 593   N  PHE A 318           
SHEET    3 AA4 5 ALA A 609  GLN A 613 -1  O  LEU A 611   N  SER A 596           
SHEET    4 AA4 5 GLY A 648  ILE A 651 -1  O  ILE A 651   N  VAL A 610           
SHEET    5 AA4 5 VAL A 642  THR A 645 -1  N  PHE A 643   O  LEU A 650           
SHEET    1 AA5 7 GLU A 324  ARG A 328  0                                        
SHEET    2 AA5 7 CYS A 538  PHE A 543  1  O  ASN A 540   N  GLU A 324           
SHEET    3 AA5 7 LEU A 546  GLU A 554 -1  O  LEU A 546   N  PHE A 543           
SHEET    4 AA5 7 ILE A 584  THR A 588 -1  O  THR A 588   N  VAL A 551           
SHEET    5 AA5 7 THR A 573  ARG A 577 -1  N  VAL A 576   O  LEU A 585           
SHEET    6 AA5 7 PHE A 565  ARG A 567 -1  N  GLY A 566   O  ALA A 575           
SHEET    7 AA5 7 VAL B  42  PHE B  43  1  O  PHE B  43   N  PHE A 565           
SHEET    1 AA6 5 ASN A 354  ILE A 358  0                                        
SHEET    2 AA6 5 ASN A 394  ARG A 403 -1  O  VAL A 395   N  ILE A 358           
SHEET    3 AA6 5 PRO A 507  GLU A 516 -1  O  TYR A 508   N  ILE A 402           
SHEET    4 AA6 5 GLY A 431  ASN A 437 -1  N  CYS A 432   O  LEU A 513           
SHEET    5 AA6 5 THR A 376  CYS A 379 -1  N  LYS A 378   O  VAL A 433           
SHEET    1 AA7 3 CYS A 361  VAL A 362  0                                        
SHEET    2 AA7 3 VAL A 524  CYS A 525  1  O  CYS A 525   N  CYS A 361           
SHEET    3 AA7 3 CYS A 391  PHE A 392 -1  N  PHE A 392   O  VAL A 524           
SHEET    1 AA8 2 LEU A 452  ARG A 454  0                                        
SHEET    2 AA8 2 LEU A 492  SER A 494 -1  O  GLN A 493   N  TYR A 453           
SHEET    1 AA9 4 GLU A 654  HIS A 655  0                                        
SHEET    2 AA9 4 SER A 691  THR A 696  1  O  ALA A 694   N  GLU A 654           
SHEET    3 AA9 4 ILE A 670  GLN A 675 -1  N  SER A 673   O  ILE A 693           
SHEET    4 AA9 4 ILE A 664  GLY A 667 -1  N  ILE A 664   O  ALA A 672           
SHEET    1 AB1 2 ALA A 701  GLU A 702  0                                        
SHEET    2 AB1 2 GLN B 787  ILE B 788  1  O  ILE B 788   N  ALA A 701           
SHEET    1 AB2 3 SER A 711  PRO A 728  0                                        
SHEET    2 AB2 3 GLY A1059  ALA A1078 -1  O  PHE A1062   N  GLU A 725           
SHEET    3 AB2 3 TYR A1047  ALA A1056 -1  N  MET A1050   O  VAL A1065           
SHEET    1 AB3 5 SER A 711  PRO A 728  0                                        
SHEET    2 AB3 5 GLY A1059  ALA A1078 -1  O  PHE A1062   N  GLU A 725           
SHEET    3 AB3 5 VAL A1094  SER A1097 -1  O  SER A1097   N  THR A1076           
SHEET    4 AB3 5 TRP A1102  THR A1105 -1  O  PHE A1103   N  VAL A1096           
SHEET    5 AB3 5 GLN A1113  ILE A1114 -1  O  GLN A1113   N  VAL A1104           
SHEET    1 AB4 2 LYS A 733  VAL A 736  0                                        
SHEET    2 AB4 2 LEU A 858  LEU A 861 -1  O  THR A 859   N  SER A 735           
SHEET    1 AB5 2 GLN A 787  ILE A 788  0                                        
SHEET    2 AB5 2 ALA C 701  GLU C 702  1  O  ALA C 701   N  ILE A 788           
SHEET    1 AB6 4 THR A1120  ASN A1125  0                                        
SHEET    2 AB6 4 LYS A1086  PRO A1090 -1  N  PHE A1089   O  PHE A1121           
SHEET    3 AB6 4 ILE A1081  CYS A1082 -1  N  ILE A1081   O  HIS A1088           
SHEET    4 AB6 4 VAL A1133  ASN A1134  1  O  VAL A1133   N  CYS A1082           
SHEET    1 AB7 8 TYR B  28  ASN B  30  0                                        
SHEET    2 AB7 8 ASN B  61  PHE B  65 -1  O  VAL B  62   N  THR B  29           
SHEET    3 AB7 8 ALA B 264  TYR B 269 -1  O  TYR B 265   N  PHE B  65           
SHEET    4 AB7 8 GLY B  89  GLU B  96 -1  N  ALA B  93   O  TYR B 266           
SHEET    5 AB7 8 ASN B 188  LYS B 195 -1  O  PHE B 192   N  PHE B  92           
SHEET    6 AB7 8 PHE B 201  PRO B 209 -1  O  LYS B 202   N  LYS B 195           
SHEET    7 AB7 8 ALA B 222  LEU B 229 -1  O  LEU B 229   N  PHE B 201           
SHEET    8 AB7 8 VAL B  36  TYR B  37  1  N  VAL B  36   O  LEU B 223           
SHEET    1 AB8 3 VAL B  47  PHE B  55  0                                        
SHEET    2 AB8 3 GLN B 271  TYR B 279 -1  O  LEU B 277   N  HIS B  49           
SHEET    3 AB8 3 ILE B 285  ASP B 290 -1  O  THR B 286   N  LYS B 278           
SHEET    1 AB9 6 VAL B  83  PRO B  85  0                                        
SHEET    2 AB9 6 ARG B 237  LEU B 241 -1  O  PHE B 238   N  LEU B  84           
SHEET    3 AB9 6 GLY B 103  GLY B 107 -1  N  GLY B 103   O  LEU B 241           
SHEET    4 AB9 6 LEU B 117  ASN B 122 -1  O  LEU B 117   N  PHE B 106           
SHEET    5 AB9 6 ASN B 125  LYS B 129 -1  O  LYS B 129   N  LEU B 118           
SHEET    6 AB9 6 GLU B 169  VAL B 171 -1  O  TYR B 170   N  ILE B 128           
SHEET    1 AC1 5 GLY B 311  ARG B 319  0                                        
SHEET    2 AC1 5 PHE B 592  THR B 599 -1  O  GLY B 593   N  PHE B 318           
SHEET    3 AC1 5 ALA B 609  GLN B 613 -1  O  LEU B 611   N  SER B 596           
SHEET    4 AC1 5 GLY B 648  ILE B 651 -1  O  ILE B 651   N  VAL B 610           
SHEET    5 AC1 5 VAL B 642  THR B 645 -1  N  PHE B 643   O  LEU B 650           
SHEET    1 AC2 7 SER B 325  ARG B 328  0                                        
SHEET    2 AC2 7 CYS B 538  PHE B 543  1  O  ASN B 542   N  ARG B 328           
SHEET    3 AC2 7 LEU B 546  GLU B 554 -1  O  GLY B 548   N  PHE B 541           
SHEET    4 AC2 7 ILE B 584  THR B 588 -1  O  THR B 588   N  VAL B 551           
SHEET    5 AC2 7 THR B 573  ARG B 577 -1  N  ASP B 574   O  ILE B 587           
SHEET    6 AC2 7 PHE B 565  ARG B 567 -1  N  GLY B 566   O  ALA B 575           
SHEET    7 AC2 7 VAL C  42  PHE C  43  1  O  PHE C  43   N  PHE B 565           
SHEET    1 AC3 5 ASN B 354  ILE B 358  0                                        
SHEET    2 AC3 5 VAL B 395  ARG B 403 -1  O  VAL B 395   N  ILE B 358           
SHEET    3 AC3 5 PRO B 507  SER B 514 -1  O  VAL B 510   N  PHE B 400           
SHEET    4 AC3 5 GLY B 431  ASN B 437 -1  N  CYS B 432   O  LEU B 513           
SHEET    5 AC3 5 THR B 376  CYS B 379 -1  N  LYS B 378   O  VAL B 433           
SHEET    1 AC4 3 CYS B 361  VAL B 362  0                                        
SHEET    2 AC4 3 VAL B 524  CYS B 525  1  O  CYS B 525   N  CYS B 361           
SHEET    3 AC4 3 CYS B 391  PHE B 392 -1  N  PHE B 392   O  VAL B 524           
SHEET    1 AC5 2 LEU B 452  TYR B 453  0                                        
SHEET    2 AC5 2 GLN B 493  SER B 494 -1  O  GLN B 493   N  TYR B 453           
SHEET    1 AC6 4 GLU B 654  HIS B 655  0                                        
SHEET    2 AC6 4 SER B 691  THR B 696  1  O  ALA B 694   N  GLU B 654           
SHEET    3 AC6 4 ILE B 670  GLN B 675 -1  N  SER B 673   O  ILE B 693           
SHEET    4 AC6 4 ILE B 664  GLY B 667 -1  N  ILE B 664   O  ALA B 672           
SHEET    1 AC7 2 GLU B 702  SER B 704  0                                        
SHEET    2 AC7 2 ILE C 788  LYS C 790  1  O  ILE C 788   N  ASN B 703           
SHEET    1 AC8 3 SER B 711  PRO B 728  0                                        
SHEET    2 AC8 3 GLY B1059  ALA B1078 -1  O  GLN B1071   N  THR B 716           
SHEET    3 AC8 3 TYR B1047  ALA B1056 -1  N  MET B1050   O  VAL B1065           
SHEET    1 AC9 5 SER B 711  PRO B 728  0                                        
SHEET    2 AC9 5 GLY B1059  ALA B1078 -1  O  GLN B1071   N  THR B 716           
SHEET    3 AC9 5 VAL B1094  SER B1097 -1  O  SER B1097   N  THR B1076           
SHEET    4 AC9 5 TRP B1102  THR B1105 -1  O  PHE B1103   N  VAL B1096           
SHEET    5 AC9 5 GLN B1113  ILE B1114 -1  O  GLN B1113   N  VAL B1104           
SHEET    1 AD1 2 LYS B 733  VAL B 736  0                                        
SHEET    2 AD1 2 LEU B 858  LEU B 861 -1  O  LEU B 861   N  LYS B 733           
SHEET    1 AD2 4 THR B1120  ASN B1125  0                                        
SHEET    2 AD2 4 LYS B1086  PRO B1090 -1  N  PHE B1089   O  PHE B1121           
SHEET    3 AD2 4 ILE B1081  CYS B1082 -1  N  ILE B1081   O  HIS B1088           
SHEET    4 AD2 4 VAL B1133  ASN B1134  1  O  VAL B1133   N  CYS B1082           
SHEET    1 AD3 8 TYR C  28  ASN C  30  0                                        
SHEET    2 AD3 8 ASN C  61  PHE C  65 -1  O  VAL C  62   N  THR C  29           
SHEET    3 AD3 8 TYR C 265  TYR C 269 -1  O  TYR C 265   N  PHE C  65           
SHEET    4 AD3 8 VAL C  90  GLU C  96 -1  N  ALA C  93   O  TYR C 266           
SHEET    5 AD3 8 ASN C 188  ILE C 197 -1  O  PHE C 192   N  PHE C  92           
SHEET    6 AD3 8 TYR C 200  PRO C 209 -1  O  THR C 208   N  LEU C 189           
SHEET    7 AD3 8 ALA C 222  PRO C 230 -1  O  LEU C 226   N  ILE C 203           
SHEET    8 AD3 8 VAL C  36  TYR C  37  1  N  VAL C  36   O  LEU C 223           
SHEET    1 AD4 3 VAL C  47  PHE C  55  0                                        
SHEET    2 AD4 3 GLN C 271  TYR C 279 -1  O  LEU C 277   N  HIS C  49           
SHEET    3 AD4 3 ILE C 285  ASP C 290 -1  O  THR C 286   N  LYS C 278           
SHEET    1 AD5 6 VAL C  83  PRO C  85  0                                        
SHEET    2 AD5 6 ARG C 237  LEU C 241 -1  O  PHE C 238   N  LEU C  84           
SHEET    3 AD5 6 GLY C 103  GLY C 107 -1  N  GLY C 103   O  LEU C 241           
SHEET    4 AD5 6 LEU C 117  ASN C 122 -1  O  LEU C 117   N  PHE C 106           
SHEET    5 AD5 6 ASN C 125  LYS C 129 -1  O  LYS C 129   N  LEU C 118           
SHEET    6 AD5 6 GLU C 169  VAL C 171 -1  O  TYR C 170   N  ILE C 128           
SHEET    1 AD6 5 GLY C 311  ARG C 319  0                                        
SHEET    2 AD6 5 PHE C 592  THR C 599 -1  O  GLY C 593   N  PHE C 318           
SHEET    3 AD6 5 ALA C 609  GLN C 613 -1  O  ALA C 609   N  ILE C 598           
SHEET    4 AD6 5 GLY C 648  ILE C 651 -1  O  CYS C 649   N  TYR C 612           
SHEET    5 AD6 5 VAL C 642  THR C 645 -1  N  PHE C 643   O  LEU C 650           
SHEET    1 AD7 6 GLU C 324  ARG C 328  0                                        
SHEET    2 AD7 6 CYS C 538  PHE C 543  1  O  ASN C 542   N  ARG C 328           
SHEET    3 AD7 6 LEU C 546  GLU C 554 -1  O  LEU C 546   N  PHE C 543           
SHEET    4 AD7 6 ILE C 584  THR C 588 -1  O  THR C 588   N  VAL C 551           
SHEET    5 AD7 6 THR C 573  ARG C 577 -1  N  VAL C 576   O  LEU C 585           
SHEET    6 AD7 6 PHE C 565  ARG C 567 -1  N  GLY C 566   O  ALA C 575           
SHEET    1 AD8 3 ALA C 348  SER C 349  0                                        
SHEET    2 AD8 3 ASN C 394  ARG C 403  1  O  VAL C 401   N  ALA C 348           
SHEET    3 AD8 3 ASN C 354  ILE C 358 -1  N  ILE C 358   O  VAL C 395           
SHEET    1 AD9 5 ALA C 348  SER C 349  0                                        
SHEET    2 AD9 5 ASN C 394  ARG C 403  1  O  VAL C 401   N  ALA C 348           
SHEET    3 AD9 5 PRO C 507  GLU C 516 -1  O  VAL C 510   N  PHE C 400           
SHEET    4 AD9 5 GLY C 431  ASN C 437 -1  N  CYS C 432   O  LEU C 513           
SHEET    5 AD9 5 THR C 376  CYS C 379 -1  N  LYS C 378   O  VAL C 433           
SHEET    1 AE1 3 CYS C 361  VAL C 362  0                                        
SHEET    2 AE1 3 VAL C 524  CYS C 525  1  O  CYS C 525   N  CYS C 361           
SHEET    3 AE1 3 CYS C 391  PHE C 392 -1  N  PHE C 392   O  VAL C 524           
SHEET    1 AE2 2 LEU C 452  TYR C 453  0                                        
SHEET    2 AE2 2 GLN C 493  SER C 494 -1  O  GLN C 493   N  TYR C 453           
SHEET    1 AE3 4 GLU C 654  HIS C 655  0                                        
SHEET    2 AE3 4 SER C 691  THR C 696  1  O  ALA C 694   N  GLU C 654           
SHEET    3 AE3 4 ILE C 670  GLN C 675 -1  N  SER C 673   O  ILE C 693           
SHEET    4 AE3 4 ILE C 664  GLY C 667 -1  N  ILE C 664   O  ALA C 672           
SHEET    1 AE4 4 SER C 711  PRO C 715  0                                        
SHEET    2 AE4 4 GLU C1072  ALA C1078 -1  O  PHE C1075   N  ILE C 712           
SHEET    3 AE4 4 VAL C1094  SER C1097 -1  O  SER C1097   N  THR C1076           
SHEET    4 AE4 4 TRP C1102  THR C1105 -1  O  PHE C1103   N  VAL C1096           
SHEET    1 AE5 3 PHE C 718  PRO C 728  0                                        
SHEET    2 AE5 3 GLY C1059  PRO C1069 -1  O  PHE C1062   N  GLU C 725           
SHEET    3 AE5 3 TYR C1047  ALA C1056 -1  N  MET C1050   O  VAL C1065           
SHEET    1 AE6 2 LYS C 733  VAL C 736  0                                        
SHEET    2 AE6 2 LEU C 858  LEU C 861 -1  O  LEU C 861   N  LYS C 733           
SHEET    1 AE7 4 THR C1120  ASN C1125  0                                        
SHEET    2 AE7 4 LYS C1086  PRO C1090 -1  N  PHE C1089   O  PHE C1121           
SHEET    3 AE7 4 ILE C1081  CYS C1082 -1  N  ILE C1081   O  HIS C1088           
SHEET    4 AE7 4 VAL C1133  ASN C1134  1  O  VAL C1133   N  CYS C1082           
SSBOND   1 CYS A  131    CYS A  166                          1555   1555  2.03  
SSBOND   2 CYS A  291    CYS A  301                          1555   1555  2.03  
SSBOND   3 CYS A  336    CYS A  361                          1555   1555  2.22  
SSBOND   4 CYS A  379    CYS A  432                          1555   1555  2.04  
SSBOND   5 CYS A  391    CYS A  525                          1555   1555  2.03  
SSBOND   6 CYS A  538    CYS A  590                          1555   1555  2.02  
SSBOND   7 CYS A  617    CYS A  649                          1555   1555  2.04  
SSBOND   8 CYS A  662    CYS A  671                          1555   1555  2.03  
SSBOND   9 CYS A  738    CYS A  760                          1555   1555  2.03  
SSBOND  10 CYS A  743    CYS A  749                          1555   1555  2.03  
SSBOND  11 CYS A 1032    CYS A 1043                          1555   1555  2.03  
SSBOND  12 CYS A 1082    CYS A 1126                          1555   1555  2.02  
SSBOND  13 CYS B  131    CYS B  166                          1555   1555  2.02  
SSBOND  14 CYS B  291    CYS B  301                          1555   1555  2.02  
SSBOND  15 CYS B  379    CYS B  432                          1555   1555  2.03  
SSBOND  16 CYS B  391    CYS B  525                          1555   1555  2.04  
SSBOND  17 CYS B  538    CYS B  590                          1555   1555  2.02  
SSBOND  18 CYS B  617    CYS B  649                          1555   1555  2.05  
SSBOND  19 CYS B  662    CYS B  671                          1555   1555  2.03  
SSBOND  20 CYS B  738    CYS B  760                          1555   1555  2.02  
SSBOND  21 CYS B  743    CYS B  749                          1555   1555  2.03  
SSBOND  22 CYS B 1032    CYS B 1043                          1555   1555  2.03  
SSBOND  23 CYS B 1082    CYS B 1126                          1555   1555  2.02  
SSBOND  24 CYS C  131    CYS C  166                          1555   1555  2.02  
SSBOND  25 CYS C  291    CYS C  301                          1555   1555  2.02  
SSBOND  26 CYS C  336    CYS C  361                          1555   1555  2.20  
SSBOND  27 CYS C  379    CYS C  432                          1555   1555  2.03  
SSBOND  28 CYS C  391    CYS C  525                          1555   1555  2.02  
SSBOND  29 CYS C  538    CYS C  590                          1555   1555  2.04  
SSBOND  30 CYS C  617    CYS C  649                          1555   1555  2.03  
SSBOND  31 CYS C  662    CYS C  671                          1555   1555  2.03  
SSBOND  32 CYS C  738    CYS C  760                          1555   1555  2.02  
SSBOND  33 CYS C  743    CYS C  749                          1555   1555  2.04  
SSBOND  34 CYS C 1032    CYS C 1043                          1555   1555  2.02  
SSBOND  35 CYS C 1082    CYS C 1126                          1555   1555  2.02  
LINK         ND2 ASN A  61                 C1  NAG A1301     1555   1555  1.51  
LINK         ND2 ASN A 122                 C1  NAG A1302     1555   1555  1.51  
LINK         ND2 ASN A 234                 C1  NAG D   1     1555   1555  1.50  
LINK         ND2 ASN A 282                 C1  NAG A1305     1555   1555  1.51  
LINK         ND2 ASN A 331                 C1  NAG A1306     1555   1555  1.52  
LINK         ND2 ASN A 343                 C1  NAG A1307     1555   1555  1.51  
LINK         ND2 ASN A 603                 C1  NAG A1308     1555   1555  1.51  
LINK         ND2 ASN A 616                 C1  NAG A1309     1555   1555  1.50  
LINK         ND2 ASN A 657                 C1  NAG A1310     1555   1555  1.51  
LINK         ND2 ASN A 709                 C1  NAG A1311     1555   1555  1.51  
LINK         ND2 ASN A 717                 C1  NAG E   1     1555   1555  1.50  
LINK         ND2 ASN A 801                 C1  NAG F   1     1555   1555  1.50  
LINK         ND2 ASN A1074                 C1  NAG A1316     1555   1555  1.51  
LINK         ND2 ASN A1098                 C1  NAG G   1     1555   1555  1.51  
LINK         ND2 ASN A1134                 C1  NAG H   1     1555   1555  1.51  
LINK         ND2 ASN B  61                 C1  NAG B1301     1555   1555  1.51  
LINK         ND2 ASN B 122                 C1  NAG B1302     1555   1555  1.50  
LINK         ND2 ASN B 165                 C1  NAG B1319     1555   1555  1.51  
LINK         ND2 ASN B 234                 C1  NAG B1303     1555   1555  1.51  
LINK         ND2 ASN B 282                 C1  NAG B1304     1555   1555  1.51  
LINK         ND2 ASN B 331                 C1  NAG B1305     1555   1555  1.51  
LINK         ND2 ASN B 343                 C1  NAG B1306     1555   1555  1.54  
LINK         ND2 ASN B 603                 C1  NAG B1307     1555   1555  1.50  
LINK         ND2 ASN B 616                 C1  NAG B1308     1555   1555  1.50  
LINK         ND2 ASN B 657                 C1  NAG B1309     1555   1555  1.51  
LINK         ND2 ASN B 709                 C1  NAG B1310     1555   1555  1.51  
LINK         ND2 ASN B 717                 C1  NAG B1311     1555   1555  1.51  
LINK         ND2 ASN B 801                 C1  NAG I   1     1555   1555  1.50  
LINK         ND2 ASN B1074                 C1  NAG B1314     1555   1555  1.51  
LINK         ND2 ASN B1098                 C1  NAG J   1     1555   1555  1.51  
LINK         ND2 ASN B1134                 C1  NAG K   1     1555   1555  1.50  
LINK         ND2 ASN C  61                 C1  NAG C1301     1555   1555  1.51  
LINK         ND2 ASN C 122                 C1  NAG C1302     1555   1555  1.51  
LINK         ND2 ASN C 165                 C1  NAG C1320     1555   1555  1.51  
LINK         ND2 ASN C 234                 C1  NAG C1303     1555   1555  1.51  
LINK         ND2 ASN C 282                 C1  NAG C1304     1555   1555  1.51  
LINK         ND2 ASN C 331                 C1  NAG C1305     1555   1555  1.51  
LINK         ND2 ASN C 343                 C1  NAG C1306     1555   1555  1.50  
LINK         ND2 ASN C 603                 C1  NAG C1307     1555   1555  1.50  
LINK         ND2 ASN C 616                 C1  NAG C1308     1555   1555  1.51  
LINK         ND2 ASN C 657                 C1  NAG C1309     1555   1555  1.51  
LINK         ND2 ASN C 709                 C1  NAG C1310     1555   1555  1.50  
LINK         ND2 ASN C 717                 C1  NAG L   1     1555   1555  1.50  
LINK         ND2 ASN C 801                 C1  NAG M   1     1555   1555  1.50  
LINK         ND2 ASN C1074                 C1  NAG C1315     1555   1555  1.51  
LINK         ND2 ASN C1098                 C1  NAG N   1     1555   1555  1.50  
LINK         ND2 ASN C1134                 C1  NAG O   1     1555   1555  1.50  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.50  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.50  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.50  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.50  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.51  
LINK         O4  NAG I   1                 C1  NAG I   2     1555   1555  1.51  
LINK         O4  NAG J   1                 C1  NAG J   2     1555   1555  1.50  
LINK         O4  NAG K   1                 C1  NAG K   2     1555   1555  1.50  
LINK         O4  NAG L   1                 C1  NAG L   2     1555   1555  1.50  
LINK         O4  NAG M   1                 C1  NAG M   2     1555   1555  1.50  
LINK         O4  NAG N   1                 C1  NAG N   2     1555   1555  1.49  
LINK         O4  NAG O   1                 C1  NAG O   2     1555   1555  1.51  
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  N   ALA A  27     168.198 250.462 221.646  1.00 53.77           N  
ATOM      2  CA  ALA A  27     169.041 250.950 220.564  1.00 53.32           C  
ATOM      3  C   ALA A  27     170.297 250.086 220.460  1.00 52.13           C  
ATOM      4  O   ALA A  27     170.866 249.691 221.484  1.00 52.61           O  
ATOM      5  CB  ALA A  27     169.425 252.421 220.786  1.00 53.23           C  
ATOM      6  N   TYR A  28     170.705 249.776 219.218  1.00 52.34           N  
ATOM      7  CA  TYR A  28     171.876 248.950 218.915  1.00 50.90           C  
ATOM      8  C   TYR A  28     172.700 249.550 217.798  1.00 52.75           C  
ATOM      9  O   TYR A  28     172.173 250.267 216.945  1.00 52.34           O  
ATOM     10  CB  TYR A  28     171.451 247.547 218.532  1.00 51.97           C  
ATOM     11  CG  TYR A  28     170.737 246.835 219.622  1.00 52.60           C  
ATOM     12  CD1 TYR A  28     169.373 246.951 219.737  1.00 53.23           C  
ATOM     13  CD2 TYR A  28     171.443 246.063 220.514  1.00 54.19           C  
ATOM     14  CE1 TYR A  28     168.714 246.297 220.744  1.00 53.60           C  
ATOM     15  CE2 TYR A  28     170.787 245.404 221.520  1.00 52.79           C  
ATOM     16  CZ  TYR A  28     169.427 245.521 221.638  1.00 53.43           C  
ATOM     17  OH  TYR A  28     168.765 244.865 222.643  1.00 54.16           O  
ATOM     18  N   THR A  29     173.992 249.243 217.797  1.00 52.76           N  
ATOM     19  CA  THR A  29     174.892 249.685 216.740  1.00 52.08           C  
ATOM     20  C   THR A  29     175.774 248.566 216.207  1.00 52.21           C  
ATOM     21  O   THR A  29     175.867 247.478 216.783  1.00 52.05           O  
ATOM     22  CB  THR A  29     175.778 250.863 217.199  1.00 52.19           C  
ATOM     23  OG1 THR A  29     176.605 250.453 218.289  1.00 51.99           O  
ATOM     24  CG2 THR A  29     174.918 252.021 217.627  1.00 52.92           C  
ATOM     25  N   ASN A  30     176.409 248.863 215.083  1.00 51.53           N  
ATOM     26  CA  ASN A  30     177.347 247.992 214.388  1.00 51.08           C  
ATOM     27  C   ASN A  30     178.752 248.181 214.957  1.00 50.44           C  
ATOM     28  O   ASN A  30     179.272 249.294 214.955  1.00 50.39           O  
ATOM     29  CB  ASN A  30     177.302 248.311 212.902  1.00 50.84           C  
ATOM     30  CG  ASN A  30     178.052 247.357 212.031  1.00 50.09           C  
ATOM     31  OD1 ASN A  30     179.044 246.737 212.420  1.00 50.40           O  
ATOM     32  ND2 ASN A  30     177.577 247.223 210.814  1.00 50.82           N  
ATOM     33  N   SER A  31     179.353 247.120 215.494  1.00 49.63           N  
ATOM     34  CA  SER A  31     180.688 247.237 216.091  1.00 49.54           C  
ATOM     35  C   SER A  31     181.785 247.389 215.039  1.00 48.82           C  
ATOM     36  O   SER A  31     182.939 247.674 215.367  1.00 49.89           O  
ATOM     37  CB  SER A  31     181.011 246.027 216.933  1.00 49.30           C  
ATOM     38  OG  SER A  31     181.261 244.909 216.130  1.00 49.08           O  
ATOM     39  N   PHE A  32     181.428 247.148 213.789  1.00 49.71           N  
ATOM     40  CA  PHE A  32     182.341 247.192 212.660  1.00 50.08           C  
ATOM     41  C   PHE A  32     183.582 246.351 212.909  1.00 47.22           C  
ATOM     42  O   PHE A  32     183.487 245.153 213.164  1.00 43.75           O  
ATOM     43  CB  PHE A  32     182.740 248.629 212.340  1.00 48.79           C  
ATOM     44  CG  PHE A  32     181.612 249.476 211.896  1.00 50.90           C  
ATOM     45  CD1 PHE A  32     181.171 250.518 212.679  1.00 50.92           C  
ATOM     46  CD2 PHE A  32     180.981 249.236 210.695  1.00 51.07           C  
ATOM     47  CE1 PHE A  32     180.126 251.308 212.274  1.00 51.36           C  
ATOM     48  CE2 PHE A  32     179.934 250.021 210.283  1.00 50.85           C  
ATOM     49  CZ  PHE A  32     179.506 251.059 211.074  1.00 51.50           C  
ATOM     50  N   THR A  33     184.753 246.972 212.851  1.00 49.35           N  
ATOM     51  CA  THR A  33     186.003 246.246 213.011  1.00 47.97           C  
ATOM     52  C   THR A  33     186.707 246.599 214.308  1.00 48.05           C  
ATOM     53  O   THR A  33     187.896 246.336 214.475  1.00 48.86           O  
ATOM     54  CB  THR A  33     186.928 246.505 211.823  1.00 48.46           C  
ATOM     55  OG1 THR A  33     187.181 247.908 211.714  1.00 48.92           O  
ATOM     56  CG2 THR A  33     186.263 246.008 210.554  1.00 49.10           C  
ATOM     57  N   ARG A  34     185.982 247.229 215.217  1.00 48.26           N  
ATOM     58  CA  ARG A  34     186.535 247.589 216.510  1.00 48.24           C  
ATOM     59  C   ARG A  34     186.499 246.357 217.400  1.00 48.15           C  
ATOM     60  O   ARG A  34     185.730 245.434 217.140  1.00 47.85           O  
ATOM     61  CB  ARG A  34     185.755 248.740 217.120  1.00 48.64           C  
ATOM     62  CG  ARG A  34     185.865 250.030 216.321  1.00 49.38           C  
ATOM     63  CD  ARG A  34     185.163 251.168 216.950  1.00 50.43           C  
ATOM     64  NE  ARG A  34     185.287 252.368 216.144  1.00 51.73           N  
ATOM     65  CZ  ARG A  34     186.319 253.233 216.178  1.00 52.06           C  
ATOM     66  NH1 ARG A  34     187.348 253.070 216.993  1.00 51.86           N  
ATOM     67  NH2 ARG A  34     186.282 254.260 215.370  1.00 52.59           N  
ATOM     68  N   GLY A  35     187.327 246.319 218.442  1.00 48.88           N  
ATOM     69  CA  GLY A  35     187.308 245.144 219.309  1.00 49.02           C  
ATOM     70  C   GLY A  35     188.658 244.473 219.471  1.00 48.85           C  
ATOM     71  O   GLY A  35     188.800 243.530 220.254  1.00 48.71           O  
ATOM     72  N   VAL A  36     189.631 244.946 218.710  1.00 48.30           N  
ATOM     73  CA  VAL A  36     190.985 244.424 218.739  1.00 48.53           C  
ATOM     74  C   VAL A  36     191.864 245.180 219.708  1.00 48.93           C  
ATOM     75  O   VAL A  36     191.762 246.397 219.851  1.00 49.58           O  
ATOM     76  CB  VAL A  36     191.601 244.426 217.330  1.00 48.25           C  
ATOM     77  CG1 VAL A  36     193.084 244.040 217.374  1.00 47.97           C  
ATOM     78  CG2 VAL A  36     190.845 243.419 216.480  1.00 48.27           C  
ATOM     79  N   TYR A  37     192.703 244.432 220.389  1.00 48.61           N  
ATOM     80  CA  TYR A  37     193.676 244.953 221.318  1.00 48.67           C  
ATOM     81  C   TYR A  37     194.904 244.071 221.262  1.00 48.72           C  
ATOM     82  O   TYR A  37     194.844 242.947 220.767  1.00 49.14           O  
ATOM     83  CB  TYR A  37     193.101 245.005 222.725  1.00 48.45           C  
ATOM     84  CG  TYR A  37     192.728 243.689 223.220  1.00 47.58           C  
ATOM     85  CD1 TYR A  37     193.644 242.921 223.865  1.00 49.63           C  
ATOM     86  CD2 TYR A  37     191.458 243.242 223.032  1.00 48.57           C  
ATOM     87  CE1 TYR A  37     193.301 241.694 224.325  1.00 49.13           C  
ATOM     88  CE2 TYR A  37     191.103 242.020 223.491  1.00 48.31           C  
ATOM     89  CZ  TYR A  37     192.022 241.244 224.136  1.00 48.37           C  
ATOM     90  OH  TYR A  37     191.667 240.020 224.596  1.00 48.66           O  
ATOM     91  N   TYR A  38     196.017 244.572 221.760  1.00 48.04           N  
ATOM     92  CA  TYR A  38     197.240 243.793 221.743  1.00 47.42           C  
ATOM     93  C   TYR A  38     197.098 242.604 222.688  1.00 47.40           C  
ATOM     94  O   TYR A  38     196.945 242.803 223.890  1.00 49.15           O  
ATOM     95  CB  TYR A  38     198.415 244.666 222.169  1.00 47.78           C  
ATOM     96  CG  TYR A  38     198.761 245.725 221.168  1.00 47.54           C  
ATOM     97  CD1 TYR A  38     198.085 246.913 221.180  1.00 48.09           C  
ATOM     98  CD2 TYR A  38     199.759 245.515 220.252  1.00 47.45           C  
ATOM     99  CE1 TYR A  38     198.380 247.890 220.283  1.00 47.80           C  
ATOM    100  CE2 TYR A  38     200.067 246.503 219.348  1.00 46.73           C  
ATOM    101  CZ  TYR A  38     199.374 247.684 219.364  1.00 46.53           C  
ATOM    102  OH  TYR A  38     199.682 248.667 218.471  1.00 46.44           O  
ATOM    103  N   PRO A  39     197.172 241.361 222.188  1.00 47.70           N  
ATOM    104  CA  PRO A  39     196.938 240.131 222.928  1.00 47.65           C  
ATOM    105  C   PRO A  39     197.998 239.887 223.994  1.00 48.28           C  
ATOM    106  O   PRO A  39     197.774 239.148 224.951  1.00 48.62           O  
ATOM    107  CB  PRO A  39     197.008 239.068 221.828  1.00 47.44           C  
ATOM    108  CG  PRO A  39     197.880 239.686 220.754  1.00 47.66           C  
ATOM    109  CD  PRO A  39     197.567 241.159 220.792  1.00 47.67           C  
ATOM    110  N   ASP A  40     199.156 240.510 223.823  1.00 48.39           N  
ATOM    111  CA  ASP A  40     200.252 240.371 224.764  1.00 48.40           C  
ATOM    112  C   ASP A  40     201.106 241.631 224.738  1.00 48.54           C  
ATOM    113  O   ASP A  40     200.677 242.670 224.233  1.00 48.81           O  
ATOM    114  CB  ASP A  40     201.076 239.112 224.482  1.00 48.26           C  
ATOM    115  CG  ASP A  40     201.787 239.115 223.155  1.00 47.71           C  
ATOM    116  OD1 ASP A  40     202.036 240.173 222.617  1.00 47.65           O  
ATOM    117  OD2 ASP A  40     202.090 238.044 222.676  1.00 47.35           O  
ATOM    118  N   LYS A  41     202.288 241.560 225.333  1.00 48.98           N  
ATOM    119  CA  LYS A  41     203.150 242.722 225.451  1.00 49.03           C  
ATOM    120  C   LYS A  41     204.472 242.531 224.712  1.00 49.84           C  
ATOM    121  O   LYS A  41     205.506 243.053 225.128  1.00 49.84           O  
ATOM    122  CB  LYS A  41     203.378 243.039 226.923  1.00 50.96           C  
ATOM    123  CG  LYS A  41     202.091 243.418 227.686  1.00 50.95           C  
ATOM    124  CD  LYS A  41     202.390 243.782 229.125  1.00 52.20           C  
ATOM    125  CE  LYS A  41     201.196 244.414 229.823  1.00 52.26           C  
ATOM    126  NZ  LYS A  41     200.157 243.407 230.145  1.00 51.11           N  
ATOM    127  N   VAL A  42     204.445 241.753 223.633  1.00 48.75           N  
ATOM    128  CA  VAL A  42     205.641 241.494 222.838  1.00 47.39           C  
ATOM    129  C   VAL A  42     205.671 242.345 221.578  1.00 46.44           C  
ATOM    130  O   VAL A  42     204.673 242.453 220.866  1.00 48.22           O  
ATOM    131  CB  VAL A  42     205.715 240.007 222.469  1.00 46.72           C  
ATOM    132  CG1 VAL A  42     206.900 239.737 221.564  1.00 47.33           C  
ATOM    133  CG2 VAL A  42     205.831 239.190 223.737  1.00 47.36           C  
ATOM    134  N   PHE A  43     206.807 242.961 221.301  1.00 46.28           N  
ATOM    135  CA  PHE A  43     206.918 243.763 220.093  1.00 46.77           C  
ATOM    136  C   PHE A  43     207.055 242.896 218.853  1.00 47.21           C  
ATOM    137  O   PHE A  43     207.886 241.988 218.785  1.00 48.24           O  
ATOM    138  CB  PHE A  43     208.090 244.734 220.170  1.00 49.64           C  
ATOM    139  CG  PHE A  43     208.244 245.566 218.934  1.00 47.38           C  
ATOM    140  CD1 PHE A  43     207.505 246.708 218.752  1.00 47.74           C  
ATOM    141  CD2 PHE A  43     209.122 245.197 217.944  1.00 47.63           C  
ATOM    142  CE1 PHE A  43     207.644 247.465 217.620  1.00 47.00           C  
ATOM    143  CE2 PHE A  43     209.258 245.952 216.809  1.00 47.17           C  
ATOM    144  CZ  PHE A  43     208.518 247.089 216.649  1.00 46.98           C  
ATOM    145  N   ARG A  44     206.246 243.203 217.857  1.00 46.33           N  
ATOM    146  CA  ARG A  44     206.275 242.522 216.577  1.00 45.37           C  
ATOM    147  C   ARG A  44     206.186 243.571 215.503  1.00 45.10           C  
ATOM    148  O   ARG A  44     205.625 244.631 215.748  1.00 47.05           O  
ATOM    149  CB  ARG A  44     205.110 241.566 216.437  1.00 45.43           C  
ATOM    150  CG  ARG A  44     205.091 240.432 217.416  1.00 45.53           C  
ATOM    151  CD  ARG A  44     203.933 239.537 217.181  1.00 45.00           C  
ATOM    152  NE  ARG A  44     203.918 238.425 218.108  1.00 44.53           N  
ATOM    153  CZ  ARG A  44     203.447 238.509 219.367  1.00 45.22           C  
ATOM    154  NH1 ARG A  44     202.980 239.655 219.812  1.00 46.16           N  
ATOM    155  NH2 ARG A  44     203.454 237.456 220.159  1.00 44.75           N  
ATOM    156  N   SER A  45     206.708 243.289 214.321  1.00 45.12           N  
ATOM    157  CA  SER A  45     206.558 244.231 213.221  1.00 44.11           C  
ATOM    158  C   SER A  45     206.550 243.520 211.887  1.00 44.13           C  
ATOM    159  O   SER A  45     207.129 242.442 211.747  1.00 44.37           O  
ATOM    160  CB  SER A  45     207.666 245.256 213.257  1.00 45.51           C  
ATOM    161  OG  SER A  45     208.907 244.656 213.042  1.00 45.37           O  
ATOM    162  N   SER A  46     205.886 244.131 210.911  1.00 44.59           N  
ATOM    163  CA  SER A  46     205.830 243.610 209.547  1.00 44.14           C  
ATOM    164  C   SER A  46     205.477 242.127 209.527  1.00 43.47           C  
ATOM    165  O   SER A  46     206.160 241.326 208.887  1.00 43.84           O  
ATOM    166  CB  SER A  46     207.154 243.829 208.847  1.00 44.27           C  
ATOM    167  OG  SER A  46     207.460 245.192 208.764  1.00 44.34           O  
ATOM    168  N   VAL A  47     204.438 241.752 210.260  1.00 43.19           N  
ATOM    169  CA  VAL A  47     204.077 240.345 210.368  1.00 42.94           C  
ATOM    170  C   VAL A  47     202.589 240.118 210.547  1.00 42.68           C  
ATOM    171  O   VAL A  47     201.900 240.903 211.201  1.00 42.89           O  
ATOM    172  CB  VAL A  47     204.854 239.701 211.540  1.00 42.94           C  
ATOM    173  CG1 VAL A  47     204.447 240.338 212.846  1.00 43.79           C  
ATOM    174  CG2 VAL A  47     204.611 238.186 211.601  1.00 42.48           C  
ATOM    175  N   LEU A  48     202.101 239.011 210.002  1.00 42.77           N  
ATOM    176  CA  LEU A  48     200.727 238.601 210.229  1.00 42.69           C  
ATOM    177  C   LEU A  48     200.726 237.516 211.293  1.00 42.42           C  
ATOM    178  O   LEU A  48     201.252 236.423 211.079  1.00 42.60           O  
ATOM    179  CB  LEU A  48     200.104 238.085 208.936  1.00 42.32           C  
ATOM    180  CG  LEU A  48     200.235 239.003 207.720  1.00 42.77           C  
ATOM    181  CD1 LEU A  48     199.520 238.369 206.572  1.00 42.65           C  
ATOM    182  CD2 LEU A  48     199.678 240.367 208.029  1.00 42.92           C  
ATOM    183  N   HIS A  49     200.177 237.834 212.454  1.00 42.57           N  
ATOM    184  CA  HIS A  49     200.230 236.943 213.605  1.00 42.51           C  
ATOM    185  C   HIS A  49     198.867 236.396 213.995  1.00 42.77           C  
ATOM    186  O   HIS A  49     197.916 237.150 214.186  1.00 43.00           O  
ATOM    187  CB  HIS A  49     200.838 237.675 214.797  1.00 42.85           C  
ATOM    188  CG  HIS A  49     200.906 236.857 216.023  1.00 43.24           C  
ATOM    189  ND1 HIS A  49     201.778 235.805 216.166  1.00 43.37           N  
ATOM    190  CD2 HIS A  49     200.210 236.931 217.176  1.00 43.77           C  
ATOM    191  CE1 HIS A  49     201.612 235.261 217.356  1.00 43.44           C  
ATOM    192  NE2 HIS A  49     200.668 235.927 217.989  1.00 43.64           N  
ATOM    193  N   SER A  50     198.771 235.078 214.106  1.00 42.84           N  
ATOM    194  CA  SER A  50     197.517 234.431 214.480  1.00 42.86           C  
ATOM    195  C   SER A  50     197.435 234.203 215.978  1.00 43.12           C  
ATOM    196  O   SER A  50     198.332 233.601 216.570  1.00 43.46           O  
ATOM    197  CB  SER A  50     197.366 233.112 213.761  1.00 42.33           C  
ATOM    198  OG  SER A  50     196.254 232.411 214.242  1.00 42.99           O  
ATOM    199  N   THR A  51     196.355 234.674 216.588  1.00 43.47           N  
ATOM    200  CA  THR A  51     196.176 234.542 218.029  1.00 43.84           C  
ATOM    201  C   THR A  51     194.724 234.283 218.416  1.00 44.59           C  
ATOM    202  O   THR A  51     193.800 234.696 217.714  1.00 45.87           O  
ATOM    203  CB  THR A  51     196.667 235.816 218.737  1.00 44.59           C  
ATOM    204  OG1 THR A  51     196.641 235.621 220.153  1.00 44.89           O  
ATOM    205  CG2 THR A  51     195.771 236.992 218.377  1.00 44.51           C  
ATOM    206  N   GLN A  52     194.515 233.623 219.551  1.00 44.88           N  
ATOM    207  CA  GLN A  52     193.163 233.436 220.070  1.00 45.23           C  
ATOM    208  C   GLN A  52     193.037 234.068 221.438  1.00 46.49           C  
ATOM    209  O   GLN A  52     193.856 233.821 222.322  1.00 46.63           O  
ATOM    210  CB  GLN A  52     192.782 231.961 220.156  1.00 45.70           C  
ATOM    211  CG  GLN A  52     191.356 231.735 220.665  1.00 46.25           C  
ATOM    212  CD  GLN A  52     190.974 230.286 220.664  1.00 46.65           C  
ATOM    213  OE1 GLN A  52     191.851 229.418 220.678  1.00 45.90           O  
ATOM    214  NE2 GLN A  52     189.676 229.995 220.646  1.00 47.75           N  
ATOM    215  N   ASP A  53     192.021 234.898 221.599  1.00 46.54           N  
ATOM    216  CA  ASP A  53     191.793 235.598 222.858  1.00 47.56           C  
ATOM    217  C   ASP A  53     190.357 236.070 222.895  1.00 49.15           C  
ATOM    218  O   ASP A  53     189.609 235.861 221.943  1.00 47.63           O  
ATOM    219  CB  ASP A  53     192.767 236.782 223.016  1.00 48.14           C  
ATOM    220  CG  ASP A  53     193.105 237.166 224.481  1.00 48.84           C  
ATOM    221  OD1 ASP A  53     192.267 236.991 225.358  1.00 49.37           O  
ATOM    222  OD2 ASP A  53     194.190 237.644 224.701  1.00 48.83           O  
ATOM    223  N   LEU A  54     189.969 236.729 223.964  1.00 48.17           N  
ATOM    224  CA  LEU A  54     188.618 237.241 224.032  1.00 48.72           C  
ATOM    225  C   LEU A  54     188.551 238.601 223.360  1.00 47.72           C  
ATOM    226  O   LEU A  54     189.051 239.594 223.884  1.00 49.90           O  
ATOM    227  CB  LEU A  54     188.169 237.363 225.490  1.00 49.50           C  
ATOM    228  CG  LEU A  54     188.202 236.095 226.335  1.00 50.07           C  
ATOM    229  CD1 LEU A  54     187.789 236.453 227.744  1.00 52.75           C  
ATOM    230  CD2 LEU A  54     187.264 235.057 225.746  1.00 49.56           C  
ATOM    231  N   PHE A  55     187.940 238.634 222.186  1.00 49.33           N  
ATOM    232  CA  PHE A  55     187.851 239.841 221.371  1.00 48.67           C  
ATOM    233  C   PHE A  55     186.403 240.130 221.050  1.00 48.47           C  
ATOM    234  O   PHE A  55     185.572 239.224 221.075  1.00 48.68           O  
ATOM    235  CB  PHE A  55     188.585 239.695 220.046  1.00 47.46           C  
ATOM    236  CG  PHE A  55     190.078 239.508 220.084  1.00 47.97           C  
ATOM    237  CD1 PHE A  55     190.639 238.251 220.003  1.00 46.87           C  
ATOM    238  CD2 PHE A  55     190.917 240.595 220.160  1.00 48.35           C  
ATOM    239  CE1 PHE A  55     192.005 238.087 219.992  1.00 46.50           C  
ATOM    240  CE2 PHE A  55     192.287 240.435 220.156  1.00 47.46           C  
ATOM    241  CZ  PHE A  55     192.827 239.177 220.070  1.00 46.73           C  
ATOM    242  N   LEU A  56     186.082 241.379 220.751  1.00 48.40           N  
ATOM    243  CA  LEU A  56     184.719 241.664 220.328  1.00 48.43           C  
ATOM    244  C   LEU A  56     184.598 241.204 218.872  1.00 48.61           C  
ATOM    245  O   LEU A  56     185.382 241.657 218.041  1.00 49.00           O  
ATOM    246  CB  LEU A  56     184.425 243.163 220.422  1.00 49.21           C  
ATOM    247  CG  LEU A  56     183.010 243.629 220.103  1.00 49.35           C  
ATOM    248  CD1 LEU A  56     182.063 243.167 221.178  1.00 50.19           C  
ATOM    249  CD2 LEU A  56     183.006 245.137 219.984  1.00 49.30           C  
ATOM    250  N   PRO A  57     183.670 240.304 218.514  1.00 47.98           N  
ATOM    251  CA  PRO A  57     183.502 239.787 217.169  1.00 47.12           C  
ATOM    252  C   PRO A  57     183.243 240.935 216.220  1.00 47.09           C  
ATOM    253  O   PRO A  57     182.606 241.916 216.597  1.00 48.37           O  
ATOM    254  CB  PRO A  57     182.275 238.883 217.302  1.00 47.34           C  
ATOM    255  CG  PRO A  57     182.230 238.512 218.760  1.00 47.79           C  
ATOM    256  CD  PRO A  57     182.745 239.727 219.496  1.00 48.62           C  
ATOM    257  N   PHE A  58     183.714 240.816 214.992  1.00 46.78           N  
ATOM    258  CA  PHE A  58     183.485 241.879 214.027  1.00 46.98           C  
ATOM    259  C   PHE A  58     182.043 241.919 213.574  1.00 47.74           C  
ATOM    260  O   PHE A  58     181.371 240.892 213.480  1.00 47.45           O  
ATOM    261  CB  PHE A  58     184.423 241.747 212.836  1.00 47.50           C  
ATOM    262  CG  PHE A  58     185.828 242.217 213.084  1.00 46.95           C  
ATOM    263  CD1 PHE A  58     186.249 242.702 214.324  1.00 48.88           C  
ATOM    264  CD2 PHE A  58     186.736 242.207 212.050  1.00 47.25           C  
ATOM    265  CE1 PHE A  58     187.519 243.155 214.494  1.00 47.64           C  
ATOM    266  CE2 PHE A  58     188.017 242.660 212.232  1.00 46.51           C  
ATOM    267  CZ  PHE A  58     188.403 243.137 213.456  1.00 47.53           C  
ATOM    268  N   PHE A  59     181.567 243.137 213.340  1.00 48.10           N  
ATOM    269  CA  PHE A  59     180.206 243.413 212.914  1.00 48.32           C  
ATOM    270  C   PHE A  59     179.203 242.812 213.878  1.00 48.21           C  
ATOM    271  O   PHE A  59     178.167 242.287 213.471  1.00 48.25           O  
ATOM    272  CB  PHE A  59     179.994 242.913 211.494  1.00 47.92           C  
ATOM    273  CG  PHE A  59     180.927 243.575 210.538  1.00 47.81           C  
ATOM    274  CD1 PHE A  59     182.080 242.953 210.149  1.00 47.36           C  
ATOM    275  CD2 PHE A  59     180.654 244.830 210.039  1.00 48.58           C  
ATOM    276  CE1 PHE A  59     182.955 243.561 209.283  1.00 47.46           C  
ATOM    277  CE2 PHE A  59     181.521 245.446 209.170  1.00 48.79           C  
ATOM    278  CZ  PHE A  59     182.675 244.809 208.792  1.00 48.33           C  
ATOM    279  N   SER A  60     179.528 242.883 215.164  1.00 49.75           N  
ATOM    280  CA  SER A  60     178.687 242.350 216.214  1.00 48.77           C  
ATOM    281  C   SER A  60     177.603 243.346 216.595  1.00 50.46           C  
ATOM    282  O   SER A  60     177.685 244.536 216.259  1.00 50.45           O  
ATOM    283  CB  SER A  60     179.520 241.985 217.433  1.00 49.02           C  
ATOM    284  OG  SER A  60     180.041 243.120 218.051  1.00 49.64           O  
ATOM    285  N   ASN A  61     176.597 242.840 217.321  1.00 51.37           N  
ATOM    286  CA  ASN A  61     175.464 243.594 217.847  1.00 51.79           C  
ATOM    287  C   ASN A  61     175.770 244.102 219.260  1.00 52.04           C  
ATOM    288  O   ASN A  61     175.813 243.313 220.209  1.00 52.28           O  
ATOM    289  CB  ASN A  61     174.204 242.720 217.827  1.00 52.89           C  
ATOM    290  CG  ASN A  61     172.897 243.510 217.854  1.00 52.88           C  
ATOM    291  OD1 ASN A  61     172.870 244.675 218.268  1.00 54.28           O  
ATOM    292  ND2 ASN A  61     171.815 242.877 217.409  1.00 53.67           N  
ATOM    293  N   VAL A  62     176.009 245.422 219.404  1.00 51.33           N  
ATOM    294  CA  VAL A  62     176.369 246.029 220.694  1.00 51.27           C  
ATOM    295  C   VAL A  62     175.282 246.995 221.121  1.00 53.62           C  
ATOM    296  O   VAL A  62     174.663 247.657 220.285  1.00 50.14           O  
ATOM    297  CB  VAL A  62     177.733 246.736 220.615  1.00 52.06           C  
ATOM    298  CG1 VAL A  62     178.791 245.720 220.235  1.00 51.39           C  
ATOM    299  CG2 VAL A  62     177.695 247.871 219.614  1.00 51.45           C  
ATOM    300  N   THR A  63     175.026 247.057 222.418  1.00 51.51           N  
ATOM    301  CA  THR A  63     173.938 247.876 222.924  1.00 50.98           C  
ATOM    302  C   THR A  63     174.345 249.327 223.077  1.00 54.20           C  
ATOM    303  O   THR A  63     175.421 249.635 223.586  1.00 52.90           O  
ATOM    304  CB  THR A  63     173.421 247.328 224.255  1.00 51.73           C  
ATOM    305  OG1 THR A  63     173.019 245.969 224.076  1.00 52.64           O  
ATOM    306  CG2 THR A  63     172.214 248.131 224.713  1.00 52.99           C  
ATOM    307  N   TRP A  64     173.484 250.219 222.609  1.00 53.17           N  
ATOM    308  CA  TRP A  64     173.723 251.654 222.647  1.00 54.60           C  
ATOM    309  C   TRP A  64     172.939 252.343 223.750  1.00 54.53           C  
ATOM    310  O   TRP A  64     171.710 252.395 223.716  1.00 50.27           O  
ATOM    311  CB  TRP A  64     173.352 252.242 221.298  1.00 54.08           C  
ATOM    312  CG  TRP A  64     173.571 253.704 221.125  1.00 53.48           C  
ATOM    313  CD1 TRP A  64     174.172 254.584 221.968  1.00 54.87           C  
ATOM    314  CD2 TRP A  64     173.203 254.464 219.964  1.00 53.01           C  
ATOM    315  NE1 TRP A  64     174.193 255.826 221.408  1.00 55.98           N  
ATOM    316  CE2 TRP A  64     173.613 255.771 220.187  1.00 52.76           C  
ATOM    317  CE3 TRP A  64     172.577 254.141 218.762  1.00 52.63           C  
ATOM    318  CZ2 TRP A  64     173.423 256.762 219.257  1.00 53.80           C  
ATOM    319  CZ3 TRP A  64     172.388 255.140 217.824  1.00 54.06           C  
ATOM    320  CH2 TRP A  64     172.802 256.417 218.067  1.00 54.70           C  
ATOM    321  N   PHE A  65     173.651 252.875 224.731  1.00 55.14           N  
ATOM    322  CA  PHE A  65     173.028 253.560 225.848  1.00 53.97           C  
ATOM    323  C   PHE A  65     173.273 255.049 225.714  1.00 54.87           C  
ATOM    324  O   PHE A  65     174.412 255.505 225.782  1.00 55.78           O  
ATOM    325  CB  PHE A  65     173.628 253.084 227.153  1.00 54.52           C  
ATOM    326  CG  PHE A  65     173.423 251.652 227.410  1.00 54.33           C  
ATOM    327  CD1 PHE A  65     174.344 250.738 226.961  1.00 55.44           C  
ATOM    328  CD2 PHE A  65     172.329 251.205 228.098  1.00 53.25           C  
ATOM    329  CE1 PHE A  65     174.177 249.409 227.195  1.00 52.72           C  
ATOM    330  CE2 PHE A  65     172.158 249.868 228.333  1.00 53.94           C  
ATOM    331  CZ  PHE A  65     173.087 248.970 227.879  1.00 53.04           C  
ATOM    332  N   HIS A  66     172.224 255.824 225.491  1.00 53.36           N  
ATOM    333  CA  HIS A  66     172.447 257.247 225.296  1.00 54.46           C  
ATOM    334  C   HIS A  66     172.368 257.917 226.665  1.00 55.36           C  
ATOM    335  O   HIS A  66     172.164 257.237 227.673  1.00 55.17           O  
ATOM    336  CB  HIS A  66     171.441 257.852 224.318  1.00 55.80           C  
ATOM    337  CG  HIS A  66     172.012 259.007 223.531  1.00 56.11           C  
ATOM    338  ND1 HIS A  66     172.461 260.161 224.119  1.00 57.35           N  
ATOM    339  CD2 HIS A  66     172.195 259.165 222.199  1.00 55.90           C  
ATOM    340  CE1 HIS A  66     172.896 260.990 223.182  1.00 57.47           C  
ATOM    341  NE2 HIS A  66     172.747 260.405 222.009  1.00 57.13           N  
ATOM    342  N   ALA A  67     172.553 259.231 226.721  1.00 56.18           N  
ATOM    343  CA  ALA A  67     172.560 259.928 228.002  1.00 57.46           C  
ATOM    344  C   ALA A  67     171.928 261.314 227.935  1.00 57.75           C  
ATOM    345  O   ALA A  67     172.555 262.303 228.319  1.00 58.55           O  
ATOM    346  CB  ALA A  67     173.981 260.053 228.496  1.00 56.09           C  
ATOM    347  N   ILE A  68     170.697 261.394 227.443  1.00 58.32           N  
ATOM    348  CA  ILE A  68     169.981 262.667 227.363  1.00 60.11           C  
ATOM    349  C   ILE A  68     168.556 262.531 227.913  1.00 60.77           C  
ATOM    350  O   ILE A  68     168.018 261.422 227.969  1.00 60.44           O  
ATOM    351  CB  ILE A  68     169.967 263.204 225.914  1.00 60.43           C  
ATOM    352  CG1 ILE A  68     169.261 262.187 224.982  1.00 60.12           C  
ATOM    353  CG2 ILE A  68     171.397 263.507 225.457  1.00 58.54           C  
ATOM    354  CD1 ILE A  68     169.008 262.694 223.578  1.00 59.98           C  
ATOM    355  N   HIS A  69     167.944 263.673 228.300  1.00 61.38           N  
ATOM    356  CA  HIS A  69     166.551 263.796 228.775  1.00 62.89           C  
ATOM    357  C   HIS A  69     166.126 262.655 229.709  1.00 63.08           C  
ATOM    358  O   HIS A  69     165.221 262.819 230.531  1.00 62.73           O  
ATOM    359  CB  HIS A  69     165.563 263.897 227.579  1.00 62.68           C  
ATOM    360  CG  HIS A  69     165.725 265.165 226.736  1.00 63.02           C  
ATOM    361  ND1 HIS A  69     166.591 265.241 225.668  1.00 62.99           N  
ATOM    362  CD2 HIS A  69     165.135 266.387 226.830  1.00 63.68           C  
ATOM    363  CE1 HIS A  69     166.528 266.453 225.138  1.00 63.20           C  
ATOM    364  NE2 HIS A  69     165.650 267.167 225.825  1.00 63.33           N  
ATOM    365  N   PRO A  82     172.378 252.155 234.591  1.00 58.45           N  
ATOM    366  CA  PRO A  82     171.855 250.805 234.434  1.00 58.95           C  
ATOM    367  C   PRO A  82     172.950 249.759 234.678  1.00 58.60           C  
ATOM    368  O   PRO A  82     174.091 249.924 234.229  1.00 59.41           O  
ATOM    369  CB  PRO A  82     171.347 250.808 232.979  1.00 58.01           C  
ATOM    370  CG  PRO A  82     172.264 251.777 232.257  1.00 56.78           C  
ATOM    371  CD  PRO A  82     172.606 252.838 233.299  1.00 55.59           C  
ATOM    372  N   VAL A  83     172.595 248.677 235.393  1.00 59.20           N  
ATOM    373  CA  VAL A  83     173.527 247.585 235.697  1.00 59.09           C  
ATOM    374  C   VAL A  83     173.434 246.510 234.628  1.00 58.08           C  
ATOM    375  O   VAL A  83     172.365 245.956 234.374  1.00 58.30           O  
ATOM    376  CB  VAL A  83     173.241 246.989 237.082  1.00 59.43           C  
ATOM    377  CG1 VAL A  83     174.192 245.839 237.356  1.00 59.94           C  
ATOM    378  CG2 VAL A  83     173.411 248.070 238.135  1.00 59.77           C  
ATOM    379  N   LEU A  84     174.559 246.254 233.987  1.00 58.90           N  
ATOM    380  CA  LEU A  84     174.634 245.350 232.860  1.00 57.29           C  
ATOM    381  C   LEU A  84     175.422 244.099 233.240  1.00 61.10           C  
ATOM    382  O   LEU A  84     176.263 244.164 234.131  1.00 57.78           O  
ATOM    383  CB  LEU A  84     175.323 246.094 231.721  1.00 57.81           C  
ATOM    384  CG  LEU A  84     174.716 247.479 231.399  1.00 57.38           C  
ATOM    385  CD1 LEU A  84     175.541 248.145 230.344  1.00 56.20           C  
ATOM    386  CD2 LEU A  84     173.278 247.332 230.949  1.00 58.05           C  
ATOM    387  N   PRO A  85     175.166 242.947 232.614  1.00 57.73           N  
ATOM    388  CA  PRO A  85     175.953 241.732 232.721  1.00 57.72           C  
ATOM    389  C   PRO A  85     177.377 241.966 232.256  1.00 58.45           C  
ATOM    390  O   PRO A  85     177.608 242.759 231.348  1.00 57.89           O  
ATOM    391  CB  PRO A  85     175.226 240.774 231.777  1.00 57.58           C  
ATOM    392  CG  PRO A  85     173.820 241.302 231.704  1.00 57.80           C  
ATOM    393  CD  PRO A  85     173.954 242.807 231.813  1.00 57.76           C  
ATOM    394  N   PHE A  86     178.322 241.258 232.860  1.00 57.99           N  
ATOM    395  CA  PHE A  86     179.729 241.324 232.472  1.00 59.35           C  
ATOM    396  C   PHE A  86     180.109 240.131 231.595  1.00 58.23           C  
ATOM    397  O   PHE A  86     181.012 240.215 230.761  1.00 56.05           O  
ATOM    398  CB  PHE A  86     180.607 241.354 233.718  1.00 59.53           C  
ATOM    399  CG  PHE A  86     182.055 241.609 233.485  1.00 58.98           C  
ATOM    400  CD1 PHE A  86     182.520 242.891 233.238  1.00 57.99           C  
ATOM    401  CD2 PHE A  86     182.963 240.572 233.536  1.00 58.52           C  
ATOM    402  CE1 PHE A  86     183.861 243.123 233.045  1.00 57.18           C  
ATOM    403  CE2 PHE A  86     184.300 240.804 233.347  1.00 57.66           C  
ATOM    404  CZ  PHE A  86     184.749 242.082 233.102  1.00 57.73           C  
ATOM    405  N   ASN A  87     179.425 239.012 231.814  1.00 57.73           N  
ATOM    406  CA  ASN A  87     179.686 237.757 231.119  1.00 57.88           C  
ATOM    407  C   ASN A  87     181.155 237.345 231.200  1.00 57.79           C  
ATOM    408  O   ASN A  87     181.690 237.184 232.296  1.00 57.97           O  
ATOM    409  CB  ASN A  87     179.200 237.831 229.683  1.00 57.20           C  
ATOM    410  CG  ASN A  87     177.710 238.039 229.597  1.00 57.88           C  
ATOM    411  OD1 ASN A  87     176.971 237.718 230.537  1.00 58.47           O  
ATOM    412  ND2 ASN A  87     177.251 238.557 228.488  1.00 56.82           N  
ATOM    413  N   ASP A  88     181.805 237.161 230.048  1.00 57.07           N  
ATOM    414  CA  ASP A  88     183.192 236.705 230.018  1.00 56.85           C  
ATOM    415  C   ASP A  88     184.169 237.834 229.748  1.00 56.07           C  
ATOM    416  O   ASP A  88     185.351 237.598 229.507  1.00 54.92           O  
ATOM    417  CB  ASP A  88     183.376 235.628 228.948  1.00 56.82           C  
ATOM    418  CG  ASP A  88     182.611 234.350 229.244  1.00 58.07           C  
ATOM    419  OD1 ASP A  88     182.530 233.971 230.388  1.00 59.30           O  
ATOM    420  OD2 ASP A  88     182.109 233.761 228.317  1.00 58.43           O  
ATOM    421  N   GLY A  89     183.681 239.058 229.776  1.00 55.83           N  
ATOM    422  CA  GLY A  89     184.501 240.213 229.473  1.00 54.60           C  
ATOM    423  C   GLY A  89     183.692 241.212 228.678  1.00 53.77           C  
ATOM    424  O   GLY A  89     182.776 240.847 227.934  1.00 55.17           O  
ATOM    425  N   VAL A  90     184.030 242.477 228.838  1.00 54.04           N  
ATOM    426  CA  VAL A  90     183.271 243.548 228.229  1.00 53.02           C  
ATOM    427  C   VAL A  90     184.043 244.503 227.359  1.00 52.51           C  
ATOM    428  O   VAL A  90     185.093 245.021 227.738  1.00 53.04           O  
ATOM    429  CB  VAL A  90     182.586 244.359 229.336  1.00 54.55           C  
ATOM    430  CG1 VAL A  90     181.889 245.575 228.762  1.00 54.16           C  
ATOM    431  CG2 VAL A  90     181.585 243.478 230.025  1.00 55.95           C  
ATOM    432  N   TYR A  91     183.481 244.783 226.201  1.00 52.35           N  
ATOM    433  CA  TYR A  91     184.030 245.825 225.366  1.00 51.60           C  
ATOM    434  C   TYR A  91     183.233 247.069 225.664  1.00 52.21           C  
ATOM    435  O   TYR A  91     182.006 247.063 225.557  1.00 53.36           O  
ATOM    436  CB  TYR A  91     183.927 245.514 223.891  1.00 51.53           C  
ATOM    437  CG  TYR A  91     184.635 246.546 223.070  1.00 50.81           C  
ATOM    438  CD1 TYR A  91     185.970 246.388 222.842  1.00 50.98           C  
ATOM    439  CD2 TYR A  91     183.969 247.655 222.564  1.00 50.40           C  
ATOM    440  CE1 TYR A  91     186.658 247.308 222.108  1.00 51.43           C  
ATOM    441  CE2 TYR A  91     184.666 248.582 221.819  1.00 51.09           C  
ATOM    442  CZ  TYR A  91     186.010 248.398 221.594  1.00 51.27           C  
ATOM    443  OH  TYR A  91     186.731 249.289 220.855  1.00 51.60           O  
ATOM    444  N   PHE A  92     183.901 248.133 226.051  1.00 50.69           N  
ATOM    445  CA  PHE A  92     183.196 249.347 226.409  1.00 51.27           C  
ATOM    446  C   PHE A  92     183.707 250.512 225.598  1.00 51.88           C  
ATOM    447  O   PHE A  92     184.908 250.679 225.426  1.00 52.42           O  
ATOM    448  CB  PHE A  92     183.383 249.646 227.888  1.00 52.01           C  
ATOM    449  CG  PHE A  92     182.656 250.859 228.347  1.00 52.39           C  
ATOM    450  CD1 PHE A  92     181.417 250.746 228.922  1.00 53.54           C  
ATOM    451  CD2 PHE A  92     183.198 252.120 228.187  1.00 53.47           C  
ATOM    452  CE1 PHE A  92     180.740 251.860 229.334  1.00 54.24           C  
ATOM    453  CE2 PHE A  92     182.520 253.239 228.594  1.00 53.35           C  
ATOM    454  CZ  PHE A  92     181.291 253.109 229.171  1.00 54.09           C  
ATOM    455  N   ALA A  93     182.812 251.343 225.119  1.00 51.52           N  
ATOM    456  CA  ALA A  93     183.262 252.513 224.391  1.00 51.73           C  
ATOM    457  C   ALA A  93     182.361 253.680 224.668  1.00 54.63           C  
ATOM    458  O   ALA A  93     181.177 253.511 224.930  1.00 50.04           O  
ATOM    459  CB  ALA A  93     183.300 252.226 222.904  1.00 52.47           C  
ATOM    460  N   SER A  94     182.900 254.878 224.572  1.00 52.68           N  
ATOM    461  CA  SER A  94     182.060 256.043 224.742  1.00 53.51           C  
ATOM    462  C   SER A  94     182.489 257.212 223.893  1.00 55.43           C  
ATOM    463  O   SER A  94     183.666 257.375 223.565  1.00 56.92           O  
ATOM    464  CB  SER A  94     182.052 256.449 226.192  1.00 53.93           C  
ATOM    465  OG  SER A  94     183.327 256.841 226.605  1.00 54.94           O  
ATOM    466  N   THR A  95     181.525 258.055 223.570  1.00 56.89           N  
ATOM    467  CA  THR A  95     181.791 259.270 222.826  1.00 56.43           C  
ATOM    468  C   THR A  95     181.435 260.454 223.697  1.00 58.26           C  
ATOM    469  O   THR A  95     180.404 260.455 224.368  1.00 55.58           O  
ATOM    470  CB  THR A  95     181.003 259.282 221.512  1.00 57.35           C  
ATOM    471  OG1 THR A  95     179.608 259.132 221.795  1.00 56.67           O  
ATOM    472  CG2 THR A  95     181.458 258.142 220.613  1.00 56.79           C  
ATOM    473  N   GLU A  96     182.293 261.462 223.687  1.00 59.17           N  
ATOM    474  CA  GLU A  96     182.142 262.594 224.580  1.00 58.85           C  
ATOM    475  C   GLU A  96     182.265 263.957 223.942  1.00 60.41           C  
ATOM    476  O   GLU A  96     182.997 264.158 222.967  1.00 59.88           O  
ATOM    477  CB  GLU A  96     183.210 262.501 225.656  1.00 59.71           C  
ATOM    478  CG  GLU A  96     182.996 261.434 226.672  1.00 59.70           C  
ATOM    479  CD  GLU A  96     182.000 261.843 227.657  1.00 61.15           C  
ATOM    480  OE1 GLU A  96     181.548 262.970 227.591  1.00 61.41           O  
ATOM    481  OE2 GLU A  96     181.687 261.058 228.499  1.00 60.20           O  
ATOM    482  N   LYS A  97     181.581 264.913 224.558  1.00 60.43           N  
ATOM    483  CA  LYS A  97     181.718 266.319 224.220  1.00 60.65           C  
ATOM    484  C   LYS A  97     182.346 267.086 225.380  1.00 61.51           C  
ATOM    485  O   LYS A  97     183.085 268.046 225.171  1.00 61.41           O  
ATOM    486  CB  LYS A  97     180.366 266.933 223.854  1.00 60.76           C  
ATOM    487  CG  LYS A  97     180.447 268.402 223.449  1.00 61.05           C  
ATOM    488  CD  LYS A  97     179.100 268.943 223.004  1.00 61.54           C  
ATOM    489  CE  LYS A  97     179.197 270.417 222.633  1.00 59.35           C  
ATOM    490  NZ  LYS A  97     177.887 270.968 222.203  1.00 58.35           N  
ATOM    491  N   SER A  98     182.020 266.680 226.609  1.00 61.87           N  
ATOM    492  CA  SER A  98     182.478 267.397 227.794  1.00 61.98           C  
ATOM    493  C   SER A  98     182.949 266.469 228.915  1.00 63.16           C  
ATOM    494  O   SER A  98     182.960 266.858 230.083  1.00 62.41           O  
ATOM    495  CB  SER A  98     181.381 268.313 228.302  1.00 63.78           C  
ATOM    496  OG  SER A  98     180.236 267.590 228.628  1.00 62.25           O  
ATOM    497  N   ASN A  99     183.350 265.250 228.559  1.00 62.03           N  
ATOM    498  CA  ASN A  99     183.845 264.271 229.531  1.00 62.55           C  
ATOM    499  C   ASN A  99     182.868 264.019 230.680  1.00 60.99           C  
ATOM    500  O   ASN A  99     183.250 264.061 231.850  1.00 62.75           O  
ATOM    501  CB  ASN A  99     185.202 264.698 230.055  1.00 62.83           C  
ATOM    502  N   ILE A 100     181.608 263.781 230.336  1.00 60.03           N  
ATOM    503  CA  ILE A 100     180.559 263.517 231.312  1.00 61.20           C  
ATOM    504  C   ILE A 100     180.708 262.151 231.973  1.00 61.14           C  
ATOM    505  O   ILE A 100     180.462 262.016 233.172  1.00 62.42           O  
ATOM    506  CB  ILE A 100     179.176 263.644 230.675  1.00 61.40           C  
ATOM    507  CG1 ILE A 100     178.946 265.105 230.278  1.00 61.49           C  
ATOM    508  CG2 ILE A 100     178.100 263.152 231.645  1.00 61.66           C  
ATOM    509  CD1 ILE A 100     177.751 265.334 229.371  1.00 62.13           C  
ATOM    510  N   ILE A 101     181.050 261.127 231.196  1.00 60.51           N  
ATOM    511  CA  ILE A 101     181.248 259.801 231.770  1.00 60.67           C  
ATOM    512  C   ILE A 101     182.574 259.816 232.497  1.00 61.11           C  
ATOM    513  O   ILE A 101     183.606 260.171 231.925  1.00 59.46           O  
ATOM    514  CB  ILE A 101     181.243 258.690 230.694  1.00 60.30           C  
ATOM    515  CG1 ILE A 101     179.865 258.623 230.027  1.00 60.24           C  
ATOM    516  CG2 ILE A 101     181.607 257.335 231.338  1.00 58.49           C  
ATOM    517  CD1 ILE A 101     179.818 257.837 228.754  1.00 57.04           C  
ATOM    518  N   ARG A 102     182.547 259.457 233.771  1.00 59.93           N  
ATOM    519  CA  ARG A 102     183.754 259.530 234.568  1.00 60.34           C  
ATOM    520  C   ARG A 102     184.209 258.192 235.108  1.00 61.49           C  
ATOM    521  O   ARG A 102     185.377 258.049 235.468  1.00 63.29           O  
ATOM    522  CB  ARG A 102     183.561 260.487 235.722  1.00 62.53           C  
ATOM    523  CG  ARG A 102     183.282 261.907 235.310  1.00 61.42           C  
ATOM    524  CD  ARG A 102     183.041 262.786 236.459  1.00 62.21           C  
ATOM    525  NE  ARG A 102     182.660 264.112 236.026  1.00 63.43           N  
ATOM    526  CZ  ARG A 102     182.378 265.146 236.843  1.00 65.71           C  
ATOM    527  NH1 ARG A 102     182.447 265.002 238.149  1.00 66.66           N  
ATOM    528  NH2 ARG A 102     182.031 266.311 236.329  1.00 66.94           N  
ATOM    529  N   GLY A 103     183.324 257.208 235.199  1.00 59.90           N  
ATOM    530  CA  GLY A 103     183.784 255.995 235.854  1.00 57.79           C  
ATOM    531  C   GLY A 103     182.949 254.745 235.672  1.00 59.01           C  
ATOM    532  O   GLY A 103     181.989 254.712 234.903  1.00 56.60           O  
ATOM    533  N   TRP A 104     183.384 253.693 236.364  1.00 57.26           N  
ATOM    534  CA  TRP A 104     182.761 252.375 236.317  1.00 59.15           C  
ATOM    535  C   TRP A 104     182.706 251.693 237.677  1.00 60.46           C  
ATOM    536  O   TRP A 104     183.611 251.837 238.501  1.00 61.21           O  
ATOM    537  CB  TRP A 104     183.530 251.439 235.384  1.00 57.94           C  
ATOM    538  CG  TRP A 104     183.605 251.878 233.985  1.00 56.84           C  
ATOM    539  CD1 TRP A 104     182.784 251.510 232.975  1.00 56.79           C  
ATOM    540  CD2 TRP A 104     184.569 252.780 233.408  1.00 57.74           C  
ATOM    541  NE1 TRP A 104     183.161 252.125 231.819  1.00 55.89           N  
ATOM    542  CE2 TRP A 104     184.252 252.907 232.067  1.00 56.32           C  
ATOM    543  CE3 TRP A 104     185.656 253.481 233.919  1.00 58.13           C  
ATOM    544  CZ2 TRP A 104     184.981 253.713 231.217  1.00 54.96           C  
ATOM    545  CZ3 TRP A 104     186.385 254.290 233.069  1.00 57.75           C  
ATOM    546  CH2 TRP A 104     186.053 254.403 231.755  1.00 54.43           C  
ATOM    547  N   ILE A 105     181.684 250.873 237.868  1.00 59.80           N  
ATOM    548  CA  ILE A 105     181.587 250.004 239.032  1.00 59.24           C  
ATOM    549  C   ILE A 105     181.562 248.562 238.570  1.00 60.60           C  
ATOM    550  O   ILE A 105     180.779 248.214 237.690  1.00 53.08           O  
ATOM    551  CB  ILE A 105     180.306 250.243 239.850  1.00 60.71           C  
ATOM    552  CG1 ILE A 105     180.225 251.670 240.329  1.00 61.04           C  
ATOM    553  CG2 ILE A 105     180.310 249.296 241.052  1.00 61.98           C  
ATOM    554  CD1 ILE A 105     178.871 252.042 240.910  1.00 63.11           C  
ATOM    555  N   PHE A 106     182.392 247.714 239.154  1.00 60.05           N  
ATOM    556  CA  PHE A 106     182.352 246.299 238.784  1.00 60.12           C  
ATOM    557  C   PHE A 106     182.155 245.442 240.017  1.00 62.41           C  
ATOM    558  O   PHE A 106     182.726 245.723 241.067  1.00 63.64           O  
ATOM    559  CB  PHE A 106     183.641 245.860 238.082  1.00 60.38           C  
ATOM    560  CG  PHE A 106     183.933 246.565 236.809  1.00 59.32           C  
ATOM    561  CD1 PHE A 106     184.644 247.744 236.811  1.00 58.74           C  
ATOM    562  CD2 PHE A 106     183.508 246.052 235.604  1.00 59.29           C  
ATOM    563  CE1 PHE A 106     184.916 248.398 235.637  1.00 57.84           C  
ATOM    564  CE2 PHE A 106     183.774 246.712 234.423  1.00 58.51           C  
ATOM    565  CZ  PHE A 106     184.478 247.889 234.445  1.00 57.96           C  
ATOM    566  N   GLY A 107     181.403 244.360 239.888  1.00 61.67           N  
ATOM    567  CA  GLY A 107     181.249 243.440 241.012  1.00 62.11           C  
ATOM    568  C   GLY A 107     180.108 242.461 240.805  1.00 62.69           C  
ATOM    569  O   GLY A 107     179.796 242.072 239.677  1.00 61.73           O  
ATOM    570  N   THR A 108     179.492 242.053 241.904  1.00 63.11           N  
ATOM    571  CA  THR A 108     178.363 241.136 241.865  1.00 64.21           C  
ATOM    572  C   THR A 108     177.090 241.893 242.210  1.00 65.13           C  
ATOM    573  O   THR A 108     176.283 242.198 241.330  1.00 64.23           O  
ATOM    574  CB  THR A 108     178.563 239.966 242.831  1.00 64.54           C  
ATOM    575  OG1 THR A 108     178.762 240.478 244.158  1.00 65.29           O  
ATOM    576  CG2 THR A 108     179.776 239.161 242.401  1.00 64.90           C  
ATOM    577  N   THR A 109     176.927 242.222 243.490  1.00 64.58           N  
ATOM    578  CA  THR A 109     175.755 242.968 243.934  1.00 65.37           C  
ATOM    579  C   THR A 109     175.951 244.486 243.839  1.00 65.55           C  
ATOM    580  O   THR A 109     174.979 245.239 243.853  1.00 64.59           O  
ATOM    581  CB  THR A 109     175.383 242.579 245.370  1.00 65.05           C  
ATOM    582  OG1 THR A 109     176.461 242.911 246.250  1.00 65.14           O  
ATOM    583  CG2 THR A 109     175.116 241.082 245.445  1.00 64.26           C  
ATOM    584  N   LEU A 110     177.205 244.935 243.730  1.00 63.96           N  
ATOM    585  CA  LEU A 110     177.537 246.357 243.568  1.00 65.22           C  
ATOM    586  C   LEU A 110     176.949 247.271 244.654  1.00 65.97           C  
ATOM    587  O   LEU A 110     176.537 248.393 244.360  1.00 66.06           O  
ATOM    588  CB  LEU A 110     177.040 246.862 242.191  1.00 65.29           C  
ATOM    589  CG  LEU A 110     177.903 246.521 240.948  1.00 62.51           C  
ATOM    590  CD1 LEU A 110     177.746 245.063 240.575  1.00 63.20           C  
ATOM    591  CD2 LEU A 110     177.473 247.415 239.780  1.00 62.09           C  
ATOM    592  N   ASP A 111     176.905 246.805 245.903  1.00 67.02           N  
ATOM    593  CA  ASP A 111     176.373 247.630 246.992  1.00 68.38           C  
ATOM    594  C   ASP A 111     176.918 247.219 248.368  1.00 68.41           C  
ATOM    595  O   ASP A 111     176.396 246.292 248.987  1.00 66.60           O  
ATOM    596  CB  ASP A 111     174.839 247.553 247.022  1.00 66.76           C  
ATOM    597  N   SER A 112     177.982 247.883 248.829  1.00 65.84           N  
ATOM    598  CA  SER A 112     178.599 247.590 250.130  1.00 65.59           C  
ATOM    599  C   SER A 112     178.881 246.106 250.397  1.00 66.91           C  
ATOM    600  O   SER A 112     178.581 245.620 251.493  1.00 67.05           O  
ATOM    601  CB  SER A 112     177.714 248.111 251.249  1.00 67.75           C  
ATOM    602  OG  SER A 112     177.539 249.487 251.156  1.00 67.33           O  
ATOM    603  N   LYS A 113     179.464 245.390 249.415  1.00 65.74           N  
ATOM    604  CA  LYS A 113     179.775 243.957 249.541  1.00 67.23           C  
ATOM    605  C   LYS A 113     180.636 243.479 248.366  1.00 66.50           C  
ATOM    606  O   LYS A 113     180.274 243.638 247.195  1.00 68.10           O  
ATOM    607  CB  LYS A 113     178.468 243.107 249.630  1.00 67.31           C  
ATOM    608  CG  LYS A 113     178.653 241.565 249.923  1.00 66.78           C  
ATOM    609  CD  LYS A 113     177.273 240.834 250.115  1.00 65.52           C  
ATOM    610  CE  LYS A 113     177.439 239.311 250.404  1.00 65.14           C  
ATOM    611  NZ  LYS A 113     176.119 238.627 250.606  1.00 65.54           N  
ATOM    612  N   SER A 116     183.906 244.482 245.116  1.00 63.87           N  
ATOM    613  CA  SER A 116     183.505 245.480 244.138  1.00 63.83           C  
ATOM    614  C   SER A 116     184.656 246.460 243.859  1.00 62.66           C  
ATOM    615  O   SER A 116     185.478 246.722 244.740  1.00 63.54           O  
ATOM    616  CB  SER A 116     182.267 246.237 244.627  1.00 65.61           C  
ATOM    617  OG  SER A 116     181.156 245.388 244.732  1.00 65.18           O  
ATOM    618  N   LEU A 117     184.707 246.983 242.624  1.00 63.11           N  
ATOM    619  CA  LEU A 117     185.699 247.952 242.140  1.00 62.59           C  
ATOM    620  C   LEU A 117     185.034 249.287 241.858  1.00 62.58           C  
ATOM    621  O   LEU A 117     183.891 249.317 241.405  1.00 62.93           O  
ATOM    622  CB  LEU A 117     186.317 247.478 240.820  1.00 61.79           C  
ATOM    623  CG  LEU A 117     187.340 246.331 240.835  1.00 62.75           C  
ATOM    624  CD1 LEU A 117     186.678 245.006 241.206  1.00 62.38           C  
ATOM    625  CD2 LEU A 117     187.954 246.253 239.441  1.00 60.66           C  
ATOM    626  N   LEU A 118     185.766 250.384 242.034  1.00 63.80           N  
ATOM    627  CA  LEU A 118     185.288 251.695 241.607  1.00 63.02           C  
ATOM    628  C   LEU A 118     186.383 252.518 240.931  1.00 63.20           C  
ATOM    629  O   LEU A 118     187.398 252.856 241.542  1.00 65.46           O  
ATOM    630  CB  LEU A 118     184.755 252.483 242.806  1.00 64.22           C  
ATOM    631  CG  LEU A 118     184.301 253.941 242.524  1.00 64.19           C  
ATOM    632  CD1 LEU A 118     183.124 253.946 241.573  1.00 63.69           C  
ATOM    633  CD2 LEU A 118     183.924 254.613 243.826  1.00 65.70           C  
ATOM    634  N   ILE A 119     186.166 252.869 239.676  1.00 61.14           N  
ATOM    635  CA  ILE A 119     187.132 253.671 238.935  1.00 62.24           C  
ATOM    636  C   ILE A 119     186.506 255.001 238.561  1.00 63.26           C  
ATOM    637  O   ILE A 119     185.497 255.010 237.867  1.00 62.81           O  
ATOM    638  CB  ILE A 119     187.576 252.918 237.662  1.00 62.00           C  
ATOM    639  CG1 ILE A 119     188.229 251.563 238.066  1.00 62.01           C  
ATOM    640  CG2 ILE A 119     188.532 253.798 236.819  1.00 61.24           C  
ATOM    641  CD1 ILE A 119     188.453 250.597 236.915  1.00 59.46           C  
ATOM    642  N   VAL A 120     187.058 256.119 239.042  1.00 62.23           N  
ATOM    643  CA  VAL A 120     186.476 257.432 238.734  1.00 64.17           C  
ATOM    644  C   VAL A 120     187.495 258.499 238.352  1.00 65.38           C  
ATOM    645  O   VAL A 120     188.453 258.737 239.081  1.00 66.39           O  
ATOM    646  CB  VAL A 120     185.662 257.952 239.935  1.00 63.21           C  
ATOM    647  CG1 VAL A 120     185.097 259.348 239.637  1.00 63.58           C  
ATOM    648  CG2 VAL A 120     184.529 256.993 240.226  1.00 64.34           C  
ATOM    649  N   ASN A 121     187.247 259.205 237.256  1.00 63.44           N  
ATOM    650  CA  ASN A 121     188.082 260.345 236.905  1.00 64.45           C  
ATOM    651  C   ASN A 121     187.440 261.681 237.276  1.00 65.77           C  
ATOM    652  O   ASN A 121     186.779 262.295 236.430  1.00 66.45           O  
ATOM    653  CB  ASN A 121     188.407 260.365 235.432  1.00 66.86           C  
ATOM    654  CG  ASN A 121     189.336 261.513 235.105  1.00 67.71           C  
ATOM    655  OD1 ASN A 121     190.117 261.945 235.961  1.00 69.06           O  
ATOM    656  ND2 ASN A 121     189.261 262.016 233.902  1.00 67.81           N  
ATOM    657  N   ASN A 122     187.649 262.149 238.517  1.00 67.55           N  
ATOM    658  CA  ASN A 122     187.106 263.414 239.006  1.00 67.29           C  
ATOM    659  C   ASN A 122     188.037 264.578 238.660  1.00 68.73           C  
ATOM    660  O   ASN A 122     189.166 264.654 239.162  1.00 69.12           O  
ATOM    661  CB  ASN A 122     186.810 263.359 240.507  1.00 68.94           C  
ATOM    662  CG  ASN A 122     187.999 262.898 241.386  1.00 67.80           C  
ATOM    663  OD1 ASN A 122     188.570 261.820 241.156  1.00 68.53           O  
ATOM    664  ND2 ASN A 122     188.348 263.700 242.386  1.00 69.45           N  
ATOM    665  N   ALA A 123     187.564 265.487 237.784  1.00 68.71           N  
ATOM    666  CA  ALA A 123     188.288 266.665 237.300  1.00 69.53           C  
ATOM    667  C   ALA A 123     189.621 266.304 236.637  1.00 70.38           C  
ATOM    668  O   ALA A 123     189.638 265.794 235.517  1.00 70.33           O  
ATOM    669  CB  ALA A 123     188.494 267.659 238.439  1.00 69.92           C  
ATOM    670  N   THR A 124     190.728 266.610 237.303  1.00 69.41           N  
ATOM    671  CA  THR A 124     192.044 266.421 236.718  1.00 70.20           C  
ATOM    672  C   THR A 124     192.866 265.255 237.269  1.00 70.34           C  
ATOM    673  O   THR A 124     194.021 265.086 236.874  1.00 70.26           O  
ATOM    674  CB  THR A 124     192.852 267.721 236.880  1.00 71.20           C  
ATOM    675  N   ASN A 125     192.317 264.468 238.187  1.00 69.66           N  
ATOM    676  CA  ASN A 125     193.129 263.413 238.790  1.00 69.70           C  
ATOM    677  C   ASN A 125     192.374 262.096 238.909  1.00 68.00           C  
ATOM    678  O   ASN A 125     191.412 261.981 239.662  1.00 67.22           O  
ATOM    679  CB  ASN A 125     193.661 263.874 240.131  1.00 69.28           C  
ATOM    680  CG  ASN A 125     194.579 265.085 240.002  1.00 69.46           C  
ATOM    681  OD1 ASN A 125     194.122 266.229 240.098  1.00 69.89           O  
ATOM    682  ND2 ASN A 125     195.847 264.862 239.787  1.00 69.31           N  
ATOM    683  N   VAL A 126     192.834 261.097 238.164  1.00 67.84           N  
ATOM    684  CA  VAL A 126     192.172 259.795 238.117  1.00 68.39           C  
ATOM    685  C   VAL A 126     192.343 259.005 239.404  1.00 69.04           C  
ATOM    686  O   VAL A 126     193.457 258.834 239.898  1.00 68.04           O  
ATOM    687  CB  VAL A 126     192.727 258.953 236.947  1.00 67.83           C  
ATOM    688  CG1 VAL A 126     192.120 257.538 236.969  1.00 67.47           C  
ATOM    689  CG2 VAL A 126     192.414 259.643 235.637  1.00 69.16           C  
ATOM    690  N   VAL A 127     191.235 258.497 239.933  1.00 67.50           N  
ATOM    691  CA  VAL A 127     191.258 257.729 241.164  1.00 65.36           C  
ATOM    692  C   VAL A 127     190.722 256.309 241.009  1.00 64.98           C  
ATOM    693  O   VAL A 127     189.583 256.099 240.593  1.00 65.96           O  
ATOM    694  CB  VAL A 127     190.415 258.453 242.222  1.00 66.64           C  
ATOM    695  CG1 VAL A 127     190.386 257.653 243.516  1.00 66.28           C  
ATOM    696  CG2 VAL A 127     190.976 259.834 242.448  1.00 67.52           C  
ATOM    697  N   ILE A 128     191.528 255.336 241.397  1.00 64.62           N  
ATOM    698  CA  ILE A 128     191.100 253.945 241.385  1.00 63.49           C  
ATOM    699  C   ILE A 128     191.047 253.397 242.798  1.00 65.54           C  
ATOM    700  O   ILE A 128     192.037 253.439 243.528  1.00 65.41           O  
ATOM    701  CB  ILE A 128     192.037 253.053 240.546  1.00 64.68           C  
ATOM    702  CG1 ILE A 128     192.050 253.524 239.090  1.00 66.17           C  
ATOM    703  CG2 ILE A 128     191.589 251.573 240.659  1.00 65.22           C  
ATOM    704  CD1 ILE A 128     193.100 252.844 238.216  1.00 64.72           C  
ATOM    705  N   LYS A 129     189.900 252.866 243.180  1.00 64.80           N  
ATOM    706  CA  LYS A 129     189.750 252.254 244.489  1.00 65.09           C  
ATOM    707  C   LYS A 129     189.038 250.924 244.364  1.00 64.48           C  
ATOM    708  O   LYS A 129     188.178 250.764 243.503  1.00 65.85           O  
ATOM    709  CB  LYS A 129     188.989 253.187 245.431  1.00 65.04           C  
ATOM    710  N   VAL A 130     189.360 249.976 245.232  1.00 65.28           N  
ATOM    711  CA  VAL A 130     188.627 248.703 245.210  1.00 64.68           C  
ATOM    712  C   VAL A 130     187.881 248.412 246.520  1.00 64.27           C  
ATOM    713  O   VAL A 130     187.813 247.259 246.951  1.00 64.71           O  
ATOM    714  CB  VAL A 130     189.573 247.539 244.893  1.00 63.74           C  
ATOM    715  CG1 VAL A 130     190.181 247.740 243.501  1.00 64.68           C  
ATOM    716  CG2 VAL A 130     190.615 247.438 245.939  1.00 64.38           C  
ATOM    717  N   CYS A 131     187.362 249.466 247.162  1.00 64.05           N  
ATOM    718  CA  CYS A 131     186.627 249.391 248.421  1.00 65.52           C  
ATOM    719  C   CYS A 131     185.167 249.003 248.182  1.00 65.43           C  
ATOM    720  O   CYS A 131     184.578 249.351 247.153  1.00 65.01           O  
ATOM    721  CB  CYS A 131     186.669 250.741 249.156  1.00 66.43           C  
ATOM    722  SG  CYS A 131     188.326 251.340 249.570  1.00 67.09           S  
ATOM    723  N   GLU A 132     184.548 248.340 249.171  1.00 65.01           N  
ATOM    724  CA  GLU A 132     183.125 247.995 249.119  1.00 65.99           C  
ATOM    725  C   GLU A 132     182.293 249.211 249.512  1.00 66.32           C  
ATOM    726  O   GLU A 132     181.798 249.322 250.632  1.00 65.74           O  
ATOM    727  CB  GLU A 132     182.828 246.808 250.031  1.00 65.64           C  
ATOM    728  CG  GLU A 132     183.500 245.513 249.597  1.00 66.43           C  
ATOM    729  CD  GLU A 132     183.148 244.344 250.469  1.00 66.70           C  
ATOM    730  OE1 GLU A 132     182.702 244.555 251.566  1.00 67.54           O  
ATOM    731  OE2 GLU A 132     183.300 243.233 250.022  1.00 67.05           O  
ATOM    732  N   PHE A 133     182.173 250.126 248.560  1.00 65.59           N  
ATOM    733  CA  PHE A 133     181.527 251.417 248.748  1.00 65.37           C  
ATOM    734  C   PHE A 133     180.031 251.298 248.861  1.00 66.39           C  
ATOM    735  O   PHE A 133     179.424 250.379 248.300  1.00 66.75           O  
ATOM    736  CB  PHE A 133     181.789 252.333 247.562  1.00 65.22           C  
ATOM    737  CG  PHE A 133     183.158 252.811 247.426  1.00 66.26           C  
ATOM    738  CD1 PHE A 133     184.012 252.201 246.535  1.00 65.86           C  
ATOM    739  CD2 PHE A 133     183.611 253.877 248.165  1.00 66.29           C  
ATOM    740  CE1 PHE A 133     185.292 252.643 246.390  1.00 66.14           C  
ATOM    741  CE2 PHE A 133     184.897 254.322 248.020  1.00 66.89           C  
ATOM    742  CZ  PHE A 133     185.732 253.700 247.130  1.00 65.80           C  
ATOM    743  N   GLN A 134     179.436 252.254 249.567  1.00 66.47           N  
ATOM    744  CA  GLN A 134     177.992 252.373 249.597  1.00 66.94           C  
ATOM    745  C   GLN A 134     177.558 253.204 248.412  1.00 67.63           C  
ATOM    746  O   GLN A 134     177.960 254.360 248.275  1.00 67.77           O  
ATOM    747  CB  GLN A 134     177.503 253.029 250.894  1.00 65.95           C  
ATOM    748  CG  GLN A 134     175.982 253.243 250.943  1.00 66.58           C  
ATOM    749  CD  GLN A 134     175.233 251.931 251.010  1.00 66.44           C  
ATOM    750  OE1 GLN A 134     175.289 251.233 252.026  1.00 66.92           O  
ATOM    751  NE2 GLN A 134     174.557 251.571 249.921  1.00 68.13           N  
ATOM    752  N   PHE A 135     176.741 252.620 247.559  1.00 67.38           N  
ATOM    753  CA  PHE A 135     176.279 253.302 246.372  1.00 67.61           C  
ATOM    754  C   PHE A 135     174.806 253.638 246.476  1.00 68.63           C  
ATOM    755  O   PHE A 135     174.066 253.023 247.245  1.00 69.24           O  
ATOM    756  CB  PHE A 135     176.532 252.461 245.124  1.00 66.54           C  
ATOM    757  N   CYS A 136     174.393 254.635 245.711  1.00 68.14           N  
ATOM    758  CA  CYS A 136     172.996 255.029 245.634  1.00 68.83           C  
ATOM    759  C   CYS A 136     172.214 253.997 244.834  1.00 68.71           C  
ATOM    760  O   CYS A 136     172.800 253.172 244.133  1.00 67.77           O  
ATOM    761  CB  CYS A 136     172.849 256.394 244.955  1.00 69.34           C  
ATOM    762  N   ASN A 137     170.885 254.059 244.919  1.00 68.50           N  
ATOM    763  CA  ASN A 137     170.028 253.190 244.117  1.00 68.26           C  
ATOM    764  C   ASN A 137     170.242 253.478 242.635  1.00 67.34           C  
ATOM    765  O   ASN A 137     170.148 252.591 241.786  1.00 66.72           O  
ATOM    766  CB  ASN A 137     168.583 253.404 244.517  1.00 70.09           C  
ATOM    767  N   ASP A 138     170.606 254.719 242.356  1.00 67.01           N  
ATOM    768  CA  ASP A 138     170.960 255.183 241.027  1.00 66.96           C  
ATOM    769  C   ASP A 138     172.212 256.057 241.157  1.00 67.29           C  
ATOM    770  O   ASP A 138     172.098 257.269 241.338  1.00 66.82           O  
ATOM    771  CB  ASP A 138     169.809 255.990 240.418  1.00 68.21           C  
ATOM    772  CG  ASP A 138     170.039 256.381 238.957  1.00 69.96           C  
ATOM    773  OD1 ASP A 138     171.047 256.004 238.413  1.00 68.39           O  
ATOM    774  OD2 ASP A 138     169.199 257.053 238.401  1.00 71.35           O  
ATOM    775  N   PRO A 139     173.412 255.452 241.150  1.00 66.85           N  
ATOM    776  CA  PRO A 139     174.705 256.084 241.347  1.00 65.71           C  
ATOM    777  C   PRO A 139     174.939 257.192 240.343  1.00 64.70           C  
ATOM    778  O   PRO A 139     174.665 257.027 239.157  1.00 64.08           O  
ATOM    779  CB  PRO A 139     175.671 254.921 241.108  1.00 65.26           C  
ATOM    780  CG  PRO A 139     174.876 253.695 241.435  1.00 64.60           C  
ATOM    781  CD  PRO A 139     173.490 254.002 240.948  1.00 65.77           C  
ATOM    782  N   PHE A 140     175.465 258.311 240.809  1.00 65.85           N  
ATOM    783  CA  PHE A 140     175.745 259.423 239.921  1.00 65.13           C  
ATOM    784  C   PHE A 140     176.830 260.291 240.513  1.00 65.61           C  
ATOM    785  O   PHE A 140     177.112 260.216 241.710  1.00 66.12           O  
ATOM    786  CB  PHE A 140     174.497 260.270 239.698  1.00 65.64           C  
ATOM    787  CG  PHE A 140     174.092 261.036 240.903  1.00 66.03           C  
ATOM    788  CD1 PHE A 140     174.501 262.355 241.061  1.00 65.95           C  
ATOM    789  CD2 PHE A 140     173.327 260.457 241.889  1.00 66.70           C  
ATOM    790  CE1 PHE A 140     174.151 263.075 242.177  1.00 66.45           C  
ATOM    791  CE2 PHE A 140     172.972 261.172 243.010  1.00 67.95           C  
ATOM    792  CZ  PHE A 140     173.386 262.486 243.155  1.00 68.66           C  
ATOM    793  N   LEU A 141     177.421 261.127 239.678  1.00 65.93           N  
ATOM    794  CA  LEU A 141     178.415 262.082 240.119  1.00 66.10           C  
ATOM    795  C   LEU A 141     177.875 263.485 239.858  1.00 66.05           C  
ATOM    796  O   LEU A 141     177.135 263.694 238.898  1.00 65.36           O  
ATOM    797  CB  LEU A 141     179.712 261.796 239.362  1.00 66.18           C  
ATOM    798  CG  LEU A 141     180.214 260.307 239.488  1.00 65.59           C  
ATOM    799  CD1 LEU A 141     181.334 260.069 238.536  1.00 63.54           C  
ATOM    800  CD2 LEU A 141     180.674 260.024 240.905  1.00 67.76           C  
ATOM    801  N   GLY A 142     178.209 264.440 240.716  1.00 66.79           N  
ATOM    802  CA  GLY A 142     177.691 265.797 240.548  1.00 66.47           C  
ATOM    803  C   GLY A 142     178.595 266.673 239.686  1.00 67.42           C  
ATOM    804  O   GLY A 142     179.590 266.197 239.135  1.00 67.40           O  
ATOM    805  N   VAL A 143     178.240 267.967 239.586  1.00 67.92           N  
ATOM    806  CA  VAL A 143     178.967 268.980 238.810  1.00 69.17           C  
ATOM    807  C   VAL A 143     179.016 270.272 239.630  1.00 68.97           C  
ATOM    808  O   VAL A 143     178.047 270.635 240.301  1.00 69.22           O  
ATOM    809  CB  VAL A 143     178.293 269.236 237.400  1.00 68.50           C  
ATOM    810  CG1 VAL A 143     179.067 270.358 236.580  1.00 68.08           C  
ATOM    811  CG2 VAL A 143     178.272 267.903 236.548  1.00 68.20           C  
ATOM    812  N   CYS A 166     189.234 247.407 250.843  1.00 66.04           N  
ATOM    813  CA  CYS A 166     190.162 248.411 250.334  1.00 66.30           C  
ATOM    814  C   CYS A 166     191.573 247.814 250.198  1.00 66.85           C  
ATOM    815  O   CYS A 166     192.499 248.200 250.921  1.00 66.84           O  
ATOM    816  CB  CYS A 166     190.192 249.651 251.265  1.00 66.64           C  
ATOM    817  SG  CYS A 166     188.629 250.552 251.416  1.00 67.60           S  
ATOM    818  N   THR A 167     191.741 246.882 249.244  1.00 66.74           N  
ATOM    819  CA  THR A 167     193.009 246.178 249.013  1.00 66.73           C  
ATOM    820  C   THR A 167     193.889 246.907 248.005  1.00 66.83           C  
ATOM    821  O   THR A 167     195.030 246.515 247.764  1.00 67.83           O  
ATOM    822  CB  THR A 167     192.756 244.746 248.519  1.00 67.26           C  
ATOM    823  OG1 THR A 167     192.128 244.783 247.239  1.00 67.07           O  
ATOM    824  CG2 THR A 167     191.844 244.027 249.496  1.00 67.15           C  
ATOM    825  N   PHE A 168     193.343 247.950 247.398  1.00 67.11           N  
ATOM    826  CA  PHE A 168     194.063 248.737 246.407  1.00 66.74           C  
ATOM    827  C   PHE A 168     193.548 250.165 246.315  1.00 65.87           C  
ATOM    828  O   PHE A 168     192.338 250.418 246.350  1.00 65.83           O  
ATOM    829  CB  PHE A 168     193.990 248.094 245.018  1.00 67.65           C  
ATOM    830  CG  PHE A 168     194.692 248.887 243.960  1.00 66.16           C  
ATOM    831  CD1 PHE A 168     196.025 248.676 243.682  1.00 66.69           C  
ATOM    832  CD2 PHE A 168     194.016 249.864 243.250  1.00 65.81           C  
ATOM    833  CE1 PHE A 168     196.665 249.418 242.715  1.00 67.01           C  
ATOM    834  CE2 PHE A 168     194.657 250.602 242.291  1.00 65.24           C  
ATOM    835  CZ  PHE A 168     195.979 250.378 242.021  1.00 65.76           C  
ATOM    836  N   GLU A 169     194.478 251.097 246.177  1.00 67.28           N  
ATOM    837  CA  GLU A 169     194.156 252.483 245.906  1.00 65.25           C  
ATOM    838  C   GLU A 169     195.258 253.138 245.097  1.00 66.47           C  
ATOM    839  O   GLU A 169     196.441 252.988 245.407  1.00 64.10           O  
ATOM    840  CB  GLU A 169     193.936 253.269 247.195  1.00 65.75           C  
ATOM    841  CG  GLU A 169     193.638 254.752 246.963  1.00 66.68           C  
ATOM    842  CD  GLU A 169     193.294 255.490 248.214  1.00 67.44           C  
ATOM    843  OE1 GLU A 169     193.263 254.885 249.257  1.00 65.76           O  
ATOM    844  OE2 GLU A 169     193.048 256.670 248.127  1.00 66.18           O  
ATOM    845  N   TYR A 170     194.866 253.895 244.086  1.00 65.84           N  
ATOM    846  CA  TYR A 170     195.812 254.645 243.278  1.00 66.10           C  
ATOM    847  C   TYR A 170     195.261 255.974 242.805  1.00 65.99           C  
ATOM    848  O   TYR A 170     194.142 256.057 242.302  1.00 66.16           O  
ATOM    849  CB  TYR A 170     196.248 253.822 242.078  1.00 66.11           C  
ATOM    850  CG  TYR A 170     197.017 254.613 241.084  1.00 66.24           C  
ATOM    851  CD1 TYR A 170     198.341 254.913 241.304  1.00 66.60           C  
ATOM    852  CD2 TYR A 170     196.385 255.052 239.943  1.00 66.73           C  
ATOM    853  CE1 TYR A 170     199.035 255.660 240.381  1.00 67.35           C  
ATOM    854  CE2 TYR A 170     197.073 255.793 239.020  1.00 66.68           C  
ATOM    855  CZ  TYR A 170     198.396 256.101 239.235  1.00 67.45           C  
ATOM    856  OH  TYR A 170     199.090 256.850 238.316  1.00 67.75           O  
ATOM    857  N   VAL A 171     196.061 257.019 242.930  1.00 66.85           N  
ATOM    858  CA  VAL A 171     195.656 258.326 242.445  1.00 67.03           C  
ATOM    859  C   VAL A 171     196.702 258.898 241.490  1.00 67.37           C  
ATOM    860  O   VAL A 171     197.880 258.982 241.843  1.00 66.79           O  
ATOM    861  CB  VAL A 171     195.441 259.288 243.627  1.00 66.12           C  
ATOM    862  CG1 VAL A 171     195.032 260.674 243.116  1.00 66.66           C  
ATOM    863  CG2 VAL A 171     194.372 258.707 244.555  1.00 66.74           C  
ATOM    864  N   SER A 172     196.263 259.323 240.293  1.00 67.35           N  
ATOM    865  CA  SER A 172     197.129 259.936 239.286  1.00 67.93           C  
ATOM    866  C   SER A 172     197.375 261.399 239.669  1.00 68.67           C  
ATOM    867  O   SER A 172     196.945 262.330 238.983  1.00 68.95           O  
ATOM    868  CB  SER A 172     196.508 259.813 237.890  1.00 68.20           C  
ATOM    869  OG  SER A 172     196.424 258.481 237.489  1.00 68.73           O  
ATOM    870  N   PHE A 186     179.974 264.638 218.870  1.00 59.34           N  
ATOM    871  CA  PHE A 186     180.952 264.386 219.909  1.00 58.46           C  
ATOM    872  C   PHE A 186     182.348 264.706 219.354  1.00 58.93           C  
ATOM    873  O   PHE A 186     182.566 264.685 218.133  1.00 58.55           O  
ATOM    874  CB  PHE A 186     180.869 262.919 220.389  1.00 57.96           C  
ATOM    875  CG  PHE A 186     179.526 262.521 221.074  1.00 58.36           C  
ATOM    876  CD1 PHE A 186     178.586 261.629 220.402  1.00 58.65           C  
ATOM    877  CD2 PHE A 186     179.164 263.026 222.385  1.00 59.12           C  
ATOM    878  CE1 PHE A 186     177.342 261.253 221.030  1.00 58.40           C  
ATOM    879  CE2 PHE A 186     177.921 262.653 223.007  1.00 58.91           C  
ATOM    880  CZ  PHE A 186     177.015 261.764 222.332  1.00 57.70           C  
ATOM    881  N   LYS A 187     183.289 265.036 220.260  1.00 58.22           N  
ATOM    882  CA  LYS A 187     184.652 265.463 219.923  1.00 57.88           C  
ATOM    883  C   LYS A 187     185.721 264.429 220.261  1.00 58.06           C  
ATOM    884  O   LYS A 187     186.812 264.451 219.692  1.00 58.48           O  
ATOM    885  CB  LYS A 187     184.971 266.770 220.638  1.00 58.77           C  
ATOM    886  CG  LYS A 187     184.132 267.953 220.186  1.00 58.07           C  
ATOM    887  CD  LYS A 187     184.539 269.212 220.928  1.00 58.70           C  
ATOM    888  CE  LYS A 187     183.744 270.420 220.470  1.00 60.04           C  
ATOM    889  NZ  LYS A 187     184.148 271.654 221.204  1.00 58.53           N  
ATOM    890  N   ASN A 188     185.435 263.544 221.210  1.00 57.13           N  
ATOM    891  CA  ASN A 188     186.438 262.572 221.634  1.00 57.82           C  
ATOM    892  C   ASN A 188     185.881 261.171 221.818  1.00 57.48           C  
ATOM    893  O   ASN A 188     184.798 260.975 222.370  1.00 58.74           O  
ATOM    894  CB  ASN A 188     187.105 263.031 222.917  1.00 58.28           C  
ATOM    895  N   LEU A 189     186.643 260.188 221.361  1.00 56.38           N  
ATOM    896  CA  LEU A 189     186.296 258.788 221.543  1.00 54.47           C  
ATOM    897  C   LEU A 189     187.249 258.109 222.505  1.00 55.03           C  
ATOM    898  O   LEU A 189     188.471 258.196 222.368  1.00 56.05           O  
ATOM    899  CB  LEU A 189     186.310 258.064 220.194  1.00 55.74           C  
ATOM    900  CG  LEU A 189     186.166 256.526 220.201  1.00 55.03           C  
ATOM    901  CD1 LEU A 189     184.803 256.117 220.704  1.00 55.35           C  
ATOM    902  CD2 LEU A 189     186.363 256.009 218.793  1.00 55.72           C  
ATOM    903  N   ARG A 190     186.678 257.422 223.483  1.00 54.06           N  
ATOM    904  CA  ARG A 190     187.465 256.676 224.447  1.00 53.61           C  
ATOM    905  C   ARG A 190     186.997 255.232 224.461  1.00 52.51           C  
ATOM    906  O   ARG A 190     185.819 254.957 224.689  1.00 55.65           O  
ATOM    907  CB  ARG A 190     187.314 257.282 225.835  1.00 54.13           C  
ATOM    908  CG  ARG A 190     187.753 258.741 225.953  1.00 54.05           C  
ATOM    909  CD  ARG A 190     187.387 259.335 227.270  1.00 54.65           C  
ATOM    910  NE  ARG A 190     188.146 258.757 228.374  1.00 54.06           N  
ATOM    911  CZ  ARG A 190     187.844 258.922 229.683  1.00 54.43           C  
ATOM    912  NH1 ARG A 190     186.802 259.640 230.034  1.00 56.35           N  
ATOM    913  NH2 ARG A 190     188.598 258.363 230.617  1.00 54.65           N  
ATOM    914  N   GLU A 191     187.910 254.306 224.215  1.00 53.10           N  
ATOM    915  CA  GLU A 191     187.528 252.904 224.184  1.00 51.23           C  
ATOM    916  C   GLU A 191     188.303 252.107 225.205  1.00 53.96           C  
ATOM    917  O   GLU A 191     189.471 252.389 225.468  1.00 50.51           O  
ATOM    918  CB  GLU A 191     187.718 252.328 222.788  1.00 52.56           C  
ATOM    919  CG  GLU A 191     186.914 253.047 221.731  1.00 52.89           C  
ATOM    920  CD  GLU A 191     186.858 252.320 220.441  1.00 52.96           C  
ATOM    921  OE1 GLU A 191     187.837 252.278 219.737  1.00 52.37           O  
ATOM    922  OE2 GLU A 191     185.820 251.774 220.167  1.00 53.54           O  
ATOM    923  N   PHE A 192     187.634 251.123 225.794  1.00 51.25           N  
ATOM    924  CA  PHE A 192     188.204 250.297 226.838  1.00 52.07           C  
ATOM    925  C   PHE A 192     187.877 248.824 226.673  1.00 53.14           C  
ATOM    926  O   PHE A 192     186.832 248.463 226.136  1.00 51.70           O  
ATOM    927  CB  PHE A 192     187.661 250.747 228.185  1.00 52.55           C  
ATOM    928  CG  PHE A 192     187.919 252.167 228.474  1.00 52.21           C  
ATOM    929  CD1 PHE A 192     187.054 253.139 228.006  1.00 52.76           C  
ATOM    930  CD2 PHE A 192     189.014 252.552 229.199  1.00 53.05           C  
ATOM    931  CE1 PHE A 192     187.282 254.461 228.248  1.00 53.44           C  
ATOM    932  CE2 PHE A 192     189.250 253.881 229.447  1.00 52.70           C  
ATOM    933  CZ  PHE A 192     188.380 254.837 228.966  1.00 53.36           C  
ATOM    934  N   VAL A 193     188.737 247.974 227.195  1.00 51.83           N  
ATOM    935  CA  VAL A 193     188.413 246.561 227.306  1.00 51.94           C  
ATOM    936  C   VAL A 193     188.592 246.141 228.736  1.00 56.06           C  
ATOM    937  O   VAL A 193     189.635 246.403 229.333  1.00 50.01           O  
ATOM    938  CB  VAL A 193     189.297 245.676 226.421  1.00 51.61           C  
ATOM    939  CG1 VAL A 193     188.918 244.224 226.579  1.00 52.11           C  
ATOM    940  CG2 VAL A 193     189.159 246.099 225.013  1.00 52.01           C  
ATOM    941  N   PHE A 194     187.578 245.507 229.293  1.00 53.46           N  
ATOM    942  CA  PHE A 194     187.650 245.036 230.660  1.00 54.05           C  
ATOM    943  C   PHE A 194     187.469 243.528 230.710  1.00 54.81           C  
ATOM    944  O   PHE A 194     186.385 243.018 230.429  1.00 56.51           O  
ATOM    945  CB  PHE A 194     186.564 245.704 231.505  1.00 55.30           C  
ATOM    946  CG  PHE A 194     186.661 247.205 231.569  1.00 55.24           C  
ATOM    947  CD1 PHE A 194     185.868 248.011 230.771  1.00 54.41           C  
ATOM    948  CD2 PHE A 194     187.545 247.809 232.418  1.00 56.12           C  
ATOM    949  CE1 PHE A 194     185.964 249.390 230.841  1.00 54.26           C  
ATOM    950  CE2 PHE A 194     187.648 249.184 232.488  1.00 56.22           C  
ATOM    951  CZ  PHE A 194     186.854 249.973 231.698  1.00 55.24           C  
ATOM    952  N   LYS A 195     188.510 242.797 231.072  1.00 55.53           N  
ATOM    953  CA  LYS A 195     188.341 241.350 231.183  1.00 56.41           C  
ATOM    954  C   LYS A 195     188.949 240.875 232.490  1.00 58.09           C  
ATOM    955  O   LYS A 195     189.930 241.439 232.968  1.00 58.41           O  
ATOM    956  CB  LYS A 195     188.902 240.604 229.963  1.00 55.96           C  
ATOM    957  CG  LYS A 195     190.402 240.644 229.757  1.00 55.87           C  
ATOM    958  CD  LYS A 195     190.784 239.883 228.469  1.00 53.22           C  
ATOM    959  CE  LYS A 195     192.294 239.682 228.355  1.00 52.90           C  
ATOM    960  NZ  LYS A 195     192.688 238.964 227.095  1.00 50.99           N  
ATOM    961  N   ASN A 196     188.351 239.853 233.091  1.00 58.95           N  
ATOM    962  CA  ASN A 196     188.788 239.413 234.412  1.00 60.68           C  
ATOM    963  C   ASN A 196     189.095 237.927 234.417  1.00 60.83           C  
ATOM    964  O   ASN A 196     188.187 237.094 234.458  1.00 60.81           O  
ATOM    965  CB  ASN A 196     187.717 239.747 235.433  1.00 60.29           C  
ATOM    966  N   ILE A 197     190.374 237.596 234.316  1.00 61.96           N  
ATOM    967  CA  ILE A 197     190.779 236.206 234.189  1.00 62.67           C  
ATOM    968  C   ILE A 197     191.690 235.765 235.324  1.00 63.95           C  
ATOM    969  O   ILE A 197     192.751 236.346 235.555  1.00 63.78           O  
ATOM    970  CB  ILE A 197     191.464 235.972 232.833  1.00 61.78           C  
ATOM    971  CG1 ILE A 197     190.467 236.323 231.694  1.00 60.42           C  
ATOM    972  CG2 ILE A 197     191.941 234.521 232.731  1.00 62.64           C  
ATOM    973  CD1 ILE A 197     191.077 236.370 230.313  1.00 58.04           C  
ATOM    974  N   ASP A 198     191.265 234.720 236.023  1.00 63.77           N  
ATOM    975  CA  ASP A 198     192.007 234.126 237.130  1.00 64.63           C  
ATOM    976  C   ASP A 198     192.419 235.145 238.188  1.00 64.48           C  
ATOM    977  O   ASP A 198     193.521 235.087 238.732  1.00 65.93           O  
ATOM    978  CB  ASP A 198     193.225 233.374 236.607  1.00 65.08           C  
ATOM    979  CG  ASP A 198     192.823 232.232 235.679  1.00 64.94           C  
ATOM    980  OD1 ASP A 198     191.669 231.856 235.692  1.00 65.12           O  
ATOM    981  OD2 ASP A 198     193.669 231.739 234.973  1.00 65.78           O  
ATOM    982  N   GLY A 199     191.524 236.080 238.487  1.00 63.65           N  
ATOM    983  CA  GLY A 199     191.770 237.070 239.524  1.00 63.63           C  
ATOM    984  C   GLY A 199     192.412 238.361 239.025  1.00 64.63           C  
ATOM    985  O   GLY A 199     192.536 239.316 239.798  1.00 65.35           O  
ATOM    986  N   TYR A 200     192.825 238.403 237.760  1.00 61.44           N  
ATOM    987  CA  TYR A 200     193.462 239.602 237.226  1.00 62.00           C  
ATOM    988  C   TYR A 200     192.529 240.390 236.326  1.00 61.90           C  
ATOM    989  O   TYR A 200     192.048 239.886 235.306  1.00 61.72           O  
ATOM    990  CB  TYR A 200     194.714 239.240 236.440  1.00 62.90           C  
ATOM    991  CG  TYR A 200     195.819 238.663 237.258  1.00 63.87           C  
ATOM    992  CD1 TYR A 200     195.854 237.304 237.492  1.00 64.11           C  
ATOM    993  CD2 TYR A 200     196.813 239.483 237.761  1.00 63.96           C  
ATOM    994  CE1 TYR A 200     196.879 236.760 238.226  1.00 65.51           C  
ATOM    995  CE2 TYR A 200     197.844 238.938 238.496  1.00 65.67           C  
ATOM    996  CZ  TYR A 200     197.876 237.579 238.728  1.00 66.91           C  
ATOM    997  OH  TYR A 200     198.903 237.027 239.453  1.00 67.35           O  
ATOM    998  N   PHE A 201     192.303 241.641 236.692  1.00 60.64           N  
ATOM    999  CA  PHE A 201     191.436 242.522 235.939  1.00 59.24           C  
ATOM   1000  C   PHE A 201     192.276 243.365 235.001  1.00 59.46           C  
ATOM   1001  O   PHE A 201     193.055 244.221 235.432  1.00 59.02           O  
ATOM   1002  CB  PHE A 201     190.653 243.387 236.905  1.00 59.98           C  
ATOM   1003  CG  PHE A 201     189.565 244.181 236.322  1.00 59.90           C  
ATOM   1004  CD1 PHE A 201     188.385 243.571 235.992  1.00 60.01           C  
ATOM   1005  CD2 PHE A 201     189.693 245.537 236.128  1.00 58.31           C  
ATOM   1006  CE1 PHE A 201     187.347 244.285 235.470  1.00 58.92           C  
ATOM   1007  CE2 PHE A 201     188.652 246.261 235.609  1.00 57.88           C  
ATOM   1008  CZ  PHE A 201     187.480 245.630 235.281  1.00 57.94           C  
ATOM   1009  N   LYS A 202     192.163 243.080 233.717  1.00 57.90           N  
ATOM   1010  CA  LYS A 202     193.003 243.727 232.728  1.00 56.49           C  
ATOM   1011  C   LYS A 202     192.264 244.822 231.993  1.00 55.58           C  
ATOM   1012  O   LYS A 202     191.166 244.612 231.473  1.00 56.48           O  
ATOM   1013  CB  LYS A 202     193.544 242.698 231.745  1.00 56.47           C  
ATOM   1014  CG  LYS A 202     194.462 241.668 232.381  1.00 58.00           C  
ATOM   1015  CD  LYS A 202     195.046 240.731 231.338  1.00 57.22           C  
ATOM   1016  CE  LYS A 202     196.064 239.772 231.952  1.00 58.78           C  
ATOM   1017  NZ  LYS A 202     195.419 238.628 232.650  1.00 59.44           N  
ATOM   1018  N   ILE A 203     192.875 245.998 231.958  1.00 55.21           N  
ATOM   1019  CA  ILE A 203     192.280 247.145 231.307  1.00 53.24           C  
ATOM   1020  C   ILE A 203     193.109 247.606 230.121  1.00 54.26           C  
ATOM   1021  O   ILE A 203     194.282 247.978 230.266  1.00 54.01           O  
ATOM   1022  CB  ILE A 203     192.144 248.313 232.291  1.00 55.12           C  
ATOM   1023  CG1 ILE A 203     191.292 247.875 233.501  1.00 56.22           C  
ATOM   1024  CG2 ILE A 203     191.517 249.526 231.574  1.00 54.53           C  
ATOM   1025  CD1 ILE A 203     191.303 248.851 234.662  1.00 56.08           C  
ATOM   1026  N   TYR A 204     192.468 247.640 228.961  1.00 53.18           N  
ATOM   1027  CA  TYR A 204     193.093 248.096 227.727  1.00 52.85           C  
ATOM   1028  C   TYR A 204     192.365 249.340 227.303  1.00 54.24           C  
ATOM   1029  O   TYR A 204     191.179 249.469 227.592  1.00 51.57           O  
ATOM   1030  CB  TYR A 204     192.963 247.055 226.620  1.00 52.30           C  
ATOM   1031  CG  TYR A 204     193.507 245.702 226.956  1.00 52.24           C  
ATOM   1032  CD1 TYR A 204     192.825 244.871 227.829  1.00 51.64           C  
ATOM   1033  CD2 TYR A 204     194.659 245.274 226.375  1.00 50.51           C  
ATOM   1034  CE1 TYR A 204     193.315 243.635 228.121  1.00 52.94           C  
ATOM   1035  CE2 TYR A 204     195.156 244.028 226.666  1.00 50.95           C  
ATOM   1036  CZ  TYR A 204     194.488 243.211 227.539  1.00 51.37           C  
ATOM   1037  OH  TYR A 204     194.982 241.964 227.828  1.00 52.17           O  
ATOM   1038  N   SER A 205     193.035 250.252 226.619  1.00 50.98           N  
ATOM   1039  CA  SER A 205     192.319 251.427 226.151  1.00 51.90           C  
ATOM   1040  C   SER A 205     192.967 252.145 224.985  1.00 51.19           C  
ATOM   1041  O   SER A 205     194.117 251.887 224.617  1.00 52.10           O  
ATOM   1042  CB  SER A 205     192.134 252.408 227.280  1.00 52.07           C  
ATOM   1043  OG  SER A 205     193.345 252.960 227.644  1.00 52.89           O  
ATOM   1044  N   LYS A 206     192.187 253.036 224.387  1.00 51.74           N  
ATOM   1045  CA  LYS A 206     192.628 253.894 223.302  1.00 52.66           C  
ATOM   1046  C   LYS A 206     191.842 255.198 223.277  1.00 53.02           C  
ATOM   1047  O   LYS A 206     190.615 255.192 223.374  1.00 54.79           O  
ATOM   1048  CB  LYS A 206     192.484 253.165 221.962  1.00 51.90           C  
ATOM   1049  CG  LYS A 206     192.805 253.987 220.712  1.00 53.25           C  
ATOM   1050  CD  LYS A 206     194.292 254.237 220.563  1.00 53.55           C  
ATOM   1051  CE  LYS A 206     194.594 255.007 219.293  1.00 54.37           C  
ATOM   1052  NZ  LYS A 206     196.032 255.368 219.200  1.00 56.09           N  
ATOM   1053  N   HIS A 207     192.537 256.317 223.110  1.00 52.81           N  
ATOM   1054  CA  HIS A 207     191.865 257.602 222.953  1.00 53.73           C  
ATOM   1055  C   HIS A 207     192.145 258.161 221.568  1.00 54.93           C  
ATOM   1056  O   HIS A 207     193.270 258.071 221.070  1.00 55.03           O  
ATOM   1057  CB  HIS A 207     192.351 258.636 223.975  1.00 53.97           C  
ATOM   1058  CG  HIS A 207     192.068 258.346 225.419  1.00 54.10           C  
ATOM   1059  ND1 HIS A 207     192.468 259.203 226.421  1.00 54.85           N  
ATOM   1060  CD2 HIS A 207     191.438 257.319 226.040  1.00 53.47           C  
ATOM   1061  CE1 HIS A 207     192.106 258.716 227.588  1.00 54.93           C  
ATOM   1062  NE2 HIS A 207     191.481 257.576 227.387  1.00 53.67           N  
ATOM   1063  N   THR A 208     191.139 258.782 220.967  1.00 55.24           N  
ATOM   1064  CA  THR A 208     191.305 259.436 219.673  1.00 56.76           C  
ATOM   1065  C   THR A 208     190.249 260.519 219.492  1.00 57.24           C  
ATOM   1066  O   THR A 208     189.131 260.354 219.975  1.00 56.78           O  
ATOM   1067  CB  THR A 208     191.191 258.397 218.535  1.00 56.50           C  
ATOM   1068  OG1 THR A 208     191.391 259.023 217.257  1.00 57.20           O  
ATOM   1069  CG2 THR A 208     189.840 257.727 218.545  1.00 56.41           C  
ATOM   1070  N   PRO A 209     190.561 261.635 218.826  1.00 57.44           N  
ATOM   1071  CA  PRO A 209     189.622 262.680 218.477  1.00 58.23           C  
ATOM   1072  C   PRO A 209     188.658 262.194 217.411  1.00 58.62           C  
ATOM   1073  O   PRO A 209     189.047 261.430 216.524  1.00 57.14           O  
ATOM   1074  CB  PRO A 209     190.535 263.796 217.962  1.00 58.49           C  
ATOM   1075  CG  PRO A 209     191.782 263.085 217.477  1.00 58.37           C  
ATOM   1076  CD  PRO A 209     191.946 261.894 218.408  1.00 57.48           C  
ATOM   1077  N   ILE A 210     187.416 262.645 217.503  1.00 57.62           N  
ATOM   1078  CA  ILE A 210     186.381 262.338 216.529  1.00 57.87           C  
ATOM   1079  C   ILE A 210     185.572 263.575 216.173  1.00 58.20           C  
ATOM   1080  O   ILE A 210     185.669 264.603 216.838  1.00 57.64           O  
ATOM   1081  CB  ILE A 210     185.436 261.238 217.034  1.00 57.18           C  
ATOM   1082  CG1 ILE A 210     184.738 261.710 218.312  1.00 58.19           C  
ATOM   1083  CG2 ILE A 210     186.227 259.961 217.276  1.00 57.32           C  
ATOM   1084  CD1 ILE A 210     183.586 260.852 218.775  1.00 58.28           C  
ATOM   1085  N   ASN A 211     184.753 263.459 215.139  1.00 58.27           N  
ATOM   1086  CA  ASN A 211     183.780 264.492 214.813  1.00 58.07           C  
ATOM   1087  C   ASN A 211     182.509 263.819 214.313  1.00 58.77           C  
ATOM   1088  O   ASN A 211     182.337 263.611 213.111  1.00 58.81           O  
ATOM   1089  CB  ASN A 211     184.335 265.464 213.790  1.00 58.16           C  
ATOM   1090  CG  ASN A 211     183.418 266.634 213.549  1.00 58.98           C  
ATOM   1091  OD1 ASN A 211     182.317 266.704 214.110  1.00 58.43           O  
ATOM   1092  ND2 ASN A 211     183.851 267.555 212.724  1.00 57.86           N  
ATOM   1093  N   LEU A 212     181.659 263.407 215.251  1.00 57.21           N  
ATOM   1094  CA  LEU A 212     180.472 262.625 214.912  1.00 58.75           C  
ATOM   1095  C   LEU A 212     179.463 262.619 216.056  1.00 58.83           C  
ATOM   1096  O   LEU A 212     179.805 262.309 217.194  1.00 58.09           O  
ATOM   1097  CB  LEU A 212     180.887 261.190 214.523  1.00 58.53           C  
ATOM   1098  CG  LEU A 212     179.756 260.187 214.137  1.00 56.66           C  
ATOM   1099  CD1 LEU A 212     179.036 260.658 212.871  1.00 57.88           C  
ATOM   1100  CD2 LEU A 212     180.374 258.814 213.896  1.00 56.46           C  
ATOM   1101  N   VAL A 213     178.212 262.947 215.754  1.00 58.60           N  
ATOM   1102  CA  VAL A 213     177.167 263.033 216.776  1.00 58.67           C  
ATOM   1103  C   VAL A 213     176.165 261.892 216.697  1.00 58.47           C  
ATOM   1104  O   VAL A 213     175.065 261.988 217.236  1.00 57.46           O  
ATOM   1105  CB  VAL A 213     176.400 264.363 216.643  1.00 58.16           C  
ATOM   1106  CG1 VAL A 213     177.328 265.535 216.894  1.00 59.16           C  
ATOM   1107  CG2 VAL A 213     175.788 264.462 215.249  1.00 58.03           C  
ATOM   1108  N   ARG A 214     176.532 260.833 215.995  1.00 56.75           N  
ATOM   1109  CA  ARG A 214     175.651 259.692 215.816  1.00 56.62           C  
ATOM   1110  C   ARG A 214     176.057 258.521 216.710  1.00 56.52           C  
ATOM   1111  O   ARG A 214     175.540 258.372 217.815  1.00 55.80           O  
ATOM   1112  CB  ARG A 214     175.651 259.265 214.355  1.00 56.54           C  
ATOM   1113  CG  ARG A 214     174.786 258.057 214.011  1.00 56.33           C  
ATOM   1114  CD  ARG A 214     173.361 258.313 214.343  1.00 56.48           C  
ATOM   1115  NE  ARG A 214     172.530 257.182 213.974  1.00 56.44           N  
ATOM   1116  CZ  ARG A 214     171.284 256.929 214.401  1.00 57.09           C  
ATOM   1117  NH1 ARG A 214     170.667 257.740 215.239  1.00 57.48           N  
ATOM   1118  NH2 ARG A 214     170.695 255.836 213.956  1.00 56.79           N  
ATOM   1119  N   ASP A 215     176.978 257.690 216.230  1.00 55.89           N  
ATOM   1120  CA  ASP A 215     177.422 256.505 216.949  1.00 55.91           C  
ATOM   1121  C   ASP A 215     178.924 256.294 216.769  1.00 55.48           C  
ATOM   1122  O   ASP A 215     179.644 257.231 216.434  1.00 55.55           O  
ATOM   1123  CB  ASP A 215     176.626 255.283 216.493  1.00 54.43           C  
ATOM   1124  CG  ASP A 215     176.785 255.008 215.022  1.00 55.90           C  
ATOM   1125  OD1 ASP A 215     177.621 255.637 214.415  1.00 55.62           O  
ATOM   1126  OD2 ASP A 215     176.058 254.201 214.497  1.00 55.17           O  
ATOM   1127  N   LEU A 216     179.416 255.088 217.048  1.00 54.74           N  
ATOM   1128  CA  LEU A 216     180.844 254.833 216.933  1.00 54.65           C  
ATOM   1129  C   LEU A 216     181.279 254.949 215.472  1.00 54.57           C  
ATOM   1130  O   LEU A 216     180.706 254.277 214.617  1.00 54.30           O  
ATOM   1131  CB  LEU A 216     181.175 253.427 217.440  1.00 54.34           C  
ATOM   1132  CG  LEU A 216     180.947 253.175 218.937  1.00 54.69           C  
ATOM   1133  CD1 LEU A 216     181.114 251.691 219.220  1.00 54.70           C  
ATOM   1134  CD2 LEU A 216     181.951 253.993 219.765  1.00 55.43           C  
ATOM   1135  N   PRO A 217     182.305 255.750 215.152  1.00 54.33           N  
ATOM   1136  CA  PRO A 217     182.826 255.936 213.815  1.00 53.39           C  
ATOM   1137  C   PRO A 217     183.294 254.614 213.239  1.00 53.26           C  
ATOM   1138  O   PRO A 217     183.831 253.772 213.961  1.00 52.70           O  
ATOM   1139  CB  PRO A 217     184.020 256.873 214.039  1.00 53.68           C  
ATOM   1140  CG  PRO A 217     183.727 257.583 215.336  1.00 54.63           C  
ATOM   1141  CD  PRO A 217     182.958 256.585 216.176  1.00 54.85           C  
ATOM   1142  N   GLN A 218     183.134 254.440 211.937  1.00 52.98           N  
ATOM   1143  CA  GLN A 218     183.650 253.245 211.295  1.00 52.63           C  
ATOM   1144  C   GLN A 218     185.136 253.425 211.038  1.00 52.76           C  
ATOM   1145  O   GLN A 218     185.561 254.462 210.530  1.00 52.88           O  
ATOM   1146  CB  GLN A 218     182.907 252.956 209.995  1.00 52.57           C  
ATOM   1147  CG  GLN A 218     183.340 251.681 209.317  1.00 52.28           C  
ATOM   1148  CD  GLN A 218     182.469 251.342 208.146  1.00 52.29           C  
ATOM   1149  OE1 GLN A 218     181.558 252.096 207.797  1.00 52.14           O  
ATOM   1150  NE2 GLN A 218     182.735 250.204 207.520  1.00 52.06           N  
ATOM   1151  N   GLY A 219     185.925 252.422 211.394  1.00 52.28           N  
ATOM   1152  CA  GLY A 219     187.369 252.487 211.224  1.00 52.01           C  
ATOM   1153  C   GLY A 219     188.037 251.442 212.098  1.00 50.55           C  
ATOM   1154  O   GLY A 219     187.359 250.659 212.761  1.00 50.16           O  
ATOM   1155  N   PHE A 220     189.364 251.413 212.097  1.00 49.74           N  
ATOM   1156  CA  PHE A 220     190.071 250.416 212.886  1.00 48.45           C  
ATOM   1157  C   PHE A 220     191.214 250.993 213.696  1.00 48.35           C  
ATOM   1158  O   PHE A 220     192.023 251.773 213.192  1.00 48.07           O  
ATOM   1159  CB  PHE A 220     190.648 249.318 211.995  1.00 48.19           C  
ATOM   1160  CG  PHE A 220     191.379 248.290 212.785  1.00 47.27           C  
ATOM   1161  CD1 PHE A 220     190.719 247.215 213.316  1.00 47.30           C  
ATOM   1162  CD2 PHE A 220     192.724 248.419 213.023  1.00 46.58           C  
ATOM   1163  CE1 PHE A 220     191.382 246.286 214.064  1.00 46.51           C  
ATOM   1164  CE2 PHE A 220     193.391 247.499 213.774  1.00 47.25           C  
ATOM   1165  CZ  PHE A 220     192.722 246.428 214.296  1.00 46.67           C  
ATOM   1166  N   SER A 221     191.293 250.557 214.940  1.00 48.28           N  
ATOM   1167  CA  SER A 221     192.402 250.858 215.825  1.00 48.29           C  
ATOM   1168  C   SER A 221     192.490 249.754 216.857  1.00 48.54           C  
ATOM   1169  O   SER A 221     191.474 249.154 217.206  1.00 48.43           O  
ATOM   1170  CB  SER A 221     192.196 252.196 216.502  1.00 49.03           C  
ATOM   1171  OG  SER A 221     191.087 252.158 217.354  1.00 49.96           O  
ATOM   1172  N   ALA A 222     193.680 249.502 217.383  1.00 48.50           N  
ATOM   1173  CA  ALA A 222     193.807 248.502 218.427  1.00 48.69           C  
ATOM   1174  C   ALA A 222     194.041 249.163 219.766  1.00 49.55           C  
ATOM   1175  O   ALA A 222     194.755 250.161 219.867  1.00 49.96           O  
ATOM   1176  CB  ALA A 222     194.934 247.539 218.115  1.00 47.66           C  
ATOM   1177  N   LEU A 223     193.462 248.577 220.795  1.00 48.89           N  
ATOM   1178  CA  LEU A 223     193.610 249.074 222.153  1.00 50.96           C  
ATOM   1179  C   LEU A 223     194.812 248.428 222.815  1.00 51.94           C  
ATOM   1180  O   LEU A 223     195.165 247.295 222.497  1.00 50.89           O  
ATOM   1181  CB  LEU A 223     192.332 248.792 222.943  1.00 50.91           C  
ATOM   1182  CG  LEU A 223     191.179 249.808 222.773  1.00 51.12           C  
ATOM   1183  CD1 LEU A 223     190.763 249.931 221.306  1.00 51.41           C  
ATOM   1184  CD2 LEU A 223     190.020 249.349 223.596  1.00 51.66           C  
ATOM   1185  N   GLU A 224     195.448 249.141 223.736  1.00 51.28           N  
ATOM   1186  CA  GLU A 224     196.636 248.605 224.386  1.00 50.71           C  
ATOM   1187  C   GLU A 224     196.448 248.537 225.888  1.00 53.15           C  
ATOM   1188  O   GLU A 224     195.724 249.358 226.444  1.00 46.59           O  
ATOM   1189  CB  GLU A 224     197.826 249.499 224.047  1.00 50.51           C  
ATOM   1190  CG  GLU A 224     197.730 250.900 224.606  1.00 50.93           C  
ATOM   1191  CD  GLU A 224     198.870 251.763 224.183  1.00 51.22           C  
ATOM   1192  OE1 GLU A 224     198.925 252.115 223.030  1.00 49.65           O  
ATOM   1193  OE2 GLU A 224     199.702 252.067 225.006  1.00 51.43           O  
ATOM   1194  N   PRO A 225     197.082 247.578 226.570  1.00 51.72           N  
ATOM   1195  CA  PRO A 225     197.004 247.387 227.999  1.00 52.50           C  
ATOM   1196  C   PRO A 225     197.644 248.546 228.711  1.00 52.81           C  
ATOM   1197  O   PRO A 225     198.703 249.010 228.295  1.00 52.70           O  
ATOM   1198  CB  PRO A 225     197.790 246.093 228.215  1.00 51.89           C  
ATOM   1199  CG  PRO A 225     198.720 246.004 227.025  1.00 51.48           C  
ATOM   1200  CD  PRO A 225     197.963 246.628 225.879  1.00 51.16           C  
ATOM   1201  N   LEU A 226     197.027 248.982 229.799  1.00 52.83           N  
ATOM   1202  CA  LEU A 226     197.614 250.020 230.631  1.00 53.98           C  
ATOM   1203  C   LEU A 226     197.650 249.604 232.089  1.00 54.03           C  
ATOM   1204  O   LEU A 226     198.601 249.911 232.808  1.00 54.40           O  
ATOM   1205  CB  LEU A 226     196.835 251.332 230.513  1.00 53.31           C  
ATOM   1206  CG  LEU A 226     196.755 251.977 229.117  1.00 52.84           C  
ATOM   1207  CD1 LEU A 226     195.894 253.210 229.223  1.00 52.64           C  
ATOM   1208  CD2 LEU A 226     198.147 252.338 228.595  1.00 52.36           C  
ATOM   1209  N   VAL A 227     196.584 248.955 232.540  1.00 54.35           N  
ATOM   1210  CA  VAL A 227     196.444 248.632 233.951  1.00 55.46           C  
ATOM   1211  C   VAL A 227     196.122 247.158 234.161  1.00 56.33           C  
ATOM   1212  O   VAL A 227     195.364 246.559 233.400  1.00 57.31           O  
ATOM   1213  CB  VAL A 227     195.357 249.520 234.599  1.00 56.28           C  
ATOM   1214  CG1 VAL A 227     195.180 249.168 236.067  1.00 58.01           C  
ATOM   1215  CG2 VAL A 227     195.735 250.984 234.449  1.00 56.47           C  
ATOM   1216  N   ASP A 228     196.719 246.574 235.191  1.00 58.11           N  
ATOM   1217  CA  ASP A 228     196.461 245.187 235.560  1.00 58.93           C  
ATOM   1218  C   ASP A 228     196.280 245.098 237.071  1.00 59.70           C  
ATOM   1219  O   ASP A 228     197.240 245.258 237.828  1.00 60.95           O  
ATOM   1220  CB  ASP A 228     197.603 244.282 235.085  1.00 59.53           C  
ATOM   1221  CG  ASP A 228     197.365 242.795 235.351  1.00 60.22           C  
ATOM   1222  OD1 ASP A 228     196.515 242.481 236.143  1.00 61.37           O  
ATOM   1223  OD2 ASP A 228     198.033 241.988 234.741  1.00 60.71           O  
ATOM   1224  N   LEU A 229     195.034 244.929 237.508  1.00 60.56           N  
ATOM   1225  CA  LEU A 229     194.726 244.930 238.930  1.00 61.60           C  
ATOM   1226  C   LEU A 229     194.478 243.506 239.452  1.00 62.31           C  
ATOM   1227  O   LEU A 229     193.483 242.877 239.086  1.00 62.06           O  
ATOM   1228  CB  LEU A 229     193.471 245.775 239.217  1.00 61.58           C  
ATOM   1229  CG  LEU A 229     193.463 247.230 238.733  1.00 60.87           C  
ATOM   1230  CD1 LEU A 229     192.101 247.846 239.044  1.00 61.47           C  
ATOM   1231  CD2 LEU A 229     194.573 248.023 239.418  1.00 63.71           C  
ATOM   1232  N   PRO A 230     195.329 242.981 240.342  1.00 62.78           N  
ATOM   1233  CA  PRO A 230     195.256 241.650 240.913  1.00 63.33           C  
ATOM   1234  C   PRO A 230     194.218 241.647 242.018  1.00 63.63           C  
ATOM   1235  O   PRO A 230     194.551 241.537 243.197  1.00 64.07           O  
ATOM   1236  CB  PRO A 230     196.666 241.452 241.454  1.00 65.19           C  
ATOM   1237  CG  PRO A 230     197.087 242.846 241.870  1.00 65.24           C  
ATOM   1238  CD  PRO A 230     196.451 243.778 240.842  1.00 63.63           C  
ATOM   1239  N   ILE A 231     192.970 241.833 241.620  1.00 63.76           N  
ATOM   1240  CA  ILE A 231     191.870 242.036 242.546  1.00 63.59           C  
ATOM   1241  C   ILE A 231     191.369 240.795 243.271  1.00 64.00           C  
ATOM   1242  O   ILE A 231     190.996 240.883 244.439  1.00 64.83           O  
ATOM   1243  CB  ILE A 231     190.691 242.715 241.802  1.00 63.34           C  
ATOM   1244  CG1 ILE A 231     190.245 241.843 240.556  1.00 61.86           C  
ATOM   1245  CG2 ILE A 231     191.090 244.116 241.385  1.00 62.88           C  
ATOM   1246  CD1 ILE A 231     188.984 242.284 239.865  1.00 63.00           C  
ATOM   1247  N   GLY A 232     191.311 239.654 242.598  1.00 63.52           N  
ATOM   1248  CA  GLY A 232     190.787 238.456 243.246  1.00 63.78           C  
ATOM   1249  C   GLY A 232     189.277 238.575 243.491  1.00 63.97           C  
ATOM   1250  O   GLY A 232     188.708 237.835 244.291  1.00 63.86           O  
ATOM   1251  N   ILE A 233     188.636 239.518 242.814  1.00 64.44           N  
ATOM   1252  CA  ILE A 233     187.219 239.805 242.997  1.00 64.19           C  
ATOM   1253  C   ILE A 233     186.398 239.265 241.831  1.00 63.98           C  
ATOM   1254  O   ILE A 233     186.735 239.499 240.668  1.00 63.66           O  
ATOM   1255  CB  ILE A 233     186.975 241.332 243.166  1.00 64.02           C  
ATOM   1256  CG1 ILE A 233     187.662 241.836 244.462  1.00 64.69           C  
ATOM   1257  CG2 ILE A 233     185.470 241.662 243.150  1.00 64.33           C  
ATOM   1258  CD1 ILE A 233     187.740 243.364 244.593  1.00 65.10           C  
ATOM   1259  N   ASN A 234     185.319 238.542 242.164  1.00 65.00           N  
ATOM   1260  CA  ASN A 234     184.354 237.980 241.226  1.00 64.33           C  
ATOM   1261  C   ASN A 234     183.471 239.096 240.643  1.00 65.38           C  
ATOM   1262  O   ASN A 234     182.854 239.855 241.394  1.00 64.78           O  
ATOM   1263  CB  ASN A 234     183.517 236.905 241.922  1.00 66.45           C  
ATOM   1264  CG  ASN A 234     182.571 236.122 241.002  1.00 66.50           C  
ATOM   1265  OD1 ASN A 234     182.813 235.987 239.790  1.00 66.53           O  
ATOM   1266  ND2 ASN A 234     181.499 235.595 241.590  1.00 67.18           N  
ATOM   1267  N   ILE A 235     183.458 239.227 239.305  1.00 63.57           N  
ATOM   1268  CA  ILE A 235     182.693 240.249 238.582  1.00 63.02           C  
ATOM   1269  C   ILE A 235     181.702 239.581 237.652  1.00 62.99           C  
ATOM   1270  O   ILE A 235     182.084 238.772 236.809  1.00 62.65           O  
ATOM   1271  CB  ILE A 235     183.619 241.185 237.776  1.00 62.08           C  
ATOM   1272  CG1 ILE A 235     184.586 241.915 238.732  1.00 62.37           C  
ATOM   1273  CG2 ILE A 235     182.784 242.180 236.964  1.00 62.50           C  
ATOM   1274  CD1 ILE A 235     185.693 242.669 238.033  1.00 61.04           C  
ATOM   1275  N   THR A 236     180.429 239.909 237.823  1.00 63.75           N  
ATOM   1276  CA  THR A 236     179.376 239.346 236.997  1.00 61.78           C  
ATOM   1277  C   THR A 236     178.521 240.442 236.389  1.00 61.24           C  
ATOM   1278  O   THR A 236     177.820 240.214 235.400  1.00 61.20           O  
ATOM   1279  CB  THR A 236     178.502 238.384 237.807  1.00 63.92           C  
ATOM   1280  OG1 THR A 236     177.871 239.095 238.872  1.00 63.38           O  
ATOM   1281  CG2 THR A 236     179.337 237.258 238.383  1.00 65.47           C  
ATOM   1282  N   ARG A 237     178.579 241.627 236.994  1.00 59.61           N  
ATOM   1283  CA  ARG A 237     177.789 242.780 236.584  1.00 59.40           C  
ATOM   1284  C   ARG A 237     178.630 244.050 236.658  1.00 61.91           C  
ATOM   1285  O   ARG A 237     179.576 244.124 237.445  1.00 61.19           O  
ATOM   1286  CB  ARG A 237     176.582 242.956 237.485  1.00 62.22           C  
ATOM   1287  CG  ARG A 237     175.607 241.799 237.525  1.00 61.30           C  
ATOM   1288  CD  ARG A 237     174.419 242.127 238.365  1.00 62.70           C  
ATOM   1289  NE  ARG A 237     173.466 241.033 238.417  1.00 63.88           N  
ATOM   1290  CZ  ARG A 237     173.458 240.053 239.350  1.00 64.34           C  
ATOM   1291  NH1 ARG A 237     174.346 240.037 240.329  1.00 64.53           N  
ATOM   1292  NH2 ARG A 237     172.544 239.099 239.280  1.00 63.60           N  
ATOM   1293  N   PHE A 238     178.248 245.076 235.906  1.00 58.95           N  
ATOM   1294  CA  PHE A 238     178.940 246.351 236.019  1.00 58.21           C  
ATOM   1295  C   PHE A 238     178.019 247.529 235.721  1.00 60.59           C  
ATOM   1296  O   PHE A 238     176.936 247.362 235.163  1.00 56.27           O  
ATOM   1297  CB  PHE A 238     180.141 246.387 235.086  1.00 60.85           C  
ATOM   1298  CG  PHE A 238     179.814 246.532 233.657  1.00 58.82           C  
ATOM   1299  CD1 PHE A 238     179.922 247.780 233.063  1.00 59.15           C  
ATOM   1300  CD2 PHE A 238     179.388 245.466 232.897  1.00 57.82           C  
ATOM   1301  CE1 PHE A 238     179.621 247.955 231.744  1.00 58.05           C  
ATOM   1302  CE2 PHE A 238     179.082 245.647 231.574  1.00 57.64           C  
ATOM   1303  CZ  PHE A 238     179.202 246.891 231.002  1.00 57.65           C  
ATOM   1304  N   GLN A 239     178.448 248.727 236.099  1.00 59.08           N  
ATOM   1305  CA  GLN A 239     177.658 249.929 235.849  1.00 57.68           C  
ATOM   1306  C   GLN A 239     178.514 251.133 235.469  1.00 57.89           C  
ATOM   1307  O   GLN A 239     179.629 251.292 235.956  1.00 60.78           O  
ATOM   1308  CB  GLN A 239     176.802 250.239 237.068  1.00 59.95           C  
ATOM   1309  CG  GLN A 239     175.867 251.392 236.887  1.00 59.17           C  
ATOM   1310  CD  GLN A 239     174.800 251.407 237.926  1.00 60.64           C  
ATOM   1311  OE1 GLN A 239     174.985 250.929 239.049  1.00 61.60           O  
ATOM   1312  NE2 GLN A 239     173.649 251.944 237.556  1.00 60.77           N  
ATOM   1313  N   THR A 240     177.993 251.981 234.589  1.00 58.33           N  
ATOM   1314  CA  THR A 240     178.705 253.181 234.155  1.00 58.13           C  
ATOM   1315  C   THR A 240     178.257 254.417 234.931  1.00 58.37           C  
ATOM   1316  O   THR A 240     177.065 254.640 235.135  1.00 58.92           O  
ATOM   1317  CB  THR A 240     178.503 253.403 232.651  1.00 56.89           C  
ATOM   1318  OG1 THR A 240     178.966 252.250 231.954  1.00 56.19           O  
ATOM   1319  CG2 THR A 240     179.274 254.628 232.156  1.00 57.15           C  
ATOM   1320  N   LEU A 241     179.224 255.218 235.365  1.00 60.32           N  
ATOM   1321  CA  LEU A 241     178.953 256.422 236.141  1.00 59.83           C  
ATOM   1322  C   LEU A 241     179.182 257.731 235.371  1.00 61.03           C  
ATOM   1323  O   LEU A 241     180.270 257.963 234.828  1.00 60.79           O  
ATOM   1324  CB  LEU A 241     179.858 256.440 237.374  1.00 59.92           C  
ATOM   1325  CG  LEU A 241     179.768 255.235 238.291  1.00 58.92           C  
ATOM   1326  CD1 LEU A 241     180.779 255.398 239.402  1.00 60.23           C  
ATOM   1327  CD2 LEU A 241     178.368 255.126 238.842  1.00 62.29           C  
ATOM   1328  N   LEU A 242     178.156 258.604 235.386  1.00 60.59           N  
ATOM   1329  CA  LEU A 242     178.159 259.936 234.769  1.00 60.55           C  
ATOM   1330  C   LEU A 242     178.043 260.983 235.871  1.00 62.37           C  
ATOM   1331  O   LEU A 242     177.165 260.888 236.736  1.00 62.05           O  
ATOM   1332  CB  LEU A 242     176.982 260.093 233.756  1.00 61.97           C  
ATOM   1333  N   ALA A 263     176.429 262.239 226.349  1.00 56.71           N  
ATOM   1334  CA  ALA A 263     177.559 261.319 226.455  1.00 57.54           C  
ATOM   1335  C   ALA A 263     177.069 259.865 226.441  1.00 56.23           C  
ATOM   1336  O   ALA A 263     176.796 259.271 227.489  1.00 56.39           O  
ATOM   1337  CB  ALA A 263     178.367 261.610 227.715  1.00 59.45           C  
ATOM   1338  N   ALA A 264     176.964 259.304 225.231  1.00 55.22           N  
ATOM   1339  CA  ALA A 264     176.529 257.932 224.985  1.00 55.96           C  
ATOM   1340  C   ALA A 264     177.667 256.937 225.156  1.00 54.78           C  
ATOM   1341  O   ALA A 264     178.833 257.262 224.920  1.00 55.80           O  
ATOM   1342  CB  ALA A 264     175.967 257.813 223.586  1.00 57.15           C  
ATOM   1343  N   TYR A 265     177.313 255.708 225.508  1.00 54.70           N  
ATOM   1344  CA  TYR A 265     178.286 254.633 225.582  1.00 55.33           C  
ATOM   1345  C   TYR A 265     177.739 253.342 224.998  1.00 55.62           C  
ATOM   1346  O   TYR A 265     176.530 253.167 224.850  1.00 41.67           O  
ATOM   1347  CB  TYR A 265     178.780 254.434 227.006  1.00 55.73           C  
ATOM   1348  CG  TYR A 265     177.772 253.947 227.987  1.00 54.73           C  
ATOM   1349  CD1 TYR A 265     177.629 252.598 228.201  1.00 54.43           C  
ATOM   1350  CD2 TYR A 265     177.011 254.848 228.692  1.00 54.67           C  
ATOM   1351  CE1 TYR A 265     176.726 252.143 229.119  1.00 54.99           C  
ATOM   1352  CE2 TYR A 265     176.104 254.397 229.609  1.00 54.64           C  
ATOM   1353  CZ  TYR A 265     175.962 253.047 229.824  1.00 54.03           C  
ATOM   1354  OH  TYR A 265     175.048 252.595 230.739  1.00 56.32           O  
ATOM   1355  N   TYR A 266     178.644 252.455 224.625  1.00 55.37           N  
ATOM   1356  CA  TYR A 266     178.286 251.230 223.946  1.00 52.84           C  
ATOM   1357  C   TYR A 266     178.864 250.044 224.676  1.00 51.42           C  
ATOM   1358  O   TYR A 266     180.004 250.087 225.139  1.00 54.25           O  
ATOM   1359  CB  TYR A 266     178.830 251.296 222.523  1.00 53.82           C  
ATOM   1360  CG  TYR A 266     178.435 252.581 221.857  1.00 53.72           C  
ATOM   1361  CD1 TYR A 266     179.206 253.711 222.087  1.00 53.79           C  
ATOM   1362  CD2 TYR A 266     177.322 252.661 221.060  1.00 54.69           C  
ATOM   1363  CE1 TYR A 266     178.859 254.909 221.547  1.00 54.86           C  
ATOM   1364  CE2 TYR A 266     176.982 253.876 220.510  1.00 55.11           C  
ATOM   1365  CZ  TYR A 266     177.745 254.994 220.764  1.00 54.61           C  
ATOM   1366  OH  TYR A 266     177.384 256.204 220.254  1.00 53.11           O  
ATOM   1367  N   VAL A 267     178.088 248.979 224.771  1.00 52.57           N  
ATOM   1368  CA  VAL A 267     178.562 247.776 225.434  1.00 51.33           C  
ATOM   1369  C   VAL A 267     178.433 246.528 224.588  1.00 50.60           C  
ATOM   1370  O   VAL A 267     177.336 246.164 224.154  1.00 52.78           O  
ATOM   1371  CB  VAL A 267     177.795 247.572 226.744  1.00 52.69           C  
ATOM   1372  CG1 VAL A 267     178.225 246.280 227.423  1.00 53.29           C  
ATOM   1373  CG2 VAL A 267     178.060 248.769 227.649  1.00 53.06           C  
ATOM   1374  N   GLY A 268     179.550 245.841 224.402  1.00 52.03           N  
ATOM   1375  CA  GLY A 268     179.560 244.584 223.680  1.00 52.02           C  
ATOM   1376  C   GLY A 268     180.195 243.521 224.548  1.00 51.58           C  
ATOM   1377  O   GLY A 268     180.681 243.820 225.638  1.00 53.73           O  
ATOM   1378  N   TYR A 269     180.223 242.287 224.071  1.00 51.77           N  
ATOM   1379  CA  TYR A 269     180.833 241.230 224.860  1.00 52.19           C  
ATOM   1380  C   TYR A 269     181.886 240.493 224.077  1.00 50.66           C  
ATOM   1381  O   TYR A 269     181.747 240.273 222.874  1.00 50.62           O  
ATOM   1382  CB  TYR A 269     179.764 240.297 225.397  1.00 52.61           C  
ATOM   1383  CG  TYR A 269     178.857 241.028 226.325  1.00 53.78           C  
ATOM   1384  CD1 TYR A 269     177.707 241.619 225.850  1.00 53.95           C  
ATOM   1385  CD2 TYR A 269     179.196 241.145 227.650  1.00 54.93           C  
ATOM   1386  CE1 TYR A 269     176.898 242.323 226.705  1.00 54.26           C  
ATOM   1387  CE2 TYR A 269     178.394 241.842 228.498  1.00 55.40           C  
ATOM   1388  CZ  TYR A 269     177.246 242.436 228.034  1.00 54.89           C  
ATOM   1389  OH  TYR A 269     176.435 243.147 228.887  1.00 56.77           O  
ATOM   1390  N   LEU A 270     182.929 240.094 224.780  1.00 51.49           N  
ATOM   1391  CA  LEU A 270     184.066 239.446 224.160  1.00 49.73           C  
ATOM   1392  C   LEU A 270     183.831 237.954 224.016  1.00 49.67           C  
ATOM   1393  O   LEU A 270     183.154 237.342 224.843  1.00 50.05           O  
ATOM   1394  CB  LEU A 270     185.299 239.676 225.020  1.00 50.56           C  
ATOM   1395  CG  LEU A 270     185.637 241.128 225.376  1.00 51.50           C  
ATOM   1396  CD1 LEU A 270     186.825 241.118 226.303  1.00 52.00           C  
ATOM   1397  CD2 LEU A 270     185.934 241.937 224.135  1.00 50.89           C  
ATOM   1398  N   GLN A 271     184.398 237.367 222.968  1.00 49.32           N  
ATOM   1399  CA  GLN A 271     184.282 235.937 222.729  1.00 48.57           C  
ATOM   1400  C   GLN A 271     185.640 235.343 222.349  1.00 49.02           C  
ATOM   1401  O   GLN A 271     186.465 236.028 221.741  1.00 47.80           O  
ATOM   1402  CB  GLN A 271     183.240 235.698 221.634  1.00 48.35           C  
ATOM   1403  CG  GLN A 271     181.845 236.163 222.027  1.00 48.95           C  
ATOM   1404  CD  GLN A 271     180.795 235.813 221.012  1.00 48.21           C  
ATOM   1405  OE1 GLN A 271     181.098 235.558 219.843  1.00 47.93           O  
ATOM   1406  NE2 GLN A 271     179.541 235.797 221.446  1.00 47.91           N  
ATOM   1407  N   PRO A 272     185.887 234.060 222.654  1.00 48.07           N  
ATOM   1408  CA  PRO A 272     187.122 233.331 222.404  1.00 47.84           C  
ATOM   1409  C   PRO A 272     187.292 232.940 220.949  1.00 47.25           C  
ATOM   1410  O   PRO A 272     187.248 231.761 220.598  1.00 47.32           O  
ATOM   1411  CB  PRO A 272     186.951 232.103 223.300  1.00 48.34           C  
ATOM   1412  CG  PRO A 272     185.461 231.870 223.326  1.00 47.79           C  
ATOM   1413  CD  PRO A 272     184.854 233.260 223.339  1.00 48.11           C  
ATOM   1414  N   ARG A 273     187.479 233.944 220.110  1.00 47.05           N  
ATOM   1415  CA  ARG A 273     187.619 233.741 218.682  1.00 46.04           C  
ATOM   1416  C   ARG A 273     189.045 234.007 218.231  1.00 46.51           C  
ATOM   1417  O   ARG A 273     189.772 234.787 218.852  1.00 46.73           O  
ATOM   1418  CB  ARG A 273     186.658 234.642 217.934  1.00 46.26           C  
ATOM   1419  CG  ARG A 273     185.203 234.325 218.186  1.00 46.68           C  
ATOM   1420  CD  ARG A 273     184.301 235.265 217.496  1.00 46.50           C  
ATOM   1421  NE  ARG A 273     182.909 234.981 217.811  1.00 47.11           N  
ATOM   1422  CZ  ARG A 273     182.102 234.144 217.131  1.00 47.21           C  
ATOM   1423  NH1 ARG A 273     182.539 233.501 216.081  1.00 46.44           N  
ATOM   1424  NH2 ARG A 273     180.860 233.978 217.539  1.00 47.24           N  
ATOM   1425  N   THR A 274     189.432 233.351 217.145  1.00 45.34           N  
ATOM   1426  CA  THR A 274     190.749 233.527 216.561  1.00 44.27           C  
ATOM   1427  C   THR A 274     190.766 234.722 215.627  1.00 44.45           C  
ATOM   1428  O   THR A 274     189.807 234.954 214.887  1.00 45.53           O  
ATOM   1429  CB  THR A 274     191.189 232.266 215.791  1.00 44.59           C  
ATOM   1430  OG1 THR A 274     191.195 231.138 216.673  1.00 44.70           O  
ATOM   1431  CG2 THR A 274     192.594 232.444 215.212  1.00 44.39           C  
ATOM   1432  N   PHE A 275     191.833 235.498 215.721  1.00 43.68           N  
ATOM   1433  CA  PHE A 275     192.077 236.630 214.848  1.00 43.72           C  
ATOM   1434  C   PHE A 275     193.442 236.580 214.197  1.00 43.85           C  
ATOM   1435  O   PHE A 275     194.427 236.160 214.806  1.00 44.88           O  
ATOM   1436  CB  PHE A 275     191.938 237.950 215.602  1.00 44.73           C  
ATOM   1437  CG  PHE A 275     190.538 238.350 215.876  1.00 45.14           C  
ATOM   1438  CD1 PHE A 275     189.767 237.717 216.821  1.00 46.04           C  
ATOM   1439  CD2 PHE A 275     189.987 239.396 215.167  1.00 45.57           C  
ATOM   1440  CE1 PHE A 275     188.472 238.113 217.035  1.00 45.73           C  
ATOM   1441  CE2 PHE A 275     188.703 239.794 215.389  1.00 45.81           C  
ATOM   1442  CZ  PHE A 275     187.940 239.154 216.322  1.00 46.52           C  
ATOM   1443  N   LEU A 276     193.506 237.075 212.973  1.00 43.63           N  
ATOM   1444  CA  LEU A 276     194.785 237.275 212.313  1.00 42.95           C  
ATOM   1445  C   LEU A 276     195.095 238.754 212.413  1.00 45.08           C  
ATOM   1446  O   LEU A 276     194.345 239.579 211.896  1.00 43.22           O  
ATOM   1447  CB  LEU A 276     194.722 236.847 210.842  1.00 43.53           C  
ATOM   1448  CG  LEU A 276     196.007 236.999 210.014  1.00 42.92           C  
ATOM   1449  CD1 LEU A 276     197.077 236.031 210.527  1.00 42.75           C  
ATOM   1450  CD2 LEU A 276     195.681 236.745 208.542  1.00 41.92           C  
ATOM   1451  N   LEU A 277     196.164 239.107 213.105  1.00 43.15           N  
ATOM   1452  CA  LEU A 277     196.469 240.514 213.319  1.00 43.10           C  
ATOM   1453  C   LEU A 277     197.618 240.977 212.446  1.00 43.77           C  
ATOM   1454  O   LEU A 277     198.657 240.320 212.364  1.00 43.35           O  
ATOM   1455  CB  LEU A 277     196.818 240.740 214.790  1.00 44.29           C  
ATOM   1456  CG  LEU A 277     195.774 240.256 215.821  1.00 44.49           C  
ATOM   1457  CD1 LEU A 277     196.311 240.506 217.210  1.00 45.68           C  
ATOM   1458  CD2 LEU A 277     194.457 240.979 215.616  1.00 45.06           C  
ATOM   1459  N   LYS A 278     197.439 242.121 211.802  1.00 42.70           N  
ATOM   1460  CA  LYS A 278     198.471 242.671 210.940  1.00 42.10           C  
ATOM   1461  C   LYS A 278     199.240 243.798 211.587  1.00 45.99           C  
ATOM   1462  O   LYS A 278     198.688 244.875 211.836  1.00 43.41           O  
ATOM   1463  CB  LYS A 278     197.863 243.172 209.637  1.00 43.19           C  
ATOM   1464  CG  LYS A 278     198.852 243.800 208.677  1.00 43.06           C  
ATOM   1465  CD  LYS A 278     198.176 244.182 207.383  1.00 43.71           C  
ATOM   1466  CE  LYS A 278     199.152 244.841 206.432  1.00 44.32           C  
ATOM   1467  NZ  LYS A 278     198.503 245.222 205.150  1.00 44.43           N  
ATOM   1468  N   TYR A 279     200.532 243.555 211.811  1.00 43.11           N  
ATOM   1469  CA  TYR A 279     201.438 244.536 212.393  1.00 43.98           C  
ATOM   1470  C   TYR A 279     202.217 245.227 211.288  1.00 44.44           C  
ATOM   1471  O   TYR A 279     202.856 244.567 210.465  1.00 44.89           O  
ATOM   1472  CB  TYR A 279     202.419 243.861 213.343  1.00 45.76           C  
ATOM   1473  CG  TYR A 279     201.813 243.319 214.589  1.00 43.65           C  
ATOM   1474  CD1 TYR A 279     201.240 242.063 214.592  1.00 44.16           C  
ATOM   1475  CD2 TYR A 279     201.847 244.062 215.739  1.00 44.82           C  
ATOM   1476  CE1 TYR A 279     200.701 241.563 215.748  1.00 44.39           C  
ATOM   1477  CE2 TYR A 279     201.312 243.559 216.894  1.00 45.38           C  
ATOM   1478  CZ  TYR A 279     200.741 242.312 216.900  1.00 45.53           C  
ATOM   1479  OH  TYR A 279     200.206 241.806 218.056  1.00 46.35           O  
ATOM   1480  N   ASN A 280     202.208 246.551 211.290  1.00 43.13           N  
ATOM   1481  CA  ASN A 280     202.923 247.306 210.271  1.00 44.12           C  
ATOM   1482  C   ASN A 280     204.388 247.438 210.645  1.00 44.89           C  
ATOM   1483  O   ASN A 280     204.854 246.810 211.597  1.00 40.26           O  
ATOM   1484  CB  ASN A 280     202.298 248.670 210.040  1.00 44.57           C  
ATOM   1485  CG  ASN A 280     202.468 249.622 211.193  1.00 46.78           C  
ATOM   1486  OD1 ASN A 280     203.149 249.317 212.183  1.00 46.84           O  
ATOM   1487  ND2 ASN A 280     201.884 250.789 211.067  1.00 45.20           N  
ATOM   1488  N   GLU A 281     205.128 248.228 209.884  1.00 44.77           N  
ATOM   1489  CA  GLU A 281     206.565 248.394 210.110  1.00 44.38           C  
ATOM   1490  C   GLU A 281     206.916 248.934 211.506  1.00 44.60           C  
ATOM   1491  O   GLU A 281     207.957 248.575 212.061  1.00 44.61           O  
ATOM   1492  CB  GLU A 281     207.149 249.322 209.041  1.00 44.30           C  
ATOM   1493  N   ASN A 282     206.044 249.775 212.084  1.00 44.33           N  
ATOM   1494  CA  ASN A 282     206.237 250.398 213.396  1.00 44.88           C  
ATOM   1495  C   ASN A 282     205.673 249.543 214.545  1.00 44.77           C  
ATOM   1496  O   ASN A 282     205.653 249.991 215.695  1.00 45.66           O  
ATOM   1497  CB  ASN A 282     205.613 251.795 213.422  1.00 45.25           C  
ATOM   1498  CG  ASN A 282     206.241 252.791 212.426  1.00 45.98           C  
ATOM   1499  OD1 ASN A 282     207.018 252.413 211.535  1.00 45.71           O  
ATOM   1500  ND2 ASN A 282     205.895 254.064 212.583  1.00 47.30           N  
ATOM   1501  N   GLY A 283     205.188 248.321 214.250  1.00 45.78           N  
ATOM   1502  CA  GLY A 283     204.647 247.393 215.242  1.00 45.42           C  
ATOM   1503  C   GLY A 283     203.245 247.745 215.709  1.00 44.98           C  
ATOM   1504  O   GLY A 283     202.810 247.326 216.782  1.00 45.67           O  
ATOM   1505  N   THR A 284     202.537 248.518 214.906  1.00 46.03           N  
ATOM   1506  CA  THR A 284     201.185 248.922 215.230  1.00 45.67           C  
ATOM   1507  C   THR A 284     200.212 248.003 214.531  1.00 45.76           C  
ATOM   1508  O   THR A 284     200.386 247.694 213.352  1.00 40.74           O  
ATOM   1509  CB  THR A 284     200.936 250.386 214.821  1.00 45.48           C  
ATOM   1510  OG1 THR A 284     201.807 251.240 215.570  1.00 45.76           O  
ATOM   1511  CG2 THR A 284     199.494 250.788 215.070  1.00 46.21           C  
ATOM   1512  N   ILE A 285     199.187 247.550 215.236  1.00 46.34           N  
ATOM   1513  CA  ILE A 285     198.214 246.716 214.564  1.00 44.74           C  
ATOM   1514  C   ILE A 285     197.371 247.644 213.710  1.00 45.05           C  
ATOM   1515  O   ILE A 285     196.774 248.594 214.218  1.00 45.52           O  
ATOM   1516  CB  ILE A 285     197.326 245.951 215.562  1.00 45.19           C  
ATOM   1517  CG1 ILE A 285     198.180 245.027 216.425  1.00 46.03           C  
ATOM   1518  CG2 ILE A 285     196.290 245.128 214.797  1.00 44.31           C  
ATOM   1519  CD1 ILE A 285     197.461 244.464 217.649  1.00 46.15           C  
ATOM   1520  N   THR A 286     197.356 247.402 212.409  1.00 44.63           N  
ATOM   1521  CA  THR A 286     196.633 248.283 211.508  1.00 45.21           C  
ATOM   1522  C   THR A 286     195.424 247.608 210.912  1.00 45.08           C  
ATOM   1523  O   THR A 286     194.514 248.281 210.431  1.00 45.32           O  
ATOM   1524  CB  THR A 286     197.532 248.807 210.384  1.00 45.69           C  
ATOM   1525  OG1 THR A 286     198.020 247.709 209.604  1.00 45.31           O  
ATOM   1526  CG2 THR A 286     198.701 249.569 210.978  1.00 45.83           C  
ATOM   1527  N   ASP A 287     195.396 246.284 210.959  1.00 44.09           N  
ATOM   1528  CA  ASP A 287     194.236 245.572 210.441  1.00 44.32           C  
ATOM   1529  C   ASP A 287     194.042 244.255 211.178  1.00 44.97           C  
ATOM   1530  O   ASP A 287     194.866 243.880 212.017  1.00 45.02           O  
ATOM   1531  CB  ASP A 287     194.425 245.333 208.936  1.00 43.96           C  
ATOM   1532  CG  ASP A 287     193.135 245.198 208.145  1.00 44.62           C  
ATOM   1533  OD1 ASP A 287     192.113 244.964 208.744  1.00 44.26           O  
ATOM   1534  OD2 ASP A 287     193.187 245.318 206.944  1.00 44.84           O  
ATOM   1535  N   ALA A 288     192.967 243.546 210.857  1.00 43.98           N  
ATOM   1536  CA  ALA A 288     192.712 242.247 211.460  1.00 43.84           C  
ATOM   1537  C   ALA A 288     191.665 241.451 210.686  1.00 43.69           C  
ATOM   1538  O   ALA A 288     190.757 242.021 210.083  1.00 44.20           O  
ATOM   1539  CB  ALA A 288     192.261 242.417 212.897  1.00 44.69           C  
ATOM   1540  N   VAL A 289     191.742 240.132 210.788  1.00 43.62           N  
ATOM   1541  CA  VAL A 289     190.715 239.261 210.233  1.00 43.37           C  
ATOM   1542  C   VAL A 289     190.026 238.482 211.325  1.00 44.73           C  
ATOM   1543  O   VAL A 289     190.671 237.767 212.090  1.00 43.93           O  
ATOM   1544  CB  VAL A 289     191.313 238.247 209.236  1.00 42.83           C  
ATOM   1545  CG1 VAL A 289     190.235 237.315 208.689  1.00 41.92           C  
ATOM   1546  CG2 VAL A 289     191.986 238.983 208.124  1.00 42.68           C  
ATOM   1547  N   ASP A 290     188.709 238.584 211.370  1.00 43.85           N  
ATOM   1548  CA  ASP A 290     187.927 237.794 212.307  1.00 43.92           C  
ATOM   1549  C   ASP A 290     187.691 236.443 211.649  1.00 42.78           C  
ATOM   1550  O   ASP A 290     186.930 236.350 210.682  1.00 43.31           O  
ATOM   1551  CB  ASP A 290     186.615 238.491 212.648  1.00 44.69           C  
ATOM   1552  CG  ASP A 290     185.746 237.686 213.612  1.00 45.49           C  
ATOM   1553  OD1 ASP A 290     185.832 236.467 213.597  1.00 44.12           O  
ATOM   1554  OD2 ASP A 290     185.008 238.292 214.369  1.00 45.58           O  
ATOM   1555  N   CYS A 291     188.391 235.410 212.132  1.00 43.05           N  
ATOM   1556  CA  CYS A 291     188.488 234.102 211.483  1.00 42.21           C  
ATOM   1557  C   CYS A 291     187.168 233.320 211.476  1.00 42.29           C  
ATOM   1558  O   CYS A 291     187.107 232.232 210.899  1.00 41.90           O  
ATOM   1559  CB  CYS A 291     189.573 233.255 212.161  1.00 43.55           C  
ATOM   1560  SG  CYS A 291     191.250 233.954 212.043  1.00 44.51           S  
ATOM   1561  N   ALA A 292     186.106 233.829 212.138  1.00 42.97           N  
ATOM   1562  CA  ALA A 292     184.793 233.172 212.158  1.00 42.74           C  
ATOM   1563  C   ALA A 292     183.677 234.126 211.748  1.00 42.78           C  
ATOM   1564  O   ALA A 292     182.508 233.865 212.029  1.00 42.56           O  
ATOM   1565  CB  ALA A 292     184.524 232.624 213.544  1.00 43.97           C  
ATOM   1566  N   LEU A 293     184.027 235.218 211.076  1.00 42.84           N  
ATOM   1567  CA  LEU A 293     183.027 236.184 210.623  1.00 41.96           C  
ATOM   1568  C   LEU A 293     182.229 235.699 209.421  1.00 41.62           C  
ATOM   1569  O   LEU A 293     181.001 235.780 209.406  1.00 42.30           O  
ATOM   1570  CB  LEU A 293     183.710 237.501 210.265  1.00 42.35           C  
ATOM   1571  CG  LEU A 293     182.833 238.620 209.679  1.00 42.67           C  
ATOM   1572  CD1 LEU A 293     181.767 239.028 210.676  1.00 44.03           C  
ATOM   1573  CD2 LEU A 293     183.725 239.790 209.325  1.00 43.45           C  
ATOM   1574  N   ASP A 294     182.930 235.233 208.397  1.00 41.27           N  
ATOM   1575  CA  ASP A 294     182.298 234.774 207.169  1.00 40.33           C  
ATOM   1576  C   ASP A 294     183.290 233.847 206.447  1.00 41.05           C  
ATOM   1577  O   ASP A 294     184.442 233.763 206.876  1.00 38.14           O  
ATOM   1578  CB  ASP A 294     181.869 235.998 206.329  1.00 40.58           C  
ATOM   1579  CG  ASP A 294     183.013 236.859 205.821  1.00 40.67           C  
ATOM   1580  OD1 ASP A 294     184.018 236.319 205.392  1.00 39.92           O  
ATOM   1581  OD2 ASP A 294     182.878 238.058 205.855  1.00 41.27           O  
ATOM   1582  N   PRO A 295     182.898 233.146 205.371  1.00 39.18           N  
ATOM   1583  CA  PRO A 295     183.729 232.227 204.616  1.00 38.48           C  
ATOM   1584  C   PRO A 295     184.947 232.854 203.949  1.00 40.21           C  
ATOM   1585  O   PRO A 295     185.908 232.148 203.653  1.00 39.05           O  
ATOM   1586  CB  PRO A 295     182.756 231.689 203.569  1.00 38.59           C  
ATOM   1587  CG  PRO A 295     181.389 231.926 204.150  1.00 38.80           C  
ATOM   1588  CD  PRO A 295     181.514 233.209 204.900  1.00 38.98           C  
ATOM   1589  N   LEU A 296     184.949 234.161 203.712  1.00 38.17           N  
ATOM   1590  CA  LEU A 296     186.121 234.729 203.066  1.00 38.40           C  
ATOM   1591  C   LEU A 296     187.152 235.014 204.116  1.00 40.84           C  
ATOM   1592  O   LEU A 296     188.356 234.895 203.880  1.00 39.45           O  
ATOM   1593  CB  LEU A 296     185.797 236.001 202.293  1.00 38.27           C  
ATOM   1594  CG  LEU A 296     187.005 236.681 201.592  1.00 38.94           C  
ATOM   1595  CD1 LEU A 296     187.690 235.723 200.602  1.00 39.13           C  
ATOM   1596  CD2 LEU A 296     186.508 237.902 200.869  1.00 39.27           C  
ATOM   1597  N   SER A 297     186.668 235.389 205.285  1.00 40.15           N  
ATOM   1598  CA  SER A 297     187.529 235.670 206.403  1.00 38.48           C  
ATOM   1599  C   SER A 297     188.191 234.370 206.821  1.00 42.33           C  
ATOM   1600  O   SER A 297     189.363 234.358 207.196  1.00 39.98           O  
ATOM   1601  CB  SER A 297     186.727 236.257 207.530  1.00 40.37           C  
ATOM   1602  OG  SER A 297     186.151 237.471 207.145  1.00 40.24           O  
ATOM   1603  N   GLU A 298     187.451 233.263 206.720  1.00 39.72           N  
ATOM   1604  CA  GLU A 298     188.012 231.960 207.038  1.00 39.13           C  
ATOM   1605  C   GLU A 298     189.153 231.639 206.085  1.00 38.29           C  
ATOM   1606  O   GLU A 298     190.207 231.165 206.516  1.00 40.80           O  
ATOM   1607  CB  GLU A 298     186.947 230.866 206.950  1.00 39.59           C  
ATOM   1608  CG  GLU A 298     185.914 230.889 208.065  1.00 39.96           C  
ATOM   1609  CD  GLU A 298     184.788 229.903 207.861  1.00 39.84           C  
ATOM   1610  OE1 GLU A 298     184.629 229.422 206.767  1.00 39.67           O  
ATOM   1611  OE2 GLU A 298     184.096 229.626 208.808  1.00 39.72           O  
ATOM   1612  N   THR A 299     188.976 231.948 204.797  1.00 39.16           N  
ATOM   1613  CA  THR A 299     190.039 231.719 203.831  1.00 39.07           C  
ATOM   1614  C   THR A 299     191.247 232.588 204.137  1.00 40.59           C  
ATOM   1615  O   THR A 299     192.377 232.097 204.133  1.00 40.53           O  
ATOM   1616  CB  THR A 299     189.563 231.983 202.394  1.00 39.52           C  
ATOM   1617  OG1 THR A 299     188.470 231.126 202.088  1.00 39.23           O  
ATOM   1618  CG2 THR A 299     190.676 231.719 201.412  1.00 40.00           C  
ATOM   1619  N   LYS A 300     191.022 233.870 204.421  1.00 39.12           N  
ATOM   1620  CA  LYS A 300     192.138 234.761 204.748  1.00 39.04           C  
ATOM   1621  C   LYS A 300     192.925 234.278 205.971  1.00 41.53           C  
ATOM   1622  O   LYS A 300     194.160 234.278 205.961  1.00 40.37           O  
ATOM   1623  CB  LYS A 300     191.639 236.192 204.980  1.00 39.67           C  
ATOM   1624  CG  LYS A 300     191.240 236.922 203.726  1.00 39.86           C  
ATOM   1625  CD  LYS A 300     190.743 238.323 204.014  1.00 39.82           C  
ATOM   1626  CE  LYS A 300     190.411 239.051 202.719  1.00 41.00           C  
ATOM   1627  NZ  LYS A 300     189.991 240.459 202.954  1.00 40.95           N  
ATOM   1628  N   CYS A 301     192.213 233.820 207.013  1.00 39.35           N  
ATOM   1629  CA  CYS A 301     192.815 233.302 208.241  1.00 40.23           C  
ATOM   1630  C   CYS A 301     193.639 232.025 207.962  1.00 40.16           C  
ATOM   1631  O   CYS A 301     194.792 231.920 208.393  1.00 40.68           O  
ATOM   1632  CB  CYS A 301     191.712 233.039 209.282  1.00 41.05           C  
ATOM   1633  SG  CYS A 301     192.287 232.615 210.933  1.00 43.56           S  
ATOM   1634  N   THR A 302     193.066 231.081 207.192  1.00 40.33           N  
ATOM   1635  CA  THR A 302     193.684 229.801 206.828  1.00 39.90           C  
ATOM   1636  C   THR A 302     194.978 229.983 206.048  1.00 40.01           C  
ATOM   1637  O   THR A 302     195.969 229.294 206.296  1.00 40.18           O  
ATOM   1638  CB  THR A 302     192.711 228.963 205.984  1.00 40.07           C  
ATOM   1639  OG1 THR A 302     191.549 228.670 206.761  1.00 39.96           O  
ATOM   1640  CG2 THR A 302     193.361 227.666 205.530  1.00 39.95           C  
ATOM   1641  N   LEU A 303     194.966 230.929 205.121  1.00 40.12           N  
ATOM   1642  CA  LEU A 303     196.112 231.199 204.271  1.00 40.03           C  
ATOM   1643  C   LEU A 303     197.083 232.182 204.908  1.00 40.13           C  
ATOM   1644  O   LEU A 303     198.100 232.524 204.306  1.00 40.27           O  
ATOM   1645  CB  LEU A 303     195.639 231.792 202.940  1.00 39.90           C  
ATOM   1646  CG  LEU A 303     194.691 230.929 202.095  1.00 39.71           C  
ATOM   1647  CD1 LEU A 303     194.257 231.737 200.889  1.00 39.56           C  
ATOM   1648  CD2 LEU A 303     195.371 229.642 201.670  1.00 39.62           C  
ATOM   1649  N   LYS A 304     196.753 232.672 206.101  1.00 40.41           N  
ATOM   1650  CA  LYS A 304     197.573 233.656 206.788  1.00 40.21           C  
ATOM   1651  C   LYS A 304     197.868 234.845 205.898  1.00 40.56           C  
ATOM   1652  O   LYS A 304     199.016 235.272 205.783  1.00 41.08           O  
ATOM   1653  CB  LYS A 304     198.884 233.034 207.260  1.00 40.52           C  
ATOM   1654  CG  LYS A 304     198.720 231.802 208.129  1.00 40.18           C  
ATOM   1655  CD  LYS A 304     198.160 232.151 209.497  1.00 40.38           C  
ATOM   1656  CE  LYS A 304     198.142 230.941 210.413  1.00 40.33           C  
ATOM   1657  NZ  LYS A 304     197.144 229.930 209.974  1.00 40.60           N  
ATOM   1658  N   SER A 305     196.840 235.379 205.258  1.00 40.55           N  
ATOM   1659  CA  SER A 305     197.030 236.516 204.378  1.00 40.74           C  
ATOM   1660  C   SER A 305     195.794 237.381 204.300  1.00 40.83           C  
ATOM   1661  O   SER A 305     194.680 236.909 204.486  1.00 41.42           O  
ATOM   1662  CB  SER A 305     197.407 236.067 202.995  1.00 41.05           C  
ATOM   1663  OG  SER A 305     197.672 237.179 202.190  1.00 41.44           O  
ATOM   1664  N   PHE A 306     195.984 238.657 204.009  1.00 41.26           N  
ATOM   1665  CA  PHE A 306     194.857 239.563 203.864  1.00 41.37           C  
ATOM   1666  C   PHE A 306     194.409 239.668 202.413  1.00 41.34           C  
ATOM   1667  O   PHE A 306     193.462 240.391 202.097  1.00 41.18           O  
ATOM   1668  CB  PHE A 306     195.206 240.935 204.442  1.00 42.10           C  
ATOM   1669  CG  PHE A 306     195.154 240.969 205.944  1.00 42.63           C  
ATOM   1670  CD1 PHE A 306     196.027 240.231 206.713  1.00 42.74           C  
ATOM   1671  CD2 PHE A 306     194.219 241.753 206.588  1.00 43.12           C  
ATOM   1672  CE1 PHE A 306     195.952 240.264 208.080  1.00 42.97           C  
ATOM   1673  CE2 PHE A 306     194.156 241.789 207.953  1.00 43.46           C  
ATOM   1674  CZ  PHE A 306     195.026 241.037 208.700  1.00 43.37           C  
ATOM   1675  N   THR A 307     195.086 238.929 201.541  1.00 41.00           N  
ATOM   1676  CA  THR A 307     194.746 238.874 200.126  1.00 40.79           C  
ATOM   1677  C   THR A 307     194.513 237.433 199.706  1.00 40.55           C  
ATOM   1678  O   THR A 307     195.309 236.548 200.016  1.00 40.69           O  
ATOM   1679  CB  THR A 307     195.854 239.496 199.252  1.00 41.09           C  
ATOM   1680  OG1 THR A 307     196.021 240.872 199.606  1.00 41.58           O  
ATOM   1681  CG2 THR A 307     195.494 239.397 197.765  1.00 40.60           C  
ATOM   1682  N   VAL A 308     193.423 237.192 198.997  1.00 40.34           N  
ATOM   1683  CA  VAL A 308     193.138 235.848 198.525  1.00 39.88           C  
ATOM   1684  C   VAL A 308     193.071 235.827 197.011  1.00 40.00           C  
ATOM   1685  O   VAL A 308     192.310 236.575 196.394  1.00 39.95           O  
ATOM   1686  CB  VAL A 308     191.833 235.315 199.125  1.00 39.78           C  
ATOM   1687  CG1 VAL A 308     191.556 233.935 198.607  1.00 39.43           C  
ATOM   1688  CG2 VAL A 308     191.942 235.318 200.625  1.00 40.10           C  
ATOM   1689  N   GLU A 309     193.867 234.956 196.419  1.00 39.65           N  
ATOM   1690  CA  GLU A 309     193.936 234.836 194.977  1.00 39.33           C  
ATOM   1691  C   GLU A 309     192.777 234.015 194.451  1.00 38.93           C  
ATOM   1692  O   GLU A 309     192.125 233.293 195.199  1.00 39.10           O  
ATOM   1693  CB  GLU A 309     195.263 234.221 194.554  1.00 39.55           C  
ATOM   1694  CG  GLU A 309     196.474 235.041 194.964  1.00 39.76           C  
ATOM   1695  CD  GLU A 309     196.502 236.405 194.335  1.00 40.51           C  
ATOM   1696  OE1 GLU A 309     195.997 236.554 193.248  1.00 40.28           O  
ATOM   1697  OE2 GLU A 309     197.028 237.302 194.946  1.00 40.61           O  
ATOM   1698  N   LYS A 310     192.494 234.161 193.172  1.00 38.85           N  
ATOM   1699  CA  LYS A 310     191.418 233.411 192.554  1.00 38.25           C  
ATOM   1700  C   LYS A 310     191.634 231.919 192.698  1.00 37.96           C  
ATOM   1701  O   LYS A 310     192.709 231.410 192.382  1.00 38.39           O  
ATOM   1702  CB  LYS A 310     191.328 233.762 191.076  1.00 38.59           C  
ATOM   1703  CG  LYS A 310     190.241 233.033 190.321  1.00 38.05           C  
ATOM   1704  CD  LYS A 310     190.130 233.505 188.879  1.00 37.60           C  
ATOM   1705  CE  LYS A 310     191.370 233.138 188.072  1.00 37.64           C  
ATOM   1706  NZ  LYS A 310     191.156 233.331 186.628  1.00 37.64           N  
ATOM   1707  N   GLY A 311     190.603 231.213 193.134  1.00 37.38           N  
ATOM   1708  CA  GLY A 311     190.704 229.770 193.261  1.00 37.13           C  
ATOM   1709  C   GLY A 311     189.761 229.199 194.300  1.00 36.61           C  
ATOM   1710  O   GLY A 311     188.888 229.891 194.825  1.00 37.22           O  
ATOM   1711  N   ILE A 312     189.919 227.911 194.561  1.00 36.55           N  
ATOM   1712  CA  ILE A 312     189.104 227.213 195.537  1.00 36.17           C  
ATOM   1713  C   ILE A 312     189.998 226.761 196.679  1.00 36.79           C  
ATOM   1714  O   ILE A 312     191.038 226.145 196.447  1.00 36.88           O  
ATOM   1715  CB  ILE A 312     188.365 226.024 194.885  1.00 35.64           C  
ATOM   1716  CG1 ILE A 312     187.476 225.325 195.919  1.00 36.30           C  
ATOM   1717  CG2 ILE A 312     189.346 225.058 194.239  1.00 36.65           C  
ATOM   1718  CD1 ILE A 312     186.470 224.337 195.322  1.00 35.66           C  
ATOM   1719  N   TYR A 313     189.609 227.073 197.906  1.00 36.75           N  
ATOM   1720  CA  TYR A 313     190.435 226.713 199.049  1.00 36.51           C  
ATOM   1721  C   TYR A 313     189.667 225.926 200.087  1.00 36.81           C  
ATOM   1722  O   TYR A 313     188.545 226.283 200.430  1.00 37.80           O  
ATOM   1723  CB  TYR A 313     190.965 227.977 199.711  1.00 37.19           C  
ATOM   1724  CG  TYR A 313     191.771 228.841 198.812  1.00 37.57           C  
ATOM   1725  CD1 TYR A 313     191.163 229.850 198.092  1.00 37.57           C  
ATOM   1726  CD2 TYR A 313     193.115 228.633 198.705  1.00 38.16           C  
ATOM   1727  CE1 TYR A 313     191.917 230.649 197.271  1.00 37.77           C  
ATOM   1728  CE2 TYR A 313     193.868 229.427 197.889  1.00 38.09           C  
ATOM   1729  CZ  TYR A 313     193.279 230.431 197.176  1.00 38.19           C  
ATOM   1730  OH  TYR A 313     194.047 231.222 196.369  1.00 38.78           O  
ATOM   1731  N   GLN A 314     190.284 224.896 200.649  1.00 37.01           N  
ATOM   1732  CA  GLN A 314     189.639 224.167 201.736  1.00 37.30           C  
ATOM   1733  C   GLN A 314     190.032 224.808 203.047  1.00 37.69           C  
ATOM   1734  O   GLN A 314     191.218 224.932 203.344  1.00 37.78           O  
ATOM   1735  CB  GLN A 314     190.011 222.692 201.725  1.00 37.03           C  
ATOM   1736  CG  GLN A 314     189.311 221.891 202.801  1.00 37.22           C  
ATOM   1737  CD  GLN A 314     189.588 220.426 202.681  1.00 37.00           C  
ATOM   1738  OE1 GLN A 314     189.149 219.768 201.731  1.00 36.31           O  
ATOM   1739  NE2 GLN A 314     190.326 219.888 203.644  1.00 36.20           N  
ATOM   1740  N   THR A 315     189.041 225.254 203.809  1.00 38.01           N  
ATOM   1741  CA  THR A 315     189.328 225.997 205.030  1.00 38.41           C  
ATOM   1742  C   THR A 315     188.780 225.378 206.301  1.00 38.81           C  
ATOM   1743  O   THR A 315     189.275 225.657 207.393  1.00 38.96           O  
ATOM   1744  CB  THR A 315     188.748 227.409 204.934  1.00 38.82           C  
ATOM   1745  OG1 THR A 315     187.323 227.328 204.831  1.00 38.68           O  
ATOM   1746  CG2 THR A 315     189.284 228.138 203.735  1.00 38.70           C  
ATOM   1747  N   SER A 316     187.743 224.562 206.192  1.00 38.81           N  
ATOM   1748  CA  SER A 316     187.128 224.078 207.417  1.00 39.33           C  
ATOM   1749  C   SER A 316     186.454 222.731 207.255  1.00 39.90           C  
ATOM   1750  O   SER A 316     186.679 222.013 206.276  1.00 39.98           O  
ATOM   1751  CB  SER A 316     186.131 225.097 207.933  1.00 39.61           C  
ATOM   1752  OG  SER A 316     185.763 224.810 209.254  1.00 40.14           O  
ATOM   1753  N   ASN A 317     185.644 222.384 208.244  1.00 40.54           N  
ATOM   1754  CA  ASN A 317     184.925 221.125 208.284  1.00 40.96           C  
ATOM   1755  C   ASN A 317     183.578 221.349 208.956  1.00 41.31           C  
ATOM   1756  O   ASN A 317     183.508 221.755 210.115  1.00 42.00           O  
ATOM   1757  CB  ASN A 317     185.749 220.058 208.984  1.00 41.07           C  
ATOM   1758  CG  ASN A 317     185.147 218.671 208.887  1.00 41.32           C  
ATOM   1759  OD1 ASN A 317     183.927 218.498 208.905  1.00 43.35           O  
ATOM   1760  ND2 ASN A 317     185.997 217.676 208.780  1.00 40.32           N  
ATOM   1761  N   PHE A 318     182.516 221.169 208.191  1.00 41.55           N  
ATOM   1762  CA  PHE A 318     181.162 221.366 208.659  1.00 42.11           C  
ATOM   1763  C   PHE A 318     180.831 220.248 209.596  1.00 45.13           C  
ATOM   1764  O   PHE A 318     181.054 219.092 209.255  1.00 41.03           O  
ATOM   1765  CB  PHE A 318     180.196 221.340 207.477  1.00 42.35           C  
ATOM   1766  CG  PHE A 318     178.752 221.361 207.840  1.00 43.16           C  
ATOM   1767  CD1 PHE A 318     178.124 222.520 208.248  1.00 43.42           C  
ATOM   1768  CD2 PHE A 318     178.007 220.195 207.761  1.00 43.82           C  
ATOM   1769  CE1 PHE A 318     176.780 222.514 208.570  1.00 43.50           C  
ATOM   1770  CE2 PHE A 318     176.670 220.186 208.082  1.00 44.23           C  
ATOM   1771  CZ  PHE A 318     176.054 221.347 208.487  1.00 44.65           C  
ATOM   1772  N   ARG A 319     180.301 220.563 210.768  1.00 44.63           N  
ATOM   1773  CA  ARG A 319     179.935 219.502 211.691  1.00 45.09           C  
ATOM   1774  C   ARG A 319     178.639 219.803 212.410  1.00 47.19           C  
ATOM   1775  O   ARG A 319     178.500 220.846 213.054  1.00 48.51           O  
ATOM   1776  CB  ARG A 319     181.035 219.282 212.719  1.00 44.78           C  
ATOM   1777  CG  ARG A 319     182.382 218.905 212.127  1.00 43.39           C  
ATOM   1778  CD  ARG A 319     183.396 218.578 213.155  1.00 42.74           C  
ATOM   1779  NE  ARG A 319     183.063 217.358 213.877  1.00 42.45           N  
ATOM   1780  CZ  ARG A 319     183.257 216.111 213.405  1.00 42.29           C  
ATOM   1781  NH1 ARG A 319     183.757 215.926 212.209  1.00 42.16           N  
ATOM   1782  NH2 ARG A 319     182.940 215.076 214.151  1.00 41.47           N  
ATOM   1783  N   VAL A 320     177.720 218.853 212.359  1.00 47.92           N  
ATOM   1784  CA  VAL A 320     176.471 218.973 213.086  1.00 50.06           C  
ATOM   1785  C   VAL A 320     176.728 218.744 214.564  1.00 51.16           C  
ATOM   1786  O   VAL A 320     177.408 217.793 214.945  1.00 51.44           O  
ATOM   1787  CB  VAL A 320     175.435 217.973 212.545  1.00 49.86           C  
ATOM   1788  CG1 VAL A 320     174.176 217.991 213.403  1.00 52.37           C  
ATOM   1789  CG2 VAL A 320     175.095 218.344 211.104  1.00 48.73           C  
ATOM   1790  N   GLN A 321     176.214 219.640 215.392  1.00 52.58           N  
ATOM   1791  CA  GLN A 321     176.435 219.553 216.825  1.00 52.65           C  
ATOM   1792  C   GLN A 321     175.302 218.789 217.492  1.00 54.82           C  
ATOM   1793  O   GLN A 321     174.178 218.816 216.993  1.00 54.73           O  
ATOM   1794  CB  GLN A 321     176.541 220.965 217.401  1.00 53.54           C  
ATOM   1795  CG  GLN A 321     177.641 221.770 216.774  1.00 52.88           C  
ATOM   1796  CD  GLN A 321     178.972 221.112 216.949  1.00 53.14           C  
ATOM   1797  OE1 GLN A 321     179.398 220.844 218.076  1.00 53.79           O  
ATOM   1798  NE2 GLN A 321     179.641 220.829 215.841  1.00 51.74           N  
ATOM   1799  N   PRO A 322     175.570 218.100 218.608  1.00 54.50           N  
ATOM   1800  CA  PRO A 322     174.599 217.397 219.411  1.00 55.31           C  
ATOM   1801  C   PRO A 322     173.667 218.374 220.091  1.00 55.88           C  
ATOM   1802  O   PRO A 322     174.102 219.430 220.550  1.00 56.06           O  
ATOM   1803  CB  PRO A 322     175.475 216.638 220.409  1.00 56.00           C  
ATOM   1804  CG  PRO A 322     176.758 217.431 220.484  1.00 54.97           C  
ATOM   1805  CD  PRO A 322     176.948 218.005 219.099  1.00 54.73           C  
ATOM   1806  N   THR A 323     172.398 217.995 220.205  1.00 56.83           N  
ATOM   1807  CA  THR A 323     171.412 218.847 220.862  1.00 57.39           C  
ATOM   1808  C   THR A 323     170.881 218.275 222.177  1.00 57.95           C  
ATOM   1809  O   THR A 323     170.292 219.002 222.976  1.00 58.33           O  
ATOM   1810  CB  THR A 323     170.239 219.120 219.912  1.00 58.44           C  
ATOM   1811  OG1 THR A 323     169.587 217.887 219.580  1.00 57.91           O  
ATOM   1812  CG2 THR A 323     170.765 219.769 218.640  1.00 58.06           C  
ATOM   1813  N   GLU A 324     171.089 216.981 222.398  1.00 57.89           N  
ATOM   1814  CA  GLU A 324     170.582 216.291 223.585  1.00 58.36           C  
ATOM   1815  C   GLU A 324     171.702 215.538 224.281  1.00 58.33           C  
ATOM   1816  O   GLU A 324     172.708 215.192 223.657  1.00 58.51           O  
ATOM   1817  CB  GLU A 324     169.489 215.274 223.236  1.00 58.96           C  
ATOM   1818  CG  GLU A 324     168.308 215.806 222.457  1.00 58.67           C  
ATOM   1819  CD  GLU A 324     167.410 216.693 223.261  1.00 59.47           C  
ATOM   1820  OE1 GLU A 324     167.511 216.680 224.465  1.00 59.17           O  
ATOM   1821  OE2 GLU A 324     166.613 217.384 222.670  1.00 59.51           O  
ATOM   1822  N   SER A 325     171.515 215.262 225.565  1.00 59.25           N  
ATOM   1823  CA  SER A 325     172.461 214.444 226.318  1.00 58.62           C  
ATOM   1824  C   SER A 325     171.757 213.210 226.863  1.00 59.76           C  
ATOM   1825  O   SER A 325     170.866 213.311 227.708  1.00 61.06           O  
ATOM   1826  CB  SER A 325     173.073 215.239 227.453  1.00 59.31           C  
ATOM   1827  OG  SER A 325     173.909 214.431 228.235  1.00 60.03           O  
ATOM   1828  N   ILE A 326     172.132 212.050 226.342  1.00 59.26           N  
ATOM   1829  CA  ILE A 326     171.478 210.800 226.691  1.00 59.60           C  
ATOM   1830  C   ILE A 326     172.367 209.895 227.499  1.00 60.35           C  
ATOM   1831  O   ILE A 326     173.354 209.361 226.996  1.00 60.97           O  
ATOM   1832  CB  ILE A 326     171.024 210.057 225.433  1.00 60.63           C  
ATOM   1833  CG1 ILE A 326     170.026 210.923 224.690  1.00 60.07           C  
ATOM   1834  CG2 ILE A 326     170.433 208.680 225.799  1.00 60.80           C  
ATOM   1835  CD1 ILE A 326     169.717 210.435 223.327  1.00 60.76           C  
ATOM   1836  N   VAL A 327     171.984 209.685 228.738  1.00 60.57           N  
ATOM   1837  CA  VAL A 327     172.749 208.861 229.646  1.00 60.64           C  
ATOM   1838  C   VAL A 327     171.928 207.667 230.081  1.00 62.59           C  
ATOM   1839  O   VAL A 327     170.813 207.823 230.585  1.00 63.41           O  
ATOM   1840  CB  VAL A 327     173.167 209.692 230.869  1.00 61.63           C  
ATOM   1841  CG1 VAL A 327     173.955 208.841 231.840  1.00 61.49           C  
ATOM   1842  CG2 VAL A 327     173.984 210.890 230.403  1.00 61.00           C  
ATOM   1843  N   ARG A 328     172.464 206.469 229.884  1.00 60.81           N  
ATOM   1844  CA  ARG A 328     171.737 205.286 230.302  1.00 63.29           C  
ATOM   1845  C   ARG A 328     172.632 204.252 230.973  1.00 64.06           C  
ATOM   1846  O   ARG A 328     173.739 203.954 230.518  1.00 62.72           O  
ATOM   1847  CB  ARG A 328     171.027 204.648 229.124  1.00 62.60           C  
ATOM   1848  CG  ARG A 328     170.192 205.599 228.313  1.00 62.80           C  
ATOM   1849  CD  ARG A 328     169.211 204.914 227.468  1.00 62.50           C  
ATOM   1850  NE  ARG A 328     168.002 204.567 228.218  1.00 63.58           N  
ATOM   1851  CZ  ARG A 328     166.863 204.083 227.685  1.00 63.32           C  
ATOM   1852  NH1 ARG A 328     166.767 203.843 226.401  1.00 63.61           N  
ATOM   1853  NH2 ARG A 328     165.840 203.856 228.479  1.00 64.50           N  
ATOM   1854  N   PHE A 329     172.103 203.691 232.045  1.00 64.41           N  
ATOM   1855  CA  PHE A 329     172.702 202.613 232.809  1.00 63.16           C  
ATOM   1856  C   PHE A 329     171.553 201.677 233.134  1.00 65.51           C  
ATOM   1857  O   PHE A 329     170.419 202.144 233.165  1.00 65.59           O  
ATOM   1858  CB  PHE A 329     173.325 203.158 234.097  1.00 64.57           C  
ATOM   1859  CG  PHE A 329     174.437 204.158 233.910  1.00 64.15           C  
ATOM   1860  CD1 PHE A 329     174.195 205.514 233.954  1.00 64.04           C  
ATOM   1861  CD2 PHE A 329     175.729 203.737 233.711  1.00 64.07           C  
ATOM   1862  CE1 PHE A 329     175.232 206.410 233.810  1.00 63.13           C  
ATOM   1863  CE2 PHE A 329     176.762 204.630 233.569  1.00 63.02           C  
ATOM   1864  CZ  PHE A 329     176.513 205.967 233.620  1.00 62.03           C  
ATOM   1865  N   PRO A 330     171.772 200.388 233.393  1.00 64.61           N  
ATOM   1866  CA  PRO A 330     170.733 199.473 233.804  1.00 65.32           C  
ATOM   1867  C   PRO A 330     170.162 200.032 235.095  1.00 66.66           C  
ATOM   1868  O   PRO A 330     170.939 200.467 235.953  1.00 67.15           O  
ATOM   1869  CB  PRO A 330     171.499 198.155 233.997  1.00 65.84           C  
ATOM   1870  CG  PRO A 330     172.956 198.576 234.175  1.00 66.03           C  
ATOM   1871  CD  PRO A 330     173.108 199.811 233.314  1.00 64.75           C  
ATOM   1872  N   ASN A 331     168.824 200.016 235.261  1.00 67.02           N  
ATOM   1873  CA  ASN A 331     168.197 200.629 236.436  1.00 67.10           C  
ATOM   1874  C   ASN A 331     168.237 199.700 237.656  1.00 68.27           C  
ATOM   1875  O   ASN A 331     167.217 199.141 238.074  1.00 68.55           O  
ATOM   1876  CB  ASN A 331     166.787 201.142 236.129  1.00 67.23           C  
ATOM   1877  CG  ASN A 331     165.794 200.135 235.482  1.00 67.62           C  
ATOM   1878  OD1 ASN A 331     165.167 199.334 236.191  1.00 68.62           O  
ATOM   1879  ND2 ASN A 331     165.633 200.212 234.161  1.00 67.85           N  
ATOM   1880  N   ILE A 332     169.437 199.593 238.234  1.00 68.42           N  
ATOM   1881  CA  ILE A 332     169.736 198.837 239.444  1.00 68.99           C  
ATOM   1882  C   ILE A 332     169.417 199.745 240.623  1.00 70.37           C  
ATOM   1883  O   ILE A 332     169.835 200.899 240.642  1.00 70.11           O  
ATOM   1884  CB  ILE A 332     171.221 198.418 239.469  1.00 69.59           C  
ATOM   1885  CG1 ILE A 332     171.520 197.523 238.260  1.00 68.65           C  
ATOM   1886  CG2 ILE A 332     171.560 197.686 240.772  1.00 71.31           C  
ATOM   1887  CD1 ILE A 332     173.005 197.285 238.011  1.00 69.32           C  
ATOM   1888  N   THR A 333     168.634 199.252 241.569  1.00 70.55           N  
ATOM   1889  CA  THR A 333     168.220 200.057 242.713  1.00 70.70           C  
ATOM   1890  C   THR A 333     168.896 199.592 243.992  1.00 70.15           C  
ATOM   1891  O   THR A 333     168.569 200.042 245.090  1.00 71.46           O  
ATOM   1892  CB  THR A 333     166.697 200.001 242.882  1.00 71.55           C  
ATOM   1893  OG1 THR A 333     166.292 198.642 243.106  1.00 70.71           O  
ATOM   1894  CG2 THR A 333     166.018 200.531 241.617  1.00 70.08           C  
ATOM   1895  N   ASN A 334     169.818 198.660 243.840  1.00 70.15           N  
ATOM   1896  CA  ASN A 334     170.523 198.045 244.950  1.00 71.08           C  
ATOM   1897  C   ASN A 334     171.752 198.831 245.391  1.00 71.77           C  
ATOM   1898  O   ASN A 334     172.724 198.933 244.645  1.00 71.84           O  
ATOM   1899  CB  ASN A 334     170.933 196.635 244.581  1.00 71.48           C  
ATOM   1900  CG  ASN A 334     171.599 195.936 245.707  1.00 71.10           C  
ATOM   1901  OD1 ASN A 334     171.226 196.131 246.869  1.00 72.78           O  
ATOM   1902  ND2 ASN A 334     172.584 195.137 245.405  1.00 72.47           N  
ATOM   1903  N   LEU A 335     171.705 199.402 246.592  1.00 71.59           N  
ATOM   1904  CA  LEU A 335     172.838 200.172 247.100  1.00 72.84           C  
ATOM   1905  C   LEU A 335     174.013 199.218 247.277  1.00 72.97           C  
ATOM   1906  O   LEU A 335     173.837 198.136 247.843  1.00 73.61           O  
ATOM   1907  CB  LEU A 335     172.481 200.835 248.439  1.00 72.42           C  
ATOM   1908  CG  LEU A 335     173.569 201.738 249.085  1.00 73.24           C  
ATOM   1909  CD1 LEU A 335     173.803 202.980 248.223  1.00 72.80           C  
ATOM   1910  CD2 LEU A 335     173.118 202.136 250.485  1.00 72.73           C  
ATOM   1911  N   CYS A 336     175.201 199.602 246.783  1.00 72.30           N  
ATOM   1912  CA  CYS A 336     176.365 198.713 246.784  1.00 72.56           C  
ATOM   1913  C   CYS A 336     177.025 198.648 248.170  1.00 73.78           C  
ATOM   1914  O   CYS A 336     177.437 199.683 248.705  1.00 74.00           O  
ATOM   1915  CB  CYS A 336     177.372 199.182 245.729  1.00 71.97           C  
ATOM   1916  SG  CYS A 336     178.583 197.968 245.290  1.00 70.37           S  
ATOM   1917  N   PRO A 337     177.201 197.422 248.785  1.00 74.43           N  
ATOM   1918  CA  PRO A 337     177.649 197.183 250.152  1.00 75.51           C  
ATOM   1919  C   PRO A 337     179.141 197.377 250.376  1.00 75.27           C  
ATOM   1920  O   PRO A 337     179.861 196.438 250.711  1.00 75.57           O  
ATOM   1921  CB  PRO A 337     177.264 195.719 250.364  1.00 74.74           C  
ATOM   1922  CG  PRO A 337     177.426 195.084 249.015  1.00 74.64           C  
ATOM   1923  CD  PRO A 337     176.945 196.128 248.045  1.00 74.17           C  
ATOM   1924  N   PHE A 338     179.602 198.606 250.223  1.00 75.34           N  
ATOM   1925  CA  PHE A 338     180.995 198.898 250.514  1.00 76.44           C  
ATOM   1926  C   PHE A 338     181.215 198.889 252.020  1.00 77.65           C  
ATOM   1927  O   PHE A 338     182.301 198.587 252.502  1.00 77.97           O  
ATOM   1928  CB  PHE A 338     181.420 200.231 249.917  1.00 75.85           C  
ATOM   1929  CG  PHE A 338     181.634 200.168 248.441  1.00 74.95           C  
ATOM   1930  CD1 PHE A 338     180.764 200.789 247.577  1.00 74.57           C  
ATOM   1931  CD2 PHE A 338     182.714 199.477 247.912  1.00 74.80           C  
ATOM   1932  CE1 PHE A 338     180.970 200.730 246.225  1.00 73.13           C  
ATOM   1933  CE2 PHE A 338     182.921 199.418 246.558  1.00 73.45           C  
ATOM   1934  CZ  PHE A 338     182.046 200.045 245.711  1.00 73.57           C  
ATOM   1935  N   GLY A 339     180.170 199.188 252.783  1.00 76.78           N  
ATOM   1936  CA  GLY A 339     180.279 199.187 254.237  1.00 77.42           C  
ATOM   1937  C   GLY A 339     180.707 197.819 254.763  1.00 78.44           C  
ATOM   1938  O   GLY A 339     181.451 197.726 255.735  1.00 79.34           O  
ATOM   1939  N   GLU A 340     180.300 196.752 254.082  1.00 76.87           N  
ATOM   1940  CA  GLU A 340     180.634 195.396 254.505  1.00 78.02           C  
ATOM   1941  C   GLU A 340     182.098 195.050 254.246  1.00 78.40           C  
ATOM   1942  O   GLU A 340     182.589 194.011 254.688  1.00 77.98           O  
ATOM   1943  CB  GLU A 340     179.747 194.383 253.788  1.00 77.73           C  
ATOM   1944  N   VAL A 341     182.782 195.903 253.499  1.00 78.15           N  
ATOM   1945  CA  VAL A 341     184.181 195.713 253.177  1.00 78.18           C  
ATOM   1946  C   VAL A 341     185.051 196.643 254.006  1.00 78.31           C  
ATOM   1947  O   VAL A 341     186.027 196.221 254.622  1.00 78.89           O  
ATOM   1948  CB  VAL A 341     184.421 196.007 251.686  1.00 78.04           C  
ATOM   1949  CG1 VAL A 341     185.897 195.912 251.362  1.00 77.87           C  
ATOM   1950  CG2 VAL A 341     183.611 195.032 250.836  1.00 77.13           C  
ATOM   1951  N   PHE A 342     184.692 197.917 253.996  1.00 77.84           N  
ATOM   1952  CA  PHE A 342     185.460 198.965 254.657  1.00 78.75           C  
ATOM   1953  C   PHE A 342     185.237 199.077 256.171  1.00 79.83           C  
ATOM   1954  O   PHE A 342     186.172 199.415 256.899  1.00 79.45           O  
ATOM   1955  CB  PHE A 342     185.163 200.290 253.973  1.00 79.20           C  
ATOM   1956  CG  PHE A 342     185.813 200.378 252.644  1.00 78.64           C  
ATOM   1957  CD1 PHE A 342     185.172 199.930 251.508  1.00 77.05           C  
ATOM   1958  CD2 PHE A 342     187.073 200.899 252.524  1.00 78.32           C  
ATOM   1959  CE1 PHE A 342     185.784 199.998 250.291  1.00 76.64           C  
ATOM   1960  CE2 PHE A 342     187.687 200.972 251.308  1.00 77.50           C  
ATOM   1961  CZ  PHE A 342     187.041 200.517 250.190  1.00 76.68           C  
ATOM   1962  N   ASN A 343     184.011 198.795 256.640  1.00 79.55           N  
ATOM   1963  CA  ASN A 343     183.624 198.865 258.054  1.00 80.43           C  
ATOM   1964  C   ASN A 343     183.430 197.461 258.648  1.00 81.22           C  
ATOM   1965  O   ASN A 343     182.678 197.280 259.608  1.00 81.49           O  
ATOM   1966  CB  ASN A 343     182.369 199.731 258.223  1.00 80.59           C  
ATOM   1967  CG  ASN A 343     182.644 201.248 258.189  1.00 80.23           C  
ATOM   1968  OD1 ASN A 343     183.760 201.700 257.883  1.00 80.73           O  
ATOM   1969  ND2 ASN A 343     181.620 202.028 258.512  1.00 80.21           N  
ATOM   1970  N   ALA A 344     184.132 196.456 258.081  1.00 80.66           N  
ATOM   1971  CA  ALA A 344     184.105 195.064 258.522  1.00 81.29           C  
ATOM   1972  C   ALA A 344     184.688 194.933 259.918  1.00 82.53           C  
ATOM   1973  O   ALA A 344     185.586 195.681 260.303  1.00 82.60           O  
ATOM   1974  CB  ALA A 344     184.882 194.188 257.555  1.00 81.18           C  
ATOM   1975  N   THR A 345     184.190 193.970 260.676  1.00 83.03           N  
ATOM   1976  CA  THR A 345     184.691 193.763 262.022  1.00 83.40           C  
ATOM   1977  C   THR A 345     186.010 193.012 262.020  1.00 83.51           C  
ATOM   1978  O   THR A 345     186.746 193.032 263.006  1.00 83.09           O  
ATOM   1979  CB  THR A 345     183.662 192.991 262.858  1.00 85.35           C  
ATOM   1980  N   ARG A 346     186.311 192.344 260.912  1.00 83.05           N  
ATOM   1981  CA  ARG A 346     187.543 191.582 260.812  1.00 83.88           C  
ATOM   1982  C   ARG A 346     188.147 191.620 259.418  1.00 83.83           C  
ATOM   1983  O   ARG A 346     187.457 191.407 258.421  1.00 82.54           O  
ATOM   1984  CB  ARG A 346     187.292 190.133 261.195  1.00 85.30           C  
ATOM   1985  CG  ARG A 346     188.528 189.250 261.225  1.00 86.32           C  
ATOM   1986  CD  ARG A 346     188.186 187.856 261.590  1.00 88.11           C  
ATOM   1987  NE  ARG A 346     187.658 187.761 262.944  1.00 89.75           N  
ATOM   1988  CZ  ARG A 346     188.407 187.665 264.064  1.00 91.47           C  
ATOM   1989  NH1 ARG A 346     189.722 187.656 263.988  1.00 91.54           N  
ATOM   1990  NH2 ARG A 346     187.814 187.581 265.243  1.00 90.86           N  
ATOM   1991  N   PHE A 347     189.453 191.840 259.365  1.00 83.31           N  
ATOM   1992  CA  PHE A 347     190.232 191.758 258.139  1.00 82.03           C  
ATOM   1993  C   PHE A 347     191.144 190.550 258.169  1.00 82.62           C  
ATOM   1994  O   PHE A 347     191.605 190.142 259.236  1.00 82.97           O  
ATOM   1995  CB  PHE A 347     191.067 193.008 257.910  1.00 81.43           C  
ATOM   1996  CG  PHE A 347     190.363 194.155 257.263  1.00 81.18           C  
ATOM   1997  CD1 PHE A 347     189.130 194.610 257.683  1.00 81.67           C  
ATOM   1998  CD2 PHE A 347     190.977 194.797 256.199  1.00 81.19           C  
ATOM   1999  CE1 PHE A 347     188.524 195.663 257.040  1.00 81.35           C  
ATOM   2000  CE2 PHE A 347     190.374 195.848 255.565  1.00 80.63           C  
ATOM   2001  CZ  PHE A 347     189.140 196.278 255.986  1.00 80.01           C  
ATOM   2002  N   ALA A 348     191.407 189.994 257.000  1.00 81.98           N  
ATOM   2003  CA  ALA A 348     192.311 188.868 256.849  1.00 80.92           C  
ATOM   2004  C   ALA A 348     193.762 189.312 256.944  1.00 81.85           C  
ATOM   2005  O   ALA A 348     194.086 190.482 256.726  1.00 81.70           O  
ATOM   2006  CB  ALA A 348     192.071 188.178 255.520  1.00 79.88           C  
ATOM   2007  N   SER A 349     194.631 188.359 257.254  1.00 82.49           N  
ATOM   2008  CA  SER A 349     196.056 188.613 257.240  1.00 82.09           C  
ATOM   2009  C   SER A 349     196.480 188.791 255.803  1.00 82.06           C  
ATOM   2010  O   SER A 349     195.773 188.376 254.890  1.00 81.17           O  
ATOM   2011  CB  SER A 349     196.805 187.461 257.857  1.00 83.12           C  
ATOM   2012  OG  SER A 349     196.741 186.329 257.040  1.00 82.69           O  
ATOM   2013  N   VAL A 350     197.630 189.394 255.586  1.00 81.61           N  
ATOM   2014  CA  VAL A 350     198.050 189.645 254.223  1.00 81.33           C  
ATOM   2015  C   VAL A 350     198.519 188.409 253.467  1.00 82.83           C  
ATOM   2016  O   VAL A 350     198.307 188.319 252.263  1.00 81.97           O  
ATOM   2017  CB  VAL A 350     199.101 190.750 254.185  1.00 82.24           C  
ATOM   2018  CG1 VAL A 350     200.412 190.256 254.752  1.00 82.82           C  
ATOM   2019  CG2 VAL A 350     199.228 191.235 252.737  1.00 81.89           C  
ATOM   2020  N   TYR A 351     199.148 187.442 254.130  1.00 82.00           N  
ATOM   2021  CA  TYR A 351     199.603 186.274 253.370  1.00 82.68           C  
ATOM   2022  C   TYR A 351     198.403 185.516 252.827  1.00 82.00           C  
ATOM   2023  O   TYR A 351     198.483 184.856 251.792  1.00 82.19           O  
ATOM   2024  CB  TYR A 351     200.481 185.348 254.215  1.00 82.89           C  
ATOM   2025  CG  TYR A 351     199.744 184.249 254.910  1.00 83.18           C  
ATOM   2026  CD1 TYR A 351     199.678 182.999 254.325  1.00 84.29           C  
ATOM   2027  CD2 TYR A 351     199.130 184.478 256.107  1.00 83.06           C  
ATOM   2028  CE1 TYR A 351     199.001 181.980 254.951  1.00 84.55           C  
ATOM   2029  CE2 TYR A 351     198.446 183.465 256.736  1.00 83.57           C  
ATOM   2030  CZ  TYR A 351     198.382 182.220 256.164  1.00 83.40           C  
ATOM   2031  OH  TYR A 351     197.697 181.210 256.792  1.00 84.48           O  
ATOM   2032  N   ALA A 352     197.272 185.660 253.500  1.00 81.80           N  
ATOM   2033  CA  ALA A 352     196.038 185.012 253.113  1.00 81.15           C  
ATOM   2034  C   ALA A 352     194.954 186.059 252.976  1.00 80.48           C  
ATOM   2035  O   ALA A 352     193.908 185.984 253.623  1.00 80.58           O  
ATOM   2036  CB  ALA A 352     195.653 183.962 254.132  1.00 83.19           C  
ATOM   2037  N   TRP A 353     195.225 187.039 252.127  1.00 80.63           N  
ATOM   2038  CA  TRP A 353     194.342 188.172 251.913  1.00 79.04           C  
ATOM   2039  C   TRP A 353     193.008 187.700 251.376  1.00 78.88           C  
ATOM   2040  O   TRP A 353     192.944 186.706 250.654  1.00 78.79           O  
ATOM   2041  CB  TRP A 353     195.017 189.153 250.948  1.00 80.09           C  
ATOM   2042  CG  TRP A 353     195.540 188.535 249.651  1.00 79.59           C  
ATOM   2043  CD1 TRP A 353     196.771 187.966 249.446  1.00 80.10           C  
ATOM   2044  CD2 TRP A 353     194.870 188.472 248.376  1.00 78.65           C  
ATOM   2045  NE1 TRP A 353     196.893 187.561 248.141  1.00 80.15           N  
ATOM   2046  CE2 TRP A 353     195.751 187.866 247.478  1.00 79.01           C  
ATOM   2047  CE3 TRP A 353     193.625 188.882 247.925  1.00 78.35           C  
ATOM   2048  CZ2 TRP A 353     195.421 187.668 246.168  1.00 79.20           C  
ATOM   2049  CZ3 TRP A 353     193.302 188.675 246.599  1.00 77.75           C  
ATOM   2050  CH2 TRP A 353     194.179 188.083 245.746  1.00 78.63           C  
ATOM   2051  N   ASN A 354     191.923 188.375 251.750  1.00 77.87           N  
ATOM   2052  CA  ASN A 354     190.627 187.926 251.282  1.00 77.13           C  
ATOM   2053  C   ASN A 354     190.217 188.727 250.068  1.00 77.66           C  
ATOM   2054  O   ASN A 354     190.905 189.678 249.696  1.00 75.86           O  
ATOM   2055  CB  ASN A 354     189.603 188.065 252.397  1.00 76.69           C  
ATOM   2056  CG  ASN A 354     188.462 187.094 252.304  1.00 77.14           C  
ATOM   2057  OD1 ASN A 354     188.187 186.521 251.245  1.00 76.77           O  
ATOM   2058  ND2 ASN A 354     187.783 186.902 253.403  1.00 76.89           N  
ATOM   2059  N   ARG A 355     189.077 188.391 249.488  1.00 75.74           N  
ATOM   2060  CA  ARG A 355     188.558 189.174 248.383  1.00 74.62           C  
ATOM   2061  C   ARG A 355     187.069 188.970 248.229  1.00 74.07           C  
ATOM   2062  O   ARG A 355     186.593 187.836 248.160  1.00 74.42           O  
ATOM   2063  CB  ARG A 355     189.249 188.818 247.082  1.00 74.70           C  
ATOM   2064  CG  ARG A 355     188.954 187.440 246.531  1.00 75.18           C  
ATOM   2065  CD  ARG A 355     189.874 187.096 245.430  1.00 75.64           C  
ATOM   2066  NE  ARG A 355     189.743 188.013 244.308  1.00 74.83           N  
ATOM   2067  CZ  ARG A 355     190.472 187.954 243.178  1.00 74.41           C  
ATOM   2068  NH1 ARG A 355     191.370 187.004 243.019  1.00 74.34           N  
ATOM   2069  NH2 ARG A 355     190.287 188.852 242.228  1.00 73.98           N  
ATOM   2070  N   LYS A 356     186.335 190.064 248.140  1.00 74.09           N  
ATOM   2071  CA  LYS A 356     184.904 189.971 247.924  1.00 73.30           C  
ATOM   2072  C   LYS A 356     184.545 190.424 246.526  1.00 73.47           C  
ATOM   2073  O   LYS A 356     185.090 191.404 246.018  1.00 73.64           O  
ATOM   2074  CB  LYS A 356     184.136 190.788 248.965  1.00 73.32           C  
ATOM   2075  CG  LYS A 356     182.621 190.673 248.825  1.00 74.27           C  
ATOM   2076  CD  LYS A 356     181.878 191.320 249.981  1.00 74.11           C  
ATOM   2077  CE  LYS A 356     180.367 191.179 249.789  1.00 73.81           C  
ATOM   2078  NZ  LYS A 356     179.593 191.705 250.950  1.00 75.38           N  
ATOM   2079  N   ARG A 357     183.616 189.717 245.899  1.00 73.14           N  
ATOM   2080  CA  ARG A 357     183.153 190.142 244.592  1.00 72.16           C  
ATOM   2081  C   ARG A 357     181.988 191.089 244.750  1.00 73.00           C  
ATOM   2082  O   ARG A 357     181.005 190.782 245.425  1.00 72.55           O  
ATOM   2083  CB  ARG A 357     182.708 188.975 243.733  1.00 72.92           C  
ATOM   2084  CG  ARG A 357     182.270 189.384 242.321  1.00 72.50           C  
ATOM   2085  CD  ARG A 357     181.580 188.306 241.617  1.00 72.74           C  
ATOM   2086  NE  ARG A 357     181.185 188.715 240.267  1.00 71.78           N  
ATOM   2087  CZ  ARG A 357     180.033 188.381 239.651  1.00 72.18           C  
ATOM   2088  NH1 ARG A 357     179.124 187.644 240.257  1.00 71.65           N  
ATOM   2089  NH2 ARG A 357     179.828 188.814 238.422  1.00 71.43           N  
ATOM   2090  N   ILE A 358     182.094 192.227 244.103  1.00 72.41           N  
ATOM   2091  CA  ILE A 358     181.058 193.230 244.103  1.00 72.56           C  
ATOM   2092  C   ILE A 358     180.350 193.236 242.754  1.00 72.27           C  
ATOM   2093  O   ILE A 358     180.975 193.405 241.700  1.00 71.75           O  
ATOM   2094  CB  ILE A 358     181.678 194.589 244.434  1.00 72.17           C  
ATOM   2095  CG1 ILE A 358     182.287 194.536 245.849  1.00 72.17           C  
ATOM   2096  CG2 ILE A 358     180.674 195.666 244.297  1.00 71.97           C  
ATOM   2097  CD1 ILE A 358     183.170 195.711 246.189  1.00 72.12           C  
ATOM   2098  N   SER A 359     179.040 193.018 242.792  1.00 71.78           N  
ATOM   2099  CA  SER A 359     178.241 192.908 241.583  1.00 71.84           C  
ATOM   2100  C   SER A 359     176.789 193.317 241.807  1.00 71.68           C  
ATOM   2101  O   SER A 359     176.318 193.403 242.939  1.00 71.85           O  
ATOM   2102  CB  SER A 359     178.295 191.487 241.067  1.00 71.62           C  
ATOM   2103  OG  SER A 359     177.666 190.604 241.956  1.00 72.50           O  
ATOM   2104  N   ASN A 360     176.085 193.564 240.707  1.00 70.38           N  
ATOM   2105  CA  ASN A 360     174.661 193.904 240.691  1.00 71.39           C  
ATOM   2106  C   ASN A 360     174.300 194.988 241.694  1.00 70.86           C  
ATOM   2107  O   ASN A 360     173.415 194.769 242.531  1.00 71.03           O  
ATOM   2108  CB  ASN A 360     173.802 192.676 240.918  1.00 71.38           C  
ATOM   2109  CG  ASN A 360     172.358 192.922 240.556  1.00 71.54           C  
ATOM   2110  OD1 ASN A 360     172.058 193.699 239.641  1.00 70.60           O  
ATOM   2111  ND2 ASN A 360     171.463 192.271 241.254  1.00 70.57           N  
ATOM   2112  N   CYS A 361     174.993 196.135 241.630  1.00 70.43           N  
ATOM   2113  CA  CYS A 361     174.813 197.206 242.598  1.00 70.91           C  
ATOM   2114  C   CYS A 361     175.099 198.586 241.995  1.00 70.58           C  
ATOM   2115  O   CYS A 361     175.708 198.701 240.927  1.00 70.58           O  
ATOM   2116  CB  CYS A 361     175.741 196.964 243.814  1.00 71.03           C  
ATOM   2117  SG  CYS A 361     177.599 197.117 243.494  1.00 72.93           S  
ATOM   2118  N   VAL A 362     174.678 199.633 242.725  1.00 70.57           N  
ATOM   2119  CA  VAL A 362     174.968 201.028 242.413  1.00 71.19           C  
ATOM   2120  C   VAL A 362     176.091 201.486 243.314  1.00 70.65           C  
ATOM   2121  O   VAL A 362     175.923 201.627 244.530  1.00 71.99           O  
ATOM   2122  CB  VAL A 362     173.742 201.912 242.651  1.00 69.84           C  
ATOM   2123  CG1 VAL A 362     174.079 203.364 242.290  1.00 69.88           C  
ATOM   2124  CG2 VAL A 362     172.585 201.379 241.839  1.00 70.16           C  
ATOM   2125  N   ALA A 363     177.250 201.660 242.718  1.00 70.17           N  
ATOM   2126  CA  ALA A 363     178.454 201.913 243.471  1.00 71.00           C  
ATOM   2127  C   ALA A 363     178.715 203.388 243.616  1.00 71.51           C  
ATOM   2128  O   ALA A 363     179.180 204.043 242.688  1.00 71.13           O  
ATOM   2129  CB  ALA A 363     179.623 201.227 242.800  1.00 70.47           C  
ATOM   2130  N   ASP A 364     178.396 203.916 244.783  1.00 71.73           N  
ATOM   2131  CA  ASP A 364     178.593 205.327 245.028  1.00 70.72           C  
ATOM   2132  C   ASP A 364     179.969 205.514 245.622  1.00 71.16           C  
ATOM   2133  O   ASP A 364     180.210 205.157 246.775  1.00 73.57           O  
ATOM   2134  CB  ASP A 364     177.522 205.893 245.953  1.00 71.80           C  
ATOM   2135  CG  ASP A 364     177.664 207.390 246.124  1.00 72.59           C  
ATOM   2136  OD1 ASP A 364     178.727 207.910 245.824  1.00 71.81           O  
ATOM   2137  OD2 ASP A 364     176.719 208.015 246.538  1.00 73.08           O  
ATOM   2138  N   TYR A 365     180.893 206.028 244.828  1.00 70.92           N  
ATOM   2139  CA  TYR A 365     182.272 206.107 245.259  1.00 71.41           C  
ATOM   2140  C   TYR A 365     182.577 207.447 245.896  1.00 72.81           C  
ATOM   2141  O   TYR A 365     183.708 207.684 246.327  1.00 74.60           O  
ATOM   2142  CB  TYR A 365     183.207 205.880 244.079  1.00 69.83           C  
ATOM   2143  CG  TYR A 365     183.161 204.491 243.495  1.00 69.79           C  
ATOM   2144  CD1 TYR A 365     182.415 204.243 242.361  1.00 68.90           C  
ATOM   2145  CD2 TYR A 365     183.884 203.469 244.081  1.00 70.61           C  
ATOM   2146  CE1 TYR A 365     182.396 202.987 241.813  1.00 68.93           C  
ATOM   2147  CE2 TYR A 365     183.860 202.208 243.531  1.00 70.89           C  
ATOM   2148  CZ  TYR A 365     183.121 201.968 242.400  1.00 69.92           C  
ATOM   2149  OH  TYR A 365     183.099 200.712 241.849  1.00 70.83           O  
ATOM   2150  N   SER A 366     181.579 208.334 245.951  1.00 73.45           N  
ATOM   2151  CA  SER A 366     181.816 209.643 246.535  1.00 74.32           C  
ATOM   2152  C   SER A 366     181.873 209.500 248.037  1.00 74.59           C  
ATOM   2153  O   SER A 366     182.515 210.290 248.721  1.00 75.75           O  
ATOM   2154  CB  SER A 366     180.729 210.635 246.169  1.00 74.48           C  
ATOM   2155  OG  SER A 366     179.541 210.353 246.845  1.00 74.76           O  
ATOM   2156  N   VAL A 367     181.247 208.451 248.552  1.00 74.37           N  
ATOM   2157  CA  VAL A 367     181.249 208.222 249.978  1.00 75.64           C  
ATOM   2158  C   VAL A 367     182.641 207.839 250.432  1.00 75.96           C  
ATOM   2159  O   VAL A 367     183.173 208.408 251.386  1.00 76.31           O  
ATOM   2160  CB  VAL A 367     180.263 207.095 250.330  1.00 74.96           C  
ATOM   2161  CG1 VAL A 367     180.371 206.733 251.813  1.00 76.75           C  
ATOM   2162  CG2 VAL A 367     178.856 207.541 249.978  1.00 74.91           C  
ATOM   2163  N   LEU A 368     183.241 206.889 249.729  1.00 75.05           N  
ATOM   2164  CA  LEU A 368     184.566 206.424 250.079  1.00 75.44           C  
ATOM   2165  C   LEU A 368     185.600 207.504 249.832  1.00 75.66           C  
ATOM   2166  O   LEU A 368     186.554 207.649 250.593  1.00 76.03           O  
ATOM   2167  CB  LEU A 368     184.915 205.185 249.251  1.00 76.61           C  
ATOM   2168  CG  LEU A 368     184.096 203.921 249.524  1.00 76.82           C  
ATOM   2169  CD1 LEU A 368     184.451 202.879 248.472  1.00 76.21           C  
ATOM   2170  CD2 LEU A 368     184.400 203.396 250.922  1.00 77.85           C  
ATOM   2171  N   TYR A 369     185.419 208.260 248.762  1.00 75.21           N  
ATOM   2172  CA  TYR A 369     186.355 209.311 248.427  1.00 76.13           C  
ATOM   2173  C   TYR A 369     186.295 210.486 249.395  1.00 74.75           C  
ATOM   2174  O   TYR A 369     187.331 210.997 249.821  1.00 76.28           O  
ATOM   2175  CB  TYR A 369     186.127 209.780 247.002  1.00 74.96           C  
ATOM   2176  CG  TYR A 369     187.077 210.832 246.603  1.00 74.62           C  
ATOM   2177  CD1 TYR A 369     188.410 210.518 246.459  1.00 73.45           C  
ATOM   2178  CD2 TYR A 369     186.630 212.115 246.377  1.00 75.42           C  
ATOM   2179  CE1 TYR A 369     189.302 211.484 246.095  1.00 73.96           C  
ATOM   2180  CE2 TYR A 369     187.520 213.085 246.007  1.00 76.51           C  
ATOM   2181  CZ  TYR A 369     188.852 212.771 245.868  1.00 75.39           C  
ATOM   2182  OH  TYR A 369     189.740 213.733 245.497  1.00 78.71           O  
ATOM   2183  N   ASN A 370     185.084 210.935 249.724  1.00 78.22           N  
ATOM   2184  CA  ASN A 370     184.913 212.087 250.594  1.00 77.29           C  
ATOM   2185  C   ASN A 370     185.243 211.781 252.049  1.00 78.60           C  
ATOM   2186  O   ASN A 370     185.678 212.672 252.789  1.00 78.95           O  
ATOM   2187  CB  ASN A 370     183.508 212.629 250.473  1.00 77.31           C  
ATOM   2188  CG  ASN A 370     183.284 213.317 249.164  1.00 77.33           C  
ATOM   2189  OD1 ASN A 370     184.214 213.863 248.558  1.00 77.37           O  
ATOM   2190  ND2 ASN A 370     182.064 213.308 248.710  1.00 77.22           N  
ATOM   2191  N   SER A 371     185.057 210.527 252.464  1.00 77.32           N  
ATOM   2192  CA  SER A 371     185.355 210.142 253.833  1.00 77.91           C  
ATOM   2193  C   SER A 371     186.765 210.524 254.238  1.00 78.75           C  
ATOM   2194  O   SER A 371     187.745 210.167 253.587  1.00 78.14           O  
ATOM   2195  CB  SER A 371     185.171 208.654 254.001  1.00 77.54           C  
ATOM   2196  OG  SER A 371     185.738 208.218 255.202  1.00 77.99           O  
ATOM   2197  N   ALA A 372     186.868 211.213 255.368  1.00 79.75           N  
ATOM   2198  CA  ALA A 372     188.147 211.696 255.874  1.00 79.21           C  
ATOM   2199  C   ALA A 372     188.853 210.651 256.723  1.00 79.06           C  
ATOM   2200  O   ALA A 372     189.944 210.894 257.234  1.00 79.45           O  
ATOM   2201  CB  ALA A 372     187.939 212.968 256.679  1.00 80.51           C  
ATOM   2202  N   SER A 373     188.226 209.493 256.886  1.00 78.32           N  
ATOM   2203  CA  SER A 373     188.795 208.434 257.712  1.00 78.62           C  
ATOM   2204  C   SER A 373     189.991 207.750 257.054  1.00 79.16           C  
ATOM   2205  O   SER A 373     190.732 207.021 257.716  1.00 79.20           O  
ATOM   2206  CB  SER A 373     187.748 207.382 258.040  1.00 79.24           C  
ATOM   2207  OG  SER A 373     187.394 206.639 256.908  1.00 78.57           O  
ATOM   2208  N   PHE A 374     190.173 207.961 255.754  1.00 79.65           N  
ATOM   2209  CA  PHE A 374     191.232 207.275 255.034  1.00 78.93           C  
ATOM   2210  C   PHE A 374     192.537 208.054 255.070  1.00 79.05           C  
ATOM   2211  O   PHE A 374     192.545 209.275 254.914  1.00 79.09           O  
ATOM   2212  CB  PHE A 374     190.797 207.018 253.593  1.00 78.37           C  
ATOM   2213  CG  PHE A 374     189.596 206.115 253.514  1.00 78.02           C  
ATOM   2214  CD1 PHE A 374     188.421 206.550 252.932  1.00 77.85           C  
ATOM   2215  CD2 PHE A 374     189.621 204.846 254.056  1.00 79.00           C  
ATOM   2216  CE1 PHE A 374     187.315 205.728 252.886  1.00 77.30           C  
ATOM   2217  CE2 PHE A 374     188.510 204.033 254.010  1.00 79.16           C  
ATOM   2218  CZ  PHE A 374     187.359 204.476 253.421  1.00 77.43           C  
ATOM   2219  N   SER A 375     193.652 207.342 255.258  1.00 78.60           N  
ATOM   2220  CA  SER A 375     194.953 207.995 255.272  1.00 78.68           C  
ATOM   2221  C   SER A 375     195.421 208.188 253.850  1.00 78.71           C  
ATOM   2222  O   SER A 375     196.158 209.125 253.535  1.00 78.43           O  
ATOM   2223  CB  SER A 375     195.960 207.162 256.030  1.00 79.78           C  
ATOM   2224  OG  SER A 375     196.272 205.995 255.327  1.00 80.26           O  
ATOM   2225  N   THR A 376     194.946 207.314 252.974  1.00 77.75           N  
ATOM   2226  CA  THR A 376     195.260 207.433 251.568  1.00 77.71           C  
ATOM   2227  C   THR A 376     194.129 206.891 250.705  1.00 77.37           C  
ATOM   2228  O   THR A 376     193.417 205.958 251.090  1.00 76.62           O  
ATOM   2229  CB  THR A 376     196.576 206.711 251.232  1.00 77.85           C  
ATOM   2230  OG1 THR A 376     196.943 207.003 249.883  1.00 75.81           O  
ATOM   2231  CG2 THR A 376     196.412 205.209 251.399  1.00 77.53           C  
ATOM   2232  N   PHE A 377     193.983 207.483 249.530  1.00 75.11           N  
ATOM   2233  CA  PHE A 377     193.026 207.062 248.519  1.00 74.17           C  
ATOM   2234  C   PHE A 377     193.672 207.335 247.181  1.00 73.31           C  
ATOM   2235  O   PHE A 377     193.598 208.453 246.668  1.00 73.95           O  
ATOM   2236  CB  PHE A 377     191.719 207.860 248.642  1.00 74.27           C  
ATOM   2237  CG  PHE A 377     190.547 207.329 247.846  1.00 73.91           C  
ATOM   2238  CD1 PHE A 377     189.421 206.881 248.507  1.00 75.38           C  
ATOM   2239  CD2 PHE A 377     190.553 207.277 246.452  1.00 73.20           C  
ATOM   2240  CE1 PHE A 377     188.345 206.400 247.811  1.00 75.04           C  
ATOM   2241  CE2 PHE A 377     189.464 206.789 245.766  1.00 73.33           C  
ATOM   2242  CZ  PHE A 377     188.364 206.353 246.446  1.00 73.97           C  
ATOM   2243  N   LYS A 378     194.348 206.345 246.631  1.00 72.60           N  
ATOM   2244  CA  LYS A 378     195.101 206.589 245.416  1.00 71.77           C  
ATOM   2245  C   LYS A 378     194.665 205.655 244.300  1.00 71.94           C  
ATOM   2246  O   LYS A 378     194.681 204.434 244.466  1.00 72.19           O  
ATOM   2247  CB  LYS A 378     196.598 206.443 245.684  1.00 71.67           C  
ATOM   2248  CG  LYS A 378     197.474 206.759 244.490  1.00 70.94           C  
ATOM   2249  CD  LYS A 378     198.937 206.784 244.871  1.00 70.96           C  
ATOM   2250  CE  LYS A 378     199.798 207.204 243.694  1.00 70.91           C  
ATOM   2251  NZ  LYS A 378     201.241 207.268 244.056  1.00 70.98           N  
ATOM   2252  N   CYS A 379     194.276 206.240 243.159  1.00 70.85           N  
ATOM   2253  CA  CYS A 379     193.842 205.500 241.979  1.00 69.81           C  
ATOM   2254  C   CYS A 379     194.955 205.518 240.934  1.00 68.78           C  
ATOM   2255  O   CYS A 379     195.715 206.482 240.851  1.00 68.84           O  
ATOM   2256  CB  CYS A 379     192.556 206.104 241.401  1.00 67.56           C  
ATOM   2257  SG  CYS A 379     191.143 206.091 242.537  1.00 70.20           S  
ATOM   2258  N   TYR A 380     195.056 204.431 240.144  1.00 67.59           N  
ATOM   2259  CA  TYR A 380     196.118 204.284 239.139  1.00 68.49           C  
ATOM   2260  C   TYR A 380     195.629 204.320 237.696  1.00 66.15           C  
ATOM   2261  O   TYR A 380     196.167 205.065 236.881  1.00 66.12           O  
ATOM   2262  CB  TYR A 380     196.889 203.001 239.431  1.00 69.61           C  
ATOM   2263  CG  TYR A 380     197.580 203.088 240.764  1.00 70.02           C  
ATOM   2264  CD1 TYR A 380     196.941 202.648 241.903  1.00 70.50           C  
ATOM   2265  CD2 TYR A 380     198.845 203.632 240.850  1.00 70.21           C  
ATOM   2266  CE1 TYR A 380     197.561 202.757 243.122  1.00 72.15           C  
ATOM   2267  CE2 TYR A 380     199.466 203.735 242.070  1.00 71.53           C  
ATOM   2268  CZ  TYR A 380     198.824 203.301 243.202  1.00 71.32           C  
ATOM   2269  OH  TYR A 380     199.435 203.405 244.422  1.00 72.90           O  
ATOM   2270  N   GLY A 381     194.623 203.525 237.362  1.00 66.04           N  
ATOM   2271  CA  GLY A 381     194.155 203.501 235.977  1.00 64.91           C  
ATOM   2272  C   GLY A 381     192.973 204.435 235.738  1.00 62.38           C  
ATOM   2273  O   GLY A 381     192.510 204.584 234.608  1.00 60.30           O  
ATOM   2274  N   VAL A 382     192.454 205.013 236.811  1.00 64.07           N  
ATOM   2275  CA  VAL A 382     191.320 205.927 236.751  1.00 61.01           C  
ATOM   2276  C   VAL A 382     191.540 207.098 237.687  1.00 60.56           C  
ATOM   2277  O   VAL A 382     192.290 206.984 238.649  1.00 64.25           O  
ATOM   2278  CB  VAL A 382     190.005 205.218 237.128  1.00 60.35           C  
ATOM   2279  CG1 VAL A 382     189.699 204.109 236.146  1.00 60.89           C  
ATOM   2280  CG2 VAL A 382     190.115 204.655 238.522  1.00 64.47           C  
ATOM   2281  N   SER A 383     190.834 208.189 237.469  1.00 60.13           N  
ATOM   2282  CA  SER A 383     190.843 209.270 238.440  1.00 60.60           C  
ATOM   2283  C   SER A 383     189.700 209.053 239.432  1.00 63.00           C  
ATOM   2284  O   SER A 383     188.628 208.592 239.044  1.00 63.56           O  
ATOM   2285  CB  SER A 383     190.737 210.604 237.739  1.00 58.48           C  
ATOM   2286  OG  SER A 383     191.906 210.861 237.010  1.00 56.20           O  
ATOM   2287  N   PRO A 384     189.892 209.379 240.714  1.00 63.10           N  
ATOM   2288  CA  PRO A 384     188.967 209.145 241.809  1.00 64.32           C  
ATOM   2289  C   PRO A 384     187.645 209.885 241.681  1.00 64.42           C  
ATOM   2290  O   PRO A 384     186.664 209.519 242.324  1.00 65.53           O  
ATOM   2291  CB  PRO A 384     189.759 209.637 243.018  1.00 67.83           C  
ATOM   2292  CG  PRO A 384     190.767 210.605 242.464  1.00 66.26           C  
ATOM   2293  CD  PRO A 384     191.130 210.057 241.113  1.00 63.82           C  
ATOM   2294  N   THR A 385     187.601 210.921 240.854  1.00 63.22           N  
ATOM   2295  CA  THR A 385     186.378 211.692 240.705  1.00 62.88           C  
ATOM   2296  C   THR A 385     185.610 211.317 239.442  1.00 62.41           C  
ATOM   2297  O   THR A 385     184.558 211.887 239.160  1.00 62.50           O  
ATOM   2298  CB  THR A 385     186.687 213.193 240.715  1.00 62.48           C  
ATOM   2299  OG1 THR A 385     187.545 213.509 239.624  1.00 61.38           O  
ATOM   2300  CG2 THR A 385     187.382 213.557 242.027  1.00 67.08           C  
ATOM   2301  N   LYS A 386     186.138 210.356 238.682  1.00 62.92           N  
ATOM   2302  CA  LYS A 386     185.488 209.864 237.467  1.00 61.77           C  
ATOM   2303  C   LYS A 386     184.784 208.549 237.761  1.00 63.34           C  
ATOM   2304  O   LYS A 386     184.079 207.990 236.918  1.00 63.91           O  
ATOM   2305  CB  LYS A 386     186.506 209.659 236.344  1.00 59.15           C  
ATOM   2306  CG  LYS A 386     187.223 210.908 235.855  1.00 57.15           C  
ATOM   2307  CD  LYS A 386     186.302 211.806 235.064  1.00 57.04           C  
ATOM   2308  CE  LYS A 386     187.081 212.929 234.404  1.00 55.19           C  
ATOM   2309  NZ  LYS A 386     186.197 213.815 233.609  1.00 55.37           N  
ATOM   2310  N   LEU A 387     184.975 208.057 238.974  1.00 63.40           N  
ATOM   2311  CA  LEU A 387     184.490 206.745 239.356  1.00 63.43           C  
ATOM   2312  C   LEU A 387     182.982 206.639 239.278  1.00 65.18           C  
ATOM   2313  O   LEU A 387     182.447 205.560 239.041  1.00 66.17           O  
ATOM   2314  CB  LEU A 387     184.941 206.418 240.782  1.00 65.86           C  
ATOM   2315  CG  LEU A 387     186.446 206.225 241.007  1.00 66.03           C  
ATOM   2316  CD1 LEU A 387     186.717 206.047 242.492  1.00 68.38           C  
ATOM   2317  CD2 LEU A 387     186.917 205.032 240.267  1.00 66.04           C  
ATOM   2318  N   ASN A 388     182.283 207.748 239.469  1.00 63.70           N  
ATOM   2319  CA  ASN A 388     180.834 207.711 239.426  1.00 65.08           C  
ATOM   2320  C   ASN A 388     180.270 207.800 238.006  1.00 64.82           C  
ATOM   2321  O   ASN A 388     179.073 207.607 237.805  1.00 65.30           O  
ATOM   2322  CB  ASN A 388     180.281 208.808 240.304  1.00 66.70           C  
ATOM   2323  CG  ASN A 388     180.485 208.504 241.755  1.00 68.19           C  
ATOM   2324  OD1 ASN A 388     180.468 207.334 242.175  1.00 69.13           O  
ATOM   2325  ND2 ASN A 388     180.690 209.530 242.528  1.00 70.43           N  
ATOM   2326  N   ASP A 389     181.118 208.088 237.019  1.00 63.97           N  
ATOM   2327  CA  ASP A 389     180.666 208.178 235.629  1.00 63.87           C  
ATOM   2328  C   ASP A 389     180.861 206.854 234.902  1.00 63.72           C  
ATOM   2329  O   ASP A 389     180.119 206.523 233.974  1.00 62.30           O  
ATOM   2330  CB  ASP A 389     181.412 209.283 234.881  1.00 64.53           C  
ATOM   2331  CG  ASP A 389     181.108 210.682 235.394  1.00 64.50           C  
ATOM   2332  OD1 ASP A 389     179.988 211.121 235.256  1.00 64.30           O  
ATOM   2333  OD2 ASP A 389     181.997 211.308 235.908  1.00 62.94           O  
ATOM   2334  N   LEU A 390     181.874 206.117 235.333  1.00 63.43           N  
ATOM   2335  CA  LEU A 390     182.254 204.835 234.755  1.00 63.55           C  
ATOM   2336  C   LEU A 390     181.314 203.734 235.235  1.00 63.82           C  
ATOM   2337  O   LEU A 390     180.663 203.878 236.266  1.00 66.20           O  
ATOM   2338  CB  LEU A 390     183.693 204.481 235.182  1.00 63.60           C  
ATOM   2339  CG  LEU A 390     184.813 205.433 234.727  1.00 61.33           C  
ATOM   2340  CD1 LEU A 390     186.125 205.020 235.403  1.00 61.13           C  
ATOM   2341  CD2 LEU A 390     184.952 205.380 233.213  1.00 58.63           C  
ATOM   2342  N   CYS A 391     181.258 202.623 234.464  1.00 64.62           N  
ATOM   2343  CA  CYS A 391     180.551 201.430 234.882  1.00 65.49           C  
ATOM   2344  C   CYS A 391     181.381 200.195 234.473  1.00 66.36           C  
ATOM   2345  O   CYS A 391     181.910 200.144 233.354  1.00 66.47           O  
ATOM   2346  CB  CYS A 391     179.145 201.345 234.250  1.00 64.69           C  
ATOM   2347  SG  CYS A 391     178.171 199.948 234.845  1.00 68.73           S  
ATOM   2348  N   PHE A 392     181.528 199.257 235.414  1.00 66.86           N  
ATOM   2349  CA  PHE A 392     182.405 198.090 235.310  1.00 68.04           C  
ATOM   2350  C   PHE A 392     181.603 196.809 235.202  1.00 68.69           C  
ATOM   2351  O   PHE A 392     180.406 196.785 235.507  1.00 68.35           O  
ATOM   2352  CB  PHE A 392     183.278 198.009 236.556  1.00 68.62           C  
ATOM   2353  CG  PHE A 392     183.926 199.292 236.877  1.00 68.88           C  
ATOM   2354  CD1 PHE A 392     183.424 200.053 237.908  1.00 68.61           C  
ATOM   2355  CD2 PHE A 392     184.992 199.762 236.161  1.00 70.22           C  
ATOM   2356  CE1 PHE A 392     183.988 201.253 238.232  1.00 68.69           C  
ATOM   2357  CE2 PHE A 392     185.568 200.982 236.477  1.00 68.76           C  
ATOM   2358  CZ  PHE A 392     185.062 201.725 237.517  1.00 68.34           C  
ATOM   2359  N   THR A 393     182.263 195.734 234.790  1.00 68.56           N  
ATOM   2360  CA  THR A 393     181.588 194.447 234.766  1.00 68.97           C  
ATOM   2361  C   THR A 393     181.820 193.663 236.046  1.00 69.53           C  
ATOM   2362  O   THR A 393     181.027 192.789 236.391  1.00 69.65           O  
ATOM   2363  CB  THR A 393     182.057 193.612 233.582  1.00 69.14           C  
ATOM   2364  OG1 THR A 393     183.475 193.437 233.685  1.00 69.88           O  
ATOM   2365  CG2 THR A 393     181.691 194.289 232.294  1.00 68.88           C  
ATOM   2366  N   ASN A 394     182.908 193.970 236.738  1.00 70.08           N  
ATOM   2367  CA  ASN A 394     183.262 193.327 238.000  1.00 70.90           C  
ATOM   2368  C   ASN A 394     184.103 194.249 238.858  1.00 71.25           C  
ATOM   2369  O   ASN A 394     185.046 194.878 238.369  1.00 71.70           O  
ATOM   2370  CB  ASN A 394     184.019 192.017 237.806  1.00 70.69           C  
ATOM   2371  CG  ASN A 394     183.184 190.897 237.285  1.00 71.92           C  
ATOM   2372  OD1 ASN A 394     182.302 190.388 237.998  1.00 71.67           O  
ATOM   2373  ND2 ASN A 394     183.454 190.473 236.076  1.00 70.97           N  
ATOM   2374  N   VAL A 395     183.801 194.300 240.145  1.00 70.63           N  
ATOM   2375  CA  VAL A 395     184.674 194.999 241.066  1.00 70.60           C  
ATOM   2376  C   VAL A 395     185.099 194.049 242.171  1.00 72.36           C  
ATOM   2377  O   VAL A 395     184.264 193.428 242.821  1.00 71.72           O  
ATOM   2378  CB  VAL A 395     183.995 196.253 241.641  1.00 70.85           C  
ATOM   2379  CG1 VAL A 395     184.927 196.923 242.661  1.00 71.03           C  
ATOM   2380  CG2 VAL A 395     183.657 197.203 240.498  1.00 69.89           C  
ATOM   2381  N   TYR A 396     186.393 193.910 242.378  1.00 72.09           N  
ATOM   2382  CA  TYR A 396     186.847 193.034 243.446  1.00 71.92           C  
ATOM   2383  C   TYR A 396     187.509 193.819 244.545  1.00 73.37           C  
ATOM   2384  O   TYR A 396     188.340 194.690 244.294  1.00 74.08           O  
ATOM   2385  CB  TYR A 396     187.786 191.956 242.923  1.00 73.22           C  
ATOM   2386  CG  TYR A 396     187.098 190.907 242.109  1.00 72.97           C  
ATOM   2387  CD1 TYR A 396     186.969 191.054 240.744  1.00 72.60           C  
ATOM   2388  CD2 TYR A 396     186.591 189.784 242.740  1.00 72.52           C  
ATOM   2389  CE1 TYR A 396     186.338 190.074 240.006  1.00 72.82           C  
ATOM   2390  CE2 TYR A 396     185.962 188.806 242.003  1.00 73.50           C  
ATOM   2391  CZ  TYR A 396     185.835 188.947 240.642  1.00 73.19           C  
ATOM   2392  OH  TYR A 396     185.208 187.969 239.907  1.00 72.46           O  
ATOM   2393  N   ALA A 397     187.140 193.505 245.773  1.00 72.61           N  
ATOM   2394  CA  ALA A 397     187.700 194.189 246.919  1.00 73.30           C  
ATOM   2395  C   ALA A 397     188.633 193.286 247.696  1.00 75.20           C  
ATOM   2396  O   ALA A 397     188.183 192.427 248.455  1.00 76.05           O  
ATOM   2397  CB  ALA A 397     186.588 194.680 247.813  1.00 74.25           C  
ATOM   2398  N   ASP A 398     189.930 193.491 247.510  1.00 75.30           N  
ATOM   2399  CA  ASP A 398     190.949 192.672 248.153  1.00 75.37           C  
ATOM   2400  C   ASP A 398     191.280 193.282 249.508  1.00 77.27           C  
ATOM   2401  O   ASP A 398     191.684 194.440 249.596  1.00 77.22           O  
ATOM   2402  CB  ASP A 398     192.180 192.548 247.262  1.00 76.03           C  
ATOM   2403  CG  ASP A 398     191.891 191.754 245.977  1.00 76.31           C  
ATOM   2404  OD1 ASP A 398     190.889 191.081 245.919  1.00 76.21           O  
ATOM   2405  OD2 ASP A 398     192.668 191.835 245.068  1.00 76.84           O  
ATOM   2406  N   SER A 399     191.029 192.529 250.572  1.00 77.47           N  
ATOM   2407  CA  SER A 399     191.094 193.065 251.934  1.00 77.46           C  
ATOM   2408  C   SER A 399     192.099 192.381 252.863  1.00 79.54           C  
ATOM   2409  O   SER A 399     192.050 191.164 253.081  1.00 79.50           O  
ATOM   2410  CB  SER A 399     189.713 192.989 252.543  1.00 78.89           C  
ATOM   2411  OG  SER A 399     189.741 193.366 253.875  1.00 79.98           O  
ATOM   2412  N   PHE A 400     193.021 193.181 253.410  1.00 79.23           N  
ATOM   2413  CA  PHE A 400     194.063 192.665 254.299  1.00 81.52           C  
ATOM   2414  C   PHE A 400     194.691 193.695 255.250  1.00 81.16           C  
ATOM   2415  O   PHE A 400     194.555 194.905 255.062  1.00 80.41           O  
ATOM   2416  CB  PHE A 400     195.158 192.029 253.471  1.00 80.67           C  
ATOM   2417  CG  PHE A 400     195.708 192.935 252.435  1.00 80.35           C  
ATOM   2418  CD1 PHE A 400     196.757 193.771 252.717  1.00 80.59           C  
ATOM   2419  CD2 PHE A 400     195.173 192.948 251.162  1.00 79.87           C  
ATOM   2420  CE1 PHE A 400     197.273 194.603 251.758  1.00 79.90           C  
ATOM   2421  CE2 PHE A 400     195.678 193.779 250.205  1.00 79.67           C  
ATOM   2422  CZ  PHE A 400     196.731 194.607 250.501  1.00 79.74           C  
ATOM   2423  N   VAL A 401     195.411 193.198 256.265  1.00 81.96           N  
ATOM   2424  CA  VAL A 401     196.147 194.066 257.197  1.00 81.46           C  
ATOM   2425  C   VAL A 401     197.669 193.943 257.117  1.00 82.06           C  
ATOM   2426  O   VAL A 401     198.230 192.854 257.233  1.00 83.26           O  
ATOM   2427  CB  VAL A 401     195.733 193.780 258.649  1.00 82.63           C  
ATOM   2428  CG1 VAL A 401     196.545 194.648 259.632  1.00 84.29           C  
ATOM   2429  CG2 VAL A 401     194.275 194.054 258.798  1.00 82.21           C  
ATOM   2430  N   ILE A 402     198.316 195.091 256.935  1.00 81.81           N  
ATOM   2431  CA  ILE A 402     199.777 195.227 256.901  1.00 83.52           C  
ATOM   2432  C   ILE A 402     200.235 196.385 257.773  1.00 81.33           C  
ATOM   2433  O   ILE A 402     199.420 197.200 258.194  1.00 82.92           O  
ATOM   2434  CB  ILE A 402     200.310 195.401 255.475  1.00 82.53           C  
ATOM   2435  CG1 ILE A 402     199.673 196.631 254.838  1.00 82.28           C  
ATOM   2436  CG2 ILE A 402     200.078 194.147 254.680  1.00 82.59           C  
ATOM   2437  CD1 ILE A 402     200.265 197.011 253.518  1.00 82.78           C  
ATOM   2438  N   ARG A 403     201.531 196.467 258.051  1.00 85.14           N  
ATOM   2439  CA  ARG A 403     202.046 197.600 258.815  1.00 83.75           C  
ATOM   2440  C   ARG A 403     202.158 198.847 257.945  1.00 84.26           C  
ATOM   2441  O   ARG A 403     202.465 198.753 256.757  1.00 83.78           O  
ATOM   2442  CB  ARG A 403     203.382 197.253 259.454  1.00 85.62           C  
ATOM   2443  CG  ARG A 403     204.505 196.889 258.505  1.00 84.48           C  
ATOM   2444  CD  ARG A 403     205.693 196.385 259.265  1.00 84.98           C  
ATOM   2445  NE  ARG A 403     206.501 197.466 259.807  1.00 85.18           N  
ATOM   2446  CZ  ARG A 403     207.545 198.032 259.168  1.00 84.99           C  
ATOM   2447  NH1 ARG A 403     207.909 197.596 257.980  1.00 84.69           N  
ATOM   2448  NH2 ARG A 403     208.209 199.024 259.733  1.00 86.21           N  
ATOM   2449  N   GLY A 404     201.955 200.008 258.563  1.00 83.72           N  
ATOM   2450  CA  GLY A 404     201.955 201.316 257.901  1.00 83.24           C  
ATOM   2451  C   GLY A 404     203.104 201.580 256.942  1.00 82.77           C  
ATOM   2452  O   GLY A 404     202.881 202.022 255.814  1.00 83.38           O  
ATOM   2453  N   ASP A 405     204.329 201.299 257.349  1.00 82.89           N  
ATOM   2454  CA  ASP A 405     205.469 201.585 256.479  1.00 83.95           C  
ATOM   2455  C   ASP A 405     205.430 200.840 255.150  1.00 84.02           C  
ATOM   2456  O   ASP A 405     206.096 201.241 254.194  1.00 83.17           O  
ATOM   2457  CB  ASP A 405     206.795 201.265 257.169  1.00 83.99           C  
ATOM   2458  N   GLU A 406     204.696 199.738 255.085  1.00 83.49           N  
ATOM   2459  CA  GLU A 406     204.672 198.938 253.872  1.00 82.91           C  
ATOM   2460  C   GLU A 406     203.412 199.165 253.042  1.00 83.02           C  
ATOM   2461  O   GLU A 406     203.192 198.487 252.041  1.00 82.60           O  
ATOM   2462  CB  GLU A 406     204.880 197.464 254.218  1.00 84.16           C  
ATOM   2463  N   VAL A 407     202.603 200.151 253.421  1.00 82.65           N  
ATOM   2464  CA  VAL A 407     201.400 200.471 252.658  1.00 82.44           C  
ATOM   2465  C   VAL A 407     201.785 200.953 251.271  1.00 82.23           C  
ATOM   2466  O   VAL A 407     201.071 200.712 250.302  1.00 82.04           O  
ATOM   2467  CB  VAL A 407     200.506 201.494 253.386  1.00 82.72           C  
ATOM   2468  CG1 VAL A 407     199.370 201.964 252.471  1.00 81.31           C  
ATOM   2469  CG2 VAL A 407     199.904 200.833 254.631  1.00 82.37           C  
ATOM   2470  N   ARG A 408     202.928 201.618 251.170  1.00 82.34           N  
ATOM   2471  CA  ARG A 408     203.439 202.108 249.898  1.00 82.59           C  
ATOM   2472  C   ARG A 408     203.741 200.986 248.899  1.00 81.79           C  
ATOM   2473  O   ARG A 408     203.910 201.249 247.711  1.00 80.65           O  
ATOM   2474  CB  ARG A 408     204.702 202.919 250.122  1.00 83.08           C  
ATOM   2475  CG  ARG A 408     205.874 202.117 250.666  1.00 82.64           C  
ATOM   2476  CD  ARG A 408     207.067 202.962 250.891  1.00 83.76           C  
ATOM   2477  NE  ARG A 408     207.654 203.403 249.637  1.00 83.24           N  
ATOM   2478  CZ  ARG A 408     208.514 202.675 248.893  1.00 83.03           C  
ATOM   2479  NH1 ARG A 408     208.885 201.474 249.289  1.00 82.23           N  
ATOM   2480  NH2 ARG A 408     208.985 203.169 247.762  1.00 83.23           N  
ATOM   2481  N   GLN A 409     203.826 199.738 249.364  1.00 81.27           N  
ATOM   2482  CA  GLN A 409     204.088 198.629 248.456  1.00 80.83           C  
ATOM   2483  C   GLN A 409     202.814 198.150 247.775  1.00 80.20           C  
ATOM   2484  O   GLN A 409     202.866 197.351 246.837  1.00 78.90           O  
ATOM   2485  CB  GLN A 409     204.744 197.450 249.180  1.00 81.31           C  
ATOM   2486  CG  GLN A 409     206.179 197.670 249.614  1.00 81.86           C  
ATOM   2487  CD  GLN A 409     206.703 196.475 250.410  1.00 83.12           C  
ATOM   2488  OE1 GLN A 409     206.706 195.315 249.954  1.00 82.59           O  
ATOM   2489  NE2 GLN A 409     207.126 196.761 251.630  1.00 82.78           N  
ATOM   2490  N   ILE A 410     201.660 198.632 248.225  1.00 80.35           N  
ATOM   2491  CA  ILE A 410     200.429 198.193 247.598  1.00 79.43           C  
ATOM   2492  C   ILE A 410     200.131 199.132 246.447  1.00 78.70           C  
ATOM   2493  O   ILE A 410     199.360 200.082 246.565  1.00 76.60           O  
ATOM   2494  CB  ILE A 410     199.256 198.175 248.591  1.00 79.40           C  
ATOM   2495  CG1 ILE A 410     199.651 197.398 249.883  1.00 80.43           C  
ATOM   2496  CG2 ILE A 410     198.026 197.559 247.923  1.00 78.84           C  
ATOM   2497  CD1 ILE A 410     200.115 195.967 249.670  1.00 80.98           C  
ATOM   2498  N   ALA A 411     200.782 198.852 245.337  1.00 77.33           N  
ATOM   2499  CA  ALA A 411     200.705 199.656 244.133  1.00 75.26           C  
ATOM   2500  C   ALA A 411     201.296 198.838 242.993  1.00 75.44           C  
ATOM   2501  O   ALA A 411     201.996 197.861 243.256  1.00 76.15           O  
ATOM   2502  CB  ALA A 411     201.443 200.976 244.338  1.00 75.72           C  
ATOM   2503  N   PRO A 412     200.984 199.157 241.739  1.00 75.26           N  
ATOM   2504  CA  PRO A 412     201.629 198.629 240.559  1.00 74.39           C  
ATOM   2505  C   PRO A 412     203.063 199.119 240.511  1.00 74.05           C  
ATOM   2506  O   PRO A 412     203.347 200.227 240.972  1.00 75.68           O  
ATOM   2507  CB  PRO A 412     200.781 199.220 239.428  1.00 73.71           C  
ATOM   2508  CG  PRO A 412     200.122 200.438 240.026  1.00 72.93           C  
ATOM   2509  CD  PRO A 412     199.875 200.074 241.464  1.00 73.85           C  
ATOM   2510  N   GLY A 413     203.960 198.308 239.958  1.00 72.50           N  
ATOM   2511  CA  GLY A 413     205.344 198.709 239.780  1.00 73.32           C  
ATOM   2512  C   GLY A 413     206.181 198.688 241.056  1.00 74.74           C  
ATOM   2513  O   GLY A 413     207.194 199.382 241.139  1.00 74.59           O  
ATOM   2514  N   GLN A 414     205.763 197.932 242.064  1.00 76.07           N  
ATOM   2515  CA  GLN A 414     206.503 197.937 243.320  1.00 76.78           C  
ATOM   2516  C   GLN A 414     207.268 196.657 243.579  1.00 78.05           C  
ATOM   2517  O   GLN A 414     206.916 195.593 243.067  1.00 77.97           O  
ATOM   2518  CB  GLN A 414     205.565 198.202 244.484  1.00 78.13           C  
ATOM   2519  CG  GLN A 414     204.774 199.448 244.318  1.00 77.91           C  
ATOM   2520  CD  GLN A 414     205.632 200.658 244.143  1.00 76.40           C  
ATOM   2521  OE1 GLN A 414     206.498 200.957 244.971  1.00 78.89           O  
ATOM   2522  NE2 GLN A 414     205.408 201.369 243.041  1.00 77.18           N  
ATOM   2523  N   THR A 415     208.288 196.772 244.424  1.00 78.81           N  
ATOM   2524  CA  THR A 415     209.074 195.642 244.911  1.00 80.09           C  
ATOM   2525  C   THR A 415     209.150 195.700 246.427  1.00 80.73           C  
ATOM   2526  O   THR A 415     208.845 196.731 247.028  1.00 80.90           O  
ATOM   2527  CB  THR A 415     210.502 195.654 244.346  1.00 78.70           C  
ATOM   2528  N   GLY A 416     209.579 194.611 247.050  1.00 80.49           N  
ATOM   2529  CA  GLY A 416     209.721 194.597 248.500  1.00 81.75           C  
ATOM   2530  C   GLY A 416     209.149 193.330 249.113  1.00 82.45           C  
ATOM   2531  O   GLY A 416     208.599 192.476 248.420  1.00 82.25           O  
ATOM   2532  N   LYS A 417     209.247 193.211 250.429  1.00 82.23           N  
ATOM   2533  CA  LYS A 417     208.807 191.998 251.104  1.00 82.65           C  
ATOM   2534  C   LYS A 417     207.362 191.653 250.810  1.00 82.42           C  
ATOM   2535  O   LYS A 417     207.012 190.478 250.696  1.00 83.18           O  
ATOM   2536  CB  LYS A 417     208.996 192.127 252.609  1.00 83.18           C  
ATOM   2537  CG  LYS A 417     210.424 192.092 253.042  1.00 83.93           C  
ATOM   2538  CD  LYS A 417     210.546 192.180 254.545  1.00 84.54           C  
ATOM   2539  CE  LYS A 417     211.979 192.081 254.964  1.00 85.96           C  
ATOM   2540  NZ  LYS A 417     212.138 192.303 256.433  1.00 86.21           N  
ATOM   2541  N   ILE A 418     206.516 192.664 250.695  1.00 82.02           N  
ATOM   2542  CA  ILE A 418     205.125 192.394 250.438  1.00 83.31           C  
ATOM   2543  C   ILE A 418     204.882 192.312 248.937  1.00 80.29           C  
ATOM   2544  O   ILE A 418     204.306 191.345 248.436  1.00 81.76           O  
ATOM   2545  CB  ILE A 418     204.228 193.475 251.074  1.00 82.44           C  
ATOM   2546  CG1 ILE A 418     204.476 193.548 252.604  1.00 83.23           C  
ATOM   2547  CG2 ILE A 418     202.757 193.203 250.775  1.00 82.38           C  
ATOM   2548  CD1 ILE A 418     204.145 192.283 253.398  1.00 83.08           C  
ATOM   2549  N   ALA A 419     205.354 193.310 248.204  1.00 83.52           N  
ATOM   2550  CA  ALA A 419     205.077 193.384 246.775  1.00 81.57           C  
ATOM   2551  C   ALA A 419     205.575 192.157 245.997  1.00 81.35           C  
ATOM   2552  O   ALA A 419     204.948 191.757 245.017  1.00 81.86           O  
ATOM   2553  CB  ALA A 419     205.706 194.635 246.194  1.00 81.23           C  
ATOM   2554  N   ASP A 420     206.710 191.573 246.391  1.00 81.52           N  
ATOM   2555  CA  ASP A 420     207.236 190.445 245.630  1.00 81.90           C  
ATOM   2556  C   ASP A 420     206.780 189.069 246.115  1.00 83.26           C  
ATOM   2557  O   ASP A 420     206.599 188.169 245.299  1.00 82.92           O  
ATOM   2558  CB  ASP A 420     208.767 190.468 245.623  1.00 82.70           C  
ATOM   2559  N   TYR A 421     206.621 188.881 247.426  1.00 83.60           N  
ATOM   2560  CA  TYR A 421     206.329 187.541 247.937  1.00 83.64           C  
ATOM   2561  C   TYR A 421     205.016 187.375 248.675  1.00 83.58           C  
ATOM   2562  O   TYR A 421     204.708 186.271 249.121  1.00 83.76           O  
ATOM   2563  CB  TYR A 421     207.432 187.091 248.889  1.00 83.58           C  
ATOM   2564  CG  TYR A 421     208.764 187.089 248.270  1.00 84.23           C  
ATOM   2565  CD1 TYR A 421     209.717 187.975 248.719  1.00 83.83           C  
ATOM   2566  CD2 TYR A 421     209.040 186.221 247.244  1.00 84.01           C  
ATOM   2567  CE1 TYR A 421     210.963 187.984 248.134  1.00 85.48           C  
ATOM   2568  CE2 TYR A 421     210.273 186.220 246.654  1.00 84.52           C  
ATOM   2569  CZ  TYR A 421     211.241 187.098 247.093  1.00 85.11           C  
ATOM   2570  OH  TYR A 421     212.476 187.111 246.495  1.00 87.73           O  
ATOM   2571  N   ASN A 422     204.259 188.441 248.860  1.00 82.81           N  
ATOM   2572  CA  ASN A 422     203.093 188.347 249.709  1.00 82.33           C  
ATOM   2573  C   ASN A 422     201.793 188.774 249.022  1.00 82.72           C  
ATOM   2574  O   ASN A 422     200.802 188.044 249.037  1.00 81.77           O  
ATOM   2575  CB  ASN A 422     203.382 189.157 250.929  1.00 83.19           C  
ATOM   2576  CG  ASN A 422     202.466 189.018 251.908  1.00 82.03           C  
ATOM   2577  OD1 ASN A 422     201.788 189.984 252.174  1.00 82.90           O  
ATOM   2578  ND2 ASN A 422     202.369 187.868 252.493  1.00 83.25           N  
ATOM   2579  N   TYR A 423     201.804 189.962 248.430  1.00 81.96           N  
ATOM   2580  CA  TYR A 423     200.645 190.523 247.739  1.00 81.24           C  
ATOM   2581  C   TYR A 423     201.103 191.422 246.606  1.00 80.82           C  
ATOM   2582  O   TYR A 423     201.742 192.444 246.843  1.00 81.64           O  
ATOM   2583  CB  TYR A 423     199.772 191.339 248.683  1.00 81.53           C  
ATOM   2584  CG  TYR A 423     198.559 191.925 247.996  1.00 80.38           C  
ATOM   2585  CD1 TYR A 423     197.440 191.157 247.813  1.00 80.18           C  
ATOM   2586  CD2 TYR A 423     198.576 193.225 247.545  1.00 79.67           C  
ATOM   2587  CE1 TYR A 423     196.332 191.678 247.195  1.00 78.64           C  
ATOM   2588  CE2 TYR A 423     197.466 193.750 246.927  1.00 78.99           C  
ATOM   2589  CZ  TYR A 423     196.350 192.978 246.756  1.00 78.75           C  
ATOM   2590  OH  TYR A 423     195.243 193.499 246.150  1.00 77.31           O  
ATOM   2591  N   LYS A 424     200.739 191.078 245.383  1.00 80.31           N  
ATOM   2592  CA  LYS A 424     201.231 191.836 244.246  1.00 79.73           C  
ATOM   2593  C   LYS A 424     200.128 192.343 243.338  1.00 79.02           C  
ATOM   2594  O   LYS A 424     199.195 191.608 243.009  1.00 79.21           O  
ATOM   2595  CB  LYS A 424     202.183 190.959 243.434  1.00 79.57           C  
ATOM   2596  CG  LYS A 424     202.876 191.658 242.294  1.00 79.10           C  
ATOM   2597  CD  LYS A 424     203.891 190.741 241.647  1.00 80.20           C  
ATOM   2598  CE  LYS A 424     204.613 191.423 240.502  1.00 80.83           C  
ATOM   2599  NZ  LYS A 424     205.510 192.513 240.984  1.00 79.59           N  
ATOM   2600  N   LEU A 425     200.266 193.584 242.886  1.00 77.54           N  
ATOM   2601  CA  LEU A 425     199.345 194.124 241.896  1.00 76.70           C  
ATOM   2602  C   LEU A 425     200.010 194.140 240.526  1.00 76.56           C  
ATOM   2603  O   LEU A 425     201.217 194.373 240.448  1.00 76.82           O  
ATOM   2604  CB  LEU A 425     198.899 195.544 242.267  1.00 75.04           C  
ATOM   2605  CG  LEU A 425     198.113 195.701 243.565  1.00 76.28           C  
ATOM   2606  CD1 LEU A 425     197.838 197.170 243.788  1.00 75.92           C  
ATOM   2607  CD2 LEU A 425     196.803 194.932 243.473  1.00 76.46           C  
ATOM   2608  N   PRO A 426     199.255 193.945 239.436  1.00 75.31           N  
ATOM   2609  CA  PRO A 426     199.722 194.004 238.066  1.00 74.46           C  
ATOM   2610  C   PRO A 426     200.294 195.374 237.789  1.00 74.24           C  
ATOM   2611  O   PRO A 426     199.777 196.366 238.292  1.00 74.11           O  
ATOM   2612  CB  PRO A 426     198.440 193.810 237.251  1.00 74.22           C  
ATOM   2613  CG  PRO A 426     197.476 193.123 238.169  1.00 75.65           C  
ATOM   2614  CD  PRO A 426     197.822 193.611 239.565  1.00 76.09           C  
ATOM   2615  N   ASP A 427     201.302 195.457 236.937  1.00 73.46           N  
ATOM   2616  CA  ASP A 427     201.880 196.758 236.616  1.00 73.59           C  
ATOM   2617  C   ASP A 427     200.919 197.585 235.765  1.00 73.82           C  
ATOM   2618  O   ASP A 427     201.062 198.802 235.650  1.00 73.72           O  
ATOM   2619  CB  ASP A 427     203.224 196.587 235.918  1.00 72.79           C  
ATOM   2620  N   ASP A 428     199.930 196.913 235.181  1.00 73.27           N  
ATOM   2621  CA  ASP A 428     198.882 197.539 234.391  1.00 73.17           C  
ATOM   2622  C   ASP A 428     197.564 197.582 235.162  1.00 72.98           C  
ATOM   2623  O   ASP A 428     196.484 197.693 234.576  1.00 72.66           O  
ATOM   2624  CB  ASP A 428     198.712 196.805 233.064  1.00 73.42           C  
ATOM   2625  CG  ASP A 428     198.414 195.332 233.249  1.00 74.13           C  
ATOM   2626  OD1 ASP A 428     197.901 194.726 232.337  1.00 74.79           O  
ATOM   2627  OD2 ASP A 428     198.759 194.802 234.289  1.00 73.79           O  
ATOM   2628  N   PHE A 429     197.662 197.510 236.483  1.00 72.93           N  
ATOM   2629  CA  PHE A 429     196.511 197.523 237.365  1.00 72.75           C  
ATOM   2630  C   PHE A 429     195.597 198.715 237.176  1.00 71.65           C  
ATOM   2631  O   PHE A 429     196.039 199.863 237.125  1.00 70.76           O  
ATOM   2632  CB  PHE A 429     197.012 197.518 238.810  1.00 73.41           C  
ATOM   2633  CG  PHE A 429     195.976 197.733 239.857  1.00 73.65           C  
ATOM   2634  CD1 PHE A 429     195.111 196.736 240.228  1.00 73.47           C  
ATOM   2635  CD2 PHE A 429     195.886 198.965 240.491  1.00 71.89           C  
ATOM   2636  CE1 PHE A 429     194.174 196.962 241.207  1.00 73.15           C  
ATOM   2637  CE2 PHE A 429     194.952 199.187 241.466  1.00 71.43           C  
ATOM   2638  CZ  PHE A 429     194.097 198.185 241.822  1.00 72.71           C  
ATOM   2639  N   THR A 430     194.301 198.427 237.103  1.00 71.83           N  
ATOM   2640  CA  THR A 430     193.283 199.458 237.038  1.00 70.07           C  
ATOM   2641  C   THR A 430     192.410 199.287 238.258  1.00 71.16           C  
ATOM   2642  O   THR A 430     191.866 198.208 238.495  1.00 71.74           O  
ATOM   2643  CB  THR A 430     192.425 199.374 235.764  1.00 69.59           C  
ATOM   2644  OG1 THR A 430     193.262 199.509 234.611  1.00 69.84           O  
ATOM   2645  CG2 THR A 430     191.387 200.510 235.750  1.00 68.05           C  
ATOM   2646  N   GLY A 431     192.305 200.336 239.040  1.00 70.30           N  
ATOM   2647  CA  GLY A 431     191.589 200.281 240.293  1.00 70.89           C  
ATOM   2648  C   GLY A 431     192.138 201.340 241.229  1.00 71.64           C  
ATOM   2649  O   GLY A 431     192.962 202.166 240.812  1.00 70.82           O  
ATOM   2650  N   CYS A 432     191.662 201.316 242.483  1.00 71.72           N  
ATOM   2651  CA  CYS A 432     192.052 202.269 243.526  1.00 71.18           C  
ATOM   2652  C   CYS A 432     192.472 201.528 244.798  1.00 72.49           C  
ATOM   2653  O   CYS A 432     191.838 200.545 245.193  1.00 73.70           O  
ATOM   2654  CB  CYS A 432     190.896 203.254 243.842  1.00 72.77           C  
ATOM   2655  SG  CYS A 432     190.300 204.244 242.402  1.00 70.23           S  
ATOM   2656  N   VAL A 433     193.535 202.020 245.447  1.00 71.88           N  
ATOM   2657  CA  VAL A 433     194.054 201.486 246.705  1.00 73.70           C  
ATOM   2658  C   VAL A 433     193.710 202.429 247.843  1.00 75.18           C  
ATOM   2659  O   VAL A 433     194.102 203.598 247.848  1.00 75.80           O  
ATOM   2660  CB  VAL A 433     195.574 201.295 246.625  1.00 73.42           C  
ATOM   2661  CG1 VAL A 433     196.097 200.778 247.955  1.00 75.21           C  
ATOM   2662  CG2 VAL A 433     195.905 200.313 245.497  1.00 73.79           C  
ATOM   2663  N   ILE A 434     192.955 201.920 248.797  1.00 74.02           N  
ATOM   2664  CA  ILE A 434     192.491 202.719 249.912  1.00 74.16           C  
ATOM   2665  C   ILE A 434     192.997 202.133 251.218  1.00 76.86           C  
ATOM   2666  O   ILE A 434     192.881 200.931 251.446  1.00 77.93           O  
ATOM   2667  CB  ILE A 434     190.960 202.769 249.912  1.00 75.71           C  
ATOM   2668  CG1 ILE A 434     190.462 203.360 248.583  1.00 74.91           C  
ATOM   2669  CG2 ILE A 434     190.480 203.614 251.086  1.00 77.63           C  
ATOM   2670  CD1 ILE A 434     188.984 203.161 248.334  1.00 74.85           C  
ATOM   2671  N   ALA A 435     193.563 202.962 252.085  1.00 77.15           N  
ATOM   2672  CA  ALA A 435     194.063 202.422 253.344  1.00 78.54           C  
ATOM   2673  C   ALA A 435     193.894 203.401 254.497  1.00 78.80           C  
ATOM   2674  O   ALA A 435     193.856 204.623 254.307  1.00 78.78           O  
ATOM   2675  CB  ALA A 435     195.522 202.024 253.207  1.00 79.32           C  
ATOM   2676  N   TRP A 436     193.788 202.847 255.705  1.00 79.37           N  
ATOM   2677  CA  TRP A 436     193.668 203.663 256.904  1.00 81.40           C  
ATOM   2678  C   TRP A 436     194.244 202.985 258.133  1.00 82.96           C  
ATOM   2679  O   TRP A 436     194.338 201.759 258.198  1.00 74.75           O  
ATOM   2680  CB  TRP A 436     192.203 204.012 257.127  1.00 78.84           C  
ATOM   2681  CG  TRP A 436     191.297 202.863 257.406  1.00 79.27           C  
ATOM   2682  CD1 TRP A 436     190.829 202.488 258.621  1.00 82.05           C  
ATOM   2683  CD2 TRP A 436     190.738 201.918 256.453  1.00 80.07           C  
ATOM   2684  NE1 TRP A 436     190.007 201.400 258.495  1.00 80.69           N  
ATOM   2685  CE2 TRP A 436     189.946 201.039 257.173  1.00 80.84           C  
ATOM   2686  CE3 TRP A 436     190.845 201.756 255.066  1.00 80.74           C  
ATOM   2687  CZ2 TRP A 436     189.257 200.012 256.561  1.00 80.12           C  
ATOM   2688  CZ3 TRP A 436     190.165 200.727 254.460  1.00 78.00           C  
ATOM   2689  CH2 TRP A 436     189.390 199.881 255.188  1.00 80.06           C  
ATOM   2690  N   ASN A 437     194.619 203.788 259.117  1.00 81.65           N  
ATOM   2691  CA  ASN A 437     195.152 203.272 260.365  1.00 82.97           C  
ATOM   2692  C   ASN A 437     194.075 202.590 261.187  1.00 82.11           C  
ATOM   2693  O   ASN A 437     192.965 203.102 261.322  1.00 82.83           O  
ATOM   2694  CB  ASN A 437     195.817 204.389 261.138  1.00 83.17           C  
ATOM   2695  CG  ASN A 437     194.914 205.568 261.309  1.00 83.07           C  
ATOM   2696  OD1 ASN A 437     194.316 206.043 260.333  1.00 83.19           O  
ATOM   2697  ND2 ASN A 437     194.797 206.061 262.513  1.00 82.59           N  
ATOM   2698  N   SER A 438     194.421 201.443 261.756  1.00 83.06           N  
ATOM   2699  CA  SER A 438     193.513 200.680 262.604  1.00 84.79           C  
ATOM   2700  C   SER A 438     194.130 200.460 263.976  1.00 83.71           C  
ATOM   2701  O   SER A 438     193.773 199.538 264.710  1.00 85.88           O  
ATOM   2702  CB  SER A 438     193.183 199.358 261.955  1.00 84.16           C  
ATOM   2703  OG  SER A 438     194.342 198.615 261.727  1.00 84.26           O  
ATOM   2704  N   ASN A 439     195.065 201.323 264.340  1.00 85.44           N  
ATOM   2705  CA  ASN A 439     195.771 201.179 265.605  1.00 85.55           C  
ATOM   2706  C   ASN A 439     194.827 201.109 266.798  1.00 85.82           C  
ATOM   2707  O   ASN A 439     195.081 200.377 267.752  1.00 86.45           O  
ATOM   2708  CB  ASN A 439     196.744 202.319 265.797  1.00 86.22           C  
ATOM   2709  CG  ASN A 439     197.626 202.098 266.973  1.00 88.08           C  
ATOM   2710  OD1 ASN A 439     198.436 201.165 266.979  1.00 87.08           O  
ATOM   2711  ND2 ASN A 439     197.480 202.926 267.979  1.00 87.86           N  
ATOM   2712  N   ASN A 440     193.725 201.847 266.738  1.00 85.26           N  
ATOM   2713  CA  ASN A 440     192.786 201.903 267.845  1.00 86.15           C  
ATOM   2714  C   ASN A 440     191.677 200.864 267.746  1.00 86.56           C  
ATOM   2715  O   ASN A 440     190.723 200.899 268.524  1.00 85.76           O  
ATOM   2716  CB  ASN A 440     192.180 203.283 267.916  1.00 86.35           C  
ATOM   2717  N   LEU A 441     191.787 199.953 266.791  1.00 85.52           N  
ATOM   2718  CA  LEU A 441     190.783 198.910 266.630  1.00 85.91           C  
ATOM   2719  C   LEU A 441     191.410 197.504 266.624  1.00 86.15           C  
ATOM   2720  O   LEU A 441     190.960 196.628 267.366  1.00 85.49           O  
ATOM   2721  CB  LEU A 441     189.964 199.177 265.357  1.00 85.18           C  
ATOM   2722  CG  LEU A 441     188.702 198.308 265.148  1.00 84.69           C  
ATOM   2723  CD1 LEU A 441     187.680 199.111 264.354  1.00 84.67           C  
ATOM   2724  CD2 LEU A 441     189.056 197.047 264.392  1.00 83.90           C  
ATOM   2725  N   ASP A 442     192.444 197.291 265.784  1.00 84.87           N  
ATOM   2726  CA  ASP A 442     193.134 196.006 265.629  1.00 86.06           C  
ATOM   2727  C   ASP A 442     194.318 195.974 266.590  1.00 85.45           C  
ATOM   2728  O   ASP A 442     194.713 194.919 267.097  1.00 85.87           O  
ATOM   2729  CB  ASP A 442     193.622 195.789 264.166  1.00 85.27           C  
ATOM   2730  N   ASN A 448     198.435 192.070 269.370  1.00 87.60           N  
ATOM   2731  CA  ASN A 448     197.710 191.319 268.356  1.00 86.70           C  
ATOM   2732  C   ASN A 448     198.716 190.733 267.354  1.00 87.42           C  
ATOM   2733  O   ASN A 448     199.236 191.446 266.490  1.00 87.15           O  
ATOM   2734  CB  ASN A 448     196.656 192.198 267.660  1.00 86.54           C  
ATOM   2735  CG  ASN A 448     195.693 191.413 266.686  1.00 86.85           C  
ATOM   2736  OD1 ASN A 448     195.982 190.284 266.222  1.00 86.35           O  
ATOM   2737  ND2 ASN A 448     194.543 192.034 266.388  1.00 86.51           N  
ATOM   2738  N   TYR A 449     198.954 189.421 267.465  1.00 87.14           N  
ATOM   2739  CA  TYR A 449     199.904 188.662 266.648  1.00 86.81           C  
ATOM   2740  C   TYR A 449     199.178 187.717 265.705  1.00 86.35           C  
ATOM   2741  O   TYR A 449     199.734 186.705 265.282  1.00 86.30           O  
ATOM   2742  CB  TYR A 449     200.851 187.885 267.558  1.00 86.99           C  
ATOM   2743  CG  TYR A 449     201.717 188.783 268.414  1.00 87.47           C  
ATOM   2744  CD1 TYR A 449     201.236 189.256 269.628  1.00 87.50           C  
ATOM   2745  CD2 TYR A 449     202.990 189.128 267.995  1.00 87.15           C  
ATOM   2746  CE1 TYR A 449     202.019 190.077 270.408  1.00 88.61           C  
ATOM   2747  CE2 TYR A 449     203.775 189.947 268.784  1.00 88.49           C  
ATOM   2748  CZ  TYR A 449     203.291 190.423 269.982  1.00 88.17           C  
ATOM   2749  OH  TYR A 449     204.069 191.245 270.765  1.00 87.91           O  
ATOM   2750  N   ASN A 450     197.931 188.043 265.369  1.00 86.27           N  
ATOM   2751  CA  ASN A 450     197.136 187.162 264.522  1.00 86.97           C  
ATOM   2752  C   ASN A 450     197.264 187.514 263.047  1.00 86.67           C  
ATOM   2753  O   ASN A 450     196.548 186.968 262.207  1.00 84.61           O  
ATOM   2754  CB  ASN A 450     195.680 187.224 264.931  1.00 86.60           C  
ATOM   2755  CG  ASN A 450     195.451 186.702 266.313  1.00 87.20           C  
ATOM   2756  OD1 ASN A 450     195.459 185.490 266.564  1.00 86.43           O  
ATOM   2757  ND2 ASN A 450     195.252 187.613 267.232  1.00 88.40           N  
ATOM   2758  N   TYR A 451     198.177 188.420 262.723  1.00 86.14           N  
ATOM   2759  CA  TYR A 451     198.377 188.797 261.336  1.00 85.37           C  
ATOM   2760  C   TYR A 451     199.713 188.301 260.820  1.00 84.87           C  
ATOM   2761  O   TYR A 451     200.770 188.778 261.239  1.00 85.39           O  
ATOM   2762  CB  TYR A 451     198.301 190.308 261.167  1.00 84.48           C  
ATOM   2763  CG  TYR A 451     196.991 190.880 261.570  1.00 84.49           C  
ATOM   2764  CD1 TYR A 451     196.895 191.564 262.752  1.00 85.02           C  
ATOM   2765  CD2 TYR A 451     195.878 190.706 260.773  1.00 83.87           C  
ATOM   2766  CE1 TYR A 451     195.701 192.092 263.140  1.00 85.61           C  
ATOM   2767  CE2 TYR A 451     194.670 191.228 261.164  1.00 84.07           C  
ATOM   2768  CZ  TYR A 451     194.584 191.924 262.346  1.00 84.91           C  
ATOM   2769  OH  TYR A 451     193.389 192.450 262.756  1.00 85.54           O  
ATOM   2770  N   LEU A 452     199.663 187.344 259.902  1.00 83.67           N  
ATOM   2771  CA  LEU A 452     200.872 186.788 259.330  1.00 84.59           C  
ATOM   2772  C   LEU A 452     201.163 187.348 257.949  1.00 84.30           C  
ATOM   2773  O   LEU A 452     200.250 187.627 257.161  1.00 84.23           O  
ATOM   2774  CB  LEU A 452     200.791 185.259 259.239  1.00 84.75           C  
ATOM   2775  CG  LEU A 452     200.640 184.466 260.557  1.00 85.27           C  
ATOM   2776  CD1 LEU A 452     200.484 182.991 260.232  1.00 84.24           C  
ATOM   2777  CD2 LEU A 452     201.862 184.672 261.430  1.00 85.65           C  
ATOM   2778  N   TYR A 453     202.451 187.451 257.657  1.00 84.34           N  
ATOM   2779  CA  TYR A 453     202.952 187.890 256.369  1.00 84.07           C  
ATOM   2780  C   TYR A 453     204.144 187.023 256.010  1.00 84.50           C  
ATOM   2781  O   TYR A 453     204.701 186.338 256.865  1.00 84.68           O  
ATOM   2782  CB  TYR A 453     203.289 189.375 256.405  1.00 83.95           C  
ATOM   2783  CG  TYR A 453     204.467 189.754 257.233  1.00 84.78           C  
ATOM   2784  CD1 TYR A 453     205.666 190.044 256.619  1.00 84.90           C  
ATOM   2785  CD2 TYR A 453     204.358 189.812 258.609  1.00 84.70           C  
ATOM   2786  CE1 TYR A 453     206.750 190.410 257.378  1.00 85.01           C  
ATOM   2787  CE2 TYR A 453     205.441 190.170 259.368  1.00 86.80           C  
ATOM   2788  CZ  TYR A 453     206.633 190.470 258.762  1.00 84.54           C  
ATOM   2789  OH  TYR A 453     207.715 190.840 259.526  1.00 85.96           O  
ATOM   2790  N   ARG A 454     204.490 186.986 254.737  1.00 83.42           N  
ATOM   2791  CA  ARG A 454     205.548 186.095 254.294  1.00 83.87           C  
ATOM   2792  C   ARG A 454     206.869 186.789 254.079  1.00 84.98           C  
ATOM   2793  O   ARG A 454     206.928 187.879 253.512  1.00 85.02           O  
ATOM   2794  CB  ARG A 454     205.140 185.408 253.005  1.00 83.79           C  
ATOM   2795  CG  ARG A 454     206.131 184.412 252.477  1.00 85.15           C  
ATOM   2796  CD  ARG A 454     205.542 183.548 251.443  1.00 85.13           C  
ATOM   2797  NE  ARG A 454     204.574 182.576 251.971  1.00 86.22           N  
ATOM   2798  CZ  ARG A 454     203.784 181.826 251.180  1.00 86.21           C  
ATOM   2799  NH1 ARG A 454     202.942 180.942 251.668  1.00 87.72           N  
ATOM   2800  NH2 ARG A 454     203.867 181.975 249.872  1.00 86.99           N  
ATOM   2801  N   LEU A 455     207.935 186.126 254.501  1.00 85.34           N  
ATOM   2802  CA  LEU A 455     209.279 186.606 254.265  1.00 85.37           C  
ATOM   2803  C   LEU A 455     209.952 185.804 253.177  1.00 85.04           C  
ATOM   2804  O   LEU A 455     210.683 186.358 252.352  1.00 85.34           O  
ATOM   2805  CB  LEU A 455     210.143 186.445 255.511  1.00 85.29           C  
ATOM   2806  CG  LEU A 455     210.118 187.535 256.543  1.00 84.85           C  
ATOM   2807  CD1 LEU A 455     208.730 187.694 257.105  1.00 84.57           C  
ATOM   2808  CD2 LEU A 455     211.110 187.156 257.632  1.00 84.80           C  
ATOM   2809  N   PHE A 456     209.723 184.495 253.171  1.00 84.72           N  
ATOM   2810  CA  PHE A 456     210.468 183.668 252.235  1.00 85.59           C  
ATOM   2811  C   PHE A 456     209.594 182.857 251.293  1.00 85.53           C  
ATOM   2812  O   PHE A 456     208.620 182.230 251.702  1.00 85.76           O  
ATOM   2813  CB  PHE A 456     211.377 182.712 253.011  1.00 86.32           C  
ATOM   2814  CG  PHE A 456     212.300 183.429 253.975  1.00 85.80           C  
ATOM   2815  CD1 PHE A 456     213.406 184.117 253.516  1.00 86.01           C  
ATOM   2816  CD2 PHE A 456     212.053 183.416 255.349  1.00 85.52           C  
ATOM   2817  CE1 PHE A 456     214.237 184.780 254.399  1.00 86.08           C  
ATOM   2818  CE2 PHE A 456     212.884 184.074 256.230  1.00 86.17           C  
ATOM   2819  CZ  PHE A 456     213.976 184.759 255.753  1.00 85.60           C  
ATOM   2820  N   ARG A 457     209.991 182.832 250.025  1.00 84.92           N  
ATOM   2821  CA  ARG A 457     209.334 182.035 248.998  1.00 85.16           C  
ATOM   2822  C   ARG A 457     210.391 181.682 247.960  1.00 86.03           C  
ATOM   2823  O   ARG A 457     211.341 182.439 247.759  1.00 86.06           O  
ATOM   2824  CB  ARG A 457     208.177 182.797 248.359  1.00 84.93           C  
ATOM   2825  CG  ARG A 457     207.211 181.975 247.473  1.00 85.21           C  
ATOM   2826  CD  ARG A 457     206.026 182.811 247.058  1.00 84.94           C  
ATOM   2827  NE  ARG A 457     204.957 182.024 246.398  1.00 86.03           N  
ATOM   2828  CZ  ARG A 457     204.838 181.818 245.070  1.00 84.60           C  
ATOM   2829  NH1 ARG A 457     205.726 182.310 244.234  1.00 84.90           N  
ATOM   2830  NH2 ARG A 457     203.808 181.123 244.615  1.00 84.79           N  
ATOM   2831  N   LYS A 458     210.219 180.546 247.299  1.00 85.87           N  
ATOM   2832  CA  LYS A 458     211.154 180.104 246.264  1.00 85.98           C  
ATOM   2833  C   LYS A 458     211.246 181.074 245.092  1.00 85.42           C  
ATOM   2834  O   LYS A 458     212.287 181.168 244.436  1.00 85.52           O  
ATOM   2835  CB  LYS A 458     210.731 178.734 245.751  1.00 86.79           C  
ATOM   2836  N   SER A 459     210.154 181.758 244.802  1.00 85.33           N  
ATOM   2837  CA  SER A 459     210.100 182.700 243.694  1.00 85.63           C  
ATOM   2838  C   SER A 459     209.070 183.776 243.966  1.00 85.23           C  
ATOM   2839  O   SER A 459     208.249 183.647 244.874  1.00 84.99           O  
ATOM   2840  CB  SER A 459     209.769 181.989 242.399  1.00 85.14           C  
ATOM   2841  OG  SER A 459     208.461 181.497 242.413  1.00 85.09           O  
ATOM   2842  N   ASN A 460     209.111 184.839 243.175  1.00 84.66           N  
ATOM   2843  CA  ASN A 460     208.154 185.927 243.294  1.00 84.16           C  
ATOM   2844  C   ASN A 460     206.788 185.427 242.880  1.00 84.08           C  
ATOM   2845  O   ASN A 460     206.684 184.596 241.972  1.00 83.26           O  
ATOM   2846  CB  ASN A 460     208.573 187.100 242.438  1.00 84.39           C  
ATOM   2847  CG  ASN A 460     209.920 187.637 242.818  1.00 83.43           C  
ATOM   2848  OD1 ASN A 460     210.451 187.337 243.886  1.00 83.60           O  
ATOM   2849  ND2 ASN A 460     210.491 188.434 241.961  1.00 84.42           N  
ATOM   2850  N   LEU A 461     205.740 185.920 243.517  1.00 83.51           N  
ATOM   2851  CA  LEU A 461     204.400 185.488 243.141  1.00 83.15           C  
ATOM   2852  C   LEU A 461     203.799 186.355 242.047  1.00 83.18           C  
ATOM   2853  O   LEU A 461     204.273 187.460 241.777  1.00 82.73           O  
ATOM   2854  CB  LEU A 461     203.468 185.386 244.368  1.00 82.54           C  
ATOM   2855  CG  LEU A 461     203.300 186.612 245.301  1.00 83.25           C  
ATOM   2856  CD1 LEU A 461     202.367 187.642 244.720  1.00 82.33           C  
ATOM   2857  CD2 LEU A 461     202.721 186.113 246.600  1.00 82.58           C  
ATOM   2858  N   LYS A 462     202.781 185.819 241.385  1.00 82.40           N  
ATOM   2859  CA  LYS A 462     202.106 186.522 240.308  1.00 81.64           C  
ATOM   2860  C   LYS A 462     201.111 187.534 240.849  1.00 82.21           C  
ATOM   2861  O   LYS A 462     200.696 187.426 242.007  1.00 79.95           O  
ATOM   2862  CB  LYS A 462     201.420 185.519 239.381  1.00 82.19           C  
ATOM   2863  CG  LYS A 462     202.382 184.675 238.580  1.00 82.56           C  
ATOM   2864  CD  LYS A 462     201.659 183.745 237.635  1.00 84.28           C  
ATOM   2865  CE  LYS A 462     202.647 182.933 236.822  1.00 84.37           C  
ATOM   2866  NZ  LYS A 462     201.966 182.044 235.854  1.00 85.10           N  
ATOM   2867  N   PRO A 463     200.738 188.553 240.067  1.00 80.41           N  
ATOM   2868  CA  PRO A 463     199.723 189.519 240.393  1.00 79.69           C  
ATOM   2869  C   PRO A 463     198.436 188.821 240.791  1.00 80.19           C  
ATOM   2870  O   PRO A 463     197.970 187.920 240.098  1.00 79.97           O  
ATOM   2871  CB  PRO A 463     199.585 190.284 239.079  1.00 77.94           C  
ATOM   2872  CG  PRO A 463     200.943 190.188 238.448  1.00 79.19           C  
ATOM   2873  CD  PRO A 463     201.418 188.799 238.775  1.00 81.57           C  
ATOM   2874  N   PHE A 464     197.885 189.251 241.914  1.00 79.28           N  
ATOM   2875  CA  PHE A 464     196.678 188.695 242.509  1.00 78.92           C  
ATOM   2876  C   PHE A 464     196.781 187.216 242.855  1.00 80.03           C  
ATOM   2877  O   PHE A 464     195.756 186.547 243.000  1.00 79.05           O  
ATOM   2878  CB  PHE A 464     195.460 188.923 241.615  1.00 79.47           C  
ATOM   2879  CG  PHE A 464     195.087 190.361 241.479  1.00 78.43           C  
ATOM   2880  CD1 PHE A 464     194.646 191.066 242.584  1.00 77.67           C  
ATOM   2881  CD2 PHE A 464     195.148 191.013 240.264  1.00 78.54           C  
ATOM   2882  CE1 PHE A 464     194.282 192.381 242.482  1.00 76.96           C  
ATOM   2883  CE2 PHE A 464     194.772 192.337 240.167  1.00 77.01           C  
ATOM   2884  CZ  PHE A 464     194.345 193.017 241.277  1.00 76.57           C  
ATOM   2885  N   GLU A 465     197.987 186.708 243.042  1.00 80.31           N  
ATOM   2886  CA  GLU A 465     198.139 185.335 243.500  1.00 80.68           C  
ATOM   2887  C   GLU A 465     198.018 185.277 245.019  1.00 80.97           C  
ATOM   2888  O   GLU A 465     198.597 186.081 245.745  1.00 81.22           O  
ATOM   2889  CB  GLU A 465     199.460 184.722 243.040  1.00 81.70           C  
ATOM   2890  N   ARG A 466     197.248 184.302 245.488  1.00 81.09           N  
ATOM   2891  CA  ARG A 466     197.069 184.074 246.915  1.00 81.88           C  
ATOM   2892  C   ARG A 466     197.540 182.688 247.288  1.00 82.73           C  
ATOM   2893  O   ARG A 466     196.900 181.697 246.927  1.00 83.28           O  
ATOM   2894  CB  ARG A 466     195.612 184.215 247.307  1.00 80.80           C  
ATOM   2895  CG  ARG A 466     195.345 184.080 248.788  1.00 81.00           C  
ATOM   2896  CD  ARG A 466     193.960 184.451 249.114  1.00 80.05           C  
ATOM   2897  NE  ARG A 466     192.989 183.567 248.485  1.00 79.85           N  
ATOM   2898  CZ  ARG A 466     191.651 183.769 248.475  1.00 78.55           C  
ATOM   2899  NH1 ARG A 466     191.128 184.823 249.071  1.00 77.72           N  
ATOM   2900  NH2 ARG A 466     190.861 182.897 247.858  1.00 78.96           N  
ATOM   2901  N   ASP A 467     198.667 182.595 247.975  1.00 84.71           N  
ATOM   2902  CA  ASP A 467     199.201 181.287 248.304  1.00 85.94           C  
ATOM   2903  C   ASP A 467     198.662 180.833 249.660  1.00 86.74           C  
ATOM   2904  O   ASP A 467     197.991 181.585 250.351  1.00 85.28           O  
ATOM   2905  CB  ASP A 467     200.726 181.371 248.339  1.00 86.83           C  
ATOM   2906  CG  ASP A 467     201.456 180.052 248.119  1.00 87.20           C  
ATOM   2907  OD1 ASP A 467     202.658 180.102 247.956  1.00 87.59           O  
ATOM   2908  OD2 ASP A 467     200.835 179.020 248.152  1.00 87.82           O  
ATOM   2909  N   ILE A 468     199.030 179.616 250.051  1.00 87.29           N  
ATOM   2910  CA  ILE A 468     198.701 179.066 251.355  1.00 87.69           C  
ATOM   2911  C   ILE A 468     199.756 178.024 251.749  1.00 88.65           C  
ATOM   2912  O   ILE A 468     199.529 176.835 251.564  1.00 88.80           O  
ATOM   2913  CB  ILE A 468     197.296 178.384 251.395  1.00 88.09           C  
ATOM   2914  CG1 ILE A 468     196.137 179.374 251.013  1.00 88.61           C  
ATOM   2915  CG2 ILE A 468     197.046 177.853 252.808  1.00 88.27           C  
ATOM   2916  CD1 ILE A 468     194.782 178.724 250.858  1.00 89.38           C  
ATOM   2917  N   SER A 469     200.890 178.457 252.293  1.00 87.86           N  
ATOM   2918  CA  SER A 469     201.917 177.479 252.716  1.00 89.07           C  
ATOM   2919  C   SER A 469     202.579 177.888 254.028  1.00 89.15           C  
ATOM   2920  O   SER A 469     202.773 179.078 254.288  1.00 87.68           O  
ATOM   2921  CB  SER A 469     202.972 177.287 251.634  1.00 88.94           C  
ATOM   2922  OG  SER A 469     202.434 176.736 250.466  1.00 88.81           O  
ATOM   2923  N   THR A 470     202.964 176.875 254.833  1.00 89.25           N  
ATOM   2924  CA  THR A 470     203.640 177.039 256.124  1.00 88.96           C  
ATOM   2925  C   THR A 470     204.989 176.310 256.122  1.00 88.53           C  
ATOM   2926  O   THR A 470     205.646 176.165 255.083  1.00 87.67           O  
ATOM   2927  CB  THR A 470     202.737 176.525 257.294  1.00 89.73           C  
ATOM   2928  OG1 THR A 470     202.357 175.152 257.063  1.00 88.96           O  
ATOM   2929  CG2 THR A 470     201.455 177.413 257.484  1.00 88.44           C  
ATOM   2930  N   PHE A 490     209.785 177.582 258.319  1.00 87.03           N  
ATOM   2931  CA  PHE A 490     208.518 178.294 258.432  1.00 86.44           C  
ATOM   2932  C   PHE A 490     208.718 179.729 257.854  1.00 86.77           C  
ATOM   2933  O   PHE A 490     209.357 180.554 258.515  1.00 86.37           O  
ATOM   2934  CB  PHE A 490     208.059 178.328 259.909  1.00 87.10           C  
ATOM   2935  CG  PHE A 490     206.613 178.841 260.163  1.00 87.02           C  
ATOM   2936  CD1 PHE A 490     205.462 177.971 259.939  1.00 88.44           C  
ATOM   2937  CD2 PHE A 490     206.365 180.188 260.657  1.00 87.17           C  
ATOM   2938  CE1 PHE A 490     204.123 178.439 260.203  1.00 89.06           C  
ATOM   2939  CE2 PHE A 490     205.025 180.646 260.921  1.00 87.49           C  
ATOM   2940  CZ  PHE A 490     203.908 179.771 260.693  1.00 87.76           C  
ATOM   2941  N   PRO A 491     208.201 180.059 256.629  1.00 86.84           N  
ATOM   2942  CA  PRO A 491     208.406 181.311 255.901  1.00 85.93           C  
ATOM   2943  C   PRO A 491     207.519 182.466 256.356  1.00 86.25           C  
ATOM   2944  O   PRO A 491     207.633 183.578 255.824  1.00 85.17           O  
ATOM   2945  CB  PRO A 491     208.056 180.909 254.470  1.00 86.92           C  
ATOM   2946  CG  PRO A 491     206.964 179.888 254.617  1.00 87.09           C  
ATOM   2947  CD  PRO A 491     207.300 179.116 255.883  1.00 87.15           C  
ATOM   2948  N   LEU A 492     206.610 182.193 257.291  1.00 85.85           N  
ATOM   2949  CA  LEU A 492     205.656 183.199 257.761  1.00 86.06           C  
ATOM   2950  C   LEU A 492     206.069 183.776 259.099  1.00 86.15           C  
ATOM   2951  O   LEU A 492     206.635 183.091 259.945  1.00 86.72           O  
ATOM   2952  CB  LEU A 492     204.245 182.605 257.892  1.00 85.22           C  
ATOM   2953  CG  LEU A 492     203.580 182.062 256.610  1.00 85.74           C  
ATOM   2954  CD1 LEU A 492     202.262 181.401 256.979  1.00 85.96           C  
ATOM   2955  CD2 LEU A 492     203.338 183.205 255.611  1.00 85.61           C  
ATOM   2956  N   GLN A 493     205.769 185.049 259.291  1.00 85.16           N  
ATOM   2957  CA  GLN A 493     206.053 185.736 260.541  1.00 85.59           C  
ATOM   2958  C   GLN A 493     204.870 186.592 260.929  1.00 86.26           C  
ATOM   2959  O   GLN A 493     204.042 186.938 260.086  1.00 84.15           O  
ATOM   2960  CB  GLN A 493     207.312 186.588 260.439  1.00 85.26           C  
ATOM   2961  CG  GLN A 493     208.563 185.804 260.055  1.00 85.11           C  
ATOM   2962  CD  GLN A 493     209.012 184.841 261.119  1.00 86.87           C  
ATOM   2963  OE1 GLN A 493     208.763 185.052 262.308  1.00 85.92           O  
ATOM   2964  NE2 GLN A 493     209.670 183.763 260.706  1.00 85.82           N  
ATOM   2965  N   SER A 494     204.757 186.903 262.206  1.00 85.68           N  
ATOM   2966  CA  SER A 494     203.669 187.749 262.655  1.00 85.69           C  
ATOM   2967  C   SER A 494     204.095 189.192 262.737  1.00 85.63           C  
ATOM   2968  O   SER A 494     205.265 189.492 262.984  1.00 85.83           O  
ATOM   2969  CB  SER A 494     203.188 187.277 264.008  1.00 85.88           C  
ATOM   2970  OG  SER A 494     204.217 187.371 264.955  1.00 86.79           O  
ATOM   2971  N   TYR A 495     203.127 190.083 262.605  1.00 86.11           N  
ATOM   2972  CA  TYR A 495     203.377 191.487 262.858  1.00 86.36           C  
ATOM   2973  C   TYR A 495     203.183 191.764 264.332  1.00 87.33           C  
ATOM   2974  O   TYR A 495     202.124 191.476 264.886  1.00 86.16           O  
ATOM   2975  CB  TYR A 495     202.414 192.383 262.100  1.00 86.20           C  
ATOM   2976  CG  TYR A 495     202.577 192.484 260.609  1.00 85.70           C  
ATOM   2977  CD1 TYR A 495     201.635 191.908 259.777  1.00 84.97           C  
ATOM   2978  CD2 TYR A 495     203.647 193.173 260.074  1.00 84.94           C  
ATOM   2979  CE1 TYR A 495     201.760 192.027 258.417  1.00 84.98           C  
ATOM   2980  CE2 TYR A 495     203.777 193.283 258.708  1.00 84.90           C  
ATOM   2981  CZ  TYR A 495     202.839 192.719 257.886  1.00 84.87           C  
ATOM   2982  OH  TYR A 495     202.975 192.825 256.531  1.00 84.67           O  
ATOM   2983  N   GLY A 496     204.177 192.366 264.965  1.00 86.59           N  
ATOM   2984  CA  GLY A 496     204.080 192.664 266.388  1.00 86.75           C  
ATOM   2985  C   GLY A 496     203.268 193.923 266.636  1.00 88.31           C  
ATOM   2986  O   GLY A 496     203.810 194.939 267.079  1.00 88.22           O  
ATOM   2987  N   PHE A 497     201.976 193.860 266.327  1.00 87.36           N  
ATOM   2988  CA  PHE A 497     201.108 195.019 266.459  1.00 87.77           C  
ATOM   2989  C   PHE A 497     200.619 195.229 267.880  1.00 88.70           C  
ATOM   2990  O   PHE A 497     200.065 194.331 268.516  1.00 87.79           O  
ATOM   2991  CB  PHE A 497     199.888 194.905 265.542  1.00 87.30           C  
ATOM   2992  CG  PHE A 497     200.168 195.046 264.071  1.00 87.41           C  
ATOM   2993  CD1 PHE A 497     199.584 194.175 263.184  1.00 86.59           C  
ATOM   2994  CD2 PHE A 497     200.995 196.039 263.573  1.00 85.89           C  
ATOM   2995  CE1 PHE A 497     199.806 194.283 261.835  1.00 86.41           C  
ATOM   2996  CE2 PHE A 497     201.225 196.148 262.232  1.00 85.73           C  
ATOM   2997  CZ  PHE A 497     200.628 195.268 261.358  1.00 85.63           C  
ATOM   2998  N   GLN A 498     200.802 196.449 268.356  1.00 88.92           N  
ATOM   2999  CA  GLN A 498     200.349 196.883 269.663  1.00 90.68           C  
ATOM   3000  C   GLN A 498     199.773 198.285 269.506  1.00 89.69           C  
ATOM   3001  O   GLN A 498     200.252 199.041 268.661  1.00 88.92           O  
ATOM   3002  CB  GLN A 498     201.514 196.880 270.671  1.00 89.09           C  
ATOM   3003  CG  GLN A 498     202.078 195.503 270.988  1.00 89.71           C  
ATOM   3004  CD  GLN A 498     201.134 194.687 271.851  1.00 89.14           C  
ATOM   3005  OE1 GLN A 498     200.504 195.217 272.772  1.00 89.21           O  
ATOM   3006  NE2 GLN A 498     201.028 193.403 271.558  1.00 88.87           N  
ATOM   3007  N   PRO A 499     198.782 198.676 270.317  1.00 91.39           N  
ATOM   3008  CA  PRO A 499     198.165 199.995 270.338  1.00 89.61           C  
ATOM   3009  C   PRO A 499     199.175 201.057 270.753  1.00 90.27           C  
ATOM   3010  O   PRO A 499     198.976 202.253 270.534  1.00 90.41           O  
ATOM   3011  CB  PRO A 499     197.028 199.821 271.357  1.00 89.64           C  
ATOM   3012  CG  PRO A 499     197.452 198.650 272.224  1.00 89.48           C  
ATOM   3013  CD  PRO A 499     198.218 197.728 271.295  1.00 89.52           C  
ATOM   3014  N   THR A 500     200.281 200.602 271.329  1.00 89.26           N  
ATOM   3015  CA  THR A 500     201.352 201.470 271.783  1.00 90.07           C  
ATOM   3016  C   THR A 500     202.412 201.790 270.708  1.00 89.82           C  
ATOM   3017  O   THR A 500     203.323 202.577 270.976  1.00 88.69           O  
ATOM   3018  CB  THR A 500     202.055 200.834 272.991  1.00 89.48           C  
ATOM   3019  OG1 THR A 500     202.649 199.590 272.596  1.00 91.14           O  
ATOM   3020  CG2 THR A 500     201.039 200.571 274.095  1.00 90.46           C  
ATOM   3021  N   ASN A 501     202.312 201.182 269.500  1.00 89.33           N  
ATOM   3022  CA  ASN A 501     203.268 201.404 268.412  1.00 89.76           C  
ATOM   3023  C   ASN A 501     203.032 202.787 267.807  1.00 88.90           C  
ATOM   3024  O   ASN A 501     203.836 203.288 267.017  1.00 87.94           O  
ATOM   3025  CB  ASN A 501     203.174 200.317 267.323  1.00 88.58           C  
ATOM   3026  CG  ASN A 501     203.633 198.880 267.760  1.00 89.53           C  
ATOM   3027  OD1 ASN A 501     204.162 198.661 268.863  1.00 89.11           O  
ATOM   3028  ND2 ASN A 501     203.443 197.910 266.855  1.00 88.16           N  
ATOM   3029  N   VAL A 503     204.541 205.151 264.400  1.00 87.88           N  
ATOM   3030  CA  VAL A 503     203.416 205.213 263.464  1.00 86.32           C  
ATOM   3031  C   VAL A 503     203.574 204.147 262.363  1.00 86.39           C  
ATOM   3032  O   VAL A 503     202.598 203.500 261.977  1.00 85.90           O  
ATOM   3033  CB  VAL A 503     203.263 206.662 262.850  1.00 87.78           C  
ATOM   3034  CG1 VAL A 503     202.111 206.715 261.749  1.00 86.98           C  
ATOM   3035  CG2 VAL A 503     202.932 207.702 263.995  1.00 86.89           C  
ATOM   3036  N   GLY A 504     204.808 203.954 261.866  1.00 85.97           N  
ATOM   3037  CA  GLY A 504     205.129 203.011 260.786  1.00 85.13           C  
ATOM   3038  C   GLY A 504     204.886 201.558 261.183  1.00 86.19           C  
ATOM   3039  O   GLY A 504     204.785 200.667 260.334  1.00 85.58           O  
ATOM   3040  N   TYR A 505     204.769 201.328 262.484  1.00 85.48           N  
ATOM   3041  CA  TYR A 505     204.533 199.998 263.010  1.00 85.46           C  
ATOM   3042  C   TYR A 505     203.088 199.809 263.433  1.00 86.28           C  
ATOM   3043  O   TYR A 505     202.736 198.784 264.019  1.00 86.60           O  
ATOM   3044  CB  TYR A 505     205.470 199.732 264.177  1.00 86.75           C  
ATOM   3045  N   GLN A 506     202.241 200.786 263.148  1.00 84.97           N  
ATOM   3046  CA  GLN A 506     200.836 200.635 263.461  1.00 86.49           C  
ATOM   3047  C   GLN A 506     200.217 199.836 262.330  1.00 85.35           C  
ATOM   3048  O   GLN A 506     200.712 199.898 261.204  1.00 84.91           O  
ATOM   3049  CB  GLN A 506     200.163 201.998 263.615  1.00 85.38           C  
ATOM   3050  CG  GLN A 506     200.637 202.778 264.827  1.00 86.22           C  
ATOM   3051  CD  GLN A 506     199.946 204.117 264.962  1.00 86.77           C  
ATOM   3052  OE1 GLN A 506     199.003 204.415 264.228  1.00 86.64           O  
ATOM   3053  NE2 GLN A 506     200.405 204.933 265.902  1.00 87.41           N  
ATOM   3054  N   PRO A 507     199.183 199.038 262.593  1.00 84.87           N  
ATOM   3055  CA  PRO A 507     198.452 198.292 261.601  1.00 84.63           C  
ATOM   3056  C   PRO A 507     197.629 199.212 260.732  1.00 84.89           C  
ATOM   3057  O   PRO A 507     197.024 200.166 261.227  1.00 82.80           O  
ATOM   3058  CB  PRO A 507     197.569 197.376 262.451  1.00 84.65           C  
ATOM   3059  CG  PRO A 507     197.399 198.109 263.761  1.00 86.17           C  
ATOM   3060  CD  PRO A 507     198.702 198.871 263.966  1.00 86.66           C  
ATOM   3061  N   TYR A 508     197.562 198.877 259.454  1.00 84.88           N  
ATOM   3062  CA  TYR A 508     196.704 199.543 258.499  1.00 82.98           C  
ATOM   3063  C   TYR A 508     195.812 198.564 257.782  1.00 82.31           C  
ATOM   3064  O   TYR A 508     196.239 197.485 257.353  1.00 82.49           O  
ATOM   3065  CB  TYR A 508     197.517 200.347 257.488  1.00 81.48           C  
ATOM   3066  CG  TYR A 508     197.976 201.685 257.985  1.00 82.01           C  
ATOM   3067  CD1 TYR A 508     198.921 201.802 258.974  1.00 84.14           C  
ATOM   3068  CD2 TYR A 508     197.444 202.816 257.408  1.00 81.63           C  
ATOM   3069  CE1 TYR A 508     199.328 203.044 259.394  1.00 83.98           C  
ATOM   3070  CE2 TYR A 508     197.846 204.054 257.822  1.00 83.23           C  
ATOM   3071  CZ  TYR A 508     198.785 204.173 258.810  1.00 83.21           C  
ATOM   3072  OH  TYR A 508     199.192 205.418 259.222  1.00 81.53           O  
ATOM   3073  N   ARG A 509     194.574 198.967 257.618  1.00 79.59           N  
ATOM   3074  CA  ARG A 509     193.620 198.189 256.873  1.00 83.84           C  
ATOM   3075  C   ARG A 509     193.645 198.645 255.441  1.00 80.06           C  
ATOM   3076  O   ARG A 509     193.496 199.829 255.147  1.00 80.23           O  
ATOM   3077  CB  ARG A 509     192.239 198.312 257.472  1.00 81.63           C  
ATOM   3078  CG  ARG A 509     192.045 197.513 258.737  1.00 81.10           C  
ATOM   3079  CD  ARG A 509     190.697 197.667 259.286  1.00 81.84           C  
ATOM   3080  NE  ARG A 509     190.440 196.693 260.334  1.00 82.27           N  
ATOM   3081  CZ  ARG A 509     189.211 196.298 260.729  1.00 83.09           C  
ATOM   3082  NH1 ARG A 509     188.143 196.822 260.163  1.00 82.13           N  
ATOM   3083  NH2 ARG A 509     189.089 195.386 261.681  1.00 82.86           N  
ATOM   3084  N   VAL A 510     193.898 197.706 254.549  1.00 80.24           N  
ATOM   3085  CA  VAL A 510     194.030 198.021 253.146  1.00 79.02           C  
ATOM   3086  C   VAL A 510     192.964 197.331 252.327  1.00 79.89           C  
ATOM   3087  O   VAL A 510     192.755 196.121 252.441  1.00 76.10           O  
ATOM   3088  CB  VAL A 510     195.410 197.596 252.633  1.00 79.19           C  
ATOM   3089  CG1 VAL A 510     195.546 197.926 251.159  1.00 78.12           C  
ATOM   3090  CG2 VAL A 510     196.499 198.277 253.434  1.00 80.78           C  
ATOM   3091  N   VAL A 511     192.277 198.112 251.509  1.00 76.95           N  
ATOM   3092  CA  VAL A 511     191.305 197.572 250.589  1.00 76.12           C  
ATOM   3093  C   VAL A 511     191.656 197.994 249.177  1.00 76.28           C  
ATOM   3094  O   VAL A 511     191.764 199.185 248.884  1.00 76.04           O  
ATOM   3095  CB  VAL A 511     189.881 198.042 250.928  1.00 76.85           C  
ATOM   3096  CG1 VAL A 511     188.893 197.473 249.912  1.00 76.13           C  
ATOM   3097  CG2 VAL A 511     189.516 197.583 252.326  1.00 78.37           C  
ATOM   3098  N   VAL A 512     191.822 197.027 248.297  1.00 75.28           N  
ATOM   3099  CA  VAL A 512     192.131 197.349 246.919  1.00 74.46           C  
ATOM   3100  C   VAL A 512     190.928 197.066 246.048  1.00 74.81           C  
ATOM   3101  O   VAL A 512     190.435 195.943 246.006  1.00 74.01           O  
ATOM   3102  CB  VAL A 512     193.339 196.537 246.426  1.00 75.70           C  
ATOM   3103  CG1 VAL A 512     193.629 196.872 244.979  1.00 73.67           C  
ATOM   3104  CG2 VAL A 512     194.536 196.830 247.311  1.00 75.45           C  
ATOM   3105  N   LEU A 513     190.448 198.085 245.356  1.00 73.09           N  
ATOM   3106  CA  LEU A 513     189.300 197.914 244.489  1.00 72.11           C  
ATOM   3107  C   LEU A 513     189.763 197.777 243.053  1.00 72.86           C  
ATOM   3108  O   LEU A 513     190.176 198.751 242.423  1.00 71.43           O  
ATOM   3109  CB  LEU A 513     188.330 199.097 244.623  1.00 72.78           C  
ATOM   3110  CG  LEU A 513     187.759 199.367 246.036  1.00 73.24           C  
ATOM   3111  CD1 LEU A 513     186.817 200.556 245.967  1.00 72.73           C  
ATOM   3112  CD2 LEU A 513     187.026 198.135 246.551  1.00 74.38           C  
ATOM   3113  N   SER A 514     189.707 196.549 242.554  1.00 71.83           N  
ATOM   3114  CA  SER A 514     190.155 196.205 241.213  1.00 70.57           C  
ATOM   3115  C   SER A 514     189.001 196.266 240.246  1.00 71.35           C  
ATOM   3116  O   SER A 514     187.960 195.639 240.458  1.00 71.77           O  
ATOM   3117  CB  SER A 514     190.772 194.825 241.212  1.00 73.31           C  
ATOM   3118  OG  SER A 514     191.071 194.402 239.918  1.00 72.81           O  
ATOM   3119  N   PHE A 515     189.153 197.048 239.194  1.00 70.85           N  
ATOM   3120  CA  PHE A 515     188.069 197.272 238.247  1.00 70.55           C  
ATOM   3121  C   PHE A 515     188.288 196.530 236.944  1.00 71.06           C  
ATOM   3122  O   PHE A 515     189.318 196.713 236.284  1.00 70.47           O  
ATOM   3123  CB  PHE A 515     187.980 198.768 237.940  1.00 70.04           C  
ATOM   3124  CG  PHE A 515     187.664 199.644 239.133  1.00 69.90           C  
ATOM   3125  CD1 PHE A 515     186.896 199.200 240.171  1.00 70.80           C  
ATOM   3126  CD2 PHE A 515     188.158 200.932 239.209  1.00 69.54           C  
ATOM   3127  CE1 PHE A 515     186.622 199.995 241.256  1.00 71.01           C  
ATOM   3128  CE2 PHE A 515     187.892 201.723 240.299  1.00 70.28           C  
ATOM   3129  CZ  PHE A 515     187.121 201.257 241.321  1.00 70.66           C  
ATOM   3130  N   GLU A 516     187.308 195.736 236.530  1.00 70.50           N  
ATOM   3131  CA  GLU A 516     187.434 195.078 235.251  1.00 70.26           C  
ATOM   3132  C   GLU A 516     186.690 195.886 234.185  1.00 70.49           C  
ATOM   3133  O   GLU A 516     185.491 196.133 234.281  1.00 70.21           O  
ATOM   3134  CB  GLU A 516     186.950 193.629 235.299  1.00 70.41           C  
ATOM   3135  CG  GLU A 516     187.179 192.898 233.997  1.00 70.54           C  
ATOM   3136  CD  GLU A 516     186.899 191.436 234.018  1.00 71.09           C  
ATOM   3137  OE1 GLU A 516     185.919 191.013 234.572  1.00 71.81           O  
ATOM   3138  OE2 GLU A 516     187.713 190.726 233.507  1.00 71.43           O  
ATOM   3139  N   LEU A 517     187.443 196.310 233.188  1.00 70.18           N  
ATOM   3140  CA  LEU A 517     186.943 197.141 232.097  1.00 70.11           C  
ATOM   3141  C   LEU A 517     186.851 196.333 230.813  1.00 70.82           C  
ATOM   3142  O   LEU A 517     186.901 196.864 229.710  1.00 69.34           O  
ATOM   3143  CB  LEU A 517     187.878 198.351 231.879  1.00 69.08           C  
ATOM   3144  CG  LEU A 517     187.703 199.597 232.817  1.00 68.87           C  
ATOM   3145  CD1 LEU A 517     186.219 200.058 232.792  1.00 68.91           C  
ATOM   3146  CD2 LEU A 517     188.157 199.236 234.240  1.00 70.40           C  
ATOM   3147  N   LEU A 518     186.705 195.027 230.974  1.00 69.85           N  
ATOM   3148  CA  LEU A 518     186.496 194.144 229.849  1.00 69.75           C  
ATOM   3149  C   LEU A 518     185.009 194.032 229.691  1.00 69.30           C  
ATOM   3150  O   LEU A 518     184.351 193.289 230.428  1.00 68.17           O  
ATOM   3151  CB  LEU A 518     187.137 192.765 230.100  1.00 70.61           C  
ATOM   3152  N   HIS A 519     184.461 194.798 228.773  1.00 69.21           N  
ATOM   3153  CA  HIS A 519     183.034 194.881 228.747  1.00 69.82           C  
ATOM   3154  C   HIS A 519     182.316 193.657 228.210  1.00 68.00           C  
ATOM   3155  O   HIS A 519     182.726 192.993 227.252  1.00 67.82           O  
ATOM   3156  CB  HIS A 519     182.567 196.162 228.075  1.00 67.83           C  
ATOM   3157  N   ALA A 520     181.235 193.422 228.889  1.00 67.46           N  
ATOM   3158  CA  ALA A 520     180.237 192.384 228.789  1.00 66.68           C  
ATOM   3159  C   ALA A 520     179.079 193.130 229.428  1.00 66.19           C  
ATOM   3160  O   ALA A 520     179.279 194.319 229.697  1.00 65.39           O  
ATOM   3161  CB  ALA A 520     180.723 191.105 229.466  1.00 65.73           C  
ATOM   3162  N   PRO A 521     177.894 192.589 229.680  1.00 65.59           N  
ATOM   3163  CA  PRO A 521     176.824 193.437 230.137  1.00 65.71           C  
ATOM   3164  C   PRO A 521     177.268 194.113 231.409  1.00 67.56           C  
ATOM   3165  O   PRO A 521     177.793 193.470 232.322  1.00 67.11           O  
ATOM   3166  CB  PRO A 521     175.655 192.478 230.289  1.00 66.24           C  
ATOM   3167  CG  PRO A 521     176.288 191.065 230.345  1.00 65.63           C  
ATOM   3168  CD  PRO A 521     177.643 191.166 229.691  1.00 65.72           C  
ATOM   3169  N   ALA A 522     177.076 195.421 231.446  1.00 66.80           N  
ATOM   3170  CA  ALA A 522     177.539 196.244 232.550  1.00 67.22           C  
ATOM   3171  C   ALA A 522     176.857 195.822 233.821  1.00 68.15           C  
ATOM   3172  O   ALA A 522     175.662 195.542 233.817  1.00 67.44           O  
ATOM   3173  CB  ALA A 522     177.277 197.689 232.223  1.00 66.71           C  
ATOM   3174  N   THR A 523     177.618 195.753 234.912  1.00 67.25           N  
ATOM   3175  CA  THR A 523     177.058 195.262 236.157  1.00 69.04           C  
ATOM   3176  C   THR A 523     177.148 196.228 237.337  1.00 69.28           C  
ATOM   3177  O   THR A 523     176.230 196.286 238.161  1.00 70.18           O  
ATOM   3178  CB  THR A 523     177.742 193.934 236.505  1.00 69.50           C  
ATOM   3179  OG1 THR A 523     177.514 193.015 235.441  1.00 69.30           O  
ATOM   3180  CG2 THR A 523     177.193 193.370 237.755  1.00 70.50           C  
ATOM   3181  N   VAL A 524     178.261 196.940 237.462  1.00 67.79           N  
ATOM   3182  CA  VAL A 524     178.464 197.815 238.603  1.00 67.26           C  
ATOM   3183  C   VAL A 524     178.624 199.263 238.156  1.00 69.15           C  
ATOM   3184  O   VAL A 524     179.728 199.673 237.779  1.00 69.54           O  
ATOM   3185  CB  VAL A 524     179.730 197.393 239.369  1.00 69.09           C  
ATOM   3186  CG1 VAL A 524     179.941 198.279 240.583  1.00 69.65           C  
ATOM   3187  CG2 VAL A 524     179.618 195.941 239.784  1.00 69.39           C  
ATOM   3188  N   CYS A 525     177.527 200.033 238.198  1.00 68.02           N  
ATOM   3189  CA  CYS A 525     177.471 201.400 237.681  1.00 67.82           C  
ATOM   3190  C   CYS A 525     177.403 202.391 238.836  1.00 67.71           C  
ATOM   3191  O   CYS A 525     176.960 202.031 239.929  1.00 69.28           O  
ATOM   3192  CB  CYS A 525     176.253 201.580 236.741  1.00 68.26           C  
ATOM   3193  SG  CYS A 525     176.268 200.536 235.220  1.00 64.84           S  
ATOM   3194  N   GLY A 526     177.838 203.639 238.596  1.00 66.57           N  
ATOM   3195  CA  GLY A 526     177.791 204.704 239.604  1.00 67.14           C  
ATOM   3196  C   GLY A 526     176.374 205.264 239.776  1.00 68.20           C  
ATOM   3197  O   GLY A 526     175.449 204.875 239.059  1.00 67.14           O  
ATOM   3198  N   PRO A 527     176.206 206.220 240.697  1.00 66.91           N  
ATOM   3199  CA  PRO A 527     174.974 206.852 241.118  1.00 68.15           C  
ATOM   3200  C   PRO A 527     174.517 207.916 240.142  1.00 67.46           C  
ATOM   3201  O   PRO A 527     174.468 209.099 240.479  1.00 67.37           O  
ATOM   3202  CB  PRO A 527     175.381 207.467 242.453  1.00 69.70           C  
ATOM   3203  CG  PRO A 527     176.825 207.832 242.247  1.00 68.60           C  
ATOM   3204  CD  PRO A 527     177.383 206.727 241.370  1.00 67.83           C  
ATOM   3205  N   LYS A 528     174.205 207.501 238.932  1.00 67.21           N  
ATOM   3206  CA  LYS A 528     173.773 208.434 237.908  1.00 66.54           C  
ATOM   3207  C   LYS A 528     172.337 208.184 237.524  1.00 66.14           C  
ATOM   3208  O   LYS A 528     171.877 207.044 237.502  1.00 67.12           O  
ATOM   3209  CB  LYS A 528     174.673 208.329 236.687  1.00 66.23           C  
ATOM   3210  N   LYS A 529     171.624 209.257 237.226  1.00 66.90           N  
ATOM   3211  CA  LYS A 529     170.246 209.133 236.797  1.00 66.52           C  
ATOM   3212  C   LYS A 529     170.167 208.929 235.302  1.00 65.87           C  
ATOM   3213  O   LYS A 529     170.772 209.676 234.533  1.00 65.45           O  
ATOM   3214  CB  LYS A 529     169.440 210.367 237.187  1.00 67.36           C  
ATOM   3215  CG  LYS A 529     169.242 210.550 238.680  1.00 68.21           C  
ATOM   3216  CD  LYS A 529     168.359 211.761 238.969  1.00 69.68           C  
ATOM   3217  CE  LYS A 529     168.144 211.954 240.464  1.00 71.56           C  
ATOM   3218  NZ  LYS A 529     167.299 213.148 240.755  1.00 72.64           N  
ATOM   3219  N   SER A 530     169.413 207.926 234.896  1.00 66.07           N  
ATOM   3220  CA  SER A 530     169.213 207.669 233.491  1.00 65.07           C  
ATOM   3221  C   SER A 530     168.178 208.619 232.937  1.00 64.99           C  
ATOM   3222  O   SER A 530     167.345 209.148 233.675  1.00 65.48           O  
ATOM   3223  CB  SER A 530     168.742 206.254 233.286  1.00 64.45           C  
ATOM   3224  OG  SER A 530     167.459 206.080 233.829  1.00 65.64           O  
ATOM   3225  N   THR A 531     168.183 208.775 231.631  1.00 64.24           N  
ATOM   3226  CA  THR A 531     167.183 209.578 230.952  1.00 64.48           C  
ATOM   3227  C   THR A 531     166.588 208.819 229.781  1.00 64.26           C  
ATOM   3228  O   THR A 531     166.853 207.631 229.602  1.00 64.25           O  
ATOM   3229  CB  THR A 531     167.765 210.916 230.488  1.00 63.79           C  
ATOM   3230  OG1 THR A 531     166.698 211.764 230.038  1.00 64.69           O  
ATOM   3231  CG2 THR A 531     168.762 210.699 229.385  1.00 63.09           C  
ATOM   3232  N   ASN A 532     165.746 209.495 229.018  1.00 64.10           N  
ATOM   3233  CA  ASN A 532     165.094 208.881 227.875  1.00 63.80           C  
ATOM   3234  C   ASN A 532     165.987 208.977 226.662  1.00 63.27           C  
ATOM   3235  O   ASN A 532     166.847 209.853 226.579  1.00 63.06           O  
ATOM   3236  CB  ASN A 532     163.750 209.519 227.606  1.00 64.41           C  
ATOM   3237  CG  ASN A 532     162.753 209.209 228.674  1.00 64.45           C  
ATOM   3238  OD1 ASN A 532     162.698 208.085 229.185  1.00 63.23           O  
ATOM   3239  ND2 ASN A 532     161.959 210.181 229.027  1.00 64.98           N  
ATOM   3240  N   LEU A 533     165.785 208.079 225.717  1.00 63.01           N  
ATOM   3241  CA  LEU A 533     166.596 208.089 224.520  1.00 62.90           C  
ATOM   3242  C   LEU A 533     165.863 208.748 223.369  1.00 62.37           C  
ATOM   3243  O   LEU A 533     164.688 208.477 223.124  1.00 62.58           O  
ATOM   3244  CB  LEU A 533     167.001 206.656 224.182  1.00 63.58           C  
ATOM   3245  CG  LEU A 533     168.012 206.462 223.060  1.00 62.77           C  
ATOM   3246  CD1 LEU A 533     168.885 205.282 223.418  1.00 62.56           C  
ATOM   3247  CD2 LEU A 533     167.298 206.203 221.743  1.00 61.84           C  
ATOM   3248  N   VAL A 534     166.571 209.614 222.665  1.00 62.27           N  
ATOM   3249  CA  VAL A 534     166.031 210.330 221.529  1.00 61.69           C  
ATOM   3250  C   VAL A 534     166.593 209.759 220.242  1.00 60.98           C  
ATOM   3251  O   VAL A 534     167.802 209.760 220.036  1.00 59.94           O  
ATOM   3252  CB  VAL A 534     166.395 211.819 221.643  1.00 61.10           C  
ATOM   3253  CG1 VAL A 534     165.846 212.589 220.474  1.00 60.93           C  
ATOM   3254  CG2 VAL A 534     165.866 212.355 222.961  1.00 60.70           C  
ATOM   3255  N   LYS A 535     165.717 209.259 219.386  1.00 61.20           N  
ATOM   3256  CA  LYS A 535     166.157 208.627 218.152  1.00 60.09           C  
ATOM   3257  C   LYS A 535     166.191 209.589 216.974  1.00 60.09           C  
ATOM   3258  O   LYS A 535     165.423 210.548 216.910  1.00 59.84           O  
ATOM   3259  CB  LYS A 535     165.268 207.429 217.826  1.00 60.02           C  
ATOM   3260  CG  LYS A 535     165.382 206.303 218.837  1.00 61.97           C  
ATOM   3261  CD  LYS A 535     164.499 205.116 218.495  1.00 61.10           C  
ATOM   3262  CE  LYS A 535     164.693 203.996 219.515  1.00 60.71           C  
ATOM   3263  NZ  LYS A 535     163.852 202.800 219.217  1.00 60.40           N  
ATOM   3264  N   ASN A 536     167.058 209.264 216.019  1.00 59.61           N  
ATOM   3265  CA  ASN A 536     167.214 209.951 214.740  1.00 59.42           C  
ATOM   3266  C   ASN A 536     167.633 211.417 214.852  1.00 59.53           C  
ATOM   3267  O   ASN A 536     167.290 212.231 213.994  1.00 60.65           O  
ATOM   3268  CB  ASN A 536     165.927 209.849 213.956  1.00 60.19           C  
ATOM   3269  CG  ASN A 536     165.486 208.434 213.784  1.00 60.74           C  
ATOM   3270  OD1 ASN A 536     166.281 207.531 213.504  1.00 59.88           O  
ATOM   3271  ND2 ASN A 536     164.210 208.214 213.954  1.00 60.90           N  
ATOM   3272  N   LYS A 537     168.402 211.748 215.882  1.00 58.55           N  
ATOM   3273  CA  LYS A 537     168.939 213.091 216.053  1.00 58.32           C  
ATOM   3274  C   LYS A 537     170.398 212.991 216.472  1.00 58.45           C  
ATOM   3275  O   LYS A 537     170.793 211.970 217.035  1.00 58.39           O  
ATOM   3276  CB  LYS A 537     168.145 213.883 217.094  1.00 59.02           C  
ATOM   3277  CG  LYS A 537     166.698 214.117 216.727  1.00 59.99           C  
ATOM   3278  CD  LYS A 537     166.040 215.104 217.669  1.00 60.50           C  
ATOM   3279  CE  LYS A 537     164.565 215.266 217.347  1.00 61.27           C  
ATOM   3280  NZ  LYS A 537     163.907 216.271 218.232  1.00 61.45           N  
ATOM   3281  N   CYS A 538     171.190 214.052 216.227  1.00 57.43           N  
ATOM   3282  CA  CYS A 538     172.575 214.113 216.697  1.00 56.34           C  
ATOM   3283  C   CYS A 538     172.587 214.367 218.204  1.00 56.86           C  
ATOM   3284  O   CYS A 538     172.087 215.394 218.670  1.00 57.51           O  
ATOM   3285  CB  CYS A 538     173.347 215.228 215.968  1.00 56.97           C  
ATOM   3286  SG  CYS A 538     175.091 215.386 216.450  1.00 54.05           S  
ATOM   3287  N   VAL A 539     173.127 213.397 218.967  1.00 56.69           N  
ATOM   3288  CA  VAL A 539     173.136 213.442 220.427  1.00 56.99           C  
ATOM   3289  C   VAL A 539     174.499 213.119 221.020  1.00 56.59           C  
ATOM   3290  O   VAL A 539     175.328 212.438 220.412  1.00 55.34           O  
ATOM   3291  CB  VAL A 539     172.104 212.437 220.981  1.00 57.06           C  
ATOM   3292  CG1 VAL A 539     170.694 212.777 220.469  1.00 57.82           C  
ATOM   3293  CG2 VAL A 539     172.486 211.037 220.551  1.00 57.09           C  
ATOM   3294  N   ASN A 540     174.691 213.571 222.247  1.00 55.51           N  
ATOM   3295  CA  ASN A 540     175.852 213.247 223.058  1.00 55.75           C  
ATOM   3296  C   ASN A 540     175.434 212.115 223.986  1.00 57.97           C  
ATOM   3297  O   ASN A 540     174.550 212.304 224.820  1.00 57.99           O  
ATOM   3298  CB  ASN A 540     176.320 214.478 223.814  1.00 56.25           C  
ATOM   3299  CG  ASN A 540     177.584 214.272 224.590  1.00 56.65           C  
ATOM   3300  OD1 ASN A 540     177.950 213.151 224.958  1.00 56.56           O  
ATOM   3301  ND2 ASN A 540     178.275 215.356 224.852  1.00 56.52           N  
ATOM   3302  N   PHE A 541     175.971 210.921 223.782  1.00 56.90           N  
ATOM   3303  CA  PHE A 541     175.489 209.771 224.537  1.00 56.71           C  
ATOM   3304  C   PHE A 541     176.508 209.171 225.496  1.00 57.06           C  
ATOM   3305  O   PHE A 541     177.721 209.303 225.322  1.00 56.58           O  
ATOM   3306  CB  PHE A 541     174.999 208.673 223.596  1.00 56.43           C  
ATOM   3307  CG  PHE A 541     176.037 208.199 222.650  1.00 56.71           C  
ATOM   3308  CD1 PHE A 541     176.964 207.249 223.037  1.00 57.70           C  
ATOM   3309  CD2 PHE A 541     176.089 208.687 221.363  1.00 56.50           C  
ATOM   3310  CE1 PHE A 541     177.925 206.810 222.166  1.00 55.98           C  
ATOM   3311  CE2 PHE A 541     177.046 208.244 220.489  1.00 56.58           C  
ATOM   3312  CZ  PHE A 541     177.968 207.310 220.892  1.00 55.32           C  
ATOM   3313  N   ASN A 542     175.978 208.463 226.493  1.00 57.61           N  
ATOM   3314  CA  ASN A 542     176.746 207.695 227.467  1.00 57.19           C  
ATOM   3315  C   ASN A 542     176.060 206.374 227.805  1.00 59.08           C  
ATOM   3316  O   ASN A 542     175.053 206.360 228.515  1.00 60.12           O  
ATOM   3317  CB  ASN A 542     176.964 208.499 228.736  1.00 58.42           C  
ATOM   3318  CG  ASN A 542     177.796 207.766 229.771  1.00 58.14           C  
ATOM   3319  OD1 ASN A 542     177.708 206.534 229.886  1.00 59.42           O  
ATOM   3320  ND2 ASN A 542     178.583 208.499 230.522  1.00 58.26           N  
ATOM   3321  N   PHE A 543     176.588 205.268 227.295  1.00 58.71           N  
ATOM   3322  CA  PHE A 543     176.007 203.960 227.578  1.00 59.31           C  
ATOM   3323  C   PHE A 543     176.934 203.152 228.468  1.00 59.41           C  
ATOM   3324  O   PHE A 543     177.979 202.686 228.026  1.00 59.39           O  
ATOM   3325  CB  PHE A 543     175.743 203.178 226.296  1.00 59.16           C  
ATOM   3326  CG  PHE A 543     174.714 203.780 225.415  1.00 59.33           C  
ATOM   3327  CD1 PHE A 543     175.072 204.537 224.330  1.00 58.98           C  
ATOM   3328  CD2 PHE A 543     173.381 203.586 225.676  1.00 60.21           C  
ATOM   3329  CE1 PHE A 543     174.112 205.087 223.514  1.00 58.70           C  
ATOM   3330  CE2 PHE A 543     172.416 204.127 224.871  1.00 60.55           C  
ATOM   3331  CZ  PHE A 543     172.783 204.880 223.786  1.00 59.34           C  
ATOM   3332  N   ASN A 544     176.583 203.014 229.733  1.00 60.25           N  
ATOM   3333  CA  ASN A 544     177.431 202.296 230.678  1.00 60.80           C  
ATOM   3334  C   ASN A 544     178.858 202.837 230.731  1.00 60.70           C  
ATOM   3335  O   ASN A 544     179.805 202.068 230.885  1.00 61.90           O  
ATOM   3336  CB  ASN A 544     177.486 200.828 230.328  1.00 61.77           C  
ATOM   3337  CG  ASN A 544     176.165 200.190 230.348  1.00 62.12           C  
ATOM   3338  OD1 ASN A 544     175.330 200.480 231.206  1.00 63.90           O  
ATOM   3339  ND2 ASN A 544     175.944 199.303 229.409  1.00 63.27           N  
ATOM   3340  N   GLY A 545     179.031 204.147 230.609  1.00 60.52           N  
ATOM   3341  CA  GLY A 545     180.364 204.732 230.650  1.00 59.42           C  
ATOM   3342  C   GLY A 545     180.979 204.886 229.256  1.00 57.78           C  
ATOM   3343  O   GLY A 545     182.013 205.534 229.104  1.00 57.05           O  
ATOM   3344  N   LEU A 546     180.336 204.317 228.237  1.00 58.24           N  
ATOM   3345  CA  LEU A 546     180.823 204.418 226.866  1.00 56.69           C  
ATOM   3346  C   LEU A 546     180.273 205.667 226.221  1.00 57.18           C  
ATOM   3347  O   LEU A 546     179.077 205.759 225.940  1.00 55.08           O  
ATOM   3348  CB  LEU A 546     180.365 203.197 226.054  1.00 56.74           C  
ATOM   3349  CG  LEU A 546     180.716 203.163 224.552  1.00 55.64           C  
ATOM   3350  CD1 LEU A 546     182.226 203.135 224.359  1.00 55.21           C  
ATOM   3351  CD2 LEU A 546     180.063 201.926 223.933  1.00 55.88           C  
ATOM   3352  N   THR A 547     181.138 206.636 225.977  1.00 56.30           N  
ATOM   3353  CA  THR A 547     180.664 207.916 225.492  1.00 55.57           C  
ATOM   3354  C   THR A 547     181.062 208.212 224.069  1.00 54.69           C  
ATOM   3355  O   THR A 547     182.055 207.692 223.559  1.00 53.87           O  
ATOM   3356  CB  THR A 547     181.193 209.042 226.385  1.00 55.10           C  
ATOM   3357  OG1 THR A 547     182.626 209.068 226.320  1.00 51.90           O  
ATOM   3358  CG2 THR A 547     180.761 208.804 227.811  1.00 55.92           C  
ATOM   3359  N   GLY A 548     180.315 209.117 223.459  1.00 54.73           N  
ATOM   3360  CA  GLY A 548     180.615 209.588 222.118  1.00 54.02           C  
ATOM   3361  C   GLY A 548     179.490 210.452 221.574  1.00 54.94           C  
ATOM   3362  O   GLY A 548     178.503 210.709 222.261  1.00 55.46           O  
ATOM   3363  N   THR A 549     179.662 210.919 220.348  1.00 54.08           N  
ATOM   3364  CA  THR A 549     178.664 211.746 219.689  1.00 54.76           C  
ATOM   3365  C   THR A 549     178.236 211.079 218.398  1.00 54.32           C  
ATOM   3366  O   THR A 549     179.074 210.601 217.633  1.00 53.05           O  
ATOM   3367  CB  THR A 549     179.202 213.162 219.413  1.00 53.05           C  
ATOM   3368  OG1 THR A 549     179.548 213.785 220.653  1.00 53.36           O  
ATOM   3369  CG2 THR A 549     178.150 214.008 218.704  1.00 54.93           C  
ATOM   3370  N   GLY A 550     176.936 211.024 218.167  1.00 54.84           N  
ATOM   3371  CA  GLY A 550     176.423 210.397 216.958  1.00 54.24           C  
ATOM   3372  C   GLY A 550     174.916 210.301 216.973  1.00 54.54           C  
ATOM   3373  O   GLY A 550     174.270 210.658 217.954  1.00 55.77           O  
ATOM   3374  N   VAL A 551     174.364 209.814 215.879  1.00 54.40           N  
ATOM   3375  CA  VAL A 551     172.935 209.653 215.730  1.00 56.07           C  
ATOM   3376  C   VAL A 551     172.546 208.222 216.053  1.00 56.98           C  
ATOM   3377  O   VAL A 551     173.127 207.279 215.517  1.00 55.86           O  
ATOM   3378  CB  VAL A 551     172.516 210.000 214.291  1.00 56.29           C  
ATOM   3379  CG1 VAL A 551     171.017 209.827 214.125  1.00 57.62           C  
ATOM   3380  CG2 VAL A 551     172.939 211.425 213.973  1.00 55.24           C  
ATOM   3381  N   LEU A 552     171.575 208.062 216.938  1.00 56.71           N  
ATOM   3382  CA  LEU A 552     171.128 206.743 217.359  1.00 57.51           C  
ATOM   3383  C   LEU A 552     169.902 206.323 216.565  1.00 58.08           C  
ATOM   3384  O   LEU A 552     168.877 207.005 216.612  1.00 59.51           O  
ATOM   3385  CB  LEU A 552     170.762 206.783 218.847  1.00 57.25           C  
ATOM   3386  CG  LEU A 552     171.830 207.358 219.802  1.00 58.07           C  
ATOM   3387  CD1 LEU A 552     171.250 207.441 221.194  1.00 59.23           C  
ATOM   3388  CD2 LEU A 552     173.065 206.488 219.790  1.00 57.46           C  
ATOM   3389  N   THR A 553     170.003 205.221 215.829  1.00 57.69           N  
ATOM   3390  CA  THR A 553     168.875 204.768 215.017  1.00 58.52           C  
ATOM   3391  C   THR A 553     168.587 203.299 215.255  1.00 59.62           C  
ATOM   3392  O   THR A 553     169.464 202.549 215.672  1.00 59.04           O  
ATOM   3393  CB  THR A 553     169.143 204.970 213.513  1.00 58.45           C  
ATOM   3394  OG1 THR A 553     170.190 204.090 213.082  1.00 58.23           O  
ATOM   3395  CG2 THR A 553     169.577 206.397 213.252  1.00 59.40           C  
ATOM   3396  N   GLU A 554     167.381 202.859 214.928  1.00 58.79           N  
ATOM   3397  CA  GLU A 554     167.064 201.442 215.048  1.00 58.94           C  
ATOM   3398  C   GLU A 554     167.939 200.634 214.108  1.00 58.65           C  
ATOM   3399  O   GLU A 554     168.051 200.969 212.927  1.00 59.08           O  
ATOM   3400  CB  GLU A 554     165.590 201.203 214.731  1.00 59.23           C  
ATOM   3401  CG  GLU A 554     165.125 199.768 214.910  1.00 59.53           C  
ATOM   3402  CD  GLU A 554     163.659 199.606 214.644  1.00 59.49           C  
ATOM   3403  OE1 GLU A 554     163.031 200.581 214.307  1.00 58.91           O  
ATOM   3404  OE2 GLU A 554     163.161 198.515 214.784  1.00 58.31           O  
ATOM   3405  N   SER A 555     168.557 199.573 214.618  1.00 58.15           N  
ATOM   3406  CA  SER A 555     169.419 198.744 213.788  1.00 58.02           C  
ATOM   3407  C   SER A 555     168.682 197.554 213.215  1.00 59.11           C  
ATOM   3408  O   SER A 555     167.662 197.123 213.749  1.00 59.03           O  
ATOM   3409  CB  SER A 555     170.563 198.200 214.600  1.00 58.41           C  
ATOM   3410  OG  SER A 555     170.103 197.239 215.493  1.00 58.53           O  
ATOM   3411  N   ASN A 556     169.262 196.952 212.185  1.00 59.27           N  
ATOM   3412  CA  ASN A 556     168.775 195.683 211.670  1.00 58.39           C  
ATOM   3413  C   ASN A 556     169.873 194.636 211.811  1.00 58.31           C  
ATOM   3414  O   ASN A 556     169.888 193.627 211.108  1.00 58.36           O  
ATOM   3415  CB  ASN A 556     168.309 195.815 210.235  1.00 58.06           C  
ATOM   3416  CG  ASN A 556     169.410 196.207 209.309  1.00 58.52           C  
ATOM   3417  OD1 ASN A 556     170.391 196.841 209.724  1.00 58.20           O  
ATOM   3418  ND2 ASN A 556     169.278 195.851 208.057  1.00 58.60           N  
ATOM   3419  N   LYS A 557     170.800 194.901 212.727  1.00 58.33           N  
ATOM   3420  CA  LYS A 557     171.917 194.012 212.995  1.00 57.91           C  
ATOM   3421  C   LYS A 557     171.477 192.824 213.819  1.00 57.92           C  
ATOM   3422  O   LYS A 557     170.773 192.964 214.821  1.00 58.36           O  
ATOM   3423  CB  LYS A 557     173.034 194.765 213.710  1.00 58.00           C  
ATOM   3424  CG  LYS A 557     173.705 195.824 212.858  1.00 57.47           C  
ATOM   3425  CD  LYS A 557     174.731 196.618 213.651  1.00 57.26           C  
ATOM   3426  CE  LYS A 557     175.344 197.731 212.803  1.00 56.57           C  
ATOM   3427  NZ  LYS A 557     176.378 197.225 211.865  1.00 56.64           N  
ATOM   3428  N   LYS A 558     171.914 191.646 213.415  1.00 57.43           N  
ATOM   3429  CA  LYS A 558     171.523 190.426 214.097  1.00 57.76           C  
ATOM   3430  C   LYS A 558     172.380 190.154 215.315  1.00 58.24           C  
ATOM   3431  O   LYS A 558     173.214 189.253 215.310  1.00 57.71           O  
ATOM   3432  CB  LYS A 558     171.605 189.239 213.138  1.00 57.80           C  
ATOM   3433  CG  LYS A 558     170.774 189.377 211.855  1.00 57.91           C  
ATOM   3434  CD  LYS A 558     169.277 189.426 212.134  1.00 58.23           C  
ATOM   3435  CE  LYS A 558     168.482 189.425 210.834  1.00 58.53           C  
ATOM   3436  NZ  LYS A 558     167.013 189.481 211.078  1.00 59.70           N  
ATOM   3437  N   PHE A 559     172.173 190.924 216.369  1.00 57.92           N  
ATOM   3438  CA  PHE A 559     172.940 190.691 217.582  1.00 57.89           C  
ATOM   3439  C   PHE A 559     172.528 189.400 218.242  1.00 58.66           C  
ATOM   3440  O   PHE A 559     171.345 189.059 218.292  1.00 58.74           O  
ATOM   3441  CB  PHE A 559     172.774 191.802 218.608  1.00 58.86           C  
ATOM   3442  CG  PHE A 559     173.680 192.967 218.453  1.00 59.05           C  
ATOM   3443  CD1 PHE A 559     173.887 193.598 217.245  1.00 58.58           C  
ATOM   3444  CD2 PHE A 559     174.345 193.436 219.568  1.00 58.61           C  
ATOM   3445  CE1 PHE A 559     174.744 194.679 217.171  1.00 58.44           C  
ATOM   3446  CE2 PHE A 559     175.186 194.498 219.496  1.00 57.87           C  
ATOM   3447  CZ  PHE A 559     175.391 195.128 218.300  1.00 57.43           C  
ATOM   3448  N   LEU A 560     173.511 188.701 218.780  1.00 58.98           N  
ATOM   3449  CA  LEU A 560     173.267 187.486 219.524  1.00 58.63           C  
ATOM   3450  C   LEU A 560     172.930 187.888 220.961  1.00 58.81           C  
ATOM   3451  O   LEU A 560     173.281 188.992 221.374  1.00 59.03           O  
ATOM   3452  CB  LEU A 560     174.503 186.582 219.421  1.00 59.10           C  
ATOM   3453  CG  LEU A 560     174.888 186.160 217.974  1.00 58.93           C  
ATOM   3454  CD1 LEU A 560     176.223 185.443 217.987  1.00 58.02           C  
ATOM   3455  CD2 LEU A 560     173.812 185.242 217.397  1.00 58.85           C  
ATOM   3456  N   PRO A 561     172.245 187.038 221.740  1.00 58.44           N  
ATOM   3457  CA  PRO A 561     171.787 187.287 223.103  1.00 59.06           C  
ATOM   3458  C   PRO A 561     172.880 187.707 224.081  1.00 59.21           C  
ATOM   3459  O   PRO A 561     172.591 188.286 225.127  1.00 58.94           O  
ATOM   3460  CB  PRO A 561     171.216 185.922 223.507  1.00 59.28           C  
ATOM   3461  CG  PRO A 561     170.816 185.272 222.211  1.00 59.48           C  
ATOM   3462  CD  PRO A 561     171.858 185.705 221.221  1.00 59.40           C  
ATOM   3463  N   PHE A 562     174.126 187.401 223.761  1.00 58.30           N  
ATOM   3464  CA  PHE A 562     175.224 187.718 224.654  1.00 59.05           C  
ATOM   3465  C   PHE A 562     176.021 188.945 224.236  1.00 59.00           C  
ATOM   3466  O   PHE A 562     176.917 189.368 224.963  1.00 59.48           O  
ATOM   3467  CB  PHE A 562     176.162 186.520 224.741  1.00 58.91           C  
ATOM   3468  CG  PHE A 562     176.772 186.135 223.426  1.00 58.66           C  
ATOM   3469  CD1 PHE A 562     177.945 186.716 222.995  1.00 57.80           C  
ATOM   3470  CD2 PHE A 562     176.172 185.193 222.621  1.00 58.65           C  
ATOM   3471  CE1 PHE A 562     178.513 186.359 221.797  1.00 57.97           C  
ATOM   3472  CE2 PHE A 562     176.732 184.842 221.425  1.00 57.93           C  
ATOM   3473  CZ  PHE A 562     177.905 185.422 221.012  1.00 57.84           C  
ATOM   3474  N   GLN A 563     175.722 189.508 223.072  1.00 58.78           N  
ATOM   3475  CA  GLN A 563     176.524 190.607 222.552  1.00 58.33           C  
ATOM   3476  C   GLN A 563     176.014 191.962 223.023  1.00 58.61           C  
ATOM   3477  O   GLN A 563     174.834 192.280 222.891  1.00 60.18           O  
ATOM   3478  CB  GLN A 563     176.581 190.522 221.031  1.00 57.60           C  
ATOM   3479  CG  GLN A 563     177.303 189.273 220.562  1.00 57.32           C  
ATOM   3480  CD  GLN A 563     177.353 189.112 219.079  1.00 58.07           C  
ATOM   3481  OE1 GLN A 563     176.337 189.243 218.391  1.00 57.91           O  
ATOM   3482  NE2 GLN A 563     178.536 188.811 218.555  1.00 56.73           N  
ATOM   3483  N   GLN A 564     176.917 192.753 223.591  1.00 58.04           N  
ATOM   3484  CA  GLN A 564     176.535 194.029 224.193  1.00 59.24           C  
ATOM   3485  C   GLN A 564     176.656 195.216 223.249  1.00 59.71           C  
ATOM   3486  O   GLN A 564     175.904 196.182 223.364  1.00 61.06           O  
ATOM   3487  CB  GLN A 564     177.345 194.265 225.470  1.00 60.98           C  
ATOM   3488  CG  GLN A 564     177.007 195.550 226.220  1.00 61.34           C  
ATOM   3489  CD  GLN A 564     175.553 195.626 226.656  1.00 61.05           C  
ATOM   3490  OE1 GLN A 564     174.910 194.619 226.991  1.00 61.88           O  
ATOM   3491  NE2 GLN A 564     175.016 196.838 226.646  1.00 61.41           N  
ATOM   3492  N   PHE A 565     177.627 195.172 222.357  1.00 58.99           N  
ATOM   3493  CA  PHE A 565     177.845 196.242 221.395  1.00 58.04           C  
ATOM   3494  C   PHE A 565     178.635 195.677 220.240  1.00 56.76           C  
ATOM   3495  O   PHE A 565     179.186 194.586 220.361  1.00 53.51           O  
ATOM   3496  CB  PHE A 565     178.548 197.438 222.022  1.00 57.67           C  
ATOM   3497  CG  PHE A 565     179.889 197.176 222.493  1.00 58.17           C  
ATOM   3498  CD1 PHE A 565     180.961 197.421 221.676  1.00 56.87           C  
ATOM   3499  CD2 PHE A 565     180.106 196.694 223.762  1.00 59.00           C  
ATOM   3500  CE1 PHE A 565     182.226 197.191 222.113  1.00 55.75           C  
ATOM   3501  CE2 PHE A 565     181.377 196.457 224.209  1.00 59.75           C  
ATOM   3502  CZ  PHE A 565     182.442 196.708 223.382  1.00 57.96           C  
ATOM   3503  N   GLY A 566     178.684 196.401 219.133  1.00 56.51           N  
ATOM   3504  CA  GLY A 566     179.478 195.982 217.988  1.00 56.18           C  
ATOM   3505  C   GLY A 566     180.536 197.010 217.667  1.00 56.20           C  
ATOM   3506  O   GLY A 566     180.450 198.151 218.127  1.00 55.22           O  
ATOM   3507  N   ARG A 567     181.502 196.620 216.840  1.00 53.62           N  
ATOM   3508  CA  ARG A 567     182.593 197.513 216.449  1.00 52.76           C  
ATOM   3509  C   ARG A 567     182.851 197.567 214.948  1.00 53.35           C  
ATOM   3510  O   ARG A 567     182.567 196.621 214.211  1.00 53.46           O  
ATOM   3511  CB  ARG A 567     183.901 197.127 217.125  1.00 51.88           C  
ATOM   3512  CG  ARG A 567     183.985 197.359 218.624  1.00 52.59           C  
ATOM   3513  CD  ARG A 567     185.326 196.945 219.143  1.00 51.32           C  
ATOM   3514  NE  ARG A 567     185.422 197.007 220.597  1.00 52.23           N  
ATOM   3515  CZ  ARG A 567     185.807 198.089 221.315  1.00 52.14           C  
ATOM   3516  NH1 ARG A 567     186.132 199.211 220.714  1.00 50.78           N  
ATOM   3517  NH2 ARG A 567     185.859 198.016 222.636  1.00 52.95           N  
ATOM   3518  N   ASP A 568     183.428 198.689 214.521  1.00 52.18           N  
ATOM   3519  CA  ASP A 568     183.855 198.920 213.145  1.00 51.29           C  
ATOM   3520  C   ASP A 568     185.303 198.449 212.954  1.00 51.61           C  
ATOM   3521  O   ASP A 568     185.953 198.020 213.907  1.00 49.68           O  
ATOM   3522  CB  ASP A 568     183.729 200.424 212.827  1.00 51.53           C  
ATOM   3523  N   ILE A 569     185.825 198.585 211.740  1.00 49.79           N  
ATOM   3524  CA  ILE A 569     187.199 198.194 211.417  1.00 49.72           C  
ATOM   3525  C   ILE A 569     188.217 199.062 212.149  1.00 48.74           C  
ATOM   3526  O   ILE A 569     189.346 198.646 212.398  1.00 47.17           O  
ATOM   3527  CB  ILE A 569     187.440 198.258 209.891  1.00 49.41           C  
ATOM   3528  CG1 ILE A 569     188.733 197.490 209.484  1.00 47.76           C  
ATOM   3529  CG2 ILE A 569     187.533 199.706 209.423  1.00 48.66           C  
ATOM   3530  CD1 ILE A 569     188.681 195.977 209.691  1.00 49.20           C  
ATOM   3531  N   ALA A 570     187.801 200.274 212.496  1.00 48.56           N  
ATOM   3532  CA  ALA A 570     188.633 201.249 213.190  1.00 47.51           C  
ATOM   3533  C   ALA A 570     188.661 200.978 214.691  1.00 48.36           C  
ATOM   3534  O   ALA A 570     189.284 201.718 215.450  1.00 46.30           O  
ATOM   3535  CB  ALA A 570     188.113 202.651 212.931  1.00 45.47           C  
ATOM   3536  N   ASP A 571     187.963 199.925 215.111  1.00 48.93           N  
ATOM   3537  CA  ASP A 571     187.816 199.545 216.509  1.00 49.72           C  
ATOM   3538  C   ASP A 571     187.041 200.599 217.289  1.00 50.44           C  
ATOM   3539  O   ASP A 571     187.307 200.841 218.467  1.00 49.71           O  
ATOM   3540  CB  ASP A 571     189.190 199.332 217.160  1.00 47.94           C  
ATOM   3541  N   THR A 572     186.053 201.202 216.636  1.00 50.86           N  
ATOM   3542  CA  THR A 572     185.178 202.161 217.281  1.00 51.11           C  
ATOM   3543  C   THR A 572     183.799 201.544 217.361  1.00 52.95           C  
ATOM   3544  O   THR A 572     183.487 200.620 216.610  1.00 52.83           O  
ATOM   3545  CB  THR A 572     185.130 203.482 216.496  1.00 50.98           C  
ATOM   3546  OG1 THR A 572     184.543 203.254 215.204  1.00 51.27           O  
ATOM   3547  CG2 THR A 572     186.545 204.015 216.313  1.00 49.81           C  
ATOM   3548  N   THR A 573     182.957 202.048 218.246  1.00 53.00           N  
ATOM   3549  CA  THR A 573     181.635 201.461 218.398  1.00 53.83           C  
ATOM   3550  C   THR A 573     180.783 201.667 217.154  1.00 54.43           C  
ATOM   3551  O   THR A 573     180.661 202.779 216.645  1.00 54.32           O  
ATOM   3552  CB  THR A 573     180.926 202.051 219.625  1.00 54.78           C  
ATOM   3553  OG1 THR A 573     181.738 201.838 220.785  1.00 55.04           O  
ATOM   3554  CG2 THR A 573     179.579 201.396 219.841  1.00 55.56           C  
ATOM   3555  N   ASP A 574     180.194 200.579 216.674  1.00 54.71           N  
ATOM   3556  CA  ASP A 574     179.321 200.574 215.505  1.00 54.07           C  
ATOM   3557  C   ASP A 574     177.858 200.616 215.925  1.00 56.15           C  
ATOM   3558  O   ASP A 574     177.028 201.268 215.289  1.00 57.44           O  
ATOM   3559  CB  ASP A 574     179.612 199.324 214.663  1.00 56.49           C  
ATOM   3560  CG  ASP A 574     178.830 199.214 213.360  1.00 55.84           C  
ATOM   3561  OD1 ASP A 574     178.796 200.157 212.617  1.00 55.90           O  
ATOM   3562  OD2 ASP A 574     178.290 198.152 213.103  1.00 56.07           O  
ATOM   3563  N   ALA A 575     177.550 199.886 216.987  1.00 56.06           N  
ATOM   3564  CA  ALA A 575     176.186 199.774 217.496  1.00 56.44           C  
ATOM   3565  C   ALA A 575     176.219 199.389 218.955  1.00 57.94           C  
ATOM   3566  O   ALA A 575     177.200 198.816 219.423  1.00 58.06           O  
ATOM   3567  CB  ALA A 575     175.396 198.751 216.702  1.00 57.22           C  
ATOM   3568  N   VAL A 576     175.147 199.682 219.679  1.00 57.57           N  
ATOM   3569  CA  VAL A 576     175.060 199.269 221.073  1.00 58.31           C  
ATOM   3570  C   VAL A 576     173.739 198.628 221.441  1.00 59.06           C  
ATOM   3571  O   VAL A 576     172.695 198.940 220.867  1.00 59.31           O  
ATOM   3572  CB  VAL A 576     175.268 200.475 222.007  1.00 58.58           C  
ATOM   3573  CG1 VAL A 576     176.643 201.045 221.821  1.00 58.15           C  
ATOM   3574  CG2 VAL A 576     174.206 201.543 221.714  1.00 58.40           C  
ATOM   3575  N   ARG A 577     173.774 197.801 222.473  1.00 59.40           N  
ATOM   3576  CA  ARG A 577     172.559 197.312 223.083  1.00 59.61           C  
ATOM   3577  C   ARG A 577     172.199 198.254 224.207  1.00 61.19           C  
ATOM   3578  O   ARG A 577     173.009 198.519 225.096  1.00 61.71           O  
ATOM   3579  CB  ARG A 577     172.729 195.897 223.605  1.00 60.48           C  
ATOM   3580  CG  ARG A 577     171.491 195.300 224.246  1.00 60.70           C  
ATOM   3581  CD  ARG A 577     171.592 193.833 224.369  1.00 59.58           C  
ATOM   3582  NE  ARG A 577     172.675 193.419 225.251  1.00 60.68           N  
ATOM   3583  CZ  ARG A 577     172.997 192.140 225.512  1.00 59.74           C  
ATOM   3584  NH1 ARG A 577     172.304 191.155 224.973  1.00 60.14           N  
ATOM   3585  NH2 ARG A 577     174.014 191.894 226.314  1.00 60.83           N  
ATOM   3586  N   ASP A 578     171.000 198.793 224.155  1.00 61.76           N  
ATOM   3587  CA  ASP A 578     170.576 199.735 225.170  1.00 61.19           C  
ATOM   3588  C   ASP A 578     170.513 199.028 226.537  1.00 62.25           C  
ATOM   3589  O   ASP A 578     169.907 197.964 226.650  1.00 62.55           O  
ATOM   3590  CB  ASP A 578     169.244 200.366 224.781  1.00 61.42           C  
ATOM   3591  CG  ASP A 578     168.817 201.429 225.723  1.00 63.24           C  
ATOM   3592  OD1 ASP A 578     168.443 201.103 226.842  1.00 63.74           O  
ATOM   3593  OD2 ASP A 578     168.873 202.581 225.345  1.00 63.16           O  
ATOM   3594  N   PRO A 579     171.165 199.564 227.581  1.00 61.94           N  
ATOM   3595  CA  PRO A 579     171.275 198.990 228.909  1.00 62.71           C  
ATOM   3596  C   PRO A 579     169.965 198.894 229.683  1.00 64.62           C  
ATOM   3597  O   PRO A 579     169.892 198.160 230.664  1.00 64.79           O  
ATOM   3598  CB  PRO A 579     172.236 199.950 229.604  1.00 63.46           C  
ATOM   3599  CG  PRO A 579     172.101 201.235 228.872  1.00 63.07           C  
ATOM   3600  CD  PRO A 579     171.835 200.850 227.439  1.00 63.04           C  
ATOM   3601  N   GLN A 580     168.943 199.648 229.284  1.00 63.74           N  
ATOM   3602  CA  GLN A 580     167.679 199.600 230.008  1.00 64.50           C  
ATOM   3603  C   GLN A 580     166.619 198.866 229.204  1.00 63.30           C  
ATOM   3604  O   GLN A 580     165.749 198.196 229.766  1.00 64.71           O  
ATOM   3605  CB  GLN A 580     167.200 201.010 230.366  1.00 64.33           C  
ATOM   3606  CG  GLN A 580     168.103 201.727 231.344  1.00 64.66           C  
ATOM   3607  CD  GLN A 580     167.575 203.093 231.786  1.00 64.59           C  
ATOM   3608  OE1 GLN A 580     167.177 203.962 230.992  1.00 64.23           O  
ATOM   3609  NE2 GLN A 580     167.570 203.289 233.090  1.00 65.12           N  
ATOM   3610  N   THR A 581     166.702 199.000 227.884  1.00 63.18           N  
ATOM   3611  CA  THR A 581     165.748 198.404 226.959  1.00 63.13           C  
ATOM   3612  C   THR A 581     166.459 197.408 226.060  1.00 63.26           C  
ATOM   3613  O   THR A 581     167.462 197.737 225.440  1.00 62.81           O  
ATOM   3614  CB  THR A 581     165.087 199.494 226.095  1.00 62.32           C  
ATOM   3615  OG1 THR A 581     164.406 200.419 226.944  1.00 63.16           O  
ATOM   3616  CG2 THR A 581     164.098 198.879 225.113  1.00 62.39           C  
ATOM   3617  N   LEU A 582     165.929 196.206 225.924  1.00 62.61           N  
ATOM   3618  CA  LEU A 582     166.632 195.226 225.108  1.00 62.30           C  
ATOM   3619  C   LEU A 582     166.379 195.416 223.618  1.00 61.72           C  
ATOM   3620  O   LEU A 582     165.683 194.630 222.976  1.00 62.39           O  
ATOM   3621  CB  LEU A 582     166.241 193.810 225.535  1.00 62.34           C  
ATOM   3622  N   GLU A 583     166.986 196.471 223.085  1.00 61.85           N  
ATOM   3623  CA  GLU A 583     166.916 196.842 221.679  1.00 61.44           C  
ATOM   3624  C   GLU A 583     168.302 197.245 221.197  1.00 61.34           C  
ATOM   3625  O   GLU A 583     169.143 197.689 221.984  1.00 60.93           O  
ATOM   3626  CB  GLU A 583     165.937 197.998 221.441  1.00 61.61           C  
ATOM   3627  N   ILE A 584     168.537 197.096 219.902  1.00 60.27           N  
ATOM   3628  CA  ILE A 584     169.834 197.437 219.337  1.00 59.32           C  
ATOM   3629  C   ILE A 584     169.766 198.706 218.509  1.00 59.81           C  
ATOM   3630  O   ILE A 584     168.893 198.863 217.650  1.00 60.27           O  
ATOM   3631  CB  ILE A 584     170.375 196.293 218.470  1.00 60.06           C  
ATOM   3632  CG1 ILE A 584     170.373 194.961 219.255  1.00 59.52           C  
ATOM   3633  CG2 ILE A 584     171.790 196.634 217.974  1.00 58.60           C  
ATOM   3634  CD1 ILE A 584     171.180 194.953 220.532  1.00 59.18           C  
ATOM   3635  N   LEU A 585     170.688 199.615 218.795  1.00 58.93           N  
ATOM   3636  CA  LEU A 585     170.757 200.886 218.100  1.00 58.30           C  
ATOM   3637  C   LEU A 585     172.082 201.069 217.385  1.00 58.26           C  
ATOM   3638  O   LEU A 585     173.145 200.816 217.951  1.00 58.67           O  
ATOM   3639  CB  LEU A 585     170.571 202.016 219.103  1.00 58.68           C  
ATOM   3640  CG  LEU A 585     169.309 201.938 219.937  1.00 60.04           C  
ATOM   3641  CD1 LEU A 585     169.352 203.009 220.971  1.00 59.94           C  
ATOM   3642  CD2 LEU A 585     168.089 202.094 219.049  1.00 59.35           C  
ATOM   3643  N   ASP A 586     172.017 201.537 216.150  1.00 57.92           N  
ATOM   3644  CA  ASP A 586     173.210 201.831 215.372  1.00 57.10           C  
ATOM   3645  C   ASP A 586     173.690 203.219 215.704  1.00 57.32           C  
ATOM   3646  O   ASP A 586     172.877 204.118 215.926  1.00 57.98           O  
ATOM   3647  CB  ASP A 586     172.933 201.740 213.874  1.00 57.63           C  
ATOM   3648  N   ILE A 587     174.999 203.423 215.723  1.00 56.39           N  
ATOM   3649  CA  ILE A 587     175.498 204.763 215.968  1.00 55.34           C  
ATOM   3650  C   ILE A 587     176.181 205.317 214.738  1.00 54.24           C  
ATOM   3651  O   ILE A 587     177.273 204.889 214.369  1.00 53.78           O  
ATOM   3652  CB  ILE A 587     176.476 204.784 217.146  1.00 55.74           C  
ATOM   3653  CG1 ILE A 587     175.768 204.235 218.399  1.00 55.80           C  
ATOM   3654  CG2 ILE A 587     176.973 206.218 217.365  1.00 54.98           C  
ATOM   3655  CD1 ILE A 587     176.657 204.025 219.584  1.00 57.35           C  
ATOM   3656  N   THR A 588     175.560 206.298 214.118  1.00 54.17           N  
ATOM   3657  CA  THR A 588     176.142 206.895 212.931  1.00 52.69           C  
ATOM   3658  C   THR A 588     176.661 208.277 213.291  1.00 52.79           C  
ATOM   3659  O   THR A 588     175.872 209.148 213.639  1.00 53.72           O  
ATOM   3660  CB  THR A 588     175.122 207.004 211.786  1.00 53.55           C  
ATOM   3661  OG1 THR A 588     174.659 205.697 211.431  1.00 53.79           O  
ATOM   3662  CG2 THR A 588     175.778 207.644 210.571  1.00 52.05           C  
ATOM   3663  N   PRO A 589     177.962 208.535 213.203  1.00 50.97           N  
ATOM   3664  CA  PRO A 589     178.567 209.795 213.563  1.00 50.62           C  
ATOM   3665  C   PRO A 589     177.797 210.895 212.861  1.00 50.50           C  
ATOM   3666  O   PRO A 589     177.336 210.697 211.735  1.00 49.30           O  
ATOM   3667  CB  PRO A 589     179.992 209.632 213.038  1.00 48.36           C  
ATOM   3668  CG  PRO A 589     180.234 208.140 213.121  1.00 48.21           C  
ATOM   3669  CD  PRO A 589     178.909 207.510 212.763  1.00 49.39           C  
ATOM   3670  N   CYS A 590     177.637 212.042 213.537  1.00 51.00           N  
ATOM   3671  CA  CYS A 590     176.835 213.167 213.054  1.00 50.38           C  
ATOM   3672  C   CYS A 590     177.427 213.711 211.752  1.00 48.31           C  
ATOM   3673  O   CYS A 590     178.649 213.720 211.575  1.00 47.57           O  
ATOM   3674  CB  CYS A 590     176.758 214.272 214.130  1.00 52.48           C  
ATOM   3675  SG  CYS A 590     175.944 213.734 215.664  1.00 52.61           S  
ATOM   3676  N   SER A 591     176.545 214.144 210.832  1.00 48.51           N  
ATOM   3677  CA  SER A 591     176.915 214.597 209.490  1.00 46.70           C  
ATOM   3678  C   SER A 591     177.991 215.671 209.490  1.00 46.00           C  
ATOM   3679  O   SER A 591     177.964 216.612 210.288  1.00 46.24           O  
ATOM   3680  CB  SER A 591     175.684 215.115 208.788  1.00 47.00           C  
ATOM   3681  OG  SER A 591     174.737 214.094 208.642  1.00 47.30           O  
ATOM   3682  N   PHE A 592     178.950 215.501 208.594  1.00 44.94           N  
ATOM   3683  CA  PHE A 592     180.065 216.412 208.490  1.00 43.14           C  
ATOM   3684  C   PHE A 592     180.621 216.386 207.084  1.00 42.83           C  
ATOM   3685  O   PHE A 592     180.292 215.495 206.300  1.00 42.56           O  
ATOM   3686  CB  PHE A 592     181.182 216.011 209.454  1.00 42.27           C  
ATOM   3687  CG  PHE A 592     181.867 214.752 209.048  1.00 43.51           C  
ATOM   3688  CD1 PHE A 592     183.046 214.804 208.313  1.00 42.61           C  
ATOM   3689  CD2 PHE A 592     181.341 213.520 209.362  1.00 43.42           C  
ATOM   3690  CE1 PHE A 592     183.677 213.651 207.904  1.00 41.63           C  
ATOM   3691  CE2 PHE A 592     181.968 212.365 208.954  1.00 42.43           C  
ATOM   3692  CZ  PHE A 592     183.137 212.430 208.222  1.00 41.65           C  
ATOM   3693  N   GLY A 593     181.490 217.337 206.780  1.00 42.34           N  
ATOM   3694  CA  GLY A 593     182.199 217.322 205.506  1.00 41.31           C  
ATOM   3695  C   GLY A 593     183.131 218.510 205.372  1.00 40.65           C  
ATOM   3696  O   GLY A 593     183.002 219.497 206.088  1.00 41.74           O  
ATOM   3697  N   GLY A 594     184.064 218.433 204.440  1.00 40.05           N  
ATOM   3698  CA  GLY A 594     185.008 219.527 204.263  1.00 39.47           C  
ATOM   3699  C   GLY A 594     184.305 220.745 203.697  1.00 38.95           C  
ATOM   3700  O   GLY A 594     183.323 220.624 202.968  1.00 39.80           O  
ATOM   3701  N   VAL A 595     184.804 221.924 204.025  1.00 39.04           N  
ATOM   3702  CA  VAL A 595     184.221 223.129 203.468  1.00 38.26           C  
ATOM   3703  C   VAL A 595     185.247 223.897 202.671  1.00 38.09           C  
ATOM   3704  O   VAL A 595     186.306 224.278 203.189  1.00 38.88           O  
ATOM   3705  CB  VAL A 595     183.642 224.028 204.565  1.00 38.96           C  
ATOM   3706  CG1 VAL A 595     183.063 225.278 203.954  1.00 38.51           C  
ATOM   3707  CG2 VAL A 595     182.582 223.283 205.302  1.00 39.80           C  
ATOM   3708  N   SER A 596     184.910 224.137 201.413  1.00 37.87           N  
ATOM   3709  CA  SER A 596     185.775 224.872 200.515  1.00 36.96           C  
ATOM   3710  C   SER A 596     185.138 226.167 200.068  1.00 36.53           C  
ATOM   3711  O   SER A 596     183.942 226.235 199.797  1.00 38.16           O  
ATOM   3712  CB  SER A 596     186.131 224.034 199.309  1.00 37.36           C  
ATOM   3713  OG  SER A 596     186.916 222.937 199.670  1.00 37.48           O  
ATOM   3714  N   VAL A 597     185.945 227.197 199.974  1.00 36.49           N  
ATOM   3715  CA  VAL A 597     185.457 228.489 199.562  1.00 36.52           C  
ATOM   3716  C   VAL A 597     185.939 228.815 198.170  1.00 36.47           C  
ATOM   3717  O   VAL A 597     187.133 228.766 197.875  1.00 38.09           O  
ATOM   3718  CB  VAL A 597     185.904 229.554 200.561  1.00 36.99           C  
ATOM   3719  CG1 VAL A 597     185.401 230.924 200.140  1.00 37.51           C  
ATOM   3720  CG2 VAL A 597     185.378 229.179 201.930  1.00 37.87           C  
ATOM   3721  N   ILE A 598     184.988 229.116 197.312  1.00 36.56           N  
ATOM   3722  CA  ILE A 598     185.223 229.410 195.917  1.00 36.54           C  
ATOM   3723  C   ILE A 598     185.206 230.894 195.716  1.00 36.08           C  
ATOM   3724  O   ILE A 598     184.189 231.554 195.931  1.00 37.38           O  
ATOM   3725  CB  ILE A 598     184.133 228.749 195.087  1.00 36.36           C  
ATOM   3726  CG1 ILE A 598     184.222 227.256 195.305  1.00 36.16           C  
ATOM   3727  CG2 ILE A 598     184.266 229.127 193.625  1.00 36.66           C  
ATOM   3728  CD1 ILE A 598     183.015 226.511 194.897  1.00 36.37           C  
ATOM   3729  N   THR A 599     186.334 231.446 195.323  1.00 36.94           N  
ATOM   3730  CA  THR A 599     186.406 232.884 195.289  1.00 37.02           C  
ATOM   3731  C   THR A 599     187.204 233.430 194.105  1.00 37.49           C  
ATOM   3732  O   THR A 599     188.203 232.837 193.699  1.00 38.46           O  
ATOM   3733  CB  THR A 599     187.021 233.346 196.626  1.00 37.18           C  
ATOM   3734  OG1 THR A 599     187.070 234.762 196.689  1.00 37.72           O  
ATOM   3735  CG2 THR A 599     188.413 232.800 196.792  1.00 37.45           C  
ATOM   3736  N   PRO A 600     186.771 234.548 193.514  1.00 37.61           N  
ATOM   3737  CA  PRO A 600     187.510 235.342 192.571  1.00 37.84           C  
ATOM   3738  C   PRO A 600     188.547 236.058 193.390  1.00 38.16           C  
ATOM   3739  O   PRO A 600     188.395 236.160 194.601  1.00 38.51           O  
ATOM   3740  CB  PRO A 600     186.448 236.263 191.983  1.00 38.30           C  
ATOM   3741  CG  PRO A 600     185.439 236.407 193.087  1.00 37.86           C  
ATOM   3742  CD  PRO A 600     185.428 235.067 193.796  1.00 37.54           C  
ATOM   3743  N   GLY A 601     189.578 236.585 192.776  1.00 38.74           N  
ATOM   3744  CA  GLY A 601     190.564 237.244 193.610  1.00 39.27           C  
ATOM   3745  C   GLY A 601     189.944 238.437 194.323  1.00 39.57           C  
ATOM   3746  O   GLY A 601     189.105 239.143 193.748  1.00 40.56           O  
ATOM   3747  N   THR A 602     190.430 238.712 195.535  1.00 39.39           N  
ATOM   3748  CA  THR A 602     189.946 239.843 196.341  1.00 39.63           C  
ATOM   3749  C   THR A 602     190.291 241.219 195.742  1.00 39.88           C  
ATOM   3750  O   THR A 602     189.788 242.241 196.206  1.00 39.73           O  
ATOM   3751  CB  THR A 602     190.457 239.744 197.790  1.00 39.72           C  
ATOM   3752  OG1 THR A 602     191.889 239.685 197.805  1.00 40.21           O  
ATOM   3753  CG2 THR A 602     189.895 238.503 198.426  1.00 39.69           C  
ATOM   3754  N   ASN A 603     191.113 241.228 194.675  1.00 40.05           N  
ATOM   3755  CA  ASN A 603     191.415 242.406 193.865  1.00 40.48           C  
ATOM   3756  C   ASN A 603     190.161 242.864 193.088  1.00 40.76           C  
ATOM   3757  O   ASN A 603     190.019 244.050 192.783  1.00 40.93           O  
ATOM   3758  CB  ASN A 603     192.601 242.109 192.924  1.00 41.09           C  
ATOM   3759  CG  ASN A 603     192.652 242.982 191.644  1.00 41.54           C  
ATOM   3760  OD1 ASN A 603     192.095 242.585 190.608  1.00 41.62           O  
ATOM   3761  ND2 ASN A 603     193.296 244.137 191.721  1.00 42.16           N  
ATOM   3762  N   THR A 604     189.240 241.919 192.777  1.00 39.65           N  
ATOM   3763  CA  THR A 604     188.016 242.169 192.015  1.00 40.00           C  
ATOM   3764  C   THR A 604     186.767 242.131 192.883  1.00 39.57           C  
ATOM   3765  O   THR A 604     185.888 242.984 192.745  1.00 39.53           O  
ATOM   3766  CB  THR A 604     187.859 241.130 190.887  1.00 40.03           C  
ATOM   3767  OG1 THR A 604     188.959 241.244 189.977  1.00 40.33           O  
ATOM   3768  CG2 THR A 604     186.545 241.340 190.133  1.00 39.97           C  
ATOM   3769  N   SER A 605     186.659 241.134 193.754  1.00 38.98           N  
ATOM   3770  CA  SER A 605     185.443 241.003 194.545  1.00 38.61           C  
ATOM   3771  C   SER A 605     185.634 240.222 195.834  1.00 37.62           C  
ATOM   3772  O   SER A 605     186.424 239.285 195.895  1.00 38.63           O  
ATOM   3773  CB  SER A 605     184.366 240.334 193.729  1.00 38.12           C  
ATOM   3774  OG  SER A 605     183.197 240.203 194.478  1.00 37.91           O  
ATOM   3775  N   ASN A 606     184.873 240.589 196.860  1.00 37.49           N  
ATOM   3776  CA  ASN A 606     184.885 239.855 198.121  1.00 37.21           C  
ATOM   3777  C   ASN A 606     183.719 238.879 198.216  1.00 37.05           C  
ATOM   3778  O   ASN A 606     183.470 238.294 199.269  1.00 37.07           O  
ATOM   3779  CB  ASN A 606     184.866 240.807 199.296  1.00 37.32           C  
ATOM   3780  CG  ASN A 606     186.153 241.546 199.456  1.00 38.19           C  
ATOM   3781  OD1 ASN A 606     187.239 240.973 199.321  1.00 38.84           O  
ATOM   3782  ND2 ASN A 606     186.059 242.816 199.743  1.00 37.33           N  
ATOM   3783  N   GLU A 607     182.994 238.714 197.120  1.00 36.91           N  
ATOM   3784  CA  GLU A 607     181.876 237.788 197.089  1.00 36.75           C  
ATOM   3785  C   GLU A 607     182.390 236.372 196.964  1.00 36.67           C  
ATOM   3786  O   GLU A 607     183.299 236.109 196.180  1.00 37.14           O  
ATOM   3787  CB  GLU A 607     180.949 238.121 195.930  1.00 36.57           C  
ATOM   3788  CG  GLU A 607     179.703 237.280 195.856  1.00 36.65           C  
ATOM   3789  CD  GLU A 607     178.793 237.754 194.790  1.00 36.96           C  
ATOM   3790  OE1 GLU A 607     179.134 238.707 194.144  1.00 37.34           O  
ATOM   3791  OE2 GLU A 607     177.752 237.177 194.614  1.00 36.45           O  
ATOM   3792  N   VAL A 608     181.829 235.454 197.739  1.00 36.38           N  
ATOM   3793  CA  VAL A 608     182.261 234.068 197.648  1.00 36.43           C  
ATOM   3794  C   VAL A 608     181.102 233.094 197.573  1.00 36.51           C  
ATOM   3795  O   VAL A 608     179.993 233.397 198.007  1.00 36.94           O  
ATOM   3796  CB  VAL A 608     183.136 233.699 198.850  1.00 36.23           C  
ATOM   3797  CG1 VAL A 608     184.330 234.591 198.897  1.00 37.14           C  
ATOM   3798  CG2 VAL A 608     182.354 233.815 200.130  1.00 37.19           C  
ATOM   3799  N   ALA A 609     181.390 231.895 197.086  1.00 36.54           N  
ATOM   3800  CA  ALA A 609     180.447 230.786 197.114  1.00 36.63           C  
ATOM   3801  C   ALA A 609     181.049 229.687 197.966  1.00 36.20           C  
ATOM   3802  O   ALA A 609     182.268 229.540 198.018  1.00 38.00           O  
ATOM   3803  CB  ALA A 609     180.142 230.288 195.716  1.00 37.21           C  
ATOM   3804  N   VAL A 610     180.221 228.920 198.649  1.00 36.93           N  
ATOM   3805  CA  VAL A 610     180.766 227.895 199.524  1.00 36.87           C  
ATOM   3806  C   VAL A 610     180.318 226.501 199.167  1.00 36.61           C  
ATOM   3807  O   VAL A 610     179.133 226.233 198.987  1.00 38.31           O  
ATOM   3808  CB  VAL A 610     180.399 228.194 200.979  1.00 37.37           C  
ATOM   3809  CG1 VAL A 610     180.939 227.107 201.890  1.00 38.23           C  
ATOM   3810  CG2 VAL A 610     180.976 229.533 201.367  1.00 37.58           C  
ATOM   3811  N   LEU A 611     181.283 225.610 199.063  1.00 37.07           N  
ATOM   3812  CA  LEU A 611     181.016 224.221 198.771  1.00 37.22           C  
ATOM   3813  C   LEU A 611     181.127 223.345 199.998  1.00 39.53           C  
ATOM   3814  O   LEU A 611     182.176 223.274 200.641  1.00 37.19           O  
ATOM   3815  CB  LEU A 611     182.002 223.694 197.738  1.00 37.07           C  
ATOM   3816  CG  LEU A 611     181.911 222.186 197.436  1.00 37.79           C  
ATOM   3817  CD1 LEU A 611     180.602 221.870 196.715  1.00 37.98           C  
ATOM   3818  CD2 LEU A 611     183.087 221.796 196.634  1.00 37.47           C  
ATOM   3819  N   TYR A 612     180.066 222.621 200.281  1.00 37.85           N  
ATOM   3820  CA  TYR A 612     180.086 221.652 201.354  1.00 38.30           C  
ATOM   3821  C   TYR A 612     180.337 220.308 200.710  1.00 40.71           C  
ATOM   3822  O   TYR A 612     179.510 219.810 199.946  1.00 37.07           O  
ATOM   3823  CB  TYR A 612     178.782 221.708 202.126  1.00 38.92           C  
ATOM   3824  CG  TYR A 612     178.632 223.004 202.847  1.00 39.16           C  
ATOM   3825  CD1 TYR A 612     178.182 224.118 202.176  1.00 38.68           C  
ATOM   3826  CD2 TYR A 612     178.956 223.085 204.177  1.00 39.87           C  
ATOM   3827  CE1 TYR A 612     178.065 225.311 202.839  1.00 38.53           C  
ATOM   3828  CE2 TYR A 612     178.835 224.277 204.841  1.00 39.87           C  
ATOM   3829  CZ  TYR A 612     178.394 225.387 204.175  1.00 39.18           C  
ATOM   3830  OH  TYR A 612     178.275 226.581 204.837  1.00 38.94           O  
ATOM   3831  N   GLN A 613     181.509 219.755 200.965  1.00 38.18           N  
ATOM   3832  CA  GLN A 613     181.960 218.581 200.248  1.00 38.57           C  
ATOM   3833  C   GLN A 613     181.249 217.317 200.655  1.00 38.75           C  
ATOM   3834  O   GLN A 613     181.105 217.028 201.838  1.00 39.68           O  
ATOM   3835  CB  GLN A 613     183.449 218.365 200.489  1.00 38.76           C  
ATOM   3836  CG  GLN A 613     184.368 219.436 199.954  1.00 38.47           C  
ATOM   3837  CD  GLN A 613     185.781 219.167 200.406  1.00 38.33           C  
ATOM   3838  OE1 GLN A 613     186.047 218.087 200.942  1.00 37.68           O  
ATOM   3839  NE2 GLN A 613     186.686 220.114 200.224  1.00 37.94           N  
ATOM   3840  N   ASP A 614     180.885 216.528 199.658  1.00 39.74           N  
ATOM   3841  CA  ASP A 614     180.320 215.197 199.858  1.00 39.76           C  
ATOM   3842  C   ASP A 614     179.095 215.175 200.768  1.00 39.96           C  
ATOM   3843  O   ASP A 614     178.937 214.264 201.579  1.00 40.19           O  
ATOM   3844  CB  ASP A 614     181.394 214.268 200.436  1.00 39.98           C  
ATOM   3845  N   VAL A 615     178.220 216.158 200.630  1.00 40.07           N  
ATOM   3846  CA  VAL A 615     176.981 216.172 201.391  1.00 40.24           C  
ATOM   3847  C   VAL A 615     175.814 216.480 200.467  1.00 40.29           C  
ATOM   3848  O   VAL A 615     176.015 217.034 199.384  1.00 40.78           O  
ATOM   3849  CB  VAL A 615     177.006 217.217 202.527  1.00 40.14           C  
ATOM   3850  CG1 VAL A 615     178.119 216.919 203.505  1.00 40.21           C  
ATOM   3851  CG2 VAL A 615     177.165 218.580 201.934  1.00 40.16           C  
ATOM   3852  N   ASN A 616     174.608 216.159 200.937  1.00 41.04           N  
ATOM   3853  CA  ASN A 616     173.349 216.520 200.289  1.00 41.21           C  
ATOM   3854  C   ASN A 616     172.914 217.898 200.802  1.00 40.92           C  
ATOM   3855  O   ASN A 616     173.250 218.284 201.916  1.00 41.30           O  
ATOM   3856  CB  ASN A 616     172.292 215.450 200.583  1.00 41.34           C  
ATOM   3857  CG  ASN A 616     171.038 215.517 199.697  1.00 42.57           C  
ATOM   3858  OD1 ASN A 616     170.848 216.450 198.897  1.00 42.16           O  
ATOM   3859  ND2 ASN A 616     170.181 214.511 199.850  1.00 41.65           N  
ATOM   3860  N   CYS A 617     172.121 218.618 199.992  1.00 40.96           N  
ATOM   3861  CA  CYS A 617     171.600 219.936 200.386  1.00 42.20           C  
ATOM   3862  C   CYS A 617     170.414 219.776 201.330  1.00 41.86           C  
ATOM   3863  O   CYS A 617     169.258 220.020 200.972  1.00 42.18           O  
ATOM   3864  CB  CYS A 617     171.209 220.763 199.148  1.00 42.15           C  
ATOM   3865  SG  CYS A 617     172.599 221.166 198.041  1.00 40.86           S  
ATOM   3866  N   THR A 618     170.741 219.315 202.544  1.00 42.34           N  
ATOM   3867  CA  THR A 618     169.834 218.996 203.635  1.00 42.18           C  
ATOM   3868  C   THR A 618     170.334 219.563 204.955  1.00 42.70           C  
ATOM   3869  O   THR A 618     169.892 220.628 205.381  1.00 42.21           O  
ATOM   3870  CB  THR A 618     169.629 217.474 203.737  1.00 42.19           C  
ATOM   3871  OG1 THR A 618     170.893 216.829 203.858  1.00 42.31           O  
ATOM   3872  CG2 THR A 618     168.939 216.949 202.489  1.00 41.46           C  
ATOM   3873  N   GLU A 619     171.266 218.867 205.610  1.00 42.69           N  
ATOM   3874  CA  GLU A 619     171.734 219.325 206.927  1.00 42.90           C  
ATOM   3875  C   GLU A 619     172.330 220.742 206.948  1.00 43.07           C  
ATOM   3876  O   GLU A 619     172.203 221.441 207.955  1.00 43.38           O  
ATOM   3877  CB  GLU A 619     172.767 218.362 207.522  1.00 44.16           C  
ATOM   3878  N   VAL A 620     172.972 221.161 205.850  1.00 43.07           N  
ATOM   3879  CA  VAL A 620     173.597 222.476 205.704  1.00 42.39           C  
ATOM   3880  C   VAL A 620     172.514 223.562 205.676  1.00 41.91           C  
ATOM   3881  O   VAL A 620     172.759 224.719 206.034  1.00 41.42           O  
ATOM   3882  CB  VAL A 620     174.474 222.499 204.396  1.00 41.69           C  
ATOM   3883  CG1 VAL A 620     175.075 223.913 204.123  1.00 40.73           C  
ATOM   3884  CG2 VAL A 620     175.652 221.452 204.522  1.00 41.97           C  
ATOM   3885  N   ASN A 641     169.283 229.840 195.903  1.00 38.47           N  
ATOM   3886  CA  ASN A 641     170.531 229.912 195.147  1.00 37.68           C  
ATOM   3887  C   ASN A 641     171.475 228.764 195.571  1.00 37.49           C  
ATOM   3888  O   ASN A 641     172.634 228.990 195.948  1.00 37.69           O  
ATOM   3889  CB  ASN A 641     171.163 231.313 195.315  1.00 37.62           C  
ATOM   3890  CG  ASN A 641     172.294 231.656 194.289  1.00 37.75           C  
ATOM   3891  OD1 ASN A 641     172.324 231.129 193.167  1.00 37.64           O  
ATOM   3892  ND2 ASN A 641     173.201 232.557 194.680  1.00 38.35           N  
ATOM   3893  N   VAL A 642     170.946 227.526 195.518  1.00 37.53           N  
ATOM   3894  CA  VAL A 642     171.647 226.300 195.901  1.00 37.38           C  
ATOM   3895  C   VAL A 642     171.704 225.313 194.743  1.00 37.60           C  
ATOM   3896  O   VAL A 642     170.681 224.964 194.156  1.00 37.82           O  
ATOM   3897  CB  VAL A 642     170.942 225.647 197.098  1.00 37.73           C  
ATOM   3898  CG1 VAL A 642     171.657 224.383 197.488  1.00 38.38           C  
ATOM   3899  CG2 VAL A 642     170.905 226.630 198.250  1.00 37.76           C  
ATOM   3900  N   PHE A 643     172.908 224.863 194.428  1.00 37.39           N  
ATOM   3901  CA  PHE A 643     173.144 223.936 193.335  1.00 37.14           C  
ATOM   3902  C   PHE A 643     173.740 222.621 193.839  1.00 37.28           C  
ATOM   3903  O   PHE A 643     174.842 222.589 194.383  1.00 38.33           O  
ATOM   3904  CB  PHE A 643     174.073 224.609 192.312  1.00 36.86           C  
ATOM   3905  CG  PHE A 643     174.447 223.801 191.092  1.00 36.89           C  
ATOM   3906  CD1 PHE A 643     173.663 222.766 190.615  1.00 36.73           C  
ATOM   3907  CD2 PHE A 643     175.607 224.107 190.406  1.00 36.46           C  
ATOM   3908  CE1 PHE A 643     174.040 222.060 189.501  1.00 36.58           C  
ATOM   3909  CE2 PHE A 643     175.982 223.405 189.290  1.00 36.03           C  
ATOM   3910  CZ  PHE A 643     175.198 222.378 188.839  1.00 35.98           C  
ATOM   3911  N   GLN A 644     173.003 221.530 193.680  1.00 37.38           N  
ATOM   3912  CA  GLN A 644     173.507 220.240 194.136  1.00 37.50           C  
ATOM   3913  C   GLN A 644     174.376 219.631 193.054  1.00 37.42           C  
ATOM   3914  O   GLN A 644     173.913 219.419 191.933  1.00 37.28           O  
ATOM   3915  CB  GLN A 644     172.365 219.267 194.442  1.00 38.19           C  
ATOM   3916  CG  GLN A 644     172.814 217.867 194.938  1.00 38.71           C  
ATOM   3917  CD  GLN A 644     173.301 217.844 196.394  1.00 40.19           C  
ATOM   3918  OE1 GLN A 644     172.478 218.072 197.287  1.00 40.94           O  
ATOM   3919  NE2 GLN A 644     174.588 217.563 196.630  1.00 39.55           N  
ATOM   3920  N   THR A 645     175.619 219.324 193.391  1.00 37.28           N  
ATOM   3921  CA  THR A 645     176.540 218.718 192.448  1.00 37.13           C  
ATOM   3922  C   THR A 645     177.054 217.419 193.040  1.00 37.11           C  
ATOM   3923  O   THR A 645     176.891 217.172 194.232  1.00 37.96           O  
ATOM   3924  CB  THR A 645     177.715 219.663 192.127  1.00 36.47           C  
ATOM   3925  OG1 THR A 645     178.506 219.874 193.298  1.00 37.03           O  
ATOM   3926  CG2 THR A 645     177.186 221.000 191.662  1.00 36.40           C  
ATOM   3927  N   ARG A 646     177.706 216.591 192.238  1.00 36.74           N  
ATOM   3928  CA  ARG A 646     178.219 215.328 192.763  1.00 36.79           C  
ATOM   3929  C   ARG A 646     179.341 215.560 193.764  1.00 36.58           C  
ATOM   3930  O   ARG A 646     179.618 214.718 194.614  1.00 37.12           O  
ATOM   3931  CB  ARG A 646     178.698 214.439 191.639  1.00 36.72           C  
ATOM   3932  N   ALA A 647     179.980 216.714 193.664  1.00 36.51           N  
ATOM   3933  CA  ALA A 647     181.076 217.075 194.545  1.00 36.41           C  
ATOM   3934  C   ALA A 647     180.600 217.527 195.923  1.00 37.88           C  
ATOM   3935  O   ALA A 647     181.414 217.671 196.838  1.00 38.30           O  
ATOM   3936  CB  ALA A 647     181.905 218.181 193.909  1.00 35.31           C  
ATOM   3937  N   GLY A 648     179.306 217.794 196.077  1.00 38.04           N  
ATOM   3938  CA  GLY A 648     178.808 218.349 197.330  1.00 38.01           C  
ATOM   3939  C   GLY A 648     177.692 219.362 197.082  1.00 37.66           C  
ATOM   3940  O   GLY A 648     177.158 219.446 195.974  1.00 39.22           O  
ATOM   3941  N   CYS A 649     177.319 220.117 198.125  1.00 38.72           N  
ATOM   3942  CA  CYS A 649     176.251 221.116 198.042  1.00 38.89           C  
ATOM   3943  C   CYS A 649     176.894 222.502 197.886  1.00 37.54           C  
ATOM   3944  O   CYS A 649     177.598 222.970 198.789  1.00 39.58           O  
ATOM   3945  CB  CYS A 649     175.344 221.072 199.291  1.00 40.27           C  
ATOM   3946  SG  CYS A 649     173.914 222.185 199.214  1.00 40.93           S  
ATOM   3947  N   LEU A 650     176.680 223.143 196.725  1.00 37.58           N  
ATOM   3948  CA  LEU A 650     177.272 224.439 196.395  1.00 37.25           C  
ATOM   3949  C   LEU A 650     176.277 225.559 196.630  1.00 37.09           C  
ATOM   3950  O   LEU A 650     175.227 225.627 195.993  1.00 37.96           O  
ATOM   3951  CB  LEU A 650     177.741 224.423 194.938  1.00 36.98           C  
ATOM   3952  CG  LEU A 650     178.306 225.721 194.377  1.00 36.57           C  
ATOM   3953  CD1 LEU A 650     179.547 226.120 195.133  1.00 37.20           C  
ATOM   3954  CD2 LEU A 650     178.630 225.512 192.918  1.00 37.10           C  
ATOM   3955  N   ILE A 651     176.602 226.436 197.563  1.00 37.11           N  
ATOM   3956  CA  ILE A 651     175.688 227.497 197.939  1.00 36.96           C  
ATOM   3957  C   ILE A 651     176.236 228.879 197.624  1.00 37.08           C  
ATOM   3958  O   ILE A 651     177.346 229.231 198.021  1.00 37.15           O  
ATOM   3959  CB  ILE A 651     175.355 227.395 199.435  1.00 36.97           C  
ATOM   3960  CG1 ILE A 651     174.723 226.017 199.709  1.00 37.91           C  
ATOM   3961  CG2 ILE A 651     174.416 228.527 199.841  1.00 38.07           C  
ATOM   3962  CD1 ILE A 651     174.538 225.685 201.155  1.00 38.97           C  
ATOM   3963  N   GLY A 652     175.441 229.678 196.925  1.00 37.35           N  
ATOM   3964  CA  GLY A 652     175.820 231.049 196.598  1.00 37.49           C  
ATOM   3965  C   GLY A 652     176.178 231.243 195.132  1.00 37.55           C  
ATOM   3966  O   GLY A 652     176.165 232.366 194.632  1.00 37.98           O  
ATOM   3967  N   ALA A 653     176.478 230.160 194.438  1.00 37.13           N  
ATOM   3968  CA  ALA A 653     176.766 230.251 193.016  1.00 36.82           C  
ATOM   3969  C   ALA A 653     175.494 229.961 192.241  1.00 36.88           C  
ATOM   3970  O   ALA A 653     174.746 229.051 192.596  1.00 37.05           O  
ATOM   3971  CB  ALA A 653     177.864 229.287 192.620  1.00 36.81           C  
ATOM   3972  N   GLU A 654     175.261 230.706 191.172  1.00 36.80           N  
ATOM   3973  CA  GLU A 654     174.080 230.474 190.351  1.00 36.36           C  
ATOM   3974  C   GLU A 654     174.307 229.306 189.418  1.00 35.85           C  
ATOM   3975  O   GLU A 654     175.418 229.093 188.947  1.00 36.91           O  
ATOM   3976  CB  GLU A 654     173.734 231.708 189.522  1.00 36.29           C  
ATOM   3977  CG  GLU A 654     173.361 232.935 190.326  1.00 36.67           C  
ATOM   3978  CD  GLU A 654     172.954 234.096 189.457  1.00 37.20           C  
ATOM   3979  OE1 GLU A 654     173.040 233.972 188.257  1.00 36.43           O  
ATOM   3980  OE2 GLU A 654     172.552 235.104 189.992  1.00 36.03           O  
ATOM   3981  N   HIS A 655     173.259 228.569 189.102  1.00 35.80           N  
ATOM   3982  CA  HIS A 655     173.415 227.494 188.134  1.00 35.14           C  
ATOM   3983  C   HIS A 655     173.083 228.011 186.747  1.00 36.02           C  
ATOM   3984  O   HIS A 655     171.985 228.506 186.495  1.00 36.18           O  
ATOM   3985  CB  HIS A 655     172.549 226.284 188.481  1.00 36.12           C  
ATOM   3986  CG  HIS A 655     172.761 225.118 187.561  1.00 36.00           C  
ATOM   3987  ND1 HIS A 655     171.837 224.109 187.423  1.00 36.50           N  
ATOM   3988  CD2 HIS A 655     173.788 224.799 186.736  1.00 36.04           C  
ATOM   3989  CE1 HIS A 655     172.283 223.226 186.551  1.00 36.52           C  
ATOM   3990  NE2 HIS A 655     173.462 223.623 186.122  1.00 36.19           N  
ATOM   3991  N   VAL A 656     174.063 227.945 185.864  1.00 35.65           N  
ATOM   3992  CA  VAL A 656     173.943 228.457 184.511  1.00 35.39           C  
ATOM   3993  C   VAL A 656     173.930 227.313 183.494  1.00 35.44           C  
ATOM   3994  O   VAL A 656     174.770 226.417 183.564  1.00 35.57           O  
ATOM   3995  CB  VAL A 656     175.107 229.438 184.250  1.00 35.21           C  
ATOM   3996  CG1 VAL A 656     175.109 229.943 182.832  1.00 35.11           C  
ATOM   3997  CG2 VAL A 656     174.967 230.602 185.191  1.00 35.87           C  
ATOM   3998  N   ASN A 657     172.961 227.355 182.553  1.00 35.59           N  
ATOM   3999  CA  ASN A 657     172.782 226.353 181.499  1.00 35.53           C  
ATOM   4000  C   ASN A 657     173.943 226.348 180.482  1.00 34.78           C  
ATOM   4001  O   ASN A 657     174.275 225.304 179.927  1.00 34.32           O  
ATOM   4002  CB  ASN A 657     171.451 226.583 180.757  1.00 36.36           C  
ATOM   4003  CG  ASN A 657     170.267 225.745 181.285  1.00 37.07           C  
ATOM   4004  OD1 ASN A 657     170.448 224.682 181.899  1.00 37.04           O  
ATOM   4005  ND2 ASN A 657     169.055 226.234 181.029  1.00 38.00           N  
ATOM   4006  N   ASN A 658     174.545 227.523 180.238  1.00 34.55           N  
ATOM   4007  CA  ASN A 658     175.633 227.698 179.278  1.00 34.09           C  
ATOM   4008  C   ASN A 658     176.952 227.170 179.812  1.00 33.64           C  
ATOM   4009  O   ASN A 658     177.325 227.440 180.951  1.00 34.77           O  
ATOM   4010  CB  ASN A 658     175.772 229.161 178.940  1.00 34.17           C  
ATOM   4011  CG  ASN A 658     174.557 229.696 178.285  1.00 34.65           C  
ATOM   4012  OD1 ASN A 658     173.922 229.020 177.469  1.00 35.36           O  
ATOM   4013  ND2 ASN A 658     174.202 230.906 178.627  1.00 34.12           N  
ATOM   4014  N   SER A 659     177.669 226.437 178.977  1.00 33.55           N  
ATOM   4015  CA  SER A 659     178.988 225.961 179.349  1.00 32.94           C  
ATOM   4016  C   SER A 659     180.023 226.993 178.947  1.00 32.83           C  
ATOM   4017  O   SER A 659     179.793 227.782 178.030  1.00 33.39           O  
ATOM   4018  CB  SER A 659     179.275 224.635 178.675  1.00 32.56           C  
ATOM   4019  OG  SER A 659     179.345 224.779 177.282  1.00 33.98           O  
ATOM   4020  N   TYR A 660     181.173 226.964 179.600  1.00 32.77           N  
ATOM   4021  CA  TYR A 660     182.263 227.875 179.280  1.00 32.98           C  
ATOM   4022  C   TYR A 660     183.583 227.183 179.540  1.00 33.62           C  
ATOM   4023  O   TYR A 660     183.612 226.046 180.012  1.00 33.15           O  
ATOM   4024  CB  TYR A 660     182.202 229.139 180.149  1.00 33.78           C  
ATOM   4025  CG  TYR A 660     180.905 229.913 180.101  1.00 33.78           C  
ATOM   4026  CD1 TYR A 660     179.893 229.603 180.983  1.00 34.70           C  
ATOM   4027  CD2 TYR A 660     180.733 230.934 179.194  1.00 34.24           C  
ATOM   4028  CE1 TYR A 660     178.715 230.296 180.961  1.00 34.36           C  
ATOM   4029  CE2 TYR A 660     179.545 231.634 179.171  1.00 34.57           C  
ATOM   4030  CZ  TYR A 660     178.539 231.315 180.052  1.00 34.46           C  
ATOM   4031  OH  TYR A 660     177.354 232.013 180.027  1.00 34.46           O  
ATOM   4032  N   GLU A 661     184.677 227.860 179.249  1.00 33.98           N  
ATOM   4033  CA  GLU A 661     185.981 227.322 179.586  1.00 34.37           C  
ATOM   4034  C   GLU A 661     186.086 227.315 181.106  1.00 34.33           C  
ATOM   4035  O   GLU A 661     185.593 228.243 181.748  1.00 34.74           O  
ATOM   4036  CB  GLU A 661     187.080 228.174 178.959  1.00 35.19           C  
ATOM   4037  N   CYS A 662     186.706 226.277 181.688  1.00 33.97           N  
ATOM   4038  CA  CYS A 662     186.837 226.153 183.141  1.00 34.19           C  
ATOM   4039  C   CYS A 662     187.774 227.225 183.708  1.00 34.87           C  
ATOM   4040  O   CYS A 662     188.862 227.455 183.177  1.00 35.49           O  
ATOM   4041  CB  CYS A 662     187.359 224.760 183.524  1.00 34.51           C  
ATOM   4042  SG  CYS A 662     187.407 224.445 185.312  1.00 33.90           S  
ATOM   4043  N   ASP A 663     187.342 227.869 184.807  1.00 34.86           N  
ATOM   4044  CA  ASP A 663     188.098 228.903 185.515  1.00 35.15           C  
ATOM   4045  C   ASP A 663     188.509 228.351 186.879  1.00 35.09           C  
ATOM   4046  O   ASP A 663     189.650 227.924 187.056  1.00 35.07           O  
ATOM   4047  CB  ASP A 663     187.270 230.185 185.646  1.00 35.63           C  
ATOM   4048  CG  ASP A 663     188.086 231.376 186.109  1.00 36.16           C  
ATOM   4049  OD1 ASP A 663     189.279 231.354 185.926  1.00 36.07           O  
ATOM   4050  OD2 ASP A 663     187.519 232.309 186.628  1.00 36.43           O  
ATOM   4051  N   ILE A 664     187.577 228.308 187.833  1.00 34.75           N  
ATOM   4052  CA  ILE A 664     187.867 227.686 189.114  1.00 34.18           C  
ATOM   4053  C   ILE A 664     187.195 226.322 189.151  1.00 33.57           C  
ATOM   4054  O   ILE A 664     185.973 226.254 189.225  1.00 34.36           O  
ATOM   4055  CB  ILE A 664     187.301 228.501 190.286  1.00 34.60           C  
ATOM   4056  CG1 ILE A 664     187.859 229.918 190.274  1.00 35.67           C  
ATOM   4057  CG2 ILE A 664     187.640 227.783 191.597  1.00 35.13           C  
ATOM   4058  CD1 ILE A 664     187.147 230.856 191.236  1.00 36.43           C  
ATOM   4059  N   PRO A 665     187.934 225.220 189.108  1.00 33.07           N  
ATOM   4060  CA  PRO A 665     187.388 223.889 189.057  1.00 32.28           C  
ATOM   4061  C   PRO A 665     186.791 223.523 190.390  1.00 32.25           C  
ATOM   4062  O   PRO A 665     187.386 223.808 191.426  1.00 33.26           O  
ATOM   4063  CB  PRO A 665     188.617 223.050 188.741  1.00 32.12           C  
ATOM   4064  CG  PRO A 665     189.766 223.832 189.321  1.00 33.28           C  
ATOM   4065  CD  PRO A 665     189.380 225.288 189.164  1.00 33.52           C  
ATOM   4066  N   ILE A 666     185.663 222.834 190.374  1.00 32.14           N  
ATOM   4067  CA  ILE A 666     185.087 222.312 191.594  1.00 31.75           C  
ATOM   4068  C   ILE A 666     185.231 220.808 191.648  1.00 31.64           C  
ATOM   4069  O   ILE A 666     185.700 220.249 192.638  1.00 33.00           O  
ATOM   4070  CB  ILE A 666     183.618 222.712 191.723  1.00 31.90           C  
ATOM   4071  CG1 ILE A 666     183.536 224.224 191.850  1.00 32.67           C  
ATOM   4072  CG2 ILE A 666     183.008 222.017 192.890  1.00 32.94           C  
ATOM   4073  CD1 ILE A 666     182.148 224.765 191.796  1.00 33.66           C  
ATOM   4074  N   GLY A 667     184.820 220.154 190.576  1.00 31.23           N  
ATOM   4075  CA  GLY A 667     184.876 218.705 190.505  1.00 30.13           C  
ATOM   4076  C   GLY A 667     183.629 218.143 189.855  1.00 30.33           C  
ATOM   4077  O   GLY A 667     182.595 218.805 189.798  1.00 31.45           O  
ATOM   4078  N   ALA A 668     183.724 216.915 189.372  1.00 29.62           N  
ATOM   4079  CA  ALA A 668     182.608 216.217 188.761  1.00 29.91           C  
ATOM   4080  C   ALA A 668     182.020 216.981 187.587  1.00 30.41           C  
ATOM   4081  O   ALA A 668     180.805 217.005 187.396  1.00 31.29           O  
ATOM   4082  CB  ALA A 668     181.529 215.955 189.790  1.00 32.19           C  
ATOM   4083  N   GLY A 669     182.884 217.600 186.795  1.00 30.36           N  
ATOM   4084  CA  GLY A 669     182.479 218.300 185.592  1.00 30.61           C  
ATOM   4085  C   GLY A 669     182.028 219.729 185.817  1.00 31.35           C  
ATOM   4086  O   GLY A 669     181.702 220.427 184.855  1.00 32.32           O  
ATOM   4087  N   ILE A 670     181.996 220.170 187.065  1.00 31.40           N  
ATOM   4088  CA  ILE A 670     181.531 221.513 187.364  1.00 31.47           C  
ATOM   4089  C   ILE A 670     182.687 222.460 187.683  1.00 31.70           C  
ATOM   4090  O   ILE A 670     183.597 222.117 188.450  1.00 32.55           O  
ATOM   4091  CB  ILE A 670     180.531 221.498 188.541  1.00 32.01           C  
ATOM   4092  CG1 ILE A 670     179.358 220.528 188.251  1.00 32.46           C  
ATOM   4093  CG2 ILE A 670     180.003 222.908 188.820  1.00 33.24           C  
ATOM   4094  CD1 ILE A 670     178.539 220.844 187.010  1.00 32.97           C  
ATOM   4095  N   CYS A 671     182.644 223.649 187.065  1.00 32.26           N  
ATOM   4096  CA  CYS A 671     183.570 224.758 187.287  1.00 32.64           C  
ATOM   4097  C   CYS A 671     182.750 225.995 187.649  1.00 34.66           C  
ATOM   4098  O   CYS A 671     181.565 226.083 187.306  1.00 34.57           O  
ATOM   4099  CB  CYS A 671     184.459 225.030 186.055  1.00 33.26           C  
ATOM   4100  SG  CYS A 671     185.562 223.665 185.640  1.00 33.84           S  
ATOM   4101  N   ALA A 672     183.386 226.954 188.335  1.00 33.62           N  
ATOM   4102  CA  ALA A 672     182.779 228.227 188.712  1.00 34.52           C  
ATOM   4103  C   ALA A 672     183.606 229.392 188.214  1.00 34.68           C  
ATOM   4104  O   ALA A 672     184.812 229.278 187.996  1.00 35.70           O  
ATOM   4105  CB  ALA A 672     182.621 228.310 190.212  1.00 35.17           C  
ATOM   4106  N   SER A 673     182.943 230.520 188.029  1.00 35.50           N  
ATOM   4107  CA  SER A 673     183.615 231.737 187.599  1.00 35.94           C  
ATOM   4108  C   SER A 673     182.847 232.967 188.035  1.00 36.31           C  
ATOM   4109  O   SER A 673     181.690 232.880 188.446  1.00 37.27           O  
ATOM   4110  CB  SER A 673     183.755 231.751 186.102  1.00 36.35           C  
ATOM   4111  OG  SER A 673     182.506 231.874 185.513  1.00 36.62           O  
ATOM   4112  N   TYR A 674     183.488 234.122 187.947  1.00 36.71           N  
ATOM   4113  CA  TYR A 674     182.834 235.373 188.293  1.00 36.85           C  
ATOM   4114  C   TYR A 674     182.569 236.175 187.028  1.00 37.12           C  
ATOM   4115  O   TYR A 674     183.500 236.533 186.305  1.00 37.17           O  
ATOM   4116  CB  TYR A 674     183.704 236.133 189.284  1.00 37.25           C  
ATOM   4117  CG  TYR A 674     183.115 237.392 189.817  1.00 37.40           C  
ATOM   4118  CD1 TYR A 674     182.071 237.331 190.713  1.00 37.63           C  
ATOM   4119  CD2 TYR A 674     183.632 238.604 189.437  1.00 37.96           C  
ATOM   4120  CE1 TYR A 674     181.540 238.484 191.228  1.00 37.60           C  
ATOM   4121  CE2 TYR A 674     183.106 239.756 189.948  1.00 38.14           C  
ATOM   4122  CZ  TYR A 674     182.066 239.702 190.843  1.00 38.08           C  
ATOM   4123  OH  TYR A 674     181.537 240.866 191.347  1.00 38.37           O  
ATOM   4124  N   GLN A 675     181.291 236.404 186.734  1.00 37.11           N  
ATOM   4125  CA  GLN A 675     180.889 237.071 185.497  1.00 37.53           C  
ATOM   4126  C   GLN A 675     179.754 238.082 185.688  1.00 37.76           C  
ATOM   4127  O   GLN A 675     178.949 237.949 186.614  1.00 37.55           O  
ATOM   4128  CB  GLN A 675     180.471 236.039 184.435  1.00 37.46           C  
ATOM   4129  CG  GLN A 675     181.605 235.163 183.913  1.00 37.44           C  
ATOM   4130  CD  GLN A 675     181.168 234.261 182.753  1.00 37.23           C  
ATOM   4131  OE1 GLN A 675     181.359 233.044 182.778  1.00 36.72           O  
ATOM   4132  NE2 GLN A 675     180.576 234.866 181.727  1.00 35.82           N  
ATOM   4133  N   THR A 676     179.680 239.071 184.773  1.00 38.02           N  
ATOM   4134  CA  THR A 676     178.604 240.064 184.685  1.00 38.25           C  
ATOM   4135  C   THR A 676     177.286 239.389 184.273  1.00 38.77           C  
ATOM   4136  O   THR A 676     177.128 238.931 183.138  1.00 38.59           O  
ATOM   4137  CB  THR A 676     178.996 241.208 183.692  1.00 38.67           C  
ATOM   4138  OG1 THR A 676     180.209 241.827 184.146  1.00 38.37           O  
ATOM   4139  CG2 THR A 676     177.896 242.319 183.556  1.00 38.63           C  
ATOM   4140  N   GLN A 690     177.198 241.625 188.595  1.00 37.51           N  
ATOM   4141  CA  GLN A 690     178.119 240.497 188.617  1.00 37.71           C  
ATOM   4142  C   GLN A 690     177.740 239.521 189.729  1.00 37.50           C  
ATOM   4143  O   GLN A 690     177.166 239.922 190.747  1.00 37.54           O  
ATOM   4144  CB  GLN A 690     179.584 240.967 188.815  1.00 37.97           C  
ATOM   4145  CG  GLN A 690     180.199 241.841 187.676  1.00 38.11           C  
ATOM   4146  CD  GLN A 690     181.675 242.310 187.976  1.00 38.27           C  
ATOM   4147  OE1 GLN A 690     182.020 242.641 189.128  1.00 38.30           O  
ATOM   4148  NE2 GLN A 690     182.547 242.331 186.919  1.00 37.98           N  
ATOM   4149  N   SER A 691     178.070 238.236 189.523  1.00 37.37           N  
ATOM   4150  CA  SER A 691     177.838 237.158 190.489  1.00 36.94           C  
ATOM   4151  C   SER A 691     178.736 235.970 190.204  1.00 37.06           C  
ATOM   4152  O   SER A 691     179.362 235.884 189.144  1.00 37.71           O  
ATOM   4153  CB  SER A 691     176.394 236.701 190.449  1.00 36.79           C  
ATOM   4154  OG  SER A 691     176.108 236.109 189.227  1.00 36.75           O  
ATOM   4155  N   ILE A 692     178.787 235.043 191.148  1.00 36.69           N  
ATOM   4156  CA  ILE A 692     179.502 233.798 190.933  1.00 36.43           C  
ATOM   4157  C   ILE A 692     178.550 232.791 190.338  1.00 36.60           C  
ATOM   4158  O   ILE A 692     177.429 232.625 190.822  1.00 37.53           O  
ATOM   4159  CB  ILE A 692     180.113 233.248 192.229  1.00 36.76           C  
ATOM   4160  CG1 ILE A 692     181.141 234.240 192.754  1.00 36.82           C  
ATOM   4161  CG2 ILE A 692     180.756 231.877 191.963  1.00 36.73           C  
ATOM   4162  CD1 ILE A 692     181.611 233.962 194.148  1.00 37.17           C  
ATOM   4163  N   ILE A 693     178.988 232.141 189.279  1.00 36.36           N  
ATOM   4164  CA  ILE A 693     178.164 231.161 188.614  1.00 35.57           C  
ATOM   4165  C   ILE A 693     178.876 229.836 188.558  1.00 36.00           C  
ATOM   4166  O   ILE A 693     180.102 229.776 188.627  1.00 36.36           O  
ATOM   4167  CB  ILE A 693     177.826 231.599 187.184  1.00 36.06           C  
ATOM   4168  CG1 ILE A 693     179.110 231.692 186.343  1.00 36.51           C  
ATOM   4169  CG2 ILE A 693     177.106 232.947 187.219  1.00 36.54           C  
ATOM   4170  CD1 ILE A 693     178.879 231.879 184.864  1.00 36.47           C  
ATOM   4171  N   ALA A 694     178.104 228.784 188.378  1.00 35.45           N  
ATOM   4172  CA  ALA A 694     178.624 227.446 188.219  1.00 34.97           C  
ATOM   4173  C   ALA A 694     177.960 226.794 187.025  1.00 34.47           C  
ATOM   4174  O   ALA A 694     176.780 227.017 186.750  1.00 36.93           O  
ATOM   4175  CB  ALA A 694     178.394 226.644 189.479  1.00 35.58           C  
ATOM   4176  N   TYR A 695     178.729 225.995 186.315  1.00 34.36           N  
ATOM   4177  CA  TYR A 695     178.268 225.370 185.090  1.00 33.69           C  
ATOM   4178  C   TYR A 695     179.055 224.130 184.752  1.00 34.24           C  
ATOM   4179  O   TYR A 695     180.165 223.930 185.248  1.00 33.20           O  
ATOM   4180  CB  TYR A 695     178.408 226.371 183.955  1.00 33.88           C  
ATOM   4181  CG  TYR A 695     179.781 226.967 183.942  1.00 33.17           C  
ATOM   4182  CD1 TYR A 695     180.833 226.346 183.306  1.00 33.68           C  
ATOM   4183  CD2 TYR A 695     179.982 228.143 184.592  1.00 34.33           C  
ATOM   4184  CE1 TYR A 695     182.082 226.909 183.342  1.00 33.33           C  
ATOM   4185  CE2 TYR A 695     181.215 228.702 184.623  1.00 35.37           C  
ATOM   4186  CZ  TYR A 695     182.262 228.094 184.009  1.00 33.62           C  
ATOM   4187  OH  TYR A 695     183.496 228.673 184.053  1.00 34.30           O  
ATOM   4188  N   THR A 696     178.510 223.307 183.872  1.00 32.83           N  
ATOM   4189  CA  THR A 696     179.291 222.194 183.384  1.00 32.05           C  
ATOM   4190  C   THR A 696     180.292 222.759 182.407  1.00 31.84           C  
ATOM   4191  O   THR A 696     179.930 223.533 181.523  1.00 32.84           O  
ATOM   4192  CB  THR A 696     178.418 221.122 182.723  1.00 32.05           C  
ATOM   4193  OG1 THR A 696     177.464 220.638 183.675  1.00 32.21           O  
ATOM   4194  CG2 THR A 696     179.275 219.963 182.237  1.00 32.48           C  
ATOM   4195  N   MET A 697     181.552 222.412 182.581  1.00 31.55           N  
ATOM   4196  CA  MET A 697     182.596 222.981 181.740  1.00 30.87           C  
ATOM   4197  C   MET A 697     182.540 222.462 180.324  1.00 30.84           C  
ATOM   4198  O   MET A 697     182.160 221.316 180.082  1.00 30.47           O  
ATOM   4199  CB  MET A 697     183.968 222.720 182.331  1.00 31.24           C  
ATOM   4200  CG  MET A 697     184.359 221.276 182.374  1.00 30.69           C  
ATOM   4201  SD  MET A 697     186.000 221.009 183.038  1.00 31.39           S  
ATOM   4202  CE  MET A 697     187.002 221.349 181.604  1.00 30.38           C  
ATOM   4203  N   SER A 698     182.932 223.316 179.392  1.00 31.01           N  
ATOM   4204  CA  SER A 698     183.047 222.944 177.997  1.00 29.94           C  
ATOM   4205  C   SER A 698     184.361 222.230 177.762  1.00 29.12           C  
ATOM   4206  O   SER A 698     185.375 222.569 178.370  1.00 29.39           O  
ATOM   4207  CB  SER A 698     182.984 224.159 177.106  1.00 30.68           C  
ATOM   4208  OG  SER A 698     183.169 223.790 175.770  1.00 30.10           O  
ATOM   4209  N   LEU A 699     184.364 221.253 176.867  1.00 28.20           N  
ATOM   4210  CA  LEU A 699     185.596 220.545 176.557  1.00 27.37           C  
ATOM   4211  C   LEU A 699     186.258 221.130 175.326  1.00 27.13           C  
ATOM   4212  O   LEU A 699     187.294 220.643 174.879  1.00 26.61           O  
ATOM   4213  CB  LEU A 699     185.319 219.069 176.302  1.00 26.63           C  
ATOM   4214  CG  LEU A 699     184.637 218.303 177.412  1.00 26.81           C  
ATOM   4215  CD1 LEU A 699     184.471 216.883 176.964  1.00 26.20           C  
ATOM   4216  CD2 LEU A 699     185.436 218.375 178.681  1.00 27.25           C  
ATOM   4217  N   GLY A 700     185.641 222.160 174.766  1.00 27.45           N  
ATOM   4218  CA  GLY A 700     186.126 222.773 173.542  1.00 26.77           C  
ATOM   4219  C   GLY A 700     184.996 222.917 172.538  1.00 26.18           C  
ATOM   4220  O   GLY A 700     183.914 222.351 172.712  1.00 26.22           O  
ATOM   4221  N   ALA A 701     185.236 223.705 171.500  1.00 25.65           N  
ATOM   4222  CA  ALA A 701     184.235 223.924 170.468  1.00 25.68           C  
ATOM   4223  C   ALA A 701     184.031 222.662 169.665  1.00 24.83           C  
ATOM   4224  O   ALA A 701     184.986 221.935 169.403  1.00 25.66           O  
ATOM   4225  CB  ALA A 701     184.658 225.050 169.544  1.00 26.57           C  
ATOM   4226  N   GLU A 702     182.802 222.423 169.242  1.00 24.99           N  
ATOM   4227  CA  GLU A 702     182.519 221.292 168.374  1.00 24.79           C  
ATOM   4228  C   GLU A 702     182.879 221.622 166.938  1.00 24.62           C  
ATOM   4229  O   GLU A 702     182.579 222.712 166.454  1.00 25.24           O  
ATOM   4230  CB  GLU A 702     181.052 220.899 168.470  1.00 25.06           C  
ATOM   4231  CG  GLU A 702     180.668 219.714 167.610  1.00 24.98           C  
ATOM   4232  CD  GLU A 702     179.247 219.299 167.814  1.00 25.77           C  
ATOM   4233  OE1 GLU A 702     178.665 219.711 168.786  1.00 25.33           O  
ATOM   4234  OE2 GLU A 702     178.733 218.562 166.998  1.00 25.35           O  
ATOM   4235  N   ASN A 703     183.521 220.684 166.259  1.00 24.16           N  
ATOM   4236  CA  ASN A 703     183.880 220.875 164.864  1.00 23.68           C  
ATOM   4237  C   ASN A 703     183.853 219.571 164.097  1.00 23.33           C  
ATOM   4238  O   ASN A 703     184.777 218.775 164.204  1.00 24.09           O  
ATOM   4239  CB  ASN A 703     185.252 221.502 164.723  1.00 23.65           C  
ATOM   4240  CG  ASN A 703     185.549 221.823 163.281  1.00 24.03           C  
ATOM   4241  OD1 ASN A 703     184.626 221.834 162.462  1.00 24.35           O  
ATOM   4242  ND2 ASN A 703     186.787 222.079 162.946  1.00 23.89           N  
ATOM   4243  N   SER A 704     182.804 219.334 163.328  1.00 23.49           N  
ATOM   4244  CA  SER A 704     182.739 218.099 162.567  1.00 23.11           C  
ATOM   4245  C   SER A 704     183.709 218.174 161.397  1.00 22.94           C  
ATOM   4246  O   SER A 704     184.104 219.259 160.977  1.00 23.00           O  
ATOM   4247  CB  SER A 704     181.331 217.859 162.073  1.00 22.94           C  
ATOM   4248  OG  SER A 704     180.953 218.839 161.149  1.00 23.20           O  
ATOM   4249  N   VAL A 705     184.070 217.027 160.844  1.00 22.62           N  
ATOM   4250  CA  VAL A 705     184.981 217.004 159.707  1.00 22.34           C  
ATOM   4251  C   VAL A 705     184.259 216.500 158.474  1.00 22.47           C  
ATOM   4252  O   VAL A 705     183.592 215.468 158.517  1.00 22.68           O  
ATOM   4253  CB  VAL A 705     186.212 216.131 160.020  1.00 22.10           C  
ATOM   4254  CG1 VAL A 705     187.150 216.067 158.815  1.00 21.97           C  
ATOM   4255  CG2 VAL A 705     186.936 216.716 161.225  1.00 22.43           C  
ATOM   4256  N   ALA A 706     184.394 217.223 157.367  1.00 22.24           N  
ATOM   4257  CA  ALA A 706     183.694 216.875 156.133  1.00 22.07           C  
ATOM   4258  C   ALA A 706     184.376 215.727 155.414  1.00 22.23           C  
ATOM   4259  O   ALA A 706     184.896 215.875 154.311  1.00 22.52           O  
ATOM   4260  CB  ALA A 706     183.627 218.078 155.217  1.00 21.68           C  
ATOM   4261  N   TYR A 707     184.353 214.574 156.050  1.00 22.30           N  
ATOM   4262  CA  TYR A 707     184.969 213.377 155.529  1.00 22.23           C  
ATOM   4263  C   TYR A 707     184.154 212.742 154.425  1.00 22.90           C  
ATOM   4264  O   TYR A 707     182.936 212.608 154.535  1.00 23.10           O  
ATOM   4265  CB  TYR A 707     185.172 212.367 156.645  1.00 22.61           C  
ATOM   4266  CG  TYR A 707     185.684 211.058 156.154  1.00 22.56           C  
ATOM   4267  CD1 TYR A 707     187.021 210.870 155.960  1.00 22.45           C  
ATOM   4268  CD2 TYR A 707     184.796 210.043 155.872  1.00 22.89           C  
ATOM   4269  CE1 TYR A 707     187.475 209.672 155.482  1.00 22.31           C  
ATOM   4270  CE2 TYR A 707     185.250 208.848 155.391  1.00 23.06           C  
ATOM   4271  CZ  TYR A 707     186.587 208.661 155.192  1.00 22.44           C  
ATOM   4272  OH  TYR A 707     187.054 207.465 154.696  1.00 22.69           O  
ATOM   4273  N   SER A 708     184.841 212.318 153.378  1.00 22.82           N  
ATOM   4274  CA  SER A 708     184.246 211.561 152.292  1.00 22.52           C  
ATOM   4275  C   SER A 708     185.355 210.709 151.701  1.00 22.51           C  
ATOM   4276  O   SER A 708     186.531 210.962 151.963  1.00 22.34           O  
ATOM   4277  CB  SER A 708     183.619 212.480 151.254  1.00 22.75           C  
ATOM   4278  OG  SER A 708     184.580 213.180 150.543  1.00 22.52           O  
ATOM   4279  N   ASN A 709     184.994 209.714 150.886  1.00 22.44           N  
ATOM   4280  CA  ASN A 709     185.949 208.768 150.304  1.00 22.28           C  
ATOM   4281  C   ASN A 709     186.762 209.357 149.136  1.00 22.31           C  
ATOM   4282  O   ASN A 709     187.731 208.731 148.685  1.00 22.40           O  
ATOM   4283  CB  ASN A 709     185.218 207.488 149.867  1.00 22.78           C  
ATOM   4284  CG  ASN A 709     183.941 207.733 149.021  1.00 22.91           C  
ATOM   4285  OD1 ASN A 709     183.383 208.843 149.014  1.00 22.84           O  
ATOM   4286  ND2 ASN A 709     183.492 206.704 148.327  1.00 23.24           N  
ATOM   4287  N   ASN A 710     186.394 210.548 148.640  1.00 22.15           N  
ATOM   4288  CA  ASN A 710     187.041 211.208 147.510  1.00 21.38           C  
ATOM   4289  C   ASN A 710     187.354 212.684 147.724  1.00 21.62           C  
ATOM   4290  O   ASN A 710     187.422 213.428 146.748  1.00 22.53           O  
ATOM   4291  CB  ASN A 710     186.166 211.071 146.301  1.00 21.79           C  
ATOM   4292  CG  ASN A 710     184.869 211.741 146.533  1.00 22.35           C  
ATOM   4293  OD1 ASN A 710     184.551 212.154 147.668  1.00 22.47           O  
ATOM   4294  ND2 ASN A 710     184.090 211.864 145.495  1.00 22.16           N  
ATOM   4295  N   SER A 711     187.557 213.135 148.959  1.00 21.71           N  
ATOM   4296  CA  SER A 711     187.830 214.561 149.154  1.00 21.32           C  
ATOM   4297  C   SER A 711     188.956 214.804 150.130  1.00 20.82           C  
ATOM   4298  O   SER A 711     188.977 214.256 151.230  1.00 21.85           O  
ATOM   4299  CB  SER A 711     186.602 215.291 149.644  1.00 22.14           C  
ATOM   4300  OG  SER A 711     186.867 216.660 149.797  1.00 22.03           O  
ATOM   4301  N   ILE A 712     189.904 215.624 149.712  1.00 20.98           N  
ATOM   4302  CA  ILE A 712     191.058 215.938 150.530  1.00 20.44           C  
ATOM   4303  C   ILE A 712     191.210 217.436 150.719  1.00 20.79           C  
ATOM   4304  O   ILE A 712     191.059 218.208 149.774  1.00 22.05           O  
ATOM   4305  CB  ILE A 712     192.336 215.365 149.892  1.00 21.09           C  
ATOM   4306  CG1 ILE A 712     193.517 215.552 150.838  1.00 21.50           C  
ATOM   4307  CG2 ILE A 712     192.613 216.050 148.550  1.00 21.23           C  
ATOM   4308  CD1 ILE A 712     194.739 214.752 150.467  1.00 21.61           C  
ATOM   4309  N   ALA A 713     191.529 217.857 151.928  1.00 21.04           N  
ATOM   4310  CA  ALA A 713     191.797 219.267 152.155  1.00 20.43           C  
ATOM   4311  C   ALA A 713     193.289 219.497 152.154  1.00 20.75           C  
ATOM   4312  O   ALA A 713     194.031 218.867 152.904  1.00 21.14           O  
ATOM   4313  CB  ALA A 713     191.184 219.745 153.446  1.00 21.07           C  
ATOM   4314  N   ILE A 714     193.730 220.388 151.289  1.00 20.93           N  
ATOM   4315  CA  ILE A 714     195.147 220.677 151.162  1.00 20.78           C  
ATOM   4316  C   ILE A 714     195.401 222.145 151.448  1.00 20.87           C  
ATOM   4317  O   ILE A 714     194.717 222.995 150.878  1.00 21.72           O  
ATOM   4318  CB  ILE A 714     195.658 220.312 149.770  1.00 21.14           C  
ATOM   4319  CG1 ILE A 714     195.432 218.837 149.565  1.00 21.67           C  
ATOM   4320  CG2 ILE A 714     197.138 220.675 149.618  1.00 21.19           C  
ATOM   4321  CD1 ILE A 714     195.653 218.374 148.198  1.00 22.11           C  
ATOM   4322  N   PRO A 715     196.326 222.482 152.348  1.00 20.63           N  
ATOM   4323  CA  PRO A 715     196.683 223.826 152.686  1.00 19.88           C  
ATOM   4324  C   PRO A 715     197.151 224.553 151.461  1.00 20.78           C  
ATOM   4325  O   PRO A 715     197.901 223.994 150.676  1.00 21.36           O  
ATOM   4326  CB  PRO A 715     197.842 223.635 153.653  1.00 20.00           C  
ATOM   4327  CG  PRO A 715     197.621 222.288 154.230  1.00 20.44           C  
ATOM   4328  CD  PRO A 715     197.047 221.476 153.109  1.00 20.97           C  
ATOM   4329  N   THR A 716     196.745 225.795 151.322  1.00 20.24           N  
ATOM   4330  CA  THR A 716     197.180 226.665 150.233  1.00 20.40           C  
ATOM   4331  C   THR A 716     198.106 227.793 150.715  1.00 20.40           C  
ATOM   4332  O   THR A 716     198.844 228.375 149.920  1.00 20.92           O  
ATOM   4333  CB  THR A 716     195.972 227.280 149.514  1.00 20.86           C  
ATOM   4334  OG1 THR A 716     195.226 228.083 150.430  1.00 20.66           O  
ATOM   4335  CG2 THR A 716     195.069 226.201 148.949  1.00 21.11           C  
ATOM   4336  N   ASN A 717     198.081 228.077 152.026  1.00 20.41           N  
ATOM   4337  CA  ASN A 717     198.880 229.103 152.675  1.00 19.78           C  
ATOM   4338  C   ASN A 717     199.245 228.615 154.076  1.00 20.19           C  
ATOM   4339  O   ASN A 717     198.643 227.659 154.572  1.00 20.58           O  
ATOM   4340  CB  ASN A 717     198.119 230.435 152.730  1.00 20.92           C  
ATOM   4341  CG  ASN A 717     199.010 231.664 152.956  1.00 20.35           C  
ATOM   4342  OD1 ASN A 717     200.238 231.542 153.105  1.00 20.40           O  
ATOM   4343  ND2 ASN A 717     198.391 232.834 152.992  1.00 20.90           N  
ATOM   4344  N   PHE A 718     200.213 229.280 154.708  1.00 19.67           N  
ATOM   4345  CA  PHE A 718     200.711 228.920 156.035  1.00 19.59           C  
ATOM   4346  C   PHE A 718     201.210 230.125 156.785  1.00 19.68           C  
ATOM   4347  O   PHE A 718     201.512 231.163 156.190  1.00 20.41           O  
ATOM   4348  CB  PHE A 718     201.870 227.949 155.914  1.00 19.89           C  
ATOM   4349  CG  PHE A 718     203.012 228.583 155.252  1.00 19.79           C  
ATOM   4350  CD1 PHE A 718     203.979 229.215 155.985  1.00 19.94           C  
ATOM   4351  CD2 PHE A 718     203.118 228.570 153.887  1.00 20.11           C  
ATOM   4352  CE1 PHE A 718     205.019 229.824 155.372  1.00 20.12           C  
ATOM   4353  CE2 PHE A 718     204.165 229.179 153.262  1.00 20.16           C  
ATOM   4354  CZ  PHE A 718     205.115 229.811 154.004  1.00 20.00           C  
ATOM   4355  N   THR A 719     201.342 229.958 158.089  1.00 19.31           N  
ATOM   4356  CA  THR A 719     201.965 230.955 158.927  1.00 19.97           C  
ATOM   4357  C   THR A 719     203.059 230.345 159.766  1.00 20.24           C  
ATOM   4358  O   THR A 719     203.047 229.148 160.057  1.00 20.10           O  
ATOM   4359  CB  THR A 719     200.949 231.637 159.853  1.00 20.24           C  
ATOM   4360  OG1 THR A 719     200.316 230.648 160.675  1.00 19.69           O  
ATOM   4361  CG2 THR A 719     199.908 232.388 159.047  1.00 20.57           C  
ATOM   4362  N   ILE A 720     203.986 231.181 160.194  1.00 20.38           N  
ATOM   4363  CA  ILE A 720     205.005 230.753 161.122  1.00 20.16           C  
ATOM   4364  C   ILE A 720     204.679 231.326 162.474  1.00 20.68           C  
ATOM   4365  O   ILE A 720     204.551 232.539 162.629  1.00 21.19           O  
ATOM   4366  CB  ILE A 720     206.402 231.213 160.689  1.00 20.38           C  
ATOM   4367  CG1 ILE A 720     206.712 230.738 159.261  1.00 20.32           C  
ATOM   4368  CG2 ILE A 720     207.450 230.720 161.674  1.00 20.83           C  
ATOM   4369  CD1 ILE A 720     206.667 229.241 159.033  1.00 20.44           C  
ATOM   4370  N   SER A 721     204.525 230.458 163.449  1.00 20.74           N  
ATOM   4371  CA  SER A 721     204.174 230.904 164.778  1.00 21.37           C  
ATOM   4372  C   SER A 721     205.271 230.575 165.751  1.00 21.71           C  
ATOM   4373  O   SER A 721     206.047 229.642 165.539  1.00 21.94           O  
ATOM   4374  CB  SER A 721     202.878 230.268 165.222  1.00 21.55           C  
ATOM   4375  OG  SER A 721     203.003 228.885 165.292  1.00 21.14           O  
ATOM   4376  N   VAL A 722     205.340 231.343 166.824  1.00 22.32           N  
ATOM   4377  CA  VAL A 722     206.316 231.086 167.857  1.00 22.28           C  
ATOM   4378  C   VAL A 722     205.618 230.899 169.178  1.00 22.88           C  
ATOM   4379  O   VAL A 722     204.818 231.738 169.587  1.00 23.32           O  
ATOM   4380  CB  VAL A 722     207.340 232.226 167.944  1.00 23.07           C  
ATOM   4381  CG1 VAL A 722     208.340 231.948 169.058  1.00 23.05           C  
ATOM   4382  CG2 VAL A 722     208.056 232.343 166.616  1.00 22.97           C  
ATOM   4383  N   THR A 723     205.911 229.799 169.845  1.00 22.71           N  
ATOM   4384  CA  THR A 723     205.298 229.548 171.133  1.00 23.07           C  
ATOM   4385  C   THR A 723     206.354 229.531 172.209  1.00 23.30           C  
ATOM   4386  O   THR A 723     207.523 229.255 171.941  1.00 23.51           O  
ATOM   4387  CB  THR A 723     204.543 228.211 171.143  1.00 23.07           C  
ATOM   4388  OG1 THR A 723     205.469 227.136 170.956  1.00 22.56           O  
ATOM   4389  CG2 THR A 723     203.533 228.185 170.021  1.00 23.02           C  
ATOM   4390  N   THR A 724     205.952 229.784 173.439  1.00 23.30           N  
ATOM   4391  CA  THR A 724     206.918 229.782 174.518  1.00 23.06           C  
ATOM   4392  C   THR A 724     206.658 228.649 175.482  1.00 23.22           C  
ATOM   4393  O   THR A 724     205.545 228.489 175.981  1.00 23.75           O  
ATOM   4394  CB  THR A 724     206.891 231.114 175.278  1.00 23.79           C  
ATOM   4395  OG1 THR A 724     207.175 232.177 174.380  1.00 24.78           O  
ATOM   4396  CG2 THR A 724     207.926 231.121 176.357  1.00 24.40           C  
ATOM   4397  N   GLU A 725     207.692 227.871 175.753  1.00 23.14           N  
ATOM   4398  CA  GLU A 725     207.583 226.774 176.698  1.00 22.93           C  
ATOM   4399  C   GLU A 725     208.574 226.941 177.831  1.00 23.63           C  
ATOM   4400  O   GLU A 725     209.762 227.160 177.605  1.00 24.21           O  
ATOM   4401  CB  GLU A 725     207.789 225.437 176.010  1.00 22.45           C  
ATOM   4402  CG  GLU A 725     207.615 224.266 176.934  1.00 22.65           C  
ATOM   4403  CD  GLU A 725     207.584 222.969 176.234  1.00 22.43           C  
ATOM   4404  OE1 GLU A 725     208.103 222.872 175.143  1.00 21.89           O  
ATOM   4405  OE2 GLU A 725     207.019 222.052 176.786  1.00 21.66           O  
ATOM   4406  N   ILE A 726     208.076 226.872 179.054  1.00 23.38           N  
ATOM   4407  CA  ILE A 726     208.909 227.109 180.221  1.00 23.56           C  
ATOM   4408  C   ILE A 726     209.104 225.876 181.076  1.00 23.63           C  
ATOM   4409  O   ILE A 726     208.135 225.250 181.504  1.00 24.20           O  
ATOM   4410  CB  ILE A 726     208.297 228.222 181.075  1.00 24.07           C  
ATOM   4411  CG1 ILE A 726     208.181 229.487 180.260  1.00 24.40           C  
ATOM   4412  CG2 ILE A 726     209.122 228.469 182.302  1.00 24.96           C  
ATOM   4413  CD1 ILE A 726     206.797 229.769 179.746  1.00 25.09           C  
ATOM   4414  N   LEU A 727     210.363 225.548 181.340  1.00 23.68           N  
ATOM   4415  CA  LEU A 727     210.693 224.414 182.184  1.00 23.59           C  
ATOM   4416  C   LEU A 727     211.673 224.816 183.284  1.00 23.98           C  
ATOM   4417  O   LEU A 727     212.729 225.370 182.981  1.00 25.03           O  
ATOM   4418  CB  LEU A 727     211.343 223.307 181.353  1.00 23.08           C  
ATOM   4419  CG  LEU A 727     210.515 222.719 180.216  1.00 22.67           C  
ATOM   4420  CD1 LEU A 727     211.385 221.798 179.419  1.00 21.85           C  
ATOM   4421  CD2 LEU A 727     209.332 221.962 180.765  1.00 22.84           C  
ATOM   4422  N   PRO A 728     211.355 224.575 184.559  1.00 23.97           N  
ATOM   4423  CA  PRO A 728     212.245 224.734 185.684  1.00 23.98           C  
ATOM   4424  C   PRO A 728     213.424 223.814 185.512  1.00 23.72           C  
ATOM   4425  O   PRO A 728     213.270 222.702 185.017  1.00 24.47           O  
ATOM   4426  CB  PRO A 728     211.387 224.305 186.864  1.00 24.43           C  
ATOM   4427  CG  PRO A 728     209.974 224.517 186.402  1.00 25.84           C  
ATOM   4428  CD  PRO A 728     209.996 224.216 184.920  1.00 24.47           C  
ATOM   4429  N   VAL A 729     214.590 224.269 185.921  1.00 24.38           N  
ATOM   4430  CA  VAL A 729     215.787 223.449 185.853  1.00 23.93           C  
ATOM   4431  C   VAL A 729     216.375 223.201 187.226  1.00 24.57           C  
ATOM   4432  O   VAL A 729     216.924 222.131 187.480  1.00 24.73           O  
ATOM   4433  CB  VAL A 729     216.830 224.069 184.920  1.00 24.27           C  
ATOM   4434  CG1 VAL A 729     218.124 223.272 184.953  1.00 24.41           C  
ATOM   4435  CG2 VAL A 729     216.271 224.072 183.515  1.00 24.04           C  
ATOM   4436  N   SER A 730     216.327 224.201 188.098  1.00 25.04           N  
ATOM   4437  CA  SER A 730     216.981 224.046 189.385  1.00 24.97           C  
ATOM   4438  C   SER A 730     216.235 224.710 190.531  1.00 25.34           C  
ATOM   4439  O   SER A 730     215.416 225.607 190.339  1.00 25.53           O  
ATOM   4440  CB  SER A 730     218.390 224.590 189.310  1.00 25.48           C  
ATOM   4441  OG  SER A 730     218.385 225.964 189.071  1.00 25.78           O  
ATOM   4442  N   MET A 731     216.537 224.236 191.727  1.00 25.58           N  
ATOM   4443  CA  MET A 731     216.000 224.724 192.985  1.00 25.85           C  
ATOM   4444  C   MET A 731     216.977 225.652 193.660  1.00 26.16           C  
ATOM   4445  O   MET A 731     218.159 225.678 193.321  1.00 26.37           O  
ATOM   4446  CB  MET A 731     215.736 223.566 193.938  1.00 26.06           C  
ATOM   4447  CG  MET A 731     214.725 222.591 193.480  1.00 26.02           C  
ATOM   4448  SD  MET A 731     214.607 221.164 194.565  1.00 26.08           S  
ATOM   4449  CE  MET A 731     213.727 221.767 195.983  1.00 26.43           C  
ATOM   4450  N   THR A 732     216.495 226.389 194.643  1.00 26.45           N  
ATOM   4451  CA  THR A 732     217.389 227.165 195.476  1.00 26.63           C  
ATOM   4452  C   THR A 732     218.218 226.199 196.315  1.00 27.05           C  
ATOM   4453  O   THR A 732     217.678 225.271 196.921  1.00 27.00           O  
ATOM   4454  CB  THR A 732     216.608 228.141 196.373  1.00 27.34           C  
ATOM   4455  OG1 THR A 732     215.904 229.087 195.556  1.00 26.72           O  
ATOM   4456  CG2 THR A 732     217.542 228.876 197.291  1.00 28.55           C  
ATOM   4457  N   LYS A 733     219.527 226.416 196.366  1.00 27.23           N  
ATOM   4458  CA  LYS A 733     220.416 225.516 197.089  1.00 27.13           C  
ATOM   4459  C   LYS A 733     220.413 225.782 198.584  1.00 28.64           C  
ATOM   4460  O   LYS A 733     221.376 226.313 199.140  1.00 29.51           O  
ATOM   4461  CB  LYS A 733     221.838 225.639 196.558  1.00 27.38           C  
ATOM   4462  CG  LYS A 733     222.038 225.113 195.152  1.00 26.48           C  
ATOM   4463  CD  LYS A 733     223.380 225.559 194.577  1.00 27.37           C  
ATOM   4464  CE  LYS A 733     224.570 224.888 195.263  1.00 27.51           C  
ATOM   4465  NZ  LYS A 733     225.859 225.272 194.635  1.00 27.77           N  
ATOM   4466  N   THR A 734     219.319 225.412 199.230  1.00 28.48           N  
ATOM   4467  CA  THR A 734     219.189 225.613 200.662  1.00 28.57           C  
ATOM   4468  C   THR A 734     219.959 224.542 201.404  1.00 29.12           C  
ATOM   4469  O   THR A 734     219.849 223.356 201.097  1.00 28.77           O  
ATOM   4470  CB  THR A 734     217.722 225.598 201.122  1.00 28.74           C  
ATOM   4471  OG1 THR A 734     217.003 226.648 200.468  1.00 28.73           O  
ATOM   4472  CG2 THR A 734     217.630 225.789 202.641  1.00 29.28           C  
ATOM   4473  N   SER A 735     220.726 224.971 202.389  1.00 29.52           N  
ATOM   4474  CA  SER A 735     221.518 224.091 203.228  1.00 29.62           C  
ATOM   4475  C   SER A 735     221.194 224.346 204.684  1.00 30.00           C  
ATOM   4476  O   SER A 735     221.132 225.491 205.131  1.00 30.97           O  
ATOM   4477  CB  SER A 735     222.989 224.313 202.983  1.00 29.89           C  
ATOM   4478  OG  SER A 735     223.758 223.552 203.868  1.00 30.83           O  
ATOM   4479  N   VAL A 736     220.946 223.281 205.426  1.00 29.88           N  
ATOM   4480  CA  VAL A 736     220.550 223.437 206.812  1.00 30.28           C  
ATOM   4481  C   VAL A 736     221.535 222.818 207.771  1.00 30.50           C  
ATOM   4482  O   VAL A 736     221.912 221.661 207.624  1.00 30.84           O  
ATOM   4483  CB  VAL A 736     219.165 222.809 207.042  1.00 30.49           C  
ATOM   4484  CG1 VAL A 736     218.754 222.945 208.501  1.00 30.75           C  
ATOM   4485  CG2 VAL A 736     218.165 223.479 206.120  1.00 30.29           C  
ATOM   4486  N   ASP A 737     221.919 223.593 208.770  1.00 30.83           N  
ATOM   4487  CA  ASP A 737     222.753 223.128 209.862  1.00 31.00           C  
ATOM   4488  C   ASP A 737     221.837 222.522 210.916  1.00 31.89           C  
ATOM   4489  O   ASP A 737     221.232 223.265 211.696  1.00 32.11           O  
ATOM   4490  CB  ASP A 737     223.542 224.315 210.436  1.00 31.56           C  
ATOM   4491  CG  ASP A 737     224.409 223.993 211.641  1.00 32.78           C  
ATOM   4492  OD1 ASP A 737     224.177 222.983 212.267  1.00 32.69           O  
ATOM   4493  OD2 ASP A 737     225.273 224.774 211.955  1.00 34.07           O  
ATOM   4494  N   CYS A 738     221.690 221.178 210.920  1.00 31.06           N  
ATOM   4495  CA  CYS A 738     220.711 220.511 211.782  1.00 31.16           C  
ATOM   4496  C   CYS A 738     220.998 220.709 213.278  1.00 32.19           C  
ATOM   4497  O   CYS A 738     220.059 220.760 214.080  1.00 33.02           O  
ATOM   4498  CB  CYS A 738     220.651 219.004 211.462  1.00 31.68           C  
ATOM   4499  SG  CYS A 738     222.177 218.072 211.811  1.00 32.77           S  
ATOM   4500  N   THR A 739     222.281 220.872 213.664  1.00 31.55           N  
ATOM   4501  CA  THR A 739     222.663 221.086 215.055  1.00 31.28           C  
ATOM   4502  C   THR A 739     222.278 222.482 215.494  1.00 33.52           C  
ATOM   4503  O   THR A 739     221.690 222.659 216.556  1.00 33.69           O  
ATOM   4504  CB  THR A 739     224.165 220.878 215.279  1.00 31.45           C  
ATOM   4505  OG1 THR A 739     224.522 219.541 214.916  1.00 31.66           O  
ATOM   4506  CG2 THR A 739     224.518 221.118 216.745  1.00 31.45           C  
ATOM   4507  N   MET A 740     222.583 223.482 214.674  1.00 31.65           N  
ATOM   4508  CA  MET A 740     222.208 224.838 215.047  1.00 31.93           C  
ATOM   4509  C   MET A 740     220.702 225.003 215.075  1.00 32.34           C  
ATOM   4510  O   MET A 740     220.164 225.726 215.913  1.00 33.33           O  
ATOM   4511  CB  MET A 740     222.789 225.877 214.111  1.00 33.33           C  
ATOM   4512  CG  MET A 740     222.432 227.295 214.532  1.00 34.73           C  
ATOM   4513  SD  MET A 740     223.136 228.545 213.495  1.00 37.74           S  
ATOM   4514  CE  MET A 740     222.417 229.997 214.247  1.00 38.47           C  
ATOM   4515  N   TYR A 741     220.020 224.359 214.136  1.00 32.20           N  
ATOM   4516  CA  TYR A 741     218.576 224.454 214.057  1.00 31.76           C  
ATOM   4517  C   TYR A 741     217.925 223.925 215.321  1.00 32.57           C  
ATOM   4518  O   TYR A 741     217.050 224.573 215.894  1.00 33.20           O  
ATOM   4519  CB  TYR A 741     218.047 223.703 212.838  1.00 31.94           C  
ATOM   4520  CG  TYR A 741     216.551 223.683 212.770  1.00 31.83           C  
ATOM   4521  CD1 TYR A 741     215.853 224.748 212.254  1.00 32.38           C  
ATOM   4522  CD2 TYR A 741     215.876 222.595 213.247  1.00 32.03           C  
ATOM   4523  CE1 TYR A 741     214.479 224.705 212.227  1.00 32.06           C  
ATOM   4524  CE2 TYR A 741     214.521 222.553 213.220  1.00 32.09           C  
ATOM   4525  CZ  TYR A 741     213.822 223.592 212.720  1.00 31.82           C  
ATOM   4526  OH  TYR A 741     212.462 223.532 212.711  1.00 32.25           O  
ATOM   4527  N   ILE A 742     218.342 222.738 215.757  1.00 33.03           N  
ATOM   4528  CA  ILE A 742     217.743 222.118 216.931  1.00 32.64           C  
ATOM   4529  C   ILE A 742     218.260 222.699 218.259  1.00 33.57           C  
ATOM   4530  O   ILE A 742     217.467 222.997 219.154  1.00 34.62           O  
ATOM   4531  CB  ILE A 742     217.993 220.595 216.941  1.00 32.77           C  
ATOM   4532  CG1 ILE A 742     217.346 219.939 215.738  1.00 32.22           C  
ATOM   4533  CG2 ILE A 742     217.410 220.001 218.221  1.00 34.22           C  
ATOM   4534  CD1 ILE A 742     217.773 218.513 215.518  1.00 32.43           C  
ATOM   4535  N   CYS A 743     219.608 222.824 218.389  1.00 33.58           N  
ATOM   4536  CA  CYS A 743     220.288 223.202 219.612  1.00 34.34           C  
ATOM   4537  C   CYS A 743     221.189 224.442 219.403  1.00 34.72           C  
ATOM   4538  O   CYS A 743     222.407 224.389 219.607  1.00 34.98           O  
ATOM   4539  CB  CYS A 743     221.169 222.029 220.103  1.00 34.95           C  
ATOM   4540  SG  CYS A 743     220.242 220.533 220.525  1.00 36.11           S  
ATOM   4541  N   GLY A 744     220.579 225.566 219.000  1.00 34.47           N  
ATOM   4542  CA  GLY A 744     221.326 226.794 218.712  1.00 35.19           C  
ATOM   4543  C   GLY A 744     222.011 227.335 219.959  1.00 36.56           C  
ATOM   4544  O   GLY A 744     221.352 227.707 220.929  1.00 37.19           O  
ATOM   4545  N   ASP A 745     223.339 227.372 219.917  1.00 37.04           N  
ATOM   4546  CA  ASP A 745     224.170 227.858 221.012  1.00 37.40           C  
ATOM   4547  C   ASP A 745     223.874 227.186 222.351  1.00 37.26           C  
ATOM   4548  O   ASP A 745     223.943 227.833 223.397  1.00 37.86           O  
ATOM   4549  CB  ASP A 745     224.014 229.372 221.165  1.00 38.74           C  
ATOM   4550  N   SER A 746     223.601 225.883 222.340  1.00 36.64           N  
ATOM   4551  CA  SER A 746     223.336 225.181 223.590  1.00 36.68           C  
ATOM   4552  C   SER A 746     224.123 223.900 223.752  1.00 36.24           C  
ATOM   4553  O   SER A 746     223.864 222.906 223.070  1.00 37.32           O  
ATOM   4554  CB  SER A 746     221.876 224.859 223.701  1.00 37.05           C  
ATOM   4555  OG  SER A 746     221.640 224.009 224.794  1.00 37.53           O  
ATOM   4556  N   THR A 747     225.065 223.915 224.687  1.00 36.58           N  
ATOM   4557  CA  THR A 747     225.910 222.758 224.951  1.00 36.53           C  
ATOM   4558  C   THR A 747     225.100 221.614 225.529  1.00 35.90           C  
ATOM   4559  O   THR A 747     225.286 220.456 225.152  1.00 36.44           O  
ATOM   4560  CB  THR A 747     227.060 223.111 225.909  1.00 36.50           C  
ATOM   4561  OG1 THR A 747     227.890 224.113 225.307  1.00 37.35           O  
ATOM   4562  CG2 THR A 747     227.901 221.877 226.205  1.00 36.49           C  
ATOM   4563  N   GLU A 748     224.197 221.940 226.445  1.00 36.51           N  
ATOM   4564  CA  GLU A 748     223.394 220.919 227.104  1.00 36.08           C  
ATOM   4565  C   GLU A 748     222.486 220.194 226.108  1.00 36.75           C  
ATOM   4566  O   GLU A 748     222.398 218.962 226.132  1.00 36.94           O  
ATOM   4567  CB  GLU A 748     222.555 221.563 228.209  1.00 37.35           C  
ATOM   4568  N   CYS A 749     221.856 220.955 225.192  1.00 36.31           N  
ATOM   4569  CA  CYS A 749     221.007 220.403 224.140  1.00 35.84           C  
ATOM   4570  C   CYS A 749     221.826 219.540 223.166  1.00 37.15           C  
ATOM   4571  O   CYS A 749     221.387 218.443 222.814  1.00 35.50           O  
ATOM   4572  CB  CYS A 749     220.264 221.534 223.412  1.00 37.04           C  
ATOM   4573  SG  CYS A 749     219.086 221.037 222.120  1.00 37.40           S  
ATOM   4574  N   SER A 750     223.019 220.019 222.739  1.00 35.57           N  
ATOM   4575  CA  SER A 750     223.884 219.295 221.804  1.00 35.17           C  
ATOM   4576  C   SER A 750     224.290 217.945 222.376  1.00 35.64           C  
ATOM   4577  O   SER A 750     224.238 216.927 221.685  1.00 37.10           O  
ATOM   4578  CB  SER A 750     225.117 220.112 221.486  1.00 35.40           C  
ATOM   4579  OG  SER A 750     225.953 219.434 220.589  1.00 35.64           O  
ATOM   4580  N   ASN A 751     224.632 217.914 223.659  1.00 35.97           N  
ATOM   4581  CA  ASN A 751     225.009 216.654 224.273  1.00 35.18           C  
ATOM   4582  C   ASN A 751     223.866 215.647 224.213  1.00 35.40           C  
ATOM   4583  O   ASN A 751     224.104 214.448 224.052  1.00 35.98           O  
ATOM   4584  CB  ASN A 751     225.454 216.874 225.698  1.00 35.85           C  
ATOM   4585  CG  ASN A 751     226.793 217.525 225.777  1.00 36.21           C  
ATOM   4586  OD1 ASN A 751     227.550 217.550 224.800  1.00 36.38           O  
ATOM   4587  ND2 ASN A 751     227.114 218.050 226.928  1.00 36.76           N  
ATOM   4588  N   LEU A 752     222.627 216.130 224.327  1.00 35.29           N  
ATOM   4589  CA  LEU A 752     221.464 215.258 224.218  1.00 35.23           C  
ATOM   4590  C   LEU A 752     221.200 214.887 222.766  1.00 36.32           C  
ATOM   4591  O   LEU A 752     220.806 213.768 222.458  1.00 35.93           O  
ATOM   4592  CB  LEU A 752     220.216 215.946 224.780  1.00 35.98           C  
ATOM   4593  CG  LEU A 752     220.183 216.216 226.282  1.00 36.63           C  
ATOM   4594  CD1 LEU A 752     218.987 217.098 226.585  1.00 37.80           C  
ATOM   4595  CD2 LEU A 752     220.080 214.902 227.048  1.00 37.84           C  
ATOM   4596  N   LEU A 753     221.445 215.818 221.858  1.00 35.25           N  
ATOM   4597  CA  LEU A 753     221.212 215.569 220.445  1.00 34.68           C  
ATOM   4598  C   LEU A 753     222.106 214.449 219.941  1.00 35.31           C  
ATOM   4599  O   LEU A 753     221.688 213.640 219.118  1.00 35.37           O  
ATOM   4600  CB  LEU A 753     221.437 216.842 219.631  1.00 34.86           C  
ATOM   4601  CG  LEU A 753     221.161 216.763 218.116  1.00 34.65           C  
ATOM   4602  CD1 LEU A 753     219.717 216.341 217.857  1.00 34.44           C  
ATOM   4603  CD2 LEU A 753     221.423 218.137 217.509  1.00 33.62           C  
ATOM   4604  N   LEU A 754     223.319 214.370 220.470  1.00 34.85           N  
ATOM   4605  CA  LEU A 754     224.275 213.344 220.070  1.00 35.13           C  
ATOM   4606  C   LEU A 754     223.796 211.938 220.413  1.00 35.37           C  
ATOM   4607  O   LEU A 754     224.301 210.954 219.873  1.00 35.33           O  
ATOM   4608  CB  LEU A 754     225.630 213.580 220.744  1.00 35.31           C  
ATOM   4609  CG  LEU A 754     226.426 214.816 220.299  1.00 35.56           C  
ATOM   4610  CD1 LEU A 754     227.624 214.981 221.218  1.00 36.19           C  
ATOM   4611  CD2 LEU A 754     226.885 214.654 218.856  1.00 35.69           C  
ATOM   4612  N   GLN A 755     222.803 211.829 221.285  1.00 35.29           N  
ATOM   4613  CA  GLN A 755     222.291 210.532 221.688  1.00 35.22           C  
ATOM   4614  C   GLN A 755     221.467 209.926 220.565  1.00 35.72           C  
ATOM   4615  O   GLN A 755     221.085 208.758 220.624  1.00 36.69           O  
ATOM   4616  CB  GLN A 755     221.448 210.652 222.957  1.00 35.92           C  
ATOM   4617  CG  GLN A 755     222.239 211.077 224.182  1.00 36.07           C  
ATOM   4618  CD  GLN A 755     221.362 211.272 225.400  1.00 36.78           C  
ATOM   4619  OE1 GLN A 755     220.149 211.465 225.284  1.00 36.82           O  
ATOM   4620  NE2 GLN A 755     221.969 211.221 226.581  1.00 36.56           N  
ATOM   4621  N   TYR A 756     221.198 210.720 219.533  1.00 34.84           N  
ATOM   4622  CA  TYR A 756     220.419 210.280 218.394  1.00 34.58           C  
ATOM   4623  C   TYR A 756     221.314 209.838 217.247  1.00 34.50           C  
ATOM   4624  O   TYR A 756     220.834 209.512 216.157  1.00 34.44           O  
ATOM   4625  CB  TYR A 756     219.478 211.393 217.965  1.00 34.90           C  
ATOM   4626  CG  TYR A 756     218.371 211.601 218.930  1.00 35.04           C  
ATOM   4627  CD1 TYR A 756     218.556 212.407 220.027  1.00 35.21           C  
ATOM   4628  CD2 TYR A 756     217.161 210.985 218.720  1.00 35.14           C  
ATOM   4629  CE1 TYR A 756     217.536 212.592 220.915  1.00 35.05           C  
ATOM   4630  CE2 TYR A 756     216.140 211.171 219.604  1.00 35.20           C  
ATOM   4631  CZ  TYR A 756     216.324 211.969 220.699  1.00 35.26           C  
ATOM   4632  OH  TYR A 756     215.303 212.154 221.585  1.00 36.02           O  
ATOM   4633  N   GLY A 757     222.615 209.785 217.504  1.00 34.79           N  
ATOM   4634  CA  GLY A 757     223.552 209.262 216.527  1.00 34.44           C  
ATOM   4635  C   GLY A 757     223.619 210.057 215.237  1.00 33.97           C  
ATOM   4636  O   GLY A 757     223.927 211.248 215.232  1.00 33.91           O  
ATOM   4637  N   SER A 758     223.347 209.368 214.137  1.00 33.57           N  
ATOM   4638  CA  SER A 758     223.419 209.921 212.793  1.00 32.88           C  
ATOM   4639  C   SER A 758     222.129 210.573 212.334  1.00 32.71           C  
ATOM   4640  O   SER A 758     222.046 211.060 211.208  1.00 32.78           O  
ATOM   4641  CB  SER A 758     223.803 208.839 211.806  1.00 33.16           C  
ATOM   4642  OG  SER A 758     225.081 208.349 212.075  1.00 33.85           O  
ATOM   4643  N   PHE A 759     221.106 210.602 213.179  1.00 33.02           N  
ATOM   4644  CA  PHE A 759     219.855 211.218 212.733  1.00 32.09           C  
ATOM   4645  C   PHE A 759     220.033 212.651 212.249  1.00 31.74           C  
ATOM   4646  O   PHE A 759     219.361 213.050 211.303  1.00 32.21           O  
ATOM   4647  CB  PHE A 759     218.781 211.217 213.816  1.00 32.69           C  
ATOM   4648  CG  PHE A 759     217.874 210.034 213.838  1.00 32.74           C  
ATOM   4649  CD1 PHE A 759     217.587 209.391 215.019  1.00 33.51           C  
ATOM   4650  CD2 PHE A 759     217.269 209.577 212.677  1.00 32.21           C  
ATOM   4651  CE1 PHE A 759     216.732 208.329 215.051  1.00 33.51           C  
ATOM   4652  CE2 PHE A 759     216.415 208.509 212.716  1.00 32.75           C  
ATOM   4653  CZ  PHE A 759     216.153 207.891 213.912  1.00 32.95           C  
ATOM   4654  N   CYS A 760     220.905 213.431 212.905  1.00 31.76           N  
ATOM   4655  CA  CYS A 760     221.173 214.824 212.541  1.00 31.63           C  
ATOM   4656  C   CYS A 760     222.091 214.864 211.287  1.00 31.40           C  
ATOM   4657  O   CYS A 760     221.725 215.445 210.258  1.00 31.55           O  
ATOM   4658  CB  CYS A 760     221.803 215.554 213.759  1.00 32.68           C  
ATOM   4659  SG  CYS A 760     221.899 217.383 213.699  1.00 33.30           S  
ATOM   4660  N   THR A 761     223.256 214.193 211.354  1.00 31.42           N  
ATOM   4661  CA  THR A 761     224.277 214.197 210.295  1.00 31.29           C  
ATOM   4662  C   THR A 761     223.770 213.758 208.926  1.00 30.57           C  
ATOM   4663  O   THR A 761     224.146 214.346 207.910  1.00 31.12           O  
ATOM   4664  CB  THR A 761     225.467 213.300 210.677  1.00 32.13           C  
ATOM   4665  OG1 THR A 761     226.095 213.812 211.855  1.00 33.40           O  
ATOM   4666  CG2 THR A 761     226.482 213.257 209.546  1.00 32.20           C  
ATOM   4667  N   GLN A 762     222.945 212.720 208.876  1.00 30.86           N  
ATOM   4668  CA  GLN A 762     222.483 212.240 207.584  1.00 29.95           C  
ATOM   4669  C   GLN A 762     221.530 213.226 206.915  1.00 30.19           C  
ATOM   4670  O   GLN A 762     221.279 213.121 205.715  1.00 30.39           O  
ATOM   4671  CB  GLN A 762     221.831 210.864 207.688  1.00 30.36           C  
ATOM   4672  CG  GLN A 762     220.477 210.833 208.326  1.00 30.53           C  
ATOM   4673  CD  GLN A 762     219.990 209.416 208.472  1.00 30.62           C  
ATOM   4674  OE1 GLN A 762     219.553 208.785 207.503  1.00 30.57           O  
ATOM   4675  NE2 GLN A 762     220.066 208.893 209.687  1.00 31.55           N  
ATOM   4676  N   LEU A 763     220.974 214.169 207.674  1.00 30.10           N  
ATOM   4677  CA  LEU A 763     220.076 215.147 207.083  1.00 29.26           C  
ATOM   4678  C   LEU A 763     220.920 216.213 206.431  1.00 29.83           C  
ATOM   4679  O   LEU A 763     220.610 216.689 205.337  1.00 29.43           O  
ATOM   4680  CB  LEU A 763     219.170 215.760 208.148  1.00 30.37           C  
ATOM   4681  CG  LEU A 763     218.189 214.798 208.820  1.00 30.67           C  
ATOM   4682  CD1 LEU A 763     217.547 215.505 209.992  1.00 30.86           C  
ATOM   4683  CD2 LEU A 763     217.122 214.341 207.829  1.00 30.43           C  
ATOM   4684  N   ASN A 764     222.039 216.541 207.070  1.00 29.44           N  
ATOM   4685  CA  ASN A 764     222.950 217.505 206.478  1.00 29.21           C  
ATOM   4686  C   ASN A 764     223.471 216.929 205.170  1.00 28.65           C  
ATOM   4687  O   ASN A 764     223.643 217.649 204.182  1.00 28.83           O  
ATOM   4688  CB  ASN A 764     224.127 217.809 207.390  1.00 30.14           C  
ATOM   4689  CG  ASN A 764     223.819 218.675 208.594  1.00 30.74           C  
ATOM   4690  OD1 ASN A 764     222.761 219.308 208.726  1.00 30.85           O  
ATOM   4691  ND2 ASN A 764     224.777 218.715 209.487  1.00 30.88           N  
ATOM   4692  N   ARG A 765     223.700 215.617 205.166  1.00 28.87           N  
ATOM   4693  CA  ARG A 765     224.196 214.919 203.994  1.00 28.24           C  
ATOM   4694  C   ARG A 765     223.170 214.889 202.875  1.00 27.81           C  
ATOM   4695  O   ARG A 765     223.512 215.117 201.713  1.00 27.96           O  
ATOM   4696  CB  ARG A 765     224.590 213.501 204.355  1.00 29.29           C  
ATOM   4697  CG  ARG A 765     225.196 212.692 203.233  1.00 29.38           C  
ATOM   4698  CD  ARG A 765     225.732 211.399 203.729  1.00 29.86           C  
ATOM   4699  NE  ARG A 765     224.678 210.495 204.191  1.00 30.25           N  
ATOM   4700  CZ  ARG A 765     224.860 209.485 205.075  1.00 30.97           C  
ATOM   4701  NH1 ARG A 765     226.050 209.268 205.594  1.00 30.56           N  
ATOM   4702  NH2 ARG A 765     223.841 208.709 205.419  1.00 31.05           N  
ATOM   4703  N   ALA A 766     221.913 214.614 203.211  1.00 28.25           N  
ATOM   4704  CA  ALA A 766     220.869 214.558 202.201  1.00 27.69           C  
ATOM   4705  C   ALA A 766     220.700 215.896 201.501  1.00 26.85           C  
ATOM   4706  O   ALA A 766     220.579 215.948 200.276  1.00 26.89           O  
ATOM   4707  CB  ALA A 766     219.555 214.152 202.840  1.00 28.09           C  
ATOM   4708  N   LEU A 767     220.738 216.984 202.263  1.00 27.47           N  
ATOM   4709  CA  LEU A 767     220.579 218.299 201.664  1.00 26.68           C  
ATOM   4710  C   LEU A 767     221.793 218.688 200.846  1.00 26.21           C  
ATOM   4711  O   LEU A 767     221.658 219.330 199.802  1.00 26.63           O  
ATOM   4712  CB  LEU A 767     220.302 219.345 202.737  1.00 27.49           C  
ATOM   4713  CG  LEU A 767     218.939 219.237 203.443  1.00 27.87           C  
ATOM   4714  CD1 LEU A 767     218.920 220.202 204.593  1.00 29.10           C  
ATOM   4715  CD2 LEU A 767     217.803 219.560 202.466  1.00 28.07           C  
ATOM   4716  N   THR A 768     222.978 218.286 201.288  1.00 26.72           N  
ATOM   4717  CA  THR A 768     224.176 218.573 200.521  1.00 26.07           C  
ATOM   4718  C   THR A 768     224.085 217.891 199.169  1.00 25.35           C  
ATOM   4719  O   THR A 768     224.416 218.490 198.143  1.00 25.65           O  
ATOM   4720  CB  THR A 768     225.447 218.112 201.246  1.00 26.93           C  
ATOM   4721  OG1 THR A 768     225.578 218.822 202.482  1.00 27.84           O  
ATOM   4722  CG2 THR A 768     226.670 218.377 200.375  1.00 25.99           C  
ATOM   4723  N   GLY A 769     223.633 216.639 199.163  1.00 25.89           N  
ATOM   4724  CA  GLY A 769     223.505 215.886 197.927  1.00 25.13           C  
ATOM   4725  C   GLY A 769     222.577 216.589 196.949  1.00 24.70           C  
ATOM   4726  O   GLY A 769     222.869 216.658 195.753  1.00 24.84           O  
ATOM   4727  N   ILE A 770     221.489 217.159 197.456  1.00 24.84           N  
ATOM   4728  CA  ILE A 770     220.577 217.884 196.590  1.00 23.86           C  
ATOM   4729  C   ILE A 770     221.226 219.132 196.036  1.00 24.72           C  
ATOM   4730  O   ILE A 770     221.117 219.404 194.844  1.00 24.71           O  
ATOM   4731  CB  ILE A 770     219.286 218.285 197.320  1.00 24.43           C  
ATOM   4732  CG1 ILE A 770     218.502 217.040 197.758  1.00 24.90           C  
ATOM   4733  CG2 ILE A 770     218.430 219.202 196.443  1.00 24.27           C  
ATOM   4734  CD1 ILE A 770     218.118 216.073 196.648  1.00 26.02           C  
ATOM   4735  N   ALA A 771     221.920 219.889 196.869  1.00 24.61           N  
ATOM   4736  CA  ALA A 771     222.539 221.105 196.370  1.00 24.54           C  
ATOM   4737  C   ALA A 771     223.489 220.789 195.216  1.00 24.43           C  
ATOM   4738  O   ALA A 771     223.509 221.499 194.207  1.00 25.53           O  
ATOM   4739  CB  ALA A 771     223.278 221.808 197.492  1.00 25.53           C  
ATOM   4740  N   VAL A 772     224.226 219.688 195.327  1.00 23.87           N  
ATOM   4741  CA  VAL A 772     225.131 219.297 194.256  1.00 23.65           C  
ATOM   4742  C   VAL A 772     224.347 218.957 193.003  1.00 23.98           C  
ATOM   4743  O   VAL A 772     224.714 219.368 191.899  1.00 24.83           O  
ATOM   4744  CB  VAL A 772     225.988 218.096 194.672  1.00 24.04           C  
ATOM   4745  CG1 VAL A 772     226.786 217.578 193.476  1.00 23.52           C  
ATOM   4746  CG2 VAL A 772     226.919 218.519 195.789  1.00 24.46           C  
ATOM   4747  N   GLU A 773     223.262 218.215 193.178  1.00 23.98           N  
ATOM   4748  CA  GLU A 773     222.402 217.841 192.073  1.00 23.08           C  
ATOM   4749  C   GLU A 773     221.873 219.060 191.337  1.00 26.83           C  
ATOM   4750  O   GLU A 773     221.719 219.022 190.118  1.00 24.22           O  
ATOM   4751  CB  GLU A 773     221.239 216.989 192.561  1.00 23.69           C  
ATOM   4752  CG  GLU A 773     220.356 216.462 191.467  1.00 23.70           C  
ATOM   4753  CD  GLU A 773     219.334 215.506 191.975  1.00 24.08           C  
ATOM   4754  OE1 GLU A 773     218.458 215.915 192.697  1.00 24.06           O  
ATOM   4755  OE2 GLU A 773     219.435 214.348 191.650  1.00 23.68           O  
ATOM   4756  N   GLN A 774     221.583 220.139 192.056  1.00 24.04           N  
ATOM   4757  CA  GLN A 774     221.030 221.311 191.398  1.00 23.91           C  
ATOM   4758  C   GLN A 774     222.034 221.929 190.435  1.00 24.87           C  
ATOM   4759  O   GLN A 774     221.646 222.405 189.367  1.00 25.41           O  
ATOM   4760  CB  GLN A 774     220.557 222.344 192.416  1.00 24.56           C  
ATOM   4761  CG  GLN A 774     219.454 221.831 193.311  1.00 24.48           C  
ATOM   4762  CD  GLN A 774     218.362 221.164 192.541  1.00 24.68           C  
ATOM   4763  OE1 GLN A 774     217.755 221.759 191.656  1.00 25.29           O  
ATOM   4764  NE2 GLN A 774     218.102 219.909 192.854  1.00 24.51           N  
ATOM   4765  N   ASP A 775     223.326 221.870 190.756  1.00 24.46           N  
ATOM   4766  CA  ASP A 775     224.303 222.390 189.804  1.00 24.66           C  
ATOM   4767  C   ASP A 775     224.445 221.441 188.638  1.00 24.76           C  
ATOM   4768  O   ASP A 775     224.618 221.872 187.496  1.00 25.64           O  
ATOM   4769  CB  ASP A 775     225.673 222.605 190.435  1.00 26.12           C  
ATOM   4770  CG  ASP A 775     225.751 223.829 191.299  1.00 27.18           C  
ATOM   4771  OD1 ASP A 775     225.374 224.888 190.845  1.00 27.69           O  
ATOM   4772  OD2 ASP A 775     226.210 223.725 192.404  1.00 27.45           O  
ATOM   4773  N   LYS A 776     224.348 220.149 188.914  1.00 24.22           N  
ATOM   4774  CA  LYS A 776     224.411 219.167 187.850  1.00 23.81           C  
ATOM   4775  C   LYS A 776     223.294 219.407 186.847  1.00 24.06           C  
ATOM   4776  O   LYS A 776     223.525 219.359 185.640  1.00 24.58           O  
ATOM   4777  CB  LYS A 776     224.313 217.757 188.408  1.00 24.07           C  
ATOM   4778  CG  LYS A 776     224.380 216.663 187.374  1.00 24.17           C  
ATOM   4779  CD  LYS A 776     224.274 215.305 188.033  1.00 24.48           C  
ATOM   4780  CE  LYS A 776     224.187 214.200 187.006  1.00 24.74           C  
ATOM   4781  NZ  LYS A 776     224.055 212.865 187.646  1.00 24.84           N  
ATOM   4782  N   ASN A 777     222.085 219.681 187.345  1.00 24.17           N  
ATOM   4783  CA  ASN A 777     220.939 219.899 186.473  1.00 23.61           C  
ATOM   4784  C   ASN A 777     221.175 221.075 185.548  1.00 24.31           C  
ATOM   4785  O   ASN A 777     220.921 220.988 184.346  1.00 24.44           O  
ATOM   4786  CB  ASN A 777     219.687 220.174 187.281  1.00 24.19           C  
ATOM   4787  CG  ASN A 777     219.134 218.989 187.982  1.00 24.26           C  
ATOM   4788  OD1 ASN A 777     219.444 217.834 187.671  1.00 24.41           O  
ATOM   4789  ND2 ASN A 777     218.300 219.256 188.949  1.00 24.31           N  
ATOM   4790  N   THR A 778     221.707 222.162 186.086  1.00 24.01           N  
ATOM   4791  CA  THR A 778     221.945 223.326 185.263  1.00 23.60           C  
ATOM   4792  C   THR A 778     222.950 223.017 184.175  1.00 24.20           C  
ATOM   4793  O   THR A 778     222.766 223.411 183.024  1.00 24.55           O  
ATOM   4794  CB  THR A 778     222.438 224.511 186.092  1.00 24.91           C  
ATOM   4795  OG1 THR A 778     221.466 224.843 187.080  1.00 25.82           O  
ATOM   4796  CG2 THR A 778     222.649 225.703 185.213  1.00 25.96           C  
ATOM   4797  N   GLN A 779     224.022 222.315 184.518  1.00 23.84           N  
ATOM   4798  CA  GLN A 779     225.021 222.013 183.507  1.00 23.28           C  
ATOM   4799  C   GLN A 779     224.487 221.095 182.420  1.00 23.29           C  
ATOM   4800  O   GLN A 779     224.729 221.336 181.240  1.00 24.25           O  
ATOM   4801  CB  GLN A 779     226.251 221.372 184.131  1.00 23.84           C  
ATOM   4802  CG  GLN A 779     227.081 222.298 184.970  1.00 24.25           C  
ATOM   4803  CD  GLN A 779     228.212 221.566 185.625  1.00 24.84           C  
ATOM   4804  OE1 GLN A 779     228.152 220.343 185.764  1.00 24.69           O  
ATOM   4805  NE2 GLN A 779     229.251 222.287 186.024  1.00 24.66           N  
ATOM   4806  N   GLU A 780     223.703 220.083 182.780  1.00 23.46           N  
ATOM   4807  CA  GLU A 780     223.193 219.179 181.754  1.00 22.96           C  
ATOM   4808  C   GLU A 780     222.282 219.886 180.768  1.00 23.00           C  
ATOM   4809  O   GLU A 780     222.255 219.526 179.588  1.00 23.34           O  
ATOM   4810  CB  GLU A 780     222.466 217.975 182.355  1.00 23.25           C  
ATOM   4811  CG  GLU A 780     223.388 216.947 183.013  1.00 23.59           C  
ATOM   4812  CD  GLU A 780     222.668 215.698 183.441  1.00 23.64           C  
ATOM   4813  OE1 GLU A 780     221.465 215.691 183.403  1.00 22.91           O  
ATOM   4814  OE2 GLU A 780     223.326 214.744 183.793  1.00 23.67           O  
ATOM   4815  N   VAL A 781     221.536 220.877 181.241  1.00 23.15           N  
ATOM   4816  CA  VAL A 781     220.644 221.608 180.363  1.00 22.51           C  
ATOM   4817  C   VAL A 781     221.375 222.618 179.496  1.00 22.90           C  
ATOM   4818  O   VAL A 781     221.112 222.694 178.305  1.00 23.23           O  
ATOM   4819  CB  VAL A 781     219.549 222.329 181.163  1.00 22.88           C  
ATOM   4820  CG1 VAL A 781     218.701 223.210 180.238  1.00 23.20           C  
ATOM   4821  CG2 VAL A 781     218.680 221.303 181.835  1.00 22.83           C  
ATOM   4822  N   PHE A 782     222.260 223.424 180.075  1.00 23.18           N  
ATOM   4823  CA  PHE A 782     222.850 224.508 179.295  1.00 22.98           C  
ATOM   4824  C   PHE A 782     224.233 224.246 178.712  1.00 23.04           C  
ATOM   4825  O   PHE A 782     224.556 224.754 177.640  1.00 23.92           O  
ATOM   4826  CB  PHE A 782     222.919 225.765 180.147  1.00 23.65           C  
ATOM   4827  CG  PHE A 782     221.587 226.313 180.499  1.00 23.90           C  
ATOM   4828  CD1 PHE A 782     221.043 226.085 181.737  1.00 24.37           C  
ATOM   4829  CD2 PHE A 782     220.877 227.061 179.597  1.00 23.80           C  
ATOM   4830  CE1 PHE A 782     219.819 226.599 182.074  1.00 24.55           C  
ATOM   4831  CE2 PHE A 782     219.651 227.578 179.928  1.00 24.15           C  
ATOM   4832  CZ  PHE A 782     219.126 227.349 181.171  1.00 24.55           C  
ATOM   4833  N   ALA A 783     225.073 223.481 179.391  1.00 23.40           N  
ATOM   4834  CA  ALA A 783     226.441 223.302 178.920  1.00 23.11           C  
ATOM   4835  C   ALA A 783     226.514 222.155 177.930  1.00 22.86           C  
ATOM   4836  O   ALA A 783     227.172 221.146 178.175  1.00 22.89           O  
ATOM   4837  CB  ALA A 783     227.375 223.054 180.090  1.00 23.96           C  
ATOM   4838  N   GLN A 784     225.827 222.316 176.807  1.00 22.80           N  
ATOM   4839  CA  GLN A 784     225.758 221.285 175.780  1.00 22.62           C  
ATOM   4840  C   GLN A 784     226.668 221.600 174.614  1.00 22.89           C  
ATOM   4841  O   GLN A 784     226.696 220.881 173.616  1.00 23.04           O  
ATOM   4842  CB  GLN A 784     224.327 221.114 175.288  1.00 22.09           C  
ATOM   4843  CG  GLN A 784     223.396 220.655 176.363  1.00 22.57           C  
ATOM   4844  CD  GLN A 784     222.026 220.346 175.865  1.00 21.89           C  
ATOM   4845  OE1 GLN A 784     221.685 220.579 174.700  1.00 21.66           O  
ATOM   4846  NE2 GLN A 784     221.217 219.800 176.757  1.00 21.89           N  
ATOM   4847  N   VAL A 785     227.390 222.693 174.734  1.00 22.92           N  
ATOM   4848  CA  VAL A 785     228.272 223.140 173.686  1.00 23.23           C  
ATOM   4849  C   VAL A 785     229.678 223.294 174.259  1.00 23.57           C  
ATOM   4850  O   VAL A 785     229.847 223.823 175.354  1.00 23.92           O  
ATOM   4851  CB  VAL A 785     227.717 224.450 173.102  1.00 23.20           C  
ATOM   4852  CG1 VAL A 785     227.723 225.565 174.151  1.00 23.41           C  
ATOM   4853  CG2 VAL A 785     228.480 224.825 171.898  1.00 23.29           C  
ATOM   4854  N   LYS A 786     230.685 222.825 173.526  1.00 23.78           N  
ATOM   4855  CA  LYS A 786     232.068 222.862 174.010  1.00 23.98           C  
ATOM   4856  C   LYS A 786     232.795 224.149 173.643  1.00 24.41           C  
ATOM   4857  O   LYS A 786     233.931 224.385 174.073  1.00 24.61           O  
ATOM   4858  CB  LYS A 786     232.838 221.667 173.456  1.00 24.29           C  
ATOM   4859  N   GLN A 787     232.145 224.958 172.831  1.00 24.21           N  
ATOM   4860  CA  GLN A 787     232.695 226.219 172.377  1.00 23.65           C  
ATOM   4861  C   GLN A 787     231.669 227.323 172.505  1.00 24.39           C  
ATOM   4862  O   GLN A 787     230.467 227.090 172.414  1.00 24.38           O  
ATOM   4863  CB  GLN A 787     233.163 226.110 170.934  1.00 23.90           C  
ATOM   4864  CG  GLN A 787     234.258 225.101 170.722  1.00 24.18           C  
ATOM   4865  CD  GLN A 787     234.740 225.097 169.307  1.00 23.84           C  
ATOM   4866  OE1 GLN A 787     233.957 225.335 168.383  1.00 23.78           O  
ATOM   4867  NE2 GLN A 787     236.023 224.826 169.110  1.00 23.39           N  
ATOM   4868  N   ILE A 788     232.139 228.533 172.685  1.00 23.92           N  
ATOM   4869  CA  ILE A 788     231.242 229.658 172.723  1.00 24.19           C  
ATOM   4870  C   ILE A 788     231.214 230.314 171.364  1.00 24.29           C  
ATOM   4871  O   ILE A 788     232.174 230.964 170.945  1.00 24.96           O  
ATOM   4872  CB  ILE A 788     231.667 230.650 173.814  1.00 24.76           C  
ATOM   4873  CG1 ILE A 788     231.760 229.913 175.181  1.00 25.35           C  
ATOM   4874  CG2 ILE A 788     230.724 231.842 173.870  1.00 25.92           C  
ATOM   4875  CD1 ILE A 788     230.471 229.217 175.643  1.00 25.66           C  
ATOM   4876  N   TYR A 789     230.104 230.125 170.676  1.00 24.04           N  
ATOM   4877  CA  TYR A 789     229.942 230.618 169.330  1.00 23.21           C  
ATOM   4878  C   TYR A 789     229.452 232.037 169.376  1.00 23.50           C  
ATOM   4879  O   TYR A 789     228.751 232.431 170.305  1.00 24.32           O  
ATOM   4880  CB  TYR A 789     228.973 229.743 168.548  1.00 23.36           C  
ATOM   4881  CG  TYR A 789     229.473 228.353 168.365  1.00 22.85           C  
ATOM   4882  CD1 TYR A 789     228.811 227.312 168.954  1.00 23.03           C  
ATOM   4883  CD2 TYR A 789     230.607 228.115 167.633  1.00 23.03           C  
ATOM   4884  CE1 TYR A 789     229.279 226.038 168.803  1.00 22.76           C  
ATOM   4885  CE2 TYR A 789     231.076 226.842 167.491  1.00 22.98           C  
ATOM   4886  CZ  TYR A 789     230.411 225.805 168.075  1.00 22.94           C  
ATOM   4887  OH  TYR A 789     230.870 224.521 167.938  1.00 22.79           O  
ATOM   4888  N   LYS A 790     229.823 232.806 168.376  1.00 23.45           N  
ATOM   4889  CA  LYS A 790     229.385 234.179 168.292  1.00 24.02           C  
ATOM   4890  C   LYS A 790     228.889 234.498 166.900  1.00 24.09           C  
ATOM   4891  O   LYS A 790     229.446 234.028 165.902  1.00 23.94           O  
ATOM   4892  CB  LYS A 790     230.532 235.111 168.662  1.00 24.23           C  
ATOM   4893  CG  LYS A 790     231.053 234.914 170.077  1.00 24.71           C  
ATOM   4894  CD  LYS A 790     232.271 235.772 170.356  1.00 25.21           C  
ATOM   4895  CE  LYS A 790     231.908 237.225 170.596  1.00 25.32           C  
ATOM   4896  NZ  LYS A 790     233.083 238.005 171.055  1.00 24.92           N  
ATOM   4897  N   THR A 791     227.862 235.333 166.835  1.00 24.32           N  
ATOM   4898  CA  THR A 791     227.342 235.806 165.569  1.00 24.09           C  
ATOM   4899  C   THR A 791     228.245 236.908 165.040  1.00 24.34           C  
ATOM   4900  O   THR A 791     228.954 237.544 165.820  1.00 24.26           O  
ATOM   4901  CB  THR A 791     225.908 236.341 165.761  1.00 24.20           C  
ATOM   4902  OG1 THR A 791     225.930 237.374 166.749  1.00 24.40           O  
ATOM   4903  CG2 THR A 791     224.974 235.226 166.186  1.00 24.15           C  
ATOM   4904  N   PRO A 792     228.224 237.176 163.736  1.00 24.29           N  
ATOM   4905  CA  PRO A 792     228.918 238.264 163.087  1.00 24.26           C  
ATOM   4906  C   PRO A 792     228.283 239.601 163.450  1.00 24.29           C  
ATOM   4907  O   PRO A 792     227.110 239.642 163.831  1.00 24.52           O  
ATOM   4908  CB  PRO A 792     228.737 237.921 161.605  1.00 23.91           C  
ATOM   4909  CG  PRO A 792     227.482 237.101 161.559  1.00 24.00           C  
ATOM   4910  CD  PRO A 792     227.512 236.282 162.816  1.00 23.83           C  
ATOM   4911  N   PRO A 793     229.027 240.704 163.302  1.00 23.87           N  
ATOM   4912  CA  PRO A 793     228.596 242.078 163.490  1.00 24.19           C  
ATOM   4913  C   PRO A 793     227.525 242.484 162.483  1.00 24.13           C  
ATOM   4914  O   PRO A 793     226.751 243.407 162.731  1.00 24.00           O  
ATOM   4915  CB  PRO A 793     229.898 242.863 163.289  1.00 24.05           C  
ATOM   4916  CG  PRO A 793     230.782 241.953 162.463  1.00 24.01           C  
ATOM   4917  CD  PRO A 793     230.433 240.562 162.909  1.00 23.95           C  
ATOM   4918  N   ILE A 794     227.464 241.773 161.366  1.00 23.96           N  
ATOM   4919  CA  ILE A 794     226.478 242.048 160.336  1.00 24.50           C  
ATOM   4920  C   ILE A 794     225.389 240.998 160.392  1.00 24.37           C  
ATOM   4921  O   ILE A 794     225.653 239.814 160.214  1.00 23.94           O  
ATOM   4922  CB  ILE A 794     227.127 242.047 158.944  1.00 24.30           C  
ATOM   4923  CG1 ILE A 794     228.219 243.131 158.893  1.00 24.47           C  
ATOM   4924  CG2 ILE A 794     226.058 242.271 157.869  1.00 24.29           C  
ATOM   4925  CD1 ILE A 794     229.119 243.051 157.683  1.00 24.69           C  
ATOM   4926  N   LYS A 795     224.160 241.425 160.641  1.00 24.30           N  
ATOM   4927  CA  LYS A 795     223.071 240.474 160.806  1.00 24.03           C  
ATOM   4928  C   LYS A 795     222.404 240.157 159.471  1.00 24.28           C  
ATOM   4929  O   LYS A 795     221.216 240.420 159.269  1.00 24.15           O  
ATOM   4930  CB  LYS A 795     222.051 241.045 161.793  1.00 24.24           C  
ATOM   4931  CG  LYS A 795     222.658 241.480 163.145  1.00 24.35           C  
ATOM   4932  CD  LYS A 795     223.192 240.308 163.965  1.00 24.07           C  
ATOM   4933  CE  LYS A 795     223.850 240.780 165.251  1.00 24.29           C  
ATOM   4934  NZ  LYS A 795     225.158 241.441 164.990  1.00 24.01           N  
ATOM   4935  N   ASP A 796     223.164 239.567 158.562  1.00 24.12           N  
ATOM   4936  CA  ASP A 796     222.657 239.231 157.241  1.00 24.03           C  
ATOM   4937  C   ASP A 796     222.035 237.846 157.222  1.00 24.09           C  
ATOM   4938  O   ASP A 796     222.541 236.918 156.590  1.00 23.54           O  
ATOM   4939  CB  ASP A 796     223.754 239.397 156.189  1.00 24.26           C  
ATOM   4940  CG  ASP A 796     225.036 238.691 156.544  1.00 24.21           C  
ATOM   4941  OD1 ASP A 796     225.190 238.337 157.685  1.00 23.96           O  
ATOM   4942  OD2 ASP A 796     225.864 238.524 155.681  1.00 24.01           O  
ATOM   4943  N   PHE A 797     220.891 237.736 157.886  1.00 23.79           N  
ATOM   4944  CA  PHE A 797     220.207 236.462 158.055  1.00 23.13           C  
ATOM   4945  C   PHE A 797     218.985 236.326 157.163  1.00 23.30           C  
ATOM   4946  O   PHE A 797     218.012 235.671 157.520  1.00 23.79           O  
ATOM   4947  CB  PHE A 797     219.805 236.256 159.509  1.00 23.11           C  
ATOM   4948  CG  PHE A 797     220.964 236.245 160.435  1.00 22.94           C  
ATOM   4949  CD1 PHE A 797     221.041 237.139 161.467  1.00 23.81           C  
ATOM   4950  CD2 PHE A 797     221.992 235.357 160.262  1.00 23.13           C  
ATOM   4951  CE1 PHE A 797     222.120 237.133 162.313  1.00 23.63           C  
ATOM   4952  CE2 PHE A 797     223.074 235.357 161.098  1.00 23.05           C  
ATOM   4953  CZ  PHE A 797     223.138 236.245 162.127  1.00 23.35           C  
ATOM   4954  N   GLY A 798     219.017 236.969 156.009  1.00 23.31           N  
ATOM   4955  CA  GLY A 798     217.968 236.781 155.016  1.00 23.12           C  
ATOM   4956  C   GLY A 798     216.650 237.443 155.372  1.00 23.56           C  
ATOM   4957  O   GLY A 798     215.598 237.010 154.904  1.00 23.62           O  
ATOM   4958  N   GLY A 799     216.694 238.483 156.192  1.00 23.79           N  
ATOM   4959  CA  GLY A 799     215.476 239.167 156.597  1.00 24.06           C  
ATOM   4960  C   GLY A 799     214.967 238.723 157.962  1.00 24.17           C  
ATOM   4961  O   GLY A 799     214.052 239.340 158.510  1.00 24.45           O  
ATOM   4962  N   PHE A 800     215.560 237.679 158.526  1.00 24.03           N  
ATOM   4963  CA  PHE A 800     215.132 237.220 159.837  1.00 23.51           C  
ATOM   4964  C   PHE A 800     215.811 238.050 160.923  1.00 24.32           C  
ATOM   4965  O   PHE A 800     217.041 238.098 160.994  1.00 25.04           O  
ATOM   4966  CB  PHE A 800     215.478 235.749 160.013  1.00 23.64           C  
ATOM   4967  CG  PHE A 800     214.646 234.836 159.189  1.00 23.14           C  
ATOM   4968  CD1 PHE A 800     214.916 234.653 157.849  1.00 23.37           C  
ATOM   4969  CD2 PHE A 800     213.609 234.136 159.752  1.00 23.29           C  
ATOM   4970  CE1 PHE A 800     214.167 233.802 157.094  1.00 22.95           C  
ATOM   4971  CE2 PHE A 800     212.855 233.279 158.999  1.00 22.98           C  
ATOM   4972  CZ  PHE A 800     213.139 233.113 157.664  1.00 23.00           C  
ATOM   4973  N   ASN A 801     215.002 238.722 161.752  1.00 25.22           N  
ATOM   4974  CA  ASN A 801     215.461 239.616 162.813  1.00 25.73           C  
ATOM   4975  C   ASN A 801     215.535 238.879 164.153  1.00 25.87           C  
ATOM   4976  O   ASN A 801     214.518 238.593 164.780  1.00 25.90           O  
ATOM   4977  CB  ASN A 801     214.538 240.835 162.903  1.00 27.03           C  
ATOM   4978  CG  ASN A 801     215.044 241.947 163.833  1.00 28.07           C  
ATOM   4979  OD1 ASN A 801     215.982 241.749 164.633  1.00 28.53           O  
ATOM   4980  ND2 ASN A 801     214.413 243.114 163.730  1.00 29.19           N  
ATOM   4981  N   PHE A 802     216.768 238.573 164.595  1.00 26.07           N  
ATOM   4982  CA  PHE A 802     217.022 237.833 165.829  1.00 25.91           C  
ATOM   4983  C   PHE A 802     217.531 238.744 166.931  1.00 27.12           C  
ATOM   4984  O   PHE A 802     217.940 238.268 167.988  1.00 27.82           O  
ATOM   4985  CB  PHE A 802     218.057 236.737 165.598  1.00 25.48           C  
ATOM   4986  CG  PHE A 802     217.647 235.711 164.627  1.00 24.68           C  
ATOM   4987  CD1 PHE A 802     218.332 235.548 163.452  1.00 24.34           C  
ATOM   4988  CD2 PHE A 802     216.576 234.906 164.876  1.00 24.59           C  
ATOM   4989  CE1 PHE A 802     217.950 234.596 162.558  1.00 23.99           C  
ATOM   4990  CE2 PHE A 802     216.198 233.960 163.984  1.00 23.74           C  
ATOM   4991  CZ  PHE A 802     216.880 233.805 162.832  1.00 23.37           C  
ATOM   4992  N   SER A 803     217.496 240.053 166.711  1.00 27.22           N  
ATOM   4993  CA  SER A 803     218.083 240.975 167.686  1.00 27.46           C  
ATOM   4994  C   SER A 803     217.341 240.988 169.012  1.00 27.69           C  
ATOM   4995  O   SER A 803     217.866 241.458 170.019  1.00 27.84           O  
ATOM   4996  CB  SER A 803     218.124 242.382 167.149  1.00 28.05           C  
ATOM   4997  OG  SER A 803     216.843 242.910 167.057  1.00 28.43           O  
ATOM   4998  N   GLN A 804     216.124 240.469 169.024  1.00 27.37           N  
ATOM   4999  CA  GLN A 804     215.322 240.448 170.231  1.00 27.52           C  
ATOM   5000  C   GLN A 804     215.639 239.238 171.108  1.00 27.45           C  
ATOM   5001  O   GLN A 804     215.245 239.196 172.277  1.00 28.61           O  
ATOM   5002  CB  GLN A 804     213.851 240.472 169.847  1.00 27.95           C  
ATOM   5003  CG  GLN A 804     213.452 241.755 169.130  1.00 28.36           C  
ATOM   5004  CD  GLN A 804     211.987 241.793 168.736  1.00 28.44           C  
ATOM   5005  OE1 GLN A 804     211.207 240.937 169.134  1.00 28.04           O  
ATOM   5006  NE2 GLN A 804     211.604 242.789 167.956  1.00 29.58           N  
ATOM   5007  N   ILE A 805     216.355 238.259 170.545  1.00 27.26           N  
ATOM   5008  CA  ILE A 805     216.733 237.063 171.293  1.00 26.86           C  
ATOM   5009  C   ILE A 805     218.253 236.954 171.474  1.00 27.47           C  
ATOM   5010  O   ILE A 805     218.727 236.227 172.351  1.00 27.90           O  
ATOM   5011  CB  ILE A 805     216.142 235.793 170.650  1.00 26.80           C  
ATOM   5012  CG1 ILE A 805     216.641 235.610 169.225  1.00 26.40           C  
ATOM   5013  CG2 ILE A 805     214.640 235.873 170.699  1.00 26.89           C  
ATOM   5014  CD1 ILE A 805     216.311 234.259 168.645  1.00 24.85           C  
ATOM   5015  N   LEU A 806     219.008 237.708 170.671  1.00 27.62           N  
ATOM   5016  CA  LEU A 806     220.459 237.808 170.795  1.00 27.78           C  
ATOM   5017  C   LEU A 806     220.803 238.751 171.942  1.00 28.81           C  
ATOM   5018  O   LEU A 806     220.038 239.670 172.226  1.00 29.68           O  
ATOM   5019  CB  LEU A 806     221.056 238.318 169.471  1.00 27.95           C  
ATOM   5020  CG  LEU A 806     220.962 237.360 168.269  1.00 27.01           C  
ATOM   5021  CD1 LEU A 806     221.321 238.100 166.999  1.00 26.36           C  
ATOM   5022  CD2 LEU A 806     221.929 236.213 168.463  1.00 26.13           C  
ATOM   5023  N   PRO A 807     221.935 238.558 172.624  1.00 29.27           N  
ATOM   5024  CA  PRO A 807     222.376 239.356 173.749  1.00 30.27           C  
ATOM   5025  C   PRO A 807     222.667 240.785 173.351  1.00 31.08           C  
ATOM   5026  O   PRO A 807     223.208 241.032 172.274  1.00 31.26           O  
ATOM   5027  CB  PRO A 807     223.647 238.636 174.195  1.00 30.34           C  
ATOM   5028  CG  PRO A 807     224.112 237.888 172.972  1.00 29.70           C  
ATOM   5029  CD  PRO A 807     222.846 237.483 172.251  1.00 28.82           C  
ATOM   5030  N   ASP A 808     222.336 241.717 174.240  1.00 32.04           N  
ATOM   5031  CA  ASP A 808     222.599 243.129 174.036  1.00 32.63           C  
ATOM   5032  C   ASP A 808     223.924 243.527 174.696  1.00 33.18           C  
ATOM   5033  O   ASP A 808     224.009 243.576 175.924  1.00 34.00           O  
ATOM   5034  CB  ASP A 808     221.455 243.962 174.607  1.00 33.46           C  
ATOM   5035  CG  ASP A 808     221.625 245.449 174.369  1.00 33.98           C  
ATOM   5036  OD1 ASP A 808     222.738 245.882 174.107  1.00 34.51           O  
ATOM   5037  OD2 ASP A 808     220.643 246.150 174.436  1.00 34.86           O  
ATOM   5038  N   PRO A 809     224.976 243.804 173.920  1.00 34.42           N  
ATOM   5039  CA  PRO A 809     226.330 244.027 174.381  1.00 34.13           C  
ATOM   5040  C   PRO A 809     226.497 245.330 175.151  1.00 35.36           C  
ATOM   5041  O   PRO A 809     227.522 245.533 175.806  1.00 34.48           O  
ATOM   5042  CB  PRO A 809     227.124 244.056 173.069  1.00 34.63           C  
ATOM   5043  CG  PRO A 809     226.132 244.529 172.029  1.00 34.69           C  
ATOM   5044  CD  PRO A 809     224.803 243.952 172.463  1.00 34.07           C  
ATOM   5045  N   SER A 810     225.515 246.228 175.056  1.00 34.14           N  
ATOM   5046  CA  SER A 810     225.642 247.537 175.684  1.00 34.70           C  
ATOM   5047  C   SER A 810     225.282 247.520 177.163  1.00 35.02           C  
ATOM   5048  O   SER A 810     225.502 248.503 177.873  1.00 34.51           O  
ATOM   5049  CB  SER A 810     224.775 248.556 174.974  1.00 34.67           C  
ATOM   5050  OG  SER A 810     223.419 248.336 175.227  1.00 34.57           O  
ATOM   5051  N   LYS A 811     224.700 246.423 177.627  1.00 34.35           N  
ATOM   5052  CA  LYS A 811     224.255 246.354 179.008  1.00 34.83           C  
ATOM   5053  C   LYS A 811     225.325 245.752 179.927  1.00 34.88           C  
ATOM   5054  O   LYS A 811     226.215 245.050 179.453  1.00 34.03           O  
ATOM   5055  CB  LYS A 811     222.961 245.556 179.094  1.00 34.27           C  
ATOM   5056  CG  LYS A 811     221.785 246.231 178.421  1.00 34.32           C  
ATOM   5057  CD  LYS A 811     220.518 245.442 178.652  1.00 33.49           C  
ATOM   5058  CE  LYS A 811     219.320 246.100 178.005  1.00 33.50           C  
ATOM   5059  NZ  LYS A 811     218.077 245.354 178.302  1.00 32.24           N  
ATOM   5060  N   SER A 813     224.833 243.419 181.849  1.00 34.66           N  
ATOM   5061  CA  SER A 813     224.560 241.995 181.824  1.00 33.90           C  
ATOM   5062  C   SER A 813     224.233 241.629 180.392  1.00 33.89           C  
ATOM   5063  O   SER A 813     223.293 242.166 179.805  1.00 33.56           O  
ATOM   5064  CB  SER A 813     223.413 241.653 182.749  1.00 32.98           C  
ATOM   5065  OG  SER A 813     223.147 240.282 182.727  1.00 32.18           O  
ATOM   5066  N   LYS A 814     225.034 240.741 179.820  1.00 33.12           N  
ATOM   5067  CA  LYS A 814     224.945 240.425 178.400  1.00 32.65           C  
ATOM   5068  C   LYS A 814     223.765 239.529 178.077  1.00 31.68           C  
ATOM   5069  O   LYS A 814     223.927 238.359 177.735  1.00 30.94           O  
ATOM   5070  CB  LYS A 814     226.234 239.731 177.957  1.00 33.22           C  
ATOM   5071  N   ARG A 815     222.571 240.094 178.164  1.00 31.58           N  
ATOM   5072  CA  ARG A 815     221.349 239.344 177.942  1.00 30.43           C  
ATOM   5073  C   ARG A 815     220.503 240.008 176.879  1.00 30.66           C  
ATOM   5074  O   ARG A 815     220.676 241.185 176.573  1.00 31.84           O  
ATOM   5075  CB  ARG A 815     220.560 239.216 179.225  1.00 30.63           C  
ATOM   5076  CG  ARG A 815     221.308 238.507 180.316  1.00 30.96           C  
ATOM   5077  CD  ARG A 815     220.456 238.135 181.465  1.00 30.21           C  
ATOM   5078  NE  ARG A 815     219.789 239.287 182.058  1.00 30.29           N  
ATOM   5079  CZ  ARG A 815     219.515 239.442 183.365  1.00 30.25           C  
ATOM   5080  NH1 ARG A 815     219.887 238.538 184.251  1.00 29.99           N  
ATOM   5081  NH2 ARG A 815     218.868 240.525 183.740  1.00 30.29           N  
ATOM   5082  N   SER A 816     219.629 239.232 176.272  1.00 29.65           N  
ATOM   5083  CA  SER A 816     218.740 239.715 175.231  1.00 28.62           C  
ATOM   5084  C   SER A 816     217.569 240.466 175.807  1.00 28.49           C  
ATOM   5085  O   SER A 816     217.314 240.405 177.008  1.00 30.49           O  
ATOM   5086  CB  SER A 816     218.227 238.558 174.443  1.00 29.77           C  
ATOM   5087  OG  SER A 816     217.407 237.776 175.236  1.00 28.50           O  
ATOM   5088  N   PHE A 817     216.837 241.162 174.948  1.00 28.67           N  
ATOM   5089  CA  PHE A 817     215.662 241.882 175.401  1.00 28.64           C  
ATOM   5090  C   PHE A 817     214.677 240.931 176.057  1.00 30.00           C  
ATOM   5091  O   PHE A 817     214.212 241.177 177.170  1.00 29.12           O  
ATOM   5092  CB  PHE A 817     214.979 242.583 174.242  1.00 28.40           C  
ATOM   5093  CG  PHE A 817     213.801 243.374 174.652  1.00 28.54           C  
ATOM   5094  CD1 PHE A 817     213.938 244.700 174.981  1.00 28.29           C  
ATOM   5095  CD2 PHE A 817     212.556 242.801 174.727  1.00 28.72           C  
ATOM   5096  CE1 PHE A 817     212.848 245.440 175.362  1.00 28.98           C  
ATOM   5097  CE2 PHE A 817     211.468 243.533 175.103  1.00 29.01           C  
ATOM   5098  CZ  PHE A 817     211.611 244.855 175.420  1.00 29.54           C  
ATOM   5099  N   ILE A 818     214.371 239.825 175.388  1.00 28.00           N  
ATOM   5100  CA  ILE A 818     213.437 238.879 175.971  1.00 28.20           C  
ATOM   5101  C   ILE A 818     213.943 238.301 177.277  1.00 30.24           C  
ATOM   5102  O   ILE A 818     213.169 238.153 178.221  1.00 29.60           O  
ATOM   5103  CB  ILE A 818     213.024 237.788 174.976  1.00 28.28           C  
ATOM   5104  CG1 ILE A 818     212.111 238.437 173.914  1.00 28.25           C  
ATOM   5105  CG2 ILE A 818     212.344 236.628 175.693  1.00 28.35           C  
ATOM   5106  CD1 ILE A 818     211.801 237.588 172.715  1.00 27.99           C  
ATOM   5107  N   GLU A 819     215.220 237.973 177.366  1.00 28.71           N  
ATOM   5108  CA  GLU A 819     215.704 237.444 178.630  1.00 28.38           C  
ATOM   5109  C   GLU A 819     215.517 238.437 179.769  1.00 32.48           C  
ATOM   5110  O   GLU A 819     215.056 238.057 180.843  1.00 28.99           O  
ATOM   5111  CB  GLU A 819     217.158 237.037 178.513  1.00 28.75           C  
ATOM   5112  CG  GLU A 819     217.356 235.779 177.730  1.00 28.52           C  
ATOM   5113  CD  GLU A 819     218.762 235.532 177.395  1.00 28.63           C  
ATOM   5114  OE1 GLU A 819     219.390 236.418 176.870  1.00 29.38           O  
ATOM   5115  OE2 GLU A 819     219.226 234.451 177.651  1.00 28.02           O  
ATOM   5116  N   ASP A 820     215.771 239.721 179.536  1.00 28.82           N  
ATOM   5117  CA  ASP A 820     215.542 240.686 180.607  1.00 28.98           C  
ATOM   5118  C   ASP A 820     214.089 240.678 181.050  1.00 29.93           C  
ATOM   5119  O   ASP A 820     213.801 240.770 182.246  1.00 31.27           O  
ATOM   5120  CB  ASP A 820     215.934 242.097 180.189  1.00 30.10           C  
ATOM   5121  CG  ASP A 820     217.431 242.371 180.237  1.00 30.84           C  
ATOM   5122  OD1 ASP A 820     218.151 241.665 180.921  1.00 30.51           O  
ATOM   5123  OD2 ASP A 820     217.844 243.316 179.594  1.00 31.50           O  
ATOM   5124  N   LEU A 821     213.171 240.526 180.102  1.00 29.29           N  
ATOM   5125  CA  LEU A 821     211.763 240.448 180.456  1.00 29.28           C  
ATOM   5126  C   LEU A 821     211.485 239.220 181.299  1.00 28.93           C  
ATOM   5127  O   LEU A 821     210.670 239.269 182.215  1.00 30.77           O  
ATOM   5128  CB  LEU A 821     210.877 240.401 179.210  1.00 29.43           C  
ATOM   5129  CG  LEU A 821     210.333 241.730 178.699  1.00 29.77           C  
ATOM   5130  CD1 LEU A 821     211.473 242.697 178.430  1.00 29.56           C  
ATOM   5131  CD2 LEU A 821     209.531 241.464 177.427  1.00 29.67           C  
ATOM   5132  N   LEU A 822     212.155 238.114 181.002  1.00 29.21           N  
ATOM   5133  CA  LEU A 822     211.911 236.900 181.761  1.00 29.11           C  
ATOM   5134  C   LEU A 822     212.386 237.068 183.196  1.00 29.39           C  
ATOM   5135  O   LEU A 822     211.699 236.685 184.142  1.00 30.23           O  
ATOM   5136  CB  LEU A 822     212.648 235.708 181.124  1.00 28.90           C  
ATOM   5137  CG  LEU A 822     212.174 235.260 179.718  1.00 28.72           C  
ATOM   5138  CD1 LEU A 822     213.132 234.220 179.170  1.00 27.83           C  
ATOM   5139  CD2 LEU A 822     210.805 234.691 179.801  1.00 29.55           C  
ATOM   5140  N   PHE A 823     213.540 237.693 183.368  1.00 28.54           N  
ATOM   5141  CA  PHE A 823     214.103 237.880 184.698  1.00 29.06           C  
ATOM   5142  C   PHE A 823     213.270 238.811 185.548  1.00 29.61           C  
ATOM   5143  O   PHE A 823     213.065 238.564 186.735  1.00 30.00           O  
ATOM   5144  CB  PHE A 823     215.542 238.377 184.607  1.00 29.06           C  
ATOM   5145  CG  PHE A 823     216.521 237.256 184.468  1.00 29.00           C  
ATOM   5146  CD1 PHE A 823     216.822 236.697 183.245  1.00 29.24           C  
ATOM   5147  CD2 PHE A 823     217.141 236.749 185.580  1.00 29.01           C  
ATOM   5148  CE1 PHE A 823     217.706 235.654 183.142  1.00 28.55           C  
ATOM   5149  CE2 PHE A 823     218.026 235.706 185.484  1.00 28.58           C  
ATOM   5150  CZ  PHE A 823     218.308 235.155 184.263  1.00 28.31           C  
ATOM   5151  N   ASN A 824     212.731 239.843 184.937  1.00 29.87           N  
ATOM   5152  CA  ASN A 824     211.980 240.840 185.672  1.00 29.86           C  
ATOM   5153  C   ASN A 824     210.598 240.363 186.112  1.00 30.24           C  
ATOM   5154  O   ASN A 824     209.888 241.094 186.803  1.00 30.34           O  
ATOM   5155  CB  ASN A 824     211.853 242.090 184.836  1.00 30.20           C  
ATOM   5156  CG  ASN A 824     213.163 242.783 184.663  1.00 30.81           C  
ATOM   5157  OD1 ASN A 824     214.084 242.626 185.472  1.00 31.14           O  
ATOM   5158  ND2 ASN A 824     213.274 243.552 183.615  1.00 31.27           N  
ATOM   5159  N   LYS A 825     210.190 239.161 185.701  1.00 29.72           N  
ATOM   5160  CA  LYS A 825     208.868 238.674 186.070  1.00 29.60           C  
ATOM   5161  C   LYS A 825     208.887 237.533 187.082  1.00 29.78           C  
ATOM   5162  O   LYS A 825     207.828 237.027 187.452  1.00 29.94           O  
ATOM   5163  CB  LYS A 825     208.097 238.260 184.819  1.00 29.85           C  
ATOM   5164  CG  LYS A 825     207.860 239.386 183.816  1.00 30.14           C  
ATOM   5165  CD  LYS A 825     206.928 240.468 184.351  1.00 30.78           C  
ATOM   5166  CE  LYS A 825     206.722 241.560 183.312  1.00 30.92           C  
ATOM   5167  NZ  LYS A 825     205.816 242.641 183.801  1.00 29.55           N  
ATOM   5168  N   VAL A 826     210.066 237.118 187.539  1.00 29.69           N  
ATOM   5169  CA  VAL A 826     210.130 236.041 188.532  1.00 29.50           C  
ATOM   5170  C   VAL A 826     210.928 236.511 189.752  1.00 29.66           C  
ATOM   5171  O   VAL A 826     212.034 237.032 189.596  1.00 29.39           O  
ATOM   5172  CB  VAL A 826     210.760 234.762 187.933  1.00 29.00           C  
ATOM   5173  CG1 VAL A 826     210.839 233.643 188.982  1.00 28.72           C  
ATOM   5174  CG2 VAL A 826     209.937 234.302 186.749  1.00 28.55           C  
ATOM   5175  N   THR A 827     210.367 236.331 190.965  1.00 29.56           N  
ATOM   5176  CA  THR A 827     211.002 236.767 192.216  1.00 29.74           C  
ATOM   5177  C   THR A 827     211.712 235.585 192.873  1.00 29.68           C  
ATOM   5178  O   THR A 827     212.347 235.727 193.921  1.00 28.81           O  
ATOM   5179  CB  THR A 827     209.967 237.398 193.208  1.00 29.66           C  
ATOM   5180  OG1 THR A 827     208.973 236.423 193.566  1.00 29.03           O  
ATOM   5181  CG2 THR A 827     209.253 238.642 192.571  1.00 29.12           C  
ATOM   5182  N   PHE A 855     218.849 233.328 210.466  1.00 37.07           N  
ATOM   5183  CA  PHE A 855     219.774 233.050 211.567  1.00 38.29           C  
ATOM   5184  C   PHE A 855     219.374 231.788 212.369  1.00 37.47           C  
ATOM   5185  O   PHE A 855     219.691 231.668 213.557  1.00 37.40           O  
ATOM   5186  CB  PHE A 855     219.847 234.266 212.525  1.00 39.71           C  
ATOM   5187  N   ASN A 856     218.701 230.838 211.707  1.00 36.16           N  
ATOM   5188  CA  ASN A 856     218.220 229.587 212.304  1.00 35.57           C  
ATOM   5189  C   ASN A 856     219.001 228.392 211.785  1.00 34.55           C  
ATOM   5190  O   ASN A 856     218.505 227.269 211.783  1.00 34.35           O  
ATOM   5191  CB  ASN A 856     216.739 229.429 212.033  1.00 35.18           C  
ATOM   5192  CG  ASN A 856     215.934 230.487 212.724  1.00 36.47           C  
ATOM   5193  OD1 ASN A 856     215.805 230.480 213.952  1.00 37.13           O  
ATOM   5194  ND2 ASN A 856     215.394 231.405 211.961  1.00 36.98           N  
ATOM   5195  N   GLY A 857     220.212 228.641 211.299  1.00 34.73           N  
ATOM   5196  CA  GLY A 857     221.046 227.580 210.749  1.00 33.56           C  
ATOM   5197  C   GLY A 857     220.702 227.346 209.292  1.00 32.64           C  
ATOM   5198  O   GLY A 857     221.118 226.360 208.688  1.00 31.96           O  
ATOM   5199  N   LEU A 858     219.914 228.250 208.735  1.00 33.14           N  
ATOM   5200  CA  LEU A 858     219.456 228.132 207.364  1.00 32.00           C  
ATOM   5201  C   LEU A 858     220.218 229.075 206.462  1.00 32.08           C  
ATOM   5202  O   LEU A 858     220.121 230.294 206.611  1.00 32.12           O  
ATOM   5203  CB  LEU A 858     217.967 228.481 207.298  1.00 32.47           C  
ATOM   5204  CG  LEU A 858     217.067 227.757 208.310  1.00 32.97           C  
ATOM   5205  CD1 LEU A 858     215.671 228.247 208.169  1.00 32.81           C  
ATOM   5206  CD2 LEU A 858     217.118 226.297 208.087  1.00 32.94           C  
ATOM   5207  N   THR A 859     220.969 228.526 205.522  1.00 31.45           N  
ATOM   5208  CA  THR A 859     221.732 229.361 204.610  1.00 31.13           C  
ATOM   5209  C   THR A 859     221.457 228.944 203.182  1.00 30.58           C  
ATOM   5210  O   THR A 859     221.017 227.823 202.931  1.00 30.73           O  
ATOM   5211  CB  THR A 859     223.245 229.271 204.891  1.00 31.80           C  
ATOM   5212  OG1 THR A 859     223.712 227.949 204.603  1.00 31.54           O  
ATOM   5213  CG2 THR A 859     223.528 229.590 206.364  1.00 33.44           C  
ATOM   5214  N   VAL A 860     221.744 229.829 202.241  1.00 30.43           N  
ATOM   5215  CA  VAL A 860     221.589 229.501 200.835  1.00 29.50           C  
ATOM   5216  C   VAL A 860     222.895 229.655 200.095  1.00 29.85           C  
ATOM   5217  O   VAL A 860     223.546 230.696 200.166  1.00 30.16           O  
ATOM   5218  CB  VAL A 860     220.511 230.378 200.189  1.00 29.55           C  
ATOM   5219  CG1 VAL A 860     220.415 230.072 198.707  1.00 29.58           C  
ATOM   5220  CG2 VAL A 860     219.179 230.106 200.868  1.00 29.46           C  
ATOM   5221  N   LEU A 861     223.279 228.609 199.392  1.00 29.45           N  
ATOM   5222  CA  LEU A 861     224.511 228.618 198.643  1.00 29.53           C  
ATOM   5223  C   LEU A 861     224.226 229.152 197.250  1.00 29.59           C  
ATOM   5224  O   LEU A 861     223.128 228.951 196.736  1.00 29.60           O  
ATOM   5225  CB  LEU A 861     225.046 227.190 198.563  1.00 29.25           C  
ATOM   5226  CG  LEU A 861     225.318 226.497 199.904  1.00 29.79           C  
ATOM   5227  CD1 LEU A 861     225.669 225.043 199.640  1.00 29.27           C  
ATOM   5228  CD2 LEU A 861     226.458 227.201 200.637  1.00 32.68           C  
ATOM   5229  N   PRO A 862     225.165 229.846 196.618  1.00 29.72           N  
ATOM   5230  CA  PRO A 862     225.058 230.300 195.260  1.00 29.45           C  
ATOM   5231  C   PRO A 862     225.227 229.106 194.340  1.00 29.41           C  
ATOM   5232  O   PRO A 862     225.880 228.136 194.731  1.00 29.33           O  
ATOM   5233  CB  PRO A 862     226.215 231.287 195.148  1.00 30.19           C  
ATOM   5234  CG  PRO A 862     227.231 230.787 196.144  1.00 31.73           C  
ATOM   5235  CD  PRO A 862     226.413 230.200 197.288  1.00 30.79           C  
ATOM   5236  N   PRO A 863     224.685 229.169 193.124  1.00 28.97           N  
ATOM   5237  CA  PRO A 863     224.861 228.223 192.049  1.00 28.42           C  
ATOM   5238  C   PRO A 863     226.261 228.378 191.518  1.00 29.00           C  
ATOM   5239  O   PRO A 863     226.841 229.457 191.639  1.00 30.15           O  
ATOM   5240  CB  PRO A 863     223.805 228.664 191.039  1.00 28.83           C  
ATOM   5241  CG  PRO A 863     223.631 230.139 191.300  1.00 29.11           C  
ATOM   5242  CD  PRO A 863     223.828 230.304 192.789  1.00 29.05           C  
ATOM   5243  N   LEU A 864     226.793 227.339 190.899  1.00 28.80           N  
ATOM   5244  CA  LEU A 864     228.095 227.461 190.268  1.00 29.12           C  
ATOM   5245  C   LEU A 864     228.051 228.383 189.064  1.00 29.88           C  
ATOM   5246  O   LEU A 864     228.954 229.196 188.862  1.00 31.02           O  
ATOM   5247  CB  LEU A 864     228.619 226.093 189.837  1.00 28.82           C  
ATOM   5248  CG  LEU A 864     230.004 226.090 189.159  1.00 30.16           C  
ATOM   5249  CD1 LEU A 864     231.064 226.678 190.103  1.00 31.71           C  
ATOM   5250  CD2 LEU A 864     230.349 224.669 188.771  1.00 31.23           C  
ATOM   5251  N   LEU A 865     227.005 228.265 188.260  1.00 29.20           N  
ATOM   5252  CA  LEU A 865     226.879 229.093 187.076  1.00 28.77           C  
ATOM   5253  C   LEU A 865     225.953 230.264 187.339  1.00 28.67           C  
ATOM   5254  O   LEU A 865     224.760 230.083 187.583  1.00 28.88           O  
ATOM   5255  CB  LEU A 865     226.348 228.257 185.911  1.00 28.68           C  
ATOM   5256  CG  LEU A 865     227.196 227.039 185.499  1.00 28.10           C  
ATOM   5257  CD1 LEU A 865     226.470 226.271 184.421  1.00 27.03           C  
ATOM   5258  CD2 LEU A 865     228.541 227.499 184.993  1.00 29.41           C  
ATOM   5259  N   THR A 866     226.511 231.463 187.290  1.00 29.00           N  
ATOM   5260  CA  THR A 866     225.762 232.678 187.569  1.00 29.17           C  
ATOM   5261  C   THR A 866     224.937 233.082 186.363  1.00 29.58           C  
ATOM   5262  O   THR A 866     225.128 232.568 185.262  1.00 28.96           O  
ATOM   5263  CB  THR A 866     226.693 233.829 187.963  1.00 29.80           C  
ATOM   5264  OG1 THR A 866     227.520 234.181 186.861  1.00 29.72           O  
ATOM   5265  CG2 THR A 866     227.558 233.425 189.112  1.00 31.13           C  
ATOM   5266  N   ASP A 867     224.033 234.030 186.544  1.00 28.87           N  
ATOM   5267  CA  ASP A 867     223.136 234.404 185.461  1.00 28.60           C  
ATOM   5268  C   ASP A 867     223.857 234.823 184.188  1.00 28.26           C  
ATOM   5269  O   ASP A 867     223.389 234.523 183.089  1.00 28.70           O  
ATOM   5270  CB  ASP A 867     222.223 235.538 185.905  1.00 28.99           C  
ATOM   5271  CG  ASP A 867     221.194 235.104 186.931  1.00 29.47           C  
ATOM   5272  OD1 ASP A 867     221.018 233.925 187.125  1.00 29.17           O  
ATOM   5273  OD2 ASP A 867     220.573 235.963 187.505  1.00 28.90           O  
ATOM   5274  N   GLU A 868     224.986 235.513 184.313  1.00 28.60           N  
ATOM   5275  CA  GLU A 868     225.698 235.948 183.119  1.00 28.43           C  
ATOM   5276  C   GLU A 868     226.377 234.779 182.416  1.00 28.24           C  
ATOM   5277  O   GLU A 868     226.708 234.866 181.236  1.00 28.88           O  
ATOM   5278  CB  GLU A 868     226.733 237.021 183.441  1.00 29.57           C  
ATOM   5279  CG  GLU A 868     227.964 236.525 184.155  1.00 29.77           C  
ATOM   5280  CD  GLU A 868     228.925 237.621 184.461  1.00 30.64           C  
ATOM   5281  OE1 GLU A 868     228.664 238.737 184.085  1.00 30.30           O  
ATOM   5282  OE2 GLU A 868     229.931 237.348 185.068  1.00 30.73           O  
ATOM   5283  N   MET A 869     226.615 233.696 183.143  1.00 28.06           N  
ATOM   5284  CA  MET A 869     227.287 232.540 182.579  1.00 27.68           C  
ATOM   5285  C   MET A 869     226.269 231.693 181.852  1.00 28.03           C  
ATOM   5286  O   MET A 869     226.560 231.097 180.815  1.00 27.94           O  
ATOM   5287  CB  MET A 869     227.988 231.778 183.679  1.00 28.85           C  
ATOM   5288  CG  MET A 869     229.121 232.572 184.304  1.00 29.17           C  
ATOM   5289  SD  MET A 869     229.753 231.819 185.775  1.00 31.17           S  
ATOM   5290  CE  MET A 869     230.673 230.465 185.149  1.00 31.12           C  
ATOM   5291  N   ILE A 870     225.049 231.690 182.359  1.00 27.61           N  
ATOM   5292  CA  ILE A 870     223.997 230.985 181.665  1.00 26.88           C  
ATOM   5293  C   ILE A 870     223.732 231.744 180.386  1.00 27.10           C  
ATOM   5294  O   ILE A 870     223.585 231.146 179.324  1.00 27.01           O  
ATOM   5295  CB  ILE A 870     222.718 230.863 182.496  1.00 27.70           C  
ATOM   5296  CG1 ILE A 870     222.993 230.076 183.793  1.00 27.75           C  
ATOM   5297  CG2 ILE A 870     221.639 230.182 181.667  1.00 26.88           C  
ATOM   5298  CD1 ILE A 870     223.553 228.685 183.601  1.00 27.57           C  
ATOM   5299  N   ALA A 871     223.716 233.071 180.474  1.00 27.11           N  
ATOM   5300  CA  ALA A 871     223.510 233.894 179.297  1.00 26.28           C  
ATOM   5301  C   ALA A 871     224.565 233.600 178.239  1.00 25.98           C  
ATOM   5302  O   ALA A 871     224.246 233.544 177.053  1.00 26.63           O  
ATOM   5303  CB  ALA A 871     223.551 235.358 179.672  1.00 28.12           C  
ATOM   5304  N   GLN A 872     225.813 233.374 178.647  1.00 26.24           N  
ATOM   5305  CA  GLN A 872     226.830 233.025 177.666  1.00 25.48           C  
ATOM   5306  C   GLN A 872     226.550 231.676 177.022  1.00 25.43           C  
ATOM   5307  O   GLN A 872     226.752 231.516 175.818  1.00 25.97           O  
ATOM   5308  CB  GLN A 872     228.215 233.013 178.281  1.00 26.32           C  
ATOM   5309  CG  GLN A 872     228.765 234.363 178.613  1.00 26.67           C  
ATOM   5310  CD  GLN A 872     230.112 234.268 179.286  1.00 27.53           C  
ATOM   5311  OE1 GLN A 872     230.918 233.388 178.967  1.00 26.78           O  
ATOM   5312  NE2 GLN A 872     230.369 235.171 180.223  1.00 27.81           N  
ATOM   5313  N   TYR A 873     226.061 230.709 177.791  1.00 25.51           N  
ATOM   5314  CA  TYR A 873     225.745 229.423 177.188  1.00 24.42           C  
ATOM   5315  C   TYR A 873     224.576 229.526 176.228  1.00 24.99           C  
ATOM   5316  O   TYR A 873     224.620 228.949 175.142  1.00 24.55           O  
ATOM   5317  CB  TYR A 873     225.433 228.359 178.234  1.00 25.09           C  
ATOM   5318  CG  TYR A 873     226.630 227.707 178.856  1.00 24.92           C  
ATOM   5319  CD1 TYR A 873     226.756 227.654 180.227  1.00 25.67           C  
ATOM   5320  CD2 TYR A 873     227.603 227.146 178.053  1.00 25.13           C  
ATOM   5321  CE1 TYR A 873     227.848 227.040 180.787  1.00 26.14           C  
ATOM   5322  CE2 TYR A 873     228.689 226.539 178.615  1.00 25.75           C  
ATOM   5323  CZ  TYR A 873     228.813 226.481 179.973  1.00 26.31           C  
ATOM   5324  OH  TYR A 873     229.902 225.864 180.531  1.00 27.41           O  
ATOM   5325  N   THR A 874     223.538 230.272 176.591  1.00 24.74           N  
ATOM   5326  CA  THR A 874     222.400 230.369 175.696  1.00 23.88           C  
ATOM   5327  C   THR A 874     222.774 231.193 174.484  1.00 24.23           C  
ATOM   5328  O   THR A 874     222.282 230.938 173.386  1.00 24.29           O  
ATOM   5329  CB  THR A 874     221.154 230.926 176.402  1.00 24.62           C  
ATOM   5330  OG1 THR A 874     221.442 232.195 176.978  1.00 26.38           O  
ATOM   5331  CG2 THR A 874     220.715 229.968 177.490  1.00 24.79           C  
ATOM   5332  N   SER A 875     223.687 232.141 174.657  1.00 24.76           N  
ATOM   5333  CA  SER A 875     224.181 232.919 173.536  1.00 24.07           C  
ATOM   5334  C   SER A 875     224.929 232.025 172.567  1.00 23.64           C  
ATOM   5335  O   SER A 875     224.722 232.112 171.360  1.00 24.37           O  
ATOM   5336  CB  SER A 875     225.086 234.029 174.005  1.00 25.37           C  
ATOM   5337  OG  SER A 875     225.593 234.738 172.918  1.00 25.74           O  
ATOM   5338  N   ALA A 876     225.787 231.150 173.087  1.00 23.57           N  
ATOM   5339  CA  ALA A 876     226.535 230.234 172.240  1.00 23.19           C  
ATOM   5340  C   ALA A 876     225.623 229.291 171.483  1.00 23.00           C  
ATOM   5341  O   ALA A 876     225.831 229.031 170.298  1.00 23.37           O  
ATOM   5342  CB  ALA A 876     227.480 229.408 173.080  1.00 24.27           C  
ATOM   5343  N   LEU A 877     224.604 228.782 172.158  1.00 23.21           N  
ATOM   5344  CA  LEU A 877     223.688 227.850 171.531  1.00 22.43           C  
ATOM   5345  C   LEU A 877     222.863 228.553 170.484  1.00 22.59           C  
ATOM   5346  O   LEU A 877     222.597 227.998 169.419  1.00 22.95           O  
ATOM   5347  CB  LEU A 877     222.781 227.230 172.583  1.00 22.56           C  
ATOM   5348  CG  LEU A 877     223.462 226.304 173.587  1.00 22.56           C  
ATOM   5349  CD1 LEU A 877     222.496 225.992 174.666  1.00 22.38           C  
ATOM   5350  CD2 LEU A 877     223.900 225.040 172.909  1.00 22.69           C  
ATOM   5351  N   LEU A 878     222.484 229.786 170.769  1.00 23.09           N  
ATOM   5352  CA  LEU A 878     221.729 230.580 169.830  1.00 22.29           C  
ATOM   5353  C   LEU A 878     222.563 230.945 168.618  1.00 22.66           C  
ATOM   5354  O   LEU A 878     222.086 230.854 167.488  1.00 23.04           O  
ATOM   5355  CB  LEU A 878     221.211 231.830 170.529  1.00 22.81           C  
ATOM   5356  CG  LEU A 878     220.467 232.826 169.685  1.00 23.45           C  
ATOM   5357  CD1 LEU A 878     219.319 232.176 169.020  1.00 23.03           C  
ATOM   5358  CD2 LEU A 878     219.976 233.933 170.582  1.00 25.42           C  
ATOM   5359  N   ALA A 879     223.807 231.358 168.834  1.00 22.26           N  
ATOM   5360  CA  ALA A 879     224.671 231.709 167.724  1.00 21.86           C  
ATOM   5361  C   ALA A 879     224.900 230.494 166.856  1.00 21.76           C  
ATOM   5362  O   ALA A 879     224.921 230.595 165.632  1.00 22.68           O  
ATOM   5363  CB  ALA A 879     225.992 232.255 168.226  1.00 23.41           C  
ATOM   5364  N   GLY A 880     225.041 229.333 167.487  1.00 21.74           N  
ATOM   5365  CA  GLY A 880     225.228 228.090 166.766  1.00 21.27           C  
ATOM   5366  C   GLY A 880     224.004 227.793 165.918  1.00 25.65           C  
ATOM   5367  O   GLY A 880     224.108 227.539 164.718  1.00 20.35           O  
ATOM   5368  N   THR A 881     222.833 227.871 166.532  1.00 21.36           N  
ATOM   5369  CA  THR A 881     221.584 227.573 165.856  1.00 20.78           C  
ATOM   5370  C   THR A 881     221.386 228.455 164.639  1.00 21.52           C  
ATOM   5371  O   THR A 881     220.939 227.983 163.592  1.00 22.08           O  
ATOM   5372  CB  THR A 881     220.393 227.767 166.812  1.00 21.70           C  
ATOM   5373  OG1 THR A 881     220.528 226.884 167.921  1.00 21.79           O  
ATOM   5374  CG2 THR A 881     219.080 227.472 166.107  1.00 21.72           C  
ATOM   5375  N   ILE A 882     221.686 229.737 164.776  1.00 21.99           N  
ATOM   5376  CA  ILE A 882     221.505 230.671 163.680  1.00 21.50           C  
ATOM   5377  C   ILE A 882     222.520 230.514 162.553  1.00 21.66           C  
ATOM   5378  O   ILE A 882     222.142 230.575 161.387  1.00 22.12           O  
ATOM   5379  CB  ILE A 882     221.525 232.116 164.185  1.00 21.95           C  
ATOM   5380  CG1 ILE A 882     220.298 232.364 165.055  1.00 22.52           C  
ATOM   5381  CG2 ILE A 882     221.539 233.074 163.003  1.00 22.56           C  
ATOM   5382  CD1 ILE A 882     220.364 233.637 165.855  1.00 24.06           C  
ATOM   5383  N   THR A 883     223.804 230.361 162.873  1.00 21.96           N  
ATOM   5384  CA  THR A 883     224.810 230.343 161.818  1.00 21.23           C  
ATOM   5385  C   THR A 883     225.235 228.967 161.303  1.00 21.18           C  
ATOM   5386  O   THR A 883     225.850 228.894 160.238  1.00 22.25           O  
ATOM   5387  CB  THR A 883     226.082 231.071 162.277  1.00 22.01           C  
ATOM   5388  OG1 THR A 883     226.679 230.364 163.360  1.00 21.89           O  
ATOM   5389  CG2 THR A 883     225.741 232.478 162.737  1.00 22.21           C  
ATOM   5390  N   SER A 884     224.956 227.882 162.034  1.00 21.29           N  
ATOM   5391  CA  SER A 884     225.413 226.563 161.582  1.00 20.65           C  
ATOM   5392  C   SER A 884     224.367 225.443 161.668  1.00 20.42           C  
ATOM   5393  O   SER A 884     224.682 224.268 161.464  1.00 21.24           O  
ATOM   5394  CB  SER A 884     226.643 226.166 162.353  1.00 21.20           C  
ATOM   5395  OG  SER A 884     226.363 226.049 163.703  1.00 21.56           O  
ATOM   5396  N   GLY A 885     223.129 225.783 161.979  1.00 21.27           N  
ATOM   5397  CA  GLY A 885     222.070 224.786 162.052  1.00 21.00           C  
ATOM   5398  C   GLY A 885     222.350 223.712 163.082  1.00 20.97           C  
ATOM   5399  O   GLY A 885     222.652 223.999 164.235  1.00 21.40           O  
ATOM   5400  N   TRP A 886     222.243 222.461 162.674  1.00 20.46           N  
ATOM   5401  CA  TRP A 886     222.466 221.352 163.583  1.00 20.31           C  
ATOM   5402  C   TRP A 886     223.888 220.823 163.619  1.00 20.60           C  
ATOM   5403  O   TRP A 886     224.163 219.855 164.337  1.00 20.73           O  
ATOM   5404  CB  TRP A 886     221.559 220.182 163.236  1.00 20.33           C  
ATOM   5405  CG  TRP A 886     221.451 219.928 161.793  1.00 20.36           C  
ATOM   5406  CD1 TRP A 886     222.400 219.425 160.966  1.00 20.51           C  
ATOM   5407  CD2 TRP A 886     220.278 220.106 160.994  1.00 20.13           C  
ATOM   5408  NE1 TRP A 886     221.904 219.311 159.701  1.00 20.55           N  
ATOM   5409  CE2 TRP A 886     220.601 219.718 159.703  1.00 20.49           C  
ATOM   5410  CE3 TRP A 886     218.995 220.545 161.270  1.00 19.94           C  
ATOM   5411  CZ2 TRP A 886     219.681 219.764 158.678  1.00 20.67           C  
ATOM   5412  CZ3 TRP A 886     218.075 220.579 160.253  1.00 19.93           C  
ATOM   5413  CH2 TRP A 886     218.404 220.204 158.990  1.00 20.19           C  
ATOM   5414  N   THR A 887     224.794 221.407 162.843  1.00 20.45           N  
ATOM   5415  CA  THR A 887     226.107 220.799 162.764  1.00 19.68           C  
ATOM   5416  C   THR A 887     226.960 221.155 163.965  1.00 21.78           C  
ATOM   5417  O   THR A 887     227.852 220.398 164.329  1.00 20.88           O  
ATOM   5418  CB  THR A 887     226.831 221.200 161.477  1.00 20.69           C  
ATOM   5419  OG1 THR A 887     227.153 222.587 161.516  1.00 21.24           O  
ATOM   5420  CG2 THR A 887     225.911 220.940 160.298  1.00 20.79           C  
ATOM   5421  N   PHE A 888     226.663 222.261 164.645  1.00 20.59           N  
ATOM   5422  CA  PHE A 888     227.459 222.599 165.822  1.00 21.19           C  
ATOM   5423  C   PHE A 888     227.169 221.595 166.919  1.00 20.77           C  
ATOM   5424  O   PHE A 888     227.956 221.415 167.847  1.00 21.15           O  
ATOM   5425  CB  PHE A 888     227.181 224.007 166.323  1.00 21.40           C  
ATOM   5426  CG  PHE A 888     225.937 224.152 167.088  1.00 21.01           C  
ATOM   5427  CD1 PHE A 888     225.948 224.016 168.453  1.00 21.50           C  
ATOM   5428  CD2 PHE A 888     224.755 224.422 166.464  1.00 21.14           C  
ATOM   5429  CE1 PHE A 888     224.803 224.152 169.176  1.00 21.41           C  
ATOM   5430  CE2 PHE A 888     223.601 224.557 167.186  1.00 21.02           C  
ATOM   5431  CZ  PHE A 888     223.625 224.425 168.544  1.00 21.36           C  
ATOM   5432  N   GLY A 889     226.013 220.955 166.809  1.00 20.89           N  
ATOM   5433  CA  GLY A 889     225.590 219.928 167.731  1.00 20.64           C  
ATOM   5434  C   GLY A 889     226.325 218.637 167.415  1.00 20.30           C  
ATOM   5435  O   GLY A 889     227.071 218.120 168.240  1.00 20.35           O  
ATOM   5436  N   ALA A 890     226.082 218.098 166.222  1.00 20.50           N  
ATOM   5437  CA  ALA A 890     226.648 216.810 165.819  1.00 19.88           C  
ATOM   5438  C   ALA A 890     228.176 216.804 165.678  1.00 19.88           C  
ATOM   5439  O   ALA A 890     228.819 215.792 165.945  1.00 19.83           O  
ATOM   5440  CB  ALA A 890     226.036 216.380 164.500  1.00 19.62           C  
ATOM   5441  N   GLY A 891     228.761 217.895 165.208  1.00 20.24           N  
ATOM   5442  CA  GLY A 891     230.196 217.933 164.954  1.00 19.96           C  
ATOM   5443  C   GLY A 891     230.755 219.341 165.089  1.00 20.24           C  
ATOM   5444  O   GLY A 891     230.712 219.948 166.160  1.00 20.42           O  
ATOM   5445  N   ALA A 892     231.339 219.833 164.005  1.00 20.05           N  
ATOM   5446  CA  ALA A 892     231.885 221.179 163.966  1.00 20.41           C  
ATOM   5447  C   ALA A 892     230.798 222.155 163.566  1.00 20.65           C  
ATOM   5448  O   ALA A 892     229.865 221.799 162.851  1.00 21.40           O  
ATOM   5449  CB  ALA A 892     233.041 221.256 162.986  1.00 20.52           C  
ATOM   5450  N   ALA A 893     230.925 223.406 163.967  1.00 20.91           N  
ATOM   5451  CA  ALA A 893     229.945 224.370 163.506  1.00 20.73           C  
ATOM   5452  C   ALA A 893     230.272 224.744 162.078  1.00 20.77           C  
ATOM   5453  O   ALA A 893     231.269 225.414 161.818  1.00 21.08           O  
ATOM   5454  CB  ALA A 893     229.934 225.599 164.391  1.00 21.79           C  
ATOM   5455  N   LEU A 894     229.437 224.282 161.157  1.00 20.73           N  
ATOM   5456  CA  LEU A 894     229.644 224.505 159.739  1.00 20.35           C  
ATOM   5457  C   LEU A 894     228.740 225.616 159.252  1.00 20.79           C  
ATOM   5458  O   LEU A 894     227.522 225.469 159.238  1.00 21.23           O  
ATOM   5459  CB  LEU A 894     229.327 223.220 158.976  1.00 20.42           C  
ATOM   5460  CG  LEU A 894     230.118 221.979 159.378  1.00 20.20           C  
ATOM   5461  CD1 LEU A 894     229.607 220.825 158.605  1.00 20.54           C  
ATOM   5462  CD2 LEU A 894     231.581 222.180 159.096  1.00 20.00           C  
ATOM   5463  N   GLN A 895     229.326 226.726 158.845  1.00 20.79           N  
ATOM   5464  CA  GLN A 895     228.525 227.868 158.458  1.00 20.18           C  
ATOM   5465  C   GLN A 895     227.634 227.545 157.277  1.00 20.92           C  
ATOM   5466  O   GLN A 895     228.028 226.833 156.354  1.00 21.45           O  
ATOM   5467  CB  GLN A 895     229.403 229.083 158.134  1.00 20.84           C  
ATOM   5468  CG  GLN A 895     230.236 228.982 156.867  1.00 21.17           C  
ATOM   5469  CD  GLN A 895     231.551 228.344 157.098  1.00 21.28           C  
ATOM   5470  OE1 GLN A 895     231.705 227.603 158.072  1.00 21.31           O  
ATOM   5471  NE2 GLN A 895     232.503 228.598 156.212  1.00 21.25           N  
ATOM   5472  N   ILE A 896     226.423 228.072 157.321  1.00 20.99           N  
ATOM   5473  CA  ILE A 896     225.466 227.950 156.231  1.00 20.99           C  
ATOM   5474  C   ILE A 896     224.651 229.246 156.179  1.00 21.19           C  
ATOM   5475  O   ILE A 896     224.310 229.766 157.234  1.00 21.99           O  
ATOM   5476  CB  ILE A 896     224.555 226.729 156.484  1.00 21.00           C  
ATOM   5477  CG1 ILE A 896     223.648 226.475 155.289  1.00 21.18           C  
ATOM   5478  CG2 ILE A 896     223.743 226.948 157.749  1.00 21.55           C  
ATOM   5479  CD1 ILE A 896     222.935 225.154 155.306  1.00 21.02           C  
ATOM   5480  N   PRO A 897     224.302 229.794 155.011  1.00 21.07           N  
ATOM   5481  CA  PRO A 897     223.448 230.954 154.899  1.00 21.15           C  
ATOM   5482  C   PRO A 897     222.162 230.650 155.627  1.00 21.35           C  
ATOM   5483  O   PRO A 897     221.657 229.538 155.528  1.00 21.96           O  
ATOM   5484  CB  PRO A 897     223.242 231.066 153.394  1.00 21.54           C  
ATOM   5485  CG  PRO A 897     224.475 230.443 152.811  1.00 21.45           C  
ATOM   5486  CD  PRO A 897     224.814 229.301 153.741  1.00 21.23           C  
ATOM   5487  N   PHE A 898     221.620 231.618 156.348  1.00 21.69           N  
ATOM   5488  CA  PHE A 898     220.436 231.322 157.133  1.00 21.41           C  
ATOM   5489  C   PHE A 898     219.248 230.907 156.287  1.00 21.75           C  
ATOM   5490  O   PHE A 898     218.555 229.948 156.619  1.00 22.09           O  
ATOM   5491  CB  PHE A 898     220.027 232.480 158.016  1.00 22.28           C  
ATOM   5492  CG  PHE A 898     218.940 232.060 158.884  1.00 21.77           C  
ATOM   5493  CD1 PHE A 898     219.216 231.249 159.945  1.00 21.82           C  
ATOM   5494  CD2 PHE A 898     217.652 232.420 158.647  1.00 22.30           C  
ATOM   5495  CE1 PHE A 898     218.232 230.798 160.754  1.00 21.83           C  
ATOM   5496  CE2 PHE A 898     216.661 231.964 159.461  1.00 22.25           C  
ATOM   5497  CZ  PHE A 898     216.958 231.149 160.509  1.00 22.02           C  
ATOM   5498  N   ALA A 899     218.986 231.614 155.198  1.00 21.43           N  
ATOM   5499  CA  ALA A 899     217.840 231.247 154.380  1.00 21.37           C  
ATOM   5500  C   ALA A 899     218.000 229.821 153.878  1.00 20.85           C  
ATOM   5501  O   ALA A 899     217.032 229.073 153.764  1.00 21.65           O  
ATOM   5502  CB  ALA A 899     217.686 232.202 153.215  1.00 22.06           C  
ATOM   5503  N   MET A 900     219.226 229.433 153.584  1.00 21.30           N  
ATOM   5504  CA  MET A 900     219.478 228.089 153.114  1.00 20.71           C  
ATOM   5505  C   MET A 900     219.244 227.095 154.231  1.00 21.15           C  
ATOM   5506  O   MET A 900     218.675 226.029 154.015  1.00 21.11           O  
ATOM   5507  CB  MET A 900     220.877 228.007 152.561  1.00 21.18           C  
ATOM   5508  CG  MET A 900     221.190 226.762 151.815  1.00 20.92           C  
ATOM   5509  SD  MET A 900     222.743 226.905 150.970  1.00 21.87           S  
ATOM   5510  CE  MET A 900     222.249 227.933 149.596  1.00 21.66           C  
ATOM   5511  N   GLN A 901     219.620 227.459 155.441  1.00 20.83           N  
ATOM   5512  CA  GLN A 901     219.355 226.588 156.563  1.00 20.03           C  
ATOM   5513  C   GLN A 901     217.873 226.341 156.688  1.00 21.21           C  
ATOM   5514  O   GLN A 901     217.449 225.210 156.918  1.00 21.55           O  
ATOM   5515  CB  GLN A 901     219.873 227.190 157.845  1.00 21.03           C  
ATOM   5516  CG  GLN A 901     219.619 226.372 159.040  1.00 20.79           C  
ATOM   5517  CD  GLN A 901     220.287 226.959 160.199  1.00 21.25           C  
ATOM   5518  OE1 GLN A 901     221.505 227.089 160.188  1.00 21.66           O  
ATOM   5519  NE2 GLN A 901     219.539 227.327 161.215  1.00 21.40           N  
ATOM   5520  N   MET A 902     217.074 227.384 156.504  1.00 20.56           N  
ATOM   5521  CA  MET A 902     215.633 227.221 156.586  1.00 20.33           C  
ATOM   5522  C   MET A 902     215.137 226.296 155.491  1.00 20.63           C  
ATOM   5523  O   MET A 902     214.205 225.526 155.702  1.00 20.61           O  
ATOM   5524  CB  MET A 902     214.933 228.564 156.516  1.00 21.12           C  
ATOM   5525  CG  MET A 902     215.105 229.400 157.736  1.00 21.63           C  
ATOM   5526  SD  MET A 902     214.518 228.600 159.227  1.00 22.23           S  
ATOM   5527  CE  MET A 902     212.760 228.582 158.988  1.00 21.14           C  
ATOM   5528  N   ALA A 903     215.792 226.314 154.338  1.00 20.79           N  
ATOM   5529  CA  ALA A 903     215.397 225.429 153.256  1.00 19.87           C  
ATOM   5530  C   ALA A 903     215.472 223.994 153.717  1.00 19.46           C  
ATOM   5531  O   ALA A 903     214.623 223.174 153.364  1.00 20.36           O  
ATOM   5532  CB  ALA A 903     216.297 225.628 152.053  1.00 20.92           C  
ATOM   5533  N   TYR A 904     216.476 223.693 154.526  1.00 19.90           N  
ATOM   5534  CA  TYR A 904     216.640 222.340 155.011  1.00 19.40           C  
ATOM   5535  C   TYR A 904     215.544 222.047 156.015  1.00 19.20           C  
ATOM   5536  O   TYR A 904     214.981 220.952 156.030  1.00 19.80           O  
ATOM   5537  CB  TYR A 904     217.999 222.146 155.686  1.00 19.97           C  
ATOM   5538  CG  TYR A 904     219.257 222.271 154.807  1.00 20.32           C  
ATOM   5539  CD1 TYR A 904     220.454 221.804 155.321  1.00 20.44           C  
ATOM   5540  CD2 TYR A 904     219.245 222.848 153.532  1.00 20.52           C  
ATOM   5541  CE1 TYR A 904     221.611 221.902 154.594  1.00 20.43           C  
ATOM   5542  CE2 TYR A 904     220.417 222.945 152.815  1.00 20.62           C  
ATOM   5543  CZ  TYR A 904     221.589 222.470 153.343  1.00 20.72           C  
ATOM   5544  OH  TYR A 904     222.753 222.561 152.631  1.00 21.20           O  
ATOM   5545  N   ARG A 905     215.214 223.047 156.831  1.00 19.25           N  
ATOM   5546  CA  ARG A 905     214.199 222.874 157.859  1.00 18.74           C  
ATOM   5547  C   ARG A 905     212.837 222.616 157.229  1.00 19.81           C  
ATOM   5548  O   ARG A 905     212.048 221.831 157.752  1.00 19.45           O  
ATOM   5549  CB  ARG A 905     214.080 224.107 158.740  1.00 19.62           C  
ATOM   5550  CG  ARG A 905     215.326 224.534 159.508  1.00 19.62           C  
ATOM   5551  CD  ARG A 905     215.821 223.515 160.409  1.00 19.28           C  
ATOM   5552  NE  ARG A 905     216.838 224.055 161.320  1.00 19.49           N  
ATOM   5553  CZ  ARG A 905     217.109 223.573 162.551  1.00 19.43           C  
ATOM   5554  NH1 ARG A 905     216.425 222.571 163.024  1.00 19.45           N  
ATOM   5555  NH2 ARG A 905     218.062 224.112 163.286  1.00 19.91           N  
ATOM   5556  N   PHE A 906     212.559 223.272 156.107  1.00 19.68           N  
ATOM   5557  CA  PHE A 906     211.295 223.074 155.410  1.00 18.63           C  
ATOM   5558  C   PHE A 906     211.217 221.698 154.768  1.00 21.95           C  
ATOM   5559  O   PHE A 906     210.210 221.004 154.913  1.00 17.73           O  
ATOM   5560  CB  PHE A 906     211.063 224.160 154.366  1.00 19.60           C  
ATOM   5561  CG  PHE A 906     210.339 225.369 154.888  1.00 19.43           C  
ATOM   5562  CD1 PHE A 906     210.989 226.389 155.532  1.00 20.41           C  
ATOM   5563  CD2 PHE A 906     208.990 225.479 154.704  1.00 19.67           C  
ATOM   5564  CE1 PHE A 906     210.296 227.483 155.989  1.00 21.10           C  
ATOM   5565  CE2 PHE A 906     208.301 226.567 155.152  1.00 20.20           C  
ATOM   5566  CZ  PHE A 906     208.952 227.568 155.798  1.00 20.79           C  
ATOM   5567  N   ASN A 907     212.300 221.243 154.139  1.00 18.86           N  
ATOM   5568  CA  ASN A 907     212.254 219.906 153.559  1.00 18.79           C  
ATOM   5569  C   ASN A 907     212.058 218.879 154.658  1.00 18.94           C  
ATOM   5570  O   ASN A 907     211.370 217.873 154.473  1.00 19.27           O  
ATOM   5571  CB  ASN A 907     213.500 219.595 152.755  1.00 19.08           C  
ATOM   5572  CG  ASN A 907     213.498 220.237 151.404  1.00 19.79           C  
ATOM   5573  OD1 ASN A 907     212.458 220.680 150.911  1.00 20.06           O  
ATOM   5574  ND2 ASN A 907     214.630 220.275 150.774  1.00 20.38           N  
ATOM   5575  N   GLY A 908     212.594 219.175 155.832  1.00 19.04           N  
ATOM   5576  CA  GLY A 908     212.502 218.309 156.992  1.00 18.65           C  
ATOM   5577  C   GLY A 908     211.074 218.084 157.485  1.00 18.69           C  
ATOM   5578  O   GLY A 908     210.838 217.153 158.260  1.00 18.76           O  
ATOM   5579  N   ILE A 909     210.123 218.916 157.054  1.00 18.81           N  
ATOM   5580  CA  ILE A 909     208.732 218.752 157.463  1.00 18.50           C  
ATOM   5581  C   ILE A 909     207.858 218.377 156.276  1.00 18.81           C  
ATOM   5582  O   ILE A 909     206.631 218.411 156.364  1.00 19.07           O  
ATOM   5583  CB  ILE A 909     208.161 220.016 158.136  1.00 18.36           C  
ATOM   5584  CG1 ILE A 909     208.172 221.187 157.177  1.00 18.68           C  
ATOM   5585  CG2 ILE A 909     208.993 220.343 159.362  1.00 18.94           C  
ATOM   5586  CD1 ILE A 909     207.344 222.360 157.618  1.00 18.98           C  
ATOM   5587  N   GLY A 910     208.488 218.022 155.161  1.00 18.84           N  
ATOM   5588  CA  GLY A 910     207.755 217.600 153.979  1.00 18.68           C  
ATOM   5589  C   GLY A 910     207.323 218.728 153.051  1.00 18.94           C  
ATOM   5590  O   GLY A 910     206.434 218.530 152.226  1.00 19.30           O  
ATOM   5591  N   VAL A 911     207.925 219.905 153.169  1.00 19.01           N  
ATOM   5592  CA  VAL A 911     207.568 221.006 152.290  1.00 18.89           C  
ATOM   5593  C   VAL A 911     208.769 221.361 151.436  1.00 19.42           C  
ATOM   5594  O   VAL A 911     209.810 221.746 151.956  1.00 20.12           O  
ATOM   5595  CB  VAL A 911     207.104 222.217 153.111  1.00 18.94           C  
ATOM   5596  CG1 VAL A 911     206.774 223.379 152.208  1.00 19.45           C  
ATOM   5597  CG2 VAL A 911     205.883 221.834 153.912  1.00 19.32           C  
ATOM   5598  N   THR A 912     208.627 221.234 150.127  1.00 19.63           N  
ATOM   5599  CA  THR A 912     209.743 221.434 149.218  1.00 19.68           C  
ATOM   5600  C   THR A 912     210.299 222.833 149.394  1.00 20.51           C  
ATOM   5601  O   THR A 912     209.544 223.805 149.396  1.00 20.35           O  
ATOM   5602  CB  THR A 912     209.316 221.182 147.768  1.00 20.02           C  
ATOM   5603  OG1 THR A 912     208.796 219.857 147.654  1.00 20.36           O  
ATOM   5604  CG2 THR A 912     210.483 221.325 146.832  1.00 20.96           C  
ATOM   5605  N   GLN A 913     211.624 222.940 149.485  1.00 19.92           N  
ATOM   5606  CA  GLN A 913     212.288 224.205 149.780  1.00 19.95           C  
ATOM   5607  C   GLN A 913     212.013 225.340 148.817  1.00 20.48           C  
ATOM   5608  O   GLN A 913     212.343 226.485 149.120  1.00 21.52           O  
ATOM   5609  CB  GLN A 913     213.803 224.065 149.845  1.00 20.58           C  
ATOM   5610  CG  GLN A 913     214.529 223.918 148.502  1.00 20.60           C  
ATOM   5611  CD  GLN A 913     214.699 222.525 148.034  1.00 21.19           C  
ATOM   5612  OE1 GLN A 913     213.911 221.632 148.348  1.00 21.01           O  
ATOM   5613  NE2 GLN A 913     215.753 222.320 147.254  1.00 22.20           N  
ATOM   5614  N   ASN A 914     211.441 225.064 147.658  1.00 20.24           N  
ATOM   5615  CA  ASN A 914     211.178 226.167 146.760  1.00 20.57           C  
ATOM   5616  C   ASN A 914     210.113 227.054 147.377  1.00 21.18           C  
ATOM   5617  O   ASN A 914     210.012 228.230 147.044  1.00 20.98           O  
ATOM   5618  CB  ASN A 914     210.732 225.702 145.405  1.00 20.69           C  
ATOM   5619  CG  ASN A 914     209.431 225.089 145.477  1.00 20.51           C  
ATOM   5620  OD1 ASN A 914     209.283 224.005 146.038  1.00 20.86           O  
ATOM   5621  ND2 ASN A 914     208.454 225.760 144.943  1.00 20.68           N  
ATOM   5622  N   VAL A 915     209.324 226.491 148.295  1.00 20.71           N  
ATOM   5623  CA  VAL A 915     208.273 227.237 148.955  1.00 20.15           C  
ATOM   5624  C   VAL A 915     208.895 228.335 149.787  1.00 21.23           C  
ATOM   5625  O   VAL A 915     208.405 229.458 149.802  1.00 21.68           O  
ATOM   5626  CB  VAL A 915     207.406 226.328 149.830  1.00 20.13           C  
ATOM   5627  CG1 VAL A 915     206.421 227.159 150.659  1.00 20.58           C  
ATOM   5628  CG2 VAL A 915     206.660 225.365 148.939  1.00 20.16           C  
ATOM   5629  N   LEU A 916     209.972 227.997 150.477  1.00 20.71           N  
ATOM   5630  CA  LEU A 916     210.670 228.976 151.290  1.00 20.71           C  
ATOM   5631  C   LEU A 916     211.192 230.110 150.477  1.00 21.89           C  
ATOM   5632  O   LEU A 916     210.997 231.275 150.819  1.00 22.22           O  
ATOM   5633  CB  LEU A 916     211.859 228.345 151.986  1.00 21.04           C  
ATOM   5634  CG  LEU A 916     212.839 229.327 152.661  1.00 21.25           C  
ATOM   5635  CD1 LEU A 916     212.191 230.079 153.771  1.00 21.80           C  
ATOM   5636  CD2 LEU A 916     213.962 228.572 153.146  1.00 21.39           C  
ATOM   5637  N   TYR A 917     211.883 229.804 149.397  1.00 21.44           N  
ATOM   5638  CA  TYR A 917     212.515 230.864 148.653  1.00 21.09           C  
ATOM   5639  C   TYR A 917     211.489 231.755 147.989  1.00 21.02           C  
ATOM   5640  O   TYR A 917     211.603 232.980 148.020  1.00 21.99           O  
ATOM   5641  CB  TYR A 917     213.470 230.284 147.635  1.00 21.55           C  
ATOM   5642  CG  TYR A 917     214.626 229.612 148.280  1.00 21.32           C  
ATOM   5643  CD1 TYR A 917     214.786 228.258 148.157  1.00 21.19           C  
ATOM   5644  CD2 TYR A 917     215.521 230.344 149.016  1.00 21.49           C  
ATOM   5645  CE1 TYR A 917     215.845 227.638 148.749  1.00 21.32           C  
ATOM   5646  CE2 TYR A 917     216.574 229.720 149.615  1.00 21.43           C  
ATOM   5647  CZ  TYR A 917     216.740 228.374 149.476  1.00 21.44           C  
ATOM   5648  OH  TYR A 917     217.806 227.756 150.062  1.00 21.81           O  
ATOM   5649  N   GLU A 918     210.446 231.158 147.447  1.00 20.93           N  
ATOM   5650  CA  GLU A 918     209.431 231.938 146.778  1.00 20.97           C  
ATOM   5651  C   GLU A 918     208.700 232.842 147.758  1.00 21.56           C  
ATOM   5652  O   GLU A 918     208.304 233.956 147.416  1.00 21.89           O  
ATOM   5653  CB  GLU A 918     208.474 231.015 146.037  1.00 21.14           C  
ATOM   5654  CG  GLU A 918     209.137 230.314 144.845  1.00 21.06           C  
ATOM   5655  CD  GLU A 918     208.269 229.304 144.186  1.00 21.23           C  
ATOM   5656  OE1 GLU A 918     207.082 229.340 144.398  1.00 20.45           O  
ATOM   5657  OE2 GLU A 918     208.800 228.469 143.478  1.00 21.37           O  
ATOM   5658  N   ASN A 919     208.547 232.377 148.991  1.00 21.32           N  
ATOM   5659  CA  ASN A 919     207.876 233.127 150.031  1.00 20.97           C  
ATOM   5660  C   ASN A 919     208.838 233.635 151.099  1.00 21.62           C  
ATOM   5661  O   ASN A 919     208.417 233.921 152.219  1.00 22.22           O  
ATOM   5662  CB  ASN A 919     206.814 232.268 150.676  1.00 20.96           C  
ATOM   5663  CG  ASN A 919     205.713 231.942 149.750  1.00 20.84           C  
ATOM   5664  OD1 ASN A 919     204.867 232.786 149.432  1.00 21.25           O  
ATOM   5665  ND2 ASN A 919     205.697 230.725 149.286  1.00 20.70           N  
ATOM   5666  N   GLN A 920     210.121 233.773 150.785  1.00 21.38           N  
ATOM   5667  CA  GLN A 920     211.068 234.152 151.828  1.00 21.16           C  
ATOM   5668  C   GLN A 920     210.728 235.459 152.520  1.00 21.40           C  
ATOM   5669  O   GLN A 920     210.917 235.580 153.729  1.00 22.24           O  
ATOM   5670  CB  GLN A 920     212.486 234.238 151.285  1.00 21.55           C  
ATOM   5671  CG  GLN A 920     213.526 234.547 152.347  1.00 21.40           C  
ATOM   5672  CD  GLN A 920     214.912 234.474 151.807  1.00 21.85           C  
ATOM   5673  OE1 GLN A 920     215.156 233.796 150.808  1.00 22.12           O  
ATOM   5674  NE2 GLN A 920     215.841 235.166 152.448  1.00 22.50           N  
ATOM   5675  N   LYS A 921     210.250 236.453 151.781  1.00 21.70           N  
ATOM   5676  CA  LYS A 921     209.937 237.719 152.431  1.00 21.65           C  
ATOM   5677  C   LYS A 921     208.766 237.555 153.384  1.00 21.95           C  
ATOM   5678  O   LYS A 921     208.757 238.127 154.473  1.00 22.70           O  
ATOM   5679  CB  LYS A 921     209.648 238.814 151.415  1.00 22.01           C  
ATOM   5680  N   LEU A 922     207.782 236.763 152.982  1.00 21.87           N  
ATOM   5681  CA  LEU A 922     206.621 236.531 153.822  1.00 21.33           C  
ATOM   5682  C   LEU A 922     207.006 235.806 155.089  1.00 23.70           C  
ATOM   5683  O   LEU A 922     206.555 236.157 156.177  1.00 21.26           O  
ATOM   5684  CB  LEU A 922     205.581 235.693 153.083  1.00 21.68           C  
ATOM   5685  CG  LEU A 922     204.349 235.286 153.897  1.00 21.70           C  
ATOM   5686  CD1 LEU A 922     203.591 236.526 154.356  1.00 21.99           C  
ATOM   5687  CD2 LEU A 922     203.478 234.378 153.049  1.00 21.16           C  
ATOM   5688  N   ILE A 923     207.839 234.791 154.946  1.00 21.95           N  
ATOM   5689  CA  ILE A 923     208.253 233.988 156.075  1.00 21.21           C  
ATOM   5690  C   ILE A 923     209.047 234.811 157.059  1.00 22.56           C  
ATOM   5691  O   ILE A 923     208.818 234.722 158.264  1.00 22.91           O  
ATOM   5692  CB  ILE A 923     209.049 232.777 155.593  1.00 21.82           C  
ATOM   5693  CG1 ILE A 923     208.105 231.854 154.857  1.00 21.34           C  
ATOM   5694  CG2 ILE A 923     209.692 232.066 156.767  1.00 22.13           C  
ATOM   5695  CD1 ILE A 923     208.769 230.826 154.025  1.00 21.46           C  
ATOM   5696  N   ALA A 924     209.984 235.607 156.564  1.00 22.21           N  
ATOM   5697  CA  ALA A 924     210.764 236.444 157.451  1.00 22.37           C  
ATOM   5698  C   ALA A 924     209.867 237.440 158.175  1.00 23.16           C  
ATOM   5699  O   ALA A 924     210.049 237.680 159.369  1.00 23.87           O  
ATOM   5700  CB  ALA A 924     211.838 237.172 156.678  1.00 22.96           C  
ATOM   5701  N   ASN A 925     208.868 237.988 157.481  1.00 22.72           N  
ATOM   5702  CA  ASN A 925     207.972 238.947 158.112  1.00 22.41           C  
ATOM   5703  C   ASN A 925     207.099 238.296 159.170  1.00 22.92           C  
ATOM   5704  O   ASN A 925     206.882 238.873 160.238  1.00 24.60           O  
ATOM   5705  CB  ASN A 925     207.108 239.629 157.077  1.00 22.53           C  
ATOM   5706  CG  ASN A 925     207.862 240.630 156.268  1.00 22.84           C  
ATOM   5707  OD1 ASN A 925     208.879 241.177 156.707  1.00 22.73           O  
ATOM   5708  ND2 ASN A 925     207.385 240.891 155.081  1.00 22.64           N  
ATOM   5709  N   GLN A 926     206.624 237.082 158.905  1.00 22.72           N  
ATOM   5710  CA  GLN A 926     205.807 236.383 159.882  1.00 22.45           C  
ATOM   5711  C   GLN A 926     206.632 236.033 161.103  1.00 23.56           C  
ATOM   5712  O   GLN A 926     206.162 236.158 162.235  1.00 24.21           O  
ATOM   5713  CB  GLN A 926     205.214 235.111 159.287  1.00 21.91           C  
ATOM   5714  CG  GLN A 926     204.139 235.331 158.247  1.00 21.70           C  
ATOM   5715  CD  GLN A 926     203.743 234.034 157.617  1.00 21.04           C  
ATOM   5716  OE1 GLN A 926     204.482 233.058 157.749  1.00 21.58           O  
ATOM   5717  NE2 GLN A 926     202.598 233.990 156.952  1.00 21.22           N  
ATOM   5718  N   PHE A 927     207.874 235.623 160.882  1.00 23.08           N  
ATOM   5719  CA  PHE A 927     208.758 235.298 161.980  1.00 22.91           C  
ATOM   5720  C   PHE A 927     209.016 236.506 162.852  1.00 25.63           C  
ATOM   5721  O   PHE A 927     208.916 236.428 164.078  1.00 24.58           O  
ATOM   5722  CB  PHE A 927     210.083 234.756 161.479  1.00 23.54           C  
ATOM   5723  CG  PHE A 927     211.045 234.547 162.576  1.00 23.87           C  
ATOM   5724  CD1 PHE A 927     210.939 233.463 163.402  1.00 23.79           C  
ATOM   5725  CD2 PHE A 927     212.058 235.451 162.798  1.00 24.36           C  
ATOM   5726  CE1 PHE A 927     211.822 233.286 164.427  1.00 23.83           C  
ATOM   5727  CE2 PHE A 927     212.943 235.279 163.819  1.00 24.38           C  
ATOM   5728  CZ  PHE A 927     212.823 234.193 164.639  1.00 23.90           C  
ATOM   5729  N   ASN A 928     209.363 237.625 162.226  1.00 24.15           N  
ATOM   5730  CA  ASN A 928     209.702 238.822 162.964  1.00 23.99           C  
ATOM   5731  C   ASN A 928     208.513 239.295 163.780  1.00 24.66           C  
ATOM   5732  O   ASN A 928     208.669 239.724 164.927  1.00 25.49           O  
ATOM   5733  CB  ASN A 928     210.147 239.895 162.001  1.00 24.36           C  
ATOM   5734  CG  ASN A 928     211.438 239.547 161.364  1.00 24.39           C  
ATOM   5735  OD1 ASN A 928     212.191 238.726 161.890  1.00 24.87           O  
ATOM   5736  ND2 ASN A 928     211.712 240.130 160.232  1.00 24.43           N  
ATOM   5737  N   SER A 929     207.318 239.180 163.212  1.00 24.47           N  
ATOM   5738  CA  SER A 929     206.117 239.568 163.924  1.00 25.08           C  
ATOM   5739  C   SER A 929     205.899 238.670 165.127  1.00 25.70           C  
ATOM   5740  O   SER A 929     205.626 239.154 166.228  1.00 27.09           O  
ATOM   5741  CB  SER A 929     204.918 239.495 163.013  1.00 25.23           C  
ATOM   5742  OG  SER A 929     203.754 239.874 163.690  1.00 26.34           O  
ATOM   5743  N   ALA A 930     206.048 237.361 164.930  1.00 25.46           N  
ATOM   5744  CA  ALA A 930     205.826 236.410 166.004  1.00 25.16           C  
ATOM   5745  C   ALA A 930     206.750 236.667 167.184  1.00 25.90           C  
ATOM   5746  O   ALA A 930     206.321 236.575 168.333  1.00 27.05           O  
ATOM   5747  CB  ALA A 930     206.021 235.000 165.494  1.00 24.27           C  
ATOM   5748  N   ILE A 931     208.007 237.018 166.933  1.00 25.45           N  
ATOM   5749  CA  ILE A 931     208.886 237.270 168.066  1.00 25.59           C  
ATOM   5750  C   ILE A 931     208.401 238.507 168.806  1.00 26.70           C  
ATOM   5751  O   ILE A 931     208.340 238.513 170.037  1.00 27.45           O  
ATOM   5752  CB  ILE A 931     210.362 237.444 167.666  1.00 26.04           C  
ATOM   5753  CG1 ILE A 931     210.917 236.164 166.988  1.00 25.33           C  
ATOM   5754  CG2 ILE A 931     211.187 237.756 168.919  1.00 26.51           C  
ATOM   5755  CD1 ILE A 931     210.922 234.904 167.849  1.00 26.09           C  
ATOM   5756  N   GLY A 932     208.011 239.542 168.068  1.00 26.52           N  
ATOM   5757  CA  GLY A 932     207.497 240.748 168.707  1.00 26.73           C  
ATOM   5758  C   GLY A 932     206.296 240.426 169.597  1.00 26.82           C  
ATOM   5759  O   GLY A 932     206.118 241.025 170.660  1.00 28.30           O  
ATOM   5760  N   LYS A 933     205.475 239.468 169.176  1.00 26.64           N  
ATOM   5761  CA  LYS A 933     204.335 239.061 169.985  1.00 27.01           C  
ATOM   5762  C   LYS A 933     204.788 238.416 171.288  1.00 27.86           C  
ATOM   5763  O   LYS A 933     204.132 238.577 172.319  1.00 29.30           O  
ATOM   5764  CB  LYS A 933     203.415 238.118 169.219  1.00 27.30           C  
ATOM   5765  CG  LYS A 933     202.634 238.788 168.109  1.00 27.65           C  
ATOM   5766  CD  LYS A 933     201.740 237.798 167.385  1.00 27.76           C  
ATOM   5767  CE  LYS A 933     200.975 238.470 166.258  1.00 28.16           C  
ATOM   5768  NZ  LYS A 933     200.114 237.507 165.522  1.00 28.42           N  
ATOM   5769  N   ILE A 934     205.912 237.699 171.255  1.00 27.61           N  
ATOM   5770  CA  ILE A 934     206.428 237.064 172.461  1.00 27.11           C  
ATOM   5771  C   ILE A 934     206.807 238.130 173.466  1.00 28.83           C  
ATOM   5772  O   ILE A 934     206.532 237.986 174.659  1.00 28.88           O  
ATOM   5773  CB  ILE A 934     207.667 236.182 172.188  1.00 27.18           C  
ATOM   5774  CG1 ILE A 934     207.327 235.005 171.240  1.00 26.39           C  
ATOM   5775  CG2 ILE A 934     208.255 235.676 173.502  1.00 27.52           C  
ATOM   5776  CD1 ILE A 934     206.235 234.070 171.708  1.00 25.67           C  
ATOM   5777  N   GLN A 935     207.427 239.206 172.992  1.00 27.65           N  
ATOM   5778  CA  GLN A 935     207.817 240.274 173.901  1.00 28.07           C  
ATOM   5779  C   GLN A 935     206.601 240.867 174.595  1.00 28.89           C  
ATOM   5780  O   GLN A 935     206.624 241.103 175.804  1.00 29.73           O  
ATOM   5781  CB  GLN A 935     208.512 241.410 173.154  1.00 28.31           C  
ATOM   5782  CG  GLN A 935     209.861 241.101 172.594  1.00 28.16           C  
ATOM   5783  CD  GLN A 935     210.415 242.300 171.864  1.00 28.56           C  
ATOM   5784  OE1 GLN A 935     209.662 243.125 171.342  1.00 28.49           O  
ATOM   5785  NE2 GLN A 935     211.723 242.425 171.835  1.00 28.57           N  
ATOM   5786  N   ASP A 936     205.524 241.076 173.841  1.00 28.45           N  
ATOM   5787  CA  ASP A 936     204.321 241.666 174.412  1.00 28.82           C  
ATOM   5788  C   ASP A 936     203.626 240.715 175.366  1.00 29.16           C  
ATOM   5789  O   ASP A 936     203.101 241.135 176.401  1.00 30.06           O  
ATOM   5790  CB  ASP A 936     203.344 242.073 173.312  1.00 29.00           C  
ATOM   5791  CG  ASP A 936     203.787 243.297 172.529  1.00 29.20           C  
ATOM   5792  OD1 ASP A 936     204.652 244.008 172.985  1.00 29.24           O  
ATOM   5793  OD2 ASP A 936     203.245 243.516 171.476  1.00 29.02           O  
ATOM   5794  N   SER A 937     203.622 239.432 175.036  1.00 28.91           N  
ATOM   5795  CA  SER A 937     202.971 238.452 175.884  1.00 29.32           C  
ATOM   5796  C   SER A 937     203.656 238.373 177.237  1.00 30.23           C  
ATOM   5797  O   SER A 937     202.990 238.401 178.274  1.00 30.16           O  
ATOM   5798  CB  SER A 937     202.988 237.093 175.222  1.00 29.30           C  
ATOM   5799  OG  SER A 937     202.364 236.133 176.027  1.00 30.26           O  
ATOM   5800  N   LEU A 938     204.987 238.307 177.233  1.00 29.71           N  
ATOM   5801  CA  LEU A 938     205.742 238.220 178.475  1.00 29.90           C  
ATOM   5802  C   LEU A 938     205.683 239.507 179.279  1.00 30.24           C  
ATOM   5803  O   LEU A 938     205.620 239.470 180.506  1.00 30.19           O  
ATOM   5804  CB  LEU A 938     207.205 237.885 178.179  1.00 29.63           C  
ATOM   5805  CG  LEU A 938     207.495 236.479 177.643  1.00 29.58           C  
ATOM   5806  CD1 LEU A 938     208.934 236.435 177.197  1.00 29.77           C  
ATOM   5807  CD2 LEU A 938     207.231 235.429 178.732  1.00 29.54           C  
ATOM   5808  N   SER A 939     205.704 240.649 178.600  1.00 30.19           N  
ATOM   5809  CA  SER A 939     205.652 241.926 179.294  1.00 30.02           C  
ATOM   5810  C   SER A 939     204.313 242.107 180.006  1.00 30.53           C  
ATOM   5811  O   SER A 939     204.265 242.546 181.158  1.00 30.76           O  
ATOM   5812  CB  SER A 939     205.870 243.061 178.311  1.00 30.23           C  
ATOM   5813  OG  SER A 939     205.839 244.305 178.954  1.00 30.26           O  
ATOM   5814  N   SER A 940     203.228 241.774 179.308  1.00 30.00           N  
ATOM   5815  CA  SER A 940     201.873 241.943 179.814  1.00 30.30           C  
ATOM   5816  C   SER A 940     201.431 240.900 180.841  1.00 30.45           C  
ATOM   5817  O   SER A 940     200.841 241.254 181.866  1.00 30.24           O  
ATOM   5818  CB  SER A 940     200.901 241.932 178.652  1.00 30.38           C  
ATOM   5819  OG  SER A 940     199.585 242.107 179.094  1.00 30.52           O  
ATOM   5820  N   THR A 941     201.666 239.619 180.561  1.00 29.36           N  
ATOM   5821  CA  THR A 941     201.141 238.564 181.417  1.00 29.98           C  
ATOM   5822  C   THR A 941     202.201 237.983 182.351  1.00 30.76           C  
ATOM   5823  O   THR A 941     203.029 237.161 181.959  1.00 29.26           O  
ATOM   5824  CB  THR A 941     200.542 237.446 180.533  1.00 29.86           C  
ATOM   5825  OG1 THR A 941     199.484 237.989 179.734  1.00 29.63           O  
ATOM   5826  CG2 THR A 941     199.989 236.320 181.372  1.00 29.68           C  
ATOM   5827  N   ALA A 942     202.141 238.365 183.626  1.00 29.50           N  
ATOM   5828  CA  ALA A 942     203.129 237.901 184.600  1.00 29.64           C  
ATOM   5829  C   ALA A 942     203.031 236.393 184.790  1.00 29.42           C  
ATOM   5830  O   ALA A 942     204.039 235.700 184.948  1.00 29.36           O  
ATOM   5831  CB  ALA A 942     202.936 238.611 185.929  1.00 29.28           C  
ATOM   5832  N   SER A 943     201.807 235.882 184.708  1.00 29.43           N  
ATOM   5833  CA  SER A 943     201.508 234.471 184.912  1.00 29.26           C  
ATOM   5834  C   SER A 943     202.133 233.579 183.845  1.00 29.54           C  
ATOM   5835  O   SER A 943     202.113 232.352 183.961  1.00 29.01           O  
ATOM   5836  CB  SER A 943     200.007 234.252 184.961  1.00 29.62           C  
ATOM   5837  OG  SER A 943     199.416 234.505 183.723  1.00 29.40           O  
ATOM   5838  N   ALA A 944     202.680 234.187 182.797  1.00 28.99           N  
ATOM   5839  CA  ALA A 944     203.298 233.448 181.713  1.00 29.26           C  
ATOM   5840  C   ALA A 944     204.419 232.557 182.232  1.00 28.89           C  
ATOM   5841  O   ALA A 944     204.667 231.488 181.680  1.00 28.38           O  
ATOM   5842  CB  ALA A 944     203.839 234.412 180.671  1.00 29.56           C  
ATOM   5843  N   LEU A 945     205.103 232.994 183.290  1.00 28.82           N  
ATOM   5844  CA  LEU A 945     206.209 232.227 183.848  1.00 28.04           C  
ATOM   5845  C   LEU A 945     205.834 231.587 185.168  1.00 27.66           C  
ATOM   5846  O   LEU A 945     206.701 231.316 186.005  1.00 28.22           O  
ATOM   5847  CB  LEU A 945     207.430 233.114 184.051  1.00 27.84           C  
ATOM   5848  CG  LEU A 945     207.935 233.825 182.815  1.00 28.64           C  
ATOM   5849  CD1 LEU A 945     209.115 234.644 183.193  1.00 28.75           C  
ATOM   5850  CD2 LEU A 945     208.289 232.834 181.737  1.00 28.65           C  
ATOM   5851  N   GLY A 946     204.548 231.315 185.349  1.00 28.07           N  
ATOM   5852  CA  GLY A 946     204.048 230.754 186.591  1.00 27.69           C  
ATOM   5853  C   GLY A 946     204.799 229.506 187.031  1.00 27.38           C  
ATOM   5854  O   GLY A 946     204.953 229.278 188.227  1.00 27.52           O  
ATOM   5855  N   LYS A 947     205.278 228.692 186.097  1.00 27.38           N  
ATOM   5856  CA  LYS A 947     206.003 227.492 186.493  1.00 27.33           C  
ATOM   5857  C   LYS A 947     207.271 227.800 187.280  1.00 27.10           C  
ATOM   5858  O   LYS A 947     207.626 227.056 188.197  1.00 27.22           O  
ATOM   5859  CB  LYS A 947     206.352 226.638 185.280  1.00 26.92           C  
ATOM   5860  CG  LYS A 947     205.164 225.939 184.659  1.00 27.19           C  
ATOM   5861  CD  LYS A 947     205.579 225.082 183.478  1.00 26.41           C  
ATOM   5862  CE  LYS A 947     204.387 224.340 182.889  1.00 27.25           C  
ATOM   5863  NZ  LYS A 947     204.781 223.455 181.757  1.00 27.31           N  
ATOM   5864  N   LEU A 948     207.965 228.880 186.930  1.00 27.08           N  
ATOM   5865  CA  LEU A 948     209.212 229.192 187.610  1.00 27.11           C  
ATOM   5866  C   LEU A 948     208.903 229.845 188.937  1.00 27.48           C  
ATOM   5867  O   LEU A 948     209.581 229.602 189.939  1.00 27.85           O  
ATOM   5868  CB  LEU A 948     210.068 230.140 186.765  1.00 27.14           C  
ATOM   5869  CG  LEU A 948     210.547 229.607 185.416  1.00 26.39           C  
ATOM   5870  CD1 LEU A 948     211.242 230.733 184.654  1.00 27.17           C  
ATOM   5871  CD2 LEU A 948     211.496 228.439 185.608  1.00 25.68           C  
ATOM   5872  N   GLN A 949     207.855 230.657 188.951  1.00 27.31           N  
ATOM   5873  CA  GLN A 949     207.462 231.329 190.172  1.00 26.70           C  
ATOM   5874  C   GLN A 949     206.942 230.322 191.179  1.00 31.94           C  
ATOM   5875  O   GLN A 949     207.163 230.471 192.378  1.00 26.47           O  
ATOM   5876  CB  GLN A 949     206.409 232.394 189.898  1.00 28.02           C  
ATOM   5877  CG  GLN A 949     206.049 233.234 191.110  1.00 28.37           C  
ATOM   5878  CD  GLN A 949     207.221 234.046 191.634  1.00 29.07           C  
ATOM   5879  OE1 GLN A 949     207.911 234.715 190.851  1.00 29.16           O  
ATOM   5880  NE2 GLN A 949     207.445 234.006 192.944  1.00 29.19           N  
ATOM   5881  N   ASP A 950     206.267 229.285 190.693  1.00 26.91           N  
ATOM   5882  CA  ASP A 950     205.719 228.257 191.559  1.00 26.33           C  
ATOM   5883  C   ASP A 950     206.816 227.485 192.267  1.00 31.90           C  
ATOM   5884  O   ASP A 950     206.693 227.186 193.453  1.00 26.02           O  
ATOM   5885  CB  ASP A 950     204.845 227.292 190.768  1.00 26.96           C  
ATOM   5886  CG  ASP A 950     204.143 226.289 191.652  1.00 26.72           C  
ATOM   5887  OD1 ASP A 950     203.316 226.681 192.438  1.00 26.56           O  
ATOM   5888  OD2 ASP A 950     204.446 225.127 191.539  1.00 26.71           O  
ATOM   5889  N   VAL A 951     207.912 227.199 191.574  1.00 26.28           N  
ATOM   5890  CA  VAL A 951     209.004 226.501 192.232  1.00 26.74           C  
ATOM   5891  C   VAL A 951     209.559 227.358 193.350  1.00 27.10           C  
ATOM   5892  O   VAL A 951     209.811 226.865 194.453  1.00 28.56           O  
ATOM   5893  CB  VAL A 951     210.117 226.146 191.241  1.00 27.22           C  
ATOM   5894  CG1 VAL A 951     211.345 225.598 191.982  1.00 27.07           C  
ATOM   5895  CG2 VAL A 951     209.584 225.124 190.279  1.00 27.85           C  
ATOM   5896  N   VAL A 952     209.718 228.647 193.080  1.00 27.18           N  
ATOM   5897  CA  VAL A 952     210.216 229.558 194.092  1.00 26.82           C  
ATOM   5898  C   VAL A 952     209.269 229.620 195.280  1.00 27.06           C  
ATOM   5899  O   VAL A 952     209.712 229.598 196.431  1.00 28.20           O  
ATOM   5900  CB  VAL A 952     210.394 230.968 193.504  1.00 28.08           C  
ATOM   5901  CG1 VAL A 952     210.712 231.967 194.603  1.00 28.57           C  
ATOM   5902  CG2 VAL A 952     211.507 230.942 192.479  1.00 28.08           C  
ATOM   5903  N   ASN A 953     207.971 229.697 195.012  1.00 27.02           N  
ATOM   5904  CA  ASN A 953     206.998 229.792 196.083  1.00 26.43           C  
ATOM   5905  C   ASN A 953     206.962 228.536 196.940  1.00 29.08           C  
ATOM   5906  O   ASN A 953     206.868 228.633 198.164  1.00 28.29           O  
ATOM   5907  CB  ASN A 953     205.619 230.055 195.527  1.00 27.16           C  
ATOM   5908  CG  ASN A 953     205.462 231.427 194.957  1.00 27.79           C  
ATOM   5909  OD1 ASN A 953     206.288 232.326 195.160  1.00 28.40           O  
ATOM   5910  ND2 ASN A 953     204.386 231.619 194.246  1.00 28.95           N  
ATOM   5911  N   GLN A 954     207.066 227.358 196.327  1.00 26.34           N  
ATOM   5912  CA  GLN A 954     207.026 226.141 197.122  1.00 26.16           C  
ATOM   5913  C   GLN A 954     208.229 226.040 198.035  1.00 27.92           C  
ATOM   5914  O   GLN A 954     208.104 225.625 199.189  1.00 27.84           O  
ATOM   5915  CB  GLN A 954     206.980 224.887 196.253  1.00 26.39           C  
ATOM   5916  CG  GLN A 954     205.685 224.646 195.505  1.00 26.02           C  
ATOM   5917  CD  GLN A 954     205.710 223.308 194.769  1.00 26.11           C  
ATOM   5918  OE1 GLN A 954     206.194 222.309 195.322  1.00 25.62           O  
ATOM   5919  NE2 GLN A 954     205.205 223.264 193.542  1.00 25.66           N  
ATOM   5920  N   ASN A 955     209.392 226.439 197.541  1.00 26.81           N  
ATOM   5921  CA  ASN A 955     210.580 226.361 198.364  1.00 26.82           C  
ATOM   5922  C   ASN A 955     210.525 227.386 199.482  1.00 27.40           C  
ATOM   5923  O   ASN A 955     210.953 227.111 200.604  1.00 28.51           O  
ATOM   5924  CB  ASN A 955     211.808 226.534 197.509  1.00 27.38           C  
ATOM   5925  CG  ASN A 955     212.060 225.322 196.681  1.00 27.21           C  
ATOM   5926  OD1 ASN A 955     211.718 224.208 197.082  1.00 27.19           O  
ATOM   5927  ND2 ASN A 955     212.635 225.506 195.527  1.00 27.53           N  
ATOM   5928  N   ALA A 956     209.968 228.558 199.197  1.00 27.64           N  
ATOM   5929  CA  ALA A 956     209.846 229.577 200.220  1.00 27.36           C  
ATOM   5930  C   ALA A 956     208.939 229.101 201.339  1.00 27.50           C  
ATOM   5931  O   ALA A 956     209.245 229.295 202.515  1.00 28.80           O  
ATOM   5932  CB  ALA A 956     209.302 230.858 199.622  1.00 28.15           C  
ATOM   5933  N   GLN A 957     207.849 228.429 200.981  1.00 27.30           N  
ATOM   5934  CA  GLN A 957     206.934 227.921 201.985  1.00 27.63           C  
ATOM   5935  C   GLN A 957     207.587 226.842 202.816  1.00 28.18           C  
ATOM   5936  O   GLN A 957     207.389 226.787 204.031  1.00 29.55           O  
ATOM   5937  CB  GLN A 957     205.670 227.367 201.345  1.00 27.88           C  
ATOM   5938  CG  GLN A 957     204.767 228.411 200.752  1.00 27.90           C  
ATOM   5939  CD  GLN A 957     203.606 227.789 200.017  1.00 29.06           C  
ATOM   5940  OE1 GLN A 957     203.472 226.561 199.978  1.00 28.55           O  
ATOM   5941  NE2 GLN A 957     202.761 228.621 199.426  1.00 28.86           N  
ATOM   5942  N   ALA A 958     208.388 225.991 202.183  1.00 28.01           N  
ATOM   5943  CA  ALA A 958     209.046 224.923 202.915  1.00 28.07           C  
ATOM   5944  C   ALA A 958     209.938 225.491 204.006  1.00 28.27           C  
ATOM   5945  O   ALA A 958     209.973 224.961 205.120  1.00 29.41           O  
ATOM   5946  CB  ALA A 958     209.865 224.064 201.970  1.00 28.25           C  
ATOM   5947  N   LEU A 959     210.627 226.592 203.708  1.00 28.12           N  
ATOM   5948  CA  LEU A 959     211.509 227.189 204.697  1.00 27.63           C  
ATOM   5949  C   LEU A 959     210.735 227.958 205.741  1.00 28.68           C  
ATOM   5950  O   LEU A 959     211.096 227.937 206.917  1.00 30.41           O  
ATOM   5951  CB  LEU A 959     212.528 228.123 204.054  1.00 27.45           C  
ATOM   5952  CG  LEU A 959     213.836 227.478 203.608  1.00 28.13           C  
ATOM   5953  CD1 LEU A 959     213.586 226.599 202.390  1.00 28.91           C  
ATOM   5954  CD2 LEU A 959     214.847 228.570 203.310  1.00 29.09           C  
ATOM   5955  N   ASN A 960     209.664 228.629 205.339  1.00 28.47           N  
ATOM   5956  CA  ASN A 960     208.890 229.381 206.307  1.00 28.34           C  
ATOM   5957  C   ASN A 960     208.239 228.440 207.296  1.00 30.70           C  
ATOM   5958  O   ASN A 960     208.145 228.751 208.482  1.00 31.30           O  
ATOM   5959  CB  ASN A 960     207.853 230.233 205.623  1.00 28.71           C  
ATOM   5960  CG  ASN A 960     208.454 231.407 204.940  1.00 28.89           C  
ATOM   5961  OD1 ASN A 960     209.557 231.847 205.279  1.00 28.68           O  
ATOM   5962  ND2 ASN A 960     207.753 231.936 203.975  1.00 28.67           N  
ATOM   5963  N   THR A 961     207.816 227.274 206.824  1.00 28.84           N  
ATOM   5964  CA  THR A 961     207.215 226.296 207.710  1.00 29.23           C  
ATOM   5965  C   THR A 961     208.259 225.792 208.682  1.00 29.62           C  
ATOM   5966  O   THR A 961     207.998 225.685 209.880  1.00 31.26           O  
ATOM   5967  CB  THR A 961     206.616 225.114 206.933  1.00 29.46           C  
ATOM   5968  OG1 THR A 961     205.597 225.589 206.049  1.00 29.72           O  
ATOM   5969  CG2 THR A 961     206.007 224.096 207.903  1.00 29.80           C  
ATOM   5970  N   LEU A 962     209.452 225.501 208.175  1.00 29.68           N  
ATOM   5971  CA  LEU A 962     210.505 224.982 209.021  1.00 29.89           C  
ATOM   5972  C   LEU A 962     210.847 225.968 210.128  1.00 31.45           C  
ATOM   5973  O   LEU A 962     210.988 225.580 211.283  1.00 33.24           O  
ATOM   5974  CB  LEU A 962     211.755 224.691 208.179  1.00 29.65           C  
ATOM   5975  CG  LEU A 962     212.963 224.111 208.916  1.00 30.63           C  
ATOM   5976  CD1 LEU A 962     212.604 222.754 209.504  1.00 30.92           C  
ATOM   5977  CD2 LEU A 962     214.135 223.991 207.954  1.00 30.53           C  
ATOM   5978  N   VAL A 963     210.952 227.248 209.798  1.00 30.50           N  
ATOM   5979  CA  VAL A 963     211.273 228.234 210.818  1.00 31.04           C  
ATOM   5980  C   VAL A 963     210.147 228.405 211.819  1.00 31.87           C  
ATOM   5981  O   VAL A 963     210.385 228.507 213.018  1.00 34.48           O  
ATOM   5982  CB  VAL A 963     211.611 229.588 210.203  1.00 32.06           C  
ATOM   5983  CG1 VAL A 963     211.758 230.626 211.289  1.00 34.77           C  
ATOM   5984  CG2 VAL A 963     212.885 229.472 209.457  1.00 33.03           C  
ATOM   5985  N   LYS A 964     208.910 228.452 211.350  1.00 31.64           N  
ATOM   5986  CA  LYS A 964     207.796 228.618 212.270  1.00 31.72           C  
ATOM   5987  C   LYS A 964     207.722 227.490 213.285  1.00 32.24           C  
ATOM   5988  O   LYS A 964     207.336 227.722 214.426  1.00 33.32           O  
ATOM   5989  CB  LYS A 964     206.480 228.745 211.522  1.00 31.88           C  
ATOM   5990  CG  LYS A 964     206.303 230.075 210.822  1.00 32.88           C  
ATOM   5991  CD  LYS A 964     205.009 230.112 210.037  1.00 33.55           C  
ATOM   5992  CE  LYS A 964     204.835 231.439 209.315  1.00 34.04           C  
ATOM   5993  NZ  LYS A 964     203.588 231.469 208.499  1.00 34.30           N  
ATOM   5994  N   GLN A 965     208.141 226.283 212.908  1.00 32.19           N  
ATOM   5995  CA  GLN A 965     208.101 225.153 213.834  1.00 31.91           C  
ATOM   5996  C   GLN A 965     208.967 225.366 215.066  1.00 33.24           C  
ATOM   5997  O   GLN A 965     208.786 224.685 216.072  1.00 33.85           O  
ATOM   5998  CB  GLN A 965     208.511 223.845 213.156  1.00 31.72           C  
ATOM   5999  CG  GLN A 965     207.484 223.296 212.205  1.00 31.89           C  
ATOM   6000  CD  GLN A 965     206.198 222.962 212.902  1.00 31.89           C  
ATOM   6001  OE1 GLN A 965     205.298 223.804 212.921  1.00 32.10           O  
ATOM   6002  NE2 GLN A 965     206.094 221.772 213.478  1.00 31.76           N  
ATOM   6003  N   LEU A 966     209.909 226.294 215.014  1.00 32.82           N  
ATOM   6004  CA  LEU A 966     210.756 226.546 216.166  1.00 33.29           C  
ATOM   6005  C   LEU A 966     209.958 227.130 217.327  1.00 34.18           C  
ATOM   6006  O   LEU A 966     210.372 227.017 218.482  1.00 35.22           O  
ATOM   6007  CB  LEU A 966     211.890 227.498 215.792  1.00 33.72           C  
ATOM   6008  CG  LEU A 966     212.953 226.939 214.843  1.00 33.43           C  
ATOM   6009  CD1 LEU A 966     213.835 228.070 214.384  1.00 34.68           C  
ATOM   6010  CD2 LEU A 966     213.794 225.882 215.568  1.00 33.62           C  
ATOM   6011  N   SER A 967     208.815 227.757 217.028  1.00 34.04           N  
ATOM   6012  CA  SER A 967     207.978 228.378 218.048  1.00 34.39           C  
ATOM   6013  C   SER A 967     207.106 227.356 218.761  1.00 34.46           C  
ATOM   6014  O   SER A 967     206.404 227.692 219.714  1.00 35.25           O  
ATOM   6015  CB  SER A 967     207.069 229.427 217.445  1.00 35.61           C  
ATOM   6016  OG  SER A 967     206.010 228.841 216.748  1.00 34.06           O  
ATOM   6017  N   SER A 968     207.075 226.127 218.263  1.00 33.99           N  
ATOM   6018  CA  SER A 968     206.230 225.105 218.853  1.00 33.59           C  
ATOM   6019  C   SER A 968     206.831 224.564 220.143  1.00 34.53           C  
ATOM   6020  O   SER A 968     208.049 224.445 220.282  1.00 35.18           O  
ATOM   6021  CB  SER A 968     206.012 223.992 217.861  1.00 33.40           C  
ATOM   6022  OG  SER A 968     205.292 224.443 216.755  1.00 33.22           O  
ATOM   6023  N   ASN A 969     205.969 224.231 221.095  1.00 34.43           N  
ATOM   6024  CA  ASN A 969     206.420 223.676 222.361  1.00 34.43           C  
ATOM   6025  C   ASN A 969     206.659 222.179 222.293  1.00 34.65           C  
ATOM   6026  O   ASN A 969     207.516 221.649 222.992  1.00 35.81           O  
ATOM   6027  CB  ASN A 969     205.415 223.977 223.448  1.00 35.25           C  
ATOM   6028  CG  ASN A 969     205.399 225.411 223.854  1.00 36.14           C  
ATOM   6029  OD1 ASN A 969     206.402 226.118 223.762  1.00 36.53           O  
ATOM   6030  ND2 ASN A 969     204.264 225.865 224.305  1.00 36.34           N  
ATOM   6031  N   PHE A 970     205.864 221.478 221.501  1.00 33.87           N  
ATOM   6032  CA  PHE A 970     205.966 220.028 221.394  1.00 33.81           C  
ATOM   6033  C   PHE A 970     205.819 219.315 222.734  1.00 34.73           C  
ATOM   6034  O   PHE A 970     206.337 218.214 222.915  1.00 35.17           O  
ATOM   6035  CB  PHE A 970     207.295 219.618 220.770  1.00 34.04           C  
ATOM   6036  CG  PHE A 970     207.538 220.172 219.412  1.00 33.61           C  
ATOM   6037  CD1 PHE A 970     208.534 221.100 219.196  1.00 33.79           C  
ATOM   6038  CD2 PHE A 970     206.780 219.756 218.341  1.00 33.09           C  
ATOM   6039  CE1 PHE A 970     208.768 221.591 217.936  1.00 33.24           C  
ATOM   6040  CE2 PHE A 970     207.008 220.249 217.085  1.00 32.82           C  
ATOM   6041  CZ  PHE A 970     208.005 221.163 216.881  1.00 32.97           C  
ATOM   6042  N   GLY A 971     205.106 219.927 223.671  1.00 35.15           N  
ATOM   6043  CA  GLY A 971     204.889 219.338 224.985  1.00 35.49           C  
ATOM   6044  C   GLY A 971     205.823 219.918 226.042  1.00 36.13           C  
ATOM   6045  O   GLY A 971     205.658 219.657 227.234  1.00 36.83           O  
ATOM   6046  N   ALA A 972     206.803 220.694 225.610  1.00 35.95           N  
ATOM   6047  CA  ALA A 972     207.735 221.328 226.525  1.00 36.39           C  
ATOM   6048  C   ALA A 972     207.076 222.523 227.189  1.00 37.37           C  
ATOM   6049  O   ALA A 972     206.101 223.070 226.675  1.00 37.32           O  
ATOM   6050  CB  ALA A 972     208.995 221.764 225.798  1.00 37.17           C  
ATOM   6051  N   ILE A 973     207.626 222.945 228.320  1.00 38.79           N  
ATOM   6052  CA  ILE A 973     207.147 224.144 229.008  1.00 39.09           C  
ATOM   6053  C   ILE A 973     207.381 225.419 228.209  1.00 38.68           C  
ATOM   6054  O   ILE A 973     206.734 226.437 228.449  1.00 39.21           O  
ATOM   6055  CB  ILE A 973     207.810 224.308 230.390  1.00 40.27           C  
ATOM   6056  CG1 ILE A 973     209.357 224.469 230.227  1.00 41.80           C  
ATOM   6057  CG2 ILE A 973     207.440 223.135 231.281  1.00 39.93           C  
ATOM   6058  CD1 ILE A 973     210.080 224.856 231.486  1.00 44.79           C  
ATOM   6059  N   SER A 974     208.339 225.377 227.299  1.00 38.56           N  
ATOM   6060  CA  SER A 974     208.664 226.535 226.493  1.00 38.19           C  
ATOM   6061  C   SER A 974     209.337 226.148 225.197  1.00 38.03           C  
ATOM   6062  O   SER A 974     210.187 225.262 225.166  1.00 38.51           O  
ATOM   6063  CB  SER A 974     209.565 227.471 227.255  1.00 39.58           C  
ATOM   6064  OG  SER A 974     209.896 228.580 226.466  1.00 39.30           O  
ATOM   6065  N   SER A 975     209.011 226.878 224.141  1.00 37.80           N  
ATOM   6066  CA  SER A 975     209.614 226.705 222.830  1.00 36.84           C  
ATOM   6067  C   SER A 975     211.004 227.312 222.758  1.00 37.66           C  
ATOM   6068  O   SER A 975     211.720 227.122 221.775  1.00 37.48           O  
ATOM   6069  CB  SER A 975     208.734 227.338 221.790  1.00 36.90           C  
ATOM   6070  OG  SER A 975     208.667 228.717 221.978  1.00 37.41           O  
ATOM   6071  N   VAL A 976     211.373 228.072 223.781  1.00 38.32           N  
ATOM   6072  CA  VAL A 976     212.665 228.724 223.802  1.00 38.86           C  
ATOM   6073  C   VAL A 976     213.642 227.941 224.660  1.00 41.18           C  
ATOM   6074  O   VAL A 976     213.458 227.782 225.868  1.00 40.37           O  
ATOM   6075  CB  VAL A 976     212.538 230.159 224.331  1.00 39.93           C  
ATOM   6076  CG1 VAL A 976     213.900 230.827 224.376  1.00 40.53           C  
ATOM   6077  CG2 VAL A 976     211.601 230.948 223.439  1.00 39.75           C  
ATOM   6078  N   LEU A 977     214.701 227.479 224.026  1.00 39.47           N  
ATOM   6079  CA  LEU A 977     215.679 226.632 224.673  1.00 40.00           C  
ATOM   6080  C   LEU A 977     216.402 227.361 225.792  1.00 41.88           C  
ATOM   6081  O   LEU A 977     216.690 226.780 226.840  1.00 42.85           O  
ATOM   6082  CB  LEU A 977     216.660 226.136 223.616  1.00 39.25           C  
ATOM   6083  CG  LEU A 977     217.735 225.171 224.053  1.00 40.03           C  
ATOM   6084  CD1 LEU A 977     217.118 223.938 224.666  1.00 39.99           C  
ATOM   6085  CD2 LEU A 977     218.544 224.796 222.834  1.00 38.52           C  
ATOM   6086  N   ASN A 978     216.683 228.640 225.582  1.00 41.42           N  
ATOM   6087  CA  ASN A 978     217.396 229.411 226.585  1.00 41.96           C  
ATOM   6088  C   ASN A 978     216.556 229.614 227.839  1.00 44.20           C  
ATOM   6089  O   ASN A 978     217.103 229.743 228.934  1.00 44.89           O  
ATOM   6090  CB  ASN A 978     217.838 230.747 226.034  1.00 43.01           C  
ATOM   6091  CG  ASN A 978     218.934 230.613 225.034  1.00 43.89           C  
ATOM   6092  OD1 ASN A 978     219.514 229.536 224.865  1.00 42.38           O  
ATOM   6093  ND2 ASN A 978     219.250 231.690 224.370  1.00 45.05           N  
ATOM   6094  N   ASP A 979     215.230 229.642 227.694  1.00 42.97           N  
ATOM   6095  CA  ASP A 979     214.367 229.844 228.847  1.00 42.50           C  
ATOM   6096  C   ASP A 979     214.323 228.585 229.688  1.00 46.77           C  
ATOM   6097  O   ASP A 979     214.344 228.654 230.918  1.00 47.85           O  
ATOM   6098  CB  ASP A 979     212.961 230.238 228.414  1.00 42.52           C  
ATOM   6099  CG  ASP A 979     212.882 231.647 227.828  1.00 42.46           C  
ATOM   6100  OD1 ASP A 979     213.779 232.433 228.034  1.00 43.26           O  
ATOM   6101  OD2 ASP A 979     211.911 231.924 227.173  1.00 42.40           O  
ATOM   6102  N   ILE A 980     214.334 227.431 229.034  1.00 42.58           N  
ATOM   6103  CA  ILE A 980     214.354 226.180 229.772  1.00 43.39           C  
ATOM   6104  C   ILE A 980     215.636 226.078 230.569  1.00 46.46           C  
ATOM   6105  O   ILE A 980     215.614 225.694 231.737  1.00 48.43           O  
ATOM   6106  CB  ILE A 980     214.255 224.964 228.846  1.00 42.73           C  
ATOM   6107  CG1 ILE A 980     212.882 224.921 228.208  1.00 41.51           C  
ATOM   6108  CG2 ILE A 980     214.539 223.676 229.642  1.00 42.76           C  
ATOM   6109  CD1 ILE A 980     212.780 223.953 227.064  1.00 40.51           C  
ATOM   6110  N   LEU A 981     216.753 226.413 229.935  1.00 43.94           N  
ATOM   6111  CA  LEU A 981     218.047 226.346 230.595  1.00 45.25           C  
ATOM   6112  C   LEU A 981     218.183 227.370 231.721  1.00 47.17           C  
ATOM   6113  O   LEU A 981     218.839 227.101 232.729  1.00 48.40           O  
ATOM   6114  CB  LEU A 981     219.157 226.541 229.561  1.00 44.60           C  
ATOM   6115  CG  LEU A 981     219.327 225.401 228.531  1.00 43.23           C  
ATOM   6116  CD1 LEU A 981     220.267 225.855 227.435  1.00 41.59           C  
ATOM   6117  CD2 LEU A 981     219.893 224.160 229.211  1.00 42.26           C  
ATOM   6118  N   SER A 982     217.569 228.544 231.563  1.00 46.95           N  
ATOM   6119  CA  SER A 982     217.627 229.565 232.603  1.00 48.10           C  
ATOM   6120  C   SER A 982     216.739 229.228 233.796  1.00 49.48           C  
ATOM   6121  O   SER A 982     217.033 229.615 234.925  1.00 51.99           O  
ATOM   6122  CB  SER A 982     217.218 230.916 232.053  1.00 47.72           C  
ATOM   6123  OG  SER A 982     218.139 231.379 231.114  1.00 47.36           O  
ATOM   6124  N   ARG A 983     215.633 228.535 233.549  1.00 48.52           N  
ATOM   6125  CA  ARG A 983     214.699 228.213 234.615  1.00 49.62           C  
ATOM   6126  C   ARG A 983     214.973 226.904 235.333  1.00 52.01           C  
ATOM   6127  O   ARG A 983     214.760 226.812 236.542  1.00 56.05           O  
ATOM   6128  CB  ARG A 983     213.282 228.164 234.070  1.00 51.40           C  
ATOM   6129  CG  ARG A 983     212.695 229.507 233.726  1.00 52.65           C  
ATOM   6130  CD  ARG A 983     211.474 229.401 232.884  1.00 52.23           C  
ATOM   6131  NE  ARG A 983     210.402 228.621 233.499  1.00 54.45           N  
ATOM   6132  CZ  ARG A 983     209.167 228.500 232.977  1.00 56.21           C  
ATOM   6133  NH1 ARG A 983     208.853 229.131 231.874  1.00 54.57           N  
ATOM   6134  NH2 ARG A 983     208.282 227.740 233.581  1.00 57.81           N  
ATOM   6135  N   LEU A 984     215.409 225.877 234.615  1.00 49.87           N  
ATOM   6136  CA  LEU A 984     215.526 224.573 235.248  1.00 49.48           C  
ATOM   6137  C   LEU A 984     216.932 224.009 235.369  1.00 49.02           C  
ATOM   6138  O   LEU A 984     217.766 224.145 234.475  1.00 48.59           O  
ATOM   6139  CB  LEU A 984     214.685 223.572 234.472  1.00 47.44           C  
ATOM   6140  CG  LEU A 984     213.209 223.901 234.301  1.00 47.98           C  
ATOM   6141  CD1 LEU A 984     212.609 222.830 233.444  1.00 45.20           C  
ATOM   6142  CD2 LEU A 984     212.512 223.979 235.656  1.00 52.61           C  
ATOM   6143  N   ASP A 985     217.148 223.293 236.464  1.00 49.50           N  
ATOM   6144  CA  ASP A 985     218.344 222.499 236.687  1.00 48.63           C  
ATOM   6145  C   ASP A 985     218.304 221.294 235.746  1.00 47.25           C  
ATOM   6146  O   ASP A 985     217.212 220.793 235.462  1.00 45.66           O  
ATOM   6147  CB  ASP A 985     218.394 222.029 238.140  1.00 49.41           C  
ATOM   6148  CG  ASP A 985     218.704 223.127 239.118  1.00 51.97           C  
ATOM   6149  OD1 ASP A 985     219.287 224.105 238.731  1.00 52.08           O  
ATOM   6150  OD2 ASP A 985     218.330 222.988 240.256  1.00 54.61           O  
ATOM   6151  N   PRO A 986     219.459 220.763 235.307  1.00 45.57           N  
ATOM   6152  CA  PRO A 986     219.613 219.635 234.394  1.00 44.49           C  
ATOM   6153  C   PRO A 986     218.677 218.429 234.603  1.00 44.02           C  
ATOM   6154  O   PRO A 986     218.104 217.961 233.620  1.00 43.48           O  
ATOM   6155  CB  PRO A 986     221.090 219.268 234.595  1.00 44.19           C  
ATOM   6156  CG  PRO A 986     221.744 220.590 234.890  1.00 44.70           C  
ATOM   6157  CD  PRO A 986     220.749 221.334 235.757  1.00 46.04           C  
ATOM   6158  N   PRO A 987     218.425 217.922 235.827  1.00 44.14           N  
ATOM   6159  CA  PRO A 987     217.585 216.761 236.058  1.00 43.89           C  
ATOM   6160  C   PRO A 987     216.222 216.891 235.386  1.00 43.38           C  
ATOM   6161  O   PRO A 987     215.635 215.888 234.985  1.00 43.08           O  
ATOM   6162  CB  PRO A 987     217.472 216.737 237.583  1.00 44.85           C  
ATOM   6163  CG  PRO A 987     218.748 217.386 238.055  1.00 45.15           C  
ATOM   6164  CD  PRO A 987     218.979 218.496 237.071  1.00 44.92           C  
ATOM   6165  N   GLU A 988     215.712 218.121 235.272  1.00 43.31           N  
ATOM   6166  CA  GLU A 988     214.434 218.336 234.607  1.00 42.85           C  
ATOM   6167  C   GLU A 988     214.638 219.036 233.276  1.00 44.04           C  
ATOM   6168  O   GLU A 988     213.915 218.787 232.311  1.00 41.05           O  
ATOM   6169  CB  GLU A 988     213.472 219.150 235.467  1.00 43.76           C  
ATOM   6170  CG  GLU A 988     212.082 219.334 234.828  1.00 43.47           C  
ATOM   6171  CD  GLU A 988     211.314 218.056 234.684  1.00 42.65           C  
ATOM   6172  OE1 GLU A 988     211.565 217.150 235.439  1.00 43.30           O  
ATOM   6173  OE2 GLU A 988     210.478 217.977 233.804  1.00 42.13           O  
ATOM   6174  N   ALA A 989     215.632 219.914 233.204  1.00 43.70           N  
ATOM   6175  CA  ALA A 989     215.837 220.685 231.992  1.00 42.02           C  
ATOM   6176  C   ALA A 989     216.040 219.751 230.824  1.00 41.18           C  
ATOM   6177  O   ALA A 989     215.569 220.022 229.725  1.00 40.92           O  
ATOM   6178  CB  ALA A 989     217.035 221.604 232.122  1.00 43.78           C  
ATOM   6179  N   GLU A 990     216.711 218.632 231.066  1.00 41.58           N  
ATOM   6180  CA  GLU A 990     216.970 217.664 230.020  1.00 39.93           C  
ATOM   6181  C   GLU A 990     215.685 217.040 229.497  1.00 39.30           C  
ATOM   6182  O   GLU A 990     215.614 216.671 228.328  1.00 40.39           O  
ATOM   6183  CB  GLU A 990     217.930 216.588 230.514  1.00 40.30           C  
ATOM   6184  CG  GLU A 990     219.352 217.098 230.736  1.00 40.61           C  
ATOM   6185  CD  GLU A 990     220.273 216.059 231.285  1.00 41.31           C  
ATOM   6186  OE1 GLU A 990     219.834 214.956 231.501  1.00 40.58           O  
ATOM   6187  OE2 GLU A 990     221.422 216.368 231.497  1.00 40.86           O  
ATOM   6188  N   VAL A 991     214.667 216.918 230.343  1.00 39.74           N  
ATOM   6189  CA  VAL A 991     213.401 216.344 229.917  1.00 39.58           C  
ATOM   6190  C   VAL A 991     212.697 217.310 228.990  1.00 38.84           C  
ATOM   6191  O   VAL A 991     212.152 216.918 227.956  1.00 39.95           O  
ATOM   6192  CB  VAL A 991     212.495 216.052 231.120  1.00 40.69           C  
ATOM   6193  CG1 VAL A 991     211.121 215.594 230.641  1.00 39.96           C  
ATOM   6194  CG2 VAL A 991     213.148 215.005 231.996  1.00 41.37           C  
ATOM   6195  N   GLN A 992     212.697 218.579 229.374  1.00 39.24           N  
ATOM   6196  CA  GLN A 992     212.026 219.594 228.585  1.00 38.28           C  
ATOM   6197  C   GLN A 992     212.744 219.793 227.256  1.00 39.64           C  
ATOM   6198  O   GLN A 992     212.111 219.995 226.217  1.00 38.60           O  
ATOM   6199  CB  GLN A 992     211.982 220.900 229.367  1.00 40.37           C  
ATOM   6200  CG  GLN A 992     211.210 220.808 230.654  1.00 40.45           C  
ATOM   6201  CD  GLN A 992     209.823 220.353 230.437  1.00 39.42           C  
ATOM   6202  OE1 GLN A 992     209.173 220.799 229.486  1.00 39.09           O  
ATOM   6203  NE2 GLN A 992     209.326 219.470 231.302  1.00 39.74           N  
ATOM   6204  N   ILE A 993     214.064 219.680 227.282  1.00 38.24           N  
ATOM   6205  CA  ILE A 993     214.859 219.807 226.078  1.00 37.04           C  
ATOM   6206  C   ILE A 993     214.614 218.617 225.181  1.00 38.87           C  
ATOM   6207  O   ILE A 993     214.463 218.770 223.973  1.00 37.20           O  
ATOM   6208  CB  ILE A 993     216.345 219.951 226.388  1.00 38.67           C  
ATOM   6209  CG1 ILE A 993     216.566 221.262 227.094  1.00 39.43           C  
ATOM   6210  CG2 ILE A 993     217.134 219.909 225.095  1.00 38.45           C  
ATOM   6211  CD1 ILE A 993     217.915 221.408 227.736  1.00 40.12           C  
ATOM   6212  N   ASP A 994     214.565 217.425 225.758  1.00 39.20           N  
ATOM   6213  CA  ASP A 994     214.330 216.225 224.978  1.00 36.12           C  
ATOM   6214  C   ASP A 994     213.030 216.343 224.192  1.00 36.58           C  
ATOM   6215  O   ASP A 994     212.957 215.923 223.034  1.00 36.56           O  
ATOM   6216  CB  ASP A 994     214.271 215.018 225.908  1.00 37.83           C  
ATOM   6217  CG  ASP A 994     214.206 213.691 225.205  1.00 37.46           C  
ATOM   6218  OD1 ASP A 994     215.173 213.311 224.601  1.00 37.28           O  
ATOM   6219  OD2 ASP A 994     213.182 213.050 225.292  1.00 37.58           O  
ATOM   6220  N   ARG A 995     212.009 216.953 224.791  1.00 36.48           N  
ATOM   6221  CA  ARG A 995     210.752 217.128 224.078  1.00 36.02           C  
ATOM   6222  C   ARG A 995     210.946 218.037 222.866  1.00 35.18           C  
ATOM   6223  O   ARG A 995     210.410 217.760 221.787  1.00 35.24           O  
ATOM   6224  CB  ARG A 995     209.688 217.696 224.998  1.00 36.64           C  
ATOM   6225  CG  ARG A 995     209.238 216.730 226.069  1.00 37.06           C  
ATOM   6226  CD  ARG A 995     208.252 217.316 227.000  1.00 37.65           C  
ATOM   6227  NE  ARG A 995     208.012 216.419 228.116  1.00 38.04           N  
ATOM   6228  CZ  ARG A 995     207.174 216.642 229.150  1.00 37.83           C  
ATOM   6229  NH1 ARG A 995     206.447 217.740 229.225  1.00 37.23           N  
ATOM   6230  NH2 ARG A 995     207.082 215.734 230.108  1.00 36.79           N  
ATOM   6231  N   LEU A 996     211.739 219.099 223.025  1.00 35.74           N  
ATOM   6232  CA  LEU A 996     211.992 219.993 221.903  1.00 34.70           C  
ATOM   6233  C   LEU A 996     212.849 219.328 220.842  1.00 34.84           C  
ATOM   6234  O   LEU A 996     212.622 219.534 219.651  1.00 34.81           O  
ATOM   6235  CB  LEU A 996     212.695 221.282 222.343  1.00 35.34           C  
ATOM   6236  CG  LEU A 996     211.906 222.263 223.216  1.00 36.17           C  
ATOM   6237  CD1 LEU A 996     212.825 223.419 223.586  1.00 37.57           C  
ATOM   6238  CD2 LEU A 996     210.674 222.773 222.477  1.00 35.79           C  
ATOM   6239  N   ILE A 997     213.819 218.518 221.250  1.00 34.69           N  
ATOM   6240  CA  ILE A 997     214.674 217.866 220.273  1.00 33.78           C  
ATOM   6241  C   ILE A 997     213.874 216.925 219.415  1.00 33.80           C  
ATOM   6242  O   ILE A 997     214.047 216.894 218.200  1.00 33.35           O  
ATOM   6243  CB  ILE A 997     215.845 217.097 220.904  1.00 34.39           C  
ATOM   6244  CG1 ILE A 997     216.840 218.079 221.523  1.00 35.10           C  
ATOM   6245  CG2 ILE A 997     216.522 216.212 219.840  1.00 34.29           C  
ATOM   6246  CD1 ILE A 997     217.887 217.425 222.400  1.00 36.12           C  
ATOM   6247  N   THR A 998     213.003 216.137 220.020  1.00 33.85           N  
ATOM   6248  CA  THR A 998     212.231 215.210 219.220  1.00 33.14           C  
ATOM   6249  C   THR A 998     211.387 215.961 218.204  1.00 32.24           C  
ATOM   6250  O   THR A 998     211.344 215.586 217.032  1.00 32.39           O  
ATOM   6251  CB  THR A 998     211.329 214.328 220.092  1.00 34.03           C  
ATOM   6252  OG1 THR A 998     212.140 213.541 220.970  1.00 34.80           O  
ATOM   6253  CG2 THR A 998     210.500 213.402 219.213  1.00 32.88           C  
ATOM   6254  N   GLY A 999     210.722 217.025 218.641  1.00 32.96           N  
ATOM   6255  CA  GLY A 999     209.872 217.796 217.745  1.00 32.38           C  
ATOM   6256  C   GLY A 999     210.649 218.486 216.628  1.00 31.78           C  
ATOM   6257  O   GLY A 999     210.203 218.520 215.479  1.00 32.47           O  
ATOM   6258  N   ARG A1000     211.799 219.059 216.961  1.00 31.97           N  
ATOM   6259  CA  ARG A1000     212.587 219.781 215.980  1.00 31.28           C  
ATOM   6260  C   ARG A1000     213.316 218.846 215.030  1.00 32.35           C  
ATOM   6261  O   ARG A1000     213.471 219.156 213.848  1.00 31.97           O  
ATOM   6262  CB  ARG A1000     213.551 220.710 216.671  1.00 32.29           C  
ATOM   6263  CG  ARG A1000     212.880 221.884 217.323  1.00 32.67           C  
ATOM   6264  CD  ARG A1000     213.826 222.733 218.029  1.00 33.12           C  
ATOM   6265  NE  ARG A1000     213.188 223.913 218.524  1.00 33.78           N  
ATOM   6266  CZ  ARG A1000     213.801 224.876 219.217  1.00 34.47           C  
ATOM   6267  NH1 ARG A1000     215.083 224.774 219.518  1.00 34.84           N  
ATOM   6268  NH2 ARG A1000     213.116 225.944 219.593  1.00 35.72           N  
ATOM   6269  N   LEU A1001     213.739 217.694 215.527  1.00 31.40           N  
ATOM   6270  CA  LEU A1001     214.391 216.711 214.686  1.00 30.72           C  
ATOM   6271  C   LEU A1001     213.363 216.148 213.722  1.00 31.34           C  
ATOM   6272  O   LEU A1001     213.650 215.951 212.541  1.00 30.94           O  
ATOM   6273  CB  LEU A1001     215.013 215.611 215.552  1.00 31.63           C  
ATOM   6274  CG  LEU A1001     215.800 214.494 214.841  1.00 31.57           C  
ATOM   6275  CD1 LEU A1001     216.966 215.085 214.031  1.00 31.73           C  
ATOM   6276  CD2 LEU A1001     216.320 213.525 215.912  1.00 32.95           C  
ATOM   6277  N   GLN A1002     212.150 215.915 214.220  1.00 30.71           N  
ATOM   6278  CA  GLN A1002     211.058 215.438 213.393  1.00 30.11           C  
ATOM   6279  C   GLN A1002     210.720 216.464 212.323  1.00 30.72           C  
ATOM   6280  O   GLN A1002     210.415 216.097 211.186  1.00 30.82           O  
ATOM   6281  CB  GLN A1002     209.834 215.155 214.253  1.00 30.44           C  
ATOM   6282  CG  GLN A1002     208.662 214.569 213.517  1.00 30.03           C  
ATOM   6283  CD  GLN A1002     207.513 214.304 214.454  1.00 30.02           C  
ATOM   6284  OE1 GLN A1002     207.447 214.872 215.549  1.00 30.64           O  
ATOM   6285  NE2 GLN A1002     206.593 213.443 214.043  1.00 29.75           N  
ATOM   6286  N   SER A1003     210.775 217.748 212.683  1.00 30.17           N  
ATOM   6287  CA  SER A1003     210.502 218.820 211.737  1.00 29.61           C  
ATOM   6288  C   SER A1003     211.513 218.826 210.606  1.00 29.67           C  
ATOM   6289  O   SER A1003     211.134 218.941 209.438  1.00 30.38           O  
ATOM   6290  CB  SER A1003     210.494 220.158 212.430  1.00 30.94           C  
ATOM   6291  OG  SER A1003     210.238 221.182 211.520  1.00 31.39           O  
ATOM   6292  N   LEU A1004     212.796 218.668 210.928  1.00 29.96           N  
ATOM   6293  CA  LEU A1004     213.791 218.604 209.871  1.00 29.08           C  
ATOM   6294  C   LEU A1004     213.581 217.396 208.994  1.00 29.30           C  
ATOM   6295  O   LEU A1004     213.654 217.502 207.776  1.00 29.51           O  
ATOM   6296  CB  LEU A1004     215.206 218.521 210.426  1.00 29.94           C  
ATOM   6297  CG  LEU A1004     215.772 219.744 211.056  1.00 30.85           C  
ATOM   6298  CD1 LEU A1004     217.044 219.367 211.756  1.00 31.60           C  
ATOM   6299  CD2 LEU A1004     216.067 220.780 209.991  1.00 31.34           C  
ATOM   6300  N   GLN A1005     213.259 216.252 209.579  1.00 29.35           N  
ATOM   6301  CA  GLN A1005     213.076 215.072 208.754  1.00 29.01           C  
ATOM   6302  C   GLN A1005     211.943 215.283 207.773  1.00 28.44           C  
ATOM   6303  O   GLN A1005     212.047 214.886 206.610  1.00 29.10           O  
ATOM   6304  CB  GLN A1005     212.821 213.845 209.616  1.00 29.79           C  
ATOM   6305  CG  GLN A1005     214.038 213.392 210.377  1.00 30.22           C  
ATOM   6306  CD  GLN A1005     213.735 212.318 211.359  1.00 31.00           C  
ATOM   6307  OE1 GLN A1005     212.572 212.091 211.717  1.00 30.61           O  
ATOM   6308  NE2 GLN A1005     214.772 211.638 211.808  1.00 31.68           N  
ATOM   6309  N   THR A1006     210.879 215.942 208.217  1.00 28.54           N  
ATOM   6310  CA  THR A1006     209.779 216.235 207.317  1.00 28.11           C  
ATOM   6311  C   THR A1006     210.245 217.147 206.196  1.00 27.78           C  
ATOM   6312  O   THR A1006     209.980 216.880 205.026  1.00 28.17           O  
ATOM   6313  CB  THR A1006     208.612 216.899 208.062  1.00 28.98           C  
ATOM   6314  OG1 THR A1006     208.104 216.002 209.052  1.00 29.38           O  
ATOM   6315  CG2 THR A1006     207.499 217.264 207.094  1.00 28.59           C  
ATOM   6316  N   TYR A1007     210.963 218.205 206.548  1.00 28.07           N  
ATOM   6317  CA  TYR A1007     211.471 219.153 205.570  1.00 27.29           C  
ATOM   6318  C   TYR A1007     212.359 218.500 204.539  1.00 29.35           C  
ATOM   6319  O   TYR A1007     212.184 218.714 203.340  1.00 27.13           O  
ATOM   6320  CB  TYR A1007     212.233 220.266 206.266  1.00 28.69           C  
ATOM   6321  CG  TYR A1007     212.982 221.161 205.345  1.00 28.13           C  
ATOM   6322  CD1 TYR A1007     212.341 222.167 204.672  1.00 28.24           C  
ATOM   6323  CD2 TYR A1007     214.337 220.973 205.184  1.00 28.29           C  
ATOM   6324  CE1 TYR A1007     213.056 222.985 203.840  1.00 28.14           C  
ATOM   6325  CE2 TYR A1007     215.046 221.788 204.356  1.00 28.15           C  
ATOM   6326  CZ  TYR A1007     214.414 222.790 203.687  1.00 27.99           C  
ATOM   6327  OH  TYR A1007     215.133 223.608 202.863  1.00 28.37           O  
ATOM   6328  N   VAL A1008     213.322 217.714 204.994  1.00 27.22           N  
ATOM   6329  CA  VAL A1008     214.263 217.100 204.088  1.00 26.62           C  
ATOM   6330  C   VAL A1008     213.549 216.139 203.165  1.00 27.16           C  
ATOM   6331  O   VAL A1008     213.817 216.123 201.967  1.00 27.21           O  
ATOM   6332  CB  VAL A1008     215.385 216.390 204.852  1.00 27.94           C  
ATOM   6333  CG1 VAL A1008     216.253 215.605 203.901  1.00 27.75           C  
ATOM   6334  CG2 VAL A1008     216.214 217.424 205.569  1.00 28.32           C  
ATOM   6335  N   THR A1009     212.628 215.350 203.694  1.00 26.92           N  
ATOM   6336  CA  THR A1009     211.900 214.429 202.844  1.00 26.00           C  
ATOM   6337  C   THR A1009     211.164 215.189 201.755  1.00 26.43           C  
ATOM   6338  O   THR A1009     211.183 214.780 200.592  1.00 27.03           O  
ATOM   6339  CB  THR A1009     210.910 213.580 203.647  1.00 26.89           C  
ATOM   6340  OG1 THR A1009     211.627 212.789 204.596  1.00 27.73           O  
ATOM   6341  CG2 THR A1009     210.133 212.669 202.715  1.00 26.71           C  
ATOM   6342  N   GLN A1010     210.529 216.303 202.108  1.00 26.06           N  
ATOM   6343  CA  GLN A1010     209.815 217.077 201.108  1.00 25.13           C  
ATOM   6344  C   GLN A1010     210.765 217.661 200.077  1.00 26.83           C  
ATOM   6345  O   GLN A1010     210.429 217.723 198.895  1.00 25.63           O  
ATOM   6346  CB  GLN A1010     209.029 218.211 201.755  1.00 26.01           C  
ATOM   6347  CG  GLN A1010     207.908 217.757 202.645  1.00 26.16           C  
ATOM   6348  CD  GLN A1010     206.879 216.978 201.924  1.00 25.32           C  
ATOM   6349  OE1 GLN A1010     206.336 217.418 200.910  1.00 24.91           O  
ATOM   6350  NE2 GLN A1010     206.597 215.793 202.435  1.00 25.23           N  
ATOM   6351  N   GLN A1011     211.959 218.073 200.502  1.00 25.85           N  
ATOM   6352  CA  GLN A1011     212.918 218.632 199.560  1.00 25.36           C  
ATOM   6353  C   GLN A1011     213.411 217.579 198.596  1.00 25.73           C  
ATOM   6354  O   GLN A1011     213.615 217.868 197.421  1.00 26.29           O  
ATOM   6355  CB  GLN A1011     214.124 219.238 200.274  1.00 26.23           C  
ATOM   6356  CG  GLN A1011     213.835 220.490 201.049  1.00 27.07           C  
ATOM   6357  CD  GLN A1011     213.393 221.628 200.182  1.00 27.11           C  
ATOM   6358  OE1 GLN A1011     212.193 221.878 200.046  1.00 26.90           O  
ATOM   6359  NE2 GLN A1011     214.348 222.335 199.590  1.00 27.18           N  
ATOM   6360  N   LEU A1012     213.596 216.357 199.078  1.00 25.43           N  
ATOM   6361  CA  LEU A1012     214.068 215.280 198.220  1.00 25.18           C  
ATOM   6362  C   LEU A1012     213.021 214.877 197.201  1.00 25.27           C  
ATOM   6363  O   LEU A1012     213.341 214.641 196.033  1.00 25.29           O  
ATOM   6364  CB  LEU A1012     214.469 214.072 199.059  1.00 25.63           C  
ATOM   6365  CG  LEU A1012     215.944 213.969 199.446  1.00 25.71           C  
ATOM   6366  CD1 LEU A1012     216.400 215.227 200.159  1.00 26.58           C  
ATOM   6367  CD2 LEU A1012     216.117 212.772 200.342  1.00 26.23           C  
ATOM   6368  N   ILE A1013     211.765 214.828 197.614  1.00 25.08           N  
ATOM   6369  CA  ILE A1013     210.720 214.478 196.675  1.00 24.73           C  
ATOM   6370  C   ILE A1013     210.561 215.593 195.656  1.00 24.96           C  
ATOM   6371  O   ILE A1013     210.462 215.334 194.456  1.00 25.21           O  
ATOM   6372  CB  ILE A1013     209.394 214.191 197.387  1.00 25.16           C  
ATOM   6373  CG1 ILE A1013     209.552 212.917 198.235  1.00 25.70           C  
ATOM   6374  CG2 ILE A1013     208.271 214.032 196.356  1.00 25.98           C  
ATOM   6375  CD1 ILE A1013     208.426 212.667 199.208  1.00 25.74           C  
ATOM   6376  N   ARG A1014     210.534 216.836 196.124  1.00 25.23           N  
ATOM   6377  CA  ARG A1014     210.411 217.964 195.221  1.00 24.42           C  
ATOM   6378  C   ARG A1014     211.593 218.011 194.267  1.00 25.03           C  
ATOM   6379  O   ARG A1014     211.429 218.311 193.086  1.00 25.48           O  
ATOM   6380  CB  ARG A1014     210.298 219.270 195.983  1.00 25.37           C  
ATOM   6381  CG  ARG A1014     209.972 220.477 195.113  1.00 25.44           C  
ATOM   6382  CD  ARG A1014     209.797 221.734 195.900  1.00 26.05           C  
ATOM   6383  NE  ARG A1014     208.640 221.691 196.800  1.00 26.24           N  
ATOM   6384  CZ  ARG A1014     208.694 221.608 198.152  1.00 26.33           C  
ATOM   6385  NH1 ARG A1014     209.853 221.548 198.774  1.00 26.50           N  
ATOM   6386  NH2 ARG A1014     207.572 221.590 198.852  1.00 26.18           N  
ATOM   6387  N   ALA A1015     212.786 217.710 194.765  1.00 24.58           N  
ATOM   6388  CA  ALA A1015     213.970 217.713 193.927  1.00 23.97           C  
ATOM   6389  C   ALA A1015     213.854 216.695 192.817  1.00 24.31           C  
ATOM   6390  O   ALA A1015     214.339 216.937 191.716  1.00 24.98           O  
ATOM   6391  CB  ALA A1015     215.205 217.435 194.745  1.00 24.84           C  
ATOM   6392  N   ALA A1016     213.225 215.556 193.086  1.00 24.51           N  
ATOM   6393  CA  ALA A1016     213.057 214.548 192.054  1.00 23.84           C  
ATOM   6394  C   ALA A1016     212.198 215.095 190.923  1.00 23.36           C  
ATOM   6395  O   ALA A1016     212.405 214.763 189.753  1.00 24.44           O  
ATOM   6396  CB  ALA A1016     212.437 213.294 192.633  1.00 24.88           C  
ATOM   6397  N   GLU A1017     211.216 215.922 191.271  1.00 23.78           N  
ATOM   6398  CA  GLU A1017     210.355 216.534 190.269  1.00 23.07           C  
ATOM   6399  C   GLU A1017     211.135 217.514 189.411  1.00 24.04           C  
ATOM   6400  O   GLU A1017     211.018 217.516 188.182  1.00 24.19           O  
ATOM   6401  CB  GLU A1017     209.186 217.258 190.924  1.00 24.02           C  
ATOM   6402  CG  GLU A1017     208.232 217.911 189.951  1.00 23.97           C  
ATOM   6403  CD  GLU A1017     207.114 218.617 190.637  1.00 24.54           C  
ATOM   6404  OE1 GLU A1017     207.032 218.529 191.837  1.00 24.58           O  
ATOM   6405  OE2 GLU A1017     206.343 219.260 189.966  1.00 24.12           O  
ATOM   6406  N   ILE A1018     211.949 218.336 190.058  1.00 23.54           N  
ATOM   6407  CA  ILE A1018     212.744 219.314 189.338  1.00 22.93           C  
ATOM   6408  C   ILE A1018     213.773 218.621 188.479  1.00 23.96           C  
ATOM   6409  O   ILE A1018     214.031 219.054 187.360  1.00 23.47           O  
ATOM   6410  CB  ILE A1018     213.418 220.310 190.281  1.00 23.89           C  
ATOM   6411  CG1 ILE A1018     212.341 221.112 191.049  1.00 24.47           C  
ATOM   6412  CG2 ILE A1018     214.360 221.237 189.500  1.00 24.12           C  
ATOM   6413  CD1 ILE A1018     211.371 221.909 190.203  1.00 25.73           C  
ATOM   6414  N   ARG A1019     214.379 217.566 188.998  1.00 23.40           N  
ATOM   6415  CA  ARG A1019     215.341 216.799 188.234  1.00 22.70           C  
ATOM   6416  C   ARG A1019     214.700 216.252 186.978  1.00 23.09           C  
ATOM   6417  O   ARG A1019     215.289 216.322 185.903  1.00 23.09           O  
ATOM   6418  CB  ARG A1019     215.890 215.661 189.056  1.00 23.48           C  
ATOM   6419  CG  ARG A1019     216.893 214.781 188.354  1.00 23.19           C  
ATOM   6420  CD  ARG A1019     217.341 213.716 189.257  1.00 23.51           C  
ATOM   6421  NE  ARG A1019     216.250 212.825 189.619  1.00 23.87           N  
ATOM   6422  CZ  ARG A1019     216.156 212.143 190.782  1.00 24.56           C  
ATOM   6423  NH1 ARG A1019     217.094 212.251 191.707  1.00 24.33           N  
ATOM   6424  NH2 ARG A1019     215.107 211.362 190.993  1.00 25.09           N  
ATOM   6425  N   ALA A1020     213.485 215.723 187.095  1.00 22.52           N  
ATOM   6426  CA  ALA A1020     212.793 215.215 185.925  1.00 22.10           C  
ATOM   6427  C   ALA A1020     212.574 216.324 184.907  1.00 22.07           C  
ATOM   6428  O   ALA A1020     212.726 216.104 183.703  1.00 22.29           O  
ATOM   6429  CB  ALA A1020     211.465 214.609 186.322  1.00 23.08           C  
ATOM   6430  N   SER A1021     212.253 217.526 185.386  1.00 22.74           N  
ATOM   6431  CA  SER A1021     212.059 218.660 184.492  1.00 22.01           C  
ATOM   6432  C   SER A1021     213.374 219.070 183.856  1.00 21.52           C  
ATOM   6433  O   SER A1021     213.410 219.418 182.679  1.00 22.64           O  
ATOM   6434  CB  SER A1021     211.451 219.832 185.228  1.00 22.71           C  
ATOM   6435  OG  SER A1021     210.150 219.533 185.641  1.00 23.96           O  
ATOM   6436  N   ALA A1022     214.460 219.013 184.618  1.00 21.94           N  
ATOM   6437  CA  ALA A1022     215.771 219.339 184.086  1.00 21.44           C  
ATOM   6438  C   ALA A1022     216.171 218.345 183.013  1.00 21.19           C  
ATOM   6439  O   ALA A1022     216.750 218.727 182.001  1.00 22.32           O  
ATOM   6440  CB  ALA A1022     216.809 219.347 185.183  1.00 23.19           C  
ATOM   6441  N   ASN A1023     215.836 217.073 183.212  1.00 21.68           N  
ATOM   6442  CA  ASN A1023     216.164 216.056 182.228  1.00 20.93           C  
ATOM   6443  C   ASN A1023     215.370 216.288 180.963  1.00 21.06           C  
ATOM   6444  O   ASN A1023     215.896 216.154 179.858  1.00 21.17           O  
ATOM   6445  CB  ASN A1023     215.892 214.673 182.767  1.00 21.09           C  
ATOM   6446  CG  ASN A1023     216.879 214.253 183.786  1.00 21.25           C  
ATOM   6447  OD1 ASN A1023     217.967 214.820 183.893  1.00 21.25           O  
ATOM   6448  ND2 ASN A1023     216.532 213.253 184.545  1.00 21.29           N  
ATOM   6449  N   LEU A1024     214.116 216.691 181.120  1.00 21.27           N  
ATOM   6450  CA  LEU A1024     213.285 217.008 179.979  1.00 20.45           C  
ATOM   6451  C   LEU A1024     213.818 218.221 179.256  1.00 21.20           C  
ATOM   6452  O   LEU A1024     213.847 218.248 178.028  1.00 20.63           O  
ATOM   6453  CB  LEU A1024     211.850 217.275 180.411  1.00 20.69           C  
ATOM   6454  CG  LEU A1024     210.885 217.690 179.305  1.00 20.38           C  
ATOM   6455  CD1 LEU A1024     210.794 216.604 178.240  1.00 20.72           C  
ATOM   6456  CD2 LEU A1024     209.532 217.961 179.921  1.00 21.17           C  
ATOM   6457  N   ALA A1025     214.221 219.236 180.007  1.00 21.07           N  
ATOM   6458  CA  ALA A1025     214.750 220.442 179.411  1.00 20.59           C  
ATOM   6459  C   ALA A1025     216.017 220.142 178.645  1.00 20.66           C  
ATOM   6460  O   ALA A1025     216.213 220.651 177.545  1.00 21.47           O  
ATOM   6461  CB  ALA A1025     215.025 221.475 180.480  1.00 21.80           C  
ATOM   6462  N   ALA A1026     216.871 219.290 179.202  1.00 20.61           N  
ATOM   6463  CA  ALA A1026     218.100 218.927 178.525  1.00 20.47           C  
ATOM   6464  C   ALA A1026     217.785 218.162 177.262  1.00 20.20           C  
ATOM   6465  O   ALA A1026     218.441 218.352 176.235  1.00 21.01           O  
ATOM   6466  CB  ALA A1026     218.991 218.102 179.430  1.00 21.95           C  
ATOM   6467  N   THR A1027     216.766 217.307 177.327  1.00 20.57           N  
ATOM   6468  CA  THR A1027     216.365 216.528 176.172  1.00 19.80           C  
ATOM   6469  C   THR A1027     215.848 217.446 175.089  1.00 21.14           C  
ATOM   6470  O   THR A1027     216.221 217.302 173.928  1.00 19.38           O  
ATOM   6471  CB  THR A1027     215.284 215.494 176.522  1.00 20.03           C  
ATOM   6472  OG1 THR A1027     215.783 214.587 177.505  1.00 20.82           O  
ATOM   6473  CG2 THR A1027     214.902 214.708 175.283  1.00 19.60           C  
ATOM   6474  N   LYS A1028     215.008 218.408 175.457  1.00 19.59           N  
ATOM   6475  CA  LYS A1028     214.489 219.315 174.457  1.00 19.08           C  
ATOM   6476  C   LYS A1028     215.594 220.148 173.871  1.00 20.78           C  
ATOM   6477  O   LYS A1028     215.647 220.348 172.667  1.00 20.03           O  
ATOM   6478  CB  LYS A1028     213.418 220.248 175.010  1.00 19.77           C  
ATOM   6479  CG  LYS A1028     212.103 219.597 175.326  1.00 19.39           C  
ATOM   6480  CD  LYS A1028     211.072 220.637 175.658  1.00 19.95           C  
ATOM   6481  CE  LYS A1028     209.818 220.029 176.246  1.00 20.22           C  
ATOM   6482  NZ  LYS A1028     209.146 219.093 175.325  1.00 20.07           N  
ATOM   6483  N   MET A1029     216.524 220.610 174.669  1.00 20.13           N  
ATOM   6484  CA  MET A1029     217.536 221.424 174.046  1.00 20.02           C  
ATOM   6485  C   MET A1029     218.329 220.587 173.049  1.00 21.83           C  
ATOM   6486  O   MET A1029     218.552 221.011 171.914  1.00 19.63           O  
ATOM   6487  CB  MET A1029     218.413 222.056 175.095  1.00 20.49           C  
ATOM   6488  CG  MET A1029     219.249 223.168 174.584  1.00 20.73           C  
ATOM   6489  SD  MET A1029     220.103 224.007 175.870  1.00 22.59           S  
ATOM   6490  CE  MET A1029     218.810 224.810 176.813  1.00 23.11           C  
ATOM   6491  N   SER A1030     218.675 219.362 173.423  1.00 19.59           N  
ATOM   6492  CA  SER A1030     219.451 218.513 172.537  1.00 19.11           C  
ATOM   6493  C   SER A1030     218.711 218.162 171.253  1.00 19.25           C  
ATOM   6494  O   SER A1030     219.293 218.175 170.173  1.00 20.46           O  
ATOM   6495  CB  SER A1030     219.808 217.228 173.247  1.00 19.83           C  
ATOM   6496  OG  SER A1030     220.712 217.447 174.288  1.00 20.37           O  
ATOM   6497  N   GLU A1031     217.427 217.858 171.360  1.00 19.17           N  
ATOM   6498  CA  GLU A1031     216.652 217.421 170.197  1.00 18.95           C  
ATOM   6499  C   GLU A1031     215.887 218.516 169.446  1.00 18.97           C  
ATOM   6500  O   GLU A1031     215.621 218.370 168.251  1.00 19.34           O  
ATOM   6501  CB  GLU A1031     215.651 216.364 170.645  1.00 19.07           C  
ATOM   6502  CG  GLU A1031     216.287 215.120 171.196  1.00 18.94           C  
ATOM   6503  CD  GLU A1031     215.292 214.103 171.597  1.00 19.00           C  
ATOM   6504  OE1 GLU A1031     214.224 214.092 171.051  1.00 19.20           O  
ATOM   6505  OE2 GLU A1031     215.594 213.318 172.448  1.00 19.07           O  
ATOM   6506  N   CYS A1032     215.503 219.578 170.138  1.00 19.47           N  
ATOM   6507  CA  CYS A1032     214.659 220.663 169.651  1.00 19.61           C  
ATOM   6508  C   CYS A1032     215.514 221.856 169.149  1.00 20.02           C  
ATOM   6509  O   CYS A1032     215.202 222.449 168.121  1.00 20.61           O  
ATOM   6510  CB  CYS A1032     213.693 221.116 170.744  1.00 20.27           C  
ATOM   6511  SG  CYS A1032     212.290 222.035 170.168  1.00 22.08           S  
ATOM   6512  N   VAL A1033     216.572 222.224 169.913  1.00 19.60           N  
ATOM   6513  CA  VAL A1033     217.448 223.358 169.559  1.00 19.76           C  
ATOM   6514  C   VAL A1033     218.604 222.932 168.668  1.00 19.92           C  
ATOM   6515  O   VAL A1033     218.851 223.541 167.629  1.00 20.38           O  
ATOM   6516  CB  VAL A1033     218.023 224.031 170.814  1.00 20.04           C  
ATOM   6517  CG1 VAL A1033     219.021 225.095 170.418  1.00 20.70           C  
ATOM   6518  CG2 VAL A1033     216.904 224.659 171.610  1.00 21.32           C  
ATOM   6519  N   LEU A1034     219.312 221.884 169.069  1.00 20.11           N  
ATOM   6520  CA  LEU A1034     220.472 221.427 168.311  1.00 19.77           C  
ATOM   6521  C   LEU A1034     220.086 220.639 167.068  1.00 19.62           C  
ATOM   6522  O   LEU A1034     220.878 220.530 166.140  1.00 19.95           O  
ATOM   6523  CB  LEU A1034     221.378 220.545 169.176  1.00 19.74           C  
ATOM   6524  CG  LEU A1034     222.475 221.236 169.990  1.00 20.36           C  
ATOM   6525  CD1 LEU A1034     221.866 222.207 170.981  1.00 20.61           C  
ATOM   6526  CD2 LEU A1034     223.281 220.184 170.726  1.00 20.36           C  
ATOM   6527  N   GLY A1035     218.890 220.074 167.059  1.00 19.55           N  
ATOM   6528  CA  GLY A1035     218.420 219.260 165.946  1.00 19.09           C  
ATOM   6529  C   GLY A1035     217.109 219.774 165.380  1.00 18.93           C  
ATOM   6530  O   GLY A1035     216.815 220.968 165.440  1.00 19.36           O  
ATOM   6531  N   GLN A1036     216.333 218.856 164.809  1.00 18.63           N  
ATOM   6532  CA  GLN A1036     215.004 219.145 164.291  1.00 18.52           C  
ATOM   6533  C   GLN A1036     214.069 218.001 164.635  1.00 18.61           C  
ATOM   6534  O   GLN A1036     213.998 217.006 163.915  1.00 18.77           O  
ATOM   6535  CB  GLN A1036     214.995 219.349 162.782  1.00 18.83           C  
ATOM   6536  CG  GLN A1036     213.622 219.744 162.271  1.00 18.66           C  
ATOM   6537  CD  GLN A1036     213.585 220.080 160.821  1.00 18.98           C  
ATOM   6538  OE1 GLN A1036     214.511 219.781 160.061  1.00 19.23           O  
ATOM   6539  NE2 GLN A1036     212.498 220.717 160.423  1.00 19.03           N  
ATOM   6540  N   SER A1037     213.364 218.133 165.739  1.00 18.65           N  
ATOM   6541  CA  SER A1037     212.491 217.079 166.215  1.00 18.15           C  
ATOM   6542  C   SER A1037     211.325 216.788 165.297  1.00 18.25           C  
ATOM   6543  O   SER A1037     210.635 217.699 164.847  1.00 18.44           O  
ATOM   6544  CB  SER A1037     211.944 217.450 167.568  1.00 18.69           C  
ATOM   6545  OG  SER A1037     210.926 216.573 167.932  1.00 18.60           O  
ATOM   6546  N   LYS A1038     211.065 215.500 165.085  1.00 18.06           N  
ATOM   6547  CA  LYS A1038     209.909 215.050 164.323  1.00 17.85           C  
ATOM   6548  C   LYS A1038     208.839 214.520 165.256  1.00 18.00           C  
ATOM   6549  O   LYS A1038     207.834 213.957 164.825  1.00 18.46           O  
ATOM   6550  CB  LYS A1038     210.296 213.986 163.311  1.00 17.37           C  
ATOM   6551  CG  LYS A1038     211.210 214.489 162.223  1.00 17.52           C  
ATOM   6552  CD  LYS A1038     211.478 213.418 161.176  1.00 16.99           C  
ATOM   6553  CE  LYS A1038     212.429 213.927 160.099  1.00 16.76           C  
ATOM   6554  NZ  LYS A1038     211.855 215.086 159.354  1.00 17.12           N  
ATOM   6555  N   ARG A1039     209.077 214.692 166.543  1.00 18.00           N  
ATOM   6556  CA  ARG A1039     208.151 214.261 167.566  1.00 17.86           C  
ATOM   6557  C   ARG A1039     207.027 215.279 167.666  1.00 18.11           C  
ATOM   6558  O   ARG A1039     207.270 216.471 167.876  1.00 18.87           O  
ATOM   6559  CB  ARG A1039     208.886 214.131 168.886  1.00 18.51           C  
ATOM   6560  CG  ARG A1039     209.951 213.043 168.905  1.00 18.36           C  
ATOM   6561  CD  ARG A1039     210.849 213.151 170.086  1.00 18.55           C  
ATOM   6562  NE  ARG A1039     210.152 212.868 171.308  1.00 18.67           N  
ATOM   6563  CZ  ARG A1039     210.682 212.871 172.529  1.00 18.78           C  
ATOM   6564  NH1 ARG A1039     211.950 213.141 172.727  1.00 19.06           N  
ATOM   6565  NH2 ARG A1039     209.888 212.600 173.536  1.00 18.76           N  
ATOM   6566  N   VAL A1040     205.805 214.816 167.483  1.00 18.19           N  
ATOM   6567  CA  VAL A1040     204.659 215.707 167.447  1.00 18.21           C  
ATOM   6568  C   VAL A1040     204.348 216.310 168.797  1.00 18.67           C  
ATOM   6569  O   VAL A1040     204.326 215.626 169.816  1.00 19.23           O  
ATOM   6570  CB  VAL A1040     203.440 214.969 166.882  1.00 18.71           C  
ATOM   6571  CG1 VAL A1040     202.190 215.832 166.976  1.00 19.04           C  
ATOM   6572  CG2 VAL A1040     203.717 214.620 165.442  1.00 19.10           C  
ATOM   6573  N   ASP A1041     204.177 217.627 168.787  1.00 18.78           N  
ATOM   6574  CA  ASP A1041     203.880 218.452 169.948  1.00 18.91           C  
ATOM   6575  C   ASP A1041     204.969 218.403 171.008  1.00 19.15           C  
ATOM   6576  O   ASP A1041     204.781 218.880 172.127  1.00 19.36           O  
ATOM   6577  CB  ASP A1041     202.518 218.110 170.539  1.00 19.21           C  
ATOM   6578  CG  ASP A1041     201.386 218.432 169.572  1.00 19.52           C  
ATOM   6579  OD1 ASP A1041     201.632 219.111 168.608  1.00 19.39           O  
ATOM   6580  OD2 ASP A1041     200.291 218.014 169.808  1.00 19.74           O  
ATOM   6581  N   PHE A1042     206.134 217.895 170.635  1.00 19.00           N  
ATOM   6582  CA  PHE A1042     207.298 217.922 171.508  1.00 18.73           C  
ATOM   6583  C   PHE A1042     207.850 219.348 171.629  1.00 19.39           C  
ATOM   6584  O   PHE A1042     208.265 219.774 172.709  1.00 20.21           O  
ATOM   6585  CB  PHE A1042     208.353 216.954 171.001  1.00 18.94           C  
ATOM   6586  CG  PHE A1042     209.566 216.825 171.846  1.00 18.76           C  
ATOM   6587  CD1 PHE A1042     209.507 216.226 173.087  1.00 18.91           C  
ATOM   6588  CD2 PHE A1042     210.781 217.278 171.392  1.00 19.15           C  
ATOM   6589  CE1 PHE A1042     210.639 216.090 173.854  1.00 18.98           C  
ATOM   6590  CE2 PHE A1042     211.912 217.141 172.152  1.00 19.48           C  
ATOM   6591  CZ  PHE A1042     211.838 216.545 173.384  1.00 19.02           C  
ATOM   6592  N   CYS A1043     207.865 220.076 170.501  1.00 19.64           N  
ATOM   6593  CA  CYS A1043     208.352 221.449 170.387  1.00 20.04           C  
ATOM   6594  C   CYS A1043     207.195 222.404 170.015  1.00 20.20           C  
ATOM   6595  O   CYS A1043     207.323 223.238 169.113  1.00 20.51           O  
ATOM   6596  CB  CYS A1043     209.478 221.523 169.344  1.00 20.49           C  
ATOM   6597  SG  CYS A1043     210.954 220.571 169.755  1.00 20.66           S  
ATOM   6598  N   GLY A1044     206.044 222.252 170.692  1.00 20.04           N  
ATOM   6599  CA  GLY A1044     204.854 223.076 170.476  1.00 19.89           C  
ATOM   6600  C   GLY A1044     203.994 222.549 169.336  1.00 19.39           C  
ATOM   6601  O   GLY A1044     204.361 221.585 168.663  1.00 19.62           O  
ATOM   6602  N   LYS A1045     202.861 223.200 169.113  1.00 19.23           N  
ATOM   6603  CA  LYS A1045     201.934 222.832 168.052  1.00 19.21           C  
ATOM   6604  C   LYS A1045     202.506 223.205 166.698  1.00 19.62           C  
ATOM   6605  O   LYS A1045     203.142 224.248 166.565  1.00 19.86           O  
ATOM   6606  CB  LYS A1045     200.595 223.544 168.253  1.00 19.20           C  
ATOM   6607  N   GLY A1046     202.261 222.376 165.692  1.00 19.69           N  
ATOM   6608  CA  GLY A1046     202.717 222.656 164.338  1.00 19.30           C  
ATOM   6609  C   GLY A1046     203.926 221.813 163.989  1.00 19.28           C  
ATOM   6610  O   GLY A1046     204.374 220.991 164.787  1.00 19.44           O  
ATOM   6611  N   TYR A1047     204.443 221.989 162.788  1.00 19.32           N  
ATOM   6612  CA  TYR A1047     205.585 221.203 162.362  1.00 18.81           C  
ATOM   6613  C   TYR A1047     206.841 221.933 162.796  1.00 19.03           C  
ATOM   6614  O   TYR A1047     206.985 223.133 162.576  1.00 20.19           O  
ATOM   6615  CB  TYR A1047     205.542 220.987 160.862  1.00 18.89           C  
ATOM   6616  CG  TYR A1047     204.363 220.187 160.427  1.00 18.69           C  
ATOM   6617  CD1 TYR A1047     203.219 220.831 160.023  1.00 18.88           C  
ATOM   6618  CD2 TYR A1047     204.411 218.821 160.440  1.00 18.71           C  
ATOM   6619  CE1 TYR A1047     202.127 220.115 159.630  1.00 18.83           C  
ATOM   6620  CE2 TYR A1047     203.312 218.096 160.048  1.00 18.73           C  
ATOM   6621  CZ  TYR A1047     202.174 218.742 159.645  1.00 18.78           C  
ATOM   6622  OH  TYR A1047     201.076 218.021 159.259  1.00 19.57           O  
ATOM   6623  N   HIS A1048     207.750 221.237 163.448  1.00 19.16           N  
ATOM   6624  CA  HIS A1048     208.905 221.917 164.007  1.00 19.02           C  
ATOM   6625  C   HIS A1048     209.935 222.324 162.984  1.00 19.15           C  
ATOM   6626  O   HIS A1048     210.404 221.481 162.224  1.00 19.14           O  
ATOM   6627  CB  HIS A1048     209.569 221.028 165.041  1.00 19.18           C  
ATOM   6628  CG  HIS A1048     210.624 221.701 165.759  1.00 19.33           C  
ATOM   6629  ND1 HIS A1048     210.396 222.810 166.489  1.00 19.80           N  
ATOM   6630  CD2 HIS A1048     211.928 221.421 165.896  1.00 19.32           C  
ATOM   6631  CE1 HIS A1048     211.502 223.196 167.050  1.00 20.27           C  
ATOM   6632  NE2 HIS A1048     212.460 222.366 166.713  1.00 19.77           N  
ATOM   6633  N   LEU A1049     210.332 223.603 163.016  1.00 19.37           N  
ATOM   6634  CA  LEU A1049     211.395 224.106 162.152  1.00 19.08           C  
ATOM   6635  C   LEU A1049     212.658 224.390 162.950  1.00 19.41           C  
ATOM   6636  O   LEU A1049     213.756 224.059 162.522  1.00 19.73           O  
ATOM   6637  CB  LEU A1049     210.961 225.401 161.455  1.00 19.19           C  
ATOM   6638  CG  LEU A1049     209.782 225.307 160.488  1.00 19.15           C  
ATOM   6639  CD1 LEU A1049     209.424 226.693 160.032  1.00 20.04           C  
ATOM   6640  CD2 LEU A1049     210.159 224.449 159.279  1.00 19.43           C  
ATOM   6641  N   MET A1050     212.519 225.027 164.100  1.00 19.65           N  
ATOM   6642  CA  MET A1050     213.690 225.375 164.903  1.00 19.69           C  
ATOM   6643  C   MET A1050     213.276 225.913 166.251  1.00 20.36           C  
ATOM   6644  O   MET A1050     212.113 226.242 166.452  1.00 21.21           O  
ATOM   6645  CB  MET A1050     214.568 226.395 164.176  1.00 19.96           C  
ATOM   6646  CG  MET A1050     213.890 227.709 163.889  1.00 20.47           C  
ATOM   6647  SD  MET A1050     214.930 228.840 162.974  1.00 21.90           S  
ATOM   6648  CE  MET A1050     213.780 230.197 162.683  1.00 22.77           C  
ATOM   6649  N   SER A1051     214.217 226.032 167.169  1.00 20.54           N  
ATOM   6650  CA  SER A1051     213.913 226.672 168.437  1.00 20.50           C  
ATOM   6651  C   SER A1051     215.108 227.407 168.968  1.00 21.06           C  
ATOM   6652  O   SER A1051     216.244 227.125 168.587  1.00 21.72           O  
ATOM   6653  CB  SER A1051     213.449 225.669 169.466  1.00 20.91           C  
ATOM   6654  OG  SER A1051     214.442 224.751 169.748  1.00 21.19           O  
ATOM   6655  N   PHE A1052     214.844 228.342 169.862  1.00 21.66           N  
ATOM   6656  CA  PHE A1052     215.898 229.117 170.467  1.00 21.88           C  
ATOM   6657  C   PHE A1052     215.743 229.105 171.982  1.00 22.65           C  
ATOM   6658  O   PHE A1052     214.649 229.354 172.482  1.00 23.53           O  
ATOM   6659  CB  PHE A1052     215.810 230.555 169.986  1.00 22.26           C  
ATOM   6660  CG  PHE A1052     215.805 230.694 168.507  1.00 21.79           C  
ATOM   6661  CD1 PHE A1052     214.668 231.114 167.861  1.00 21.82           C  
ATOM   6662  CD2 PHE A1052     216.908 230.388 167.756  1.00 21.81           C  
ATOM   6663  CE1 PHE A1052     214.650 231.241 166.502  1.00 21.93           C  
ATOM   6664  CE2 PHE A1052     216.893 230.514 166.397  1.00 21.95           C  
ATOM   6665  CZ  PHE A1052     215.765 230.943 165.772  1.00 22.04           C  
ATOM   6666  N   PRO A1053     216.788 228.783 172.736  1.00 22.54           N  
ATOM   6667  CA  PRO A1053     216.809 228.799 174.174  1.00 22.85           C  
ATOM   6668  C   PRO A1053     216.934 230.227 174.661  1.00 23.98           C  
ATOM   6669  O   PRO A1053     217.583 231.043 174.005  1.00 24.28           O  
ATOM   6670  CB  PRO A1053     218.051 227.977 174.482  1.00 22.92           C  
ATOM   6671  CG  PRO A1053     218.965 228.243 173.314  1.00 22.68           C  
ATOM   6672  CD  PRO A1053     218.047 228.407 172.121  1.00 22.28           C  
ATOM   6673  N   GLN A1054     216.393 230.494 175.837  1.00 24.41           N  
ATOM   6674  CA  GLN A1054     216.569 231.753 176.544  1.00 25.20           C  
ATOM   6675  C   GLN A1054     216.814 231.437 178.014  1.00 25.58           C  
ATOM   6676  O   GLN A1054     216.238 230.491 178.557  1.00 25.61           O  
ATOM   6677  CB  GLN A1054     215.320 232.626 176.389  1.00 25.49           C  
ATOM   6678  CG  GLN A1054     214.985 233.047 174.959  1.00 25.09           C  
ATOM   6679  CD  GLN A1054     215.826 234.194 174.452  1.00 26.76           C  
ATOM   6680  OE1 GLN A1054     215.396 235.338 174.573  1.00 28.00           O  
ATOM   6681  NE2 GLN A1054     216.995 233.913 173.895  1.00 26.89           N  
ATOM   6682  N   SER A1055     217.654 232.214 178.679  1.00 26.12           N  
ATOM   6683  CA  SER A1055     217.854 231.992 180.102  1.00 25.73           C  
ATOM   6684  C   SER A1055     216.691 232.552 180.901  1.00 26.38           C  
ATOM   6685  O   SER A1055     215.961 233.423 180.431  1.00 27.35           O  
ATOM   6686  CB  SER A1055     219.147 232.623 180.558  1.00 26.80           C  
ATOM   6687  OG  SER A1055     219.089 234.008 180.455  1.00 27.77           O  
ATOM   6688  N   ALA A1056     216.534 232.064 182.120  1.00 26.30           N  
ATOM   6689  CA  ALA A1056     215.493 232.535 183.014  1.00 26.07           C  
ATOM   6690  C   ALA A1056     215.886 232.169 184.440  1.00 26.71           C  
ATOM   6691  O   ALA A1056     216.711 231.273 184.630  1.00 26.58           O  
ATOM   6692  CB  ALA A1056     214.158 231.918 182.638  1.00 25.99           C  
ATOM   6693  N   PRO A1057     215.366 232.840 185.463  1.00 26.37           N  
ATOM   6694  CA  PRO A1057     215.592 232.489 186.839  1.00 26.24           C  
ATOM   6695  C   PRO A1057     215.198 231.053 187.087  1.00 25.72           C  
ATOM   6696  O   PRO A1057     214.073 230.658 186.798  1.00 26.51           O  
ATOM   6697  CB  PRO A1057     214.660 233.447 187.573  1.00 26.77           C  
ATOM   6698  CG  PRO A1057     214.555 234.617 186.655  1.00 27.83           C  
ATOM   6699  CD  PRO A1057     214.548 234.025 185.266  1.00 27.33           C  
ATOM   6700  N   HIS A1058     216.119 230.286 187.635  1.00 25.52           N  
ATOM   6701  CA  HIS A1058     215.884 228.902 188.009  1.00 25.26           C  
ATOM   6702  C   HIS A1058     215.383 228.006 186.879  1.00 24.96           C  
ATOM   6703  O   HIS A1058     214.816 226.942 187.155  1.00 25.66           O  
ATOM   6704  CB  HIS A1058     214.877 228.847 189.157  1.00 25.62           C  
ATOM   6705  CG  HIS A1058     215.285 229.653 190.333  1.00 25.86           C  
ATOM   6706  ND1 HIS A1058     216.363 229.325 191.121  1.00 25.76           N  
ATOM   6707  CD2 HIS A1058     214.762 230.779 190.859  1.00 26.18           C  
ATOM   6708  CE1 HIS A1058     216.487 230.213 192.083  1.00 26.11           C  
ATOM   6709  NE2 HIS A1058     215.527 231.107 191.949  1.00 26.26           N  
ATOM   6710  N   GLY A1059     215.602 228.381 185.620  1.00 25.03           N  
ATOM   6711  CA  GLY A1059     215.089 227.533 184.551  1.00 24.79           C  
ATOM   6712  C   GLY A1059     215.401 228.007 183.148  1.00 24.41           C  
ATOM   6713  O   GLY A1059     216.213 228.905 182.937  1.00 25.13           O  
ATOM   6714  N   VAL A1060     214.779 227.353 182.175  1.00 24.60           N  
ATOM   6715  CA  VAL A1060     215.013 227.657 180.773  1.00 24.38           C  
ATOM   6716  C   VAL A1060     213.710 227.905 180.050  1.00 24.07           C  
ATOM   6717  O   VAL A1060     212.703 227.238 180.298  1.00 24.46           O  
ATOM   6718  CB  VAL A1060     215.772 226.505 180.084  1.00 24.20           C  
ATOM   6719  CG1 VAL A1060     214.944 225.252 180.072  1.00 23.99           C  
ATOM   6720  CG2 VAL A1060     216.152 226.895 178.660  1.00 24.03           C  
ATOM   6721  N   VAL A1061     213.737 228.856 179.141  1.00 24.42           N  
ATOM   6722  CA  VAL A1061     212.585 229.160 178.326  1.00 23.73           C  
ATOM   6723  C   VAL A1061     212.907 228.934 176.867  1.00 24.27           C  
ATOM   6724  O   VAL A1061     213.926 229.399 176.365  1.00 24.75           O  
ATOM   6725  CB  VAL A1061     212.138 230.602 178.578  1.00 25.09           C  
ATOM   6726  CG1 VAL A1061     211.006 230.968 177.675  1.00 24.80           C  
ATOM   6727  CG2 VAL A1061     211.711 230.717 180.022  1.00 25.77           C  
ATOM   6728  N   PHE A1062     212.061 228.183 176.187  1.00 23.48           N  
ATOM   6729  CA  PHE A1062     212.302 227.920 174.785  1.00 22.59           C  
ATOM   6730  C   PHE A1062     211.306 228.640 173.914  1.00 23.45           C  
ATOM   6731  O   PHE A1062     210.105 228.641 174.189  1.00 23.67           O  
ATOM   6732  CB  PHE A1062     212.186 226.435 174.478  1.00 22.64           C  
ATOM   6733  CG  PHE A1062     213.198 225.563 175.108  1.00 22.98           C  
ATOM   6734  CD1 PHE A1062     212.915 224.903 176.280  1.00 22.97           C  
ATOM   6735  CD2 PHE A1062     214.428 225.379 174.528  1.00 22.83           C  
ATOM   6736  CE1 PHE A1062     213.838 224.074 176.854  1.00 22.57           C  
ATOM   6737  CE2 PHE A1062     215.354 224.551 175.105  1.00 22.10           C  
ATOM   6738  CZ  PHE A1062     215.055 223.896 176.269  1.00 22.14           C  
ATOM   6739  N   LEU A1063     211.794 229.194 172.823  1.00 22.79           N  
ATOM   6740  CA  LEU A1063     210.927 229.761 171.810  1.00 22.47           C  
ATOM   6741  C   LEU A1063     210.886 228.800 170.646  1.00 22.55           C  
ATOM   6742  O   LEU A1063     211.899 228.578 169.982  1.00 22.70           O  
ATOM   6743  CB  LEU A1063     211.441 231.123 171.360  1.00 22.98           C  
ATOM   6744  CG  LEU A1063     211.630 232.162 172.463  1.00 24.07           C  
ATOM   6745  CD1 LEU A1063     212.158 233.436 171.846  1.00 25.62           C  
ATOM   6746  CD2 LEU A1063     210.312 232.408 173.180  1.00 25.00           C  
ATOM   6747  N   HIS A1064     209.736 228.190 170.421  1.00 22.04           N  
ATOM   6748  CA  HIS A1064     209.629 227.174 169.388  1.00 20.99           C  
ATOM   6749  C   HIS A1064     209.037 227.748 168.130  1.00 22.06           C  
ATOM   6750  O   HIS A1064     207.936 228.293 168.155  1.00 22.22           O  
ATOM   6751  CB  HIS A1064     208.747 226.014 169.817  1.00 21.21           C  
ATOM   6752  CG  HIS A1064     209.177 225.304 171.028  1.00 21.43           C  
ATOM   6753  ND1 HIS A1064     210.445 224.822 171.198  1.00 21.76           N  
ATOM   6754  CD2 HIS A1064     208.486 224.948 172.123  1.00 21.66           C  
ATOM   6755  CE1 HIS A1064     210.514 224.190 172.355  1.00 21.74           C  
ATOM   6756  NE2 HIS A1064     209.336 224.258 172.932  1.00 21.67           N  
ATOM   6757  N   VAL A1065     209.758 227.621 167.028  1.00 20.91           N  
ATOM   6758  CA  VAL A1065     209.313 228.153 165.757  1.00 20.35           C  
ATOM   6759  C   VAL A1065     208.721 227.025 164.937  1.00 20.18           C  
ATOM   6760  O   VAL A1065     209.396 226.034 164.639  1.00 20.83           O  
ATOM   6761  CB  VAL A1065     210.495 228.764 165.007  1.00 20.74           C  
ATOM   6762  CG1 VAL A1065     210.026 229.364 163.711  1.00 20.73           C  
ATOM   6763  CG2 VAL A1065     211.183 229.776 165.888  1.00 21.49           C  
ATOM   6764  N   THR A1066     207.450 227.163 164.586  1.00 20.42           N  
ATOM   6765  CA  THR A1066     206.766 226.089 163.892  1.00 19.66           C  
ATOM   6766  C   THR A1066     206.011 226.532 162.649  1.00 20.03           C  
ATOM   6767  O   THR A1066     205.533 227.661 162.548  1.00 20.45           O  
ATOM   6768  CB  THR A1066     205.774 225.420 164.841  1.00 20.05           C  
ATOM   6769  OG1 THR A1066     204.814 226.392 165.247  1.00 20.59           O  
ATOM   6770  CG2 THR A1066     206.466 224.841 166.066  1.00 20.07           C  
ATOM   6771  N   TYR A1067     205.846 225.587 161.736  1.00 19.43           N  
ATOM   6772  CA  TYR A1067     205.089 225.765 160.511  1.00 19.08           C  
ATOM   6773  C   TYR A1067     203.667 225.283 160.691  1.00 19.39           C  
ATOM   6774  O   TYR A1067     203.425 224.115 161.012  1.00 20.03           O  
ATOM   6775  CB  TYR A1067     205.770 224.991 159.387  1.00 19.43           C  
ATOM   6776  CG  TYR A1067     205.064 224.970 158.062  1.00 19.31           C  
ATOM   6777  CD1 TYR A1067     205.360 225.898 157.106  1.00 19.62           C  
ATOM   6778  CD2 TYR A1067     204.131 223.993 157.804  1.00 19.25           C  
ATOM   6779  CE1 TYR A1067     204.728 225.845 155.891  1.00 19.71           C  
ATOM   6780  CE2 TYR A1067     203.497 223.945 156.598  1.00 19.34           C  
ATOM   6781  CZ  TYR A1067     203.795 224.865 155.641  1.00 19.64           C  
ATOM   6782  OH  TYR A1067     203.168 224.818 154.418  1.00 20.28           O  
ATOM   6783  N   VAL A1068     202.718 226.176 160.512  1.00 19.24           N  
ATOM   6784  CA  VAL A1068     201.330 225.826 160.706  1.00 18.97           C  
ATOM   6785  C   VAL A1068     200.493 226.165 159.478  1.00 19.47           C  
ATOM   6786  O   VAL A1068     200.460 227.328 159.075  1.00 20.44           O  
ATOM   6787  CB  VAL A1068     200.783 226.587 161.919  1.00 19.28           C  
ATOM   6788  CG1 VAL A1068     199.330 226.247 162.144  1.00 19.75           C  
ATOM   6789  CG2 VAL A1068     201.604 226.234 163.137  1.00 19.86           C  
ATOM   6790  N   PRO A1069     199.811 225.197 158.857  1.00 19.02           N  
ATOM   6791  CA  PRO A1069     198.910 225.392 157.735  1.00 19.27           C  
ATOM   6792  C   PRO A1069     197.882 226.435 158.127  1.00 19.61           C  
ATOM   6793  O   PRO A1069     197.339 226.375 159.228  1.00 19.90           O  
ATOM   6794  CB  PRO A1069     198.290 224.006 157.589  1.00 19.41           C  
ATOM   6795  CG  PRO A1069     199.361 223.071 158.097  1.00 19.10           C  
ATOM   6796  CD  PRO A1069     199.990 223.804 159.251  1.00 19.12           C  
ATOM   6797  N   ALA A1070     197.621 227.401 157.253  1.00 19.48           N  
ATOM   6798  CA  ALA A1070     196.730 228.495 157.618  1.00 19.82           C  
ATOM   6799  C   ALA A1070     195.446 228.522 156.816  1.00 20.00           C  
ATOM   6800  O   ALA A1070     194.373 228.808 157.355  1.00 20.65           O  
ATOM   6801  CB  ALA A1070     197.458 229.813 157.436  1.00 20.19           C  
ATOM   6802  N   GLN A1071     195.547 228.267 155.528  1.00 19.69           N  
ATOM   6803  CA  GLN A1071     194.384 228.333 154.657  1.00 19.49           C  
ATOM   6804  C   GLN A1071     194.335 227.058 153.879  1.00 20.39           C  
ATOM   6805  O   GLN A1071     195.389 226.518 153.556  1.00 21.05           O  
ATOM   6806  CB  GLN A1071     194.468 229.524 153.710  1.00 19.88           C  
ATOM   6807  CG  GLN A1071     194.565 230.863 154.406  1.00 20.05           C  
ATOM   6808  CD  GLN A1071     194.610 232.005 153.426  1.00 20.34           C  
ATOM   6809  OE1 GLN A1071     195.048 231.839 152.287  1.00 20.75           O  
ATOM   6810  NE2 GLN A1071     194.155 233.171 153.853  1.00 20.92           N  
ATOM   6811  N   GLU A1072     193.147 226.579 153.552  1.00 19.71           N  
ATOM   6812  CA  GLU A1072     192.991 225.305 152.864  1.00 19.93           C  
ATOM   6813  C   GLU A1072     191.850 225.317 151.873  1.00 20.16           C  
ATOM   6814  O   GLU A1072     190.927 226.122 151.997  1.00 20.37           O  
ATOM   6815  CB  GLU A1072     192.737 224.214 153.889  1.00 19.67           C  
ATOM   6816  CG  GLU A1072     191.435 224.431 154.633  1.00 19.45           C  
ATOM   6817  CD  GLU A1072     191.197 223.482 155.730  1.00 19.93           C  
ATOM   6818  OE1 GLU A1072     191.831 223.615 156.748  1.00 19.11           O  
ATOM   6819  OE2 GLU A1072     190.362 222.624 155.566  1.00 20.21           O  
ATOM   6820  N   LYS A1073     191.895 224.402 150.911  1.00 20.33           N  
ATOM   6821  CA  LYS A1073     190.805 224.221 149.960  1.00 20.39           C  
ATOM   6822  C   LYS A1073     190.399 222.746 149.837  1.00 20.96           C  
ATOM   6823  O   LYS A1073     191.228 221.854 150.040  1.00 21.24           O  
ATOM   6824  CB  LYS A1073     191.188 224.789 148.592  1.00 20.98           C  
ATOM   6825  N   ASN A1074     189.111 222.513 149.492  1.00 20.79           N  
ATOM   6826  CA  ASN A1074     188.546 221.179 149.269  1.00 20.85           C  
ATOM   6827  C   ASN A1074     188.781 220.722 147.821  1.00 21.18           C  
ATOM   6828  O   ASN A1074     188.205 221.264 146.889  1.00 22.21           O  
ATOM   6829  CB  ASN A1074     187.027 221.184 149.540  1.00 21.03           C  
ATOM   6830  CG  ASN A1074     186.617 221.334 151.020  1.00 20.98           C  
ATOM   6831  OD1 ASN A1074     187.418 221.178 151.952  1.00 20.88           O  
ATOM   6832  ND2 ASN A1074     185.332 221.637 151.210  1.00 20.94           N  
ATOM   6833  N   PHE A1075     189.642 219.699 147.645  1.00 21.26           N  
ATOM   6834  CA  PHE A1075     189.980 219.140 146.329  1.00 20.98           C  
ATOM   6835  C   PHE A1075     189.430 217.737 146.212  1.00 21.23           C  
ATOM   6836  O   PHE A1075     189.318 217.023 147.207  1.00 22.40           O  
ATOM   6837  CB  PHE A1075     191.484 219.088 146.121  1.00 21.36           C  
ATOM   6838  CG  PHE A1075     192.107 220.407 146.075  1.00 21.15           C  
ATOM   6839  CD1 PHE A1075     192.681 220.937 147.198  1.00 21.28           C  
ATOM   6840  CD2 PHE A1075     192.114 221.136 144.917  1.00 21.91           C  
ATOM   6841  CE1 PHE A1075     193.258 222.172 147.168  1.00 21.31           C  
ATOM   6842  CE2 PHE A1075     192.685 222.376 144.881  1.00 21.48           C  
ATOM   6843  CZ  PHE A1075     193.258 222.895 146.012  1.00 21.32           C  
ATOM   6844  N   THR A1076     189.090 217.329 145.007  1.00 21.65           N  
ATOM   6845  CA  THR A1076     188.674 215.956 144.801  1.00 21.35           C  
ATOM   6846  C   THR A1076     189.926 215.135 144.626  1.00 21.75           C  
ATOM   6847  O   THR A1076     190.911 215.620 144.072  1.00 22.24           O  
ATOM   6848  CB  THR A1076     187.710 215.830 143.616  1.00 22.06           C  
ATOM   6849  OG1 THR A1076     186.509 216.541 143.919  1.00 22.58           O  
ATOM   6850  CG2 THR A1076     187.385 214.376 143.328  1.00 22.38           C  
ATOM   6851  N   THR A1077     189.940 213.924 145.148  1.00 21.55           N  
ATOM   6852  CA  THR A1077     191.150 213.124 145.049  1.00 21.05           C  
ATOM   6853  C   THR A1077     190.954 211.712 144.541  1.00 21.48           C  
ATOM   6854  O   THR A1077     189.837 211.273 144.265  1.00 21.68           O  
ATOM   6855  CB  THR A1077     191.868 213.076 146.394  1.00 20.83           C  
ATOM   6856  OG1 THR A1077     193.136 212.472 146.232  1.00 21.48           O  
ATOM   6857  CG2 THR A1077     191.070 212.314 147.391  1.00 21.30           C  
ATOM   6858  N   ALA A1078     192.075 211.024 144.388  1.00 21.25           N  
ATOM   6859  CA  ALA A1078     192.132 209.644 143.945  1.00 20.99           C  
ATOM   6860  C   ALA A1078     193.471 209.056 144.371  1.00 21.21           C  
ATOM   6861  O   ALA A1078     194.468 209.775 144.388  1.00 21.90           O  
ATOM   6862  CB  ALA A1078     191.975 209.558 142.437  1.00 21.76           C  
ATOM   6863  N   PRO A1079     193.534 207.768 144.710  1.00 21.06           N  
ATOM   6864  CA  PRO A1079     194.735 207.051 145.080  1.00 21.27           C  
ATOM   6865  C   PRO A1079     195.676 206.805 143.913  1.00 21.88           C  
ATOM   6866  O   PRO A1079     196.867 206.578 144.108  1.00 22.08           O  
ATOM   6867  CB  PRO A1079     194.164 205.736 145.602  1.00 21.33           C  
ATOM   6868  CG  PRO A1079     192.851 205.575 144.897  1.00 21.53           C  
ATOM   6869  CD  PRO A1079     192.317 206.968 144.744  1.00 21.49           C  
ATOM   6870  N   ALA A1080     195.140 206.837 142.703  1.00 22.31           N  
ATOM   6871  CA  ALA A1080     195.921 206.526 141.517  1.00 22.18           C  
ATOM   6872  C   ALA A1080     195.205 206.982 140.270  1.00 23.05           C  
ATOM   6873  O   ALA A1080     193.997 207.236 140.289  1.00 23.72           O  
ATOM   6874  CB  ALA A1080     196.190 205.040 141.432  1.00 22.84           C  
ATOM   6875  N   ILE A1081     195.928 207.042 139.167  1.00 23.50           N  
ATOM   6876  CA  ILE A1081     195.268 207.308 137.900  1.00 23.93           C  
ATOM   6877  C   ILE A1081     195.603 206.237 136.852  1.00 24.20           C  
ATOM   6878  O   ILE A1081     196.668 205.617 136.908  1.00 24.89           O  
ATOM   6879  CB  ILE A1081     195.643 208.701 137.379  1.00 24.02           C  
ATOM   6880  CG1 ILE A1081     197.122 208.743 137.156  1.00 24.40           C  
ATOM   6881  CG2 ILE A1081     195.193 209.787 138.371  1.00 24.22           C  
ATOM   6882  CD1 ILE A1081     197.606 209.954 136.503  1.00 25.68           C  
ATOM   6883  N   CYS A1082     194.696 206.051 135.880  1.00 24.86           N  
ATOM   6884  CA  CYS A1082     194.834 205.119 134.762  1.00 25.01           C  
ATOM   6885  C   CYS A1082     195.289 205.844 133.502  1.00 25.50           C  
ATOM   6886  O   CYS A1082     194.630 206.793 133.060  1.00 26.82           O  
ATOM   6887  CB  CYS A1082     193.498 204.421 134.460  1.00 25.95           C  
ATOM   6888  SG  CYS A1082     192.895 203.382 135.763  1.00 25.85           S  
ATOM   6889  N   HIS A1083     196.374 205.358 132.878  1.00 25.41           N  
ATOM   6890  CA  HIS A1083     196.885 205.930 131.618  1.00 26.03           C  
ATOM   6891  C   HIS A1083     196.602 204.982 130.452  1.00 26.49           C  
ATOM   6892  O   HIS A1083     195.638 205.167 129.712  1.00 26.14           O  
ATOM   6893  CB  HIS A1083     198.376 206.241 131.741  1.00 26.40           C  
ATOM   6894  CG  HIS A1083     198.970 206.911 130.547  1.00 26.97           C  
ATOM   6895  ND1 HIS A1083     198.662 208.211 130.181  1.00 27.64           N  
ATOM   6896  CD2 HIS A1083     199.869 206.473 129.648  1.00 27.06           C  
ATOM   6897  CE1 HIS A1083     199.351 208.527 129.097  1.00 28.09           C  
ATOM   6898  NE2 HIS A1083     200.086 207.490 128.757  1.00 27.84           N  
ATOM   6899  N   ASP A1084     197.392 203.919 130.337  1.00 25.89           N  
ATOM   6900  CA  ASP A1084     197.178 202.899 129.305  1.00 25.95           C  
ATOM   6901  C   ASP A1084     196.553 201.660 129.923  1.00 25.83           C  
ATOM   6902  O   ASP A1084     196.658 200.557 129.388  1.00 25.61           O  
ATOM   6903  CB  ASP A1084     198.490 202.484 128.644  1.00 25.86           C  
ATOM   6904  CG  ASP A1084     199.184 203.570 127.856  1.00 26.24           C  
ATOM   6905  OD1 ASP A1084     198.543 204.280 127.125  1.00 26.76           O  
ATOM   6906  OD2 ASP A1084     200.384 203.670 128.005  1.00 26.34           O  
ATOM   6907  N   GLY A1085     195.955 201.839 131.090  1.00 25.56           N  
ATOM   6908  CA  GLY A1085     195.397 200.743 131.871  1.00 25.63           C  
ATOM   6909  C   GLY A1085     196.346 200.430 133.016  1.00 25.21           C  
ATOM   6910  O   GLY A1085     196.007 199.696 133.949  1.00 24.80           O  
ATOM   6911  N   LYS A1086     197.538 201.010 132.928  1.00 25.26           N  
ATOM   6912  CA  LYS A1086     198.560 200.892 133.949  1.00 24.67           C  
ATOM   6913  C   LYS A1086     198.218 201.859 135.068  1.00 24.53           C  
ATOM   6914  O   LYS A1086     197.704 202.950 134.804  1.00 25.61           O  
ATOM   6915  CB  LYS A1086     199.939 201.209 133.373  1.00 25.12           C  
ATOM   6916  CG  LYS A1086     200.416 200.251 132.258  1.00 25.55           C  
ATOM   6917  CD  LYS A1086     201.919 200.437 131.941  1.00 25.57           C  
ATOM   6918  CE  LYS A1086     202.205 201.708 131.135  1.00 25.52           C  
ATOM   6919  NZ  LYS A1086     201.991 201.499 129.676  1.00 25.66           N  
ATOM   6920  N   ALA A1087     198.493 201.474 136.313  1.00 23.94           N  
ATOM   6921  CA  ALA A1087     198.190 202.344 137.450  1.00 23.00           C  
ATOM   6922  C   ALA A1087     199.389 203.185 137.874  1.00 23.33           C  
ATOM   6923  O   ALA A1087     200.436 202.661 138.261  1.00 23.87           O  
ATOM   6924  CB  ALA A1087     197.705 201.519 138.625  1.00 23.36           C  
ATOM   6925  N   HIS A1088     199.211 204.499 137.833  1.00 23.49           N  
ATOM   6926  CA  HIS A1088     200.249 205.455 138.191  1.00 23.23           C  
ATOM   6927  C   HIS A1088     200.001 206.057 139.569  1.00 23.38           C  
ATOM   6928  O   HIS A1088     198.910 206.554 139.854  1.00 24.33           O  
ATOM   6929  CB  HIS A1088     200.301 206.592 137.167  1.00 24.17           C  
ATOM   6930  CG  HIS A1088     200.734 206.198 135.799  1.00 24.49           C  
ATOM   6931  ND1 HIS A1088     201.886 206.673 135.230  1.00 25.34           N  
ATOM   6932  CD2 HIS A1088     200.182 205.376 134.887  1.00 24.82           C  
ATOM   6933  CE1 HIS A1088     202.026 206.161 134.029  1.00 26.30           C  
ATOM   6934  NE2 HIS A1088     201.011 205.367 133.797  1.00 25.30           N  
ATOM   6935  N   PHE A1089     201.018 206.027 140.418  1.00 22.93           N  
ATOM   6936  CA  PHE A1089     200.935 206.576 141.771  1.00 22.65           C  
ATOM   6937  C   PHE A1089     201.983 207.678 141.900  1.00 24.19           C  
ATOM   6938  O   PHE A1089     203.010 207.590 141.241  1.00 22.25           O  
ATOM   6939  CB  PHE A1089     201.264 205.508 142.797  1.00 22.48           C  
ATOM   6940  CG  PHE A1089     200.409 204.323 142.776  1.00 22.06           C  
ATOM   6941  CD1 PHE A1089     200.742 203.271 141.973  1.00 22.43           C  
ATOM   6942  CD2 PHE A1089     199.293 204.224 143.563  1.00 21.84           C  
ATOM   6943  CE1 PHE A1089     199.982 202.146 141.951  1.00 22.01           C  
ATOM   6944  CE2 PHE A1089     198.526 203.085 143.539  1.00 22.02           C  
ATOM   6945  CZ  PHE A1089     198.879 202.049 142.732  1.00 21.81           C  
ATOM   6946  N   PRO A1090     201.805 208.712 142.721  1.00 22.78           N  
ATOM   6947  CA  PRO A1090     202.790 209.752 142.933  1.00 22.35           C  
ATOM   6948  C   PRO A1090     204.025 209.185 143.593  1.00 22.55           C  
ATOM   6949  O   PRO A1090     203.909 208.353 144.489  1.00 22.90           O  
ATOM   6950  CB  PRO A1090     202.073 210.704 143.892  1.00 22.58           C  
ATOM   6951  CG  PRO A1090     200.622 210.360 143.764  1.00 22.86           C  
ATOM   6952  CD  PRO A1090     200.601 208.873 143.508  1.00 22.85           C  
ATOM   6953  N   ARG A1091     205.201 209.672 143.221  1.00 22.73           N  
ATOM   6954  CA  ARG A1091     206.397 209.284 143.956  1.00 22.78           C  
ATOM   6955  C   ARG A1091     206.360 209.983 145.298  1.00 22.54           C  
ATOM   6956  O   ARG A1091     206.740 209.429 146.328  1.00 22.88           O  
ATOM   6957  CB  ARG A1091     207.667 209.645 143.207  1.00 22.75           C  
ATOM   6958  CG  ARG A1091     207.955 208.792 141.994  1.00 23.14           C  
ATOM   6959  CD  ARG A1091     209.273 209.119 141.405  1.00 23.27           C  
ATOM   6960  NE  ARG A1091     209.653 208.180 140.358  1.00 23.43           N  
ATOM   6961  CZ  ARG A1091     209.286 208.275 139.067  1.00 24.43           C  
ATOM   6962  NH1 ARG A1091     208.524 209.258 138.679  1.00 24.54           N  
ATOM   6963  NH2 ARG A1091     209.695 207.376 138.191  1.00 23.71           N  
ATOM   6964  N   GLU A1092     205.875 211.211 145.263  1.00 22.26           N  
ATOM   6965  CA  GLU A1092     205.671 212.043 146.428  1.00 21.83           C  
ATOM   6966  C   GLU A1092     204.525 212.977 146.121  1.00 21.97           C  
ATOM   6967  O   GLU A1092     204.436 213.512 145.017  1.00 22.11           O  
ATOM   6968  CB  GLU A1092     206.916 212.842 146.791  1.00 21.80           C  
ATOM   6969  N   GLY A1093     203.657 213.184 147.083  1.00 21.33           N  
ATOM   6970  CA  GLY A1093     202.536 214.073 146.873  1.00 21.42           C  
ATOM   6971  C   GLY A1093     201.250 213.300 146.698  1.00 21.15           C  
ATOM   6972  O   GLY A1093     201.215 212.078 146.846  1.00 21.48           O  
ATOM   6973  N   VAL A1094     200.191 214.028 146.420  1.00 21.47           N  
ATOM   6974  CA  VAL A1094     198.867 213.463 146.306  1.00 21.37           C  
ATOM   6975  C   VAL A1094     198.168 213.954 145.052  1.00 22.21           C  
ATOM   6976  O   VAL A1094     198.353 215.102 144.651  1.00 23.19           O  
ATOM   6977  CB  VAL A1094     198.075 213.829 147.567  1.00 21.04           C  
ATOM   6978  CG1 VAL A1094     197.913 215.333 147.681  1.00 21.68           C  
ATOM   6979  CG2 VAL A1094     196.759 213.158 147.545  1.00 21.90           C  
ATOM   6980  N   PHE A1095     197.360 213.100 144.426  1.00 22.33           N  
ATOM   6981  CA  PHE A1095     196.603 213.543 143.264  1.00 22.21           C  
ATOM   6982  C   PHE A1095     195.413 214.374 143.692  1.00 22.24           C  
ATOM   6983  O   PHE A1095     194.708 214.029 144.638  1.00 22.54           O  
ATOM   6984  CB  PHE A1095     196.097 212.370 142.432  1.00 22.39           C  
ATOM   6985  CG  PHE A1095     197.135 211.640 141.668  1.00 22.92           C  
ATOM   6986  CD1 PHE A1095     197.241 210.284 141.776  1.00 23.06           C  
ATOM   6987  CD2 PHE A1095     198.007 212.298 140.837  1.00 23.81           C  
ATOM   6988  CE1 PHE A1095     198.186 209.610 141.065  1.00 23.21           C  
ATOM   6989  CE2 PHE A1095     198.954 211.611 140.139  1.00 24.05           C  
ATOM   6990  CZ  PHE A1095     199.033 210.266 140.256  1.00 23.74           C  
ATOM   6991  N   VAL A1096     195.183 215.465 142.986  1.00 22.79           N  
ATOM   6992  CA  VAL A1096     194.064 216.340 143.270  1.00 22.23           C  
ATOM   6993  C   VAL A1096     193.306 216.682 142.011  1.00 23.18           C  
ATOM   6994  O   VAL A1096     193.868 216.659 140.919  1.00 23.76           O  
ATOM   6995  CB  VAL A1096     194.563 217.645 143.897  1.00 22.60           C  
ATOM   6996  CG1 VAL A1096     195.280 217.361 145.147  1.00 22.72           C  
ATOM   6997  CG2 VAL A1096     195.476 218.357 142.948  1.00 23.20           C  
ATOM   6998  N   SER A1097     192.068 217.096 142.171  1.00 22.74           N  
ATOM   6999  CA  SER A1097     191.268 217.583 141.065  1.00 22.73           C  
ATOM   7000  C   SER A1097     190.555 218.874 141.420  1.00 23.24           C  
ATOM   7001  O   SER A1097     189.871 218.960 142.448  1.00 23.44           O  
ATOM   7002  CB  SER A1097     190.273 216.534 140.632  1.00 23.37           C  
ATOM   7003  OG  SER A1097     189.302 217.073 139.780  1.00 23.91           O  
ATOM   7004  N   ASN A1098     190.698 219.883 140.542  1.00 24.25           N  
ATOM   7005  CA  ASN A1098     190.082 221.202 140.720  1.00 24.65           C  
ATOM   7006  C   ASN A1098     188.682 221.289 140.092  1.00 25.19           C  
ATOM   7007  O   ASN A1098     188.066 222.358 140.088  1.00 25.56           O  
ATOM   7008  CB  ASN A1098     191.008 222.305 140.184  1.00 24.88           C  
ATOM   7009  CG  ASN A1098     191.068 222.434 138.631  1.00 26.02           C  
ATOM   7010  OD1 ASN A1098     190.550 221.579 137.877  1.00 25.71           O  
ATOM   7011  ND2 ASN A1098     191.710 223.515 138.172  1.00 25.87           N  
ATOM   7012  N   GLY A1099     188.160 220.153 139.594  1.00 25.18           N  
ATOM   7013  CA  GLY A1099     186.848 220.011 138.973  1.00 25.47           C  
ATOM   7014  C   GLY A1099     186.950 219.664 137.496  1.00 25.88           C  
ATOM   7015  O   GLY A1099     186.026 219.070 136.940  1.00 25.95           O  
ATOM   7016  N   THR A1100     188.070 220.005 136.858  1.00 25.42           N  
ATOM   7017  CA  THR A1100     188.234 219.654 135.449  1.00 25.82           C  
ATOM   7018  C   THR A1100     189.569 218.984 135.143  1.00 26.00           C  
ATOM   7019  O   THR A1100     189.655 218.145 134.244  1.00 25.61           O  
ATOM   7020  CB  THR A1100     188.078 220.892 134.552  1.00 25.96           C  
ATOM   7021  OG1 THR A1100     189.093 221.844 134.874  1.00 26.34           O  
ATOM   7022  CG2 THR A1100     186.715 221.524 134.757  1.00 26.28           C  
ATOM   7023  N   HIS A1101     190.610 219.332 135.891  1.00 25.14           N  
ATOM   7024  CA  HIS A1101     191.936 218.794 135.619  1.00 24.79           C  
ATOM   7025  C   HIS A1101     192.570 218.178 136.842  1.00 24.85           C  
ATOM   7026  O   HIS A1101     192.398 218.659 137.965  1.00 24.82           O  
ATOM   7027  CB  HIS A1101     192.876 219.880 135.090  1.00 25.55           C  
ATOM   7028  CG  HIS A1101     192.550 220.386 133.730  1.00 25.94           C  
ATOM   7029  ND1 HIS A1101     191.511 221.245 133.488  1.00 26.10           N  
ATOM   7030  CD2 HIS A1101     193.138 220.160 132.535  1.00 26.54           C  
ATOM   7031  CE1 HIS A1101     191.470 221.530 132.200  1.00 26.33           C  
ATOM   7032  NE2 HIS A1101     192.445 220.882 131.600  1.00 26.60           N  
ATOM   7033  N   TRP A1102     193.328 217.117 136.605  1.00 24.44           N  
ATOM   7034  CA  TRP A1102     194.068 216.444 137.653  1.00 24.04           C  
ATOM   7035  C   TRP A1102     195.499 216.924 137.734  1.00 24.15           C  
ATOM   7036  O   TRP A1102     196.176 217.066 136.718  1.00 24.99           O  
ATOM   7037  CB  TRP A1102     194.051 214.943 137.427  1.00 24.24           C  
ATOM   7038  CG  TRP A1102     192.758 214.344 137.718  1.00 23.81           C  
ATOM   7039  CD1 TRP A1102     191.736 214.165 136.863  1.00 24.43           C  
ATOM   7040  CD2 TRP A1102     192.322 213.825 138.978  1.00 23.36           C  
ATOM   7041  NE1 TRP A1102     190.687 213.584 137.506  1.00 24.06           N  
ATOM   7042  CE2 TRP A1102     191.030 213.374 138.803  1.00 23.45           C  
ATOM   7043  CE3 TRP A1102     192.914 213.719 140.223  1.00 23.61           C  
ATOM   7044  CZ2 TRP A1102     190.306 212.826 139.833  1.00 23.64           C  
ATOM   7045  CZ3 TRP A1102     192.195 213.169 141.255  1.00 22.84           C  
ATOM   7046  CH2 TRP A1102     190.922 212.736 141.065  1.00 22.84           C  
ATOM   7047  N   PHE A1103     195.957 217.129 138.955  1.00 23.89           N  
ATOM   7048  CA  PHE A1103     197.304 217.582 139.238  1.00 23.41           C  
ATOM   7049  C   PHE A1103     197.905 216.753 140.340  1.00 23.68           C  
ATOM   7050  O   PHE A1103     197.191 216.087 141.082  1.00 23.81           O  
ATOM   7051  CB  PHE A1103     197.312 219.033 139.682  1.00 23.88           C  
ATOM   7052  CG  PHE A1103     196.685 219.926 138.739  1.00 23.85           C  
ATOM   7053  CD1 PHE A1103     195.362 220.243 138.886  1.00 24.41           C  
ATOM   7054  CD2 PHE A1103     197.391 220.457 137.694  1.00 24.27           C  
ATOM   7055  CE1 PHE A1103     194.749 221.077 138.010  1.00 25.05           C  
ATOM   7056  CE2 PHE A1103     196.782 221.296 136.807  1.00 25.27           C  
ATOM   7057  CZ  PHE A1103     195.454 221.605 136.969  1.00 25.15           C  
ATOM   7058  N   VAL A1104     199.211 216.778 140.452  1.00 23.86           N  
ATOM   7059  CA  VAL A1104     199.851 216.127 141.581  1.00 23.03           C  
ATOM   7060  C   VAL A1104     200.567 217.185 142.383  1.00 22.84           C  
ATOM   7061  O   VAL A1104     201.211 218.062 141.811  1.00 24.16           O  
ATOM   7062  CB  VAL A1104     200.799 215.015 141.110  1.00 23.77           C  
ATOM   7063  CG1 VAL A1104     201.862 215.574 140.180  1.00 24.62           C  
ATOM   7064  CG2 VAL A1104     201.426 214.339 142.311  1.00 23.16           C  
ATOM   7065  N   THR A1105     200.413 217.159 143.700  1.00 22.70           N  
ATOM   7066  CA  THR A1105     201.059 218.188 144.495  1.00 22.22           C  
ATOM   7067  C   THR A1105     201.589 217.688 145.825  1.00 21.85           C  
ATOM   7068  O   THR A1105     201.138 216.670 146.346  1.00 22.41           O  
ATOM   7069  CB  THR A1105     200.104 219.348 144.743  1.00 21.90           C  
ATOM   7070  OG1 THR A1105     200.846 220.423 145.272  1.00 22.11           O  
ATOM   7071  CG2 THR A1105     199.009 218.962 145.716  1.00 21.97           C  
ATOM   7072  N   GLN A1106     202.542 218.417 146.389  1.00 21.57           N  
ATOM   7073  CA  GLN A1106     203.094 218.064 147.687  1.00 20.98           C  
ATOM   7074  C   GLN A1106     202.011 218.061 148.754  1.00 20.71           C  
ATOM   7075  O   GLN A1106     201.091 218.875 148.740  1.00 21.17           O  
ATOM   7076  CB  GLN A1106     204.246 218.987 148.049  1.00 20.75           C  
ATOM   7077  CG  GLN A1106     203.874 220.409 148.278  1.00 20.64           C  
ATOM   7078  CD  GLN A1106     205.084 221.229 148.496  1.00 20.15           C  
ATOM   7079  OE1 GLN A1106     205.974 220.814 149.243  1.00 20.06           O  
ATOM   7080  NE2 GLN A1106     205.146 222.378 147.856  1.00 20.30           N  
ATOM   7081  N   ARG A1107     202.132 217.128 149.680  1.00 20.63           N  
ATOM   7082  CA  ARG A1107     201.093 216.842 150.658  1.00 20.08           C  
ATOM   7083  C   ARG A1107     200.679 218.018 151.540  1.00 19.96           C  
ATOM   7084  O   ARG A1107     199.505 218.147 151.881  1.00 20.31           O  
ATOM   7085  CB  ARG A1107     201.576 215.731 151.568  1.00 20.02           C  
ATOM   7086  CG  ARG A1107     201.877 214.428 150.858  1.00 20.49           C  
ATOM   7087  CD  ARG A1107     202.217 213.336 151.801  1.00 20.42           C  
ATOM   7088  NE  ARG A1107     202.967 212.257 151.152  1.00 20.62           N  
ATOM   7089  CZ  ARG A1107     202.479 211.384 150.252  1.00 20.86           C  
ATOM   7090  NH1 ARG A1107     203.260 210.443 149.771  1.00 20.57           N  
ATOM   7091  NH2 ARG A1107     201.237 211.475 149.840  1.00 20.87           N  
ATOM   7092  N   ASN A1108     201.637 218.848 151.945  1.00 20.06           N  
ATOM   7093  CA  ASN A1108     201.358 219.910 152.909  1.00 19.70           C  
ATOM   7094  C   ASN A1108     201.280 221.317 152.335  1.00 19.92           C  
ATOM   7095  O   ASN A1108     201.299 222.288 153.092  1.00 20.24           O  
ATOM   7096  CB  ASN A1108     202.397 219.884 154.009  1.00 19.09           C  
ATOM   7097  CG  ASN A1108     202.285 218.681 154.875  1.00 19.34           C  
ATOM   7098  OD1 ASN A1108     201.230 218.429 155.464  1.00 19.63           O  
ATOM   7099  ND2 ASN A1108     203.344 217.923 154.975  1.00 19.02           N  
ATOM   7100  N   PHE A1109     201.217 221.451 151.021  1.00 20.45           N  
ATOM   7101  CA  PHE A1109     201.150 222.790 150.447  1.00 19.96           C  
ATOM   7102  C   PHE A1109     200.692 222.739 149.006  1.00 20.51           C  
ATOM   7103  O   PHE A1109     201.344 222.126 148.167  1.00 21.45           O  
ATOM   7104  CB  PHE A1109     202.504 223.483 150.547  1.00 20.29           C  
ATOM   7105  CG  PHE A1109     202.465 224.887 150.126  1.00 20.49           C  
ATOM   7106  CD1 PHE A1109     201.997 225.856 150.976  1.00 20.47           C  
ATOM   7107  CD2 PHE A1109     202.883 225.251 148.878  1.00 20.70           C  
ATOM   7108  CE1 PHE A1109     201.950 227.163 150.581  1.00 20.43           C  
ATOM   7109  CE2 PHE A1109     202.837 226.556 148.480  1.00 20.88           C  
ATOM   7110  CZ  PHE A1109     202.369 227.513 149.335  1.00 20.55           C  
ATOM   7111  N   TYR A1110     199.591 223.395 148.700  1.00 20.50           N  
ATOM   7112  CA  TYR A1110     199.045 223.297 147.369  1.00 20.49           C  
ATOM   7113  C   TYR A1110     199.911 223.993 146.357  1.00 20.90           C  
ATOM   7114  O   TYR A1110     200.086 225.211 146.366  1.00 20.97           O  
ATOM   7115  CB  TYR A1110     197.641 223.864 147.324  1.00 20.78           C  
ATOM   7116  CG  TYR A1110     196.990 223.722 146.003  1.00 20.88           C  
ATOM   7117  CD1 TYR A1110     196.700 222.472 145.515  1.00 21.27           C  
ATOM   7118  CD2 TYR A1110     196.668 224.838 145.279  1.00 21.12           C  
ATOM   7119  CE1 TYR A1110     196.095 222.340 144.298  1.00 21.32           C  
ATOM   7120  CE2 TYR A1110     196.055 224.708 144.061  1.00 21.16           C  
ATOM   7121  CZ  TYR A1110     195.769 223.463 143.571  1.00 21.12           C  
ATOM   7122  OH  TYR A1110     195.150 223.327 142.354  1.00 21.88           O  
ATOM   7123  N   GLU A1111     200.428 223.191 145.459  1.00 21.21           N  
ATOM   7124  CA  GLU A1111     201.318 223.623 144.412  1.00 20.83           C  
ATOM   7125  C   GLU A1111     201.210 222.642 143.263  1.00 21.42           C  
ATOM   7126  O   GLU A1111     202.025 221.728 143.166  1.00 22.28           O  
ATOM   7127  CB  GLU A1111     202.740 223.661 144.936  1.00 20.71           C  
ATOM   7128  CG  GLU A1111     203.734 224.204 143.980  1.00 20.88           C  
ATOM   7129  CD  GLU A1111     205.069 224.263 144.579  1.00 20.69           C  
ATOM   7130  OE1 GLU A1111     205.569 223.235 144.962  1.00 20.58           O  
ATOM   7131  OE2 GLU A1111     205.598 225.334 144.679  1.00 20.24           O  
ATOM   7132  N   PRO A1112     200.167 222.738 142.452  1.00 21.28           N  
ATOM   7133  CA  PRO A1112     199.778 221.748 141.484  1.00 21.91           C  
ATOM   7134  C   PRO A1112     200.787 221.656 140.372  1.00 22.82           C  
ATOM   7135  O   PRO A1112     201.228 222.675 139.843  1.00 22.98           O  
ATOM   7136  CB  PRO A1112     198.440 222.285 140.987  1.00 22.25           C  
ATOM   7137  CG  PRO A1112     198.520 223.769 141.213  1.00 21.92           C  
ATOM   7138  CD  PRO A1112     199.369 223.946 142.448  1.00 21.52           C  
ATOM   7139  N   GLN A1113     201.094 220.439 139.971  1.00 23.43           N  
ATOM   7140  CA  GLN A1113     201.969 220.197 138.849  1.00 23.52           C  
ATOM   7141  C   GLN A1113     201.273 219.311 137.849  1.00 24.35           C  
ATOM   7142  O   GLN A1113     200.404 218.516 138.204  1.00 25.16           O  
ATOM   7143  CB  GLN A1113     203.265 219.546 139.305  1.00 24.14           C  
ATOM   7144  CG  GLN A1113     204.096 220.405 140.218  1.00 23.86           C  
ATOM   7145  CD  GLN A1113     205.387 219.728 140.598  1.00 25.04           C  
ATOM   7146  OE1 GLN A1113     205.419 218.518 140.831  1.00 25.62           O  
ATOM   7147  NE2 GLN A1113     206.467 220.497 140.660  1.00 25.11           N  
ATOM   7148  N   ILE A1114     201.674 219.412 136.601  1.00 24.82           N  
ATOM   7149  CA  ILE A1114     201.139 218.526 135.591  1.00 25.45           C  
ATOM   7150  C   ILE A1114     201.589 217.127 135.927  1.00 26.04           C  
ATOM   7151  O   ILE A1114     202.735 216.923 136.325  1.00 26.66           O  
ATOM   7152  CB  ILE A1114     201.619 218.926 134.188  1.00 25.86           C  
ATOM   7153  CG1 ILE A1114     201.137 220.364 133.853  1.00 25.21           C  
ATOM   7154  CG2 ILE A1114     201.148 217.914 133.140  1.00 27.52           C  
ATOM   7155  CD1 ILE A1114     199.621 220.571 133.857  1.00 25.07           C  
ATOM   7156  N   ILE A1115     200.688 216.172 135.811  1.00 26.02           N  
ATOM   7157  CA  ILE A1115     201.047 214.812 136.124  1.00 26.29           C  
ATOM   7158  C   ILE A1115     201.845 214.244 134.978  1.00 27.75           C  
ATOM   7159  O   ILE A1115     201.375 214.222 133.839  1.00 29.18           O  
ATOM   7160  CB  ILE A1115     199.804 213.966 136.365  1.00 26.20           C  
ATOM   7161  CG1 ILE A1115     199.036 214.537 137.547  1.00 25.59           C  
ATOM   7162  CG2 ILE A1115     200.229 212.554 136.634  1.00 26.32           C  
ATOM   7163  CD1 ILE A1115     197.642 213.989 137.731  1.00 25.36           C  
ATOM   7164  N   THR A1116     203.052 213.803 135.282  1.00 27.34           N  
ATOM   7165  CA  THR A1116     203.956 213.288 134.274  1.00 27.42           C  
ATOM   7166  C   THR A1116     204.576 211.995 134.746  1.00 28.98           C  
ATOM   7167  O   THR A1116     204.485 211.642 135.927  1.00 26.69           O  
ATOM   7168  CB  THR A1116     205.106 214.262 133.974  1.00 28.61           C  
ATOM   7169  OG1 THR A1116     206.048 214.223 135.043  1.00 28.48           O  
ATOM   7170  CG2 THR A1116     204.610 215.673 133.842  1.00 28.80           C  
ATOM   7171  N   THR A1117     205.288 211.336 133.853  1.00 28.13           N  
ATOM   7172  CA  THR A1117     205.982 210.102 134.196  1.00 27.71           C  
ATOM   7173  C   THR A1117     207.159 210.361 135.133  1.00 26.81           C  
ATOM   7174  O   THR A1117     207.733 209.425 135.689  1.00 26.93           O  
ATOM   7175  CB  THR A1117     206.485 209.382 132.938  1.00 29.55           C  
ATOM   7176  OG1 THR A1117     207.402 210.231 132.240  1.00 30.97           O  
ATOM   7177  CG2 THR A1117     205.312 209.050 132.029  1.00 30.33           C  
ATOM   7178  N   ASP A1118     207.531 211.630 135.304  1.00 27.35           N  
ATOM   7179  CA  ASP A1118     208.622 211.984 136.198  1.00 27.10           C  
ATOM   7180  C   ASP A1118     208.108 212.340 137.588  1.00 26.97           C  
ATOM   7181  O   ASP A1118     208.895 212.600 138.499  1.00 26.18           O  
ATOM   7182  CB  ASP A1118     209.427 213.145 135.623  1.00 28.26           C  
ATOM   7183  N   ASN A1119     206.784 212.353 137.748  1.00 26.46           N  
ATOM   7184  CA  ASN A1119     206.160 212.646 139.029  1.00 25.53           C  
ATOM   7185  C   ASN A1119     205.556 211.390 139.628  1.00 25.54           C  
ATOM   7186  O   ASN A1119     205.434 211.277 140.849  1.00 24.93           O  
ATOM   7187  CB  ASN A1119     205.102 213.727 138.897  1.00 26.18           C  
ATOM   7188  CG  ASN A1119     205.684 215.066 138.568  1.00 26.88           C  
ATOM   7189  OD1 ASN A1119     206.792 215.372 139.015  1.00 27.43           O  
ATOM   7190  ND2 ASN A1119     204.982 215.885 137.818  1.00 26.99           N  
ATOM   7191  N   THR A1120     205.178 210.452 138.763  1.00 24.88           N  
ATOM   7192  CA  THR A1120     204.518 209.229 139.184  1.00 23.71           C  
ATOM   7193  C   THR A1120     205.317 207.995 138.811  1.00 24.25           C  
ATOM   7194  O   THR A1120     206.158 208.033 137.916  1.00 25.50           O  
ATOM   7195  CB  THR A1120     203.135 209.124 138.531  1.00 23.94           C  
ATOM   7196  OG1 THR A1120     203.281 208.987 137.124  1.00 25.02           O  
ATOM   7197  CG2 THR A1120     202.319 210.352 138.818  1.00 24.15           C  
ATOM   7198  N   PHE A1121     205.007 206.880 139.452  1.00 23.29           N  
ATOM   7199  CA  PHE A1121     205.622 205.606 139.130  1.00 22.86           C  
ATOM   7200  C   PHE A1121     204.526 204.609 138.838  1.00 23.41           C  
ATOM   7201  O   PHE A1121     203.378 204.803 139.234  1.00 22.65           O  
ATOM   7202  CB  PHE A1121     206.502 205.106 140.266  1.00 23.00           C  
ATOM   7203  CG  PHE A1121     205.759 204.707 141.480  1.00 22.42           C  
ATOM   7204  CD1 PHE A1121     205.344 203.399 141.650  1.00 22.41           C  
ATOM   7205  CD2 PHE A1121     205.469 205.622 142.456  1.00 22.95           C  
ATOM   7206  CE1 PHE A1121     204.656 203.027 142.770  1.00 22.09           C  
ATOM   7207  CE2 PHE A1121     204.784 205.250 143.577  1.00 22.65           C  
ATOM   7208  CZ  PHE A1121     204.376 203.953 143.732  1.00 21.98           C  
ATOM   7209  N   VAL A1122     204.854 203.543 138.134  1.00 22.49           N  
ATOM   7210  CA  VAL A1122     203.827 202.589 137.765  1.00 22.46           C  
ATOM   7211  C   VAL A1122     203.933 201.272 138.483  1.00 22.24           C  
ATOM   7212  O   VAL A1122     205.009 200.684 138.565  1.00 22.49           O  
ATOM   7213  CB  VAL A1122     203.871 202.333 136.265  1.00 23.26           C  
ATOM   7214  CG1 VAL A1122     202.835 201.310 135.884  1.00 23.25           C  
ATOM   7215  CG2 VAL A1122     203.617 203.618 135.557  1.00 24.45           C  
ATOM   7216  N   SER A1123     202.807 200.805 138.994  1.00 21.80           N  
ATOM   7217  CA  SER A1123     202.769 199.499 139.622  1.00 21.35           C  
ATOM   7218  C   SER A1123     201.393 198.878 139.547  1.00 21.46           C  
ATOM   7219  O   SER A1123     200.410 199.467 139.984  1.00 21.96           O  
ATOM   7220  CB  SER A1123     203.197 199.574 141.061  1.00 21.12           C  
ATOM   7221  OG  SER A1123     203.151 198.298 141.645  1.00 20.82           O  
ATOM   7222  N   GLY A1124     201.314 197.672 139.014  1.00 21.38           N  
ATOM   7223  CA  GLY A1124     200.029 197.002 138.931  1.00 21.93           C  
ATOM   7224  C   GLY A1124     199.161 197.675 137.886  1.00 22.73           C  
ATOM   7225  O   GLY A1124     199.667 198.344 136.980  1.00 23.01           O  
ATOM   7226  N   ASN A1125     197.852 197.500 138.007  1.00 23.25           N  
ATOM   7227  CA  ASN A1125     196.954 198.029 137.001  1.00 23.50           C  
ATOM   7228  C   ASN A1125     195.598 198.439 137.593  1.00 24.08           C  
ATOM   7229  O   ASN A1125     195.342 198.267 138.795  1.00 24.65           O  
ATOM   7230  CB  ASN A1125     196.804 197.010 135.880  1.00 23.66           C  
ATOM   7231  CG  ASN A1125     196.171 195.745 136.333  1.00 23.61           C  
ATOM   7232  OD1 ASN A1125     195.019 195.745 136.786  1.00 23.79           O  
ATOM   7233  ND2 ASN A1125     196.890 194.657 136.225  1.00 23.83           N  
ATOM   7234  N   CYS A1126     194.748 198.987 136.723  1.00 23.54           N  
ATOM   7235  CA  CYS A1126     193.451 199.573 137.053  1.00 23.83           C  
ATOM   7236  C   CYS A1126     192.365 198.592 137.518  1.00 23.65           C  
ATOM   7237  O   CYS A1126     191.322 199.031 138.010  1.00 23.70           O  
ATOM   7238  CB  CYS A1126     192.955 200.368 135.832  1.00 25.37           C  
ATOM   7239  SG  CYS A1126     194.037 201.754 135.430  1.00 26.45           S  
ATOM   7240  N   ASP A1127     192.599 197.275 137.388  1.00 23.89           N  
ATOM   7241  CA  ASP A1127     191.642 196.255 137.825  1.00 24.05           C  
ATOM   7242  C   ASP A1127     191.890 195.883 139.278  1.00 23.85           C  
ATOM   7243  O   ASP A1127     191.149 195.091 139.861  1.00 23.86           O  
ATOM   7244  CB  ASP A1127     191.742 195.002 136.956  1.00 23.82           C  
ATOM   7245  CG  ASP A1127     191.284 195.224 135.519  1.00 23.98           C  
ATOM   7246  OD1 ASP A1127     190.427 196.048 135.295  1.00 23.90           O  
ATOM   7247  OD2 ASP A1127     191.805 194.564 134.655  1.00 23.15           O  
ATOM   7248  N   VAL A1128     192.946 196.442 139.855  1.00 23.84           N  
ATOM   7249  CA  VAL A1128     193.307 196.127 141.222  1.00 23.43           C  
ATOM   7250  C   VAL A1128     193.049 197.291 142.169  1.00 23.46           C  
ATOM   7251  O   VAL A1128     192.509 197.099 143.257  1.00 23.31           O  
ATOM   7252  CB  VAL A1128     194.785 195.716 141.290  1.00 23.59           C  
ATOM   7253  CG1 VAL A1128     195.185 195.461 142.720  1.00 23.07           C  
ATOM   7254  CG2 VAL A1128     194.999 194.475 140.443  1.00 24.15           C  
ATOM   7255  N   VAL A1129     193.467 198.489 141.780  1.00 23.61           N  
ATOM   7256  CA  VAL A1129     193.346 199.636 142.674  1.00 22.99           C  
ATOM   7257  C   VAL A1129     191.903 200.098 142.807  1.00 22.96           C  
ATOM   7258  O   VAL A1129     191.210 200.307 141.813  1.00 23.45           O  
ATOM   7259  CB  VAL A1129     194.208 200.802 142.173  1.00 23.15           C  
ATOM   7260  CG1 VAL A1129     194.010 202.040 143.060  1.00 22.73           C  
ATOM   7261  CG2 VAL A1129     195.660 200.384 142.160  1.00 23.50           C  
ATOM   7262  N   ILE A1130     191.463 200.274 144.047  1.00 23.01           N  
ATOM   7263  CA  ILE A1130     190.105 200.702 144.341  1.00 22.95           C  
ATOM   7264  C   ILE A1130     189.968 202.212 144.263  1.00 23.01           C  
ATOM   7265  O   ILE A1130     190.691 202.939 144.937  1.00 22.89           O  
ATOM   7266  CB  ILE A1130     189.695 200.244 145.754  1.00 22.71           C  
ATOM   7267  CG1 ILE A1130     189.722 198.706 145.830  1.00 23.04           C  
ATOM   7268  CG2 ILE A1130     188.311 200.789 146.107  1.00 22.66           C  
ATOM   7269  CD1 ILE A1130     189.629 198.152 147.246  1.00 21.68           C  
ATOM   7270  N   GLY A1131     189.017 202.685 143.467  1.00 23.23           N  
ATOM   7271  CA  GLY A1131     188.786 204.120 143.354  1.00 23.12           C  
ATOM   7272  C   GLY A1131     189.757 204.818 142.416  1.00 23.03           C  
ATOM   7273  O   GLY A1131     189.996 206.017 142.550  1.00 22.78           O  
ATOM   7274  N   ILE A1132     190.323 204.072 141.480  1.00 23.21           N  
ATOM   7275  CA  ILE A1132     191.260 204.623 140.517  1.00 22.95           C  
ATOM   7276  C   ILE A1132     190.491 205.397 139.459  1.00 23.98           C  
ATOM   7277  O   ILE A1132     189.394 204.992 139.075  1.00 24.20           O  
ATOM   7278  CB  ILE A1132     192.111 203.508 139.891  1.00 23.31           C  
ATOM   7279  CG1 ILE A1132     193.296 204.129 139.196  1.00 24.20           C  
ATOM   7280  CG2 ILE A1132     191.275 202.672 138.925  1.00 23.85           C  
ATOM   7281  CD1 ILE A1132     194.425 203.175 138.875  1.00 24.42           C  
ATOM   7282  N   VAL A1133     191.042 206.515 138.994  1.00 23.94           N  
ATOM   7283  CA  VAL A1133     190.337 207.313 137.991  1.00 24.49           C  
ATOM   7284  C   VAL A1133     191.133 207.409 136.696  1.00 25.42           C  
ATOM   7285  O   VAL A1133     192.343 207.211 136.714  1.00 25.99           O  
ATOM   7286  CB  VAL A1133     190.092 208.731 138.527  1.00 24.05           C  
ATOM   7287  CG1 VAL A1133     189.270 208.667 139.790  1.00 24.64           C  
ATOM   7288  CG2 VAL A1133     191.419 209.405 138.775  1.00 23.84           C  
ATOM   7289  N   ASN A1134     190.451 207.735 135.587  1.00 26.37           N  
ATOM   7290  CA  ASN A1134     191.066 207.893 134.268  1.00 26.21           C  
ATOM   7291  C   ASN A1134     191.602 209.314 134.076  1.00 26.02           C  
ATOM   7292  O   ASN A1134     190.906 210.289 134.348  1.00 25.88           O  
ATOM   7293  CB  ASN A1134     190.064 207.547 133.164  1.00 28.53           C  
ATOM   7294  CG  ASN A1134     189.870 206.039 132.952  1.00 29.78           C  
ATOM   7295  OD1 ASN A1134     190.310 205.206 133.760  1.00 29.26           O  
ATOM   7296  ND2 ASN A1134     189.202 205.695 131.863  1.00 32.34           N  
ATOM   7297  N   ASN A1135     192.851 209.414 133.589  1.00 26.10           N  
ATOM   7298  CA  ASN A1135     193.527 210.679 133.296  1.00 26.22           C  
ATOM   7299  C   ASN A1135     194.540 210.475 132.189  1.00 26.48           C  
ATOM   7300  O   ASN A1135     194.713 209.365 131.696  1.00 26.58           O  
ATOM   7301  CB  ASN A1135     194.225 211.241 134.516  1.00 25.94           C  
ATOM   7302  CG  ASN A1135     194.413 212.713 134.422  1.00 26.34           C  
ATOM   7303  OD1 ASN A1135     193.510 213.447 134.012  1.00 26.13           O  
ATOM   7304  ND2 ASN A1135     195.586 213.166 134.765  1.00 26.28           N  
ATOM   7305  N   THR A1136     195.221 211.540 131.806  1.00 26.85           N  
ATOM   7306  CA  THR A1136     196.292 211.411 130.837  1.00 27.28           C  
ATOM   7307  C   THR A1136     197.597 211.827 131.475  1.00 27.68           C  
ATOM   7308  O   THR A1136     197.706 212.933 132.003  1.00 27.64           O  
ATOM   7309  CB  THR A1136     196.029 212.269 129.591  1.00 27.50           C  
ATOM   7310  OG1 THR A1136     194.818 211.839 128.965  1.00 27.60           O  
ATOM   7311  CG2 THR A1136     197.177 212.130 128.607  1.00 28.55           C  
ATOM   7312  N   VAL A1137     198.589 210.951 131.410  1.00 28.00           N  
ATOM   7313  CA  VAL A1137     199.893 211.243 131.970  1.00 28.08           C  
ATOM   7314  C   VAL A1137     200.815 211.741 130.880  1.00 29.09           C  
ATOM   7315  O   VAL A1137     200.952 211.114 129.832  1.00 29.57           O  
ATOM   7316  CB  VAL A1137     200.486 209.996 132.628  1.00 27.62           C  
ATOM   7317  CG1 VAL A1137     201.860 210.299 133.182  1.00 28.29           C  
ATOM   7318  CG2 VAL A1137     199.569 209.549 133.706  1.00 27.12           C  
ATOM   7319  N   TYR A1138     201.434 212.877 131.118  1.00 29.76           N  
ATOM   7320  CA  TYR A1138     202.320 213.463 130.137  1.00 31.17           C  
ATOM   7321  C   TYR A1138     203.706 212.842 130.174  1.00 33.22           C  
ATOM   7322  O   TYR A1138     204.303 212.683 131.239  1.00 30.84           O  
ATOM   7323  CB  TYR A1138     202.391 214.966 130.354  1.00 31.75           C  
ATOM   7324  CG  TYR A1138     203.403 215.671 129.509  1.00 33.65           C  
ATOM   7325  CD1 TYR A1138     203.175 215.885 128.169  1.00 35.12           C  
ATOM   7326  CD2 TYR A1138     204.568 216.121 130.088  1.00 34.41           C  
ATOM   7327  CE1 TYR A1138     204.119 216.549 127.417  1.00 36.38           C  
ATOM   7328  CE2 TYR A1138     205.497 216.781 129.348  1.00 35.32           C  
ATOM   7329  CZ  TYR A1138     205.282 216.999 128.021  1.00 36.44           C  
ATOM   7330  OH  TYR A1138     206.223 217.667 127.285  1.00 37.94           O  
ATOM   7331  N   ASP A1139     204.211 212.495 128.998  1.00 34.63           N  
ATOM   7332  CA  ASP A1139     205.550 211.947 128.849  1.00 34.40           C  
ATOM   7333  C   ASP A1139     206.456 212.974 128.172  1.00 36.50           C  
ATOM   7334  O   ASP A1139     206.331 213.185 126.965  1.00 35.02           O  
ATOM   7335  CB  ASP A1139     205.531 210.671 128.017  1.00 36.32           C  
ATOM   7336  CG  ASP A1139     206.921 210.067 127.870  1.00 37.58           C  
ATOM   7337  OD1 ASP A1139     207.850 210.647 128.410  1.00 37.00           O  
ATOM   7338  OD2 ASP A1139     207.051 209.046 127.217  1.00 39.41           O  
ATOM   7339  N   PRO A1140     207.365 213.630 128.907  1.00 36.62           N  
ATOM   7340  CA  PRO A1140     208.274 214.664 128.441  1.00 36.91           C  
ATOM   7341  C   PRO A1140     209.160 214.201 127.294  1.00 38.96           C  
ATOM   7342  O   PRO A1140     209.708 215.022 126.561  1.00 40.55           O  
ATOM   7343  CB  PRO A1140     209.118 214.950 129.686  1.00 36.38           C  
ATOM   7344  CG  PRO A1140     208.253 214.545 130.838  1.00 34.30           C  
ATOM   7345  CD  PRO A1140     207.468 213.363 130.341  1.00 34.52           C  
ATOM   7346  N   LEU A1141     209.313 212.891 127.138  1.00 38.82           N  
ATOM   7347  CA  LEU A1141     210.159 212.373 126.083  1.00 38.26           C  
ATOM   7348  C   LEU A1141     209.489 212.351 124.724  1.00 45.46           C  
ATOM   7349  O   LEU A1141     210.176 212.405 123.705  1.00 39.28           O  
ATOM   7350  CB  LEU A1141     210.637 210.957 126.428  1.00 40.20           C  
ATOM   7351  CG  LEU A1141     211.548 210.253 125.376  1.00 41.36           C  
ATOM   7352  CD1 LEU A1141     212.805 211.068 125.107  1.00 41.86           C  
ATOM   7353  CD2 LEU A1141     211.919 208.881 125.887  1.00 42.30           C  
ATOM   7354  N   GLN A1142     208.168 212.236 124.661  1.00 40.48           N  
ATOM   7355  CA  GLN A1142     207.605 212.053 123.338  1.00 40.59           C  
ATOM   7356  C   GLN A1142     207.787 213.295 122.459  1.00 40.76           C  
ATOM   7357  O   GLN A1142     208.249 213.156 121.330  1.00 41.20           O  
ATOM   7358  CB  GLN A1142     206.145 211.582 123.393  1.00 41.40           C  
ATOM   7359  CG  GLN A1142     205.984 210.220 124.035  1.00 41.04           C  
ATOM   7360  CD  GLN A1142     206.808 209.145 123.375  1.00 41.97           C  
ATOM   7361  OE1 GLN A1142     206.812 209.007 122.149  1.00 42.14           O  
ATOM   7362  NE2 GLN A1142     207.517 208.371 124.194  1.00 41.55           N  
ATOM   7363  N   PRO A1143     207.499 214.524 122.926  1.00 41.41           N  
ATOM   7364  CA  PRO A1143     207.697 215.747 122.173  1.00 42.70           C  
ATOM   7365  C   PRO A1143     209.133 215.885 121.680  1.00 42.30           C  
ATOM   7366  O   PRO A1143     209.373 216.438 120.605  1.00 44.27           O  
ATOM   7367  CB  PRO A1143     207.356 216.826 123.202  1.00 41.20           C  
ATOM   7368  CG  PRO A1143     206.408 216.146 124.146  1.00 40.27           C  
ATOM   7369  CD  PRO A1143     206.936 214.744 124.267  1.00 40.40           C  
ATOM   7370  N   GLU A1144     210.084 215.364 122.452  1.00 41.38           N  
ATOM   7371  CA  GLU A1144     211.486 215.451 122.083  1.00 41.21           C  
ATOM   7372  C   GLU A1144     211.803 214.520 120.927  1.00 42.80           C  
ATOM   7373  O   GLU A1144     212.600 214.854 120.049  1.00 44.01           O  
ATOM   7374  CB  GLU A1144     212.362 215.103 123.276  1.00 42.89           C  
ATOM   7375  N   LEU A1145     211.158 213.357 120.918  1.00 42.21           N  
ATOM   7376  CA  LEU A1145     211.355 212.384 119.856  1.00 44.39           C  
ATOM   7377  C   LEU A1145     210.691 212.873 118.577  1.00 44.53           C  
ATOM   7378  O   LEU A1145     211.213 212.673 117.479  1.00 43.76           O  
ATOM   7379  CB  LEU A1145     210.739 211.038 120.250  1.00 42.70           C  
ATOM   7380  CG  LEU A1145     211.374 210.307 121.438  1.00 41.92           C  
ATOM   7381  CD1 LEU A1145     210.465 209.172 121.831  1.00 42.23           C  
ATOM   7382  CD2 LEU A1145     212.757 209.773 121.082  1.00 43.50           C  
ATOM   7383  N   ASP A1146     209.545 213.534 118.732  1.00 43.01           N  
ATOM   7384  CA  ASP A1146     208.786 214.054 117.594  1.00 43.92           C  
ATOM   7385  C   ASP A1146     209.423 215.295 116.947  1.00 44.31           C  
ATOM   7386  O   ASP A1146     209.383 215.438 115.722  1.00 44.68           O  
ATOM   7387  CB  ASP A1146     207.359 214.397 118.026  1.00 43.96           C  
ATOM   7388  N   SER A1147     210.015 216.184 117.768  1.00 43.96           N  
ATOM   7389  CA  SER A1147     210.673 217.407 117.318  1.00 44.40           C  
ATOM   7390  C   SER A1147     212.065 217.080 116.767  1.00 44.84           C  
ATOM   7391  O   SER A1147     212.478 217.600 115.726  1.00 44.74           O  
ATOM   7392  CB  SER A1147     210.765 218.408 118.473  1.00 44.75           C  
ATOM   7393  OG  SER A1147     211.456 219.568 118.096  1.00 44.86           O  
TER    7394      SER A1147                                                      
ATOM   7395  N   ALA B  27     192.129 155.190 221.632  1.00 57.41           N  
ATOM   7396  CA  ALA B  27     191.413 155.543 220.415  1.00 56.36           C  
ATOM   7397  C   ALA B  27     191.360 157.064 220.268  1.00 55.35           C  
ATOM   7398  O   ALA B  27     191.123 157.772 221.253  1.00 57.55           O  
ATOM   7399  CB  ALA B  27     189.993 154.965 220.434  1.00 56.02           C  
ATOM   7400  N   TYR B  28     191.595 157.561 219.039  1.00 56.19           N  
ATOM   7401  CA  TYR B  28     191.588 158.994 218.713  1.00 56.19           C  
ATOM   7402  C   TYR B  28     190.751 159.268 217.479  1.00 56.07           C  
ATOM   7403  O   TYR B  28     190.627 158.415 216.600  1.00 56.75           O  
ATOM   7404  CB  TYR B  28     193.008 159.509 218.506  1.00 55.83           C  
ATOM   7405  CG  TYR B  28     193.855 159.387 219.725  1.00 56.08           C  
ATOM   7406  CD1 TYR B  28     194.546 158.219 219.968  1.00 56.31           C  
ATOM   7407  CD2 TYR B  28     193.941 160.438 220.606  1.00 57.39           C  
ATOM   7408  CE1 TYR B  28     195.321 158.102 221.092  1.00 56.34           C  
ATOM   7409  CE2 TYR B  28     194.721 160.326 221.731  1.00 56.84           C  
ATOM   7410  CZ  TYR B  28     195.408 159.161 221.976  1.00 56.55           C  
ATOM   7411  OH  TYR B  28     196.189 159.045 223.102  1.00 55.22           O  
ATOM   7412  N   THR B  29     190.202 160.473 217.414  1.00 56.36           N  
ATOM   7413  CA  THR B  29     189.406 160.924 216.282  1.00 56.64           C  
ATOM   7414  C   THR B  29     189.900 162.278 215.766  1.00 56.57           C  
ATOM   7415  O   THR B  29     190.589 163.017 216.472  1.00 56.58           O  
ATOM   7416  CB  THR B  29     187.911 160.937 216.674  1.00 56.77           C  
ATOM   7417  OG1 THR B  29     187.521 159.592 216.966  1.00 57.34           O  
ATOM   7418  CG2 THR B  29     187.005 161.478 215.578  1.00 57.33           C  
ATOM   7419  N   ASN B  30     189.613 162.552 214.496  1.00 56.41           N  
ATOM   7420  CA  ASN B  30     190.002 163.788 213.820  1.00 56.08           C  
ATOM   7421  C   ASN B  30     189.048 164.930 214.172  1.00 55.40           C  
ATOM   7422  O   ASN B  30     187.850 164.852 213.905  1.00 55.91           O  
ATOM   7423  CB  ASN B  30     190.036 163.555 212.318  1.00 55.91           C  
ATOM   7424  CG  ASN B  30     190.646 164.678 211.523  1.00 55.13           C  
ATOM   7425  OD1 ASN B  30     190.658 165.850 211.914  1.00 55.42           O  
ATOM   7426  ND2 ASN B  30     191.169 164.322 210.374  1.00 55.72           N  
ATOM   7427  N   SER B  31     189.579 165.979 214.793  1.00 55.17           N  
ATOM   7428  CA  SER B  31     188.794 167.141 215.215  1.00 55.63           C  
ATOM   7429  C   SER B  31     188.353 168.030 214.058  1.00 55.18           C  
ATOM   7430  O   SER B  31     187.498 168.905 214.224  1.00 55.78           O  
ATOM   7431  CB  SER B  31     189.605 167.990 216.150  1.00 54.75           C  
ATOM   7432  OG  SER B  31     190.692 168.534 215.475  1.00 54.22           O  
ATOM   7433  N   PHE B  32     188.961 167.825 212.905  1.00 55.08           N  
ATOM   7434  CA  PHE B  32     188.709 168.620 211.717  1.00 55.23           C  
ATOM   7435  C   PHE B  32     188.824 170.114 211.994  1.00 53.80           C  
ATOM   7436  O   PHE B  32     189.888 170.605 212.363  1.00 49.72           O  
ATOM   7437  CB  PHE B  32     187.339 168.294 211.142  1.00 54.44           C  
ATOM   7438  CG  PHE B  32     187.232 166.901 210.659  1.00 55.85           C  
ATOM   7439  CD1 PHE B  32     186.538 165.965 211.388  1.00 56.12           C  
ATOM   7440  CD2 PHE B  32     187.829 166.514 209.480  1.00 56.12           C  
ATOM   7441  CE1 PHE B  32     186.435 164.672 210.952  1.00 56.37           C  
ATOM   7442  CE2 PHE B  32     187.731 165.220 209.037  1.00 55.83           C  
ATOM   7443  CZ  PHE B  32     187.032 164.296 209.774  1.00 56.33           C  
ATOM   7444  N   THR B  33     187.730 170.843 211.815  1.00 55.08           N  
ATOM   7445  CA  THR B  33     187.743 172.290 211.976  1.00 54.04           C  
ATOM   7446  C   THR B  33     186.863 172.761 213.125  1.00 54.13           C  
ATOM   7447  O   THR B  33     186.447 173.918 213.168  1.00 55.33           O  
ATOM   7448  CB  THR B  33     187.299 172.960 210.680  1.00 54.63           C  
ATOM   7449  OG1 THR B  33     185.986 172.504 210.340  1.00 55.14           O  
ATOM   7450  CG2 THR B  33     188.268 172.592 209.568  1.00 55.01           C  
ATOM   7451  N   ARG B  34     186.541 171.858 214.039  1.00 54.34           N  
ATOM   7452  CA  ARG B  34     185.704 172.187 215.184  1.00 54.57           C  
ATOM   7453  C   ARG B  34     186.520 172.833 216.294  1.00 54.80           C  
ATOM   7454  O   ARG B  34     187.741 172.715 216.323  1.00 54.59           O  
ATOM   7455  CB  ARG B  34     184.999 170.947 215.697  1.00 54.86           C  
ATOM   7456  CG  ARG B  34     184.010 170.382 214.711  1.00 55.20           C  
ATOM   7457  CD  ARG B  34     183.235 169.252 215.253  1.00 55.82           C  
ATOM   7458  NE  ARG B  34     182.303 168.767 214.268  1.00 57.05           N  
ATOM   7459  CZ  ARG B  34     181.081 169.280 214.031  1.00 57.25           C  
ATOM   7460  NH1 ARG B  34     180.614 170.299 214.722  1.00 56.93           N  
ATOM   7461  NH2 ARG B  34     180.359 168.737 213.083  1.00 57.48           N  
ATOM   7462  N   GLY B  35     185.845 173.510 217.223  1.00 54.99           N  
ATOM   7463  CA  GLY B  35     186.534 174.088 218.374  1.00 55.17           C  
ATOM   7464  C   GLY B  35     186.642 175.605 218.323  1.00 55.47           C  
ATOM   7465  O   GLY B  35     187.380 176.213 219.105  1.00 55.39           O  
ATOM   7466  N   VAL B  36     185.921 176.206 217.388  1.00 54.95           N  
ATOM   7467  CA  VAL B  36     185.856 177.651 217.251  1.00 55.36           C  
ATOM   7468  C   VAL B  36     184.656 178.193 218.002  1.00 55.54           C  
ATOM   7469  O   VAL B  36     183.592 177.580 218.026  1.00 55.82           O  
ATOM   7470  CB  VAL B  36     185.828 178.076 215.773  1.00 54.48           C  
ATOM   7471  CG1 VAL B  36     185.589 179.589 215.646  1.00 54.67           C  
ATOM   7472  CG2 VAL B  36     187.169 177.717 215.152  1.00 54.54           C  
ATOM   7473  N   TYR B  37     184.859 179.317 218.656  1.00 55.77           N  
ATOM   7474  CA  TYR B  37     183.832 179.982 219.426  1.00 56.00           C  
ATOM   7475  C   TYR B  37     184.028 181.479 219.343  1.00 55.78           C  
ATOM   7476  O   TYR B  37     185.101 181.949 218.967  1.00 56.61           O  
ATOM   7477  CB  TYR B  37     183.882 179.514 220.873  1.00 55.92           C  
ATOM   7478  CG  TYR B  37     185.166 179.835 221.524  1.00 55.61           C  
ATOM   7479  CD1 TYR B  37     185.329 181.021 222.179  1.00 57.34           C  
ATOM   7480  CD2 TYR B  37     186.193 178.936 221.459  1.00 55.91           C  
ATOM   7481  CE1 TYR B  37     186.517 181.317 222.769  1.00 56.80           C  
ATOM   7482  CE2 TYR B  37     187.382 179.227 222.049  1.00 55.65           C  
ATOM   7483  CZ  TYR B  37     187.545 180.416 222.701  1.00 55.78           C  
ATOM   7484  OH  TYR B  37     188.729 180.712 223.286  1.00 55.66           O  
ATOM   7485  N   TYR B  38     183.001 182.229 219.696  1.00 55.37           N  
ATOM   7486  CA  TYR B  38     183.107 183.677 219.672  1.00 55.01           C  
ATOM   7487  C   TYR B  38     184.047 184.123 220.790  1.00 55.44           C  
ATOM   7488  O   TYR B  38     183.716 183.951 221.959  1.00 57.22           O  
ATOM   7489  CB  TYR B  38     181.731 184.305 219.871  1.00 55.78           C  
ATOM   7490  CG  TYR B  38     180.787 184.008 218.758  1.00 55.71           C  
ATOM   7491  CD1 TYR B  38     180.023 182.883 218.834  1.00 56.16           C  
ATOM   7492  CD2 TYR B  38     180.676 184.845 217.675  1.00 55.04           C  
ATOM   7493  CE1 TYR B  38     179.153 182.563 217.844  1.00 55.88           C  
ATOM   7494  CE2 TYR B  38     179.790 184.533 216.668  1.00 54.95           C  
ATOM   7495  CZ  TYR B  38     179.033 183.387 216.757  1.00 54.96           C  
ATOM   7496  OH  TYR B  38     178.149 183.062 215.770  1.00 54.78           O  
ATOM   7497  N   PRO B  39     185.205 184.724 220.471  1.00 55.93           N  
ATOM   7498  CA  PRO B  39     186.262 185.070 221.406  1.00 55.76           C  
ATOM   7499  C   PRO B  39     185.843 186.132 222.418  1.00 56.62           C  
ATOM   7500  O   PRO B  39     186.413 186.222 223.504  1.00 57.04           O  
ATOM   7501  CB  PRO B  39     187.363 185.590 220.476  1.00 55.23           C  
ATOM   7502  CG  PRO B  39     186.634 186.063 219.237  1.00 55.40           C  
ATOM   7503  CD  PRO B  39     185.457 185.135 219.089  1.00 55.61           C  
ATOM   7504  N   ASP B  40     184.836 186.926 222.074  1.00 56.58           N  
ATOM   7505  CA  ASP B  40     184.348 187.959 222.970  1.00 56.56           C  
ATOM   7506  C   ASP B  40     182.861 188.190 222.747  1.00 56.75           C  
ATOM   7507  O   ASP B  40     182.185 187.378 222.113  1.00 56.50           O  
ATOM   7508  CB  ASP B  40     185.156 189.251 222.818  1.00 56.36           C  
ATOM   7509  CG  ASP B  40     185.076 189.894 221.449  1.00 56.32           C  
ATOM   7510  OD1 ASP B  40     184.154 189.615 220.705  1.00 56.25           O  
ATOM   7511  OD2 ASP B  40     185.952 190.679 221.149  1.00 56.24           O  
ATOM   7512  N   LYS B  41     182.340 189.275 223.309  1.00 56.92           N  
ATOM   7513  CA  LYS B  41     180.918 189.565 223.233  1.00 57.20           C  
ATOM   7514  C   LYS B  41     180.647 190.793 222.378  1.00 57.63           C  
ATOM   7515  O   LYS B  41     179.704 191.553 222.627  1.00 58.81           O  
ATOM   7516  CB  LYS B  41     180.353 189.719 224.636  1.00 58.50           C  
ATOM   7517  CG  LYS B  41     180.471 188.440 225.453  1.00 59.05           C  
ATOM   7518  CD  LYS B  41     179.721 188.526 226.751  1.00 60.47           C  
ATOM   7519  CE  LYS B  41     179.734 187.192 227.469  1.00 61.12           C  
ATOM   7520  NZ  LYS B  41     179.011 187.248 228.764  1.00 61.87           N  
ATOM   7521  N   VAL B  42     181.503 191.008 221.382  1.00 57.35           N  
ATOM   7522  CA  VAL B  42     181.357 192.135 220.478  1.00 55.50           C  
ATOM   7523  C   VAL B  42     180.813 191.708 219.123  1.00 54.88           C  
ATOM   7524  O   VAL B  42     181.304 190.765 218.503  1.00 56.49           O  
ATOM   7525  CB  VAL B  42     182.703 192.846 220.309  1.00 55.39           C  
ATOM   7526  CG1 VAL B  42     182.586 193.971 219.308  1.00 56.17           C  
ATOM   7527  CG2 VAL B  42     183.139 193.386 221.651  1.00 55.86           C  
ATOM   7528  N   PHE B  43     179.788 192.404 218.666  1.00 55.77           N  
ATOM   7529  CA  PHE B  43     179.194 192.111 217.376  1.00 56.16           C  
ATOM   7530  C   PHE B  43     180.063 192.611 216.236  1.00 56.55           C  
ATOM   7531  O   PHE B  43     180.503 193.764 216.216  1.00 56.87           O  
ATOM   7532  CB  PHE B  43     177.804 192.722 217.255  1.00 56.33           C  
ATOM   7533  CG  PHE B  43     177.150 192.438 215.944  1.00 55.87           C  
ATOM   7534  CD1 PHE B  43     176.523 191.236 215.709  1.00 57.56           C  
ATOM   7535  CD2 PHE B  43     177.171 193.369 214.936  1.00 56.16           C  
ATOM   7536  CE1 PHE B  43     175.927 190.970 214.506  1.00 56.79           C  
ATOM   7537  CE2 PHE B  43     176.578 193.106 213.726  1.00 56.36           C  
ATOM   7538  CZ  PHE B  43     175.953 191.902 213.514  1.00 56.13           C  
ATOM   7539  N   ARG B  44     180.284 191.741 215.270  1.00 54.89           N  
ATOM   7540  CA  ARG B  44     181.029 192.069 214.071  1.00 54.05           C  
ATOM   7541  C   ARG B  44     180.272 191.488 212.910  1.00 54.28           C  
ATOM   7542  O   ARG B  44     179.595 190.483 213.082  1.00 55.02           O  
ATOM   7543  CB  ARG B  44     182.425 191.480 214.114  1.00 53.87           C  
ATOM   7544  CG  ARG B  44     183.292 192.005 215.220  1.00 54.23           C  
ATOM   7545  CD  ARG B  44     184.632 191.387 215.211  1.00 53.26           C  
ATOM   7546  NE  ARG B  44     185.462 191.912 216.274  1.00 53.16           N  
ATOM   7547  CZ  ARG B  44     185.399 191.490 217.554  1.00 54.45           C  
ATOM   7548  NH1 ARG B  44     184.535 190.554 217.893  1.00 55.23           N  
ATOM   7549  NH2 ARG B  44     186.192 192.011 218.474  1.00 54.02           N  
ATOM   7550  N   SER B  45     180.388 192.086 211.737  1.00 54.16           N  
ATOM   7551  CA  SER B  45     179.742 191.515 210.563  1.00 53.66           C  
ATOM   7552  C   SER B  45     180.520 191.807 209.300  1.00 53.61           C  
ATOM   7553  O   SER B  45     181.185 192.837 209.196  1.00 53.22           O  
ATOM   7554  CB  SER B  45     178.337 192.059 210.430  1.00 54.24           C  
ATOM   7555  OG  SER B  45     178.354 193.446 210.216  1.00 54.88           O  
ATOM   7556  N   SER B  46     180.415 190.898 208.336  1.00 52.91           N  
ATOM   7557  CA  SER B  46     181.044 191.055 207.026  1.00 53.03           C  
ATOM   7558  C   SER B  46     182.508 191.462 207.155  1.00 52.35           C  
ATOM   7559  O   SER B  46     182.949 192.435 206.540  1.00 52.64           O  
ATOM   7560  CB  SER B  46     180.293 192.081 206.202  1.00 53.36           C  
ATOM   7561  OG  SER B  46     178.966 191.686 205.996  1.00 53.55           O  
ATOM   7562  N   VAL B  47     183.248 190.749 207.991  1.00 52.25           N  
ATOM   7563  CA  VAL B  47     184.632 191.109 208.258  1.00 51.71           C  
ATOM   7564  C   VAL B  47     185.500 189.911 208.590  1.00 51.05           C  
ATOM   7565  O   VAL B  47     185.047 188.954 209.221  1.00 51.61           O  
ATOM   7566  CB  VAL B  47     184.679 192.140 209.410  1.00 51.28           C  
ATOM   7567  CG1 VAL B  47     184.155 191.516 210.687  1.00 51.94           C  
ATOM   7568  CG2 VAL B  47     186.105 192.662 209.627  1.00 50.77           C  
ATOM   7569  N   LEU B  48     186.768 189.985 208.207  1.00 50.60           N  
ATOM   7570  CA  LEU B  48     187.733 188.979 208.608  1.00 50.35           C  
ATOM   7571  C   LEU B  48     188.536 189.531 209.773  1.00 50.09           C  
ATOM   7572  O   LEU B  48     189.252 190.523 209.631  1.00 50.25           O  
ATOM   7573  CB  LEU B  48     188.653 188.614 207.446  1.00 50.28           C  
ATOM   7574  CG  LEU B  48     187.966 188.221 206.136  1.00 50.71           C  
ATOM   7575  CD1 LEU B  48     189.019 187.843 205.143  1.00 49.99           C  
ATOM   7576  CD2 LEU B  48     187.003 187.089 206.371  1.00 50.87           C  
ATOM   7577  N   HIS B  49     188.379 188.919 210.934  1.00 50.30           N  
ATOM   7578  CA  HIS B  49     188.988 189.419 212.161  1.00 50.12           C  
ATOM   7579  C   HIS B  49     190.046 188.484 212.719  1.00 51.30           C  
ATOM   7580  O   HIS B  49     189.808 187.290 212.888  1.00 50.32           O  
ATOM   7581  CB  HIS B  49     187.914 189.654 213.217  1.00 50.73           C  
ATOM   7582  CG  HIS B  49     188.453 190.103 214.516  1.00 51.27           C  
ATOM   7583  ND1 HIS B  49     188.986 191.355 214.706  1.00 51.58           N  
ATOM   7584  CD2 HIS B  49     188.545 189.468 215.704  1.00 51.90           C  
ATOM   7585  CE1 HIS B  49     189.390 191.470 215.958  1.00 51.62           C  
ATOM   7586  NE2 HIS B  49     189.131 190.340 216.584  1.00 52.10           N  
ATOM   7587  N   SER B  50     191.222 189.027 212.997  1.00 50.65           N  
ATOM   7588  CA  SER B  50     192.321 188.235 213.541  1.00 50.58           C  
ATOM   7589  C   SER B  50     192.361 188.307 215.057  1.00 50.77           C  
ATOM   7590  O   SER B  50     192.420 189.395 215.631  1.00 51.28           O  
ATOM   7591  CB  SER B  50     193.640 188.707 212.975  1.00 50.19           C  
ATOM   7592  OG  SER B  50     194.711 188.056 213.598  1.00 51.07           O  
ATOM   7593  N   THR B  51     192.340 187.148 215.703  1.00 51.04           N  
ATOM   7594  CA  THR B  51     192.351 187.085 217.160  1.00 51.54           C  
ATOM   7595  C   THR B  51     193.203 185.932 217.680  1.00 51.69           C  
ATOM   7596  O   THR B  51     193.365 184.913 217.008  1.00 53.57           O  
ATOM   7597  CB  THR B  51     190.919 186.930 217.693  1.00 52.09           C  
ATOM   7598  OG1 THR B  51     190.921 187.036 219.118  1.00 52.65           O  
ATOM   7599  CG2 THR B  51     190.361 185.575 217.295  1.00 51.89           C  
ATOM   7600  N   GLN B  52     193.728 186.076 218.892  1.00 52.40           N  
ATOM   7601  CA  GLN B  52     194.464 184.983 219.519  1.00 52.85           C  
ATOM   7602  C   GLN B  52     193.809 184.590 220.825  1.00 53.60           C  
ATOM   7603  O   GLN B  52     193.559 185.437 221.681  1.00 53.61           O  
ATOM   7604  CB  GLN B  52     195.923 185.354 219.762  1.00 52.78           C  
ATOM   7605  CG  GLN B  52     196.743 184.225 220.371  1.00 53.11           C  
ATOM   7606  CD  GLN B  52     198.193 184.578 220.486  1.00 53.56           C  
ATOM   7607  OE1 GLN B  52     198.548 185.759 220.451  1.00 53.10           O  
ATOM   7608  NE2 GLN B  52     199.053 183.576 220.621  1.00 54.42           N  
ATOM   7609  N   ASP B  53     193.507 183.308 220.960  1.00 53.49           N  
ATOM   7610  CA  ASP B  53     192.830 182.807 222.151  1.00 54.60           C  
ATOM   7611  C   ASP B  53     193.038 181.309 222.259  1.00 55.65           C  
ATOM   7612  O   ASP B  53     193.674 180.707 221.399  1.00 55.26           O  
ATOM   7613  CB  ASP B  53     191.330 183.152 222.109  1.00 55.16           C  
ATOM   7614  N   LEU B  54     192.486 180.699 223.289  1.00 54.92           N  
ATOM   7615  CA  LEU B  54     192.603 179.261 223.432  1.00 56.42           C  
ATOM   7616  C   LEU B  54     191.542 178.554 222.601  1.00 54.46           C  
ATOM   7617  O   LEU B  54     190.365 178.546 222.950  1.00 57.27           O  
ATOM   7618  CB  LEU B  54     192.459 178.853 224.906  1.00 55.95           C  
ATOM   7619  CG  LEU B  54     193.500 179.375 225.900  1.00 56.84           C  
ATOM   7620  CD1 LEU B  54     193.119 178.901 227.304  1.00 59.18           C  
ATOM   7621  CD2 LEU B  54     194.874 178.850 225.522  1.00 56.64           C  
ATOM   7622  N   PHE B  55     191.971 177.968 221.491  1.00 55.73           N  
ATOM   7623  CA  PHE B  55     191.088 177.299 220.537  1.00 55.01           C  
ATOM   7624  C   PHE B  55     191.560 175.882 220.307  1.00 55.19           C  
ATOM   7625  O   PHE B  55     192.731 175.580 220.534  1.00 55.53           O  
ATOM   7626  CB  PHE B  55     191.078 177.987 219.181  1.00 54.08           C  
ATOM   7627  CG  PHE B  55     190.511 179.370 219.101  1.00 54.06           C  
ATOM   7628  CD1 PHE B  55     191.333 180.475 219.144  1.00 53.70           C  
ATOM   7629  CD2 PHE B  55     189.154 179.564 218.943  1.00 54.74           C  
ATOM   7630  CE1 PHE B  55     190.814 181.743 219.028  1.00 53.76           C  
ATOM   7631  CE2 PHE B  55     188.629 180.835 218.833  1.00 54.65           C  
ATOM   7632  CZ  PHE B  55     189.464 181.923 218.874  1.00 54.24           C  
ATOM   7633  N   LEU B  56     190.671 175.004 219.860  1.00 54.60           N  
ATOM   7634  CA  LEU B  56     191.128 173.658 219.530  1.00 54.65           C  
ATOM   7635  C   LEU B  56     191.915 173.738 218.216  1.00 54.51           C  
ATOM   7636  O   LEU B  56     191.377 174.243 217.233  1.00 54.61           O  
ATOM   7637  CB  LEU B  56     189.942 172.718 219.335  1.00 55.08           C  
ATOM   7638  CG  LEU B  56     190.243 171.222 219.180  1.00 55.06           C  
ATOM   7639  CD1 LEU B  56     190.782 170.665 220.480  1.00 55.80           C  
ATOM   7640  CD2 LEU B  56     188.973 170.508 218.787  1.00 55.31           C  
ATOM   7641  N   PRO B  57     193.173 173.279 218.148  1.00 53.66           N  
ATOM   7642  CA  PRO B  57     193.997 173.303 216.954  1.00 52.68           C  
ATOM   7643  C   PRO B  57     193.308 172.525 215.853  1.00 53.49           C  
ATOM   7644  O   PRO B  57     192.734 171.463 216.111  1.00 54.45           O  
ATOM   7645  CB  PRO B  57     195.269 172.588 217.411  1.00 53.56           C  
ATOM   7646  CG  PRO B  57     195.293 172.758 218.902  1.00 53.86           C  
ATOM   7647  CD  PRO B  57     193.847 172.731 219.328  1.00 55.13           C  
ATOM   7648  N   PHE B  58     193.382 173.022 214.627  1.00 52.79           N  
ATOM   7649  CA  PHE B  58     192.717 172.311 213.549  1.00 52.89           C  
ATOM   7650  C   PHE B  58     193.401 171.000 213.228  1.00 53.17           C  
ATOM   7651  O   PHE B  58     194.625 170.878 213.294  1.00 52.59           O  
ATOM   7652  CB  PHE B  58     192.591 173.184 212.306  1.00 52.64           C  
ATOM   7653  CG  PHE B  58     191.427 174.152 212.321  1.00 52.65           C  
ATOM   7654  CD1 PHE B  58     190.620 174.344 213.445  1.00 53.87           C  
ATOM   7655  CD2 PHE B  58     191.116 174.857 211.177  1.00 53.05           C  
ATOM   7656  CE1 PHE B  58     189.552 175.200 213.400  1.00 53.60           C  
ATOM   7657  CE2 PHE B  58     190.046 175.722 211.143  1.00 52.28           C  
ATOM   7658  CZ  PHE B  58     189.265 175.887 212.253  1.00 53.46           C  
ATOM   7659  N   PHE B  59     192.568 170.010 212.936  1.00 53.48           N  
ATOM   7660  CA  PHE B  59     192.951 168.654 212.585  1.00 53.88           C  
ATOM   7661  C   PHE B  59     193.742 167.941 213.669  1.00 53.69           C  
ATOM   7662  O   PHE B  59     194.425 166.956 213.391  1.00 53.90           O  
ATOM   7663  CB  PHE B  59     193.702 168.654 211.261  1.00 52.95           C  
ATOM   7664  CG  PHE B  59     192.842 169.164 210.157  1.00 53.17           C  
ATOM   7665  CD1 PHE B  59     192.956 170.457 209.718  1.00 52.69           C  
ATOM   7666  CD2 PHE B  59     191.899 168.348 209.568  1.00 53.74           C  
ATOM   7667  CE1 PHE B  59     192.146 170.938 208.717  1.00 53.13           C  
ATOM   7668  CE2 PHE B  59     191.088 168.820 208.563  1.00 53.95           C  
ATOM   7669  CZ  PHE B  59     191.211 170.119 208.140  1.00 53.85           C  
ATOM   7670  N   SER B  60     193.606 168.398 214.911  1.00 53.54           N  
ATOM   7671  CA  SER B  60     194.239 167.735 216.041  1.00 53.94           C  
ATOM   7672  C   SER B  60     193.516 166.440 216.415  1.00 54.99           C  
ATOM   7673  O   SER B  60     192.386 166.197 215.970  1.00 54.99           O  
ATOM   7674  CB  SER B  60     194.286 168.667 217.237  1.00 54.08           C  
ATOM   7675  OG  SER B  60     193.005 168.945 217.727  1.00 54.46           O  
ATOM   7676  N   ASN B  61     194.188 165.614 217.239  1.00 55.60           N  
ATOM   7677  CA  ASN B  61     193.663 164.366 217.789  1.00 55.72           C  
ATOM   7678  C   ASN B  61     192.885 164.623 219.082  1.00 56.00           C  
ATOM   7679  O   ASN B  61     193.421 165.215 220.026  1.00 56.21           O  
ATOM   7680  CB  ASN B  61     194.798 163.367 218.055  1.00 56.30           C  
ATOM   7681  CG  ASN B  61     195.211 162.525 216.843  1.00 56.58           C  
ATOM   7682  OD1 ASN B  61     194.848 162.816 215.693  1.00 56.15           O  
ATOM   7683  ND2 ASN B  61     195.983 161.477 217.115  1.00 56.18           N  
ATOM   7684  N   VAL B  62     191.635 164.136 219.140  1.00 55.94           N  
ATOM   7685  CA  VAL B  62     190.797 164.198 220.338  1.00 56.20           C  
ATOM   7686  C   VAL B  62     190.585 162.778 220.812  1.00 56.89           C  
ATOM   7687  O   VAL B  62     190.297 161.887 220.009  1.00 56.63           O  
ATOM   7688  CB  VAL B  62     189.454 164.921 220.074  1.00 56.72           C  
ATOM   7689  CG1 VAL B  62     189.736 166.355 219.720  1.00 57.18           C  
ATOM   7690  CG2 VAL B  62     188.671 164.250 218.944  1.00 56.55           C  
ATOM   7691  N   THR B  63     190.789 162.550 222.100  1.00 56.93           N  
ATOM   7692  CA  THR B  63     190.701 161.200 222.623  1.00 56.09           C  
ATOM   7693  C   THR B  63     189.263 160.747 222.592  1.00 59.38           C  
ATOM   7694  O   THR B  63     188.371 161.465 223.033  1.00 56.85           O  
ATOM   7695  CB  THR B  63     191.260 161.119 224.046  1.00 57.21           C  
ATOM   7696  OG1 THR B  63     192.599 161.617 224.060  1.00 56.84           O  
ATOM   7697  CG2 THR B  63     191.275 159.678 224.510  1.00 57.69           C  
ATOM   7698  N   TRP B  64     189.037 159.566 222.043  1.00 58.93           N  
ATOM   7699  CA  TRP B  64     187.698 159.032 221.862  1.00 59.66           C  
ATOM   7700  C   TRP B  64     187.321 158.011 222.926  1.00 59.54           C  
ATOM   7701  O   TRP B  64     187.932 156.949 223.039  1.00 58.89           O  
ATOM   7702  CB  TRP B  64     187.600 158.421 220.473  1.00 58.83           C  
ATOM   7703  CG  TRP B  64     186.298 157.809 220.147  1.00 58.64           C  
ATOM   7704  CD1 TRP B  64     185.084 158.061 220.700  1.00 59.15           C  
ATOM   7705  CD2 TRP B  64     186.077 156.813 219.149  1.00 57.42           C  
ATOM   7706  NE1 TRP B  64     184.135 157.283 220.115  1.00 61.11           N  
ATOM   7707  CE2 TRP B  64     184.720 156.513 219.168  1.00 57.96           C  
ATOM   7708  CE3 TRP B  64     186.911 156.157 218.249  1.00 58.30           C  
ATOM   7709  CZ2 TRP B  64     184.171 155.579 218.324  1.00 59.16           C  
ATOM   7710  CZ3 TRP B  64     186.362 155.219 217.400  1.00 58.90           C  
ATOM   7711  CH2 TRP B  64     185.026 154.936 217.438  1.00 59.67           C  
ATOM   7712  N   PHE B  65     186.310 158.352 223.712  1.00 61.56           N  
ATOM   7713  CA  PHE B  65     185.846 157.530 224.817  1.00 60.38           C  
ATOM   7714  C   PHE B  65     184.432 157.005 224.562  1.00 62.09           C  
ATOM   7715  O   PHE B  65     183.627 157.671 223.903  1.00 61.65           O  
ATOM   7716  CB  PHE B  65     185.808 158.356 226.089  1.00 60.92           C  
ATOM   7717  CG  PHE B  65     187.095 158.899 226.529  1.00 61.52           C  
ATOM   7718  CD1 PHE B  65     187.461 160.169 226.159  1.00 61.20           C  
ATOM   7719  CD2 PHE B  65     187.941 158.166 227.325  1.00 59.48           C  
ATOM   7720  CE1 PHE B  65     188.642 160.697 226.576  1.00 58.73           C  
ATOM   7721  CE2 PHE B  65     189.132 158.695 227.744  1.00 61.35           C  
ATOM   7722  CZ  PHE B  65     189.480 159.964 227.369  1.00 60.97           C  
ATOM   7723  N   HIS B  66     184.109 155.843 225.154  1.00 59.86           N  
ATOM   7724  CA  HIS B  66     182.768 155.252 225.125  1.00 61.37           C  
ATOM   7725  C   HIS B  66     182.598 154.345 226.342  1.00 61.74           C  
ATOM   7726  O   HIS B  66     183.497 154.240 227.182  1.00 61.26           O  
ATOM   7727  CB  HIS B  66     182.523 154.465 223.806  1.00 61.26           C  
ATOM   7728  CG  HIS B  66     181.123 153.839 223.680  1.00 62.15           C  
ATOM   7729  ND1 HIS B  66     180.775 152.674 224.340  1.00 62.63           N  
ATOM   7730  CD2 HIS B  66     180.018 154.222 222.991  1.00 62.78           C  
ATOM   7731  CE1 HIS B  66     179.521 152.369 224.058  1.00 62.07           C  
ATOM   7732  NE2 HIS B  66     179.039 153.290 223.244  1.00 62.88           N  
ATOM   7733  N   ASN B  81     184.814 158.519 231.815  1.00 67.51           N  
ATOM   7734  CA  ASN B  81     184.995 157.500 232.833  1.00 68.58           C  
ATOM   7735  C   ASN B  81     186.282 157.760 233.664  1.00 69.07           C  
ATOM   7736  O   ASN B  81     186.157 157.932 234.883  1.00 69.82           O  
ATOM   7737  CB  ASN B  81     184.895 156.078 232.232  1.00 69.11           C  
ATOM   7738  N   PRO B  82     187.525 157.791 233.076  1.00 68.52           N  
ATOM   7739  CA  PRO B  82     188.775 158.102 233.759  1.00 68.71           C  
ATOM   7740  C   PRO B  82     188.846 159.578 234.071  1.00 68.00           C  
ATOM   7741  O   PRO B  82     188.176 160.382 233.426  1.00 67.86           O  
ATOM   7742  CB  PRO B  82     189.841 157.709 232.740  1.00 68.14           C  
ATOM   7743  CG  PRO B  82     189.176 157.903 231.410  1.00 67.88           C  
ATOM   7744  CD  PRO B  82     187.741 157.497 231.621  1.00 67.84           C  
ATOM   7745  N   VAL B  83     189.675 159.935 235.030  1.00 68.75           N  
ATOM   7746  CA  VAL B  83     189.871 161.336 235.335  1.00 67.59           C  
ATOM   7747  C   VAL B  83     190.961 161.878 234.412  1.00 67.01           C  
ATOM   7748  O   VAL B  83     192.045 161.302 234.316  1.00 66.96           O  
ATOM   7749  CB  VAL B  83     190.249 161.508 236.808  1.00 68.35           C  
ATOM   7750  CG1 VAL B  83     190.437 162.937 237.101  1.00 68.04           C  
ATOM   7751  CG2 VAL B  83     189.172 160.918 237.686  1.00 68.96           C  
ATOM   7752  N   LEU B  84     190.648 162.952 233.702  1.00 67.47           N  
ATOM   7753  CA  LEU B  84     191.526 163.502 232.683  1.00 66.56           C  
ATOM   7754  C   LEU B  84     192.140 164.839 233.103  1.00 66.59           C  
ATOM   7755  O   LEU B  84     191.576 165.532 233.942  1.00 65.55           O  
ATOM   7756  CB  LEU B  84     190.706 163.682 231.410  1.00 65.76           C  
ATOM   7757  CG  LEU B  84     190.003 162.413 230.899  1.00 65.64           C  
ATOM   7758  CD1 LEU B  84     189.119 162.777 229.748  1.00 64.23           C  
ATOM   7759  CD2 LEU B  84     191.032 161.380 230.469  1.00 66.16           C  
ATOM   7760  N   PRO B  85     193.297 165.222 232.556  1.00 65.36           N  
ATOM   7761  CA  PRO B  85     193.908 166.534 232.688  1.00 66.30           C  
ATOM   7762  C   PRO B  85     193.008 167.613 232.111  1.00 63.81           C  
ATOM   7763  O   PRO B  85     192.244 167.352 231.189  1.00 64.54           O  
ATOM   7764  CB  PRO B  85     195.182 166.401 231.849  1.00 64.78           C  
ATOM   7765  CG  PRO B  85     195.468 164.923 231.804  1.00 64.88           C  
ATOM   7766  CD  PRO B  85     194.113 164.254 231.815  1.00 65.20           C  
ATOM   7767  N   PHE B  86     193.110 168.823 232.643  1.00 64.67           N  
ATOM   7768  CA  PHE B  86     192.368 169.961 232.109  1.00 64.89           C  
ATOM   7769  C   PHE B  86     193.286 170.853 231.273  1.00 64.50           C  
ATOM   7770  O   PHE B  86     192.863 171.464 230.295  1.00 62.29           O  
ATOM   7771  CB  PHE B  86     191.755 170.768 233.245  1.00 65.31           C  
ATOM   7772  CG  PHE B  86     190.808 171.857 232.829  1.00 65.77           C  
ATOM   7773  CD1 PHE B  86     189.502 171.567 232.453  1.00 63.68           C  
ATOM   7774  CD2 PHE B  86     191.212 173.178 232.839  1.00 64.96           C  
ATOM   7775  CE1 PHE B  86     188.635 172.575 232.096  1.00 63.89           C  
ATOM   7776  CE2 PHE B  86     190.342 174.181 232.485  1.00 63.63           C  
ATOM   7777  CZ  PHE B  86     189.054 173.877 232.115  1.00 63.54           C  
ATOM   7778  N   ASN B  87     194.548 170.923 231.680  1.00 63.09           N  
ATOM   7779  CA  ASN B  87     195.566 171.765 231.056  1.00 63.36           C  
ATOM   7780  C   ASN B  87     195.161 173.241 230.976  1.00 63.06           C  
ATOM   7781  O   ASN B  87     194.866 173.856 232.000  1.00 63.30           O  
ATOM   7782  CB  ASN B  87     195.937 171.221 229.688  1.00 62.41           C  
ATOM   7783  CG  ASN B  87     196.534 169.841 229.765  1.00 63.20           C  
ATOM   7784  OD1 ASN B  87     197.063 169.431 230.806  1.00 63.50           O  
ATOM   7785  ND2 ASN B  87     196.473 169.121 228.678  1.00 62.26           N  
ATOM   7786  N   ASP B  88     195.160 173.813 229.768  1.00 61.90           N  
ATOM   7787  CA  ASP B  88     194.851 175.232 229.588  1.00 61.54           C  
ATOM   7788  C   ASP B  88     193.357 175.445 229.476  1.00 61.58           C  
ATOM   7789  O   ASP B  88     192.824 176.488 229.861  1.00 61.83           O  
ATOM   7790  CB  ASP B  88     195.539 175.763 228.331  1.00 61.19           C  
ATOM   7791  CG  ASP B  88     197.048 175.742 228.439  1.00 61.43           C  
ATOM   7792  OD1 ASP B  88     197.584 176.515 229.196  1.00 62.26           O  
ATOM   7793  OD2 ASP B  88     197.658 174.933 227.782  1.00 60.99           O  
ATOM   7794  N   GLY B  89     192.693 174.438 228.952  1.00 60.86           N  
ATOM   7795  CA  GLY B  89     191.263 174.434 228.751  1.00 60.15           C  
ATOM   7796  C   GLY B  89     190.900 173.185 227.981  1.00 60.74           C  
ATOM   7797  O   GLY B  89     191.760 172.542 227.369  1.00 61.46           O  
ATOM   7798  N   VAL B  90     189.631 172.830 228.019  1.00 60.21           N  
ATOM   7799  CA  VAL B  90     189.182 171.595 227.413  1.00 58.91           C  
ATOM   7800  C   VAL B  90     188.089 171.730 226.394  1.00 58.15           C  
ATOM   7801  O   VAL B  90     187.068 172.377 226.619  1.00 59.67           O  
ATOM   7802  CB  VAL B  90     188.709 170.628 228.505  1.00 60.30           C  
ATOM   7803  CG1 VAL B  90     188.101 169.373 227.896  1.00 60.11           C  
ATOM   7804  CG2 VAL B  90     189.889 170.255 229.352  1.00 61.60           C  
ATOM   7805  N   TYR B  91     188.296 171.071 225.277  1.00 58.40           N  
ATOM   7806  CA  TYR B  91     187.261 170.960 224.280  1.00 57.98           C  
ATOM   7807  C   TYR B  91     186.549 169.656 224.520  1.00 59.66           C  
ATOM   7808  O   TYR B  91     187.175 168.599 224.575  1.00 58.85           O  
ATOM   7809  CB  TYR B  91     187.811 170.973 222.878  1.00 57.24           C  
ATOM   7810  CG  TYR B  91     186.745 170.724 221.879  1.00 56.88           C  
ATOM   7811  CD1 TYR B  91     185.906 171.740 221.507  1.00 56.50           C  
ATOM   7812  CD2 TYR B  91     186.591 169.463 221.343  1.00 57.12           C  
ATOM   7813  CE1 TYR B  91     184.916 171.506 220.591  1.00 56.59           C  
ATOM   7814  CE2 TYR B  91     185.603 169.230 220.425  1.00 57.24           C  
ATOM   7815  CZ  TYR B  91     184.770 170.250 220.050  1.00 56.96           C  
ATOM   7816  OH  TYR B  91     183.792 170.028 219.130  1.00 56.54           O  
ATOM   7817  N   PHE B  92     185.251 169.709 224.666  1.00 57.77           N  
ATOM   7818  CA  PHE B  92     184.515 168.494 224.938  1.00 59.17           C  
ATOM   7819  C   PHE B  92     183.371 168.356 223.974  1.00 58.94           C  
ATOM   7820  O   PHE B  92     182.646 169.311 223.720  1.00 51.72           O  
ATOM   7821  CB  PHE B  92     183.967 168.508 226.359  1.00 58.39           C  
ATOM   7822  CG  PHE B  92     183.270 167.253 226.744  1.00 59.17           C  
ATOM   7823  CD1 PHE B  92     183.958 166.255 227.383  1.00 60.23           C  
ATOM   7824  CD2 PHE B  92     181.937 167.056 226.455  1.00 59.52           C  
ATOM   7825  CE1 PHE B  92     183.335 165.089 227.731  1.00 59.91           C  
ATOM   7826  CE2 PHE B  92     181.310 165.889 226.798  1.00 59.98           C  
ATOM   7827  CZ  PHE B  92     182.013 164.906 227.438  1.00 60.02           C  
ATOM   7828  N   ALA B  93     183.178 167.171 223.448  1.00 58.81           N  
ATOM   7829  CA  ALA B  93     182.033 166.974 222.586  1.00 58.76           C  
ATOM   7830  C   ALA B  93     181.471 165.597 222.780  1.00 60.59           C  
ATOM   7831  O   ALA B  93     182.199 164.652 223.061  1.00 58.02           O  
ATOM   7832  CB  ALA B  93     182.411 167.193 221.131  1.00 58.00           C  
ATOM   7833  N   SER B  94     180.179 165.460 222.591  1.00 59.79           N  
ATOM   7834  CA  SER B  94     179.580 164.149 222.695  1.00 59.23           C  
ATOM   7835  C   SER B  94     178.476 163.950 221.695  1.00 60.94           C  
ATOM   7836  O   SER B  94     177.805 164.895 221.280  1.00 61.67           O  
ATOM   7837  CB  SER B  94     179.049 163.940 224.095  1.00 59.92           C  
ATOM   7838  OG  SER B  94     178.013 164.838 224.373  1.00 61.19           O  
ATOM   7839  N   THR B  95     178.272 162.699 221.333  1.00 61.39           N  
ATOM   7840  CA  THR B  95     177.193 162.307 220.454  1.00 62.23           C  
ATOM   7841  C   THR B  95     176.378 161.265 221.182  1.00 64.36           C  
ATOM   7842  O   THR B  95     176.879 160.185 221.514  1.00 64.19           O  
ATOM   7843  CB  THR B  95     177.728 161.747 219.132  1.00 63.72           C  
ATOM   7844  OG1 THR B  95     178.567 160.629 219.407  1.00 62.20           O  
ATOM   7845  CG2 THR B  95     178.523 162.798 218.406  1.00 62.46           C  
ATOM   7846  N   GLU B  96     175.118 161.581 221.443  1.00 64.13           N  
ATOM   7847  CA  GLU B  96     174.316 160.691 222.261  1.00 64.05           C  
ATOM   7848  C   GLU B  96     172.962 160.325 221.695  1.00 65.39           C  
ATOM   7849  O   GLU B  96     172.365 161.045 220.888  1.00 65.30           O  
ATOM   7850  CB  GLU B  96     174.129 161.288 223.643  1.00 65.21           C  
ATOM   7851  N   LYS B  97     172.481 159.175 222.145  1.00 65.26           N  
ATOM   7852  CA  LYS B  97     171.150 158.706 221.813  1.00 66.78           C  
ATOM   7853  C   LYS B  97     170.251 158.702 223.049  1.00 67.29           C  
ATOM   7854  O   LYS B  97     169.068 159.031 222.967  1.00 67.27           O  
ATOM   7855  CB  LYS B  97     171.226 157.306 221.205  1.00 67.37           C  
ATOM   7856  CG  LYS B  97     169.898 156.757 220.728  1.00 68.04           C  
ATOM   7857  CD  LYS B  97     170.080 155.428 220.016  1.00 68.67           C  
ATOM   7858  CE  LYS B  97     168.752 154.868 219.534  1.00 69.99           C  
ATOM   7859  NZ  LYS B  97     168.928 153.577 218.815  1.00 70.18           N  
ATOM   7860  N   SER B  98     170.818 158.313 224.196  1.00 67.27           N  
ATOM   7861  CA  SER B  98     170.048 158.172 225.430  1.00 66.98           C  
ATOM   7862  C   SER B  98     170.431 159.191 226.507  1.00 68.63           C  
ATOM   7863  O   SER B  98     170.021 159.059 227.660  1.00 68.68           O  
ATOM   7864  CB  SER B  98     170.205 156.767 225.974  1.00 69.61           C  
ATOM   7865  OG  SER B  98     171.526 156.508 226.334  1.00 67.71           O  
ATOM   7866  N   ASN B  99     171.224 160.195 226.138  1.00 66.56           N  
ATOM   7867  CA  ASN B  99     171.621 161.272 227.049  1.00 66.54           C  
ATOM   7868  C   ASN B  99     172.261 160.793 228.358  1.00 66.63           C  
ATOM   7869  O   ASN B  99     171.903 161.267 229.438  1.00 67.60           O  
ATOM   7870  CB  ASN B  99     170.423 162.148 227.350  1.00 67.27           C  
ATOM   7871  CG  ASN B  99     169.835 162.770 226.107  1.00 66.06           C  
ATOM   7872  OD1 ASN B  99     170.526 163.352 225.252  1.00 65.71           O  
ATOM   7873  ND2 ASN B  99     168.540 162.653 225.988  1.00 66.17           N  
ATOM   7874  N   ILE B 100     173.204 159.863 228.258  1.00 66.62           N  
ATOM   7875  CA  ILE B 100     173.900 159.324 229.427  1.00 66.93           C  
ATOM   7876  C   ILE B 100     174.739 160.350 230.181  1.00 67.90           C  
ATOM   7877  O   ILE B 100     174.759 160.342 231.411  1.00 68.73           O  
ATOM   7878  CB  ILE B 100     174.799 158.142 229.037  1.00 67.26           C  
ATOM   7879  CG1 ILE B 100     173.920 156.969 228.615  1.00 67.69           C  
ATOM   7880  CG2 ILE B 100     175.723 157.766 230.197  1.00 67.17           C  
ATOM   7881  CD1 ILE B 100     174.656 155.837 227.927  1.00 67.10           C  
ATOM   7882  N   ILE B 101     175.470 161.197 229.466  1.00 67.47           N  
ATOM   7883  CA  ILE B 101     176.337 162.153 230.140  1.00 67.35           C  
ATOM   7884  C   ILE B 101     175.507 163.242 230.786  1.00 67.81           C  
ATOM   7885  O   ILE B 101     174.674 163.881 230.143  1.00 67.28           O  
ATOM   7886  CB  ILE B 101     177.363 162.749 229.162  1.00 66.62           C  
ATOM   7887  CG1 ILE B 101     178.264 161.615 228.657  1.00 65.69           C  
ATOM   7888  CG2 ILE B 101     178.195 163.850 229.864  1.00 65.30           C  
ATOM   7889  CD1 ILE B 101     179.091 161.963 227.462  1.00 63.40           C  
ATOM   7890  N   ARG B 102     175.728 163.437 232.076  1.00 67.15           N  
ATOM   7891  CA  ARG B 102     174.943 164.396 232.827  1.00 68.12           C  
ATOM   7892  C   ARG B 102     175.769 165.560 233.336  1.00 69.11           C  
ATOM   7893  O   ARG B 102     175.237 166.645 233.567  1.00 70.99           O  
ATOM   7894  CB  ARG B 102     174.260 163.709 234.001  1.00 70.04           C  
ATOM   7895  CG  ARG B 102     173.357 162.527 233.620  1.00 68.34           C  
ATOM   7896  CD  ARG B 102     172.197 162.932 232.765  1.00 68.41           C  
ATOM   7897  NE  ARG B 102     171.420 161.786 232.306  1.00 68.68           N  
ATOM   7898  CZ  ARG B 102     170.456 161.152 233.011  1.00 69.58           C  
ATOM   7899  NH1 ARG B 102     170.148 161.533 234.235  1.00 70.32           N  
ATOM   7900  NH2 ARG B 102     169.812 160.136 232.464  1.00 69.38           N  
ATOM   7901  N   GLY B 103     177.063 165.358 233.543  1.00 67.00           N  
ATOM   7902  CA  GLY B 103     177.809 166.451 234.148  1.00 66.81           C  
ATOM   7903  C   GLY B 103     179.309 166.274 234.204  1.00 67.04           C  
ATOM   7904  O   GLY B 103     179.868 165.361 233.599  1.00 66.32           O  
ATOM   7905  N   TRP B 104     179.952 167.215 234.891  1.00 65.84           N  
ATOM   7906  CA  TRP B 104     181.404 167.255 235.016  1.00 66.42           C  
ATOM   7907  C   TRP B 104     181.884 167.667 236.407  1.00 68.19           C  
ATOM   7908  O   TRP B 104     181.242 168.466 237.092  1.00 69.21           O  
ATOM   7909  CB  TRP B 104     181.990 168.247 234.020  1.00 65.79           C  
ATOM   7910  CG  TRP B 104     181.724 167.951 232.592  1.00 65.25           C  
ATOM   7911  CD1 TRP B 104     182.522 167.257 231.743  1.00 64.52           C  
ATOM   7912  CD2 TRP B 104     180.577 168.363 231.817  1.00 63.84           C  
ATOM   7913  NE1 TRP B 104     181.949 167.196 230.503  1.00 62.70           N  
ATOM   7914  CE2 TRP B 104     180.760 167.871 230.531  1.00 62.83           C  
ATOM   7915  CE3 TRP B 104     179.430 169.099 232.109  1.00 64.63           C  
ATOM   7916  CZ2 TRP B 104     179.836 168.087 229.529  1.00 60.70           C  
ATOM   7917  CZ3 TRP B 104     178.506 169.314 231.103  1.00 63.45           C  
ATOM   7918  CH2 TRP B 104     178.706 168.820 229.847  1.00 60.94           C  
ATOM   7919  N   ILE B 105     183.059 167.178 236.783  1.00 68.49           N  
ATOM   7920  CA  ILE B 105     183.746 167.606 237.998  1.00 68.11           C  
ATOM   7921  C   ILE B 105     185.057 168.271 237.639  1.00 72.68           C  
ATOM   7922  O   ILE B 105     185.855 167.685 236.916  1.00 60.79           O  
ATOM   7923  CB  ILE B 105     184.082 166.427 238.925  1.00 69.84           C  
ATOM   7924  CG1 ILE B 105     182.831 165.708 239.337  1.00 69.69           C  
ATOM   7925  CG2 ILE B 105     184.824 166.962 240.155  1.00 70.78           C  
ATOM   7926  CD1 ILE B 105     183.083 164.384 240.028  1.00 71.21           C  
ATOM   7927  N   PHE B 106     185.311 169.466 238.150  1.00 67.29           N  
ATOM   7928  CA  PHE B 106     186.576 170.128 237.857  1.00 68.48           C  
ATOM   7929  C   PHE B 106     187.299 170.528 239.144  1.00 70.31           C  
ATOM   7930  O   PHE B 106     186.688 171.035 240.084  1.00 71.56           O  
ATOM   7931  CB  PHE B 106     186.331 171.378 237.022  1.00 69.15           C  
ATOM   7932  CG  PHE B 106     185.638 171.174 235.715  1.00 69.14           C  
ATOM   7933  CD1 PHE B 106     184.262 171.226 235.646  1.00 68.76           C  
ATOM   7934  CD2 PHE B 106     186.346 170.957 234.553  1.00 66.94           C  
ATOM   7935  CE1 PHE B 106     183.614 171.066 234.454  1.00 67.02           C  
ATOM   7936  CE2 PHE B 106     185.692 170.784 233.351  1.00 66.48           C  
ATOM   7937  CZ  PHE B 106     184.322 170.841 233.305  1.00 66.04           C  
ATOM   7938  N   GLY B 107     188.615 170.369 239.178  1.00 69.52           N  
ATOM   7939  CA  GLY B 107     189.377 170.783 240.355  1.00 71.15           C  
ATOM   7940  C   GLY B 107     190.814 170.277 240.326  1.00 70.83           C  
ATOM   7941  O   GLY B 107     191.469 170.270 239.279  1.00 70.12           O  
ATOM   7942  N   THR B 108     191.323 169.909 241.498  1.00 70.93           N  
ATOM   7943  CA  THR B 108     192.694 169.429 241.638  1.00 71.38           C  
ATOM   7944  C   THR B 108     192.693 167.992 242.120  1.00 72.54           C  
ATOM   7945  O   THR B 108     192.903 167.062 241.343  1.00 71.19           O  
ATOM   7946  CB  THR B 108     193.498 170.293 242.622  1.00 71.75           C  
ATOM   7947  OG1 THR B 108     192.832 170.325 243.895  1.00 73.04           O  
ATOM   7948  CG2 THR B 108     193.614 171.692 242.088  1.00 70.93           C  
ATOM   7949  N   THR B 109     192.445 167.813 243.413  1.00 72.28           N  
ATOM   7950  CA  THR B 109     192.420 166.487 244.004  1.00 72.75           C  
ATOM   7951  C   THR B 109     191.067 165.801 243.826  1.00 73.11           C  
ATOM   7952  O   THR B 109     190.977 164.577 243.896  1.00 72.98           O  
ATOM   7953  CB  THR B 109     192.783 166.577 245.495  1.00 73.50           C  
ATOM   7954  OG1 THR B 109     191.831 167.410 246.171  1.00 74.60           O  
ATOM   7955  CG2 THR B 109     194.174 167.183 245.648  1.00 73.85           C  
ATOM   7956  N   LEU B 110     190.014 166.586 243.585  1.00 73.05           N  
ATOM   7957  CA  LEU B 110     188.669 166.056 243.358  1.00 73.69           C  
ATOM   7958  C   LEU B 110     188.229 165.086 244.456  1.00 75.26           C  
ATOM   7959  O   LEU B 110     187.587 164.073 244.175  1.00 73.89           O  
ATOM   7960  CB  LEU B 110     188.597 165.345 241.988  1.00 74.68           C  
ATOM   7961  CG  LEU B 110     188.413 166.250 240.733  1.00 71.80           C  
ATOM   7962  CD1 LEU B 110     189.700 166.986 240.418  1.00 71.74           C  
ATOM   7963  CD2 LEU B 110     187.997 165.387 239.543  1.00 70.55           C  
ATOM   7964  N   ASP B 111     188.580 165.390 245.702  1.00 75.57           N  
ATOM   7965  CA  ASP B 111     188.217 164.546 246.837  1.00 76.30           C  
ATOM   7966  C   ASP B 111     188.288 165.351 248.132  1.00 77.12           C  
ATOM   7967  O   ASP B 111     189.306 165.323 248.826  1.00 76.72           O  
ATOM   7968  CB  ASP B 111     189.157 163.336 246.929  1.00 74.97           C  
ATOM   7969  CG  ASP B 111     188.686 162.304 247.935  1.00 75.79           C  
ATOM   7970  OD1 ASP B 111     187.631 162.509 248.474  1.00 76.70           O  
ATOM   7971  OD2 ASP B 111     189.368 161.327 248.154  1.00 76.97           O  
ATOM   7972  N   SER B 112     187.233 166.109 248.429  1.00 76.64           N  
ATOM   7973  CA  SER B 112     187.225 167.035 249.558  1.00 77.41           C  
ATOM   7974  C   SER B 112     188.495 167.883 249.562  1.00 77.53           C  
ATOM   7975  O   SER B 112     189.039 168.198 248.503  1.00 77.25           O  
ATOM   7976  CB  SER B 112     187.094 166.278 250.864  1.00 76.53           C  
ATOM   7977  OG  SER B 112     186.848 167.159 251.927  1.00 78.23           O  
ATOM   7978  N   LYS B 113     188.962 168.248 250.761  1.00 77.06           N  
ATOM   7979  CA  LYS B 113     190.177 169.047 251.000  1.00 77.73           C  
ATOM   7980  C   LYS B 113     190.085 170.496 250.520  1.00 77.44           C  
ATOM   7981  O   LYS B 113     190.318 171.426 251.293  1.00 77.48           O  
ATOM   7982  CB  LYS B 113     191.411 168.383 250.386  1.00 78.02           C  
ATOM   7983  N   THR B 114     189.785 170.684 249.245  1.00 76.34           N  
ATOM   7984  CA  THR B 114     189.642 172.006 248.665  1.00 76.55           C  
ATOM   7985  C   THR B 114     188.354 172.101 247.860  1.00 76.53           C  
ATOM   7986  O   THR B 114     187.570 171.154 247.800  1.00 75.62           O  
ATOM   7987  CB  THR B 114     190.848 172.367 247.788  1.00 75.34           C  
ATOM   7988  OG1 THR B 114     190.783 173.764 247.453  1.00 75.25           O  
ATOM   7989  CG2 THR B 114     190.858 171.528 246.520  1.00 75.84           C  
ATOM   7990  N   GLN B 115     188.121 173.257 247.262  1.00 75.55           N  
ATOM   7991  CA  GLN B 115     186.890 173.476 246.518  1.00 75.60           C  
ATOM   7992  C   GLN B 115     186.957 172.833 245.144  1.00 74.65           C  
ATOM   7993  O   GLN B 115     187.988 172.875 244.471  1.00 73.57           O  
ATOM   7994  CB  GLN B 115     186.606 174.966 246.413  1.00 75.09           C  
ATOM   7995  CG  GLN B 115     186.300 175.613 247.741  1.00 76.25           C  
ATOM   7996  CD  GLN B 115     186.165 177.100 247.629  1.00 76.42           C  
ATOM   7997  OE1 GLN B 115     185.949 177.630 246.538  1.00 76.39           O  
ATOM   7998  NE2 GLN B 115     186.298 177.794 248.751  1.00 77.16           N  
ATOM   7999  N   SER B 116     185.834 172.281 244.705  1.00 74.63           N  
ATOM   8000  CA  SER B 116     185.738 171.654 243.397  1.00 72.92           C  
ATOM   8001  C   SER B 116     184.422 172.011 242.743  1.00 72.75           C  
ATOM   8002  O   SER B 116     183.410 172.151 243.421  1.00 74.39           O  
ATOM   8003  CB  SER B 116     185.866 170.152 243.528  1.00 72.00           C  
ATOM   8004  OG  SER B 116     185.723 169.517 242.290  1.00 70.88           O  
ATOM   8005  N   LEU B 117     184.445 172.178 241.435  1.00 71.26           N  
ATOM   8006  CA  LEU B 117     183.270 172.554 240.663  1.00 71.28           C  
ATOM   8007  C   LEU B 117     182.503 171.370 240.133  1.00 71.46           C  
ATOM   8008  O   LEU B 117     183.048 170.515 239.441  1.00 68.70           O  
ATOM   8009  CB  LEU B 117     183.703 173.439 239.489  1.00 71.84           C  
ATOM   8010  CG  LEU B 117     182.651 173.726 238.392  1.00 71.21           C  
ATOM   8011  CD1 LEU B 117     181.505 174.548 238.942  1.00 71.84           C  
ATOM   8012  CD2 LEU B 117     183.343 174.450 237.244  1.00 69.47           C  
ATOM   8013  N   LEU B 118     181.226 171.326 240.457  1.00 71.81           N  
ATOM   8014  CA  LEU B 118     180.350 170.264 240.013  1.00 71.12           C  
ATOM   8015  C   LEU B 118     179.175 170.812 239.208  1.00 71.92           C  
ATOM   8016  O   LEU B 118     178.414 171.650 239.692  1.00 72.81           O  
ATOM   8017  CB  LEU B 118     179.862 169.498 241.242  1.00 72.06           C  
ATOM   8018  CG  LEU B 118     178.856 168.396 241.020  1.00 72.55           C  
ATOM   8019  CD1 LEU B 118     179.464 167.286 240.175  1.00 70.88           C  
ATOM   8020  CD2 LEU B 118     178.448 167.864 242.373  1.00 74.02           C  
ATOM   8021  N   ILE B 119     179.043 170.351 237.965  1.00 71.06           N  
ATOM   8022  CA  ILE B 119     177.959 170.777 237.077  1.00 71.15           C  
ATOM   8023  C   ILE B 119     177.087 169.597 236.679  1.00 71.43           C  
ATOM   8024  O   ILE B 119     177.528 168.746 235.913  1.00 70.85           O  
ATOM   8025  CB  ILE B 119     178.524 171.421 235.795  1.00 70.53           C  
ATOM   8026  CG1 ILE B 119     179.384 172.646 236.157  1.00 71.53           C  
ATOM   8027  CG2 ILE B 119     177.384 171.779 234.831  1.00 71.57           C  
ATOM   8028  CD1 ILE B 119     180.161 173.217 234.998  1.00 68.93           C  
ATOM   8029  N   VAL B 120     175.859 169.526 237.197  1.00 72.04           N  
ATOM   8030  CA  VAL B 120     175.032 168.346 236.914  1.00 71.83           C  
ATOM   8031  C   VAL B 120     173.627 168.625 236.387  1.00 74.70           C  
ATOM   8032  O   VAL B 120     172.850 169.386 236.971  1.00 76.52           O  
ATOM   8033  CB  VAL B 120     174.929 167.481 238.188  1.00 73.49           C  
ATOM   8034  CG1 VAL B 120     174.026 166.276 237.942  1.00 74.20           C  
ATOM   8035  CG2 VAL B 120     176.318 167.002 238.580  1.00 73.08           C  
ATOM   8036  N   ASN B 121     173.288 167.945 235.293  1.00 73.38           N  
ATOM   8037  CA  ASN B 121     171.967 167.987 234.666  1.00 74.18           C  
ATOM   8038  C   ASN B 121     171.088 166.822 235.108  1.00 75.82           C  
ATOM   8039  O   ASN B 121     171.446 165.665 234.821  1.00 74.14           O  
ATOM   8040  CB  ASN B 121     172.098 167.928 233.158  1.00 74.78           C  
ATOM   8041  CG  ASN B 121     170.793 168.146 232.468  1.00 75.78           C  
ATOM   8042  OD1 ASN B 121     169.932 168.850 233.003  1.00 77.86           O  
ATOM   8043  ND2 ASN B 121     170.611 167.556 231.303  1.00 74.92           N  
ATOM   8044  N   ASN B 122     169.961 167.069 235.807  1.00 78.21           N  
ATOM   8045  CA  ASN B 122     169.051 165.987 236.229  1.00 78.89           C  
ATOM   8046  C   ASN B 122     167.586 166.366 236.149  1.00 79.53           C  
ATOM   8047  O   ASN B 122     167.128 167.385 236.701  1.00 78.84           O  
ATOM   8048  CB  ASN B 122     169.464 165.394 237.611  1.00 78.44           C  
ATOM   8049  CG  ASN B 122     169.175 166.196 238.924  1.00 80.29           C  
ATOM   8050  OD1 ASN B 122     169.529 165.644 239.993  1.00 80.34           O  
ATOM   8051  ND2 ASN B 122     168.585 167.396 238.918  1.00 79.95           N  
ATOM   8052  N   ALA B 123     166.814 165.537 235.403  1.00 79.78           N  
ATOM   8053  CA  ALA B 123     165.377 165.615 235.165  1.00 79.88           C  
ATOM   8054  C   ALA B 123     165.289 166.967 234.440  1.00 80.27           C  
ATOM   8055  O   ALA B 123     165.762 167.084 233.316  1.00 80.18           O  
ATOM   8056  CB  ALA B 123     164.603 165.543 236.477  1.00 80.16           C  
ATOM   8057  N   THR B 124     164.672 167.965 235.082  1.00 79.84           N  
ATOM   8058  CA  THR B 124     164.469 169.255 234.408  1.00 80.65           C  
ATOM   8059  C   THR B 124     165.468 170.416 234.398  1.00 80.19           C  
ATOM   8060  O   THR B 124     165.275 171.372 233.639  1.00 81.34           O  
ATOM   8061  CB  THR B 124     163.180 169.772 235.076  1.00 80.19           C  
ATOM   8062  N   ASN B 125     166.494 170.374 235.241  1.00 79.45           N  
ATOM   8063  CA  ASN B 125     167.378 171.539 235.337  1.00 79.64           C  
ATOM   8064  C   ASN B 125     168.826 171.170 235.622  1.00 78.35           C  
ATOM   8065  O   ASN B 125     169.180 170.006 235.809  1.00 77.98           O  
ATOM   8066  CB  ASN B 125     166.885 172.491 236.427  1.00 78.88           C  
ATOM   8067  N   VAL B 126     169.658 172.203 235.685  1.00 77.61           N  
ATOM   8068  CA  VAL B 126     171.076 172.046 235.926  1.00 76.58           C  
ATOM   8069  C   VAL B 126     171.522 172.763 237.188  1.00 77.35           C  
ATOM   8070  O   VAL B 126     171.197 173.934 237.397  1.00 77.17           O  
ATOM   8071  CB  VAL B 126     171.886 172.577 234.733  1.00 76.50           C  
ATOM   8072  CG1 VAL B 126     173.385 172.409 235.001  1.00 74.81           C  
ATOM   8073  CG2 VAL B 126     171.466 171.833 233.477  1.00 76.20           C  
ATOM   8074  N   VAL B 127     172.261 172.047 238.022  1.00 76.67           N  
ATOM   8075  CA  VAL B 127     172.773 172.611 239.263  1.00 75.74           C  
ATOM   8076  C   VAL B 127     174.284 172.768 239.241  1.00 75.11           C  
ATOM   8077  O   VAL B 127     175.027 171.806 239.032  1.00 75.12           O  
ATOM   8078  CB  VAL B 127     172.358 171.728 240.451  1.00 76.84           C  
ATOM   8079  CG1 VAL B 127     172.936 172.289 241.770  1.00 74.85           C  
ATOM   8080  CG2 VAL B 127     170.840 171.662 240.491  1.00 76.76           C  
ATOM   8081  N   ILE B 128     174.732 173.990 239.466  1.00 74.91           N  
ATOM   8082  CA  ILE B 128     176.146 174.309 239.492  1.00 74.01           C  
ATOM   8083  C   ILE B 128     176.584 174.739 240.880  1.00 75.13           C  
ATOM   8084  O   ILE B 128     176.071 175.708 241.433  1.00 75.51           O  
ATOM   8085  CB  ILE B 128     176.484 175.413 238.482  1.00 75.21           C  
ATOM   8086  CG1 ILE B 128     176.118 174.923 237.079  1.00 73.14           C  
ATOM   8087  CG2 ILE B 128     177.953 175.784 238.592  1.00 74.39           C  
ATOM   8088  CD1 ILE B 128     176.295 175.936 235.966  1.00 72.68           C  
ATOM   8089  N   LYS B 129     177.533 174.015 241.442  1.00 72.99           N  
ATOM   8090  CA  LYS B 129     178.018 174.317 242.783  1.00 74.57           C  
ATOM   8091  C   LYS B 129     179.506 174.029 242.974  1.00 73.16           C  
ATOM   8092  O   LYS B 129     180.049 173.111 242.367  1.00 74.32           O  
ATOM   8093  CB  LYS B 129     177.107 173.623 243.792  1.00 74.90           C  
ATOM   8094  CG  LYS B 129     176.732 172.177 243.456  1.00 73.78           C  
ATOM   8095  CD  LYS B 129     175.826 171.606 244.546  1.00 75.40           C  
ATOM   8096  CE  LYS B 129     175.446 170.168 244.274  1.00 75.12           C  
ATOM   8097  NZ  LYS B 129     174.533 169.629 245.320  1.00 75.60           N  
ATOM   8098  N   VAL B 130     180.172 174.841 243.810  1.00 72.96           N  
ATOM   8099  CA  VAL B 130     181.632 174.714 244.019  1.00 73.30           C  
ATOM   8100  C   VAL B 130     182.093 174.431 245.461  1.00 75.16           C  
ATOM   8101  O   VAL B 130     183.062 175.035 245.927  1.00 74.28           O  
ATOM   8102  CB  VAL B 130     182.350 175.983 243.545  1.00 72.56           C  
ATOM   8103  CG1 VAL B 130     182.188 176.142 242.069  1.00 72.31           C  
ATOM   8104  CG2 VAL B 130     181.812 177.165 244.265  1.00 74.31           C  
ATOM   8105  N   CYS B 131     181.393 173.543 246.164  1.00 75.28           N  
ATOM   8106  CA  CYS B 131     181.639 173.183 247.559  1.00 75.76           C  
ATOM   8107  C   CYS B 131     182.858 172.249 247.685  1.00 76.95           C  
ATOM   8108  O   CYS B 131     183.340 171.702 246.689  1.00 74.51           O  
ATOM   8109  CB  CYS B 131     180.403 172.474 248.144  1.00 76.89           C  
ATOM   8110  SG  CYS B 131     178.828 173.358 247.883  1.00 75.31           S  
ATOM   8111  N   GLU B 132     183.335 172.024 248.929  1.00 75.45           N  
ATOM   8112  CA  GLU B 132     184.416 171.057 249.190  1.00 76.53           C  
ATOM   8113  C   GLU B 132     183.786 169.669 249.270  1.00 76.33           C  
ATOM   8114  O   GLU B 132     183.643 169.081 250.343  1.00 76.11           O  
ATOM   8115  CB  GLU B 132     185.157 171.378 250.489  1.00 77.29           C  
ATOM   8116  N   PHE B 133     183.377 169.183 248.109  1.00 75.68           N  
ATOM   8117  CA  PHE B 133     182.572 167.982 247.986  1.00 76.06           C  
ATOM   8118  C   PHE B 133     183.322 166.723 248.314  1.00 75.97           C  
ATOM   8119  O   PHE B 133     184.459 166.526 247.876  1.00 74.94           O  
ATOM   8120  CB  PHE B 133     182.091 167.808 246.551  1.00 76.03           C  
ATOM   8121  CG  PHE B 133     181.150 168.817 246.093  1.00 76.34           C  
ATOM   8122  CD1 PHE B 133     181.558 169.764 245.184  1.00 75.87           C  
ATOM   8123  CD2 PHE B 133     179.860 168.848 246.558  1.00 75.51           C  
ATOM   8124  CE1 PHE B 133     180.707 170.724 244.756  1.00 74.97           C  
ATOM   8125  CE2 PHE B 133     178.999 169.818 246.130  1.00 74.77           C  
ATOM   8126  CZ  PHE B 133     179.435 170.758 245.232  1.00 74.90           C  
ATOM   8127  N   GLN B 134     182.642 165.827 249.011  1.00 75.69           N  
ATOM   8128  CA  GLN B 134     183.181 164.505 249.220  1.00 76.56           C  
ATOM   8129  C   GLN B 134     182.634 163.629 248.121  1.00 75.79           C  
ATOM   8130  O   GLN B 134     181.454 163.280 248.114  1.00 75.58           O  
ATOM   8131  CB  GLN B 134     182.812 163.939 250.591  1.00 77.83           C  
ATOM   8132  N   PHE B 135     183.490 163.313 247.177  1.00 75.17           N  
ATOM   8133  CA  PHE B 135     183.093 162.565 246.010  1.00 75.36           C  
ATOM   8134  C   PHE B 135     183.209 161.080 246.244  1.00 75.80           C  
ATOM   8135  O   PHE B 135     183.956 160.620 247.112  1.00 76.60           O  
ATOM   8136  CB  PHE B 135     183.921 162.957 244.787  1.00 74.48           C  
ATOM   8137  CG  PHE B 135     183.626 164.332 244.250  1.00 75.11           C  
ATOM   8138  CD1 PHE B 135     184.560 165.342 244.352  1.00 74.21           C  
ATOM   8139  CD2 PHE B 135     182.411 164.614 243.645  1.00 73.66           C  
ATOM   8140  CE1 PHE B 135     184.299 166.599 243.855  1.00 74.38           C  
ATOM   8141  CE2 PHE B 135     182.143 165.874 243.154  1.00 73.90           C  
ATOM   8142  CZ  PHE B 135     183.089 166.868 243.256  1.00 74.54           C  
ATOM   8143  N   CYS B 136     182.451 160.335 245.458  1.00 76.22           N  
ATOM   8144  CA  CYS B 136     182.527 158.892 245.454  1.00 75.91           C  
ATOM   8145  C   CYS B 136     183.828 158.499 244.783  1.00 76.68           C  
ATOM   8146  O   CYS B 136     184.369 159.265 243.988  1.00 75.58           O  
ATOM   8147  CB  CYS B 136     181.356 158.294 244.675  1.00 75.95           C  
ATOM   8148  N   ASN B 137     184.333 157.307 245.082  1.00 76.96           N  
ATOM   8149  CA  ASN B 137     185.561 156.859 244.438  1.00 77.93           C  
ATOM   8150  C   ASN B 137     185.358 156.734 242.936  1.00 77.29           C  
ATOM   8151  O   ASN B 137     186.250 157.038 242.143  1.00 78.00           O  
ATOM   8152  CB  ASN B 137     185.995 155.523 245.004  1.00 78.87           C  
ATOM   8153  N   ASP B 138     184.159 156.312 242.558  1.00 76.52           N  
ATOM   8154  CA  ASP B 138     183.784 156.103 241.171  1.00 77.36           C  
ATOM   8155  C   ASP B 138     182.394 156.689 240.905  1.00 77.10           C  
ATOM   8156  O   ASP B 138     181.419 155.940 240.869  1.00 75.78           O  
ATOM   8157  CB  ASP B 138     183.783 154.608 240.849  1.00 78.09           C  
ATOM   8158  N   PRO B 139     182.277 158.017 240.771  1.00 75.97           N  
ATOM   8159  CA  PRO B 139     181.044 158.773 240.627  1.00 74.11           C  
ATOM   8160  C   PRO B 139     180.468 158.559 239.231  1.00 73.65           C  
ATOM   8161  O   PRO B 139     181.207 158.190 238.319  1.00 73.50           O  
ATOM   8162  CB  PRO B 139     181.524 160.212 240.855  1.00 74.14           C  
ATOM   8163  CG  PRO B 139     182.947 160.216 240.364  1.00 74.42           C  
ATOM   8164  CD  PRO B 139     183.493 158.839 240.691  1.00 75.18           C  
ATOM   8165  N   PHE B 140     179.153 158.814 239.070  1.00 73.22           N  
ATOM   8166  CA  PHE B 140     178.432 158.699 237.784  1.00 71.84           C  
ATOM   8167  C   PHE B 140     176.956 159.052 237.955  1.00 71.85           C  
ATOM   8168  O   PHE B 140     176.535 160.185 237.708  1.00 72.40           O  
ATOM   8169  CB  PHE B 140     178.536 157.266 237.176  1.00 72.76           C  
ATOM   8170  CG  PHE B 140     177.887 156.118 238.014  1.00 73.23           C  
ATOM   8171  CD1 PHE B 140     178.640 155.458 239.065  1.00 73.09           C  
ATOM   8172  CD2 PHE B 140     176.525 155.672 237.761  1.00 73.53           C  
ATOM   8173  CE1 PHE B 140     178.061 154.402 239.839  1.00 73.86           C  
ATOM   8174  CE2 PHE B 140     175.944 154.609 238.538  1.00 74.10           C  
ATOM   8175  CZ  PHE B 140     176.714 153.976 239.578  1.00 73.38           C  
ATOM   8176  N   ASN B 164     181.006 170.983 252.023  1.00 77.60           N  
ATOM   8177  CA  ASN B 164     180.475 172.214 252.594  1.00 77.32           C  
ATOM   8178  C   ASN B 164     181.370 173.420 252.229  1.00 77.40           C  
ATOM   8179  O   ASN B 164     182.123 173.366 251.246  1.00 76.55           O  
ATOM   8180  CB  ASN B 164     180.238 172.033 254.120  1.00 79.17           C  
ATOM   8181  N   ASN B 165     181.272 174.541 252.980  1.00 77.85           N  
ATOM   8182  CA  ASN B 165     181.994 175.782 252.756  1.00 76.98           C  
ATOM   8183  C   ASN B 165     181.890 176.267 251.285  1.00 76.58           C  
ATOM   8184  O   ASN B 165     182.831 176.648 250.648  1.00 75.72           O  
ATOM   8185  CB  ASN B 165     183.495 175.607 253.142  1.00 77.43           C  
ATOM   8186  CG  ASN B 165     183.690 175.339 254.654  1.00 79.45           C  
ATOM   8187  OD1 ASN B 165     182.855 175.736 255.482  1.00 79.16           O  
ATOM   8188  ND2 ASN B 165     184.788 174.676 255.001  1.00 80.11           N  
ATOM   8189  N   CYS B 166     180.617 176.235 250.809  1.00 75.83           N  
ATOM   8190  CA  CYS B 166     180.222 176.581 249.446  1.00 76.29           C  
ATOM   8191  C   CYS B 166     180.328 178.097 249.223  1.00 75.82           C  
ATOM   8192  O   CYS B 166     179.811 178.879 250.028  1.00 75.44           O  
ATOM   8193  CB  CYS B 166     178.754 176.134 249.234  1.00 79.36           C  
ATOM   8194  SG  CYS B 166     178.436 174.361 249.591  1.00 83.72           S  
ATOM   8195  N   THR B 167     180.961 178.512 248.107  1.00 75.11           N  
ATOM   8196  CA  THR B 167     181.130 179.932 247.767  1.00 75.56           C  
ATOM   8197  C   THR B 167     180.200 180.360 246.647  1.00 76.04           C  
ATOM   8198  O   THR B 167     179.945 181.549 246.456  1.00 77.18           O  
ATOM   8199  CB  THR B 167     182.568 180.212 247.324  1.00 76.02           C  
ATOM   8200  OG1 THR B 167     182.837 179.489 246.122  1.00 77.12           O  
ATOM   8201  CG2 THR B 167     183.532 179.763 248.408  1.00 77.09           C  
ATOM   8202  N   PHE B 168     179.711 179.393 245.892  1.00 76.12           N  
ATOM   8203  CA  PHE B 168     178.837 179.670 244.769  1.00 76.25           C  
ATOM   8204  C   PHE B 168     177.876 178.524 244.521  1.00 75.79           C  
ATOM   8205  O   PHE B 168     178.254 177.348 244.566  1.00 75.65           O  
ATOM   8206  CB  PHE B 168     179.649 179.950 243.504  1.00 75.74           C  
ATOM   8207  CG  PHE B 168     178.830 180.089 242.286  1.00 75.84           C  
ATOM   8208  CD1 PHE B 168     178.371 181.320 241.879  1.00 75.97           C  
ATOM   8209  CD2 PHE B 168     178.500 178.972 241.540  1.00 75.08           C  
ATOM   8210  CE1 PHE B 168     177.604 181.438 240.746  1.00 76.60           C  
ATOM   8211  CE2 PHE B 168     177.732 179.091 240.419  1.00 75.54           C  
ATOM   8212  CZ  PHE B 168     177.287 180.324 240.018  1.00 75.29           C  
ATOM   8213  N   GLU B 169     176.632 178.881 244.245  1.00 75.48           N  
ATOM   8214  CA  GLU B 169     175.620 177.925 243.845  1.00 75.49           C  
ATOM   8215  C   GLU B 169     174.621 178.579 242.911  1.00 76.33           C  
ATOM   8216  O   GLU B 169     174.132 179.680 243.172  1.00 74.65           O  
ATOM   8217  CB  GLU B 169     174.894 177.331 245.053  1.00 75.60           C  
ATOM   8218  CG  GLU B 169     173.798 176.317 244.681  1.00 75.96           C  
ATOM   8219  CD  GLU B 169     173.166 175.659 245.868  1.00 77.30           C  
ATOM   8220  OE1 GLU B 169     173.629 175.872 246.962  1.00 76.39           O  
ATOM   8221  OE2 GLU B 169     172.209 174.947 245.683  1.00 75.59           O  
ATOM   8222  N   TYR B 170     174.300 177.878 241.839  1.00 75.90           N  
ATOM   8223  CA  TYR B 170     173.327 178.336 240.870  1.00 76.31           C  
ATOM   8224  C   TYR B 170     172.445 177.210 240.365  1.00 76.54           C  
ATOM   8225  O   TYR B 170     172.919 176.123 240.040  1.00 76.13           O  
ATOM   8226  CB  TYR B 170     174.034 178.997 239.693  1.00 76.36           C  
ATOM   8227  CG  TYR B 170     173.134 179.227 238.534  1.00 76.86           C  
ATOM   8228  CD1 TYR B 170     172.253 180.285 238.528  1.00 77.39           C  
ATOM   8229  CD2 TYR B 170     173.184 178.360 237.468  1.00 77.60           C  
ATOM   8230  CE1 TYR B 170     171.418 180.472 237.451  1.00 78.38           C  
ATOM   8231  CE2 TYR B 170     172.359 178.543 236.395  1.00 77.16           C  
ATOM   8232  CZ  TYR B 170     171.475 179.593 236.379  1.00 77.16           C  
ATOM   8233  OH  TYR B 170     170.646 179.778 235.298  1.00 77.94           O  
ATOM   8234  N   VAL B 171     171.153 177.477 240.263  1.00 77.32           N  
ATOM   8235  CA  VAL B 171     170.242 176.491 239.711  1.00 77.25           C  
ATOM   8236  C   VAL B 171     169.506 177.079 238.514  1.00 77.45           C  
ATOM   8237  O   VAL B 171     168.878 178.133 238.636  1.00 77.89           O  
ATOM   8238  CB  VAL B 171     169.226 176.047 240.773  1.00 75.93           C  
ATOM   8239  CG1 VAL B 171     168.272 174.979 240.179  1.00 76.59           C  
ATOM   8240  CG2 VAL B 171     169.983 175.532 242.005  1.00 76.16           C  
ATOM   8241  N   SER B 172     169.556 176.382 237.368  1.00 77.12           N  
ATOM   8242  CA  SER B 172     168.882 176.807 236.142  1.00 77.81           C  
ATOM   8243  C   SER B 172     167.382 176.575 236.275  1.00 77.88           C  
ATOM   8244  O   SER B 172     166.600 176.967 235.408  1.00 79.05           O  
ATOM   8245  CB  SER B 172     169.437 176.061 234.925  1.00 77.75           C  
ATOM   8246  N   PHE B 186     173.473 157.891 217.214  1.00 63.63           N  
ATOM   8247  CA  PHE B 186     173.836 159.016 218.067  1.00 64.50           C  
ATOM   8248  C   PHE B 186     173.508 160.331 217.331  1.00 63.39           C  
ATOM   8249  O   PHE B 186     174.360 160.878 216.623  1.00 63.30           O  
ATOM   8250  CB  PHE B 186     175.346 158.986 218.428  1.00 64.48           C  
ATOM   8251  CG  PHE B 186     175.870 157.758 219.216  1.00 64.40           C  
ATOM   8252  CD1 PHE B 186     176.833 156.843 218.609  1.00 64.39           C  
ATOM   8253  CD2 PHE B 186     175.430 157.483 220.567  1.00 63.76           C  
ATOM   8254  CE1 PHE B 186     177.334 155.708 219.341  1.00 64.10           C  
ATOM   8255  CE2 PHE B 186     175.929 156.349 221.295  1.00 64.35           C  
ATOM   8256  CZ  PHE B 186     176.882 155.466 220.683  1.00 63.66           C  
ATOM   8257  N   LYS B 187     172.266 160.830 217.482  1.00 63.65           N  
ATOM   8258  CA  LYS B 187     171.785 162.024 216.766  1.00 62.64           C  
ATOM   8259  C   LYS B 187     172.041 163.361 217.463  1.00 63.14           C  
ATOM   8260  O   LYS B 187     172.034 164.403 216.805  1.00 62.50           O  
ATOM   8261  CB  LYS B 187     170.294 161.888 216.471  1.00 63.57           C  
ATOM   8262  CG  LYS B 187     169.964 160.809 215.449  1.00 63.70           C  
ATOM   8263  CD  LYS B 187     168.467 160.730 215.177  1.00 63.96           C  
ATOM   8264  CE  LYS B 187     168.148 159.665 214.134  1.00 63.96           C  
ATOM   8265  NZ  LYS B 187     166.682 159.541 213.897  1.00 63.49           N  
ATOM   8266  N   ASN B 188     172.257 163.365 218.776  1.00 62.41           N  
ATOM   8267  CA  ASN B 188     172.456 164.638 219.467  1.00 61.45           C  
ATOM   8268  C   ASN B 188     173.918 165.002 219.630  1.00 62.37           C  
ATOM   8269  O   ASN B 188     174.620 164.392 220.436  1.00 62.77           O  
ATOM   8270  CB  ASN B 188     171.791 164.619 220.827  1.00 62.19           C  
ATOM   8271  CG  ASN B 188     170.312 164.646 220.744  1.00 62.11           C  
ATOM   8272  OD1 ASN B 188     169.734 165.670 220.352  1.00 62.88           O  
ATOM   8273  ND2 ASN B 188     169.680 163.559 221.103  1.00 63.01           N  
ATOM   8274  N   LEU B 189     174.385 165.993 218.868  1.00 60.42           N  
ATOM   8275  CA  LEU B 189     175.772 166.423 218.975  1.00 59.94           C  
ATOM   8276  C   LEU B 189     175.870 167.651 219.847  1.00 59.61           C  
ATOM   8277  O   LEU B 189     175.304 168.703 219.543  1.00 60.15           O  
ATOM   8278  CB  LEU B 189     176.385 166.739 217.606  1.00 60.78           C  
ATOM   8279  CG  LEU B 189     177.822 167.388 217.622  1.00 59.39           C  
ATOM   8280  CD1 LEU B 189     178.846 166.440 218.232  1.00 60.44           C  
ATOM   8281  CD2 LEU B 189     178.240 167.739 216.208  1.00 59.94           C  
ATOM   8282  N   ARG B 190     176.594 167.519 220.937  1.00 58.54           N  
ATOM   8283  CA  ARG B 190     176.742 168.615 221.863  1.00 58.63           C  
ATOM   8284  C   ARG B 190     178.207 168.971 221.997  1.00 59.51           C  
ATOM   8285  O   ARG B 190     179.033 168.133 222.352  1.00 60.48           O  
ATOM   8286  CB  ARG B 190     176.157 168.253 223.212  1.00 59.31           C  
ATOM   8287  CG  ARG B 190     174.664 167.944 223.201  1.00 60.29           C  
ATOM   8288  CD  ARG B 190     174.144 167.728 224.576  1.00 61.10           C  
ATOM   8289  NE  ARG B 190     172.701 167.485 224.594  1.00 62.21           N  
ATOM   8290  CZ  ARG B 190     172.102 166.267 224.614  1.00 63.29           C  
ATOM   8291  NH1 ARG B 190     172.801 165.152 224.622  1.00 63.19           N  
ATOM   8292  NH2 ARG B 190     170.785 166.184 224.638  1.00 63.31           N  
ATOM   8293  N   GLU B 191     178.528 170.212 221.687  1.00 58.74           N  
ATOM   8294  CA  GLU B 191     179.901 170.685 221.726  1.00 57.97           C  
ATOM   8295  C   GLU B 191     180.058 171.693 222.842  1.00 60.16           C  
ATOM   8296  O   GLU B 191     179.203 172.557 223.024  1.00 55.62           O  
ATOM   8297  CB  GLU B 191     180.262 171.328 220.388  1.00 58.46           C  
ATOM   8298  CG  GLU B 191     180.202 170.393 219.196  1.00 58.04           C  
ATOM   8299  CD  GLU B 191     180.330 171.126 217.887  1.00 57.48           C  
ATOM   8300  OE1 GLU B 191     179.314 171.473 217.342  1.00 58.27           O  
ATOM   8301  OE2 GLU B 191     181.425 171.338 217.427  1.00 57.13           O  
ATOM   8302  N   PHE B 192     181.153 171.594 223.580  1.00 57.78           N  
ATOM   8303  CA  PHE B 192     181.428 172.500 224.678  1.00 58.41           C  
ATOM   8304  C   PHE B 192     182.869 172.978 224.699  1.00 60.06           C  
ATOM   8305  O   PHE B 192     183.786 172.252 224.316  1.00 58.45           O  
ATOM   8306  CB  PHE B 192     181.168 171.806 226.004  1.00 58.88           C  
ATOM   8307  CG  PHE B 192     179.796 171.300 226.190  1.00 58.72           C  
ATOM   8308  CD1 PHE B 192     179.453 170.053 225.719  1.00 59.47           C  
ATOM   8309  CD2 PHE B 192     178.848 172.047 226.850  1.00 58.68           C  
ATOM   8310  CE1 PHE B 192     178.193 169.559 225.896  1.00 59.28           C  
ATOM   8311  CE2 PHE B 192     177.576 171.560 227.030  1.00 58.25           C  
ATOM   8312  CZ  PHE B 192     177.247 170.310 226.551  1.00 58.32           C  
ATOM   8313  N   VAL B 193     183.076 174.170 225.225  1.00 58.01           N  
ATOM   8314  CA  VAL B 193     184.415 174.632 225.543  1.00 58.44           C  
ATOM   8315  C   VAL B 193     184.461 175.058 226.992  1.00 61.89           C  
ATOM   8316  O   VAL B 193     183.720 175.947 227.407  1.00 59.69           O  
ATOM   8317  CB  VAL B 193     184.846 175.811 224.656  1.00 58.93           C  
ATOM   8318  CG1 VAL B 193     186.215 176.279 225.038  1.00 59.42           C  
ATOM   8319  CG2 VAL B 193     184.835 175.388 223.226  1.00 58.08           C  
ATOM   8320  N   PHE B 194     185.343 174.443 227.754  1.00 59.81           N  
ATOM   8321  CA  PHE B 194     185.495 174.776 229.158  1.00 60.44           C  
ATOM   8322  C   PHE B 194     186.847 175.433 229.366  1.00 61.80           C  
ATOM   8323  O   PHE B 194     187.884 174.779 229.250  1.00 63.17           O  
ATOM   8324  CB  PHE B 194     185.398 173.513 230.008  1.00 62.18           C  
ATOM   8325  CG  PHE B 194     184.076 172.806 229.922  1.00 62.04           C  
ATOM   8326  CD1 PHE B 194     183.883 171.771 229.033  1.00 60.47           C  
ATOM   8327  CD2 PHE B 194     183.030 173.169 230.729  1.00 62.80           C  
ATOM   8328  CE1 PHE B 194     182.671 171.121 228.969  1.00 60.08           C  
ATOM   8329  CE2 PHE B 194     181.819 172.522 230.663  1.00 62.78           C  
ATOM   8330  CZ  PHE B 194     181.644 171.498 229.780  1.00 61.08           C  
ATOM   8331  N   LYS B 195     186.868 176.727 229.644  1.00 61.70           N  
ATOM   8332  CA  LYS B 195     188.160 177.397 229.767  1.00 62.49           C  
ATOM   8333  C   LYS B 195     188.201 178.435 230.886  1.00 63.55           C  
ATOM   8334  O   LYS B 195     187.169 178.995 231.252  1.00 64.78           O  
ATOM   8335  CB  LYS B 195     188.539 178.038 228.427  1.00 62.17           C  
ATOM   8336  CG  LYS B 195     187.625 179.179 227.961  1.00 61.50           C  
ATOM   8337  CD  LYS B 195     188.029 179.681 226.562  1.00 59.00           C  
ATOM   8338  CE  LYS B 195     189.227 180.648 226.602  1.00 58.25           C  
ATOM   8339  NZ  LYS B 195     188.875 181.976 227.172  1.00 58.98           N  
ATOM   8340  N   ASN B 196     189.415 178.709 231.399  1.00 63.96           N  
ATOM   8341  CA  ASN B 196     189.674 179.763 232.389  1.00 64.74           C  
ATOM   8342  C   ASN B 196     190.473 180.895 231.748  1.00 65.02           C  
ATOM   8343  O   ASN B 196     189.942 181.696 230.974  1.00 64.36           O  
ATOM   8344  CB  ASN B 196     190.405 179.215 233.626  1.00 65.89           C  
ATOM   8345  CG  ASN B 196     189.528 178.289 234.510  1.00 67.11           C  
ATOM   8346  OD1 ASN B 196     188.424 178.688 234.894  1.00 67.66           O  
ATOM   8347  ND2 ASN B 196     190.011 177.090 234.832  1.00 67.54           N  
ATOM   8348  N   TYR B 200     188.334 183.516 235.968  1.00 69.34           N  
ATOM   8349  CA  TYR B 200     187.146 182.720 236.244  1.00 69.84           C  
ATOM   8350  C   TYR B 200     186.804 181.789 235.060  1.00 68.19           C  
ATOM   8351  O   TYR B 200     187.557 181.736 234.085  1.00 67.63           O  
ATOM   8352  CB  TYR B 200     185.982 183.634 236.722  1.00 70.63           C  
ATOM   8353  CG  TYR B 200     185.695 184.923 235.913  1.00 70.91           C  
ATOM   8354  CD1 TYR B 200     184.839 184.896 234.755  1.00 70.74           C  
ATOM   8355  CD2 TYR B 200     186.286 186.192 236.347  1.00 71.95           C  
ATOM   8356  CE1 TYR B 200     184.575 186.115 234.035  1.00 70.77           C  
ATOM   8357  CE2 TYR B 200     186.016 187.400 235.624  1.00 72.10           C  
ATOM   8358  CZ  TYR B 200     185.165 187.367 234.472  1.00 71.68           C  
ATOM   8359  OH  TYR B 200     184.906 188.528 233.767  1.00 72.10           O  
ATOM   8360  N   PHE B 201     185.721 180.988 235.212  1.00 68.46           N  
ATOM   8361  CA  PHE B 201     185.387 179.843 234.343  1.00 67.02           C  
ATOM   8362  C   PHE B 201     184.275 180.134 233.332  1.00 67.50           C  
ATOM   8363  O   PHE B 201     183.151 180.491 233.690  1.00 67.95           O  
ATOM   8364  CB  PHE B 201     185.007 178.674 235.258  1.00 68.53           C  
ATOM   8365  CG  PHE B 201     184.858 177.324 234.631  1.00 67.22           C  
ATOM   8366  CD1 PHE B 201     185.969 176.518 234.476  1.00 67.04           C  
ATOM   8367  CD2 PHE B 201     183.637 176.831 234.238  1.00 67.45           C  
ATOM   8368  CE1 PHE B 201     185.872 175.262 233.950  1.00 66.40           C  
ATOM   8369  CE2 PHE B 201     183.546 175.561 233.712  1.00 66.14           C  
ATOM   8370  CZ  PHE B 201     184.664 174.783 233.573  1.00 65.96           C  
ATOM   8371  N   LYS B 202     184.605 179.988 232.053  1.00 66.38           N  
ATOM   8372  CA  LYS B 202     183.685 180.287 230.959  1.00 64.49           C  
ATOM   8373  C   LYS B 202     183.270 179.040 230.186  1.00 62.89           C  
ATOM   8374  O   LYS B 202     184.112 178.226 229.801  1.00 64.06           O  
ATOM   8375  CB  LYS B 202     184.350 181.269 229.996  1.00 64.21           C  
ATOM   8376  CG  LYS B 202     184.831 182.571 230.644  1.00 66.66           C  
ATOM   8377  CD  LYS B 202     183.682 183.501 231.009  1.00 68.15           C  
ATOM   8378  CE  LYS B 202     183.185 184.307 229.813  1.00 68.70           C  
ATOM   8379  NZ  LYS B 202     184.120 185.414 229.469  1.00 68.23           N  
ATOM   8380  N   ILE B 203     181.968 178.897 229.937  1.00 62.14           N  
ATOM   8381  CA  ILE B 203     181.483 177.752 229.173  1.00 60.11           C  
ATOM   8382  C   ILE B 203     180.803 178.183 227.882  1.00 61.45           C  
ATOM   8383  O   ILE B 203     179.824 178.940 227.903  1.00 61.61           O  
ATOM   8384  CB  ILE B 203     180.465 176.925 229.969  1.00 62.38           C  
ATOM   8385  CG1 ILE B 203     181.069 176.481 231.304  1.00 63.89           C  
ATOM   8386  CG2 ILE B 203     180.045 175.696 229.132  1.00 60.63           C  
ATOM   8387  CD1 ILE B 203     180.060 175.866 232.275  1.00 65.22           C  
ATOM   8388  N   TYR B 204     181.279 177.638 226.769  1.00 59.42           N  
ATOM   8389  CA  TYR B 204     180.701 177.900 225.452  1.00 59.16           C  
ATOM   8390  C   TYR B 204     180.086 176.617 224.956  1.00 59.43           C  
ATOM   8391  O   TYR B 204     180.585 175.541 225.280  1.00 57.67           O  
ATOM   8392  CB  TYR B 204     181.765 178.344 224.455  1.00 59.07           C  
ATOM   8393  CG  TYR B 204     182.526 179.570 224.837  1.00 58.44           C  
ATOM   8394  CD1 TYR B 204     183.493 179.514 225.822  1.00 59.20           C  
ATOM   8395  CD2 TYR B 204     182.285 180.740 224.189  1.00 57.81           C  
ATOM   8396  CE1 TYR B 204     184.192 180.643 226.157  1.00 59.63           C  
ATOM   8397  CE2 TYR B 204     182.983 181.868 224.520  1.00 58.60           C  
ATOM   8398  CZ  TYR B 204     183.930 181.825 225.499  1.00 58.98           C  
ATOM   8399  OH  TYR B 204     184.628 182.966 225.824  1.00 60.24           O  
ATOM   8400  N   SER B 205     179.024 176.695 224.169  1.00 57.99           N  
ATOM   8401  CA  SER B 205     178.475 175.456 223.634  1.00 57.41           C  
ATOM   8402  C   SER B 205     177.610 175.618 222.397  1.00 57.25           C  
ATOM   8403  O   SER B 205     177.250 176.728 221.991  1.00 58.04           O  
ATOM   8404  CB  SER B 205     177.685 174.729 224.694  1.00 57.80           C  
ATOM   8405  OG  SER B 205     176.531 175.413 224.992  1.00 58.81           O  
ATOM   8406  N   LYS B 206     177.317 174.476 221.780  1.00 57.20           N  
ATOM   8407  CA  LYS B 206     176.441 174.385 220.619  1.00 57.48           C  
ATOM   8408  C   LYS B 206     175.745 173.024 220.569  1.00 57.61           C  
ATOM   8409  O   LYS B 206     176.367 171.990 220.806  1.00 59.87           O  
ATOM   8410  CB  LYS B 206     177.243 174.625 219.337  1.00 57.46           C  
ATOM   8411  CG  LYS B 206     176.426 174.738 218.062  1.00 58.19           C  
ATOM   8412  CD  LYS B 206     175.738 176.094 217.963  1.00 58.00           C  
ATOM   8413  CE  LYS B 206     175.001 176.249 216.649  1.00 57.72           C  
ATOM   8414  NZ  LYS B 206     174.266 177.543 216.581  1.00 56.38           N  
ATOM   8415  N   HIS B 207     174.456 173.016 220.244  1.00 58.02           N  
ATOM   8416  CA  HIS B 207     173.709 171.765 220.098  1.00 58.58           C  
ATOM   8417  C   HIS B 207     173.076 171.653 218.718  1.00 59.45           C  
ATOM   8418  O   HIS B 207     172.237 172.475 218.347  1.00 59.49           O  
ATOM   8419  CB  HIS B 207     172.624 171.656 221.175  1.00 59.44           C  
ATOM   8420  CG  HIS B 207     171.767 170.399 221.114  1.00 59.81           C  
ATOM   8421  ND1 HIS B 207     170.534 170.326 221.728  1.00 60.76           N  
ATOM   8422  CD2 HIS B 207     171.959 169.184 220.525  1.00 61.27           C  
ATOM   8423  CE1 HIS B 207     170.004 169.134 221.517  1.00 61.95           C  
ATOM   8424  NE2 HIS B 207     170.843 168.424 220.793  1.00 60.89           N  
ATOM   8425  N   THR B 208     173.502 170.654 217.951  1.00 59.34           N  
ATOM   8426  CA  THR B 208     172.969 170.435 216.612  1.00 60.28           C  
ATOM   8427  C   THR B 208     172.614 168.960 216.426  1.00 61.13           C  
ATOM   8428  O   THR B 208     173.192 168.106 217.098  1.00 61.22           O  
ATOM   8429  CB  THR B 208     173.996 170.843 215.538  1.00 58.95           C  
ATOM   8430  OG1 THR B 208     175.156 170.016 215.656  1.00 58.80           O  
ATOM   8431  CG2 THR B 208     174.397 172.286 215.719  1.00 58.15           C  
ATOM   8432  N   PRO B 209     171.652 168.633 215.556  1.00 60.87           N  
ATOM   8433  CA  PRO B 209     171.333 167.289 215.115  1.00 61.14           C  
ATOM   8434  C   PRO B 209     172.369 166.780 214.129  1.00 61.89           C  
ATOM   8435  O   PRO B 209     172.834 167.540 213.277  1.00 62.34           O  
ATOM   8436  CB  PRO B 209     169.966 167.478 214.454  1.00 62.41           C  
ATOM   8437  CG  PRO B 209     169.978 168.912 213.962  1.00 62.10           C  
ATOM   8438  CD  PRO B 209     170.797 169.679 214.988  1.00 61.20           C  
ATOM   8439  N   ILE B 210     172.683 165.492 214.209  1.00 61.93           N  
ATOM   8440  CA  ILE B 210     173.576 164.846 213.253  1.00 62.74           C  
ATOM   8441  C   ILE B 210     172.995 163.511 212.768  1.00 64.16           C  
ATOM   8442  O   ILE B 210     172.099 162.960 213.408  1.00 62.88           O  
ATOM   8443  CB  ILE B 210     174.986 164.650 213.857  1.00 63.02           C  
ATOM   8444  CG1 ILE B 210     174.924 163.738 215.093  1.00 62.86           C  
ATOM   8445  CG2 ILE B 210     175.558 166.014 214.223  1.00 61.39           C  
ATOM   8446  CD1 ILE B 210     176.279 163.261 215.590  1.00 62.77           C  
ATOM   8447  N   ASN B 211     173.530 162.987 211.649  1.00 63.04           N  
ATOM   8448  CA  ASN B 211     173.174 161.681 211.075  1.00 63.03           C  
ATOM   8449  C   ASN B 211     174.001 161.439 209.815  1.00 63.44           C  
ATOM   8450  O   ASN B 211     175.155 161.867 209.728  1.00 63.54           O  
ATOM   8451  CB  ASN B 211     171.657 161.542 210.779  1.00 62.94           C  
ATOM   8452  CG  ASN B 211     171.073 162.596 209.767  1.00 63.91           C  
ATOM   8453  OD1 ASN B 211     171.497 162.640 208.602  1.00 63.22           O  
ATOM   8454  ND2 ASN B 211     170.117 163.417 210.215  1.00 63.68           N  
ATOM   8455  N   ASP B 215     183.880 159.254 213.009  1.00 58.67           N  
ATOM   8456  CA  ASP B 215     182.894 159.134 214.084  1.00 59.03           C  
ATOM   8457  C   ASP B 215     182.354 160.507 214.517  1.00 59.48           C  
ATOM   8458  O   ASP B 215     181.151 160.652 214.754  1.00 59.40           O  
ATOM   8459  CB  ASP B 215     183.509 158.374 215.286  1.00 59.08           C  
ATOM   8460  N   LEU B 216     183.242 161.515 214.598  1.00 59.26           N  
ATOM   8461  CA  LEU B 216     182.899 162.905 214.913  1.00 59.26           C  
ATOM   8462  C   LEU B 216     182.631 163.603 213.575  1.00 58.76           C  
ATOM   8463  O   LEU B 216     183.535 163.682 212.748  1.00 58.66           O  
ATOM   8464  CB  LEU B 216     184.065 163.581 215.653  1.00 58.55           C  
ATOM   8465  CG  LEU B 216     183.895 165.052 216.080  1.00 58.55           C  
ATOM   8466  CD1 LEU B 216     182.780 165.189 217.125  1.00 59.20           C  
ATOM   8467  CD2 LEU B 216     185.221 165.535 216.657  1.00 57.53           C  
ATOM   8468  N   PRO B 217     181.410 164.075 213.300  1.00 58.93           N  
ATOM   8469  CA  PRO B 217     181.010 164.653 212.034  1.00 58.32           C  
ATOM   8470  C   PRO B 217     181.904 165.796 211.597  1.00 57.83           C  
ATOM   8471  O   PRO B 217     182.286 166.638 212.414  1.00 57.78           O  
ATOM   8472  CB  PRO B 217     179.590 165.139 212.332  1.00 58.58           C  
ATOM   8473  CG  PRO B 217     179.110 164.246 213.437  1.00 59.88           C  
ATOM   8474  CD  PRO B 217     180.322 163.987 214.288  1.00 59.31           C  
ATOM   8475  N   GLN B 218     182.209 165.840 210.308  1.00 57.86           N  
ATOM   8476  CA  GLN B 218     183.018 166.897 209.720  1.00 56.91           C  
ATOM   8477  C   GLN B 218     182.144 168.063 209.295  1.00 57.66           C  
ATOM   8478  O   GLN B 218     181.077 167.867 208.716  1.00 57.65           O  
ATOM   8479  CB  GLN B 218     183.801 166.378 208.519  1.00 57.36           C  
ATOM   8480  N   GLY B 219     182.602 169.273 209.573  1.00 57.51           N  
ATOM   8481  CA  GLY B 219     181.871 170.476 209.204  1.00 57.44           C  
ATOM   8482  C   GLY B 219     182.328 171.623 210.079  1.00 56.72           C  
ATOM   8483  O   GLY B 219     183.226 171.452 210.903  1.00 56.11           O  
ATOM   8484  N   PHE B 220     181.730 172.793 209.903  1.00 56.05           N  
ATOM   8485  CA  PHE B 220     182.145 173.937 210.695  1.00 55.06           C  
ATOM   8486  C   PHE B 220     180.976 174.668 211.321  1.00 55.14           C  
ATOM   8487  O   PHE B 220     179.978 174.961 210.662  1.00 54.63           O  
ATOM   8488  CB  PHE B 220     182.938 174.931 209.856  1.00 54.88           C  
ATOM   8489  CG  PHE B 220     183.410 176.078 210.668  1.00 54.21           C  
ATOM   8490  CD1 PHE B 220     184.595 176.003 211.357  1.00 53.81           C  
ATOM   8491  CD2 PHE B 220     182.659 177.220 210.774  1.00 53.67           C  
ATOM   8492  CE1 PHE B 220     185.021 177.044 212.124  1.00 53.22           C  
ATOM   8493  CE2 PHE B 220     183.079 178.264 211.545  1.00 54.15           C  
ATOM   8494  CZ  PHE B 220     184.262 178.179 212.219  1.00 54.41           C  
ATOM   8495  N   SER B 221     181.136 174.988 212.593  1.00 54.92           N  
ATOM   8496  CA  SER B 221     180.187 175.788 213.342  1.00 54.62           C  
ATOM   8497  C   SER B 221     180.925 176.482 214.465  1.00 54.70           C  
ATOM   8498  O   SER B 221     181.994 176.029 214.873  1.00 54.98           O  
ATOM   8499  CB  SER B 221     179.080 174.918 213.894  1.00 55.48           C  
ATOM   8500  OG  SER B 221     179.578 174.003 214.830  1.00 55.58           O  
ATOM   8501  N   ALA B 222     180.357 177.557 214.987  1.00 54.56           N  
ATOM   8502  CA  ALA B 222     180.976 178.236 216.112  1.00 55.49           C  
ATOM   8503  C   ALA B 222     180.108 178.114 217.345  1.00 56.00           C  
ATOM   8504  O   ALA B 222     178.880 178.117 217.260  1.00 56.43           O  
ATOM   8505  CB  ALA B 222     181.230 179.693 215.786  1.00 54.56           C  
ATOM   8506  N   LEU B 223     180.762 178.046 218.491  1.00 55.63           N  
ATOM   8507  CA  LEU B 223     180.096 177.936 219.780  1.00 57.59           C  
ATOM   8508  C   LEU B 223     179.975 179.301 220.434  1.00 58.01           C  
ATOM   8509  O   LEU B 223     180.798 180.184 220.189  1.00 57.41           O  
ATOM   8510  CB  LEU B 223     180.898 177.002 220.687  1.00 57.57           C  
ATOM   8511  CG  LEU B 223     180.706 175.484 220.506  1.00 57.16           C  
ATOM   8512  CD1 LEU B 223     180.988 175.055 219.071  1.00 57.45           C  
ATOM   8513  CD2 LEU B 223     181.644 174.794 221.443  1.00 57.23           C  
ATOM   8514  N   GLU B 224     178.958 179.471 221.273  1.00 58.29           N  
ATOM   8515  CA  GLU B 224     178.743 180.752 221.940  1.00 58.05           C  
ATOM   8516  C   GLU B 224     178.671 180.581 223.449  1.00 60.48           C  
ATOM   8517  O   GLU B 224     178.249 179.528 223.923  1.00 53.83           O  
ATOM   8518  CB  GLU B 224     177.455 181.378 221.406  1.00 58.22           C  
ATOM   8519  N   PRO B 225     179.094 181.590 224.228  1.00 59.87           N  
ATOM   8520  CA  PRO B 225     179.125 181.570 225.673  1.00 59.86           C  
ATOM   8521  C   PRO B 225     177.734 181.521 226.248  1.00 60.36           C  
ATOM   8522  O   PRO B 225     176.873 182.303 225.849  1.00 60.62           O  
ATOM   8523  CB  PRO B 225     179.824 182.889 226.016  1.00 60.26           C  
ATOM   8524  CG  PRO B 225     179.581 183.784 224.821  1.00 59.37           C  
ATOM   8525  CD  PRO B 225     179.532 182.863 223.628  1.00 59.42           C  
ATOM   8526  N   LEU B 226     177.530 180.636 227.210  1.00 60.50           N  
ATOM   8527  CA  LEU B 226     176.236 180.539 227.864  1.00 62.06           C  
ATOM   8528  C   LEU B 226     176.358 180.791 229.350  1.00 62.51           C  
ATOM   8529  O   LEU B 226     175.470 181.375 229.970  1.00 63.28           O  
ATOM   8530  CB  LEU B 226     175.615 179.159 227.660  1.00 61.36           C  
ATOM   8531  CG  LEU B 226     175.370 178.703 226.216  1.00 60.75           C  
ATOM   8532  CD1 LEU B 226     174.747 177.334 226.268  1.00 59.88           C  
ATOM   8533  CD2 LEU B 226     174.479 179.682 225.468  1.00 60.71           C  
ATOM   8534  N   VAL B 227     177.442 180.299 229.931  1.00 63.04           N  
ATOM   8535  CA  VAL B 227     177.616 180.360 231.369  1.00 64.13           C  
ATOM   8536  C   VAL B 227     178.937 181.008 231.733  1.00 65.32           C  
ATOM   8537  O   VAL B 227     179.959 180.772 231.088  1.00 66.07           O  
ATOM   8538  CB  VAL B 227     177.521 178.953 231.985  1.00 64.92           C  
ATOM   8539  CG1 VAL B 227     177.741 179.008 233.484  1.00 67.28           C  
ATOM   8540  CG2 VAL B 227     176.166 178.352 231.672  1.00 65.58           C  
ATOM   8541  N   ASP B 228     178.900 181.838 232.761  1.00 67.15           N  
ATOM   8542  CA  ASP B 228     180.078 182.517 233.270  1.00 68.26           C  
ATOM   8543  C   ASP B 228     180.089 182.408 234.792  1.00 69.07           C  
ATOM   8544  O   ASP B 228     179.222 182.968 235.466  1.00 69.54           O  
ATOM   8545  CB  ASP B 228     180.079 183.972 232.805  1.00 68.64           C  
ATOM   8546  CG  ASP B 228     181.316 184.708 233.181  1.00 68.85           C  
ATOM   8547  OD1 ASP B 228     181.988 184.265 234.069  1.00 69.81           O  
ATOM   8548  OD2 ASP B 228     181.610 185.702 232.553  1.00 69.42           O  
ATOM   8549  N   LEU B 229     181.004 181.598 235.321  1.00 69.07           N  
ATOM   8550  CA  LEU B 229     181.037 181.302 236.746  1.00 71.79           C  
ATOM   8551  C   LEU B 229     182.207 182.001 237.450  1.00 71.66           C  
ATOM   8552  O   LEU B 229     183.358 181.571 237.309  1.00 71.86           O  
ATOM   8553  CB  LEU B 229     181.186 179.792 236.967  1.00 71.18           C  
ATOM   8554  CG  LEU B 229     180.183 178.887 236.284  1.00 71.04           C  
ATOM   8555  CD1 LEU B 229     180.547 177.442 236.595  1.00 71.07           C  
ATOM   8556  CD2 LEU B 229     178.781 179.207 236.767  1.00 72.10           C  
ATOM   8557  N   PRO B 230     181.950 183.034 238.266  1.00 72.26           N  
ATOM   8558  CA  PRO B 230     182.928 183.842 238.974  1.00 72.07           C  
ATOM   8559  C   PRO B 230     183.371 183.110 240.228  1.00 72.83           C  
ATOM   8560  O   PRO B 230     183.152 183.580 241.343  1.00 73.32           O  
ATOM   8561  CB  PRO B 230     182.123 185.088 239.306  1.00 71.90           C  
ATOM   8562  CG  PRO B 230     180.723 184.551 239.533  1.00 72.81           C  
ATOM   8563  CD  PRO B 230     180.563 183.417 238.540  1.00 72.84           C  
ATOM   8564  N   ILE B 231     183.938 181.933 240.032  1.00 72.53           N  
ATOM   8565  CA  ILE B 231     184.255 181.031 241.127  1.00 72.72           C  
ATOM   8566  C   ILE B 231     185.725 181.017 241.559  1.00 73.25           C  
ATOM   8567  O   ILE B 231     186.022 180.848 242.740  1.00 73.65           O  
ATOM   8568  CB  ILE B 231     183.707 179.640 240.769  1.00 72.92           C  
ATOM   8569  CG1 ILE B 231     184.368 179.109 239.458  1.00 72.82           C  
ATOM   8570  CG2 ILE B 231     182.185 179.747 240.635  1.00 73.65           C  
ATOM   8571  CD1 ILE B 231     183.992 177.708 239.067  1.00 72.78           C  
ATOM   8572  N   GLY B 232     186.654 181.154 240.619  1.00 73.55           N  
ATOM   8573  CA  GLY B 232     188.070 181.166 240.985  1.00 73.12           C  
ATOM   8574  C   GLY B 232     188.609 179.797 241.406  1.00 73.06           C  
ATOM   8575  O   GLY B 232     189.550 179.713 242.195  1.00 73.28           O  
ATOM   8576  N   ILE B 233     188.011 178.729 240.897  1.00 73.74           N  
ATOM   8577  CA  ILE B 233     188.432 177.381 241.253  1.00 73.31           C  
ATOM   8578  C   ILE B 233     189.671 176.972 240.462  1.00 72.01           C  
ATOM   8579  O   ILE B 233     189.712 177.142 239.244  1.00 71.49           O  
ATOM   8580  CB  ILE B 233     187.286 176.366 241.006  1.00 72.71           C  
ATOM   8581  CG1 ILE B 233     186.052 176.728 241.868  1.00 72.76           C  
ATOM   8582  CG2 ILE B 233     187.737 174.924 241.277  1.00 72.56           C  
ATOM   8583  CD1 ILE B 233     186.262 176.709 243.366  1.00 72.30           C  
ATOM   8584  N   ASN B 234     190.673 176.406 241.169  1.00 71.93           N  
ATOM   8585  CA  ASN B 234     191.896 175.903 240.543  1.00 71.59           C  
ATOM   8586  C   ASN B 234     191.599 174.540 239.908  1.00 71.58           C  
ATOM   8587  O   ASN B 234     191.297 173.575 240.594  1.00 71.85           O  
ATOM   8588  CB  ASN B 234     193.020 175.787 241.591  1.00 71.05           C  
ATOM   8589  CG  ASN B 234     194.397 175.381 241.000  1.00 71.30           C  
ATOM   8590  OD1 ASN B 234     194.694 175.657 239.825  1.00 71.73           O  
ATOM   8591  ND2 ASN B 234     195.226 174.735 241.821  1.00 71.68           N  
ATOM   8592  N   ILE B 235     191.587 174.520 238.561  1.00 70.70           N  
ATOM   8593  CA  ILE B 235     191.236 173.339 237.781  1.00 69.39           C  
ATOM   8594  C   ILE B 235     192.416 172.882 236.958  1.00 68.77           C  
ATOM   8595  O   ILE B 235     192.869 173.584 236.055  1.00 68.57           O  
ATOM   8596  CB  ILE B 235     190.051 173.624 236.858  1.00 68.27           C  
ATOM   8597  CG1 ILE B 235     188.838 174.062 237.696  1.00 69.62           C  
ATOM   8598  CG2 ILE B 235     189.749 172.374 236.060  1.00 68.80           C  
ATOM   8599  CD1 ILE B 235     187.694 174.643 236.900  1.00 68.56           C  
ATOM   8600  N   THR B 236     192.904 171.699 237.274  1.00 68.98           N  
ATOM   8601  CA  THR B 236     194.039 171.121 236.589  1.00 68.95           C  
ATOM   8602  C   THR B 236     193.631 169.767 236.065  1.00 68.38           C  
ATOM   8603  O   THR B 236     194.282 169.196 235.186  1.00 67.86           O  
ATOM   8604  CB  THR B 236     195.234 170.969 237.542  1.00 69.55           C  
ATOM   8605  OG1 THR B 236     194.905 170.032 238.571  1.00 69.94           O  
ATOM   8606  CG2 THR B 236     195.546 172.310 238.184  1.00 70.71           C  
ATOM   8607  N   ARG B 237     192.553 169.261 236.649  1.00 67.47           N  
ATOM   8608  CA  ARG B 237     192.041 167.918 236.423  1.00 67.32           C  
ATOM   8609  C   ARG B 237     190.511 167.910 236.404  1.00 68.35           C  
ATOM   8610  O   ARG B 237     189.879 168.688 237.120  1.00 66.79           O  
ATOM   8611  CB  ARG B 237     192.587 167.037 237.534  1.00 68.81           C  
ATOM   8612  CG  ARG B 237     192.246 165.607 237.486  1.00 68.29           C  
ATOM   8613  CD  ARG B 237     193.050 164.831 238.491  1.00 69.11           C  
ATOM   8614  NE  ARG B 237     194.455 164.766 238.119  1.00 69.63           N  
ATOM   8615  CZ  ARG B 237     194.982 163.872 237.252  1.00 69.65           C  
ATOM   8616  NH1 ARG B 237     194.213 162.972 236.677  1.00 68.53           N  
ATOM   8617  NH2 ARG B 237     196.275 163.903 236.981  1.00 68.66           N  
ATOM   8618  N   PHE B 238     189.901 167.039 235.596  1.00 67.63           N  
ATOM   8619  CA  PHE B 238     188.445 166.968 235.582  1.00 67.61           C  
ATOM   8620  C   PHE B 238     187.936 165.569 235.242  1.00 67.58           C  
ATOM   8621  O   PHE B 238     188.666 164.739 234.704  1.00 66.46           O  
ATOM   8622  CB  PHE B 238     187.862 167.938 234.557  1.00 67.43           C  
ATOM   8623  CG  PHE B 238     187.939 167.467 233.148  1.00 66.63           C  
ATOM   8624  CD1 PHE B 238     186.816 166.900 232.559  1.00 66.12           C  
ATOM   8625  CD2 PHE B 238     189.095 167.552 232.411  1.00 66.42           C  
ATOM   8626  CE1 PHE B 238     186.850 166.439 231.265  1.00 65.07           C  
ATOM   8627  CE2 PHE B 238     189.126 167.087 231.111  1.00 64.42           C  
ATOM   8628  CZ  PHE B 238     188.005 166.534 230.543  1.00 64.23           C  
ATOM   8629  N   GLN B 239     186.668 165.314 235.536  1.00 68.25           N  
ATOM   8630  CA  GLN B 239     186.060 164.031 235.210  1.00 66.46           C  
ATOM   8631  C   GLN B 239     184.672 164.196 234.613  1.00 67.68           C  
ATOM   8632  O   GLN B 239     183.897 165.046 235.046  1.00 66.37           O  
ATOM   8633  CB  GLN B 239     185.979 163.154 236.453  1.00 68.77           C  
ATOM   8634  N   THR B 240     184.353 163.373 233.623  1.00 66.81           N  
ATOM   8635  CA  THR B 240     183.031 163.386 233.007  1.00 65.37           C  
ATOM   8636  C   THR B 240     182.125 162.388 233.715  1.00 66.11           C  
ATOM   8637  O   THR B 240     182.511 161.244 233.951  1.00 66.64           O  
ATOM   8638  CB  THR B 240     183.116 163.049 231.506  1.00 65.29           C  
ATOM   8639  OG1 THR B 240     183.964 164.000 230.856  1.00 65.04           O  
ATOM   8640  CG2 THR B 240     181.739 163.099 230.850  1.00 64.30           C  
ATOM   8641  N   LEU B 241     180.926 162.829 234.067  1.00 67.49           N  
ATOM   8642  CA  LEU B 241     179.960 162.002 234.779  1.00 67.77           C  
ATOM   8643  C   LEU B 241     178.876 161.446 233.855  1.00 67.92           C  
ATOM   8644  O   LEU B 241     178.098 162.210 233.267  1.00 68.00           O  
ATOM   8645  CB  LEU B 241     179.298 162.823 235.890  1.00 68.29           C  
ATOM   8646  CG  LEU B 241     180.249 163.444 236.913  1.00 67.37           C  
ATOM   8647  CD1 LEU B 241     179.449 164.312 237.864  1.00 68.05           C  
ATOM   8648  CD2 LEU B 241     180.982 162.329 237.667  1.00 69.86           C  
ATOM   8649  N   LEU B 242     178.817 160.104 233.764  1.00 67.31           N  
ATOM   8650  CA  LEU B 242     177.898 159.358 232.901  1.00 67.73           C  
ATOM   8651  C   LEU B 242     176.711 158.837 233.718  1.00 68.74           C  
ATOM   8652  O   LEU B 242     176.706 157.707 234.214  1.00 70.79           O  
ATOM   8653  CB  LEU B 242     178.656 158.187 232.185  1.00 66.91           C  
ATOM   8654  CG  LEU B 242     179.466 158.556 230.839  1.00 66.54           C  
ATOM   8655  CD1 LEU B 242     180.697 159.459 231.173  1.00 66.25           C  
ATOM   8656  CD2 LEU B 242     179.916 157.252 230.117  1.00 64.74           C  
ATOM   8657  N   ALA B 263     176.843 156.129 224.636  1.00 62.38           N  
ATOM   8658  CA  ALA B 263     177.285 157.514 224.537  1.00 63.71           C  
ATOM   8659  C   ALA B 263     178.770 157.575 224.193  1.00 62.03           C  
ATOM   8660  O   ALA B 263     179.601 156.998 224.906  1.00 61.41           O  
ATOM   8661  CB  ALA B 263     177.032 158.266 225.847  1.00 64.82           C  
ATOM   8662  N   ALA B 264     179.105 158.293 223.109  1.00 61.91           N  
ATOM   8663  CA  ALA B 264     180.486 158.506 222.675  1.00 62.24           C  
ATOM   8664  C   ALA B 264     180.874 159.947 222.945  1.00 62.61           C  
ATOM   8665  O   ALA B 264     180.073 160.860 222.741  1.00 61.99           O  
ATOM   8666  CB  ALA B 264     180.633 158.179 221.201  1.00 60.50           C  
ATOM   8667  N   TYR B 265     182.101 160.169 223.381  1.00 61.62           N  
ATOM   8668  CA  TYR B 265     182.539 161.537 223.602  1.00 60.89           C  
ATOM   8669  C   TYR B 265     184.014 161.726 223.348  1.00 71.73           C  
ATOM   8670  O   TYR B 265     184.797 160.778 223.364  1.00 45.88           O  
ATOM   8671  CB  TYR B 265     182.119 162.008 224.988  1.00 61.48           C  
ATOM   8672  CG  TYR B 265     182.657 161.230 226.116  1.00 61.95           C  
ATOM   8673  CD1 TYR B 265     183.762 161.669 226.812  1.00 61.47           C  
ATOM   8674  CD2 TYR B 265     182.029 160.060 226.466  1.00 61.97           C  
ATOM   8675  CE1 TYR B 265     184.225 160.931 227.873  1.00 62.13           C  
ATOM   8676  CE2 TYR B 265     182.484 159.329 227.505  1.00 63.41           C  
ATOM   8677  CZ  TYR B 265     183.571 159.752 228.213  1.00 60.48           C  
ATOM   8678  OH  TYR B 265     184.012 158.997 229.255  1.00 63.06           O  
ATOM   8679  N   TYR B 266     184.384 162.967 223.088  1.00 60.03           N  
ATOM   8680  CA  TYR B 266     185.729 163.287 222.694  1.00 59.04           C  
ATOM   8681  C   TYR B 266     186.323 164.377 223.553  1.00 58.51           C  
ATOM   8682  O   TYR B 266     185.665 165.371 223.862  1.00 59.69           O  
ATOM   8683  CB  TYR B 266     185.701 163.740 221.241  1.00 58.15           C  
ATOM   8684  CG  TYR B 266     184.988 162.760 220.365  1.00 59.33           C  
ATOM   8685  CD1 TYR B 266     183.615 162.868 220.217  1.00 58.65           C  
ATOM   8686  CD2 TYR B 266     185.670 161.755 219.729  1.00 60.04           C  
ATOM   8687  CE1 TYR B 266     182.931 161.971 219.444  1.00 59.32           C  
ATOM   8688  CE2 TYR B 266     184.980 160.860 218.948  1.00 59.10           C  
ATOM   8689  CZ  TYR B 266     183.619 160.967 218.812  1.00 58.97           C  
ATOM   8690  OH  TYR B 266     182.947 160.067 218.046  1.00 58.49           O  
ATOM   8691  N   VAL B 267     187.585 164.215 223.908  1.00 59.14           N  
ATOM   8692  CA  VAL B 267     188.258 165.239 224.685  1.00 56.83           C  
ATOM   8693  C   VAL B 267     189.499 165.773 223.999  1.00 56.82           C  
ATOM   8694  O   VAL B 267     190.443 165.032 223.710  1.00 58.85           O  
ATOM   8695  CB  VAL B 267     188.636 164.689 226.065  1.00 58.26           C  
ATOM   8696  CG1 VAL B 267     189.370 165.756 226.877  1.00 59.29           C  
ATOM   8697  CG2 VAL B 267     187.363 164.241 226.773  1.00 59.04           C  
ATOM   8698  N   GLY B 268     189.502 167.074 223.764  1.00 57.19           N  
ATOM   8699  CA  GLY B 268     190.631 167.743 223.151  1.00 57.63           C  
ATOM   8700  C   GLY B 268     191.136 168.828 224.069  1.00 58.07           C  
ATOM   8701  O   GLY B 268     190.551 169.083 225.120  1.00 59.62           O  
ATOM   8702  N   TYR B 269     192.200 169.495 223.672  1.00 57.73           N  
ATOM   8703  CA  TYR B 269     192.732 170.551 224.509  1.00 58.26           C  
ATOM   8704  C   TYR B 269     192.949 171.804 223.711  1.00 56.39           C  
ATOM   8705  O   TYR B 269     193.309 171.749 222.536  1.00 56.41           O  
ATOM   8706  CB  TYR B 269     194.004 170.081 225.189  1.00 58.42           C  
ATOM   8707  CG  TYR B 269     193.734 168.894 226.053  1.00 59.45           C  
ATOM   8708  CD1 TYR B 269     193.370 169.073 227.362  1.00 60.87           C  
ATOM   8709  CD2 TYR B 269     193.821 167.620 225.525  1.00 59.86           C  
ATOM   8710  CE1 TYR B 269     193.097 167.991 228.143  1.00 61.33           C  
ATOM   8711  CE2 TYR B 269     193.544 166.534 226.310  1.00 60.04           C  
ATOM   8712  CZ  TYR B 269     193.183 166.714 227.615  1.00 60.94           C  
ATOM   8713  OH  TYR B 269     192.899 165.623 228.399  1.00 63.03           O  
ATOM   8714  N   LEU B 270     192.754 172.929 224.363  1.00 57.47           N  
ATOM   8715  CA  LEU B 270     192.878 174.206 223.701  1.00 55.70           C  
ATOM   8716  C   LEU B 270     194.312 174.693 223.741  1.00 55.41           C  
ATOM   8717  O   LEU B 270     195.056 174.381 224.670  1.00 56.63           O  
ATOM   8718  CB  LEU B 270     192.002 175.230 224.396  1.00 56.99           C  
ATOM   8719  CG  LEU B 270     190.533 174.881 224.597  1.00 57.02           C  
ATOM   8720  CD1 LEU B 270     189.902 175.998 225.377  1.00 57.95           C  
ATOM   8721  CD2 LEU B 270     189.831 174.683 223.273  1.00 56.61           C  
ATOM   8722  N   GLN B 271     194.693 175.468 222.735  1.00 55.48           N  
ATOM   8723  CA  GLN B 271     196.017 176.061 222.668  1.00 54.68           C  
ATOM   8724  C   GLN B 271     195.915 177.527 222.254  1.00 56.83           C  
ATOM   8725  O   GLN B 271     195.000 177.893 221.514  1.00 51.94           O  
ATOM   8726  CB  GLN B 271     196.873 175.284 221.673  1.00 54.62           C  
ATOM   8727  CG  GLN B 271     197.140 173.850 222.068  1.00 55.10           C  
ATOM   8728  CD  GLN B 271     198.063 173.160 221.096  1.00 54.40           C  
ATOM   8729  OE1 GLN B 271     198.550 173.781 220.146  1.00 54.21           O  
ATOM   8730  NE2 GLN B 271     198.311 171.877 221.318  1.00 53.77           N  
ATOM   8731  N   PRO B 272     196.859 178.382 222.669  1.00 54.67           N  
ATOM   8732  CA  PRO B 272     196.922 179.806 222.375  1.00 54.50           C  
ATOM   8733  C   PRO B 272     197.390 180.082 220.954  1.00 53.93           C  
ATOM   8734  O   PRO B 272     198.483 180.604 220.731  1.00 54.32           O  
ATOM   8735  CB  PRO B 272     197.927 180.296 223.417  1.00 54.69           C  
ATOM   8736  CG  PRO B 272     198.850 179.120 223.620  1.00 54.31           C  
ATOM   8737  CD  PRO B 272     197.948 177.903 223.537  1.00 54.45           C  
ATOM   8738  N   ARG B 273     196.558 179.690 220.002  1.00 54.03           N  
ATOM   8739  CA  ARG B 273     196.842 179.815 218.583  1.00 52.86           C  
ATOM   8740  C   ARG B 273     196.064 180.975 217.985  1.00 53.11           C  
ATOM   8741  O   ARG B 273     194.970 181.309 218.450  1.00 54.05           O  
ATOM   8742  CB  ARG B 273     196.494 178.512 217.887  1.00 52.55           C  
ATOM   8743  CG  ARG B 273     197.351 177.346 218.343  1.00 53.01           C  
ATOM   8744  CD  ARG B 273     196.764 176.026 218.009  1.00 53.08           C  
ATOM   8745  NE  ARG B 273     196.907 175.627 216.625  1.00 52.25           N  
ATOM   8746  CZ  ARG B 273     197.979 174.996 216.113  1.00 51.62           C  
ATOM   8747  NH1 ARG B 273     199.032 174.722 216.859  1.00 52.30           N  
ATOM   8748  NH2 ARG B 273     197.945 174.649 214.850  1.00 51.02           N  
ATOM   8749  N   THR B 274     196.636 181.591 216.960  1.00 52.21           N  
ATOM   8750  CA  THR B 274     195.984 182.691 216.270  1.00 51.07           C  
ATOM   8751  C   THR B 274     195.056 182.163 215.195  1.00 51.77           C  
ATOM   8752  O   THR B 274     195.402 181.220 214.482  1.00 51.60           O  
ATOM   8753  CB  THR B 274     197.010 183.646 215.633  1.00 51.72           C  
ATOM   8754  OG1 THR B 274     197.886 184.156 216.644  1.00 52.08           O  
ATOM   8755  CG2 THR B 274     196.304 184.820 214.953  1.00 51.66           C  
ATOM   8756  N   PHE B 275     193.867 182.742 215.129  1.00 50.39           N  
ATOM   8757  CA  PHE B 275     192.887 182.420 214.108  1.00 50.39           C  
ATOM   8758  C   PHE B 275     192.385 183.631 213.353  1.00 52.33           C  
ATOM   8759  O   PHE B 275     192.175 184.703 213.924  1.00 52.27           O  
ATOM   8760  CB  PHE B 275     191.683 181.695 214.703  1.00 51.33           C  
ATOM   8761  CG  PHE B 275     191.925 180.272 215.013  1.00 51.57           C  
ATOM   8762  CD1 PHE B 275     192.667 179.874 216.096  1.00 53.03           C  
ATOM   8763  CD2 PHE B 275     191.382 179.310 214.196  1.00 51.91           C  
ATOM   8764  CE1 PHE B 275     192.869 178.538 216.341  1.00 52.10           C  
ATOM   8765  CE2 PHE B 275     191.574 177.988 214.445  1.00 51.75           C  
ATOM   8766  CZ  PHE B 275     192.319 177.594 215.518  1.00 52.22           C  
ATOM   8767  N   LEU B 276     192.118 183.427 212.074  1.00 50.56           N  
ATOM   8768  CA  LEU B 276     191.432 184.436 211.285  1.00 49.86           C  
ATOM   8769  C   LEU B 276     189.983 183.998 211.197  1.00 51.92           C  
ATOM   8770  O   LEU B 276     189.690 182.932 210.660  1.00 50.65           O  
ATOM   8771  CB  LEU B 276     192.045 184.551 209.883  1.00 50.89           C  
ATOM   8772  CG  LEU B 276     191.427 185.593 208.932  1.00 50.16           C  
ATOM   8773  CD1 LEU B 276     191.686 187.004 209.464  1.00 49.79           C  
ATOM   8774  CD2 LEU B 276     192.022 185.408 207.531  1.00 48.65           C  
ATOM   8775  N   LEU B 277     189.078 184.780 211.760  1.00 50.74           N  
ATOM   8776  CA  LEU B 277     187.678 184.384 211.799  1.00 50.54           C  
ATOM   8777  C   LEU B 277     186.851 185.139 210.777  1.00 51.72           C  
ATOM   8778  O   LEU B 277     186.924 186.365 210.682  1.00 50.71           O  
ATOM   8779  CB  LEU B 277     187.116 184.632 213.201  1.00 51.75           C  
ATOM   8780  CG  LEU B 277     187.873 183.954 214.370  1.00 52.20           C  
ATOM   8781  CD1 LEU B 277     187.223 184.366 215.671  1.00 53.65           C  
ATOM   8782  CD2 LEU B 277     187.847 182.441 214.212  1.00 52.51           C  
ATOM   8783  N   LYS B 278     186.056 184.400 210.016  1.00 50.61           N  
ATOM   8784  CA  LYS B 278     185.211 184.991 208.991  1.00 50.82           C  
ATOM   8785  C   LYS B 278     183.779 185.172 209.446  1.00 53.30           C  
ATOM   8786  O   LYS B 278     183.049 184.191 209.625  1.00 52.39           O  
ATOM   8787  CB  LYS B 278     185.240 184.128 207.734  1.00 51.22           C  
ATOM   8788  CG  LYS B 278     184.396 184.634 206.584  1.00 51.38           C  
ATOM   8789  CD  LYS B 278     184.584 183.766 205.354  1.00 51.02           C  
ATOM   8790  CE  LYS B 278     183.752 184.272 204.192  1.00 51.47           C  
ATOM   8791  NZ  LYS B 278     183.908 183.416 202.988  1.00 51.19           N  
ATOM   8792  N   TYR B 279     183.374 186.436 209.599  1.00 51.77           N  
ATOM   8793  CA  TYR B 279     182.026 186.795 210.022  1.00 52.52           C  
ATOM   8794  C   TYR B 279     181.176 187.166 208.815  1.00 53.14           C  
ATOM   8795  O   TYR B 279     181.553 188.036 208.025  1.00 52.76           O  
ATOM   8796  CB  TYR B 279     182.063 187.983 210.980  1.00 52.93           C  
ATOM   8797  CG  TYR B 279     182.656 187.699 212.325  1.00 53.10           C  
ATOM   8798  CD1 TYR B 279     184.020 187.789 212.521  1.00 52.04           C  
ATOM   8799  CD2 TYR B 279     181.832 187.373 213.372  1.00 53.82           C  
ATOM   8800  CE1 TYR B 279     184.549 187.546 213.766  1.00 52.51           C  
ATOM   8801  CE2 TYR B 279     182.358 187.135 214.615  1.00 53.71           C  
ATOM   8802  CZ  TYR B 279     183.714 187.222 214.813  1.00 53.72           C  
ATOM   8803  OH  TYR B 279     184.245 186.988 216.055  1.00 53.88           O  
ATOM   8804  N   ASN B 280     180.006 186.551 208.697  1.00 53.17           N  
ATOM   8805  CA  ASN B 280     179.101 186.837 207.589  1.00 52.67           C  
ATOM   8806  C   ASN B 280     178.237 188.048 207.906  1.00 53.51           C  
ATOM   8807  O   ASN B 280     178.480 188.757 208.884  1.00 53.67           O  
ATOM   8808  CB  ASN B 280     178.241 185.636 207.241  1.00 53.56           C  
ATOM   8809  CG  ASN B 280     177.223 185.297 208.289  1.00 55.65           C  
ATOM   8810  OD1 ASN B 280     177.058 186.023 209.281  1.00 54.82           O  
ATOM   8811  ND2 ASN B 280     176.516 184.216 208.075  1.00 54.52           N  
ATOM   8812  N   GLU B 281     177.249 188.313 207.060  1.00 53.09           N  
ATOM   8813  CA  GLU B 281     176.376 189.480 207.221  1.00 54.34           C  
ATOM   8814  C   GLU B 281     175.605 189.507 208.554  1.00 55.06           C  
ATOM   8815  O   GLU B 281     175.347 190.587 209.093  1.00 54.10           O  
ATOM   8816  CB  GLU B 281     175.379 189.548 206.060  1.00 53.96           C  
ATOM   8817  CG  GLU B 281     176.010 189.821 204.701  1.00 53.75           C  
ATOM   8818  CD  GLU B 281     176.558 188.587 204.041  1.00 53.79           C  
ATOM   8819  OE1 GLU B 281     176.452 187.536 204.622  1.00 53.87           O  
ATOM   8820  OE2 GLU B 281     177.084 188.695 202.962  1.00 53.70           O  
ATOM   8821  N   ASN B 282     175.256 188.327 209.093  1.00 54.38           N  
ATOM   8822  CA  ASN B 282     174.509 188.181 210.345  1.00 54.54           C  
ATOM   8823  C   ASN B 282     175.435 188.124 211.573  1.00 54.88           C  
ATOM   8824  O   ASN B 282     174.970 187.869 212.687  1.00 55.36           O  
ATOM   8825  CB  ASN B 282     173.621 186.934 210.297  1.00 55.36           C  
ATOM   8826  CG  ASN B 282     172.528 186.980 209.213  1.00 56.81           C  
ATOM   8827  OD1 ASN B 282     172.532 187.852 208.330  1.00 55.52           O  
ATOM   8828  ND2 ASN B 282     171.595 186.036 209.284  1.00 57.07           N  
ATOM   8829  N   GLY B 283     176.756 188.307 211.379  1.00 54.80           N  
ATOM   8830  CA  GLY B 283     177.751 188.285 212.448  1.00 54.68           C  
ATOM   8831  C   GLY B 283     178.051 186.880 212.937  1.00 54.41           C  
ATOM   8832  O   GLY B 283     178.510 186.686 214.062  1.00 54.48           O  
ATOM   8833  N   THR B 284     177.781 185.902 212.095  1.00 54.12           N  
ATOM   8834  CA  THR B 284     178.014 184.519 212.435  1.00 54.54           C  
ATOM   8835  C   THR B 284     179.354 184.088 211.896  1.00 53.32           C  
ATOM   8836  O   THR B 284     179.695 184.392 210.754  1.00 50.28           O  
ATOM   8837  CB  THR B 284     176.895 183.623 211.880  1.00 54.71           C  
ATOM   8838  OG1 THR B 284     175.655 183.986 212.495  1.00 54.48           O  
ATOM   8839  CG2 THR B 284     177.184 182.157 212.142  1.00 54.61           C  
ATOM   8840  N   ILE B 285     180.128 183.385 212.705  1.00 54.84           N  
ATOM   8841  CA  ILE B 285     181.397 182.909 212.205  1.00 53.41           C  
ATOM   8842  C   ILE B 285     181.086 181.713 211.328  1.00 53.34           C  
ATOM   8843  O   ILE B 285     180.520 180.725 211.799  1.00 53.43           O  
ATOM   8844  CB  ILE B 285     182.336 182.503 213.353  1.00 53.77           C  
ATOM   8845  CG1 ILE B 285     182.618 183.705 214.247  1.00 54.17           C  
ATOM   8846  CG2 ILE B 285     183.645 181.964 212.780  1.00 52.78           C  
ATOM   8847  CD1 ILE B 285     183.257 183.350 215.584  1.00 54.22           C  
ATOM   8848  N   THR B 286     181.432 181.813 210.053  1.00 53.28           N  
ATOM   8849  CA  THR B 286     181.112 180.757 209.108  1.00 53.35           C  
ATOM   8850  C   THR B 286     182.346 179.990 208.704  1.00 52.87           C  
ATOM   8851  O   THR B 286     182.246 178.857 208.237  1.00 52.98           O  
ATOM   8852  CB  THR B 286     180.420 181.310 207.857  1.00 53.79           C  
ATOM   8853  OG1 THR B 286     181.295 182.226 207.190  1.00 53.00           O  
ATOM   8854  CG2 THR B 286     179.140 182.026 208.249  1.00 54.05           C  
ATOM   8855  N   ASP B 287     183.510 180.590 208.907  1.00 51.72           N  
ATOM   8856  CA  ASP B 287     184.749 179.885 208.600  1.00 52.28           C  
ATOM   8857  C   ASP B 287     185.876 180.370 209.503  1.00 52.94           C  
ATOM   8858  O   ASP B 287     185.693 181.307 210.286  1.00 52.32           O  
ATOM   8859  CB  ASP B 287     185.101 180.104 207.121  1.00 51.78           C  
ATOM   8860  CG  ASP B 287     185.953 179.002 206.489  1.00 52.10           C  
ATOM   8861  OD1 ASP B 287     186.547 178.244 207.214  1.00 51.77           O  
ATOM   8862  OD2 ASP B 287     186.008 178.944 205.284  1.00 52.14           O  
ATOM   8863  N   ALA B 288     187.042 179.746 209.387  1.00 51.56           N  
ATOM   8864  CA  ALA B 288     188.199 180.159 210.167  1.00 50.37           C  
ATOM   8865  C   ALA B 288     189.498 179.591 209.604  1.00 50.69           C  
ATOM   8866  O   ALA B 288     189.531 178.469 209.100  1.00 50.87           O  
ATOM   8867  CB  ALA B 288     188.038 179.723 211.612  1.00 51.62           C  
ATOM   8868  N   VAL B 289     190.587 180.323 209.788  1.00 50.44           N  
ATOM   8869  CA  VAL B 289     191.902 179.817 209.419  1.00 49.79           C  
ATOM   8870  C   VAL B 289     192.770 179.637 210.638  1.00 51.68           C  
ATOM   8871  O   VAL B 289     193.006 180.582 211.388  1.00 49.85           O  
ATOM   8872  CB  VAL B 289     192.634 180.781 208.465  1.00 50.08           C  
ATOM   8873  CG1 VAL B 289     194.010 180.246 208.115  1.00 48.81           C  
ATOM   8874  CG2 VAL B 289     191.827 180.980 207.235  1.00 49.43           C  
ATOM   8875  N   ASP B 290     193.286 178.434 210.816  1.00 50.12           N  
ATOM   8876  CA  ASP B 290     194.221 178.189 211.900  1.00 50.92           C  
ATOM   8877  C   ASP B 290     195.604 178.594 211.406  1.00 49.37           C  
ATOM   8878  O   ASP B 290     196.189 177.901 210.569  1.00 49.17           O  
ATOM   8879  CB  ASP B 290     194.207 176.728 212.344  1.00 50.48           C  
ATOM   8880  CG  ASP B 290     195.207 176.482 213.467  1.00 49.63           C  
ATOM   8881  OD1 ASP B 290     196.087 177.310 213.619  1.00 51.49           O  
ATOM   8882  OD2 ASP B 290     195.116 175.483 214.163  1.00 52.05           O  
ATOM   8883  N   CYS B 291     196.102 179.737 211.882  1.00 49.06           N  
ATOM   8884  CA  CYS B 291     197.310 180.395 211.377  1.00 48.31           C  
ATOM   8885  C   CYS B 291     198.586 179.584 211.638  1.00 48.68           C  
ATOM   8886  O   CYS B 291     199.651 179.932 211.116  1.00 47.95           O  
ATOM   8887  CB  CYS B 291     197.466 181.783 212.011  1.00 50.44           C  
ATOM   8888  SG  CYS B 291     196.070 182.917 211.726  1.00 51.12           S  
ATOM   8889  N   ALA B 292     198.520 178.536 212.480  1.00 49.09           N  
ATOM   8890  CA  ALA B 292     199.666 177.690 212.826  1.00 48.96           C  
ATOM   8891  C   ALA B 292     199.515 176.268 212.281  1.00 49.03           C  
ATOM   8892  O   ALA B 292     200.296 175.383 212.634  1.00 48.70           O  
ATOM   8893  CB  ALA B 292     199.832 177.664 214.333  1.00 49.86           C  
ATOM   8894  N   LEU B 293     198.517 176.042 211.433  1.00 48.82           N  
ATOM   8895  CA  LEU B 293     198.261 174.713 210.879  1.00 47.67           C  
ATOM   8896  C   LEU B 293     199.257 174.269 209.812  1.00 47.73           C  
ATOM   8897  O   LEU B 293     199.647 173.102 209.774  1.00 47.98           O  
ATOM   8898  CB  LEU B 293     196.854 174.668 210.283  1.00 48.16           C  
ATOM   8899  CG  LEU B 293     196.392 173.340 209.643  1.00 48.78           C  
ATOM   8900  CD1 LEU B 293     196.411 172.219 210.667  1.00 50.21           C  
ATOM   8901  CD2 LEU B 293     194.995 173.541 209.087  1.00 49.72           C  
ATOM   8902  N   ASP B 294     199.645 175.185 208.934  1.00 47.57           N  
ATOM   8903  CA  ASP B 294     200.498 174.872 207.792  1.00 46.23           C  
ATOM   8904  C   ASP B 294     200.859 176.174 207.053  1.00 46.03           C  
ATOM   8905  O   ASP B 294     200.224 177.202 207.292  1.00 42.77           O  
ATOM   8906  CB  ASP B 294     199.776 173.855 206.877  1.00 46.08           C  
ATOM   8907  CG  ASP B 294     198.419 174.323 206.382  1.00 46.00           C  
ATOM   8908  OD1 ASP B 294     198.284 175.479 206.039  1.00 46.37           O  
ATOM   8909  OD2 ASP B 294     197.523 173.517 206.339  1.00 47.30           O  
ATOM   8910  N   PRO B 295     201.899 176.185 206.200  1.00 44.82           N  
ATOM   8911  CA  PRO B 295     202.342 177.318 205.404  1.00 43.77           C  
ATOM   8912  C   PRO B 295     201.251 178.010 204.597  1.00 46.66           C  
ATOM   8913  O   PRO B 295     201.244 179.234 204.494  1.00 44.50           O  
ATOM   8914  CB  PRO B 295     203.387 176.673 204.504  1.00 43.55           C  
ATOM   8915  CG  PRO B 295     203.936 175.543 205.326  1.00 44.22           C  
ATOM   8916  CD  PRO B 295     202.749 174.990 206.051  1.00 44.73           C  
ATOM   8917  N   LEU B 296     200.289 177.263 204.063  1.00 43.25           N  
ATOM   8918  CA  LEU B 296     199.241 177.932 203.306  1.00 43.37           C  
ATOM   8919  C   LEU B 296     198.351 178.745 204.220  1.00 46.23           C  
ATOM   8920  O   LEU B 296     197.937 179.853 203.869  1.00 44.92           O  
ATOM   8921  CB  LEU B 296     198.393 176.943 202.516  1.00 43.60           C  
ATOM   8922  CG  LEU B 296     197.225 177.566 201.699  1.00 44.41           C  
ATOM   8923  CD1 LEU B 296     197.741 178.625 200.704  1.00 44.59           C  
ATOM   8924  CD2 LEU B 296     196.512 176.458 200.963  1.00 44.10           C  
ATOM   8925  N   SER B 297     198.048 178.199 205.389  1.00 45.63           N  
ATOM   8926  CA  SER B 297     197.217 178.902 206.343  1.00 43.88           C  
ATOM   8927  C   SER B 297     197.948 180.146 206.823  1.00 48.49           C  
ATOM   8928  O   SER B 297     197.343 181.207 206.985  1.00 44.96           O  
ATOM   8929  CB  SER B 297     196.871 178.001 207.499  1.00 46.49           C  
ATOM   8930  OG  SER B 297     196.090 176.927 207.066  1.00 46.16           O  
ATOM   8931  N   GLU B 298     199.268 180.046 206.984  1.00 44.79           N  
ATOM   8932  CA  GLU B 298     200.045 181.205 207.399  1.00 44.44           C  
ATOM   8933  C   GLU B 298     199.899 182.313 206.365  1.00 43.85           C  
ATOM   8934  O   GLU B 298     199.717 183.479 206.726  1.00 45.41           O  
ATOM   8935  CB  GLU B 298     201.525 180.846 207.558  1.00 44.49           C  
ATOM   8936  CG  GLU B 298     201.843 179.952 208.742  1.00 45.10           C  
ATOM   8937  CD  GLU B 298     203.273 179.471 208.755  1.00 45.19           C  
ATOM   8938  OE1 GLU B 298     203.941 179.618 207.762  1.00 44.63           O  
ATOM   8939  OE2 GLU B 298     203.692 178.952 209.760  1.00 45.38           O  
ATOM   8940  N   THR B 299     199.919 181.947 205.081  1.00 42.92           N  
ATOM   8941  CA  THR B 299     199.737 182.923 204.017  1.00 43.62           C  
ATOM   8942  C   THR B 299     198.354 183.545 204.091  1.00 46.36           C  
ATOM   8943  O   THR B 299     198.218 184.765 203.990  1.00 45.54           O  
ATOM   8944  CB  THR B 299     199.937 182.293 202.627  1.00 43.87           C  
ATOM   8945  OG1 THR B 299     201.246 181.748 202.532  1.00 43.07           O  
ATOM   8946  CG2 THR B 299     199.765 183.335 201.546  1.00 44.04           C  
ATOM   8947  N   LYS B 300     197.327 182.720 204.283  1.00 44.87           N  
ATOM   8948  CA  LYS B 300     195.967 183.246 204.387  1.00 44.09           C  
ATOM   8949  C   LYS B 300     195.816 184.257 205.527  1.00 47.19           C  
ATOM   8950  O   LYS B 300     195.211 185.317 205.340  1.00 46.30           O  
ATOM   8951  CB  LYS B 300     194.960 182.109 204.570  1.00 45.27           C  
ATOM   8952  CG  LYS B 300     194.706 181.286 203.337  1.00 44.66           C  
ATOM   8953  CD  LYS B 300     193.711 180.180 203.610  1.00 45.03           C  
ATOM   8954  CE  LYS B 300     193.430 179.371 202.359  1.00 45.81           C  
ATOM   8955  NZ  LYS B 300     192.428 178.299 202.607  1.00 46.14           N  
ATOM   8956  N   CYS B 301     196.400 183.961 206.705  1.00 44.65           N  
ATOM   8957  CA  CYS B 301     196.359 184.872 207.855  1.00 46.55           C  
ATOM   8958  C   CYS B 301     197.156 186.165 207.598  1.00 45.45           C  
ATOM   8959  O   CYS B 301     196.679 187.258 207.919  1.00 45.98           O  
ATOM   8960  CB  CYS B 301     196.861 184.166 209.124  1.00 47.33           C  
ATOM   8961  SG  CYS B 301     195.724 182.896 209.738  1.00 49.55           S  
ATOM   8962  N   THR B 302     198.335 186.051 206.962  1.00 45.46           N  
ATOM   8963  CA  THR B 302     199.214 187.177 206.626  1.00 45.10           C  
ATOM   8964  C   THR B 302     198.525 188.171 205.704  1.00 44.77           C  
ATOM   8965  O   THR B 302     198.620 189.384 205.892  1.00 45.17           O  
ATOM   8966  CB  THR B 302     200.494 186.671 205.941  1.00 44.81           C  
ATOM   8967  OG1 THR B 302     201.214 185.830 206.844  1.00 44.38           O  
ATOM   8968  CG2 THR B 302     201.378 187.832 205.514  1.00 43.92           C  
ATOM   8969  N   LEU B 303     197.812 187.642 204.721  1.00 45.01           N  
ATOM   8970  CA  LEU B 303     197.124 188.452 203.732  1.00 45.06           C  
ATOM   8971  C   LEU B 303     195.709 188.805 204.168  1.00 45.47           C  
ATOM   8972  O   LEU B 303     194.980 189.466 203.429  1.00 45.36           O  
ATOM   8973  CB  LEU B 303     197.043 187.682 202.409  1.00 44.98           C  
ATOM   8974  CG  LEU B 303     198.383 187.252 201.778  1.00 44.26           C  
ATOM   8975  CD1 LEU B 303     198.090 186.417 200.543  1.00 43.98           C  
ATOM   8976  CD2 LEU B 303     199.224 188.465 201.424  1.00 44.13           C  
ATOM   8977  N   LYS B 304     195.302 188.327 205.342  1.00 45.82           N  
ATOM   8978  CA  LYS B 304     193.958 188.549 205.850  1.00 45.88           C  
ATOM   8979  C   LYS B 304     192.908 188.165 204.828  1.00 45.92           C  
ATOM   8980  O   LYS B 304     191.990 188.936 204.552  1.00 46.70           O  
ATOM   8981  CB  LYS B 304     193.769 190.005 206.269  1.00 45.84           C  
ATOM   8982  CG  LYS B 304     194.774 190.498 207.303  1.00 45.49           C  
ATOM   8983  CD  LYS B 304     194.530 189.871 208.672  1.00 46.33           C  
ATOM   8984  CE  LYS B 304     195.451 190.459 209.732  1.00 46.53           C  
ATOM   8985  NZ  LYS B 304     196.869 190.073 209.511  1.00 46.14           N  
ATOM   8986  N   SER B 305     193.043 186.979 204.254  1.00 45.99           N  
ATOM   8987  CA  SER B 305     192.088 186.526 203.261  1.00 46.08           C  
ATOM   8988  C   SER B 305     191.976 185.017 203.225  1.00 46.35           C  
ATOM   8989  O   SER B 305     192.925 184.305 203.529  1.00 46.60           O  
ATOM   8990  CB  SER B 305     192.460 187.026 201.894  1.00 46.13           C  
ATOM   8991  OG  SER B 305     191.484 186.644 200.969  1.00 46.47           O  
ATOM   8992  N   PHE B 306     190.814 184.523 202.829  1.00 46.92           N  
ATOM   8993  CA  PHE B 306     190.610 183.087 202.714  1.00 46.65           C  
ATOM   8994  C   PHE B 306     190.936 182.588 201.314  1.00 46.58           C  
ATOM   8995  O   PHE B 306     190.832 181.393 201.032  1.00 46.27           O  
ATOM   8996  CB  PHE B 306     189.180 182.723 203.111  1.00 47.66           C  
ATOM   8997  CG  PHE B 306     188.960 182.731 204.599  1.00 48.79           C  
ATOM   8998  CD1 PHE B 306     189.090 183.885 205.345  1.00 49.37           C  
ATOM   8999  CD2 PHE B 306     188.618 181.565 205.256  1.00 49.85           C  
ATOM   9000  CE1 PHE B 306     188.903 183.866 206.699  1.00 49.87           C  
ATOM   9001  CE2 PHE B 306     188.424 181.556 206.610  1.00 50.40           C  
ATOM   9002  CZ  PHE B 306     188.572 182.710 207.332  1.00 49.96           C  
ATOM   9003  N   THR B 307     191.337 183.512 200.447  1.00 46.01           N  
ATOM   9004  CA  THR B 307     191.739 183.193 199.085  1.00 45.68           C  
ATOM   9005  C   THR B 307     193.145 183.710 198.839  1.00 45.32           C  
ATOM   9006  O   THR B 307     193.456 184.859 199.149  1.00 45.49           O  
ATOM   9007  CB  THR B 307     190.774 183.804 198.051  1.00 46.09           C  
ATOM   9008  OG1 THR B 307     189.460 183.276 198.256  1.00 46.96           O  
ATOM   9009  CG2 THR B 307     191.229 183.478 196.630  1.00 45.58           C  
ATOM   9010  N   VAL B 308     194.000 182.868 198.282  1.00 45.02           N  
ATOM   9011  CA  VAL B 308     195.362 183.296 198.005  1.00 44.60           C  
ATOM   9012  C   VAL B 308     195.646 183.241 196.516  1.00 44.51           C  
ATOM   9013  O   VAL B 308     195.477 182.207 195.864  1.00 44.10           O  
ATOM   9014  CB  VAL B 308     196.377 182.447 198.785  1.00 44.44           C  
ATOM   9015  CG1 VAL B 308     197.777 182.897 198.470  1.00 43.88           C  
ATOM   9016  CG2 VAL B 308     196.093 182.563 200.265  1.00 44.72           C  
ATOM   9017  N   GLU B 309     196.088 184.367 195.987  1.00 44.32           N  
ATOM   9018  CA  GLU B 309     196.392 184.506 194.576  1.00 44.25           C  
ATOM   9019  C   GLU B 309     197.730 183.872 194.252  1.00 42.79           C  
ATOM   9020  O   GLU B 309     198.564 183.684 195.131  1.00 43.29           O  
ATOM   9021  CB  GLU B 309     196.397 185.981 194.188  1.00 44.93           C  
ATOM   9022  N   LYS B 310     197.923 183.520 192.995  1.00 42.81           N  
ATOM   9023  CA  LYS B 310     199.182 182.934 192.571  1.00 41.90           C  
ATOM   9024  C   LYS B 310     200.346 183.863 192.841  1.00 41.30           C  
ATOM   9025  O   LYS B 310     200.306 185.038 192.476  1.00 41.93           O  
ATOM   9026  CB  LYS B 310     199.142 182.622 191.082  1.00 41.96           C  
ATOM   9027  CG  LYS B 310     200.415 182.011 190.546  1.00 41.11           C  
ATOM   9028  CD  LYS B 310     200.293 181.611 189.086  1.00 40.80           C  
ATOM   9029  CE  LYS B 310     200.157 182.827 188.178  1.00 40.55           C  
ATOM   9030  NZ  LYS B 310     200.321 182.466 186.757  1.00 39.83           N  
ATOM   9031  N   GLY B 311     201.400 183.331 193.439  1.00 40.69           N  
ATOM   9032  CA  GLY B 311     202.582 184.137 193.688  1.00 40.42           C  
ATOM   9033  C   GLY B 311     203.398 183.647 194.865  1.00 39.82           C  
ATOM   9034  O   GLY B 311     203.165 182.565 195.405  1.00 40.47           O  
ATOM   9035  N   ILE B 312     204.392 184.440 195.229  1.00 39.60           N  
ATOM   9036  CA  ILE B 312     205.264 184.122 196.343  1.00 39.41           C  
ATOM   9037  C   ILE B 312     205.058 185.162 197.430  1.00 39.88           C  
ATOM   9038  O   ILE B 312     205.125 186.361 197.165  1.00 40.38           O  
ATOM   9039  CB  ILE B 312     206.736 184.054 195.881  1.00 38.70           C  
ATOM   9040  CG1 ILE B 312     207.643 183.678 197.052  1.00 39.21           C  
ATOM   9041  CG2 ILE B 312     207.166 185.361 195.231  1.00 39.63           C  
ATOM   9042  CD1 ILE B 312     209.060 183.271 196.643  1.00 38.03           C  
ATOM   9043  N   TYR B 313     204.800 184.711 198.649  1.00 39.94           N  
ATOM   9044  CA  TYR B 313     204.554 185.648 199.735  1.00 39.90           C  
ATOM   9045  C   TYR B 313     205.446 185.383 200.926  1.00 40.26           C  
ATOM   9046  O   TYR B 313     205.609 184.238 201.335  1.00 40.63           O  
ATOM   9047  CB  TYR B 313     203.109 185.529 200.198  1.00 40.49           C  
ATOM   9048  CG  TYR B 313     202.105 185.756 199.130  1.00 41.02           C  
ATOM   9049  CD1 TYR B 313     201.606 184.685 198.414  1.00 40.97           C  
ATOM   9050  CD2 TYR B 313     201.679 187.024 198.859  1.00 41.94           C  
ATOM   9051  CE1 TYR B 313     200.673 184.898 197.434  1.00 41.60           C  
ATOM   9052  CE2 TYR B 313     200.748 187.239 197.882  1.00 42.15           C  
ATOM   9053  CZ  TYR B 313     200.244 186.186 197.173  1.00 42.08           C  
ATOM   9054  OH  TYR B 313     199.311 186.414 196.201  1.00 43.22           O  
ATOM   9055  N   GLN B 314     205.967 186.435 201.541  1.00 40.23           N  
ATOM   9056  CA  GLN B 314     206.727 186.250 202.770  1.00 40.33           C  
ATOM   9057  C   GLN B 314     205.765 186.316 203.935  1.00 40.89           C  
ATOM   9058  O   GLN B 314     205.046 187.301 204.088  1.00 41.27           O  
ATOM   9059  CB  GLN B 314     207.833 187.287 202.919  1.00 40.20           C  
ATOM   9060  CG  GLN B 314     208.684 187.084 204.157  1.00 40.38           C  
ATOM   9061  CD  GLN B 314     209.845 188.031 204.216  1.00 40.34           C  
ATOM   9062  OE1 GLN B 314     210.751 187.992 203.372  1.00 40.07           O  
ATOM   9063  NE2 GLN B 314     209.837 188.902 205.215  1.00 39.36           N  
ATOM   9064  N   THR B 315     205.722 185.254 204.728  1.00 40.89           N  
ATOM   9065  CA  THR B 315     204.745 185.176 205.807  1.00 41.47           C  
ATOM   9066  C   THR B 315     205.356 185.140 207.190  1.00 41.67           C  
ATOM   9067  O   THR B 315     204.709 185.507 208.172  1.00 41.95           O  
ATOM   9068  CB  THR B 315     203.898 183.915 205.659  1.00 42.44           C  
ATOM   9069  OG1 THR B 315     204.740 182.762 205.777  1.00 41.92           O  
ATOM   9070  CG2 THR B 315     203.211 183.885 204.328  1.00 42.42           C  
ATOM   9071  N   SER B 316     206.590 184.686 207.289  1.00 41.44           N  
ATOM   9072  CA  SER B 316     207.179 184.534 208.606  1.00 41.90           C  
ATOM   9073  C   SER B 316     208.684 184.627 208.566  1.00 41.76           C  
ATOM   9074  O   SER B 316     209.264 185.059 207.567  1.00 42.50           O  
ATOM   9075  CB  SER B 316     206.763 183.211 209.215  1.00 42.16           C  
ATOM   9076  OG  SER B 316     207.058 183.182 210.584  1.00 42.57           O  
ATOM   9077  N   ASN B 317     209.307 184.253 209.673  1.00 42.10           N  
ATOM   9078  CA  ASN B 317     210.750 184.285 209.809  1.00 42.09           C  
ATOM   9079  C   ASN B 317     211.251 183.046 210.520  1.00 42.85           C  
ATOM   9080  O   ASN B 317     210.774 182.689 211.597  1.00 43.22           O  
ATOM   9081  CB  ASN B 317     211.205 185.536 210.525  1.00 42.22           C  
ATOM   9082  CG  ASN B 317     210.956 186.779 209.725  1.00 41.60           C  
ATOM   9083  OD1 ASN B 317     211.653 187.053 208.740  1.00 41.08           O  
ATOM   9084  ND2 ASN B 317     209.975 187.542 210.126  1.00 41.21           N  
ATOM   9085  N   PHE B 318     212.207 182.390 209.896  1.00 43.07           N  
ATOM   9086  CA  PHE B 318     212.846 181.213 210.435  1.00 44.38           C  
ATOM   9087  C   PHE B 318     214.006 181.649 211.277  1.00 46.11           C  
ATOM   9088  O   PHE B 318     214.778 182.514 210.863  1.00 46.12           O  
ATOM   9089  CB  PHE B 318     213.339 180.315 209.310  1.00 44.46           C  
ATOM   9090  CG  PHE B 318     214.175 179.167 209.752  1.00 45.40           C  
ATOM   9091  CD1 PHE B 318     213.608 178.043 210.315  1.00 46.10           C  
ATOM   9092  CD2 PHE B 318     215.548 179.211 209.596  1.00 45.84           C  
ATOM   9093  CE1 PHE B 318     214.398 176.985 210.714  1.00 45.85           C  
ATOM   9094  CE2 PHE B 318     216.337 178.159 209.991  1.00 46.25           C  
ATOM   9095  CZ  PHE B 318     215.761 177.044 210.552  1.00 46.39           C  
ATOM   9096  N   ARG B 319     214.129 181.085 212.464  1.00 45.70           N  
ATOM   9097  CA  ARG B 319     215.262 181.416 213.298  1.00 47.30           C  
ATOM   9098  C   ARG B 319     215.636 180.252 214.187  1.00 49.07           C  
ATOM   9099  O   ARG B 319     214.803 179.733 214.935  1.00 50.03           O  
ATOM   9100  CB  ARG B 319     214.950 182.648 214.127  1.00 46.92           C  
ATOM   9101  CG  ARG B 319     216.115 183.222 214.906  1.00 46.87           C  
ATOM   9102  CD  ARG B 319     215.756 184.511 215.570  1.00 45.84           C  
ATOM   9103  NE  ARG B 319     215.363 185.535 214.586  1.00 44.51           N  
ATOM   9104  CZ  ARG B 319     214.106 186.018 214.399  1.00 44.07           C  
ATOM   9105  NH1 ARG B 319     213.101 185.597 215.141  1.00 43.80           N  
ATOM   9106  NH2 ARG B 319     213.884 186.922 213.459  1.00 42.64           N  
ATOM   9107  N   VAL B 320     216.905 179.882 214.142  1.00 49.49           N  
ATOM   9108  CA  VAL B 320     217.411 178.814 214.978  1.00 51.80           C  
ATOM   9109  C   VAL B 320     217.518 179.297 216.409  1.00 52.61           C  
ATOM   9110  O   VAL B 320     218.064 180.364 216.678  1.00 53.10           O  
ATOM   9111  CB  VAL B 320     218.772 178.324 214.460  1.00 51.65           C  
ATOM   9112  CG1 VAL B 320     219.374 177.301 215.419  1.00 53.92           C  
ATOM   9113  CG2 VAL B 320     218.582 177.706 213.086  1.00 49.32           C  
ATOM   9114  N   GLN B 321     216.975 178.512 217.322  1.00 54.51           N  
ATOM   9115  CA  GLN B 321     216.970 178.878 218.722  1.00 54.79           C  
ATOM   9116  C   GLN B 321     218.186 178.301 219.422  1.00 56.96           C  
ATOM   9117  O   GLN B 321     218.695 177.263 218.998  1.00 56.70           O  
ATOM   9118  CB  GLN B 321     215.685 178.360 219.368  1.00 55.75           C  
ATOM   9119  CG  GLN B 321     214.447 178.900 218.719  1.00 55.20           C  
ATOM   9120  CD  GLN B 321     214.402 180.391 218.786  1.00 55.40           C  
ATOM   9121  OE1 GLN B 321     214.447 180.974 219.872  1.00 56.45           O  
ATOM   9122  NE2 GLN B 321     214.324 181.031 217.628  1.00 53.02           N  
ATOM   9123  N   PRO B 322     218.666 178.941 220.491  1.00 57.06           N  
ATOM   9124  CA  PRO B 322     219.742 178.474 221.324  1.00 58.18           C  
ATOM   9125  C   PRO B 322     219.318 177.198 222.011  1.00 58.48           C  
ATOM   9126  O   PRO B 322     218.165 177.063 222.422  1.00 59.13           O  
ATOM   9127  CB  PRO B 322     219.956 179.637 222.297  1.00 59.09           C  
ATOM   9128  CG  PRO B 322     218.650 180.395 222.294  1.00 58.11           C  
ATOM   9129  CD  PRO B 322     218.099 180.232 220.896  1.00 57.12           C  
ATOM   9130  N   THR B 323     220.257 176.280 222.165  1.00 59.95           N  
ATOM   9131  CA  THR B 323     219.957 174.993 222.783  1.00 60.34           C  
ATOM   9132  C   THR B 323     220.386 174.918 224.242  1.00 60.93           C  
ATOM   9133  O   THR B 323     219.860 174.116 225.016  1.00 61.64           O  
ATOM   9134  CB  THR B 323     220.659 173.872 222.002  1.00 60.81           C  
ATOM   9135  OG1 THR B 323     222.077 174.065 222.069  1.00 60.70           O  
ATOM   9136  CG2 THR B 323     220.226 173.878 220.546  1.00 60.41           C  
ATOM   9137  N   GLU B 324     221.335 175.758 224.615  1.00 61.41           N  
ATOM   9138  CA  GLU B 324     221.876 175.792 225.962  1.00 62.66           C  
ATOM   9139  C   GLU B 324     222.532 177.133 226.202  1.00 62.94           C  
ATOM   9140  O   GLU B 324     222.776 177.870 225.243  1.00 61.96           O  
ATOM   9141  CB  GLU B 324     222.862 174.644 226.182  1.00 62.14           C  
ATOM   9142  CG  GLU B 324     224.094 174.655 225.299  1.00 62.71           C  
ATOM   9143  CD  GLU B 324     224.933 173.437 225.535  1.00 62.98           C  
ATOM   9144  OE1 GLU B 324     225.407 173.278 226.634  1.00 62.95           O  
ATOM   9145  OE2 GLU B 324     225.091 172.652 224.629  1.00 62.34           O  
ATOM   9146  N   SER B 325     222.818 177.443 227.461  1.00 62.82           N  
ATOM   9147  CA  SER B 325     223.509 178.682 227.785  1.00 63.53           C  
ATOM   9148  C   SER B 325     224.946 178.414 228.212  1.00 64.30           C  
ATOM   9149  O   SER B 325     225.227 177.427 228.889  1.00 64.82           O  
ATOM   9150  CB  SER B 325     222.780 179.415 228.891  1.00 63.62           C  
ATOM   9151  OG  SER B 325     221.490 179.779 228.487  1.00 62.78           O  
ATOM   9152  N   ILE B 326     225.843 179.305 227.812  1.00 64.05           N  
ATOM   9153  CA  ILE B 326     227.253 179.228 228.175  1.00 65.44           C  
ATOM   9154  C   ILE B 326     227.719 180.470 228.899  1.00 67.68           C  
ATOM   9155  O   ILE B 326     227.709 181.566 228.338  1.00 67.22           O  
ATOM   9156  CB  ILE B 326     228.129 178.997 226.933  1.00 66.36           C  
ATOM   9157  CG1 ILE B 326     227.773 177.652 226.310  1.00 65.20           C  
ATOM   9158  CG2 ILE B 326     229.614 179.101 227.282  1.00 67.17           C  
ATOM   9159  CD1 ILE B 326     228.419 177.406 224.988  1.00 65.77           C  
ATOM   9160  N   VAL B 327     228.171 180.293 230.129  1.00 68.51           N  
ATOM   9161  CA  VAL B 327     228.615 181.412 230.935  1.00 67.56           C  
ATOM   9162  C   VAL B 327     230.088 181.284 231.283  1.00 70.44           C  
ATOM   9163  O   VAL B 327     230.507 180.311 231.906  1.00 71.43           O  
ATOM   9164  CB  VAL B 327     227.772 181.484 232.216  1.00 70.37           C  
ATOM   9165  CG1 VAL B 327     228.229 182.621 233.066  1.00 70.92           C  
ATOM   9166  CG2 VAL B 327     226.300 181.632 231.845  1.00 69.00           C  
ATOM   9167  N   ARG B 328     230.885 182.264 230.878  1.00 70.14           N  
ATOM   9168  CA  ARG B 328     232.318 182.169 231.098  1.00 72.00           C  
ATOM   9169  C   ARG B 328     232.913 183.417 231.747  1.00 71.87           C  
ATOM   9170  O   ARG B 328     232.761 184.539 231.251  1.00 70.89           O  
ATOM   9171  CB  ARG B 328     233.024 181.925 229.772  1.00 70.04           C  
ATOM   9172  CG  ARG B 328     232.525 180.717 228.973  1.00 69.32           C  
ATOM   9173  CD  ARG B 328     232.959 179.407 229.516  1.00 69.56           C  
ATOM   9174  NE  ARG B 328     234.366 179.185 229.298  1.00 70.74           N  
ATOM   9175  CZ  ARG B 328     235.082 178.164 229.807  1.00 70.27           C  
ATOM   9176  NH1 ARG B 328     234.518 177.252 230.574  1.00 70.71           N  
ATOM   9177  NH2 ARG B 328     236.366 178.086 229.530  1.00 70.63           N  
ATOM   9178  N   PHE B 329     233.639 183.183 232.828  1.00 73.01           N  
ATOM   9179  CA  PHE B 329     234.366 184.206 233.560  1.00 74.03           C  
ATOM   9180  C   PHE B 329     235.795 183.717 233.803  1.00 74.92           C  
ATOM   9181  O   PHE B 329     236.033 182.513 233.744  1.00 75.05           O  
ATOM   9182  CB  PHE B 329     233.652 184.530 234.872  1.00 76.09           C  
ATOM   9183  CG  PHE B 329     232.327 185.164 234.666  1.00 76.45           C  
ATOM   9184  CD1 PHE B 329     231.159 184.445 234.784  1.00 77.49           C  
ATOM   9185  CD2 PHE B 329     232.249 186.501 234.331  1.00 74.79           C  
ATOM   9186  CE1 PHE B 329     229.942 185.060 234.584  1.00 75.91           C  
ATOM   9187  CE2 PHE B 329     231.036 187.107 234.124  1.00 74.06           C  
ATOM   9188  CZ  PHE B 329     229.883 186.386 234.253  1.00 74.49           C  
ATOM   9189  N   PRO B 330     236.757 184.616 234.075  1.00 75.20           N  
ATOM   9190  CA  PRO B 330     238.149 184.314 234.364  1.00 76.64           C  
ATOM   9191  C   PRO B 330     238.247 183.408 235.573  1.00 80.18           C  
ATOM   9192  O   PRO B 330     237.319 183.366 236.384  1.00 81.59           O  
ATOM   9193  CB  PRO B 330     238.744 185.696 234.657  1.00 77.71           C  
ATOM   9194  CG  PRO B 330     237.830 186.665 233.962  1.00 75.15           C  
ATOM   9195  CD  PRO B 330     236.461 186.060 234.084  1.00 75.66           C  
ATOM   9196  N   ASN B 331     239.382 182.697 235.708  1.00 80.26           N  
ATOM   9197  CA  ASN B 331     239.640 181.792 236.829  1.00 84.61           C  
ATOM   9198  C   ASN B 331     239.400 182.510 238.167  1.00 91.64           C  
ATOM   9199  O   ASN B 331     239.907 183.609 238.396  1.00 92.67           O  
ATOM   9200  CB  ASN B 331     241.062 181.230 236.759  1.00 84.16           C  
ATOM   9201  CG  ASN B 331     241.305 180.321 235.539  1.00 79.48           C  
ATOM   9202  OD1 ASN B 331     240.633 180.451 234.503  1.00 77.42           O  
ATOM   9203  ND2 ASN B 331     242.263 179.413 235.656  1.00 79.19           N  
ATOM   9204  N   ILE B 332     238.624 181.855 239.038  1.00 94.42           N  
ATOM   9205  CA  ILE B 332     238.111 182.358 240.319  1.00 97.17           C  
ATOM   9206  C   ILE B 332     239.157 182.541 241.425  1.00100.99           C  
ATOM   9207  O   ILE B 332     238.824 182.557 242.605  1.00103.66           O  
ATOM   9208  CB  ILE B 332     236.975 181.414 240.790  1.00 98.46           C  
ATOM   9209  CG1 ILE B 332     236.054 182.095 241.832  1.00101.63           C  
ATOM   9210  CG2 ILE B 332     237.560 180.115 241.357  1.00 99.25           C  
ATOM   9211  CD1 ILE B 332     235.287 183.268 241.267  1.00103.62           C  
ATOM   9212  N   THR B 333     240.416 182.627 241.053  1.00100.67           N  
ATOM   9213  CA  THR B 333     241.489 182.767 242.022  1.00103.23           C  
ATOM   9214  C   THR B 333     241.453 184.163 242.638  1.00106.33           C  
ATOM   9215  O   THR B 333     240.686 185.019 242.199  1.00105.74           O  
ATOM   9216  CB  THR B 333     242.856 182.526 241.357  1.00102.45           C  
ATOM   9217  N   ASN B 334     242.268 184.375 243.674  1.00107.87           N  
ATOM   9218  CA  ASN B 334     242.337 185.639 244.418  1.00110.03           C  
ATOM   9219  C   ASN B 334     241.104 185.876 245.286  1.00112.92           C  
ATOM   9220  O   ASN B 334     240.341 186.821 245.073  1.00116.25           O  
ATOM   9221  CB  ASN B 334     242.558 186.818 243.488  1.00108.75           C  
ATOM   9222  N   LEU B 335     240.946 185.020 246.289  1.00114.67           N  
ATOM   9223  CA  LEU B 335     239.838 185.094 247.231  1.00119.29           C  
ATOM   9224  C   LEU B 335     240.282 185.877 248.459  1.00122.01           C  
ATOM   9225  O   LEU B 335     241.478 185.910 248.761  1.00122.08           O  
ATOM   9226  CB  LEU B 335     239.418 183.681 247.686  1.00117.97           C  
ATOM   9227  CG  LEU B 335     238.509 182.863 246.750  1.00115.13           C  
ATOM   9228  CD1 LEU B 335     239.295 182.380 245.537  1.00110.81           C  
ATOM   9229  CD2 LEU B 335     237.943 181.683 247.526  1.00118.99           C  
ATOM   9230  N   CYS B 336     239.321 186.488 249.179  1.00122.58           N  
ATOM   9231  CA  CYS B 336     239.606 187.176 250.438  1.00127.39           C  
ATOM   9232  C   CYS B 336     239.813 186.165 251.573  1.00129.39           C  
ATOM   9233  O   CYS B 336     239.132 185.141 251.624  1.00130.29           O  
ATOM   9234  CB  CYS B 336     238.480 188.160 250.807  1.00127.06           C  
ATOM   9235  SG  CYS B 336     238.543 189.737 249.899  1.00125.58           S  
ATOM   9236  N   PRO B 337     240.733 186.455 252.550  1.00130.63           N  
ATOM   9237  CA  PRO B 337     241.183 185.558 253.599  1.00134.67           C  
ATOM   9238  C   PRO B 337     240.185 185.381 254.726  1.00137.72           C  
ATOM   9239  O   PRO B 337     240.468 185.724 255.871  1.00139.18           O  
ATOM   9240  CB  PRO B 337     242.445 186.263 254.107  1.00135.15           C  
ATOM   9241  CG  PRO B 337     242.147 187.726 253.945  1.00132.09           C  
ATOM   9242  CD  PRO B 337     241.376 187.823 252.654  1.00130.69           C  
ATOM   9243  N   PHE B 338     239.033 184.792 254.426  1.00136.35           N  
ATOM   9244  CA  PHE B 338     238.076 184.529 255.489  1.00139.39           C  
ATOM   9245  C   PHE B 338     238.692 183.505 256.432  1.00141.92           C  
ATOM   9246  O   PHE B 338     238.407 183.490 257.622  1.00142.05           O  
ATOM   9247  CB  PHE B 338     236.731 184.014 254.959  1.00137.26           C  
ATOM   9248  CG  PHE B 338     235.836 185.071 254.334  1.00137.34           C  
ATOM   9249  CD1 PHE B 338     235.342 184.906 253.045  1.00134.92           C  
ATOM   9250  CD2 PHE B 338     235.481 186.223 255.030  1.00138.36           C  
ATOM   9251  CE1 PHE B 338     234.523 185.859 252.473  1.00133.77           C  
ATOM   9252  CE2 PHE B 338     234.663 187.171 254.453  1.00136.47           C  
ATOM   9253  CZ  PHE B 338     234.187 186.988 253.176  1.00133.97           C  
ATOM   9254  N   GLY B 339     239.598 182.682 255.912  1.00138.63           N  
ATOM   9255  CA  GLY B 339     240.275 181.660 256.709  1.00142.14           C  
ATOM   9256  C   GLY B 339     241.227 182.252 257.753  1.00142.18           C  
ATOM   9257  O   GLY B 339     241.718 181.529 258.619  1.00143.99           O  
ATOM   9258  N   GLU B 340     241.513 183.554 257.677  1.00143.04           N  
ATOM   9259  CA  GLU B 340     242.360 184.183 258.684  1.00141.86           C  
ATOM   9260  C   GLU B 340     241.488 184.896 259.708  1.00142.92           C  
ATOM   9261  O   GLU B 340     241.983 185.474 260.681  1.00145.26           O  
ATOM   9262  CB  GLU B 340     243.350 185.164 258.048  1.00141.48           C  
ATOM   9263  N   VAL B 341     240.184 184.880 259.465  1.00141.70           N  
ATOM   9264  CA  VAL B 341     239.224 185.547 260.313  1.00142.98           C  
ATOM   9265  C   VAL B 341     238.435 184.541 261.127  1.00145.12           C  
ATOM   9266  O   VAL B 341     238.275 184.698 262.337  1.00147.21           O  
ATOM   9267  CB  VAL B 341     238.260 186.396 259.465  1.00142.23           C  
ATOM   9268  CG1 VAL B 341     237.202 187.008 260.345  1.00145.02           C  
ATOM   9269  CG2 VAL B 341     239.033 187.479 258.735  1.00141.95           C  
ATOM   9270  N   PHE B 342     237.925 183.513 260.462  1.00146.29           N  
ATOM   9271  CA  PHE B 342     237.076 182.514 261.103  1.00145.85           C  
ATOM   9272  C   PHE B 342     237.823 181.314 261.713  1.00147.04           C  
ATOM   9273  O   PHE B 342     237.380 180.751 262.712  1.00146.45           O  
ATOM   9274  CB  PHE B 342     236.038 182.046 260.098  1.00146.26           C  
ATOM   9275  CG  PHE B 342     235.057 183.129 259.789  1.00145.77           C  
ATOM   9276  CD1 PHE B 342     235.285 184.065 258.783  1.00143.39           C  
ATOM   9277  CD2 PHE B 342     233.907 183.221 260.513  1.00147.09           C  
ATOM   9278  CE1 PHE B 342     234.371 185.062 258.540  1.00143.84           C  
ATOM   9279  CE2 PHE B 342     232.997 184.203 260.274  1.00145.20           C  
ATOM   9280  CZ  PHE B 342     233.227 185.132 259.287  1.00144.67           C  
ATOM   9281  N   ASN B 343     238.974 180.956 261.117  1.00145.32           N  
ATOM   9282  CA  ASN B 343     239.867 179.884 261.597  1.00147.05           C  
ATOM   9283  C   ASN B 343     241.078 180.460 262.353  1.00147.88           C  
ATOM   9284  O   ASN B 343     242.111 179.819 262.455  1.00149.59           O  
ATOM   9285  CB  ASN B 343     240.392 179.006 260.442  1.00146.01           C  
ATOM   9286  CG  ASN B 343     239.355 178.540 259.388  1.00145.80           C  
ATOM   9287  OD1 ASN B 343     238.697 179.355 258.743  1.00144.73           O  
ATOM   9288  ND2 ASN B 343     239.272 177.217 259.233  1.00146.52           N  
ATOM   9289  N   ALA B 344     240.944 181.687 262.889  1.00148.30           N  
ATOM   9290  CA  ALA B 344     242.034 182.377 263.594  1.00150.20           C  
ATOM   9291  C   ALA B 344     242.405 181.639 264.884  1.00152.53           C  
ATOM   9292  O   ALA B 344     241.539 181.137 265.596  1.00150.93           O  
ATOM   9293  CB  ALA B 344     241.621 183.811 263.867  1.00150.13           C  
ATOM   9294  N   THR B 345     243.702 181.584 265.178  1.00153.25           N  
ATOM   9295  CA  THR B 345     244.205 180.909 266.374  1.00153.47           C  
ATOM   9296  C   THR B 345     243.776 181.651 267.634  1.00153.58           C  
ATOM   9297  O   THR B 345     243.430 181.032 268.643  1.00154.58           O  
ATOM   9298  CB  THR B 345     245.738 180.778 266.337  1.00152.85           C  
ATOM   9299  N   ARG B 346     243.814 182.978 267.573  1.00153.85           N  
ATOM   9300  CA  ARG B 346     243.422 183.800 268.700  1.00154.34           C  
ATOM   9301  C   ARG B 346     242.479 184.916 268.291  1.00153.52           C  
ATOM   9302  O   ARG B 346     242.603 185.505 267.217  1.00152.43           O  
ATOM   9303  CB  ARG B 346     244.633 184.413 269.404  1.00153.45           C  
ATOM   9304  N   PHE B 347     241.538 185.193 269.186  1.00153.53           N  
ATOM   9305  CA  PHE B 347     240.552 186.253 269.059  1.00153.55           C  
ATOM   9306  C   PHE B 347     240.717 187.305 270.148  1.00154.34           C  
ATOM   9307  O   PHE B 347     241.213 187.018 271.236  1.00153.56           O  
ATOM   9308  CB  PHE B 347     239.139 185.681 269.115  1.00154.44           C  
ATOM   9309  N   ALA B 348     240.301 188.523 269.832  1.00153.18           N  
ATOM   9310  CA  ALA B 348     240.298 189.654 270.753  1.00153.11           C  
ATOM   9311  C   ALA B 348     239.046 189.664 271.624  1.00154.70           C  
ATOM   9312  O   ALA B 348     238.071 188.972 271.331  1.00153.36           O  
ATOM   9313  CB  ALA B 348     240.399 190.948 269.977  1.00150.35           C  
ATOM   9314  N   SER B 349     239.080 190.452 272.696  1.00153.94           N  
ATOM   9315  CA  SER B 349     237.919 190.643 273.557  1.00159.27           C  
ATOM   9316  C   SER B 349     236.928 191.593 272.906  1.00146.66           C  
ATOM   9317  O   SER B 349     237.245 192.251 271.920  1.00161.13           O  
ATOM   9318  CB  SER B 349     238.351 191.175 274.900  1.00156.96           C  
ATOM   9319  N   VAL B 350     235.723 191.670 273.456  1.00155.02           N  
ATOM   9320  CA  VAL B 350     234.702 192.535 272.885  1.00153.71           C  
ATOM   9321  C   VAL B 350     234.963 194.015 273.108  1.00149.40           C  
ATOM   9322  O   VAL B 350     234.641 194.826 272.249  1.00158.87           O  
ATOM   9323  CB  VAL B 350     233.323 192.129 273.407  1.00155.79           C  
ATOM   9324  N   TYR B 351     235.531 194.387 274.252  1.00159.13           N  
ATOM   9325  CA  TYR B 351     235.811 195.799 274.483  1.00160.63           C  
ATOM   9326  C   TYR B 351     236.753 196.348 273.416  1.00155.05           C  
ATOM   9327  O   TYR B 351     236.559 197.448 272.894  1.00153.51           O  
ATOM   9328  CB  TYR B 351     236.402 196.024 275.866  1.00154.83           C  
ATOM   9329  N   ALA B 352     237.798 195.584 273.119  1.00154.84           N  
ATOM   9330  CA  ALA B 352     238.806 195.977 272.147  1.00153.94           C  
ATOM   9331  C   ALA B 352     238.983 194.884 271.100  1.00157.64           C  
ATOM   9332  O   ALA B 352     239.938 194.110 271.153  1.00151.10           O  
ATOM   9333  CB  ALA B 352     240.124 196.267 272.844  1.00155.30           C  
ATOM   9334  N   TRP B 353     238.040 194.826 270.164  1.00154.38           N  
ATOM   9335  CA  TRP B 353     237.963 193.779 269.151  1.00153.98           C  
ATOM   9336  C   TRP B 353     238.906 194.057 267.985  1.00151.56           C  
ATOM   9337  O   TRP B 353     239.360 195.191 267.813  1.00151.04           O  
ATOM   9338  CB  TRP B 353     236.536 193.659 268.635  1.00152.73           C  
ATOM   9339  N   ASN B 354     239.220 193.019 267.204  1.00149.21           N  
ATOM   9340  CA  ASN B 354     240.082 193.174 266.032  1.00150.48           C  
ATOM   9341  C   ASN B 354     239.275 193.613 264.822  1.00146.20           C  
ATOM   9342  O   ASN B 354     238.174 193.121 264.597  1.00152.60           O  
ATOM   9343  CB  ASN B 354     240.825 191.887 265.722  1.00150.41           C  
ATOM   9344  N   ARG B 355     239.826 194.515 264.018  1.00145.55           N  
ATOM   9345  CA  ARG B 355     239.126 194.970 262.820  1.00143.85           C  
ATOM   9346  C   ARG B 355     239.975 194.765 261.574  1.00143.05           C  
ATOM   9347  O   ARG B 355     240.918 195.515 261.319  1.00142.21           O  
ATOM   9348  CB  ARG B 355     238.734 196.431 262.966  1.00143.68           C  
ATOM   9349  N   LYS B 356     239.650 193.726 260.814  1.00140.44           N  
ATOM   9350  CA  LYS B 356     240.421 193.371 259.628  1.00137.53           C  
ATOM   9351  C   LYS B 356     239.712 193.816 258.358  1.00135.62           C  
ATOM   9352  O   LYS B 356     238.517 193.579 258.182  1.00136.51           O  
ATOM   9353  CB  LYS B 356     240.687 191.867 259.612  1.00139.43           C  
ATOM   9354  N   ARG B 357     240.443 194.469 257.465  1.00131.43           N  
ATOM   9355  CA  ARG B 357     239.826 194.946 256.235  1.00131.36           C  
ATOM   9356  C   ARG B 357     239.898 193.926 255.109  1.00129.23           C  
ATOM   9357  O   ARG B 357     240.960 193.399 254.780  1.00127.36           O  
ATOM   9358  CB  ARG B 357     240.448 196.249 255.770  1.00125.48           C  
ATOM   9359  N   ILE B 358     238.743 193.677 254.520  1.00126.41           N  
ATOM   9360  CA  ILE B 358     238.548 192.753 253.424  1.00127.09           C  
ATOM   9361  C   ILE B 358     238.391 193.528 252.115  1.00123.93           C  
ATOM   9362  O   ILE B 358     237.517 194.393 251.982  1.00124.48           O  
ATOM   9363  CB  ILE B 358     237.323 191.875 253.746  1.00128.04           C  
ATOM   9364  N   SER B 359     239.277 193.248 251.159  1.00122.19           N  
ATOM   9365  CA  SER B 359     239.316 194.010 249.919  1.00119.10           C  
ATOM   9366  C   SER B 359     239.991 193.296 248.754  1.00115.77           C  
ATOM   9367  O   SER B 359     240.756 192.351 248.942  1.00116.24           O  
ATOM   9368  CB  SER B 359     240.038 195.304 250.175  1.00115.44           C  
ATOM   9369  N   ASN B 360     239.757 193.830 247.552  1.00116.74           N  
ATOM   9370  CA  ASN B 360     240.449 193.430 246.323  1.00114.97           C  
ATOM   9371  C   ASN B 360     240.402 191.925 246.046  1.00114.97           C  
ATOM   9372  O   ASN B 360     241.460 191.299 245.921  1.00115.35           O  
ATOM   9373  CB  ASN B 360     241.890 193.905 246.401  1.00112.03           C  
ATOM   9374  N   CYS B 361     239.186 191.339 245.982  1.00116.85           N  
ATOM   9375  CA  CYS B 361     239.030 189.881 245.853  1.00117.43           C  
ATOM   9376  C   CYS B 361     237.653 189.452 245.316  1.00118.30           C  
ATOM   9377  O   CYS B 361     236.731 190.272 245.177  1.00120.31           O  
ATOM   9378  CB  CYS B 361     239.208 189.203 247.239  1.00117.17           C  
ATOM   9379  SG  CYS B 361     237.805 189.500 248.421  1.00117.18           S  
ATOM   9380  N   VAL B 362     237.522 188.121 245.114  1.00117.91           N  
ATOM   9381  CA  VAL B 362     236.243 187.442 244.911  1.00119.02           C  
ATOM   9382  C   VAL B 362     235.901 186.746 246.231  1.00119.75           C  
ATOM   9383  O   VAL B 362     236.559 185.797 246.653  1.00119.42           O  
ATOM   9384  CB  VAL B 362     236.281 186.454 243.720  1.00115.77           C  
ATOM   9385  N   ALA B 363     234.920 187.301 246.926  1.00121.06           N  
ATOM   9386  CA  ALA B 363     234.592 186.891 248.285  1.00124.31           C  
ATOM   9387  C   ALA B 363     233.535 185.810 248.291  1.00124.97           C  
ATOM   9388  O   ALA B 363     232.374 186.050 247.965  1.00125.01           O  
ATOM   9389  CB  ALA B 363     234.125 188.088 249.090  1.00124.67           C  
ATOM   9390  N   ASP B 364     233.954 184.599 248.610  1.00127.22           N  
ATOM   9391  CA  ASP B 364     233.053 183.460 248.569  1.00128.42           C  
ATOM   9392  C   ASP B 364     232.378 183.276 249.915  1.00132.63           C  
ATOM   9393  O   ASP B 364     233.020 182.884 250.889  1.00132.32           O  
ATOM   9394  CB  ASP B 364     233.799 182.191 248.160  1.00127.86           C  
ATOM   9395  N   TYR B 365     231.088 183.579 249.976  1.00132.80           N  
ATOM   9396  CA  TYR B 365     230.349 183.537 251.225  1.00133.79           C  
ATOM   9397  C   TYR B 365     229.554 182.243 251.369  1.00133.61           C  
ATOM   9398  O   TYR B 365     228.801 182.084 252.334  1.00136.72           O  
ATOM   9399  CB  TYR B 365     229.377 184.712 251.302  1.00132.18           C  
ATOM   9400  N   SER B 366     229.693 181.328 250.401  1.00133.82           N  
ATOM   9401  CA  SER B 366     228.915 180.094 250.453  1.00135.68           C  
ATOM   9402  C   SER B 366     229.473 179.162 251.503  1.00139.23           C  
ATOM   9403  O   SER B 366     228.739 178.377 252.100  1.00139.47           O  
ATOM   9404  CB  SER B 366     228.915 179.371 249.120  1.00135.72           C  
ATOM   9405  N   VAL B 367     230.764 179.283 251.773  1.00136.86           N  
ATOM   9406  CA  VAL B 367     231.384 178.443 252.772  1.00138.07           C  
ATOM   9407  C   VAL B 367     230.851 178.805 254.140  1.00139.38           C  
ATOM   9408  O   VAL B 367     230.474 177.936 254.923  1.00139.95           O  
ATOM   9409  CB  VAL B 367     232.914 178.623 252.748  1.00137.82           C  
ATOM   9410  N   LEU B 368     230.805 180.098 254.422  1.00138.02           N  
ATOM   9411  CA  LEU B 368     230.353 180.559 255.717  1.00146.01           C  
ATOM   9412  C   LEU B 368     228.869 180.277 255.923  1.00133.59           C  
ATOM   9413  O   LEU B 368     228.453 179.889 257.014  1.00145.62           O  
ATOM   9414  CB  LEU B 368     230.626 182.061 255.839  1.00140.85           C  
ATOM   9415  N   TYR B 369     228.076 180.458 254.867  1.00146.18           N  
ATOM   9416  CA  TYR B 369     226.637 180.232 254.932  1.00140.65           C  
ATOM   9417  C   TYR B 369     226.257 178.765 255.097  1.00137.06           C  
ATOM   9418  O   TYR B 369     225.415 178.426 255.930  1.00142.92           O  
ATOM   9419  CB  TYR B 369     225.953 180.801 253.692  1.00140.98           C  
ATOM   9420  N   ASN B 370     226.841 177.896 254.274  1.00146.11           N  
ATOM   9421  CA  ASN B 370     226.475 176.486 254.281  1.00141.34           C  
ATOM   9422  C   ASN B 370     227.141 175.667 255.382  1.00143.17           C  
ATOM   9423  O   ASN B 370     226.604 174.637 255.790  1.00144.35           O  
ATOM   9424  CB  ASN B 370     226.768 175.864 252.931  1.00140.74           C  
ATOM   9425  N   SER B 371     228.309 176.089 255.856  1.00143.92           N  
ATOM   9426  CA  SER B 371     229.018 175.303 256.856  1.00144.61           C  
ATOM   9427  C   SER B 371     228.189 175.112 258.122  1.00143.85           C  
ATOM   9428  O   SER B 371     227.557 176.038 258.630  1.00146.10           O  
ATOM   9429  CB  SER B 371     230.352 175.948 257.172  1.00144.88           C  
ATOM   9430  N   ALA B 372     228.206 173.886 258.644  1.00148.61           N  
ATOM   9431  CA  ALA B 372     227.438 173.518 259.835  1.00146.22           C  
ATOM   9432  C   ALA B 372     228.207 173.822 261.111  1.00147.50           C  
ATOM   9433  O   ALA B 372     227.740 173.545 262.214  1.00148.16           O  
ATOM   9434  CB  ALA B 372     227.073 172.043 259.790  1.00146.20           C  
ATOM   9435  N   SER B 373     229.399 174.375 260.950  1.00146.77           N  
ATOM   9436  CA  SER B 373     230.282 174.703 262.060  1.00147.72           C  
ATOM   9437  C   SER B 373     229.804 175.911 262.854  1.00148.77           C  
ATOM   9438  O   SER B 373     230.325 176.191 263.934  1.00148.30           O  
ATOM   9439  CB  SER B 373     231.671 174.992 261.541  1.00148.62           C  
ATOM   9440  N   PHE B 374     228.849 176.653 262.309  1.00148.06           N  
ATOM   9441  CA  PHE B 374     228.391 177.860 262.968  1.00148.57           C  
ATOM   9442  C   PHE B 374     227.092 177.625 263.716  1.00147.48           C  
ATOM   9443  O   PHE B 374     226.227 176.878 263.258  1.00149.31           O  
ATOM   9444  CB  PHE B 374     228.237 178.981 261.947  1.00147.76           C  
ATOM   9445  N   SER B 375     226.946 178.272 264.874  1.00146.95           N  
ATOM   9446  CA  SER B 375     225.722 178.127 265.646  1.00148.64           C  
ATOM   9447  C   SER B 375     224.657 179.050 265.091  1.00148.76           C  
ATOM   9448  O   SER B 375     223.459 178.779 265.192  1.00149.98           O  
ATOM   9449  CB  SER B 375     225.972 178.438 267.109  1.00148.92           C  
ATOM   9450  N   THR B 376     225.101 180.132 264.464  1.00148.21           N  
ATOM   9451  CA  THR B 376     224.173 181.059 263.849  1.00149.68           C  
ATOM   9452  C   THR B 376     224.801 181.808 262.677  1.00147.04           C  
ATOM   9453  O   THR B 376     226.011 182.058 262.647  1.00150.52           O  
ATOM   9454  CB  THR B 376     223.629 182.056 264.886  1.00148.10           C  
ATOM   9455  N   PHE B 377     223.955 182.172 261.719  1.00145.29           N  
ATOM   9456  CA  PHE B 377     224.341 182.976 260.566  1.00145.24           C  
ATOM   9457  C   PHE B 377     223.184 183.884 260.182  1.00144.25           C  
ATOM   9458  O   PHE B 377     222.190 183.416 259.623  1.00145.95           O  
ATOM   9459  CB  PHE B 377     224.691 182.074 259.372  1.00145.19           C  
ATOM   9460  N   LYS B 378     223.296 185.173 260.480  1.00144.87           N  
ATOM   9461  CA  LYS B 378     222.212 186.099 260.162  1.00145.15           C  
ATOM   9462  C   LYS B 378     222.729 187.353 259.465  1.00146.79           C  
ATOM   9463  O   LYS B 378     223.762 187.894 259.854  1.00145.23           O  
ATOM   9464  CB  LYS B 378     221.453 186.506 261.435  1.00144.84           C  
ATOM   9465  N   CYS B 379     221.978 187.828 258.459  1.00145.37           N  
ATOM   9466  CA  CYS B 379     222.262 189.074 257.743  1.00144.32           C  
ATOM   9467  C   CYS B 379     221.068 190.012 257.905  1.00143.22           C  
ATOM   9468  O   CYS B 379     219.924 189.563 257.933  1.00143.70           O  
ATOM   9469  CB  CYS B 379     222.536 188.801 256.255  1.00143.47           C  
ATOM   9470  SG  CYS B 379     223.977 187.735 255.942  1.00139.91           S  
ATOM   9471  N   TYR B 380     221.350 191.322 258.050  1.00145.09           N  
ATOM   9472  CA  TYR B 380     220.307 192.324 258.332  1.00144.02           C  
ATOM   9473  C   TYR B 380     219.995 193.243 257.158  1.00143.01           C  
ATOM   9474  O   TYR B 380     218.829 193.476 256.842  1.00141.77           O  
ATOM   9475  CB  TYR B 380     220.737 193.125 259.557  1.00145.11           C  
ATOM   9476  N   GLY B 381     221.025 193.772 256.512  1.00143.45           N  
ATOM   9477  CA  GLY B 381     220.811 194.682 255.392  1.00143.62           C  
ATOM   9478  C   GLY B 381     220.622 193.947 254.067  1.00141.46           C  
ATOM   9479  O   GLY B 381     220.037 194.488 253.128  1.00142.44           O  
ATOM   9480  N   VAL B 382     221.140 192.724 253.981  1.00142.12           N  
ATOM   9481  CA  VAL B 382     221.060 191.944 252.754  1.00140.11           C  
ATOM   9482  C   VAL B 382     220.594 190.523 253.030  1.00139.01           C  
ATOM   9483  O   VAL B 382     220.753 190.016 254.137  1.00141.43           O  
ATOM   9484  CB  VAL B 382     222.435 191.890 252.057  1.00139.17           C  
ATOM   9485  N   SER B 383     220.088 189.857 252.000  1.00138.55           N  
ATOM   9486  CA  SER B 383     219.745 188.444 252.098  1.00138.04           C  
ATOM   9487  C   SER B 383     221.032 187.606 252.156  1.00136.86           C  
ATOM   9488  O   SER B 383     221.920 187.809 251.330  1.00137.77           O  
ATOM   9489  CB  SER B 383     218.890 188.046 250.909  1.00137.02           C  
ATOM   9490  N   PRO B 384     221.145 186.636 253.079  1.00138.84           N  
ATOM   9491  CA  PRO B 384     222.313 185.798 253.315  1.00138.77           C  
ATOM   9492  C   PRO B 384     222.631 184.874 252.144  1.00135.25           C  
ATOM   9493  O   PRO B 384     223.736 184.346 252.040  1.00137.72           O  
ATOM   9494  CB  PRO B 384     221.902 184.999 254.560  1.00140.65           C  
ATOM   9495  CG  PRO B 384     220.397 184.980 254.533  1.00138.72           C  
ATOM   9496  CD  PRO B 384     219.999 186.321 253.947  1.00138.08           C  
ATOM   9497  N   THR B 385     221.661 184.681 251.259  1.00137.89           N  
ATOM   9498  CA  THR B 385     221.837 183.798 250.118  1.00136.54           C  
ATOM   9499  C   THR B 385     222.162 184.556 248.836  1.00136.51           C  
ATOM   9500  O   THR B 385     222.316 183.945 247.781  1.00135.33           O  
ATOM   9501  CB  THR B 385     220.576 182.957 249.884  1.00138.96           C  
ATOM   9502  N   LYS B 386     222.241 185.886 248.914  1.00135.80           N  
ATOM   9503  CA  LYS B 386     222.547 186.702 247.739  1.00133.63           C  
ATOM   9504  C   LYS B 386     223.947 187.280 247.845  1.00131.66           C  
ATOM   9505  O   LYS B 386     224.377 188.076 247.012  1.00132.12           O  
ATOM   9506  CB  LYS B 386     221.523 187.823 247.558  1.00133.66           C  
ATOM   9507  N   LEU B 387     224.676 186.850 248.857  1.00132.20           N  
ATOM   9508  CA  LEU B 387     225.987 187.403 249.135  1.00131.67           C  
ATOM   9509  C   LEU B 387     226.976 187.168 248.008  1.00128.85           C  
ATOM   9510  O   LEU B 387     227.886 187.971 247.817  1.00130.82           O  
ATOM   9511  CB  LEU B 387     226.530 186.817 250.436  1.00134.30           C  
ATOM   9512  N   ASN B 388     226.794 186.098 247.238  1.00131.18           N  
ATOM   9513  CA  ASN B 388     227.706 185.843 246.134  1.00128.10           C  
ATOM   9514  C   ASN B 388     227.288 186.549 244.844  1.00126.77           C  
ATOM   9515  O   ASN B 388     227.983 186.462 243.835  1.00123.70           O  
ATOM   9516  CB  ASN B 388     227.854 184.362 245.891  1.00128.22           C  
ATOM   9517  N   ASP B 389     226.146 187.235 244.864  1.00128.85           N  
ATOM   9518  CA  ASP B 389     225.702 188.005 243.704  1.00129.38           C  
ATOM   9519  C   ASP B 389     226.045 189.475 243.904  1.00128.38           C  
ATOM   9520  O   ASP B 389     226.310 190.211 242.951  1.00128.04           O  
ATOM   9521  CB  ASP B 389     224.202 187.839 243.468  1.00129.90           C  
ATOM   9522  N   LEU B 390     226.042 189.877 245.166  1.00128.88           N  
ATOM   9523  CA  LEU B 390     226.299 191.239 245.608  1.00128.90           C  
ATOM   9524  C   LEU B 390     227.789 191.596 245.567  1.00127.81           C  
ATOM   9525  O   LEU B 390     228.648 190.706 245.528  1.00126.22           O  
ATOM   9526  CB  LEU B 390     225.771 191.403 247.044  1.00128.86           C  
ATOM   9527  N   CYS B 391     228.077 192.911 245.556  1.00127.65           N  
ATOM   9528  CA  CYS B 391     229.428 193.460 245.662  1.00127.77           C  
ATOM   9529  C   CYS B 391     229.390 194.709 246.542  1.00127.78           C  
ATOM   9530  O   CYS B 391     228.472 195.527 246.428  1.00128.67           O  
ATOM   9531  CB  CYS B 391     230.009 193.800 244.277  1.00127.72           C  
ATOM   9532  SG  CYS B 391     231.750 194.349 244.320  1.00127.37           S  
ATOM   9533  N   PHE B 392     230.371 194.823 247.451  1.00127.25           N  
ATOM   9534  CA  PHE B 392     230.447 195.884 248.450  1.00127.48           C  
ATOM   9535  C   PHE B 392     231.706 196.704 248.226  1.00126.38           C  
ATOM   9536  O   PHE B 392     232.735 196.186 247.785  1.00127.04           O  
ATOM   9537  CB  PHE B 392     230.465 195.239 249.829  1.00130.49           C  
ATOM   9538  N   THR B 393     231.653 197.991 248.538  1.00127.17           N  
ATOM   9539  CA  THR B 393     232.830 198.805 248.295  1.00126.58           C  
ATOM   9540  C   THR B 393     233.993 198.317 249.141  1.00124.13           C  
ATOM   9541  O   THR B 393     235.087 198.082 248.626  1.00123.30           O  
ATOM   9542  CB  THR B 393     232.560 200.287 248.601  1.00124.94           C  
ATOM   9543  N   ASN B 394     233.720 198.120 250.429  1.00126.50           N  
ATOM   9544  CA  ASN B 394     234.693 197.643 251.403  1.00127.02           C  
ATOM   9545  C   ASN B 394     233.979 196.689 252.344  1.00127.93           C  
ATOM   9546  O   ASN B 394     232.797 196.885 252.626  1.00129.71           O  
ATOM   9547  CB  ASN B 394     235.254 198.791 252.228  1.00126.06           C  
ATOM   9548  N   VAL B 395     234.679 195.690 252.867  1.00129.72           N  
ATOM   9549  CA  VAL B 395     234.090 194.839 253.892  1.00135.99           C  
ATOM   9550  C   VAL B 395     234.990 194.771 255.121  1.00125.78           C  
ATOM   9551  O   VAL B 395     236.197 194.602 255.000  1.00137.45           O  
ATOM   9552  CB  VAL B 395     233.793 193.433 253.331  1.00130.37           C  
ATOM   9553  N   TYR B 396     234.423 194.927 256.306  1.00141.25           N  
ATOM   9554  CA  TYR B 396     235.259 194.856 257.503  1.00132.91           C  
ATOM   9555  C   TYR B 396     234.837 193.751 258.447  1.00139.86           C  
ATOM   9556  O   TYR B 396     233.660 193.596 258.756  1.00140.75           O  
ATOM   9557  CB  TYR B 396     235.252 196.187 258.238  1.00135.94           C  
ATOM   9558  N   ALA B 397     235.818 192.998 258.928  1.00136.81           N  
ATOM   9559  CA  ALA B 397     235.571 191.918 259.868  1.00141.07           C  
ATOM   9560  C   ALA B 397     235.906 192.322 261.290  1.00143.60           C  
ATOM   9561  O   ALA B 397     237.079 192.419 261.660  1.00141.16           O  
ATOM   9562  CB  ALA B 397     236.380 190.695 259.488  1.00139.30           C  
ATOM   9563  N   ASP B 398     234.868 192.526 262.088  1.00143.12           N  
ATOM   9564  CA  ASP B 398     235.007 192.893 263.487  1.00151.97           C  
ATOM   9565  C   ASP B 398     234.949 191.604 264.309  1.00142.87           C  
ATOM   9566  O   ASP B 398     233.909 190.947 264.385  1.00150.63           O  
ATOM   9567  CB  ASP B 398     233.898 193.874 263.870  1.00147.57           C  
ATOM   9568  N   SER B 399     236.093 191.197 264.856  1.00150.68           N  
ATOM   9569  CA  SER B 399     236.237 189.884 265.491  1.00154.41           C  
ATOM   9570  C   SER B 399     236.503 189.912 267.000  1.00141.79           C  
ATOM   9571  O   SER B 399     237.446 190.556 267.479  1.00158.71           O  
ATOM   9572  CB  SER B 399     237.344 189.125 264.799  1.00148.04           C  
ATOM   9573  N   PHE B 400     235.652 189.202 267.750  1.00155.36           N  
ATOM   9574  CA  PHE B 400     235.733 189.172 269.212  1.00148.12           C  
ATOM   9575  C   PHE B 400     235.107 187.946 269.895  1.00149.61           C  
ATOM   9576  O   PHE B 400     234.301 187.229 269.304  1.00154.50           O  
ATOM   9577  CB  PHE B 400     235.080 190.428 269.764  1.00156.62           C  
ATOM   9578  N   VAL B 401     235.466 187.733 271.169  1.00155.31           N  
ATOM   9579  CA  VAL B 401     234.863 186.670 271.989  1.00158.50           C  
ATOM   9580  C   VAL B 401     233.969 187.199 273.107  1.00159.41           C  
ATOM   9581  O   VAL B 401     234.390 188.017 273.928  1.00155.50           O  
ATOM   9582  CB  VAL B 401     235.939 185.772 272.625  1.00155.94           C  
ATOM   9583  N   ILE B 402     232.731 186.709 273.118  1.00154.12           N  
ATOM   9584  CA  ILE B 402     231.720 187.064 274.116  1.00156.24           C  
ATOM   9585  C   ILE B 402     231.015 185.858 274.710  1.00146.37           C  
ATOM   9586  O   ILE B 402     231.125 184.746 274.205  1.00152.19           O  
ATOM   9587  CB  ILE B 402     230.699 188.043 273.541  1.00157.06           C  
ATOM   9588  N   ARG B 403     230.290 186.082 275.793  1.00156.83           N  
ATOM   9589  CA  ARG B 403     229.531 185.021 276.440  1.00166.06           C  
ATOM   9590  C   ARG B 403     228.258 184.699 275.652  1.00151.31           C  
ATOM   9591  O   ARG B 403     227.603 185.602 275.136  1.00166.75           O  
ATOM   9592  CB  ARG B 403     229.210 185.439 277.865  1.00156.96           C  
ATOM   9593  N   GLY B 404     227.917 183.412 275.573  1.00164.01           N  
ATOM   9594  CA  GLY B 404     226.760 182.901 274.825  1.00158.38           C  
ATOM   9595  C   GLY B 404     225.463 183.684 274.984  1.00157.80           C  
ATOM   9596  O   GLY B 404     224.862 184.099 273.994  1.00160.97           O  
ATOM   9597  N   ASP B 405     225.032 183.924 276.212  1.00157.42           N  
ATOM   9598  CA  ASP B 405     223.774 184.641 276.435  1.00161.50           C  
ATOM   9599  C   ASP B 405     223.778 186.047 275.842  1.00157.99           C  
ATOM   9600  O   ASP B 405     222.722 186.632 275.592  1.00154.23           O  
ATOM   9601  CB  ASP B 405     223.479 184.776 277.925  1.00156.86           C  
ATOM   9602  N   GLU B 406     224.964 186.612 275.669  1.00155.82           N  
ATOM   9603  CA  GLU B 406     225.121 187.979 275.212  1.00163.65           C  
ATOM   9604  C   GLU B 406     225.301 188.060 273.694  1.00141.75           C  
ATOM   9605  O   GLU B 406     225.375 189.148 273.124  1.00161.95           O  
ATOM   9606  CB  GLU B 406     226.303 188.607 275.944  1.00156.21           C  
ATOM   9607  N   VAL B 407     225.313 186.909 273.026  1.00162.22           N  
ATOM   9608  CA  VAL B 407     225.489 186.856 271.578  1.00157.94           C  
ATOM   9609  C   VAL B 407     224.344 187.561 270.874  1.00160.17           C  
ATOM   9610  O   VAL B 407     224.540 188.185 269.833  1.00153.92           O  
ATOM   9611  CB  VAL B 407     225.649 185.403 271.081  1.00154.17           C  
ATOM   9612  N   ARG B 408     223.151 187.477 271.446  1.00157.19           N  
ATOM   9613  CA  ARG B 408     221.965 188.106 270.880  1.00154.57           C  
ATOM   9614  C   ARG B 408     222.081 189.630 270.787  1.00158.92           C  
ATOM   9615  O   ARG B 408     221.278 190.271 270.112  1.00153.13           O  
ATOM   9616  CB  ARG B 408     220.739 187.772 271.714  1.00157.04           C  
ATOM   9617  N   GLN B 409     223.060 190.222 271.472  1.00154.83           N  
ATOM   9618  CA  GLN B 409     223.226 191.669 271.429  1.00157.71           C  
ATOM   9619  C   GLN B 409     223.959 192.117 270.173  1.00157.05           C  
ATOM   9620  O   GLN B 409     224.011 193.313 269.874  1.00154.53           O  
ATOM   9621  CB  GLN B 409     223.993 192.171 272.653  1.00157.72           C  
ATOM   9622  N   ILE B 410     224.526 191.179 269.418  1.00151.43           N  
ATOM   9623  CA  ILE B 410     225.265 191.585 268.235  1.00152.82           C  
ATOM   9624  C   ILE B 410     224.296 191.667 267.069  1.00154.90           C  
ATOM   9625  O   ILE B 410     224.222 190.778 266.222  1.00152.67           O  
ATOM   9626  CB  ILE B 410     226.395 190.592 267.910  1.00153.53           C  
ATOM   9627  N   ALA B 411     223.555 192.760 267.051  1.00153.00           N  
ATOM   9628  CA  ALA B 411     222.527 193.026 266.059  1.00152.45           C  
ATOM   9629  C   ALA B 411     222.178 194.511 266.125  1.00154.27           C  
ATOM   9630  O   ALA B 411     222.440 195.147 267.144  1.00152.61           O  
ATOM   9631  CB  ALA B 411     221.311 192.143 266.324  1.00153.10           C  
ATOM   9632  N   PRO B 412     221.647 195.104 265.054  1.00152.14           N  
ATOM   9633  CA  PRO B 412     221.139 196.462 265.019  1.00152.22           C  
ATOM   9634  C   PRO B 412     219.916 196.615 265.911  1.00153.11           C  
ATOM   9635  O   PRO B 412     219.062 195.729 265.955  1.00153.37           O  
ATOM   9636  CB  PRO B 412     220.790 196.647 263.539  1.00150.63           C  
ATOM   9637  CG  PRO B 412     220.612 195.244 262.993  1.00149.64           C  
ATOM   9638  CD  PRO B 412     221.581 194.393 263.774  1.00150.71           C  
ATOM   9639  N   GLY B 413     219.814 197.758 266.586  1.00152.73           N  
ATOM   9640  CA  GLY B 413     218.658 198.059 267.426  1.00153.33           C  
ATOM   9641  C   GLY B 413     218.698 197.362 268.787  1.00153.47           C  
ATOM   9642  O   GLY B 413     217.654 197.143 269.403  1.00154.67           O  
ATOM   9643  N   GLN B 414     219.888 196.987 269.248  1.00152.64           N  
ATOM   9644  CA  GLN B 414     220.008 196.291 270.523  1.00154.80           C  
ATOM   9645  C   GLN B 414     220.612 197.153 271.614  1.00157.12           C  
ATOM   9646  O   GLN B 414     221.339 198.110 271.340  1.00156.33           O  
ATOM   9647  CB  GLN B 414     220.838 195.023 270.373  1.00154.41           C  
ATOM   9648  N   THR B 415     220.333 196.771 272.856  1.00154.09           N  
ATOM   9649  CA  THR B 415     220.908 197.393 274.043  1.00156.02           C  
ATOM   9650  C   THR B 415     221.503 196.312 274.937  1.00156.86           C  
ATOM   9651  O   THR B 415     221.225 195.125 274.754  1.00156.80           O  
ATOM   9652  CB  THR B 415     219.850 198.187 274.827  1.00156.56           C  
ATOM   9653  N   GLY B 416     222.309 196.711 275.912  1.00156.57           N  
ATOM   9654  CA  GLY B 416     222.907 195.745 276.828  1.00156.27           C  
ATOM   9655  C   GLY B 416     224.389 196.020 277.043  1.00157.69           C  
ATOM   9656  O   GLY B 416     224.952 196.950 276.472  1.00160.63           O  
ATOM   9657  N   LYS B 417     225.040 195.197 277.854  1.00157.61           N  
ATOM   9658  CA  LYS B 417     226.440 195.438 278.185  1.00157.09           C  
ATOM   9659  C   LYS B 417     227.314 195.579 276.944  1.00156.52           C  
ATOM   9660  O   LYS B 417     228.188 196.446 276.886  1.00158.66           O  
ATOM   9661  CB  LYS B 417     226.984 194.296 279.045  1.00157.80           C  
ATOM   9662  N   ILE B 418     227.071 194.757 275.933  1.00161.96           N  
ATOM   9663  CA  ILE B 418     227.899 194.833 274.747  1.00158.26           C  
ATOM   9664  C   ILE B 418     227.388 195.887 273.809  1.00148.78           C  
ATOM   9665  O   ILE B 418     228.140 196.755 273.364  1.00149.82           O  
ATOM   9666  CB  ILE B 418     227.951 193.509 273.984  1.00155.81           C  
ATOM   9667  N   ALA B 419     226.100 195.830 273.520  1.00157.76           N  
ATOM   9668  CA  ALA B 419     225.525 196.737 272.548  1.00158.93           C  
ATOM   9669  C   ALA B 419     225.740 198.200 272.939  1.00157.34           C  
ATOM   9670  O   ALA B 419     225.897 199.050 272.065  1.00156.26           O  
ATOM   9671  CB  ALA B 419     224.049 196.452 272.387  1.00156.02           C  
ATOM   9672  N   ASP B 420     225.726 198.508 274.236  1.00158.29           N  
ATOM   9673  CA  ASP B 420     225.898 199.893 274.656  1.00157.01           C  
ATOM   9674  C   ASP B 420     227.334 200.298 275.016  1.00156.32           C  
ATOM   9675  O   ASP B 420     227.701 201.456 274.816  1.00158.25           O  
ATOM   9676  CB  ASP B 420     224.991 200.211 275.850  1.00156.65           C  
ATOM   9677  N   TYR B 421     228.148 199.390 275.574  1.00154.57           N  
ATOM   9678  CA  TYR B 421     229.463 199.815 276.055  1.00159.78           C  
ATOM   9679  C   TYR B 421     230.684 199.194 275.378  1.00157.51           C  
ATOM   9680  O   TYR B 421     231.808 199.636 275.622  1.00155.13           O  
ATOM   9681  CB  TYR B 421     229.545 199.563 277.554  1.00159.98           C  
ATOM   9682  N   ASN B 422     230.500 198.161 274.561  1.00157.35           N  
ATOM   9683  CA  ASN B 422     231.659 197.480 274.000  1.00162.25           C  
ATOM   9684  C   ASN B 422     231.657 197.477 272.492  1.00158.53           C  
ATOM   9685  O   ASN B 422     232.596 197.945 271.860  1.00153.99           O  
ATOM   9686  CB  ASN B 422     231.704 196.065 274.498  1.00161.01           C  
ATOM   9687  N   TYR B 423     230.605 196.922 271.921  1.00156.97           N  
ATOM   9688  CA  TYR B 423     230.505 196.764 270.486  1.00150.29           C  
ATOM   9689  C   TYR B 423     229.113 197.099 269.998  1.00155.55           C  
ATOM   9690  O   TYR B 423     228.217 196.253 269.989  1.00154.86           O  
ATOM   9691  CB  TYR B 423     230.874 195.344 270.078  1.00153.00           C  
ATOM   9692  N   LYS B 424     228.933 198.346 269.601  1.00155.02           N  
ATOM   9693  CA  LYS B 424     227.643 198.821 269.142  1.00154.04           C  
ATOM   9694  C   LYS B 424     227.554 198.762 267.627  1.00153.87           C  
ATOM   9695  O   LYS B 424     228.487 199.162 266.929  1.00154.68           O  
ATOM   9696  CB  LYS B 424     227.401 200.257 269.618  1.00152.44           C  
ATOM   9697  N   LEU B 425     226.423 198.300 267.115  1.00151.94           N  
ATOM   9698  CA  LEU B 425     226.172 198.355 265.683  1.00150.71           C  
ATOM   9699  C   LEU B 425     225.221 199.507 265.382  1.00150.74           C  
ATOM   9700  O   LEU B 425     224.472 199.921 266.267  1.00151.28           O  
ATOM   9701  CB  LEU B 425     225.589 197.034 265.156  1.00150.40           C  
ATOM   9702  N   PRO B 426     225.254 200.059 264.163  1.00149.70           N  
ATOM   9703  CA  PRO B 426     224.314 201.028 263.636  1.00150.63           C  
ATOM   9704  C   PRO B 426     222.921 200.428 263.597  1.00153.47           C  
ATOM   9705  O   PRO B 426     222.770 199.213 263.501  1.00153.56           O  
ATOM   9706  CB  PRO B 426     224.831 201.277 262.213  1.00151.04           C  
ATOM   9707  CG  PRO B 426     226.278 200.877 262.235  1.00149.88           C  
ATOM   9708  CD  PRO B 426     226.371 199.752 263.248  1.00150.91           C  
ATOM   9709  N   ASP B 427     221.902 201.277 263.613  1.00150.29           N  
ATOM   9710  CA  ASP B 427     220.527 200.795 263.522  1.00151.29           C  
ATOM   9711  C   ASP B 427     220.201 200.482 262.069  1.00150.59           C  
ATOM   9712  O   ASP B 427     219.356 199.639 261.774  1.00152.47           O  
ATOM   9713  CB  ASP B 427     219.557 201.831 264.082  1.00151.68           C  
ATOM   9714  N   ASP B 428     220.907 201.156 261.167  1.00150.14           N  
ATOM   9715  CA  ASP B 428     220.799 200.975 259.728  1.00150.04           C  
ATOM   9716  C   ASP B 428     221.962 200.123 259.215  1.00148.58           C  
ATOM   9717  O   ASP B 428     222.396 200.251 258.069  1.00149.61           O  
ATOM   9718  CB  ASP B 428     220.761 202.338 259.039  1.00151.09           C  
ATOM   9719  N   PHE B 429     222.462 199.254 260.088  1.00148.84           N  
ATOM   9720  CA  PHE B 429     223.590 198.385 259.797  1.00146.98           C  
ATOM   9721  C   PHE B 429     223.367 197.467 258.617  1.00147.12           C  
ATOM   9722  O   PHE B 429     222.342 196.793 258.511  1.00145.85           O  
ATOM   9723  CB  PHE B 429     223.897 197.515 261.021  1.00146.70           C  
ATOM   9724  N   THR B 430     224.368 197.420 257.749  1.00145.91           N  
ATOM   9725  CA  THR B 430     224.371 196.502 256.631  1.00145.87           C  
ATOM   9726  C   THR B 430     225.589 195.623 256.787  1.00141.39           C  
ATOM   9727  O   THR B 430     226.717 196.116 256.877  1.00139.81           O  
ATOM   9728  CB  THR B 430     224.404 197.229 255.274  1.00144.49           C  
ATOM   9729  N   GLY B 431     225.354 194.330 256.831  1.00142.18           N  
ATOM   9730  CA  GLY B 431     226.396 193.355 257.057  1.00144.68           C  
ATOM   9731  C   GLY B 431     225.771 192.083 257.598  1.00145.44           C  
ATOM   9732  O   GLY B 431     224.536 191.986 257.689  1.00139.66           O  
ATOM   9733  N   CYS B 432     226.631 191.116 257.937  1.00144.03           N  
ATOM   9734  CA  CYS B 432     226.242 189.798 258.444  1.00143.55           C  
ATOM   9735  C   CYS B 432     226.975 189.477 259.754  1.00146.96           C  
ATOM   9736  O   CYS B 432     228.166 189.768 259.902  1.00147.10           O  
ATOM   9737  CB  CYS B 432     226.526 188.706 257.383  1.00144.40           C  
ATOM   9738  SG  CYS B 432     225.614 188.926 255.807  1.00139.12           S  
ATOM   9739  N   VAL B 433     226.255 188.853 260.697  1.00144.58           N  
ATOM   9740  CA  VAL B 433     226.780 188.428 261.995  1.00145.22           C  
ATOM   9741  C   VAL B 433     226.836 186.908 262.065  1.00146.00           C  
ATOM   9742  O   VAL B 433     225.817 186.220 261.950  1.00148.27           O  
ATOM   9743  CB  VAL B 433     225.905 188.984 263.131  1.00145.99           C  
ATOM   9744  N   ILE B 434     228.043 186.395 262.237  1.00146.00           N  
ATOM   9745  CA  ILE B 434     228.290 184.962 262.260  1.00149.37           C  
ATOM   9746  C   ILE B 434     228.918 184.557 263.586  1.00147.50           C  
ATOM   9747  O   ILE B 434     229.860 185.199 264.051  1.00149.41           O  
ATOM   9748  CB  ILE B 434     229.213 184.580 261.096  1.00148.47           C  
ATOM   9749  N   ALA B 435     228.408 183.499 264.211  1.00147.25           N  
ATOM   9750  CA  ALA B 435     228.977 183.111 265.500  1.00158.84           C  
ATOM   9751  C   ALA B 435     228.972 181.604 265.726  1.00144.89           C  
ATOM   9752  O   ALA B 435     228.137 180.868 265.188  1.00159.56           O  
ATOM   9753  CB  ALA B 435     228.228 183.798 266.629  1.00149.57           C  
ATOM   9754  N   TRP B 436     229.923 181.157 266.545  1.00155.80           N  
ATOM   9755  CA  TRP B 436     230.028 179.754 266.920  1.00163.46           C  
ATOM   9756  C   TRP B 436     230.656 179.604 268.298  1.00146.90           C  
ATOM   9757  O   TRP B 436     231.368 180.493 268.762  1.00121.37           O  
ATOM   9758  CB  TRP B 436     230.833 179.019 265.856  1.00151.78           C  
ATOM   9759  N   ASN B 437     230.402 178.483 268.965  1.00155.53           N  
ATOM   9760  CA  ASN B 437     230.972 178.293 270.292  1.00160.49           C  
ATOM   9761  C   ASN B 437     232.432 177.865 270.233  1.00159.52           C  
ATOM   9762  O   ASN B 437     232.847 177.135 269.331  1.00152.37           O  
ATOM   9763  CB  ASN B 437     230.128 177.337 271.112  1.00153.15           C  
ATOM   9764  N   SER B 438     233.190 178.297 271.234  1.00156.36           N  
ATOM   9765  CA  SER B 438     234.608 177.993 271.371  1.00169.56           C  
ATOM   9766  C   SER B 438     234.918 177.373 272.733  1.00140.68           C  
ATOM   9767  O   SER B 438     235.960 177.640 273.348  1.00159.04           O  
ATOM   9768  CB  SER B 438     235.398 179.260 271.160  1.00164.02           C  
ATOM   9769  N   ASN B 439     234.002 176.529 273.202  1.00165.50           N  
ATOM   9770  CA  ASN B 439     234.130 175.891 274.508  1.00168.21           C  
ATOM   9771  C   ASN B 439     235.333 174.958 274.580  1.00164.19           C  
ATOM   9772  O   ASN B 439     235.889 174.733 275.650  1.00159.06           O  
ATOM   9773  CB  ASN B 439     232.864 175.136 274.854  1.00155.92           C  
ATOM   9774  N   ASN B 440     235.738 174.401 273.446  1.00156.30           N  
ATOM   9775  CA  ASN B 440     236.890 173.519 273.428  1.00158.83           C  
ATOM   9776  C   ASN B 440     238.135 174.223 272.906  1.00160.36           C  
ATOM   9777  O   ASN B 440     239.131 173.568 272.594  1.00162.43           O  
ATOM   9778  CB  ASN B 440     236.587 172.290 272.597  1.00160.35           C  
ATOM   9779  N   LEU B 441     238.077 175.549 272.798  1.00158.50           N  
ATOM   9780  CA  LEU B 441     239.196 176.301 272.255  1.00157.96           C  
ATOM   9781  C   LEU B 441     239.678 177.379 273.220  1.00161.96           C  
ATOM   9782  O   LEU B 441     240.856 177.423 273.579  1.00161.53           O  
ATOM   9783  CB  LEU B 441     238.775 176.967 270.942  1.00160.48           C  
ATOM   9784  N   ASP B 442     238.766 178.270 273.619  1.00160.55           N  
ATOM   9785  CA  ASP B 442     239.138 179.392 274.474  1.00159.01           C  
ATOM   9786  C   ASP B 442     238.901 179.097 275.946  1.00158.30           C  
ATOM   9787  O   ASP B 442     239.614 179.603 276.808  1.00158.81           O  
ATOM   9788  CB  ASP B 442     238.371 180.654 274.078  1.00158.55           C  
ATOM   9789  N   SER B 443     237.889 178.298 276.254  1.00161.66           N  
ATOM   9790  CA  SER B 443     237.605 178.038 277.666  1.00161.72           C  
ATOM   9791  C   SER B 443     238.744 177.260 278.309  1.00161.92           C  
ATOM   9792  O   SER B 443     239.359 176.403 277.671  1.00160.67           O  
ATOM   9793  CB  SER B 443     236.317 177.276 277.832  1.00155.40           C  
ATOM   9794  N   LYS B 444     239.016 177.552 279.578  1.00166.71           N  
ATOM   9795  CA  LYS B 444     240.064 176.851 280.315  1.00163.00           C  
ATOM   9796  C   LYS B 444     239.512 176.319 281.622  1.00158.20           C  
ATOM   9797  O   LYS B 444     238.599 176.897 282.197  1.00156.34           O  
ATOM   9798  CB  LYS B 444     241.262 177.773 280.576  1.00161.91           C  
ATOM   9799  N   VAL B 445     240.072 175.229 282.120  1.00164.20           N  
ATOM   9800  CA  VAL B 445     239.529 174.618 283.329  1.00161.91           C  
ATOM   9801  C   VAL B 445     239.539 175.576 284.513  1.00163.94           C  
ATOM   9802  O   VAL B 445     238.572 175.636 285.272  1.00163.49           O  
ATOM   9803  CB  VAL B 445     240.301 173.332 283.673  1.00162.60           C  
ATOM   9804  N   GLY B 446     240.622 176.331 284.666  1.00162.97           N  
ATOM   9805  CA  GLY B 446     240.731 177.277 285.770  1.00162.49           C  
ATOM   9806  C   GLY B 446     240.048 178.613 285.469  1.00161.77           C  
ATOM   9807  O   GLY B 446     240.030 179.507 286.315  1.00162.12           O  
ATOM   9808  N   GLY B 447     239.509 178.751 284.260  1.00161.49           N  
ATOM   9809  CA  GLY B 447     238.847 179.970 283.820  1.00160.77           C  
ATOM   9810  C   GLY B 447     239.730 180.832 282.929  1.00162.83           C  
ATOM   9811  O   GLY B 447     240.838 181.220 283.307  1.00162.58           O  
ATOM   9812  N   ASN B 448     239.229 181.143 281.740  1.00160.34           N  
ATOM   9813  CA  ASN B 448     239.945 182.014 280.824  1.00161.13           C  
ATOM   9814  C   ASN B 448     239.439 183.424 281.042  1.00162.48           C  
ATOM   9815  O   ASN B 448     238.310 183.744 280.675  1.00158.93           O  
ATOM   9816  CB  ASN B 448     239.785 181.609 279.371  1.00160.09           C  
ATOM   9817  N   TYR B 449     240.259 184.242 281.686  1.00158.98           N  
ATOM   9818  CA  TYR B 449     239.883 185.593 282.082  1.00162.73           C  
ATOM   9819  C   TYR B 449     240.581 186.643 281.233  1.00163.36           C  
ATOM   9820  O   TYR B 449     240.694 187.803 281.629  1.00158.86           O  
ATOM   9821  CB  TYR B 449     240.209 185.816 283.554  1.00160.01           C  
ATOM   9822  N   ASN B 450     241.062 186.236 280.063  1.00157.53           N  
ATOM   9823  CA  ASN B 450     241.777 187.152 279.183  1.00160.70           C  
ATOM   9824  C   ASN B 450     240.821 187.976 278.334  1.00162.24           C  
ATOM   9825  O   ASN B 450     241.243 188.853 277.580  1.00159.91           O  
ATOM   9826  CB  ASN B 450     242.727 186.390 278.283  1.00159.78           C  
ATOM   9827  N   TYR B 451     239.533 187.689 278.450  1.00157.34           N  
ATOM   9828  CA  TYR B 451     238.535 188.400 277.677  1.00157.34           C  
ATOM   9829  C   TYR B 451     237.777 189.377 278.549  1.00157.54           C  
ATOM   9830  O   TYR B 451     237.089 188.978 279.491  1.00161.30           O  
ATOM   9831  CB  TYR B 451     237.581 187.417 277.018  1.00160.59           C  
ATOM   9832  N   LEU B 452     237.905 190.662 278.234  1.00161.19           N  
ATOM   9833  CA  LEU B 452     237.284 191.694 279.041  1.00166.48           C  
ATOM   9834  C   LEU B 452     236.248 192.521 278.299  1.00160.49           C  
ATOM   9835  O   LEU B 452     236.330 192.727 277.080  1.00157.33           O  
ATOM   9836  CB  LEU B 452     238.349 192.617 279.630  1.00160.55           C  
ATOM   9837  N   TYR B 453     235.287 192.996 279.078  1.00160.49           N  
ATOM   9838  CA  TYR B 453     234.177 193.806 278.616  1.00161.34           C  
ATOM   9839  C   TYR B 453     233.889 194.935 279.608  1.00168.27           C  
ATOM   9840  O   TYR B 453     234.184 194.813 280.797  1.00152.89           O  
ATOM   9841  CB  TYR B 453     232.948 192.907 278.467  1.00160.55           C  
ATOM   9842  N   ARG B 454     233.275 196.023 279.124  1.00157.61           N  
ATOM   9843  CA  ARG B 454     232.828 197.151 279.945  1.00157.27           C  
ATOM   9844  C   ARG B 454     231.364 196.941 280.344  1.00159.49           C  
ATOM   9845  O   ARG B 454     230.565 196.384 279.586  1.00156.96           O  
ATOM   9846  CB  ARG B 454     233.005 198.489 279.195  1.00157.05           C  
ATOM   9847  N   LYS B 462     229.066 204.991 270.649  1.00153.93           N  
ATOM   9848  CA  LYS B 462     228.688 205.149 269.254  1.00152.43           C  
ATOM   9849  C   LYS B 462     229.007 203.848 268.475  1.00155.16           C  
ATOM   9850  O   LYS B 462     229.774 203.015 268.981  1.00150.68           O  
ATOM   9851  CB  LYS B 462     229.410 206.383 268.635  1.00154.12           C  
ATOM   9852  N   PRO B 463     228.401 203.605 267.267  1.00151.86           N  
ATOM   9853  CA  PRO B 463     228.629 202.437 266.423  1.00151.48           C  
ATOM   9854  C   PRO B 463     230.101 202.247 266.099  1.00154.80           C  
ATOM   9855  O   PRO B 463     230.776 203.192 265.683  1.00152.47           O  
ATOM   9856  CB  PRO B 463     227.824 202.768 265.166  1.00152.48           C  
ATOM   9857  CG  PRO B 463     226.727 203.685 265.634  1.00151.57           C  
ATOM   9858  CD  PRO B 463     227.372 204.542 266.686  1.00153.50           C  
ATOM   9859  N   PHE B 464     230.586 201.034 266.306  1.00149.92           N  
ATOM   9860  CA  PHE B 464     231.971 200.658 266.069  1.00153.01           C  
ATOM   9861  C   PHE B 464     232.977 201.513 266.839  1.00151.81           C  
ATOM   9862  O   PHE B 464     234.155 201.557 266.478  1.00152.50           O  
ATOM   9863  CB  PHE B 464     232.289 200.707 264.577  1.00151.50           C  
ATOM   9864  N   GLU B 465     232.547 202.148 267.928  1.00152.57           N  
ATOM   9865  CA  GLU B 465     233.476 202.940 268.721  1.00154.04           C  
ATOM   9866  C   GLU B 465     234.239 202.034 269.684  1.00154.81           C  
ATOM   9867  O   GLU B 465     233.666 201.537 270.655  1.00153.77           O  
ATOM   9868  CB  GLU B 465     232.729 204.021 269.510  1.00152.84           C  
ATOM   9869  N   ARG B 466     235.539 201.826 269.411  1.00153.57           N  
ATOM   9870  CA  ARG B 466     236.401 200.924 270.174  1.00153.44           C  
ATOM   9871  C   ARG B 466     237.126 201.694 271.281  1.00154.47           C  
ATOM   9872  O   ARG B 466     238.010 202.514 271.019  1.00152.60           O  
ATOM   9873  CB  ARG B 466     237.404 200.214 269.234  1.00153.10           C  
ATOM   9874  N   PRO B 491     237.124 199.699 285.342  1.00159.49           N  
ATOM   9875  CA  PRO B 491     236.172 199.940 284.258  1.00159.25           C  
ATOM   9876  C   PRO B 491     235.730 198.642 283.558  1.00162.18           C  
ATOM   9877  O   PRO B 491     234.552 198.502 283.212  1.00158.68           O  
ATOM   9878  CB  PRO B 491     236.955 200.885 283.312  1.00160.39           C  
ATOM   9879  CG  PRO B 491     238.418 200.608 283.606  1.00159.60           C  
ATOM   9880  CD  PRO B 491     238.452 200.293 285.088  1.00160.62           C  
ATOM   9881  N   LEU B 492     236.677 197.708 283.337  1.00157.84           N  
ATOM   9882  CA  LEU B 492     236.426 196.436 282.654  1.00161.95           C  
ATOM   9883  C   LEU B 492     236.385 195.264 283.617  1.00165.15           C  
ATOM   9884  O   LEU B 492     237.058 195.259 284.649  1.00159.57           O  
ATOM   9885  CB  LEU B 492     237.514 196.159 281.617  1.00159.99           C  
ATOM   9886  N   GLN B 493     235.619 194.253 283.239  1.00163.93           N  
ATOM   9887  CA  GLN B 493     235.523 193.003 283.971  1.00166.51           C  
ATOM   9888  C   GLN B 493     235.855 191.847 283.040  1.00157.60           C  
ATOM   9889  O   GLN B 493     235.721 191.962 281.823  1.00127.81           O  
ATOM   9890  CB  GLN B 493     234.124 192.836 284.564  1.00158.96           C  
ATOM   9891  N   SER B 494     236.314 190.737 283.602  1.00160.96           N  
ATOM   9892  CA  SER B 494     236.645 189.580 282.778  1.00165.71           C  
ATOM   9893  C   SER B 494     235.549 188.524 282.784  1.00164.10           C  
ATOM   9894  O   SER B 494     234.761 188.429 283.727  1.00160.11           O  
ATOM   9895  CB  SER B 494     237.954 188.974 283.241  1.00158.83           C  
ATOM   9896  N   TYR B 495     235.526 187.714 281.728  1.00161.89           N  
ATOM   9897  CA  TYR B 495     234.599 186.594 281.632  1.00159.59           C  
ATOM   9898  C   TYR B 495     235.213 185.328 282.208  1.00154.48           C  
ATOM   9899  O   TYR B 495     236.321 184.949 281.845  1.00164.06           O  
ATOM   9900  CB  TYR B 495     234.244 186.292 280.181  1.00157.21           C  
ATOM   9901  N   GLY B 496     234.480 184.631 283.060  1.00162.34           N  
ATOM   9902  CA  GLY B 496     234.970 183.371 283.612  1.00161.00           C  
ATOM   9903  C   GLY B 496     234.672 182.207 282.685  1.00162.89           C  
ATOM   9904  O   GLY B 496     233.788 181.399 282.966  1.00162.50           O  
ATOM   9905  N   PHE B 497     235.387 182.117 281.570  1.00162.33           N  
ATOM   9906  CA  PHE B 497     235.065 181.064 280.617  1.00157.40           C  
ATOM   9907  C   PHE B 497     235.691 179.725 280.995  1.00159.23           C  
ATOM   9908  O   PHE B 497     236.918 179.578 281.022  1.00158.77           O  
ATOM   9909  CB  PHE B 497     235.525 181.450 279.211  1.00160.03           C  
ATOM   9910  N   GLN B 498     234.827 178.751 281.285  1.00162.15           N  
ATOM   9911  CA  GLN B 498     235.231 177.414 281.707  1.00164.40           C  
ATOM   9912  C   GLN B 498     234.459 176.365 280.903  1.00162.67           C  
ATOM   9913  O   GLN B 498     233.265 176.541 280.658  1.00163.93           O  
ATOM   9914  CB  GLN B 498     234.969 177.228 283.210  1.00162.13           C  
ATOM   9915  N   PRO B 499     235.096 175.240 280.547  1.00154.85           N  
ATOM   9916  CA  PRO B 499     234.564 174.164 279.731  1.00162.41           C  
ATOM   9917  C   PRO B 499     233.426 173.415 280.402  1.00161.14           C  
ATOM   9918  O   PRO B 499     232.681 172.692 279.741  1.00161.69           O  
ATOM   9919  CB  PRO B 499     235.789 173.262 279.529  1.00160.66           C  
ATOM   9920  CG  PRO B 499     236.680 173.552 280.713  1.00161.87           C  
ATOM   9921  CD  PRO B 499     236.470 175.013 281.003  1.00166.83           C  
ATOM   9922  N   THR B 500     233.299 173.595 281.715  1.00160.34           N  
ATOM   9923  CA  THR B 500     232.301 172.904 282.510  1.00161.79           C  
ATOM   9924  C   THR B 500     231.040 173.726 282.742  1.00162.04           C  
ATOM   9925  O   THR B 500     230.123 173.267 283.426  1.00163.05           O  
ATOM   9926  CB  THR B 500     232.888 172.516 283.876  1.00163.01           C  
ATOM   9927  N   ASN B 501     230.985 174.945 282.210  1.00160.27           N  
ATOM   9928  CA  ASN B 501     229.799 175.764 282.432  1.00162.04           C  
ATOM   9929  C   ASN B 501     228.699 175.425 281.425  1.00162.18           C  
ATOM   9930  O   ASN B 501     228.882 174.580 280.548  1.00161.76           O  
ATOM   9931  CB  ASN B 501     230.131 177.241 282.386  1.00160.44           C  
ATOM   9932  N   GLY B 502     227.549 176.088 281.548  1.00159.11           N  
ATOM   9933  CA  GLY B 502     226.421 175.812 280.661  1.00160.75           C  
ATOM   9934  C   GLY B 502     226.597 176.481 279.307  1.00162.34           C  
ATOM   9935  O   GLY B 502     227.544 177.232 279.097  1.00154.94           O  
ATOM   9936  N   VAL B 503     225.656 176.252 278.395  1.00158.69           N  
ATOM   9937  CA  VAL B 503     225.778 176.786 277.040  1.00159.79           C  
ATOM   9938  C   VAL B 503     225.805 178.306 277.019  1.00160.10           C  
ATOM   9939  O   VAL B 503     226.601 178.911 276.305  1.00160.70           O  
ATOM   9940  CB  VAL B 503     224.640 176.271 276.143  1.00160.25           C  
ATOM   9941  N   GLY B 504     224.957 178.926 277.826  1.00158.76           N  
ATOM   9942  CA  GLY B 504     224.870 180.381 277.875  1.00162.71           C  
ATOM   9943  C   GLY B 504     226.132 181.002 278.464  1.00147.72           C  
ATOM   9944  O   GLY B 504     226.344 182.213 278.372  1.00156.40           O  
ATOM   9945  N   TYR B 505     226.976 180.174 279.073  1.00172.51           N  
ATOM   9946  CA  TYR B 505     228.195 180.646 279.693  1.00167.69           C  
ATOM   9947  C   TYR B 505     229.426 180.301 278.874  1.00158.59           C  
ATOM   9948  O   TYR B 505     230.548 180.622 279.270  1.00159.24           O  
ATOM   9949  CB  TYR B 505     228.318 180.043 281.077  1.00157.01           C  
ATOM   9950  N   GLN B 506     229.230 179.655 277.731  1.00166.29           N  
ATOM   9951  CA  GLN B 506     230.359 179.304 276.895  1.00160.63           C  
ATOM   9952  C   GLN B 506     230.800 180.563 276.182  1.00162.16           C  
ATOM   9953  O   GLN B 506     229.986 181.471 275.997  1.00127.61           O  
ATOM   9954  CB  GLN B 506     229.980 178.227 275.867  1.00155.77           C  
ATOM   9955  N   PRO B 507     232.076 180.683 275.824  1.00159.41           N  
ATOM   9956  CA  PRO B 507     232.583 181.704 274.950  1.00160.31           C  
ATOM   9957  C   PRO B 507     232.118 181.422 273.546  1.00142.39           C  
ATOM   9958  O   PRO B 507     232.097 180.263 273.120  1.00181.08           O  
ATOM   9959  CB  PRO B 507     234.097 181.556 275.081  1.00161.74           C  
ATOM   9960  CG  PRO B 507     234.309 180.122 275.484  1.00162.56           C  
ATOM   9961  CD  PRO B 507     233.081 179.746 276.319  1.00160.32           C  
ATOM   9962  N   TYR B 508     231.817 182.476 272.823  1.00159.63           N  
ATOM   9963  CA  TYR B 508     231.495 182.397 271.420  1.00168.00           C  
ATOM   9964  C   TYR B 508     232.379 183.315 270.629  1.00155.22           C  
ATOM   9965  O   TYR B 508     232.615 184.466 271.006  1.00158.16           O  
ATOM   9966  CB  TYR B 508     230.022 182.726 271.174  1.00160.45           C  
ATOM   9967  N   ARG B 509     232.839 182.808 269.508  1.00154.71           N  
ATOM   9968  CA  ARG B 509     233.636 183.586 268.597  1.00155.68           C  
ATOM   9969  C   ARG B 509     232.699 184.231 267.610  1.00154.19           C  
ATOM   9970  O   ARG B 509     231.918 183.561 266.933  1.00147.83           O  
ATOM   9971  CB  ARG B 509     234.676 182.720 267.925  1.00152.45           C  
ATOM   9972  N   VAL B 510     232.709 185.549 267.601  1.00148.03           N  
ATOM   9973  CA  VAL B 510     231.782 186.295 266.788  1.00151.30           C  
ATOM   9974  C   VAL B 510     232.511 187.158 265.788  1.00145.62           C  
ATOM   9975  O   VAL B 510     233.440 187.893 266.132  1.00150.07           O  
ATOM   9976  CB  VAL B 510     230.895 187.184 267.672  1.00152.89           C  
ATOM   9977  N   VAL B 511     232.102 187.044 264.541  1.00150.95           N  
ATOM   9978  CA  VAL B 511     232.660 187.870 263.496  1.00148.19           C  
ATOM   9979  C   VAL B 511     231.553 188.626 262.801  1.00145.26           C  
ATOM   9980  O   VAL B 511     230.599 188.032 262.295  1.00152.42           O  
ATOM   9981  CB  VAL B 511     233.421 187.027 262.470  1.00147.76           C  
ATOM   9982  N   VAL B 512     231.687 189.935 262.758  1.00145.26           N  
ATOM   9983  CA  VAL B 512     230.701 190.743 262.080  1.00146.60           C  
ATOM   9984  C   VAL B 512     231.301 191.319 260.819  1.00135.65           C  
ATOM   9985  O   VAL B 512     232.307 192.023 260.867  1.00149.42           O  
ATOM   9986  CB  VAL B 512     230.215 191.869 262.993  1.00146.17           C  
ATOM   9987  N   LEU B 513     230.687 191.014 259.689  1.00143.10           N  
ATOM   9988  CA  LEU B 513     231.173 191.509 258.419  1.00144.38           C  
ATOM   9989  C   LEU B 513     230.333 192.703 258.005  1.00132.12           C  
ATOM   9990  O   LEU B 513     229.181 192.553 257.597  1.00149.31           O  
ATOM   9991  CB  LEU B 513     231.109 190.408 257.350  1.00140.62           C  
ATOM   9992  N   SER B 514     230.905 193.892 258.157  1.00141.89           N  
ATOM   9993  CA  SER B 514     230.215 195.140 257.858  1.00137.57           C  
ATOM   9994  C   SER B 514     230.437 195.487 256.393  1.00137.30           C  
ATOM   9995  O   SER B 514     231.571 195.420 255.913  1.00135.99           O  
ATOM   9996  CB  SER B 514     230.722 196.258 258.744  1.00140.49           C  
ATOM   9997  N   PHE B 515     229.357 195.834 255.680  1.00139.61           N  
ATOM   9998  CA  PHE B 515     229.385 196.117 254.242  1.00136.70           C  
ATOM   9999  C   PHE B 515     229.247 197.617 254.001  1.00136.26           C  
ATOM  10000  O   PHE B 515     229.162 198.077 252.858  1.00135.11           O  
ATOM  10001  CB  PHE B 515     228.242 195.343 253.543  1.00137.65           C  
ATOM  10002  N   ALA B 522     233.759 199.264 243.361  1.00115.67           N  
ATOM  10003  CA  ALA B 522     233.718 198.379 244.515  1.00122.38           C  
ATOM  10004  C   ALA B 522     234.751 197.263 244.341  1.00121.35           C  
ATOM  10005  O   ALA B 522     234.948 196.778 243.220  1.00121.68           O  
ATOM  10006  CB  ALA B 522     232.309 197.798 244.693  1.00124.66           C  
ATOM  10007  N   THR B 523     235.428 196.868 245.446  1.00121.17           N  
ATOM  10008  CA  THR B 523     236.502 195.866 245.400  1.00119.69           C  
ATOM  10009  C   THR B 523     236.188 194.508 246.040  1.00119.22           C  
ATOM  10010  O   THR B 523     236.975 193.574 245.867  1.00120.25           O  
ATOM  10011  CB  THR B 523     237.782 196.438 246.027  1.00117.29           C  
ATOM  10012  N   VAL B 524     235.082 194.366 246.779  1.00120.38           N  
ATOM  10013  CA  VAL B 524     234.784 193.043 247.337  1.00121.46           C  
ATOM  10014  C   VAL B 524     233.525 192.493 246.689  1.00121.56           C  
ATOM  10015  O   VAL B 524     232.417 192.814 247.127  1.00124.82           O  
ATOM  10016  CB  VAL B 524     234.557 193.104 248.859  1.00125.11           C  
ATOM  10017  N   CYS B 525     233.688 191.654 245.654  1.00123.02           N  
ATOM  10018  CA  CYS B 525     232.563 191.143 244.862  1.00123.24           C  
ATOM  10019  C   CYS B 525     232.451 189.641 245.053  1.00121.87           C  
ATOM  10020  O   CYS B 525     233.464 188.975 245.256  1.00119.94           O  
ATOM  10021  CB  CYS B 525     232.734 191.475 243.358  1.00125.05           C  
ATOM  10022  SG  CYS B 525     232.784 193.274 242.923  1.00126.06           S  
ATOM  10023  N   GLY B 526     231.230 189.093 244.948  1.00122.29           N  
ATOM  10024  CA  GLY B 526     231.020 187.647 245.014  1.00120.76           C  
ATOM  10025  C   GLY B 526     231.592 186.961 243.768  1.00116.67           C  
ATOM  10026  O   GLY B 526     231.838 187.617 242.754  1.00113.50           O  
ATOM  10027  N   PRO B 527     231.813 185.649 243.836  1.00116.58           N  
ATOM  10028  CA  PRO B 527     232.326 184.792 242.795  1.00110.76           C  
ATOM  10029  C   PRO B 527     231.319 184.562 241.688  1.00106.56           C  
ATOM  10030  O   PRO B 527     230.116 184.533 241.938  1.00108.19           O  
ATOM  10031  CB  PRO B 527     232.593 183.491 243.562  1.00113.56           C  
ATOM  10032  CG  PRO B 527     231.610 183.520 244.684  1.00120.77           C  
ATOM  10033  CD  PRO B 527     231.537 184.966 245.075  1.00119.79           C  
ATOM  10034  N   LYS B 528     231.821 184.317 240.484  1.00102.69           N  
ATOM  10035  CA  LYS B 528     230.970 183.958 239.363  1.00 96.93           C  
ATOM  10036  C   LYS B 528     231.371 182.591 238.848  1.00 92.57           C  
ATOM  10037  O   LYS B 528     232.499 182.394 238.397  1.00 88.86           O  
ATOM  10038  CB  LYS B 528     231.095 184.984 238.237  1.00 91.74           C  
ATOM  10039  N   LYS B 529     230.448 181.643 238.918  1.00 89.00           N  
ATOM  10040  CA  LYS B 529     230.735 180.283 238.493  1.00 83.91           C  
ATOM  10041  C   LYS B 529     230.518 180.142 236.998  1.00 81.80           C  
ATOM  10042  O   LYS B 529     229.484 180.555 236.473  1.00 80.58           O  
ATOM  10043  CB  LYS B 529     229.861 179.286 239.261  1.00 85.06           C  
ATOM  10044  N   SER B 530     231.497 179.564 236.320  1.00 80.58           N  
ATOM  10045  CA  SER B 530     231.418 179.357 234.885  1.00 76.37           C  
ATOM  10046  C   SER B 530     230.872 177.981 234.543  1.00 75.78           C  
ATOM  10047  O   SER B 530     230.899 177.062 235.363  1.00 76.44           O  
ATOM  10048  CB  SER B 530     232.786 179.526 234.270  1.00 75.11           C  
ATOM  10049  OG  SER B 530     233.251 180.829 234.456  1.00 75.29           O  
ATOM  10050  N   THR B 531     230.407 177.846 233.312  1.00 73.33           N  
ATOM  10051  CA  THR B 531     229.910 176.592 232.768  1.00 71.84           C  
ATOM  10052  C   THR B 531     230.861 176.102 231.693  1.00 71.88           C  
ATOM  10053  O   THR B 531     231.807 176.801 231.326  1.00 71.20           O  
ATOM  10054  CB  THR B 531     228.511 176.759 232.156  1.00 70.76           C  
ATOM  10055  OG1 THR B 531     228.606 177.534 230.953  1.00 69.94           O  
ATOM  10056  CG2 THR B 531     227.605 177.481 233.142  1.00 72.19           C  
ATOM  10057  N   ASN B 532     230.618 174.902 231.187  1.00 70.70           N  
ATOM  10058  CA  ASN B 532     231.439 174.369 230.113  1.00 69.52           C  
ATOM  10059  C   ASN B 532     231.097 175.078 228.815  1.00 68.54           C  
ATOM  10060  O   ASN B 532     230.007 175.634 228.673  1.00 68.27           O  
ATOM  10061  CB  ASN B 532     231.265 172.869 229.978  1.00 69.17           C  
ATOM  10062  CG  ASN B 532     232.366 172.231 229.162  1.00 69.64           C  
ATOM  10063  OD1 ASN B 532     233.331 172.901 228.765  1.00 69.13           O  
ATOM  10064  ND2 ASN B 532     232.237 170.957 228.902  1.00 68.80           N  
ATOM  10065  N   LEU B 533     232.032 175.074 227.877  1.00 68.32           N  
ATOM  10066  CA  LEU B 533     231.801 175.728 226.599  1.00 67.30           C  
ATOM  10067  C   LEU B 533     231.588 174.712 225.494  1.00 66.47           C  
ATOM  10068  O   LEU B 533     232.416 173.831 225.265  1.00 66.00           O  
ATOM  10069  CB  LEU B 533     232.978 176.651 226.258  1.00 67.76           C  
ATOM  10070  CG  LEU B 533     232.784 177.614 225.060  1.00 66.56           C  
ATOM  10071  CD1 LEU B 533     233.580 178.861 225.324  1.00 67.54           C  
ATOM  10072  CD2 LEU B 533     233.253 176.974 223.764  1.00 64.76           C  
ATOM  10073  N   VAL B 534     230.476 174.859 224.794  1.00 65.07           N  
ATOM  10074  CA  VAL B 534     230.119 173.982 223.699  1.00 64.27           C  
ATOM  10075  C   VAL B 534     230.242 174.703 222.371  1.00 64.40           C  
ATOM  10076  O   VAL B 534     229.633 175.748 222.163  1.00 62.75           O  
ATOM  10077  CB  VAL B 534     228.687 173.468 223.893  1.00 64.31           C  
ATOM  10078  CG1 VAL B 534     228.283 172.577 222.743  1.00 63.14           C  
ATOM  10079  CG2 VAL B 534     228.616 172.722 225.210  1.00 64.47           C  
ATOM  10080  N   LYS B 535     231.050 174.149 221.484  1.00 63.24           N  
ATOM  10081  CA  LYS B 535     231.318 174.769 220.195  1.00 61.64           C  
ATOM  10082  C   LYS B 535     230.433 174.235 219.078  1.00 61.31           C  
ATOM  10083  O   LYS B 535     229.892 173.132 219.163  1.00 61.57           O  
ATOM  10084  CB  LYS B 535     232.784 174.574 219.818  1.00 61.80           C  
ATOM  10085  CG  LYS B 535     233.752 175.265 220.752  1.00 63.23           C  
ATOM  10086  CD  LYS B 535     235.194 175.029 220.351  1.00 62.50           C  
ATOM  10087  CE  LYS B 535     236.144 175.764 221.284  1.00 62.46           C  
ATOM  10088  NZ  LYS B 535     237.572 175.562 220.904  1.00 62.08           N  
ATOM  10089  N   ASN B 536     230.336 175.032 218.017  1.00 60.64           N  
ATOM  10090  CA  ASN B 536     229.651 174.715 216.766  1.00 60.50           C  
ATOM  10091  C   ASN B 536     228.150 174.470 216.902  1.00 60.44           C  
ATOM  10092  O   ASN B 536     227.562 173.749 216.095  1.00 61.08           O  
ATOM  10093  CB  ASN B 536     230.310 173.513 216.127  1.00 60.79           C  
ATOM  10094  CG  ASN B 536     231.780 173.719 215.913  1.00 61.60           C  
ATOM  10095  OD1 ASN B 536     232.231 174.789 215.493  1.00 60.99           O  
ATOM  10096  ND2 ASN B 536     232.550 172.703 216.202  1.00 62.01           N  
ATOM  10097  N   LYS B 537     227.525 175.096 217.890  1.00 60.09           N  
ATOM  10098  CA  LYS B 537     226.085 175.007 218.092  1.00 59.63           C  
ATOM  10099  C   LYS B 537     225.543 176.383 218.450  1.00 60.72           C  
ATOM  10100  O   LYS B 537     226.288 177.207 218.981  1.00 60.75           O  
ATOM  10101  CB  LYS B 537     225.746 174.000 219.195  1.00 59.82           C  
ATOM  10102  CG  LYS B 537     226.127 172.564 218.878  1.00 60.62           C  
ATOM  10103  CD  LYS B 537     225.684 171.629 219.983  1.00 60.91           C  
ATOM  10104  CE  LYS B 537     225.964 170.165 219.650  1.00 61.59           C  
ATOM  10105  NZ  LYS B 537     227.421 169.879 219.526  1.00 60.52           N  
ATOM  10106  N   CYS B 538     224.243 176.625 218.187  1.00 59.39           N  
ATOM  10107  CA  CYS B 538     223.589 177.877 218.572  1.00 58.90           C  
ATOM  10108  C   CYS B 538     223.366 177.899 220.086  1.00 59.84           C  
ATOM  10109  O   CYS B 538     222.673 177.037 220.634  1.00 60.57           O  
ATOM  10110  CB  CYS B 538     222.245 178.034 217.838  1.00 59.36           C  
ATOM  10111  SG  CYS B 538     221.369 179.587 218.185  1.00 57.43           S  
ATOM  10112  N   VAL B 539     223.991 178.881 220.760  1.00 59.30           N  
ATOM  10113  CA  VAL B 539     223.962 179.020 222.216  1.00 59.79           C  
ATOM  10114  C   VAL B 539     223.653 180.436 222.661  1.00 60.21           C  
ATOM  10115  O   VAL B 539     223.870 181.406 221.931  1.00 59.87           O  
ATOM  10116  CB  VAL B 539     225.325 178.613 222.809  1.00 60.31           C  
ATOM  10117  CG1 VAL B 539     225.637 177.148 222.480  1.00 60.99           C  
ATOM  10118  CG2 VAL B 539     226.402 179.534 222.243  1.00 61.04           C  
ATOM  10119  N   ASN B 540     223.200 180.546 223.899  1.00 59.88           N  
ATOM  10120  CA  ASN B 540     223.007 181.831 224.550  1.00 60.74           C  
ATOM  10121  C   ASN B 540     224.225 182.065 225.430  1.00 62.25           C  
ATOM  10122  O   ASN B 540     224.408 181.378 226.435  1.00 62.96           O  
ATOM  10123  CB  ASN B 540     221.711 181.847 225.337  1.00 61.01           C  
ATOM  10124  CG  ASN B 540     221.387 183.192 225.925  1.00 61.76           C  
ATOM  10125  OD1 ASN B 540     222.267 184.025 226.166  1.00 61.37           O  
ATOM  10126  ND2 ASN B 540     220.117 183.424 226.162  1.00 61.63           N  
ATOM  10127  N   PHE B 541     225.105 182.959 225.020  1.00 61.78           N  
ATOM  10128  CA  PHE B 541     226.371 183.097 225.718  1.00 62.73           C  
ATOM  10129  C   PHE B 541     226.482 184.336 226.584  1.00 63.46           C  
ATOM  10130  O   PHE B 541     225.831 185.358 226.349  1.00 62.60           O  
ATOM  10131  CB  PHE B 541     227.537 183.087 224.739  1.00 61.26           C  
ATOM  10132  CG  PHE B 541     227.435 184.118 223.675  1.00 61.12           C  
ATOM  10133  CD1 PHE B 541     227.816 185.424 223.911  1.00 61.50           C  
ATOM  10134  CD2 PHE B 541     226.973 183.783 222.422  1.00 61.38           C  
ATOM  10135  CE1 PHE B 541     227.721 186.366 222.926  1.00 61.28           C  
ATOM  10136  CE2 PHE B 541     226.886 184.729 221.439  1.00 61.25           C  
ATOM  10137  CZ  PHE B 541     227.255 186.020 221.694  1.00 59.61           C  
ATOM  10138  N   ASN B 542     227.371 184.234 227.564  1.00 64.55           N  
ATOM  10139  CA  ASN B 542     227.742 185.313 228.464  1.00 64.41           C  
ATOM  10140  C   ASN B 542     229.245 185.303 228.710  1.00 64.91           C  
ATOM  10141  O   ASN B 542     229.755 184.454 229.440  1.00 67.09           O  
ATOM  10142  CB  ASN B 542     226.980 185.180 229.772  1.00 66.40           C  
ATOM  10143  CG  ASN B 542     227.239 186.291 230.747  1.00 67.19           C  
ATOM  10144  OD1 ASN B 542     228.216 187.030 230.628  1.00 67.01           O  
ATOM  10145  ND2 ASN B 542     226.373 186.419 231.723  1.00 67.79           N  
ATOM  10146  N   PHE B 543     229.959 186.213 228.062  1.00 64.64           N  
ATOM  10147  CA  PHE B 543     231.409 186.292 228.195  1.00 66.04           C  
ATOM  10148  C   PHE B 543     231.802 187.561 228.911  1.00 65.68           C  
ATOM  10149  O   PHE B 543     231.680 188.659 228.362  1.00 65.27           O  
ATOM  10150  CB  PHE B 543     232.119 186.256 226.842  1.00 64.23           C  
ATOM  10151  CG  PHE B 543     232.095 184.941 226.159  1.00 64.80           C  
ATOM  10152  CD1 PHE B 543     231.116 184.617 225.259  1.00 64.21           C  
ATOM  10153  CD2 PHE B 543     233.084 184.022 226.420  1.00 65.71           C  
ATOM  10154  CE1 PHE B 543     231.126 183.394 224.631  1.00 63.61           C  
ATOM  10155  CE2 PHE B 543     233.100 182.804 225.801  1.00 66.03           C  
ATOM  10156  CZ  PHE B 543     232.120 182.489 224.906  1.00 65.07           C  
ATOM  10157  N   ASN B 544     232.299 187.425 230.127  1.00 67.32           N  
ATOM  10158  CA  ASN B 544     232.649 188.600 230.902  1.00 66.47           C  
ATOM  10159  C   ASN B 544     231.466 189.567 230.968  1.00 66.26           C  
ATOM  10160  O   ASN B 544     230.475 189.298 231.644  1.00 66.51           O  
ATOM  10161  CB  ASN B 544     233.882 189.273 230.327  1.00 65.67           C  
ATOM  10162  CG  ASN B 544     235.075 188.393 230.369  1.00 66.86           C  
ATOM  10163  OD1 ASN B 544     235.168 187.492 231.202  1.00 69.20           O  
ATOM  10164  ND2 ASN B 544     236.003 188.633 229.483  1.00 64.83           N  
ATOM  10165  N   GLY B 545     231.587 190.717 230.305  1.00 65.29           N  
ATOM  10166  CA  GLY B 545     230.550 191.740 230.362  1.00 65.16           C  
ATOM  10167  C   GLY B 545     229.533 191.744 229.213  1.00 64.25           C  
ATOM  10168  O   GLY B 545     228.653 192.605 229.192  1.00 64.20           O  
ATOM  10169  N   LEU B 546     229.637 190.829 228.248  1.00 63.88           N  
ATOM  10170  CA  LEU B 546     228.673 190.858 227.144  1.00 63.16           C  
ATOM  10171  C   LEU B 546     227.884 189.572 227.011  1.00 63.39           C  
ATOM  10172  O   LEU B 546     228.368 188.484 227.325  1.00 63.35           O  
ATOM  10173  CB  LEU B 546     229.348 191.193 225.797  1.00 62.33           C  
ATOM  10174  CG  LEU B 546     230.419 190.217 225.210  1.00 61.58           C  
ATOM  10175  CD1 LEU B 546     229.767 189.074 224.414  1.00 61.85           C  
ATOM  10176  CD2 LEU B 546     231.311 191.014 224.276  1.00 59.86           C  
ATOM  10177  N   THR B 547     226.675 189.698 226.482  1.00 62.55           N  
ATOM  10178  CA  THR B 547     225.834 188.545 226.219  1.00 62.32           C  
ATOM  10179  C   THR B 547     225.270 188.598 224.812  1.00 61.12           C  
ATOM  10180  O   THR B 547     225.238 189.660 224.186  1.00 61.02           O  
ATOM  10181  CB  THR B 547     224.668 188.475 227.221  1.00 62.46           C  
ATOM  10182  OG1 THR B 547     223.809 189.611 227.035  1.00 59.14           O  
ATOM  10183  CG2 THR B 547     225.195 188.478 228.643  1.00 63.12           C  
ATOM  10184  N   GLY B 548     224.778 187.465 224.334  1.00 60.45           N  
ATOM  10185  CA  GLY B 548     224.134 187.415 223.028  1.00 60.01           C  
ATOM  10186  C   GLY B 548     223.866 185.989 222.586  1.00 60.70           C  
ATOM  10187  O   GLY B 548     224.110 185.043 223.330  1.00 60.39           O  
ATOM  10188  N   THR B 549     223.328 185.841 221.383  1.00 58.57           N  
ATOM  10189  CA  THR B 549     223.026 184.524 220.844  1.00 59.19           C  
ATOM  10190  C   THR B 549     223.784 184.323 219.548  1.00 59.19           C  
ATOM  10191  O   THR B 549     223.801 185.203 218.686  1.00 58.14           O  
ATOM  10192  CB  THR B 549     221.512 184.338 220.624  1.00 58.18           C  
ATOM  10193  OG1 THR B 549     220.835 184.481 221.875  1.00 58.32           O  
ATOM  10194  CG2 THR B 549     221.218 182.953 220.054  1.00 58.59           C  
ATOM  10195  N   GLY B 550     224.428 183.175 219.417  1.00 58.28           N  
ATOM  10196  CA  GLY B 550     225.205 182.893 218.219  1.00 58.12           C  
ATOM  10197  C   GLY B 550     225.913 181.560 218.310  1.00 57.60           C  
ATOM  10198  O   GLY B 550     225.757 180.821 219.279  1.00 59.04           O  
ATOM  10199  N   VAL B 551     226.684 181.251 217.287  1.00 56.64           N  
ATOM  10200  CA  VAL B 551     227.408 180.002 217.216  1.00 58.90           C  
ATOM  10201  C   VAL B 551     228.880 180.266 217.451  1.00 59.46           C  
ATOM  10202  O   VAL B 551     229.489 181.077 216.757  1.00 57.81           O  
ATOM  10203  CB  VAL B 551     227.205 179.360 215.836  1.00 58.21           C  
ATOM  10204  CG1 VAL B 551     227.955 178.043 215.758  1.00 58.95           C  
ATOM  10205  CG2 VAL B 551     225.716 179.169 215.585  1.00 57.53           C  
ATOM  10206  N   LEU B 552     229.450 179.595 218.438  1.00 58.93           N  
ATOM  10207  CA  LEU B 552     230.842 179.817 218.796  1.00 58.99           C  
ATOM  10208  C   LEU B 552     231.748 178.854 218.054  1.00 59.44           C  
ATOM  10209  O   LEU B 552     231.608 177.641 218.201  1.00 60.51           O  
ATOM  10210  CB  LEU B 552     231.028 179.588 220.300  1.00 59.67           C  
ATOM  10211  CG  LEU B 552     230.112 180.380 221.242  1.00 60.45           C  
ATOM  10212  CD1 LEU B 552     230.366 179.910 222.668  1.00 64.01           C  
ATOM  10213  CD2 LEU B 552     230.376 181.869 221.094  1.00 60.14           C  
ATOM  10214  N   THR B 553     232.669 179.383 217.259  1.00 58.28           N  
ATOM  10215  CA  THR B 553     233.576 178.522 216.505  1.00 59.51           C  
ATOM  10216  C   THR B 553     235.015 178.974 216.661  1.00 60.41           C  
ATOM  10217  O   THR B 553     235.284 180.144 216.916  1.00 59.60           O  
ATOM  10218  CB  THR B 553     233.234 178.519 215.007  1.00 59.48           C  
ATOM  10219  OG1 THR B 553     233.486 179.815 214.459  1.00 59.11           O  
ATOM  10220  CG2 THR B 553     231.772 178.178 214.802  1.00 60.11           C  
ATOM  10221  N   GLU B 554     235.958 178.076 216.433  1.00 59.67           N  
ATOM  10222  CA  GLU B 554     237.360 178.468 216.488  1.00 59.78           C  
ATOM  10223  C   GLU B 554     237.643 179.516 215.422  1.00 59.40           C  
ATOM  10224  O   GLU B 554     237.267 179.337 214.264  1.00 59.69           O  
ATOM  10225  CB  GLU B 554     238.251 177.243 216.297  1.00 60.01           C  
ATOM  10226  N   SER B 555     238.299 180.608 215.807  1.00 58.60           N  
ATOM  10227  CA  SER B 555     238.600 181.684 214.865  1.00 58.98           C  
ATOM  10228  C   SER B 555     240.015 181.585 214.341  1.00 59.15           C  
ATOM  10229  O   SER B 555     240.838 180.829 214.858  1.00 59.56           O  
ATOM  10230  CB  SER B 555     238.487 183.033 215.520  1.00 58.99           C  
ATOM  10231  OG  SER B 555     239.614 183.276 216.289  1.00 59.16           O  
ATOM  10232  N   ASN B 556     240.312 182.399 213.344  1.00 58.89           N  
ATOM  10233  CA  ASN B 556     241.662 182.535 212.835  1.00 58.52           C  
ATOM  10234  C   ASN B 556     242.154 183.959 213.074  1.00 57.74           C  
ATOM  10235  O   ASN B 556     243.011 184.461 212.345  1.00 58.10           O  
ATOM  10236  CB  ASN B 556     241.711 182.167 211.370  1.00 58.50           C  
ATOM  10237  CG  ASN B 556     240.852 183.061 210.544  1.00 59.00           C  
ATOM  10238  OD1 ASN B 556     239.887 183.648 211.056  1.00 58.55           O  
ATOM  10239  ND2 ASN B 556     241.168 183.180 209.282  1.00 59.60           N  
ATOM  10240  N   LYS B 557     241.583 184.615 214.085  1.00 57.79           N  
ATOM  10241  CA  LYS B 557     241.950 185.985 214.412  1.00 57.81           C  
ATOM  10242  C   LYS B 557     243.103 186.011 215.392  1.00 56.75           C  
ATOM  10243  O   LYS B 557     243.285 185.084 216.180  1.00 57.00           O  
ATOM  10244  CB  LYS B 557     240.760 186.744 214.994  1.00 57.20           C  
ATOM  10245  CG  LYS B 557     239.596 186.949 214.037  1.00 57.05           C  
ATOM  10246  CD  LYS B 557     238.489 187.756 214.704  1.00 56.82           C  
ATOM  10247  CE  LYS B 557     237.232 187.847 213.844  1.00 56.18           C  
ATOM  10248  NZ  LYS B 557     237.414 188.713 212.645  1.00 55.14           N  
ATOM  10249  N   LYS B 558     243.875 187.088 215.361  1.00 55.92           N  
ATOM  10250  CA  LYS B 558     244.992 187.231 216.280  1.00 55.80           C  
ATOM  10251  C   LYS B 558     244.828 188.443 217.175  1.00 55.39           C  
ATOM  10252  O   LYS B 558     245.259 189.540 216.828  1.00 54.17           O  
ATOM  10253  CB  LYS B 558     246.303 187.344 215.500  1.00 56.33           C  
ATOM  10254  CG  LYS B 558     246.572 186.197 214.519  1.00 56.79           C  
ATOM  10255  CD  LYS B 558     246.828 184.876 215.234  1.00 57.78           C  
ATOM  10256  CE  LYS B 558     247.172 183.774 214.243  1.00 58.02           C  
ATOM  10257  NZ  LYS B 558     247.412 182.470 214.922  1.00 58.83           N  
ATOM  10258  N   PHE B 559     244.199 188.244 218.323  1.00 55.44           N  
ATOM  10259  CA  PHE B 559     243.963 189.337 219.254  1.00 54.61           C  
ATOM  10260  C   PHE B 559     245.240 189.680 219.981  1.00 54.43           C  
ATOM  10261  O   PHE B 559     246.051 188.800 220.268  1.00 54.35           O  
ATOM  10262  CB  PHE B 559     242.916 188.983 220.307  1.00 54.88           C  
ATOM  10263  CG  PHE B 559     241.480 189.041 219.901  1.00 55.13           C  
ATOM  10264  CD1 PHE B 559     241.063 188.922 218.588  1.00 54.98           C  
ATOM  10265  CD2 PHE B 559     240.522 189.214 220.884  1.00 55.60           C  
ATOM  10266  CE1 PHE B 559     239.725 188.973 218.285  1.00 55.51           C  
ATOM  10267  CE2 PHE B 559     239.196 189.260 220.576  1.00 56.16           C  
ATOM  10268  CZ  PHE B 559     238.796 189.138 219.278  1.00 56.11           C  
ATOM  10269  N   LEU B 560     245.394 190.945 220.329  1.00 53.51           N  
ATOM  10270  CA  LEU B 560     246.528 191.354 221.126  1.00 53.54           C  
ATOM  10271  C   LEU B 560     246.284 190.854 222.550  1.00 54.07           C  
ATOM  10272  O   LEU B 560     245.132 190.634 222.923  1.00 54.12           O  
ATOM  10273  CB  LEU B 560     246.677 192.880 221.077  1.00 53.06           C  
ATOM  10274  CG  LEU B 560     246.904 193.483 219.679  1.00 52.57           C  
ATOM  10275  CD1 LEU B 560     246.920 194.994 219.788  1.00 51.24           C  
ATOM  10276  CD2 LEU B 560     248.208 192.973 219.088  1.00 52.34           C  
ATOM  10277  N   PRO B 561     247.325 190.668 223.368  1.00 53.49           N  
ATOM  10278  CA  PRO B 561     247.277 190.150 224.728  1.00 53.68           C  
ATOM  10279  C   PRO B 561     246.305 190.861 225.666  1.00 53.48           C  
ATOM  10280  O   PRO B 561     245.920 190.300 226.690  1.00 54.13           O  
ATOM  10281  CB  PRO B 561     248.717 190.361 225.201  1.00 53.46           C  
ATOM  10282  CG  PRO B 561     249.543 190.306 223.950  1.00 53.32           C  
ATOM  10283  CD  PRO B 561     248.698 190.953 222.893  1.00 53.38           C  
ATOM  10284  N   PHE B 562     245.932 192.093 225.352  1.00 53.03           N  
ATOM  10285  CA  PHE B 562     245.039 192.846 226.220  1.00 53.34           C  
ATOM  10286  C   PHE B 562     243.637 192.995 225.649  1.00 53.47           C  
ATOM  10287  O   PHE B 562     242.780 193.615 226.277  1.00 53.95           O  
ATOM  10288  CB  PHE B 562     245.611 194.231 226.467  1.00 52.97           C  
ATOM  10289  CG  PHE B 562     245.714 195.027 225.228  1.00 52.53           C  
ATOM  10290  CD1 PHE B 562     244.671 195.832 224.817  1.00 52.47           C  
ATOM  10291  CD2 PHE B 562     246.844 194.958 224.454  1.00 52.60           C  
ATOM  10292  CE1 PHE B 562     244.767 196.556 223.665  1.00 51.68           C  
ATOM  10293  CE2 PHE B 562     246.941 195.677 223.304  1.00 51.77           C  
ATOM  10294  CZ  PHE B 562     245.905 196.474 222.908  1.00 51.56           C  
ATOM  10295  N   GLN B 563     243.409 192.472 224.452  1.00 53.54           N  
ATOM  10296  CA  GLN B 563     242.112 192.613 223.808  1.00 52.96           C  
ATOM  10297  C   GLN B 563     241.209 191.447 224.171  1.00 55.43           C  
ATOM  10298  O   GLN B 563     241.617 190.285 224.122  1.00 55.57           O  
ATOM  10299  CB  GLN B 563     242.277 192.755 222.292  1.00 53.39           C  
ATOM  10300  CG  GLN B 563     242.931 194.078 221.889  1.00 52.21           C  
ATOM  10301  CD  GLN B 563     243.309 194.173 220.422  1.00 52.48           C  
ATOM  10302  OE1 GLN B 563     243.628 193.160 219.795  1.00 52.70           O  
ATOM  10303  NE2 GLN B 563     243.302 195.389 219.869  1.00 51.48           N  
ATOM  10304  N   GLN B 564     239.987 191.771 224.565  1.00 54.24           N  
ATOM  10305  CA  GLN B 564     239.032 190.768 225.002  1.00 56.31           C  
ATOM  10306  C   GLN B 564     237.935 190.506 223.996  1.00 56.76           C  
ATOM  10307  O   GLN B 564     237.393 189.403 223.935  1.00 56.67           O  
ATOM  10308  CB  GLN B 564     238.387 191.194 226.315  1.00 56.84           C  
ATOM  10309  CG  GLN B 564     239.353 191.368 227.442  1.00 56.12           C  
ATOM  10310  CD  GLN B 564     240.065 190.091 227.769  1.00 57.43           C  
ATOM  10311  OE1 GLN B 564     239.448 189.025 227.842  1.00 57.70           O  
ATOM  10312  NE2 GLN B 564     241.369 190.184 227.968  1.00 56.03           N  
ATOM  10313  N   PHE B 565     237.570 191.517 223.228  1.00 54.98           N  
ATOM  10314  CA  PHE B 565     236.448 191.349 222.318  1.00 54.85           C  
ATOM  10315  C   PHE B 565     236.852 191.825 220.952  1.00 55.37           C  
ATOM  10316  O   PHE B 565     237.696 192.698 220.848  1.00 53.35           O  
ATOM  10317  CB  PHE B 565     235.250 192.148 222.805  1.00 55.78           C  
ATOM  10318  CG  PHE B 565     234.945 191.890 224.236  1.00 57.13           C  
ATOM  10319  CD1 PHE B 565     234.583 190.638 224.687  1.00 57.58           C  
ATOM  10320  CD2 PHE B 565     235.022 192.919 225.146  1.00 57.00           C  
ATOM  10321  CE1 PHE B 565     234.308 190.417 226.018  1.00 59.09           C  
ATOM  10322  CE2 PHE B 565     234.748 192.706 226.474  1.00 57.77           C  
ATOM  10323  CZ  PHE B 565     234.391 191.454 226.910  1.00 59.67           C  
ATOM  10324  N   GLY B 566     236.257 191.273 219.915  1.00 54.40           N  
ATOM  10325  CA  GLY B 566     236.486 191.748 218.559  1.00 53.13           C  
ATOM  10326  C   GLY B 566     235.282 192.515 218.061  1.00 53.97           C  
ATOM  10327  O   GLY B 566     234.153 192.262 218.486  1.00 52.84           O  
ATOM  10328  N   ARG B 567     235.509 193.425 217.130  1.00 51.90           N  
ATOM  10329  CA  ARG B 567     234.414 194.187 216.574  1.00 50.49           C  
ATOM  10330  C   ARG B 567     234.485 194.253 215.054  1.00 51.90           C  
ATOM  10331  O   ARG B 567     235.542 194.506 214.475  1.00 51.74           O  
ATOM  10332  CB  ARG B 567     234.425 195.589 217.145  1.00 51.77           C  
ATOM  10333  CG  ARG B 567     233.160 196.371 216.979  1.00 51.04           C  
ATOM  10334  CD  ARG B 567     232.242 196.115 218.110  1.00 50.59           C  
ATOM  10335  NE  ARG B 567     232.681 196.788 219.321  1.00 50.77           N  
ATOM  10336  CZ  ARG B 567     232.162 196.579 220.545  1.00 51.29           C  
ATOM  10337  NH1 ARG B 567     231.193 195.710 220.706  1.00 51.71           N  
ATOM  10338  NH2 ARG B 567     232.624 197.255 221.581  1.00 50.64           N  
ATOM  10339  N   ASP B 568     233.330 194.072 214.433  1.00 51.92           N  
ATOM  10340  CA  ASP B 568     233.142 194.171 212.999  1.00 51.27           C  
ATOM  10341  C   ASP B 568     233.047 195.642 212.650  1.00 50.28           C  
ATOM  10342  O   ASP B 568     233.123 196.495 213.533  1.00 50.08           O  
ATOM  10343  CB  ASP B 568     231.860 193.428 212.591  1.00 51.24           C  
ATOM  10344  CG  ASP B 568     231.835 192.944 211.140  1.00 51.39           C  
ATOM  10345  OD1 ASP B 568     232.501 193.533 210.324  1.00 51.14           O  
ATOM  10346  OD2 ASP B 568     231.139 192.002 210.865  1.00 51.66           O  
ATOM  10347  N   ILE B 569     232.875 195.955 211.380  1.00 49.56           N  
ATOM  10348  CA  ILE B 569     232.916 197.342 210.964  1.00 48.88           C  
ATOM  10349  C   ILE B 569     231.771 198.161 211.553  1.00 48.10           C  
ATOM  10350  O   ILE B 569     231.995 199.235 212.103  1.00 47.58           O  
ATOM  10351  CB  ILE B 569     232.843 197.435 209.426  1.00 49.35           C  
ATOM  10352  CG1 ILE B 569     234.044 196.681 208.770  1.00 49.58           C  
ATOM  10353  CG2 ILE B 569     232.805 198.904 208.984  1.00 48.50           C  
ATOM  10354  CD1 ILE B 569     235.423 197.187 209.129  1.00 49.40           C  
ATOM  10355  N   ALA B 570     230.543 197.660 211.466  1.00 48.07           N  
ATOM  10356  CA  ALA B 570     229.405 198.429 211.964  1.00 46.14           C  
ATOM  10357  C   ALA B 570     229.092 198.135 213.428  1.00 46.63           C  
ATOM  10358  O   ALA B 570     227.984 197.713 213.761  1.00 44.91           O  
ATOM  10359  CB  ALA B 570     228.181 198.162 211.111  1.00 42.68           C  
ATOM  10360  N   ASP B 571     230.077 198.338 214.291  1.00 46.44           N  
ATOM  10361  CA  ASP B 571     229.923 198.194 215.739  1.00 47.11           C  
ATOM  10362  C   ASP B 571     229.224 196.907 216.184  1.00 47.91           C  
ATOM  10363  O   ASP B 571     228.384 196.931 217.084  1.00 47.68           O  
ATOM  10364  CB  ASP B 571     229.194 199.402 216.318  1.00 45.15           C  
ATOM  10365  CG  ASP B 571     230.001 200.692 216.154  1.00 44.93           C  
ATOM  10366  OD1 ASP B 571     231.205 200.618 216.049  1.00 45.28           O  
ATOM  10367  OD2 ASP B 571     229.409 201.748 216.144  1.00 43.48           O  
ATOM  10368  N   THR B 572     229.584 195.786 215.584  1.00 47.63           N  
ATOM  10369  CA  THR B 572     228.979 194.505 215.939  1.00 49.26           C  
ATOM  10370  C   THR B 572     230.027 193.533 216.467  1.00 52.08           C  
ATOM  10371  O   THR B 572     231.089 193.391 215.877  1.00 51.40           O  
ATOM  10372  CB  THR B 572     228.249 193.912 214.714  1.00 48.56           C  
ATOM  10373  OG1 THR B 572     227.194 194.807 214.308  1.00 46.05           O  
ATOM  10374  CG2 THR B 572     227.657 192.558 215.027  1.00 49.22           C  
ATOM  10375  N   THR B 573     229.758 192.864 217.585  1.00 51.50           N  
ATOM  10376  CA  THR B 573     230.753 191.923 218.109  1.00 53.06           C  
ATOM  10377  C   THR B 573     230.942 190.780 217.121  1.00 53.17           C  
ATOM  10378  O   THR B 573     229.972 190.133 216.731  1.00 53.23           O  
ATOM  10379  CB  THR B 573     230.323 191.354 219.478  1.00 53.34           C  
ATOM  10380  OG1 THR B 573     230.157 192.429 220.412  1.00 53.26           O  
ATOM  10381  CG2 THR B 573     231.377 190.382 220.015  1.00 54.84           C  
ATOM  10382  N   ASP B 574     232.187 190.514 216.726  1.00 53.66           N  
ATOM  10383  CA  ASP B 574     232.434 189.453 215.752  1.00 53.90           C  
ATOM  10384  C   ASP B 574     233.081 188.226 216.367  1.00 55.97           C  
ATOM  10385  O   ASP B 574     232.917 187.115 215.864  1.00 57.96           O  
ATOM  10386  CB  ASP B 574     233.310 189.958 214.612  1.00 54.76           C  
ATOM  10387  CG  ASP B 574     234.686 190.383 215.065  1.00 56.23           C  
ATOM  10388  OD1 ASP B 574     234.962 190.294 216.243  1.00 55.26           O  
ATOM  10389  OD2 ASP B 574     235.477 190.758 214.226  1.00 54.67           O  
ATOM  10390  N   ALA B 575     233.829 188.438 217.433  1.00 55.40           N  
ATOM  10391  CA  ALA B 575     234.569 187.383 218.111  1.00 56.45           C  
ATOM  10392  C   ALA B 575     234.840 187.759 219.553  1.00 57.22           C  
ATOM  10393  O   ALA B 575     234.816 188.935 219.910  1.00 58.09           O  
ATOM  10394  CB  ALA B 575     235.879 187.119 217.390  1.00 55.73           C  
ATOM  10395  N   VAL B 576     235.104 186.763 220.385  1.00 57.83           N  
ATOM  10396  CA  VAL B 576     235.489 187.013 221.767  1.00 57.83           C  
ATOM  10397  C   VAL B 576     236.684 186.181 222.207  1.00 59.00           C  
ATOM  10398  O   VAL B 576     236.924 185.091 221.687  1.00 59.27           O  
ATOM  10399  CB  VAL B 576     234.311 186.714 222.708  1.00 59.61           C  
ATOM  10400  CG1 VAL B 576     233.149 187.631 222.405  1.00 58.77           C  
ATOM  10401  CG2 VAL B 576     233.890 185.262 222.538  1.00 59.51           C  
ATOM  10402  N   ARG B 577     237.384 186.661 223.226  1.00 58.74           N  
ATOM  10403  CA  ARG B 577     238.414 185.873 223.871  1.00 59.79           C  
ATOM  10404  C   ARG B 577     237.819 185.148 225.054  1.00 63.59           C  
ATOM  10405  O   ARG B 577     237.230 185.768 225.939  1.00 64.00           O  
ATOM  10406  CB  ARG B 577     239.560 186.742 224.365  1.00 59.42           C  
ATOM  10407  CG  ARG B 577     240.685 185.962 225.040  1.00 60.38           C  
ATOM  10408  CD  ARG B 577     241.742 186.842 225.598  1.00 59.15           C  
ATOM  10409  NE  ARG B 577     242.558 187.483 224.582  1.00 57.49           N  
ATOM  10410  CZ  ARG B 577     243.603 186.894 223.953  1.00 57.30           C  
ATOM  10411  NH1 ARG B 577     243.917 185.647 224.223  1.00 60.41           N  
ATOM  10412  NH2 ARG B 577     244.311 187.572 223.072  1.00 56.06           N  
ATOM  10413  N   ASP B 578     237.968 183.836 225.088  1.00 64.39           N  
ATOM  10414  CA  ASP B 578     237.468 183.098 226.233  1.00 65.42           C  
ATOM  10415  C   ASP B 578     238.321 183.456 227.451  1.00 67.19           C  
ATOM  10416  O   ASP B 578     239.545 183.390 227.376  1.00 66.82           O  
ATOM  10417  CB  ASP B 578     237.473 181.595 226.001  1.00 65.64           C  
ATOM  10418  CG  ASP B 578     236.874 180.861 227.185  1.00 68.55           C  
ATOM  10419  OD1 ASP B 578     235.671 180.880 227.301  1.00 66.97           O  
ATOM  10420  OD2 ASP B 578     237.616 180.345 228.009  1.00 70.07           O  
ATOM  10421  N   PRO B 579     237.722 183.877 228.566  1.00 67.63           N  
ATOM  10422  CA  PRO B 579     238.394 184.331 229.760  1.00 69.38           C  
ATOM  10423  C   PRO B 579     239.191 183.264 230.515  1.00 71.11           C  
ATOM  10424  O   PRO B 579     239.999 183.621 231.371  1.00 72.10           O  
ATOM  10425  CB  PRO B 579     237.237 184.859 230.601  1.00 70.76           C  
ATOM  10426  CG  PRO B 579     236.033 184.128 230.116  1.00 70.42           C  
ATOM  10427  CD  PRO B 579     236.262 183.927 228.648  1.00 67.96           C  
ATOM  10428  N   GLN B 580     238.971 181.969 230.242  1.00 70.30           N  
ATOM  10429  CA  GLN B 580     239.735 180.951 230.963  1.00 71.32           C  
ATOM  10430  C   GLN B 580     240.773 180.313 230.057  1.00 70.25           C  
ATOM  10431  O   GLN B 580     241.915 180.083 230.456  1.00 70.47           O  
ATOM  10432  CB  GLN B 580     238.825 179.869 231.521  1.00 71.56           C  
ATOM  10433  CG  GLN B 580     237.869 180.359 232.540  1.00 72.72           C  
ATOM  10434  CD  GLN B 580     237.134 179.238 233.206  1.00 73.10           C  
ATOM  10435  OE1 GLN B 580     237.304 178.062 232.858  1.00 72.77           O  
ATOM  10436  NE2 GLN B 580     236.317 179.587 234.178  1.00 75.36           N  
ATOM  10437  N   THR B 581     240.380 180.038 228.824  1.00 67.58           N  
ATOM  10438  CA  THR B 581     241.292 179.466 227.856  1.00 66.70           C  
ATOM  10439  C   THR B 581     241.647 180.561 226.885  1.00 66.76           C  
ATOM  10440  O   THR B 581     240.768 181.179 226.295  1.00 66.32           O  
ATOM  10441  CB  THR B 581     240.663 178.275 227.116  1.00 66.52           C  
ATOM  10442  OG1 THR B 581     240.337 177.252 228.060  1.00 68.01           O  
ATOM  10443  CG2 THR B 581     241.634 177.719 226.081  1.00 65.97           C  
ATOM  10444  N   LEU B 582     242.922 180.820 226.693  1.00 65.27           N  
ATOM  10445  CA  LEU B 582     243.274 181.961 225.870  1.00 64.31           C  
ATOM  10446  C   LEU B 582     243.225 181.631 224.388  1.00 63.54           C  
ATOM  10447  O   LEU B 582     244.249 181.520 223.712  1.00 63.69           O  
ATOM  10448  CB  LEU B 582     244.644 182.486 226.288  1.00 64.39           C  
ATOM  10449  CG  LEU B 582     244.764 182.899 227.790  1.00 65.29           C  
ATOM  10450  CD1 LEU B 582     246.181 183.375 228.054  1.00 64.90           C  
ATOM  10451  CD2 LEU B 582     243.737 183.997 228.137  1.00 64.52           C  
ATOM  10452  N   GLU B 583     241.996 181.498 223.905  1.00 63.68           N  
ATOM  10453  CA  GLU B 583     241.657 181.174 222.531  1.00 62.80           C  
ATOM  10454  C   GLU B 583     240.617 182.163 222.033  1.00 62.06           C  
ATOM  10455  O   GLU B 583     239.826 182.697 222.817  1.00 62.02           O  
ATOM  10456  CB  GLU B 583     241.093 179.752 222.426  1.00 63.50           C  
ATOM  10457  N   ILE B 584     240.604 182.399 220.730  1.00 61.04           N  
ATOM  10458  CA  ILE B 584     239.638 183.326 220.164  1.00 59.97           C  
ATOM  10459  C   ILE B 584     238.552 182.598 219.404  1.00 59.31           C  
ATOM  10460  O   ILE B 584     238.833 181.765 218.537  1.00 59.32           O  
ATOM  10461  CB  ILE B 584     240.324 184.351 219.245  1.00 59.70           C  
ATOM  10462  CG1 ILE B 584     241.477 185.055 219.991  1.00 58.02           C  
ATOM  10463  CG2 ILE B 584     239.302 185.368 218.730  1.00 58.46           C  
ATOM  10464  CD1 ILE B 584     241.082 185.743 221.280  1.00 58.94           C  
ATOM  10465  N   LEU B 585     237.312 182.916 219.749  1.00 59.18           N  
ATOM  10466  CA  LEU B 585     236.158 182.289 219.137  1.00 59.43           C  
ATOM  10467  C   LEU B 585     235.351 183.279 218.325  1.00 59.08           C  
ATOM  10468  O   LEU B 585     235.021 184.363 218.803  1.00 58.41           O  
ATOM  10469  CB  LEU B 585     235.253 181.709 220.222  1.00 59.27           C  
ATOM  10470  CG  LEU B 585     235.913 180.752 221.201  1.00 60.60           C  
ATOM  10471  CD1 LEU B 585     234.907 180.381 222.265  1.00 62.00           C  
ATOM  10472  CD2 LEU B 585     236.415 179.519 220.466  1.00 60.46           C  
ATOM  10473  N   ASP B 586     235.012 182.897 217.106  1.00 59.25           N  
ATOM  10474  CA  ASP B 586     234.161 183.718 216.263  1.00 57.88           C  
ATOM  10475  C   ASP B 586     232.725 183.515 216.664  1.00 58.73           C  
ATOM  10476  O   ASP B 586     232.337 182.413 217.053  1.00 59.43           O  
ATOM  10477  CB  ASP B 586     234.314 183.364 214.786  1.00 58.79           C  
ATOM  10478  CG  ASP B 586     235.587 183.859 214.165  1.00 58.26           C  
ATOM  10479  OD1 ASP B 586     236.177 184.770 214.686  1.00 58.30           O  
ATOM  10480  OD2 ASP B 586     235.976 183.318 213.164  1.00 60.15           O  
ATOM  10481  N   ILE B 587     231.916 184.550 216.536  1.00 57.68           N  
ATOM  10482  CA  ILE B 587     230.501 184.395 216.795  1.00 57.12           C  
ATOM  10483  C   ILE B 587     229.696 184.575 215.526  1.00 55.86           C  
ATOM  10484  O   ILE B 587     229.530 185.687 215.029  1.00 54.91           O  
ATOM  10485  CB  ILE B 587     230.021 185.398 217.849  1.00 57.60           C  
ATOM  10486  CG1 ILE B 587     230.811 185.190 219.143  1.00 57.54           C  
ATOM  10487  CG2 ILE B 587     228.520 185.204 218.085  1.00 56.96           C  
ATOM  10488  CD1 ILE B 587     230.618 186.259 220.166  1.00 58.32           C  
ATOM  10489  N   THR B 588     229.162 183.483 215.019  1.00 56.09           N  
ATOM  10490  CA  THR B 588     228.358 183.547 213.816  1.00 54.76           C  
ATOM  10491  C   THR B 588     226.901 183.614 214.246  1.00 56.08           C  
ATOM  10492  O   THR B 588     226.462 182.766 215.012  1.00 56.57           O  
ATOM  10493  CB  THR B 588     228.601 182.329 212.907  1.00 55.82           C  
ATOM  10494  OG1 THR B 588     229.972 182.305 212.501  1.00 55.62           O  
ATOM  10495  CG2 THR B 588     227.721 182.405 211.673  1.00 54.85           C  
ATOM  10496  N   PRO B 589     226.123 184.602 213.825  1.00 54.63           N  
ATOM  10497  CA  PRO B 589     224.729 184.724 214.178  1.00 53.99           C  
ATOM  10498  C   PRO B 589     224.032 183.424 213.824  1.00 53.64           C  
ATOM  10499  O   PRO B 589     224.350 182.830 212.791  1.00 52.99           O  
ATOM  10500  CB  PRO B 589     224.267 185.876 213.285  1.00 52.36           C  
ATOM  10501  CG  PRO B 589     225.519 186.700 213.067  1.00 53.17           C  
ATOM  10502  CD  PRO B 589     226.646 185.689 212.999  1.00 53.99           C  
ATOM  10503  N   CYS B 590     223.082 182.983 214.666  1.00 54.23           N  
ATOM  10504  CA  CYS B 590     222.334 181.743 214.440  1.00 52.86           C  
ATOM  10505  C   CYS B 590     221.474 181.927 213.188  1.00 50.61           C  
ATOM  10506  O   CYS B 590     220.894 182.998 212.986  1.00 49.85           O  
ATOM  10507  CB  CYS B 590     221.469 181.378 215.667  1.00 54.46           C  
ATOM  10508  SG  CYS B 590     222.437 180.957 217.146  1.00 54.91           S  
ATOM  10509  N   SER B 591     221.418 180.890 212.334  1.00 50.26           N  
ATOM  10510  CA  SER B 591     220.744 180.954 211.034  1.00 48.86           C  
ATOM  10511  C   SER B 591     219.319 181.469 211.097  1.00 47.18           C  
ATOM  10512  O   SER B 591     218.513 181.038 211.926  1.00 47.92           O  
ATOM  10513  CB  SER B 591     220.727 179.590 210.393  1.00 48.19           C  
ATOM  10514  OG  SER B 591     219.976 179.620 209.223  1.00 47.03           O  
ATOM  10515  N   PHE B 592     219.021 182.412 210.217  1.00 46.66           N  
ATOM  10516  CA  PHE B 592     217.699 182.988 210.163  1.00 45.24           C  
ATOM  10517  C   PHE B 592     217.428 183.517 208.774  1.00 44.23           C  
ATOM  10518  O   PHE B 592     218.355 183.744 207.996  1.00 44.16           O  
ATOM  10519  CB  PHE B 592     217.559 184.141 211.160  1.00 44.85           C  
ATOM  10520  CG  PHE B 592     218.305 185.382 210.758  1.00 44.50           C  
ATOM  10521  CD1 PHE B 592     217.655 186.394 210.064  1.00 43.09           C  
ATOM  10522  CD2 PHE B 592     219.644 185.543 211.053  1.00 44.88           C  
ATOM  10523  CE1 PHE B 592     218.325 187.532 209.679  1.00 41.79           C  
ATOM  10524  CE2 PHE B 592     220.319 186.684 210.668  1.00 43.92           C  
ATOM  10525  CZ  PHE B 592     219.657 187.679 209.979  1.00 41.43           C  
ATOM  10526  N   GLY B 593     216.164 183.759 208.485  1.00 43.83           N  
ATOM  10527  CA  GLY B 593     215.782 184.379 207.227  1.00 42.77           C  
ATOM  10528  C   GLY B 593     214.279 184.373 207.056  1.00 42.08           C  
ATOM  10529  O   GLY B 593     213.560 183.709 207.802  1.00 42.85           O  
ATOM  10530  N   GLY B 594     213.799 185.105 206.068  1.00 41.57           N  
ATOM  10531  CA  GLY B 594     212.370 185.158 205.825  1.00 40.93           C  
ATOM  10532  C   GLY B 594     211.882 183.822 205.305  1.00 41.05           C  
ATOM  10533  O   GLY B 594     212.627 183.079 204.664  1.00 40.74           O  
ATOM  10534  N   VAL B 595     210.627 183.518 205.570  1.00 40.69           N  
ATOM  10535  CA  VAL B 595     210.042 182.300 205.053  1.00 40.37           C  
ATOM  10536  C   VAL B 595     208.940 182.656 204.091  1.00 41.19           C  
ATOM  10537  O   VAL B 595     207.966 183.329 204.461  1.00 40.77           O  
ATOM  10538  CB  VAL B 595     209.493 181.426 206.179  1.00 41.10           C  
ATOM  10539  CG1 VAL B 595     208.899 180.157 205.607  1.00 40.57           C  
ATOM  10540  CG2 VAL B 595     210.597 181.118 207.125  1.00 41.86           C  
ATOM  10541  N   SER B 596     209.101 182.207 202.856  1.00 40.37           N  
ATOM  10542  CA  SER B 596     208.156 182.526 201.812  1.00 40.02           C  
ATOM  10543  C   SER B 596     207.420 181.312 201.309  1.00 39.42           C  
ATOM  10544  O   SER B 596     207.986 180.234 201.143  1.00 40.53           O  
ATOM  10545  CB  SER B 596     208.858 183.211 200.663  1.00 40.11           C  
ATOM  10546  OG  SER B 596     209.365 184.454 201.055  1.00 40.36           O  
ATOM  10547  N   VAL B 597     206.148 181.499 201.042  1.00 39.82           N  
ATOM  10548  CA  VAL B 597     205.323 180.431 200.545  1.00 39.90           C  
ATOM  10549  C   VAL B 597     205.023 180.643 199.082  1.00 40.32           C  
ATOM  10550  O   VAL B 597     204.513 181.686 198.675  1.00 41.20           O  
ATOM  10551  CB  VAL B 597     204.033 180.347 201.360  1.00 40.66           C  
ATOM  10552  CG1 VAL B 597     203.152 179.231 200.843  1.00 41.40           C  
ATOM  10553  CG2 VAL B 597     204.391 180.117 202.809  1.00 41.55           C  
ATOM  10554  N   ILE B 598     205.374 179.646 198.299  1.00 39.80           N  
ATOM  10555  CA  ILE B 598     205.212 179.654 196.865  1.00 39.71           C  
ATOM  10556  C   ILE B 598     203.969 178.898 196.520  1.00 39.53           C  
ATOM  10557  O   ILE B 598     203.869 177.693 196.755  1.00 40.88           O  
ATOM  10558  CB  ILE B 598     206.429 179.000 196.225  1.00 39.45           C  
ATOM  10559  CG1 ILE B 598     207.641 179.819 196.586  1.00 38.98           C  
ATOM  10560  CG2 ILE B 598     206.249 178.860 194.729  1.00 39.34           C  
ATOM  10561  CD1 ILE B 598     208.926 179.134 196.356  1.00 39.38           C  
ATOM  10562  N   THR B 599     202.993 179.596 195.984  1.00 40.45           N  
ATOM  10563  CA  THR B 599     201.719 178.951 195.804  1.00 40.49           C  
ATOM  10564  C   THR B 599     201.036 179.307 194.486  1.00 41.11           C  
ATOM  10565  O   THR B 599     201.097 180.453 194.040  1.00 42.22           O  
ATOM  10566  CB  THR B 599     200.828 179.335 197.000  1.00 40.97           C  
ATOM  10567  OG1 THR B 599     199.571 178.689 196.906  1.00 41.55           O  
ATOM  10568  CG2 THR B 599     200.613 180.824 197.052  1.00 41.15           C  
ATOM  10569  N   PRO B 600     200.395 178.337 193.827  1.00 41.34           N  
ATOM  10570  CA  PRO B 600     199.496 178.525 192.722  1.00 41.77           C  
ATOM  10571  C   PRO B 600     198.246 179.083 193.342  1.00 41.95           C  
ATOM  10572  O   PRO B 600     198.056 178.943 194.545  1.00 42.39           O  
ATOM  10573  CB  PRO B 600     199.335 177.116 192.160  1.00 41.91           C  
ATOM  10574  CG  PRO B 600     199.548 176.221 193.349  1.00 41.48           C  
ATOM  10575  CD  PRO B 600     200.578 176.931 194.206  1.00 41.20           C  
ATOM  10576  N   GLY B 601     197.375 179.685 192.573  1.00 42.62           N  
ATOM  10577  CA  GLY B 601     196.201 180.226 193.230  1.00 43.12           C  
ATOM  10578  C   GLY B 601     195.396 179.103 193.868  1.00 44.04           C  
ATOM  10579  O   GLY B 601     195.299 178.004 193.307  1.00 44.17           O  
ATOM  10580  N   THR B 602     194.742 179.413 194.990  1.00 43.90           N  
ATOM  10581  CA  THR B 602     193.906 178.437 195.705  1.00 44.00           C  
ATOM  10582  C   THR B 602     192.654 178.003 194.918  1.00 44.53           C  
ATOM  10583  O   THR B 602     191.968 177.061 195.310  1.00 43.91           O  
ATOM  10584  CB  THR B 602     193.513 178.968 197.097  1.00 44.01           C  
ATOM  10585  OG1 THR B 602     192.850 180.233 196.972  1.00 44.62           O  
ATOM  10586  CG2 THR B 602     194.753 179.126 197.936  1.00 44.06           C  
ATOM  10587  N   ASN B 603     192.392 178.667 193.777  1.00 44.70           N  
ATOM  10588  CA  ASN B 603     191.358 178.296 192.816  1.00 45.45           C  
ATOM  10589  C   ASN B 603     191.723 176.993 192.084  1.00 45.72           C  
ATOM  10590  O   ASN B 603     190.838 176.300 191.569  1.00 45.25           O  
ATOM  10591  CB  ASN B 603     191.138 179.441 191.806  1.00 46.60           C  
ATOM  10592  CG  ASN B 603     189.721 180.016 191.830  1.00 47.09           C  
ATOM  10593  OD1 ASN B 603     189.466 181.023 192.507  1.00 48.59           O  
ATOM  10594  ND2 ASN B 603     188.820 179.394 191.092  1.00 48.56           N  
ATOM  10595  N   THR B 604     193.034 176.657 192.019  1.00 44.08           N  
ATOM  10596  CA  THR B 604     193.573 175.478 191.339  1.00 43.98           C  
ATOM  10597  C   THR B 604     194.103 174.443 192.320  1.00 43.50           C  
ATOM  10598  O   THR B 604     193.883 173.244 192.145  1.00 43.40           O  
ATOM  10599  CB  THR B 604     194.723 175.872 190.388  1.00 43.60           C  
ATOM  10600  OG1 THR B 604     194.234 176.776 189.394  1.00 44.33           O  
ATOM  10601  CG2 THR B 604     195.311 174.638 189.707  1.00 43.21           C  
ATOM  10602  N   SER B 605     194.836 174.890 193.335  1.00 43.24           N  
ATOM  10603  CA  SER B 605     195.442 173.941 194.260  1.00 42.85           C  
ATOM  10604  C   SER B 605     195.773 174.536 195.620  1.00 42.22           C  
ATOM  10605  O   SER B 605     196.156 175.697 195.728  1.00 43.02           O  
ATOM  10606  CB  SER B 605     196.700 173.367 193.658  1.00 41.96           C  
ATOM  10607  OG  SER B 605     197.299 172.468 194.539  1.00 41.85           O  
ATOM  10608  N   ASN B 606     195.671 173.711 196.657  1.00 41.67           N  
ATOM  10609  CA  ASN B 606     196.055 174.119 198.004  1.00 41.52           C  
ATOM  10610  C   ASN B 606     197.427 173.579 198.381  1.00 41.34           C  
ATOM  10611  O   ASN B 606     197.803 173.571 199.553  1.00 41.57           O  
ATOM  10612  CB  ASN B 606     195.019 173.687 199.013  1.00 41.63           C  
ATOM  10613  CG  ASN B 606     193.745 174.447 198.867  1.00 42.38           C  
ATOM  10614  OD1 ASN B 606     193.748 175.640 198.542  1.00 42.84           O  
ATOM  10615  ND2 ASN B 606     192.645 173.783 199.098  1.00 41.70           N  
ATOM  10616  N   GLU B 607     198.159 173.100 197.388  1.00 41.07           N  
ATOM  10617  CA  GLU B 607     199.508 172.605 197.594  1.00 40.76           C  
ATOM  10618  C   GLU B 607     200.477 173.766 197.539  1.00 40.52           C  
ATOM  10619  O   GLU B 607     200.360 174.630 196.674  1.00 41.04           O  
ATOM  10620  CB  GLU B 607     199.857 171.574 196.534  1.00 40.81           C  
ATOM  10621  CG  GLU B 607     201.202 170.915 196.701  1.00 40.63           C  
ATOM  10622  CD  GLU B 607     201.419 169.877 195.667  1.00 41.09           C  
ATOM  10623  OE1 GLU B 607     200.517 169.660 194.898  1.00 41.20           O  
ATOM  10624  OE2 GLU B 607     202.476 169.297 195.631  1.00 41.06           O  
ATOM  10625  N   VAL B 608     201.422 173.811 198.466  1.00 40.20           N  
ATOM  10626  CA  VAL B 608     202.405 174.882 198.442  1.00 40.27           C  
ATOM  10627  C   VAL B 608     203.819 174.367 198.620  1.00 40.09           C  
ATOM  10628  O   VAL B 608     204.030 173.287 199.167  1.00 40.51           O  
ATOM  10629  CB  VAL B 608     202.107 175.913 199.534  1.00 40.34           C  
ATOM  10630  CG1 VAL B 608     200.741 176.482 199.330  1.00 41.58           C  
ATOM  10631  CG2 VAL B 608     202.208 175.294 200.900  1.00 41.33           C  
ATOM  10632  N   ALA B 609     204.786 175.177 198.216  1.00 39.94           N  
ATOM  10633  CA  ALA B 609     206.193 174.900 198.472  1.00 39.85           C  
ATOM  10634  C   ALA B 609     206.737 175.999 199.363  1.00 39.42           C  
ATOM  10635  O   ALA B 609     206.282 177.137 199.292  1.00 40.96           O  
ATOM  10636  CB  ALA B 609     206.977 174.810 197.178  1.00 39.94           C  
ATOM  10637  N   VAL B 610     207.701 175.680 200.209  1.00 39.84           N  
ATOM  10638  CA  VAL B 610     208.220 176.704 201.103  1.00 39.90           C  
ATOM  10639  C   VAL B 610     209.689 176.989 200.907  1.00 39.35           C  
ATOM  10640  O   VAL B 610     210.526 176.089 200.884  1.00 40.28           O  
ATOM  10641  CB  VAL B 610     207.970 176.323 202.565  1.00 40.19           C  
ATOM  10642  CG1 VAL B 610     208.548 177.386 203.494  1.00 40.70           C  
ATOM  10643  CG2 VAL B 610     206.489 176.195 202.789  1.00 41.09           C  
ATOM  10644  N   LEU B 611     209.991 178.262 200.762  1.00 39.68           N  
ATOM  10645  CA  LEU B 611     211.346 178.731 200.598  1.00 39.48           C  
ATOM  10646  C   LEU B 611     211.881 179.358 201.867  1.00 42.67           C  
ATOM  10647  O   LEU B 611     211.346 180.353 202.357  1.00 38.74           O  
ATOM  10648  CB  LEU B 611     211.392 179.780 199.496  1.00 39.51           C  
ATOM  10649  CG  LEU B 611     212.735 180.472 199.262  1.00 39.49           C  
ATOM  10650  CD1 LEU B 611     213.750 179.481 198.683  1.00 39.78           C  
ATOM  10651  CD2 LEU B 611     212.499 181.634 198.365  1.00 38.96           C  
ATOM  10652  N   TYR B 612     212.969 178.817 202.371  1.00 39.76           N  
ATOM  10653  CA  TYR B 612     213.616 179.409 203.521  1.00 39.93           C  
ATOM  10654  C   TYR B 612     214.748 180.254 202.993  1.00 41.97           C  
ATOM  10655  O   TYR B 612     215.712 179.733 202.429  1.00 39.00           O  
ATOM  10656  CB  TYR B 612     214.091 178.331 204.476  1.00 40.54           C  
ATOM  10657  CG  TYR B 612     212.971 177.609 205.128  1.00 40.86           C  
ATOM  10658  CD1 TYR B 612     212.328 176.583 204.481  1.00 40.80           C  
ATOM  10659  CD2 TYR B 612     212.586 177.980 206.385  1.00 41.77           C  
ATOM  10660  CE1 TYR B 612     211.288 175.938 205.101  1.00 40.82           C  
ATOM  10661  CE2 TYR B 612     211.554 177.337 207.006  1.00 41.78           C  
ATOM  10662  CZ  TYR B 612     210.904 176.320 206.368  1.00 41.10           C  
ATOM  10663  OH  TYR B 612     209.864 175.675 206.987  1.00 41.37           O  
ATOM  10664  N   GLN B 613     214.611 181.563 203.124  1.00 39.99           N  
ATOM  10665  CA  GLN B 613     215.531 182.476 202.475  1.00 40.40           C  
ATOM  10666  C   GLN B 613     216.908 182.479 203.101  1.00 40.71           C  
ATOM  10667  O   GLN B 613     217.050 182.571 204.314  1.00 41.60           O  
ATOM  10668  CB  GLN B 613     214.980 183.895 202.545  1.00 40.44           C  
ATOM  10669  CG  GLN B 613     213.696 184.136 201.782  1.00 40.36           C  
ATOM  10670  CD  GLN B 613     213.143 185.502 202.124  1.00 40.39           C  
ATOM  10671  OE1 GLN B 613     213.896 186.357 202.600  1.00 39.68           O  
ATOM  10672  NE2 GLN B 613     211.852 185.722 201.916  1.00 40.36           N  
ATOM  10673  N   ASP B 614     217.920 182.431 202.252  1.00 40.76           N  
ATOM  10674  CA  ASP B 614     219.317 182.562 202.659  1.00 41.04           C  
ATOM  10675  C   ASP B 614     219.736 181.622 203.790  1.00 41.25           C  
ATOM  10676  O   ASP B 614     220.479 182.014 204.688  1.00 41.43           O  
ATOM  10677  CB  ASP B 614     219.608 184.009 203.070  1.00 41.17           C  
ATOM  10678  CG  ASP B 614     221.106 184.366 203.025  1.00 41.30           C  
ATOM  10679  OD1 ASP B 614     221.818 183.745 202.265  1.00 41.12           O  
ATOM  10680  OD2 ASP B 614     221.516 185.266 203.730  1.00 39.73           O  
ATOM  10681  N   VAL B 615     219.284 180.380 203.741  1.00 41.21           N  
ATOM  10682  CA  VAL B 615     219.704 179.375 204.706  1.00 41.59           C  
ATOM  10683  C   VAL B 615     220.087 178.112 203.948  1.00 41.24           C  
ATOM  10684  O   VAL B 615     219.729 177.970 202.776  1.00 42.34           O  
ATOM  10685  CB  VAL B 615     218.607 179.049 205.747  1.00 42.15           C  
ATOM  10686  CG1 VAL B 615     218.228 180.288 206.547  1.00 42.78           C  
ATOM  10687  CG2 VAL B 615     217.418 178.487 205.060  1.00 41.60           C  
ATOM  10688  N   ASN B 616     220.787 177.204 204.641  1.00 42.13           N  
ATOM  10689  CA  ASN B 616     221.134 175.882 204.112  1.00 42.08           C  
ATOM  10690  C   ASN B 616     219.972 174.918 204.327  1.00 41.88           C  
ATOM  10691  O   ASN B 616     218.956 175.277 204.933  1.00 42.70           O  
ATOM  10692  CB  ASN B 616     222.419 175.368 204.789  1.00 42.37           C  
ATOM  10693  CG  ASN B 616     223.399 174.731 203.809  1.00 43.60           C  
ATOM  10694  OD1 ASN B 616     223.009 173.823 203.054  1.00 43.15           O  
ATOM  10695  ND2 ASN B 616     224.647 175.201 203.828  1.00 42.71           N  
ATOM  10696  N   CYS B 617     220.124 173.669 203.866  1.00 41.86           N  
ATOM  10697  CA  CYS B 617     219.107 172.627 204.022  1.00 43.27           C  
ATOM  10698  C   CYS B 617     219.430 171.653 205.165  1.00 43.01           C  
ATOM  10699  O   CYS B 617     218.900 170.540 205.210  1.00 42.96           O  
ATOM  10700  CB  CYS B 617     218.901 171.859 202.704  1.00 43.14           C  
ATOM  10701  SG  CYS B 617     218.145 172.840 201.364  1.00 42.47           S  
ATOM  10702  N   THR B 618     220.272 172.087 206.127  1.00 43.35           N  
ATOM  10703  CA  THR B 618     220.620 171.331 207.333  1.00 43.29           C  
ATOM  10704  C   THR B 618     219.920 171.916 208.557  1.00 43.39           C  
ATOM  10705  O   THR B 618     219.392 171.181 209.390  1.00 43.26           O  
ATOM  10706  CB  THR B 618     222.143 171.328 207.559  1.00 43.37           C  
ATOM  10707  OG1 THR B 618     222.784 170.677 206.462  1.00 43.13           O  
ATOM  10708  CG2 THR B 618     222.495 170.602 208.843  1.00 44.38           C  
ATOM  10709  N   GLU B 619     219.906 173.239 208.653  1.00 43.33           N  
ATOM  10710  CA  GLU B 619     219.298 173.949 209.778  1.00 43.72           C  
ATOM  10711  C   GLU B 619     217.771 173.822 209.851  1.00 43.73           C  
ATOM  10712  O   GLU B 619     217.209 173.783 210.947  1.00 44.62           O  
ATOM  10713  CB  GLU B 619     219.690 175.427 209.727  1.00 44.32           C  
ATOM  10714  CG  GLU B 619     221.169 175.681 209.995  1.00 44.66           C  
ATOM  10715  CD  GLU B 619     222.043 175.401 208.807  1.00 43.87           C  
ATOM  10716  OE1 GLU B 619     221.515 175.106 207.760  1.00 43.66           O  
ATOM  10717  OE2 GLU B 619     223.238 175.474 208.941  1.00 44.33           O  
ATOM  10718  N   VAL B 620     217.104 173.783 208.686  1.00 43.62           N  
ATOM  10719  CA  VAL B 620     215.648 173.712 208.571  1.00 43.67           C  
ATOM  10720  C   VAL B 620     215.188 172.293 208.927  1.00 42.82           C  
ATOM  10721  O   VAL B 620     214.099 172.093 209.471  1.00 42.46           O  
ATOM  10722  CB  VAL B 620     215.196 174.114 207.113  1.00 43.16           C  
ATOM  10723  CG1 VAL B 620     213.644 173.975 206.929  1.00 42.82           C  
ATOM  10724  CG2 VAL B 620     215.625 175.606 206.794  1.00 43.50           C  
ATOM  10725  N   ASN B 641     212.570 165.550 198.616  1.00 41.22           N  
ATOM  10726  CA  ASN B 641     212.007 166.560 197.723  1.00 40.23           C  
ATOM  10727  C   ASN B 641     212.454 167.973 198.168  1.00 40.04           C  
ATOM  10728  O   ASN B 641     211.625 168.872 198.378  1.00 40.04           O  
ATOM  10729  CB  ASN B 641     210.471 166.403 197.659  1.00 39.57           C  
ATOM  10730  CG  ASN B 641     209.777 167.164 196.479  1.00 40.11           C  
ATOM  10731  OD1 ASN B 641     210.373 167.377 195.412  1.00 39.97           O  
ATOM  10732  ND2 ASN B 641     208.513 167.547 196.679  1.00 40.69           N  
ATOM  10733  N   VAL B 642     213.782 168.144 198.325  1.00 39.98           N  
ATOM  10734  CA  VAL B 642     214.418 169.392 198.754  1.00 39.69           C  
ATOM  10735  C   VAL B 642     215.444 169.864 197.735  1.00 39.60           C  
ATOM  10736  O   VAL B 642     216.336 169.115 197.338  1.00 39.52           O  
ATOM  10737  CB  VAL B 642     215.096 169.201 200.116  1.00 40.35           C  
ATOM  10738  CG1 VAL B 642     215.754 170.488 200.541  1.00 40.71           C  
ATOM  10739  CG2 VAL B 642     214.061 168.756 201.131  1.00 40.30           C  
ATOM  10740  N   PHE B 643     215.311 171.113 197.318  1.00 39.51           N  
ATOM  10741  CA  PHE B 643     216.183 171.711 196.322  1.00 39.27           C  
ATOM  10742  C   PHE B 643     216.926 172.926 196.871  1.00 39.33           C  
ATOM  10743  O   PHE B 643     216.320 173.943 197.207  1.00 40.59           O  
ATOM  10744  CB  PHE B 643     215.330 172.092 195.105  1.00 38.87           C  
ATOM  10745  CG  PHE B 643     216.035 172.731 193.940  1.00 38.71           C  
ATOM  10746  CD1 PHE B 643     217.380 172.529 193.677  1.00 38.63           C  
ATOM  10747  CD2 PHE B 643     215.315 173.539 193.081  1.00 38.09           C  
ATOM  10748  CE1 PHE B 643     217.976 173.130 192.595  1.00 38.52           C  
ATOM  10749  CE2 PHE B 643     215.907 174.136 192.000  1.00 37.95           C  
ATOM  10750  CZ  PHE B 643     217.241 173.933 191.758  1.00 37.99           C  
ATOM  10751  N   GLN B 644     218.243 172.829 196.972  1.00 39.57           N  
ATOM  10752  CA  GLN B 644     219.012 173.958 197.478  1.00 39.76           C  
ATOM  10753  C   GLN B 644     219.321 174.906 196.334  1.00 39.59           C  
ATOM  10754  O   GLN B 644     219.936 174.508 195.345  1.00 39.67           O  
ATOM  10755  CB  GLN B 644     220.330 173.500 198.108  1.00 40.23           C  
ATOM  10756  CG  GLN B 644     221.218 174.642 198.667  1.00 40.51           C  
ATOM  10757  CD  GLN B 644     220.720 175.244 199.989  1.00 41.31           C  
ATOM  10758  OE1 GLN B 644     220.700 174.537 200.994  1.00 42.05           O  
ATOM  10759  NE2 GLN B 644     220.342 176.522 200.001  1.00 41.18           N  
ATOM  10760  N   THR B 645     218.921 176.161 196.479  1.00 39.66           N  
ATOM  10761  CA  THR B 645     219.173 177.172 195.469  1.00 39.64           C  
ATOM  10762  C   THR B 645     219.941 178.316 196.104  1.00 39.68           C  
ATOM  10763  O   THR B 645     219.994 178.426 197.326  1.00 40.37           O  
ATOM  10764  CB  THR B 645     217.854 177.695 194.865  1.00 39.18           C  
ATOM  10765  OG1 THR B 645     217.094 178.377 195.866  1.00 39.49           O  
ATOM  10766  CG2 THR B 645     217.033 176.540 194.348  1.00 38.79           C  
ATOM  10767  N   ARG B 646     220.512 179.200 195.298  1.00 39.54           N  
ATOM  10768  CA  ARG B 646     221.237 180.330 195.870  1.00 39.83           C  
ATOM  10769  C   ARG B 646     220.347 181.192 196.757  1.00 39.44           C  
ATOM  10770  O   ARG B 646     220.808 181.764 197.743  1.00 40.14           O  
ATOM  10771  CB  ARG B 646     221.857 181.185 194.785  1.00 39.81           C  
ATOM  10772  N   ALA B 647     219.071 181.280 196.405  1.00 39.42           N  
ATOM  10773  CA  ALA B 647     218.103 182.091 197.132  1.00 38.96           C  
ATOM  10774  C   ALA B 647     217.727 181.524 198.500  1.00 40.24           C  
ATOM  10775  O   ALA B 647     217.117 182.229 199.307  1.00 40.38           O  
ATOM  10776  CB  ALA B 647     216.842 182.241 196.296  1.00 37.63           C  
ATOM  10777  N   GLY B 648     218.030 180.258 198.758  1.00 40.19           N  
ATOM  10778  CA  GLY B 648     217.599 179.631 200.003  1.00 40.11           C  
ATOM  10779  C   GLY B 648     217.289 178.152 199.801  1.00 39.70           C  
ATOM  10780  O   GLY B 648     217.591 177.592 198.747  1.00 41.88           O  
ATOM  10781  N   CYS B 649     216.709 177.512 200.825  1.00 40.28           N  
ATOM  10782  CA  CYS B 649     216.377 176.085 200.783  1.00 40.49           C  
ATOM  10783  C   CYS B 649     214.891 175.939 200.429  1.00 39.54           C  
ATOM  10784  O   CYS B 649     214.021 176.387 201.185  1.00 41.95           O  
ATOM  10785  CB  CYS B 649     216.694 175.400 202.129  1.00 41.92           C  
ATOM  10786  SG  CYS B 649     216.407 173.605 202.140  1.00 42.45           S  
ATOM  10787  N   LEU B 650     214.603 175.341 199.261  1.00 39.53           N  
ATOM  10788  CA  LEU B 650     213.245 175.184 198.740  1.00 39.37           C  
ATOM  10789  C   LEU B 650     212.720 173.779 198.988  1.00 39.43           C  
ATOM  10790  O   LEU B 650     213.256 172.793 198.480  1.00 39.99           O  
ATOM  10791  CB  LEU B 650     213.244 175.505 197.247  1.00 39.34           C  
ATOM  10792  CG  LEU B 650     211.938 175.339 196.505  1.00 39.07           C  
ATOM  10793  CD1 LEU B 650     210.907 176.307 197.041  1.00 39.62           C  
ATOM  10794  CD2 LEU B 650     212.196 175.590 195.044  1.00 39.57           C  
ATOM  10795  N   ILE B 651     211.668 173.686 199.782  1.00 39.50           N  
ATOM  10796  CA  ILE B 651     211.130 172.398 200.173  1.00 39.61           C  
ATOM  10797  C   ILE B 651     209.723 172.161 199.644  1.00 39.74           C  
ATOM  10798  O   ILE B 651     208.818 172.967 199.855  1.00 39.84           O  
ATOM  10799  CB  ILE B 651     211.139 172.282 201.706  1.00 39.45           C  
ATOM  10800  CG1 ILE B 651     212.594 172.426 202.206  1.00 40.21           C  
ATOM  10801  CG2 ILE B 651     210.526 170.952 202.142  1.00 40.06           C  
ATOM  10802  CD1 ILE B 651     212.741 172.563 203.688  1.00 41.41           C  
ATOM  10803  N   GLY B 652     209.530 171.032 198.971  1.00 39.76           N  
ATOM  10804  CA  GLY B 652     208.216 170.662 198.450  1.00 39.73           C  
ATOM  10805  C   GLY B 652     208.093 170.814 196.938  1.00 39.94           C  
ATOM  10806  O   GLY B 652     207.197 170.233 196.327  1.00 40.30           O  
ATOM  10807  N   ALA B 653     208.988 171.573 196.330  1.00 39.65           N  
ATOM  10808  CA  ALA B 653     208.977 171.718 194.882  1.00 39.22           C  
ATOM  10809  C   ALA B 653     209.944 170.715 194.277  1.00 39.30           C  
ATOM  10810  O   ALA B 653     211.048 170.533 194.789  1.00 39.46           O  
ATOM  10811  CB  ALA B 653     209.357 173.125 194.473  1.00 39.02           C  
ATOM  10812  N   GLU B 654     209.552 170.088 193.178  1.00 39.40           N  
ATOM  10813  CA  GLU B 654     210.432 169.127 192.523  1.00 38.83           C  
ATOM  10814  C   GLU B 654     211.495 169.830 191.707  1.00 38.05           C  
ATOM  10815  O   GLU B 654     211.240 170.873 191.117  1.00 38.81           O  
ATOM  10816  CB  GLU B 654     209.644 168.198 191.603  1.00 38.82           C  
ATOM  10817  CG  GLU B 654     208.643 167.310 192.297  1.00 39.00           C  
ATOM  10818  CD  GLU B 654     207.968 166.361 191.350  1.00 39.08           C  
ATOM  10819  OE1 GLU B 654     208.212 166.459 190.170  1.00 38.12           O  
ATOM  10820  OE2 GLU B 654     207.217 165.531 191.803  1.00 38.60           O  
ATOM  10821  N   HIS B 655     212.678 169.247 191.618  1.00 37.65           N  
ATOM  10822  CA  HIS B 655     213.693 169.847 190.765  1.00 36.99           C  
ATOM  10823  C   HIS B 655     213.605 169.247 189.376  1.00 37.51           C  
ATOM  10824  O   HIS B 655     213.737 168.037 189.192  1.00 37.81           O  
ATOM  10825  CB  HIS B 655     215.099 169.667 191.334  1.00 37.85           C  
ATOM  10826  CG  HIS B 655     216.152 170.381 190.538  1.00 37.71           C  
ATOM  10827  ND1 HIS B 655     217.489 170.066 190.629  1.00 38.16           N  
ATOM  10828  CD2 HIS B 655     216.067 171.394 189.640  1.00 37.63           C  
ATOM  10829  CE1 HIS B 655     218.177 170.850 189.819  1.00 38.44           C  
ATOM  10830  NE2 HIS B 655     217.337 171.661 189.210  1.00 37.98           N  
ATOM  10831  N   VAL B 656     213.326 170.096 188.404  1.00 37.32           N  
ATOM  10832  CA  VAL B 656     213.125 169.678 187.030  1.00 36.88           C  
ATOM  10833  C   VAL B 656     214.242 170.201 186.122  1.00 37.13           C  
ATOM  10834  O   VAL B 656     214.573 171.385 186.171  1.00 37.03           O  
ATOM  10835  CB  VAL B 656     211.739 170.173 186.564  1.00 36.78           C  
ATOM  10836  CG1 VAL B 656     211.492 169.849 185.115  1.00 36.89           C  
ATOM  10837  CG2 VAL B 656     210.691 169.513 187.415  1.00 37.74           C  
ATOM  10838  N   ASN B 657     214.818 169.300 185.296  1.00 37.28           N  
ATOM  10839  CA  ASN B 657     215.903 169.612 184.357  1.00 37.26           C  
ATOM  10840  C   ASN B 657     215.445 170.521 183.203  1.00 36.66           C  
ATOM  10841  O   ASN B 657     216.235 171.315 182.692  1.00 36.45           O  
ATOM  10842  CB  ASN B 657     216.507 168.317 183.785  1.00 38.11           C  
ATOM  10843  CG  ASN B 657     217.778 167.831 184.508  1.00 38.91           C  
ATOM  10844  OD1 ASN B 657     218.445 168.588 185.231  1.00 38.94           O  
ATOM  10845  ND2 ASN B 657     218.107 166.560 184.300  1.00 39.73           N  
ATOM  10846  N   ASN B 658     214.173 170.400 182.786  1.00 36.30           N  
ATOM  10847  CA  ASN B 658     213.602 171.169 181.681  1.00 35.97           C  
ATOM  10848  C   ASN B 658     213.293 172.595 182.093  1.00 35.56           C  
ATOM  10849  O   ASN B 658     212.684 172.831 183.134  1.00 36.39           O  
ATOM  10850  CB  ASN B 658     212.349 170.495 181.190  1.00 35.89           C  
ATOM  10851  CG  ASN B 658     212.628 169.155 180.636  1.00 36.29           C  
ATOM  10852  OD1 ASN B 658     213.626 168.949 179.938  1.00 36.44           O  
ATOM  10853  ND2 ASN B 658     211.771 168.217 180.933  1.00 36.07           N  
ATOM  10854  N   SER B 659     213.710 173.545 181.270  1.00 35.49           N  
ATOM  10855  CA  SER B 659     213.429 174.945 181.520  1.00 34.84           C  
ATOM  10856  C   SER B 659     212.079 175.323 180.953  1.00 34.79           C  
ATOM  10857  O   SER B 659     211.616 174.714 179.990  1.00 35.53           O  
ATOM  10858  CB  SER B 659     214.495 175.797 180.879  1.00 34.16           C  
ATOM  10859  OG  SER B 659     214.483 175.623 179.487  1.00 35.60           O  
ATOM  10860  N   TYR B 660     211.480 176.366 181.499  1.00 34.59           N  
ATOM  10861  CA  TYR B 660     210.208 176.866 181.001  1.00 35.07           C  
ATOM  10862  C   TYR B 660     210.160 178.367 181.184  1.00 35.80           C  
ATOM  10863  O   TYR B 660     211.091 178.960 181.729  1.00 34.86           O  
ATOM  10864  CB  TYR B 660     209.037 176.237 181.763  1.00 35.88           C  
ATOM  10865  CG  TYR B 660     209.014 174.727 181.779  1.00 35.91           C  
ATOM  10866  CD1 TYR B 660     209.651 174.047 182.796  1.00 36.50           C  
ATOM  10867  CD2 TYR B 660     208.359 174.024 180.792  1.00 36.61           C  
ATOM  10868  CE1 TYR B 660     209.638 172.678 182.828  1.00 36.39           C  
ATOM  10869  CE2 TYR B 660     208.345 172.643 180.826  1.00 36.80           C  
ATOM  10870  CZ  TYR B 660     208.983 171.973 181.841  1.00 36.63           C  
ATOM  10871  OH  TYR B 660     208.968 170.597 181.876  1.00 35.91           O  
ATOM  10872  N   GLU B 661     209.088 178.989 180.731  1.00 36.22           N  
ATOM  10873  CA  GLU B 661     208.908 180.411 180.958  1.00 36.66           C  
ATOM  10874  C   GLU B 661     208.671 180.615 182.450  1.00 36.82           C  
ATOM  10875  O   GLU B 661     208.000 179.793 183.072  1.00 37.13           O  
ATOM  10876  CB  GLU B 661     207.736 180.925 180.130  1.00 37.63           C  
ATOM  10877  N   CYS B 662     209.226 181.696 183.025  1.00 36.26           N  
ATOM  10878  CA  CYS B 662     209.094 181.965 184.462  1.00 36.35           C  
ATOM  10879  C   CYS B 662     207.647 182.318 184.827  1.00 36.87           C  
ATOM  10880  O   CYS B 662     207.011 183.139 184.178  1.00 37.55           O  
ATOM  10881  CB  CYS B 662     210.022 183.121 184.876  1.00 36.97           C  
ATOM  10882  SG  CYS B 662     210.058 183.446 186.666  1.00 36.26           S  
ATOM  10883  N   ASP B 663     207.145 181.677 185.902  1.00 36.96           N  
ATOM  10884  CA  ASP B 663     205.792 181.876 186.427  1.00 37.17           C  
ATOM  10885  C   ASP B 663     205.896 182.565 187.785  1.00 37.19           C  
ATOM  10886  O   ASP B 663     205.737 183.783 187.872  1.00 37.13           O  
ATOM  10887  CB  ASP B 663     205.051 180.541 186.529  1.00 37.69           C  
ATOM  10888  CG  ASP B 663     203.565 180.703 186.805  1.00 38.44           C  
ATOM  10889  OD1 ASP B 663     203.048 181.762 186.540  1.00 38.33           O  
ATOM  10890  OD2 ASP B 663     202.950 179.769 187.264  1.00 38.69           O  
ATOM  10891  N   ILE B 664     206.208 181.812 188.840  1.00 36.91           N  
ATOM  10892  CA  ILE B 664     206.431 182.432 190.133  1.00 36.47           C  
ATOM  10893  C   ILE B 664     207.931 182.494 190.378  1.00 35.79           C  
ATOM  10894  O   ILE B 664     208.558 181.454 190.558  1.00 36.68           O  
ATOM  10895  CB  ILE B 664     205.809 181.617 191.276  1.00 37.11           C  
ATOM  10896  CG1 ILE B 664     204.311 181.431 191.051  1.00 38.26           C  
ATOM  10897  CG2 ILE B 664     206.078 182.345 192.596  1.00 37.87           C  
ATOM  10898  CD1 ILE B 664     203.678 180.416 191.993  1.00 39.46           C  
ATOM  10899  N   PRO B 665     208.550 183.667 190.391  1.00 35.26           N  
ATOM  10900  CA  PRO B 665     209.975 183.825 190.517  1.00 34.49           C  
ATOM  10901  C   PRO B 665     210.431 183.502 191.920  1.00 34.62           C  
ATOM  10902  O   PRO B 665     209.783 183.900 192.884  1.00 35.79           O  
ATOM  10903  CB  PRO B 665     210.159 185.301 190.195  1.00 34.59           C  
ATOM  10904  CG  PRO B 665     208.860 185.943 190.601  1.00 36.03           C  
ATOM  10905  CD  PRO B 665     207.797 184.904 190.325  1.00 36.07           C  
ATOM  10906  N   ILE B 666     211.582 182.857 192.032  1.00 34.42           N  
ATOM  10907  CA  ILE B 666     212.217 182.622 193.315  1.00 33.99           C  
ATOM  10908  C   ILE B 666     213.459 183.474 193.467  1.00 33.76           C  
ATOM  10909  O   ILE B 666     213.635 184.164 194.470  1.00 35.12           O  
ATOM  10910  CB  ILE B 666     212.534 181.136 193.493  1.00 34.12           C  
ATOM  10911  CG1 ILE B 666     211.213 180.381 193.578  1.00 34.79           C  
ATOM  10912  CG2 ILE B 666     213.428 180.908 194.686  1.00 35.14           C  
ATOM  10913  CD1 ILE B 666     211.351 178.905 193.568  1.00 35.85           C  
ATOM  10914  N   GLY B 667     214.317 183.432 192.463  1.00 33.11           N  
ATOM  10915  CA  GLY B 667     215.549 184.200 192.492  1.00 32.01           C  
ATOM  10916  C   GLY B 667     216.722 183.387 191.989  1.00 32.03           C  
ATOM  10917  O   GLY B 667     216.681 182.159 191.980  1.00 33.35           O  
ATOM  10918  N   ALA B 668     217.775 184.075 191.576  1.00 31.25           N  
ATOM  10919  CA  ALA B 668     218.996 183.449 191.106  1.00 31.63           C  
ATOM  10920  C   ALA B 668     218.748 182.501 189.943  1.00 32.27           C  
ATOM  10921  O   ALA B 668     219.367 181.442 189.854  1.00 33.06           O  
ATOM  10922  CB  ALA B 668     219.667 182.705 192.241  1.00 33.86           C  
ATOM  10923  N   GLY B 669     217.851 182.886 189.045  1.00 32.17           N  
ATOM  10924  CA  GLY B 669     217.575 182.116 187.848  1.00 32.31           C  
ATOM  10925  C   GLY B 669     216.524 181.037 188.035  1.00 32.94           C  
ATOM  10926  O   GLY B 669     216.149 180.377 187.066  1.00 33.92           O  
ATOM  10927  N   ILE B 670     216.053 180.846 189.259  1.00 33.06           N  
ATOM  10928  CA  ILE B 670     215.075 179.805 189.531  1.00 33.26           C  
ATOM  10929  C   ILE B 670     213.658 180.372 189.657  1.00 33.61           C  
ATOM  10930  O   ILE B 670     213.440 181.388 190.330  1.00 35.48           O  
ATOM  10931  CB  ILE B 670     215.436 179.033 190.820  1.00 33.99           C  
ATOM  10932  CG1 ILE B 670     216.873 178.463 190.737  1.00 34.48           C  
ATOM  10933  CG2 ILE B 670     214.425 177.906 191.077  1.00 35.11           C  
ATOM  10934  CD1 ILE B 670     217.127 177.493 189.597  1.00 34.92           C  
ATOM  10935  N   CYS B 671     212.706 179.708 188.987  1.00 34.11           N  
ATOM  10936  CA  CYS B 671     211.274 180.002 189.032  1.00 34.54           C  
ATOM  10937  C   CYS B 671     210.534 178.702 189.348  1.00 36.97           C  
ATOM  10938  O   CYS B 671     211.071 177.610 189.126  1.00 36.23           O  
ATOM  10939  CB  CYS B 671     210.770 180.618 187.709  1.00 35.20           C  
ATOM  10940  SG  CYS B 671     211.536 182.209 187.308  1.00 35.30           S  
ATOM  10941  N   ALA B 672     209.298 178.818 189.858  1.00 35.69           N  
ATOM  10942  CA  ALA B 672     208.438 177.677 190.172  1.00 36.79           C  
ATOM  10943  C   ALA B 672     207.073 177.818 189.532  1.00 37.01           C  
ATOM  10944  O   ALA B 672     206.606 178.920 189.241  1.00 37.66           O  
ATOM  10945  CB  ALA B 672     208.287 177.530 191.668  1.00 37.49           C  
ATOM  10946  N   SER B 673     206.437 176.680 189.302  1.00 37.97           N  
ATOM  10947  CA  SER B 673     205.104 176.651 188.713  1.00 38.55           C  
ATOM  10948  C   SER B 673     204.366 175.372 189.064  1.00 38.79           C  
ATOM  10949  O   SER B 673     204.959 174.411 189.551  1.00 39.59           O  
ATOM  10950  CB  SER B 673     205.203 176.761 187.217  1.00 38.89           C  
ATOM  10951  OG  SER B 673     205.786 175.616 186.699  1.00 39.04           O  
ATOM  10952  N   TYR B 674     203.066 175.356 188.809  1.00 39.35           N  
ATOM  10953  CA  TYR B 674     202.254 174.169 189.040  1.00 39.49           C  
ATOM  10954  C   TYR B 674     201.909 173.518 187.706  1.00 39.79           C  
ATOM  10955  O   TYR B 674     201.204 174.103 186.882  1.00 40.06           O  
ATOM  10956  CB  TYR B 674     201.009 174.571 189.826  1.00 40.05           C  
ATOM  10957  CG  TYR B 674     200.096 173.457 190.225  1.00 40.62           C  
ATOM  10958  CD1 TYR B 674     200.418 172.631 191.285  1.00 41.09           C  
ATOM  10959  CD2 TYR B 674     198.921 173.276 189.545  1.00 41.29           C  
ATOM  10960  CE1 TYR B 674     199.559 171.620 191.657  1.00 40.98           C  
ATOM  10961  CE2 TYR B 674     198.066 172.277 189.910  1.00 41.74           C  
ATOM  10962  CZ  TYR B 674     198.372 171.450 190.960  1.00 41.76           C  
ATOM  10963  OH  TYR B 674     197.500 170.437 191.303  1.00 42.07           O  
ATOM  10964  N   GLN B 675     202.458 172.328 187.474  1.00 39.69           N  
ATOM  10965  CA  GLN B 675     202.301 171.641 186.192  1.00 40.15           C  
ATOM  10966  C   GLN B 675     202.082 170.133 186.339  1.00 40.42           C  
ATOM  10967  O   GLN B 675     202.509 169.538 187.329  1.00 40.60           O  
ATOM  10968  CB  GLN B 675     203.514 171.899 185.282  1.00 39.79           C  
ATOM  10969  CG  GLN B 675     203.643 173.334 184.783  1.00 39.84           C  
ATOM  10970  CD  GLN B 675     204.763 173.504 183.749  1.00 39.37           C  
ATOM  10971  OE1 GLN B 675     205.779 174.155 183.998  1.00 38.75           O  
ATOM  10972  NE2 GLN B 675     204.569 172.908 182.575  1.00 37.75           N  
ATOM  10973  N   THR B 676     201.436 169.524 185.322  1.00 40.81           N  
ATOM  10974  CA  THR B 676     201.176 168.082 185.217  1.00 41.26           C  
ATOM  10975  C   THR B 676     202.485 167.275 185.292  1.00 41.31           C  
ATOM  10976  O   THR B 676     203.203 167.124 184.300  1.00 41.10           O  
ATOM  10977  CB  THR B 676     200.393 167.773 183.898  1.00 41.55           C  
ATOM  10978  OG1 THR B 676     199.177 168.543 183.879  1.00 40.65           O  
ATOM  10979  CG2 THR B 676     200.018 166.259 183.749  1.00 42.83           C  
ATOM  10980  N   SER B 689     198.671 163.816 189.376  1.00 42.86           N  
ATOM  10981  CA  SER B 689     199.501 164.062 188.199  1.00 43.24           C  
ATOM  10982  C   SER B 689     200.256 165.401 188.290  1.00 42.48           C  
ATOM  10983  O   SER B 689     201.406 165.487 187.852  1.00 42.33           O  
ATOM  10984  CB  SER B 689     198.643 164.013 186.935  1.00 43.22           C  
ATOM  10985  OG  SER B 689     198.113 162.739 186.733  1.00 43.61           O  
ATOM  10986  N   GLN B 690     199.595 166.441 188.831  1.00 42.29           N  
ATOM  10987  CA  GLN B 690     200.149 167.791 188.970  1.00 41.96           C  
ATOM  10988  C   GLN B 690     200.880 167.982 190.287  1.00 41.20           C  
ATOM  10989  O   GLN B 690     200.498 167.414 191.310  1.00 41.54           O  
ATOM  10990  CB  GLN B 690     199.042 168.833 188.875  1.00 41.65           C  
ATOM  10991  CG  GLN B 690     198.328 168.903 187.558  1.00 41.90           C  
ATOM  10992  CD  GLN B 690     197.178 169.878 187.612  1.00 41.71           C  
ATOM  10993  OE1 GLN B 690     196.434 169.911 188.603  1.00 42.11           O  
ATOM  10994  NE2 GLN B 690     197.022 170.686 186.568  1.00 41.00           N  
ATOM  10995  N   SER B 691     201.915 168.812 190.251  1.00 40.73           N  
ATOM  10996  CA  SER B 691     202.677 169.178 191.436  1.00 40.16           C  
ATOM  10997  C   SER B 691     203.432 170.479 191.209  1.00 40.66           C  
ATOM  10998  O   SER B 691     203.502 170.979 190.083  1.00 40.90           O  
ATOM  10999  CB  SER B 691     203.648 168.077 191.794  1.00 40.09           C  
ATOM  11000  OG  SER B 691     204.638 167.960 190.822  1.00 39.69           O  
ATOM  11001  N   ILE B 692     203.999 171.034 192.271  1.00 39.52           N  
ATOM  11002  CA  ILE B 692     204.819 172.226 192.127  1.00 39.05           C  
ATOM  11003  C   ILE B 692     206.236 171.840 191.761  1.00 39.08           C  
ATOM  11004  O   ILE B 692     206.831 170.960 192.389  1.00 39.83           O  
ATOM  11005  CB  ILE B 692     204.828 173.081 193.400  1.00 39.18           C  
ATOM  11006  CG1 ILE B 692     203.417 173.564 193.682  1.00 39.65           C  
ATOM  11007  CG2 ILE B 692     205.794 174.269 193.225  1.00 39.00           C  
ATOM  11008  CD1 ILE B 692     203.243 174.179 195.031  1.00 40.29           C  
ATOM  11009  N   ILE B 693     206.765 172.494 190.743  1.00 38.79           N  
ATOM  11010  CA  ILE B 693     208.110 172.226 190.286  1.00 38.17           C  
ATOM  11011  C   ILE B 693     208.931 173.494 190.295  1.00 38.48           C  
ATOM  11012  O   ILE B 693     208.390 174.596 190.232  1.00 38.37           O  
ATOM  11013  CB  ILE B 693     208.107 171.655 188.861  1.00 38.64           C  
ATOM  11014  CG1 ILE B 693     207.547 172.696 187.866  1.00 39.14           C  
ATOM  11015  CG2 ILE B 693     207.267 170.380 188.828  1.00 39.37           C  
ATOM  11016  CD1 ILE B 693     207.731 172.333 186.408  1.00 39.02           C  
ATOM  11017  N   ALA B 694     210.240 173.326 190.314  1.00 37.27           N  
ATOM  11018  CA  ALA B 694     211.178 174.426 190.234  1.00 37.03           C  
ATOM  11019  C   ALA B 694     212.234 174.106 189.195  1.00 36.16           C  
ATOM  11020  O   ALA B 694     212.661 172.960 189.049  1.00 38.75           O  
ATOM  11021  CB  ALA B 694     211.803 174.682 191.585  1.00 37.36           C  
ATOM  11022  N   TYR B 695     212.645 175.129 188.471  1.00 35.96           N  
ATOM  11023  CA  TYR B 695     213.561 174.970 187.356  1.00 35.13           C  
ATOM  11024  C   TYR B 695     214.311 176.241 187.041  1.00 35.79           C  
ATOM  11025  O   TYR B 695     213.902 177.331 187.445  1.00 34.23           O  
ATOM  11026  CB  TYR B 695     212.755 174.552 186.137  1.00 35.45           C  
ATOM  11027  CG  TYR B 695     211.588 175.473 185.938  1.00 34.90           C  
ATOM  11028  CD1 TYR B 695     211.710 176.651 185.236  1.00 35.70           C  
ATOM  11029  CD2 TYR B 695     210.386 175.133 186.488  1.00 36.48           C  
ATOM  11030  CE1 TYR B 695     210.625 177.482 185.100  1.00 35.37           C  
ATOM  11031  CE2 TYR B 695     209.315 175.952 186.350  1.00 37.22           C  
ATOM  11032  CZ  TYR B 695     209.426 177.119 185.668  1.00 35.61           C  
ATOM  11033  OH  TYR B 695     208.336 177.924 185.541  1.00 36.45           O  
ATOM  11034  N   THR B 696     215.391 176.117 186.284  1.00 34.50           N  
ATOM  11035  CA  THR B 696     216.065 177.304 185.797  1.00 33.91           C  
ATOM  11036  C   THR B 696     215.226 177.846 184.666  1.00 33.43           C  
ATOM  11037  O   THR B 696     214.843 177.102 183.766  1.00 34.49           O  
ATOM  11038  CB  THR B 696     217.490 177.000 185.321  1.00 33.76           C  
ATOM  11039  OG1 THR B 696     218.244 176.447 186.404  1.00 34.05           O  
ATOM  11040  CG2 THR B 696     218.170 178.261 184.837  1.00 33.65           C  
ATOM  11041  N   MET B 697     214.905 179.124 184.718  1.00 33.15           N  
ATOM  11042  CA  MET B 697     214.012 179.678 183.715  1.00 32.54           C  
ATOM  11043  C   MET B 697     214.667 179.783 182.359  1.00 32.37           C  
ATOM  11044  O   MET B 697     215.864 180.049 182.252  1.00 31.98           O  
ATOM  11045  CB  MET B 697     213.490 181.041 184.139  1.00 33.01           C  
ATOM  11046  CG  MET B 697     214.537 182.115 184.269  1.00 32.40           C  
ATOM  11047  SD  MET B 697     213.831 183.689 184.723  1.00 32.99           S  
ATOM  11048  CE  MET B 697     215.281 184.688 184.852  1.00 30.85           C  
ATOM  11049  N   SER B 698     213.861 179.593 181.327  1.00 32.54           N  
ATOM  11050  CA  SER B 698     214.286 179.797 179.958  1.00 31.11           C  
ATOM  11051  C   SER B 698     214.297 181.278 179.663  1.00 29.87           C  
ATOM  11052  O   SER B 698     213.436 182.015 180.140  1.00 30.28           O  
ATOM  11053  CB  SER B 698     213.359 179.109 178.989  1.00 31.76           C  
ATOM  11054  OG  SER B 698     213.743 179.382 177.671  1.00 30.51           O  
ATOM  11055  N   LEU B 699     215.242 181.726 178.856  1.00 28.92           N  
ATOM  11056  CA  LEU B 699     215.273 183.132 178.497  1.00 27.93           C  
ATOM  11057  C   LEU B 699     214.608 183.342 177.152  1.00 27.88           C  
ATOM  11058  O   LEU B 699     214.588 184.451 176.622  1.00 27.38           O  
ATOM  11059  CB  LEU B 699     216.704 183.629 178.432  1.00 27.46           C  
ATOM  11060  CG  LEU B 699     217.537 183.427 179.677  1.00 27.78           C  
ATOM  11061  CD1 LEU B 699     218.883 184.031 179.425  1.00 27.02           C  
ATOM  11062  CD2 LEU B 699     216.860 184.034 180.896  1.00 28.47           C  
ATOM  11063  N   GLY B 700     214.079 182.261 176.598  1.00 27.96           N  
ATOM  11064  CA  GLY B 700     213.458 182.279 175.288  1.00 27.12           C  
ATOM  11065  C   GLY B 700     214.060 181.182 174.434  1.00 26.66           C  
ATOM  11066  O   GLY B 700     215.090 180.602 174.784  1.00 26.92           O  
ATOM  11067  N   ALA B 701     213.404 180.865 173.329  1.00 26.02           N  
ATOM  11068  CA  ALA B 701     213.912 179.838 172.435  1.00 25.53           C  
ATOM  11069  C   ALA B 701     215.177 180.343 171.791  1.00 24.96           C  
ATOM  11070  O   ALA B 701     215.268 181.531 171.484  1.00 25.53           O  
ATOM  11071  CB  ALA B 701     212.885 179.497 171.373  1.00 26.09           C  
ATOM  11072  N   GLU B 702     216.147 179.470 171.565  1.00 25.19           N  
ATOM  11073  CA  GLU B 702     217.328 179.930 170.859  1.00 24.96           C  
ATOM  11074  C   GLU B 702     217.054 179.933 169.375  1.00 24.73           C  
ATOM  11075  O   GLU B 702     216.239 179.149 168.882  1.00 24.81           O  
ATOM  11076  CB  GLU B 702     218.561 179.075 171.152  1.00 24.90           C  
ATOM  11077  CG  GLU B 702     218.570 177.697 170.514  1.00 25.59           C  
ATOM  11078  CD  GLU B 702     219.888 176.975 170.722  1.00 26.18           C  
ATOM  11079  OE1 GLU B 702     220.797 177.549 171.293  1.00 25.64           O  
ATOM  11080  OE2 GLU B 702     220.000 175.862 170.274  1.00 25.87           O  
ATOM  11081  N   ASN B 703     217.779 180.770 168.661  1.00 24.48           N  
ATOM  11082  CA  ASN B 703     217.711 180.812 167.216  1.00 23.42           C  
ATOM  11083  C   ASN B 703     219.044 181.266 166.663  1.00 23.26           C  
ATOM  11084  O   ASN B 703     219.965 181.596 167.412  1.00 24.20           O  
ATOM  11085  CB  ASN B 703     216.594 181.753 166.772  1.00 23.37           C  
ATOM  11086  CG  ASN B 703     216.033 181.431 165.407  1.00 23.78           C  
ATOM  11087  OD1 ASN B 703     216.611 180.632 164.669  1.00 23.96           O  
ATOM  11088  ND2 ASN B 703     214.936 182.043 165.051  1.00 23.39           N  
ATOM  11089  N   SER B 704     219.138 181.320 165.356  1.00 23.03           N  
ATOM  11090  CA  SER B 704     220.334 181.819 164.721  1.00 22.91           C  
ATOM  11091  C   SER B 704     219.972 182.488 163.423  1.00 22.52           C  
ATOM  11092  O   SER B 704     219.023 182.100 162.741  1.00 22.64           O  
ATOM  11093  CB  SER B 704     221.316 180.691 164.481  1.00 22.66           C  
ATOM  11094  OG  SER B 704     220.793 179.751 163.592  1.00 22.34           O  
ATOM  11095  N   VAL B 705     220.746 183.485 163.068  1.00 22.11           N  
ATOM  11096  CA  VAL B 705     220.541 184.167 161.818  1.00 21.89           C  
ATOM  11097  C   VAL B 705     221.496 183.589 160.803  1.00 22.04           C  
ATOM  11098  O   VAL B 705     222.692 183.480 161.068  1.00 22.25           O  
ATOM  11099  CB  VAL B 705     220.757 185.673 162.010  1.00 21.90           C  
ATOM  11100  CG1 VAL B 705     220.613 186.396 160.702  1.00 22.44           C  
ATOM  11101  CG2 VAL B 705     219.737 186.194 163.008  1.00 22.12           C  
ATOM  11102  N   ALA B 706     220.987 183.219 159.639  1.00 21.84           N  
ATOM  11103  CA  ALA B 706     221.825 182.602 158.620  1.00 21.82           C  
ATOM  11104  C   ALA B 706     222.638 183.658 157.899  1.00 22.12           C  
ATOM  11105  O   ALA B 706     222.439 183.917 156.716  1.00 22.45           O  
ATOM  11106  CB  ALA B 706     220.970 181.841 157.631  1.00 21.28           C  
ATOM  11107  N   TYR B 707     223.556 184.261 158.634  1.00 22.30           N  
ATOM  11108  CA  TYR B 707     224.392 185.325 158.135  1.00 22.03           C  
ATOM  11109  C   TYR B 707     225.417 184.819 157.157  1.00 22.88           C  
ATOM  11110  O   TYR B 707     226.056 183.794 157.385  1.00 22.97           O  
ATOM  11111  CB  TYR B 707     225.121 186.024 159.273  1.00 22.68           C  
ATOM  11112  CG  TYR B 707     226.034 187.095 158.778  1.00 22.55           C  
ATOM  11113  CD1 TYR B 707     225.548 188.343 158.536  1.00 22.23           C  
ATOM  11114  CD2 TYR B 707     227.363 186.810 158.529  1.00 23.35           C  
ATOM  11115  CE1 TYR B 707     226.371 189.309 158.043  1.00 22.22           C  
ATOM  11116  CE2 TYR B 707     228.190 187.780 158.026  1.00 23.55           C  
ATOM  11117  CZ  TYR B 707     227.695 189.026 157.777  1.00 22.67           C  
ATOM  11118  OH  TYR B 707     228.506 190.006 157.249  1.00 23.33           O  
ATOM  11119  N   SER B 708     225.588 185.562 156.087  1.00 22.88           N  
ATOM  11120  CA  SER B 708     226.629 185.322 155.115  1.00 22.47           C  
ATOM  11121  C   SER B 708     226.854 186.650 154.420  1.00 22.60           C  
ATOM  11122  O   SER B 708     226.012 187.543 154.537  1.00 22.60           O  
ATOM  11123  CB  SER B 708     226.226 184.232 154.151  1.00 22.76           C  
ATOM  11124  OG  SER B 708     225.165 184.646 153.377  1.00 22.54           O  
ATOM  11125  N   ASN B 709     227.956 186.784 153.679  1.00 22.35           N  
ATOM  11126  CA  ASN B 709     228.306 188.036 153.007  1.00 22.26           C  
ATOM  11127  C   ASN B 709     227.444 188.326 151.756  1.00 22.54           C  
ATOM  11128  O   ASN B 709     227.476 189.451 151.247  1.00 22.33           O  
ATOM  11129  CB  ASN B 709     229.796 188.053 152.657  1.00 23.01           C  
ATOM  11130  CG  ASN B 709     230.275 186.868 151.784  1.00 22.97           C  
ATOM  11131  OD1 ASN B 709     229.469 186.053 151.309  1.00 23.23           O  
ATOM  11132  ND2 ASN B 709     231.569 186.786 151.586  1.00 23.31           N  
ATOM  11133  N   ASN B 710     226.686 187.334 151.252  1.00 22.40           N  
ATOM  11134  CA  ASN B 710     225.863 187.476 150.045  1.00 21.34           C  
ATOM  11135  C   ASN B 710     224.428 186.977 150.183  1.00 21.46           C  
ATOM  11136  O   ASN B 710     223.844 186.555 149.188  1.00 22.39           O  
ATOM  11137  CB  ASN B 710     226.535 186.778 148.895  1.00 21.79           C  
ATOM  11138  CG  ASN B 710     226.678 185.327 149.144  1.00 22.46           C  
ATOM  11139  OD1 ASN B 710     226.415 184.847 150.254  1.00 22.63           O  
ATOM  11140  ND2 ASN B 710     227.094 184.603 148.140  1.00 22.26           N  
ATOM  11141  N   SER B 711     223.827 187.039 151.369  1.00 21.59           N  
ATOM  11142  CA  SER B 711     222.450 186.557 151.497  1.00 21.31           C  
ATOM  11143  C   SER B 711     221.595 187.480 152.331  1.00 20.74           C  
ATOM  11144  O   SER B 711     221.968 187.874 153.433  1.00 21.66           O  
ATOM  11145  CB  SER B 711     222.406 185.187 152.122  1.00 22.25           C  
ATOM  11146  OG  SER B 711     221.086 184.720 152.210  1.00 22.19           O  
ATOM  11147  N   ILE B 712     220.446 187.836 151.785  1.00 20.85           N  
ATOM  11148  CA  ILE B 712     219.531 188.739 152.450  1.00 20.25           C  
ATOM  11149  C   ILE B 712     218.138 188.141 152.521  1.00 20.37           C  
ATOM  11150  O   ILE B 712     217.661 187.544 151.560  1.00 21.37           O  
ATOM  11151  CB  ILE B 712     219.492 190.084 151.706  1.00 20.79           C  
ATOM  11152  CG1 ILE B 712     218.692 191.112 152.492  1.00 21.19           C  
ATOM  11153  CG2 ILE B 712     218.873 189.891 150.324  1.00 21.00           C  
ATOM  11154  CD1 ILE B 712     218.915 192.540 152.032  1.00 21.63           C  
ATOM  11155  N   ALA B 713     217.473 188.309 153.646  1.00 20.87           N  
ATOM  11156  CA  ALA B 713     216.096 187.852 153.740  1.00 20.04           C  
ATOM  11157  C   ALA B 713     215.164 189.031 153.596  1.00 20.33           C  
ATOM  11158  O   ALA B 713     215.331 190.060 154.248  1.00 20.78           O  
ATOM  11159  CB  ALA B 713     215.843 187.127 155.034  1.00 20.67           C  
ATOM  11160  N   ILE B 714     214.190 188.882 152.720  1.00 20.22           N  
ATOM  11161  CA  ILE B 714     213.221 189.934 152.467  1.00 20.09           C  
ATOM  11162  C   ILE B 714     211.825 189.363 152.643  1.00 19.78           C  
ATOM  11163  O   ILE B 714     211.556 188.277 152.128  1.00 20.94           O  
ATOM  11164  CB  ILE B 714     213.391 190.491 151.039  1.00 20.39           C  
ATOM  11165  CG1 ILE B 714     214.795 191.046 150.894  1.00 21.02           C  
ATOM  11166  CG2 ILE B 714     212.346 191.567 150.721  1.00 20.41           C  
ATOM  11167  CD1 ILE B 714     215.168 191.397 149.513  1.00 21.40           C  
ATOM  11168  N   PRO B 715     210.936 190.018 153.396  1.00 19.71           N  
ATOM  11169  CA  PRO B 715     209.582 189.594 153.605  1.00 19.08           C  
ATOM  11170  C   PRO B 715     208.838 189.677 152.299  1.00 19.69           C  
ATOM  11171  O   PRO B 715     209.031 190.623 151.548  1.00 20.45           O  
ATOM  11172  CB  PRO B 715     209.068 190.595 154.632  1.00 19.00           C  
ATOM  11173  CG  PRO B 715     209.943 191.802 154.465  1.00 19.66           C  
ATOM  11174  CD  PRO B 715     211.283 191.270 154.059  1.00 19.99           C  
ATOM  11175  N   THR B 716     207.980 188.711 152.055  1.00 19.13           N  
ATOM  11176  CA  THR B 716     207.124 188.654 150.869  1.00 19.21           C  
ATOM  11177  C   THR B 716     205.647 188.930 151.186  1.00 19.07           C  
ATOM  11178  O   THR B 716     204.872 189.268 150.289  1.00 19.44           O  
ATOM  11179  CB  THR B 716     207.237 187.280 150.199  1.00 19.79           C  
ATOM  11180  OG1 THR B 716     206.784 186.270 151.107  1.00 19.42           O  
ATOM  11181  CG2 THR B 716     208.675 186.984 149.796  1.00 19.85           C  
ATOM  11182  N   ASN B 717     205.270 188.812 152.464  1.00 19.15           N  
ATOM  11183  CA  ASN B 717     203.931 189.042 152.983  1.00 18.22           C  
ATOM  11184  C   ASN B 717     204.067 189.780 154.311  1.00 18.58           C  
ATOM  11185  O   ASN B 717     205.175 189.928 154.827  1.00 19.14           O  
ATOM  11186  CB  ASN B 717     203.175 187.711 153.144  1.00 19.07           C  
ATOM  11187  CG  ASN B 717     201.639 187.840 153.138  1.00 18.44           C  
ATOM  11188  OD1 ASN B 717     201.091 188.941 153.277  1.00 18.62           O  
ATOM  11189  ND2 ASN B 717     200.965 186.704 152.986  1.00 18.80           N  
ATOM  11190  N   PHE B 718     202.945 190.239 154.862  1.00 18.37           N  
ATOM  11191  CA  PHE B 718     202.914 190.947 156.138  1.00 18.54           C  
ATOM  11192  C   PHE B 718     201.568 190.797 156.790  1.00 18.54           C  
ATOM  11193  O   PHE B 718     200.582 190.452 156.133  1.00 19.05           O  
ATOM  11194  CB  PHE B 718     203.187 192.426 155.938  1.00 18.81           C  
ATOM  11195  CG  PHE B 718     202.155 193.034 155.129  1.00 18.53           C  
ATOM  11196  CD1 PHE B 718     201.061 193.586 155.718  1.00 18.71           C  
ATOM  11197  CD2 PHE B 718     202.255 193.039 153.768  1.00 18.98           C  
ATOM  11198  CE1 PHE B 718     200.085 194.125 154.971  1.00 19.17           C  
ATOM  11199  CE2 PHE B 718     201.274 193.583 153.001  1.00 19.13           C  
ATOM  11200  CZ  PHE B 718     200.182 194.123 153.603  1.00 19.14           C  
ATOM  11201  N   THR B 719     201.529 191.097 158.073  1.00 18.22           N  
ATOM  11202  CA  THR B 719     200.281 191.150 158.795  1.00 18.85           C  
ATOM  11203  C   THR B 719     200.161 192.455 159.538  1.00 19.34           C  
ATOM  11204  O   THR B 719     201.159 193.096 159.870  1.00 19.10           O  
ATOM  11205  CB  THR B 719     200.156 189.993 159.796  1.00 18.96           C  
ATOM  11206  OG1 THR B 719     201.200 190.091 160.770  1.00 18.85           O  
ATOM  11207  CG2 THR B 719     200.253 188.660 159.084  1.00 19.14           C  
ATOM  11208  N   ILE B 720     198.936 192.827 159.845  1.00 19.30           N  
ATOM  11209  CA  ILE B 720     198.699 193.971 160.690  1.00 19.23           C  
ATOM  11210  C   ILE B 720     198.276 193.461 162.037  1.00 19.85           C  
ATOM  11211  O   ILE B 720     197.347 192.663 162.144  1.00 20.29           O  
ATOM  11212  CB  ILE B 720     197.620 194.895 160.119  1.00 19.49           C  
ATOM  11213  CG1 ILE B 720     197.988 195.342 158.694  1.00 19.47           C  
ATOM  11214  CG2 ILE B 720     197.406 196.094 161.036  1.00 20.08           C  
ATOM  11215  CD1 ILE B 720     199.303 196.092 158.548  1.00 19.53           C  
ATOM  11216  N   SER B 721     198.975 193.891 163.061  1.00 19.88           N  
ATOM  11217  CA  SER B 721     198.665 193.435 164.395  1.00 20.67           C  
ATOM  11218  C   SER B 721     198.277 194.599 165.256  1.00 21.00           C  
ATOM  11219  O   SER B 721     198.708 195.729 165.026  1.00 21.44           O  
ATOM  11220  CB  SER B 721     199.848 192.720 165.003  1.00 20.92           C  
ATOM  11221  OG  SER B 721     200.928 193.589 165.162  1.00 20.53           O  
ATOM  11222  N   VAL B 722     197.470 194.326 166.262  1.00 21.71           N  
ATOM  11223  CA  VAL B 722     197.089 195.352 167.200  1.00 21.74           C  
ATOM  11224  C   VAL B 722     197.494 194.932 168.588  1.00 22.32           C  
ATOM  11225  O   VAL B 722     197.143 193.842 169.038  1.00 22.79           O  
ATOM  11226  CB  VAL B 722     195.580 195.625 167.128  1.00 22.41           C  
ATOM  11227  CG1 VAL B 722     195.183 196.682 168.150  1.00 22.68           C  
ATOM  11228  CG2 VAL B 722     195.237 196.102 165.731  1.00 22.23           C  
ATOM  11229  N   THR B 723     198.237 195.786 169.265  1.00 22.21           N  
ATOM  11230  CA  THR B 723     198.654 195.477 170.619  1.00 22.52           C  
ATOM  11231  C   THR B 723     198.025 196.466 171.569  1.00 22.75           C  
ATOM  11232  O   THR B 723     197.662 197.572 171.173  1.00 23.16           O  
ATOM  11233  CB  THR B 723     200.184 195.518 170.762  1.00 22.44           C  
ATOM  11234  OG1 THR B 723     200.659 196.849 170.528  1.00 22.28           O  
ATOM  11235  CG2 THR B 723     200.818 194.584 169.751  1.00 22.54           C  
ATOM  11236  N   THR B 724     197.915 196.096 172.832  1.00 22.96           N  
ATOM  11237  CA  THR B 724     197.302 197.001 173.789  1.00 22.71           C  
ATOM  11238  C   THR B 724     198.287 197.441 174.849  1.00 22.78           C  
ATOM  11239  O   THR B 724     198.896 196.615 175.527  1.00 23.48           O  
ATOM  11240  CB  THR B 724     196.091 196.340 174.461  1.00 23.27           C  
ATOM  11241  OG1 THR B 724     195.141 195.982 173.470  1.00 24.31           O  
ATOM  11242  CG2 THR B 724     195.443 197.298 175.409  1.00 24.00           C  
ATOM  11243  N   GLU B 725     198.427 198.748 175.001  1.00 22.80           N  
ATOM  11244  CA  GLU B 725     199.315 199.294 176.010  1.00 22.54           C  
ATOM  11245  C   GLU B 725     198.531 200.055 177.055  1.00 23.18           C  
ATOM  11246  O   GLU B 725     197.836 201.024 176.755  1.00 23.87           O  
ATOM  11247  CB  GLU B 725     200.368 200.200 175.397  1.00 22.34           C  
ATOM  11248  CG  GLU B 725     201.357 200.705 176.408  1.00 22.42           C  
ATOM  11249  CD  GLU B 725     202.476 201.489 175.823  1.00 22.15           C  
ATOM  11250  OE1 GLU B 725     202.389 201.915 174.690  1.00 21.78           O  
ATOM  11251  OE2 GLU B 725     203.455 201.655 176.505  1.00 21.79           O  
ATOM  11252  N   ILE B 726     198.633 199.600 178.289  1.00 23.34           N  
ATOM  11253  CA  ILE B 726     197.855 200.162 179.378  1.00 23.40           C  
ATOM  11254  C   ILE B 726     198.714 200.952 180.342  1.00 23.50           C  
ATOM  11255  O   ILE B 726     199.680 200.421 180.885  1.00 24.12           O  
ATOM  11256  CB  ILE B 726     197.146 199.020 180.114  1.00 23.97           C  
ATOM  11257  CG1 ILE B 726     196.229 198.297 179.117  1.00 24.51           C  
ATOM  11258  CG2 ILE B 726     196.371 199.552 181.312  1.00 25.03           C  
ATOM  11259  CD1 ILE B 726     195.732 196.988 179.563  1.00 26.18           C  
ATOM  11260  N   LEU B 727     198.361 202.218 180.545  1.00 23.51           N  
ATOM  11261  CA  LEU B 727     199.101 203.079 181.454  1.00 23.15           C  
ATOM  11262  C   LEU B 727     198.157 203.773 182.426  1.00 23.73           C  
ATOM  11263  O   LEU B 727     197.101 204.248 182.010  1.00 24.80           O  
ATOM  11264  CB  LEU B 727     199.835 204.165 180.667  1.00 22.69           C  
ATOM  11265  CG  LEU B 727     200.873 203.705 179.667  1.00 22.52           C  
ATOM  11266  CD1 LEU B 727     201.288 204.868 178.835  1.00 21.62           C  
ATOM  11267  CD2 LEU B 727     202.072 203.144 180.384  1.00 22.75           C  
ATOM  11268  N   PRO B 728     198.499 203.865 183.712  1.00 23.45           N  
ATOM  11269  CA  PRO B 728     197.785 204.629 184.702  1.00 23.63           C  
ATOM  11270  C   PRO B 728     198.052 206.095 184.470  1.00 23.55           C  
ATOM  11271  O   PRO B 728     199.141 206.470 184.039  1.00 24.14           O  
ATOM  11272  CB  PRO B 728     198.370 204.113 186.007  1.00 24.07           C  
ATOM  11273  CG  PRO B 728     199.757 203.677 185.651  1.00 24.57           C  
ATOM  11274  CD  PRO B 728     199.663 203.160 184.222  1.00 23.86           C  
ATOM  11275  N   VAL B 729     197.075 206.922 184.777  1.00 24.19           N  
ATOM  11276  CA  VAL B 729     197.229 208.362 184.657  1.00 23.84           C  
ATOM  11277  C   VAL B 729     197.031 209.075 185.981  1.00 24.37           C  
ATOM  11278  O   VAL B 729     197.684 210.085 186.246  1.00 24.42           O  
ATOM  11279  CB  VAL B 729     196.280 208.916 183.589  1.00 24.22           C  
ATOM  11280  CG1 VAL B 729     196.347 210.429 183.542  1.00 24.37           C  
ATOM  11281  CG2 VAL B 729     196.685 208.349 182.241  1.00 23.97           C  
ATOM  11282  N   SER B 730     196.089 208.600 186.788  1.00 24.81           N  
ATOM  11283  CA  SER B 730     195.778 209.323 188.006  1.00 24.80           C  
ATOM  11284  C   SER B 730     195.456 208.426 189.188  1.00 25.34           C  
ATOM  11285  O   SER B 730     195.057 207.271 189.039  1.00 25.47           O  
ATOM  11286  CB  SER B 730     194.615 210.254 187.767  1.00 25.20           C  
ATOM  11287  OG  SER B 730     193.457 209.537 187.465  1.00 25.71           O  
ATOM  11288  N   MET B 731     195.634 208.996 190.365  1.00 25.40           N  
ATOM  11289  CA  MET B 731     195.325 208.388 191.644  1.00 25.77           C  
ATOM  11290  C   MET B 731     193.970 208.835 192.121  1.00 26.07           C  
ATOM  11291  O   MET B 731     193.456 209.863 191.683  1.00 26.25           O  
ATOM  11292  CB  MET B 731     196.341 208.806 192.695  1.00 26.06           C  
ATOM  11293  CG  MET B 731     197.729 208.372 192.445  1.00 25.93           C  
ATOM  11294  SD  MET B 731     198.880 209.076 193.630  1.00 25.96           S  
ATOM  11295  CE  MET B 731     198.578 208.184 195.134  1.00 26.51           C  
ATOM  11296  N   THR B 732     193.412 208.097 193.061  1.00 26.56           N  
ATOM  11297  CA  THR B 732     192.215 208.560 193.731  1.00 26.85           C  
ATOM  11298  C   THR B 732     192.559 209.842 194.480  1.00 27.19           C  
ATOM  11299  O   THR B 732     193.562 209.901 195.194  1.00 27.15           O  
ATOM  11300  CB  THR B 732     191.675 207.492 194.700  1.00 27.35           C  
ATOM  11301  OG1 THR B 732     191.309 206.317 193.967  1.00 26.90           O  
ATOM  11302  CG2 THR B 732     190.483 208.008 195.437  1.00 28.52           C  
ATOM  11303  N   LYS B 733     191.726 210.868 194.342  1.00 27.38           N  
ATOM  11304  CA  LYS B 733     192.001 212.141 194.995  1.00 27.11           C  
ATOM  11305  C   LYS B 733     191.619 212.107 196.456  1.00 28.36           C  
ATOM  11306  O   LYS B 733     190.605 212.668 196.872  1.00 29.18           O  
ATOM  11307  CB  LYS B 733     191.253 213.270 194.308  1.00 27.36           C  
ATOM  11308  CG  LYS B 733     191.760 213.622 192.935  1.00 26.53           C  
ATOM  11309  CD  LYS B 733     190.794 214.545 192.219  1.00 27.21           C  
ATOM  11310  CE  LYS B 733     190.703 215.930 192.870  1.00 27.16           C  
ATOM  11311  NZ  LYS B 733     189.806 216.830 192.115  1.00 27.45           N  
ATOM  11312  N   THR B 734     192.432 211.420 197.229  1.00 28.34           N  
ATOM  11313  CA  THR B 734     192.177 211.249 198.642  1.00 28.49           C  
ATOM  11314  C   THR B 734     192.590 212.481 199.418  1.00 28.91           C  
ATOM  11315  O   THR B 734     193.645 213.065 199.173  1.00 28.29           O  
ATOM  11316  CB  THR B 734     192.905 210.021 199.188  1.00 28.77           C  
ATOM  11317  OG1 THR B 734     192.447 208.849 198.503  1.00 28.61           O  
ATOM  11318  CG2 THR B 734     192.646 209.870 200.655  1.00 29.34           C  
ATOM  11319  N   SER B 735     191.751 212.869 200.363  1.00 29.25           N  
ATOM  11320  CA  SER B 735     192.015 214.013 201.217  1.00 29.38           C  
ATOM  11321  C   SER B 735     191.705 213.662 202.658  1.00 29.81           C  
ATOM  11322  O   SER B 735     190.634 213.138 202.971  1.00 30.76           O  
ATOM  11323  CB  SER B 735     191.186 215.197 200.783  1.00 29.86           C  
ATOM  11324  OG  SER B 735     191.398 216.290 201.627  1.00 30.97           O  
ATOM  11325  N   VAL B 736     192.669 213.900 203.532  1.00 29.61           N  
ATOM  11326  CA  VAL B 736     192.519 213.537 204.928  1.00 30.04           C  
ATOM  11327  C   VAL B 736     192.547 214.746 205.826  1.00 30.08           C  
ATOM  11328  O   VAL B 736     193.468 215.553 205.759  1.00 30.36           O  
ATOM  11329  CB  VAL B 736     193.634 212.559 205.347  1.00 30.29           C  
ATOM  11330  CG1 VAL B 736     193.522 212.231 206.823  1.00 30.82           C  
ATOM  11331  CG2 VAL B 736     193.523 211.291 204.511  1.00 30.32           C  
ATOM  11332  N   ASP B 737     191.545 214.849 206.685  1.00 30.43           N  
ATOM  11333  CA  ASP B 737     191.486 215.909 207.673  1.00 30.63           C  
ATOM  11334  C   ASP B 737     192.296 215.466 208.884  1.00 31.49           C  
ATOM  11335  O   ASP B 737     191.829 214.630 209.664  1.00 32.00           O  
ATOM  11336  CB  ASP B 737     190.027 216.194 208.063  1.00 31.41           C  
ATOM  11337  CG  ASP B 737     189.879 217.296 209.114  1.00 32.46           C  
ATOM  11338  OD1 ASP B 737     190.758 217.404 209.944  1.00 32.09           O  
ATOM  11339  OD2 ASP B 737     188.897 218.003 209.099  1.00 34.54           O  
ATOM  11340  N   CYS B 738     193.532 215.992 209.015  1.00 30.64           N  
ATOM  11341  CA  CYS B 738     194.479 215.542 210.036  1.00 30.72           C  
ATOM  11342  C   CYS B 738     193.980 215.763 211.475  1.00 31.87           C  
ATOM  11343  O   CYS B 738     194.303 214.969 212.360  1.00 32.86           O  
ATOM  11344  CB  CYS B 738     195.824 216.270 209.855  1.00 31.24           C  
ATOM  11345  SG  CYS B 738     195.734 218.080 210.030  1.00 31.94           S  
ATOM  11346  N   THR B 739     193.163 216.812 211.713  1.00 31.20           N  
ATOM  11347  CA  THR B 739     192.642 217.104 213.045  1.00 30.95           C  
ATOM  11348  C   THR B 739     191.569 216.108 213.404  1.00 32.96           C  
ATOM  11349  O   THR B 739     191.563 215.560 214.503  1.00 33.59           O  
ATOM  11350  CB  THR B 739     192.067 218.522 213.144  1.00 31.32           C  
ATOM  11351  OG1 THR B 739     193.086 219.474 212.835  1.00 31.40           O  
ATOM  11352  CG2 THR B 739     191.546 218.776 214.555  1.00 31.38           C  
ATOM  11353  N   MET B 740     190.662 215.849 212.474  1.00 31.38           N  
ATOM  11354  CA  MET B 740     189.607 214.895 212.757  1.00 31.97           C  
ATOM  11355  C   MET B 740     190.165 213.492 212.930  1.00 32.03           C  
ATOM  11356  O   MET B 740     189.658 212.712 213.736  1.00 33.26           O  
ATOM  11357  CB  MET B 740     188.550 214.906 211.673  1.00 33.58           C  
ATOM  11358  CG  MET B 740     187.394 213.987 211.972  1.00 35.37           C  
ATOM  11359  SD  MET B 740     186.090 214.087 210.767  1.00 39.50           S  
ATOM  11360  CE  MET B 740     185.062 212.776 211.392  1.00 39.89           C  
ATOM  11361  N   TYR B 741     191.200 213.167 212.162  1.00 32.17           N  
ATOM  11362  CA  TYR B 741     191.832 211.861 212.237  1.00 32.02           C  
ATOM  11363  C   TYR B 741     192.454 211.624 213.601  1.00 32.43           C  
ATOM  11364  O   TYR B 741     192.253 210.573 214.210  1.00 33.35           O  
ATOM  11365  CB  TYR B 741     192.890 211.706 211.149  1.00 32.03           C  
ATOM  11366  CG  TYR B 741     193.652 210.414 211.236  1.00 32.20           C  
ATOM  11367  CD1 TYR B 741     193.120 209.248 210.741  1.00 32.81           C  
ATOM  11368  CD2 TYR B 741     194.884 210.399 211.826  1.00 32.32           C  
ATOM  11369  CE1 TYR B 741     193.837 208.076 210.845  1.00 32.56           C  
ATOM  11370  CE2 TYR B 741     195.589 209.245 211.931  1.00 32.48           C  
ATOM  11371  CZ  TYR B 741     195.079 208.093 211.450  1.00 32.28           C  
ATOM  11372  OH  TYR B 741     195.800 206.945 211.574  1.00 32.75           O  
ATOM  11373  N   ILE B 742     193.228 212.596 214.081  1.00 33.11           N  
ATOM  11374  CA  ILE B 742     193.921 212.439 215.352  1.00 32.82           C  
ATOM  11375  C   ILE B 742     193.024 212.692 216.579  1.00 33.65           C  
ATOM  11376  O   ILE B 742     193.042 211.900 217.524  1.00 34.80           O  
ATOM  11377  CB  ILE B 742     195.135 213.389 215.441  1.00 32.85           C  
ATOM  11378  CG1 ILE B 742     196.138 213.076 214.351  1.00 32.50           C  
ATOM  11379  CG2 ILE B 742     195.806 213.222 216.806  1.00 34.20           C  
ATOM  11380  CD1 ILE B 742     197.200 214.123 214.187  1.00 32.54           C  
ATOM  11381  N   CYS B 743     192.265 213.815 216.577  1.00 33.60           N  
ATOM  11382  CA  CYS B 743     191.494 214.305 217.715  1.00 34.50           C  
ATOM  11383  C   CYS B 743     190.011 214.468 217.367  1.00 34.73           C  
ATOM  11384  O   CYS B 743     189.458 215.595 217.465  1.00 35.24           O  
ATOM  11385  CB  CYS B 743     192.072 215.642 218.204  1.00 34.92           C  
ATOM  11386  SG  CYS B 743     193.771 215.551 218.824  1.00 35.93           S  
ATOM  11387  N   GLY B 744     189.339 213.391 216.968  1.00 34.90           N  
ATOM  11388  CA  GLY B 744     187.940 213.442 216.542  1.00 35.50           C  
ATOM  11389  C   GLY B 744     187.020 213.793 217.699  1.00 37.08           C  
ATOM  11390  O   GLY B 744     186.974 213.087 218.704  1.00 37.78           O  
ATOM  11391  N   ASP B 745     186.280 214.884 217.542  1.00 37.58           N  
ATOM  11392  CA  ASP B 745     185.350 215.355 218.559  1.00 37.85           C  
ATOM  11393  C   ASP B 745     185.990 215.526 219.934  1.00 37.54           C  
ATOM  11394  O   ASP B 745     185.344 215.276 220.951  1.00 38.21           O  
ATOM  11395  CB  ASP B 745     184.166 214.393 218.675  1.00 38.90           C  
ATOM  11396  CG  ASP B 745     183.309 214.363 217.426  1.00 40.50           C  
ATOM  11397  OD1 ASP B 745     183.114 215.403 216.835  1.00 40.66           O  
ATOM  11398  OD2 ASP B 745     182.840 213.310 217.064  1.00 41.87           O  
ATOM  11399  N   SER B 746     187.236 215.995 219.987  1.00 36.81           N  
ATOM  11400  CA  SER B 746     187.871 216.199 221.283  1.00 36.72           C  
ATOM  11401  C   SER B 746     188.590 217.523 221.415  1.00 35.85           C  
ATOM  11402  O   SER B 746     189.640 217.739 220.806  1.00 36.90           O  
ATOM  11403  CB  SER B 746     188.849 215.094 221.559  1.00 37.25           C  
ATOM  11404  OG  SER B 746     189.603 215.377 222.714  1.00 37.62           O  
ATOM  11405  N   THR B 747     188.039 218.397 222.247  1.00 36.04           N  
ATOM  11406  CA  THR B 747     188.615 219.714 222.475  1.00 35.82           C  
ATOM  11407  C   THR B 747     189.942 219.601 223.203  1.00 35.17           C  
ATOM  11408  O   THR B 747     190.901 220.305 222.880  1.00 36.56           O  
ATOM  11409  CB  THR B 747     187.657 220.613 223.273  1.00 35.79           C  
ATOM  11410  OG1 THR B 747     186.448 220.802 222.528  1.00 36.38           O  
ATOM  11411  CG2 THR B 747     188.301 221.965 223.527  1.00 36.07           C  
ATOM  11412  N   GLU B 748     189.997 218.713 224.188  1.00 36.30           N  
ATOM  11413  CA  GLU B 748     191.205 218.552 224.988  1.00 35.68           C  
ATOM  11414  C   GLU B 748     192.374 218.052 224.139  1.00 35.63           C  
ATOM  11415  O   GLU B 748     193.487 218.578 224.243  1.00 35.94           O  
ATOM  11416  CB  GLU B 748     190.933 217.575 226.134  1.00 36.70           C  
ATOM  11417  N   CYS B 749     192.106 217.073 223.254  1.00 35.57           N  
ATOM  11418  CA  CYS B 749     193.101 216.533 222.333  1.00 35.44           C  
ATOM  11419  C   CYS B 749     193.564 217.605 221.333  1.00 34.70           C  
ATOM  11420  O   CYS B 749     194.768 217.724 221.086  1.00 35.85           O  
ATOM  11421  CB  CYS B 749     192.539 215.294 221.623  1.00 36.74           C  
ATOM  11422  SG  CYS B 749     193.671 214.411 220.505  1.00 37.26           S  
ATOM  11423  N   SER B 750     192.623 218.396 220.765  1.00 35.22           N  
ATOM  11424  CA  SER B 750     192.943 219.447 219.796  1.00 34.32           C  
ATOM  11425  C   SER B 750     193.884 220.479 220.404  1.00 34.41           C  
ATOM  11426  O   SER B 750     194.877 220.865 219.787  1.00 35.39           O  
ATOM  11427  CB  SER B 750     191.680 220.126 219.319  1.00 34.57           C  
ATOM  11428  OG  SER B 750     191.973 221.135 218.393  1.00 34.49           O  
ATOM  11429  N   ASN B 751     193.623 220.869 221.647  1.00 34.51           N  
ATOM  11430  CA  ASN B 751     194.486 221.836 222.299  1.00 33.99           C  
ATOM  11431  C   ASN B 751     195.912 221.308 222.428  1.00 33.94           C  
ATOM  11432  O   ASN B 751     196.868 222.080 222.345  1.00 34.19           O  
ATOM  11433  CB  ASN B 751     193.927 222.216 223.649  1.00 34.67           C  
ATOM  11434  CG  ASN B 751     192.728 223.094 223.535  1.00 34.99           C  
ATOM  11435  OD1 ASN B 751     192.484 223.699 222.486  1.00 34.83           O  
ATOM  11436  ND2 ASN B 751     191.969 223.184 224.594  1.00 35.59           N  
ATOM  11437  N   LEU B 752     196.058 219.997 222.620  1.00 34.21           N  
ATOM  11438  CA  LEU B 752     197.382 219.387 222.691  1.00 34.01           C  
ATOM  11439  C   LEU B 752     197.991 219.272 221.302  1.00 34.42           C  
ATOM  11440  O   LEU B 752     199.192 219.448 221.117  1.00 34.07           O  
ATOM  11441  CB  LEU B 752     197.295 217.990 223.313  1.00 34.87           C  
ATOM  11442  CG  LEU B 752     196.887 217.915 224.781  1.00 35.88           C  
ATOM  11443  CD1 LEU B 752     196.603 216.469 225.128  1.00 37.02           C  
ATOM  11444  CD2 LEU B 752     198.005 218.459 225.662  1.00 36.86           C  
ATOM  11445  N   LEU B 753     197.158 219.010 220.307  1.00 33.62           N  
ATOM  11446  CA  LEU B 753     197.634 218.870 218.940  1.00 33.04           C  
ATOM  11447  C   LEU B 753     198.252 220.170 218.455  1.00 32.94           C  
ATOM  11448  O   LEU B 753     199.238 220.156 217.725  1.00 33.73           O  
ATOM  11449  CB  LEU B 753     196.497 218.433 218.013  1.00 33.40           C  
ATOM  11450  CG  LEU B 753     196.859 218.151 216.534  1.00 32.96           C  
ATOM  11451  CD1 LEU B 753     197.928 217.069 216.443  1.00 33.26           C  
ATOM  11452  CD2 LEU B 753     195.595 217.695 215.807  1.00 32.98           C  
ATOM  11453  N   LEU B 754     197.709 221.295 218.898  1.00 33.05           N  
ATOM  11454  CA  LEU B 754     198.209 222.606 218.499  1.00 33.06           C  
ATOM  11455  C   LEU B 754     199.632 222.867 218.978  1.00 33.09           C  
ATOM  11456  O   LEU B 754     200.309 223.764 218.475  1.00 32.97           O  
ATOM  11457  CB  LEU B 754     197.300 223.713 219.038  1.00 33.47           C  
ATOM  11458  CG  LEU B 754     195.890 223.805 218.441  1.00 33.91           C  
ATOM  11459  CD1 LEU B 754     195.086 224.825 219.233  1.00 34.49           C  
ATOM  11460  CD2 LEU B 754     195.968 224.215 216.976  1.00 33.87           C  
ATOM  11461  N   GLN B 755     200.117 222.077 219.926  1.00 32.98           N  
ATOM  11462  CA  GLN B 755     201.458 222.279 220.444  1.00 32.72           C  
ATOM  11463  C   GLN B 755     202.487 221.774 219.448  1.00 33.15           C  
ATOM  11464  O   GLN B 755     203.688 221.982 219.622  1.00 34.06           O  
ATOM  11465  CB  GLN B 755     201.639 221.579 221.787  1.00 33.41           C  
ATOM  11466  CG  GLN B 755     200.785 222.149 222.897  1.00 33.54           C  
ATOM  11467  CD  GLN B 755     201.017 221.450 224.208  1.00 34.18           C  
ATOM  11468  OE1 GLN B 755     201.566 220.347 224.244  1.00 34.48           O  
ATOM  11469  NE2 GLN B 755     200.607 222.085 225.300  1.00 33.15           N  
ATOM  11470  N   TYR B 756     202.011 221.126 218.392  1.00 32.53           N  
ATOM  11471  CA  TYR B 756     202.862 220.589 217.350  1.00 32.24           C  
ATOM  11472  C   TYR B 756     202.915 221.534 216.159  1.00 32.08           C  
ATOM  11473  O   TYR B 756     203.472 221.205 215.106  1.00 32.38           O  
ATOM  11474  CB  TYR B 756     202.361 219.212 216.951  1.00 32.44           C  
ATOM  11475  CG  TYR B 756     202.582 218.205 218.026  1.00 32.61           C  
ATOM  11476  CD1 TYR B 756     201.637 218.023 219.012  1.00 32.98           C  
ATOM  11477  CD2 TYR B 756     203.736 217.465 218.031  1.00 32.90           C  
ATOM  11478  CE1 TYR B 756     201.851 217.107 220.006  1.00 33.08           C  
ATOM  11479  CE2 TYR B 756     203.954 216.546 219.021  1.00 33.28           C  
ATOM  11480  CZ  TYR B 756     203.018 216.366 220.008  1.00 33.63           C  
ATOM  11481  OH  TYR B 756     203.240 215.449 221.004  1.00 34.87           O  
ATOM  11482  N   GLY B 757     202.364 222.729 216.343  1.00 32.44           N  
ATOM  11483  CA  GLY B 757     202.445 223.771 215.337  1.00 32.19           C  
ATOM  11484  C   GLY B 757     201.753 223.445 214.031  1.00 31.89           C  
ATOM  11485  O   GLY B 757     200.561 223.141 213.991  1.00 32.08           O  
ATOM  11486  N   SER B 758     202.517 223.532 212.954  1.00 31.52           N  
ATOM  11487  CA  SER B 758     202.030 223.332 211.604  1.00 30.81           C  
ATOM  11488  C   SER B 758     202.090 221.899 211.118  1.00 30.56           C  
ATOM  11489  O   SER B 758     201.711 221.628 209.982  1.00 31.02           O  
ATOM  11490  CB  SER B 758     202.819 224.197 210.644  1.00 30.94           C  
ATOM  11491  OG  SER B 758     202.646 225.554 210.930  1.00 31.89           O  
ATOM  11492  N   PHE B 759     202.543 220.958 211.940  1.00 31.14           N  
ATOM  11493  CA  PHE B 759     202.641 219.592 211.415  1.00 30.34           C  
ATOM  11494  C   PHE B 759     201.329 219.107 210.789  1.00 30.14           C  
ATOM  11495  O   PHE B 759     201.356 218.490 209.723  1.00 30.83           O  
ATOM  11496  CB  PHE B 759     203.063 218.586 212.499  1.00 30.40           C  
ATOM  11497  CG  PHE B 759     204.553 218.381 212.700  1.00 30.68           C  
ATOM  11498  CD1 PHE B 759     205.069 218.235 213.972  1.00 31.21           C  
ATOM  11499  CD2 PHE B 759     205.433 218.288 211.626  1.00 30.36           C  
ATOM  11500  CE1 PHE B 759     206.407 218.017 214.175  1.00 31.23           C  
ATOM  11501  CE2 PHE B 759     206.770 218.071 211.835  1.00 30.71           C  
ATOM  11502  CZ  PHE B 759     207.253 217.937 213.116  1.00 30.81           C  
ATOM  11503  N   CYS B 760     200.190 219.382 211.440  1.00 30.12           N  
ATOM  11504  CA  CYS B 760     198.869 218.959 210.966  1.00 30.19           C  
ATOM  11505  C   CYS B 760     198.522 219.671 209.621  1.00 30.19           C  
ATOM  11506  O   CYS B 760     198.139 219.017 208.640  1.00 30.09           O  
ATOM  11507  CB  CYS B 760     197.831 219.258 212.082  1.00 31.57           C  
ATOM  11508  SG  CYS B 760     196.198 218.454 211.962  1.00 32.71           S  
ATOM  11509  N   THR B 761     198.725 221.003 209.556  1.00 29.70           N  
ATOM  11510  CA  THR B 761     198.447 221.818 208.363  1.00 29.57           C  
ATOM  11511  C   THR B 761     199.293 221.410 207.167  1.00 29.07           C  
ATOM  11512  O   THR B 761     198.802 221.355 206.038  1.00 29.70           O  
ATOM  11513  CB  THR B 761     198.682 223.313 208.641  1.00 30.33           C  
ATOM  11514  OG1 THR B 761     197.771 223.764 209.648  1.00 31.40           O  
ATOM  11515  CG2 THR B 761     198.480 224.130 207.369  1.00 29.84           C  
ATOM  11516  N   GLN B 762     200.568 221.147 207.410  1.00 29.37           N  
ATOM  11517  CA  GLN B 762     201.476 220.765 206.349  1.00 28.38           C  
ATOM  11518  C   GLN B 762     201.034 219.462 205.699  1.00 28.88           C  
ATOM  11519  O   GLN B 762     201.124 219.313 204.479  1.00 28.89           O  
ATOM  11520  CB  GLN B 762     202.893 220.641 206.891  1.00 28.66           C  
ATOM  11521  CG  GLN B 762     203.924 220.334 205.843  1.00 28.87           C  
ATOM  11522  CD  GLN B 762     205.318 220.372 206.396  1.00 29.57           C  
ATOM  11523  OE1 GLN B 762     205.524 220.418 207.611  1.00 29.03           O  
ATOM  11524  NE2 GLN B 762     206.298 220.359 205.505  1.00 28.42           N  
ATOM  11525  N   LEU B 763     200.541 218.524 206.502  1.00 29.22           N  
ATOM  11526  CA  LEU B 763     200.058 217.259 205.968  1.00 28.31           C  
ATOM  11527  C   LEU B 763     198.830 217.475 205.094  1.00 28.51           C  
ATOM  11528  O   LEU B 763     198.724 216.900 204.006  1.00 28.89           O  
ATOM  11529  CB  LEU B 763     199.710 216.321 207.124  1.00 29.63           C  
ATOM  11530  CG  LEU B 763     200.897 215.825 207.959  1.00 29.87           C  
ATOM  11531  CD1 LEU B 763     200.375 215.206 209.237  1.00 30.44           C  
ATOM  11532  CD2 LEU B 763     201.690 214.802 207.184  1.00 30.22           C  
ATOM  11533  N   ASN B 764     197.926 218.351 205.530  1.00 28.69           N  
ATOM  11534  CA  ASN B 764     196.742 218.628 204.726  1.00 28.27           C  
ATOM  11535  C   ASN B 764     197.140 219.265 203.401  1.00 27.67           C  
ATOM  11536  O   ASN B 764     196.539 218.988 202.358  1.00 27.89           O  
ATOM  11537  CB  ASN B 764     195.775 219.555 205.442  1.00 29.19           C  
ATOM  11538  CG  ASN B 764     194.979 218.930 206.576  1.00 29.80           C  
ATOM  11539  OD1 ASN B 764     194.928 217.708 206.784  1.00 29.92           O  
ATOM  11540  ND2 ASN B 764     194.325 219.795 207.315  1.00 30.07           N  
ATOM  11541  N   ARG B 765     198.162 220.117 203.441  1.00 27.87           N  
ATOM  11542  CA  ARG B 765     198.630 220.804 202.250  1.00 27.29           C  
ATOM  11543  C   ARG B 765     199.241 219.841 201.248  1.00 26.91           C  
ATOM  11544  O   ARG B 765     198.996 219.956 200.046  1.00 26.92           O  
ATOM  11545  CB  ARG B 765     199.653 221.861 202.612  1.00 28.01           C  
ATOM  11546  CG  ARG B 765     200.108 222.738 201.461  1.00 27.98           C  
ATOM  11547  CD  ARG B 765     201.067 223.766 201.919  1.00 28.33           C  
ATOM  11548  NE  ARG B 765     200.462 224.658 202.895  1.00 28.71           N  
ATOM  11549  CZ  ARG B 765     201.140 225.442 203.754  1.00 29.30           C  
ATOM  11550  NH1 ARG B 765     202.455 225.453 203.752  1.00 28.59           N  
ATOM  11551  NH2 ARG B 765     200.476 226.207 204.605  1.00 29.05           N  
ATOM  11552  N   ALA B 766     200.041 218.897 201.730  1.00 27.20           N  
ATOM  11553  CA  ALA B 766     200.681 217.940 200.840  1.00 26.76           C  
ATOM  11554  C   ALA B 766     199.656 217.095 200.100  1.00 26.01           C  
ATOM  11555  O   ALA B 766     199.790 216.868 198.895  1.00 26.10           O  
ATOM  11556  CB  ALA B 766     201.604 217.042 201.631  1.00 27.09           C  
ATOM  11557  N   LEU B 767     198.609 216.665 200.798  1.00 26.55           N  
ATOM  11558  CA  LEU B 767     197.584 215.857 200.154  1.00 25.84           C  
ATOM  11559  C   LEU B 767     196.780 216.681 199.172  1.00 25.66           C  
ATOM  11560  O   LEU B 767     196.368 216.177 198.124  1.00 25.92           O  
ATOM  11561  CB  LEU B 767     196.669 215.215 201.192  1.00 26.65           C  
ATOM  11562  CG  LEU B 767     197.309 214.125 202.067  1.00 27.19           C  
ATOM  11563  CD1 LEU B 767     196.343 213.747 203.161  1.00 28.74           C  
ATOM  11564  CD2 LEU B 767     197.647 212.896 201.221  1.00 27.37           C  
ATOM  11565  N   THR B 768     196.564 217.952 199.489  1.00 25.91           N  
ATOM  11566  CA  THR B 768     195.859 218.825 198.568  1.00 25.14           C  
ATOM  11567  C   THR B 768     196.658 218.958 197.289  1.00 24.48           C  
ATOM  11568  O   THR B 768     196.099 218.893 196.193  1.00 25.02           O  
ATOM  11569  CB  THR B 768     195.619 220.214 199.169  1.00 25.84           C  
ATOM  11570  OG1 THR B 768     194.795 220.095 200.333  1.00 26.42           O  
ATOM  11571  CG2 THR B 768     194.932 221.108 198.148  1.00 24.88           C  
ATOM  11572  N   GLY B 769     197.969 219.135 197.424  1.00 25.07           N  
ATOM  11573  CA  GLY B 769     198.838 219.273 196.269  1.00 24.34           C  
ATOM  11574  C   GLY B 769     198.741 218.054 195.366  1.00 24.01           C  
ATOM  11575  O   GLY B 769     198.660 218.192 194.142  1.00 23.96           O  
ATOM  11576  N   ILE B 770     198.688 216.861 195.958  1.00 24.49           N  
ATOM  11577  CA  ILE B 770     198.541 215.664 195.148  1.00 23.58           C  
ATOM  11578  C   ILE B 770     197.209 215.665 194.435  1.00 24.03           C  
ATOM  11579  O   ILE B 770     197.153 215.420 193.233  1.00 24.60           O  
ATOM  11580  CB  ILE B 770     198.623 214.367 195.977  1.00 24.16           C  
ATOM  11581  CG1 ILE B 770     200.029 214.177 196.529  1.00 24.72           C  
ATOM  11582  CG2 ILE B 770     198.201 213.161 195.111  1.00 24.51           C  
ATOM  11583  CD1 ILE B 770     200.130 213.072 197.571  1.00 25.59           C  
ATOM  11584  N   ALA B 771     196.133 215.955 195.153  1.00 24.06           N  
ATOM  11585  CA  ALA B 771     194.820 215.903 194.537  1.00 24.21           C  
ATOM  11586  C   ALA B 771     194.739 216.820 193.324  1.00 24.05           C  
ATOM  11587  O   ALA B 771     194.201 216.433 192.289  1.00 25.23           O  
ATOM  11588  CB  ALA B 771     193.758 216.284 195.550  1.00 25.27           C  
ATOM  11589  N   VAL B 772     195.335 218.003 193.411  1.00 23.47           N  
ATOM  11590  CA  VAL B 772     195.322 218.914 192.274  1.00 23.29           C  
ATOM  11591  C   VAL B 772     196.123 218.343 191.115  1.00 23.61           C  
ATOM  11592  O   VAL B 772     195.677 218.366 189.964  1.00 24.29           O  
ATOM  11593  CB  VAL B 772     195.888 220.284 192.665  1.00 23.50           C  
ATOM  11594  CG1 VAL B 772     196.047 221.164 191.425  1.00 22.94           C  
ATOM  11595  CG2 VAL B 772     194.952 220.937 193.663  1.00 23.68           C  
ATOM  11596  N   GLU B 773     197.293 217.802 191.424  1.00 23.65           N  
ATOM  11597  CA  GLU B 773     198.154 217.200 190.423  1.00 22.81           C  
ATOM  11598  C   GLU B 773     197.436 216.110 189.647  1.00 25.82           C  
ATOM  11599  O   GLU B 773     197.681 215.936 188.454  1.00 23.76           O  
ATOM  11600  CB  GLU B 773     199.401 216.623 191.071  1.00 23.41           C  
ATOM  11601  CG  GLU B 773     200.402 216.058 190.105  1.00 23.27           C  
ATOM  11602  CD  GLU B 773     201.633 215.605 190.795  1.00 23.55           C  
ATOM  11603  OE1 GLU B 773     201.592 214.604 191.464  1.00 24.00           O  
ATOM  11604  OE2 GLU B 773     202.626 216.268 190.668  1.00 22.92           O  
ATOM  11605  N   GLN B 774     196.557 215.366 190.307  1.00 23.68           N  
ATOM  11606  CA  GLN B 774     195.884 214.276 189.628  1.00 23.69           C  
ATOM  11607  C   GLN B 774     194.944 214.776 188.534  1.00 24.59           C  
ATOM  11608  O   GLN B 774     194.711 214.062 187.558  1.00 24.89           O  
ATOM  11609  CB  GLN B 774     195.137 213.392 190.619  1.00 24.33           C  
ATOM  11610  CG  GLN B 774     196.046 212.777 191.654  1.00 24.29           C  
ATOM  11611  CD  GLN B 774     197.297 212.189 191.055  1.00 24.22           C  
ATOM  11612  OE1 GLN B 774     197.249 211.223 190.302  1.00 25.04           O  
ATOM  11613  NE2 GLN B 774     198.438 212.780 191.370  1.00 24.30           N  
ATOM  11614  N   ASP B 775     194.414 215.993 188.660  1.00 24.15           N  
ATOM  11615  CA  ASP B 775     193.581 216.504 187.580  1.00 24.31           C  
ATOM  11616  C   ASP B 775     194.474 217.013 186.482  1.00 24.13           C  
ATOM  11617  O   ASP B 775     194.145 216.904 185.302  1.00 25.05           O  
ATOM  11618  CB  ASP B 775     192.647 217.623 188.025  1.00 25.62           C  
ATOM  11619  CG  ASP B 775     191.482 217.148 188.848  1.00 26.53           C  
ATOM  11620  OD1 ASP B 775     190.794 216.252 188.412  1.00 27.11           O  
ATOM  11621  OD2 ASP B 775     191.249 217.698 189.892  1.00 26.77           O  
ATOM  11622  N   LYS B 776     195.621 217.556 186.865  1.00 24.05           N  
ATOM  11623  CA  LYS B 776     196.575 218.029 185.884  1.00 23.46           C  
ATOM  11624  C   LYS B 776     197.019 216.875 185.000  1.00 23.85           C  
ATOM  11625  O   LYS B 776     197.122 217.031 183.786  1.00 23.66           O  
ATOM  11626  CB  LYS B 776     197.777 218.670 186.560  1.00 23.62           C  
ATOM  11627  CG  LYS B 776     198.799 219.252 185.615  1.00 23.55           C  
ATOM  11628  CD  LYS B 776     199.927 219.900 186.395  1.00 23.85           C  
ATOM  11629  CE  LYS B 776     201.002 220.443 185.479  1.00 24.04           C  
ATOM  11630  NZ  LYS B 776     202.111 221.071 186.250  1.00 24.00           N  
ATOM  11631  N   ASN B 777     197.255 215.708 185.603  1.00 23.80           N  
ATOM  11632  CA  ASN B 777     197.689 214.550 184.835  1.00 23.62           C  
ATOM  11633  C   ASN B 777     196.646 214.148 183.812  1.00 24.00           C  
ATOM  11634  O   ASN B 777     196.967 213.919 182.646  1.00 24.09           O  
ATOM  11635  CB  ASN B 777     197.933 213.351 185.722  1.00 23.94           C  
ATOM  11636  CG  ASN B 777     199.132 213.420 186.569  1.00 23.65           C  
ATOM  11637  OD1 ASN B 777     199.991 214.300 186.457  1.00 23.75           O  
ATOM  11638  ND2 ASN B 777     199.217 212.453 187.436  1.00 23.73           N  
ATOM  11639  N   THR B 778     195.388 214.087 184.226  1.00 23.42           N  
ATOM  11640  CA  THR B 778     194.347 213.679 183.307  1.00 23.24           C  
ATOM  11641  C   THR B 778     194.212 214.697 182.192  1.00 23.63           C  
ATOM  11642  O   THR B 778     194.014 214.340 181.030  1.00 24.25           O  
ATOM  11643  CB  THR B 778     193.005 213.504 184.018  1.00 24.48           C  
ATOM  11644  OG1 THR B 778     193.139 212.549 185.066  1.00 25.01           O  
ATOM  11645  CG2 THR B 778     191.978 212.994 183.055  1.00 25.72           C  
ATOM  11646  N   GLN B 779     194.298 215.971 182.545  1.00 23.53           N  
ATOM  11647  CA  GLN B 779     194.156 217.037 181.573  1.00 22.76           C  
ATOM  11648  C   GLN B 779     195.245 216.954 180.510  1.00 23.06           C  
ATOM  11649  O   GLN B 779     194.957 217.023 179.319  1.00 23.77           O  
ATOM  11650  CB  GLN B 779     194.245 218.389 182.283  1.00 23.38           C  
ATOM  11651  CG  GLN B 779     193.922 219.606 181.444  1.00 23.01           C  
ATOM  11652  CD  GLN B 779     192.443 219.742 181.153  1.00 23.75           C  
ATOM  11653  OE1 GLN B 779     191.599 219.359 181.966  1.00 24.25           O  
ATOM  11654  NE2 GLN B 779     192.114 220.305 180.004  1.00 23.48           N  
ATOM  11655  N   GLU B 780     196.497 216.754 180.925  1.00 23.12           N  
ATOM  11656  CA  GLU B 780     197.597 216.679 179.967  1.00 22.57           C  
ATOM  11657  C   GLU B 780     197.532 215.455 179.070  1.00 22.70           C  
ATOM  11658  O   GLU B 780     197.920 215.525 177.902  1.00 22.86           O  
ATOM  11659  CB  GLU B 780     198.953 216.716 180.669  1.00 22.67           C  
ATOM  11660  CG  GLU B 780     199.310 218.066 181.265  1.00 23.07           C  
ATOM  11661  CD  GLU B 780     200.687 218.098 181.855  1.00 23.37           C  
ATOM  11662  OE1 GLU B 780     201.276 217.055 181.982  1.00 22.66           O  
ATOM  11663  OE2 GLU B 780     201.156 219.169 182.175  1.00 23.27           O  
ATOM  11664  N   VAL B 781     197.062 214.336 179.607  1.00 22.86           N  
ATOM  11665  CA  VAL B 781     196.970 213.125 178.812  1.00 22.35           C  
ATOM  11666  C   VAL B 781     195.836 213.164 177.809  1.00 22.85           C  
ATOM  11667  O   VAL B 781     196.018 212.729 176.681  1.00 23.26           O  
ATOM  11668  CB  VAL B 781     196.818 211.879 179.695  1.00 23.07           C  
ATOM  11669  CG1 VAL B 781     196.555 210.636 178.827  1.00 23.18           C  
ATOM  11670  CG2 VAL B 781     198.082 211.683 180.487  1.00 23.05           C  
ATOM  11671  N   PHE B 782     194.651 213.620 178.206  1.00 23.06           N  
ATOM  11672  CA  PHE B 782     193.518 213.547 177.289  1.00 22.86           C  
ATOM  11673  C   PHE B 782     193.155 214.828 176.552  1.00 22.67           C  
ATOM  11674  O   PHE B 782     192.685 214.771 175.418  1.00 23.26           O  
ATOM  11675  CB  PHE B 782     192.289 213.065 178.035  1.00 23.44           C  
ATOM  11676  CG  PHE B 782     192.403 211.675 178.489  1.00 23.75           C  
ATOM  11677  CD1 PHE B 782     192.758 211.394 179.778  1.00 24.29           C  
ATOM  11678  CD2 PHE B 782     192.152 210.641 177.630  1.00 24.00           C  
ATOM  11679  CE1 PHE B 782     192.856 210.103 180.212  1.00 24.69           C  
ATOM  11680  CE2 PHE B 782     192.248 209.345 178.056  1.00 24.45           C  
ATOM  11681  CZ  PHE B 782     192.598 209.078 179.352  1.00 25.09           C  
ATOM  11682  N   ALA B 783     193.336 215.988 177.164  1.00 22.86           N  
ATOM  11683  CA  ALA B 783     192.893 217.219 176.524  1.00 22.91           C  
ATOM  11684  C   ALA B 783     193.966 217.772 175.607  1.00 22.63           C  
ATOM  11685  O   ALA B 783     194.474 218.873 175.818  1.00 22.71           O  
ATOM  11686  CB  ALA B 783     192.522 218.255 177.563  1.00 23.42           C  
ATOM  11687  N   GLN B 784     194.311 217.007 174.582  1.00 22.68           N  
ATOM  11688  CA  GLN B 784     195.350 217.417 173.647  1.00 22.52           C  
ATOM  11689  C   GLN B 784     194.759 217.962 172.370  1.00 22.61           C  
ATOM  11690  O   GLN B 784     195.478 218.346 171.448  1.00 22.59           O  
ATOM  11691  CB  GLN B 784     196.287 216.261 173.335  1.00 22.31           C  
ATOM  11692  CG  GLN B 784     197.029 215.782 174.533  1.00 22.42           C  
ATOM  11693  CD  GLN B 784     198.063 214.767 174.210  1.00 21.85           C  
ATOM  11694  OE1 GLN B 784     198.230 214.341 173.063  1.00 21.54           O  
ATOM  11695  NE2 GLN B 784     198.783 214.370 175.237  1.00 22.02           N  
ATOM  11696  N   VAL B 785     193.445 217.983 172.313  1.00 22.69           N  
ATOM  11697  CA  VAL B 785     192.748 218.459 171.145  1.00 22.87           C  
ATOM  11698  C   VAL B 785     191.877 219.638 171.549  1.00 23.34           C  
ATOM  11699  O   VAL B 785     191.145 219.564 172.533  1.00 23.49           O  
ATOM  11700  CB  VAL B 785     191.924 217.306 170.542  1.00 22.73           C  
ATOM  11701  CG1 VAL B 785     190.869 216.797 171.530  1.00 22.81           C  
ATOM  11702  CG2 VAL B 785     191.303 217.752 169.283  1.00 22.93           C  
ATOM  11703  N   LYS B 786     191.961 220.732 170.799  1.00 23.52           N  
ATOM  11704  CA  LYS B 786     191.189 221.924 171.132  1.00 23.72           C  
ATOM  11705  C   LYS B 786     189.724 221.804 170.761  1.00 24.10           C  
ATOM  11706  O   LYS B 786     188.863 222.394 171.411  1.00 24.46           O  
ATOM  11707  CB  LYS B 786     191.773 223.159 170.457  1.00 23.81           C  
ATOM  11708  N   GLN B 787     189.442 221.074 169.698  1.00 23.71           N  
ATOM  11709  CA  GLN B 787     188.078 220.942 169.222  1.00 23.15           C  
ATOM  11710  C   GLN B 787     187.564 219.535 169.419  1.00 23.55           C  
ATOM  11711  O   GLN B 787     188.331 218.577 169.461  1.00 24.48           O  
ATOM  11712  CB  GLN B 787     187.997 221.320 167.753  1.00 23.73           C  
ATOM  11713  CG  GLN B 787     188.372 222.750 167.474  1.00 23.81           C  
ATOM  11714  CD  GLN B 787     188.289 223.072 166.010  1.00 23.96           C  
ATOM  11715  OE1 GLN B 787     188.599 222.225 165.163  1.00 23.98           O  
ATOM  11716  NE2 GLN B 787     187.880 224.294 165.692  1.00 23.21           N  
ATOM  11717  N   ILE B 788     186.259 219.400 169.507  1.00 24.07           N  
ATOM  11718  CA  ILE B 788     185.683 218.081 169.606  1.00 23.99           C  
ATOM  11719  C   ILE B 788     185.223 217.619 168.243  1.00 24.37           C  
ATOM  11720  O   ILE B 788     184.252 218.133 167.686  1.00 25.18           O  
ATOM  11721  CB  ILE B 788     184.521 218.066 170.610  1.00 24.62           C  
ATOM  11722  CG1 ILE B 788     185.009 218.595 171.991  1.00 25.11           C  
ATOM  11723  CG2 ILE B 788     183.908 216.676 170.716  1.00 25.87           C  
ATOM  11724  CD1 ILE B 788     186.181 217.824 172.620  1.00 25.17           C  
ATOM  11725  N   TYR B 789     185.938 216.644 167.711  1.00 23.92           N  
ATOM  11726  CA  TYR B 789     185.678 216.126 166.387  1.00 23.13           C  
ATOM  11727  C   TYR B 789     184.710 214.978 166.492  1.00 23.67           C  
ATOM  11728  O   TYR B 789     184.669 214.282 167.504  1.00 24.52           O  
ATOM  11729  CB  TYR B 789     186.970 215.657 165.721  1.00 23.31           C  
ATOM  11730  CG  TYR B 789     187.968 216.747 165.530  1.00 22.82           C  
ATOM  11731  CD1 TYR B 789     189.136 216.721 166.239  1.00 22.94           C  
ATOM  11732  CD2 TYR B 789     187.713 217.783 164.676  1.00 23.15           C  
ATOM  11733  CE1 TYR B 789     190.043 217.726 166.087  1.00 22.85           C  
ATOM  11734  CE2 TYR B 789     188.617 218.795 164.532  1.00 22.99           C  
ATOM  11735  CZ  TYR B 789     189.783 218.764 165.238  1.00 22.87           C  
ATOM  11736  OH  TYR B 789     190.702 219.775 165.114  1.00 22.66           O  
ATOM  11737  N   LYS B 790     183.929 214.784 165.453  1.00 24.00           N  
ATOM  11738  CA  LYS B 790     183.002 213.676 165.401  1.00 24.56           C  
ATOM  11739  C   LYS B 790     183.081 213.027 164.045  1.00 24.59           C  
ATOM  11740  O   LYS B 790     183.284 213.715 163.044  1.00 24.30           O  
ATOM  11741  CB  LYS B 790     181.584 214.161 165.654  1.00 24.73           C  
ATOM  11742  CG  LYS B 790     181.365 214.760 167.017  1.00 25.15           C  
ATOM  11743  CD  LYS B 790     179.932 215.180 167.187  1.00 25.11           C  
ATOM  11744  CE  LYS B 790     179.695 215.805 168.541  1.00 25.06           C  
ATOM  11745  NZ  LYS B 790     178.305 216.301 168.666  1.00 24.50           N  
ATOM  11746  N   THR B 791     182.890 211.720 163.991  1.00 24.73           N  
ATOM  11747  CA  THR B 791     182.824 211.064 162.704  1.00 24.57           C  
ATOM  11748  C   THR B 791     181.446 211.322 162.118  1.00 24.64           C  
ATOM  11749  O   THR B 791     180.502 211.564 162.868  1.00 24.42           O  
ATOM  11750  CB  THR B 791     183.062 209.551 162.853  1.00 24.80           C  
ATOM  11751  OG1 THR B 791     182.088 209.019 163.754  1.00 25.12           O  
ATOM  11752  CG2 THR B 791     184.467 209.275 163.367  1.00 24.74           C  
ATOM  11753  N   PRO B 792     181.298 211.253 160.800  1.00 24.59           N  
ATOM  11754  CA  PRO B 792     180.056 211.335 160.071  1.00 24.58           C  
ATOM  11755  C   PRO B 792     179.269 210.048 160.245  1.00 24.65           C  
ATOM  11756  O   PRO B 792     179.812 209.058 160.743  1.00 25.20           O  
ATOM  11757  CB  PRO B 792     180.542 211.537 158.631  1.00 24.46           C  
ATOM  11758  CG  PRO B 792     181.867 210.863 158.591  1.00 24.23           C  
ATOM  11759  CD  PRO B 792     182.485 211.141 159.939  1.00 24.29           C  
ATOM  11760  N   PRO B 793     177.993 210.038 159.846  1.00 24.38           N  
ATOM  11761  CA  PRO B 793     177.131 208.875 159.745  1.00 24.66           C  
ATOM  11762  C   PRO B 793     177.687 207.884 158.726  1.00 25.12           C  
ATOM  11763  O   PRO B 793     177.362 206.698 158.757  1.00 24.76           O  
ATOM  11764  CB  PRO B 793     175.793 209.486 159.308  1.00 25.22           C  
ATOM  11765  CG  PRO B 793     176.155 210.821 158.687  1.00 24.78           C  
ATOM  11766  CD  PRO B 793     177.342 211.304 159.476  1.00 24.40           C  
ATOM  11767  N   ILE B 794     178.544 208.379 157.843  1.00 24.88           N  
ATOM  11768  CA  ILE B 794     179.193 207.572 156.830  1.00 24.66           C  
ATOM  11769  C   ILE B 794     180.378 206.843 157.437  1.00 24.43           C  
ATOM  11770  O   ILE B 794     181.297 207.463 157.962  1.00 24.12           O  
ATOM  11771  CB  ILE B 794     179.663 208.475 155.674  1.00 24.75           C  
ATOM  11772  N   LYS B 795     180.372 205.523 157.339  1.00 24.33           N  
ATOM  11773  CA  LYS B 795     181.426 204.719 157.939  1.00 24.54           C  
ATOM  11774  C   LYS B 795     182.337 204.116 156.888  1.00 24.72           C  
ATOM  11775  O   LYS B 795     183.072 203.158 157.144  1.00 23.87           O  
ATOM  11776  CB  LYS B 795     180.829 203.640 158.837  1.00 24.66           C  
ATOM  11777  CG  LYS B 795     179.973 204.194 159.985  1.00 24.77           C  
ATOM  11778  CD  LYS B 795     180.799 205.050 160.959  1.00 24.88           C  
ATOM  11779  CE  LYS B 795     179.980 205.484 162.158  1.00 25.16           C  
ATOM  11780  NZ  LYS B 795     178.932 206.470 161.783  1.00 24.71           N  
ATOM  11781  N   ASP B 796     182.293 204.667 155.690  1.00 24.01           N  
ATOM  11782  CA  ASP B 796     183.122 204.129 154.640  1.00 23.87           C  
ATOM  11783  C   ASP B 796     184.546 204.621 154.783  1.00 23.67           C  
ATOM  11784  O   ASP B 796     184.919 205.692 154.299  1.00 23.39           O  
ATOM  11785  CB  ASP B 796     182.602 204.498 153.260  1.00 23.70           C  
ATOM  11786  N   PHE B 797     185.337 203.806 155.452  1.00 23.40           N  
ATOM  11787  CA  PHE B 797     186.732 204.092 155.696  1.00 22.91           C  
ATOM  11788  C   PHE B 797     187.600 203.152 154.883  1.00 23.02           C  
ATOM  11789  O   PHE B 797     188.738 202.871 155.245  1.00 23.38           O  
ATOM  11790  CB  PHE B 797     187.057 203.991 157.180  1.00 23.08           C  
ATOM  11791  CG  PHE B 797     186.288 204.964 158.001  1.00 22.84           C  
ATOM  11792  CD1 PHE B 797     185.341 204.531 158.889  1.00 23.70           C  
ATOM  11793  CD2 PHE B 797     186.495 206.316 157.869  1.00 22.85           C  
ATOM  11794  CE1 PHE B 797     184.619 205.427 159.639  1.00 23.93           C  
ATOM  11795  CE2 PHE B 797     185.772 207.216 158.609  1.00 23.12           C  
ATOM  11796  CZ  PHE B 797     184.832 206.771 159.497  1.00 23.76           C  
ATOM  11797  N   GLY B 798     187.059 202.657 153.773  1.00 23.20           N  
ATOM  11798  CA  GLY B 798     187.831 201.799 152.889  1.00 22.77           C  
ATOM  11799  C   GLY B 798     187.870 200.345 153.331  1.00 23.16           C  
ATOM  11800  O   GLY B 798     188.780 199.609 152.954  1.00 23.16           O  
ATOM  11801  N   GLY B 799     186.890 199.926 154.124  1.00 23.37           N  
ATOM  11802  CA  GLY B 799     186.835 198.548 154.599  1.00 23.58           C  
ATOM  11803  C   GLY B 799     187.305 198.401 156.036  1.00 23.78           C  
ATOM  11804  O   GLY B 799     187.152 197.337 156.636  1.00 24.09           O  
ATOM  11805  N   PHE B 800     187.850 199.469 156.594  1.00 23.70           N  
ATOM  11806  CA  PHE B 800     188.316 199.442 157.972  1.00 23.26           C  
ATOM  11807  C   PHE B 800     187.145 199.696 158.915  1.00 24.18           C  
ATOM  11808  O   PHE B 800     186.484 200.731 158.822  1.00 24.61           O  
ATOM  11809  CB  PHE B 800     189.387 200.500 158.180  1.00 23.19           C  
ATOM  11810  CG  PHE B 800     190.665 200.184 157.500  1.00 22.74           C  
ATOM  11811  CD1 PHE B 800     190.831 200.447 156.159  1.00 23.03           C  
ATOM  11812  CD2 PHE B 800     191.714 199.640 158.198  1.00 22.69           C  
ATOM  11813  CE1 PHE B 800     192.010 200.168 155.530  1.00 22.46           C  
ATOM  11814  CE2 PHE B 800     192.899 199.359 157.574  1.00 22.42           C  
ATOM  11815  CZ  PHE B 800     193.044 199.625 156.233  1.00 22.16           C  
ATOM  11816  N   ASN B 801     186.880 198.729 159.800  1.00 25.11           N  
ATOM  11817  CA  ASN B 801     185.765 198.744 160.741  1.00 25.48           C  
ATOM  11818  C   ASN B 801     186.209 199.276 162.109  1.00 25.62           C  
ATOM  11819  O   ASN B 801     186.893 198.582 162.864  1.00 25.64           O  
ATOM  11820  CB  ASN B 801     185.159 197.345 160.851  1.00 26.77           C  
ATOM  11821  CG  ASN B 801     183.858 197.272 161.657  1.00 28.03           C  
ATOM  11822  OD1 ASN B 801     183.473 198.233 162.357  1.00 28.34           O  
ATOM  11823  ND2 ASN B 801     183.187 196.127 161.563  1.00 29.07           N  
ATOM  11824  N   PHE B 802     185.812 200.517 162.426  1.00 25.87           N  
ATOM  11825  CA  PHE B 802     186.182 201.198 163.668  1.00 25.75           C  
ATOM  11826  C   PHE B 802     185.016 201.264 164.638  1.00 26.98           C  
ATOM  11827  O   PHE B 802     185.098 201.944 165.660  1.00 27.69           O  
ATOM  11828  CB  PHE B 802     186.643 202.622 163.387  1.00 25.17           C  
ATOM  11829  CG  PHE B 802     187.833 202.714 162.535  1.00 24.30           C  
ATOM  11830  CD1 PHE B 802     187.769 203.337 161.322  1.00 23.94           C  
ATOM  11831  CD2 PHE B 802     189.019 202.177 162.934  1.00 24.16           C  
ATOM  11832  CE1 PHE B 802     188.873 203.426 160.535  1.00 23.71           C  
ATOM  11833  CE2 PHE B 802     190.116 202.266 162.149  1.00 23.43           C  
ATOM  11834  CZ  PHE B 802     190.043 202.886 160.957  1.00 23.12           C  
ATOM  11835  N   SER B 803     183.934 200.555 164.344  1.00 26.86           N  
ATOM  11836  CA  SER B 803     182.737 200.673 165.174  1.00 27.16           C  
ATOM  11837  C   SER B 803     182.928 200.139 166.584  1.00 27.63           C  
ATOM  11838  O   SER B 803     182.127 200.424 167.471  1.00 27.97           O  
ATOM  11839  CB  SER B 803     181.568 199.958 164.543  1.00 27.94           C  
ATOM  11840  OG  SER B 803     181.764 198.582 164.561  1.00 28.50           O  
ATOM  11841  N   GLN B 804     183.980 199.363 166.803  1.00 27.48           N  
ATOM  11842  CA  GLN B 804     184.224 198.787 168.113  1.00 27.67           C  
ATOM  11843  C   GLN B 804     185.108 199.674 168.982  1.00 27.65           C  
ATOM  11844  O   GLN B 804     185.299 199.398 170.172  1.00 28.38           O  
ATOM  11845  CB  GLN B 804     184.842 197.413 167.945  1.00 28.08           C  
ATOM  11846  CG  GLN B 804     183.959 196.469 167.136  1.00 28.74           C  
ATOM  11847  CD  GLN B 804     182.567 196.309 167.734  1.00 29.34           C  
ATOM  11848  OE1 GLN B 804     182.408 195.805 168.843  1.00 28.91           O  
ATOM  11849  NE2 GLN B 804     181.550 196.753 167.008  1.00 29.92           N  
ATOM  11850  N   ILE B 805     185.656 200.738 168.390  1.00 27.25           N  
ATOM  11851  CA  ILE B 805     186.476 201.680 169.142  1.00 26.80           C  
ATOM  11852  C   ILE B 805     185.826 203.062 169.187  1.00 27.07           C  
ATOM  11853  O   ILE B 805     186.159 203.881 170.047  1.00 27.68           O  
ATOM  11854  CB  ILE B 805     187.918 201.742 168.608  1.00 26.91           C  
ATOM  11855  CG1 ILE B 805     187.955 202.189 167.159  1.00 26.39           C  
ATOM  11856  CG2 ILE B 805     188.561 200.394 168.783  1.00 27.08           C  
ATOM  11857  CD1 ILE B 805     189.339 202.539 166.682  1.00 24.81           C  
ATOM  11858  N   LEU B 806     184.865 203.299 168.293  1.00 27.28           N  
ATOM  11859  CA  LEU B 806     184.079 204.523 168.295  1.00 27.68           C  
ATOM  11860  C   LEU B 806     182.965 204.411 169.332  1.00 28.59           C  
ATOM  11861  O   LEU B 806     182.504 203.305 169.612  1.00 29.32           O  
ATOM  11862  CB  LEU B 806     183.489 204.777 166.901  1.00 27.72           C  
ATOM  11863  CG  LEU B 806     184.494 205.114 165.790  1.00 26.78           C  
ATOM  11864  CD1 LEU B 806     183.811 205.036 164.441  1.00 26.40           C  
ATOM  11865  CD2 LEU B 806     185.015 206.525 165.999  1.00 26.18           C  
ATOM  11866  N   PRO B 807     182.517 205.516 169.932  1.00 29.21           N  
ATOM  11867  CA  PRO B 807     181.439 205.573 170.896  1.00 30.20           C  
ATOM  11868  C   PRO B 807     180.159 204.981 170.365  1.00 30.81           C  
ATOM  11869  O   PRO B 807     179.796 205.224 169.214  1.00 31.38           O  
ATOM  11870  CB  PRO B 807     181.265 207.071 171.110  1.00 30.27           C  
ATOM  11871  CG  PRO B 807     182.594 207.656 170.797  1.00 29.49           C  
ATOM  11872  CD  PRO B 807     183.147 206.814 169.671  1.00 28.75           C  
ATOM  11873  N   ASP B 808     179.452 204.247 171.216  1.00 32.12           N  
ATOM  11874  CA  ASP B 808     178.163 203.682 170.867  1.00 32.44           C  
ATOM  11875  C   ASP B 808     177.063 204.673 171.258  1.00 33.46           C  
ATOM  11876  O   ASP B 808     176.835 204.894 172.449  1.00 33.76           O  
ATOM  11877  CB  ASP B 808     177.957 202.344 171.572  1.00 33.47           C  
ATOM  11878  CG  ASP B 808     176.655 201.666 171.191  1.00 33.93           C  
ATOM  11879  OD1 ASP B 808     175.746 202.346 170.735  1.00 34.35           O  
ATOM  11880  OD2 ASP B 808     176.572 200.468 171.341  1.00 34.26           O  
ATOM  11881  N   PRO B 809     176.387 205.310 170.294  1.00 34.50           N  
ATOM  11882  CA  PRO B 809     175.446 206.394 170.491  1.00 34.27           C  
ATOM  11883  C   PRO B 809     174.167 205.956 171.192  1.00 34.95           C  
ATOM  11884  O   PRO B 809     173.399 206.797 171.662  1.00 34.80           O  
ATOM  11885  CB  PRO B 809     175.162 206.852 169.054  1.00 34.86           C  
ATOM  11886  CG  PRO B 809     175.401 205.628 168.203  1.00 34.69           C  
ATOM  11887  CD  PRO B 809     176.530 204.886 168.887  1.00 34.12           C  
ATOM  11888  N   SER B 810     173.921 204.646 171.248  1.00 34.35           N  
ATOM  11889  CA  SER B 810     172.680 204.146 171.825  1.00 34.76           C  
ATOM  11890  C   SER B 810     172.738 203.983 173.339  1.00 35.15           C  
ATOM  11891  O   SER B 810     171.718 203.712 173.975  1.00 34.80           O  
ATOM  11892  CB  SER B 810     172.302 202.818 171.197  1.00 34.89           C  
ATOM  11893  OG  SER B 810     173.161 201.794 171.610  1.00 34.67           O  
ATOM  11894  N   LYS B 811     173.924 204.111 173.922  1.00 34.16           N  
ATOM  11895  CA  LYS B 811     174.063 203.876 175.354  1.00 35.36           C  
ATOM  11896  C   LYS B 811     173.910 205.151 176.204  1.00 35.54           C  
ATOM  11897  O   LYS B 811     174.084 206.259 175.696  1.00 34.07           O  
ATOM  11898  CB  LYS B 811     175.395 203.196 175.637  1.00 34.03           C  
ATOM  11899  CG  LYS B 811     175.470 201.787 175.095  1.00 34.36           C  
ATOM  11900  CD  LYS B 811     176.736 201.103 175.542  1.00 33.46           C  
ATOM  11901  CE  LYS B 811     176.811 199.682 175.029  1.00 33.54           C  
ATOM  11902  NZ  LYS B 811     178.018 198.993 175.533  1.00 32.08           N  
ATOM  11903  N   SER B 813     175.931 206.111 178.337  1.00 34.46           N  
ATOM  11904  CA  SER B 813     177.272 206.660 178.431  1.00 33.65           C  
ATOM  11905  C   SER B 813     177.922 206.401 177.092  1.00 33.86           C  
ATOM  11906  O   SER B 813     177.985 205.256 176.638  1.00 33.19           O  
ATOM  11907  CB  SER B 813     178.053 206.003 179.546  1.00 33.03           C  
ATOM  11908  OG  SER B 813     179.338 206.544 179.635  1.00 31.90           O  
ATOM  11909  N   LYS B 814     178.362 207.461 176.431  1.00 33.17           N  
ATOM  11910  CA  LYS B 814     178.813 207.332 175.055  1.00 32.40           C  
ATOM  11911  C   LYS B 814     180.221 206.780 174.960  1.00 31.82           C  
ATOM  11912  O   LYS B 814     181.173 207.503 174.671  1.00 30.81           O  
ATOM  11913  CB  LYS B 814     178.740 208.685 174.350  1.00 33.24           C  
ATOM  11914  N   ARG B 815     180.336 205.481 175.189  1.00 31.35           N  
ATOM  11915  CA  ARG B 815     181.614 204.795 175.180  1.00 30.31           C  
ATOM  11916  C   ARG B 815     181.573 203.677 174.157  1.00 30.40           C  
ATOM  11917  O   ARG B 815     180.500 203.231 173.755  1.00 31.38           O  
ATOM  11918  CB  ARG B 815     181.930 204.240 176.555  1.00 30.55           C  
ATOM  11919  CG  ARG B 815     181.994 205.291 177.628  1.00 30.82           C  
ATOM  11920  CD  ARG B 815     182.651 204.822 178.873  1.00 30.01           C  
ATOM  11921  NE  ARG B 815     181.994 203.656 179.449  1.00 30.04           N  
ATOM  11922  CZ  ARG B 815     181.948 203.357 180.761  1.00 29.77           C  
ATOM  11923  NH1 ARG B 815     182.483 204.156 181.662  1.00 29.31           N  
ATOM  11924  NH2 ARG B 815     181.347 202.244 181.127  1.00 29.62           N  
ATOM  11925  N   SER B 816     182.733 203.265 173.685  1.00 29.29           N  
ATOM  11926  CA  SER B 816     182.823 202.210 172.691  1.00 28.36           C  
ATOM  11927  C   SER B 816     182.697 200.852 173.340  1.00 28.28           C  
ATOM  11928  O   SER B 816     182.743 200.736 174.564  1.00 30.20           O  
ATOM  11929  CB  SER B 816     184.134 202.291 171.971  1.00 29.57           C  
ATOM  11930  OG  SER B 816     185.175 201.832 172.775  1.00 29.17           O  
ATOM  11931  N   PHE B 817     182.552 199.812 172.525  1.00 28.52           N  
ATOM  11932  CA  PHE B 817     182.449 198.464 173.064  1.00 28.43           C  
ATOM  11933  C   PHE B 817     183.683 198.136 173.890  1.00 29.34           C  
ATOM  11934  O   PHE B 817     183.578 197.667 175.024  1.00 28.84           O  
ATOM  11935  CB  PHE B 817     182.312 197.443 171.946  1.00 28.59           C  
ATOM  11936  CG  PHE B 817     182.081 196.056 172.434  1.00 28.42           C  
ATOM  11937  CD1 PHE B 817     180.796 195.591 172.591  1.00 28.18           C  
ATOM  11938  CD2 PHE B 817     183.128 195.218 172.748  1.00 28.54           C  
ATOM  11939  CE1 PHE B 817     180.562 194.316 173.040  1.00 28.66           C  
ATOM  11940  CE2 PHE B 817     182.897 193.942 173.193  1.00 28.84           C  
ATOM  11941  CZ  PHE B 817     181.615 193.491 173.339  1.00 29.43           C  
ATOM  11942  N   ILE B 818     184.859 198.401 173.330  1.00 28.08           N  
ATOM  11943  CA  ILE B 818     186.086 198.129 174.056  1.00 27.97           C  
ATOM  11944  C   ILE B 818     186.210 198.948 175.329  1.00 30.41           C  
ATOM  11945  O   ILE B 818     186.616 198.415 176.359  1.00 29.73           O  
ATOM  11946  CB  ILE B 818     187.318 198.276 173.157  1.00 28.20           C  
ATOM  11947  CG1 ILE B 818     187.313 197.103 172.159  1.00 28.19           C  
ATOM  11948  CG2 ILE B 818     188.599 198.321 173.996  1.00 28.12           C  
ATOM  11949  CD1 ILE B 818     188.282 197.216 171.021  1.00 28.05           C  
ATOM  11950  N   GLU B 819     185.850 200.221 175.297  1.00 28.52           N  
ATOM  11951  CA  GLU B 819     185.952 201.003 176.518  1.00 28.11           C  
ATOM  11952  C   GLU B 819     185.109 200.396 177.629  1.00 30.30           C  
ATOM  11953  O   GLU B 819     185.575 200.279 178.763  1.00 29.43           O  
ATOM  11954  CB  GLU B 819     185.532 202.442 176.272  1.00 28.72           C  
ATOM  11955  CG  GLU B 819     186.521 203.234 175.470  1.00 28.30           C  
ATOM  11956  CD  GLU B 819     186.049 204.602 175.144  1.00 28.54           C  
ATOM  11957  OE1 GLU B 819     184.962 204.758 174.642  1.00 29.36           O  
ATOM  11958  OE2 GLU B 819     186.784 205.517 175.414  1.00 27.97           O  
ATOM  11959  N   ASP B 820     183.906 199.923 177.311  1.00 28.84           N  
ATOM  11960  CA  ASP B 820     183.102 199.278 178.342  1.00 28.85           C  
ATOM  11961  C   ASP B 820     183.806 198.061 178.915  1.00 30.33           C  
ATOM  11962  O   ASP B 820     183.748 197.825 180.123  1.00 30.41           O  
ATOM  11963  CB  ASP B 820     181.736 198.857 177.814  1.00 29.98           C  
ATOM  11964  CG  ASP B 820     180.727 199.992 177.693  1.00 30.64           C  
ATOM  11965  OD1 ASP B 820     180.881 201.013 178.338  1.00 30.28           O  
ATOM  11966  OD2 ASP B 820     179.779 199.812 176.955  1.00 31.21           O  
ATOM  11967  N   LEU B 821     184.508 197.307 178.073  1.00 28.93           N  
ATOM  11968  CA  LEU B 821     185.224 196.149 178.585  1.00 29.10           C  
ATOM  11969  C   LEU B 821     186.298 196.588 179.558  1.00 29.11           C  
ATOM  11970  O   LEU B 821     186.537 195.926 180.562  1.00 30.53           O  
ATOM  11971  CB  LEU B 821     185.928 195.360 177.473  1.00 29.25           C  
ATOM  11972  CG  LEU B 821     185.077 194.625 176.449  1.00 29.14           C  
ATOM  11973  CD1 LEU B 821     186.017 194.047 175.389  1.00 29.38           C  
ATOM  11974  CD2 LEU B 821     184.280 193.522 177.117  1.00 30.21           C  
ATOM  11975  N   LEU B 822     186.955 197.702 179.270  1.00 28.87           N  
ATOM  11976  CA  LEU B 822     188.039 198.146 180.131  1.00 28.84           C  
ATOM  11977  C   LEU B 822     187.503 198.548 181.498  1.00 29.44           C  
ATOM  11978  O   LEU B 822     188.062 198.183 182.531  1.00 30.32           O  
ATOM  11979  CB  LEU B 822     188.762 199.335 179.482  1.00 28.76           C  
ATOM  11980  CG  LEU B 822     189.514 199.044 178.154  1.00 28.66           C  
ATOM  11981  CD1 LEU B 822     189.977 200.350 177.546  1.00 27.74           C  
ATOM  11982  CD2 LEU B 822     190.690 198.138 178.403  1.00 29.35           C  
ATOM  11983  N   PHE B 823     186.379 199.246 181.519  1.00 28.58           N  
ATOM  11984  CA  PHE B 823     185.811 199.693 182.784  1.00 28.73           C  
ATOM  11985  C   PHE B 823     185.288 198.542 183.615  1.00 29.35           C  
ATOM  11986  O   PHE B 823     185.431 198.527 184.837  1.00 30.02           O  
ATOM  11987  CB  PHE B 823     184.709 200.719 182.549  1.00 28.76           C  
ATOM  11988  CG  PHE B 823     185.236 202.109 182.371  1.00 28.66           C  
ATOM  11989  CD1 PHE B 823     185.558 202.604 181.125  1.00 28.88           C  
ATOM  11990  CD2 PHE B 823     185.414 202.930 183.466  1.00 28.53           C  
ATOM  11991  CE1 PHE B 823     186.051 203.878 180.978  1.00 28.11           C  
ATOM  11992  CE2 PHE B 823     185.903 204.207 183.320  1.00 27.93           C  
ATOM  11993  CZ  PHE B 823     186.223 204.680 182.074  1.00 27.69           C  
ATOM  11994  N   ASN B 824     184.725 197.549 182.959  1.00 29.69           N  
ATOM  11995  CA  ASN B 824     184.106 196.444 183.663  1.00 29.85           C  
ATOM  11996  C   ASN B 824     185.114 195.449 184.225  1.00 29.83           C  
ATOM  11997  O   ASN B 824     184.723 194.478 184.872  1.00 30.53           O  
ATOM  11998  CB  ASN B 824     183.131 195.742 182.748  1.00 30.17           C  
ATOM  11999  CG  ASN B 824     181.942 196.599 182.424  1.00 30.77           C  
ATOM  12000  OD1 ASN B 824     181.577 197.505 183.183  1.00 30.72           O  
ATOM  12001  ND2 ASN B 824     181.325 196.332 181.304  1.00 30.93           N  
ATOM  12002  N   LYS B 825     186.403 195.658 183.965  1.00 29.59           N  
ATOM  12003  CA  LYS B 825     187.412 194.734 184.461  1.00 29.82           C  
ATOM  12004  C   LYS B 825     188.272 195.338 185.560  1.00 29.96           C  
ATOM  12005  O   LYS B 825     189.241 194.716 185.995  1.00 29.89           O  
ATOM  12006  CB  LYS B 825     188.283 194.232 183.309  1.00 29.94           C  
ATOM  12007  CG  LYS B 825     187.506 193.480 182.221  1.00 30.19           C  
ATOM  12008  CD  LYS B 825     186.941 192.149 182.693  1.00 30.74           C  
ATOM  12009  CE  LYS B 825     186.106 191.510 181.598  1.00 30.87           C  
ATOM  12010  NZ  LYS B 825     185.504 190.215 182.025  1.00 30.62           N  
ATOM  12011  N   VAL B 826     187.927 196.539 186.024  1.00 29.77           N  
ATOM  12012  CA  VAL B 826     188.700 197.167 187.096  1.00 29.53           C  
ATOM  12013  C   VAL B 826     187.797 197.511 188.284  1.00 29.84           C  
ATOM  12014  O   VAL B 826     186.749 198.131 188.105  1.00 29.85           O  
ATOM  12015  CB  VAL B 826     189.407 198.435 186.588  1.00 29.16           C  
ATOM  12016  CG1 VAL B 826     190.217 199.101 187.708  1.00 29.03           C  
ATOM  12017  CG2 VAL B 826     190.312 198.069 185.443  1.00 28.68           C  
ATOM  12018  N   THR B 827     188.212 197.103 189.497  1.00 29.83           N  
ATOM  12019  CA  THR B 827     187.471 197.334 190.737  1.00 30.00           C  
ATOM  12020  C   THR B 827     187.901 198.679 191.336  1.00 29.87           C  
ATOM  12021  O   THR B 827     187.124 199.353 192.016  1.00 29.41           O  
ATOM  12022  CB  THR B 827     187.694 196.150 191.736  1.00 29.93           C  
ATOM  12023  OG1 THR B 827     187.221 194.934 191.131  1.00 29.25           O  
ATOM  12024  CG2 THR B 827     186.929 196.358 193.095  1.00 29.20           C  
ATOM  12025  N   LYS B 854     186.347 206.296 206.727  1.00 37.39           N  
ATOM  12026  CA  LYS B 854     185.034 206.725 206.247  1.00 39.43           C  
ATOM  12027  C   LYS B 854     184.513 207.877 207.119  1.00 39.45           C  
ATOM  12028  O   LYS B 854     184.212 208.963 206.614  1.00 39.10           O  
ATOM  12029  CB  LYS B 854     184.048 205.523 206.208  1.00 41.15           C  
ATOM  12030  CG  LYS B 854     182.614 205.827 205.625  1.00 41.81           C  
ATOM  12031  CD  LYS B 854     181.735 204.532 205.497  1.00 42.19           C  
ATOM  12032  CE  LYS B 854     180.320 204.833 204.912  1.00 43.73           C  
ATOM  12033  NZ  LYS B 854     179.491 203.587 204.750  1.00 45.23           N  
ATOM  12034  N   PHE B 855     184.430 207.630 208.434  1.00 39.55           N  
ATOM  12035  CA  PHE B 855     184.012 208.598 209.450  1.00 39.54           C  
ATOM  12036  C   PHE B 855     185.217 209.030 210.262  1.00 38.66           C  
ATOM  12037  O   PHE B 855     185.080 209.566 211.358  1.00 38.68           O  
ATOM  12038  CB  PHE B 855     182.978 207.989 210.384  1.00 41.39           C  
ATOM  12039  CG  PHE B 855     181.695 207.603 209.722  1.00 42.28           C  
ATOM  12040  CD1 PHE B 855     181.478 206.304 209.316  1.00 42.59           C  
ATOM  12041  CD2 PHE B 855     180.691 208.532 209.526  1.00 43.48           C  
ATOM  12042  CE1 PHE B 855     180.289 205.943 208.723  1.00 43.53           C  
ATOM  12043  CE2 PHE B 855     179.503 208.178 208.935  1.00 44.87           C  
ATOM  12044  CZ  PHE B 855     179.301 206.880 208.531  1.00 44.67           C  
ATOM  12045  N   ASN B 856     186.403 208.759 209.730  1.00 37.26           N  
ATOM  12046  CA  ASN B 856     187.654 209.044 210.419  1.00 36.38           C  
ATOM  12047  C   ASN B 856     188.414 210.217 209.814  1.00 34.84           C  
ATOM  12048  O   ASN B 856     189.623 210.333 209.989  1.00 34.24           O  
ATOM  12049  CB  ASN B 856     188.520 207.807 210.424  1.00 36.01           C  
ATOM  12050  CG  ASN B 856     187.920 206.711 211.239  1.00 37.51           C  
ATOM  12051  OD1 ASN B 856     187.816 206.820 212.464  1.00 38.19           O  
ATOM  12052  ND2 ASN B 856     187.519 205.651 210.587  1.00 37.98           N  
ATOM  12053  N   GLY B 857     187.717 211.069 209.072  1.00 35.58           N  
ATOM  12054  CA  GLY B 857     188.343 212.235 208.455  1.00 33.67           C  
ATOM  12055  C   GLY B 857     188.922 211.913 207.086  1.00 32.20           C  
ATOM  12056  O   GLY B 857     189.557 212.757 206.457  1.00 31.79           O  
ATOM  12057  N   LEU B 858     188.699 210.688 206.631  1.00 33.16           N  
ATOM  12058  CA  LEU B 858     189.218 210.208 205.357  1.00 31.92           C  
ATOM  12059  C   LEU B 858     188.150 210.271 204.289  1.00 32.12           C  
ATOM  12060  O   LEU B 858     187.186 209.507 204.326  1.00 32.72           O  
ATOM  12061  CB  LEU B 858     189.675 208.751 205.490  1.00 32.60           C  
ATOM  12062  CG  LEU B 858     191.064 208.473 206.093  1.00 32.54           C  
ATOM  12063  CD1 LEU B 858     191.213 209.127 207.446  1.00 32.83           C  
ATOM  12064  CD2 LEU B 858     191.210 206.990 206.244  1.00 32.77           C  
ATOM  12065  N   THR B 859     188.321 211.172 203.334  1.00 31.33           N  
ATOM  12066  CA  THR B 859     187.320 211.373 202.302  1.00 30.98           C  
ATOM  12067  C   THR B 859     187.947 211.315 200.921  1.00 30.52           C  
ATOM  12068  O   THR B 859     189.168 211.402 200.776  1.00 30.46           O  
ATOM  12069  CB  THR B 859     186.626 212.729 202.488  1.00 31.54           C  
ATOM  12070  OG1 THR B 859     187.572 213.775 202.251  1.00 31.14           O  
ATOM  12071  CG2 THR B 859     186.066 212.867 203.906  1.00 33.21           C  
ATOM  12072  N   VAL B 860     187.108 211.177 199.901  1.00 30.37           N  
ATOM  12073  CA  VAL B 860     187.582 211.178 198.527  1.00 29.69           C  
ATOM  12074  C   VAL B 860     186.893 212.237 197.691  1.00 30.00           C  
ATOM  12075  O   VAL B 860     185.667 212.322 197.656  1.00 30.32           O  
ATOM  12076  CB  VAL B 860     187.386 209.798 197.890  1.00 29.60           C  
ATOM  12077  CG1 VAL B 860     187.801 209.839 196.439  1.00 29.75           C  
ATOM  12078  CG2 VAL B 860     188.226 208.780 198.648  1.00 29.64           C  
ATOM  12079  N   LEU B 861     187.695 213.039 197.013  1.00 29.44           N  
ATOM  12080  CA  LEU B 861     187.188 214.083 196.155  1.00 29.32           C  
ATOM  12081  C   LEU B 861     187.015 213.503 194.760  1.00 29.33           C  
ATOM  12082  O   LEU B 861     187.775 212.616 194.378  1.00 29.61           O  
ATOM  12083  CB  LEU B 861     188.201 215.226 196.128  1.00 29.27           C  
ATOM  12084  CG  LEU B 861     188.552 215.843 197.488  1.00 29.83           C  
ATOM  12085  CD1 LEU B 861     189.702 216.816 197.304  1.00 29.40           C  
ATOM  12086  CD2 LEU B 861     187.334 216.553 198.069  1.00 32.72           C  
ATOM  12087  N   PRO B 862     186.034 213.952 193.986  1.00 29.39           N  
ATOM  12088  CA  PRO B 862     185.828 213.562 192.616  1.00 29.04           C  
ATOM  12089  C   PRO B 862     186.867 214.241 191.747  1.00 28.89           C  
ATOM  12090  O   PRO B 862     187.352 215.313 192.119  1.00 29.05           O  
ATOM  12091  CB  PRO B 862     184.427 214.091 192.334  1.00 29.40           C  
ATOM  12092  CG  PRO B 862     184.301 215.282 193.235  1.00 30.64           C  
ATOM  12093  CD  PRO B 862     185.068 214.912 194.496  1.00 30.35           C  
ATOM  12094  N   PRO B 863     187.178 213.672 190.583  1.00 28.43           N  
ATOM  12095  CA  PRO B 863     188.012 214.227 189.544  1.00 28.06           C  
ATOM  12096  C   PRO B 863     187.261 215.342 188.866  1.00 28.22           C  
ATOM  12097  O   PRO B 863     186.031 215.323 188.845  1.00 29.44           O  
ATOM  12098  CB  PRO B 863     188.224 213.034 188.617  1.00 28.51           C  
ATOM  12099  CG  PRO B 863     186.999 212.179 188.821  1.00 28.87           C  
ATOM  12100  CD  PRO B 863     186.631 212.354 190.274  1.00 28.63           C  
ATOM  12101  N   LEU B 864     187.980 216.284 188.278  1.00 28.06           N  
ATOM  12102  CA  LEU B 864     187.333 217.322 187.497  1.00 28.22           C  
ATOM  12103  C   LEU B 864     186.716 216.756 186.240  1.00 28.87           C  
ATOM  12104  O   LEU B 864     185.591 217.102 185.879  1.00 29.86           O  
ATOM  12105  CB  LEU B 864     188.327 218.412 187.104  1.00 28.23           C  
ATOM  12106  CG  LEU B 864     187.755 219.564 186.249  1.00 29.08           C  
ATOM  12107  CD1 LEU B 864     186.640 220.286 187.009  1.00 30.06           C  
ATOM  12108  CD2 LEU B 864     188.878 220.511 185.893  1.00 30.01           C  
ATOM  12109  N   LEU B 865     187.448 215.883 185.569  1.00 28.27           N  
ATOM  12110  CA  LEU B 865     186.965 215.309 184.333  1.00 28.08           C  
ATOM  12111  C   LEU B 865     186.366 213.942 184.592  1.00 28.06           C  
ATOM  12112  O   LEU B 865     187.066 213.003 184.969  1.00 28.36           O  
ATOM  12113  CB  LEU B 865     188.109 215.202 183.322  1.00 27.64           C  
ATOM  12114  CG  LEU B 865     188.852 216.518 182.970  1.00 27.39           C  
ATOM  12115  CD1 LEU B 865     190.000 216.206 182.031  1.00 25.97           C  
ATOM  12116  CD2 LEU B 865     187.900 217.497 182.326  1.00 27.95           C  
ATOM  12117  N   THR B 866     185.062 213.846 184.398  1.00 28.33           N  
ATOM  12118  CA  THR B 866     184.316 212.628 184.660  1.00 28.61           C  
ATOM  12119  C   THR B 866     184.481 211.645 183.522  1.00 28.84           C  
ATOM  12120  O   THR B 866     184.951 212.003 182.443  1.00 27.97           O  
ATOM  12121  CB  THR B 866     182.826 212.930 184.845  1.00 29.31           C  
ATOM  12122  OG1 THR B 866     182.280 213.419 183.621  1.00 28.95           O  
ATOM  12123  CG2 THR B 866     182.633 213.959 185.921  1.00 29.90           C  
ATOM  12124  N   ASP B 867     184.056 210.406 183.732  1.00 28.37           N  
ATOM  12125  CA  ASP B 867     184.216 209.391 182.701  1.00 28.01           C  
ATOM  12126  C   ASP B 867     183.544 209.781 181.396  1.00 27.75           C  
ATOM  12127  O   ASP B 867     184.052 209.472 180.319  1.00 27.99           O  
ATOM  12128  CB  ASP B 867     183.649 208.059 183.173  1.00 28.36           C  
ATOM  12129  CG  ASP B 867     184.493 207.397 184.250  1.00 28.74           C  
ATOM  12130  OD1 ASP B 867     185.617 207.795 184.445  1.00 28.25           O  
ATOM  12131  OD2 ASP B 867     183.998 206.493 184.874  1.00 28.10           O  
ATOM  12132  N   GLU B 868     182.400 210.447 181.478  1.00 27.89           N  
ATOM  12133  CA  GLU B 868     181.713 210.866 180.267  1.00 27.70           C  
ATOM  12134  C   GLU B 868     182.542 211.885 179.503  1.00 27.76           C  
ATOM  12135  O   GLU B 868     182.646 211.833 178.278  1.00 28.64           O  
ATOM  12136  CB  GLU B 868     180.351 211.459 180.596  1.00 28.56           C  
ATOM  12137  CG  GLU B 868     179.557 211.880 179.378  1.00 29.14           C  
ATOM  12138  CD  GLU B 868     178.198 212.391 179.719  1.00 29.63           C  
ATOM  12139  OE1 GLU B 868     177.878 212.440 180.880  1.00 29.70           O  
ATOM  12140  OE2 GLU B 868     177.473 212.733 178.816  1.00 29.07           O  
ATOM  12141  N   MET B 869     183.125 212.821 180.231  1.00 27.76           N  
ATOM  12142  CA  MET B 869     183.928 213.875 179.634  1.00 26.97           C  
ATOM  12143  C   MET B 869     185.193 213.316 179.010  1.00 27.41           C  
ATOM  12144  O   MET B 869     185.615 213.760 177.941  1.00 27.03           O  
ATOM  12145  CB  MET B 869     184.232 214.913 180.686  1.00 28.23           C  
ATOM  12146  CG  MET B 869     182.995 215.679 181.120  1.00 28.52           C  
ATOM  12147  SD  MET B 869     183.241 216.596 182.616  1.00 30.42           S  
ATOM  12148  CE  MET B 869     184.286 217.908 182.106  1.00 29.41           C  
ATOM  12149  N   ILE B 870     185.788 212.323 179.655  1.00 27.15           N  
ATOM  12150  CA  ILE B 870     186.965 211.704 179.082  1.00 26.15           C  
ATOM  12151  C   ILE B 870     186.570 210.977 177.820  1.00 26.66           C  
ATOM  12152  O   ILE B 870     187.266 211.068 176.812  1.00 26.20           O  
ATOM  12153  CB  ILE B 870     187.664 210.747 180.055  1.00 27.11           C  
ATOM  12154  CG1 ILE B 870     188.181 211.517 181.287  1.00 27.32           C  
ATOM  12155  CG2 ILE B 870     188.806 210.028 179.345  1.00 26.49           C  
ATOM  12156  CD1 ILE B 870     189.159 212.636 180.992  1.00 26.85           C  
ATOM  12157  N   ALA B 871     185.436 210.285 177.844  1.00 26.89           N  
ATOM  12158  CA  ALA B 871     184.980 209.589 176.656  1.00 25.83           C  
ATOM  12159  C   ALA B 871     184.832 210.567 175.499  1.00 25.82           C  
ATOM  12160  O   ALA B 871     185.146 210.230 174.359  1.00 26.38           O  
ATOM  12161  CB  ALA B 871     183.664 208.889 176.927  1.00 27.71           C  
ATOM  12162  N   GLN B 872     184.380 211.789 175.778  1.00 26.11           N  
ATOM  12163  CA  GLN B 872     184.268 212.783 174.721  1.00 25.40           C  
ATOM  12164  C   GLN B 872     185.637 213.199 174.198  1.00 25.13           C  
ATOM  12165  O   GLN B 872     185.800 213.411 172.995  1.00 25.78           O  
ATOM  12166  CB  GLN B 872     183.490 214.001 175.189  1.00 26.07           C  
ATOM  12167  CG  GLN B 872     182.022 213.739 175.392  1.00 26.26           C  
ATOM  12168  CD  GLN B 872     181.280 214.946 175.894  1.00 26.91           C  
ATOM  12169  OE1 GLN B 872     181.580 216.080 175.512  1.00 25.97           O  
ATOM  12170  NE2 GLN B 872     180.299 214.714 176.750  1.00 27.29           N  
ATOM  12171  N   TYR B 873     186.635 213.291 175.074  1.00 25.01           N  
ATOM  12172  CA  TYR B 873     187.969 213.628 174.595  1.00 24.11           C  
ATOM  12173  C   TYR B 873     188.548 212.515 173.746  1.00 24.49           C  
ATOM  12174  O   TYR B 873     189.140 212.782 172.700  1.00 24.58           O  
ATOM  12175  CB  TYR B 873     188.939 213.919 175.736  1.00 24.69           C  
ATOM  12176  CG  TYR B 873     188.911 215.317 176.279  1.00 24.44           C  
ATOM  12177  CD1 TYR B 873     188.855 215.523 177.638  1.00 25.05           C  
ATOM  12178  CD2 TYR B 873     188.971 216.397 175.421  1.00 24.50           C  
ATOM  12179  CE1 TYR B 873     188.860 216.798 178.133  1.00 25.12           C  
ATOM  12180  CE2 TYR B 873     188.970 217.665 175.919  1.00 25.05           C  
ATOM  12181  CZ  TYR B 873     188.919 217.869 177.264  1.00 25.32           C  
ATOM  12182  OH  TYR B 873     188.928 219.148 177.754  1.00 26.00           O  
ATOM  12183  N   THR B 874     188.365 211.265 174.162  1.00 24.52           N  
ATOM  12184  CA  THR B 874     188.917 210.171 173.386  1.00 23.81           C  
ATOM  12185  C   THR B 874     188.142 210.014 172.097  1.00 24.11           C  
ATOM  12186  O   THR B 874     188.708 209.627 171.076  1.00 24.16           O  
ATOM  12187  CB  THR B 874     188.968 208.860 174.184  1.00 24.29           C  
ATOM  12188  OG1 THR B 874     187.672 208.530 174.664  1.00 25.86           O  
ATOM  12189  CG2 THR B 874     189.914 209.013 175.356  1.00 24.42           C  
ATOM  12190  N   SER B 875     186.866 210.375 172.114  1.00 24.39           N  
ATOM  12191  CA  SER B 875     186.079 210.353 170.900  1.00 23.76           C  
ATOM  12192  C   SER B 875     186.629 211.361 169.910  1.00 23.26           C  
ATOM  12193  O   SER B 875     186.807 211.042 168.737  1.00 24.08           O  
ATOM  12194  CB  SER B 875     184.635 210.669 171.188  1.00 25.27           C  
ATOM  12195  OG  SER B 875     183.891 210.671 170.009  1.00 25.78           O  
ATOM  12196  N   ALA B 876     186.924 212.573 170.379  1.00 23.25           N  
ATOM  12197  CA  ALA B 876     187.470 213.610 169.514  1.00 22.91           C  
ATOM  12198  C   ALA B 876     188.819 213.225 168.938  1.00 23.04           C  
ATOM  12199  O   ALA B 876     189.093 213.459 167.761  1.00 23.15           O  
ATOM  12200  CB  ALA B 876     187.628 214.897 170.290  1.00 24.10           C  
ATOM  12201  N   LEU B 877     189.666 212.626 169.759  1.00 23.00           N  
ATOM  12202  CA  LEU B 877     190.988 212.234 169.312  1.00 22.08           C  
ATOM  12203  C   LEU B 877     190.893 211.136 168.289  1.00 22.26           C  
ATOM  12204  O   LEU B 877     191.613 211.139 167.291  1.00 22.73           O  
ATOM  12205  CB  LEU B 877     191.798 211.749 170.501  1.00 22.42           C  
ATOM  12206  CG  LEU B 877     192.199 212.805 171.502  1.00 22.52           C  
ATOM  12207  CD1 LEU B 877     192.651 212.126 172.746  1.00 22.69           C  
ATOM  12208  CD2 LEU B 877     193.319 213.632 170.933  1.00 22.30           C  
ATOM  12209  N   LEU B 878     189.981 210.209 168.520  1.00 22.91           N  
ATOM  12210  CA  LEU B 878     189.770 209.112 167.609  1.00 22.15           C  
ATOM  12211  C   LEU B 878     189.152 209.572 166.302  1.00 22.55           C  
ATOM  12212  O   LEU B 878     189.580 209.146 165.232  1.00 22.87           O  
ATOM  12213  CB  LEU B 878     188.898 208.067 168.284  1.00 22.44           C  
ATOM  12214  CG  LEU B 878     188.516 206.882 167.467  1.00 23.32           C  
ATOM  12215  CD1 LEU B 878     189.724 206.208 166.947  1.00 22.86           C  
ATOM  12216  CD2 LEU B 878     187.752 205.937 168.345  1.00 25.20           C  
ATOM  12217  N   ALA B 879     188.149 210.439 166.372  1.00 22.23           N  
ATOM  12218  CA  ALA B 879     187.522 210.934 165.163  1.00 21.83           C  
ATOM  12219  C   ALA B 879     188.540 211.699 164.350  1.00 21.56           C  
ATOM  12220  O   ALA B 879     188.562 211.602 163.126  1.00 22.57           O  
ATOM  12221  CB  ALA B 879     186.335 211.815 165.494  1.00 23.34           C  
ATOM  12222  N   GLY B 880     189.408 212.438 165.032  1.00 21.72           N  
ATOM  12223  CA  GLY B 880     190.458 213.184 164.369  1.00 21.37           C  
ATOM  12224  C   GLY B 880     191.400 212.228 163.663  1.00 25.52           C  
ATOM  12225  O   GLY B 880     191.671 212.366 162.470  1.00 20.81           O  
ATOM  12226  N   THR B 881     191.863 211.219 164.388  1.00 21.27           N  
ATOM  12227  CA  THR B 881     192.806 210.252 163.853  1.00 20.96           C  
ATOM  12228  C   THR B 881     192.266 209.572 162.610  1.00 21.51           C  
ATOM  12229  O   THR B 881     192.997 209.378 161.638  1.00 22.06           O  
ATOM  12230  CB  THR B 881     193.132 209.175 164.907  1.00 21.55           C  
ATOM  12231  OG1 THR B 881     193.714 209.789 166.052  1.00 21.63           O  
ATOM  12232  CG2 THR B 881     194.108 208.147 164.351  1.00 21.45           C  
ATOM  12233  N   ILE B 882     191.000 209.186 162.644  1.00 21.84           N  
ATOM  12234  CA  ILE B 882     190.395 208.491 161.525  1.00 21.22           C  
ATOM  12235  C   ILE B 882     190.131 209.371 160.309  1.00 21.46           C  
ATOM  12236  O   ILE B 882     190.384 208.940 159.189  1.00 22.19           O  
ATOM  12237  CB  ILE B 882     189.095 207.805 161.950  1.00 21.83           C  
ATOM  12238  CG1 ILE B 882     189.415 206.677 162.925  1.00 22.40           C  
ATOM  12239  CG2 ILE B 882     188.375 207.257 160.724  1.00 22.62           C  
ATOM  12240  CD1 ILE B 882     188.212 206.140 163.648  1.00 23.81           C  
ATOM  12241  N   THR B 883     189.585 210.571 160.496  1.00 21.92           N  
ATOM  12242  CA  THR B 883     189.203 211.372 159.338  1.00 21.26           C  
ATOM  12243  C   THR B 883     190.224 212.406 158.865  1.00 21.24           C  
ATOM  12244  O   THR B 883     190.101 212.899 157.743  1.00 22.19           O  
ATOM  12245  CB  THR B 883     187.887 212.117 159.608  1.00 22.02           C  
ATOM  12246  OG1 THR B 883     188.075 213.060 160.659  1.00 21.94           O  
ATOM  12247  CG2 THR B 883     186.803 211.134 160.011  1.00 22.43           C  
ATOM  12248  N   SER B 884     191.208 212.771 159.692  1.00 21.24           N  
ATOM  12249  CA  SER B 884     192.163 213.806 159.289  1.00 20.68           C  
ATOM  12250  C   SER B 884     193.633 213.452 159.544  1.00 20.30           C  
ATOM  12251  O   SER B 884     194.519 214.302 159.429  1.00 21.20           O  
ATOM  12252  CB  SER B 884     191.823 215.104 159.975  1.00 21.27           C  
ATOM  12253  OG  SER B 884     191.921 214.979 161.350  1.00 21.53           O  
ATOM  12254  N   GLY B 885     193.904 212.210 159.897  1.00 21.10           N  
ATOM  12255  CA  GLY B 885     195.276 211.783 160.130  1.00 20.86           C  
ATOM  12256  C   GLY B 885     195.930 212.571 161.246  1.00 21.05           C  
ATOM  12257  O   GLY B 885     195.398 212.666 162.346  1.00 21.58           O  
ATOM  12258  N   TRP B 886     197.101 213.118 160.972  1.00 20.37           N  
ATOM  12259  CA  TRP B 886     197.838 213.882 161.965  1.00 20.17           C  
ATOM  12260  C   TRP B 886     197.657 215.386 161.856  1.00 20.63           C  
ATOM  12261  O   TRP B 886     198.320 216.139 162.576  1.00 20.66           O  
ATOM  12262  CB  TRP B 886     199.321 213.585 161.869  1.00 20.32           C  
ATOM  12263  CG  TRP B 886     199.834 213.590 160.487  1.00 20.27           C  
ATOM  12264  CD1 TRP B 886     200.096 214.665 159.704  1.00 20.47           C  
ATOM  12265  CD2 TRP B 886     200.203 212.436 159.720  1.00 20.25           C  
ATOM  12266  NE1 TRP B 886     200.580 214.254 158.492  1.00 20.47           N  
ATOM  12267  CE2 TRP B 886     200.656 212.890 158.491  1.00 20.47           C  
ATOM  12268  CE3 TRP B 886     200.193 211.076 159.980  1.00 20.06           C  
ATOM  12269  CZ2 TRP B 886     201.092 212.024 157.512  1.00 20.47           C  
ATOM  12270  CZ3 TRP B 886     200.634 210.209 159.005  1.00 20.07           C  
ATOM  12271  CH2 TRP B 886     201.070 210.669 157.805  1.00 20.06           C  
ATOM  12272  N   THR B 887     196.800 215.841 160.951  1.00 20.44           N  
ATOM  12273  CA  THR B 887     196.721 217.274 160.742  1.00 19.74           C  
ATOM  12274  C   THR B 887     195.880 217.940 161.808  1.00 21.97           C  
ATOM  12275  O   THR B 887     196.060 219.122 162.086  1.00 20.81           O  
ATOM  12276  CB  THR B 887     196.161 217.602 159.362  1.00 20.69           C  
ATOM  12277  OG1 THR B 887     194.784 217.243 159.306  1.00 21.44           O  
ATOM  12278  CG2 THR B 887     196.924 216.795 158.325  1.00 20.77           C  
ATOM  12279  N   PHE B 888     195.000 217.192 162.464  1.00 21.10           N  
ATOM  12280  CA  PHE B 888     194.207 217.789 163.532  1.00 21.00           C  
ATOM  12281  C   PHE B 888     195.120 218.094 164.702  1.00 20.93           C  
ATOM  12282  O   PHE B 888     194.811 218.915 165.564  1.00 21.19           O  
ATOM  12283  CB  PHE B 888     193.078 216.878 163.986  1.00 21.50           C  
ATOM  12284  CG  PHE B 888     193.503 215.774 164.858  1.00 21.09           C  
ATOM  12285  CD1 PHE B 888     193.505 215.937 166.221  1.00 21.57           C  
ATOM  12286  CD2 PHE B 888     193.903 214.577 164.337  1.00 21.06           C  
ATOM  12287  CE1 PHE B 888     193.892 214.926 167.046  1.00 21.57           C  
ATOM  12288  CE2 PHE B 888     194.297 213.558 165.162  1.00 21.12           C  
ATOM  12289  CZ  PHE B 888     194.290 213.732 166.517  1.00 21.26           C  
ATOM  12290  N   GLY B 889     196.246 217.395 164.735  1.00 21.26           N  
ATOM  12291  CA  GLY B 889     197.258 217.584 165.749  1.00 20.76           C  
ATOM  12292  C   GLY B 889     198.056 218.834 165.422  1.00 20.24           C  
ATOM  12293  O   GLY B 889     198.108 219.779 166.207  1.00 20.51           O  
ATOM  12294  N   ALA B 890     198.690 218.831 164.248  1.00 20.72           N  
ATOM  12295  CA  ALA B 890     199.552 219.934 163.824  1.00 20.38           C  
ATOM  12296  C   ALA B 890     198.811 221.269 163.680  1.00 20.32           C  
ATOM  12297  O   ALA B 890     199.384 222.323 163.949  1.00 20.19           O  
ATOM  12298  CB  ALA B 890     200.216 219.594 162.504  1.00 19.98           C  
ATOM  12299  N   GLY B 891     197.562 221.244 163.235  1.00 20.56           N  
ATOM  12300  CA  GLY B 891     196.827 222.484 163.026  1.00 20.49           C  
ATOM  12301  C   GLY B 891     195.333 222.249 162.838  1.00 20.76           C  
ATOM  12302  O   GLY B 891     194.615 221.939 163.788  1.00 20.96           O  
ATOM  12303  N   ALA B 892     194.859 222.466 161.617  1.00 20.49           N  
ATOM  12304  CA  ALA B 892     193.456 222.256 161.287  1.00 20.63           C  
ATOM  12305  C   ALA B 892     193.207 220.801 160.940  1.00 20.92           C  
ATOM  12306  O   ALA B 892     194.067 220.134 160.372  1.00 21.67           O  
ATOM  12307  CB  ALA B 892     193.052 223.143 160.122  1.00 20.62           C  
ATOM  12308  N   ALA B 893     192.011 220.308 161.214  1.00 21.03           N  
ATOM  12309  CA  ALA B 893     191.706 218.949 160.805  1.00 20.76           C  
ATOM  12310  C   ALA B 893     191.382 218.944 159.327  1.00 20.88           C  
ATOM  12311  O   ALA B 893     190.361 219.485 158.909  1.00 21.01           O  
ATOM  12312  CB  ALA B 893     190.548 218.391 161.607  1.00 21.72           C  
ATOM  12313  N   LEU B 894     192.271 218.349 158.546  1.00 20.93           N  
ATOM  12314  CA  LEU B 894     192.139 218.311 157.101  1.00 20.51           C  
ATOM  12315  C   LEU B 894     191.650 216.954 156.646  1.00 20.89           C  
ATOM  12316  O   LEU B 894     192.366 215.964 156.754  1.00 21.30           O  
ATOM  12317  CB  LEU B 894     193.500 218.597 156.474  1.00 20.59           C  
ATOM  12318  CG  LEU B 894     194.154 219.910 156.881  1.00 20.47           C  
ATOM  12319  CD1 LEU B 894     195.511 219.968 156.303  1.00 21.13           C  
ATOM  12320  CD2 LEU B 894     193.342 221.059 156.385  1.00 20.34           C  
ATOM  12321  N   GLN B 895     190.439 216.900 156.124  1.00 20.96           N  
ATOM  12322  CA  GLN B 895     189.869 215.620 155.760  1.00 20.45           C  
ATOM  12323  C   GLN B 895     190.698 214.930 154.696  1.00 21.19           C  
ATOM  12324  O   GLN B 895     191.223 215.565 153.781  1.00 21.67           O  
ATOM  12325  CB  GLN B 895     188.417 215.766 155.284  1.00 21.20           C  
ATOM  12326  CG  GLN B 895     188.216 216.467 153.951  1.00 21.54           C  
ATOM  12327  CD  GLN B 895     188.090 217.933 154.096  1.00 21.40           C  
ATOM  12328  OE1 GLN B 895     188.584 218.488 155.080  1.00 21.41           O  
ATOM  12329  NE2 GLN B 895     187.458 218.577 153.128  1.00 21.29           N  
ATOM  12330  N   ILE B 896     190.814 213.619 154.829  1.00 21.21           N  
ATOM  12331  CA  ILE B 896     191.490 212.783 153.849  1.00 21.07           C  
ATOM  12332  C   ILE B 896     190.794 211.418 153.822  1.00 21.24           C  
ATOM  12333  O   ILE B 896     190.433 210.921 154.883  1.00 21.95           O  
ATOM  12334  CB  ILE B 896     192.978 212.636 154.238  1.00 21.17           C  
ATOM  12335  CG1 ILE B 896     193.749 211.902 153.147  1.00 21.26           C  
ATOM  12336  CG2 ILE B 896     193.097 211.915 155.579  1.00 21.56           C  
ATOM  12337  CD1 ILE B 896     195.244 211.954 153.283  1.00 21.20           C  
ATOM  12338  N   PRO B 897     190.595 210.771 152.668  1.00 21.10           N  
ATOM  12339  CA  PRO B 897     190.044 209.438 152.582  1.00 21.10           C  
ATOM  12340  C   PRO B 897     190.888 208.536 153.442  1.00 21.26           C  
ATOM  12341  O   PRO B 897     192.109 208.647 153.431  1.00 22.03           O  
ATOM  12342  CB  PRO B 897     190.179 209.122 151.100  1.00 21.34           C  
ATOM  12343  CG  PRO B 897     190.117 210.465 150.444  1.00 21.55           C  
ATOM  12344  CD  PRO B 897     190.859 211.389 151.379  1.00 21.22           C  
ATOM  12345  N   PHE B 898     190.259 207.634 154.176  1.00 21.49           N  
ATOM  12346  CA  PHE B 898     191.038 206.815 155.083  1.00 21.05           C  
ATOM  12347  C   PHE B 898     192.066 205.963 154.361  1.00 21.47           C  
ATOM  12348  O   PHE B 898     193.201 205.839 154.814  1.00 22.14           O  
ATOM  12349  CB  PHE B 898     190.163 205.929 155.939  1.00 22.13           C  
ATOM  12350  CG  PHE B 898     190.966 205.273 156.961  1.00 21.63           C  
ATOM  12351  CD1 PHE B 898     191.397 205.997 158.031  1.00 21.88           C  
ATOM  12352  CD2 PHE B 898     191.327 203.968 156.862  1.00 22.02           C  
ATOM  12353  CE1 PHE B 898     192.177 205.439 158.983  1.00 21.73           C  
ATOM  12354  CE2 PHE B 898     192.112 203.405 157.820  1.00 21.99           C  
ATOM  12355  CZ  PHE B 898     192.540 204.149 158.874  1.00 21.75           C  
ATOM  12356  N   ALA B 899     191.690 205.359 153.246  1.00 21.15           N  
ATOM  12357  CA  ALA B 899     192.640 204.511 152.543  1.00 20.90           C  
ATOM  12358  C   ALA B 899     193.876 205.306 152.138  1.00 20.57           C  
ATOM  12359  O   ALA B 899     194.987 204.780 152.138  1.00 21.40           O  
ATOM  12360  CB  ALA B 899     191.998 203.891 151.321  1.00 21.33           C  
ATOM  12361  N   MET B 900     193.702 206.572 151.784  1.00 21.05           N  
ATOM  12362  CA  MET B 900     194.854 207.368 151.405  1.00 20.31           C  
ATOM  12363  C   MET B 900     195.675 207.701 152.623  1.00 20.53           C  
ATOM  12364  O   MET B 900     196.904 207.690 152.574  1.00 20.85           O  
ATOM  12365  CB  MET B 900     194.428 208.613 150.672  1.00 20.82           C  
ATOM  12366  CG  MET B 900     193.814 208.308 149.335  1.00 20.77           C  
ATOM  12367  SD  MET B 900     193.327 209.741 148.459  1.00 21.75           S  
ATOM  12368  CE  MET B 900     194.912 210.295 147.922  1.00 20.63           C  
ATOM  12369  N   GLN B 901     195.010 207.926 153.739  1.00 20.47           N  
ATOM  12370  CA  GLN B 901     195.733 208.169 154.965  1.00 20.06           C  
ATOM  12371  C   GLN B 901     196.634 207.000 155.269  1.00 20.71           C  
ATOM  12372  O   GLN B 901     197.783 207.188 155.666  1.00 21.30           O  
ATOM  12373  CB  GLN B 901     194.784 208.383 156.119  1.00 20.95           C  
ATOM  12374  CG  GLN B 901     195.454 208.579 157.411  1.00 20.65           C  
ATOM  12375  CD  GLN B 901     194.481 208.936 158.430  1.00 21.09           C  
ATOM  12376  OE1 GLN B 901     193.754 209.905 158.244  1.00 21.60           O  
ATOM  12377  NE2 GLN B 901     194.426 208.198 159.517  1.00 21.22           N  
ATOM  12378  N   MET B 902     196.127 205.791 155.069  1.00 20.52           N  
ATOM  12379  CA  MET B 902     196.941 204.614 155.303  1.00 20.10           C  
ATOM  12380  C   MET B 902     198.103 204.569 154.335  1.00 20.01           C  
ATOM  12381  O   MET B 902     199.206 204.183 154.708  1.00 20.72           O  
ATOM  12382  CB  MET B 902     196.109 203.354 155.204  1.00 20.75           C  
ATOM  12383  CG  MET B 902     195.168 203.164 156.334  1.00 21.22           C  
ATOM  12384  SD  MET B 902     195.986 203.087 157.926  1.00 21.81           S  
ATOM  12385  CE  MET B 902     196.825 201.527 157.847  1.00 20.90           C  
ATOM  12386  N   ALA B 903     197.897 205.022 153.107  1.00 20.68           N  
ATOM  12387  CA  ALA B 903     198.984 205.023 152.145  1.00 19.45           C  
ATOM  12388  C   ALA B 903     200.123 205.869 152.656  1.00 19.07           C  
ATOM  12389  O   ALA B 903     201.289 205.545 152.430  1.00 20.47           O  
ATOM  12390  CB  ALA B 903     198.522 205.541 150.803  1.00 20.79           C  
ATOM  12391  N   TYR B 904     199.798 206.952 153.350  1.00 19.57           N  
ATOM  12392  CA  TYR B 904     200.840 207.814 153.872  1.00 19.31           C  
ATOM  12393  C   TYR B 904     201.527 207.095 155.019  1.00 19.16           C  
ATOM  12394  O   TYR B 904     202.749 207.145 155.151  1.00 19.77           O  
ATOM  12395  CB  TYR B 904     200.274 209.133 154.397  1.00 19.88           C  
ATOM  12396  CG  TYR B 904     199.621 210.088 153.394  1.00 20.36           C  
ATOM  12397  CD1 TYR B 904     199.269 209.709 152.097  1.00 20.46           C  
ATOM  12398  CD2 TYR B 904     199.357 211.380 153.817  1.00 20.47           C  
ATOM  12399  CE1 TYR B 904     198.661 210.622 151.263  1.00 20.43           C  
ATOM  12400  CE2 TYR B 904     198.759 212.280 152.978  1.00 20.24           C  
ATOM  12401  CZ  TYR B 904     198.413 211.910 151.713  1.00 20.44           C  
ATOM  12402  OH  TYR B 904     197.808 212.818 150.888  1.00 20.88           O  
ATOM  12403  N   ARG B 905     200.726 206.421 155.842  1.00 19.39           N  
ATOM  12404  CA  ARG B 905     201.217 205.687 157.000  1.00 18.63           C  
ATOM  12405  C   ARG B 905     202.167 204.567 156.578  1.00 19.54           C  
ATOM  12406  O   ARG B 905     203.168 204.310 157.244  1.00 19.34           O  
ATOM  12407  CB  ARG B 905     200.039 205.105 157.764  1.00 19.45           C  
ATOM  12408  CG  ARG B 905     199.058 206.145 158.317  1.00 19.32           C  
ATOM  12409  CD  ARG B 905     199.353 206.503 159.676  1.00 19.15           C  
ATOM  12410  NE  ARG B 905     198.458 207.525 160.191  1.00 19.28           N  
ATOM  12411  CZ  ARG B 905     198.588 208.111 161.401  1.00 19.43           C  
ATOM  12412  NH1 ARG B 905     199.555 207.742 162.204  1.00 19.41           N  
ATOM  12413  NH2 ARG B 905     197.748 209.052 161.773  1.00 20.11           N  
ATOM  12414  N   PHE B 906     201.866 203.914 155.457  1.00 19.13           N  
ATOM  12415  CA  PHE B 906     202.725 202.862 154.924  1.00 18.35           C  
ATOM  12416  C   PHE B 906     203.995 203.438 154.336  1.00 20.65           C  
ATOM  12417  O   PHE B 906     205.093 202.946 154.599  1.00 18.18           O  
ATOM  12418  CB  PHE B 906     202.006 202.043 153.856  1.00 19.06           C  
ATOM  12419  CG  PHE B 906     201.253 200.858 154.366  1.00 19.09           C  
ATOM  12420  CD1 PHE B 906     199.981 200.956 154.865  1.00 20.19           C  
ATOM  12421  CD2 PHE B 906     201.829 199.623 154.311  1.00 19.16           C  
ATOM  12422  CE1 PHE B 906     199.315 199.839 155.308  1.00 20.77           C  
ATOM  12423  CE2 PHE B 906     201.167 198.513 154.746  1.00 19.81           C  
ATOM  12424  CZ  PHE B 906     199.912 198.622 155.247  1.00 20.35           C  
ATOM  12425  N   ASN B 907     203.868 204.525 153.588  1.00 18.69           N  
ATOM  12426  CA  ASN B 907     205.036 205.139 152.989  1.00 18.29           C  
ATOM  12427  C   ASN B 907     205.994 205.581 154.086  1.00 18.41           C  
ATOM  12428  O   ASN B 907     207.214 205.480 153.948  1.00 18.81           O  
ATOM  12429  CB  ASN B 907     204.622 206.304 152.125  1.00 18.67           C  
ATOM  12430  CG  ASN B 907     205.698 206.766 151.237  1.00 18.75           C  
ATOM  12431  OD1 ASN B 907     206.123 206.042 150.331  1.00 19.18           O  
ATOM  12432  ND2 ASN B 907     206.164 207.962 151.464  1.00 18.76           N  
ATOM  12433  N   GLY B 908     205.426 206.002 155.209  1.00 18.71           N  
ATOM  12434  CA  GLY B 908     206.166 206.475 156.364  1.00 18.48           C  
ATOM  12435  C   GLY B 908     207.024 205.410 157.042  1.00 18.40           C  
ATOM  12436  O   GLY B 908     207.882 205.749 157.862  1.00 18.48           O  
ATOM  12437  N   ILE B 909     206.805 204.135 156.722  1.00 18.36           N  
ATOM  12438  CA  ILE B 909     207.609 203.071 157.308  1.00 18.11           C  
ATOM  12439  C   ILE B 909     208.447 202.386 156.244  1.00 18.42           C  
ATOM  12440  O   ILE B 909     208.993 201.309 156.474  1.00 18.55           O  
ATOM  12441  CB  ILE B 909     206.765 202.016 158.043  1.00 17.88           C  
ATOM  12442  CG1 ILE B 909     205.802 201.339 157.088  1.00 18.13           C  
ATOM  12443  CG2 ILE B 909     206.010 202.686 159.169  1.00 18.65           C  
ATOM  12444  CD1 ILE B 909     205.175 200.084 157.619  1.00 18.18           C  
ATOM  12445  N   GLY B 910     208.555 203.010 155.076  1.00 18.50           N  
ATOM  12446  CA  GLY B 910     209.376 202.460 154.012  1.00 18.31           C  
ATOM  12447  C   GLY B 910     208.665 201.458 153.111  1.00 18.54           C  
ATOM  12448  O   GLY B 910     209.323 200.669 152.436  1.00 18.82           O  
ATOM  12449  N   VAL B 911     207.339 201.458 153.098  1.00 18.53           N  
ATOM  12450  CA  VAL B 911     206.618 200.547 152.231  1.00 18.41           C  
ATOM  12451  C   VAL B 911     205.850 201.356 151.203  1.00 19.06           C  
ATOM  12452  O   VAL B 911     205.003 202.175 151.546  1.00 19.68           O  
ATOM  12453  CB  VAL B 911     205.683 199.652 153.047  1.00 18.40           C  
ATOM  12454  CG1 VAL B 911     204.913 198.736 152.136  1.00 18.90           C  
ATOM  12455  CG2 VAL B 911     206.500 198.839 154.025  1.00 18.52           C  
ATOM  12456  N   THR B 912     206.148 201.124 149.939  1.00 19.26           N  
ATOM  12457  CA  THR B 912     205.603 201.920 148.851  1.00 19.36           C  
ATOM  12458  C   THR B 912     204.078 201.895 148.863  1.00 19.62           C  
ATOM  12459  O   THR B 912     203.467 200.871 149.157  1.00 20.63           O  
ATOM  12460  CB  THR B 912     206.154 201.429 147.504  1.00 19.91           C  
ATOM  12461  OG1 THR B 912     207.578 201.464 147.544  1.00 20.54           O  
ATOM  12462  CG2 THR B 912     205.698 202.330 146.388  1.00 20.88           C  
ATOM  12463  N   GLN B 913     203.463 203.030 148.537  1.00 19.84           N  
ATOM  12464  CA  GLN B 913     202.011 203.201 148.592  1.00 19.43           C  
ATOM  12465  C   GLN B 913     201.235 202.143 147.836  1.00 19.95           C  
ATOM  12466  O   GLN B 913     200.135 201.761 148.236  1.00 20.97           O  
ATOM  12467  CB  GLN B 913     201.599 204.522 147.966  1.00 20.07           C  
ATOM  12468  CG  GLN B 913     201.975 205.757 148.693  1.00 20.37           C  
ATOM  12469  CD  GLN B 913     201.450 206.939 147.931  1.00 21.13           C  
ATOM  12470  OE1 GLN B 913     201.468 206.919 146.699  1.00 21.98           O  
ATOM  12471  NE2 GLN B 913     200.965 207.958 148.622  1.00 20.96           N  
ATOM  12472  N   ASN B 914     201.780 201.665 146.734  1.00 20.05           N  
ATOM  12473  CA  ASN B 914     201.037 200.723 145.930  1.00 20.12           C  
ATOM  12474  C   ASN B 914     200.783 199.432 146.686  1.00 20.51           C  
ATOM  12475  O   ASN B 914     199.863 198.697 146.346  1.00 20.53           O  
ATOM  12476  CB  ASN B 914     201.760 200.412 144.649  1.00 20.34           C  
ATOM  12477  CG  ASN B 914     202.960 199.649 144.908  1.00 19.91           C  
ATOM  12478  OD1 ASN B 914     203.880 200.134 145.561  1.00 20.27           O  
ATOM  12479  ND2 ASN B 914     202.982 198.442 144.435  1.00 20.02           N  
ATOM  12480  N   VAL B 915     201.592 199.146 147.705  1.00 20.12           N  
ATOM  12481  CA  VAL B 915     201.427 197.905 148.439  1.00 19.47           C  
ATOM  12482  C   VAL B 915     200.100 197.938 149.151  1.00 20.58           C  
ATOM  12483  O   VAL B 915     199.361 196.954 149.130  1.00 21.41           O  
ATOM  12484  CB  VAL B 915     202.564 197.700 149.447  1.00 19.61           C  
ATOM  12485  CG1 VAL B 915     202.285 196.481 150.333  1.00 19.88           C  
ATOM  12486  CG2 VAL B 915     203.858 197.524 148.687  1.00 19.52           C  
ATOM  12487  N   LEU B 916     199.780 199.070 149.762  1.00 20.06           N  
ATOM  12488  CA  LEU B 916     198.506 199.210 150.427  1.00 20.03           C  
ATOM  12489  C   LEU B 916     197.355 199.041 149.480  1.00 21.22           C  
ATOM  12490  O   LEU B 916     196.414 198.310 149.760  1.00 21.25           O  
ATOM  12491  CB  LEU B 916     198.346 200.588 151.047  1.00 20.51           C  
ATOM  12492  CG  LEU B 916     196.914 200.929 151.541  1.00 20.72           C  
ATOM  12493  CD1 LEU B 916     196.478 200.024 152.643  1.00 20.97           C  
ATOM  12494  CD2 LEU B 916     196.903 202.287 151.981  1.00 20.81           C  
ATOM  12495  N   TYR B 917     197.402 199.740 148.360  1.00 20.61           N  
ATOM  12496  CA  TYR B 917     196.242 199.722 147.496  1.00 20.18           C  
ATOM  12497  C   TYR B 917     196.034 198.358 146.876  1.00 20.32           C  
ATOM  12498  O   TYR B 917     194.911 197.856 146.826  1.00 21.19           O  
ATOM  12499  CB  TYR B 917     196.384 200.786 146.428  1.00 20.97           C  
ATOM  12500  CG  TYR B 917     196.355 202.161 147.002  1.00 20.73           C  
ATOM  12501  CD1 TYR B 917     197.455 202.974 146.884  1.00 20.75           C  
ATOM  12502  CD2 TYR B 917     195.240 202.609 147.666  1.00 20.82           C  
ATOM  12503  CE1 TYR B 917     197.440 204.229 147.408  1.00 20.82           C  
ATOM  12504  CE2 TYR B 917     195.231 203.866 148.198  1.00 20.78           C  
ATOM  12505  CZ  TYR B 917     196.326 204.672 148.062  1.00 20.75           C  
ATOM  12506  OH  TYR B 917     196.309 205.926 148.577  1.00 21.11           O  
ATOM  12507  N   GLU B 918     197.110 197.714 146.469  1.00 20.30           N  
ATOM  12508  CA  GLU B 918     196.994 196.408 145.856  1.00 20.26           C  
ATOM  12509  C   GLU B 918     196.483 195.379 146.858  1.00 20.70           C  
ATOM  12510  O   GLU B 918     195.744 194.465 146.503  1.00 21.09           O  
ATOM  12511  CB  GLU B 918     198.328 195.990 145.248  1.00 20.27           C  
ATOM  12512  CG  GLU B 918     198.740 196.845 144.037  1.00 20.10           C  
ATOM  12513  CD  GLU B 918     200.109 196.527 143.527  1.00 20.24           C  
ATOM  12514  OE1 GLU B 918     200.624 195.498 143.883  1.00 19.67           O  
ATOM  12515  OE2 GLU B 918     200.657 197.329 142.798  1.00 20.43           O  
ATOM  12516  N   ASN B 919     196.859 195.551 148.121  1.00 20.54           N  
ATOM  12517  CA  ASN B 919     196.447 194.655 149.183  1.00 20.00           C  
ATOM  12518  C   ASN B 919     195.430 195.290 150.123  1.00 21.16           C  
ATOM  12519  O   ASN B 919     195.280 194.846 151.260  1.00 21.54           O  
ATOM  12520  CB  ASN B 919     197.655 194.209 149.975  1.00 20.19           C  
ATOM  12521  CG  ASN B 919     198.561 193.362 149.185  1.00 20.23           C  
ATOM  12522  OD1 ASN B 919     198.260 192.199 148.892  1.00 20.81           O  
ATOM  12523  ND2 ASN B 919     199.679 193.913 148.807  1.00 20.12           N  
ATOM  12524  N   GLN B 920     194.704 196.307 149.676  1.00 20.66           N  
ATOM  12525  CA  GLN B 920     193.797 196.991 150.593  1.00 20.43           C  
ATOM  12526  C   GLN B 920     192.775 196.080 151.243  1.00 20.61           C  
ATOM  12527  O   GLN B 920     192.448 196.260 152.415  1.00 21.47           O  
ATOM  12528  CB  GLN B 920     193.064 198.127 149.898  1.00 20.80           C  
ATOM  12529  CG  GLN B 920     192.161 198.922 150.819  1.00 20.70           C  
ATOM  12530  CD  GLN B 920     191.592 200.116 150.139  1.00 21.16           C  
ATOM  12531  OE1 GLN B 920     192.163 200.611 149.165  1.00 21.50           O  
ATOM  12532  NE2 GLN B 920     190.465 200.599 150.630  1.00 21.73           N  
ATOM  12533  N   LYS B 921     192.239 195.119 150.504  1.00 20.74           N  
ATOM  12534  CA  LYS B 921     191.237 194.244 151.099  1.00 20.68           C  
ATOM  12535  C   LYS B 921     191.864 193.361 152.168  1.00 21.06           C  
ATOM  12536  O   LYS B 921     191.267 193.121 153.217  1.00 21.65           O  
ATOM  12537  CB  LYS B 921     190.544 193.403 150.036  1.00 20.90           C  
ATOM  12538  CG  LYS B 921     189.617 194.202 149.134  1.00 21.07           C  
ATOM  12539  CD  LYS B 921     188.948 193.316 148.095  1.00 20.72           C  
ATOM  12540  CE  LYS B 921     188.011 194.119 147.198  1.00 19.69           C  
ATOM  12541  NZ  LYS B 921     187.367 193.263 146.162  1.00 20.85           N  
ATOM  12542  N   LEU B 922     193.079 192.894 151.910  1.00 20.85           N  
ATOM  12543  CA  LEU B 922     193.789 192.053 152.860  1.00 20.29           C  
ATOM  12544  C   LEU B 922     194.081 192.812 154.133  1.00 22.10           C  
ATOM  12545  O   LEU B 922     193.898 192.294 155.233  1.00 21.31           O  
ATOM  12546  CB  LEU B 922     195.115 191.585 152.260  1.00 20.52           C  
ATOM  12547  CG  LEU B 922     196.046 190.770 153.178  1.00 20.41           C  
ATOM  12548  CD1 LEU B 922     195.370 189.476 153.601  1.00 20.94           C  
ATOM  12549  CD2 LEU B 922     197.355 190.504 152.435  1.00 19.94           C  
ATOM  12550  N   ILE B 923     194.545 194.039 153.976  1.00 20.94           N  
ATOM  12551  CA  ILE B 923     194.921 194.872 155.097  1.00 20.29           C  
ATOM  12552  C   ILE B 923     193.724 195.226 155.945  1.00 21.76           C  
ATOM  12553  O   ILE B 923     193.788 195.143 157.171  1.00 22.15           O  
ATOM  12554  CB  ILE B 923     195.622 196.130 154.592  1.00 20.90           C  
ATOM  12555  CG1 ILE B 923     196.942 195.724 154.000  1.00 20.45           C  
ATOM  12556  CG2 ILE B 923     195.823 197.119 155.727  1.00 21.44           C  
ATOM  12557  CD1 ILE B 923     197.580 196.752 153.148  1.00 20.82           C  
ATOM  12558  N   ALA B 924     192.632 195.627 155.310  1.00 21.37           N  
ATOM  12559  CA  ALA B 924     191.440 195.966 156.059  1.00 21.42           C  
ATOM  12560  C   ALA B 924     190.923 194.751 156.816  1.00 22.29           C  
ATOM  12561  O   ALA B 924     190.504 194.868 157.968  1.00 22.85           O  
ATOM  12562  CB  ALA B 924     190.372 196.498 155.134  1.00 22.32           C  
ATOM  12563  N   ASN B 925     190.990 193.571 156.200  1.00 21.87           N  
ATOM  12564  CA  ASN B 925     190.507 192.374 156.866  1.00 21.50           C  
ATOM  12565  C   ASN B 925     191.386 191.991 158.042  1.00 22.10           C  
ATOM  12566  O   ASN B 925     190.874 191.606 159.095  1.00 23.69           O  
ATOM  12567  CB  ASN B 925     190.409 191.228 155.891  1.00 21.55           C  
ATOM  12568  CG  ASN B 925     189.256 191.368 154.959  1.00 21.68           C  
ATOM  12569  OD1 ASN B 925     188.256 192.025 155.266  1.00 21.68           O  
ATOM  12570  ND2 ASN B 925     189.365 190.755 153.812  1.00 21.61           N  
ATOM  12571  N   GLN B 926     192.702 192.135 157.896  1.00 21.65           N  
ATOM  12572  CA  GLN B 926     193.599 191.822 158.997  1.00 21.43           C  
ATOM  12573  C   GLN B 926     193.368 192.779 160.149  1.00 22.62           C  
ATOM  12574  O   GLN B 926     193.368 192.372 161.311  1.00 23.51           O  
ATOM  12575  CB  GLN B 926     195.056 191.896 158.556  1.00 20.96           C  
ATOM  12576  CG  GLN B 926     195.502 190.786 157.627  1.00 20.62           C  
ATOM  12577  CD  GLN B 926     196.888 191.039 157.125  1.00 19.85           C  
ATOM  12578  OE1 GLN B 926     197.361 192.171 157.233  1.00 20.37           O  
ATOM  12579  NE2 GLN B 926     197.553 190.021 156.596  1.00 19.84           N  
ATOM  12580  N   PHE B 927     193.138 194.045 159.831  1.00 22.26           N  
ATOM  12581  CA  PHE B 927     192.860 195.029 160.856  1.00 22.10           C  
ATOM  12582  C   PHE B 927     191.602 194.678 161.623  1.00 24.35           C  
ATOM  12583  O   PHE B 927     191.589 194.699 162.855  1.00 23.75           O  
ATOM  12584  CB  PHE B 927     192.714 196.419 160.260  1.00 22.86           C  
ATOM  12585  CG  PHE B 927     192.292 197.418 161.263  1.00 23.19           C  
ATOM  12586  CD1 PHE B 927     193.187 197.925 162.162  1.00 23.04           C  
ATOM  12587  CD2 PHE B 927     190.984 197.843 161.320  1.00 23.60           C  
ATOM  12588  CE1 PHE B 927     192.788 198.832 163.099  1.00 23.00           C  
ATOM  12589  CE2 PHE B 927     190.581 198.750 162.254  1.00 23.78           C  
ATOM  12590  CZ  PHE B 927     191.486 199.244 163.148  1.00 23.11           C  
ATOM  12591  N   ASN B 928     190.533 194.371 160.897  1.00 23.15           N  
ATOM  12592  CA  ASN B 928     189.258 194.095 161.527  1.00 23.16           C  
ATOM  12593  C   ASN B 928     189.351 192.867 162.417  1.00 23.75           C  
ATOM  12594  O   ASN B 928     188.779 192.837 163.512  1.00 24.82           O  
ATOM  12595  CB  ASN B 928     188.207 193.903 160.461  1.00 23.52           C  
ATOM  12596  CG  ASN B 928     187.930 195.174 159.731  1.00 23.89           C  
ATOM  12597  OD1 ASN B 928     188.201 196.262 160.243  1.00 24.32           O  
ATOM  12598  ND2 ASN B 928     187.417 195.065 158.538  1.00 23.86           N  
ATOM  12599  N   SER B 929     190.101 191.867 161.968  1.00 23.86           N  
ATOM  12600  CA  SER B 929     190.290 190.660 162.752  1.00 24.09           C  
ATOM  12601  C   SER B 929     191.053 190.971 164.026  1.00 24.67           C  
ATOM  12602  O   SER B 929     190.672 190.523 165.111  1.00 25.97           O  
ATOM  12603  CB  SER B 929     191.034 189.621 161.950  1.00 24.12           C  
ATOM  12604  OG  SER B 929     191.205 188.447 162.690  1.00 25.31           O  
ATOM  12605  N   ALA B 930     192.119 191.764 163.905  1.00 24.30           N  
ATOM  12606  CA  ALA B 930     192.935 192.107 165.056  1.00 24.21           C  
ATOM  12607  C   ALA B 930     192.119 192.817 166.125  1.00 25.38           C  
ATOM  12608  O   ALA B 930     192.296 192.551 167.313  1.00 26.27           O  
ATOM  12609  CB  ALA B 930     194.096 192.977 164.629  1.00 23.40           C  
ATOM  12610  N   ILE B 931     191.199 193.692 165.729  1.00 24.87           N  
ATOM  12611  CA  ILE B 931     190.391 194.364 166.737  1.00 24.93           C  
ATOM  12612  C   ILE B 931     189.517 193.350 167.455  1.00 25.44           C  
ATOM  12613  O   ILE B 931     189.423 193.372 168.684  1.00 26.96           O  
ATOM  12614  CB  ILE B 931     189.519 195.489 166.143  1.00 25.07           C  
ATOM  12615  CG1 ILE B 931     190.406 196.632 165.553  1.00 24.50           C  
ATOM  12616  CG2 ILE B 931     188.564 196.042 167.215  1.00 26.38           C  
ATOM  12617  CD1 ILE B 931     191.314 197.358 166.547  1.00 24.87           C  
ATOM  12618  N   GLY B 932     188.914 192.430 166.713  1.00 25.43           N  
ATOM  12619  CA  GLY B 932     188.093 191.405 167.346  1.00 26.00           C  
ATOM  12620  C   GLY B 932     188.903 190.608 168.371  1.00 26.28           C  
ATOM  12621  O   GLY B 932     188.388 190.228 169.425  1.00 27.47           O  
ATOM  12622  N   LYS B 933     190.176 190.368 168.075  1.00 26.02           N  
ATOM  12623  CA  LYS B 933     191.034 189.648 169.005  1.00 26.21           C  
ATOM  12624  C   LYS B 933     191.253 190.439 170.288  1.00 26.91           C  
ATOM  12625  O   LYS B 933     191.350 189.853 171.370  1.00 28.10           O  
ATOM  12626  CB  LYS B 933     192.369 189.295 168.361  1.00 26.38           C  
ATOM  12627  CG  LYS B 933     192.268 188.218 167.301  1.00 26.52           C  
ATOM  12628  CD  LYS B 933     193.620 187.906 166.692  1.00 26.67           C  
ATOM  12629  CE  LYS B 933     193.506 186.825 165.627  1.00 27.34           C  
ATOM  12630  NZ  LYS B 933     194.823 186.524 164.998  1.00 27.97           N  
ATOM  12631  N   ILE B 934     191.315 191.765 170.181  1.00 26.74           N  
ATOM  12632  CA  ILE B 934     191.500 192.601 171.360  1.00 26.42           C  
ATOM  12633  C   ILE B 934     190.310 192.446 172.278  1.00 28.48           C  
ATOM  12634  O   ILE B 934     190.471 192.341 173.495  1.00 28.68           O  
ATOM  12635  CB  ILE B 934     191.659 194.096 171.006  1.00 26.52           C  
ATOM  12636  CG1 ILE B 934     192.936 194.342 170.176  1.00 25.67           C  
ATOM  12637  CG2 ILE B 934     191.652 194.952 172.272  1.00 27.09           C  
ATOM  12638  CD1 ILE B 934     194.235 193.928 170.829  1.00 25.23           C  
ATOM  12639  N   GLN B 935     189.116 192.419 171.703  1.00 27.35           N  
ATOM  12640  CA  GLN B 935     187.920 192.273 172.515  1.00 27.25           C  
ATOM  12641  C   GLN B 935     187.910 190.949 173.250  1.00 28.71           C  
ATOM  12642  O   GLN B 935     187.540 190.892 174.421  1.00 29.23           O  
ATOM  12643  CB  GLN B 935     186.674 192.344 171.659  1.00 27.68           C  
ATOM  12644  CG  GLN B 935     186.418 193.665 171.084  1.00 27.73           C  
ATOM  12645  CD  GLN B 935     185.222 193.648 170.219  1.00 28.38           C  
ATOM  12646  OE1 GLN B 935     184.833 192.612 169.676  1.00 28.44           O  
ATOM  12647  NE2 GLN B 935     184.613 194.788 170.089  1.00 28.70           N  
ATOM  12648  N   ASP B 936     188.340 189.886 172.581  1.00 27.92           N  
ATOM  12649  CA  ASP B 936     188.347 188.582 173.223  1.00 28.16           C  
ATOM  12650  C   ASP B 936     189.371 188.521 174.338  1.00 28.87           C  
ATOM  12651  O   ASP B 936     189.111 187.942 175.393  1.00 29.70           O  
ATOM  12652  CB  ASP B 936     188.640 187.482 172.210  1.00 28.30           C  
ATOM  12653  CG  ASP B 936     187.483 187.207 171.263  1.00 28.50           C  
ATOM  12654  OD1 ASP B 936     186.383 187.630 171.534  1.00 28.13           O  
ATOM  12655  OD2 ASP B 936     187.713 186.558 170.273  1.00 27.85           O  
ATOM  12656  N   SER B 937     190.529 189.134 174.126  1.00 28.06           N  
ATOM  12657  CA  SER B 937     191.565 189.128 175.145  1.00 28.90           C  
ATOM  12658  C   SER B 937     191.113 189.876 176.389  1.00 29.93           C  
ATOM  12659  O   SER B 937     191.267 189.381 177.511  1.00 30.04           O  
ATOM  12660  CB  SER B 937     192.831 189.754 174.605  1.00 28.82           C  
ATOM  12661  OG  SER B 937     193.842 189.758 175.574  1.00 29.69           O  
ATOM  12662  N   LEU B 938     190.536 191.061 176.192  1.00 29.49           N  
ATOM  12663  CA  LEU B 938     190.081 191.874 177.309  1.00 29.67           C  
ATOM  12664  C   LEU B 938     188.880 191.258 178.005  1.00 29.73           C  
ATOM  12665  O   LEU B 938     188.763 191.337 179.226  1.00 30.13           O  
ATOM  12666  CB  LEU B 938     189.716 193.281 176.826  1.00 29.41           C  
ATOM  12667  CG  LEU B 938     190.869 194.171 176.339  1.00 29.71           C  
ATOM  12668  CD1 LEU B 938     190.277 195.427 175.745  1.00 29.90           C  
ATOM  12669  CD2 LEU B 938     191.797 194.512 177.491  1.00 29.57           C  
ATOM  12670  N   SER B 939     187.981 190.649 177.239  1.00 30.29           N  
ATOM  12671  CA  SER B 939     186.804 190.026 177.814  1.00 29.52           C  
ATOM  12672  C   SER B 939     187.180 188.805 178.643  1.00 30.26           C  
ATOM  12673  O   SER B 939     186.657 188.603 179.741  1.00 30.63           O  
ATOM  12674  CB  SER B 939     185.828 189.641 176.721  1.00 29.93           C  
ATOM  12675  OG  SER B 939     184.689 189.021 177.251  1.00 29.96           O  
ATOM  12676  N   SER B 940     188.083 187.982 178.111  1.00 30.01           N  
ATOM  12677  CA  SER B 940     188.491 186.745 178.761  1.00 30.14           C  
ATOM  12678  C   SER B 940     189.247 186.944 180.070  1.00 30.44           C  
ATOM  12679  O   SER B 940     188.948 186.277 181.063  1.00 30.20           O  
ATOM  12680  CB  SER B 940     189.346 185.934 177.812  1.00 30.26           C  
ATOM  12681  OG  SER B 940     189.756 184.733 178.402  1.00 30.62           O  
ATOM  12682  N   THR B 941     190.235 187.839 180.100  1.00 29.40           N  
ATOM  12683  CA  THR B 941     191.003 187.967 181.331  1.00 30.01           C  
ATOM  12684  C   THR B 941     191.146 189.394 181.837  1.00 30.37           C  
ATOM  12685  O   THR B 941     191.459 190.320 181.091  1.00 29.34           O  
ATOM  12686  CB  THR B 941     192.398 187.344 181.183  1.00 29.76           C  
ATOM  12687  OG1 THR B 941     193.071 187.443 182.441  1.00 29.44           O  
ATOM  12688  CG2 THR B 941     193.218 188.066 180.103  1.00 29.64           C  
ATOM  12689  N   ALA B 942     190.965 189.555 183.145  1.00 29.59           N  
ATOM  12690  CA  ALA B 942     191.104 190.856 183.790  1.00 29.89           C  
ATOM  12691  C   ALA B 942     192.553 191.137 184.175  1.00 29.55           C  
ATOM  12692  O   ALA B 942     192.883 192.243 184.605  1.00 29.23           O  
ATOM  12693  CB  ALA B 942     190.218 190.929 185.024  1.00 30.20           C  
ATOM  12694  N   SER B 943     193.435 190.150 184.000  1.00 29.36           N  
ATOM  12695  CA  SER B 943     194.842 190.328 184.356  1.00 29.30           C  
ATOM  12696  C   SER B 943     195.475 191.303 183.383  1.00 29.49           C  
ATOM  12697  O   SER B 943     196.534 191.882 183.639  1.00 29.05           O  
ATOM  12698  CB  SER B 943     195.587 189.010 184.314  1.00 29.24           C  
ATOM  12699  OG  SER B 943     195.741 188.557 182.998  1.00 29.00           O  
ATOM  12700  N   ALA B 944     194.790 191.492 182.267  1.00 28.95           N  
ATOM  12701  CA  ALA B 944     195.206 192.372 181.199  1.00 29.15           C  
ATOM  12702  C   ALA B 944     195.337 193.804 181.695  1.00 28.78           C  
ATOM  12703  O   ALA B 944     196.157 194.560 181.186  1.00 27.99           O  
ATOM  12704  CB  ALA B 944     194.206 192.304 180.055  1.00 29.38           C  
ATOM  12705  N   LEU B 945     194.524 194.182 182.681  1.00 28.63           N  
ATOM  12706  CA  LEU B 945     194.519 195.548 183.185  1.00 28.25           C  
ATOM  12707  C   LEU B 945     195.132 195.629 184.568  1.00 27.94           C  
ATOM  12708  O   LEU B 945     194.849 196.557 185.331  1.00 28.43           O  
ATOM  12709  CB  LEU B 945     193.088 196.106 183.213  1.00 28.16           C  
ATOM  12710  CG  LEU B 945     192.592 196.779 181.915  1.00 28.06           C  
ATOM  12711  CD1 LEU B 945     192.400 195.748 180.832  1.00 28.98           C  
ATOM  12712  CD2 LEU B 945     191.299 197.492 182.182  1.00 28.78           C  
ATOM  12713  N   GLY B 946     196.028 194.695 184.875  1.00 28.21           N  
ATOM  12714  CA  GLY B 946     196.686 194.670 186.171  1.00 27.96           C  
ATOM  12715  C   GLY B 946     197.360 195.997 186.497  1.00 27.58           C  
ATOM  12716  O   GLY B 946     197.416 196.397 187.657  1.00 27.82           O  
ATOM  12717  N   LYS B 947     197.861 196.699 185.488  1.00 27.68           N  
ATOM  12718  CA  LYS B 947     198.508 197.982 185.727  1.00 27.68           C  
ATOM  12719  C   LYS B 947     197.577 199.029 186.329  1.00 27.33           C  
ATOM  12720  O   LYS B 947     198.031 199.901 187.068  1.00 27.13           O  
ATOM  12721  CB  LYS B 947     199.129 198.517 184.447  1.00 27.07           C  
ATOM  12722  CG  LYS B 947     200.368 197.769 184.017  1.00 27.35           C  
ATOM  12723  CD  LYS B 947     200.933 198.340 182.741  1.00 26.47           C  
ATOM  12724  CE  LYS B 947     202.230 197.662 182.353  1.00 27.17           C  
ATOM  12725  NZ  LYS B 947     202.767 198.193 181.070  1.00 26.97           N  
ATOM  12726  N   LEU B 948     196.283 198.974 186.018  1.00 27.28           N  
ATOM  12727  CA  LEU B 948     195.370 199.961 186.577  1.00 27.25           C  
ATOM  12728  C   LEU B 948     194.838 199.465 187.911  1.00 27.50           C  
ATOM  12729  O   LEU B 948     194.608 200.251 188.835  1.00 27.93           O  
ATOM  12730  CB  LEU B 948     194.198 200.224 185.624  1.00 27.26           C  
ATOM  12731  CG  LEU B 948     194.557 200.776 184.237  1.00 26.58           C  
ATOM  12732  CD1 LEU B 948     193.298 200.883 183.399  1.00 26.91           C  
ATOM  12733  CD2 LEU B 948     195.211 202.128 184.362  1.00 25.51           C  
ATOM  12734  N   GLN B 949     194.659 198.152 188.018  1.00 27.65           N  
ATOM  12735  CA  GLN B 949     194.148 197.561 189.245  1.00 27.04           C  
ATOM  12736  C   GLN B 949     195.161 197.713 190.365  1.00 32.66           C  
ATOM  12737  O   GLN B 949     194.789 197.902 191.520  1.00 25.80           O  
ATOM  12738  CB  GLN B 949     193.797 196.091 189.048  1.00 28.10           C  
ATOM  12739  CG  GLN B 949     193.136 195.445 190.258  1.00 28.51           C  
ATOM  12740  CD  GLN B 949     191.782 196.055 190.599  1.00 29.23           C  
ATOM  12741  OE1 GLN B 949     190.911 196.155 189.725  1.00 29.40           O  
ATOM  12742  NE2 GLN B 949     191.596 196.448 191.857  1.00 29.29           N  
ATOM  12743  N   ASP B 950     196.441 197.648 190.017  1.00 27.43           N  
ATOM  12744  CA  ASP B 950     197.525 197.793 190.975  1.00 26.53           C  
ATOM  12745  C   ASP B 950     197.498 199.156 191.644  1.00 30.91           C  
ATOM  12746  O   ASP B 950     197.789 199.276 192.833  1.00 26.42           O  
ATOM  12747  CB  ASP B 950     198.864 197.577 190.267  1.00 27.29           C  
ATOM  12748  CG  ASP B 950     200.082 197.727 191.163  1.00 26.93           C  
ATOM  12749  OD1 ASP B 950     200.145 197.101 192.195  1.00 26.89           O  
ATOM  12750  OD2 ASP B 950     200.959 198.473 190.796  1.00 26.93           O  
ATOM  12751  N   VAL B 951     197.128 200.185 190.899  1.00 26.43           N  
ATOM  12752  CA  VAL B 951     197.069 201.517 191.467  1.00 27.01           C  
ATOM  12753  C   VAL B 951     195.948 201.575 192.479  1.00 27.53           C  
ATOM  12754  O   VAL B 951     196.112 202.110 193.579  1.00 28.68           O  
ATOM  12755  CB  VAL B 951     196.853 202.571 190.374  1.00 27.42           C  
ATOM  12756  CG1 VAL B 951     196.623 203.946 190.997  1.00 27.55           C  
ATOM  12757  CG2 VAL B 951     198.060 202.588 189.476  1.00 27.43           C  
ATOM  12758  N   VAL B 952     194.813 201.002 192.110  1.00 27.51           N  
ATOM  12759  CA  VAL B 952     193.662 200.973 192.989  1.00 27.06           C  
ATOM  12760  C   VAL B 952     193.974 200.203 194.261  1.00 27.36           C  
ATOM  12761  O   VAL B 952     193.599 200.626 195.356  1.00 28.33           O  
ATOM  12762  CB  VAL B 952     192.464 200.326 192.272  1.00 28.30           C  
ATOM  12763  CG1 VAL B 952     191.316 200.103 193.242  1.00 29.10           C  
ATOM  12764  CG2 VAL B 952     192.028 201.219 191.123  1.00 28.26           C  
ATOM  12765  N   ASN B 953     194.646 199.066 194.121  1.00 27.30           N  
ATOM  12766  CA  ASN B 953     194.945 198.241 195.274  1.00 26.79           C  
ATOM  12767  C   ASN B 953     195.917 198.911 196.223  1.00 29.61           C  
ATOM  12768  O   ASN B 953     195.722 198.862 197.437  1.00 28.49           O  
ATOM  12769  CB  ASN B 953     195.518 196.912 194.845  1.00 27.53           C  
ATOM  12770  CG  ASN B 953     194.525 196.027 194.197  1.00 28.16           C  
ATOM  12771  OD1 ASN B 953     193.312 196.249 194.263  1.00 28.49           O  
ATOM  12772  ND2 ASN B 953     195.017 194.995 193.571  1.00 29.09           N  
ATOM  12773  N   GLN B 954     196.949 199.562 195.697  1.00 26.97           N  
ATOM  12774  CA  GLN B 954     197.909 200.193 196.584  1.00 26.37           C  
ATOM  12775  C   GLN B 954     197.300 201.358 197.333  1.00 27.95           C  
ATOM  12776  O   GLN B 954     197.601 201.561 198.511  1.00 28.17           O  
ATOM  12777  CB  GLN B 954     199.146 200.652 195.831  1.00 26.39           C  
ATOM  12778  CG  GLN B 954     200.024 199.528 195.349  1.00 26.19           C  
ATOM  12779  CD  GLN B 954     201.248 200.026 194.619  1.00 25.99           C  
ATOM  12780  OE1 GLN B 954     201.802 201.092 194.940  1.00 25.73           O  
ATOM  12781  NE2 GLN B 954     201.683 199.264 193.627  1.00 25.77           N  
ATOM  12782  N   ASN B 955     196.428 202.113 196.678  1.00 27.19           N  
ATOM  12783  CA  ASN B 955     195.807 203.233 197.357  1.00 27.34           C  
ATOM  12784  C   ASN B 955     194.854 202.738 198.434  1.00 27.88           C  
ATOM  12785  O   ASN B 955     194.787 203.310 199.525  1.00 29.02           O  
ATOM  12786  CB  ASN B 955     195.096 204.113 196.360  1.00 27.96           C  
ATOM  12787  CG  ASN B 955     196.051 204.915 195.538  1.00 27.76           C  
ATOM  12788  OD1 ASN B 955     197.160 205.229 195.977  1.00 27.47           O  
ATOM  12789  ND2 ASN B 955     195.648 205.245 194.342  1.00 27.68           N  
ATOM  12790  N   ALA B 956     194.146 201.646 198.152  1.00 27.78           N  
ATOM  12791  CA  ALA B 956     193.244 201.081 199.136  1.00 27.91           C  
ATOM  12792  C   ALA B 956     194.013 200.589 200.348  1.00 28.31           C  
ATOM  12793  O   ALA B 956     193.595 200.818 201.481  1.00 29.78           O  
ATOM  12794  CB  ALA B 956     192.456 199.939 198.530  1.00 28.61           C  
ATOM  12795  N   GLN B 957     195.163 199.962 200.118  1.00 27.91           N  
ATOM  12796  CA  GLN B 957     195.973 199.462 201.216  1.00 28.31           C  
ATOM  12797  C   GLN B 957     196.525 200.592 202.054  1.00 29.25           C  
ATOM  12798  O   GLN B 957     196.575 200.489 203.281  1.00 30.49           O  
ATOM  12799  CB  GLN B 957     197.123 198.610 200.700  1.00 28.51           C  
ATOM  12800  CG  GLN B 957     196.704 197.284 200.132  1.00 28.31           C  
ATOM  12801  CD  GLN B 957     197.865 196.562 199.501  1.00 29.39           C  
ATOM  12802  OE1 GLN B 957     198.974 197.102 199.434  1.00 28.82           O  
ATOM  12803  NE2 GLN B 957     197.628 195.345 199.033  1.00 29.00           N  
ATOM  12804  N   ALA B 958     196.922 201.686 201.412  1.00 28.68           N  
ATOM  12805  CA  ALA B 958     197.460 202.811 202.153  1.00 28.60           C  
ATOM  12806  C   ALA B 958     196.428 203.337 203.136  1.00 28.70           C  
ATOM  12807  O   ALA B 958     196.763 203.667 204.276  1.00 30.35           O  
ATOM  12808  CB  ALA B 958     197.889 203.912 201.201  1.00 28.64           C  
ATOM  12809  N   LEU B 959     195.166 203.383 202.715  1.00 28.68           N  
ATOM  12810  CA  LEU B 959     194.119 203.856 203.604  1.00 28.69           C  
ATOM  12811  C   LEU B 959     193.653 202.810 204.588  1.00 29.87           C  
ATOM  12812  O   LEU B 959     193.293 203.147 205.714  1.00 31.31           O  
ATOM  12813  CB  LEU B 959     192.934 204.383 202.810  1.00 28.60           C  
ATOM  12814  CG  LEU B 959     193.183 205.676 202.054  1.00 29.28           C  
ATOM  12815  CD1 LEU B 959     191.983 205.970 201.185  1.00 29.82           C  
ATOM  12816  CD2 LEU B 959     193.416 206.819 203.057  1.00 30.11           C  
ATOM  12817  N   ASN B 960     193.668 201.546 204.207  1.00 29.20           N  
ATOM  12818  CA  ASN B 960     193.253 200.538 205.158  1.00 29.14           C  
ATOM  12819  C   ASN B 960     194.252 200.504 206.296  1.00 31.72           C  
ATOM  12820  O   ASN B 960     193.877 200.328 207.455  1.00 32.15           O  
ATOM  12821  CB  ASN B 960     193.134 199.190 204.497  1.00 29.83           C  
ATOM  12822  CG  ASN B 960     191.947 199.108 203.600  1.00 30.13           C  
ATOM  12823  OD1 ASN B 960     190.978 199.859 203.752  1.00 29.95           O  
ATOM  12824  ND2 ASN B 960     191.997 198.207 202.655  1.00 29.83           N  
ATOM  12825  N   THR B 961     195.524 200.715 205.971  1.00 29.71           N  
ATOM  12826  CA  THR B 961     196.565 200.746 206.980  1.00 30.11           C  
ATOM  12827  C   THR B 961     196.368 201.949 207.877  1.00 30.61           C  
ATOM  12828  O   THR B 961     196.449 201.838 209.101  1.00 32.32           O  
ATOM  12829  CB  THR B 961     197.964 200.809 206.344  1.00 30.53           C  
ATOM  12830  OG1 THR B 961     198.168 199.654 205.521  1.00 30.38           O  
ATOM  12831  CG2 THR B 961     199.041 200.851 207.428  1.00 31.51           C  
ATOM  12832  N   LEU B 962     196.085 203.099 207.272  1.00 30.60           N  
ATOM  12833  CA  LEU B 962     195.917 204.320 208.032  1.00 30.64           C  
ATOM  12834  C   LEU B 962     194.769 204.192 209.020  1.00 32.33           C  
ATOM  12835  O   LEU B 962     194.898 204.585 210.174  1.00 34.03           O  
ATOM  12836  CB  LEU B 962     195.659 205.496 207.079  1.00 30.29           C  
ATOM  12837  CG  LEU B 962     195.496 206.880 207.715  1.00 31.07           C  
ATOM  12838  CD1 LEU B 962     196.777 207.267 208.444  1.00 31.38           C  
ATOM  12839  CD2 LEU B 962     195.166 207.901 206.629  1.00 30.88           C  
ATOM  12840  N   VAL B 963     193.655 203.611 208.595  1.00 31.41           N  
ATOM  12841  CA  VAL B 963     192.536 203.452 209.509  1.00 32.02           C  
ATOM  12842  C   VAL B 963     192.855 202.471 210.617  1.00 32.57           C  
ATOM  12843  O   VAL B 963     192.550 202.718 211.779  1.00 34.87           O  
ATOM  12844  CB  VAL B 963     191.276 202.988 208.779  1.00 32.51           C  
ATOM  12845  CG1 VAL B 963     190.180 202.648 209.782  1.00 36.85           C  
ATOM  12846  CG2 VAL B 963     190.817 204.076 207.886  1.00 32.93           C  
ATOM  12847  N   LYS B 964     193.467 201.348 210.281  1.00 32.54           N  
ATOM  12848  CA  LYS B 964     193.769 200.359 211.300  1.00 33.31           C  
ATOM  12849  C   LYS B 964     194.669 200.918 212.388  1.00 33.53           C  
ATOM  12850  O   LYS B 964     194.530 200.541 213.550  1.00 34.73           O  
ATOM  12851  CB  LYS B 964     194.368 199.108 210.679  1.00 33.46           C  
ATOM  12852  CG  LYS B 964     193.346 198.280 209.925  1.00 35.06           C  
ATOM  12853  CD  LYS B 964     193.972 197.081 209.255  1.00 35.29           C  
ATOM  12854  CE  LYS B 964     192.933 196.294 208.472  1.00 37.05           C  
ATOM  12855  NZ  LYS B 964     193.534 195.133 207.766  1.00 37.75           N  
ATOM  12856  N   GLN B 965     195.547 201.858 212.047  1.00 33.06           N  
ATOM  12857  CA  GLN B 965     196.440 202.446 213.041  1.00 33.00           C  
ATOM  12858  C   GLN B 965     195.701 203.158 214.163  1.00 34.13           C  
ATOM  12859  O   GLN B 965     196.270 203.382 215.229  1.00 34.90           O  
ATOM  12860  CB  GLN B 965     197.436 203.414 212.403  1.00 32.77           C  
ATOM  12861  CG  GLN B 965     198.515 202.740 211.611  1.00 32.90           C  
ATOM  12862  CD  GLN B 965     199.341 201.842 212.468  1.00 33.29           C  
ATOM  12863  OE1 GLN B 965     199.074 200.638 212.504  1.00 33.51           O  
ATOM  12864  NE2 GLN B 965     200.318 202.388 213.173  1.00 33.13           N  
ATOM  12865  N   LEU B 966     194.444 203.514 213.951  1.00 33.81           N  
ATOM  12866  CA  LEU B 966     193.675 204.192 214.983  1.00 34.29           C  
ATOM  12867  C   LEU B 966     193.452 203.291 216.188  1.00 35.41           C  
ATOM  12868  O   LEU B 966     193.231 203.774 217.300  1.00 36.44           O  
ATOM  12869  CB  LEU B 966     192.320 204.635 214.434  1.00 34.65           C  
ATOM  12870  CG  LEU B 966     192.339 205.760 213.403  1.00 34.13           C  
ATOM  12871  CD1 LEU B 966     190.972 205.867 212.777  1.00 35.61           C  
ATOM  12872  CD2 LEU B 966     192.706 207.082 214.085  1.00 34.24           C  
ATOM  12873  N   SER B 967     193.502 201.979 215.972  1.00 35.07           N  
ATOM  12874  CA  SER B 967     193.262 201.014 217.034  1.00 36.03           C  
ATOM  12875  C   SER B 967     194.501 200.762 217.888  1.00 35.53           C  
ATOM  12876  O   SER B 967     194.438 200.031 218.877  1.00 36.60           O  
ATOM  12877  CB  SER B 967     192.777 199.701 216.462  1.00 37.92           C  
ATOM  12878  OG  SER B 967     193.796 199.038 215.772  1.00 35.78           O  
ATOM  12879  N   SER B 968     195.642 201.319 217.498  1.00 35.14           N  
ATOM  12880  CA  SER B 968     196.864 201.094 218.254  1.00 35.03           C  
ATOM  12881  C   SER B 968     196.929 201.965 219.501  1.00 36.14           C  
ATOM  12882  O   SER B 968     196.410 203.081 219.531  1.00 36.66           O  
ATOM  12883  CB  SER B 968     198.067 201.338 217.381  1.00 34.91           C  
ATOM  12884  OG  SER B 968     198.146 200.386 216.373  1.00 34.77           O  
ATOM  12885  N   ASN B 969     197.573 201.454 220.542  1.00 35.88           N  
ATOM  12886  CA  ASN B 969     197.722 202.208 221.776  1.00 35.80           C  
ATOM  12887  C   ASN B 969     198.923 203.137 221.764  1.00 36.01           C  
ATOM  12888  O   ASN B 969     198.907 204.190 222.393  1.00 36.78           O  
ATOM  12889  CB  ASN B 969     197.828 201.264 222.950  1.00 36.68           C  
ATOM  12890  CG  ASN B 969     196.543 200.582 223.281  1.00 37.45           C  
ATOM  12891  OD1 ASN B 969     195.451 201.087 223.010  1.00 37.98           O  
ATOM  12892  ND2 ASN B 969     196.648 199.423 223.869  1.00 37.63           N  
ATOM  12893  N   PHE B 970     199.997 202.729 221.109  1.00 35.75           N  
ATOM  12894  CA  PHE B 970     201.227 203.514 221.080  1.00 35.42           C  
ATOM  12895  C   PHE B 970     201.757 203.845 222.468  1.00 36.13           C  
ATOM  12896  O   PHE B 970     202.387 204.884 222.662  1.00 36.48           O  
ATOM  12897  CB  PHE B 970     201.018 204.827 220.331  1.00 35.27           C  
ATOM  12898  CG  PHE B 970     200.486 204.675 218.959  1.00 34.95           C  
ATOM  12899  CD1 PHE B 970     199.209 205.091 218.655  1.00 34.75           C  
ATOM  12900  CD2 PHE B 970     201.256 204.125 217.965  1.00 34.72           C  
ATOM  12901  CE1 PHE B 970     198.720 204.966 217.382  1.00 34.39           C  
ATOM  12902  CE2 PHE B 970     200.767 203.992 216.693  1.00 34.26           C  
ATOM  12903  CZ  PHE B 970     199.501 204.419 216.399  1.00 34.13           C  
ATOM  12904  N   GLY B 971     201.516 202.973 223.443  1.00 36.61           N  
ATOM  12905  CA  GLY B 971     201.976 203.208 224.804  1.00 36.78           C  
ATOM  12906  C   GLY B 971     200.872 203.745 225.704  1.00 37.06           C  
ATOM  12907  O   GLY B 971     201.029 203.800 226.925  1.00 37.53           O  
ATOM  12908  N   ALA B 972     199.758 204.148 225.115  1.00 36.95           N  
ATOM  12909  CA  ALA B 972     198.631 204.656 225.869  1.00 37.44           C  
ATOM  12910  C   ALA B 972     197.889 203.520 226.549  1.00 38.06           C  
ATOM  12911  O   ALA B 972     198.014 202.359 226.152  1.00 38.24           O  
ATOM  12912  CB  ALA B 972     197.679 205.432 224.978  1.00 38.23           C  
ATOM  12913  N   ILE B 973     197.113 203.857 227.564  1.00 39.21           N  
ATOM  12914  CA  ILE B 973     196.277 202.880 228.252  1.00 39.40           C  
ATOM  12915  C   ILE B 973     195.106 202.415 227.386  1.00 39.29           C  
ATOM  12916  O   ILE B 973     194.614 201.299 227.551  1.00 39.29           O  
ATOM  12917  CB  ILE B 973     195.795 203.420 229.619  1.00 40.42           C  
ATOM  12918  CG1 ILE B 973     195.016 204.752 229.481  1.00 41.26           C  
ATOM  12919  CG2 ILE B 973     196.983 203.601 230.541  1.00 40.78           C  
ATOM  12920  CD1 ILE B 973     193.519 204.605 229.514  1.00 44.07           C  
ATOM  12921  N   SER B 974     194.666 203.262 226.464  1.00 39.51           N  
ATOM  12922  CA  SER B 974     193.600 202.896 225.538  1.00 39.34           C  
ATOM  12923  C   SER B 974     193.748 203.614 224.213  1.00 39.44           C  
ATOM  12924  O   SER B 974     194.105 204.788 224.166  1.00 39.65           O  
ATOM  12925  CB  SER B 974     192.242 203.212 226.117  1.00 40.51           C  
ATOM  12926  OG  SER B 974     191.232 202.909 225.190  1.00 40.79           O  
ATOM  12927  N   SER B 975     193.420 202.911 223.131  1.00 39.03           N  
ATOM  12928  CA  SER B 975     193.440 203.458 221.780  1.00 37.99           C  
ATOM  12929  C   SER B 975     192.280 204.401 221.525  1.00 39.16           C  
ATOM  12930  O   SER B 975     192.260 205.113 220.520  1.00 38.94           O  
ATOM  12931  CB  SER B 975     193.373 202.354 220.756  1.00 38.04           C  
ATOM  12932  OG  SER B 975     192.129 201.717 220.788  1.00 38.79           O  
ATOM  12933  N   VAL B 976     191.296 204.379 222.411  1.00 39.67           N  
ATOM  12934  CA  VAL B 976     190.116 205.194 222.232  1.00 40.08           C  
ATOM  12935  C   VAL B 976     190.212 206.466 223.050  1.00 42.54           C  
ATOM  12936  O   VAL B 976     190.302 206.438 224.277  1.00 41.92           O  
ATOM  12937  CB  VAL B 976     188.862 204.403 222.616  1.00 41.15           C  
ATOM  12938  CG1 VAL B 976     187.621 205.263 222.461  1.00 41.98           C  
ATOM  12939  CG2 VAL B 976     188.766 203.179 221.741  1.00 41.18           C  
ATOM  12940  N   LEU B 977     190.171 207.582 222.356  1.00 40.93           N  
ATOM  12941  CA  LEU B 977     190.350 208.878 222.970  1.00 41.24           C  
ATOM  12942  C   LEU B 977     189.256 209.183 223.973  1.00 43.75           C  
ATOM  12943  O   LEU B 977     189.512 209.754 225.033  1.00 44.51           O  
ATOM  12944  CB  LEU B 977     190.390 209.930 221.869  1.00 40.40           C  
ATOM  12945  CG  LEU B 977     190.611 211.356 222.278  1.00 41.08           C  
ATOM  12946  CD1 LEU B 977     191.906 211.487 223.037  1.00 40.72           C  
ATOM  12947  CD2 LEU B 977     190.649 212.191 221.025  1.00 39.51           C  
ATOM  12948  N   ASN B 978     188.037 208.781 223.652  1.00 43.10           N  
ATOM  12949  CA  ASN B 978     186.914 209.042 224.535  1.00 43.79           C  
ATOM  12950  C   ASN B 978     187.014 208.237 225.824  1.00 45.51           C  
ATOM  12951  O   ASN B 978     186.541 208.686 226.867  1.00 46.63           O  
ATOM  12952  CB  ASN B 978     185.614 208.760 223.820  1.00 45.44           C  
ATOM  12953  CG  ASN B 978     185.310 209.808 222.810  1.00 46.71           C  
ATOM  12954  OD1 ASN B 978     185.723 210.962 222.958  1.00 45.12           O  
ATOM  12955  ND2 ASN B 978     184.611 209.439 221.770  1.00 48.32           N  
ATOM  12956  N   ASP B 979     187.642 207.061 225.766  1.00 44.79           N  
ATOM  12957  CA  ASP B 979     187.784 206.228 226.951  1.00 44.27           C  
ATOM  12958  C   ASP B 979     188.855 206.794 227.865  1.00 47.71           C  
ATOM  12959  O   ASP B 979     188.796 206.624 229.081  1.00 48.25           O  
ATOM  12960  CB  ASP B 979     188.127 204.785 226.585  1.00 44.47           C  
ATOM  12961  CG  ASP B 979     186.974 204.018 225.908  1.00 44.20           C  
ATOM  12962  OD1 ASP B 979     185.840 204.428 225.997  1.00 45.43           O  
ATOM  12963  OD2 ASP B 979     187.256 203.012 225.302  1.00 44.34           O  
ATOM  12964  N   ILE B 980     189.836 207.483 227.293  1.00 44.11           N  
ATOM  12965  CA  ILE B 980     190.831 208.129 228.135  1.00 45.19           C  
ATOM  12966  C   ILE B 980     190.195 209.301 228.861  1.00 47.54           C  
ATOM  12967  O   ILE B 980     190.344 209.446 230.072  1.00 50.44           O  
ATOM  12968  CB  ILE B 980     192.025 208.658 227.331  1.00 44.04           C  
ATOM  12969  CG1 ILE B 980     192.808 207.499 226.743  1.00 42.74           C  
ATOM  12970  CG2 ILE B 980     192.919 209.527 228.238  1.00 44.01           C  
ATOM  12971  CD1 ILE B 980     193.809 207.916 225.702  1.00 41.51           C  
ATOM  12972  N   LEU B 981     189.471 210.125 228.118  1.00 45.63           N  
ATOM  12973  CA  LEU B 981     188.862 211.324 228.678  1.00 46.89           C  
ATOM  12974  C   LEU B 981     187.801 211.021 229.731  1.00 48.53           C  
ATOM  12975  O   LEU B 981     187.643 211.775 230.690  1.00 50.38           O  
ATOM  12976  CB  LEU B 981     188.258 212.153 227.546  1.00 45.97           C  
ATOM  12977  CG  LEU B 981     189.269 212.805 226.578  1.00 44.15           C  
ATOM  12978  CD1 LEU B 981     188.531 213.351 225.374  1.00 42.74           C  
ATOM  12979  CD2 LEU B 981     190.007 213.936 227.284  1.00 42.88           C  
ATOM  12980  N   SER B 982     187.072 209.922 229.565  1.00 48.92           N  
ATOM  12981  CA  SER B 982     186.040 209.558 230.525  1.00 50.00           C  
ATOM  12982  C   SER B 982     186.622 208.924 231.789  1.00 52.05           C  
ATOM  12983  O   SER B 982     185.907 208.706 232.765  1.00 54.33           O  
ATOM  12984  CB  SER B 982     185.040 208.611 229.889  1.00 50.57           C  
ATOM  12985  OG  SER B 982     185.589 207.341 229.685  1.00 50.14           O  
ATOM  12986  N   ARG B 983     187.909 208.585 231.765  1.00 50.87           N  
ATOM  12987  CA  ARG B 983     188.536 207.919 232.898  1.00 52.35           C  
ATOM  12988  C   ARG B 983     189.507 208.798 233.663  1.00 53.59           C  
ATOM  12989  O   ARG B 983     189.610 208.687 234.885  1.00 58.11           O  
ATOM  12990  CB  ARG B 983     189.273 206.667 232.448  1.00 52.90           C  
ATOM  12991  CG  ARG B 983     188.381 205.498 232.083  1.00 53.78           C  
ATOM  12992  CD  ARG B 983     189.107 204.395 231.410  1.00 53.32           C  
ATOM  12993  NE  ARG B 983     190.235 203.924 232.182  1.00 55.40           N  
ATOM  12994  CZ  ARG B 983     190.952 202.826 231.890  1.00 57.63           C  
ATOM  12995  NH1 ARG B 983     190.618 202.070 230.866  1.00 57.10           N  
ATOM  12996  NH2 ARG B 983     191.995 202.512 232.631  1.00 57.71           N  
ATOM  12997  N   LEU B 984     190.238 209.655 232.967  1.00 51.66           N  
ATOM  12998  CA  LEU B 984     191.266 210.429 233.639  1.00 51.71           C  
ATOM  12999  C   LEU B 984     191.029 211.933 233.656  1.00 51.99           C  
ATOM  13000  O   LEU B 984     190.578 212.527 232.679  1.00 51.75           O  
ATOM  13001  CB  LEU B 984     192.611 210.148 232.970  1.00 50.03           C  
ATOM  13002  CG  LEU B 984     193.077 208.685 232.942  1.00 50.60           C  
ATOM  13003  CD1 LEU B 984     194.367 208.609 232.148  1.00 47.20           C  
ATOM  13004  CD2 LEU B 984     193.284 208.171 234.361  1.00 54.99           C  
ATOM  13005  N   ASP B 985     191.420 212.550 234.761  1.00 52.44           N  
ATOM  13006  CA  ASP B 985     191.452 213.997 234.900  1.00 52.06           C  
ATOM  13007  C   ASP B 985     192.551 214.536 233.991  1.00 51.41           C  
ATOM  13008  O   ASP B 985     193.546 213.842 233.791  1.00 48.70           O  
ATOM  13009  CB  ASP B 985     191.744 214.379 236.351  1.00 53.07           C  
ATOM  13010  CG  ASP B 985     190.600 214.126 237.284  1.00 55.10           C  
ATOM  13011  OD1 ASP B 985     189.485 214.023 236.830  1.00 55.20           O  
ATOM  13012  OD2 ASP B 985     190.853 214.021 238.457  1.00 57.64           O  
ATOM  13013  N   PRO B 986     192.442 215.770 233.479  1.00 50.18           N  
ATOM  13014  CA  PRO B 986     193.393 216.420 232.587  1.00 48.64           C  
ATOM  13015  C   PRO B 986     194.890 216.230 232.917  1.00 49.00           C  
ATOM  13016  O   PRO B 986     195.647 215.884 232.013  1.00 46.78           O  
ATOM  13017  CB  PRO B 986     192.947 217.887 232.673  1.00 48.92           C  
ATOM  13018  CG  PRO B 986     191.454 217.785 232.874  1.00 49.91           C  
ATOM  13019  CD  PRO B 986     191.262 216.601 233.800  1.00 50.43           C  
ATOM  13020  N   PRO B 987     195.371 216.362 234.166  1.00 49.37           N  
ATOM  13021  CA  PRO B 987     196.783 216.246 234.495  1.00 49.46           C  
ATOM  13022  C   PRO B 987     197.365 214.890 234.102  1.00 48.45           C  
ATOM  13023  O   PRO B 987     198.577 214.752 233.954  1.00 48.12           O  
ATOM  13024  CB  PRO B 987     196.791 216.430 236.015  1.00 53.41           C  
ATOM  13025  CG  PRO B 987     195.525 217.188 236.317  1.00 55.15           C  
ATOM  13026  CD  PRO B 987     194.523 216.641 235.338  1.00 51.00           C  
ATOM  13027  N   GLU B 988     196.499 213.884 233.971  1.00 48.29           N  
ATOM  13028  CA  GLU B 988     196.925 212.541 233.602  1.00 46.91           C  
ATOM  13029  C   GLU B 988     196.413 212.164 232.216  1.00 45.99           C  
ATOM  13030  O   GLU B 988     197.059 211.406 231.486  1.00 44.93           O  
ATOM  13031  CB  GLU B 988     196.447 211.547 234.656  1.00 48.74           C  
ATOM  13032  CG  GLU B 988     197.075 211.781 236.032  1.00 49.32           C  
ATOM  13033  CD  GLU B 988     196.573 210.849 237.091  1.00 50.78           C  
ATOM  13034  OE1 GLU B 988     195.670 210.106 236.818  1.00 51.56           O  
ATOM  13035  OE2 GLU B 988     197.096 210.882 238.179  1.00 49.52           O  
ATOM  13036  N   ALA B 989     195.239 212.682 231.863  1.00 46.52           N  
ATOM  13037  CA  ALA B 989     194.626 212.387 230.579  1.00 44.66           C  
ATOM  13038  C   ALA B 989     195.494 212.919 229.467  1.00 43.22           C  
ATOM  13039  O   ALA B 989     195.628 212.288 228.423  1.00 41.17           O  
ATOM  13040  CB  ALA B 989     193.243 213.003 230.483  1.00 46.42           C  
ATOM  13041  N   GLU B 990     196.107 214.074 229.700  1.00 43.51           N  
ATOM  13042  CA  GLU B 990     196.942 214.705 228.697  1.00 40.65           C  
ATOM  13043  C   GLU B 990     198.145 213.848 228.365  1.00 40.80           C  
ATOM  13044  O   GLU B 990     198.608 213.844 227.231  1.00 39.97           O  
ATOM  13045  CB  GLU B 990     197.381 216.093 229.150  1.00 41.34           C  
ATOM  13046  CG  GLU B 990     196.253 217.128 229.174  1.00 41.80           C  
ATOM  13047  CD  GLU B 990     196.689 218.466 229.692  1.00 42.35           C  
ATOM  13048  OE1 GLU B 990     197.837 218.601 230.044  1.00 41.61           O  
ATOM  13049  OE2 GLU B 990     195.873 219.356 229.739  1.00 42.54           O  
ATOM  13050  N   VAL B 991     198.663 213.120 229.342  1.00 40.60           N  
ATOM  13051  CA  VAL B 991     199.813 212.277 229.084  1.00 39.93           C  
ATOM  13052  C   VAL B 991     199.417 211.135 228.171  1.00 39.68           C  
ATOM  13053  O   VAL B 991     200.113 210.831 227.199  1.00 40.12           O  
ATOM  13054  CB  VAL B 991     200.389 211.727 230.392  1.00 40.91           C  
ATOM  13055  CG1 VAL B 991     201.488 210.705 230.099  1.00 39.51           C  
ATOM  13056  CG2 VAL B 991     200.925 212.886 231.212  1.00 42.58           C  
ATOM  13057  N   GLN B 992     198.284 210.515 228.468  1.00 39.37           N  
ATOM  13058  CA  GLN B 992     197.827 209.402 227.655  1.00 38.61           C  
ATOM  13059  C   GLN B 992     197.480 209.869 226.250  1.00 39.65           C  
ATOM  13060  O   GLN B 992     197.730 209.163 225.269  1.00 39.05           O  
ATOM  13061  CB  GLN B 992     196.613 208.759 228.302  1.00 40.94           C  
ATOM  13062  CG  GLN B 992     196.905 208.154 229.618  1.00 40.92           C  
ATOM  13063  CD  GLN B 992     197.968 207.151 229.517  1.00 39.80           C  
ATOM  13064  OE1 GLN B 992     197.930 206.298 228.631  1.00 39.73           O  
ATOM  13065  NE2 GLN B 992     198.947 207.223 230.404  1.00 40.04           N  
ATOM  13066  N   ILE B 993     196.941 211.074 226.147  1.00 38.92           N  
ATOM  13067  CA  ILE B 993     196.587 211.619 224.857  1.00 36.93           C  
ATOM  13068  C   ILE B 993     197.831 211.952 224.063  1.00 41.47           C  
ATOM  13069  O   ILE B 993     197.893 211.650 222.875  1.00 36.01           O  
ATOM  13070  CB  ILE B 993     195.665 212.823 224.981  1.00 38.42           C  
ATOM  13071  CG1 ILE B 993     194.353 212.355 225.555  1.00 39.28           C  
ATOM  13072  CG2 ILE B 993     195.453 213.433 223.606  1.00 37.80           C  
ATOM  13073  CD1 ILE B 993     193.445 213.454 226.013  1.00 40.42           C  
ATOM  13074  N   ASP B 994     198.841 212.546 224.692  1.00 39.06           N  
ATOM  13075  CA  ASP B 994     200.062 212.838 223.959  1.00 35.97           C  
ATOM  13076  C   ASP B 994     200.625 211.578 223.329  1.00 36.04           C  
ATOM  13077  O   ASP B 994     201.152 211.622 222.215  1.00 36.22           O  
ATOM  13078  CB  ASP B 994     201.137 213.451 224.853  1.00 37.57           C  
ATOM  13079  CG  ASP B 994     200.937 214.925 225.186  1.00 37.89           C  
ATOM  13080  OD1 ASP B 994     200.140 215.572 224.553  1.00 37.28           O  
ATOM  13081  OD2 ASP B 994     201.616 215.399 226.069  1.00 38.48           O  
ATOM  13082  N   ARG B 995     200.503 210.444 224.012  1.00 36.62           N  
ATOM  13083  CA  ARG B 995     201.007 209.206 223.438  1.00 36.10           C  
ATOM  13084  C   ARG B 995     200.235 208.858 222.164  1.00 35.06           C  
ATOM  13085  O   ARG B 995     200.837 208.463 221.161  1.00 35.77           O  
ATOM  13086  CB  ARG B 995     200.921 208.074 224.447  1.00 36.84           C  
ATOM  13087  CG  ARG B 995     201.878 208.235 225.616  1.00 37.61           C  
ATOM  13088  CD  ARG B 995     201.753 207.158 226.620  1.00 38.25           C  
ATOM  13089  NE  ARG B 995     202.544 207.457 227.803  1.00 38.65           N  
ATOM  13090  CZ  ARG B 995     202.660 206.672 228.896  1.00 38.36           C  
ATOM  13091  NH1 ARG B 995     202.051 205.505 228.973  1.00 37.90           N  
ATOM  13092  NH2 ARG B 995     203.404 207.085 229.910  1.00 37.71           N  
ATOM  13093  N   LEU B 996     198.914 209.053 222.179  1.00 35.61           N  
ATOM  13094  CA  LEU B 996     198.128 208.773 220.983  1.00 34.65           C  
ATOM  13095  C   LEU B 996     198.396 209.781 219.880  1.00 34.84           C  
ATOM  13096  O   LEU B 996     198.435 209.413 218.707  1.00 35.47           O  
ATOM  13097  CB  LEU B 996     196.623 208.782 221.263  1.00 35.16           C  
ATOM  13098  CG  LEU B 996     196.057 207.675 222.146  1.00 36.71           C  
ATOM  13099  CD1 LEU B 996     194.564 207.918 222.317  1.00 38.46           C  
ATOM  13100  CD2 LEU B 996     196.313 206.308 221.526  1.00 36.68           C  
ATOM  13101  N   ILE B 997     198.593 211.047 220.232  1.00 34.25           N  
ATOM  13102  CA  ILE B 997     198.841 212.046 219.207  1.00 33.36           C  
ATOM  13103  C   ILE B 997     200.140 211.764 218.505  1.00 34.00           C  
ATOM  13104  O   ILE B 997     200.216 211.857 217.284  1.00 33.48           O  
ATOM  13105  CB  ILE B 997     198.860 213.484 219.744  1.00 33.82           C  
ATOM  13106  CG1 ILE B 997     197.454 213.892 220.190  1.00 34.34           C  
ATOM  13107  CG2 ILE B 997     199.398 214.437 218.657  1.00 33.44           C  
ATOM  13108  CD1 ILE B 997     197.411 215.185 220.974  1.00 35.21           C  
ATOM  13109  N   THR B 998     201.180 211.432 219.249  1.00 33.64           N  
ATOM  13110  CA  THR B 998     202.446 211.173 218.600  1.00 32.94           C  
ATOM  13111  C   THR B 998     202.309 210.016 217.627  1.00 32.30           C  
ATOM  13112  O   THR B 998     202.779 210.098 216.491  1.00 32.71           O  
ATOM  13113  CB  THR B 998     203.548 210.862 219.619  1.00 34.04           C  
ATOM  13114  OG1 THR B 998     203.740 211.995 220.471  1.00 34.35           O  
ATOM  13115  CG2 THR B 998     204.853 210.550 218.897  1.00 33.17           C  
ATOM  13116  N   GLY B 999     201.655 208.944 218.056  1.00 33.17           N  
ATOM  13117  CA  GLY B 999     201.487 207.777 217.202  1.00 32.74           C  
ATOM  13118  C   GLY B 999     200.642 208.061 215.967  1.00 32.06           C  
ATOM  13119  O   GLY B 999     200.970 207.619 214.864  1.00 32.75           O  
ATOM  13120  N   ARG B1000     199.540 208.776 216.146  1.00 32.14           N  
ATOM  13121  CA  ARG B1000     198.641 209.051 215.042  1.00 31.58           C  
ATOM  13122  C   ARG B1000     199.200 210.099 214.095  1.00 31.94           C  
ATOM  13123  O   ARG B1000     198.991 210.019 212.883  1.00 32.56           O  
ATOM  13124  CB  ARG B1000     197.290 209.465 215.567  1.00 32.49           C  
ATOM  13125  CG  ARG B1000     196.531 208.338 216.205  1.00 32.96           C  
ATOM  13126  CD  ARG B1000     195.253 208.777 216.743  1.00 33.34           C  
ATOM  13127  NE  ARG B1000     194.498 207.669 217.239  1.00 34.16           N  
ATOM  13128  CZ  ARG B1000     193.290 207.759 217.802  1.00 34.93           C  
ATOM  13129  NH1 ARG B1000     192.705 208.934 217.959  1.00 35.69           N  
ATOM  13130  NH2 ARG B1000     192.675 206.657 218.194  1.00 36.37           N  
ATOM  13131  N   LEU B1001     199.933 211.063 214.628  1.00 31.45           N  
ATOM  13132  CA  LEU B1001     200.547 212.079 213.802  1.00 30.74           C  
ATOM  13133  C   LEU B1001     201.642 211.436 212.975  1.00 32.01           C  
ATOM  13134  O   LEU B1001     201.789 211.727 211.788  1.00 30.91           O  
ATOM  13135  CB  LEU B1001     201.105 213.205 214.676  1.00 31.45           C  
ATOM  13136  CG  LEU B1001     201.748 214.403 213.964  1.00 30.82           C  
ATOM  13137  CD1 LEU B1001     200.735 215.077 213.033  1.00 31.46           C  
ATOM  13138  CD2 LEU B1001     202.239 215.385 215.026  1.00 31.58           C  
ATOM  13139  N   GLN B1002     202.400 210.536 213.597  1.00 30.72           N  
ATOM  13140  CA  GLN B1002     203.450 209.816 212.907  1.00 30.22           C  
ATOM  13141  C   GLN B1002     202.854 208.944 211.814  1.00 32.32           C  
ATOM  13142  O   GLN B1002     203.447 208.798 210.743  1.00 30.56           O  
ATOM  13143  CB  GLN B1002     204.244 208.971 213.894  1.00 30.94           C  
ATOM  13144  CG  GLN B1002     205.440 208.268 213.312  1.00 30.88           C  
ATOM  13145  CD  GLN B1002     206.199 207.524 214.380  1.00 31.16           C  
ATOM  13146  OE1 GLN B1002     205.691 207.328 215.488  1.00 31.31           O  
ATOM  13147  NE2 GLN B1002     207.420 207.103 214.072  1.00 31.21           N  
ATOM  13148  N   SER B1003     201.682 208.366 212.081  1.00 30.38           N  
ATOM  13149  CA  SER B1003     201.003 207.533 211.098  1.00 30.13           C  
ATOM  13150  C   SER B1003     200.628 208.338 209.868  1.00 30.02           C  
ATOM  13151  O   SER B1003     200.855 207.888 208.742  1.00 30.65           O  
ATOM  13152  CB  SER B1003     199.772 206.898 211.690  1.00 31.23           C  
ATOM  13153  OG  SER B1003     199.129 206.104 210.744  1.00 31.68           O  
ATOM  13154  N   LEU B1004     200.087 209.541 210.065  1.00 30.31           N  
ATOM  13155  CA  LEU B1004     199.769 210.381 208.920  1.00 29.21           C  
ATOM  13156  C   LEU B1004     201.016 210.769 208.165  1.00 29.27           C  
ATOM  13157  O   LEU B1004     201.027 210.734 206.941  1.00 29.83           O  
ATOM  13158  CB  LEU B1004     199.062 211.663 209.335  1.00 30.12           C  
ATOM  13159  CG  LEU B1004     197.645 211.550 209.804  1.00 30.81           C  
ATOM  13160  CD1 LEU B1004     197.241 212.865 210.419  1.00 31.77           C  
ATOM  13161  CD2 LEU B1004     196.736 211.237 208.626  1.00 31.52           C  
ATOM  13162  N   GLN B1005     202.095 211.083 208.866  1.00 29.30           N  
ATOM  13163  CA  GLN B1005     203.306 211.470 208.163  1.00 29.03           C  
ATOM  13164  C   GLN B1005     203.787 210.340 207.278  1.00 28.71           C  
ATOM  13165  O   GLN B1005     204.210 210.575 206.142  1.00 29.30           O  
ATOM  13166  CB  GLN B1005     204.390 211.886 209.152  1.00 29.84           C  
ATOM  13167  CG  GLN B1005     204.099 213.203 209.839  1.00 29.94           C  
ATOM  13168  CD  GLN B1005     205.022 213.493 210.979  1.00 30.28           C  
ATOM  13169  OE1 GLN B1005     205.830 212.649 211.387  1.00 29.97           O  
ATOM  13170  NE2 GLN B1005     204.908 214.696 211.514  1.00 30.56           N  
ATOM  13171  N   THR B1006     203.682 209.109 207.765  1.00 29.10           N  
ATOM  13172  CA  THR B1006     204.062 207.964 206.957  1.00 28.70           C  
ATOM  13173  C   THR B1006     203.167 207.859 205.735  1.00 27.98           C  
ATOM  13174  O   THR B1006     203.656 207.693 204.618  1.00 28.23           O  
ATOM  13175  CB  THR B1006     203.973 206.661 207.766  1.00 29.98           C  
ATOM  13176  OG1 THR B1006     204.887 206.721 208.863  1.00 30.19           O  
ATOM  13177  CG2 THR B1006     204.309 205.464 206.894  1.00 30.09           C  
ATOM  13178  N   TYR B1007     201.862 207.979 205.941  1.00 28.41           N  
ATOM  13179  CA  TYR B1007     200.899 207.901 204.857  1.00 27.55           C  
ATOM  13180  C   TYR B1007     201.146 208.945 203.791  1.00 29.36           C  
ATOM  13181  O   TYR B1007     201.182 208.622 202.605  1.00 27.42           O  
ATOM  13182  CB  TYR B1007     199.485 208.044 205.400  1.00 28.89           C  
ATOM  13183  CG  TYR B1007     198.448 208.209 204.347  1.00 28.42           C  
ATOM  13184  CD1 TYR B1007     197.986 207.127 203.640  1.00 28.83           C  
ATOM  13185  CD2 TYR B1007     197.950 209.463 204.094  1.00 28.43           C  
ATOM  13186  CE1 TYR B1007     197.030 207.312 202.674  1.00 28.78           C  
ATOM  13187  CE2 TYR B1007     197.002 209.641 203.138  1.00 28.47           C  
ATOM  13188  CZ  TYR B1007     196.546 208.577 202.429  1.00 28.51           C  
ATOM  13189  OH  TYR B1007     195.602 208.769 201.466  1.00 29.08           O  
ATOM  13190  N   VAL B1008     201.311 210.192 204.201  1.00 27.44           N  
ATOM  13191  CA  VAL B1008     201.487 211.267 203.247  1.00 26.73           C  
ATOM  13192  C   VAL B1008     202.767 211.084 202.463  1.00 26.95           C  
ATOM  13193  O   VAL B1008     202.778 211.301 201.252  1.00 27.25           O  
ATOM  13194  CB  VAL B1008     201.468 212.635 203.930  1.00 27.83           C  
ATOM  13195  CG1 VAL B1008     201.838 213.712 202.943  1.00 27.35           C  
ATOM  13196  CG2 VAL B1008     200.081 212.894 204.472  1.00 28.29           C  
ATOM  13197  N   THR B1009     203.845 210.695 203.130  1.00 26.99           N  
ATOM  13198  CA  THR B1009     205.094 210.481 202.425  1.00 25.74           C  
ATOM  13199  C   THR B1009     204.919 209.410 201.367  1.00 26.57           C  
ATOM  13200  O   THR B1009     205.388 209.567 200.237  1.00 26.97           O  
ATOM  13201  CB  THR B1009     206.227 210.086 203.379  1.00 26.92           C  
ATOM  13202  OG1 THR B1009     206.454 211.145 204.308  1.00 28.16           O  
ATOM  13203  CG2 THR B1009     207.500 209.824 202.593  1.00 26.59           C  
ATOM  13204  N   GLN B1010     204.234 208.322 201.709  1.00 26.14           N  
ATOM  13205  CA  GLN B1010     204.025 207.264 200.740  1.00 25.14           C  
ATOM  13206  C   GLN B1010     203.166 207.736 199.582  1.00 26.93           C  
ATOM  13207  O   GLN B1010     203.409 207.352 198.438  1.00 25.75           O  
ATOM  13208  CB  GLN B1010     203.370 206.052 201.392  1.00 25.98           C  
ATOM  13209  CG  GLN B1010     204.241 205.347 202.394  1.00 26.10           C  
ATOM  13210  CD  GLN B1010     205.470 204.778 201.785  1.00 25.15           C  
ATOM  13211  OE1 GLN B1010     205.412 204.053 200.791  1.00 25.08           O  
ATOM  13212  NE2 GLN B1010     206.609 205.105 202.370  1.00 24.90           N  
ATOM  13213  N   GLN B1011     202.175 208.585 199.854  1.00 25.93           N  
ATOM  13214  CA  GLN B1011     201.330 209.082 198.781  1.00 25.23           C  
ATOM  13215  C   GLN B1011     202.105 209.998 197.859  1.00 26.26           C  
ATOM  13216  O   GLN B1011     201.883 209.980 196.653  1.00 26.19           O  
ATOM  13217  CB  GLN B1011     200.117 209.835 199.319  1.00 26.21           C  
ATOM  13218  CG  GLN B1011     199.111 208.989 200.032  1.00 27.21           C  
ATOM  13219  CD  GLN B1011     198.456 207.983 199.148  1.00 27.30           C  
ATOM  13220  OE1 GLN B1011     198.867 206.821 199.118  1.00 27.23           O  
ATOM  13221  NE2 GLN B1011     197.426 208.402 198.425  1.00 27.48           N  
ATOM  13222  N   LEU B1012     203.015 210.798 198.406  1.00 25.28           N  
ATOM  13223  CA  LEU B1012     203.808 211.696 197.576  1.00 25.22           C  
ATOM  13224  C   LEU B1012     204.753 210.928 196.676  1.00 25.42           C  
ATOM  13225  O   LEU B1012     204.912 211.264 195.501  1.00 25.65           O  
ATOM  13226  CB  LEU B1012     204.614 212.657 198.445  1.00 25.59           C  
ATOM  13227  CG  LEU B1012     203.838 213.742 199.169  1.00 25.47           C  
ATOM  13228  CD1 LEU B1012     204.723 214.358 200.201  1.00 25.29           C  
ATOM  13229  CD2 LEU B1012     203.404 214.814 198.184  1.00 25.80           C  
ATOM  13230  N   ILE B1013     205.359 209.879 197.204  1.00 25.24           N  
ATOM  13231  CA  ILE B1013     206.266 209.093 196.395  1.00 24.98           C  
ATOM  13232  C   ILE B1013     205.482 208.344 195.331  1.00 25.10           C  
ATOM  13233  O   ILE B1013     205.885 208.311 194.167  1.00 25.53           O  
ATOM  13234  CB  ILE B1013     207.101 208.140 197.255  1.00 25.28           C  
ATOM  13235  CG1 ILE B1013     208.035 208.977 198.145  1.00 25.67           C  
ATOM  13236  CG2 ILE B1013     207.901 207.193 196.358  1.00 26.20           C  
ATOM  13237  CD1 ILE B1013     208.715 208.207 199.247  1.00 26.23           C  
ATOM  13238  N   ARG B1014     204.364 207.736 195.717  1.00 25.33           N  
ATOM  13239  CA  ARG B1014     203.536 207.032 194.754  1.00 24.63           C  
ATOM  13240  C   ARG B1014     203.014 207.998 193.703  1.00 25.04           C  
ATOM  13241  O   ARG B1014     202.922 207.650 192.527  1.00 25.56           O  
ATOM  13242  CB  ARG B1014     202.382 206.314 195.428  1.00 25.45           C  
ATOM  13243  CG  ARG B1014     201.589 205.399 194.498  1.00 25.38           C  
ATOM  13244  CD  ARG B1014     200.515 204.630 195.202  1.00 26.05           C  
ATOM  13245  NE  ARG B1014     201.043 203.684 196.188  1.00 26.17           N  
ATOM  13246  CZ  ARG B1014     200.956 203.822 197.534  1.00 26.40           C  
ATOM  13247  NH1 ARG B1014     200.369 204.876 198.060  1.00 26.57           N  
ATOM  13248  NH2 ARG B1014     201.463 202.890 198.323  1.00 26.33           N  
ATOM  13249  N   ALA B1015     202.667 209.212 194.117  1.00 24.71           N  
ATOM  13250  CA  ALA B1015     202.186 210.214 193.185  1.00 24.22           C  
ATOM  13251  C   ALA B1015     203.247 210.542 192.161  1.00 24.32           C  
ATOM  13252  O   ALA B1015     202.924 210.794 191.005  1.00 24.59           O  
ATOM  13253  CB  ALA B1015     201.762 211.472 193.915  1.00 25.27           C  
ATOM  13254  N   ALA B1016     204.513 210.551 192.568  1.00 24.77           N  
ATOM  13255  CA  ALA B1016     205.581 210.836 191.626  1.00 24.24           C  
ATOM  13256  C   ALA B1016     205.636 209.761 190.552  1.00 23.40           C  
ATOM  13257  O   ALA B1016     205.849 210.060 189.377  1.00 24.29           O  
ATOM  13258  CB  ALA B1016     206.911 210.929 192.346  1.00 25.20           C  
ATOM  13259  N   GLU B1017     205.415 208.511 190.951  1.00 24.04           N  
ATOM  13260  CA  GLU B1017     205.408 207.406 190.000  1.00 23.20           C  
ATOM  13261  C   GLU B1017     204.280 207.555 188.996  1.00 23.70           C  
ATOM  13262  O   GLU B1017     204.480 207.381 187.792  1.00 24.06           O  
ATOM  13263  CB  GLU B1017     205.265 206.071 190.720  1.00 24.18           C  
ATOM  13264  CG  GLU B1017     205.268 204.865 189.802  1.00 24.29           C  
ATOM  13265  CD  GLU B1017     205.153 203.570 190.547  1.00 24.65           C  
ATOM  13266  OE1 GLU B1017     205.143 203.600 191.753  1.00 24.45           O  
ATOM  13267  OE2 GLU B1017     205.069 202.547 189.910  1.00 24.01           O  
ATOM  13268  N   ILE B1018     203.099 207.900 189.491  1.00 23.92           N  
ATOM  13269  CA  ILE B1018     201.945 208.086 188.629  1.00 23.07           C  
ATOM  13270  C   ILE B1018     202.142 209.286 187.730  1.00 23.90           C  
ATOM  13271  O   ILE B1018     201.755 209.249 186.567  1.00 23.01           O  
ATOM  13272  CB  ILE B1018     200.648 208.220 189.434  1.00 23.87           C  
ATOM  13273  CG1 ILE B1018     200.375 206.918 190.224  1.00 24.35           C  
ATOM  13274  CG2 ILE B1018     199.482 208.558 188.513  1.00 23.99           C  
ATOM  13275  CD1 ILE B1018     200.208 205.659 189.401  1.00 25.65           C  
ATOM  13276  N   ARG B1019     202.714 210.358 188.262  1.00 23.35           N  
ATOM  13277  CA  ARG B1019     202.987 211.541 187.469  1.00 22.33           C  
ATOM  13278  C   ARG B1019     203.871 211.182 186.294  1.00 24.25           C  
ATOM  13279  O   ARG B1019     203.607 211.598 185.168  1.00 23.02           O  
ATOM  13280  CB  ARG B1019     203.669 212.598 188.313  1.00 23.33           C  
ATOM  13281  CG  ARG B1019     203.987 213.902 187.614  1.00 22.75           C  
ATOM  13282  CD  ARG B1019     204.724 214.816 188.531  1.00 22.83           C  
ATOM  13283  NE  ARG B1019     206.053 214.306 188.873  1.00 23.23           N  
ATOM  13284  CZ  ARG B1019     207.165 214.462 188.124  1.00 23.28           C  
ATOM  13285  NH1 ARG B1019     207.116 215.126 186.991  1.00 22.85           N  
ATOM  13286  NH2 ARG B1019     208.313 213.951 188.536  1.00 23.43           N  
ATOM  13287  N   ALA B1020     204.914 210.395 186.546  1.00 22.38           N  
ATOM  13288  CA  ALA B1020     205.803 209.974 185.478  1.00 22.38           C  
ATOM  13289  C   ALA B1020     205.056 209.150 184.440  1.00 22.13           C  
ATOM  13290  O   ALA B1020     205.266 209.323 183.238  1.00 22.23           O  
ATOM  13291  CB  ALA B1020     206.954 209.171 186.047  1.00 23.39           C  
ATOM  13292  N   SER B1021     204.156 208.281 184.895  1.00 22.79           N  
ATOM  13293  CA  SER B1021     203.361 207.478 183.979  1.00 22.22           C  
ATOM  13294  C   SER B1021     202.458 208.366 183.145  1.00 21.66           C  
ATOM  13295  O   SER B1021     202.320 208.160 181.941  1.00 22.70           O  
ATOM  13296  CB  SER B1021     202.541 206.451 184.729  1.00 22.92           C  
ATOM  13297  OG  SER B1021     201.789 205.664 183.848  1.00 23.16           O  
ATOM  13298  N   ALA B1022     201.839 209.355 183.776  1.00 21.97           N  
ATOM  13299  CA  ALA B1022     200.971 210.277 183.067  1.00 21.61           C  
ATOM  13300  C   ALA B1022     201.750 211.058 182.031  1.00 21.40           C  
ATOM  13301  O   ALA B1022     201.251 211.300 180.937  1.00 22.47           O  
ATOM  13302  CB  ALA B1022     200.313 211.241 184.026  1.00 23.30           C  
ATOM  13303  N   ASN B1023     202.982 211.435 182.355  1.00 21.59           N  
ATOM  13304  CA  ASN B1023     203.788 212.178 181.404  1.00 20.93           C  
ATOM  13305  C   ASN B1023     204.131 211.304 180.219  1.00 21.35           C  
ATOM  13306  O   ASN B1023     204.118 211.766 179.076  1.00 21.45           O  
ATOM  13307  CB  ASN B1023     205.042 212.706 182.052  1.00 21.23           C  
ATOM  13308  CG  ASN B1023     204.775 213.842 182.963  1.00 21.37           C  
ATOM  13309  OD1 ASN B1023     203.724 214.482 182.901  1.00 21.30           O  
ATOM  13310  ND2 ASN B1023     205.715 214.123 183.816  1.00 21.53           N  
ATOM  13311  N   LEU B1024     204.388 210.027 180.476  1.00 21.35           N  
ATOM  13312  CA  LEU B1024     204.660 209.094 179.402  1.00 20.47           C  
ATOM  13313  C   LEU B1024     203.428 208.905 178.553  1.00 21.29           C  
ATOM  13314  O   LEU B1024     203.517 208.867 177.329  1.00 20.38           O  
ATOM  13315  CB  LEU B1024     205.088 207.738 179.950  1.00 20.57           C  
ATOM  13316  CG  LEU B1024     205.386 206.650 178.912  1.00 20.22           C  
ATOM  13317  CD1 LEU B1024     206.536 207.087 178.009  1.00 20.71           C  
ATOM  13318  CD2 LEU B1024     205.717 205.362 179.638  1.00 20.94           C  
ATOM  13319  N   ALA B1025     202.278 208.769 179.198  1.00 20.90           N  
ATOM  13320  CA  ALA B1025     201.036 208.580 178.482  1.00 20.50           C  
ATOM  13321  C   ALA B1025     200.732 209.781 177.614  1.00 20.38           C  
ATOM  13322  O   ALA B1025     200.295 209.628 176.476  1.00 21.70           O  
ATOM  13323  CB  ALA B1025     199.903 208.349 179.457  1.00 21.92           C  
ATOM  13324  N   ALA B1026     200.986 210.980 178.131  1.00 20.69           N  
ATOM  13325  CA  ALA B1026     200.752 212.188 177.363  1.00 20.50           C  
ATOM  13326  C   ALA B1026     201.701 212.250 176.184  1.00 20.25           C  
ATOM  13327  O   ALA B1026     201.304 212.635 175.083  1.00 21.12           O  
ATOM  13328  CB  ALA B1026     200.916 213.416 178.236  1.00 21.91           C  
ATOM  13329  N   THR B1027     202.948 211.833 176.404  1.00 20.68           N  
ATOM  13330  CA  THR B1027     203.935 211.823 175.339  1.00 19.79           C  
ATOM  13331  C   THR B1027     203.497 210.869 174.259  1.00 21.09           C  
ATOM  13332  O   THR B1027     203.540 211.198 173.075  1.00 19.29           O  
ATOM  13333  CB  THR B1027     205.323 211.397 175.843  1.00 20.02           C  
ATOM  13334  OG1 THR B1027     205.785 212.315 176.831  1.00 20.99           O  
ATOM  13335  CG2 THR B1027     206.307 211.371 174.689  1.00 19.58           C  
ATOM  13336  N   LYS B1028     203.056 209.688 174.660  1.00 19.85           N  
ATOM  13337  CA  LYS B1028     202.610 208.715 173.694  1.00 19.13           C  
ATOM  13338  C   LYS B1028     201.419 209.204 172.936  1.00 20.80           C  
ATOM  13339  O   LYS B1028     201.373 209.077 171.726  1.00 19.99           O  
ATOM  13340  CB  LYS B1028     202.275 207.401 174.361  1.00 19.89           C  
ATOM  13341  CG  LYS B1028     203.463 206.626 174.773  1.00 19.45           C  
ATOM  13342  CD  LYS B1028     203.068 205.428 175.539  1.00 20.12           C  
ATOM  13343  CE  LYS B1028     204.262 204.580 175.850  1.00 20.10           C  
ATOM  13344  NZ  LYS B1028     204.664 203.796 174.670  1.00 20.00           N  
ATOM  13345  N   MET B1029     200.461 209.819 173.583  1.00 20.17           N  
ATOM  13346  CA  MET B1029     199.339 210.256 172.789  1.00 20.10           C  
ATOM  13347  C   MET B1029     199.781 211.290 171.763  1.00 20.96           C  
ATOM  13348  O   MET B1029     199.401 211.223 170.592  1.00 20.56           O  
ATOM  13349  CB  MET B1029     198.245 210.797 173.668  1.00 20.48           C  
ATOM  13350  CG  MET B1029     196.979 211.020 172.942  1.00 20.75           C  
ATOM  13351  SD  MET B1029     195.715 211.576 174.000  1.00 22.22           S  
ATOM  13352  CE  MET B1029     195.320 210.137 174.998  1.00 23.05           C  
ATOM  13353  N   SER B1030     200.639 212.217 172.174  1.00 19.69           N  
ATOM  13354  CA  SER B1030     201.072 213.267 171.273  1.00 19.30           C  
ATOM  13355  C   SER B1030     201.843 212.736 170.080  1.00 19.42           C  
ATOM  13356  O   SER B1030     201.661 213.204 168.962  1.00 20.50           O  
ATOM  13357  CB  SER B1030     201.952 214.248 172.009  1.00 20.06           C  
ATOM  13358  OG  SER B1030     201.231 214.972 172.964  1.00 20.66           O  
ATOM  13359  N   GLU B1031     202.708 211.757 170.310  1.00 19.18           N  
ATOM  13360  CA  GLU B1031     203.548 211.219 169.232  1.00 19.01           C  
ATOM  13361  C   GLU B1031     203.015 209.958 168.525  1.00 19.12           C  
ATOM  13362  O   GLU B1031     203.410 209.681 167.392  1.00 19.32           O  
ATOM  13363  CB  GLU B1031     204.935 210.904 169.788  1.00 18.92           C  
ATOM  13364  CG  GLU B1031     205.629 212.085 170.359  1.00 18.81           C  
ATOM  13365  CD  GLU B1031     206.942 211.757 170.924  1.00 18.88           C  
ATOM  13366  OE1 GLU B1031     207.545 210.813 170.491  1.00 18.97           O  
ATOM  13367  OE2 GLU B1031     207.372 212.451 171.805  1.00 18.92           O  
ATOM  13368  N   CYS B1032     202.168 209.191 169.212  1.00 19.47           N  
ATOM  13369  CA  CYS B1032     201.645 207.889 168.739  1.00 19.35           C  
ATOM  13370  C   CYS B1032     200.276 208.017 168.091  1.00 19.98           C  
ATOM  13371  O   CYS B1032     199.967 207.294 167.115  1.00 20.54           O  
ATOM  13372  CB  CYS B1032     201.595 206.918 169.932  1.00 20.30           C  
ATOM  13373  SG  CYS B1032     201.546 205.205 169.473  1.00 22.36           S  
ATOM  13374  N   VAL B1033     199.381 208.887 168.619  1.00 19.55           N  
ATOM  13375  CA  VAL B1033     198.002 209.070 168.155  1.00 19.54           C  
ATOM  13376  C   VAL B1033     197.872 210.263 167.230  1.00 19.92           C  
ATOM  13377  O   VAL B1033     197.269 210.176 166.164  1.00 20.32           O  
ATOM  13378  CB  VAL B1033     197.057 209.267 169.347  1.00 19.83           C  
ATOM  13379  CG1 VAL B1033     195.664 209.553 168.874  1.00 20.41           C  
ATOM  13380  CG2 VAL B1033     197.068 208.040 170.208  1.00 21.10           C  
ATOM  13381  N   LEU B1034     198.482 211.376 167.622  1.00 20.00           N  
ATOM  13382  CA  LEU B1034     198.404 212.632 166.872  1.00 19.59           C  
ATOM  13383  C   LEU B1034     199.460 212.698 165.779  1.00 19.45           C  
ATOM  13384  O   LEU B1034     199.631 213.730 165.133  1.00 19.75           O  
ATOM  13385  CB  LEU B1034     198.604 213.838 167.798  1.00 19.67           C  
ATOM  13386  CG  LEU B1034     197.375 214.410 168.501  1.00 20.33           C  
ATOM  13387  CD1 LEU B1034     196.847 213.421 169.507  1.00 20.57           C  
ATOM  13388  CD2 LEU B1034     197.758 215.702 169.190  1.00 20.61           C  
ATOM  13389  N   GLY B1035     200.188 211.606 165.603  1.00 19.16           N  
ATOM  13390  CA  GLY B1035     201.271 211.522 164.638  1.00 19.05           C  
ATOM  13391  C   GLY B1035     201.649 210.076 164.383  1.00 18.94           C  
ATOM  13392  O   GLY B1035     200.876 209.162 164.672  1.00 19.40           O  
ATOM  13393  N   GLN B1036     202.806 209.883 163.763  1.00 18.52           N  
ATOM  13394  CA  GLN B1036     203.327 208.561 163.469  1.00 18.35           C  
ATOM  13395  C   GLN B1036     204.755 208.448 163.968  1.00 18.53           C  
ATOM  13396  O   GLN B1036     205.692 208.907 163.315  1.00 18.75           O  
ATOM  13397  CB  GLN B1036     203.288 208.269 161.978  1.00 18.53           C  
ATOM  13398  CG  GLN B1036     203.793 206.898 161.635  1.00 18.53           C  
ATOM  13399  CD  GLN B1036     203.656 206.582 160.191  1.00 18.85           C  
ATOM  13400  OE1 GLN B1036     203.503 207.479 159.356  1.00 19.22           O  
ATOM  13401  NE2 GLN B1036     203.708 205.306 159.871  1.00 18.83           N  
ATOM  13402  N   SER B1037     204.915 207.850 165.132  1.00 18.54           N  
ATOM  13403  CA  SER B1037     206.213 207.713 165.756  1.00 17.94           C  
ATOM  13404  C   SER B1037     207.113 206.795 164.956  1.00 18.09           C  
ATOM  13405  O   SER B1037     206.658 205.791 164.412  1.00 18.36           O  
ATOM  13406  CB  SER B1037     206.060 207.160 167.149  1.00 18.62           C  
ATOM  13407  OG  SER B1037     207.305 206.980 167.737  1.00 18.48           O  
ATOM  13408  N   LYS B1038     208.398 207.130 164.910  1.00 17.86           N  
ATOM  13409  CA  LYS B1038     209.410 206.283 164.288  1.00 17.68           C  
ATOM  13410  C   LYS B1038     210.292 205.656 165.350  1.00 17.90           C  
ATOM  13411  O   LYS B1038     211.370 205.139 165.059  1.00 18.18           O  
ATOM  13412  CB  LYS B1038     210.259 207.071 163.298  1.00 17.15           C  
ATOM  13413  CG  LYS B1038     209.487 207.574 162.104  1.00 17.30           C  
ATOM  13414  CD  LYS B1038     210.389 208.280 161.104  1.00 16.71           C  
ATOM  13415  CE  LYS B1038     209.585 208.797 159.917  1.00 16.42           C  
ATOM  13416  NZ  LYS B1038     208.968 207.681 159.135  1.00 16.90           N  
ATOM  13417  N   ARG B1039     209.848 205.753 166.592  1.00 18.03           N  
ATOM  13418  CA  ARG B1039     210.588 205.236 167.723  1.00 17.96           C  
ATOM  13419  C   ARG B1039     210.288 203.753 167.916  1.00 18.43           C  
ATOM  13420  O   ARG B1039     209.132 203.348 168.059  1.00 18.95           O  
ATOM  13421  CB  ARG B1039     210.230 206.033 168.961  1.00 18.64           C  
ATOM  13422  CG  ARG B1039     210.654 207.491 168.909  1.00 18.48           C  
ATOM  13423  CD  ARG B1039     210.001 208.294 169.974  1.00 18.64           C  
ATOM  13424  NE  ARG B1039     210.451 207.900 171.275  1.00 18.73           N  
ATOM  13425  CZ  ARG B1039     210.048 208.416 172.435  1.00 18.76           C  
ATOM  13426  NH1 ARG B1039     209.164 209.387 172.487  1.00 18.80           N  
ATOM  13427  NH2 ARG B1039     210.568 207.918 173.532  1.00 18.88           N  
ATOM  13428  N   VAL B1040     211.333 202.946 167.887  1.00 18.50           N  
ATOM  13429  CA  VAL B1040     211.194 201.500 167.957  1.00 18.45           C  
ATOM  13430  C   VAL B1040     210.716 201.016 169.307  1.00 18.98           C  
ATOM  13431  O   VAL B1040     211.183 201.463 170.352  1.00 19.45           O  
ATOM  13432  CB  VAL B1040     212.519 200.834 167.569  1.00 18.80           C  
ATOM  13433  CG1 VAL B1040     212.468 199.337 167.796  1.00 19.27           C  
ATOM  13434  CG2 VAL B1040     212.782 201.114 166.112  1.00 19.37           C  
ATOM  13435  N   ASP B1041     209.712 200.147 169.263  1.00 19.01           N  
ATOM  13436  CA  ASP B1041     209.051 199.552 170.419  1.00 19.24           C  
ATOM  13437  C   ASP B1041     208.364 200.582 171.291  1.00 19.46           C  
ATOM  13438  O   ASP B1041     207.925 200.272 172.399  1.00 19.70           O  
ATOM  13439  CB  ASP B1041     209.998 198.728 171.273  1.00 19.49           C  
ATOM  13440  CG  ASP B1041     210.610 197.569 170.528  1.00 19.67           C  
ATOM  13441  OD1 ASP B1041     210.369 197.431 169.361  1.00 19.48           O  
ATOM  13442  OD2 ASP B1041     211.282 196.789 171.149  1.00 19.88           O  
ATOM  13443  N   PHE B1042     208.234 201.796 170.785  1.00 19.23           N  
ATOM  13444  CA  PHE B1042     207.522 202.833 171.506  1.00 19.00           C  
ATOM  13445  C   PHE B1042     206.007 202.594 171.473  1.00 19.34           C  
ATOM  13446  O   PHE B1042     205.334 202.781 172.487  1.00 20.10           O  
ATOM  13447  CB  PHE B1042     207.900 204.199 170.955  1.00 19.09           C  
ATOM  13448  CG  PHE B1042     207.341 205.356 171.686  1.00 18.70           C  
ATOM  13449  CD1 PHE B1042     207.739 205.638 172.974  1.00 18.77           C  
ATOM  13450  CD2 PHE B1042     206.439 206.186 171.079  1.00 18.95           C  
ATOM  13451  CE1 PHE B1042     207.236 206.728 173.639  1.00 18.70           C  
ATOM  13452  CE2 PHE B1042     205.936 207.277 171.734  1.00 19.44           C  
ATOM  13453  CZ  PHE B1042     206.338 207.548 173.019  1.00 18.81           C  
ATOM  13454  N   CYS B1043     205.480 202.180 170.307  1.00 19.63           N  
ATOM  13455  CA  CYS B1043     204.060 201.916 170.066  1.00 20.15           C  
ATOM  13456  C   CYS B1043     203.867 200.511 169.458  1.00 20.25           C  
ATOM  13457  O   CYS B1043     203.464 200.372 168.301  1.00 20.37           O  
ATOM  13458  CB  CYS B1043     203.462 202.983 169.130  1.00 20.63           C  
ATOM  13459  SG  CYS B1043     203.479 204.661 169.760  1.00 20.92           S  
ATOM  13460  N   GLY B1044     204.168 199.482 170.245  1.00 20.08           N  
ATOM  13461  CA  GLY B1044     204.006 198.106 169.808  1.00 20.11           C  
ATOM  13462  C   GLY B1044     205.090 197.536 168.910  1.00 19.49           C  
ATOM  13463  O   GLY B1044     205.829 198.267 168.249  1.00 19.90           O  
ATOM  13464  N   LYS B1045     205.181 196.210 168.893  1.00 19.33           N  
ATOM  13465  CA  LYS B1045     206.163 195.512 168.071  1.00 19.25           C  
ATOM  13466  C   LYS B1045     205.853 195.689 166.588  1.00 19.50           C  
ATOM  13467  O   LYS B1045     204.690 195.733 166.189  1.00 19.67           O  
ATOM  13468  CB  LYS B1045     206.201 194.025 168.428  1.00 19.23           C  
ATOM  13469  N   GLY B1046     206.900 195.789 165.776  1.00 19.37           N  
ATOM  13470  CA  GLY B1046     206.739 195.965 164.344  1.00 18.94           C  
ATOM  13471  C   GLY B1046     207.080 197.379 163.918  1.00 18.90           C  
ATOM  13472  O   GLY B1046     207.997 197.993 164.465  1.00 19.31           O  
ATOM  13473  N   TYR B1047     206.344 197.900 162.942  1.00 18.94           N  
ATOM  13474  CA  TYR B1047     206.583 199.245 162.465  1.00 18.55           C  
ATOM  13475  C   TYR B1047     205.318 200.032 162.710  1.00 18.91           C  
ATOM  13476  O   TYR B1047     204.228 199.631 162.309  1.00 19.60           O  
ATOM  13477  CB  TYR B1047     206.952 199.246 160.992  1.00 18.44           C  
ATOM  13478  CG  TYR B1047     208.259 198.605 160.707  1.00 18.13           C  
ATOM  13479  CD1 TYR B1047     208.302 197.279 160.361  1.00 18.22           C  
ATOM  13480  CD2 TYR B1047     209.414 199.333 160.789  1.00 18.12           C  
ATOM  13481  CE1 TYR B1047     209.496 196.679 160.097  1.00 18.16           C  
ATOM  13482  CE2 TYR B1047     210.619 198.731 160.528  1.00 18.06           C  
ATOM  13483  CZ  TYR B1047     210.659 197.408 160.183  1.00 18.13           C  
ATOM  13484  OH  TYR B1047     211.861 196.803 159.926  1.00 19.27           O  
ATOM  13485  N   HIS B1048     205.434 201.137 163.409  1.00 19.03           N  
ATOM  13486  CA  HIS B1048     204.236 201.853 163.786  1.00 18.97           C  
ATOM  13487  C   HIS B1048     203.526 202.472 162.618  1.00 18.92           C  
ATOM  13488  O   HIS B1048     204.156 203.135 161.799  1.00 18.95           O  
ATOM  13489  CB  HIS B1048     204.558 202.939 164.794  1.00 19.17           C  
ATOM  13490  CG  HIS B1048     203.363 203.563 165.330  1.00 19.06           C  
ATOM  13491  ND1 HIS B1048     202.422 202.853 165.989  1.00 19.58           N  
ATOM  13492  CD2 HIS B1048     202.946 204.836 165.331  1.00 19.02           C  
ATOM  13493  CE1 HIS B1048     201.470 203.644 166.376  1.00 20.02           C  
ATOM  13494  NE2 HIS B1048     201.756 204.868 165.998  1.00 19.68           N  
ATOM  13495  N   LEU B1049     202.209 202.290 162.568  1.00 19.05           N  
ATOM  13496  CA  LEU B1049     201.387 202.947 161.577  1.00 18.90           C  
ATOM  13497  C   LEU B1049     200.535 204.000 162.247  1.00 19.47           C  
ATOM  13498  O   LEU B1049     200.672 205.187 161.957  1.00 20.05           O  
ATOM  13499  CB  LEU B1049     200.483 201.940 160.860  1.00 18.82           C  
ATOM  13500  CG  LEU B1049     201.173 200.883 160.001  1.00 18.71           C  
ATOM  13501  CD1 LEU B1049     200.141 199.906 159.527  1.00 19.45           C  
ATOM  13502  CD2 LEU B1049     201.848 201.540 158.798  1.00 18.95           C  
ATOM  13503  N   MET B1050     199.676 203.571 163.162  1.00 19.20           N  
ATOM  13504  CA  MET B1050     198.738 204.470 163.824  1.00 19.33           C  
ATOM  13505  C   MET B1050     198.297 203.899 165.151  1.00 19.96           C  
ATOM  13506  O   MET B1050     198.537 202.729 165.431  1.00 20.96           O  
ATOM  13507  CB  MET B1050     197.518 204.705 162.944  1.00 19.71           C  
ATOM  13508  CG  MET B1050     196.725 203.454 162.662  1.00 20.11           C  
ATOM  13509  SD  MET B1050     195.332 203.732 161.586  1.00 21.57           S  
ATOM  13510  CE  MET B1050     194.787 202.030 161.340  1.00 22.16           C  
ATOM  13511  N   SER B1051     197.643 204.707 165.964  1.00 20.05           N  
ATOM  13512  CA  SER B1051     197.103 204.198 167.212  1.00 20.18           C  
ATOM  13513  C   SER B1051     195.820 204.889 167.576  1.00 20.78           C  
ATOM  13514  O   SER B1051     195.528 205.982 167.088  1.00 21.48           O  
ATOM  13515  CB  SER B1051     198.083 204.367 168.342  1.00 20.55           C  
ATOM  13516  OG  SER B1051     198.324 205.707 168.587  1.00 21.02           O  
ATOM  13517  N   PHE B1052     195.062 204.251 168.449  1.00 21.36           N  
ATOM  13518  CA  PHE B1052     193.807 204.803 168.900  1.00 21.47           C  
ATOM  13519  C   PHE B1052     193.742 204.763 170.422  1.00 22.22           C  
ATOM  13520  O   PHE B1052     194.009 203.719 171.010  1.00 23.27           O  
ATOM  13521  CB  PHE B1052     192.664 203.960 168.359  1.00 22.12           C  
ATOM  13522  CG  PHE B1052     192.699 203.769 166.889  1.00 21.56           C  
ATOM  13523  CD1 PHE B1052     192.934 202.520 166.364  1.00 21.29           C  
ATOM  13524  CD2 PHE B1052     192.525 204.818 166.028  1.00 21.80           C  
ATOM  13525  CE1 PHE B1052     192.972 202.333 165.015  1.00 21.43           C  
ATOM  13526  CE2 PHE B1052     192.563 204.634 164.677  1.00 21.89           C  
ATOM  13527  CZ  PHE B1052     192.783 203.391 164.172  1.00 21.75           C  
ATOM  13528  N   PRO B1053     193.425 205.865 171.094  1.00 22.39           N  
ATOM  13529  CA  PRO B1053     193.253 205.940 172.520  1.00 22.73           C  
ATOM  13530  C   PRO B1053     191.906 205.365 172.897  1.00 23.69           C  
ATOM  13531  O   PRO B1053     190.955 205.480 172.124  1.00 24.15           O  
ATOM  13532  CB  PRO B1053     193.327 207.435 172.775  1.00 22.80           C  
ATOM  13533  CG  PRO B1053     192.761 208.043 171.520  1.00 22.61           C  
ATOM  13534  CD  PRO B1053     193.190 207.111 170.397  1.00 22.20           C  
ATOM  13535  N   GLN B1054     191.811 204.838 174.103  1.00 24.11           N  
ATOM  13536  CA  GLN B1054     190.558 204.413 174.706  1.00 25.11           C  
ATOM  13537  C   GLN B1054     190.550 204.889 176.153  1.00 25.66           C  
ATOM  13538  O   GLN B1054     191.591 204.904 176.813  1.00 25.57           O  
ATOM  13539  CB  GLN B1054     190.435 202.888 174.648  1.00 25.35           C  
ATOM  13540  CG  GLN B1054     190.401 202.287 173.248  1.00 25.11           C  
ATOM  13541  CD  GLN B1054     189.058 202.409 172.569  1.00 26.78           C  
ATOM  13542  OE1 GLN B1054     188.272 201.468 172.646  1.00 27.77           O  
ATOM  13543  NE2 GLN B1054     188.787 203.533 171.921  1.00 27.03           N  
ATOM  13544  N   SER B1055     189.393 205.274 176.670  1.00 25.92           N  
ATOM  13545  CA  SER B1055     189.348 205.652 178.071  1.00 25.43           C  
ATOM  13546  C   SER B1055     189.391 204.414 178.943  1.00 26.23           C  
ATOM  13547  O   SER B1055     189.073 203.312 178.497  1.00 27.33           O  
ATOM  13548  CB  SER B1055     188.113 206.464 178.373  1.00 26.61           C  
ATOM  13549  OG  SER B1055     186.965 205.700 178.223  1.00 27.55           O  
ATOM  13550  N   ALA B1056     189.777 204.602 180.189  1.00 26.30           N  
ATOM  13551  CA  ALA B1056     189.867 203.522 181.152  1.00 26.01           C  
ATOM  13552  C   ALA B1056     189.813 204.139 182.539  1.00 26.68           C  
ATOM  13553  O   ALA B1056     190.145 205.314 182.698  1.00 26.75           O  
ATOM  13554  CB  ALA B1056     191.153 202.743 180.919  1.00 25.91           C  
ATOM  13555  N   PRO B1057     189.380 203.414 183.560  1.00 26.21           N  
ATOM  13556  CA  PRO B1057     189.320 203.911 184.905  1.00 26.09           C  
ATOM  13557  C   PRO B1057     190.716 204.226 185.391  1.00 25.72           C  
ATOM  13558  O   PRO B1057     191.595 203.369 185.362  1.00 26.08           O  
ATOM  13559  CB  PRO B1057     188.677 202.752 185.656  1.00 26.70           C  
ATOM  13560  CG  PRO B1057     188.945 201.543 184.797  1.00 27.32           C  
ATOM  13561  CD  PRO B1057     188.963 202.041 183.385  1.00 27.27           C  
ATOM  13562  N   HIS B1058     190.905 205.459 185.831  1.00 25.64           N  
ATOM  13563  CA  HIS B1058     192.173 205.951 186.349  1.00 25.29           C  
ATOM  13564  C   HIS B1058     193.330 205.849 185.361  1.00 24.86           C  
ATOM  13565  O   HIS B1058     194.494 205.873 185.780  1.00 25.53           O  
ATOM  13566  CB  HIS B1058     192.550 205.209 187.628  1.00 25.72           C  
ATOM  13567  CG  HIS B1058     191.524 205.311 188.688  1.00 26.11           C  
ATOM  13568  ND1 HIS B1058     191.208 206.501 189.303  1.00 25.97           N  
ATOM  13569  CD2 HIS B1058     190.735 204.374 189.252  1.00 26.67           C  
ATOM  13570  CE1 HIS B1058     190.273 206.291 190.203  1.00 26.40           C  
ATOM  13571  NE2 HIS B1058     189.965 205.009 190.192  1.00 26.73           N  
ATOM  13572  N   GLY B1059     193.045 205.778 184.062  1.00 25.21           N  
ATOM  13573  CA  GLY B1059     194.143 205.654 183.112  1.00 24.87           C  
ATOM  13574  C   GLY B1059     193.720 205.660 181.658  1.00 24.55           C  
ATOM  13575  O   GLY B1059     192.580 205.967 181.321  1.00 25.15           O  
ATOM  13576  N   VAL B1060     194.677 205.371 180.788  1.00 24.54           N  
ATOM  13577  CA  VAL B1060     194.449 205.390 179.351  1.00 24.36           C  
ATOM  13578  C   VAL B1060     194.941 204.109 178.726  1.00 23.83           C  
ATOM  13579  O   VAL B1060     195.968 203.561 179.129  1.00 24.44           O  
ATOM  13580  CB  VAL B1060     195.162 206.594 178.701  1.00 24.20           C  
ATOM  13581  CG1 VAL B1060     196.652 206.473 178.851  1.00 23.80           C  
ATOM  13582  CG2 VAL B1060     194.790 206.700 177.225  1.00 23.88           C  
ATOM  13583  N   VAL B1061     194.214 203.634 177.737  1.00 24.15           N  
ATOM  13584  CA  VAL B1061     194.614 202.443 177.026  1.00 23.48           C  
ATOM  13585  C   VAL B1061     194.788 202.729 175.554  1.00 24.08           C  
ATOM  13586  O   VAL B1061     193.922 203.326 174.920  1.00 24.53           O  
ATOM  13587  CB  VAL B1061     193.585 201.344 177.253  1.00 24.91           C  
ATOM  13588  CG1 VAL B1061     193.955 200.113 176.486  1.00 24.55           C  
ATOM  13589  CG2 VAL B1061     193.528 201.071 178.728  1.00 25.41           C  
ATOM  13590  N   PHE B1062     195.921 202.335 175.006  1.00 23.02           N  
ATOM  13591  CA  PHE B1062     196.161 202.579 173.602  1.00 22.23           C  
ATOM  13592  C   PHE B1062     196.124 201.305 172.796  1.00 23.09           C  
ATOM  13593  O   PHE B1062     196.708 200.291 173.179  1.00 23.21           O  
ATOM  13594  CB  PHE B1062     197.525 203.207 173.389  1.00 22.31           C  
ATOM  13595  CG  PHE B1062     197.715 204.542 173.977  1.00 22.68           C  
ATOM  13596  CD1 PHE B1062     198.276 204.679 175.224  1.00 22.59           C  
ATOM  13597  CD2 PHE B1062     197.357 205.668 173.285  1.00 22.76           C  
ATOM  13598  CE1 PHE B1062     198.476 205.920 175.766  1.00 22.34           C  
ATOM  13599  CE2 PHE B1062     197.554 206.911 173.828  1.00 22.36           C  
ATOM  13600  CZ  PHE B1062     198.117 207.035 175.070  1.00 22.22           C  
ATOM  13601  N   LEU B1063     195.501 201.381 171.637  1.00 22.42           N  
ATOM  13602  CA  LEU B1063     195.537 200.292 170.683  1.00 22.11           C  
ATOM  13603  C   LEU B1063     196.509 200.662 169.588  1.00 22.37           C  
ATOM  13604  O   LEU B1063     196.282 201.617 168.846  1.00 22.55           O  
ATOM  13605  CB  LEU B1063     194.149 200.041 170.103  1.00 22.64           C  
ATOM  13606  CG  LEU B1063     193.049 199.730 171.115  1.00 23.54           C  
ATOM  13607  CD1 LEU B1063     191.743 199.552 170.374  1.00 25.14           C  
ATOM  13608  CD2 LEU B1063     193.406 198.475 171.904  1.00 24.62           C  
ATOM  13609  N   HIS B1064     197.614 199.943 169.512  1.00 21.74           N  
ATOM  13610  CA  HIS B1064     198.657 200.286 168.560  1.00 20.67           C  
ATOM  13611  C   HIS B1064     198.582 199.404 167.344  1.00 21.26           C  
ATOM  13612  O   HIS B1064     198.661 198.184 167.456  1.00 21.68           O  
ATOM  13613  CB  HIS B1064     200.041 200.135 169.166  1.00 21.02           C  
ATOM  13614  CG  HIS B1064     200.273 200.953 170.354  1.00 21.22           C  
ATOM  13615  ND1 HIS B1064     199.988 202.287 170.400  1.00 21.73           N  
ATOM  13616  CD2 HIS B1064     200.807 200.640 171.543  1.00 21.51           C  
ATOM  13617  CE1 HIS B1064     200.344 202.765 171.573  1.00 21.91           C  
ATOM  13618  NE2 HIS B1064     200.841 201.784 172.283  1.00 21.65           N  
ATOM  13619  N   VAL B1065     198.433 200.016 166.182  1.00 20.36           N  
ATOM  13620  CA  VAL B1065     198.315 199.278 164.944  1.00 19.93           C  
ATOM  13621  C   VAL B1065     199.656 199.295 164.250  1.00 19.85           C  
ATOM  13622  O   VAL B1065     200.153 200.362 163.874  1.00 20.39           O  
ATOM  13623  CB  VAL B1065     197.276 199.935 164.041  1.00 20.30           C  
ATOM  13624  CG1 VAL B1065     197.107 199.128 162.775  1.00 20.25           C  
ATOM  13625  CG2 VAL B1065     195.988 200.094 164.795  1.00 21.00           C  
ATOM  13626  N   THR B1066     200.247 198.122 164.081  1.00 19.88           N  
ATOM  13627  CA  THR B1066     201.582 198.068 163.521  1.00 19.07           C  
ATOM  13628  C   THR B1066     201.708 197.102 162.358  1.00 19.24           C  
ATOM  13629  O   THR B1066     200.990 196.102 162.263  1.00 19.92           O  
ATOM  13630  CB  THR B1066     202.590 197.673 164.608  1.00 19.43           C  
ATOM  13631  OG1 THR B1066     202.320 196.342 165.049  1.00 19.94           O  
ATOM  13632  CG2 THR B1066     202.501 198.602 165.798  1.00 19.83           C  
ATOM  13633  N   TYR B1067     202.675 197.388 161.502  1.00 18.91           N  
ATOM  13634  CA  TYR B1067     203.009 196.569 160.353  1.00 18.19           C  
ATOM  13635  C   TYR B1067     204.088 195.573 160.714  1.00 18.78           C  
ATOM  13636  O   TYR B1067     205.194 195.945 161.113  1.00 19.35           O  
ATOM  13637  CB  TYR B1067     203.482 197.478 159.223  1.00 18.66           C  
ATOM  13638  CG  TYR B1067     203.977 196.805 157.980  1.00 18.42           C  
ATOM  13639  CD1 TYR B1067     203.117 196.502 156.966  1.00 18.64           C  
ATOM  13640  CD2 TYR B1067     205.314 196.516 157.855  1.00 18.34           C  
ATOM  13641  CE1 TYR B1067     203.594 195.916 155.826  1.00 18.65           C  
ATOM  13642  CE2 TYR B1067     205.790 195.924 156.723  1.00 18.35           C  
ATOM  13643  CZ  TYR B1067     204.935 195.626 155.708  1.00 18.58           C  
ATOM  13644  OH  TYR B1067     205.404 195.037 154.558  1.00 19.31           O  
ATOM  13645  N   VAL B1068     203.773 194.301 160.588  1.00 18.31           N  
ATOM  13646  CA  VAL B1068     204.717 193.269 160.939  1.00 18.02           C  
ATOM  13647  C   VAL B1068     205.033 192.403 159.732  1.00 18.49           C  
ATOM  13648  O   VAL B1068     204.134 191.779 159.185  1.00 19.12           O  
ATOM  13649  CB  VAL B1068     204.132 192.397 162.050  1.00 18.33           C  
ATOM  13650  CG1 VAL B1068     205.109 191.300 162.426  1.00 18.85           C  
ATOM  13651  CG2 VAL B1068     203.821 193.266 163.235  1.00 19.02           C  
ATOM  13652  N   PRO B1069     206.288 192.349 159.283  1.00 17.99           N  
ATOM  13653  CA  PRO B1069     206.743 191.507 158.197  1.00 18.11           C  
ATOM  13654  C   PRO B1069     206.396 190.069 158.534  1.00 18.45           C  
ATOM  13655  O   PRO B1069     206.511 189.671 159.684  1.00 19.03           O  
ATOM  13656  CB  PRO B1069     208.249 191.744 158.223  1.00 18.27           C  
ATOM  13657  CG  PRO B1069     208.413 193.113 158.827  1.00 18.32           C  
ATOM  13658  CD  PRO B1069     207.314 193.224 159.847  1.00 18.29           C  
ATOM  13659  N   ALA B1070     205.970 189.289 157.541  1.00 18.37           N  
ATOM  13660  CA  ALA B1070     205.574 187.916 157.817  1.00 18.48           C  
ATOM  13661  C   ALA B1070     205.954 186.571 157.212  1.00 18.63           C  
ATOM  13662  O   ALA B1070     206.115 185.588 157.934  1.00 18.79           O  
ATOM  13663  CB  ALA B1070     204.092 187.736 157.531  1.00 18.72           C  
ATOM  13664  N   GLN B1071     206.094 186.534 155.899  1.00 18.49           N  
ATOM  13665  CA  GLN B1071     206.413 185.295 155.205  1.00 18.47           C  
ATOM  13666  C   GLN B1071     207.639 185.910 154.577  1.00 18.85           C  
ATOM  13667  O   GLN B1071     207.612 187.076 154.190  1.00 19.74           O  
ATOM  13668  CB  GLN B1071     205.466 184.812 154.119  1.00 18.71           C  
ATOM  13669  CG  GLN B1071     204.266 184.047 154.642  1.00 18.59           C  
ATOM  13670  CD  GLN B1071     203.245 183.746 153.561  1.00 18.87           C  
ATOM  13671  OE1 GLN B1071     202.061 183.586 153.856  1.00 18.65           O  
ATOM  13672  NE2 GLN B1071     203.685 183.676 152.311  1.00 19.20           N  
ATOM  13673  N   GLU B1072     208.721 185.144 154.488  1.00 18.74           N  
ATOM  13674  CA  GLU B1072     209.985 185.644 153.954  1.00 18.93           C  
ATOM  13675  C   GLU B1072     210.688 184.637 153.067  1.00 19.43           C  
ATOM  13676  O   GLU B1072     210.423 183.433 153.140  1.00 19.74           O  
ATOM  13677  CB  GLU B1072     210.925 186.047 155.092  1.00 18.79           C  
ATOM  13678  CG  GLU B1072     211.325 184.894 155.983  1.00 18.48           C  
ATOM  13679  CD  GLU B1072     212.254 185.272 157.108  1.00 18.95           C  
ATOM  13680  OE1 GLU B1072     211.811 185.370 158.213  1.00 18.33           O  
ATOM  13681  OE2 GLU B1072     213.410 185.442 156.849  1.00 19.28           O  
ATOM  13682  N   LYS B1073     211.594 185.140 152.236  1.00 19.33           N  
ATOM  13683  CA  LYS B1073     212.431 184.296 151.394  1.00 19.72           C  
ATOM  13684  C   LYS B1073     213.912 184.683 151.450  1.00 20.07           C  
ATOM  13685  O   LYS B1073     214.254 185.851 151.665  1.00 20.90           O  
ATOM  13686  CB  LYS B1073     211.939 184.334 149.950  1.00 20.10           C  
ATOM  13687  CG  LYS B1073     210.594 183.701 149.727  1.00 20.22           C  
ATOM  13688  CD  LYS B1073     210.238 183.689 148.248  1.00 20.28           C  
ATOM  13689  CE  LYS B1073     208.869 183.066 148.020  1.00 19.81           C  
ATOM  13690  NZ  LYS B1073     208.496 183.041 146.578  1.00 20.85           N  
ATOM  13691  N   ASN B1074     214.782 183.684 151.217  1.00 20.32           N  
ATOM  13692  CA  ASN B1074     216.232 183.809 151.138  1.00 20.41           C  
ATOM  13693  C   ASN B1074     216.673 184.199 149.716  1.00 20.63           C  
ATOM  13694  O   ASN B1074     216.557 183.392 148.792  1.00 21.80           O  
ATOM  13695  CB  ASN B1074     216.917 182.495 151.531  1.00 20.80           C  
ATOM  13696  CG  ASN B1074     216.967 182.202 153.038  1.00 20.88           C  
ATOM  13697  OD1 ASN B1074     216.665 183.046 153.896  1.00 20.75           O  
ATOM  13698  ND2 ASN B1074     217.368 180.973 153.344  1.00 20.92           N  
ATOM  13699  N   PHE B1075     217.194 185.425 149.544  1.00 21.03           N  
ATOM  13700  CA  PHE B1075     217.659 185.938 148.249  1.00 20.65           C  
ATOM  13701  C   PHE B1075     219.161 186.126 148.267  1.00 20.99           C  
ATOM  13702  O   PHE B1075     219.745 186.433 149.305  1.00 21.99           O  
ATOM  13703  CB  PHE B1075     217.011 187.272 147.926  1.00 20.96           C  
ATOM  13704  CG  PHE B1075     215.571 187.185 147.747  1.00 20.59           C  
ATOM  13705  CD1 PHE B1075     214.726 187.473 148.783  1.00 20.58           C  
ATOM  13706  CD2 PHE B1075     215.044 186.804 146.548  1.00 21.60           C  
ATOM  13707  CE1 PHE B1075     213.373 187.383 148.622  1.00 20.87           C  
ATOM  13708  CE2 PHE B1075     213.693 186.707 146.381  1.00 21.30           C  
ATOM  13709  CZ  PHE B1075     212.855 186.997 147.423  1.00 20.90           C  
ATOM  13710  N   THR B1076     219.791 185.966 147.120  1.00 21.36           N  
ATOM  13711  CA  THR B1076     221.206 186.266 147.024  1.00 21.15           C  
ATOM  13712  C   THR B1076     221.323 187.750 146.770  1.00 21.60           C  
ATOM  13713  O   THR B1076     220.466 188.330 146.105  1.00 22.05           O  
ATOM  13714  CB  THR B1076     221.886 185.426 145.938  1.00 21.75           C  
ATOM  13715  OG1 THR B1076     221.809 184.046 146.300  1.00 22.26           O  
ATOM  13716  CG2 THR B1076     223.339 185.827 145.771  1.00 21.83           C  
ATOM  13717  N   THR B1077     222.323 188.393 147.341  1.00 21.35           N  
ATOM  13718  CA  THR B1077     222.443 189.833 147.158  1.00 20.77           C  
ATOM  13719  C   THR B1077     223.818 190.325 146.757  1.00 21.20           C  
ATOM  13720  O   THR B1077     224.764 189.551 146.610  1.00 21.52           O  
ATOM  13721  CB  THR B1077     221.988 190.571 148.412  1.00 20.82           C  
ATOM  13722  OG1 THR B1077     221.928 191.965 148.148  1.00 21.46           O  
ATOM  13723  CG2 THR B1077     222.911 190.305 149.546  1.00 21.36           C  
ATOM  13724  N   ALA B1078     223.891 191.631 146.540  1.00 21.00           N  
ATOM  13725  CA  ALA B1078     225.105 192.340 146.181  1.00 20.98           C  
ATOM  13726  C   ALA B1078     224.911 193.810 146.520  1.00 21.11           C  
ATOM  13727  O   ALA B1078     223.798 194.312 146.393  1.00 21.94           O  
ATOM  13728  CB  ALA B1078     225.408 192.181 144.702  1.00 21.89           C  
ATOM  13729  N   PRO B1079     225.957 194.524 146.937  1.00 21.03           N  
ATOM  13730  CA  PRO B1079     225.948 195.941 147.239  1.00 21.24           C  
ATOM  13731  C   PRO B1079     225.832 196.836 146.016  1.00 21.81           C  
ATOM  13732  O   PRO B1079     225.466 198.002 146.132  1.00 22.00           O  
ATOM  13733  CB  PRO B1079     227.300 196.122 147.919  1.00 21.34           C  
ATOM  13734  CG  PRO B1079     228.165 195.027 147.371  1.00 21.74           C  
ATOM  13735  CD  PRO B1079     227.240 193.867 147.151  1.00 21.50           C  
ATOM  13736  N   ALA B1080     226.174 196.303 144.854  1.00 22.21           N  
ATOM  13737  CA  ALA B1080     226.198 197.086 143.630  1.00 22.13           C  
ATOM  13738  C   ALA B1080     226.269 196.175 142.428  1.00 22.99           C  
ATOM  13739  O   ALA B1080     226.615 194.997 142.558  1.00 23.73           O  
ATOM  13740  CB  ALA B1080     227.377 198.038 143.631  1.00 22.72           C  
ATOM  13741  N   ILE B1081     225.994 196.717 141.254  1.00 23.53           N  
ATOM  13742  CA  ILE B1081     226.206 195.944 140.038  1.00 24.09           C  
ATOM  13743  C   ILE B1081     227.085 196.694 139.030  1.00 24.34           C  
ATOM  13744  O   ILE B1081     227.111 197.928 139.015  1.00 24.90           O  
ATOM  13745  CB  ILE B1081     224.865 195.564 139.396  1.00 24.29           C  
ATOM  13746  CG1 ILE B1081     224.130 196.821 139.048  1.00 24.66           C  
ATOM  13747  CG2 ILE B1081     224.058 194.665 140.331  1.00 24.33           C  
ATOM  13748  CD1 ILE B1081     222.883 196.626 138.314  1.00 25.75           C  
ATOM  13749  N   CYS B1082     227.780 195.942 138.167  1.00 24.85           N  
ATOM  13750  CA  CYS B1082     228.621 196.461 137.092  1.00 25.03           C  
ATOM  13751  C   CYS B1082     227.862 196.442 135.769  1.00 25.43           C  
ATOM  13752  O   CYS B1082     227.277 195.426 135.403  1.00 26.54           O  
ATOM  13753  CB  CYS B1082     229.901 195.623 136.932  1.00 25.88           C  
ATOM  13754  SG  CYS B1082     231.007 195.679 138.332  1.00 26.00           S  
ATOM  13755  N   HIS B1083     227.933 197.554 135.019  1.00 25.46           N  
ATOM  13756  CA  HIS B1083     227.304 197.644 133.691  1.00 25.83           C  
ATOM  13757  C   HIS B1083     228.344 197.899 132.599  1.00 26.32           C  
ATOM  13758  O   HIS B1083     228.751 196.978 131.898  1.00 25.83           O  
ATOM  13759  CB  HIS B1083     226.240 198.724 133.694  1.00 26.10           C  
ATOM  13760  CG  HIS B1083     225.535 198.857 132.418  1.00 26.60           C  
ATOM  13761  ND1 HIS B1083     224.626 197.924 131.963  1.00 27.41           N  
ATOM  13762  CD2 HIS B1083     225.589 199.814 131.484  1.00 26.91           C  
ATOM  13763  CE1 HIS B1083     224.162 198.312 130.795  1.00 27.70           C  
ATOM  13764  NE2 HIS B1083     224.732 199.453 130.483  1.00 27.72           N  
ATOM  13765  N   ASP B1084     228.828 199.131 132.502  1.00 25.92           N  
ATOM  13766  CA  ASP B1084     229.885 199.472 131.545  1.00 25.92           C  
ATOM  13767  C   ASP B1084     231.215 199.620 132.259  1.00 25.85           C  
ATOM  13768  O   ASP B1084     232.125 200.301 131.790  1.00 25.72           O  
ATOM  13769  CB  ASP B1084     229.566 200.754 130.772  1.00 25.87           C  
ATOM  13770  CG  ASP B1084     228.426 200.600 129.764  1.00 26.46           C  
ATOM  13771  OD1 ASP B1084     228.360 199.585 129.114  1.00 26.85           O  
ATOM  13772  OD2 ASP B1084     227.632 201.507 129.653  1.00 26.23           O  
ATOM  13773  N   GLY B1085     231.301 199.007 133.430  1.00 25.55           N  
ATOM  13774  CA  GLY B1085     232.471 199.070 134.292  1.00 25.88           C  
ATOM  13775  C   GLY B1085     232.208 200.032 135.441  1.00 25.50           C  
ATOM  13776  O   GLY B1085     232.910 200.026 136.456  1.00 25.20           O  
ATOM  13777  N   LYS B1086     231.176 200.846 135.267  1.00 25.28           N  
ATOM  13778  CA  LYS B1086     230.726 201.780 136.280  1.00 24.59           C  
ATOM  13779  C   LYS B1086     229.870 201.035 137.292  1.00 24.58           C  
ATOM  13780  O   LYS B1086     229.202 200.056 136.939  1.00 25.65           O  
ATOM  13781  CB  LYS B1086     229.968 202.937 135.629  1.00 24.98           C  
ATOM  13782  CG  LYS B1086     228.786 202.497 134.756  1.00 25.09           C  
ATOM  13783  CD  LYS B1086     228.022 203.674 134.113  1.00 25.50           C  
ATOM  13784  CE  LYS B1086     228.889 204.469 133.142  1.00 25.33           C  
ATOM  13785  NZ  LYS B1086     228.069 205.339 132.239  1.00 25.02           N  
ATOM  13786  N   ALA B1087     229.884 201.495 138.543  1.00 24.05           N  
ATOM  13787  CA  ALA B1087     229.102 200.850 139.596  1.00 23.07           C  
ATOM  13788  C   ALA B1087     227.752 201.517 139.813  1.00 23.27           C  
ATOM  13789  O   ALA B1087     227.663 202.714 140.092  1.00 24.24           O  
ATOM  13790  CB  ALA B1087     229.874 200.855 140.903  1.00 23.43           C  
ATOM  13791  N   HIS B1088     226.703 200.711 139.739  1.00 23.50           N  
ATOM  13792  CA  HIS B1088     225.335 201.160 139.951  1.00 23.22           C  
ATOM  13793  C   HIS B1088     224.815 200.732 141.317  1.00 23.38           C  
ATOM  13794  O   HIS B1088     224.891 199.560 141.684  1.00 24.44           O  
ATOM  13795  CB  HIS B1088     224.409 200.583 138.881  1.00 24.19           C  
ATOM  13796  CG  HIS B1088     224.610 201.103 137.510  1.00 24.73           C  
ATOM  13797  ND1 HIS B1088     223.682 201.892 136.879  1.00 25.47           N  
ATOM  13798  CD2 HIS B1088     225.625 200.958 136.639  1.00 25.18           C  
ATOM  13799  CE1 HIS B1088     224.113 202.204 135.680  1.00 26.38           C  
ATOM  13800  NE2 HIS B1088     225.287 201.656 135.509  1.00 25.62           N  
ATOM  13801  N   PHE B1089     224.272 201.684 142.059  1.00 22.76           N  
ATOM  13802  CA  PHE B1089     223.714 201.443 143.388  1.00 22.37           C  
ATOM  13803  C   PHE B1089     222.234 201.770 143.341  1.00 23.95           C  
ATOM  13804  O   PHE B1089     221.844 202.655 142.594  1.00 21.84           O  
ATOM  13805  CB  PHE B1089     224.371 202.363 144.397  1.00 22.06           C  
ATOM  13806  CG  PHE B1089     225.799 202.181 144.567  1.00 21.84           C  
ATOM  13807  CD1 PHE B1089     226.664 202.917 143.814  1.00 22.47           C  
ATOM  13808  CD2 PHE B1089     226.304 201.299 145.481  1.00 21.69           C  
ATOM  13809  CE1 PHE B1089     228.003 202.781 143.970  1.00 21.97           C  
ATOM  13810  CE2 PHE B1089     227.656 201.162 145.635  1.00 21.81           C  
ATOM  13811  CZ  PHE B1089     228.501 201.910 144.877  1.00 21.72           C  
ATOM  13812  N   PRO B1090     221.377 201.116 144.113  1.00 22.51           N  
ATOM  13813  CA  PRO B1090     219.961 201.383 144.130  1.00 22.17           C  
ATOM  13814  C   PRO B1090     219.705 202.730 144.765  1.00 22.27           C  
ATOM  13815  O   PRO B1090     220.329 203.066 145.770  1.00 22.69           O  
ATOM  13816  CB  PRO B1090     219.424 200.234 144.976  1.00 22.39           C  
ATOM  13817  CG  PRO B1090     220.579 199.851 145.870  1.00 22.52           C  
ATOM  13818  CD  PRO B1090     221.832 200.128 145.066  1.00 22.68           C  
ATOM  13819  N   ARG B1091     218.744 203.476 144.241  1.00 22.39           N  
ATOM  13820  CA  ARG B1091     218.360 204.716 144.897  1.00 22.30           C  
ATOM  13821  C   ARG B1091     217.548 204.390 146.132  1.00 22.11           C  
ATOM  13822  O   ARG B1091     217.639 205.065 147.155  1.00 22.31           O  
ATOM  13823  CB  ARG B1091     217.548 205.615 143.980  1.00 22.41           C  
ATOM  13824  CG  ARG B1091     218.323 206.272 142.856  1.00 22.64           C  
ATOM  13825  CD  ARG B1091     217.478 207.245 142.120  1.00 22.79           C  
ATOM  13826  NE  ARG B1091     218.235 207.993 141.125  1.00 23.09           N  
ATOM  13827  CZ  ARG B1091     218.455 207.591 139.859  1.00 24.15           C  
ATOM  13828  NH1 ARG B1091     217.982 206.446 139.447  1.00 24.22           N  
ATOM  13829  NH2 ARG B1091     219.148 208.351 139.031  1.00 22.94           N  
ATOM  13830  N   GLU B1092     216.755 203.339 146.013  1.00 21.97           N  
ATOM  13831  CA  GLU B1092     215.880 202.855 147.062  1.00 21.79           C  
ATOM  13832  C   GLU B1092     215.814 201.344 146.978  1.00 21.58           C  
ATOM  13833  O   GLU B1092     215.661 200.791 145.891  1.00 22.02           O  
ATOM  13834  CB  GLU B1092     214.484 203.462 146.908  1.00 22.00           C  
ATOM  13835  N   GLY B1093     215.920 200.675 148.110  1.00 21.36           N  
ATOM  13836  CA  GLY B1093     215.828 199.226 148.122  1.00 21.35           C  
ATOM  13837  C   GLY B1093     217.186 198.575 147.969  1.00 21.37           C  
ATOM  13838  O   GLY B1093     218.211 199.197 148.247  1.00 21.54           O  
ATOM  13839  N   VAL B1094     217.172 197.294 147.629  1.00 21.67           N  
ATOM  13840  CA  VAL B1094     218.375 196.484 147.518  1.00 21.67           C  
ATOM  13841  C   VAL B1094     218.390 195.672 146.248  1.00 22.46           C  
ATOM  13842  O   VAL B1094     217.339 195.414 145.663  1.00 23.17           O  
ATOM  13843  CB  VAL B1094     218.484 195.516 148.695  1.00 21.52           C  
ATOM  13844  CG1 VAL B1094     218.610 196.253 149.967  1.00 21.62           C  
ATOM  13845  CG2 VAL B1094     217.250 194.646 148.742  1.00 21.63           C  
ATOM  13846  N   PHE B1095     219.569 195.207 145.850  1.00 22.45           N  
ATOM  13847  CA  PHE B1095     219.637 194.276 144.740  1.00 22.22           C  
ATOM  13848  C   PHE B1095     219.449 192.865 145.252  1.00 22.33           C  
ATOM  13849  O   PHE B1095     219.994 192.495 146.290  1.00 22.85           O  
ATOM  13850  CB  PHE B1095     220.966 194.367 144.005  1.00 22.48           C  
ATOM  13851  CG  PHE B1095     221.169 195.620 143.251  1.00 23.00           C  
ATOM  13852  CD1 PHE B1095     220.255 196.044 142.320  1.00 23.92           C  
ATOM  13853  CD2 PHE B1095     222.291 196.364 143.444  1.00 23.06           C  
ATOM  13854  CE1 PHE B1095     220.461 197.192 141.617  1.00 24.03           C  
ATOM  13855  CE2 PHE B1095     222.491 197.502 142.729  1.00 23.22           C  
ATOM  13856  CZ  PHE B1095     221.584 197.914 141.827  1.00 23.71           C  
ATOM  13857  N   VAL B1096     218.677 192.078 144.529  1.00 22.65           N  
ATOM  13858  CA  VAL B1096     218.445 190.695 144.892  1.00 22.05           C  
ATOM  13859  C   VAL B1096     218.622 189.790 143.701  1.00 23.25           C  
ATOM  13860  O   VAL B1096     218.468 190.219 142.562  1.00 23.65           O  
ATOM  13861  CB  VAL B1096     217.024 190.514 145.430  1.00 22.37           C  
ATOM  13862  CG1 VAL B1096     216.830 191.346 146.617  1.00 22.20           C  
ATOM  13863  CG2 VAL B1096     216.021 190.892 144.381  1.00 23.01           C  
ATOM  13864  N   SER B1097     218.853 188.522 143.967  1.00 22.63           N  
ATOM  13865  CA  SER B1097     218.929 187.517 142.929  1.00 22.53           C  
ATOM  13866  C   SER B1097     218.127 186.283 143.286  1.00 22.95           C  
ATOM  13867  O   SER B1097     218.277 185.724 144.380  1.00 23.30           O  
ATOM  13868  CB  SER B1097     220.369 187.150 142.660  1.00 23.11           C  
ATOM  13869  OG  SER B1097     220.468 185.977 141.903  1.00 23.95           O  
ATOM  13870  N   ASN B1098     217.288 185.836 142.338  1.00 24.07           N  
ATOM  13871  CA  ASN B1098     216.444 184.649 142.501  1.00 24.64           C  
ATOM  13872  C   ASN B1098     217.139 183.364 142.024  1.00 25.20           C  
ATOM  13873  O   ASN B1098     216.533 182.290 142.021  1.00 25.53           O  
ATOM  13874  CB  ASN B1098     215.091 184.849 141.799  1.00 25.28           C  
ATOM  13875  CG  ASN B1098     215.134 184.785 140.250  1.00 26.36           C  
ATOM  13876  OD1 ASN B1098     216.214 184.700 139.623  1.00 25.18           O  
ATOM  13877  ND2 ASN B1098     213.945 184.827 139.641  1.00 26.22           N  
ATOM  13878  N   GLY B1099     218.430 183.465 141.660  1.00 25.09           N  
ATOM  13879  CA  GLY B1099     219.279 182.374 141.198  1.00 25.35           C  
ATOM  13880  C   GLY B1099     219.667 182.528 139.736  1.00 25.83           C  
ATOM  13881  O   GLY B1099     220.697 182.000 139.317  1.00 25.96           O  
ATOM  13882  N   THR B1100     218.875 183.264 138.959  1.00 25.50           N  
ATOM  13883  CA  THR B1100     219.240 183.477 137.561  1.00 25.77           C  
ATOM  13884  C   THR B1100     219.222 184.944 137.153  1.00 25.91           C  
ATOM  13885  O   THR B1100     219.999 185.359 136.292  1.00 25.67           O  
ATOM  13886  CB  THR B1100     218.317 182.688 136.622  1.00 26.18           C  
ATOM  13887  OG1 THR B1100     216.977 183.152 136.776  1.00 26.63           O  
ATOM  13888  CG2 THR B1100     218.375 181.208 136.951  1.00 26.23           C  
ATOM  13889  N   HIS B1101     218.356 185.738 137.773  1.00 25.23           N  
ATOM  13890  CA  HIS B1101     218.231 187.140 137.394  1.00 24.89           C  
ATOM  13891  C   HIS B1101     218.298 188.074 138.578  1.00 25.05           C  
ATOM  13892  O   HIS B1101     217.839 187.750 139.677  1.00 24.84           O  
ATOM  13893  CB  HIS B1101     216.919 187.402 136.656  1.00 25.58           C  
ATOM  13894  CG  HIS B1101     216.830 186.792 135.306  1.00 26.09           C  
ATOM  13895  ND1 HIS B1101     216.536 185.468 135.107  1.00 26.32           N  
ATOM  13896  CD2 HIS B1101     216.988 187.332 134.078  1.00 26.33           C  
ATOM  13897  CE1 HIS B1101     216.513 185.216 133.812  1.00 26.52           C  
ATOM  13898  NE2 HIS B1101     216.786 186.330 133.167  1.00 26.86           N  
ATOM  13899  N   TRP B1102     218.858 189.252 138.332  1.00 24.20           N  
ATOM  13900  CA  TRP B1102     218.956 190.294 139.335  1.00 23.59           C  
ATOM  13901  C   TRP B1102     217.836 191.303 139.218  1.00 24.11           C  
ATOM  13902  O   TRP B1102     217.510 191.748 138.119  1.00 24.86           O  
ATOM  13903  CB  TRP B1102     220.287 191.001 139.209  1.00 24.03           C  
ATOM  13904  CG  TRP B1102     221.399 190.197 139.675  1.00 23.65           C  
ATOM  13905  CD1 TRP B1102     222.149 189.349 138.946  1.00 24.13           C  
ATOM  13906  CD2 TRP B1102     221.916 190.149 141.005  1.00 23.21           C  
ATOM  13907  NE1 TRP B1102     223.091 188.766 139.735  1.00 23.48           N  
ATOM  13908  CE2 TRP B1102     222.960 189.244 141.000  1.00 23.21           C  
ATOM  13909  CE3 TRP B1102     221.576 190.788 142.185  1.00 23.42           C  
ATOM  13910  CZ2 TRP B1102     223.672 188.951 142.136  1.00 23.35           C  
ATOM  13911  CZ3 TRP B1102     222.287 190.499 143.322  1.00 22.72           C  
ATOM  13912  CH2 TRP B1102     223.309 189.600 143.298  1.00 22.59           C  
ATOM  13913  N   PHE B1103     217.287 191.675 140.364  1.00 24.05           N  
ATOM  13914  CA  PHE B1103     216.193 192.627 140.475  1.00 23.46           C  
ATOM  13915  C   PHE B1103     216.487 193.629 141.564  1.00 23.64           C  
ATOM  13916  O   PHE B1103     217.329 193.386 142.423  1.00 23.85           O  
ATOM  13917  CB  PHE B1103     214.895 191.917 140.815  1.00 23.69           C  
ATOM  13918  CG  PHE B1103     214.551 190.878 139.866  1.00 23.77           C  
ATOM  13919  CD1 PHE B1103     214.929 189.588 140.109  1.00 24.11           C  
ATOM  13920  CD2 PHE B1103     213.860 191.167 138.720  1.00 24.11           C  
ATOM  13921  CE1 PHE B1103     214.625 188.600 139.228  1.00 25.15           C  
ATOM  13922  CE2 PHE B1103     213.553 190.178 137.830  1.00 25.32           C  
ATOM  13923  CZ  PHE B1103     213.940 188.891 138.089  1.00 25.07           C  
ATOM  13924  N   VAL B1104     215.815 194.755 141.538  1.00 23.60           N  
ATOM  13925  CA  VAL B1104     215.950 195.704 142.633  1.00 23.17           C  
ATOM  13926  C   VAL B1104     214.609 195.846 143.307  1.00 22.74           C  
ATOM  13927  O   VAL B1104     213.584 195.911 142.634  1.00 24.00           O  
ATOM  13928  CB  VAL B1104     216.492 197.055 142.143  1.00 23.73           C  
ATOM  13929  CG1 VAL B1104     215.597 197.636 141.078  1.00 24.65           C  
ATOM  13930  CG2 VAL B1104     216.621 198.010 143.311  1.00 23.23           C  
ATOM  13931  N   THR B1105     214.588 195.830 144.631  1.00 22.64           N  
ATOM  13932  CA  THR B1105     213.300 195.909 145.295  1.00 22.24           C  
ATOM  13933  C   THR B1105     213.344 196.600 146.641  1.00 21.55           C  
ATOM  13934  O   THR B1105     214.376 196.626 147.311  1.00 22.32           O  
ATOM  13935  CB  THR B1105     212.713 194.514 145.475  1.00 21.54           C  
ATOM  13936  OG1 THR B1105     211.360 194.640 145.868  1.00 21.92           O  
ATOM  13937  CG2 THR B1105     213.469 193.735 146.523  1.00 21.52           C  
ATOM  13938  N   GLN B1106     212.211 197.155 147.049  1.00 21.31           N  
ATOM  13939  CA  GLN B1106     212.121 197.782 148.354  1.00 20.72           C  
ATOM  13940  C   GLN B1106     212.449 196.765 149.434  1.00 20.17           C  
ATOM  13941  O   GLN B1106     211.976 195.632 149.414  1.00 20.80           O  
ATOM  13942  CB  GLN B1106     210.744 198.411 148.547  1.00 20.51           C  
ATOM  13943  CG  GLN B1106     209.606 197.443 148.592  1.00 20.18           C  
ATOM  13944  CD  GLN B1106     208.291 198.143 148.595  1.00 19.79           C  
ATOM  13945  OE1 GLN B1106     208.136 199.194 149.234  1.00 19.77           O  
ATOM  13946  NE2 GLN B1106     207.337 197.583 147.876  1.00 19.90           N  
ATOM  13947  N   ARG B1107     213.257 197.187 150.386  1.00 20.23           N  
ATOM  13948  CA  ARG B1107     213.772 196.314 151.429  1.00 19.84           C  
ATOM  13949  C   ARG B1107     212.748 195.784 152.429  1.00 19.54           C  
ATOM  13950  O   ARG B1107     213.004 194.782 153.092  1.00 19.93           O  
ATOM  13951  CB  ARG B1107     214.899 197.040 152.139  1.00 20.03           C  
ATOM  13952  CG  ARG B1107     214.497 198.340 152.794  1.00 20.00           C  
ATOM  13953  CD  ARG B1107     215.672 199.133 153.227  1.00 20.35           C  
ATOM  13954  NE  ARG B1107     216.512 199.534 152.085  1.00 20.61           N  
ATOM  13955  CZ  ARG B1107     217.410 200.542 152.097  1.00 20.76           C  
ATOM  13956  NH1 ARG B1107     217.566 201.267 153.184  1.00 20.66           N  
ATOM  13957  NH2 ARG B1107     218.143 200.810 151.013  1.00 20.71           N  
ATOM  13958  N   ASN B1108     211.602 196.441 152.559  1.00 19.55           N  
ATOM  13959  CA  ASN B1108     210.609 195.993 153.530  1.00 19.04           C  
ATOM  13960  C   ASN B1108     209.463 195.180 152.935  1.00 19.29           C  
ATOM  13961  O   ASN B1108     208.505 194.865 153.643  1.00 19.30           O  
ATOM  13962  CB  ASN B1108     210.056 197.174 154.291  1.00 18.44           C  
ATOM  13963  CG  ASN B1108     211.061 197.775 155.204  1.00 18.69           C  
ATOM  13964  OD1 ASN B1108     211.816 197.063 155.874  1.00 18.76           O  
ATOM  13965  ND2 ASN B1108     211.097 199.076 155.252  1.00 18.43           N  
ATOM  13966  N   PHE B1109     209.537 194.859 151.648  1.00 19.78           N  
ATOM  13967  CA  PHE B1109     208.482 194.076 151.007  1.00 19.22           C  
ATOM  13968  C   PHE B1109     208.918 193.620 149.625  1.00 19.77           C  
ATOM  13969  O   PHE B1109     209.149 194.442 148.745  1.00 20.78           O  
ATOM  13970  CB  PHE B1109     207.195 194.891 150.906  1.00 19.51           C  
ATOM  13971  CG  PHE B1109     206.057 194.126 150.372  1.00 19.66           C  
ATOM  13972  CD1 PHE B1109     205.347 193.269 151.176  1.00 19.44           C  
ATOM  13973  CD2 PHE B1109     205.693 194.251 149.060  1.00 19.92           C  
ATOM  13974  CE1 PHE B1109     204.292 192.552 150.670  1.00 19.42           C  
ATOM  13975  CE2 PHE B1109     204.642 193.538 148.554  1.00 19.95           C  
ATOM  13976  CZ  PHE B1109     203.940 192.687 149.363  1.00 19.34           C  
ATOM  13977  N   TYR B1110     209.024 192.321 149.416  1.00 19.73           N  
ATOM  13978  CA  TYR B1110     209.537 191.834 148.153  1.00 19.83           C  
ATOM  13979  C   TYR B1110     208.620 192.168 147.001  1.00 20.47           C  
ATOM  13980  O   TYR B1110     207.466 191.745 146.944  1.00 20.32           O  
ATOM  13981  CB  TYR B1110     209.755 190.336 148.210  1.00 20.19           C  
ATOM  13982  CG  TYR B1110     210.314 189.780 146.966  1.00 20.56           C  
ATOM  13983  CD1 TYR B1110     211.580 190.127 146.573  1.00 21.06           C  
ATOM  13984  CD2 TYR B1110     209.569 188.912 146.213  1.00 20.80           C  
ATOM  13985  CE1 TYR B1110     212.102 189.612 145.424  1.00 21.05           C  
ATOM  13986  CE2 TYR B1110     210.093 188.387 145.063  1.00 21.00           C  
ATOM  13987  CZ  TYR B1110     211.357 188.737 144.668  1.00 21.00           C  
ATOM  13988  OH  TYR B1110     211.890 188.213 143.519  1.00 21.89           O  
ATOM  13989  N   GLU B1111     209.168 192.897 146.054  1.00 21.07           N  
ATOM  13990  CA  GLU B1111     208.445 193.344 144.886  1.00 20.57           C  
ATOM  13991  C   GLU B1111     209.442 193.681 143.784  1.00 21.14           C  
ATOM  13992  O   GLU B1111     209.800 194.848 143.624  1.00 21.92           O  
ATOM  13993  CB  GLU B1111     207.627 194.569 145.249  1.00 20.34           C  
ATOM  13994  CG  GLU B1111     206.728 195.050 144.180  1.00 20.67           C  
ATOM  13995  CD  GLU B1111     205.990 196.243 144.600  1.00 20.39           C  
ATOM  13996  OE1 GLU B1111     206.621 197.221 144.909  1.00 20.34           O  
ATOM  13997  OE2 GLU B1111     204.793 196.188 144.633  1.00 19.83           O  
ATOM  13998  N   PRO B1112     209.959 192.684 143.073  1.00 20.87           N  
ATOM  13999  CA  PRO B1112     211.121 192.771 142.219  1.00 21.58           C  
ATOM  14000  C   PRO B1112     210.872 193.649 141.021  1.00 22.45           C  
ATOM  14001  O   PRO B1112     209.876 193.476 140.321  1.00 22.58           O  
ATOM  14002  CB  PRO B1112     211.328 191.319 141.805  1.00 22.14           C  
ATOM  14003  CG  PRO B1112     209.964 190.691 141.917  1.00 21.39           C  
ATOM  14004  CD  PRO B1112     209.280 191.408 143.054  1.00 21.17           C  
ATOM  14005  N   GLN B1113     211.804 194.549 140.751  1.00 22.80           N  
ATOM  14006  CA  GLN B1113     211.724 195.402 139.587  1.00 23.07           C  
ATOM  14007  C   GLN B1113     212.881 195.122 138.664  1.00 24.05           C  
ATOM  14008  O   GLN B1113     213.949 194.695 139.100  1.00 24.78           O  
ATOM  14009  CB  GLN B1113     211.746 196.868 139.991  1.00 23.46           C  
ATOM  14010  CG  GLN B1113     210.696 197.225 140.978  1.00 22.88           C  
ATOM  14011  CD  GLN B1113     209.342 197.009 140.432  1.00 22.92           C  
ATOM  14012  OE1 GLN B1113     209.001 197.506 139.356  1.00 23.23           O  
ATOM  14013  NE2 GLN B1113     208.546 196.252 141.159  1.00 22.51           N  
ATOM  14014  N   ILE B1114     212.709 195.428 137.397  1.00 24.64           N  
ATOM  14015  CA  ILE B1114     213.827 195.345 136.482  1.00 25.30           C  
ATOM  14016  C   ILE B1114     214.792 196.442 136.852  1.00 25.63           C  
ATOM  14017  O   ILE B1114     214.377 197.565 137.132  1.00 26.26           O  
ATOM  14018  CB  ILE B1114     213.377 195.494 135.021  1.00 25.71           C  
ATOM  14019  CG1 ILE B1114     212.391 194.353 134.646  1.00 25.56           C  
ATOM  14020  CG2 ILE B1114     214.588 195.528 134.078  1.00 27.25           C  
ATOM  14021  CD1 ILE B1114     212.947 192.932 134.773  1.00 25.47           C  
ATOM  14022  N   ILE B1115     216.068 196.119 136.885  1.00 25.81           N  
ATOM  14023  CA  ILE B1115     217.053 197.117 137.221  1.00 26.04           C  
ATOM  14024  C   ILE B1115     217.288 198.010 136.030  1.00 27.50           C  
ATOM  14025  O   ILE B1115     217.668 197.540 134.956  1.00 29.09           O  
ATOM  14026  CB  ILE B1115     218.359 196.462 137.648  1.00 25.96           C  
ATOM  14027  CG1 ILE B1115     218.107 195.640 138.894  1.00 25.36           C  
ATOM  14028  CG2 ILE B1115     219.374 197.529 137.906  1.00 26.17           C  
ATOM  14029  CD1 ILE B1115     219.201 194.685 139.262  1.00 25.29           C  
ATOM  14030  N   THR B1116     217.044 199.292 136.228  1.00 26.98           N  
ATOM  14031  CA  THR B1116     217.160 200.268 135.167  1.00 27.09           C  
ATOM  14032  C   THR B1116     217.908 201.475 135.672  1.00 28.27           C  
ATOM  14033  O   THR B1116     218.115 201.629 136.878  1.00 26.57           O  
ATOM  14034  CB  THR B1116     215.789 200.750 134.667  1.00 28.01           C  
ATOM  14035  OG1 THR B1116     215.224 201.647 135.618  1.00 28.08           O  
ATOM  14036  CG2 THR B1116     214.845 199.606 134.491  1.00 28.68           C  
ATOM  14037  N   THR B1117     218.229 202.381 134.767  1.00 27.66           N  
ATOM  14038  CA  THR B1117     218.917 203.612 135.134  1.00 27.24           C  
ATOM  14039  C   THR B1117     218.017 204.544 135.941  1.00 26.50           C  
ATOM  14040  O   THR B1117     218.484 205.537 136.499  1.00 26.44           O  
ATOM  14041  CB  THR B1117     219.426 204.350 133.891  1.00 28.84           C  
ATOM  14042  OG1 THR B1117     218.316 204.681 133.051  1.00 29.96           O  
ATOM  14043  CG2 THR B1117     220.393 203.464 133.125  1.00 29.82           C  
ATOM  14044  N   ASP B1118     216.724 204.234 135.995  1.00 26.89           N  
ATOM  14045  CA  ASP B1118     215.785 205.032 136.765  1.00 26.58           C  
ATOM  14046  C   ASP B1118     215.638 204.487 138.179  1.00 26.34           C  
ATOM  14047  O   ASP B1118     214.967 205.090 139.016  1.00 25.72           O  
ATOM  14048  CB  ASP B1118     214.423 205.060 136.085  1.00 27.34           C  
ATOM  14049  CG  ASP B1118     214.431 205.788 134.752  1.00 28.47           C  
ATOM  14050  OD1 ASP B1118     215.192 206.714 134.585  1.00 27.86           O  
ATOM  14051  OD2 ASP B1118     213.673 205.397 133.902  1.00 29.04           O  
ATOM  14052  N   ASN B1119     216.254 203.334 138.441  1.00 25.92           N  
ATOM  14053  CA  ASN B1119     216.196 202.711 139.755  1.00 25.16           C  
ATOM  14054  C   ASN B1119     217.522 202.842 140.476  1.00 25.04           C  
ATOM  14055  O   ASN B1119     217.564 202.831 141.708  1.00 24.75           O  
ATOM  14056  CB  ASN B1119     215.791 201.254 139.661  1.00 25.65           C  
ATOM  14057  CG  ASN B1119     214.379 201.083 139.212  1.00 26.58           C  
ATOM  14058  OD1 ASN B1119     213.528 201.906 139.557  1.00 27.13           O  
ATOM  14059  ND2 ASN B1119     214.086 200.042 138.466  1.00 26.79           N  
ATOM  14060  N   THR B1120     218.602 202.963 139.711  1.00 24.54           N  
ATOM  14061  CA  THR B1120     219.934 203.039 140.282  1.00 23.49           C  
ATOM  14062  C   THR B1120     220.635 204.337 139.933  1.00 23.91           C  
ATOM  14063  O   THR B1120     220.302 204.993 138.951  1.00 25.04           O  
ATOM  14064  CB  THR B1120     220.793 201.881 139.770  1.00 23.87           C  
ATOM  14065  OG1 THR B1120     221.023 202.034 138.373  1.00 24.81           O  
ATOM  14066  CG2 THR B1120     220.075 200.576 139.990  1.00 24.15           C  
ATOM  14067  N   PHE B1121     221.664 204.667 140.692  1.00 22.79           N  
ATOM  14068  CA  PHE B1121     222.498 205.816 140.400  1.00 22.63           C  
ATOM  14069  C   PHE B1121     223.925 205.345 140.254  1.00 23.38           C  
ATOM  14070  O   PHE B1121     224.286 204.274 140.736  1.00 22.44           O  
ATOM  14071  CB  PHE B1121     222.393 206.879 141.485  1.00 22.76           C  
ATOM  14072  CG  PHE B1121     222.952 206.478 142.795  1.00 22.19           C  
ATOM  14073  CD1 PHE B1121     224.266 206.759 143.123  1.00 22.20           C  
ATOM  14074  CD2 PHE B1121     222.173 205.818 143.707  1.00 22.89           C  
ATOM  14075  CE1 PHE B1121     224.775 206.385 144.338  1.00 21.81           C  
ATOM  14076  CE2 PHE B1121     222.676 205.444 144.918  1.00 22.47           C  
ATOM  14077  CZ  PHE B1121     223.980 205.727 145.235  1.00 21.70           C  
ATOM  14078  N   VAL B1122     224.742 206.123 139.574  1.00 22.20           N  
ATOM  14079  CA  VAL B1122     226.109 205.702 139.336  1.00 22.28           C  
ATOM  14080  C   VAL B1122     227.126 206.477 140.131  1.00 22.26           C  
ATOM  14081  O   VAL B1122     227.104 207.707 140.151  1.00 22.67           O  
ATOM  14082  CB  VAL B1122     226.436 205.832 137.854  1.00 23.13           C  
ATOM  14083  CG1 VAL B1122     227.882 205.460 137.610  1.00 23.51           C  
ATOM  14084  CG2 VAL B1122     225.515 204.935 137.086  1.00 24.17           C  
ATOM  14085  N   SER B1123     228.026 205.753 140.777  1.00 22.03           N  
ATOM  14086  CA  SER B1123     229.102 206.395 141.508  1.00 21.70           C  
ATOM  14087  C   SER B1123     230.325 205.506 141.609  1.00 21.89           C  
ATOM  14088  O   SER B1123     230.253 204.386 142.104  1.00 22.16           O  
ATOM  14089  CB  SER B1123     228.651 206.786 142.891  1.00 21.38           C  
ATOM  14090  OG  SER B1123     229.693 207.419 143.580  1.00 21.31           O  
ATOM  14091  N   GLY B1124     231.462 206.006 141.161  1.00 21.94           N  
ATOM  14092  CA  GLY B1124     232.685 205.224 141.246  1.00 22.49           C  
ATOM  14093  C   GLY B1124     232.633 204.066 140.266  1.00 23.13           C  
ATOM  14094  O   GLY B1124     231.903 204.115 139.272  1.00 23.18           O  
ATOM  14095  N   ASN B1125     233.411 203.020 140.535  1.00 23.44           N  
ATOM  14096  CA  ASN B1125     233.488 201.922 139.591  1.00 24.03           C  
ATOM  14097  C   ASN B1125     233.747 200.564 140.266  1.00 23.90           C  
ATOM  14098  O   ASN B1125     233.907 200.472 141.493  1.00 24.34           O  
ATOM  14099  CB  ASN B1125     234.539 202.251 138.540  1.00 23.92           C  
ATOM  14100  CG  ASN B1125     235.904 202.369 139.113  1.00 23.74           C  
ATOM  14101  OD1 ASN B1125     236.432 201.402 139.676  1.00 24.02           O  
ATOM  14102  ND2 ASN B1125     236.500 203.529 138.985  1.00 23.98           N  
ATOM  14103  N   CYS B1126     233.774 199.519 139.431  1.00 23.65           N  
ATOM  14104  CA  CYS B1126     233.885 198.114 139.816  1.00 24.17           C  
ATOM  14105  C   CYS B1126     235.212 197.696 140.468  1.00 24.38           C  
ATOM  14106  O   CYS B1126     235.291 196.604 141.037  1.00 24.05           O  
ATOM  14107  CB  CYS B1126     233.620 197.241 138.573  1.00 25.55           C  
ATOM  14108  SG  CYS B1126     231.932 197.426 137.932  1.00 26.00           S  
ATOM  14109  N   ASP B1127     236.249 198.550 140.410  1.00 24.35           N  
ATOM  14110  CA  ASP B1127     237.555 198.248 141.002  1.00 24.27           C  
ATOM  14111  C   ASP B1127     237.606 198.695 142.455  1.00 24.25           C  
ATOM  14112  O   ASP B1127     238.604 198.484 143.144  1.00 24.27           O  
ATOM  14113  CB  ASP B1127     238.674 198.931 140.220  1.00 24.12           C  
ATOM  14114  CG  ASP B1127     238.840 198.378 138.813  1.00 24.35           C  
ATOM  14115  OD1 ASP B1127     238.567 197.218 138.601  1.00 24.26           O  
ATOM  14116  OD2 ASP B1127     239.234 199.129 137.955  1.00 23.87           O  
ATOM  14117  N   VAL B1128     236.534 199.328 142.916  1.00 24.17           N  
ATOM  14118  CA  VAL B1128     236.489 199.832 144.275  1.00 23.75           C  
ATOM  14119  C   VAL B1128     235.499 199.078 145.153  1.00 23.54           C  
ATOM  14120  O   VAL B1128     235.810 198.750 146.297  1.00 23.36           O  
ATOM  14121  CB  VAL B1128     236.143 201.329 144.265  1.00 24.13           C  
ATOM  14122  CG1 VAL B1128     236.022 201.851 145.684  1.00 23.41           C  
ATOM  14123  CG2 VAL B1128     237.221 202.082 143.502  1.00 24.30           C  
ATOM  14124  N   VAL B1129     234.292 198.844 144.648  1.00 23.73           N  
ATOM  14125  CA  VAL B1129     233.253 198.259 145.492  1.00 23.09           C  
ATOM  14126  C   VAL B1129     233.462 196.772 145.754  1.00 23.04           C  
ATOM  14127  O   VAL B1129     233.584 195.963 144.833  1.00 23.51           O  
ATOM  14128  CB  VAL B1129     231.877 198.470 144.852  1.00 23.21           C  
ATOM  14129  CG1 VAL B1129     230.784 197.785 145.687  1.00 22.80           C  
ATOM  14130  CG2 VAL B1129     231.606 199.946 144.728  1.00 23.54           C  
ATOM  14131  N   ILE B1130     233.460 196.416 147.030  1.00 22.91           N  
ATOM  14132  CA  ILE B1130     233.681 195.047 147.451  1.00 22.84           C  
ATOM  14133  C   ILE B1130     232.416 194.230 147.316  1.00 22.91           C  
ATOM  14134  O   ILE B1130     231.385 194.578 147.880  1.00 22.79           O  
ATOM  14135  CB  ILE B1130     234.143 195.011 148.918  1.00 22.66           C  
ATOM  14136  CG1 ILE B1130     235.477 195.763 149.058  1.00 23.21           C  
ATOM  14137  CG2 ILE B1130     234.272 193.563 149.390  1.00 22.95           C  
ATOM  14138  CD1 ILE B1130     235.877 196.058 150.496  1.00 22.56           C  
ATOM  14139  N   GLY B1131     232.496 193.127 146.591  1.00 22.99           N  
ATOM  14140  CA  GLY B1131     231.338 192.263 146.425  1.00 22.95           C  
ATOM  14141  C   GLY B1131     230.451 192.663 145.257  1.00 23.17           C  
ATOM  14142  O   GLY B1131     229.365 192.111 145.093  1.00 22.89           O  
ATOM  14143  N   ILE B1132     230.907 193.607 144.442  1.00 23.27           N  
ATOM  14144  CA  ILE B1132     230.129 194.046 143.292  1.00 22.98           C  
ATOM  14145  C   ILE B1132     230.022 192.916 142.281  1.00 23.82           C  
ATOM  14146  O   ILE B1132     230.974 192.161 142.096  1.00 24.43           O  
ATOM  14147  CB  ILE B1132     230.758 195.297 142.657  1.00 23.31           C  
ATOM  14148  CG1 ILE B1132     229.767 195.940 141.727  1.00 24.10           C  
ATOM  14149  CG2 ILE B1132     232.029 194.937 141.914  1.00 24.17           C  
ATOM  14150  CD1 ILE B1132     230.086 197.363 141.344  1.00 24.63           C  
ATOM  14151  N   VAL B1133     228.860 192.780 141.645  1.00 23.98           N  
ATOM  14152  CA  VAL B1133     228.660 191.702 140.677  1.00 24.45           C  
ATOM  14153  C   VAL B1133     228.317 192.251 139.299  1.00 25.30           C  
ATOM  14154  O   VAL B1133     227.882 193.392 139.196  1.00 25.60           O  
ATOM  14155  CB  VAL B1133     227.512 190.787 141.140  1.00 23.71           C  
ATOM  14156  CG1 VAL B1133     227.831 190.193 142.491  1.00 24.61           C  
ATOM  14157  CG2 VAL B1133     226.227 191.585 141.186  1.00 23.59           C  
ATOM  14158  N   ASN B1134     228.485 191.427 138.251  1.00 25.92           N  
ATOM  14159  CA  ASN B1134     228.136 191.784 136.876  1.00 25.93           C  
ATOM  14160  C   ASN B1134     226.637 191.620 136.620  1.00 25.75           C  
ATOM  14161  O   ASN B1134     226.036 190.626 137.030  1.00 25.27           O  
ATOM  14162  CB  ASN B1134     228.934 190.942 135.876  1.00 27.34           C  
ATOM  14163  CG  ASN B1134     230.198 191.628 135.375  1.00 28.47           C  
ATOM  14164  OD1 ASN B1134     230.141 192.759 134.869  1.00 28.10           O  
ATOM  14165  ND2 ASN B1134     231.320 190.951 135.501  1.00 30.15           N  
ATOM  14166  N   ASN B1135     226.055 192.586 135.895  1.00 25.90           N  
ATOM  14167  CA  ASN B1135     224.660 192.575 135.463  1.00 26.04           C  
ATOM  14168  C   ASN B1135     224.487 193.418 134.214  1.00 26.44           C  
ATOM  14169  O   ASN B1135     225.431 194.039 133.737  1.00 26.60           O  
ATOM  14170  CB  ASN B1135     223.757 193.106 136.558  1.00 26.10           C  
ATOM  14171  CG  ASN B1135     222.346 192.706 136.390  1.00 26.46           C  
ATOM  14172  OD1 ASN B1135     222.023 191.860 135.553  1.00 26.58           O  
ATOM  14173  ND2 ASN B1135     221.482 193.324 137.128  1.00 26.24           N  
ATOM  14174  N   THR B1136     223.269 193.469 133.709  1.00 26.84           N  
ATOM  14175  CA  THR B1136     222.946 194.380 132.629  1.00 27.20           C  
ATOM  14176  C   THR B1136     221.893 195.349 133.117  1.00 27.43           C  
ATOM  14177  O   THR B1136     220.838 194.929 133.589  1.00 27.64           O  
ATOM  14178  CB  THR B1136     222.424 193.635 131.390  1.00 27.32           C  
ATOM  14179  OG1 THR B1136     223.426 192.733 130.917  1.00 27.58           O  
ATOM  14180  CG2 THR B1136     222.078 194.622 130.286  1.00 28.38           C  
ATOM  14181  N   VAL B1137     222.167 196.639 132.990  1.00 27.88           N  
ATOM  14182  CA  VAL B1137     221.213 197.651 133.408  1.00 28.00           C  
ATOM  14183  C   VAL B1137     220.435 198.152 132.212  1.00 28.96           C  
ATOM  14184  O   VAL B1137     221.012 198.569 131.209  1.00 29.32           O  
ATOM  14185  CB  VAL B1137     221.924 198.817 134.099  1.00 27.43           C  
ATOM  14186  CG1 VAL B1137     220.923 199.883 134.490  1.00 28.03           C  
ATOM  14187  CG2 VAL B1137     222.626 198.299 135.303  1.00 27.25           C  
ATOM  14188  N   TYR B1138     219.123 198.095 132.313  1.00 29.54           N  
ATOM  14189  CA  TYR B1138     218.267 198.501 131.222  1.00 30.78           C  
ATOM  14190  C   TYR B1138     218.067 200.003 131.173  1.00 33.26           C  
ATOM  14191  O   TYR B1138     217.777 200.640 132.185  1.00 29.87           O  
ATOM  14192  CB  TYR B1138     216.931 197.784 131.331  1.00 31.40           C  
ATOM  14193  CG  TYR B1138     215.903 198.234 130.339  1.00 33.39           C  
ATOM  14194  CD1 TYR B1138     216.010 197.886 129.011  1.00 34.76           C  
ATOM  14195  CD2 TYR B1138     214.834 198.989 130.765  1.00 34.07           C  
ATOM  14196  CE1 TYR B1138     215.046 198.298 128.118  1.00 35.94           C  
ATOM  14197  CE2 TYR B1138     213.878 199.391 129.885  1.00 35.05           C  
ATOM  14198  CZ  TYR B1138     213.976 199.052 128.569  1.00 36.11           C  
ATOM  14199  OH  TYR B1138     213.005 199.458 127.694  1.00 37.70           O  
ATOM  14200  N   ASP B1139     218.216 200.564 129.983  1.00 34.24           N  
ATOM  14201  CA  ASP B1139     217.992 201.981 129.759  1.00 34.11           C  
ATOM  14202  C   ASP B1139     216.729 202.181 128.917  1.00 36.17           C  
ATOM  14203  O   ASP B1139     216.762 201.927 127.713  1.00 36.54           O  
ATOM  14204  CB  ASP B1139     219.176 202.613 129.042  1.00 35.35           C  
ATOM  14205  CG  ASP B1139     218.980 204.095 128.852  1.00 36.65           C  
ATOM  14206  OD1 ASP B1139     217.943 204.585 129.269  1.00 36.39           O  
ATOM  14207  OD2 ASP B1139     219.838 204.730 128.286  1.00 38.94           O  
ATOM  14208  N   PRO B1140     215.608 202.620 129.508  1.00 36.46           N  
ATOM  14209  CA  PRO B1140     214.319 202.828 128.871  1.00 36.40           C  
ATOM  14210  C   PRO B1140     214.391 203.810 127.712  1.00 38.48           C  
ATOM  14211  O   PRO B1140     213.505 203.832 126.857  1.00 40.60           O  
ATOM  14212  CB  PRO B1140     213.473 203.406 130.008  1.00 35.85           C  
ATOM  14213  CG  PRO B1140     214.131 202.921 131.262  1.00 33.88           C  
ATOM  14214  CD  PRO B1140     215.601 202.887 130.944  1.00 34.00           C  
ATOM  14215  N   LEU B1141     215.430 204.637 127.687  1.00 38.74           N  
ATOM  14216  CA  LEU B1141     215.574 205.613 126.628  1.00 38.55           C  
ATOM  14217  C   LEU B1141     216.001 205.002 125.306  1.00 41.79           C  
ATOM  14218  O   LEU B1141     215.610 205.490 124.244  1.00 41.34           O  
ATOM  14219  CB  LEU B1141     216.581 206.697 127.030  1.00 39.98           C  
ATOM  14220  CG  LEU B1141     216.857 207.793 125.976  1.00 41.35           C  
ATOM  14221  CD1 LEU B1141     215.566 208.520 125.602  1.00 41.99           C  
ATOM  14222  CD2 LEU B1141     217.883 208.774 126.528  1.00 42.28           C  
ATOM  14223  N   GLN B1142     216.856 203.986 125.331  1.00 39.70           N  
ATOM  14224  CA  GLN B1142     217.366 203.526 124.055  1.00 40.81           C  
ATOM  14225  C   GLN B1142     216.270 203.044 123.102  1.00 41.39           C  
ATOM  14226  O   GLN B1142     216.253 203.484 121.957  1.00 42.41           O  
ATOM  14227  CB  GLN B1142     218.483 202.491 124.183  1.00 41.81           C  
ATOM  14228  N   PRO B1143     215.351 202.143 123.499  1.00 41.82           N  
ATOM  14229  CA  PRO B1143     214.276 201.641 122.660  1.00 42.80           C  
ATOM  14230  C   PRO B1143     213.453 202.765 122.045  1.00 42.73           C  
ATOM  14231  O   PRO B1143     212.993 202.650 120.907  1.00 43.85           O  
ATOM  14232  CB  PRO B1143     213.445 200.827 123.650  1.00 40.80           C  
ATOM  14233  CG  PRO B1143     214.436 200.389 124.681  1.00 40.08           C  
ATOM  14234  CD  PRO B1143     215.350 201.571 124.852  1.00 40.28           C  
ATOM  14235  N   GLU B1144     213.289 203.860 122.783  1.00 42.44           N  
ATOM  14236  CA  GLU B1144     212.518 204.990 122.299  1.00 42.26           C  
ATOM  14237  C   GLU B1144     213.260 205.727 121.199  1.00 43.13           C  
ATOM  14238  O   GLU B1144     212.654 206.194 120.233  1.00 44.46           O  
ATOM  14239  CB  GLU B1144     212.219 205.942 123.449  1.00 43.45           C  
ATOM  14240  CG  GLU B1144     211.263 205.398 124.501  1.00 42.53           C  
ATOM  14241  CD  GLU B1144     209.880 205.134 123.978  1.00 43.53           C  
ATOM  14242  OE1 GLU B1144     209.342 205.970 123.287  1.00 43.23           O  
ATOM  14243  OE2 GLU B1144     209.357 204.091 124.277  1.00 43.31           O  
ATOM  14244  N   LEU B1145     214.580 205.810 121.333  1.00 41.97           N  
ATOM  14245  CA  LEU B1145     215.402 206.467 120.330  1.00 44.12           C  
ATOM  14246  C   LEU B1145     215.527 205.591 119.090  1.00 44.97           C  
ATOM  14247  O   LEU B1145     215.539 206.093 117.965  1.00 44.37           O  
ATOM  14248  CB  LEU B1145     216.801 206.751 120.889  1.00 44.06           C  
ATOM  14249  N   ASP B1146     215.601 204.274 119.301  1.00 44.13           N  
ATOM  14250  CA  ASP B1146     215.735 203.321 118.196  1.00 44.43           C  
ATOM  14251  C   ASP B1146     214.449 203.171 117.367  1.00 44.90           C  
ATOM  14252  O   ASP B1146     214.519 203.033 116.143  1.00 45.04           O  
ATOM  14253  CB  ASP B1146     216.142 201.931 118.710  1.00 44.58           C  
ATOM  14254  N   SER B1147     213.279 203.203 118.034  1.00 44.15           N  
ATOM  14255  CA  SER B1147     211.967 203.076 117.404  1.00 44.82           C  
ATOM  14256  C   SER B1147     211.571 204.401 116.746  1.00 45.32           C  
ATOM  14257  O   SER B1147     211.033 204.426 115.634  1.00 45.29           O  
ATOM  14258  CB  SER B1147     210.928 202.652 118.444  1.00 44.75           C  
ATOM  14259  OG  SER B1147     209.644 202.575 117.887  1.00 45.15           O  
TER   14260      SER B1147                                                      
ATOM  14261  N   ALA C  27     262.092 224.816 229.070  1.00 52.78           N  
ATOM  14262  CA  ALA C  27     262.433 223.954 227.947  1.00 51.64           C  
ATOM  14263  C   ALA C  27     261.197 223.170 227.503  1.00 50.02           C  
ATOM  14264  O   ALA C  27     260.518 222.562 228.336  1.00 52.55           O  
ATOM  14265  CB  ALA C  27     263.567 222.989 228.320  1.00 51.40           C  
ATOM  14266  N   TYR C  28     260.894 223.216 226.194  1.00 50.67           N  
ATOM  14267  CA  TYR C  28     259.748 222.529 225.585  1.00 49.55           C  
ATOM  14268  C   TYR C  28     260.147 221.816 224.312  1.00 50.77           C  
ATOM  14269  O   TYR C  28     261.028 222.277 223.585  1.00 50.78           O  
ATOM  14270  CB  TYR C  28     258.632 223.521 225.280  1.00 50.93           C  
ATOM  14271  CG  TYR C  28     258.038 224.154 226.498  1.00 50.87           C  
ATOM  14272  CD1 TYR C  28     258.674 225.216 227.114  1.00 50.93           C  
ATOM  14273  CD2 TYR C  28     256.849 223.682 226.997  1.00 51.53           C  
ATOM  14274  CE1 TYR C  28     258.126 225.794 228.227  1.00 50.89           C  
ATOM  14275  CE2 TYR C  28     256.296 224.263 228.109  1.00 51.36           C  
ATOM  14276  CZ  TYR C  28     256.932 225.315 228.725  1.00 51.05           C  
ATOM  14277  OH  TYR C  28     256.380 225.895 229.840  1.00 50.64           O  
ATOM  14278  N   THR C  29     259.472 220.709 224.028  1.00 50.85           N  
ATOM  14279  CA  THR C  29     259.692 219.975 222.789  1.00 51.47           C  
ATOM  14280  C   THR C  29     258.391 219.648 222.061  1.00 50.68           C  
ATOM  14281  O   THR C  29     257.295 219.787 222.610  1.00 50.84           O  
ATOM  14282  CB  THR C  29     260.505 218.690 223.034  1.00 51.33           C  
ATOM  14283  OG1 THR C  29     259.793 217.824 223.921  1.00 51.12           O  
ATOM  14284  CG2 THR C  29     261.859 219.035 223.627  1.00 52.18           C  
ATOM  14285  N   ASN C  30     258.542 219.221 220.810  1.00 50.60           N  
ATOM  14286  CA  ASN C  30     257.451 218.858 219.907  1.00 50.22           C  
ATOM  14287  C   ASN C  30     256.987 217.415 220.120  1.00 49.18           C  
ATOM  14288  O   ASN C  30     257.766 216.477 219.965  1.00 49.50           O  
ATOM  14289  CB  ASN C  30     257.912 219.079 218.474  1.00 49.91           C  
ATOM  14290  CG  ASN C  30     256.840 218.958 217.431  1.00 49.40           C  
ATOM  14291  OD1 ASN C  30     255.801 218.315 217.606  1.00 50.15           O  
ATOM  14292  ND2 ASN C  30     257.088 219.590 216.307  1.00 50.43           N  
ATOM  14293  N   SER C  31     255.726 217.238 220.511  1.00 48.32           N  
ATOM  14294  CA  SER C  31     255.155 215.912 220.773  1.00 49.42           C  
ATOM  14295  C   SER C  31     254.912 215.106 219.499  1.00 48.42           C  
ATOM  14296  O   SER C  31     254.655 213.898 219.547  1.00 48.77           O  
ATOM  14297  CB  SER C  31     253.838 216.048 221.486  1.00 48.65           C  
ATOM  14298  OG  SER C  31     252.899 216.630 220.647  1.00 49.06           O  
ATOM  14299  N   PHE C  32     254.972 215.784 218.367  1.00 49.75           N  
ATOM  14300  CA  PHE C  32     254.734 215.197 217.062  1.00 50.76           C  
ATOM  14301  C   PHE C  32     253.432 214.415 217.001  1.00 49.38           C  
ATOM  14302  O   PHE C  32     252.355 214.971 217.210  1.00 40.21           O  
ATOM  14303  CB  PHE C  32     255.895 214.297 216.655  1.00 48.58           C  
ATOM  14304  CG  PHE C  32     257.166 215.031 216.424  1.00 50.79           C  
ATOM  14305  CD1 PHE C  32     258.160 215.013 217.367  1.00 49.74           C  
ATOM  14306  CD2 PHE C  32     257.371 215.743 215.260  1.00 49.63           C  
ATOM  14307  CE1 PHE C  32     259.337 215.688 217.164  1.00 50.21           C  
ATOM  14308  CE2 PHE C  32     258.547 216.423 215.049  1.00 49.92           C  
ATOM  14309  CZ  PHE C  32     259.531 216.394 216.005  1.00 50.39           C  
ATOM  14310  N   THR C  33     253.529 213.122 216.713  1.00 49.32           N  
ATOM  14311  CA  THR C  33     252.360 212.277 216.535  1.00 48.68           C  
ATOM  14312  C   THR C  33     252.262 211.182 217.575  1.00 48.26           C  
ATOM  14313  O   THR C  33     251.642 210.148 217.338  1.00 48.50           O  
ATOM  14314  CB  THR C  33     252.367 211.654 215.140  1.00 48.75           C  
ATOM  14315  OG1 THR C  33     253.576 210.903 214.960  1.00 49.39           O  
ATOM  14316  CG2 THR C  33     252.297 212.760 214.105  1.00 49.63           C  
ATOM  14317  N   ARG C  34     252.916 211.377 218.710  1.00 48.61           N  
ATOM  14318  CA  ARG C  34     252.879 210.383 219.769  1.00 47.55           C  
ATOM  14319  C   ARG C  34     251.868 210.779 220.832  1.00 48.12           C  
ATOM  14320  O   ARG C  34     251.402 211.914 220.857  1.00 48.15           O  
ATOM  14321  CB  ARG C  34     254.257 210.173 220.358  1.00 47.95           C  
ATOM  14322  CG  ARG C  34     255.215 209.636 219.336  1.00 48.71           C  
ATOM  14323  CD  ARG C  34     256.376 208.991 219.897  1.00 49.14           C  
ATOM  14324  NE  ARG C  34     257.228 208.469 218.830  1.00 50.75           N  
ATOM  14325  CZ  ARG C  34     258.023 207.387 218.934  1.00 51.17           C  
ATOM  14326  NH1 ARG C  34     258.062 206.700 220.046  1.00 51.80           N  
ATOM  14327  NH2 ARG C  34     258.761 206.999 217.908  1.00 51.74           N  
ATOM  14328  N   GLY C  35     251.500 209.833 221.693  1.00 48.48           N  
ATOM  14329  CA  GLY C  35     250.503 210.119 222.719  1.00 48.49           C  
ATOM  14330  C   GLY C  35     249.171 209.451 222.405  1.00 48.79           C  
ATOM  14331  O   GLY C  35     248.108 209.878 222.871  1.00 48.80           O  
ATOM  14332  N   VAL C  36     249.251 208.409 221.586  1.00 48.82           N  
ATOM  14333  CA  VAL C  36     248.122 207.582 221.205  1.00 49.01           C  
ATOM  14334  C   VAL C  36     248.211 206.245 221.906  1.00 49.43           C  
ATOM  14335  O   VAL C  36     249.288 205.675 222.061  1.00 50.43           O  
ATOM  14336  CB  VAL C  36     248.053 207.403 219.678  1.00 48.45           C  
ATOM  14337  CG1 VAL C  36     246.946 206.414 219.287  1.00 48.56           C  
ATOM  14338  CG2 VAL C  36     247.767 208.757 219.064  1.00 48.70           C  
ATOM  14339  N   TYR C  37     247.079 205.777 222.372  1.00 49.04           N  
ATOM  14340  CA  TYR C  37     246.986 204.524 223.081  1.00 49.15           C  
ATOM  14341  C   TYR C  37     245.704 203.844 222.695  1.00 49.23           C  
ATOM  14342  O   TYR C  37     244.798 204.479 222.161  1.00 49.41           O  
ATOM  14343  CB  TYR C  37     247.060 204.762 224.580  1.00 49.68           C  
ATOM  14344  CG  TYR C  37     245.962 205.596 225.076  1.00 48.90           C  
ATOM  14345  CD1 TYR C  37     244.795 205.024 225.487  1.00 50.51           C  
ATOM  14346  CD2 TYR C  37     246.123 206.950 225.123  1.00 49.14           C  
ATOM  14347  CE1 TYR C  37     243.784 205.804 225.941  1.00 50.14           C  
ATOM  14348  CE2 TYR C  37     245.115 207.734 225.577  1.00 49.10           C  
ATOM  14349  CZ  TYR C  37     243.946 207.162 225.985  1.00 49.26           C  
ATOM  14350  OH  TYR C  37     242.929 207.936 226.438  1.00 49.32           O  
ATOM  14351  N   TYR C  38     245.624 202.556 222.950  1.00 49.07           N  
ATOM  14352  CA  TYR C  38     244.419 201.829 222.612  1.00 49.12           C  
ATOM  14353  C   TYR C  38     243.334 202.231 223.602  1.00 49.21           C  
ATOM  14354  O   TYR C  38     243.456 201.918 224.783  1.00 49.95           O  
ATOM  14355  CB  TYR C  38     244.666 200.332 222.697  1.00 49.56           C  
ATOM  14356  CG  TYR C  38     245.664 199.818 221.705  1.00 49.17           C  
ATOM  14357  CD1 TYR C  38     246.986 199.902 222.015  1.00 50.04           C  
ATOM  14358  CD2 TYR C  38     245.271 199.242 220.520  1.00 49.36           C  
ATOM  14359  CE1 TYR C  38     247.936 199.430 221.172  1.00 50.17           C  
ATOM  14360  CE2 TYR C  38     246.229 198.754 219.657  1.00 49.20           C  
ATOM  14361  CZ  TYR C  38     247.567 198.853 219.992  1.00 49.26           C  
ATOM  14362  OH  TYR C  38     248.544 198.368 219.163  1.00 49.26           O  
ATOM  14363  N   PRO C  39     242.254 202.889 223.161  1.00 49.50           N  
ATOM  14364  CA  PRO C  39     241.215 203.461 223.996  1.00 49.42           C  
ATOM  14365  C   PRO C  39     240.427 202.399 224.743  1.00 50.14           C  
ATOM  14366  O   PRO C  39     239.782 202.682 225.751  1.00 50.77           O  
ATOM  14367  CB  PRO C  39     240.339 204.194 222.977  1.00 49.16           C  
ATOM  14368  CG  PRO C  39     240.577 203.467 221.673  1.00 49.37           C  
ATOM  14369  CD  PRO C  39     242.014 203.019 221.722  1.00 49.42           C  
ATOM  14370  N   ASP C  40     240.468 201.174 224.242  1.00 50.31           N  
ATOM  14371  CA  ASP C  40     239.742 200.083 224.856  1.00 50.70           C  
ATOM  14372  C   ASP C  40     240.429 198.751 224.598  1.00 51.00           C  
ATOM  14373  O   ASP C  40     241.581 198.700 224.165  1.00 50.78           O  
ATOM  14374  CB  ASP C  40     238.287 200.066 224.381  1.00 50.99           C  
ATOM  14375  CG  ASP C  40     238.114 199.850 222.891  1.00 50.79           C  
ATOM  14376  OD1 ASP C  40     239.014 199.348 222.242  1.00 50.76           O  
ATOM  14377  OD2 ASP C  40     237.058 200.188 222.400  1.00 51.27           O  
ATOM  14378  N   LYS C  41     239.725 197.672 224.904  1.00 51.53           N  
ATOM  14379  CA  LYS C  41     240.258 196.328 224.778  1.00 52.03           C  
ATOM  14380  C   LYS C  41     239.598 195.591 223.629  1.00 53.53           C  
ATOM  14381  O   LYS C  41     239.420 194.368 223.677  1.00 53.61           O  
ATOM  14382  CB  LYS C  41     240.059 195.574 226.084  1.00 53.32           C  
ATOM  14383  CG  LYS C  41     240.822 196.167 227.251  1.00 53.59           C  
ATOM  14384  CD  LYS C  41     240.624 195.347 228.505  1.00 56.29           C  
ATOM  14385  CE  LYS C  41     241.408 195.919 229.669  1.00 57.47           C  
ATOM  14386  NZ  LYS C  41     241.186 195.142 230.918  1.00 59.45           N  
ATOM  14387  N   VAL C  42     239.202 196.335 222.604  1.00 52.03           N  
ATOM  14388  CA  VAL C  42     238.534 195.726 221.477  1.00 50.83           C  
ATOM  14389  C   VAL C  42     239.418 195.590 220.240  1.00 50.28           C  
ATOM  14390  O   VAL C  42     240.018 196.553 219.763  1.00 52.03           O  
ATOM  14391  CB  VAL C  42     237.277 196.532 221.157  1.00 50.77           C  
ATOM  14392  CG1 VAL C  42     236.576 195.980 219.952  1.00 52.52           C  
ATOM  14393  CG2 VAL C  42     236.363 196.492 222.359  1.00 51.37           C  
ATOM  14394  N   PHE C  43     239.480 194.373 219.728  1.00 51.52           N  
ATOM  14395  CA  PHE C  43     240.203 194.033 218.523  1.00 52.26           C  
ATOM  14396  C   PHE C  43     239.454 194.527 217.312  1.00 52.66           C  
ATOM  14397  O   PHE C  43     238.259 194.278 217.148  1.00 53.16           O  
ATOM  14398  CB  PHE C  43     240.391 192.519 218.423  1.00 52.87           C  
ATOM  14399  CG  PHE C  43     240.988 192.046 217.138  1.00 51.76           C  
ATOM  14400  CD1 PHE C  43     242.341 192.006 216.940  1.00 52.22           C  
ATOM  14401  CD2 PHE C  43     240.170 191.636 216.112  1.00 52.51           C  
ATOM  14402  CE1 PHE C  43     242.869 191.561 215.757  1.00 52.08           C  
ATOM  14403  CE2 PHE C  43     240.695 191.197 214.926  1.00 52.41           C  
ATOM  14404  CZ  PHE C  43     242.050 191.159 214.751  1.00 52.03           C  
ATOM  14405  N   ARG C  44     240.161 195.223 216.456  1.00 50.56           N  
ATOM  14406  CA  ARG C  44     239.595 195.745 215.236  1.00 48.92           C  
ATOM  14407  C   ARG C  44     240.612 195.508 214.160  1.00 50.76           C  
ATOM  14408  O   ARG C  44     241.801 195.618 214.425  1.00 48.77           O  
ATOM  14409  CB  ARG C  44     239.310 197.225 215.371  1.00 49.56           C  
ATOM  14410  CG  ARG C  44     238.278 197.592 216.393  1.00 49.72           C  
ATOM  14411  CD  ARG C  44     238.067 199.055 216.438  1.00 48.58           C  
ATOM  14412  NE  ARG C  44     237.063 199.426 217.413  1.00 48.91           N  
ATOM  14413  CZ  ARG C  44     237.309 199.573 218.733  1.00 49.82           C  
ATOM  14414  NH1 ARG C  44     238.519 199.360 219.208  1.00 50.08           N  
ATOM  14415  NH2 ARG C  44     236.339 199.919 219.559  1.00 49.56           N  
ATOM  14416  N   SER C  45     240.193 195.204 212.951  1.00 49.46           N  
ATOM  14417  CA  SER C  45     241.202 194.999 211.933  1.00 47.88           C  
ATOM  14418  C   SER C  45     240.800 195.576 210.604  1.00 48.45           C  
ATOM  14419  O   SER C  45     239.622 195.604 210.246  1.00 48.56           O  
ATOM  14420  CB  SER C  45     241.506 193.526 211.799  1.00 49.84           C  
ATOM  14421  OG  SER C  45     240.379 192.807 211.400  1.00 49.76           O  
ATOM  14422  N   SER C  46     241.803 196.058 209.885  1.00 48.32           N  
ATOM  14423  CA  SER C  46     241.621 196.646 208.558  1.00 47.79           C  
ATOM  14424  C   SER C  46     240.482 197.662 208.570  1.00 47.65           C  
ATOM  14425  O   SER C  46     239.594 197.629 207.716  1.00 47.90           O  
ATOM  14426  CB  SER C  46     241.335 195.566 207.534  1.00 48.66           C  
ATOM  14427  N   VAL C  47     240.488 198.533 209.567  1.00 47.32           N  
ATOM  14428  CA  VAL C  47     239.400 199.481 209.742  1.00 46.99           C  
ATOM  14429  C   VAL C  47     239.861 200.805 210.303  1.00 46.11           C  
ATOM  14430  O   VAL C  47     240.797 200.864 211.100  1.00 46.65           O  
ATOM  14431  CB  VAL C  47     238.316 198.860 210.646  1.00 46.99           C  
ATOM  14432  CG1 VAL C  47     238.873 198.571 211.993  1.00 47.68           C  
ATOM  14433  CG2 VAL C  47     237.104 199.795 210.791  1.00 46.85           C  
ATOM  14434  N   LEU C  48     239.186 201.866 209.896  1.00 46.05           N  
ATOM  14435  CA  LEU C  48     239.446 203.183 210.435  1.00 45.85           C  
ATOM  14436  C   LEU C  48     238.354 203.520 211.439  1.00 45.40           C  
ATOM  14437  O   LEU C  48     237.181 203.625 211.083  1.00 45.45           O  
ATOM  14438  CB  LEU C  48     239.480 204.191 209.300  1.00 45.61           C  
ATOM  14439  CG  LEU C  48     240.372 203.804 208.120  1.00 46.43           C  
ATOM  14440  CD1 LEU C  48     240.282 204.865 207.102  1.00 45.94           C  
ATOM  14441  CD2 LEU C  48     241.785 203.609 208.578  1.00 46.16           C  
ATOM  14442  N   HIS C  49     238.738 203.642 212.700  1.00 45.70           N  
ATOM  14443  CA  HIS C  49     237.783 203.831 213.785  1.00 45.51           C  
ATOM  14444  C   HIS C  49     237.867 205.208 214.418  1.00 45.52           C  
ATOM  14445  O   HIS C  49     238.938 205.650 214.826  1.00 45.29           O  
ATOM  14446  CB  HIS C  49     238.007 202.769 214.857  1.00 45.99           C  
ATOM  14447  CG  HIS C  49     237.109 202.906 216.020  1.00 46.58           C  
ATOM  14448  ND1 HIS C  49     235.762 202.660 215.945  1.00 46.69           N  
ATOM  14449  CD2 HIS C  49     237.359 203.258 217.298  1.00 46.86           C  
ATOM  14450  CE1 HIS C  49     235.216 202.862 217.129  1.00 46.77           C  
ATOM  14451  NE2 HIS C  49     236.163 203.222 217.968  1.00 47.02           N  
ATOM  14452  N   SER C  50     236.738 205.895 214.488  1.00 45.79           N  
ATOM  14453  CA  SER C  50     236.694 207.228 215.079  1.00 45.63           C  
ATOM  14454  C   SER C  50     236.272 207.165 216.535  1.00 45.82           C  
ATOM  14455  O   SER C  50     235.235 206.593 216.863  1.00 46.06           O  
ATOM  14456  CB  SER C  50     235.741 208.120 214.316  1.00 45.80           C  
ATOM  14457  OG  SER C  50     235.595 209.356 214.954  1.00 46.23           O  
ATOM  14458  N   THR C  51     237.079 207.756 217.406  1.00 46.10           N  
ATOM  14459  CA  THR C  51     236.783 207.734 218.834  1.00 46.26           C  
ATOM  14460  C   THR C  51     237.190 209.020 219.540  1.00 46.74           C  
ATOM  14461  O   THR C  51     238.124 209.708 219.121  1.00 47.50           O  
ATOM  14462  CB  THR C  51     237.494 206.550 219.500  1.00 46.63           C  
ATOM  14463  OG1 THR C  51     237.087 206.449 220.865  1.00 46.91           O  
ATOM  14464  CG2 THR C  51     238.995 206.745 219.437  1.00 46.65           C  
ATOM  14465  N   GLN C  52     236.504 209.339 220.631  1.00 46.82           N  
ATOM  14466  CA  GLN C  52     236.880 210.493 221.435  1.00 47.04           C  
ATOM  14467  C   GLN C  52     237.299 210.054 222.820  1.00 47.62           C  
ATOM  14468  O   GLN C  52     236.571 209.332 223.499  1.00 47.94           O  
ATOM  14469  CB  GLN C  52     235.744 211.504 221.537  1.00 47.28           C  
ATOM  14470  CG  GLN C  52     236.122 212.768 222.302  1.00 47.54           C  
ATOM  14471  CD  GLN C  52     235.014 213.768 222.298  1.00 48.15           C  
ATOM  14472  OE1 GLN C  52     233.856 213.402 222.081  1.00 47.05           O  
ATOM  14473  NE2 GLN C  52     235.333 215.035 222.531  1.00 48.83           N  
ATOM  14474  N   ASP C  53     238.483 210.480 223.215  1.00 47.44           N  
ATOM  14475  CA  ASP C  53     239.054 210.122 224.510  1.00 48.49           C  
ATOM  14476  C   ASP C  53     240.124 211.138 224.842  1.00 49.64           C  
ATOM  14477  O   ASP C  53     240.376 212.052 224.065  1.00 48.75           O  
ATOM  14478  CB  ASP C  53     239.627 208.691 224.494  1.00 48.88           C  
ATOM  14479  CG  ASP C  53     239.642 207.970 225.877  1.00 49.52           C  
ATOM  14480  OD1 ASP C  53     239.816 208.622 226.892  1.00 50.15           O  
ATOM  14481  OD2 ASP C  53     239.499 206.774 225.892  1.00 49.50           O  
ATOM  14482  N   LEU C  54     240.769 210.981 225.977  1.00 48.88           N  
ATOM  14483  CA  LEU C  54     241.803 211.928 226.340  1.00 49.41           C  
ATOM  14484  C   LEU C  54     243.142 211.497 225.763  1.00 47.99           C  
ATOM  14485  O   LEU C  54     243.753 210.533 226.216  1.00 50.68           O  
ATOM  14486  CB  LEU C  54     241.895 212.021 227.863  1.00 49.94           C  
ATOM  14487  CG  LEU C  54     240.613 212.375 228.605  1.00 50.37           C  
ATOM  14488  CD1 LEU C  54     240.888 212.321 230.077  1.00 52.50           C  
ATOM  14489  CD2 LEU C  54     240.156 213.757 228.205  1.00 50.33           C  
ATOM  14490  N   PHE C  55     243.591 212.216 224.742  1.00 50.10           N  
ATOM  14491  CA  PHE C  55     244.806 211.897 224.011  1.00 48.88           C  
ATOM  14492  C   PHE C  55     245.713 213.105 223.996  1.00 48.91           C  
ATOM  14493  O   PHE C  55     245.249 214.220 224.193  1.00 48.74           O  
ATOM  14494  CB  PHE C  55     244.543 211.533 222.565  1.00 48.34           C  
ATOM  14495  CG  PHE C  55     243.730 210.317 222.300  1.00 47.98           C  
ATOM  14496  CD1 PHE C  55     242.380 210.413 222.065  1.00 47.61           C  
ATOM  14497  CD2 PHE C  55     244.322 209.084 222.249  1.00 48.84           C  
ATOM  14498  CE1 PHE C  55     241.637 209.298 221.777  1.00 47.28           C  
ATOM  14499  CE2 PHE C  55     243.584 207.958 221.968  1.00 48.55           C  
ATOM  14500  CZ  PHE C  55     242.236 208.069 221.730  1.00 47.57           C  
ATOM  14501  N   LEU C  56     246.993 212.890 223.765  1.00 49.05           N  
ATOM  14502  CA  LEU C  56     247.871 214.041 223.657  1.00 48.13           C  
ATOM  14503  C   LEU C  56     247.672 214.676 222.284  1.00 48.35           C  
ATOM  14504  O   LEU C  56     247.853 213.982 221.276  1.00 49.13           O  
ATOM  14505  CB  LEU C  56     249.314 213.602 223.790  1.00 48.80           C  
ATOM  14506  CG  LEU C  56     250.360 214.680 223.854  1.00 48.47           C  
ATOM  14507  CD1 LEU C  56     250.213 215.457 225.154  1.00 49.39           C  
ATOM  14508  CD2 LEU C  56     251.701 214.036 223.760  1.00 48.63           C  
ATOM  14509  N   PRO C  57     247.284 215.948 222.158  1.00 47.94           N  
ATOM  14510  CA  PRO C  57     247.058 216.621 220.903  1.00 47.30           C  
ATOM  14511  C   PRO C  57     248.320 216.576 220.062  1.00 46.79           C  
ATOM  14512  O   PRO C  57     249.429 216.767 220.588  1.00 48.37           O  
ATOM  14513  CB  PRO C  57     246.736 218.052 221.329  1.00 47.40           C  
ATOM  14514  CG  PRO C  57     246.242 217.921 222.746  1.00 47.91           C  
ATOM  14515  CD  PRO C  57     247.035 216.782 223.341  1.00 48.54           C  
ATOM  14516  N   PHE C  58     248.176 216.358 218.768  1.00 47.27           N  
ATOM  14517  CA  PHE C  58     249.336 216.272 217.915  1.00 46.62           C  
ATOM  14518  C   PHE C  58     250.025 217.609 217.767  1.00 47.60           C  
ATOM  14519  O   PHE C  58     249.390 218.658 217.696  1.00 47.22           O  
ATOM  14520  CB  PHE C  58     248.991 215.707 216.545  1.00 47.56           C  
ATOM  14521  CG  PHE C  58     248.792 214.212 216.494  1.00 47.40           C  
ATOM  14522  CD1 PHE C  58     248.894 213.403 217.621  1.00 48.68           C  
ATOM  14523  CD2 PHE C  58     248.534 213.603 215.281  1.00 47.11           C  
ATOM  14524  CE1 PHE C  58     248.742 212.050 217.517  1.00 47.80           C  
ATOM  14525  CE2 PHE C  58     248.378 212.244 215.189  1.00 46.56           C  
ATOM  14526  CZ  PHE C  58     248.487 211.472 216.308  1.00 47.31           C  
ATOM  14527  N   PHE C  59     251.346 217.534 217.751  1.00 48.13           N  
ATOM  14528  CA  PHE C  59     252.252 218.663 217.609  1.00 48.23           C  
ATOM  14529  C   PHE C  59     252.137 219.680 218.725  1.00 47.73           C  
ATOM  14530  O   PHE C  59     252.615 220.811 218.586  1.00 47.68           O  
ATOM  14531  CB  PHE C  59     252.057 219.306 216.244  1.00 47.41           C  
ATOM  14532  CG  PHE C  59     252.373 218.347 215.148  1.00 47.59           C  
ATOM  14533  CD1 PHE C  59     251.378 217.674 214.490  1.00 47.27           C  
ATOM  14534  CD2 PHE C  59     253.679 218.109 214.786  1.00 48.26           C  
ATOM  14535  CE1 PHE C  59     251.671 216.773 213.495  1.00 47.64           C  
ATOM  14536  CE2 PHE C  59     253.981 217.214 213.790  1.00 48.74           C  
ATOM  14537  CZ  PHE C  59     252.973 216.541 213.146  1.00 48.51           C  
ATOM  14538  N   SER C  60     251.574 219.286 219.868  1.00 47.53           N  
ATOM  14539  CA  SER C  60     251.528 220.138 221.039  1.00 48.13           C  
ATOM  14540  C   SER C  60     252.892 220.196 221.734  1.00 49.15           C  
ATOM  14541  O   SER C  60     253.773 219.372 221.445  1.00 49.33           O  
ATOM  14542  CB  SER C  60     250.465 219.662 222.011  1.00 48.06           C  
ATOM  14543  OG  SER C  60     250.796 218.416 222.553  1.00 48.15           O  
ATOM  14544  N   ASN C  61     253.057 221.180 222.645  1.00 50.08           N  
ATOM  14545  CA  ASN C  61     254.266 221.353 223.455  1.00 50.29           C  
ATOM  14546  C   ASN C  61     254.209 220.482 224.714  1.00 50.82           C  
ATOM  14547  O   ASN C  61     253.205 220.474 225.428  1.00 50.75           O  
ATOM  14548  CB  ASN C  61     254.457 222.820 223.860  1.00 51.18           C  
ATOM  14549  CG  ASN C  61     254.508 223.802 222.684  1.00 51.68           C  
ATOM  14550  OD1 ASN C  61     254.960 223.455 221.581  1.00 51.70           O  
ATOM  14551  ND2 ASN C  61     254.045 225.021 222.931  1.00 52.32           N  
ATOM  14552  N   VAL C  62     255.322 219.794 225.008  1.00 50.29           N  
ATOM  14553  CA  VAL C  62     255.493 219.012 226.235  1.00 50.74           C  
ATOM  14554  C   VAL C  62     256.658 219.595 226.999  1.00 51.93           C  
ATOM  14555  O   VAL C  62     257.667 219.981 226.404  1.00 50.22           O  
ATOM  14556  CB  VAL C  62     255.705 217.516 225.933  1.00 50.86           C  
ATOM  14557  CG1 VAL C  62     254.470 216.979 225.261  1.00 50.60           C  
ATOM  14558  CG2 VAL C  62     256.924 217.311 225.046  1.00 50.61           C  
ATOM  14559  N   THR C  63     256.518 219.705 228.308  1.00 51.05           N  
ATOM  14560  CA  THR C  63     257.579 220.313 229.081  1.00 49.88           C  
ATOM  14561  C   THR C  63     258.730 219.339 229.197  1.00 53.20           C  
ATOM  14562  O   THR C  63     258.542 218.168 229.529  1.00 50.53           O  
ATOM  14563  CB  THR C  63     257.080 220.751 230.461  1.00 51.10           C  
ATOM  14564  OG1 THR C  63     255.980 221.654 230.302  1.00 51.68           O  
ATOM  14565  CG2 THR C  63     258.194 221.465 231.205  1.00 52.35           C  
ATOM  14566  N   TRP C  64     259.921 219.820 228.879  1.00 51.70           N  
ATOM  14567  CA  TRP C  64     261.120 219.008 228.845  1.00 53.57           C  
ATOM  14568  C   TRP C  64     261.992 219.182 230.077  1.00 53.30           C  
ATOM  14569  O   TRP C  64     262.478 220.276 230.361  1.00 49.44           O  
ATOM  14570  CB  TRP C  64     261.890 219.341 227.580  1.00 52.95           C  
ATOM  14571  CG  TRP C  64     263.163 218.630 227.389  1.00 51.75           C  
ATOM  14572  CD1 TRP C  64     263.590 217.477 227.966  1.00 53.03           C  
ATOM  14573  CD2 TRP C  64     264.206 219.035 226.499  1.00 51.72           C  
ATOM  14574  NE1 TRP C  64     264.815 217.147 227.487  1.00 54.09           N  
ATOM  14575  CE2 TRP C  64     265.204 218.082 226.585  1.00 52.47           C  
ATOM  14576  CE3 TRP C  64     264.365 220.118 225.631  1.00 52.20           C  
ATOM  14577  CZ2 TRP C  64     266.351 218.164 225.833  1.00 53.45           C  
ATOM  14578  CZ3 TRP C  64     265.519 220.202 224.877  1.00 53.39           C  
ATOM  14579  CH2 TRP C  64     266.485 219.249 224.973  1.00 53.84           C  
ATOM  14580  N   PHE C  65     262.173 218.098 230.819  1.00 53.13           N  
ATOM  14581  CA  PHE C  65     262.940 218.126 232.052  1.00 52.17           C  
ATOM  14582  C   PHE C  65     264.230 217.324 231.900  1.00 53.69           C  
ATOM  14583  O   PHE C  65     264.238 216.283 231.236  1.00 54.44           O  
ATOM  14584  CB  PHE C  65     262.114 217.515 233.169  1.00 53.01           C  
ATOM  14585  CG  PHE C  65     260.849 218.224 233.427  1.00 52.98           C  
ATOM  14586  CD1 PHE C  65     259.693 217.813 232.805  1.00 54.56           C  
ATOM  14587  CD2 PHE C  65     260.794 219.290 234.285  1.00 52.94           C  
ATOM  14588  CE1 PHE C  65     258.510 218.450 233.041  1.00 54.30           C  
ATOM  14589  CE2 PHE C  65     259.607 219.934 234.523  1.00 54.12           C  
ATOM  14590  CZ  PHE C  65     258.464 219.510 233.902  1.00 53.15           C  
ATOM  14591  N   HIS C  66     265.302 217.770 232.573  1.00 52.01           N  
ATOM  14592  CA  HIS C  66     266.599 217.086 232.588  1.00 52.90           C  
ATOM  14593  C   HIS C  66     266.798 216.372 233.923  1.00 53.51           C  
ATOM  14594  O   HIS C  66     266.749 216.990 234.989  1.00 54.72           O  
ATOM  14595  CB  HIS C  66     267.755 218.083 232.329  1.00 53.75           C  
ATOM  14596  CG  HIS C  66     267.740 218.708 230.939  1.00 53.86           C  
ATOM  14597  ND1 HIS C  66     268.366 218.125 229.859  1.00 54.12           N  
ATOM  14598  CD2 HIS C  66     267.167 219.851 230.472  1.00 53.84           C  
ATOM  14599  CE1 HIS C  66     268.185 218.886 228.789  1.00 54.54           C  
ATOM  14600  NE2 HIS C  66     267.461 219.939 229.137  1.00 53.92           N  
ATOM  14601  N   ASN C  81     263.104 217.131 240.742  1.00 61.18           N  
ATOM  14602  CA  ASN C  81     261.796 216.605 241.113  1.00 61.15           C  
ATOM  14603  C   ASN C  81     260.785 217.749 241.406  1.00 61.00           C  
ATOM  14604  O   ASN C  81     260.505 218.031 242.577  1.00 61.58           O  
ATOM  14605  CB  ASN C  81     261.923 215.625 242.305  1.00 62.31           C  
ATOM  14606  N   PRO C  82     260.247 218.459 240.369  1.00 59.92           N  
ATOM  14607  CA  PRO C  82     259.185 219.454 240.478  1.00 59.58           C  
ATOM  14608  C   PRO C  82     257.832 218.786 240.668  1.00 59.04           C  
ATOM  14609  O   PRO C  82     257.627 217.669 240.196  1.00 59.70           O  
ATOM  14610  CB  PRO C  82     259.268 220.180 239.134  1.00 59.06           C  
ATOM  14611  CG  PRO C  82     259.783 219.137 238.164  1.00 58.61           C  
ATOM  14612  CD  PRO C  82     260.744 218.286 238.963  1.00 58.95           C  
ATOM  14613  N   VAL C  83     256.895 219.485 241.289  1.00 59.16           N  
ATOM  14614  CA  VAL C  83     255.532 218.977 241.356  1.00 58.63           C  
ATOM  14615  C   VAL C  83     254.740 219.574 240.217  1.00 58.50           C  
ATOM  14616  O   VAL C  83     254.744 220.788 240.018  1.00 59.30           O  
ATOM  14617  CB  VAL C  83     254.861 219.305 242.699  1.00 59.61           C  
ATOM  14618  CG1 VAL C  83     253.408 218.807 242.698  1.00 58.83           C  
ATOM  14619  CG2 VAL C  83     255.642 218.643 243.821  1.00 61.50           C  
ATOM  14620  N   LEU C  84     254.099 218.718 239.447  1.00 58.72           N  
ATOM  14621  CA  LEU C  84     253.374 219.150 238.276  1.00 57.46           C  
ATOM  14622  C   LEU C  84     251.882 218.885 238.470  1.00 58.95           C  
ATOM  14623  O   LEU C  84     251.518 217.984 239.223  1.00 57.80           O  
ATOM  14624  CB  LEU C  84     253.923 218.381 237.077  1.00 58.12           C  
ATOM  14625  CG  LEU C  84     255.465 218.465 236.899  1.00 57.79           C  
ATOM  14626  CD1 LEU C  84     255.880 217.550 235.789  1.00 57.68           C  
ATOM  14627  CD2 LEU C  84     255.892 219.893 236.600  1.00 58.62           C  
ATOM  14628  N   PRO C  85     250.995 219.656 237.839  1.00 57.35           N  
ATOM  14629  CA  PRO C  85     249.568 219.416 237.777  1.00 57.26           C  
ATOM  14630  C   PRO C  85     249.283 218.101 237.082  1.00 57.05           C  
ATOM  14631  O   PRO C  85     250.038 217.693 236.206  1.00 56.64           O  
ATOM  14632  CB  PRO C  85     249.060 220.588 236.931  1.00 57.12           C  
ATOM  14633  CG  PRO C  85     250.116 221.655 237.065  1.00 57.51           C  
ATOM  14634  CD  PRO C  85     251.426 220.906 237.207  1.00 57.76           C  
ATOM  14635  N   PHE C  86     248.190 217.453 237.448  1.00 56.03           N  
ATOM  14636  CA  PHE C  86     247.754 216.236 236.769  1.00 57.13           C  
ATOM  14637  C   PHE C  86     246.703 216.560 235.713  1.00 57.35           C  
ATOM  14638  O   PHE C  86     246.582 215.867 234.701  1.00 54.99           O  
ATOM  14639  CB  PHE C  86     247.190 215.246 237.776  1.00 57.10           C  
ATOM  14640  CG  PHE C  86     246.861 213.893 237.234  1.00 57.22           C  
ATOM  14641  CD1 PHE C  86     247.858 212.968 236.971  1.00 56.33           C  
ATOM  14642  CD2 PHE C  86     245.548 213.531 237.010  1.00 56.88           C  
ATOM  14643  CE1 PHE C  86     247.540 211.714 236.497  1.00 55.81           C  
ATOM  14644  CE2 PHE C  86     245.233 212.280 236.541  1.00 55.96           C  
ATOM  14645  CZ  PHE C  86     246.231 211.372 236.285  1.00 56.59           C  
ATOM  14646  N   ASN C  87     245.930 217.611 235.966  1.00 55.57           N  
ATOM  14647  CA  ASN C  87     244.839 218.034 235.098  1.00 55.70           C  
ATOM  14648  C   ASN C  87     243.863 216.898 234.802  1.00 55.54           C  
ATOM  14649  O   ASN C  87     243.294 216.317 235.726  1.00 55.52           O  
ATOM  14650  CB  ASN C  87     245.387 218.655 233.825  1.00 54.99           C  
ATOM  14651  CG  ASN C  87     246.191 219.903 234.098  1.00 56.11           C  
ATOM  14652  OD1 ASN C  87     245.999 220.562 235.129  1.00 56.77           O  
ATOM  14653  ND2 ASN C  87     247.072 220.250 233.197  1.00 55.67           N  
ATOM  14654  N   ASP C  88     243.657 216.585 233.520  1.00 54.82           N  
ATOM  14655  CA  ASP C  88     242.707 215.547 233.127  1.00 54.51           C  
ATOM  14656  C   ASP C  88     243.400 214.233 232.826  1.00 54.10           C  
ATOM  14657  O   ASP C  88     242.774 213.273 232.380  1.00 53.64           O  
ATOM  14658  CB  ASP C  88     241.914 215.985 231.890  1.00 54.17           C  
ATOM  14659  N   GLY C  89     244.698 214.189 233.052  1.00 53.83           N  
ATOM  14660  CA  GLY C  89     245.484 213.019 232.730  1.00 53.84           C  
ATOM  14661  C   GLY C  89     246.822 213.455 232.175  1.00 51.91           C  
ATOM  14662  O   GLY C  89     246.963 214.553 231.626  1.00 53.82           O  
ATOM  14663  N   VAL C  90     247.807 212.595 232.319  1.00 53.09           N  
ATOM  14664  CA  VAL C  90     249.160 212.941 231.950  1.00 51.72           C  
ATOM  14665  C   VAL C  90     249.825 212.039 230.943  1.00 50.55           C  
ATOM  14666  O   VAL C  90     249.838 210.815 231.081  1.00 52.53           O  
ATOM  14667  CB  VAL C  90     250.013 212.966 233.222  1.00 53.00           C  
ATOM  14668  CG1 VAL C  90     251.463 213.233 232.891  1.00 53.04           C  
ATOM  14669  CG2 VAL C  90     249.476 214.037 234.130  1.00 54.22           C  
ATOM  14670  N   TYR C  91     250.428 212.655 229.944  1.00 50.57           N  
ATOM  14671  CA  TYR C  91     251.273 211.915 229.035  1.00 50.03           C  
ATOM  14672  C   TYR C  91     252.681 212.027 229.549  1.00 51.02           C  
ATOM  14673  O   TYR C  91     253.215 213.129 229.680  1.00 52.70           O  
ATOM  14674  CB  TYR C  91     251.219 212.441 227.617  1.00 49.54           C  
ATOM  14675  CG  TYR C  91     252.270 211.792 226.749  1.00 49.85           C  
ATOM  14676  CD1 TYR C  91     252.083 210.525 226.256  1.00 49.79           C  
ATOM  14677  CD2 TYR C  91     253.438 212.475 226.463  1.00 49.89           C  
ATOM  14678  CE1 TYR C  91     253.047 209.939 225.471  1.00 50.30           C  
ATOM  14679  CE2 TYR C  91     254.398 211.894 225.677  1.00 49.49           C  
ATOM  14680  CZ  TYR C  91     254.203 210.632 225.181  1.00 50.02           C  
ATOM  14681  OH  TYR C  91     255.156 210.049 224.392  1.00 50.31           O  
ATOM  14682  N   PHE C  92     253.295 210.914 229.847  1.00 48.80           N  
ATOM  14683  CA  PHE C  92     254.637 210.948 230.379  1.00 49.84           C  
ATOM  14684  C   PHE C  92     255.554 210.166 229.482  1.00 53.79           C  
ATOM  14685  O   PHE C  92     255.225 209.063 229.061  1.00 46.31           O  
ATOM  14686  CB  PHE C  92     254.670 210.353 231.780  1.00 50.71           C  
ATOM  14687  CG  PHE C  92     256.025 210.352 232.419  1.00 51.03           C  
ATOM  14688  CD1 PHE C  92     256.410 211.397 233.205  1.00 52.40           C  
ATOM  14689  CD2 PHE C  92     256.914 209.316 232.226  1.00 52.04           C  
ATOM  14690  CE1 PHE C  92     257.641 211.421 233.793  1.00 52.52           C  
ATOM  14691  CE2 PHE C  92     258.158 209.332 232.814  1.00 52.68           C  
ATOM  14692  CZ  PHE C  92     258.519 210.387 233.600  1.00 53.14           C  
ATOM  14693  N   ALA C  93     256.716 210.692 229.193  1.00 50.80           N  
ATOM  14694  CA  ALA C  93     257.652 209.905 228.420  1.00 50.78           C  
ATOM  14695  C   ALA C  93     259.031 210.116 228.937  1.00 51.66           C  
ATOM  14696  O   ALA C  93     259.389 211.214 229.351  1.00 51.22           O  
ATOM  14697  CB  ALA C  93     257.581 210.249 226.947  1.00 51.03           C  
ATOM  14698  N   SER C  94     259.835 209.086 228.882  1.00 51.61           N  
ATOM  14699  CA  SER C  94     261.189 209.238 229.348  1.00 51.52           C  
ATOM  14700  C   SER C  94     262.176 208.471 228.527  1.00 53.87           C  
ATOM  14701  O   SER C  94     261.850 207.460 227.904  1.00 54.96           O  
ATOM  14702  CB  SER C  94     261.285 208.784 230.776  1.00 53.09           C  
ATOM  14703  OG  SER C  94     261.016 207.412 230.885  1.00 53.67           O  
ATOM  14704  N   THR C  95     263.406 208.930 228.557  1.00 54.92           N  
ATOM  14705  CA  THR C  95     264.461 208.229 227.873  1.00 54.43           C  
ATOM  14706  C   THR C  95     265.511 207.820 228.875  1.00 55.77           C  
ATOM  14707  O   THR C  95     265.756 208.525 229.854  1.00 55.53           O  
ATOM  14708  CB  THR C  95     265.047 209.100 226.770  1.00 55.71           C  
ATOM  14709  OG1 THR C  95     265.530 210.319 227.338  1.00 55.18           O  
ATOM  14710  CG2 THR C  95     263.989 209.406 225.743  1.00 55.42           C  
ATOM  14711  N   GLU C  96     266.131 206.677 228.628  1.00 56.54           N  
ATOM  14712  CA  GLU C  96     267.071 206.122 229.581  1.00 57.54           C  
ATOM  14713  C   GLU C  96     268.377 205.613 229.005  1.00 58.37           C  
ATOM  14714  O   GLU C  96     268.470 205.190 227.842  1.00 57.08           O  
ATOM  14715  CB  GLU C  96     266.415 204.966 230.335  1.00 58.84           C  
ATOM  14716  CG  GLU C  96     265.308 205.354 231.289  1.00 58.78           C  
ATOM  14717  CD  GLU C  96     265.830 206.031 232.519  1.00 60.12           C  
ATOM  14718  OE1 GLU C  96     267.036 206.098 232.674  1.00 60.18           O  
ATOM  14719  OE2 GLU C  96     265.030 206.453 233.320  1.00 58.89           O  
ATOM  14720  N   LYS C  97     269.382 205.650 229.875  1.00 59.01           N  
ATOM  14721  CA  LYS C  97     270.682 205.038 229.671  1.00 59.52           C  
ATOM  14722  C   LYS C  97     271.028 204.191 230.885  1.00 60.33           C  
ATOM  14723  O   LYS C  97     271.735 203.190 230.779  1.00 60.88           O  
ATOM  14724  CB  LYS C  97     271.766 206.092 229.446  1.00 59.93           C  
ATOM  14725  N   SER C  98     270.567 204.637 232.059  1.00 60.70           N  
ATOM  14726  CA  SER C  98     270.959 204.012 233.317  1.00 61.21           C  
ATOM  14727  C   SER C  98     269.816 203.822 234.314  1.00 61.28           C  
ATOM  14728  O   SER C  98     270.054 203.742 235.518  1.00 61.21           O  
ATOM  14729  CB  SER C  98     272.064 204.820 233.965  1.00 61.35           C  
ATOM  14730  OG  SER C  98     271.651 206.130 234.198  1.00 61.30           O  
ATOM  14731  N   ASN C  99     268.582 203.733 233.825  1.00 60.66           N  
ATOM  14732  CA  ASN C  99     267.428 203.512 234.699  1.00 61.51           C  
ATOM  14733  C   ASN C  99     267.344 204.535 235.835  1.00 61.53           C  
ATOM  14734  O   ASN C  99     267.199 204.161 237.001  1.00 61.96           O  
ATOM  14735  CB  ASN C  99     267.465 202.099 235.264  1.00 61.47           C  
ATOM  14736  CG  ASN C  99     266.148 201.656 235.841  1.00 61.92           C  
ATOM  14737  OD1 ASN C  99     265.079 202.052 235.363  1.00 61.69           O  
ATOM  14738  ND2 ASN C  99     266.204 200.834 236.862  1.00 62.94           N  
ATOM  14739  N   ILE C 100     267.455 205.817 235.491  1.00 61.36           N  
ATOM  14740  CA  ILE C 100     267.402 206.899 236.473  1.00 61.39           C  
ATOM  14741  C   ILE C 100     266.009 207.105 237.059  1.00 60.01           C  
ATOM  14742  O   ILE C 100     265.871 207.343 238.260  1.00 60.78           O  
ATOM  14743  CB  ILE C 100     267.893 208.227 235.869  1.00 61.18           C  
ATOM  14744  CG1 ILE C 100     269.384 208.109 235.538  1.00 61.66           C  
ATOM  14745  CG2 ILE C 100     267.643 209.375 236.861  1.00 59.94           C  
ATOM  14746  CD1 ILE C 100     269.932 209.233 234.677  1.00 61.76           C  
ATOM  14747  N   ILE C 101     264.984 207.076 236.214  1.00 59.45           N  
ATOM  14748  CA  ILE C 101     263.619 207.277 236.693  1.00 60.25           C  
ATOM  14749  C   ILE C 101     263.087 205.984 237.282  1.00 61.18           C  
ATOM  14750  O   ILE C 101     263.135 204.933 236.644  1.00 60.13           O  
ATOM  14751  CB  ILE C 101     262.714 207.802 235.570  1.00 60.04           C  
ATOM  14752  CG1 ILE C 101     263.243 209.172 235.146  1.00 59.58           C  
ATOM  14753  CG2 ILE C 101     261.245 207.896 236.059  1.00 58.60           C  
ATOM  14754  CD1 ILE C 101     262.723 209.665 233.864  1.00 56.18           C  
ATOM  14755  N   ARG C 102     262.598 206.061 238.515  1.00 61.04           N  
ATOM  14756  CA  ARG C 102     262.152 204.872 239.221  1.00 60.97           C  
ATOM  14757  C   ARG C 102     260.646 204.831 239.420  1.00 61.27           C  
ATOM  14758  O   ARG C 102     260.061 203.752 239.500  1.00 63.50           O  
ATOM  14759  CB  ARG C 102     262.824 204.801 240.578  1.00 62.19           C  
ATOM  14760  CG  ARG C 102     264.352 204.864 240.540  1.00 62.07           C  
ATOM  14761  CD  ARG C 102     264.983 203.645 239.980  1.00 62.23           C  
ATOM  14762  NE  ARG C 102     266.424 203.822 239.823  1.00 61.79           N  
ATOM  14763  CZ  ARG C 102     267.345 203.736 240.810  1.00 62.49           C  
ATOM  14764  NH1 ARG C 102     266.987 203.479 242.053  1.00 63.18           N  
ATOM  14765  NH2 ARG C 102     268.622 203.916 240.526  1.00 62.41           N  
ATOM  14766  N   GLY C 103     260.002 205.986 239.530  1.00 59.51           N  
ATOM  14767  CA  GLY C 103     258.580 205.937 239.840  1.00 58.22           C  
ATOM  14768  C   GLY C 103     257.877 207.277 239.878  1.00 57.60           C  
ATOM  14769  O   GLY C 103     258.423 208.296 239.462  1.00 58.03           O  
ATOM  14770  N   TRP C 104     256.628 207.241 240.329  1.00 57.41           N  
ATOM  14771  CA  TRP C 104     255.764 208.413 240.382  1.00 58.79           C  
ATOM  14772  C   TRP C 104     254.926 208.480 241.649  1.00 61.62           C  
ATOM  14773  O   TRP C 104     254.570 207.457 242.236  1.00 61.66           O  
ATOM  14774  CB  TRP C 104     254.787 208.418 239.214  1.00 57.22           C  
ATOM  14775  CG  TRP C 104     255.407 208.391 237.888  1.00 55.90           C  
ATOM  14776  CD1 TRP C 104     255.730 209.454 237.116  1.00 55.79           C  
ATOM  14777  CD2 TRP C 104     255.773 207.226 237.140  1.00 55.34           C  
ATOM  14778  NE1 TRP C 104     256.286 209.030 235.950  1.00 54.38           N  
ATOM  14779  CE2 TRP C 104     256.318 207.666 235.947  1.00 54.74           C  
ATOM  14780  CE3 TRP C 104     255.683 205.861 237.385  1.00 55.94           C  
ATOM  14781  CZ2 TRP C 104     256.783 206.788 234.990  1.00 53.08           C  
ATOM  14782  CZ3 TRP C 104     256.148 204.983 236.427  1.00 55.21           C  
ATOM  14783  CH2 TRP C 104     256.684 205.437 235.262  1.00 53.18           C  
ATOM  14784  N   ILE C 105     254.554 209.690 242.029  1.00 59.81           N  
ATOM  14785  CA  ILE C 105     253.588 209.888 243.097  1.00 60.09           C  
ATOM  14786  C   ILE C 105     252.392 210.646 242.570  1.00 61.26           C  
ATOM  14787  O   ILE C 105     252.553 211.715 241.991  1.00 53.11           O  
ATOM  14788  CB  ILE C 105     254.162 210.688 244.267  1.00 62.38           C  
ATOM  14789  CG1 ILE C 105     255.351 209.984 244.846  1.00 62.29           C  
ATOM  14790  CG2 ILE C 105     253.072 210.874 245.328  1.00 62.35           C  
ATOM  14791  CD1 ILE C 105     256.148 210.823 245.818  1.00 63.34           C  
ATOM  14792  N   PHE C 106     251.197 210.123 242.789  1.00 60.10           N  
ATOM  14793  CA  PHE C 106     249.993 210.819 242.348  1.00 60.34           C  
ATOM  14794  C   PHE C 106     249.056 211.060 243.519  1.00 62.52           C  
ATOM  14795  O   PHE C 106     248.826 210.168 244.329  1.00 64.62           O  
ATOM  14796  CB  PHE C 106     249.253 209.999 241.297  1.00 60.33           C  
ATOM  14797  CG  PHE C 106     250.016 209.721 240.059  1.00 59.24           C  
ATOM  14798  CD1 PHE C 106     250.801 208.592 239.960  1.00 58.59           C  
ATOM  14799  CD2 PHE C 106     249.947 210.573 238.985  1.00 58.69           C  
ATOM  14800  CE1 PHE C 106     251.502 208.328 238.812  1.00 57.36           C  
ATOM  14801  CE2 PHE C 106     250.659 210.316 237.832  1.00 58.05           C  
ATOM  14802  CZ  PHE C 106     251.437 209.189 237.751  1.00 56.30           C  
ATOM  14803  N   GLY C 107     248.461 212.236 243.593  1.00 62.05           N  
ATOM  14804  CA  GLY C 107     247.524 212.517 244.680  1.00 62.24           C  
ATOM  14805  C   GLY C 107     247.100 213.976 244.689  1.00 62.49           C  
ATOM  14806  O   GLY C 107     247.055 214.624 243.643  1.00 58.64           O  
ATOM  14807  N   THR C 108     246.780 214.489 245.869  1.00 64.31           N  
ATOM  14808  CA  THR C 108     246.356 215.873 246.022  1.00 64.86           C  
ATOM  14809  C   THR C 108     247.391 216.634 246.838  1.00 65.15           C  
ATOM  14810  O   THR C 108     248.179 217.410 246.294  1.00 64.84           O  
ATOM  14811  CB  THR C 108     244.988 215.967 246.706  1.00 64.95           C  
ATOM  14812  OG1 THR C 108     245.048 215.321 247.978  1.00 65.05           O  
ATOM  14813  CG2 THR C 108     243.953 215.279 245.853  1.00 63.24           C  
ATOM  14814  N   THR C 109     247.384 216.406 248.149  1.00 65.80           N  
ATOM  14815  CA  THR C 109     248.302 217.094 249.046  1.00 65.75           C  
ATOM  14816  C   THR C 109     249.679 216.430 249.150  1.00 66.14           C  
ATOM  14817  O   THR C 109     250.664 217.101 249.454  1.00 66.18           O  
ATOM  14818  CB  THR C 109     247.685 217.188 250.447  1.00 65.55           C  
ATOM  14819  OG1 THR C 109     247.423 215.867 250.931  1.00 66.51           O  
ATOM  14820  CG2 THR C 109     246.384 217.968 250.395  1.00 66.25           C  
ATOM  14821  N   LEU C 110     249.758 215.119 248.903  1.00 65.83           N  
ATOM  14822  CA  LEU C 110     251.033 214.391 248.940  1.00 66.29           C  
ATOM  14823  C   LEU C 110     251.844 214.685 250.216  1.00 67.15           C  
ATOM  14824  O   LEU C 110     253.059 214.874 250.150  1.00 66.25           O  
ATOM  14825  CB  LEU C 110     251.893 214.763 247.707  1.00 65.83           C  
ATOM  14826  N   ASP C 111     251.174 214.748 251.369  1.00 67.68           N  
ATOM  14827  CA  ASP C 111     251.836 215.095 252.631  1.00 67.92           C  
ATOM  14828  C   ASP C 111     251.158 214.451 253.841  1.00 68.71           C  
ATOM  14829  O   ASP C 111     250.756 215.144 254.772  1.00 69.73           O  
ATOM  14830  CB  ASP C 111     251.850 216.625 252.794  1.00 67.84           C  
ATOM  14831  CG  ASP C 111     252.756 217.156 253.921  1.00 68.29           C  
ATOM  14832  OD1 ASP C 111     253.692 216.485 254.288  1.00 68.42           O  
ATOM  14833  OD2 ASP C 111     252.504 218.247 254.390  1.00 68.14           O  
ATOM  14834  N   SER C 112     250.961 213.134 253.793  1.00 68.27           N  
ATOM  14835  CA  SER C 112     250.319 212.383 254.875  1.00 68.83           C  
ATOM  14836  C   SER C 112     249.031 213.017 255.385  1.00 69.24           C  
ATOM  14837  O   SER C 112     248.752 212.978 256.585  1.00 68.95           O  
ATOM  14838  CB  SER C 112     251.269 212.240 256.036  1.00 68.55           C  
ATOM  14839  N   LYS C 113     248.233 213.575 254.485  1.00 68.33           N  
ATOM  14840  CA  LYS C 113     246.972 214.190 254.875  1.00 68.93           C  
ATOM  14841  C   LYS C 113     245.814 213.370 254.346  1.00 69.36           C  
ATOM  14842  O   LYS C 113     244.735 213.326 254.937  1.00 70.72           O  
ATOM  14843  CB  LYS C 113     246.895 215.626 254.354  1.00 69.94           C  
ATOM  14844  CG  LYS C 113     245.898 216.530 255.083  1.00 68.99           C  
ATOM  14845  CD  LYS C 113     244.555 216.621 254.361  1.00 69.73           C  
ATOM  14846  CE  LYS C 113     243.650 217.646 255.033  1.00 71.10           C  
ATOM  14847  NZ  LYS C 113     242.302 217.703 254.403  1.00 72.54           N  
ATOM  14848  N   THR C 114     246.043 212.742 253.202  1.00 69.03           N  
ATOM  14849  CA  THR C 114     245.041 211.932 252.538  1.00 69.47           C  
ATOM  14850  C   THR C 114     245.725 210.857 251.713  1.00 70.57           C  
ATOM  14851  O   THR C 114     246.937 210.664 251.819  1.00 69.46           O  
ATOM  14852  CB  THR C 114     244.103 212.791 251.673  1.00 69.00           C  
ATOM  14853  OG1 THR C 114     243.003 211.983 251.228  1.00 68.44           O  
ATOM  14854  CG2 THR C 114     244.839 213.368 250.482  1.00 68.89           C  
ATOM  14855  N   GLN C 115     244.949 210.149 250.908  1.00 68.57           N  
ATOM  14856  CA  GLN C 115     245.458 209.020 250.144  1.00 68.71           C  
ATOM  14857  C   GLN C 115     246.187 209.452 248.882  1.00 67.30           C  
ATOM  14858  O   GLN C 115     245.797 210.411 248.219  1.00 66.69           O  
ATOM  14859  CB  GLN C 115     244.309 208.094 249.778  1.00 68.90           C  
ATOM  14860  N   SER C 116     247.219 208.704 248.524  1.00 67.14           N  
ATOM  14861  CA  SER C 116     247.965 208.948 247.301  1.00 65.07           C  
ATOM  14862  C   SER C 116     248.542 207.649 246.767  1.00 66.86           C  
ATOM  14863  O   SER C 116     248.689 206.677 247.501  1.00 67.80           O  
ATOM  14864  CB  SER C 116     249.080 209.946 247.558  1.00 65.37           C  
ATOM  14865  OG  SER C 116     250.031 209.421 248.435  1.00 66.46           O  
ATOM  14866  N   LEU C 117     248.895 207.648 245.494  1.00 64.26           N  
ATOM  14867  CA  LEU C 117     249.474 206.491 244.832  1.00 63.09           C  
ATOM  14868  C   LEU C 117     250.970 206.587 244.725  1.00 64.55           C  
ATOM  14869  O   LEU C 117     251.506 207.561 244.202  1.00 63.30           O  
ATOM  14870  CB  LEU C 117     248.950 206.371 243.403  1.00 63.44           C  
ATOM  14871  CG  LEU C 117     247.678 205.620 243.177  1.00 63.81           C  
ATOM  14872  CD1 LEU C 117     246.519 206.316 243.892  1.00 64.19           C  
ATOM  14873  CD2 LEU C 117     247.443 205.539 241.679  1.00 61.31           C  
ATOM  14874  N   LEU C 118     251.648 205.560 245.182  1.00 64.32           N  
ATOM  14875  CA  LEU C 118     253.086 205.488 245.053  1.00 64.51           C  
ATOM  14876  C   LEU C 118     253.452 204.315 244.167  1.00 64.76           C  
ATOM  14877  O   LEU C 118     253.212 203.159 244.521  1.00 67.35           O  
ATOM  14878  CB  LEU C 118     253.729 205.336 246.433  1.00 66.11           C  
ATOM  14879  CG  LEU C 118     255.253 205.182 246.475  1.00 66.09           C  
ATOM  14880  CD1 LEU C 118     255.920 206.439 245.925  1.00 65.55           C  
ATOM  14881  CD2 LEU C 118     255.668 204.932 247.910  1.00 66.69           C  
ATOM  14882  N   ILE C 119     254.005 204.609 243.001  1.00 62.61           N  
ATOM  14883  CA  ILE C 119     254.366 203.566 242.055  1.00 63.31           C  
ATOM  14884  C   ILE C 119     255.864 203.567 241.839  1.00 63.53           C  
ATOM  14885  O   ILE C 119     256.390 204.455 241.171  1.00 63.95           O  
ATOM  14886  CB  ILE C 119     253.640 203.789 240.714  1.00 62.90           C  
ATOM  14887  CG1 ILE C 119     252.104 203.791 240.960  1.00 64.21           C  
ATOM  14888  CG2 ILE C 119     254.061 202.714 239.698  1.00 62.91           C  
ATOM  14889  CD1 ILE C 119     251.269 204.221 239.773  1.00 60.63           C  
ATOM  14890  N   VAL C 120     256.560 202.594 242.415  1.00 64.46           N  
ATOM  14891  CA  VAL C 120     258.018 202.588 242.335  1.00 66.06           C  
ATOM  14892  C   VAL C 120     258.621 201.264 241.907  1.00 67.58           C  
ATOM  14893  O   VAL C 120     258.310 200.217 242.466  1.00 69.23           O  
ATOM  14894  CB  VAL C 120     258.625 202.988 243.694  1.00 66.03           C  
ATOM  14895  CG1 VAL C 120     260.155 202.932 243.636  1.00 66.84           C  
ATOM  14896  CG2 VAL C 120     258.176 204.387 244.049  1.00 64.71           C  
ATOM  14897  N   ASN C 121     259.527 201.322 240.944  1.00 65.81           N  
ATOM  14898  CA  ASN C 121     260.278 200.148 240.535  1.00 67.84           C  
ATOM  14899  C   ASN C 121     261.640 200.159 241.227  1.00 68.37           C  
ATOM  14900  O   ASN C 121     262.546 200.857 240.764  1.00 68.95           O  
ATOM  14901  CB  ASN C 121     260.445 200.133 239.028  1.00 68.41           C  
ATOM  14902  CG  ASN C 121     261.114 198.892 238.522  1.00 69.88           C  
ATOM  14903  OD1 ASN C 121     261.671 198.101 239.289  1.00 71.97           O  
ATOM  14904  ND2 ASN C 121     261.070 198.704 237.228  1.00 68.77           N  
ATOM  14905  N   ASN C 122     261.783 199.416 242.355  1.00 69.82           N  
ATOM  14906  CA  ASN C 122     263.021 199.416 243.130  1.00 71.50           C  
ATOM  14907  C   ASN C 122     263.868 198.167 242.816  1.00 72.55           C  
ATOM  14908  O   ASN C 122     263.536 197.049 243.240  1.00 72.62           O  
ATOM  14909  CB  ASN C 122     262.764 199.577 244.633  1.00 73.12           C  
ATOM  14910  CG  ASN C 122     261.760 198.579 245.252  1.00 71.69           C  
ATOM  14911  OD1 ASN C 122     260.597 198.506 244.825  1.00 72.07           O  
ATOM  14912  ND2 ASN C 122     262.203 197.836 246.259  1.00 72.88           N  
ATOM  14913  N   ALA C 123     264.940 198.369 242.033  1.00 71.78           N  
ATOM  14914  CA  ALA C 123     265.896 197.353 241.569  1.00 72.40           C  
ATOM  14915  C   ALA C 123     264.945 196.482 240.755  1.00 72.62           C  
ATOM  14916  O   ALA C 123     264.459 196.902 239.704  1.00 72.87           O  
ATOM  14917  CB  ALA C 123     266.562 196.652 242.753  1.00 72.35           C  
ATOM  14918  N   THR C 124     264.727 195.254 241.217  1.00 71.80           N  
ATOM  14919  CA  THR C 124     263.906 194.296 240.489  1.00 73.36           C  
ATOM  14920  C   THR C 124     262.397 194.145 240.654  1.00 72.26           C  
ATOM  14921  O   THR C 124     261.781 193.354 239.939  1.00 72.86           O  
ATOM  14922  CB  THR C 124     264.592 192.959 240.839  1.00 72.99           C  
ATOM  14923  N   ASN C 125     261.792 194.849 241.608  1.00 71.57           N  
ATOM  14924  CA  ASN C 125     260.381 194.592 241.892  1.00 71.70           C  
ATOM  14925  C   ASN C 125     259.521 195.846 241.903  1.00 71.23           C  
ATOM  14926  O   ASN C 125     259.761 196.780 242.668  1.00 70.83           O  
ATOM  14927  CB  ASN C 125     260.244 193.834 243.196  1.00 72.79           C  
ATOM  14928  N   VAL C 126     258.494 195.844 241.064  1.00 71.77           N  
ATOM  14929  CA  VAL C 126     257.579 196.973 240.998  1.00 71.00           C  
ATOM  14930  C   VAL C 126     256.570 196.929 242.130  1.00 71.73           C  
ATOM  14931  O   VAL C 126     255.837 195.954 242.291  1.00 71.03           O  
ATOM  14932  CB  VAL C 126     256.828 196.986 239.655  1.00 70.32           C  
ATOM  14933  CG1 VAL C 126     255.811 198.131 239.630  1.00 70.11           C  
ATOM  14934  CG2 VAL C 126     257.830 197.126 238.526  1.00 71.17           C  
ATOM  14935  N   VAL C 127     256.522 198.006 242.899  1.00 70.15           N  
ATOM  14936  CA  VAL C 127     255.636 198.106 244.043  1.00 69.91           C  
ATOM  14937  C   VAL C 127     254.610 199.219 243.901  1.00 69.48           C  
ATOM  14938  O   VAL C 127     254.962 200.386 243.722  1.00 69.77           O  
ATOM  14939  CB  VAL C 127     256.469 198.369 245.310  1.00 70.25           C  
ATOM  14940  CG1 VAL C 127     255.559 198.526 246.525  1.00 71.16           C  
ATOM  14941  CG2 VAL C 127     257.457 197.228 245.511  1.00 70.47           C  
ATOM  14942  N   ILE C 128     253.342 198.861 244.016  1.00 69.03           N  
ATOM  14943  CA  ILE C 128     252.267 199.838 243.971  1.00 68.40           C  
ATOM  14944  C   ILE C 128     251.524 199.880 245.294  1.00 71.32           C  
ATOM  14945  O   ILE C 128     250.980 198.872 245.746  1.00 72.94           O  
ATOM  14946  CB  ILE C 128     251.259 199.534 242.849  1.00 69.39           C  
ATOM  14947  CG1 ILE C 128     251.971 199.551 241.487  1.00 68.96           C  
ATOM  14948  CG2 ILE C 128     250.111 200.556 242.901  1.00 68.33           C  
ATOM  14949  CD1 ILE C 128     251.112 199.099 240.313  1.00 67.08           C  
ATOM  14950  N   LYS C 129     251.475 201.053 245.901  1.00 68.42           N  
ATOM  14951  CA  LYS C 129     250.748 201.235 247.153  1.00 70.27           C  
ATOM  14952  C   LYS C 129     249.875 202.474 247.110  1.00 69.56           C  
ATOM  14953  O   LYS C 129     250.240 203.473 246.497  1.00 69.13           O  
ATOM  14954  CB  LYS C 129     251.719 201.325 248.320  1.00 70.20           C  
ATOM  14955  N   VAL C 130     248.741 202.436 247.797  1.00 70.50           N  
ATOM  14956  CA  VAL C 130     247.870 203.624 247.858  1.00 69.41           C  
ATOM  14957  C   VAL C 130     247.703 204.198 249.273  1.00 70.78           C  
ATOM  14958  O   VAL C 130     246.637 204.729 249.597  1.00 69.71           O  
ATOM  14959  CB  VAL C 130     246.476 203.301 247.329  1.00 70.85           C  
ATOM  14960  CG1 VAL C 130     246.560 202.895 245.887  1.00 69.45           C  
ATOM  14961  CG2 VAL C 130     245.862 202.249 248.156  1.00 76.23           C  
ATOM  14962  N   CYS C 131     248.736 204.040 250.106  1.00 70.87           N  
ATOM  14963  CA  CYS C 131     248.741 204.412 251.519  1.00 71.31           C  
ATOM  14964  C   CYS C 131     248.785 205.931 251.700  1.00 69.93           C  
ATOM  14965  O   CYS C 131     249.284 206.662 250.844  1.00 69.16           O  
ATOM  14966  CB  CYS C 131     249.956 203.785 252.224  1.00 71.56           C  
ATOM  14967  SG  CYS C 131     250.094 201.976 252.047  1.00 71.66           S  
ATOM  14968  N   GLU C 132     248.312 206.411 252.866  1.00 70.76           N  
ATOM  14969  CA  GLU C 132     248.385 207.838 253.211  1.00 70.46           C  
ATOM  14970  C   GLU C 132     249.821 208.150 253.628  1.00 69.64           C  
ATOM  14971  O   GLU C 132     250.156 208.219 254.810  1.00 68.37           O  
ATOM  14972  CB  GLU C 132     247.398 208.179 254.329  1.00 71.22           C  
ATOM  14973  N   PHE C 133     250.666 208.269 252.612  1.00 68.45           N  
ATOM  14974  CA  PHE C 133     252.106 208.391 252.756  1.00 68.81           C  
ATOM  14975  C   PHE C 133     252.605 209.758 253.156  1.00 68.56           C  
ATOM  14976  O   PHE C 133     252.111 210.789 252.688  1.00 68.15           O  
ATOM  14977  CB  PHE C 133     252.799 208.079 251.438  1.00 68.44           C  
ATOM  14978  CG  PHE C 133     252.870 206.663 251.033  1.00 68.42           C  
ATOM  14979  CD1 PHE C 133     252.092 206.181 249.993  1.00 68.97           C  
ATOM  14980  CD2 PHE C 133     253.736 205.807 251.669  1.00 67.75           C  
ATOM  14981  CE1 PHE C 133     252.186 204.871 249.606  1.00 69.35           C  
ATOM  14982  CE2 PHE C 133     253.830 204.498 251.289  1.00 69.44           C  
ATOM  14983  CZ  PHE C 133     253.058 204.031 250.259  1.00 69.18           C  
ATOM  14984  N   GLN C 134     253.664 209.743 253.955  1.00 68.31           N  
ATOM  14985  CA  GLN C 134     254.436 210.931 254.255  1.00 67.67           C  
ATOM  14986  C   GLN C 134     255.627 210.967 253.326  1.00 68.07           C  
ATOM  14987  O   GLN C 134     256.447 210.049 253.326  1.00 67.55           O  
ATOM  14988  CB  GLN C 134     254.928 210.940 255.703  1.00 69.37           C  
ATOM  14989  N   PHE C 135     255.727 212.016 252.535  1.00 67.30           N  
ATOM  14990  CA  PHE C 135     256.812 212.123 251.584  1.00 68.19           C  
ATOM  14991  C   PHE C 135     257.843 213.139 252.034  1.00 68.42           C  
ATOM  14992  O   PHE C 135     257.547 214.032 252.830  1.00 68.65           O  
ATOM  14993  CB  PHE C 135     256.276 212.472 250.200  1.00 66.95           C  
ATOM  14994  CG  PHE C 135     255.417 211.382 249.618  1.00 66.86           C  
ATOM  14995  CD1 PHE C 135     254.067 211.581 249.402  1.00 66.22           C  
ATOM  14996  CD2 PHE C 135     255.960 210.145 249.308  1.00 65.78           C  
ATOM  14997  CE1 PHE C 135     253.285 210.581 248.876  1.00 66.02           C  
ATOM  14998  CE2 PHE C 135     255.179 209.143 248.788  1.00 66.08           C  
ATOM  14999  CZ  PHE C 135     253.843 209.360 248.564  1.00 66.58           C  
ATOM  15000  N   CYS C 136     259.055 212.981 251.522  1.00 68.74           N  
ATOM  15001  CA  CYS C 136     260.159 213.885 251.801  1.00 67.98           C  
ATOM  15002  C   CYS C 136     259.935 215.241 251.149  1.00 68.59           C  
ATOM  15003  O   CYS C 136     259.134 215.369 250.225  1.00 67.28           O  
ATOM  15004  CB  CYS C 136     261.467 213.304 251.264  1.00 67.68           C  
ATOM  15005  N   ASN C 137     260.682 216.250 251.605  1.00 68.69           N  
ATOM  15006  CA  ASN C 137     260.598 217.585 251.016  1.00 68.71           C  
ATOM  15007  C   ASN C 137     260.989 217.550 249.542  1.00 68.19           C  
ATOM  15008  O   ASN C 137     260.446 218.290 248.722  1.00 67.52           O  
ATOM  15009  CB  ASN C 137     261.510 218.548 251.755  1.00 70.36           C  
ATOM  15010  N   ASP C 138     261.931 216.674 249.215  1.00 67.35           N  
ATOM  15011  CA  ASP C 138     262.400 216.480 247.851  1.00 67.58           C  
ATOM  15012  C   ASP C 138     262.811 215.018 247.684  1.00 67.33           C  
ATOM  15013  O   ASP C 138     263.989 214.693 247.825  1.00 66.29           O  
ATOM  15014  CB  ASP C 138     263.587 217.405 247.556  1.00 69.17           C  
ATOM  15015  N   PRO C 139     261.847 214.110 247.469  1.00 67.09           N  
ATOM  15016  CA  PRO C 139     262.019 212.668 247.386  1.00 66.38           C  
ATOM  15017  C   PRO C 139     262.963 212.266 246.268  1.00 65.04           C  
ATOM  15018  O   PRO C 139     262.894 212.807 245.164  1.00 65.38           O  
ATOM  15019  CB  PRO C 139     260.593 212.187 247.084  1.00 64.59           C  
ATOM  15020  CG  PRO C 139     259.694 213.282 247.594  1.00 65.93           C  
ATOM  15021  CD  PRO C 139     260.451 214.554 247.319  1.00 66.12           C  
ATOM  15022  N   PHE C 140     263.817 211.289 246.539  1.00 65.09           N  
ATOM  15023  CA  PHE C 140     264.728 210.775 245.527  1.00 64.93           C  
ATOM  15024  C   PHE C 140     265.164 209.371 245.890  1.00 64.49           C  
ATOM  15025  O   PHE C 140     264.997 208.940 247.032  1.00 64.92           O  
ATOM  15026  CB  PHE C 140     265.956 211.669 245.375  1.00 63.79           C  
ATOM  15027  CG  PHE C 140     266.861 211.664 246.557  1.00 65.47           C  
ATOM  15028  CD1 PHE C 140     267.942 210.798 246.608  1.00 66.66           C  
ATOM  15029  CD2 PHE C 140     266.644 212.516 247.615  1.00 65.81           C  
ATOM  15030  CE1 PHE C 140     268.782 210.786 247.696  1.00 67.17           C  
ATOM  15031  CE2 PHE C 140     267.482 212.509 248.707  1.00 66.54           C  
ATOM  15032  CZ  PHE C 140     268.553 211.643 248.749  1.00 66.53           C  
ATOM  15033  N   LEU C 141     265.743 208.665 244.931  1.00 64.94           N  
ATOM  15034  CA  LEU C 141     266.282 207.347 245.201  1.00 64.80           C  
ATOM  15035  C   LEU C 141     267.775 207.328 244.906  1.00 64.66           C  
ATOM  15036  O   LEU C 141     268.235 207.941 243.943  1.00 64.60           O  
ATOM  15037  CB  LEU C 141     265.550 206.292 244.366  1.00 64.05           C  
ATOM  15038  CG  LEU C 141     264.064 206.045 244.756  1.00 64.76           C  
ATOM  15039  CD1 LEU C 141     263.141 206.957 243.922  1.00 62.31           C  
ATOM  15040  CD2 LEU C 141     263.725 204.576 244.538  1.00 64.49           C  
ATOM  15041  N   GLY C 142     268.534 206.636 245.747  1.00 65.06           N  
ATOM  15042  CA  GLY C 142     269.980 206.553 245.577  1.00 64.25           C  
ATOM  15043  C   GLY C 142     270.403 205.275 244.860  1.00 64.25           C  
ATOM  15044  O   GLY C 142     269.571 204.574 244.277  1.00 64.48           O  
ATOM  15045  N   VAL C 143     271.714 204.979 244.920  1.00 65.37           N  
ATOM  15046  CA  VAL C 143     272.343 203.822 244.276  1.00 65.00           C  
ATOM  15047  C   VAL C 143     273.213 203.106 245.310  1.00 64.77           C  
ATOM  15048  O   VAL C 143     273.935 203.741 246.083  1.00 64.59           O  
ATOM  15049  CB  VAL C 143     273.201 204.263 243.023  1.00 64.88           C  
ATOM  15050  CG1 VAL C 143     273.912 203.021 242.338  1.00 65.42           C  
ATOM  15051  CG2 VAL C 143     272.283 204.989 241.957  1.00 64.64           C  
ATOM  15052  N   ASN C 165     247.366 203.822 257.116  1.00 76.21           N  
ATOM  15053  CA  ASN C 165     246.146 203.602 256.353  1.00 75.53           C  
ATOM  15054  C   ASN C 165     246.472 203.237 254.894  1.00 75.92           C  
ATOM  15055  O   ASN C 165     246.908 204.083 254.121  1.00 74.52           O  
ATOM  15056  CB  ASN C 165     245.237 204.836 256.410  1.00 75.79           C  
ATOM  15057  CG  ASN C 165     244.496 204.983 257.749  1.00 76.12           C  
ATOM  15058  OD1 ASN C 165     243.703 204.101 258.122  1.00 77.08           O  
ATOM  15059  ND2 ASN C 165     244.742 206.072 258.460  1.00 76.45           N  
ATOM  15060  N   CYS C 166     246.263 201.949 254.544  1.00 77.91           N  
ATOM  15061  CA  CYS C 166     246.519 201.395 253.203  1.00 77.82           C  
ATOM  15062  C   CYS C 166     245.280 200.614 252.754  1.00 81.11           C  
ATOM  15063  O   CYS C 166     244.739 199.828 253.539  1.00 83.11           O  
ATOM  15064  CB  CYS C 166     247.743 200.446 253.223  1.00 76.16           C  
ATOM  15065  SG  CYS C 166     249.305 201.215 253.749  1.00 79.21           S  
ATOM  15066  N   THR C 167     244.840 200.822 251.493  1.00 81.58           N  
ATOM  15067  CA  THR C 167     243.652 200.156 250.934  1.00 86.58           C  
ATOM  15068  C   THR C 167     243.958 199.223 249.757  1.00 87.49           C  
ATOM  15069  O   THR C 167     243.124 198.392 249.378  1.00 90.36           O  
ATOM  15070  CB  THR C 167     242.595 201.198 250.533  1.00 87.62           C  
ATOM  15071  OG1 THR C 167     243.130 202.087 249.555  1.00 83.99           O  
ATOM  15072  CG2 THR C 167     242.178 201.988 251.761  1.00 89.46           C  
ATOM  15073  N   PHE C 168     245.142 199.364 249.185  1.00 82.32           N  
ATOM  15074  CA  PHE C 168     245.583 198.547 248.064  1.00 81.27           C  
ATOM  15075  C   PHE C 168     247.093 198.413 248.073  1.00 78.60           C  
ATOM  15076  O   PHE C 168     247.814 199.379 248.353  1.00 76.56           O  
ATOM  15077  CB  PHE C 168     245.132 199.124 246.712  1.00 81.97           C  
ATOM  15078  CG  PHE C 168     245.674 198.377 245.538  1.00 80.27           C  
ATOM  15079  CD1 PHE C 168     244.980 197.325 244.979  1.00 83.34           C  
ATOM  15080  CD2 PHE C 168     246.906 198.722 244.999  1.00 76.45           C  
ATOM  15081  CE1 PHE C 168     245.498 196.635 243.907  1.00 80.71           C  
ATOM  15082  CE2 PHE C 168     247.423 198.032 243.935  1.00 74.84           C  
ATOM  15083  CZ  PHE C 168     246.717 196.988 243.386  1.00 76.59           C  
ATOM  15084  N   GLU C 169     247.565 197.214 247.770  1.00 78.96           N  
ATOM  15085  CA  GLU C 169     248.978 196.954 247.597  1.00 75.57           C  
ATOM  15086  C   GLU C 169     249.196 195.864 246.568  1.00 74.88           C  
ATOM  15087  O   GLU C 169     248.538 194.823 246.599  1.00 74.49           O  
ATOM  15088  CB  GLU C 169     249.638 196.548 248.912  1.00 74.30           C  
ATOM  15089  N   TYR C 170     250.153 196.086 245.686  1.00 72.31           N  
ATOM  15090  CA  TYR C 170     250.551 195.089 244.711  1.00 72.06           C  
ATOM  15091  C   TYR C 170     252.052 195.072 244.497  1.00 72.32           C  
ATOM  15092  O   TYR C 170     252.681 196.117 244.346  1.00 71.80           O  
ATOM  15093  CB  TYR C 170     249.857 195.331 243.378  1.00 73.51           C  
ATOM  15094  CG  TYR C 170     250.471 194.539 242.286  1.00 72.32           C  
ATOM  15095  CD1 TYR C 170     250.155 193.212 242.117  1.00 72.70           C  
ATOM  15096  CD2 TYR C 170     251.390 195.143 241.462  1.00 72.18           C  
ATOM  15097  CE1 TYR C 170     250.767 192.489 241.120  1.00 72.83           C  
ATOM  15098  CE2 TYR C 170     251.996 194.433 240.474  1.00 71.59           C  
ATOM  15099  CZ  TYR C 170     251.693 193.107 240.298  1.00 72.23           C  
ATOM  15100  OH  TYR C 170     252.320 192.386 239.312  1.00 72.16           O  
ATOM  15101  N   VAL C 171     252.636 193.883 244.456  1.00 72.55           N  
ATOM  15102  CA  VAL C 171     254.056 193.775 244.169  1.00 72.07           C  
ATOM  15103  C   VAL C 171     254.317 192.770 243.048  1.00 71.24           C  
ATOM  15104  O   VAL C 171     253.846 191.634 243.117  1.00 71.66           O  
ATOM  15105  CB  VAL C 171     254.833 193.361 245.434  1.00 71.15           C  
ATOM  15106  CG1 VAL C 171     256.332 193.233 245.112  1.00 71.13           C  
ATOM  15107  CG2 VAL C 171     254.597 194.399 246.535  1.00 71.03           C  
ATOM  15108  N   SER C 172     255.105 193.178 242.037  1.00 71.58           N  
ATOM  15109  CA  SER C 172     255.507 192.316 240.927  1.00 72.11           C  
ATOM  15110  C   SER C 172     256.677 191.441 241.393  1.00 72.72           C  
ATOM  15111  O   SER C 172     257.823 191.616 240.970  1.00 72.36           O  
ATOM  15112  CB  SER C 172     255.886 193.148 239.696  1.00 72.09           C  
ATOM  15113  N   PHE C 186     270.364 208.727 224.134  1.00 56.07           N  
ATOM  15114  CA  PHE C 186     269.725 207.719 224.962  1.00 55.85           C  
ATOM  15115  C   PHE C 186     269.531 206.423 224.159  1.00 56.03           C  
ATOM  15116  O   PHE C 186     269.547 206.439 222.920  1.00 54.88           O  
ATOM  15117  CB  PHE C 186     268.373 208.241 225.502  1.00 56.46           C  
ATOM  15118  CG  PHE C 186     268.468 209.398 226.537  1.00 55.86           C  
ATOM  15119  CD1 PHE C 186     268.338 210.780 226.119  1.00 56.79           C  
ATOM  15120  CD2 PHE C 186     268.667 209.131 227.950  1.00 57.13           C  
ATOM  15121  CE1 PHE C 186     268.414 211.852 227.074  1.00 55.49           C  
ATOM  15122  CE2 PHE C 186     268.741 210.197 228.909  1.00 56.44           C  
ATOM  15123  CZ  PHE C 186     268.617 211.557 228.470  1.00 56.21           C  
ATOM  15124  N   LYS C 187     269.370 205.288 224.880  1.00 55.56           N  
ATOM  15125  CA  LYS C 187     269.249 203.944 224.292  1.00 55.74           C  
ATOM  15126  C   LYS C 187     267.829 203.389 224.332  1.00 55.84           C  
ATOM  15127  O   LYS C 187     267.461 202.557 223.500  1.00 55.61           O  
ATOM  15128  CB  LYS C 187     270.188 202.978 225.012  1.00 56.12           C  
ATOM  15129  CG  LYS C 187     271.669 203.247 224.773  1.00 55.43           C  
ATOM  15130  CD  LYS C 187     272.537 202.218 225.488  1.00 54.90           C  
ATOM  15131  CE  LYS C 187     274.002 202.306 225.054  1.00 54.34           C  
ATOM  15132  NZ  LYS C 187     274.662 203.553 225.524  1.00 54.51           N  
ATOM  15133  N   ASN C 188     267.031 203.827 225.300  1.00 55.81           N  
ATOM  15134  CA  ASN C 188     265.667 203.321 225.415  1.00 55.37           C  
ATOM  15135  C   ASN C 188     264.656 204.418 225.674  1.00 55.43           C  
ATOM  15136  O   ASN C 188     264.951 205.418 226.328  1.00 56.30           O  
ATOM  15137  CB  ASN C 188     265.571 202.259 226.489  1.00 55.98           C  
ATOM  15138  CG  ASN C 188     266.235 200.981 226.088  1.00 56.48           C  
ATOM  15139  OD1 ASN C 188     267.361 200.682 226.499  1.00 56.54           O  
ATOM  15140  ND2 ASN C 188     265.550 200.210 225.284  1.00 55.97           N  
ATOM  15141  N   LEU C 189     263.449 204.203 225.168  1.00 55.08           N  
ATOM  15142  CA  LEU C 189     262.317 205.093 225.380  1.00 54.20           C  
ATOM  15143  C   LEU C 189     261.159 204.368 226.044  1.00 53.26           C  
ATOM  15144  O   LEU C 189     260.745 203.289 225.609  1.00 54.91           O  
ATOM  15145  CB  LEU C 189     261.880 205.689 224.042  1.00 54.28           C  
ATOM  15146  CG  LEU C 189     260.576 206.488 223.993  1.00 53.71           C  
ATOM  15147  CD1 LEU C 189     260.670 207.735 224.828  1.00 53.47           C  
ATOM  15148  CD2 LEU C 189     260.321 206.864 222.568  1.00 54.34           C  
ATOM  15149  N   ARG C 190     260.649 204.961 227.113  1.00 52.81           N  
ATOM  15150  CA  ARG C 190     259.528 204.402 227.842  1.00 51.91           C  
ATOM  15151  C   ARG C 190     258.394 205.413 227.925  1.00 53.62           C  
ATOM  15152  O   ARG C 190     258.508 206.438 228.601  1.00 54.18           O  
ATOM  15153  CB  ARG C 190     259.955 203.999 229.240  1.00 53.37           C  
ATOM  15154  CG  ARG C 190     261.074 202.984 229.299  1.00 54.39           C  
ATOM  15155  CD  ARG C 190     261.394 202.615 230.703  1.00 55.57           C  
ATOM  15156  NE  ARG C 190     262.467 201.633 230.784  1.00 57.07           N  
ATOM  15157  CZ  ARG C 190     262.916 201.070 231.929  1.00 58.24           C  
ATOM  15158  NH1 ARG C 190     262.378 201.397 233.086  1.00 58.60           N  
ATOM  15159  NH2 ARG C 190     263.897 200.185 231.886  1.00 59.64           N  
ATOM  15160  N   GLU C 191     257.308 205.140 227.221  1.00 52.03           N  
ATOM  15161  CA  GLU C 191     256.181 206.065 227.196  1.00 49.95           C  
ATOM  15162  C   GLU C 191     255.062 205.553 228.072  1.00 54.17           C  
ATOM  15163  O   GLU C 191     254.807 204.353 228.108  1.00 50.03           O  
ATOM  15164  CB  GLU C 191     255.692 206.264 225.768  1.00 51.84           C  
ATOM  15165  N   PHE C 192     254.393 206.460 228.771  1.00 50.66           N  
ATOM  15166  CA  PHE C 192     253.302 206.108 229.657  1.00 50.53           C  
ATOM  15167  C   PHE C 192     252.116 207.052 229.557  1.00 50.05           C  
ATOM  15168  O   PHE C 192     252.276 208.260 229.397  1.00 53.59           O  
ATOM  15169  CB  PHE C 192     253.786 206.146 231.097  1.00 51.40           C  
ATOM  15170  CG  PHE C 192     254.897 205.234 231.396  1.00 51.45           C  
ATOM  15171  CD1 PHE C 192     256.204 205.606 231.152  1.00 51.50           C  
ATOM  15172  CD2 PHE C 192     254.651 204.008 231.931  1.00 51.62           C  
ATOM  15173  CE1 PHE C 192     257.235 204.761 231.435  1.00 51.95           C  
ATOM  15174  CE2 PHE C 192     255.678 203.148 232.216  1.00 51.58           C  
ATOM  15175  CZ  PHE C 192     256.978 203.525 231.966  1.00 52.39           C  
ATOM  15176  N   VAL C 193     250.922 206.525 229.743  1.00 50.42           N  
ATOM  15177  CA  VAL C 193     249.756 207.381 229.892  1.00 51.04           C  
ATOM  15178  C   VAL C 193     249.049 207.102 231.187  1.00 51.50           C  
ATOM  15179  O   VAL C 193     248.631 205.977 231.449  1.00 53.50           O  
ATOM  15180  CB  VAL C 193     248.777 207.233 228.727  1.00 50.86           C  
ATOM  15181  CG1 VAL C 193     247.539 208.051 228.983  1.00 51.60           C  
ATOM  15182  CG2 VAL C 193     249.439 207.713 227.477  1.00 50.97           C  
ATOM  15183  N   PHE C 194     248.903 208.139 231.992  1.00 51.89           N  
ATOM  15184  CA  PHE C 194     248.252 208.016 233.280  1.00 52.33           C  
ATOM  15185  C   PHE C 194     246.965 208.821 233.308  1.00 52.85           C  
ATOM  15186  O   PHE C 194     246.996 210.050 233.270  1.00 55.09           O  
ATOM  15187  CB  PHE C 194     249.170 208.545 234.379  1.00 53.78           C  
ATOM  15188  CG  PHE C 194     250.475 207.824 234.511  1.00 53.75           C  
ATOM  15189  CD1 PHE C 194     251.617 208.305 233.903  1.00 52.91           C  
ATOM  15190  CD2 PHE C 194     250.567 206.679 235.243  1.00 54.32           C  
ATOM  15191  CE1 PHE C 194     252.817 207.643 234.041  1.00 52.49           C  
ATOM  15192  CE2 PHE C 194     251.761 206.012 235.380  1.00 54.39           C  
ATOM  15193  CZ  PHE C 194     252.886 206.498 234.775  1.00 53.21           C  
ATOM  15194  N   LYS C 195     245.828 208.159 233.393  1.00 53.83           N  
ATOM  15195  CA  LYS C 195     244.584 208.917 233.488  1.00 54.82           C  
ATOM  15196  C   LYS C 195     243.735 208.337 234.602  1.00 56.13           C  
ATOM  15197  O   LYS C 195     243.828 207.151 234.906  1.00 57.44           O  
ATOM  15198  CB  LYS C 195     243.834 208.985 232.152  1.00 54.37           C  
ATOM  15199  CG  LYS C 195     243.299 207.688 231.609  1.00 54.23           C  
ATOM  15200  CD  LYS C 195     242.623 207.911 230.248  1.00 52.54           C  
ATOM  15201  CE  LYS C 195     241.826 206.686 229.814  1.00 52.60           C  
ATOM  15202  NZ  LYS C 195     241.188 206.866 228.467  1.00 51.26           N  
ATOM  15203  N   ASN C 196     242.927 209.168 235.238  1.00 57.07           N  
ATOM  15204  CA  ASN C 196     242.157 208.701 236.381  1.00 57.99           C  
ATOM  15205  C   ASN C 196     240.684 209.019 236.208  1.00 59.03           C  
ATOM  15206  O   ASN C 196     240.255 210.156 236.411  1.00 59.33           O  
ATOM  15207  CB  ASN C 196     242.705 209.325 237.647  1.00 58.99           C  
ATOM  15208  CG  ASN C 196     242.126 208.753 238.899  1.00 59.97           C  
ATOM  15209  OD1 ASN C 196     241.697 207.596 238.935  1.00 59.33           O  
ATOM  15210  ND2 ASN C 196     242.123 209.552 239.931  1.00 61.06           N  
ATOM  15211  N   ILE C 197     239.921 208.027 235.770  1.00 59.26           N  
ATOM  15212  CA  ILE C 197     238.522 208.248 235.448  1.00 60.11           C  
ATOM  15213  C   ILE C 197     237.589 207.381 236.272  1.00 61.23           C  
ATOM  15214  O   ILE C 197     237.683 206.155 236.270  1.00 60.61           O  
ATOM  15215  CB  ILE C 197     238.271 208.033 233.947  1.00 59.27           C  
ATOM  15216  CG1 ILE C 197     239.129 209.047 233.153  1.00 57.83           C  
ATOM  15217  CG2 ILE C 197     236.777 208.180 233.626  1.00 59.69           C  
ATOM  15218  CD1 ILE C 197     239.130 208.840 231.669  1.00 55.43           C  
ATOM  15219  N   ASP C 198     236.662 208.040 236.954  1.00 60.42           N  
ATOM  15220  CA  ASP C 198     235.645 207.390 237.771  1.00 60.79           C  
ATOM  15221  C   ASP C 198     236.232 206.436 238.803  1.00 60.86           C  
ATOM  15222  O   ASP C 198     235.677 205.372 239.075  1.00 61.16           O  
ATOM  15223  CB  ASP C 198     234.650 206.655 236.877  1.00 60.88           C  
ATOM  15224  N   GLY C 199     237.350 206.829 239.400  1.00 60.95           N  
ATOM  15225  CA  GLY C 199     237.970 206.035 240.447  1.00 61.43           C  
ATOM  15226  C   GLY C 199     238.971 205.008 239.933  1.00 62.02           C  
ATOM  15227  O   GLY C 199     239.616 204.328 240.734  1.00 63.40           O  
ATOM  15228  N   TYR C 200     239.104 204.877 238.617  1.00 59.29           N  
ATOM  15229  CA  TYR C 200     240.045 203.912 238.069  1.00 60.75           C  
ATOM  15230  C   TYR C 200     241.272 204.575 237.479  1.00 60.34           C  
ATOM  15231  O   TYR C 200     241.173 205.437 236.600  1.00 59.50           O  
ATOM  15232  CB  TYR C 200     239.380 203.063 237.006  1.00 60.04           C  
ATOM  15233  CG  TYR C 200     238.356 202.129 237.525  1.00 62.03           C  
ATOM  15234  CD1 TYR C 200     237.042 202.535 237.623  1.00 61.87           C  
ATOM  15235  CD2 TYR C 200     238.726 200.851 237.898  1.00 62.13           C  
ATOM  15236  CE1 TYR C 200     236.093 201.662 238.094  1.00 62.93           C  
ATOM  15237  CE2 TYR C 200     237.778 199.976 238.368  1.00 63.21           C  
ATOM  15238  CZ  TYR C 200     236.465 200.376 238.466  1.00 63.86           C  
ATOM  15239  OH  TYR C 200     235.513 199.505 238.934  1.00 66.40           O  
ATOM  15240  N   PHE C 201     242.432 204.139 237.935  1.00 58.89           N  
ATOM  15241  CA  PHE C 201     243.684 204.675 237.445  1.00 58.80           C  
ATOM  15242  C   PHE C 201     244.184 203.793 236.319  1.00 58.67           C  
ATOM  15243  O   PHE C 201     244.514 202.623 236.526  1.00 57.45           O  
ATOM  15244  CB  PHE C 201     244.695 204.736 238.571  1.00 58.20           C  
ATOM  15245  CG  PHE C 201     245.881 205.558 238.300  1.00 58.27           C  
ATOM  15246  CD1 PHE C 201     245.753 206.921 238.230  1.00 57.77           C  
ATOM  15247  CD2 PHE C 201     247.123 205.001 238.144  1.00 57.24           C  
ATOM  15248  CE1 PHE C 201     246.838 207.721 238.002  1.00 57.76           C  
ATOM  15249  CE2 PHE C 201     248.216 205.802 237.921  1.00 56.45           C  
ATOM  15250  CZ  PHE C 201     248.068 207.161 237.850  1.00 57.09           C  
ATOM  15251  N   LYS C 202     244.174 204.336 235.115  1.00 56.47           N  
ATOM  15252  CA  LYS C 202     244.520 203.571 233.932  1.00 55.09           C  
ATOM  15253  C   LYS C 202     245.948 203.856 233.525  1.00 53.49           C  
ATOM  15254  O   LYS C 202     246.312 205.012 233.300  1.00 55.29           O  
ATOM  15255  CB  LYS C 202     243.600 203.941 232.768  1.00 54.75           C  
ATOM  15256  CG  LYS C 202     242.100 203.860 233.041  1.00 55.92           C  
ATOM  15257  CD  LYS C 202     241.626 202.442 233.271  1.00 58.19           C  
ATOM  15258  CE  LYS C 202     240.105 202.388 233.361  1.00 59.51           C  
ATOM  15259  NZ  LYS C 202     239.616 201.027 233.694  1.00 60.38           N  
ATOM  15260  N   ILE C 203     246.759 202.813 233.415  1.00 53.55           N  
ATOM  15261  CA  ILE C 203     248.138 203.006 233.005  1.00 52.30           C  
ATOM  15262  C   ILE C 203     248.423 202.271 231.710  1.00 51.10           C  
ATOM  15263  O   ILE C 203     248.296 201.042 231.637  1.00 55.50           O  
ATOM  15264  CB  ILE C 203     249.124 202.503 234.062  1.00 53.77           C  
ATOM  15265  CG1 ILE C 203     248.864 203.204 235.403  1.00 54.51           C  
ATOM  15266  CG2 ILE C 203     250.559 202.777 233.577  1.00 52.56           C  
ATOM  15267  CD1 ILE C 203     249.622 202.607 236.583  1.00 55.93           C  
ATOM  15268  N   TYR C 204     248.870 203.020 230.715  1.00 51.75           N  
ATOM  15269  CA  TYR C 204     249.233 202.467 229.417  1.00 50.63           C  
ATOM  15270  C   TYR C 204     250.708 202.682 229.240  1.00 52.54           C  
ATOM  15271  O   TYR C 204     251.238 203.666 229.748  1.00 50.87           O  
ATOM  15272  CB  TYR C 204     248.502 203.187 228.295  1.00 51.11           C  
ATOM  15273  CG  TYR C 204     247.026 203.205 228.427  1.00 50.95           C  
ATOM  15274  CD1 TYR C 204     246.431 204.116 229.268  1.00 51.17           C  
ATOM  15275  CD2 TYR C 204     246.262 202.346 227.703  1.00 51.17           C  
ATOM  15276  CE1 TYR C 204     245.077 204.157 229.389  1.00 52.35           C  
ATOM  15277  CE2 TYR C 204     244.899 202.381 227.821  1.00 51.29           C  
ATOM  15278  CZ  TYR C 204     244.306 203.283 228.662  1.00 51.66           C  
ATOM  15279  OH  TYR C 204     242.939 203.316 228.775  1.00 52.44           O  
ATOM  15280  N   SER C 205     251.387 201.804 228.523  1.00 50.41           N  
ATOM  15281  CA  SER C 205     252.795 202.072 228.285  1.00 50.60           C  
ATOM  15282  C   SER C 205     253.349 201.368 227.070  1.00 50.52           C  
ATOM  15283  O   SER C 205     252.796 200.377 226.607  1.00 53.12           O  
ATOM  15284  CB  SER C 205     253.606 201.696 229.494  1.00 50.99           C  
ATOM  15285  OG  SER C 205     253.602 200.338 229.665  1.00 51.58           O  
ATOM  15286  N   LYS C 206     254.472 201.878 226.583  1.00 50.48           N  
ATOM  15287  CA  LYS C 206     255.191 201.297 225.459  1.00 51.01           C  
ATOM  15288  C   LYS C 206     256.694 201.387 225.645  1.00 51.98           C  
ATOM  15289  O   LYS C 206     257.231 202.446 225.971  1.00 52.60           O  
ATOM  15290  CB  LYS C 206     254.795 201.998 224.153  1.00 51.63           C  
ATOM  15291  CG  LYS C 206     255.592 201.602 222.909  1.00 52.17           C  
ATOM  15292  CD  LYS C 206     255.213 200.227 222.416  1.00 52.12           C  
ATOM  15293  CE  LYS C 206     255.963 199.871 221.154  1.00 53.55           C  
ATOM  15294  NZ  LYS C 206     255.694 198.474 220.739  1.00 54.38           N  
ATOM  15295  N   HIS C 207     257.384 200.287 225.376  1.00 52.43           N  
ATOM  15296  CA  HIS C 207     258.836 200.279 225.433  1.00 53.29           C  
ATOM  15297  C   HIS C 207     259.410 200.075 224.048  1.00 53.89           C  
ATOM  15298  O   HIS C 207     258.944 199.221 223.290  1.00 53.94           O  
ATOM  15299  CB  HIS C 207     259.342 199.156 226.343  1.00 53.18           C  
ATOM  15300  CG  HIS C 207     258.956 199.308 227.773  1.00 53.81           C  
ATOM  15301  ND1 HIS C 207     257.656 199.171 228.215  1.00 53.50           N  
ATOM  15302  CD2 HIS C 207     259.701 199.562 228.869  1.00 54.44           C  
ATOM  15303  CE1 HIS C 207     257.618 199.354 229.520  1.00 54.30           C  
ATOM  15304  NE2 HIS C 207     258.846 199.591 229.943  1.00 55.59           N  
ATOM  15305  N   THR C 208     260.446 200.836 223.730  1.00 53.94           N  
ATOM  15306  CA  THR C 208     261.124 200.698 222.450  1.00 54.66           C  
ATOM  15307  C   THR C 208     262.564 201.187 222.557  1.00 54.89           C  
ATOM  15308  O   THR C 208     262.839 202.079 223.358  1.00 55.53           O  
ATOM  15309  CB  THR C 208     260.375 201.506 221.368  1.00 55.16           C  
ATOM  15310  OG1 THR C 208     260.997 201.327 220.083  1.00 56.07           O  
ATOM  15311  CG2 THR C 208     260.359 202.980 221.709  1.00 54.82           C  
ATOM  15312  N   PRO C 209     263.509 200.595 221.817  1.00 55.28           N  
ATOM  15313  CA  PRO C 209     264.873 201.064 221.668  1.00 56.08           C  
ATOM  15314  C   PRO C 209     264.918 202.327 220.828  1.00 56.23           C  
ATOM  15315  O   PRO C 209     264.148 202.466 219.875  1.00 55.52           O  
ATOM  15316  CB  PRO C 209     265.559 199.886 220.972  1.00 56.29           C  
ATOM  15317  CG  PRO C 209     264.445 199.171 220.232  1.00 56.75           C  
ATOM  15318  CD  PRO C 209     263.215 199.339 221.105  1.00 55.88           C  
ATOM  15319  N   ILE C 210     265.829 203.223 221.177  1.00 55.01           N  
ATOM  15320  CA  ILE C 210     266.066 204.453 220.436  1.00 55.73           C  
ATOM  15321  C   ILE C 210     267.553 204.725 220.260  1.00 56.57           C  
ATOM  15322  O   ILE C 210     268.391 204.100 220.905  1.00 55.48           O  
ATOM  15323  CB  ILE C 210     265.406 205.665 221.113  1.00 55.49           C  
ATOM  15324  CG1 ILE C 210     265.988 205.851 222.514  1.00 56.11           C  
ATOM  15325  CG2 ILE C 210     263.897 205.463 221.169  1.00 54.99           C  
ATOM  15326  CD1 ILE C 210     265.644 207.158 223.184  1.00 55.22           C  
ATOM  15327  N   ASN C 211     267.870 205.692 219.407  1.00 55.46           N  
ATOM  15328  CA  ASN C 211     269.230 206.200 219.284  1.00 55.11           C  
ATOM  15329  C   ASN C 211     269.162 207.708 219.085  1.00 55.36           C  
ATOM  15330  O   ASN C 211     269.189 208.198 217.955  1.00 54.92           O  
ATOM  15331  CB  ASN C 211     269.970 205.519 218.148  1.00 55.90           C  
ATOM  15332  N   LEU C 212     268.978 208.425 220.190  1.00 54.96           N  
ATOM  15333  CA  LEU C 212     268.727 209.866 220.142  1.00 55.14           C  
ATOM  15334  C   LEU C 212     268.888 210.515 221.511  1.00 55.82           C  
ATOM  15335  O   LEU C 212     268.318 210.052 222.497  1.00 55.42           O  
ATOM  15336  CB  LEU C 212     267.325 210.125 219.564  1.00 56.06           C  
ATOM  15337  CG  LEU C 212     266.825 211.595 219.516  1.00 54.87           C  
ATOM  15338  CD1 LEU C 212     267.714 212.435 218.600  1.00 55.74           C  
ATOM  15339  CD2 LEU C 212     265.389 211.593 218.991  1.00 53.85           C  
ATOM  15340  N   VAL C 213     269.684 211.579 221.585  1.00 55.24           N  
ATOM  15341  CA  VAL C 213     269.933 212.242 222.861  1.00 55.48           C  
ATOM  15342  C   VAL C 213     269.123 213.526 223.095  1.00 55.13           C  
ATOM  15343  O   VAL C 213     268.784 213.846 224.229  1.00 54.73           O  
ATOM  15344  CB  VAL C 213     271.448 212.514 223.018  1.00 56.10           C  
ATOM  15345  N   ARG C 214     268.891 214.292 222.036  1.00 54.46           N  
ATOM  15346  CA  ARG C 214     268.307 215.630 222.162  1.00 54.38           C  
ATOM  15347  C   ARG C 214     266.800 215.737 222.412  1.00 54.36           C  
ATOM  15348  O   ARG C 214     266.353 216.715 223.009  1.00 53.95           O  
ATOM  15349  CB  ARG C 214     268.606 216.418 220.906  1.00 54.34           C  
ATOM  15350  CG  ARG C 214     270.042 216.838 220.741  1.00 54.36           C  
ATOM  15351  CD  ARG C 214     270.176 217.788 219.638  1.00 54.74           C  
ATOM  15352  NE  ARG C 214     269.754 217.192 218.376  1.00 55.53           N  
ATOM  15353  CZ  ARG C 214     270.533 216.457 217.556  1.00 56.42           C  
ATOM  15354  NH1 ARG C 214     271.790 216.218 217.866  1.00 55.32           N  
ATOM  15355  NH2 ARG C 214     270.025 215.973 216.434  1.00 55.36           N  
ATOM  15356  N   ASP C 215     266.010 214.810 221.892  1.00 54.16           N  
ATOM  15357  CA  ASP C 215     264.557 214.977 221.904  1.00 54.51           C  
ATOM  15358  C   ASP C 215     263.839 213.632 221.815  1.00 54.03           C  
ATOM  15359  O   ASP C 215     264.468 212.581 221.791  1.00 53.68           O  
ATOM  15360  CB  ASP C 215     264.163 215.904 220.724  1.00 53.89           C  
ATOM  15361  N   LEU C 216     262.518 213.668 221.805  1.00 53.58           N  
ATOM  15362  CA  LEU C 216     261.740 212.474 221.538  1.00 53.23           C  
ATOM  15363  C   LEU C 216     261.886 212.201 220.049  1.00 53.27           C  
ATOM  15364  O   LEU C 216     261.990 213.140 219.263  1.00 53.25           O  
ATOM  15365  CB  LEU C 216     260.259 212.707 221.891  1.00 53.70           C  
ATOM  15366  CG  LEU C 216     259.937 212.877 223.361  1.00 52.95           C  
ATOM  15367  CD1 LEU C 216     258.461 213.316 223.486  1.00 53.21           C  
ATOM  15368  CD2 LEU C 216     260.184 211.531 224.102  1.00 53.93           C  
ATOM  15369  N   PRO C 217     261.907 210.941 219.626  1.00 53.26           N  
ATOM  15370  CA  PRO C 217     261.961 210.551 218.249  1.00 52.57           C  
ATOM  15371  C   PRO C 217     260.656 210.869 217.567  1.00 52.19           C  
ATOM  15372  O   PRO C 217     259.592 210.793 218.193  1.00 51.81           O  
ATOM  15373  CB  PRO C 217     262.236 209.052 218.335  1.00 52.47           C  
ATOM  15374  CG  PRO C 217     261.675 208.642 219.685  1.00 52.53           C  
ATOM  15375  CD  PRO C 217     261.882 209.845 220.582  1.00 53.23           C  
ATOM  15376  N   GLN C 218     260.720 211.173 216.284  1.00 52.12           N  
ATOM  15377  CA  GLN C 218     259.520 211.343 215.496  1.00 51.88           C  
ATOM  15378  C   GLN C 218     259.120 209.994 214.937  1.00 52.38           C  
ATOM  15379  O   GLN C 218     259.961 209.266 214.404  1.00 52.80           O  
ATOM  15380  CB  GLN C 218     259.724 212.355 214.372  1.00 51.86           C  
ATOM  15381  CG  GLN C 218     258.476 212.624 213.563  1.00 51.63           C  
ATOM  15382  CD  GLN C 218     258.663 213.741 212.566  1.00 51.52           C  
ATOM  15383  OE1 GLN C 218     259.765 214.272 212.404  1.00 51.04           O  
ATOM  15384  NE2 GLN C 218     257.584 214.111 211.883  1.00 51.96           N  
ATOM  15385  N   GLY C 219     257.857 209.651 215.070  1.00 52.22           N  
ATOM  15386  CA  GLY C 219     257.352 208.375 214.588  1.00 52.00           C  
ATOM  15387  C   GLY C 219     256.035 208.082 215.265  1.00 50.57           C  
ATOM  15388  O   GLY C 219     255.532 208.907 216.028  1.00 50.06           O  
ATOM  15389  N   PHE C 220     255.465 206.921 214.992  1.00 50.29           N  
ATOM  15390  CA  PHE C 220     254.178 206.593 215.575  1.00 49.26           C  
ATOM  15391  C   PHE C 220     254.131 205.196 216.160  1.00 49.29           C  
ATOM  15392  O   PHE C 220     254.571 204.230 215.538  1.00 49.22           O  
ATOM  15393  CB  PHE C 220     253.070 206.709 214.534  1.00 49.17           C  
ATOM  15394  CG  PHE C 220     251.752 206.367 215.097  1.00 48.38           C  
ATOM  15395  CD1 PHE C 220     251.008 207.318 215.743  1.00 47.86           C  
ATOM  15396  CD2 PHE C 220     251.266 205.087 215.013  1.00 47.68           C  
ATOM  15397  CE1 PHE C 220     249.805 207.002 216.291  1.00 47.57           C  
ATOM  15398  CE2 PHE C 220     250.065 204.766 215.565  1.00 48.08           C  
ATOM  15399  CZ  PHE C 220     249.330 205.725 216.206  1.00 48.94           C  
ATOM  15400  N   SER C 221     253.548 205.102 217.341  1.00 49.22           N  
ATOM  15401  CA  SER C 221     253.265 203.840 217.994  1.00 49.27           C  
ATOM  15402  C   SER C 221     252.101 204.056 218.933  1.00 49.41           C  
ATOM  15403  O   SER C 221     251.862 205.179 219.373  1.00 49.22           O  
ATOM  15404  CB  SER C 221     254.469 203.344 218.759  1.00 49.99           C  
ATOM  15405  OG  SER C 221     254.785 204.218 219.804  1.00 50.60           O  
ATOM  15406  N   ALA C 222     251.396 202.991 219.273  1.00 49.39           N  
ATOM  15407  CA  ALA C 222     250.311 203.108 220.229  1.00 49.38           C  
ATOM  15408  C   ALA C 222     250.661 202.340 221.483  1.00 50.28           C  
ATOM  15409  O   ALA C 222     251.330 201.309 221.423  1.00 50.59           O  
ATOM  15410  CB  ALA C 222     249.012 202.615 219.630  1.00 49.03           C  
ATOM  15411  N   LEU C 223     250.196 202.840 222.613  1.00 49.90           N  
ATOM  15412  CA  LEU C 223     250.487 202.229 223.901  1.00 50.74           C  
ATOM  15413  C   LEU C 223     249.385 201.296 224.387  1.00 51.63           C  
ATOM  15414  O   LEU C 223     248.225 201.696 224.524  1.00 51.50           O  
ATOM  15415  CB  LEU C 223     250.670 203.337 224.941  1.00 50.88           C  
ATOM  15416  CG  LEU C 223     252.015 204.080 224.982  1.00 50.64           C  
ATOM  15417  CD1 LEU C 223     252.368 204.675 223.614  1.00 51.25           C  
ATOM  15418  CD2 LEU C 223     251.916 205.181 226.011  1.00 50.64           C  
ATOM  15419  N   GLU C 224     249.746 200.047 224.669  1.00 50.60           N  
ATOM  15420  CA  GLU C 224     248.797 199.094 225.228  1.00 50.81           C  
ATOM  15421  C   GLU C 224     248.615 199.350 226.721  1.00 52.67           C  
ATOM  15422  O   GLU C 224     249.540 199.847 227.364  1.00 47.76           O  
ATOM  15423  CB  GLU C 224     249.275 197.654 224.986  1.00 51.18           C  
ATOM  15424  CG  GLU C 224     250.555 197.228 225.720  1.00 51.81           C  
ATOM  15425  CD  GLU C 224     251.797 197.581 224.957  1.00 51.35           C  
ATOM  15426  OE1 GLU C 224     251.676 198.299 223.998  1.00 51.21           O  
ATOM  15427  OE2 GLU C 224     252.858 197.124 225.313  1.00 50.96           O  
ATOM  15428  N   PRO C 225     247.445 199.045 227.294  1.00 51.58           N  
ATOM  15429  CA  PRO C 225     247.161 199.104 228.711  1.00 52.03           C  
ATOM  15430  C   PRO C 225     247.900 198.009 229.438  1.00 52.27           C  
ATOM  15431  O   PRO C 225     247.978 196.889 228.939  1.00 52.46           O  
ATOM  15432  CB  PRO C 225     245.648 198.886 228.765  1.00 51.94           C  
ATOM  15433  CG  PRO C 225     245.330 198.117 227.511  1.00 52.40           C  
ATOM  15434  CD  PRO C 225     246.312 198.624 226.472  1.00 51.72           C  
ATOM  15435  N   LEU C 226     248.385 198.307 230.635  1.00 52.42           N  
ATOM  15436  CA  LEU C 226     249.000 197.277 231.458  1.00 53.31           C  
ATOM  15437  C   LEU C 226     248.322 197.140 232.802  1.00 53.78           C  
ATOM  15438  O   LEU C 226     248.156 196.033 233.314  1.00 54.08           O  
ATOM  15439  CB  LEU C 226     250.478 197.564 231.711  1.00 52.70           C  
ATOM  15440  CG  LEU C 226     251.402 197.629 230.502  1.00 52.08           C  
ATOM  15441  CD1 LEU C 226     252.788 197.924 231.005  1.00 52.40           C  
ATOM  15442  CD2 LEU C 226     251.381 196.324 229.724  1.00 52.47           C  
ATOM  15443  N   VAL C 227     247.985 198.268 233.405  1.00 53.79           N  
ATOM  15444  CA  VAL C 227     247.469 198.259 234.763  1.00 54.62           C  
ATOM  15445  C   VAL C 227     246.168 199.037 234.862  1.00 55.47           C  
ATOM  15446  O   VAL C 227     245.989 200.059 234.200  1.00 55.45           O  
ATOM  15447  CB  VAL C 227     248.520 198.823 235.738  1.00 55.88           C  
ATOM  15448  CG1 VAL C 227     247.986 198.835 237.145  1.00 58.19           C  
ATOM  15449  CG2 VAL C 227     249.787 197.993 235.665  1.00 56.52           C  
ATOM  15450  N   ASP C 228     245.253 198.532 235.675  1.00 57.38           N  
ATOM  15451  CA  ASP C 228     243.974 199.184 235.913  1.00 58.24           C  
ATOM  15452  C   ASP C 228     243.653 199.096 237.404  1.00 59.38           C  
ATOM  15453  O   ASP C 228     243.272 198.035 237.901  1.00 60.72           O  
ATOM  15454  CB  ASP C 228     242.900 198.502 235.060  1.00 58.58           C  
ATOM  15455  CG  ASP C 228     241.541 199.162 235.096  1.00 59.41           C  
ATOM  15456  OD1 ASP C 228     241.296 199.989 235.929  1.00 59.97           O  
ATOM  15457  OD2 ASP C 228     240.741 198.865 234.231  1.00 60.17           O  
ATOM  15458  N   LEU C 229     243.889 200.186 238.133  1.00 59.32           N  
ATOM  15459  CA  LEU C 229     243.757 200.159 239.585  1.00 60.99           C  
ATOM  15460  C   LEU C 229     242.441 200.779 240.082  1.00 62.28           C  
ATOM  15461  O   LEU C 229     242.184 201.961 239.843  1.00 61.61           O  
ATOM  15462  CB  LEU C 229     244.904 200.934 240.244  1.00 61.13           C  
ATOM  15463  CG  LEU C 229     246.323 200.566 239.868  1.00 61.45           C  
ATOM  15464  CD1 LEU C 229     247.279 201.539 240.547  1.00 62.23           C  
ATOM  15465  CD2 LEU C 229     246.621 199.140 240.299  1.00 64.88           C  
ATOM  15466  N   PRO C 230     241.611 200.035 240.826  1.00 62.97           N  
ATOM  15467  CA  PRO C 230     240.362 200.478 241.419  1.00 63.14           C  
ATOM  15468  C   PRO C 230     240.654 201.248 242.699  1.00 63.72           C  
ATOM  15469  O   PRO C 230     240.362 200.773 243.795  1.00 66.50           O  
ATOM  15470  CB  PRO C 230     239.650 199.156 241.698  1.00 66.18           C  
ATOM  15471  CG  PRO C 230     240.778 198.196 242.010  1.00 68.02           C  
ATOM  15472  CD  PRO C 230     241.935 198.630 241.109  1.00 63.99           C  
ATOM  15473  N   ILE C 231     241.284 202.404 242.552  1.00 62.98           N  
ATOM  15474  CA  ILE C 231     241.767 203.164 243.696  1.00 63.64           C  
ATOM  15475  C   ILE C 231     240.719 204.009 244.417  1.00 63.50           C  
ATOM  15476  O   ILE C 231     240.744 204.094 245.644  1.00 64.03           O  
ATOM  15477  CB  ILE C 231     242.962 204.053 243.268  1.00 63.04           C  
ATOM  15478  CG1 ILE C 231     242.548 205.062 242.120  1.00 62.50           C  
ATOM  15479  CG2 ILE C 231     244.079 203.163 242.816  1.00 63.63           C  
ATOM  15480  CD1 ILE C 231     243.566 206.123 241.784  1.00 62.30           C  
ATOM  15481  N   GLY C 232     239.821 204.653 243.680  1.00 63.27           N  
ATOM  15482  CA  GLY C 232     238.826 205.516 244.310  1.00 63.27           C  
ATOM  15483  C   GLY C 232     239.464 206.773 244.914  1.00 63.32           C  
ATOM  15484  O   GLY C 232     238.918 207.363 245.842  1.00 63.91           O  
ATOM  15485  N   ILE C 233     240.630 207.166 244.407  1.00 63.15           N  
ATOM  15486  CA  ILE C 233     241.397 208.289 244.946  1.00 62.69           C  
ATOM  15487  C   ILE C 233     241.484 209.457 243.963  1.00 62.51           C  
ATOM  15488  O   ILE C 233     241.820 209.254 242.795  1.00 62.37           O  
ATOM  15489  CB  ILE C 233     242.819 207.817 245.341  1.00 63.42           C  
ATOM  15490  CG1 ILE C 233     242.712 206.789 246.472  1.00 64.58           C  
ATOM  15491  CG2 ILE C 233     243.720 209.001 245.734  1.00 64.67           C  
ATOM  15492  CD1 ILE C 233     243.984 206.019 246.742  1.00 67.54           C  
ATOM  15493  N   ASN C 234     241.191 210.679 244.458  1.00 62.47           N  
ATOM  15494  CA  ASN C 234     241.281 211.926 243.693  1.00 62.57           C  
ATOM  15495  C   ASN C 234     242.750 212.320 243.486  1.00 62.55           C  
ATOM  15496  O   ASN C 234     243.519 212.390 244.439  1.00 62.62           O  
ATOM  15497  CB  ASN C 234     240.527 213.059 244.405  1.00 61.75           C  
ATOM  15498  CG  ASN C 234     238.993 212.886 244.421  1.00 60.81           C  
ATOM  15499  OD1 ASN C 234     238.446 211.940 243.832  1.00 62.13           O  
ATOM  15500  ND2 ASN C 234     238.308 213.802 245.104  1.00 61.92           N  
ATOM  15501  N   ILE C 235     243.129 212.568 242.219  1.00 61.55           N  
ATOM  15502  CA  ILE C 235     244.483 212.982 241.831  1.00 61.76           C  
ATOM  15503  C   ILE C 235     244.431 214.326 241.123  1.00 61.54           C  
ATOM  15504  O   ILE C 235     243.732 214.474 240.123  1.00 60.92           O  
ATOM  15505  CB  ILE C 235     245.136 211.936 240.909  1.00 60.45           C  
ATOM  15506  CG1 ILE C 235     245.267 210.584 241.655  1.00 60.74           C  
ATOM  15507  CG2 ILE C 235     246.488 212.445 240.429  1.00 61.83           C  
ATOM  15508  CD1 ILE C 235     245.621 209.411 240.763  1.00 60.71           C  
ATOM  15509  N   THR C 236     245.165 215.301 241.645  1.00 61.21           N  
ATOM  15510  CA  THR C 236     245.208 216.628 241.054  1.00 60.58           C  
ATOM  15511  C   THR C 236     246.637 217.058 240.749  1.00 59.55           C  
ATOM  15512  O   THR C 236     246.860 217.953 239.929  1.00 61.13           O  
ATOM  15513  CB  THR C 236     244.538 217.658 241.977  1.00 61.68           C  
ATOM  15514  OG1 THR C 236     245.239 217.719 243.224  1.00 62.06           O  
ATOM  15515  CG2 THR C 236     243.097 217.253 242.237  1.00 62.23           C  
ATOM  15516  N   ARG C 237     247.595 216.425 241.420  1.00 58.59           N  
ATOM  15517  CA  ARG C 237     249.018 216.729 241.300  1.00 58.62           C  
ATOM  15518  C   ARG C 237     249.829 215.452 241.250  1.00 60.24           C  
ATOM  15519  O   ARG C 237     249.424 214.431 241.809  1.00 61.17           O  
ATOM  15520  CB  ARG C 237     249.511 217.537 242.485  1.00 60.64           C  
ATOM  15521  CG  ARG C 237     248.917 218.909 242.645  1.00 61.63           C  
ATOM  15522  CD  ARG C 237     249.452 219.568 243.852  1.00 63.16           C  
ATOM  15523  NE  ARG C 237     248.808 220.838 244.113  1.00 66.74           N  
ATOM  15524  CZ  ARG C 237     248.908 221.519 245.271  1.00 68.48           C  
ATOM  15525  NH1 ARG C 237     249.626 221.030 246.262  1.00 66.95           N  
ATOM  15526  NH2 ARG C 237     248.283 222.677 245.412  1.00 67.58           N  
ATOM  15527  N   PHE C 238     251.012 215.521 240.659  1.00 58.31           N  
ATOM  15528  CA  PHE C 238     251.894 214.374 240.703  1.00 58.27           C  
ATOM  15529  C   PHE C 238     253.346 214.809 240.639  1.00 59.57           C  
ATOM  15530  O   PHE C 238     253.655 215.941 240.272  1.00 57.85           O  
ATOM  15531  CB  PHE C 238     251.616 213.431 239.541  1.00 60.07           C  
ATOM  15532  CG  PHE C 238     252.173 213.874 238.253  1.00 57.12           C  
ATOM  15533  CD1 PHE C 238     253.377 213.339 237.822  1.00 57.83           C  
ATOM  15534  CD2 PHE C 238     251.549 214.812 237.474  1.00 56.76           C  
ATOM  15535  CE1 PHE C 238     253.937 213.728 236.641  1.00 56.75           C  
ATOM  15536  CE2 PHE C 238     252.115 215.207 236.283  1.00 56.36           C  
ATOM  15537  CZ  PHE C 238     253.308 214.662 235.871  1.00 56.81           C  
ATOM  15538  N   GLN C 239     254.245 213.909 240.987  1.00 58.66           N  
ATOM  15539  CA  GLN C 239     255.665 214.197 240.843  1.00 58.34           C  
ATOM  15540  C   GLN C 239     256.429 212.965 240.374  1.00 59.02           C  
ATOM  15541  O   GLN C 239     256.004 211.834 240.614  1.00 57.82           O  
ATOM  15542  CB  GLN C 239     256.235 214.754 242.145  1.00 61.10           C  
ATOM  15543  CG  GLN C 239     256.126 213.845 243.330  1.00 60.80           C  
ATOM  15544  CD  GLN C 239     256.768 214.424 244.589  1.00 63.26           C  
ATOM  15545  OE1 GLN C 239     257.955 214.222 244.860  1.00 64.30           O  
ATOM  15546  NE2 GLN C 239     255.983 215.153 245.370  1.00 63.46           N  
ATOM  15547  N   THR C 240     257.554 213.179 239.700  1.00 58.00           N  
ATOM  15548  CA  THR C 240     258.352 212.074 239.175  1.00 57.49           C  
ATOM  15549  C   THR C 240     259.583 211.817 240.037  1.00 58.30           C  
ATOM  15550  O   THR C 240     260.348 212.731 240.341  1.00 58.82           O  
ATOM  15551  CB  THR C 240     258.787 212.352 237.724  1.00 56.94           C  
ATOM  15552  OG1 THR C 240     257.629 212.550 236.904  1.00 56.42           O  
ATOM  15553  CG2 THR C 240     259.571 211.180 237.161  1.00 56.14           C  
ATOM  15554  N   LEU C 241     259.767 210.558 240.412  1.00 60.09           N  
ATOM  15555  CA  LEU C 241     260.852 210.127 241.284  1.00 58.54           C  
ATOM  15556  C   LEU C 241     262.035 209.533 240.513  1.00 60.53           C  
ATOM  15557  O   LEU C 241     261.883 208.529 239.804  1.00 60.17           O  
ATOM  15558  CB  LEU C 241     260.324 209.061 242.240  1.00 58.82           C  
ATOM  15559  CG  LEU C 241     259.087 209.429 243.034  1.00 59.30           C  
ATOM  15560  CD1 LEU C 241     258.661 208.220 243.838  1.00 59.09           C  
ATOM  15561  CD2 LEU C 241     259.395 210.606 243.924  1.00 62.33           C  
ATOM  15562  N   LEU C 242     263.220 210.144 240.679  1.00 58.85           N  
ATOM  15563  CA  LEU C 242     264.470 209.746 240.027  1.00 59.65           C  
ATOM  15564  C   LEU C 242     265.401 209.135 241.067  1.00 61.24           C  
ATOM  15565  O   LEU C 242     265.568 209.690 242.158  1.00 61.63           O  
ATOM  15566  CB  LEU C 242     265.148 210.974 239.338  1.00 60.41           C  
ATOM  15567  N   ALA C 264     266.383 212.203 231.364  1.00 53.94           N  
ATOM  15568  CA  ALA C 264     265.469 213.239 230.901  1.00 53.88           C  
ATOM  15569  C   ALA C 264     264.075 212.641 230.665  1.00 53.45           C  
ATOM  15570  O   ALA C 264     263.947 211.438 230.389  1.00 54.09           O  
ATOM  15571  CB  ALA C 264     266.000 213.887 229.620  1.00 53.15           C  
ATOM  15572  N   TYR C 265     263.035 213.487 230.776  1.00 53.39           N  
ATOM  15573  CA  TYR C 265     261.636 213.101 230.571  1.00 54.44           C  
ATOM  15574  C   TYR C 265     260.785 214.274 230.096  1.00 53.77           C  
ATOM  15575  O   TYR C 265     261.185 215.439 230.199  1.00 42.58           O  
ATOM  15576  CB  TYR C 265     261.057 212.467 231.834  1.00 53.78           C  
ATOM  15577  CG  TYR C 265     261.016 213.318 233.022  1.00 53.30           C  
ATOM  15578  CD1 TYR C 265     259.871 213.999 233.328  1.00 53.71           C  
ATOM  15579  CD2 TYR C 265     262.121 213.398 233.826  1.00 53.97           C  
ATOM  15580  CE1 TYR C 265     259.824 214.759 234.460  1.00 54.15           C  
ATOM  15581  CE2 TYR C 265     262.088 214.153 234.951  1.00 53.30           C  
ATOM  15582  CZ  TYR C 265     260.941 214.832 235.281  1.00 54.12           C  
ATOM  15583  OH  TYR C 265     260.905 215.586 236.424  1.00 56.02           O  
ATOM  15584  N   TYR C 266     259.607 213.949 229.568  1.00 54.25           N  
ATOM  15585  CA  TYR C 266     258.699 214.915 228.998  1.00 51.24           C  
ATOM  15586  C   TYR C 266     257.323 214.766 229.600  1.00 49.92           C  
ATOM  15587  O   TYR C 266     256.844 213.651 229.795  1.00 52.69           O  
ATOM  15588  CB  TYR C 266     258.656 214.687 227.484  1.00 52.27           C  
ATOM  15589  CG  TYR C 266     260.017 214.671 226.906  1.00 52.04           C  
ATOM  15590  CD1 TYR C 266     260.702 213.465 226.884  1.00 52.29           C  
ATOM  15591  CD2 TYR C 266     260.618 215.830 226.394  1.00 53.52           C  
ATOM  15592  CE1 TYR C 266     261.975 213.409 226.366  1.00 52.69           C  
ATOM  15593  CE2 TYR C 266     261.908 215.739 225.863  1.00 53.14           C  
ATOM  15594  CZ  TYR C 266     262.568 214.537 225.862  1.00 53.45           C  
ATOM  15595  OH  TYR C 266     263.821 214.472 225.347  1.00 52.30           O  
ATOM  15596  N   VAL C 267     256.665 215.881 229.883  1.00 51.82           N  
ATOM  15597  CA  VAL C 267     255.299 215.817 230.388  1.00 50.19           C  
ATOM  15598  C   VAL C 267     254.320 216.626 229.556  1.00 49.95           C  
ATOM  15599  O   VAL C 267     254.474 217.841 229.395  1.00 51.91           O  
ATOM  15600  CB  VAL C 267     255.235 216.306 231.839  1.00 51.70           C  
ATOM  15601  CG1 VAL C 267     253.796 216.285 232.329  1.00 52.57           C  
ATOM  15602  CG2 VAL C 267     256.108 215.406 232.712  1.00 52.24           C  
ATOM  15603  N   GLY C 268     253.288 215.960 229.061  1.00 50.28           N  
ATOM  15604  CA  GLY C 268     252.243 216.612 228.293  1.00 50.51           C  
ATOM  15605  C   GLY C 268     250.913 216.404 228.979  1.00 50.22           C  
ATOM  15606  O   GLY C 268     250.832 215.691 229.976  1.00 52.26           O  
ATOM  15607  N   TYR C 269     249.862 216.990 228.443  1.00 49.99           N  
ATOM  15608  CA  TYR C 269     248.557 216.787 229.046  1.00 50.85           C  
ATOM  15609  C   TYR C 269     247.551 216.351 228.024  1.00 49.81           C  
ATOM  15610  O   TYR C 269     247.582 216.788 226.875  1.00 49.98           O  
ATOM  15611  CB  TYR C 269     248.123 218.025 229.801  1.00 51.33           C  
ATOM  15612  CG  TYR C 269     249.025 218.254 230.970  1.00 52.51           C  
ATOM  15613  CD1 TYR C 269     250.148 219.048 230.848  1.00 53.38           C  
ATOM  15614  CD2 TYR C 269     248.754 217.630 232.159  1.00 53.64           C  
ATOM  15615  CE1 TYR C 269     250.989 219.215 231.924  1.00 53.30           C  
ATOM  15616  CE2 TYR C 269     249.584 217.799 233.220  1.00 54.13           C  
ATOM  15617  CZ  TYR C 269     250.705 218.587 233.112  1.00 54.45           C  
ATOM  15618  OH  TYR C 269     251.548 218.753 234.183  1.00 56.22           O  
ATOM  15619  N   LEU C 270     246.660 215.483 228.459  1.00 50.42           N  
ATOM  15620  CA  LEU C 270     245.685 214.890 227.575  1.00 49.71           C  
ATOM  15621  C   LEU C 270     244.484 215.797 227.426  1.00 49.64           C  
ATOM  15622  O   LEU C 270     244.124 216.519 228.355  1.00 49.91           O  
ATOM  15623  CB  LEU C 270     245.229 213.563 228.157  1.00 50.49           C  
ATOM  15624  CG  LEU C 270     246.313 212.547 228.518  1.00 50.66           C  
ATOM  15625  CD1 LEU C 270     245.638 211.353 229.139  1.00 51.74           C  
ATOM  15626  CD2 LEU C 270     247.102 212.140 227.299  1.00 50.47           C  
ATOM  15627  N   GLN C 271     243.859 215.754 226.259  1.00 49.54           N  
ATOM  15628  CA  GLN C 271     242.666 216.539 226.012  1.00 48.60           C  
ATOM  15629  C   GLN C 271     241.603 215.690 225.318  1.00 49.56           C  
ATOM  15630  O   GLN C 271     241.940 214.775 224.562  1.00 48.31           O  
ATOM  15631  CB  GLN C 271     243.035 217.764 225.178  1.00 48.52           C  
ATOM  15632  CG  GLN C 271     244.000 218.699 225.888  1.00 48.57           C  
ATOM  15633  CD  GLN C 271     244.257 219.964 225.129  1.00 48.05           C  
ATOM  15634  OE1 GLN C 271     244.004 220.046 223.921  1.00 47.92           O  
ATOM  15635  NE2 GLN C 271     244.769 220.971 225.827  1.00 47.96           N  
ATOM  15636  N   PRO C 272     240.316 215.991 225.523  1.00 48.48           N  
ATOM  15637  CA  PRO C 272     239.165 215.288 224.978  1.00 48.45           C  
ATOM  15638  C   PRO C 272     238.941 215.582 223.509  1.00 48.02           C  
ATOM  15639  O   PRO C 272     237.972 216.243 223.133  1.00 48.15           O  
ATOM  15640  CB  PRO C 272     238.029 215.825 225.853  1.00 48.92           C  
ATOM  15641  CG  PRO C 272     238.468 217.223 226.215  1.00 48.43           C  
ATOM  15642  CD  PRO C 272     239.962 217.117 226.410  1.00 48.54           C  
ATOM  15643  N   ARG C 273     239.857 215.095 222.687  1.00 47.66           N  
ATOM  15644  CA  ARG C 273     239.808 215.312 221.255  1.00 46.75           C  
ATOM  15645  C   ARG C 273     239.490 214.022 220.520  1.00 47.71           C  
ATOM  15646  O   ARG C 273     239.794 212.927 221.000  1.00 47.96           O  
ATOM  15647  CB  ARG C 273     241.127 215.874 220.766  1.00 46.88           C  
ATOM  15648  CG  ARG C 273     241.443 217.245 221.299  1.00 47.30           C  
ATOM  15649  CD  ARG C 273     242.762 217.730 220.851  1.00 46.78           C  
ATOM  15650  NE  ARG C 273     243.057 219.035 221.427  1.00 47.50           N  
ATOM  15651  CZ  ARG C 273     242.778 220.225 220.862  1.00 47.69           C  
ATOM  15652  NH1 ARG C 273     242.209 220.291 219.685  1.00 47.02           N  
ATOM  15653  NH2 ARG C 273     243.086 221.329 221.515  1.00 47.45           N  
ATOM  15654  N   THR C 274     238.878 214.166 219.354  1.00 46.62           N  
ATOM  15655  CA  THR C 274     238.542 213.036 218.511  1.00 45.52           C  
ATOM  15656  C   THR C 274     239.717 212.656 217.636  1.00 46.21           C  
ATOM  15657  O   THR C 274     240.412 213.526 217.105  1.00 46.94           O  
ATOM  15658  CB  THR C 274     237.329 213.350 217.618  1.00 46.16           C  
ATOM  15659  OG1 THR C 274     236.212 213.715 218.435  1.00 46.32           O  
ATOM  15660  CG2 THR C 274     236.944 212.131 216.777  1.00 46.29           C  
ATOM  15661  N   PHE C 275     239.954 211.357 217.537  1.00 45.30           N  
ATOM  15662  CA  PHE C 275     240.972 210.797 216.668  1.00 45.30           C  
ATOM  15663  C   PHE C 275     240.427 209.731 215.743  1.00 46.60           C  
ATOM  15664  O   PHE C 275     239.558 208.941 216.119  1.00 46.68           O  
ATOM  15665  CB  PHE C 275     242.122 210.205 217.477  1.00 46.01           C  
ATOM  15666  CG  PHE C 275     243.031 211.215 218.051  1.00 46.18           C  
ATOM  15667  CD1 PHE C 275     242.667 211.998 219.115  1.00 46.70           C  
ATOM  15668  CD2 PHE C 275     244.286 211.377 217.513  1.00 46.37           C  
ATOM  15669  CE1 PHE C 275     243.531 212.931 219.615  1.00 46.46           C  
ATOM  15670  CE2 PHE C 275     245.148 212.300 218.018  1.00 46.31           C  
ATOM  15671  CZ  PHE C 275     244.774 213.082 219.069  1.00 46.81           C  
ATOM  15672  N   LEU C 276     240.989 209.675 214.547  1.00 45.38           N  
ATOM  15673  CA  LEU C 276     240.698 208.581 213.636  1.00 45.06           C  
ATOM  15674  C   LEU C 276     241.855 207.605 213.749  1.00 47.00           C  
ATOM  15675  O   LEU C 276     242.998 207.964 213.478  1.00 45.87           O  
ATOM  15676  CB  LEU C 276     240.561 209.083 212.194  1.00 45.80           C  
ATOM  15677  CG  LEU C 276     240.230 208.039 211.115  1.00 45.39           C  
ATOM  15678  CD1 LEU C 276     238.821 207.494 211.334  1.00 45.11           C  
ATOM  15679  CD2 LEU C 276     240.372 208.687 209.732  1.00 44.31           C  
ATOM  15680  N   LEU C 277     241.582 206.389 214.187  1.00 45.86           N  
ATOM  15681  CA  LEU C 277     242.640 205.415 214.409  1.00 45.66           C  
ATOM  15682  C   LEU C 277     242.656 204.348 213.328  1.00 47.22           C  
ATOM  15683  O   LEU C 277     241.631 203.734 213.029  1.00 44.72           O  
ATOM  15684  CB  LEU C 277     242.443 204.763 215.779  1.00 46.55           C  
ATOM  15685  CG  LEU C 277     242.353 205.729 216.985  1.00 46.62           C  
ATOM  15686  CD1 LEU C 277     242.052 204.925 218.229  1.00 47.99           C  
ATOM  15687  CD2 LEU C 277     243.657 206.501 217.146  1.00 46.79           C  
ATOM  15688  N   LYS C 278     243.826 204.129 212.742  1.00 45.83           N  
ATOM  15689  CA  LYS C 278     243.972 203.134 211.689  1.00 45.49           C  
ATOM  15690  C   LYS C 278     244.462 201.806 212.215  1.00 48.90           C  
ATOM  15691  O   LYS C 278     245.619 201.686 212.633  1.00 46.57           O  
ATOM  15692  CB  LYS C 278     244.939 203.623 210.617  1.00 46.12           C  
ATOM  15693  CG  LYS C 278     245.157 202.666 209.467  1.00 46.07           C  
ATOM  15694  CD  LYS C 278     246.030 203.295 208.403  1.00 46.28           C  
ATOM  15695  CE  LYS C 278     246.243 202.351 207.239  1.00 45.84           C  
ATOM  15696  NZ  LYS C 278     247.111 202.953 206.190  1.00 45.78           N  
ATOM  15697  N   TYR C 279     243.593 200.799 212.145  1.00 46.94           N  
ATOM  15698  CA  TYR C 279     243.919 199.457 212.600  1.00 47.89           C  
ATOM  15699  C   TYR C 279     244.333 198.576 211.435  1.00 48.10           C  
ATOM  15700  O   TYR C 279     243.667 198.540 210.396  1.00 47.76           O  
ATOM  15701  CB  TYR C 279     242.733 198.833 213.321  1.00 48.96           C  
ATOM  15702  CG  TYR C 279     242.469 199.404 214.681  1.00 47.99           C  
ATOM  15703  CD1 TYR C 279     241.706 200.547 214.834  1.00 46.89           C  
ATOM  15704  CD2 TYR C 279     242.980 198.764 215.784  1.00 48.47           C  
ATOM  15705  CE1 TYR C 279     241.468 201.044 216.095  1.00 47.80           C  
ATOM  15706  CE2 TYR C 279     242.738 199.255 217.038  1.00 48.78           C  
ATOM  15707  CZ  TYR C 279     241.986 200.390 217.198  1.00 48.48           C  
ATOM  15708  OH  TYR C 279     241.749 200.879 218.459  1.00 49.08           O  
ATOM  15709  N   ASN C 280     245.415 197.829 211.621  1.00 47.79           N  
ATOM  15710  CA  ASN C 280     245.899 196.918 210.592  1.00 47.77           C  
ATOM  15711  C   ASN C 280     245.261 195.553 210.752  1.00 48.40           C  
ATOM  15712  O   ASN C 280     244.385 195.363 211.592  1.00 47.65           O  
ATOM  15713  CB  ASN C 280     247.410 196.796 210.598  1.00 48.24           C  
ATOM  15714  CG  ASN C 280     247.961 196.095 211.807  1.00 50.44           C  
ATOM  15715  OD1 ASN C 280     247.215 195.584 212.660  1.00 50.53           O  
ATOM  15716  ND2 ASN C 280     249.266 196.032 211.878  1.00 48.98           N  
ATOM  15717  N   GLU C 281     245.691 194.607 209.934  1.00 48.21           N  
ATOM  15718  CA  GLU C 281     245.153 193.247 209.955  1.00 48.95           C  
ATOM  15719  C   GLU C 281     245.358 192.504 211.289  1.00 48.92           C  
ATOM  15720  O   GLU C 281     244.589 191.595 211.610  1.00 49.08           O  
ATOM  15721  CB  GLU C 281     245.790 192.402 208.844  1.00 48.35           C  
ATOM  15722  N   ASN C 282     246.405 192.877 212.044  1.00 48.39           N  
ATOM  15723  CA  ASN C 282     246.817 192.225 213.290  1.00 49.13           C  
ATOM  15724  C   ASN C 282     246.221 192.877 214.543  1.00 49.39           C  
ATOM  15725  O   ASN C 282     246.561 192.481 215.663  1.00 50.28           O  
ATOM  15726  CB  ASN C 282     248.345 192.187 213.385  1.00 49.20           C  
ATOM  15727  CG  ASN C 282     249.017 191.237 212.375  1.00 49.82           C  
ATOM  15728  OD1 ASN C 282     248.404 190.813 211.381  1.00 49.84           O  
ATOM  15729  ND2 ASN C 282     250.276 190.909 212.635  1.00 50.69           N  
ATOM  15730  N   GLY C 283     245.323 193.872 214.397  1.00 49.99           N  
ATOM  15731  CA  GLY C 283     244.668 194.518 215.538  1.00 50.89           C  
ATOM  15732  C   GLY C 283     245.439 195.673 216.157  1.00 50.25           C  
ATOM  15733  O   GLY C 283     245.043 196.182 217.211  1.00 50.71           O  
ATOM  15734  N   THR C 284     246.542 196.086 215.537  1.00 49.70           N  
ATOM  15735  CA  THR C 284     247.319 197.169 216.114  1.00 49.51           C  
ATOM  15736  C   THR C 284     246.969 198.479 215.458  1.00 50.19           C  
ATOM  15737  O   THR C 284     246.467 198.503 214.337  1.00 41.50           O  
ATOM  15738  CB  THR C 284     248.830 196.939 215.953  1.00 49.42           C  
ATOM  15739  OG1 THR C 284     249.171 196.956 214.574  1.00 48.99           O  
ATOM  15740  CG2 THR C 284     249.211 195.612 216.533  1.00 50.30           C  
ATOM  15741  N   ILE C 285     247.309 199.574 216.118  1.00 49.98           N  
ATOM  15742  CA  ILE C 285     247.114 200.882 215.531  1.00 48.28           C  
ATOM  15743  C   ILE C 285     248.411 201.272 214.860  1.00 47.73           C  
ATOM  15744  O   ILE C 285     249.460 201.303 215.501  1.00 48.25           O  
ATOM  15745  CB  ILE C 285     246.729 201.923 216.593  1.00 48.13           C  
ATOM  15746  CG1 ILE C 285     245.439 201.509 217.279  1.00 48.78           C  
ATOM  15747  CG2 ILE C 285     246.548 203.284 215.939  1.00 46.54           C  
ATOM  15748  CD1 ILE C 285     245.136 202.281 218.552  1.00 48.25           C  
ATOM  15749  N   THR C 286     248.347 201.532 213.565  1.00 47.92           N  
ATOM  15750  CA  THR C 286     249.543 201.854 212.810  1.00 48.03           C  
ATOM  15751  C   THR C 286     249.599 203.327 212.462  1.00 47.15           C  
ATOM  15752  O   THR C 286     250.664 203.845 212.129  1.00 47.25           O  
ATOM  15753  CB  THR C 286     249.636 201.008 211.538  1.00 48.28           C  
ATOM  15754  OG1 THR C 286     248.516 201.282 210.695  1.00 47.53           O  
ATOM  15755  CG2 THR C 286     249.636 199.543 211.914  1.00 48.78           C  
ATOM  15756  N   ASP C 287     248.463 204.008 212.556  1.00 45.79           N  
ATOM  15757  CA  ASP C 287     248.451 205.446 212.295  1.00 47.65           C  
ATOM  15758  C   ASP C 287     247.301 206.126 213.038  1.00 47.53           C  
ATOM  15759  O   ASP C 287     246.480 205.454 213.668  1.00 46.49           O  
ATOM  15760  CB  ASP C 287     248.345 205.682 210.782  1.00 46.16           C  
ATOM  15761  CG  ASP C 287     248.944 206.996 210.295  1.00 46.25           C  
ATOM  15762  OD1 ASP C 287     249.131 207.878 211.095  1.00 46.03           O  
ATOM  15763  OD2 ASP C 287     249.195 207.105 209.119  1.00 46.54           O  
ATOM  15764  N   ALA C 288     247.232 207.452 212.949  1.00 46.01           N  
ATOM  15765  CA  ALA C 288     246.150 208.200 213.580  1.00 45.19           C  
ATOM  15766  C   ALA C 288     246.017 209.614 213.007  1.00 45.63           C  
ATOM  15767  O   ALA C 288     247.009 210.242 212.638  1.00 45.97           O  
ATOM  15768  CB  ALA C 288     246.378 208.275 215.078  1.00 46.13           C  
ATOM  15769  N   VAL C 289     244.798 210.148 213.028  1.00 45.32           N  
ATOM  15770  CA  VAL C 289     244.562 211.539 212.649  1.00 45.13           C  
ATOM  15771  C   VAL C 289     243.991 212.327 213.805  1.00 45.87           C  
ATOM  15772  O   VAL C 289     242.966 211.954 214.371  1.00 45.43           O  
ATOM  15773  CB  VAL C 289     243.560 211.651 211.479  1.00 44.94           C  
ATOM  15774  CG1 VAL C 289     243.314 213.107 211.118  1.00 44.09           C  
ATOM  15775  CG2 VAL C 289     244.069 210.900 210.302  1.00 44.78           C  
ATOM  15776  N   ASP C 290     244.626 213.445 214.126  1.00 45.25           N  
ATOM  15777  CA  ASP C 290     244.096 214.345 215.141  1.00 45.11           C  
ATOM  15778  C   ASP C 290     243.097 215.254 214.443  1.00 44.47           C  
ATOM  15779  O   ASP C 290     243.494 216.111 213.648  1.00 44.79           O  
ATOM  15780  CB  ASP C 290     245.208 215.153 215.800  1.00 45.54           C  
ATOM  15781  CG  ASP C 290     244.694 216.104 216.870  1.00 45.99           C  
ATOM  15782  OD1 ASP C 290     243.567 216.563 216.752  1.00 45.01           O  
ATOM  15783  OD2 ASP C 290     245.423 216.358 217.812  1.00 45.72           O  
ATOM  15784  N   CYS C 291     241.803 215.030 214.693  1.00 44.23           N  
ATOM  15785  CA  CYS C 291     240.701 215.631 213.942  1.00 43.81           C  
ATOM  15786  C   CYS C 291     240.587 217.151 214.124  1.00 44.24           C  
ATOM  15787  O   CYS C 291     239.784 217.787 213.437  1.00 43.81           O  
ATOM  15788  CB  CYS C 291     239.371 214.979 214.343  1.00 45.25           C  
ATOM  15789  SG  CYS C 291     239.281 213.193 214.023  1.00 46.46           S  
ATOM  15790  N   ALA C 292     241.346 217.747 215.065  1.00 44.30           N  
ATOM  15791  CA  ALA C 292     241.314 219.189 215.327  1.00 43.79           C  
ATOM  15792  C   ALA C 292     242.676 219.829 215.113  1.00 43.92           C  
ATOM  15793  O   ALA C 292     242.919 220.938 215.587  1.00 43.40           O  
ATOM  15794  CB  ALA C 292     240.844 219.432 216.744  1.00 44.79           C  
ATOM  15795  N   LEU C 293     243.566 219.142 214.410  1.00 43.69           N  
ATOM  15796  CA  LEU C 293     244.894 219.685 214.160  1.00 43.38           C  
ATOM  15797  C   LEU C 293     244.898 220.769 213.083  1.00 43.18           C  
ATOM  15798  O   LEU C 293     245.477 221.838 213.275  1.00 43.62           O  
ATOM  15799  CB  LEU C 293     245.838 218.553 213.757  1.00 43.65           C  
ATOM  15800  CG  LEU C 293     247.288 218.929 213.413  1.00 44.05           C  
ATOM  15801  CD1 LEU C 293     247.969 219.564 214.621  1.00 44.68           C  
ATOM  15802  CD2 LEU C 293     248.016 217.672 212.977  1.00 44.67           C  
ATOM  15803  N   ASP C 294     244.270 220.490 211.946  1.00 43.15           N  
ATOM  15804  CA  ASP C 294     244.210 221.446 210.846  1.00 42.40           C  
ATOM  15805  C   ASP C 294     243.026 221.053 209.936  1.00 42.77           C  
ATOM  15806  O   ASP C 294     242.423 220.004 210.170  1.00 39.49           O  
ATOM  15807  CB  ASP C 294     245.570 221.471 210.115  1.00 42.56           C  
ATOM  15808  CG  ASP C 294     245.907 220.208 209.364  1.00 42.71           C  
ATOM  15809  OD1 ASP C 294     245.022 219.634 208.748  1.00 41.97           O  
ATOM  15810  OD2 ASP C 294     247.055 219.823 209.387  1.00 43.19           O  
ATOM  15811  N   PRO C 295     242.661 221.856 208.917  1.00 41.75           N  
ATOM  15812  CA  PRO C 295     241.563 221.621 207.988  1.00 40.89           C  
ATOM  15813  C   PRO C 295     241.680 220.351 207.151  1.00 42.25           C  
ATOM  15814  O   PRO C 295     240.670 219.836 206.669  1.00 41.85           O  
ATOM  15815  CB  PRO C 295     241.622 222.861 207.096  1.00 40.95           C  
ATOM  15816  CG  PRO C 295     242.324 223.900 207.925  1.00 41.11           C  
ATOM  15817  CD  PRO C 295     243.343 223.136 208.699  1.00 41.19           C  
ATOM  15818  N   LEU C 296     242.882 219.824 206.970  1.00 40.73           N  
ATOM  15819  CA  LEU C 296     242.984 218.616 206.174  1.00 40.81           C  
ATOM  15820  C   LEU C 296     242.653 217.437 207.051  1.00 42.59           C  
ATOM  15821  O   LEU C 296     241.995 216.492 206.616  1.00 42.24           O  
ATOM  15822  CB  LEU C 296     244.366 218.461 205.547  1.00 41.22           C  
ATOM  15823  CG  LEU C 296     244.592 217.161 204.738  1.00 41.66           C  
ATOM  15824  CD1 LEU C 296     243.572 217.029 203.605  1.00 41.70           C  
ATOM  15825  CD2 LEU C 296     245.997 217.179 204.176  1.00 41.86           C  
ATOM  15826  N   SER C 297     243.092 217.506 208.296  1.00 42.23           N  
ATOM  15827  CA  SER C 297     242.793 216.459 209.245  1.00 40.56           C  
ATOM  15828  C   SER C 297     241.294 216.422 209.488  1.00 45.94           C  
ATOM  15829  O   SER C 297     240.705 215.345 209.594  1.00 41.57           O  
ATOM  15830  CB  SER C 297     243.539 216.692 210.531  1.00 42.68           C  
ATOM  15831  OG  SER C 297     244.920 216.575 210.334  1.00 42.31           O  
ATOM  15832  N   GLU C 298     240.661 217.595 209.519  1.00 41.24           N  
ATOM  15833  CA  GLU C 298     239.219 217.651 209.702  1.00 41.46           C  
ATOM  15834  C   GLU C 298     238.533 216.940 208.545  1.00 40.97           C  
ATOM  15835  O   GLU C 298     237.593 216.166 208.752  1.00 42.22           O  
ATOM  15836  CB  GLU C 298     238.738 219.103 209.775  1.00 41.65           C  
ATOM  15837  CG  GLU C 298     239.127 219.845 211.052  1.00 42.05           C  
ATOM  15838  CD  GLU C 298     238.837 221.330 210.999  1.00 41.98           C  
ATOM  15839  OE1 GLU C 298     238.548 221.824 209.937  1.00 41.64           O  
ATOM  15840  OE2 GLU C 298     238.911 221.969 212.022  1.00 41.79           O  
ATOM  15841  N   THR C 299     239.041 217.153 207.330  1.00 40.01           N  
ATOM  15842  CA  THR C 299     238.493 216.497 206.154  1.00 40.66           C  
ATOM  15843  C   THR C 299     238.660 214.993 206.244  1.00 43.21           C  
ATOM  15844  O   THR C 299     237.719 214.244 205.978  1.00 42.82           O  
ATOM  15845  CB  THR C 299     239.169 217.006 204.869  1.00 40.97           C  
ATOM  15846  OG1 THR C 299     238.958 218.409 204.738  1.00 40.70           O  
ATOM  15847  CG2 THR C 299     238.584 216.307 203.656  1.00 41.36           C  
ATOM  15848  N   LYS C 300     239.848 214.542 206.632  1.00 41.33           N  
ATOM  15849  CA  LYS C 300     240.102 213.109 206.740  1.00 40.96           C  
ATOM  15850  C   LYS C 300     239.156 212.424 207.729  1.00 44.87           C  
ATOM  15851  O   LYS C 300     238.622 211.352 207.428  1.00 42.56           O  
ATOM  15852  CB  LYS C 300     241.556 212.856 207.149  1.00 41.84           C  
ATOM  15853  CG  LYS C 300     242.580 213.137 206.066  1.00 41.45           C  
ATOM  15854  CD  LYS C 300     243.983 212.895 206.577  1.00 41.52           C  
ATOM  15855  CE  LYS C 300     245.018 213.148 205.504  1.00 42.71           C  
ATOM  15856  NZ  LYS C 300     246.394 212.888 205.998  1.00 42.91           N  
ATOM  15857  N   CYS C 301     238.924 213.044 208.901  1.00 41.38           N  
ATOM  15858  CA  CYS C 301     238.025 212.504 209.927  1.00 43.17           C  
ATOM  15859  C   CYS C 301     236.554 212.500 209.477  1.00 42.50           C  
ATOM  15860  O   CYS C 301     235.831 211.539 209.755  1.00 43.30           O  
ATOM  15861  CB  CYS C 301     238.187 213.275 211.248  1.00 43.88           C  
ATOM  15862  SG  CYS C 301     239.769 212.966 212.076  1.00 45.25           S  
ATOM  15863  N   THR C 302     236.128 213.548 208.747  1.00 42.98           N  
ATOM  15864  CA  THR C 302     234.775 213.680 208.194  1.00 42.27           C  
ATOM  15865  C   THR C 302     234.505 212.588 207.163  1.00 42.27           C  
ATOM  15866  O   THR C 302     233.438 211.975 207.147  1.00 42.70           O  
ATOM  15867  CB  THR C 302     234.600 215.061 207.537  1.00 42.16           C  
ATOM  15868  OG1 THR C 302     234.792 216.079 208.521  1.00 41.72           O  
ATOM  15869  CG2 THR C 302     233.212 215.205 206.936  1.00 41.59           C  
ATOM  15870  N   LEU C 303     235.499 212.340 206.316  1.00 42.26           N  
ATOM  15871  CA  LEU C 303     235.420 211.319 205.283  1.00 42.23           C  
ATOM  15872  C   LEU C 303     235.774 209.945 205.828  1.00 42.45           C  
ATOM  15873  O   LEU C 303     235.486 208.928 205.198  1.00 42.77           O  
ATOM  15874  CB  LEU C 303     236.369 211.667 204.135  1.00 42.23           C  
ATOM  15875  CG  LEU C 303     235.815 212.580 203.034  1.00 42.01           C  
ATOM  15876  CD1 LEU C 303     235.268 213.876 203.631  1.00 42.07           C  
ATOM  15877  CD2 LEU C 303     236.926 212.891 202.076  1.00 42.00           C  
ATOM  15878  N   LYS C 304     236.400 209.922 207.001  1.00 43.05           N  
ATOM  15879  CA  LYS C 304     236.837 208.702 207.654  1.00 43.16           C  
ATOM  15880  C   LYS C 304     237.807 207.938 206.780  1.00 42.90           C  
ATOM  15881  O   LYS C 304     237.675 206.730 206.594  1.00 43.53           O  
ATOM  15882  CB  LYS C 304     235.638 207.834 208.020  1.00 43.19           C  
ATOM  15883  CG  LYS C 304     234.656 208.526 208.940  1.00 43.49           C  
ATOM  15884  CD  LYS C 304     233.492 207.636 209.282  1.00 44.65           C  
ATOM  15885  CE  LYS C 304     232.493 208.377 210.140  1.00 44.67           C  
ATOM  15886  NZ  LYS C 304     231.299 207.553 210.429  1.00 45.29           N  
ATOM  15887  N   SER C 305     238.783 208.659 206.241  1.00 42.71           N  
ATOM  15888  CA  SER C 305     239.809 208.068 205.399  1.00 42.81           C  
ATOM  15889  C   SER C 305     241.129 208.808 205.552  1.00 42.47           C  
ATOM  15890  O   SER C 305     241.157 210.028 205.670  1.00 43.16           O  
ATOM  15891  CB  SER C 305     239.350 208.047 203.959  1.00 43.02           C  
ATOM  15892  OG  SER C 305     240.322 207.483 203.122  1.00 43.22           O  
ATOM  15893  N   PHE C 306     242.229 208.063 205.560  1.00 43.24           N  
ATOM  15894  CA  PHE C 306     243.560 208.654 205.698  1.00 43.30           C  
ATOM  15895  C   PHE C 306     244.035 209.334 204.434  1.00 43.10           C  
ATOM  15896  O   PHE C 306     244.983 210.118 204.463  1.00 42.95           O  
ATOM  15897  CB  PHE C 306     244.565 207.620 206.178  1.00 43.71           C  
ATOM  15898  CG  PHE C 306     244.529 207.473 207.649  1.00 44.64           C  
ATOM  15899  CD1 PHE C 306     243.457 206.908 208.272  1.00 44.95           C  
ATOM  15900  CD2 PHE C 306     245.583 207.913 208.417  1.00 45.04           C  
ATOM  15901  CE1 PHE C 306     243.422 206.795 209.630  1.00 45.70           C  
ATOM  15902  CE2 PHE C 306     245.552 207.791 209.772  1.00 45.65           C  
ATOM  15903  CZ  PHE C 306     244.462 207.231 210.379  1.00 43.97           C  
ATOM  15904  N   THR C 307     243.392 209.018 203.327  1.00 42.92           N  
ATOM  15905  CA  THR C 307     243.674 209.684 202.071  1.00 42.87           C  
ATOM  15906  C   THR C 307     242.366 210.208 201.532  1.00 43.06           C  
ATOM  15907  O   THR C 307     241.325 209.570 201.690  1.00 42.87           O  
ATOM  15908  CB  THR C 307     244.314 208.738 201.044  1.00 43.14           C  
ATOM  15909  OG1 THR C 307     243.417 207.654 200.772  1.00 43.23           O  
ATOM  15910  CG2 THR C 307     245.623 208.187 201.580  1.00 42.92           C  
ATOM  15911  N   VAL C 308     242.397 211.348 200.873  1.00 43.07           N  
ATOM  15912  CA  VAL C 308     241.161 211.863 200.326  1.00 43.02           C  
ATOM  15913  C   VAL C 308     241.327 212.252 198.870  1.00 43.11           C  
ATOM  15914  O   VAL C 308     242.408 212.670 198.438  1.00 43.08           O  
ATOM  15915  CB  VAL C 308     240.650 213.042 201.173  1.00 42.55           C  
ATOM  15916  CG1 VAL C 308     240.358 212.574 202.608  1.00 42.45           C  
ATOM  15917  CG2 VAL C 308     241.660 214.114 201.204  1.00 42.29           C  
ATOM  15918  N   GLU C 309     240.238 212.128 198.131  1.00 43.29           N  
ATOM  15919  CA  GLU C 309     240.202 212.456 196.722  1.00 43.42           C  
ATOM  15920  C   GLU C 309     240.055 213.943 196.545  1.00 42.11           C  
ATOM  15921  O   GLU C 309     239.593 214.636 197.449  1.00 42.09           O  
ATOM  15922  CB  GLU C 309     239.058 211.720 196.036  1.00 44.01           C  
ATOM  15923  CG  GLU C 309     239.211 210.207 196.041  1.00 45.33           C  
ATOM  15924  CD  GLU C 309     238.096 209.508 195.325  1.00 48.01           C  
ATOM  15925  OE1 GLU C 309     237.178 210.173 194.910  1.00 46.60           O  
ATOM  15926  OE2 GLU C 309     238.160 208.309 195.189  1.00 47.64           O  
ATOM  15927  N   LYS C 310     240.450 214.440 195.388  1.00 42.23           N  
ATOM  15928  CA  LYS C 310     240.331 215.859 195.145  1.00 41.20           C  
ATOM  15929  C   LYS C 310     238.877 216.279 195.115  1.00 40.68           C  
ATOM  15930  O   LYS C 310     238.026 215.579 194.563  1.00 41.37           O  
ATOM  15931  CB  LYS C 310     240.981 216.241 193.827  1.00 41.28           C  
ATOM  15932  CG  LYS C 310     240.212 215.799 192.593  1.00 41.49           C  
ATOM  15933  CD  LYS C 310     241.034 215.990 191.331  1.00 41.41           C  
ATOM  15934  CE  LYS C 310     241.258 217.460 191.032  1.00 39.70           C  
ATOM  15935  NZ  LYS C 310     241.881 217.662 189.712  1.00 39.44           N  
ATOM  15936  N   GLY C 311     238.606 217.446 195.668  1.00 40.27           N  
ATOM  15937  CA  GLY C 311     237.264 218.000 195.664  1.00 39.81           C  
ATOM  15938  C   GLY C 311     237.052 218.933 196.840  1.00 39.43           C  
ATOM  15939  O   GLY C 311     237.979 219.224 197.595  1.00 39.77           O  
ATOM  15940  N   ILE C 312     235.834 219.427 196.980  1.00 38.89           N  
ATOM  15941  CA  ILE C 312     235.515 220.330 198.072  1.00 38.74           C  
ATOM  15942  C   ILE C 312     234.565 219.630 199.026  1.00 38.99           C  
ATOM  15943  O   ILE C 312     233.535 219.104 198.607  1.00 39.40           O  
ATOM  15944  CB  ILE C 312     234.924 221.655 197.536  1.00 38.22           C  
ATOM  15945  CG1 ILE C 312     234.652 222.617 198.696  1.00 38.59           C  
ATOM  15946  CG2 ILE C 312     233.666 221.402 196.710  1.00 38.82           C  
ATOM  15947  CD1 ILE C 312     234.382 224.065 198.271  1.00 37.86           C  
ATOM  15948  N   TYR C 313     234.913 219.609 200.305  1.00 38.98           N  
ATOM  15949  CA  TYR C 313     234.078 218.919 201.280  1.00 38.72           C  
ATOM  15950  C   TYR C 313     233.681 219.819 202.430  1.00 38.71           C  
ATOM  15951  O   TYR C 313     234.505 220.571 202.941  1.00 39.52           O  
ATOM  15952  CB  TYR C 313     234.828 217.720 201.847  1.00 39.18           C  
ATOM  15953  CG  TYR C 313     235.254 216.736 200.816  1.00 39.73           C  
ATOM  15954  CD1 TYR C 313     236.530 216.797 200.285  1.00 39.93           C  
ATOM  15955  CD2 TYR C 313     234.375 215.777 200.393  1.00 40.66           C  
ATOM  15956  CE1 TYR C 313     236.919 215.885 199.334  1.00 40.26           C  
ATOM  15957  CE2 TYR C 313     234.758 214.869 199.445  1.00 41.11           C  
ATOM  15958  CZ  TYR C 313     236.021 214.916 198.917  1.00 40.84           C  
ATOM  15959  OH  TYR C 313     236.388 213.998 197.974  1.00 41.78           O  
ATOM  15960  N   GLN C 314     232.441 219.703 202.887  1.00 38.52           N  
ATOM  15961  CA  GLN C 314     232.023 220.460 204.060  1.00 38.28           C  
ATOM  15962  C   GLN C 314     232.365 219.661 205.297  1.00 38.86           C  
ATOM  15963  O   GLN C 314     231.944 218.514 205.428  1.00 39.41           O  
ATOM  15964  CB  GLN C 314     230.538 220.787 204.014  1.00 38.13           C  
ATOM  15965  CG  GLN C 314     230.071 221.622 205.184  1.00 38.21           C  
ATOM  15966  CD  GLN C 314     228.647 222.052 205.033  1.00 37.85           C  
ATOM  15967  OE1 GLN C 314     228.321 222.877 204.169  1.00 36.96           O  
ATOM  15968  NE2 GLN C 314     227.773 221.500 205.868  1.00 35.97           N  
ATOM  15969  N   THR C 315     233.159 220.249 206.182  1.00 38.80           N  
ATOM  15970  CA  THR C 315     233.652 219.514 207.339  1.00 39.34           C  
ATOM  15971  C   THR C 315     233.214 220.076 208.679  1.00 39.47           C  
ATOM  15972  O   THR C 315     233.181 219.354 209.677  1.00 39.71           O  
ATOM  15973  CB  THR C 315     235.183 219.494 207.323  1.00 40.12           C  
ATOM  15974  OG1 THR C 315     235.672 220.836 207.437  1.00 39.61           O  
ATOM  15975  CG2 THR C 315     235.703 218.886 206.041  1.00 40.20           C  
ATOM  15976  N   SER C 316     232.891 221.358 208.728  1.00 39.07           N  
ATOM  15977  CA  SER C 316     232.578 221.950 210.022  1.00 39.33           C  
ATOM  15978  C   SER C 316     231.702 223.179 209.910  1.00 39.20           C  
ATOM  15979  O   SER C 316     231.107 223.443 208.862  1.00 39.91           O  
ATOM  15980  CB  SER C 316     233.858 222.305 210.751  1.00 39.45           C  
ATOM  15981  OG  SER C 316     233.604 222.571 212.103  1.00 39.42           O  
ATOM  15982  N   ASN C 317     231.604 223.906 211.017  1.00 39.24           N  
ATOM  15983  CA  ASN C 317     230.821 225.125 211.107  1.00 39.16           C  
ATOM  15984  C   ASN C 317     231.573 226.187 211.886  1.00 39.62           C  
ATOM  15985  O   ASN C 317     231.997 225.968 213.020  1.00 40.13           O  
ATOM  15986  CB  ASN C 317     229.467 224.867 211.722  1.00 39.18           C  
ATOM  15987  CG  ASN C 317     228.585 224.051 210.834  1.00 38.40           C  
ATOM  15988  OD1 ASN C 317     228.079 224.545 209.820  1.00 38.02           O  
ATOM  15989  ND2 ASN C 317     228.387 222.810 211.186  1.00 37.70           N  
ATOM  15990  N   PHE C 318     231.754 227.326 211.251  1.00 39.77           N  
ATOM  15991  CA  PHE C 318     232.436 228.464 211.821  1.00 40.32           C  
ATOM  15992  C   PHE C 318     231.467 229.274 212.625  1.00 42.25           C  
ATOM  15993  O   PHE C 318     230.354 229.538 212.170  1.00 42.36           O  
ATOM  15994  CB  PHE C 318     233.021 229.327 210.716  1.00 40.61           C  
ATOM  15995  CG  PHE C 318     233.555 230.634 211.162  1.00 41.26           C  
ATOM  15996  CD1 PHE C 318     234.738 230.723 211.861  1.00 41.78           C  
ATOM  15997  CD2 PHE C 318     232.869 231.797 210.864  1.00 41.04           C  
ATOM  15998  CE1 PHE C 318     235.224 231.947 212.257  1.00 41.93           C  
ATOM  15999  CE2 PHE C 318     233.352 233.018 211.257  1.00 41.37           C  
ATOM  16000  CZ  PHE C 318     234.531 233.093 211.955  1.00 41.99           C  
ATOM  16001  N   ARG C 319     231.871 229.657 213.824  1.00 41.19           N  
ATOM  16002  CA  ARG C 319     231.033 230.497 214.653  1.00 41.53           C  
ATOM  16003  C   ARG C 319     231.871 231.530 215.370  1.00 42.50           C  
ATOM  16004  O   ARG C 319     232.841 231.185 216.051  1.00 43.23           O  
ATOM  16005  CB  ARG C 319     230.276 229.660 215.672  1.00 41.49           C  
ATOM  16006  CG  ARG C 319     229.379 228.600 215.068  1.00 41.05           C  
ATOM  16007  CD  ARG C 319     228.552 227.895 216.082  1.00 41.05           C  
ATOM  16008  NE  ARG C 319     227.575 228.788 216.689  1.00 39.98           N  
ATOM  16009  CZ  ARG C 319     226.416 229.158 216.113  1.00 39.78           C  
ATOM  16010  NH1 ARG C 319     226.104 228.720 214.918  1.00 39.77           N  
ATOM  16011  NH2 ARG C 319     225.600 229.966 216.754  1.00 39.21           N  
ATOM  16012  N   VAL C 320     231.472 232.787 215.262  1.00 42.79           N  
ATOM  16013  CA  VAL C 320     232.156 233.835 215.990  1.00 44.27           C  
ATOM  16014  C   VAL C 320     231.775 233.719 217.450  1.00 44.45           C  
ATOM  16015  O   VAL C 320     230.598 233.599 217.784  1.00 45.53           O  
ATOM  16016  CB  VAL C 320     231.799 235.221 215.431  1.00 44.41           C  
ATOM  16017  CG1 VAL C 320     232.418 236.315 216.287  1.00 45.52           C  
ATOM  16018  CG2 VAL C 320     232.303 235.328 214.010  1.00 42.85           C  
ATOM  16019  N   GLN C 321     232.774 233.710 218.316  1.00 45.62           N  
ATOM  16020  CA  GLN C 321     232.530 233.524 219.732  1.00 45.68           C  
ATOM  16021  C   GLN C 321     232.350 234.848 220.450  1.00 46.88           C  
ATOM  16022  O   GLN C 321     232.924 235.853 220.030  1.00 46.72           O  
ATOM  16023  CB  GLN C 321     233.697 232.754 220.349  1.00 46.14           C  
ATOM  16024  CG  GLN C 321     233.890 231.406 219.743  1.00 45.58           C  
ATOM  16025  CD  GLN C 321     232.668 230.567 219.896  1.00 45.51           C  
ATOM  16026  OE1 GLN C 321     232.195 230.328 221.011  1.00 46.21           O  
ATOM  16027  NE2 GLN C 321     232.128 230.119 218.778  1.00 44.64           N  
ATOM  16028  N   PRO C 322     231.570 234.871 221.534  1.00 46.53           N  
ATOM  16029  CA  PRO C 322     231.387 236.001 222.404  1.00 46.96           C  
ATOM  16030  C   PRO C 322     232.678 236.291 223.126  1.00 47.96           C  
ATOM  16031  O   PRO C 322     233.387 235.370 223.533  1.00 48.15           O  
ATOM  16032  CB  PRO C 322     230.277 235.532 223.342  1.00 49.16           C  
ATOM  16033  CG  PRO C 322     230.358 234.021 223.312  1.00 47.27           C  
ATOM  16034  CD  PRO C 322     230.814 233.673 221.923  1.00 46.74           C  
ATOM  16035  N   THR C 323     232.965 237.567 223.312  1.00 47.94           N  
ATOM  16036  CA  THR C 323     234.177 237.968 224.000  1.00 48.97           C  
ATOM  16037  C   THR C 323     233.883 238.564 225.363  1.00 49.16           C  
ATOM  16038  O   THR C 323     234.739 238.543 226.248  1.00 49.67           O  
ATOM  16039  CB  THR C 323     234.950 238.978 223.149  1.00 49.59           C  
ATOM  16040  OG1 THR C 323     234.139 240.142 222.936  1.00 49.60           O  
ATOM  16041  CG2 THR C 323     235.321 238.367 221.808  1.00 49.70           C  
ATOM  16042  N   GLU C 324     232.663 239.056 225.543  1.00 48.97           N  
ATOM  16043  CA  GLU C 324     232.284 239.682 226.808  1.00 49.40           C  
ATOM  16044  C   GLU C 324     230.998 239.078 227.352  1.00 49.89           C  
ATOM  16045  O   GLU C 324     230.391 238.211 226.720  1.00 50.42           O  
ATOM  16046  CB  GLU C 324     232.105 241.198 226.639  1.00 49.76           C  
ATOM  16047  N   SER C 325     230.592 239.543 228.525  1.00 50.31           N  
ATOM  16048  CA  SER C 325     229.355 239.104 229.160  1.00 50.42           C  
ATOM  16049  C   SER C 325     228.647 240.297 229.773  1.00 50.68           C  
ATOM  16050  O   SER C 325     229.229 241.027 230.576  1.00 51.80           O  
ATOM  16051  CB  SER C 325     229.640 238.064 230.224  1.00 50.58           C  
ATOM  16052  OG  SER C 325     228.464 237.674 230.874  1.00 51.24           O  
ATOM  16053  N   ILE C 326     227.411 240.520 229.358  1.00 51.10           N  
ATOM  16054  CA  ILE C 326     226.653 241.675 229.800  1.00 51.13           C  
ATOM  16055  C   ILE C 326     225.448 241.304 230.619  1.00 52.61           C  
ATOM  16056  O   ILE C 326     224.538 240.623 230.143  1.00 52.86           O  
ATOM  16057  CB  ILE C 326     226.196 242.513 228.606  1.00 51.71           C  
ATOM  16058  CG1 ILE C 326     227.415 243.013 227.872  1.00 51.48           C  
ATOM  16059  CG2 ILE C 326     225.283 243.661 229.067  1.00 52.25           C  
ATOM  16060  CD1 ILE C 326     227.098 243.639 226.581  1.00 51.80           C  
ATOM  16061  N   VAL C 327     225.417 241.808 231.835  1.00 52.74           N  
ATOM  16062  CA  VAL C 327     224.303 241.538 232.718  1.00 52.75           C  
ATOM  16063  C   VAL C 327     223.542 242.813 233.018  1.00 54.74           C  
ATOM  16064  O   VAL C 327     224.081 243.767 233.575  1.00 55.43           O  
ATOM  16065  CB  VAL C 327     224.803 240.892 234.015  1.00 54.60           C  
ATOM  16066  CG1 VAL C 327     223.662 240.642 234.933  1.00 54.77           C  
ATOM  16067  CG2 VAL C 327     225.510 239.596 233.684  1.00 54.46           C  
ATOM  16068  N   ARG C 328     222.280 242.842 232.634  1.00 53.15           N  
ATOM  16069  CA  ARG C 328     221.485 244.034 232.834  1.00 53.70           C  
ATOM  16070  C   ARG C 328     220.218 243.758 233.628  1.00 56.07           C  
ATOM  16071  O   ARG C 328     219.402 242.908 233.264  1.00 54.31           O  
ATOM  16072  CB  ARG C 328     221.100 244.608 231.489  1.00 53.67           C  
ATOM  16073  CG  ARG C 328     222.246 245.030 230.589  1.00 52.30           C  
ATOM  16074  CD  ARG C 328     222.398 246.500 230.485  1.00 52.92           C  
ATOM  16075  NE  ARG C 328     223.426 247.044 231.333  1.00 53.65           N  
ATOM  16076  CZ  ARG C 328     223.756 248.352 231.353  1.00 53.92           C  
ATOM  16077  NH1 ARG C 328     223.132 249.202 230.571  1.00 53.36           N  
ATOM  16078  NH2 ARG C 328     224.705 248.781 232.150  1.00 54.18           N  
ATOM  16079  N   PHE C 329     220.040 244.534 234.678  1.00 55.59           N  
ATOM  16080  CA  PHE C 329     218.856 244.502 235.519  1.00 55.68           C  
ATOM  16081  C   PHE C 329     218.528 245.936 235.892  1.00 56.88           C  
ATOM  16082  O   PHE C 329     219.435 246.763 235.937  1.00 57.56           O  
ATOM  16083  CB  PHE C 329     219.089 243.644 236.771  1.00 56.90           C  
ATOM  16084  CG  PHE C 329     219.253 242.164 236.515  1.00 56.68           C  
ATOM  16085  CD1 PHE C 329     220.485 241.576 236.427  1.00 55.97           C  
ATOM  16086  CD2 PHE C 329     218.143 241.361 236.376  1.00 57.01           C  
ATOM  16087  CE1 PHE C 329     220.591 240.212 236.209  1.00 55.55           C  
ATOM  16088  CE2 PHE C 329     218.254 240.008 236.163  1.00 55.90           C  
ATOM  16089  CZ  PHE C 329     219.477 239.438 236.080  1.00 55.29           C  
ATOM  16090  N   PRO C 330     217.274 246.275 236.186  1.00 56.30           N  
ATOM  16091  CA  PRO C 330     216.869 247.594 236.605  1.00 57.69           C  
ATOM  16092  C   PRO C 330     217.614 247.930 237.886  1.00 59.91           C  
ATOM  16093  O   PRO C 330     217.822 247.053 238.729  1.00 59.47           O  
ATOM  16094  CB  PRO C 330     215.357 247.431 236.812  1.00 58.60           C  
ATOM  16095  CG  PRO C 330     215.151 245.936 236.984  1.00 59.11           C  
ATOM  16096  CD  PRO C 330     216.192 245.306 236.103  1.00 57.81           C  
ATOM  16097  N   ASN C 331     217.999 249.205 238.043  1.00 59.35           N  
ATOM  16098  CA  ASN C 331     218.792 249.672 239.180  1.00 59.50           C  
ATOM  16099  C   ASN C 331     217.911 249.890 240.420  1.00 61.40           C  
ATOM  16100  O   ASN C 331     217.694 251.009 240.878  1.00 61.58           O  
ATOM  16101  CB  ASN C 331     219.594 250.951 238.818  1.00 60.68           C  
ATOM  16102  CG  ASN C 331     218.927 251.871 237.759  1.00 61.24           C  
ATOM  16103  OD1 ASN C 331     218.440 251.372 236.733  1.00 59.37           O  
ATOM  16104  ND2 ASN C 331     218.910 253.181 237.994  1.00 61.17           N  
ATOM  16105  N   ILE C 332     217.433 248.758 240.965  1.00 61.60           N  
ATOM  16106  CA  ILE C 332     216.613 248.676 242.172  1.00 63.01           C  
ATOM  16107  C   ILE C 332     217.474 248.115 243.286  1.00 64.02           C  
ATOM  16108  O   ILE C 332     218.013 247.019 243.166  1.00 64.02           O  
ATOM  16109  CB  ILE C 332     215.378 247.776 241.950  1.00 62.60           C  
ATOM  16110  CG1 ILE C 332     214.514 248.375 240.825  1.00 62.05           C  
ATOM  16111  CG2 ILE C 332     214.574 247.620 243.265  1.00 64.46           C  
ATOM  16112  CD1 ILE C 332     213.397 247.470 240.334  1.00 62.45           C  
ATOM  16113  N   THR C 333     217.622 248.880 244.358  1.00 64.34           N  
ATOM  16114  CA  THR C 333     218.470 248.476 245.478  1.00 64.60           C  
ATOM  16115  C   THR C 333     217.650 248.188 246.731  1.00 65.11           C  
ATOM  16116  O   THR C 333     218.194 247.899 247.797  1.00 65.81           O  
ATOM  16117  CB  THR C 333     219.529 249.554 245.773  1.00 65.61           C  
ATOM  16118  OG1 THR C 333     218.885 250.792 246.101  1.00 65.49           O  
ATOM  16119  CG2 THR C 333     220.439 249.759 244.564  1.00 64.10           C  
ATOM  16120  N   ASN C 334     216.335 248.284 246.593  1.00 65.28           N  
ATOM  16121  CA  ASN C 334     215.405 248.050 247.689  1.00 65.92           C  
ATOM  16122  C   ASN C 334     215.364 246.583 248.099  1.00 67.11           C  
ATOM  16123  O   ASN C 334     215.087 245.720 247.273  1.00 66.80           O  
ATOM  16124  CB  ASN C 334     214.024 248.522 247.289  1.00 66.36           C  
ATOM  16125  CG  ASN C 334     213.042 248.410 248.390  1.00 67.07           C  
ATOM  16126  OD1 ASN C 334     213.355 248.720 249.548  1.00 67.20           O  
ATOM  16127  ND2 ASN C 334     211.855 247.977 248.063  1.00 68.02           N  
ATOM  16128  N   LEU C 335     215.596 246.306 249.379  1.00 67.13           N  
ATOM  16129  CA  LEU C 335     215.558 244.927 249.860  1.00 67.46           C  
ATOM  16130  C   LEU C 335     214.122 244.432 249.795  1.00 68.85           C  
ATOM  16131  O   LEU C 335     213.194 245.210 250.043  1.00 69.52           O  
ATOM  16132  CB  LEU C 335     216.098 244.847 251.295  1.00 68.29           C  
ATOM  16133  CG  LEU C 335     217.593 245.214 251.476  1.00 68.22           C  
ATOM  16134  CD1 LEU C 335     217.920 245.262 252.963  1.00 67.89           C  
ATOM  16135  CD2 LEU C 335     218.473 244.179 250.772  1.00 68.23           C  
ATOM  16136  N   CYS C 336     213.917 243.145 249.464  1.00 68.59           N  
ATOM  16137  CA  CYS C 336     212.599 242.580 249.271  1.00 69.61           C  
ATOM  16138  C   CYS C 336     212.023 242.023 250.581  1.00 72.27           C  
ATOM  16139  O   CYS C 336     212.650 241.128 251.184  1.00 73.21           O  
ATOM  16140  CB  CYS C 336     212.628 241.482 248.195  1.00 69.03           C  
ATOM  16141  SG  CYS C 336     211.032 241.103 247.508  1.00 68.68           S  
ATOM  16142  N   PRO C 337     210.832 242.481 251.065  1.00 73.03           N  
ATOM  16143  CA  PRO C 337     210.243 242.180 252.363  1.00 74.99           C  
ATOM  16144  C   PRO C 337     209.650 240.778 252.473  1.00 75.49           C  
ATOM  16145  O   PRO C 337     208.452 240.621 252.697  1.00 76.33           O  
ATOM  16146  CB  PRO C 337     209.142 243.236 252.468  1.00 74.00           C  
ATOM  16147  CG  PRO C 337     208.683 243.451 251.054  1.00 73.07           C  
ATOM  16148  CD  PRO C 337     209.942 243.390 250.238  1.00 72.50           C  
ATOM  16149  N   PHE C 338     210.494 239.763 252.346  1.00 74.84           N  
ATOM  16150  CA  PHE C 338     210.017 238.401 252.538  1.00 76.32           C  
ATOM  16151  C   PHE C 338     209.818 238.133 254.022  1.00 78.20           C  
ATOM  16152  O   PHE C 338     208.949 237.360 254.412  1.00 79.03           O  
ATOM  16153  CB  PHE C 338     210.962 237.366 251.938  1.00 76.26           C  
ATOM  16154  CG  PHE C 338     210.902 237.280 250.443  1.00 74.95           C  
ATOM  16155  CD1 PHE C 338     211.950 237.728 249.678  1.00 73.56           C  
ATOM  16156  CD2 PHE C 338     209.786 236.753 249.800  1.00 74.32           C  
ATOM  16157  CE1 PHE C 338     211.901 237.652 248.312  1.00 72.31           C  
ATOM  16158  CE2 PHE C 338     209.737 236.679 248.426  1.00 73.58           C  
ATOM  16159  CZ  PHE C 338     210.797 237.129 247.682  1.00 72.15           C  
ATOM  16160  N   GLY C 339     210.590 238.800 254.868  1.00 77.61           N  
ATOM  16161  CA  GLY C 339     210.453 238.604 256.309  1.00 79.01           C  
ATOM  16162  C   GLY C 339     209.041 238.949 256.770  1.00 80.37           C  
ATOM  16163  O   GLY C 339     208.484 238.297 257.651  1.00 81.15           O  
ATOM  16164  N   GLU C 340     208.422 239.923 256.115  1.00 78.99           N  
ATOM  16165  CA  GLU C 340     207.076 240.362 256.460  1.00 78.83           C  
ATOM  16166  C   GLU C 340     206.021 239.328 256.079  1.00 79.58           C  
ATOM  16167  O   GLU C 340     204.851 239.461 256.437  1.00 80.78           O  
ATOM  16168  CB  GLU C 340     206.767 241.685 255.763  1.00 78.37           C  
ATOM  16169  N   VAL C 341     206.427 238.320 255.319  1.00 79.09           N  
ATOM  16170  CA  VAL C 341     205.542 237.253 254.896  1.00 80.31           C  
ATOM  16171  C   VAL C 341     205.765 236.007 255.743  1.00 81.29           C  
ATOM  16172  O   VAL C 341     204.818 235.402 256.240  1.00 82.38           O  
ATOM  16173  CB  VAL C 341     205.805 236.902 253.419  1.00 79.71           C  
ATOM  16174  CG1 VAL C 341     204.942 235.736 252.991  1.00 79.30           C  
ATOM  16175  CG2 VAL C 341     205.537 238.109 252.559  1.00 77.90           C  
ATOM  16176  N   PHE C 342     207.025 235.622 255.882  1.00 80.54           N  
ATOM  16177  CA  PHE C 342     207.397 234.386 256.570  1.00 81.76           C  
ATOM  16178  C   PHE C 342     207.459 234.477 258.103  1.00 83.44           C  
ATOM  16179  O   PHE C 342     207.204 233.481 258.782  1.00 83.94           O  
ATOM  16180  CB  PHE C 342     208.721 233.894 256.002  1.00 81.45           C  
ATOM  16181  CG  PHE C 342     208.552 233.381 254.611  1.00 81.33           C  
ATOM  16182  CD1 PHE C 342     208.685 234.219 253.525  1.00 79.35           C  
ATOM  16183  CD2 PHE C 342     208.241 232.066 254.386  1.00 81.46           C  
ATOM  16184  CE1 PHE C 342     208.505 233.755 252.253  1.00 78.61           C  
ATOM  16185  CE2 PHE C 342     208.064 231.596 253.115  1.00 80.67           C  
ATOM  16186  CZ  PHE C 342     208.194 232.445 252.047  1.00 79.76           C  
ATOM  16187  N   ASN C 343     207.786 235.665 258.650  1.00 83.03           N  
ATOM  16188  CA  ASN C 343     207.890 235.916 260.086  1.00 84.37           C  
ATOM  16189  C   ASN C 343     206.680 236.737 260.594  1.00 84.97           C  
ATOM  16190  O   ASN C 343     206.777 237.423 261.621  1.00 86.53           O  
ATOM  16191  CB  ASN C 343     209.213 236.623 260.418  1.00 83.74           C  
ATOM  16192  CG  ASN C 343     210.405 235.659 260.517  1.00 83.87           C  
ATOM  16193  OD1 ASN C 343     210.358 234.697 261.302  1.00 84.97           O  
ATOM  16194  ND2 ASN C 343     211.463 235.914 259.756  1.00 83.28           N  
ATOM  16195  N   ALA C 344     205.540 236.659 259.888  1.00 85.08           N  
ATOM  16196  CA  ALA C 344     204.300 237.359 260.234  1.00 86.43           C  
ATOM  16197  C   ALA C 344     203.739 236.872 261.565  1.00 88.41           C  
ATOM  16198  O   ALA C 344     203.792 235.682 261.883  1.00 87.52           O  
ATOM  16199  CB  ALA C 344     203.274 237.173 259.130  1.00 86.60           C  
ATOM  16200  N   THR C 345     203.189 237.802 262.335  1.00 88.25           N  
ATOM  16201  CA  THR C 345     202.598 237.499 263.629  1.00 89.89           C  
ATOM  16202  C   THR C 345     201.389 236.593 263.473  1.00 90.05           C  
ATOM  16203  O   THR C 345     201.193 235.658 264.254  1.00 90.96           O  
ATOM  16204  CB  THR C 345     202.197 238.799 264.350  1.00 91.11           C  
ATOM  16205  OG1 THR C 345     203.359 239.615 264.527  1.00 89.77           O  
ATOM  16206  CG2 THR C 345     201.584 238.513 265.707  1.00 92.02           C  
ATOM  16207  N   ARG C 346     200.578 236.873 262.460  1.00 90.01           N  
ATOM  16208  CA  ARG C 346     199.392 236.078 262.193  1.00 90.36           C  
ATOM  16209  C   ARG C 346     199.250 235.724 260.728  1.00 89.75           C  
ATOM  16210  O   ARG C 346     199.510 236.532 259.838  1.00 88.37           O  
ATOM  16211  CB  ARG C 346     198.126 236.798 262.634  1.00 90.67           C  
ATOM  16212  N   PHE C 347     198.802 234.501 260.506  1.00 89.81           N  
ATOM  16213  CA  PHE C 347     198.498 233.968 259.193  1.00 87.99           C  
ATOM  16214  C   PHE C 347     196.995 233.796 259.063  1.00 89.23           C  
ATOM  16215  O   PHE C 347     196.309 233.562 260.057  1.00 89.24           O  
ATOM  16216  CB  PHE C 347     199.226 232.643 258.990  1.00 87.64           C  
ATOM  16217  CG  PHE C 347     200.682 232.765 258.669  1.00 87.23           C  
ATOM  16218  CD1 PHE C 347     201.586 233.369 259.528  1.00 88.05           C  
ATOM  16219  CD2 PHE C 347     201.154 232.244 257.483  1.00 87.29           C  
ATOM  16220  CE1 PHE C 347     202.913 233.466 259.183  1.00 87.62           C  
ATOM  16221  CE2 PHE C 347     202.476 232.338 257.146  1.00 85.79           C  
ATOM  16222  CZ  PHE C 347     203.355 232.954 257.994  1.00 86.05           C  
ATOM  16223  N   ALA C 348     196.491 233.942 257.849  1.00 88.04           N  
ATOM  16224  CA  ALA C 348     195.070 233.802 257.565  1.00 88.85           C  
ATOM  16225  C   ALA C 348     194.645 232.346 257.536  1.00 88.30           C  
ATOM  16226  O   ALA C 348     195.470 231.452 257.358  1.00 88.06           O  
ATOM  16227  CB  ALA C 348     194.737 234.457 256.240  1.00 86.69           C  
ATOM  16228  N   SER C 349     193.350 232.120 257.702  1.00 88.48           N  
ATOM  16229  CA  SER C 349     192.779 230.794 257.574  1.00 89.56           C  
ATOM  16230  C   SER C 349     192.760 230.368 256.116  1.00 88.90           C  
ATOM  16231  O   SER C 349     192.804 231.205 255.213  1.00 87.81           O  
ATOM  16232  CB  SER C 349     191.385 230.804 258.143  1.00 91.05           C  
ATOM  16233  OG  SER C 349     190.558 231.640 257.390  1.00 90.41           O  
ATOM  16234  N   VAL C 350     192.655 229.074 255.869  1.00 88.69           N  
ATOM  16235  CA  VAL C 350     192.693 228.589 254.498  1.00 88.50           C  
ATOM  16236  C   VAL C 350     191.487 229.014 253.675  1.00 88.27           C  
ATOM  16237  O   VAL C 350     191.607 229.177 252.470  1.00 88.90           O  
ATOM  16238  CB  VAL C 350     192.859 227.063 254.465  1.00 89.71           C  
ATOM  16239  CG1 VAL C 350     191.577 226.367 254.839  1.00 92.03           C  
ATOM  16240  CG2 VAL C 350     193.335 226.633 253.078  1.00 88.75           C  
ATOM  16241  N   TYR C 351     190.322 229.198 254.289  1.00 90.93           N  
ATOM  16242  CA  TYR C 351     189.162 229.611 253.499  1.00 89.92           C  
ATOM  16243  C   TYR C 351     189.302 231.057 253.011  1.00 90.39           C  
ATOM  16244  O   TYR C 351     188.576 231.484 252.114  1.00 89.95           O  
ATOM  16245  CB  TYR C 351     187.856 229.465 254.287  1.00 91.77           C  
ATOM  16246  CG  TYR C 351     187.419 230.675 255.052  1.00 92.58           C  
ATOM  16247  CD1 TYR C 351     186.548 231.582 254.473  1.00 90.74           C  
ATOM  16248  CD2 TYR C 351     187.875 230.884 256.316  1.00 91.64           C  
ATOM  16249  CE1 TYR C 351     186.139 232.689 255.181  1.00 92.07           C  
ATOM  16250  CE2 TYR C 351     187.471 231.990 257.023  1.00 92.03           C  
ATOM  16251  CZ  TYR C 351     186.608 232.886 256.462  1.00 92.18           C  
ATOM  16252  OH  TYR C 351     186.205 233.986 257.175  1.00 91.87           O  
ATOM  16253  N   ALA C 352     190.180 231.827 253.643  1.00 89.02           N  
ATOM  16254  CA  ALA C 352     190.329 233.244 253.347  1.00 87.39           C  
ATOM  16255  C   ALA C 352     191.792 233.637 253.367  1.00 86.34           C  
ATOM  16256  O   ALA C 352     192.211 234.452 254.184  1.00 86.45           O  
ATOM  16257  CB  ALA C 352     189.558 234.074 254.351  1.00 89.79           C  
ATOM  16258  N   TRP C 353     192.569 233.041 252.476  1.00 86.21           N  
ATOM  16259  CA  TRP C 353     194.015 233.226 252.444  1.00 84.84           C  
ATOM  16260  C   TRP C 353     194.416 234.653 252.086  1.00 82.89           C  
ATOM  16261  O   TRP C 353     193.693 235.349 251.374  1.00 82.67           O  
ATOM  16262  CB  TRP C 353     194.624 232.219 251.474  1.00 85.22           C  
ATOM  16263  CG  TRP C 353     193.791 231.982 250.266  1.00 85.04           C  
ATOM  16264  CD1 TRP C 353     192.836 231.034 250.153  1.00 85.73           C  
ATOM  16265  CD2 TRP C 353     193.824 232.655 249.008  1.00 82.82           C  
ATOM  16266  NE1 TRP C 353     192.269 231.073 248.932  1.00 83.95           N  
ATOM  16267  CE2 TRP C 353     192.858 232.052 248.207  1.00 83.10           C  
ATOM  16268  CE3 TRP C 353     194.576 233.692 248.500  1.00 81.71           C  
ATOM  16269  CZ2 TRP C 353     192.631 232.451 246.929  1.00 83.40           C  
ATOM  16270  CZ3 TRP C 353     194.341 234.092 247.211  1.00 80.87           C  
ATOM  16271  CH2 TRP C 353     193.398 233.492 246.446  1.00 82.41           C  
ATOM  16272  N   ASN C 354     195.563 235.090 252.612  1.00 81.10           N  
ATOM  16273  CA  ASN C 354     196.077 236.442 252.405  1.00 80.72           C  
ATOM  16274  C   ASN C 354     197.049 236.559 251.237  1.00 80.07           C  
ATOM  16275  O   ASN C 354     198.137 235.993 251.275  1.00 79.54           O  
ATOM  16276  CB  ASN C 354     196.741 236.952 253.666  1.00 80.94           C  
ATOM  16277  CG  ASN C 354     197.234 238.360 253.522  1.00 79.85           C  
ATOM  16278  OD1 ASN C 354     196.792 239.093 252.629  1.00 79.17           O  
ATOM  16279  ND2 ASN C 354     198.142 238.753 254.379  1.00 79.97           N  
ATOM  16280  N   ARG C 355     196.650 237.273 250.194  1.00 79.53           N  
ATOM  16281  CA  ARG C 355     197.476 237.443 249.001  1.00 77.20           C  
ATOM  16282  C   ARG C 355     198.230 238.768 249.011  1.00 75.99           C  
ATOM  16283  O   ARG C 355     197.640 239.823 248.772  1.00 75.55           O  
ATOM  16284  CB  ARG C 355     196.599 237.392 247.772  1.00 76.48           C  
ATOM  16285  CG  ARG C 355     197.302 237.484 246.444  1.00 75.42           C  
ATOM  16286  CD  ARG C 355     196.337 237.222 245.359  1.00 74.61           C  
ATOM  16287  NE  ARG C 355     196.922 237.281 244.053  1.00 72.44           N  
ATOM  16288  CZ  ARG C 355     197.595 236.276 243.475  1.00 73.14           C  
ATOM  16289  NH1 ARG C 355     197.804 235.149 244.128  1.00 75.83           N  
ATOM  16290  NH2 ARG C 355     198.044 236.429 242.246  1.00 71.50           N  
ATOM  16291  N   LYS C 356     199.529 238.716 249.278  1.00 75.06           N  
ATOM  16292  CA  LYS C 356     200.343 239.924 249.337  1.00 73.94           C  
ATOM  16293  C   LYS C 356     201.131 240.141 248.054  1.00 73.44           C  
ATOM  16294  O   LYS C 356     201.799 239.233 247.560  1.00 72.88           O  
ATOM  16295  CB  LYS C 356     201.307 239.880 250.516  1.00 73.83           C  
ATOM  16296  CG  LYS C 356     202.132 241.153 250.681  1.00 74.13           C  
ATOM  16297  CD  LYS C 356     203.041 241.057 251.870  1.00 74.30           C  
ATOM  16298  CE  LYS C 356     203.819 242.340 252.098  1.00 75.57           C  
ATOM  16299  NZ  LYS C 356     204.722 242.202 253.257  1.00 76.17           N  
ATOM  16300  N   ARG C 357     201.075 241.354 247.518  1.00 71.84           N  
ATOM  16301  CA  ARG C 357     201.821 241.653 246.304  1.00 70.70           C  
ATOM  16302  C   ARG C 357     203.230 242.139 246.603  1.00 70.46           C  
ATOM  16303  O   ARG C 357     203.427 243.105 247.340  1.00 70.79           O  
ATOM  16304  CB  ARG C 357     201.121 242.714 245.479  1.00 70.58           C  
ATOM  16305  CG  ARG C 357     201.828 243.053 244.172  1.00 69.44           C  
ATOM  16306  CD  ARG C 357     201.115 244.083 243.409  1.00 68.74           C  
ATOM  16307  NE  ARG C 357     201.770 244.356 242.137  1.00 67.88           N  
ATOM  16308  CZ  ARG C 357     201.527 245.422 241.356  1.00 68.02           C  
ATOM  16309  NH1 ARG C 357     200.644 246.333 241.712  1.00 66.40           N  
ATOM  16310  NH2 ARG C 357     202.190 245.543 240.223  1.00 67.95           N  
ATOM  16311  N   ILE C 358     204.202 241.485 245.986  1.00 70.85           N  
ATOM  16312  CA  ILE C 358     205.604 241.828 246.107  1.00 69.64           C  
ATOM  16313  C   ILE C 358     206.111 242.450 244.811  1.00 68.94           C  
ATOM  16314  O   ILE C 358     206.024 241.846 243.737  1.00 69.35           O  
ATOM  16315  CB  ILE C 358     206.409 240.571 246.457  1.00 70.65           C  
ATOM  16316  CG1 ILE C 358     205.934 240.030 247.817  1.00 69.50           C  
ATOM  16317  CG2 ILE C 358     207.879 240.856 246.442  1.00 69.34           C  
ATOM  16318  CD1 ILE C 358     206.432 238.645 248.146  1.00 71.18           C  
ATOM  16319  N   SER C 359     206.634 243.668 244.910  1.00 68.31           N  
ATOM  16320  CA  SER C 359     207.108 244.383 243.734  1.00 67.40           C  
ATOM  16321  C   SER C 359     208.212 245.372 244.076  1.00 67.63           C  
ATOM  16322  O   SER C 359     208.428 245.709 245.238  1.00 67.27           O  
ATOM  16323  CB  SER C 359     205.964 245.120 243.070  1.00 67.90           C  
ATOM  16324  OG  SER C 359     205.519 246.177 243.867  1.00 68.88           O  
ATOM  16325  N   ASN C 360     208.903 245.838 243.045  1.00 66.93           N  
ATOM  16326  CA  ASN C 360     209.951 246.855 243.165  1.00 66.38           C  
ATOM  16327  C   ASN C 360     210.995 246.529 244.225  1.00 66.16           C  
ATOM  16328  O   ASN C 360     211.238 247.356 245.111  1.00 65.67           O  
ATOM  16329  CB  ASN C 360     209.343 248.214 243.439  1.00 66.56           C  
ATOM  16330  CG  ASN C 360     210.327 249.339 243.210  1.00 66.23           C  
ATOM  16331  OD1 ASN C 360     211.225 249.233 242.367  1.00 65.14           O  
ATOM  16332  ND2 ASN C 360     210.175 250.415 243.944  1.00 66.33           N  
ATOM  16333  N   CYS C 361     211.599 245.329 244.145  1.00 65.48           N  
ATOM  16334  CA  CYS C 361     212.566 244.872 245.136  1.00 66.63           C  
ATOM  16335  C   CYS C 361     213.622 243.932 244.541  1.00 66.19           C  
ATOM  16336  O   CYS C 361     213.425 243.354 243.467  1.00 66.76           O  
ATOM  16337  CB  CYS C 361     211.831 244.137 246.284  1.00 67.14           C  
ATOM  16338  SG  CYS C 361     210.982 242.514 245.818  1.00 69.13           S  
ATOM  16339  N   VAL C 362     214.719 243.739 245.297  1.00 67.01           N  
ATOM  16340  CA  VAL C 362     215.759 242.756 245.005  1.00 67.21           C  
ATOM  16341  C   VAL C 362     215.460 241.514 245.820  1.00 66.71           C  
ATOM  16342  O   VAL C 362     215.634 241.498 247.040  1.00 67.99           O  
ATOM  16343  CB  VAL C 362     217.149 243.284 245.377  1.00 65.66           C  
ATOM  16344  CG1 VAL C 362     218.198 242.230 245.044  1.00 65.36           C  
ATOM  16345  CG2 VAL C 362     217.407 244.570 244.635  1.00 65.35           C  
ATOM  16346  N   ALA C 363     214.978 240.492 245.145  1.00 66.15           N  
ATOM  16347  CA  ALA C 363     214.466 239.309 245.806  1.00 67.17           C  
ATOM  16348  C   ALA C 363     215.533 238.257 245.984  1.00 67.48           C  
ATOM  16349  O   ALA C 363     215.916 237.576 245.037  1.00 67.37           O  
ATOM  16350  CB  ALA C 363     213.305 238.747 245.013  1.00 67.60           C  
ATOM  16351  N   ASP C 364     216.035 238.141 247.201  1.00 69.28           N  
ATOM  16352  CA  ASP C 364     217.079 237.176 247.486  1.00 68.11           C  
ATOM  16353  C   ASP C 364     216.441 235.900 247.996  1.00 68.88           C  
ATOM  16354  O   ASP C 364     215.920 235.856 249.111  1.00 71.39           O  
ATOM  16355  CB  ASP C 364     218.084 237.727 248.490  1.00 69.28           C  
ATOM  16356  CG  ASP C 364     219.240 236.775 248.726  1.00 69.96           C  
ATOM  16357  OD1 ASP C 364     219.115 235.609 248.390  1.00 70.07           O  
ATOM  16358  OD2 ASP C 364     220.246 237.209 249.230  1.00 70.91           O  
ATOM  16359  N   TYR C 365     216.437 234.871 247.168  1.00 68.49           N  
ATOM  16360  CA  TYR C 365     215.734 233.648 247.495  1.00 68.93           C  
ATOM  16361  C   TYR C 365     216.651 232.631 248.143  1.00 71.37           C  
ATOM  16362  O   TYR C 365     216.215 231.523 248.462  1.00 73.22           O  
ATOM  16363  CB  TYR C 365     215.121 233.038 246.241  1.00 67.93           C  
ATOM  16364  CG  TYR C 365     214.009 233.839 245.618  1.00 67.90           C  
ATOM  16365  CD1 TYR C 365     214.286 234.712 244.586  1.00 67.60           C  
ATOM  16366  CD2 TYR C 365     212.707 233.676 246.052  1.00 68.97           C  
ATOM  16367  CE1 TYR C 365     213.272 235.415 243.990  1.00 66.58           C  
ATOM  16368  CE2 TYR C 365     211.694 234.385 245.453  1.00 68.85           C  
ATOM  16369  CZ  TYR C 365     211.974 235.250 244.426  1.00 67.46           C  
ATOM  16370  OH  TYR C 365     210.961 235.952 243.828  1.00 69.12           O  
ATOM  16371  N   SER C 366     217.925 232.991 248.333  1.00 71.79           N  
ATOM  16372  CA  SER C 366     218.854 232.047 248.937  1.00 73.65           C  
ATOM  16373  C   SER C 366     218.557 231.946 250.414  1.00 73.91           C  
ATOM  16374  O   SER C 366     218.807 230.920 251.042  1.00 74.73           O  
ATOM  16375  CB  SER C 366     220.300 232.470 248.750  1.00 72.39           C  
ATOM  16376  OG  SER C 366     220.607 233.577 249.543  1.00 72.25           O  
ATOM  16377  N   VAL C 367     217.955 232.992 250.960  1.00 73.06           N  
ATOM  16378  CA  VAL C 367     217.614 232.997 252.362  1.00 74.48           C  
ATOM  16379  C   VAL C 367     216.522 231.984 252.629  1.00 75.45           C  
ATOM  16380  O   VAL C 367     216.633 231.160 253.536  1.00 76.54           O  
ATOM  16381  CB  VAL C 367     217.134 234.400 252.772  1.00 74.27           C  
ATOM  16382  CG1 VAL C 367     216.602 234.393 254.210  1.00 77.45           C  
ATOM  16383  CG2 VAL C 367     218.288 235.376 252.621  1.00 73.62           C  
ATOM  16384  N   LEU C 368     215.474 232.029 251.821  1.00 74.83           N  
ATOM  16385  CA  LEU C 368     214.357 231.131 252.007  1.00 75.80           C  
ATOM  16386  C   LEU C 368     214.720 229.702 251.647  1.00 75.57           C  
ATOM  16387  O   LEU C 368     214.281 228.761 252.305  1.00 76.98           O  
ATOM  16388  CB  LEU C 368     213.175 231.594 251.153  1.00 76.94           C  
ATOM  16389  CG  LEU C 368     212.538 232.930 251.535  1.00 77.49           C  
ATOM  16390  CD1 LEU C 368     211.534 233.320 250.459  1.00 76.28           C  
ATOM  16391  CD2 LEU C 368     211.851 232.802 252.884  1.00 79.34           C  
ATOM  16392  N   TYR C 369     215.521 229.535 250.603  1.00 74.99           N  
ATOM  16393  CA  TYR C 369     215.921 228.208 250.173  1.00 75.77           C  
ATOM  16394  C   TYR C 369     216.836 227.515 251.170  1.00 74.06           C  
ATOM  16395  O   TYR C 369     216.633 226.345 251.494  1.00 75.60           O  
ATOM  16396  CB  TYR C 369     216.580 228.265 248.802  1.00 74.03           C  
ATOM  16397  CG  TYR C 369     217.080 226.936 248.364  1.00 73.32           C  
ATOM  16398  CD1 TYR C 369     216.183 225.937 248.050  1.00 72.11           C  
ATOM  16399  CD2 TYR C 369     218.436 226.707 248.279  1.00 73.43           C  
ATOM  16400  CE1 TYR C 369     216.642 224.703 247.655  1.00 71.26           C  
ATOM  16401  CE2 TYR C 369     218.899 225.477 247.883  1.00 74.07           C  
ATOM  16402  CZ  TYR C 369     218.008 224.475 247.570  1.00 72.13           C  
ATOM  16403  OH  TYR C 369     218.473 223.242 247.177  1.00 70.02           O  
ATOM  16404  N   ASN C 370     217.864 228.221 251.634  1.00 77.97           N  
ATOM  16405  CA  ASN C 370     218.834 227.627 252.537  1.00 76.10           C  
ATOM  16406  C   ASN C 370     218.315 227.485 253.960  1.00 77.91           C  
ATOM  16407  O   ASN C 370     218.755 226.600 254.694  1.00 78.78           O  
ATOM  16408  CB  ASN C 370     220.115 228.422 252.519  1.00 77.08           C  
ATOM  16409  CG  ASN C 370     220.865 228.236 251.240  1.00 75.68           C  
ATOM  16410  OD1 ASN C 370     220.793 227.182 250.598  1.00 75.85           O  
ATOM  16411  ND2 ASN C 370     221.584 229.247 250.845  1.00 75.58           N  
ATOM  16412  N   SER C 371     217.383 228.343 254.364  1.00 77.20           N  
ATOM  16413  CA  SER C 371     216.863 228.269 255.717  1.00 79.10           C  
ATOM  16414  C   SER C 371     216.344 226.879 256.047  1.00 80.15           C  
ATOM  16415  O   SER C 371     215.517 226.310 255.337  1.00 79.90           O  
ATOM  16416  CB  SER C 371     215.767 229.295 255.897  1.00 79.37           C  
ATOM  16417  OG  SER C 371     215.083 229.092 257.097  1.00 80.11           O  
ATOM  16418  N   ALA C 372     216.805 226.350 257.178  1.00 81.22           N  
ATOM  16419  CA  ALA C 372     216.446 225.007 257.627  1.00 81.06           C  
ATOM  16420  C   ALA C 372     215.142 225.015 258.406  1.00 81.60           C  
ATOM  16421  O   ALA C 372     214.680 223.976 258.874  1.00 81.87           O  
ATOM  16422  CB  ALA C 372     217.560 224.425 258.481  1.00 82.59           C  
ATOM  16423  N   SER C 373     214.559 226.194 258.555  1.00 80.99           N  
ATOM  16424  CA  SER C 373     213.324 226.364 259.310  1.00 81.74           C  
ATOM  16425  C   SER C 373     212.111 225.792 258.586  1.00 82.02           C  
ATOM  16426  O   SER C 373     211.043 225.651 259.183  1.00 82.29           O  
ATOM  16427  CB  SER C 373     213.062 227.831 259.592  1.00 82.05           C  
ATOM  16428  OG  SER C 373     212.714 228.514 258.421  1.00 81.55           O  
ATOM  16429  N   PHE C 374     212.260 225.492 257.301  1.00 81.95           N  
ATOM  16430  CA  PHE C 374     211.134 225.023 256.517  1.00 82.83           C  
ATOM  16431  C   PHE C 374     211.059 223.509 256.462  1.00 82.67           C  
ATOM  16432  O   PHE C 374     212.078 222.829 256.348  1.00 82.63           O  
ATOM  16433  CB  PHE C 374     211.209 225.599 255.110  1.00 81.54           C  
ATOM  16434  CG  PHE C 374     211.138 227.089 255.121  1.00 81.11           C  
ATOM  16435  CD1 PHE C 374     212.185 227.848 254.642  1.00 80.51           C  
ATOM  16436  CD2 PHE C 374     210.046 227.742 255.653  1.00 82.28           C  
ATOM  16437  CE1 PHE C 374     212.127 229.220 254.683  1.00 79.92           C  
ATOM  16438  CE2 PHE C 374     209.994 229.113 255.698  1.00 82.80           C  
ATOM  16439  CZ  PHE C 374     211.035 229.853 255.208  1.00 80.35           C  
ATOM  16440  N   SER C 375     209.837 222.979 256.505  1.00 82.73           N  
ATOM  16441  CA  SER C 375     209.631 221.544 256.395  1.00 82.74           C  
ATOM  16442  C   SER C 375     209.733 221.143 254.943  1.00 82.57           C  
ATOM  16443  O   SER C 375     210.196 220.052 254.607  1.00 82.17           O  
ATOM  16444  CB  SER C 375     208.270 221.151 256.934  1.00 84.21           C  
ATOM  16445  OG  SER C 375     208.176 221.396 258.311  1.00 85.82           O  
ATOM  16446  N   THR C 376     209.314 222.052 254.074  1.00 81.24           N  
ATOM  16447  CA  THR C 376     209.388 221.801 252.650  1.00 80.98           C  
ATOM  16448  C   THR C 376     209.612 223.089 251.868  1.00 80.03           C  
ATOM  16449  O   THR C 376     209.163 224.168 252.268  1.00 80.25           O  
ATOM  16450  CB  THR C 376     208.117 221.094 252.150  1.00 81.33           C  
ATOM  16451  OG1 THR C 376     208.299 220.703 250.789  1.00 78.17           O  
ATOM  16452  CG2 THR C 376     206.917 222.026 252.255  1.00 81.93           C  
ATOM  16453  N   PHE C 377     210.298 222.953 250.740  1.00 77.44           N  
ATOM  16454  CA  PHE C 377     210.538 224.033 249.794  1.00 75.93           C  
ATOM  16455  C   PHE C 377     210.511 223.427 248.406  1.00 74.80           C  
ATOM  16456  O   PHE C 377     211.511 222.873 247.948  1.00 74.66           O  
ATOM  16457  CB  PHE C 377     211.906 224.684 250.042  1.00 76.69           C  
ATOM  16458  CG  PHE C 377     212.157 225.969 249.284  1.00 75.18           C  
ATOM  16459  CD1 PHE C 377     212.227 227.166 249.963  1.00 76.81           C  
ATOM  16460  CD2 PHE C 377     212.324 225.993 247.901  1.00 74.34           C  
ATOM  16461  CE1 PHE C 377     212.452 228.338 249.291  1.00 76.08           C  
ATOM  16462  CE2 PHE C 377     212.548 227.180 247.243  1.00 73.18           C  
ATOM  16463  CZ  PHE C 377     212.611 228.346 247.939  1.00 74.26           C  
ATOM  16464  N   LYS C 378     209.372 223.499 247.738  1.00 74.38           N  
ATOM  16465  CA  LYS C 378     209.265 222.828 246.452  1.00 73.60           C  
ATOM  16466  C   LYS C 378     208.775 223.771 245.358  1.00 73.31           C  
ATOM  16467  O   LYS C 378     207.734 224.413 245.503  1.00 73.46           O  
ATOM  16468  CB  LYS C 378     208.333 221.613 246.570  1.00 73.33           C  
ATOM  16469  N   CYS C 379     209.532 223.827 244.251  1.00 71.92           N  
ATOM  16470  CA  CYS C 379     209.225 224.655 243.087  1.00 70.21           C  
ATOM  16471  C   CYS C 379     208.732 223.773 241.938  1.00 69.51           C  
ATOM  16472  O   CYS C 379     209.152 222.621 241.808  1.00 70.53           O  
ATOM  16473  CB  CYS C 379     210.464 225.450 242.650  1.00 67.50           C  
ATOM  16474  SG  CYS C 379     211.135 226.561 243.919  1.00 68.80           S  
ATOM  16475  N   TYR C 380     207.835 224.330 241.096  1.00 68.91           N  
ATOM  16476  CA  TYR C 380     207.230 223.588 239.978  1.00 69.73           C  
ATOM  16477  C   TYR C 380     207.693 224.034 238.594  1.00 66.36           C  
ATOM  16478  O   TYR C 380     208.205 223.225 237.824  1.00 66.14           O  
ATOM  16479  CB  TYR C 380     205.711 223.693 240.086  1.00 70.89           C  
ATOM  16480  CG  TYR C 380     205.203 223.044 241.331  1.00 71.80           C  
ATOM  16481  CD1 TYR C 380     204.987 223.801 242.458  1.00 72.44           C  
ATOM  16482  CD2 TYR C 380     204.972 221.684 241.354  1.00 72.83           C  
ATOM  16483  CE1 TYR C 380     204.545 223.200 243.606  1.00 74.61           C  
ATOM  16484  CE2 TYR C 380     204.526 221.084 242.505  1.00 74.53           C  
ATOM  16485  CZ  TYR C 380     204.315 221.840 243.628  1.00 74.64           C  
ATOM  16486  OH  TYR C 380     203.876 221.245 244.783  1.00 76.90           O  
ATOM  16487  N   GLY C 381     207.516 225.305 238.262  1.00 65.86           N  
ATOM  16488  CA  GLY C 381     207.882 225.770 236.925  1.00 64.37           C  
ATOM  16489  C   GLY C 381     209.324 226.258 236.849  1.00 61.58           C  
ATOM  16490  O   GLY C 381     209.812 226.611 235.772  1.00 58.60           O  
ATOM  16491  N   VAL C 382     209.975 226.331 237.999  1.00 63.10           N  
ATOM  16492  CA  VAL C 382     211.358 226.777 238.095  1.00 59.65           C  
ATOM  16493  C   VAL C 382     212.128 225.902 239.062  1.00 59.98           C  
ATOM  16494  O   VAL C 382     211.539 225.285 239.943  1.00 63.51           O  
ATOM  16495  CB  VAL C 382     211.442 228.244 238.555  1.00 59.37           C  
ATOM  16496  CG1 VAL C 382     210.768 229.159 237.547  1.00 59.31           C  
ATOM  16497  CG2 VAL C 382     210.784 228.392 239.904  1.00 63.53           C  
ATOM  16498  N   SER C 383     213.441 225.909 238.957  1.00 58.46           N  
ATOM  16499  CA  SER C 383     214.267 225.259 239.958  1.00 58.66           C  
ATOM  16500  C   SER C 383     214.597 226.260 241.062  1.00 62.03           C  
ATOM  16501  O   SER C 383     214.809 227.437 240.781  1.00 61.93           O  
ATOM  16502  CB  SER C 383     215.511 224.697 239.319  1.00 56.21           C  
ATOM  16503  OG  SER C 383     215.187 223.606 238.508  1.00 54.08           O  
ATOM  16504  N   PRO C 384     214.670 225.819 242.320  1.00 62.01           N  
ATOM  16505  CA  PRO C 384     214.865 226.628 243.511  1.00 63.18           C  
ATOM  16506  C   PRO C 384     216.192 227.374 243.566  1.00 63.04           C  
ATOM  16507  O   PRO C 384     216.327 228.343 244.309  1.00 64.71           O  
ATOM  16508  CB  PRO C 384     214.773 225.588 244.626  1.00 66.07           C  
ATOM  16509  CG  PRO C 384     215.121 224.276 243.978  1.00 64.27           C  
ATOM  16510  CD  PRO C 384     214.573 224.376 242.587  1.00 62.66           C  
ATOM  16511  N   THR C 385     217.177 226.941 242.789  1.00 60.73           N  
ATOM  16512  CA  THR C 385     218.473 227.608 242.831  1.00 60.46           C  
ATOM  16513  C   THR C 385     218.670 228.543 241.645  1.00 59.99           C  
ATOM  16514  O   THR C 385     219.682 229.236 241.553  1.00 59.95           O  
ATOM  16515  CB  THR C 385     219.626 226.596 242.907  1.00 59.55           C  
ATOM  16516  OG1 THR C 385     219.656 225.785 241.726  1.00 58.47           O  
ATOM  16517  CG2 THR C 385     219.464 225.710 244.132  1.00 63.39           C  
ATOM  16518  N   LYS C 386     217.688 228.584 240.747  1.00 60.34           N  
ATOM  16519  CA  LYS C 386     217.736 229.467 239.587  1.00 58.89           C  
ATOM  16520  C   LYS C 386     217.012 230.765 239.899  1.00 60.62           C  
ATOM  16521  O   LYS C 386     217.028 231.714 239.114  1.00 61.04           O  
ATOM  16522  CB  LYS C 386     217.100 228.801 238.369  1.00 57.27           C  
ATOM  16523  CG  LYS C 386     217.808 227.553 237.839  1.00 54.97           C  
ATOM  16524  CD  LYS C 386     219.115 227.900 237.164  1.00 54.44           C  
ATOM  16525  CE  LYS C 386     219.667 226.709 236.408  1.00 51.90           C  
ATOM  16526  NZ  LYS C 386     220.951 227.028 235.747  1.00 52.10           N  
ATOM  16527  N   LEU C 387     216.382 230.800 241.061  1.00 60.97           N  
ATOM  16528  CA  LEU C 387     215.518 231.897 241.445  1.00 60.97           C  
ATOM  16529  C   LEU C 387     216.248 233.223 241.540  1.00 62.36           C  
ATOM  16530  O   LEU C 387     215.648 234.273 241.330  1.00 63.17           O  
ATOM  16531  CB  LEU C 387     214.866 231.587 242.793  1.00 63.70           C  
ATOM  16532  CG  LEU C 387     213.882 230.411 242.830  1.00 64.13           C  
ATOM  16533  CD1 LEU C 387     213.444 230.160 244.268  1.00 66.90           C  
ATOM  16534  CD2 LEU C 387     212.692 230.716 241.985  1.00 64.77           C  
ATOM  16535  N   ASN C 388     217.539 233.192 241.845  1.00 61.31           N  
ATOM  16536  CA  ASN C 388     218.290 234.432 241.958  1.00 61.33           C  
ATOM  16537  C   ASN C 388     218.807 234.950 240.621  1.00 61.21           C  
ATOM  16538  O   ASN C 388     219.336 236.056 240.558  1.00 61.35           O  
ATOM  16539  CB  ASN C 388     219.437 234.254 242.926  1.00 62.87           C  
ATOM  16540  CG  ASN C 388     218.965 234.167 244.332  1.00 65.38           C  
ATOM  16541  OD1 ASN C 388     217.977 234.813 244.702  1.00 66.56           O  
ATOM  16542  ND2 ASN C 388     219.644 233.382 245.122  1.00 67.61           N  
ATOM  16543  N   ASP C 389     218.670 234.161 239.555  1.00 60.48           N  
ATOM  16544  CA  ASP C 389     219.134 234.584 238.234  1.00 60.10           C  
ATOM  16545  C   ASP C 389     217.989 235.169 237.425  1.00 59.86           C  
ATOM  16546  O   ASP C 389     218.181 236.049 236.583  1.00 58.27           O  
ATOM  16547  CB  ASP C 389     219.750 233.411 237.472  1.00 60.77           C  
ATOM  16548  CG  ASP C 389     221.016 232.850 238.125  1.00 60.64           C  
ATOM  16549  OD1 ASP C 389     221.952 233.597 238.345  1.00 60.00           O  
ATOM  16550  OD2 ASP C 389     221.045 231.674 238.380  1.00 59.92           O  
ATOM  16551  N   LEU C 390     216.797 234.664 237.699  1.00 60.32           N  
ATOM  16552  CA  LEU C 390     215.568 235.045 237.022  1.00 60.20           C  
ATOM  16553  C   LEU C 390     215.047 236.374 237.549  1.00 60.00           C  
ATOM  16554  O   LEU C 390     215.425 236.799 238.644  1.00 62.03           O  
ATOM  16555  CB  LEU C 390     214.494 233.977 237.268  1.00 60.58           C  
ATOM  16556  CG  LEU C 390     214.795 232.562 236.784  1.00 58.84           C  
ATOM  16557  CD1 LEU C 390     213.726 231.639 237.337  1.00 59.76           C  
ATOM  16558  CD2 LEU C 390     214.816 232.512 235.263  1.00 56.99           C  
ATOM  16559  N   CYS C 391     214.167 237.021 236.766  1.00 60.44           N  
ATOM  16560  CA  CYS C 391     213.455 238.216 237.193  1.00 61.22           C  
ATOM  16561  C   CYS C 391     211.992 238.090 236.759  1.00 61.94           C  
ATOM  16562  O   CYS C 391     211.695 237.585 235.678  1.00 61.59           O  
ATOM  16563  CB  CYS C 391     214.092 239.484 236.569  1.00 59.97           C  
ATOM  16564  SG  CYS C 391     213.453 241.025 237.266  1.00 62.95           S  
ATOM  16565  N   PHE C 392     211.080 238.478 237.663  1.00 63.06           N  
ATOM  16566  CA  PHE C 392     209.629 238.316 237.517  1.00 63.56           C  
ATOM  16567  C   PHE C 392     208.948 239.664 237.390  1.00 64.21           C  
ATOM  16568  O   PHE C 392     209.493 240.685 237.819  1.00 63.34           O  
ATOM  16569  CB  PHE C 392     209.097 237.568 238.734  1.00 65.05           C  
ATOM  16570  CG  PHE C 392     209.814 236.255 238.964  1.00 65.71           C  
ATOM  16571  CD1 PHE C 392     210.753 236.132 239.986  1.00 65.26           C  
ATOM  16572  CD2 PHE C 392     209.583 235.157 238.157  1.00 66.01           C  
ATOM  16573  CE1 PHE C 392     211.419 234.939 240.198  1.00 65.65           C  
ATOM  16574  CE2 PHE C 392     210.252 233.962 238.370  1.00 66.13           C  
ATOM  16575  CZ  PHE C 392     211.167 233.858 239.392  1.00 65.98           C  
ATOM  16576  N   THR C 393     207.766 239.697 236.793  1.00 63.71           N  
ATOM  16577  CA  THR C 393     207.072 240.974 236.697  1.00 64.82           C  
ATOM  16578  C   THR C 393     206.400 241.279 238.021  1.00 66.27           C  
ATOM  16579  O   THR C 393     206.337 242.431 238.452  1.00 65.67           O  
ATOM  16580  CB  THR C 393     206.031 240.963 235.580  1.00 64.24           C  
ATOM  16581  OG1 THR C 393     205.046 239.997 235.870  1.00 65.59           O  
ATOM  16582  CG2 THR C 393     206.702 240.598 234.273  1.00 63.09           C  
ATOM  16583  N   ASN C 394     205.917 240.227 238.662  1.00 66.30           N  
ATOM  16584  CA  ASN C 394     205.283 240.304 239.973  1.00 67.37           C  
ATOM  16585  C   ASN C 394     205.461 238.996 240.720  1.00 68.13           C  
ATOM  16586  O   ASN C 394     205.531 237.923 240.112  1.00 67.54           O  
ATOM  16587  CB  ASN C 394     203.796 240.625 239.874  1.00 67.43           C  
ATOM  16588  CG  ASN C 394     203.493 242.017 239.425  1.00 67.11           C  
ATOM  16589  OD1 ASN C 394     203.716 242.992 240.164  1.00 68.01           O  
ATOM  16590  ND2 ASN C 394     202.967 242.138 238.229  1.00 66.81           N  
ATOM  16591  N   VAL C 395     205.492 239.081 242.043  1.00 68.31           N  
ATOM  16592  CA  VAL C 395     205.463 237.898 242.882  1.00 68.50           C  
ATOM  16593  C   VAL C 395     204.335 238.020 243.889  1.00 70.44           C  
ATOM  16594  O   VAL C 395     204.206 239.037 244.565  1.00 68.70           O  
ATOM  16595  CB  VAL C 395     206.817 237.685 243.589  1.00 69.49           C  
ATOM  16596  CG1 VAL C 395     206.742 236.476 244.542  1.00 70.35           C  
ATOM  16597  CG2 VAL C 395     207.897 237.463 242.533  1.00 67.79           C  
ATOM  16598  N   TYR C 396     203.498 237.001 243.988  1.00 69.75           N  
ATOM  16599  CA  TYR C 396     202.417 237.075 244.959  1.00 70.07           C  
ATOM  16600  C   TYR C 396     202.579 236.020 246.026  1.00 72.57           C  
ATOM  16601  O   TYR C 396     202.791 234.848 245.729  1.00 73.68           O  
ATOM  16602  CB  TYR C 396     201.061 236.951 244.277  1.00 70.48           C  
ATOM  16603  CG  TYR C 396     200.779 238.089 243.355  1.00 70.51           C  
ATOM  16604  CD1 TYR C 396     201.181 238.014 242.038  1.00 69.94           C  
ATOM  16605  CD2 TYR C 396     200.125 239.216 243.819  1.00 70.19           C  
ATOM  16606  CE1 TYR C 396     200.940 239.059 241.185  1.00 69.27           C  
ATOM  16607  CE2 TYR C 396     199.882 240.265 242.961  1.00 69.48           C  
ATOM  16608  CZ  TYR C 396     200.293 240.188 241.647  1.00 67.72           C  
ATOM  16609  OH  TYR C 396     200.061 241.227 240.783  1.00 68.25           O  
ATOM  16610  N   ALA C 397     202.494 236.442 247.276  1.00 73.74           N  
ATOM  16611  CA  ALA C 397     202.643 235.519 248.388  1.00 74.49           C  
ATOM  16612  C   ALA C 397     201.304 235.214 249.031  1.00 76.73           C  
ATOM  16613  O   ALA C 397     200.719 236.072 249.694  1.00 76.94           O  
ATOM  16614  CB  ALA C 397     203.593 236.092 249.421  1.00 74.49           C  
ATOM  16615  N   ASP C 398     200.825 233.991 248.843  1.00 77.06           N  
ATOM  16616  CA  ASP C 398     199.553 233.578 249.418  1.00 78.59           C  
ATOM  16617  C   ASP C 398     199.824 232.888 250.751  1.00 80.35           C  
ATOM  16618  O   ASP C 398     200.387 231.795 250.794  1.00 80.89           O  
ATOM  16619  CB  ASP C 398     198.803 232.649 248.466  1.00 79.12           C  
ATOM  16620  N   SER C 399     199.473 233.568 251.836  1.00 81.53           N  
ATOM  16621  CA  SER C 399     199.768 233.140 253.201  1.00 81.78           C  
ATOM  16622  C   SER C 399     198.560 232.613 253.974  1.00 83.34           C  
ATOM  16623  O   SER C 399     197.563 233.323 254.156  1.00 84.54           O  
ATOM  16624  CB  SER C 399     200.361 234.306 253.949  1.00 82.59           C  
ATOM  16625  OG  SER C 399     200.430 234.035 255.305  1.00 84.28           O  
ATOM  16626  N   PHE C 400     198.653 231.366 254.441  1.00 85.03           N  
ATOM  16627  CA  PHE C 400     197.552 230.754 255.185  1.00 86.34           C  
ATOM  16628  C   PHE C 400     197.956 229.577 256.099  1.00 87.34           C  
ATOM  16629  O   PHE C 400     199.049 229.024 255.977  1.00 87.29           O  
ATOM  16630  CB  PHE C 400     196.472 230.334 254.199  1.00 86.69           C  
ATOM  16631  CG  PHE C 400     196.974 229.448 253.107  1.00 84.70           C  
ATOM  16632  CD1 PHE C 400     196.923 228.102 253.244  1.00 85.94           C  
ATOM  16633  CD2 PHE C 400     197.512 229.976 251.941  1.00 84.01           C  
ATOM  16634  CE1 PHE C 400     197.391 227.262 252.260  1.00 85.87           C  
ATOM  16635  CE2 PHE C 400     197.984 229.150 250.953  1.00 84.65           C  
ATOM  16636  CZ  PHE C 400     197.923 227.788 251.114  1.00 84.77           C  
ATOM  16637  N   VAL C 401     197.057 229.196 257.018  1.00 88.86           N  
ATOM  16638  CA  VAL C 401     197.283 228.056 257.923  1.00 89.02           C  
ATOM  16639  C   VAL C 401     196.411 226.842 257.618  1.00 89.23           C  
ATOM  16640  O   VAL C 401     195.186 226.939 257.543  1.00 90.09           O  
ATOM  16641  CB  VAL C 401     197.025 228.455 259.389  1.00 91.20           C  
ATOM  16642  N   ILE C 402     197.064 225.693 257.462  1.00 89.14           N  
ATOM  16643  CA  ILE C 402     196.389 224.422 257.198  1.00 91.36           C  
ATOM  16644  C   ILE C 402     196.866 223.309 258.113  1.00 91.70           C  
ATOM  16645  O   ILE C 402     197.873 223.444 258.801  1.00 92.02           O  
ATOM  16646  CB  ILE C 402     196.565 223.974 255.749  1.00 91.43           C  
ATOM  16647  N   ARG C 403     196.146 222.199 258.105  1.00 91.59           N  
ATOM  16648  CA  ARG C 403     196.537 221.015 258.854  1.00 92.38           C  
ATOM  16649  C   ARG C 403     197.600 220.204 258.104  1.00 90.70           C  
ATOM  16650  O   ARG C 403     197.538 220.077 256.882  1.00 91.09           O  
ATOM  16651  CB  ARG C 403     195.307 220.175 259.134  1.00 92.54           C  
ATOM  16652  CG  ARG C 403     195.488 219.087 260.132  1.00 96.30           C  
ATOM  16653  CD  ARG C 403     194.184 218.646 260.689  1.00 93.86           C  
ATOM  16654  NE  ARG C 403     193.351 218.022 259.688  1.00 94.08           N  
ATOM  16655  CZ  ARG C 403     192.069 217.646 259.879  1.00 96.37           C  
ATOM  16656  NH1 ARG C 403     191.476 217.841 261.041  1.00 94.78           N  
ATOM  16657  NH2 ARG C 403     191.402 217.078 258.894  1.00 94.30           N  
ATOM  16658  N   GLY C 404     198.543 219.634 258.852  1.00102.09           N  
ATOM  16659  CA  GLY C 404     199.675 218.853 258.338  1.00 90.42           C  
ATOM  16660  C   GLY C 404     199.365 217.846 257.235  1.00 92.87           C  
ATOM  16661  O   GLY C 404     200.024 217.848 256.194  1.00 91.74           O  
ATOM  16662  N   ASP C 405     198.368 216.997 257.427  1.00 92.73           N  
ATOM  16663  CA  ASP C 405     198.055 215.988 256.417  1.00 93.16           C  
ATOM  16664  C   ASP C 405     197.564 216.571 255.095  1.00 92.67           C  
ATOM  16665  O   ASP C 405     197.491 215.860 254.092  1.00 91.65           O  
ATOM  16666  CB  ASP C 405     197.025 214.978 256.930  1.00 93.89           C  
ATOM  16667  N   GLU C 406     197.193 217.847 255.081  1.00 91.35           N  
ATOM  16668  CA  GLU C 406     196.696 218.454 253.859  1.00 91.66           C  
ATOM  16669  C   GLU C 406     197.747 219.325 253.173  1.00 90.73           C  
ATOM  16670  O   GLU C 406     197.455 219.998 252.186  1.00 89.79           O  
ATOM  16671  CB  GLU C 406     195.428 219.260 254.123  1.00 91.22           C  
ATOM  16672  CG  GLU C 406     194.261 218.437 254.664  1.00 91.35           C  
ATOM  16673  CD  GLU C 406     192.932 219.182 254.664  1.00 91.10           C  
ATOM  16674  OE1 GLU C 406     192.791 220.138 255.397  1.00 93.10           O  
ATOM  16675  OE2 GLU C 406     192.066 218.794 253.904  1.00 91.26           O  
ATOM  16676  N   VAL C 407     198.985 219.288 253.658  1.00 90.44           N  
ATOM  16677  CA  VAL C 407     200.057 220.063 253.039  1.00 90.25           C  
ATOM  16678  C   VAL C 407     200.280 219.600 251.608  1.00 90.08           C  
ATOM  16679  O   VAL C 407     200.587 220.401 250.728  1.00 88.51           O  
ATOM  16680  CB  VAL C 407     201.364 219.990 253.860  1.00 91.09           C  
ATOM  16681  CG1 VAL C 407     202.528 220.622 253.081  1.00 88.22           C  
ATOM  16682  CG2 VAL C 407     201.172 220.750 255.183  1.00 90.71           C  
ATOM  16683  N   ARG C 408     200.113 218.306 251.371  1.00 89.86           N  
ATOM  16684  CA  ARG C 408     200.288 217.729 250.045  1.00 89.45           C  
ATOM  16685  C   ARG C 408     199.263 218.240 249.027  1.00 87.93           C  
ATOM  16686  O   ARG C 408     199.434 218.035 247.829  1.00 86.46           O  
ATOM  16687  CB  ARG C 408     200.200 216.214 250.110  1.00 90.05           C  
ATOM  16688  CG  ARG C 408     198.815 215.664 250.422  1.00 89.50           C  
ATOM  16689  CD  ARG C 408     198.833 214.185 250.536  1.00 91.83           C  
ATOM  16690  NE  ARG C 408     197.522 213.650 250.875  1.00 90.95           N  
ATOM  16691  CZ  ARG C 408     196.543 213.371 249.988  1.00 91.73           C  
ATOM  16692  NH1 ARG C 408     196.725 213.587 248.701  1.00 91.12           N  
ATOM  16693  NH2 ARG C 408     195.393 212.878 250.415  1.00 89.71           N  
ATOM  16694  N   GLN C 409     198.190 218.889 249.490  1.00 87.40           N  
ATOM  16695  CA  GLN C 409     197.191 219.421 248.568  1.00 87.19           C  
ATOM  16696  C   GLN C 409     197.622 220.764 248.002  1.00 86.51           C  
ATOM  16697  O   GLN C 409     197.016 221.263 247.051  1.00 84.66           O  
ATOM  16698  CB  GLN C 409     195.824 219.600 249.240  1.00 87.23           C  
ATOM  16699  CG  GLN C 409     195.106 218.328 249.614  1.00 87.94           C  
ATOM  16700  CD  GLN C 409     193.795 218.622 250.348  1.00 90.56           C  
ATOM  16701  OE1 GLN C 409     192.992 219.492 249.956  1.00 87.67           O  
ATOM  16702  NE2 GLN C 409     193.584 217.893 251.437  1.00 89.23           N  
ATOM  16703  N   ILE C 410     198.665 221.369 248.566  1.00 85.91           N  
ATOM  16704  CA  ILE C 410     199.067 222.669 248.060  1.00 84.58           C  
ATOM  16705  C   ILE C 410     200.054 222.448 246.933  1.00 83.63           C  
ATOM  16706  O   ILE C 410     201.269 222.557 247.099  1.00 81.49           O  
ATOM  16707  CB  ILE C 410     199.701 223.539 249.157  1.00 85.50           C  
ATOM  16708  CG1 ILE C 410     198.799 223.558 250.429  1.00 86.51           C  
ATOM  16709  CG2 ILE C 410     199.933 224.958 248.623  1.00 83.38           C  
ATOM  16710  CD1 ILE C 410     197.369 224.032 250.219  1.00 86.96           C  
ATOM  16711  N   ALA C 411     199.496 222.127 245.783  1.00 82.26           N  
ATOM  16712  CA  ALA C 411     200.240 221.792 244.586  1.00 80.68           C  
ATOM  16713  C   ALA C 411     199.279 221.873 243.402  1.00 81.64           C  
ATOM  16714  O   ALA C 411     198.066 221.858 243.607  1.00 81.77           O  
ATOM  16715  CB  ALA C 411     200.860 220.404 244.738  1.00 80.74           C  
ATOM  16716  N   PRO C 412     199.774 222.037 242.178  1.00 80.18           N  
ATOM  16717  CA  PRO C 412     199.017 221.959 240.948  1.00 79.29           C  
ATOM  16718  C   PRO C 412     198.545 220.535 240.702  1.00 80.59           C  
ATOM  16719  O   PRO C 412     199.252 219.582 241.042  1.00 81.34           O  
ATOM  16720  CB  PRO C 412     200.046 222.407 239.906  1.00 78.97           C  
ATOM  16721  CG  PRO C 412     201.387 222.122 240.533  1.00 77.31           C  
ATOM  16722  CD  PRO C 412     201.185 222.365 242.001  1.00 78.79           C  
ATOM  16723  N   GLY C 413     197.369 220.399 240.089  1.00 79.90           N  
ATOM  16724  CA  GLY C 413     196.833 219.100 239.697  1.00 78.28           C  
ATOM  16725  C   GLY C 413     196.309 218.302 240.882  1.00 80.54           C  
ATOM  16726  O   GLY C 413     196.305 217.071 240.854  1.00 79.72           O  
ATOM  16727  N   GLN C 414     195.904 218.989 241.943  1.00 81.67           N  
ATOM  16728  CA  GLN C 414     195.449 218.296 243.137  1.00 82.84           C  
ATOM  16729  C   GLN C 414     193.963 218.415 243.379  1.00 84.17           C  
ATOM  16730  O   GLN C 414     193.319 219.366 242.934  1.00 84.09           O  
ATOM  16731  CB  GLN C 414     196.187 218.802 244.362  1.00 83.25           C  
ATOM  16732  CG  GLN C 414     197.655 218.691 244.245  1.00 82.70           C  
ATOM  16733  CD  GLN C 414     198.106 217.292 244.008  1.00 81.67           C  
ATOM  16734  OE1 GLN C 414     197.781 216.376 244.769  1.00 84.03           O  
ATOM  16735  NE2 GLN C 414     198.855 217.101 242.927  1.00 82.06           N  
ATOM  16736  N   THR C 415     193.449 217.461 244.140  1.00 84.33           N  
ATOM  16737  CA  THR C 415     192.070 217.443 244.601  1.00 85.46           C  
ATOM  16738  C   THR C 415     192.055 217.287 246.115  1.00 86.50           C  
ATOM  16739  O   THR C 415     193.042 216.844 246.704  1.00 86.15           O  
ATOM  16740  CB  THR C 415     191.301 216.287 243.948  1.00 84.22           C  
ATOM  16741  N   GLY C 416     190.940 217.627 246.750  1.00 86.38           N  
ATOM  16742  CA  GLY C 416     190.842 217.495 248.201  1.00 87.80           C  
ATOM  16743  C   GLY C 416     190.059 218.650 248.811  1.00 91.17           C  
ATOM  16744  O   GLY C 416     189.648 219.572 248.113  1.00 88.90           O  
ATOM  16745  N   LYS C 417     189.860 218.626 250.123  1.00 89.63           N  
ATOM  16746  CA  LYS C 417     189.021 219.644 250.745  1.00 89.72           C  
ATOM  16747  C   LYS C 417     189.593 221.048 250.555  1.00 87.87           C  
ATOM  16748  O   LYS C 417     188.847 222.010 250.374  1.00 88.91           O  
ATOM  16749  CB  LYS C 417     188.846 219.355 252.236  1.00 90.66           C  
ATOM  16750  N   ILE C 418     190.911 221.180 250.568  1.00 88.50           N  
ATOM  16751  CA  ILE C 418     191.489 222.496 250.370  1.00 88.84           C  
ATOM  16752  C   ILE C 418     191.636 222.775 248.899  1.00 80.06           C  
ATOM  16753  O   ILE C 418     191.215 223.825 248.408  1.00113.31           O  
ATOM  16754  CB  ILE C 418     192.839 222.655 251.075  1.00 88.84           C  
ATOM  16755  N   ALA C 419     192.184 221.813 248.174  1.00 85.74           N  
ATOM  16756  CA  ALA C 419     192.413 222.005 246.755  1.00 88.38           C  
ATOM  16757  C   ALA C 419     191.119 222.367 246.022  1.00 87.53           C  
ATOM  16758  O   ALA C 419     191.149 223.139 245.066  1.00 86.07           O  
ATOM  16759  CB  ALA C 419     193.010 220.748 246.150  1.00 85.78           C  
ATOM  16760  N   ASP C 420     189.985 221.803 246.449  1.00 87.72           N  
ATOM  16761  CA  ASP C 420     188.722 222.066 245.772  1.00 87.42           C  
ATOM  16762  C   ASP C 420     187.858 223.190 246.369  1.00 88.17           C  
ATOM  16763  O   ASP C 420     187.146 223.862 245.622  1.00 89.08           O  
ATOM  16764  CB  ASP C 420     187.884 220.787 245.710  1.00 89.09           C  
ATOM  16765  N   TYR C 421     187.873 223.396 247.694  1.00 89.74           N  
ATOM  16766  CA  TYR C 421     186.948 224.372 248.275  1.00 89.21           C  
ATOM  16767  C   TYR C 421     187.578 225.618 248.904  1.00 90.11           C  
ATOM  16768  O   TYR C 421     186.853 226.552 249.252  1.00 89.86           O  
ATOM  16769  CB  TYR C 421     186.080 223.689 249.331  1.00 91.34           C  
ATOM  16770  CG  TYR C 421     185.229 222.585 248.797  1.00 91.22           C  
ATOM  16771  CD1 TYR C 421     185.665 221.284 248.899  1.00 91.56           C  
ATOM  16772  CD2 TYR C 421     184.009 222.870 248.210  1.00 90.10           C  
ATOM  16773  CE1 TYR C 421     184.892 220.261 248.415  1.00 90.75           C  
ATOM  16774  CE2 TYR C 421     183.230 221.848 247.726  1.00 90.50           C  
ATOM  16775  CZ  TYR C 421     183.670 220.545 247.827  1.00 92.23           C  
ATOM  16776  OH  TYR C 421     182.893 219.515 247.343  1.00 91.70           O  
ATOM  16777  N   ASN C 422     188.896 225.627 249.122  1.00 89.37           N  
ATOM  16778  CA  ASN C 422     189.490 226.743 249.856  1.00 88.92           C  
ATOM  16779  C   ASN C 422     190.615 227.444 249.092  1.00 88.88           C  
ATOM  16780  O   ASN C 422     190.637 228.675 248.999  1.00 86.64           O  
ATOM  16781  CB  ASN C 422     190.001 226.239 251.183  1.00 89.49           C  
ATOM  16782  N   TYR C 423     191.550 226.654 248.565  1.00 87.52           N  
ATOM  16783  CA  TYR C 423     192.739 227.179 247.900  1.00 86.26           C  
ATOM  16784  C   TYR C 423     193.162 226.315 246.727  1.00 86.75           C  
ATOM  16785  O   TYR C 423     193.831 225.295 246.895  1.00 85.20           O  
ATOM  16786  CB  TYR C 423     193.906 227.286 248.879  1.00 85.25           C  
ATOM  16787  CG  TYR C 423     195.147 227.911 248.281  1.00 84.85           C  
ATOM  16788  CD1 TYR C 423     195.182 229.259 248.055  1.00 83.59           C  
ATOM  16789  CD2 TYR C 423     196.242 227.135 247.963  1.00 84.63           C  
ATOM  16790  CE1 TYR C 423     196.285 229.856 247.528  1.00 81.87           C  
ATOM  16791  CE2 TYR C 423     197.358 227.732 247.431  1.00 82.98           C  
ATOM  16792  CZ  TYR C 423     197.377 229.092 247.218  1.00 81.55           C  
ATOM  16793  OH  TYR C 423     198.485 229.694 246.700  1.00 80.23           O  
ATOM  16794  N   LYS C 424     192.784 226.735 245.530  1.00 84.34           N  
ATOM  16795  CA  LYS C 424     193.085 225.974 244.329  1.00 83.03           C  
ATOM  16796  C   LYS C 424     194.194 226.629 243.522  1.00 82.71           C  
ATOM  16797  O   LYS C 424     194.161 227.832 243.264  1.00 81.92           O  
ATOM  16798  CB  LYS C 424     191.831 225.830 243.461  1.00 82.88           C  
ATOM  16799  CG  LYS C 424     192.020 225.005 242.188  1.00 82.26           C  
ATOM  16800  CD  LYS C 424     190.687 224.782 241.471  1.00 82.82           C  
ATOM  16801  CE  LYS C 424     190.871 224.108 240.107  1.00 81.95           C  
ATOM  16802  NZ  LYS C 424     191.336 222.689 240.228  1.00 83.42           N  
ATOM  16803  N   LEU C 425     195.164 225.832 243.102  1.00 81.52           N  
ATOM  16804  CA  LEU C 425     196.221 226.315 242.224  1.00 80.87           C  
ATOM  16805  C   LEU C 425     195.930 225.917 240.779  1.00 81.21           C  
ATOM  16806  O   LEU C 425     195.189 224.961 240.552  1.00 81.07           O  
ATOM  16807  CB  LEU C 425     197.592 225.767 242.652  1.00 79.35           C  
ATOM  16808  CG  LEU C 425     198.117 226.223 244.015  1.00 80.00           C  
ATOM  16809  CD1 LEU C 425     199.400 225.476 244.326  1.00 78.85           C  
ATOM  16810  CD2 LEU C 425     198.393 227.722 243.975  1.00 79.44           C  
ATOM  16811  N   PRO C 426     196.462 226.654 239.794  1.00 79.34           N  
ATOM  16812  CA  PRO C 426     196.471 226.327 238.383  1.00 78.19           C  
ATOM  16813  C   PRO C 426     197.246 225.045 238.150  1.00 77.54           C  
ATOM  16814  O   PRO C 426     198.120 224.699 238.940  1.00 77.65           O  
ATOM  16815  CB  PRO C 426     197.205 227.514 237.753  1.00 78.29           C  
ATOM  16816  CG  PRO C 426     197.072 228.634 238.740  1.00 79.09           C  
ATOM  16817  CD  PRO C 426     197.038 227.976 240.100  1.00 78.76           C  
ATOM  16818  N   ASP C 427     196.973 224.369 237.042  1.00 77.44           N  
ATOM  16819  CA  ASP C 427     197.696 223.145 236.711  1.00 77.37           C  
ATOM  16820  C   ASP C 427     199.044 223.493 236.099  1.00 77.50           C  
ATOM  16821  O   ASP C 427     199.997 222.720 236.184  1.00 77.35           O  
ATOM  16822  CB  ASP C 427     196.883 222.289 235.743  1.00 76.52           C  
ATOM  16823  CG  ASP C 427     195.611 221.764 236.367  1.00 76.67           C  
ATOM  16824  OD1 ASP C 427     195.692 220.984 237.286  1.00 74.85           O  
ATOM  16825  OD2 ASP C 427     194.561 222.162 235.928  1.00 76.99           O  
ATOM  16826  N   ASP C 428     199.119 224.677 235.494  1.00 76.72           N  
ATOM  16827  CA  ASP C 428     200.326 225.196 234.872  1.00 76.05           C  
ATOM  16828  C   ASP C 428     201.001 226.210 235.793  1.00 76.46           C  
ATOM  16829  O   ASP C 428     201.691 227.126 235.344  1.00 75.18           O  
ATOM  16830  CB  ASP C 428     199.986 225.825 233.524  1.00 77.02           C  
ATOM  16831  CG  ASP C 428     198.942 226.925 233.642  1.00 77.35           C  
ATOM  16832  OD1 ASP C 428     198.855 227.742 232.755  1.00 77.86           O  
ATOM  16833  OD2 ASP C 428     198.192 226.902 234.604  1.00 77.51           O  
ATOM  16834  N   PHE C 429     200.786 226.035 237.089  1.00 76.19           N  
ATOM  16835  CA  PHE C 429     201.319 226.917 238.109  1.00 75.21           C  
ATOM  16836  C   PHE C 429     202.830 227.042 238.073  1.00 73.74           C  
ATOM  16837  O   PHE C 429     203.559 226.050 238.042  1.00 72.20           O  
ATOM  16838  CB  PHE C 429     200.913 226.401 239.490  1.00 75.57           C  
ATOM  16839  CG  PHE C 429     201.519 227.152 240.632  1.00 75.69           C  
ATOM  16840  CD1 PHE C 429     201.075 228.412 240.977  1.00 75.62           C  
ATOM  16841  CD2 PHE C 429     202.552 226.581 241.370  1.00 73.74           C  
ATOM  16842  CE1 PHE C 429     201.648 229.088 242.027  1.00 74.11           C  
ATOM  16843  CE2 PHE C 429     203.121 227.257 242.422  1.00 73.96           C  
ATOM  16844  CZ  PHE C 429     202.668 228.511 242.749  1.00 73.66           C  
ATOM  16845  N   THR C 430     203.292 228.286 238.125  1.00 73.17           N  
ATOM  16846  CA  THR C 430     204.707 228.578 238.210  1.00 70.89           C  
ATOM  16847  C   THR C 430     204.920 229.311 239.514  1.00 72.04           C  
ATOM  16848  O   THR C 430     204.258 230.314 239.786  1.00 72.51           O  
ATOM  16849  CB  THR C 430     205.212 229.430 237.034  1.00 69.02           C  
ATOM  16850  OG1 THR C 430     204.978 228.737 235.798  1.00 69.85           O  
ATOM  16851  CG2 THR C 430     206.724 229.677 237.191  1.00 67.32           C  
ATOM  16852  N   GLY C 431     205.814 228.796 240.328  1.00 72.29           N  
ATOM  16853  CA  GLY C 431     206.033 229.340 241.653  1.00 71.69           C  
ATOM  16854  C   GLY C 431     206.631 228.270 242.539  1.00 72.08           C  
ATOM  16855  O   GLY C 431     206.941 227.169 242.060  1.00 71.69           O  
ATOM  16856  N   CYS C 432     206.795 228.608 243.826  1.00 72.79           N  
ATOM  16857  CA  CYS C 432     207.353 227.721 244.845  1.00 72.95           C  
ATOM  16858  C   CYS C 432     206.431 227.713 246.068  1.00 74.64           C  
ATOM  16859  O   CYS C 432     205.938 228.765 246.492  1.00 75.49           O  
ATOM  16860  CB  CYS C 432     208.785 228.155 245.256  1.00 73.97           C  
ATOM  16861  SG  CYS C 432     210.003 228.247 243.872  1.00 69.41           S  
ATOM  16862  N   VAL C 433     206.216 226.521 246.639  1.00 74.68           N  
ATOM  16863  CA  VAL C 433     205.419 226.311 247.846  1.00 77.22           C  
ATOM  16864  C   VAL C 433     206.333 226.047 249.025  1.00 77.86           C  
ATOM  16865  O   VAL C 433     207.137 225.112 249.014  1.00 77.78           O  
ATOM  16866  CB  VAL C 433     204.452 225.131 247.659  1.00 76.30           C  
ATOM  16867  CG1 VAL C 433     203.677 224.872 248.948  1.00 78.80           C  
ATOM  16868  CG2 VAL C 433     203.479 225.447 246.525  1.00 76.92           C  
ATOM  16869  N   ILE C 434     206.221 226.895 250.033  1.00 77.61           N  
ATOM  16870  CA  ILE C 434     207.058 226.797 251.211  1.00 78.33           C  
ATOM  16871  C   ILE C 434     206.191 226.606 252.448  1.00 80.31           C  
ATOM  16872  O   ILE C 434     205.229 227.344 252.656  1.00 81.77           O  
ATOM  16873  CB  ILE C 434     207.914 228.064 251.348  1.00 78.90           C  
ATOM  16874  CG1 ILE C 434     208.773 228.244 250.086  1.00 77.36           C  
ATOM  16875  CG2 ILE C 434     208.801 227.941 252.575  1.00 80.32           C  
ATOM  16876  CD1 ILE C 434     209.405 229.612 249.956  1.00 77.35           C  
ATOM  16877  N   ALA C 435     206.512 225.620 253.275  1.00 81.21           N  
ATOM  16878  CA  ALA C 435     205.693 225.407 254.465  1.00 83.16           C  
ATOM  16879  C   ALA C 435     206.514 224.920 255.647  1.00 83.39           C  
ATOM  16880  O   ALA C 435     207.552 224.266 255.488  1.00 84.27           O  
ATOM  16881  CB  ALA C 435     204.572 224.422 254.171  1.00 83.91           C  
ATOM  16882  N   TRP C 436     206.029 225.240 256.845  1.00 86.67           N  
ATOM  16883  CA  TRP C 436     206.686 224.816 258.071  1.00 84.55           C  
ATOM  16884  C   TRP C 436     205.701 224.618 259.207  1.00 83.33           C  
ATOM  16885  O   TRP C 436     204.601 225.168 259.202  1.00 98.41           O  
ATOM  16886  CB  TRP C 436     207.747 225.839 258.448  1.00 85.29           C  
ATOM  16887  CG  TRP C 436     207.243 227.195 258.795  1.00 85.24           C  
ATOM  16888  CD1 TRP C 436     207.095 227.698 260.044  1.00 86.35           C  
ATOM  16889  CD2 TRP C 436     206.805 228.241 257.888  1.00 84.92           C  
ATOM  16890  NE1 TRP C 436     206.625 228.978 259.982  1.00 86.47           N  
ATOM  16891  CE2 TRP C 436     206.439 229.322 258.670  1.00 85.85           C  
ATOM  16892  CE3 TRP C 436     206.699 228.343 256.496  1.00 84.26           C  
ATOM  16893  CZ2 TRP C 436     205.979 230.494 258.118  1.00 85.39           C  
ATOM  16894  CZ3 TRP C 436     206.230 229.511 255.947  1.00 83.82           C  
ATOM  16895  CH2 TRP C 436     205.881 230.560 256.737  1.00 84.00           C  
ATOM  16896  N   ASN C 437     206.099 223.824 260.188  1.00 88.95           N  
ATOM  16897  CA  ASN C 437     205.252 223.556 261.340  1.00 89.15           C  
ATOM  16898  C   ASN C 437     205.109 224.773 262.242  1.00 89.74           C  
ATOM  16899  O   ASN C 437     206.083 225.474 262.511  1.00 89.13           O  
ATOM  16900  CB  ASN C 437     205.797 222.365 262.098  1.00 90.12           C  
ATOM  16901  N   SER C 438     203.897 224.984 262.746  1.00 89.83           N  
ATOM  16902  CA  SER C 438     203.600 226.077 263.664  1.00 91.28           C  
ATOM  16903  C   SER C 438     202.969 225.547 264.951  1.00 98.55           C  
ATOM  16904  O   SER C 438     202.163 226.217 265.611  1.00 97.33           O  
ATOM  16905  CB  SER C 438     202.700 227.077 262.983  1.00 90.08           C  
ATOM  16906  OG  SER C 438     201.531 226.475 262.535  1.00 91.04           O  
ATOM  16907  N   ASN C 439     203.371 224.336 265.324  1.00 93.51           N  
ATOM  16908  CA  ASN C 439     202.859 223.675 266.519  1.00 95.06           C  
ATOM  16909  C   ASN C 439     203.231 224.440 267.782  1.00 94.72           C  
ATOM  16910  O   ASN C 439     202.554 224.340 268.801  1.00 95.14           O  
ATOM  16911  CB  ASN C 439     203.368 222.253 266.603  1.00 94.83           C  
ATOM  16912  CG  ASN C 439     202.609 221.442 267.595  1.00 96.40           C  
ATOM  16913  OD1 ASN C 439     201.385 221.336 267.473  1.00 96.98           O  
ATOM  16914  ND2 ASN C 439     203.293 220.870 268.563  1.00 96.87           N  
ATOM  16915  N   ASN C 440     204.319 225.197 267.724  1.00 94.05           N  
ATOM  16916  CA  ASN C 440     204.749 225.984 268.863  1.00 95.02           C  
ATOM  16917  C   ASN C 440     204.352 227.448 268.724  1.00 94.52           C  
ATOM  16918  O   ASN C 440     204.824 228.293 269.487  1.00 94.56           O  
ATOM  16919  CB  ASN C 440     206.245 225.867 269.032  1.00 96.38           C  
ATOM  16920  N   LEU C 441     203.496 227.751 267.751  1.00 92.60           N  
ATOM  16921  CA  LEU C 441     203.095 229.127 267.511  1.00 94.25           C  
ATOM  16922  C   LEU C 441     201.581 229.298 267.550  1.00 94.84           C  
ATOM  16923  O   LEU C 441     201.058 230.124 268.298  1.00 95.71           O  
ATOM  16924  CB  LEU C 441     203.596 229.576 266.137  1.00 93.59           C  
ATOM  16925  N   ASP C 442     200.882 228.537 266.709  1.00 94.48           N  
ATOM  16926  CA  ASP C 442     199.440 228.689 266.578  1.00 95.03           C  
ATOM  16927  C   ASP C 442     198.664 227.714 267.454  1.00 96.65           C  
ATOM  16928  O   ASP C 442     197.578 228.034 267.928  1.00 96.23           O  
ATOM  16929  CB  ASP C 442     199.021 228.515 265.117  1.00 94.66           C  
ATOM  16930  N   SER C 443     199.200 226.517 267.670  1.00 94.42           N  
ATOM  16931  CA  SER C 443     198.457 225.531 268.466  1.00 98.11           C  
ATOM  16932  C   SER C 443     198.313 226.003 269.914  1.00 98.54           C  
ATOM  16933  O   SER C 443     199.222 226.648 270.442  1.00 97.82           O  
ATOM  16934  CB  SER C 443     199.145 224.190 268.444  1.00 98.09           C  
ATOM  16935  N   LYS C 444     197.173 225.670 270.559  1.00 98.53           N  
ATOM  16936  CA  LYS C 444     196.895 226.044 271.956  1.00 98.61           C  
ATOM  16937  C   LYS C 444     196.235 224.892 272.713  1.00 99.49           C  
ATOM  16938  O   LYS C 444     195.788 223.907 272.125  1.00 99.42           O  
ATOM  16939  CB  LYS C 444     195.994 227.313 272.042  1.00 99.59           C  
ATOM  16940  N   ASN C 448     193.546 225.722 269.520  1.00 97.51           N  
ATOM  16941  CA  ASN C 448     193.271 226.896 268.712  1.00 97.64           C  
ATOM  16942  C   ASN C 448     192.258 226.521 267.620  1.00 96.93           C  
ATOM  16943  O   ASN C 448     192.550 225.701 266.743  1.00 95.65           O  
ATOM  16944  CB  ASN C 448     194.562 227.485 268.114  1.00 96.42           C  
ATOM  16945  CG  ASN C 448     194.367 228.896 267.421  1.00 96.43           C  
ATOM  16946  OD1 ASN C 448     193.267 229.235 266.947  1.00 96.02           O  
ATOM  16947  ND2 ASN C 448     195.438 229.696 267.366  1.00 96.13           N  
ATOM  16948  N   TYR C 449     191.062 227.125 267.694  1.00 96.75           N  
ATOM  16949  CA  TYR C 449     189.935 226.879 266.788  1.00 97.90           C  
ATOM  16950  C   TYR C 449     189.600 228.109 265.952  1.00 98.36           C  
ATOM  16951  O   TYR C 449     188.459 228.283 265.526  1.00 96.70           O  
ATOM  16952  CB  TYR C 449     188.720 226.432 267.598  1.00 98.29           C  
ATOM  16953  N   ASN C 450     190.592 228.969 265.717  1.00 95.22           N  
ATOM  16954  CA  ASN C 450     190.357 230.202 264.968  1.00 96.53           C  
ATOM  16955  C   ASN C 450     190.675 230.076 263.484  1.00 95.84           C  
ATOM  16956  O   ASN C 450     190.690 231.071 262.761  1.00 95.05           O  
ATOM  16957  CB  ASN C 450     191.171 231.334 265.551  1.00 97.18           C  
ATOM  16958  CG  ASN C 450     190.734 231.698 266.917  1.00 96.44           C  
ATOM  16959  OD1 ASN C 450     189.686 232.322 267.120  1.00 95.42           O  
ATOM  16960  ND2 ASN C 450     191.521 231.312 267.878  1.00 97.40           N  
ATOM  16961  N   TYR C 451     190.929 228.861 263.023  1.00 95.41           N  
ATOM  16962  CA  TYR C 451     191.223 228.652 261.616  1.00 94.54           C  
ATOM  16963  C   TYR C 451     190.104 227.882 260.939  1.00 95.87           C  
ATOM  16964  O   TYR C 451     189.876 226.706 261.236  1.00 95.21           O  
ATOM  16965  CB  TYR C 451     192.554 227.932 261.460  1.00 93.84           C  
ATOM  16966  CG  TYR C 451     193.669 228.725 262.038  1.00 94.16           C  
ATOM  16967  CD1 TYR C 451     194.159 228.402 263.281  1.00 94.83           C  
ATOM  16968  CD2 TYR C 451     194.183 229.801 261.346  1.00 92.64           C  
ATOM  16969  CE1 TYR C 451     195.168 229.142 263.827  1.00 95.22           C  
ATOM  16970  CE2 TYR C 451     195.191 230.547 261.894  1.00 92.68           C  
ATOM  16971  CZ  TYR C 451     195.683 230.218 263.131  1.00 93.77           C  
ATOM  16972  OH  TYR C 451     196.682 230.961 263.691  1.00 94.37           O  
ATOM  16973  N   LEU C 452     189.394 228.563 260.040  1.00 94.07           N  
ATOM  16974  CA  LEU C 452     188.242 227.983 259.366  1.00 93.81           C  
ATOM  16975  C   LEU C 452     188.539 227.487 257.955  1.00 94.18           C  
ATOM  16976  O   LEU C 452     189.415 228.016 257.257  1.00 92.44           O  
ATOM  16977  CB  LEU C 452     187.091 228.993 259.312  1.00 94.77           C  
ATOM  16978  N   TYR C 453     187.779 226.468 257.551  1.00 93.16           N  
ATOM  16979  CA  TYR C 453     187.872 225.860 256.228  1.00 90.54           C  
ATOM  16980  C   TYR C 453     186.541 225.223 255.814  1.00 94.79           C  
ATOM  16981  O   TYR C 453     185.717 224.903 256.670  1.00101.10           O  
ATOM  16982  CB  TYR C 453     188.943 224.778 256.254  1.00 93.53           C  
ATOM  16983  CG  TYR C 453     188.548 223.578 257.072  1.00 92.39           C  
ATOM  16984  CD1 TYR C 453     188.059 222.445 256.450  1.00 93.84           C  
ATOM  16985  CD2 TYR C 453     188.662 223.610 258.440  1.00100.89           C  
ATOM  16986  CE1 TYR C 453     187.701 221.352 257.203  1.00 93.81           C  
ATOM  16987  CE2 TYR C 453     188.309 222.522 259.188  1.00 93.82           C  
ATOM  16988  CZ  TYR C 453     187.833 221.394 258.578  1.00 95.78           C  
ATOM  16989  OH  TYR C 453     187.482 220.305 259.339  1.00 95.82           O  
ATOM  16990  N   ARG C 454     186.366 224.969 254.510  1.00 93.40           N  
ATOM  16991  CA  ARG C 454     185.248 224.176 253.979  1.00 92.98           C  
ATOM  16992  C   ARG C 454     185.703 222.739 253.721  1.00 92.54           C  
ATOM  16993  O   ARG C 454     186.780 222.507 253.167  1.00 91.90           O  
ATOM  16994  CB  ARG C 454     184.706 224.784 252.687  1.00 92.45           C  
ATOM  16995  CG  ARG C 454     183.903 226.113 252.837  1.00 92.38           C  
ATOM  16996  CD  ARG C 454     183.534 226.734 251.500  1.00 93.60           C  
ATOM  16997  NE  ARG C 454     184.698 227.417 250.865  1.00 92.16           N  
ATOM  16998  CZ  ARG C 454     185.079 228.735 251.024  1.00 92.96           C  
ATOM  16999  NH1 ARG C 454     184.381 229.577 251.776  1.00 92.40           N  
ATOM  17000  NH2 ARG C 454     186.149 229.169 250.391  1.00 91.35           N  
ATOM  17001  N   LYS C 462     187.602 227.713 241.072  1.00 79.96           N  
ATOM  17002  CA  LYS C 462     188.588 228.172 240.108  1.00 80.06           C  
ATOM  17003  C   LYS C 462     189.921 228.491 240.824  1.00 81.92           C  
ATOM  17004  O   LYS C 462     189.914 228.709 242.044  1.00 82.58           O  
ATOM  17005  CB  LYS C 462     188.066 229.416 239.336  1.00 81.52           C  
ATOM  17006  N   PRO C 463     191.094 228.493 240.113  1.00 81.07           N  
ATOM  17007  CA  PRO C 463     192.403 228.845 240.646  1.00 80.78           C  
ATOM  17008  C   PRO C 463     192.385 230.238 241.253  1.00 80.84           C  
ATOM  17009  O   PRO C 463     191.851 231.172 240.656  1.00 79.55           O  
ATOM  17010  CB  PRO C 463     193.298 228.786 239.405  1.00 80.65           C  
ATOM  17011  CG  PRO C 463     192.621 227.809 238.486  1.00 80.10           C  
ATOM  17012  CD  PRO C 463     191.153 228.068 238.672  1.00 81.20           C  
ATOM  17013  N   PHE C 464     192.950 230.354 242.442  1.00 80.72           N  
ATOM  17014  CA  PHE C 464     193.015 231.606 243.184  1.00 80.15           C  
ATOM  17015  C   PHE C 464     191.649 232.230 243.472  1.00 81.08           C  
ATOM  17016  O   PHE C 464     191.558 233.437 243.704  1.00 81.13           O  
ATOM  17017  CB  PHE C 464     193.918 232.605 242.471  1.00 80.14           C  
ATOM  17018  CG  PHE C 464     195.330 232.124 242.360  1.00 79.44           C  
ATOM  17019  CD1 PHE C 464     195.863 231.762 241.142  1.00 78.93           C  
ATOM  17020  CD2 PHE C 464     196.130 232.027 243.486  1.00 79.28           C  
ATOM  17021  CE1 PHE C 464     197.165 231.321 241.048  1.00 79.04           C  
ATOM  17022  CE2 PHE C 464     197.428 231.581 243.393  1.00 79.13           C  
ATOM  17023  CZ  PHE C 464     197.946 231.229 242.171  1.00 78.26           C  
ATOM  17024  N   GLU C 465     190.596 231.415 243.506  1.00 81.65           N  
ATOM  17025  CA  GLU C 465     189.280 231.907 243.893  1.00 82.18           C  
ATOM  17026  C   GLU C 465     189.183 231.966 245.408  1.00 83.06           C  
ATOM  17027  O   GLU C 465     189.402 230.963 246.086  1.00 83.47           O  
ATOM  17028  CB  GLU C 465     188.172 230.992 243.352  1.00 81.54           C  
ATOM  17029  N   ARG C 466     188.843 233.128 245.943  1.00 82.71           N  
ATOM  17030  CA  ARG C 466     188.748 233.279 247.388  1.00 84.34           C  
ATOM  17031  C   ARG C 466     187.323 233.588 247.823  1.00 86.30           C  
ATOM  17032  O   ARG C 466     186.894 234.740 247.822  1.00 86.76           O  
ATOM  17033  CB  ARG C 466     189.689 234.374 247.860  1.00 83.53           C  
ATOM  17034  CG  ARG C 466     189.802 234.548 249.358  1.00 84.16           C  
ATOM  17035  CD  ARG C 466     190.945 235.422 249.702  1.00 84.49           C  
ATOM  17036  NE  ARG C 466     190.804 236.729 249.103  1.00 82.47           N  
ATOM  17037  CZ  ARG C 466     191.689 237.738 249.216  1.00 82.51           C  
ATOM  17038  NH1 ARG C 466     192.784 237.597 249.926  1.00 81.42           N  
ATOM  17039  NH2 ARG C 466     191.449 238.883 248.606  1.00 81.55           N  
ATOM  17040  N   ASP C 467     186.595 232.537 248.183  1.00 87.92           N  
ATOM  17041  CA  ASP C 467     185.201 232.641 248.593  1.00 90.18           C  
ATOM  17042  C   ASP C 467     185.100 232.790 250.106  1.00 90.88           C  
ATOM  17043  O   ASP C 467     185.474 231.884 250.853  1.00 90.98           O  
ATOM  17044  CB  ASP C 467     184.384 231.423 248.142  1.00 89.85           C  
ATOM  17045  CG  ASP C 467     182.882 231.554 248.478  1.00 90.84           C  
ATOM  17046  OD1 ASP C 467     182.534 232.498 249.155  1.00 92.34           O  
ATOM  17047  OD2 ASP C 467     182.111 230.718 248.066  1.00 91.90           O  
ATOM  17048  N   ILE C 468     184.661 233.953 250.550  1.00 90.89           N  
ATOM  17049  CA  ILE C 468     184.601 234.219 251.975  1.00 91.32           C  
ATOM  17050  C   ILE C 468     183.171 234.345 252.472  1.00 93.47           C  
ATOM  17051  O   ILE C 468     182.941 234.807 253.587  1.00 93.58           O  
ATOM  17052  CB  ILE C 468     185.389 235.484 252.325  1.00 92.47           C  
ATOM  17053  CG1 ILE C 468     184.760 236.710 251.601  1.00 92.77           C  
ATOM  17054  CG2 ILE C 468     186.846 235.274 251.933  1.00 89.85           C  
ATOM  17055  CD1 ILE C 468     185.311 238.055 252.051  1.00 93.33           C  
ATOM  17056  N   SER C 469     182.213 233.950 251.641  1.00 93.18           N  
ATOM  17057  CA  SER C 469     180.799 233.999 252.023  1.00 94.28           C  
ATOM  17058  C   SER C 469     180.548 233.052 253.198  1.00 95.57           C  
ATOM  17059  O   SER C 469     181.161 231.989 253.286  1.00 95.59           O  
ATOM  17060  CB  SER C 469     179.919 233.601 250.855  1.00 94.84           C  
ATOM  17061  N   THR C 470     179.632 233.452 254.102  1.00 96.37           N  
ATOM  17062  CA  THR C 470     179.250 232.693 255.293  1.00 96.42           C  
ATOM  17063  C   THR C 470     177.804 232.216 255.176  1.00 96.92           C  
ATOM  17064  O   THR C 470     176.854 232.971 255.429  1.00 96.86           O  
ATOM  17065  CB  THR C 470     179.453 233.539 256.586  1.00 97.90           C  
ATOM  17066  N   PRO C 491     178.696 226.521 256.482  1.00 98.00           N  
ATOM  17067  CA  PRO C 491     179.721 226.003 255.565  1.00 97.12           C  
ATOM  17068  C   PRO C 491     181.146 225.882 256.109  1.00 96.31           C  
ATOM  17069  O   PRO C 491     181.949 225.134 255.548  1.00 94.56           O  
ATOM  17070  CB  PRO C 491     179.699 227.036 254.427  1.00 96.52           C  
ATOM  17071  CG  PRO C 491     179.194 228.310 255.056  1.00 98.14           C  
ATOM  17072  CD  PRO C 491     178.178 227.869 256.058  1.00 98.31           C  
ATOM  17073  N   LEU C 492     181.478 226.602 257.169  1.00 96.13           N  
ATOM  17074  CA  LEU C 492     182.843 226.545 257.674  1.00 95.81           C  
ATOM  17075  C   LEU C 492     182.982 225.740 258.954  1.00 96.42           C  
ATOM  17076  O   LEU C 492     182.152 225.820 259.862  1.00 96.38           O  
ATOM  17077  CB  LEU C 492     183.370 227.960 257.912  1.00 94.33           C  
ATOM  17078  CG  LEU C 492     183.462 228.873 256.671  1.00 94.17           C  
ATOM  17079  CD1 LEU C 492     183.773 230.288 257.094  1.00 93.51           C  
ATOM  17080  CD2 LEU C 492     184.566 228.376 255.767  1.00 93.66           C  
ATOM  17081  N   GLN C 493     184.078 225.005 259.028  1.00 96.46           N  
ATOM  17082  CA  GLN C 493     184.452 224.217 260.183  1.00 94.76           C  
ATOM  17083  C   GLN C 493     185.793 224.701 260.678  1.00 94.02           C  
ATOM  17084  O   GLN C 493     186.554 225.286 259.910  1.00 94.10           O  
ATOM  17085  CB  GLN C 493     184.502 222.739 259.815  1.00 95.18           C  
ATOM  17086  CG  GLN C 493     183.164 222.187 259.333  1.00 95.69           C  
ATOM  17087  CD  GLN C 493     182.963 222.330 257.819  1.00 95.76           C  
ATOM  17088  OE1 GLN C 493     183.852 221.993 257.033  1.00 94.85           O  
ATOM  17089  NE2 GLN C 493     181.793 222.817 257.409  1.00 97.00           N  
ATOM  17090  N   SER C 494     186.087 224.491 261.954  1.00 95.95           N  
ATOM  17091  CA  SER C 494     187.382 224.896 262.476  1.00 96.21           C  
ATOM  17092  C   SER C 494     188.324 223.718 262.641  1.00 95.52           C  
ATOM  17093  O   SER C 494     187.886 222.584 262.846  1.00 95.62           O  
ATOM  17094  CB  SER C 494     187.208 225.575 263.804  1.00 96.06           C  
ATOM  17095  OG  SER C 494     186.614 224.708 264.727  1.00 96.84           O  
ATOM  17096  N   TYR C 495     189.617 224.002 262.602  1.00 94.95           N  
ATOM  17097  CA  TYR C 495     190.621 222.986 262.873  1.00 95.45           C  
ATOM  17098  C   TYR C 495     190.989 222.979 264.350  1.00 97.27           C  
ATOM  17099  O   TYR C 495     191.383 224.002 264.903  1.00 97.33           O  
ATOM  17100  CB  TYR C 495     191.903 223.248 262.093  1.00 95.69           C  
ATOM  17101  CG  TYR C 495     191.860 223.087 260.588  1.00 96.18           C  
ATOM  17102  CD1 TYR C 495     191.813 224.206 259.774  1.00 95.11           C  
ATOM  17103  CD2 TYR C 495     191.907 221.824 260.024  1.00 96.24           C  
ATOM  17104  CE1 TYR C 495     191.825 224.059 258.404  1.00 94.95           C  
ATOM  17105  CE2 TYR C 495     191.912 221.675 258.650  1.00 94.22           C  
ATOM  17106  CZ  TYR C 495     191.873 222.785 257.840  1.00 94.14           C  
ATOM  17107  OH  TYR C 495     191.895 222.642 256.465  1.00 92.99           O  
ATOM  17108  N   GLY C 496     190.912 221.824 264.986  1.00 96.63           N  
ATOM  17109  CA  GLY C 496     191.266 221.734 266.400  1.00 96.99           C  
ATOM  17110  C   GLY C 496     192.767 221.600 266.593  1.00 98.18           C  
ATOM  17111  O   GLY C 496     193.269 220.499 266.823  1.00 97.26           O  
ATOM  17112  N   PHE C 497     193.496 222.706 266.478  1.00 96.76           N  
ATOM  17113  CA  PHE C 497     194.947 222.626 266.561  1.00 97.05           C  
ATOM  17114  C   PHE C 497     195.449 222.656 268.000  1.00 98.25           C  
ATOM  17115  O   PHE C 497     195.286 223.649 268.715  1.00 98.11           O  
ATOM  17116  CB  PHE C 497     195.598 223.772 265.784  1.00 98.10           C  
ATOM  17117  CG  PHE C 497     195.453 223.697 264.280  1.00 96.84           C  
ATOM  17118  CD1 PHE C 497     195.052 224.814 263.562  1.00 96.32           C  
ATOM  17119  CD2 PHE C 497     195.720 222.528 263.582  1.00 95.26           C  
ATOM  17120  CE1 PHE C 497     194.931 224.767 262.187  1.00 94.88           C  
ATOM  17121  CE2 PHE C 497     195.597 222.480 262.223  1.00 95.83           C  
ATOM  17122  CZ  PHE C 497     195.205 223.599 261.519  1.00 95.97           C  
ATOM  17123  N   GLN C 498     196.064 221.555 268.419  1.00 98.25           N  
ATOM  17124  CA  GLN C 498     196.564 221.412 269.778  1.00 99.16           C  
ATOM  17125  C   GLN C 498     198.007 220.916 269.743  1.00 98.79           C  
ATOM  17126  O   GLN C 498     198.344 220.073 268.910  1.00 98.11           O  
ATOM  17127  CB  GLN C 498     195.675 220.444 270.566  1.00 99.38           C  
ATOM  17128  N   PRO C 499     198.859 221.374 270.671  1.00 98.68           N  
ATOM  17129  CA  PRO C 499     200.283 221.106 270.745  1.00 99.28           C  
ATOM  17130  C   PRO C 499     200.605 219.647 271.015  1.00 99.10           C  
ATOM  17131  O   PRO C 499     201.741 219.215 270.819  1.00 99.45           O  
ATOM  17132  CB  PRO C 499     200.730 222.004 271.905  1.00 97.62           C  
ATOM  17133  CG  PRO C 499     199.492 222.201 272.743  1.00 98.20           C  
ATOM  17134  CD  PRO C 499     198.359 222.232 271.755  1.00 98.02           C  
ATOM  17135  N   THR C 500     199.604 218.898 271.460  1.00 98.74           N  
ATOM  17136  CA  THR C 500     199.768 217.504 271.818  1.00 99.61           C  
ATOM  17137  C   THR C 500     199.316 216.541 270.731  1.00 99.66           C  
ATOM  17138  O   THR C 500     199.300 215.330 270.954  1.00 99.31           O  
ATOM  17139  CB  THR C 500     198.975 217.188 273.091  1.00 99.50           C  
ATOM  17140  N   ASN C 501     198.914 217.052 269.569  1.00 99.06           N  
ATOM  17141  CA  ASN C 501     198.442 216.140 268.537  1.00 98.96           C  
ATOM  17142  C   ASN C 501     199.592 215.524 267.746  1.00 98.04           C  
ATOM  17143  O   ASN C 501     200.757 215.903 267.910  1.00 97.95           O  
ATOM  17144  CB  ASN C 501     197.503 216.848 267.583  1.00 98.14           C  
ATOM  17145  CG  ASN C 501     196.200 217.241 268.193  1.00 99.06           C  
ATOM  17146  OD1 ASN C 501     195.756 216.658 269.188  1.00 98.36           O  
ATOM  17147  ND2 ASN C 501     195.556 218.212 267.599  1.00 98.45           N  
ATOM  17148  N   GLY C 502     199.245 214.609 266.837  1.00 97.56           N  
ATOM  17149  CA  GLY C 502     200.242 213.964 265.996  1.00 98.24           C  
ATOM  17150  C   GLY C 502     200.653 214.917 264.900  1.00 97.76           C  
ATOM  17151  O   GLY C 502     199.963 215.896 264.645  1.00 97.67           O  
ATOM  17152  N   VAL C 503     201.725 214.601 264.194  1.00 96.40           N  
ATOM  17153  CA  VAL C 503     202.255 215.531 263.202  1.00 96.26           C  
ATOM  17154  C   VAL C 503     201.242 215.889 262.128  1.00 96.38           C  
ATOM  17155  O   VAL C 503     201.144 217.043 261.718  1.00 94.46           O  
ATOM  17156  CB  VAL C 503     203.522 214.952 262.554  1.00 96.15           C  
ATOM  17157  CG1 VAL C 503     203.958 215.825 261.381  1.00 96.17           C  
ATOM  17158  CG2 VAL C 503     204.628 214.884 263.603  1.00 96.87           C  
ATOM  17159  N   GLY C 504     200.483 214.907 261.673  1.00 95.90           N  
ATOM  17160  CA  GLY C 504     199.513 215.123 260.605  1.00 94.75           C  
ATOM  17161  C   GLY C 504     198.372 216.039 261.032  1.00 94.87           C  
ATOM  17162  O   GLY C 504     197.622 216.552 260.196  1.00 93.75           O  
ATOM  17163  N   TYR C 505     198.235 216.249 262.333  1.00 93.95           N  
ATOM  17164  CA  TYR C 505     197.167 217.072 262.852  1.00 94.85           C  
ATOM  17165  C   TYR C 505     197.666 218.394 263.407  1.00 95.13           C  
ATOM  17166  O   TYR C 505     196.890 219.175 263.960  1.00 96.50           O  
ATOM  17167  CB  TYR C 505     196.417 216.287 263.903  1.00 96.12           C  
ATOM  17168  N   GLN C 506     198.956 218.654 263.259  1.00 94.80           N  
ATOM  17169  CA  GLN C 506     199.521 219.905 263.718  1.00 94.34           C  
ATOM  17170  C   GLN C 506     199.282 220.922 262.620  1.00 93.00           C  
ATOM  17171  O   GLN C 506     199.093 220.532 261.467  1.00 95.04           O  
ATOM  17172  CB  GLN C 506     201.013 219.735 264.037  1.00 95.41           C  
ATOM  17173  CG  GLN C 506     201.272 218.854 265.262  1.00 97.39           C  
ATOM  17174  CD  GLN C 506     202.739 218.608 265.541  1.00 96.63           C  
ATOM  17175  OE1 GLN C 506     203.612 219.280 264.983  1.00 96.73           O  
ATOM  17176  NE2 GLN C 506     203.023 217.637 266.411  1.00 96.95           N  
ATOM  17177  N   PRO C 507     199.202 222.212 262.938  1.00 95.55           N  
ATOM  17178  CA  PRO C 507     199.110 223.288 261.986  1.00 95.04           C  
ATOM  17179  C   PRO C 507     200.427 223.517 261.289  1.00 88.90           C  
ATOM  17180  O   PRO C 507     201.492 223.387 261.905  1.00 93.57           O  
ATOM  17181  CB  PRO C 507     198.751 224.483 262.858  1.00 93.20           C  
ATOM  17182  CG  PRO C 507     199.330 224.152 264.200  1.00 94.74           C  
ATOM  17183  CD  PRO C 507     199.196 222.636 264.333  1.00 94.24           C  
ATOM  17184  N   TYR C 508     200.331 223.927 260.040  1.00 91.25           N  
ATOM  17185  CA  TYR C 508     201.449 224.377 259.240  1.00 90.02           C  
ATOM  17186  C   TYR C 508     201.160 225.724 258.625  1.00 89.79           C  
ATOM  17187  O   TYR C 508     200.055 225.996 258.147  1.00 88.26           O  
ATOM  17188  CB  TYR C 508     201.786 223.361 258.149  1.00 89.01           C  
ATOM  17189  CG  TYR C 508     202.515 222.157 258.645  1.00 89.33           C  
ATOM  17190  CD1 TYR C 508     201.886 221.213 259.414  1.00 90.25           C  
ATOM  17191  CD2 TYR C 508     203.838 221.997 258.302  1.00 88.76           C  
ATOM  17192  CE1 TYR C 508     202.580 220.117 259.855  1.00 92.04           C  
ATOM  17193  CE2 TYR C 508     204.533 220.905 258.736  1.00 89.81           C  
ATOM  17194  CZ  TYR C 508     203.909 219.966 259.513  1.00 90.52           C  
ATOM  17195  OH  TYR C 508     204.602 218.867 259.952  1.00 92.53           O  
ATOM  17196  N   ARG C 509     202.177 226.557 258.606  1.00 88.06           N  
ATOM  17197  CA  ARG C 509     202.088 227.839 257.953  1.00 86.39           C  
ATOM  17198  C   ARG C 509     202.572 227.681 256.536  1.00 84.31           C  
ATOM  17199  O   ARG C 509     203.663 227.162 256.288  1.00 84.36           O  
ATOM  17200  CB  ARG C 509     202.870 228.883 258.713  1.00 87.13           C  
ATOM  17201  CG  ARG C 509     202.200 229.327 259.991  1.00 88.49           C  
ATOM  17202  CD  ARG C 509     203.052 230.218 260.798  1.00 88.90           C  
ATOM  17203  NE  ARG C 509     202.314 230.774 261.927  1.00 90.28           N  
ATOM  17204  CZ  ARG C 509     202.667 231.876 262.623  1.00 90.38           C  
ATOM  17205  NH1 ARG C 509     203.760 232.541 262.317  1.00 88.07           N  
ATOM  17206  NH2 ARG C 509     201.904 232.292 263.614  1.00 91.33           N  
ATOM  17207  N   VAL C 510     201.728 228.067 255.597  1.00 87.50           N  
ATOM  17208  CA  VAL C 510     202.029 227.885 254.196  1.00 84.19           C  
ATOM  17209  C   VAL C 510     202.109 229.194 253.457  1.00 83.92           C  
ATOM  17210  O   VAL C 510     201.215 230.041 253.555  1.00 82.18           O  
ATOM  17211  CB  VAL C 510     200.950 227.018 253.525  1.00 84.88           C  
ATOM  17212  CG1 VAL C 510     201.267 226.834 252.056  1.00 83.50           C  
ATOM  17213  CG2 VAL C 510     200.861 225.695 254.213  1.00 86.75           C  
ATOM  17214  N   VAL C 511     203.185 229.364 252.721  1.00 81.19           N  
ATOM  17215  CA  VAL C 511     203.341 230.509 251.858  1.00 79.94           C  
ATOM  17216  C   VAL C 511     203.580 230.043 250.440  1.00 79.59           C  
ATOM  17217  O   VAL C 511     204.552 229.345 250.162  1.00 78.57           O  
ATOM  17218  CB  VAL C 511     204.502 231.393 252.307  1.00 80.66           C  
ATOM  17219  CG1 VAL C 511     204.670 232.560 251.340  1.00 78.78           C  
ATOM  17220  CG2 VAL C 511     204.231 231.903 253.707  1.00 82.30           C  
ATOM  17221  N   VAL C 512     202.715 230.456 249.536  1.00 79.12           N  
ATOM  17222  CA  VAL C 512     202.912 230.096 248.150  1.00 77.01           C  
ATOM  17223  C   VAL C 512     203.351 231.316 247.379  1.00 76.61           C  
ATOM  17224  O   VAL C 512     202.647 232.318 247.348  1.00 75.94           O  
ATOM  17225  CB  VAL C 512     201.623 229.528 247.539  1.00 77.66           C  
ATOM  17226  CG1 VAL C 512     201.849 229.181 246.070  1.00 76.56           C  
ATOM  17227  CG2 VAL C 512     201.200 228.319 248.335  1.00 78.57           C  
ATOM  17228  N   LEU C 513     204.520 231.226 246.766  1.00 74.93           N  
ATOM  17229  CA  LEU C 513     205.035 232.336 245.994  1.00 73.58           C  
ATOM  17230  C   LEU C 513     204.759 232.090 244.529  1.00 74.08           C  
ATOM  17231  O   LEU C 513     205.405 231.258 243.890  1.00 71.09           O  
ATOM  17232  CB  LEU C 513     206.542 232.510 246.216  1.00 73.80           C  
ATOM  17233  CG  LEU C 513     207.011 232.745 247.661  1.00 74.48           C  
ATOM  17234  CD1 LEU C 513     208.526 232.852 247.672  1.00 72.98           C  
ATOM  17235  CD2 LEU C 513     206.377 234.015 248.213  1.00 75.24           C  
ATOM  17236  N   SER C 514     203.774 232.803 244.010  1.00 71.46           N  
ATOM  17237  CA  SER C 514     203.350 232.666 242.633  1.00 70.67           C  
ATOM  17238  C   SER C 514     204.163 233.606 241.785  1.00 70.32           C  
ATOM  17239  O   SER C 514     204.245 234.805 242.087  1.00 69.97           O  
ATOM  17240  CB  SER C 514     201.874 232.969 242.500  1.00 73.83           C  
ATOM  17241  OG  SER C 514     201.471 232.933 241.154  1.00 73.87           O  
ATOM  17242  N   PHE C 515     204.788 233.085 240.755  1.00 70.08           N  
ATOM  17243  CA  PHE C 515     205.654 233.910 239.938  1.00 68.85           C  
ATOM  17244  C   PHE C 515     205.023 234.268 238.621  1.00 68.10           C  
ATOM  17245  O   PHE C 515     204.563 233.386 237.883  1.00 68.18           O  
ATOM  17246  CB  PHE C 515     206.963 233.189 239.666  1.00 68.25           C  
ATOM  17247  CG  PHE C 515     207.778 232.865 240.881  1.00 68.02           C  
ATOM  17248  CD1 PHE C 515     207.728 233.641 242.014  1.00 68.65           C  
ATOM  17249  CD2 PHE C 515     208.587 231.759 240.897  1.00 68.62           C  
ATOM  17250  CE1 PHE C 515     208.463 233.314 243.129  1.00 70.96           C  
ATOM  17251  CE2 PHE C 515     209.307 231.431 242.013  1.00 70.66           C  
ATOM  17252  CZ  PHE C 515     209.246 232.203 243.128  1.00 70.01           C  
ATOM  17253  N   GLU C 516     205.031 235.541 238.288  1.00 67.78           N  
ATOM  17254  CA  GLU C 516     204.536 235.968 237.000  1.00 66.61           C  
ATOM  17255  C   GLU C 516     205.729 236.039 236.063  1.00 65.47           C  
ATOM  17256  O   GLU C 516     206.634 236.856 236.230  1.00 65.70           O  
ATOM  17257  CB  GLU C 516     203.815 237.300 237.096  1.00 66.97           C  
ATOM  17258  N   LEU C 517     205.715 235.156 235.073  1.00 64.38           N  
ATOM  17259  CA  LEU C 517     206.836 235.016 234.159  1.00 64.04           C  
ATOM  17260  C   LEU C 517     207.018 236.269 233.335  1.00 64.43           C  
ATOM  17261  O   LEU C 517     206.099 237.050 233.148  1.00 64.01           O  
ATOM  17262  CB  LEU C 517     206.624 233.812 233.246  1.00 63.35           C  
ATOM  17263  CG  LEU C 517     206.707 232.413 233.942  1.00 63.82           C  
ATOM  17264  CD1 LEU C 517     206.220 231.341 232.979  1.00 63.71           C  
ATOM  17265  CD2 LEU C 517     208.195 232.178 234.333  1.00 62.57           C  
ATOM  17266  N   LEU C 518     208.249 236.463 232.874  1.00 61.64           N  
ATOM  17267  CA  LEU C 518     208.539 237.707 232.175  1.00 61.66           C  
ATOM  17268  C   LEU C 518     207.818 237.757 230.845  1.00 61.83           C  
ATOM  17269  O   LEU C 518     208.131 237.008 229.916  1.00 60.46           O  
ATOM  17270  CB  LEU C 518     210.074 237.854 231.970  1.00 61.32           C  
ATOM  17271  CG  LEU C 518     210.605 239.255 231.507  1.00 60.51           C  
ATOM  17272  CD1 LEU C 518     212.103 239.339 231.805  1.00 59.30           C  
ATOM  17273  CD2 LEU C 518     210.378 239.481 230.020  1.00 58.55           C  
ATOM  17274  N   HIS C 519     206.877 238.686 230.784  1.00 60.43           N  
ATOM  17275  CA  HIS C 519     206.057 238.961 229.622  1.00 60.36           C  
ATOM  17276  C   HIS C 519     206.068 240.463 229.418  1.00 59.22           C  
ATOM  17277  O   HIS C 519     205.515 240.985 228.449  1.00 56.19           O  
ATOM  17278  CB  HIS C 519     204.609 238.495 229.827  1.00 61.01           C  
ATOM  17279  CG  HIS C 519     204.446 237.027 230.041  1.00 61.79           C  
ATOM  17280  ND1 HIS C 519     204.722 236.092 229.069  1.00 62.24           N  
ATOM  17281  CD2 HIS C 519     204.011 236.340 231.113  1.00 63.22           C  
ATOM  17282  CE1 HIS C 519     204.475 234.883 229.564  1.00 62.94           C  
ATOM  17283  NE2 HIS C 519     204.047 235.014 230.790  1.00 63.03           N  
ATOM  17284  N   ALA C 520     206.625 241.144 230.403  1.00 58.91           N  
ATOM  17285  CA  ALA C 520     206.592 242.591 230.506  1.00 57.89           C  
ATOM  17286  C   ALA C 520     207.851 243.012 231.235  1.00 58.13           C  
ATOM  17287  O   ALA C 520     208.580 242.159 231.727  1.00 57.67           O  
ATOM  17288  CB  ALA C 520     205.352 243.032 231.266  1.00 57.19           C  
ATOM  17289  N   PRO C 521     208.201 244.290 231.272  1.00 56.70           N  
ATOM  17290  CA  PRO C 521     209.387 244.719 231.926  1.00 57.52           C  
ATOM  17291  C   PRO C 521     209.304 244.146 233.315  1.00 59.20           C  
ATOM  17292  O   PRO C 521     208.322 244.346 234.036  1.00 59.76           O  
ATOM  17293  CB  PRO C 521     209.268 246.233 231.871  1.00 57.27           C  
ATOM  17294  CG  PRO C 521     208.395 246.484 230.645  1.00 54.82           C  
ATOM  17295  CD  PRO C 521     207.393 245.352 230.680  1.00 55.61           C  
ATOM  17296  N   ALA C 522     210.320 243.408 233.680  1.00 59.24           N  
ATOM  17297  CA  ALA C 522     210.324 242.735 234.949  1.00 61.28           C  
ATOM  17298  C   ALA C 522     210.598 243.743 236.048  1.00 62.16           C  
ATOM  17299  O   ALA C 522     211.218 244.775 235.799  1.00 61.87           O  
ATOM  17300  CB  ALA C 522     211.316 241.618 234.935  1.00 61.85           C  
ATOM  17301  N   THR C 523     210.103 243.465 237.243  1.00 63.45           N  
ATOM  17302  CA  THR C 523     210.287 244.376 238.365  1.00 63.36           C  
ATOM  17303  C   THR C 523     210.939 243.717 239.589  1.00 63.97           C  
ATOM  17304  O   THR C 523     211.571 244.393 240.401  1.00 64.95           O  
ATOM  17305  CB  THR C 523     208.945 245.028 238.748  1.00 64.53           C  
ATOM  17306  OG1 THR C 523     208.392 245.707 237.617  1.00 64.09           O  
ATOM  17307  CG2 THR C 523     209.161 246.028 239.843  1.00 65.42           C  
ATOM  17308  N   VAL C 524     210.743 242.412 239.754  1.00 63.31           N  
ATOM  17309  CA  VAL C 524     211.275 241.717 240.923  1.00 62.09           C  
ATOM  17310  C   VAL C 524     212.438 240.826 240.509  1.00 64.03           C  
ATOM  17311  O   VAL C 524     212.221 239.700 240.053  1.00 65.10           O  
ATOM  17312  CB  VAL C 524     210.189 240.836 241.563  1.00 63.93           C  
ATOM  17313  CG1 VAL C 524     210.751 240.132 242.783  1.00 65.52           C  
ATOM  17314  CG2 VAL C 524     209.012 241.687 241.930  1.00 66.15           C  
ATOM  17315  N   CYS C 525     213.668 241.331 240.665  1.00 63.38           N  
ATOM  17316  CA  CYS C 525     214.889 240.677 240.181  1.00 63.25           C  
ATOM  17317  C   CYS C 525     215.711 240.181 241.357  1.00 63.23           C  
ATOM  17318  O   CYS C 525     215.632 240.746 242.446  1.00 65.59           O  
ATOM  17319  CB  CYS C 525     215.740 241.642 239.316  1.00 62.07           C  
ATOM  17320  SG  CYS C 525     214.952 242.276 237.786  1.00 59.87           S  
ATOM  17321  N   GLY C 526     216.535 239.145 241.130  1.00 62.15           N  
ATOM  17322  CA  GLY C 526     217.438 238.618 242.151  1.00 63.41           C  
ATOM  17323  C   GLY C 526     218.632 239.546 242.372  1.00 62.91           C  
ATOM  17324  O   GLY C 526     218.794 240.542 241.665  1.00 62.84           O  
ATOM  17325  N   PRO C 527     219.500 239.204 243.323  1.00 62.73           N  
ATOM  17326  CA  PRO C 527     220.665 239.943 243.762  1.00 62.93           C  
ATOM  17327  C   PRO C 527     221.822 239.779 242.799  1.00 61.73           C  
ATOM  17328  O   PRO C 527     222.875 239.254 243.157  1.00 61.87           O  
ATOM  17329  CB  PRO C 527     220.955 239.287 245.111  1.00 65.15           C  
ATOM  17330  CG  PRO C 527     220.515 237.853 244.913  1.00 65.07           C  
ATOM  17331  CD  PRO C 527     219.290 237.948 244.029  1.00 64.55           C  
ATOM  17332  N   LYS C 528     221.608 240.214 241.571  1.00 61.40           N  
ATOM  17333  CA  LYS C 528     222.622 240.110 240.544  1.00 59.95           C  
ATOM  17334  C   LYS C 528     223.347 241.418 240.365  1.00 59.21           C  
ATOM  17335  O   LYS C 528     222.753 242.492 240.464  1.00 59.15           O  
ATOM  17336  CB  LYS C 528     221.996 239.683 239.227  1.00 59.02           C  
ATOM  17337  CG  LYS C 528     221.306 238.324 239.257  1.00 59.50           C  
ATOM  17338  CD  LYS C 528     222.298 237.160 239.352  1.00 59.83           C  
ATOM  17339  CE  LYS C 528     223.085 236.968 238.057  1.00 58.06           C  
ATOM  17340  NZ  LYS C 528     223.864 235.704 238.080  1.00 58.31           N  
ATOM  17341  N   LYS C 529     224.631 241.324 240.077  1.00 58.79           N  
ATOM  17342  CA  LYS C 529     225.418 242.500 239.792  1.00 58.19           C  
ATOM  17343  C   LYS C 529     225.375 242.789 238.311  1.00 57.76           C  
ATOM  17344  O   LYS C 529     225.706 241.928 237.497  1.00 57.29           O  
ATOM  17345  CB  LYS C 529     226.861 242.299 240.255  1.00 58.69           C  
ATOM  17346  CG  LYS C 529     227.817 243.454 239.930  1.00 58.92           C  
ATOM  17347  CD  LYS C 529     227.566 244.687 240.803  1.00 59.26           C  
ATOM  17348  CE  LYS C 529     228.512 245.828 240.429  1.00 58.90           C  
ATOM  17349  NZ  LYS C 529     228.044 246.580 239.221  1.00 57.77           N  
ATOM  17350  N   SER C 530     224.975 243.998 237.964  1.00 57.29           N  
ATOM  17351  CA  SER C 530     224.936 244.380 236.570  1.00 56.14           C  
ATOM  17352  C   SER C 530     226.315 244.800 236.093  1.00 55.89           C  
ATOM  17353  O   SER C 530     227.209 245.117 236.889  1.00 56.33           O  
ATOM  17354  CB  SER C 530     223.937 245.495 236.344  1.00 55.78           C  
ATOM  17355  OG  SER C 530     224.354 246.693 236.937  1.00 56.72           O  
ATOM  17356  N   THR C 531     226.469 244.839 234.783  1.00 55.24           N  
ATOM  17357  CA  THR C 531     227.704 245.258 234.149  1.00 54.80           C  
ATOM  17358  C   THR C 531     227.405 246.373 233.191  1.00 54.22           C  
ATOM  17359  O   THR C 531     226.244 246.700 232.955  1.00 54.41           O  
ATOM  17360  CB  THR C 531     228.354 244.133 233.337  1.00 54.41           C  
ATOM  17361  OG1 THR C 531     227.582 243.906 232.147  1.00 53.45           O  
ATOM  17362  CG2 THR C 531     228.390 242.857 234.156  1.00 55.12           C  
ATOM  17363  N   ASN C 532     228.448 246.934 232.611  1.00 54.16           N  
ATOM  17364  CA  ASN C 532     228.283 247.923 231.568  1.00 53.92           C  
ATOM  17365  C   ASN C 532     227.883 247.197 230.298  1.00 53.27           C  
ATOM  17366  O   ASN C 532     228.049 245.977 230.195  1.00 53.65           O  
ATOM  17367  CB  ASN C 532     229.546 248.733 231.364  1.00 53.99           C  
ATOM  17368  CG  ASN C 532     229.290 250.015 230.606  1.00 53.92           C  
ATOM  17369  OD1 ASN C 532     228.142 250.328 230.258  1.00 53.69           O  
ATOM  17370  ND2 ASN C 532     230.334 250.755 230.343  1.00 53.76           N  
ATOM  17371  N   LEU C 533     227.308 247.929 229.357  1.00 53.16           N  
ATOM  17372  CA  LEU C 533     226.913 247.332 228.094  1.00 52.70           C  
ATOM  17373  C   LEU C 533     227.882 247.684 226.977  1.00 52.52           C  
ATOM  17374  O   LEU C 533     228.261 248.840 226.793  1.00 52.44           O  
ATOM  17375  CB  LEU C 533     225.479 247.744 227.744  1.00 53.22           C  
ATOM  17376  CG  LEU C 533     224.879 247.139 226.464  1.00 52.36           C  
ATOM  17377  CD1 LEU C 533     223.423 246.851 226.691  1.00 52.98           C  
ATOM  17378  CD2 LEU C 533     225.027 248.106 225.328  1.00 51.11           C  
ATOM  17379  N   VAL C 534     228.258 246.666 226.219  1.00 52.08           N  
ATOM  17380  CA  VAL C 534     229.183 246.786 225.107  1.00 51.41           C  
ATOM  17381  C   VAL C 534     228.468 246.606 223.779  1.00 51.18           C  
ATOM  17382  O   VAL C 534     227.854 245.572 223.539  1.00 50.58           O  
ATOM  17383  CB  VAL C 534     230.278 245.711 225.239  1.00 51.40           C  
ATOM  17384  CG1 VAL C 534     231.245 245.793 224.087  1.00 51.31           C  
ATOM  17385  CG2 VAL C 534     230.989 245.888 226.569  1.00 51.99           C  
ATOM  17386  N   LYS C 535     228.550 247.608 222.916  1.00 50.43           N  
ATOM  17387  CA  LYS C 535     227.856 247.544 221.634  1.00 49.94           C  
ATOM  17388  C   LYS C 535     228.764 247.109 220.489  1.00 50.03           C  
ATOM  17389  O   LYS C 535     229.976 247.321 220.520  1.00 49.98           O  
ATOM  17390  CB  LYS C 535     227.213 248.891 221.312  1.00 49.77           C  
ATOM  17391  CG  LYS C 535     226.136 249.279 222.298  1.00 49.87           C  
ATOM  17392  CD  LYS C 535     225.459 250.591 221.959  1.00 48.63           C  
ATOM  17393  CE  LYS C 535     224.392 250.933 223.008  1.00 49.03           C  
ATOM  17394  NZ  LYS C 535     223.669 252.198 222.694  1.00 48.60           N  
ATOM  17395  N   ASN C 536     228.133 246.546 219.460  1.00 49.55           N  
ATOM  17396  CA  ASN C 536     228.761 246.111 218.209  1.00 50.04           C  
ATOM  17397  C   ASN C 536     229.803 245.001 218.360  1.00 50.29           C  
ATOM  17398  O   ASN C 536     230.720 244.896 217.545  1.00 50.69           O  
ATOM  17399  CB  ASN C 536     229.396 247.293 217.507  1.00 50.22           C  
ATOM  17400  CG  ASN C 536     228.410 248.327 217.121  1.00 49.88           C  
ATOM  17401  OD1 ASN C 536     227.384 248.035 216.499  1.00 49.79           O  
ATOM  17402  ND2 ASN C 536     228.689 249.550 217.477  1.00 50.04           N  
ATOM  17403  N   LYS C 537     229.648 244.155 219.367  1.00 49.67           N  
ATOM  17404  CA  LYS C 537     230.541 243.022 219.565  1.00 49.52           C  
ATOM  17405  C   LYS C 537     229.717 241.819 220.004  1.00 48.46           C  
ATOM  17406  O   LYS C 537     228.650 242.010 220.588  1.00 50.11           O  
ATOM  17407  CB  LYS C 537     231.600 243.352 220.618  1.00 49.97           C  
ATOM  17408  CG  LYS C 537     232.497 244.524 220.253  1.00 51.19           C  
ATOM  17409  CD  LYS C 537     233.612 244.708 221.259  1.00 51.65           C  
ATOM  17410  CE  LYS C 537     234.452 245.927 220.924  1.00 52.45           C  
ATOM  17411  NZ  LYS C 537     235.571 246.115 221.891  1.00 53.60           N  
ATOM  17412  N   CYS C 538     230.207 240.582 219.751  1.00 48.99           N  
ATOM  17413  CA  CYS C 538     229.539 239.384 220.263  1.00 48.12           C  
ATOM  17414  C   CYS C 538     229.724 239.257 221.777  1.00 49.07           C  
ATOM  17415  O   CYS C 538     230.851 239.246 222.285  1.00 49.25           O  
ATOM  17416  CB  CYS C 538     230.068 238.111 219.573  1.00 48.76           C  
ATOM  17417  SG  CYS C 538     229.466 237.874 217.902  1.00 47.81           S  
ATOM  17418  N   VAL C 539     228.585 239.151 222.477  1.00 48.10           N  
ATOM  17419  CA  VAL C 539     228.532 239.043 223.924  1.00 47.88           C  
ATOM  17420  C   VAL C 539     227.584 237.948 224.357  1.00 49.42           C  
ATOM  17421  O   VAL C 539     226.640 237.598 223.643  1.00 46.35           O  
ATOM  17422  CB  VAL C 539     228.027 240.372 224.516  1.00 48.42           C  
ATOM  17423  CG1 VAL C 539     228.935 241.519 224.089  1.00 49.19           C  
ATOM  17424  CG2 VAL C 539     226.605 240.617 224.047  1.00 48.90           C  
ATOM  17425  N   ASN C 540     227.777 237.488 225.576  1.00 47.95           N  
ATOM  17426  CA  ASN C 540     226.799 236.649 226.235  1.00 47.72           C  
ATOM  17427  C   ASN C 540     225.925 237.600 227.021  1.00 50.21           C  
ATOM  17428  O   ASN C 540     226.412 238.258 227.938  1.00 50.92           O  
ATOM  17429  CB  ASN C 540     227.460 235.639 227.151  1.00 49.15           C  
ATOM  17430  CG  ASN C 540     228.274 234.631 226.420  1.00 49.15           C  
ATOM  17431  OD1 ASN C 540     227.770 233.934 225.536  1.00 48.15           O  
ATOM  17432  ND2 ASN C 540     229.529 234.527 226.773  1.00 49.54           N  
ATOM  17433  N   PHE C 541     224.669 237.750 226.642  1.00 48.64           N  
ATOM  17434  CA  PHE C 541     223.862 238.753 227.319  1.00 48.36           C  
ATOM  17435  C   PHE C 541     222.761 238.163 228.175  1.00 49.25           C  
ATOM  17436  O   PHE C 541     222.254 237.066 227.921  1.00 49.70           O  
ATOM  17437  CB  PHE C 541     223.259 239.743 226.328  1.00 48.78           C  
ATOM  17438  CG  PHE C 541     222.419 239.124 225.276  1.00 48.57           C  
ATOM  17439  CD1 PHE C 541     221.105 238.790 225.529  1.00 49.52           C  
ATOM  17440  CD2 PHE C 541     222.926 238.897 224.015  1.00 48.24           C  
ATOM  17441  CE1 PHE C 541     220.327 238.230 224.557  1.00 48.47           C  
ATOM  17442  CE2 PHE C 541     222.146 238.343 223.042  1.00 48.06           C  
ATOM  17443  CZ  PHE C 541     220.849 238.005 223.314  1.00 47.69           C  
ATOM  17444  N   ASN C 542     222.371 238.943 229.175  1.00 49.50           N  
ATOM  17445  CA  ASN C 542     221.279 238.629 230.081  1.00 49.27           C  
ATOM  17446  C   ASN C 542     220.481 239.871 230.442  1.00 51.45           C  
ATOM  17447  O   ASN C 542     220.940 240.704 231.223  1.00 52.70           O  
ATOM  17448  CB  ASN C 542     221.821 237.971 231.338  1.00 51.09           C  
ATOM  17449  CG  ASN C 542     220.745 237.551 232.304  1.00 50.86           C  
ATOM  17450  OD1 ASN C 542     219.693 238.202 232.408  1.00 52.60           O  
ATOM  17451  ND2 ASN C 542     220.993 236.477 233.014  1.00 50.95           N  
ATOM  17452  N   PHE C 543     219.295 240.009 229.868  1.00 50.34           N  
ATOM  17453  CA  PHE C 543     218.443 241.156 230.145  1.00 51.52           C  
ATOM  17454  C   PHE C 543     217.241 240.730 230.970  1.00 51.77           C  
ATOM  17455  O   PHE C 543     216.316 240.106 230.458  1.00 52.72           O  
ATOM  17456  CB  PHE C 543     217.962 241.806 228.852  1.00 51.42           C  
ATOM  17457  CG  PHE C 543     219.026 242.491 228.053  1.00 51.33           C  
ATOM  17458  CD1 PHE C 543     219.746 241.818 227.097  1.00 50.72           C  
ATOM  17459  CD2 PHE C 543     219.286 243.823 228.254  1.00 51.71           C  
ATOM  17460  CE1 PHE C 543     220.706 242.471 226.360  1.00 50.41           C  
ATOM  17461  CE2 PHE C 543     220.239 244.477 227.525  1.00 51.64           C  
ATOM  17462  CZ  PHE C 543     220.949 243.801 226.578  1.00 50.67           C  
ATOM  17463  N   ASN C 544     217.266 241.025 232.256  1.00 52.59           N  
ATOM  17464  CA  ASN C 544     216.200 240.619 233.166  1.00 54.50           C  
ATOM  17465  C   ASN C 544     215.917 239.122 233.127  1.00 53.87           C  
ATOM  17466  O   ASN C 544     214.768 238.704 233.249  1.00 55.95           O  
ATOM  17467  CB  ASN C 544     214.917 241.363 232.864  1.00 55.56           C  
ATOM  17468  CG  ASN C 544     215.059 242.804 233.009  1.00 55.41           C  
ATOM  17469  OD1 ASN C 544     215.884 243.274 233.790  1.00 55.52           O  
ATOM  17470  ND2 ASN C 544     214.269 243.543 232.280  1.00 56.21           N  
ATOM  17471  N   GLY C 545     216.944 238.303 232.971  1.00 52.72           N  
ATOM  17472  CA  GLY C 545     216.742 236.863 232.935  1.00 52.86           C  
ATOM  17473  C   GLY C 545     216.587 236.315 231.515  1.00 50.92           C  
ATOM  17474  O   GLY C 545     216.597 235.100 231.320  1.00 50.01           O  
ATOM  17475  N   LEU C 546     216.455 237.200 230.529  1.00 50.76           N  
ATOM  17476  CA  LEU C 546     216.314 236.796 229.133  1.00 49.67           C  
ATOM  17477  C   LEU C 546     217.694 236.721 228.501  1.00 49.75           C  
ATOM  17478  O   LEU C 546     218.377 237.737 228.359  1.00 48.60           O  
ATOM  17479  CB  LEU C 546     215.437 237.820 228.388  1.00 49.80           C  
ATOM  17480  CG  LEU C 546     215.173 237.592 226.874  1.00 48.31           C  
ATOM  17481  CD1 LEU C 546     214.390 236.303 226.662  1.00 47.86           C  
ATOM  17482  CD2 LEU C 546     214.383 238.792 226.317  1.00 48.78           C  
ATOM  17483  N   THR C 547     218.121 235.519 228.139  1.00 48.48           N  
ATOM  17484  CA  THR C 547     219.492 235.348 227.693  1.00 48.11           C  
ATOM  17485  C   THR C 547     219.648 234.875 226.268  1.00 47.47           C  
ATOM  17486  O   THR C 547     218.728 234.312 225.667  1.00 47.36           O  
ATOM  17487  CB  THR C 547     220.213 234.335 228.588  1.00 48.12           C  
ATOM  17488  OG1 THR C 547     219.619 233.041 228.421  1.00 46.60           O  
ATOM  17489  CG2 THR C 547     220.091 234.748 230.034  1.00 49.20           C  
ATOM  17490  N   GLY C 548     220.863 235.059 225.764  1.00 47.34           N  
ATOM  17491  CA  GLY C 548     221.260 234.601 224.442  1.00 47.07           C  
ATOM  17492  C   GLY C 548     222.648 235.106 224.080  1.00 47.12           C  
ATOM  17493  O   GLY C 548     223.309 235.762 224.887  1.00 48.47           O  
ATOM  17494  N   THR C 549     223.097 234.769 222.878  1.00 46.44           N  
ATOM  17495  CA  THR C 549     224.405 235.188 222.393  1.00 46.81           C  
ATOM  17496  C   THR C 549     224.224 235.965 221.109  1.00 46.73           C  
ATOM  17497  O   THR C 549     223.482 235.540 220.224  1.00 46.37           O  
ATOM  17498  CB  THR C 549     225.331 233.982 222.134  1.00 45.65           C  
ATOM  17499  OG1 THR C 549     225.492 233.238 223.341  1.00 46.24           O  
ATOM  17500  CG2 THR C 549     226.711 234.461 221.657  1.00 46.92           C  
ATOM  17501  N   GLY C 550     224.882 237.105 221.000  1.00 46.79           N  
ATOM  17502  CA  GLY C 550     224.750 237.886 219.780  1.00 46.81           C  
ATOM  17503  C   GLY C 550     225.324 239.271 219.912  1.00 46.85           C  
ATOM  17504  O   GLY C 550     225.916 239.622 220.930  1.00 48.19           O  
ATOM  17505  N   VAL C 551     225.157 240.052 218.862  1.00 46.98           N  
ATOM  17506  CA  VAL C 551     225.663 241.407 218.811  1.00 47.71           C  
ATOM  17507  C   VAL C 551     224.555 242.406 219.106  1.00 47.24           C  
ATOM  17508  O   VAL C 551     223.489 242.361 218.497  1.00 48.10           O  
ATOM  17509  CB  VAL C 551     226.253 241.679 217.422  1.00 47.92           C  
ATOM  17510  CG1 VAL C 551     226.775 243.088 217.349  1.00 48.84           C  
ATOM  17511  CG2 VAL C 551     227.350 240.674 217.145  1.00 48.27           C  
ATOM  17512  N   LEU C 552     224.808 243.302 220.046  1.00 48.32           N  
ATOM  17513  CA  LEU C 552     223.834 244.313 220.435  1.00 48.55           C  
ATOM  17514  C   LEU C 552     224.120 245.631 219.728  1.00 48.37           C  
ATOM  17515  O   LEU C 552     225.217 246.172 219.871  1.00 50.39           O  
ATOM  17516  CB  LEU C 552     223.920 244.543 221.946  1.00 48.56           C  
ATOM  17517  CG  LEU C 552     223.805 243.299 222.841  1.00 49.43           C  
ATOM  17518  CD1 LEU C 552     224.061 243.713 224.270  1.00 50.74           C  
ATOM  17519  CD2 LEU C 552     222.430 242.676 222.694  1.00 48.87           C  
ATOM  17520  N   THR C 553     223.156 246.142 218.966  1.00 47.80           N  
ATOM  17521  CA  THR C 553     223.359 247.407 218.255  1.00 48.38           C  
ATOM  17522  C   THR C 553     222.174 248.333 218.457  1.00 49.39           C  
ATOM  17523  O   THR C 553     221.081 247.882 218.793  1.00 47.74           O  
ATOM  17524  CB  THR C 553     223.532 247.193 216.741  1.00 48.29           C  
ATOM  17525  OG1 THR C 553     222.284 246.789 216.164  1.00 48.34           O  
ATOM  17526  CG2 THR C 553     224.555 246.104 216.485  1.00 49.37           C  
ATOM  17527  N   GLU C 554     222.347 249.617 218.192  1.00 48.37           N  
ATOM  17528  CA  GLU C 554     221.213 250.524 218.293  1.00 48.58           C  
ATOM  17529  C   GLU C 554     220.146 250.141 217.288  1.00 49.13           C  
ATOM  17530  O   GLU C 554     220.456 249.875 216.127  1.00 48.57           O  
ATOM  17531  CB  GLU C 554     221.641 251.970 218.049  1.00 48.49           C  
ATOM  17532  CG  GLU C 554     222.600 252.529 219.083  1.00 48.36           C  
ATOM  17533  CD  GLU C 554     224.040 252.245 218.772  1.00 48.31           C  
ATOM  17534  OE1 GLU C 554     224.298 251.445 217.904  1.00 48.47           O  
ATOM  17535  OE2 GLU C 554     224.888 252.837 219.396  1.00 48.17           O  
ATOM  17536  N   SER C 555     218.889 250.131 217.722  1.00 48.34           N  
ATOM  17537  CA  SER C 555     217.799 249.808 216.816  1.00 48.33           C  
ATOM  17538  C   SER C 555     217.126 251.068 216.327  1.00 48.89           C  
ATOM  17539  O   SER C 555     217.353 252.158 216.850  1.00 48.77           O  
ATOM  17540  CB  SER C 555     216.735 248.996 217.505  1.00 49.43           C  
ATOM  17541  OG  SER C 555     215.944 249.816 218.293  1.00 49.91           O  
ATOM  17542  N   ASN C 556     216.251 250.902 215.355  1.00 48.82           N  
ATOM  17543  CA  ASN C 556     215.393 251.968 214.886  1.00 49.06           C  
ATOM  17544  C   ASN C 556     213.949 251.544 215.101  1.00 48.70           C  
ATOM  17545  O   ASN C 556     213.048 251.969 214.378  1.00 49.24           O  
ATOM  17546  CB  ASN C 556     215.671 252.282 213.436  1.00 48.85           C  
ATOM  17547  CG  ASN C 556     215.420 251.104 212.561  1.00 49.13           C  
ATOM  17548  OD1 ASN C 556     215.500 249.958 213.026  1.00 48.90           O  
ATOM  17549  ND2 ASN C 556     215.124 251.347 211.310  1.00 48.93           N  
ATOM  17550  N   LYS C 557     213.744 250.667 216.083  1.00 48.84           N  
ATOM  17551  CA  LYS C 557     212.425 250.132 216.381  1.00 49.00           C  
ATOM  17552  C   LYS C 557     211.704 251.017 217.370  1.00 48.95           C  
ATOM  17553  O   LYS C 557     212.325 251.694 218.188  1.00 49.03           O  
ATOM  17554  CB  LYS C 557     212.534 248.710 216.919  1.00 48.60           C  
ATOM  17555  CG  LYS C 557     213.078 247.714 215.910  1.00 48.60           C  
ATOM  17556  CD  LYS C 557     213.301 246.353 216.540  1.00 48.47           C  
ATOM  17557  CE  LYS C 557     213.993 245.388 215.574  1.00 48.05           C  
ATOM  17558  NZ  LYS C 557     213.058 244.785 214.592  1.00 46.94           N  
ATOM  17559  N   LYS C 558     210.385 251.007 217.299  1.00 49.02           N  
ATOM  17560  CA  LYS C 558     209.579 251.806 218.197  1.00 49.16           C  
ATOM  17561  C   LYS C 558     208.726 250.938 219.093  1.00 49.16           C  
ATOM  17562  O   LYS C 558     207.623 250.550 218.718  1.00 48.74           O  
ATOM  17563  CB  LYS C 558     208.682 252.746 217.394  1.00 49.55           C  
ATOM  17564  CG  LYS C 558     209.417 253.621 216.380  1.00 50.23           C  
ATOM  17565  CD  LYS C 558     210.315 254.650 217.052  1.00 51.13           C  
ATOM  17566  CE  LYS C 558     210.962 255.561 216.021  1.00 51.52           C  
ATOM  17567  NZ  LYS C 558     211.869 256.562 216.650  1.00 52.37           N  
ATOM  17568  N   PHE C 559     209.235 250.630 220.274  1.00 49.34           N  
ATOM  17569  CA  PHE C 559     208.492 249.804 221.209  1.00 49.59           C  
ATOM  17570  C   PHE C 559     207.442 250.625 221.911  1.00 49.74           C  
ATOM  17571  O   PHE C 559     207.652 251.806 222.193  1.00 49.54           O  
ATOM  17572  CB  PHE C 559     209.384 249.198 222.282  1.00 49.61           C  
ATOM  17573  CG  PHE C 559     210.190 248.014 221.907  1.00 49.15           C  
ATOM  17574  CD1 PHE C 559     210.510 247.693 220.600  1.00 49.15           C  
ATOM  17575  CD2 PHE C 559     210.636 247.198 222.911  1.00 49.30           C  
ATOM  17576  CE1 PHE C 559     211.264 246.575 220.333  1.00 48.12           C  
ATOM  17577  CE2 PHE C 559     211.381 246.104 222.648  1.00 49.81           C  
ATOM  17578  CZ  PHE C 559     211.699 245.782 221.361  1.00 49.07           C  
ATOM  17579  N   LEU C 560     206.336 249.993 222.240  1.00 48.98           N  
ATOM  17580  CA  LEU C 560     205.324 250.654 223.027  1.00 49.46           C  
ATOM  17581  C   LEU C 560     205.809 250.654 224.477  1.00 49.96           C  
ATOM  17582  O   LEU C 560     206.628 249.811 224.840  1.00 49.96           O  
ATOM  17583  CB  LEU C 560     203.982 249.935 222.845  1.00 50.10           C  
ATOM  17584  CG  LEU C 560     203.433 249.923 221.392  1.00 49.91           C  
ATOM  17585  CD1 LEU C 560     202.210 249.048 221.318  1.00 49.06           C  
ATOM  17586  CD2 LEU C 560     203.075 251.338 220.954  1.00 49.89           C  
ATOM  17587  N   PRO C 561     205.348 251.580 225.326  1.00 49.78           N  
ATOM  17588  CA  PRO C 561     205.747 251.758 226.716  1.00 50.00           C  
ATOM  17589  C   PRO C 561     205.652 250.507 227.588  1.00 49.81           C  
ATOM  17590  O   PRO C 561     206.307 250.428 228.625  1.00 50.24           O  
ATOM  17591  CB  PRO C 561     204.753 252.817 227.199  1.00 50.10           C  
ATOM  17592  CG  PRO C 561     204.392 253.593 225.967  1.00 50.04           C  
ATOM  17593  CD  PRO C 561     204.363 252.579 224.860  1.00 50.04           C  
ATOM  17594  N   PHE C 562     204.827 249.547 227.196  1.00 50.48           N  
ATOM  17595  CA  PHE C 562     204.645 248.337 227.988  1.00 50.44           C  
ATOM  17596  C   PHE C 562     205.399 247.130 227.442  1.00 51.48           C  
ATOM  17597  O   PHE C 562     205.275 246.029 227.979  1.00 51.19           O  
ATOM  17598  CB  PHE C 562     203.164 248.006 228.059  1.00 50.45           C  
ATOM  17599  CG  PHE C 562     202.540 247.871 226.711  1.00 50.30           C  
ATOM  17600  CD1 PHE C 562     202.563 246.673 226.037  1.00 49.49           C  
ATOM  17601  CD2 PHE C 562     201.936 248.952 226.109  1.00 50.53           C  
ATOM  17602  CE1 PHE C 562     201.984 246.549 224.797  1.00 49.45           C  
ATOM  17603  CE2 PHE C 562     201.367 248.831 224.877  1.00 50.12           C  
ATOM  17604  CZ  PHE C 562     201.387 247.625 224.222  1.00 49.84           C  
ATOM  17605  N   GLN C 563     206.163 247.320 226.371  1.00 50.27           N  
ATOM  17606  CA  GLN C 563     206.877 246.209 225.753  1.00 49.11           C  
ATOM  17607  C   GLN C 563     208.332 246.156 226.204  1.00 50.71           C  
ATOM  17608  O   GLN C 563     209.040 247.166 226.203  1.00 51.37           O  
ATOM  17609  CB  GLN C 563     206.771 246.309 224.234  1.00 49.80           C  
ATOM  17610  CG  GLN C 563     205.340 246.195 223.751  1.00 49.09           C  
ATOM  17611  CD  GLN C 563     205.172 246.351 222.267  1.00 49.57           C  
ATOM  17612  OE1 GLN C 563     205.758 247.243 221.645  1.00 49.44           O  
ATOM  17613  NE2 GLN C 563     204.354 245.493 221.676  1.00 48.49           N  
ATOM  17614  N   GLN C 564     208.771 244.960 226.585  1.00 50.83           N  
ATOM  17615  CA  GLN C 564     210.132 244.728 227.061  1.00 51.69           C  
ATOM  17616  C   GLN C 564     211.054 244.164 225.998  1.00 51.29           C  
ATOM  17617  O   GLN C 564     212.266 244.385 226.029  1.00 51.79           O  
ATOM  17618  CB  GLN C 564     210.098 243.817 228.284  1.00 53.92           C  
ATOM  17619  CG  GLN C 564     211.445 243.425 228.820  1.00 53.22           C  
ATOM  17620  CD  GLN C 564     212.324 244.601 229.157  1.00 53.17           C  
ATOM  17621  OE1 GLN C 564     211.948 245.550 229.852  1.00 53.73           O  
ATOM  17622  NE2 GLN C 564     213.534 244.533 228.633  1.00 52.88           N  
ATOM  17623  N   PHE C 565     210.497 243.395 225.090  1.00 50.01           N  
ATOM  17624  CA  PHE C 565     211.280 242.777 224.043  1.00 48.83           C  
ATOM  17625  C   PHE C 565     210.379 242.465 222.879  1.00 49.82           C  
ATOM  17626  O   PHE C 565     209.156 242.423 223.035  1.00 46.09           O  
ATOM  17627  CB  PHE C 565     211.974 241.516 224.535  1.00 49.11           C  
ATOM  17628  CG  PHE C 565     211.063 240.443 224.912  1.00 49.39           C  
ATOM  17629  CD1 PHE C 565     210.732 239.476 224.001  1.00 48.29           C  
ATOM  17630  CD2 PHE C 565     210.522 240.383 226.174  1.00 50.38           C  
ATOM  17631  CE1 PHE C 565     209.886 238.467 224.336  1.00 47.75           C  
ATOM  17632  CE2 PHE C 565     209.666 239.370 226.516  1.00 51.85           C  
ATOM  17633  CZ  PHE C 565     209.347 238.408 225.598  1.00 49.37           C  
ATOM  17634  N   GLY C 566     210.979 242.229 221.730  1.00 47.05           N  
ATOM  17635  CA  GLY C 566     210.228 241.792 220.575  1.00 46.68           C  
ATOM  17636  C   GLY C 566     210.669 240.415 220.153  1.00 46.53           C  
ATOM  17637  O   GLY C 566     211.665 239.890 220.653  1.00 46.67           O  
ATOM  17638  N   ARG C 567     209.958 239.851 219.197  1.00 45.28           N  
ATOM  17639  CA  ARG C 567     210.285 238.528 218.697  1.00 43.91           C  
ATOM  17640  C   ARG C 567     210.313 238.476 217.185  1.00 43.93           C  
ATOM  17641  O   ARG C 567     209.601 239.213 216.502  1.00 44.46           O  
ATOM  17642  CB  ARG C 567     209.303 237.480 219.193  1.00 43.38           C  
ATOM  17643  CG  ARG C 567     209.336 237.173 220.683  1.00 43.86           C  
ATOM  17644  CD  ARG C 567     208.331 236.113 221.015  1.00 43.40           C  
ATOM  17645  NE  ARG C 567     208.145 235.916 222.451  1.00 43.90           N  
ATOM  17646  CZ  ARG C 567     208.862 235.078 223.238  1.00 43.57           C  
ATOM  17647  NH1 ARG C 567     209.844 234.344 222.753  1.00 42.97           N  
ATOM  17648  NH2 ARG C 567     208.567 234.994 224.529  1.00 44.70           N  
ATOM  17649  N   ASP C 568     211.122 237.564 216.674  1.00 43.59           N  
ATOM  17650  CA  ASP C 568     211.201 237.283 215.255  1.00 42.85           C  
ATOM  17651  C   ASP C 568     210.161 236.222 214.916  1.00 42.06           C  
ATOM  17652  O   ASP C 568     209.473 235.717 215.801  1.00 41.99           O  
ATOM  17653  CB  ASP C 568     212.622 236.806 214.911  1.00 43.02           C  
ATOM  17654  CG  ASP C 568     213.037 237.002 213.443  1.00 43.51           C  
ATOM  17655  OD1 ASP C 568     212.172 237.074 212.601  1.00 43.64           O  
ATOM  17656  OD2 ASP C 568     214.213 237.057 213.184  1.00 43.07           O  
ATOM  17657  N   ILE C 569     210.076 235.842 213.655  1.00 41.52           N  
ATOM  17658  CA  ILE C 569     209.130 234.820 213.222  1.00 40.90           C  
ATOM  17659  C   ILE C 569     209.482 233.467 213.838  1.00 40.13           C  
ATOM  17660  O   ILE C 569     208.634 232.592 213.988  1.00 38.47           O  
ATOM  17661  CB  ILE C 569     209.093 234.741 211.679  1.00 40.46           C  
ATOM  17662  CG1 ILE C 569     207.837 233.976 211.181  1.00 39.28           C  
ATOM  17663  CG2 ILE C 569     210.351 234.083 211.151  1.00 39.75           C  
ATOM  17664  CD1 ILE C 569     206.511 234.683 211.450  1.00 40.21           C  
ATOM  17665  N   ALA C 570     210.749 233.313 214.202  1.00 40.19           N  
ATOM  17666  CA  ALA C 570     211.285 232.098 214.803  1.00 39.02           C  
ATOM  17667  C   ALA C 570     210.996 232.037 216.297  1.00 39.96           C  
ATOM  17668  O   ALA C 570     211.393 231.090 216.974  1.00 39.06           O  
ATOM  17669  CB  ALA C 570     212.783 232.032 214.578  1.00 39.13           C  
ATOM  17670  N   ASP C 571     210.348 233.074 216.821  1.00 41.28           N  
ATOM  17671  CA  ASP C 571     210.034 233.210 218.242  1.00 41.35           C  
ATOM  17672  C   ASP C 571     211.273 233.519 219.074  1.00 41.29           C  
ATOM  17673  O   ASP C 571     211.221 233.548 220.305  1.00 41.96           O  
ATOM  17674  CB  ASP C 571     209.388 231.927 218.767  1.00 40.22           C  
ATOM  17675  CG  ASP C 571     208.380 232.155 219.893  1.00 40.62           C  
ATOM  17676  OD1 ASP C 571     207.627 233.099 219.812  1.00 41.30           O  
ATOM  17677  OD2 ASP C 571     208.351 231.368 220.805  1.00 39.96           O  
ATOM  17678  N   THR C 572     212.379 233.803 218.405  1.00 41.61           N  
ATOM  17679  CA  THR C 572     213.582 234.198 219.105  1.00 42.69           C  
ATOM  17680  C   THR C 572     213.516 235.683 219.364  1.00 44.46           C  
ATOM  17681  O   THR C 572     212.770 236.399 218.697  1.00 44.36           O  
ATOM  17682  CB  THR C 572     214.834 233.846 218.290  1.00 42.65           C  
ATOM  17683  OG1 THR C 572     214.827 234.575 217.054  1.00 42.68           O  
ATOM  17684  CG2 THR C 572     214.840 232.352 217.995  1.00 42.02           C  
ATOM  17685  N   THR C 573     214.321 236.169 220.290  1.00 44.17           N  
ATOM  17686  CA  THR C 573     214.296 237.589 220.592  1.00 44.94           C  
ATOM  17687  C   THR C 573     214.882 238.394 219.442  1.00 45.20           C  
ATOM  17688  O   THR C 573     215.961 238.087 218.944  1.00 45.41           O  
ATOM  17689  CB  THR C 573     215.061 237.874 221.887  1.00 45.95           C  
ATOM  17690  OG1 THR C 573     214.515 237.076 222.943  1.00 46.15           O  
ATOM  17691  CG2 THR C 573     214.934 239.328 222.268  1.00 46.85           C  
ATOM  17692  N   ASP C 574     214.154 239.420 219.016  1.00 46.25           N  
ATOM  17693  CA  ASP C 574     214.581 240.289 217.919  1.00 45.46           C  
ATOM  17694  C   ASP C 574     215.317 241.512 218.440  1.00 47.08           C  
ATOM  17695  O   ASP C 574     216.330 241.937 217.882  1.00 48.19           O  
ATOM  17696  CB  ASP C 574     213.359 240.709 217.089  1.00 46.87           C  
ATOM  17697  CG  ASP C 574     213.674 241.566 215.853  1.00 47.28           C  
ATOM  17698  OD1 ASP C 574     214.558 241.226 215.115  1.00 46.88           O  
ATOM  17699  OD2 ASP C 574     212.986 242.555 215.650  1.00 47.71           O  
ATOM  17700  N   ALA C 575     214.773 242.085 219.500  1.00 47.10           N  
ATOM  17701  CA  ALA C 575     215.303 243.289 220.112  1.00 46.83           C  
ATOM  17702  C   ALA C 575     214.852 243.351 221.552  1.00 48.07           C  
ATOM  17703  O   ALA C 575     213.839 242.749 221.914  1.00 49.89           O  
ATOM  17704  CB  ALA C 575     214.849 244.519 219.351  1.00 48.01           C  
ATOM  17705  N   VAL C 576     215.598 244.077 222.371  1.00 48.90           N  
ATOM  17706  CA  VAL C 576     215.244 244.255 223.773  1.00 49.48           C  
ATOM  17707  C   VAL C 576     215.323 245.693 224.246  1.00 50.20           C  
ATOM  17708  O   VAL C 576     216.080 246.502 223.709  1.00 50.09           O  
ATOM  17709  CB  VAL C 576     216.172 243.415 224.663  1.00 49.86           C  
ATOM  17710  CG1 VAL C 576     215.996 241.959 224.373  1.00 49.46           C  
ATOM  17711  CG2 VAL C 576     217.617 243.823 224.405  1.00 49.23           C  
ATOM  17712  N   ARG C 577     214.597 245.983 225.314  1.00 50.40           N  
ATOM  17713  CA  ARG C 577     214.714 247.257 225.992  1.00 50.50           C  
ATOM  17714  C   ARG C 577     215.714 247.145 227.127  1.00 52.27           C  
ATOM  17715  O   ARG C 577     215.585 246.294 228.008  1.00 52.76           O  
ATOM  17716  CB  ARG C 577     213.376 247.691 226.559  1.00 51.42           C  
ATOM  17717  CG  ARG C 577     213.374 249.042 227.244  1.00 51.10           C  
ATOM  17718  CD  ARG C 577     212.093 249.282 227.929  1.00 51.62           C  
ATOM  17719  NE  ARG C 577     210.972 249.268 227.020  1.00 50.82           N  
ATOM  17720  CZ  ARG C 577     210.554 250.302 226.275  1.00 50.94           C  
ATOM  17721  NH1 ARG C 577     211.173 251.466 226.306  1.00 51.06           N  
ATOM  17722  NH2 ARG C 577     209.505 250.126 225.511  1.00 50.45           N  
ATOM  17723  N   ASP C 578     216.708 248.007 227.127  1.00 51.73           N  
ATOM  17724  CA  ASP C 578     217.669 247.991 228.214  1.00 51.49           C  
ATOM  17725  C   ASP C 578     216.963 248.465 229.498  1.00 53.30           C  
ATOM  17726  O   ASP C 578     216.341 249.522 229.491  1.00 53.63           O  
ATOM  17727  CB  ASP C 578     218.887 248.849 227.877  1.00 51.81           C  
ATOM  17728  CG  ASP C 578     219.933 248.828 228.956  1.00 54.15           C  
ATOM  17729  OD1 ASP C 578     219.609 249.196 230.068  1.00 55.20           O  
ATOM  17730  OD2 ASP C 578     221.042 248.439 228.693  1.00 51.74           O  
ATOM  17731  N   PRO C 579     216.967 247.683 230.582  1.00 52.83           N  
ATOM  17732  CA  PRO C 579     216.266 247.952 231.823  1.00 54.21           C  
ATOM  17733  C   PRO C 579     216.796 249.154 232.603  1.00 54.89           C  
ATOM  17734  O   PRO C 579     216.119 249.654 233.499  1.00 54.84           O  
ATOM  17735  CB  PRO C 579     216.480 246.662 232.605  1.00 54.78           C  
ATOM  17736  CG  PRO C 579     217.740 246.078 232.051  1.00 54.69           C  
ATOM  17737  CD  PRO C 579     217.741 246.453 230.590  1.00 52.65           C  
ATOM  17738  N   GLN C 580     218.010 249.605 232.293  1.00 53.90           N  
ATOM  17739  CA  GLN C 580     218.581 250.740 233.007  1.00 53.85           C  
ATOM  17740  C   GLN C 580     218.488 252.003 232.165  1.00 54.03           C  
ATOM  17741  O   GLN C 580     218.300 253.103 232.687  1.00 55.10           O  
ATOM  17742  CB  GLN C 580     220.035 250.468 233.388  1.00 55.32           C  
ATOM  17743  CG  GLN C 580     220.207 249.333 234.364  1.00 55.27           C  
ATOM  17744  CD  GLN C 580     221.644 249.144 234.788  1.00 56.32           C  
ATOM  17745  OE1 GLN C 580     222.534 249.908 234.396  1.00 56.47           O  
ATOM  17746  NE2 GLN C 580     221.878 248.122 235.594  1.00 57.12           N  
ATOM  17747  N   THR C 581     218.616 251.837 230.858  1.00 52.93           N  
ATOM  17748  CA  THR C 581     218.556 252.950 229.923  1.00 51.86           C  
ATOM  17749  C   THR C 581     217.405 252.748 228.964  1.00 53.71           C  
ATOM  17750  O   THR C 581     217.304 251.712 228.318  1.00 51.23           O  
ATOM  17751  CB  THR C 581     219.868 253.086 229.139  1.00 52.55           C  
ATOM  17752  OG1 THR C 581     220.937 253.331 230.053  1.00 53.40           O  
ATOM  17753  CG2 THR C 581     219.781 254.234 228.138  1.00 52.54           C  
ATOM  17754  N   LEU C 582     216.556 253.745 228.815  1.00 51.72           N  
ATOM  17755  CA  LEU C 582     215.394 253.555 227.964  1.00 51.27           C  
ATOM  17756  C   LEU C 582     215.726 253.701 226.488  1.00 51.10           C  
ATOM  17757  O   LEU C 582     215.396 254.695 225.843  1.00 51.83           O  
ATOM  17758  CB  LEU C 582     214.296 254.537 228.364  1.00 51.51           C  
ATOM  17759  CG  LEU C 582     213.778 254.409 229.814  1.00 51.04           C  
ATOM  17760  CD1 LEU C 582     212.781 255.522 230.078  1.00 51.70           C  
ATOM  17761  CD2 LEU C 582     213.122 253.039 230.019  1.00 50.27           C  
ATOM  17762  N   GLU C 583     216.377 252.668 225.974  1.00 51.53           N  
ATOM  17763  CA  GLU C 583     216.803 252.561 224.591  1.00 50.66           C  
ATOM  17764  C   GLU C 583     216.503 251.160 224.088  1.00 51.08           C  
ATOM  17765  O   GLU C 583     216.492 250.198 224.863  1.00 51.36           O  
ATOM  17766  CB  GLU C 583     218.303 252.842 224.447  1.00 50.61           C  
ATOM  17767  CG  GLU C 583     219.216 251.828 225.150  1.00 51.12           C  
ATOM  17768  CD  GLU C 583     220.692 252.146 225.004  1.00 51.23           C  
ATOM  17769  OE1 GLU C 583     221.097 252.525 223.927  1.00 50.24           O  
ATOM  17770  OE2 GLU C 583     221.419 251.999 225.958  1.00 51.48           O  
ATOM  17771  N   ILE C 584     216.277 251.034 222.789  1.00 50.08           N  
ATOM  17772  CA  ILE C 584     216.008 249.727 222.212  1.00 49.50           C  
ATOM  17773  C   ILE C 584     217.187 249.237 221.399  1.00 49.25           C  
ATOM  17774  O   ILE C 584     217.687 249.943 220.518  1.00 49.28           O  
ATOM  17775  CB  ILE C 584     214.745 249.752 221.338  1.00 49.90           C  
ATOM  17776  CG1 ILE C 584     213.542 250.303 222.139  1.00 49.86           C  
ATOM  17777  CG2 ILE C 584     214.446 248.354 220.791  1.00 48.74           C  
ATOM  17778  CD1 ILE C 584     213.219 249.556 223.419  1.00 50.33           C  
ATOM  17779  N   LEU C 585     217.628 248.026 221.711  1.00 48.91           N  
ATOM  17780  CA  LEU C 585     218.765 247.430 221.035  1.00 47.74           C  
ATOM  17781  C   LEU C 585     218.370 246.219 220.222  1.00 48.95           C  
ATOM  17782  O   LEU C 585     217.645 245.343 220.697  1.00 49.60           O  
ATOM  17783  CB  LEU C 585     219.813 247.007 222.059  1.00 48.66           C  
ATOM  17784  CG  LEU C 585     220.304 248.092 223.002  1.00 49.43           C  
ATOM  17785  CD1 LEU C 585     221.245 247.471 223.994  1.00 49.93           C  
ATOM  17786  CD2 LEU C 585     220.994 249.204 222.214  1.00 48.90           C  
ATOM  17787  N   ASP C 586     218.871 246.162 219.000  1.00 48.21           N  
ATOM  17788  CA  ASP C 586     218.649 245.027 218.119  1.00 48.07           C  
ATOM  17789  C   ASP C 586     219.616 243.925 218.453  1.00 48.19           C  
ATOM  17790  O   ASP C 586     220.774 244.191 218.777  1.00 49.13           O  
ATOM  17791  CB  ASP C 586     218.837 245.408 216.651  1.00 48.39           C  
ATOM  17792  CG  ASP C 586     217.706 246.198 216.078  1.00 48.27           C  
ATOM  17793  OD1 ASP C 586     216.636 246.156 216.624  1.00 48.67           O  
ATOM  17794  OD2 ASP C 586     217.908 246.849 215.088  1.00 49.45           O  
ATOM  17795  N   ILE C 587     219.177 242.684 218.336  1.00 47.43           N  
ATOM  17796  CA  ILE C 587     220.096 241.586 218.542  1.00 47.27           C  
ATOM  17797  C   ILE C 587     220.362 240.866 217.239  1.00 46.63           C  
ATOM  17798  O   ILE C 587     219.468 240.252 216.660  1.00 46.83           O  
ATOM  17799  CB  ILE C 587     219.552 240.596 219.574  1.00 46.88           C  
ATOM  17800  CG1 ILE C 587     219.326 241.328 220.901  1.00 47.61           C  
ATOM  17801  CG2 ILE C 587     220.548 239.443 219.742  1.00 47.06           C  
ATOM  17802  CD1 ILE C 587     218.542 240.556 221.908  1.00 48.24           C  
ATOM  17803  N   THR C 588     221.601 240.918 216.792  1.00 46.80           N  
ATOM  17804  CA  THR C 588     221.990 240.236 215.572  1.00 46.05           C  
ATOM  17805  C   THR C 588     222.883 239.063 215.950  1.00 46.18           C  
ATOM  17806  O   THR C 588     223.999 239.274 216.414  1.00 47.31           O  
ATOM  17807  CB  THR C 588     222.737 241.167 214.607  1.00 46.58           C  
ATOM  17808  OG1 THR C 588     221.892 242.262 214.244  1.00 46.68           O  
ATOM  17809  CG2 THR C 588     223.113 240.402 213.357  1.00 46.03           C  
ATOM  17810  N   PRO C 589     222.440 237.823 215.776  1.00 44.89           N  
ATOM  17811  CA  PRO C 589     223.173 236.633 216.136  1.00 45.04           C  
ATOM  17812  C   PRO C 589     224.545 236.691 215.485  1.00 45.15           C  
ATOM  17813  O   PRO C 589     224.690 237.263 214.403  1.00 44.50           O  
ATOM  17814  CB  PRO C 589     222.287 235.524 215.576  1.00 44.03           C  
ATOM  17815  CG  PRO C 589     220.900 236.130 215.589  1.00 43.82           C  
ATOM  17816  CD  PRO C 589     221.105 237.573 215.240  1.00 44.75           C  
ATOM  17817  N   CYS C 590     225.553 236.130 216.167  1.00 45.49           N  
ATOM  17818  CA  CYS C 590     226.952 236.155 215.734  1.00 45.03           C  
ATOM  17819  C   CYS C 590     227.137 235.406 214.415  1.00 44.13           C  
ATOM  17820  O   CYS C 590     226.501 234.372 214.192  1.00 43.60           O  
ATOM  17821  CB  CYS C 590     227.862 235.547 216.823  1.00 44.92           C  
ATOM  17822  SG  CYS C 590     227.975 236.542 218.313  1.00 46.35           S  
ATOM  17823  N   SER C 591     228.011 235.940 213.537  1.00 44.13           N  
ATOM  17824  CA  SER C 591     228.279 235.372 212.212  1.00 42.61           C  
ATOM  17825  C   SER C 591     228.696 233.919 212.265  1.00 41.98           C  
ATOM  17826  O   SER C 591     229.496 233.508 213.110  1.00 42.80           O  
ATOM  17827  CB  SER C 591     229.357 236.156 211.502  1.00 42.55           C  
ATOM  17828  OG  SER C 591     229.700 235.532 210.296  1.00 41.91           O  
ATOM  17829  N   PHE C 592     228.132 233.143 211.364  1.00 41.45           N  
ATOM  17830  CA  PHE C 592     228.410 231.732 211.301  1.00 40.09           C  
ATOM  17831  C   PHE C 592     228.222 231.242 209.889  1.00 40.29           C  
ATOM  17832  O   PHE C 592     227.614 231.923 209.064  1.00 40.44           O  
ATOM  17833  CB  PHE C 592     227.461 230.959 212.209  1.00 40.58           C  
ATOM  17834  CG  PHE C 592     226.057 230.983 211.712  1.00 40.71           C  
ATOM  17835  CD1 PHE C 592     225.579 229.951 210.918  1.00 40.39           C  
ATOM  17836  CD2 PHE C 592     225.215 232.035 212.006  1.00 41.00           C  
ATOM  17837  CE1 PHE C 592     224.292 229.973 210.429  1.00 39.63           C  
ATOM  17838  CE2 PHE C 592     223.926 232.062 211.519  1.00 40.42           C  
ATOM  17839  CZ  PHE C 592     223.464 231.029 210.729  1.00 38.98           C  
ATOM  17840  N   GLY C 593     228.716 230.051 209.622  1.00 40.00           N  
ATOM  17841  CA  GLY C 593     228.500 229.428 208.328  1.00 39.46           C  
ATOM  17842  C   GLY C 593     229.261 228.128 208.226  1.00 39.22           C  
ATOM  17843  O   GLY C 593     230.123 227.838 209.053  1.00 39.81           O  
ATOM  17844  N   GLY C 594     228.956 227.345 207.210  1.00 39.01           N  
ATOM  17845  CA  GLY C 594     229.641 226.077 207.036  1.00 38.67           C  
ATOM  17846  C   GLY C 594     231.080 226.317 206.630  1.00 38.52           C  
ATOM  17847  O   GLY C 594     231.414 227.368 206.084  1.00 39.33           O  
ATOM  17848  N   VAL C 595     231.936 225.353 206.907  1.00 38.64           N  
ATOM  17849  CA  VAL C 595     233.321 225.459 206.494  1.00 38.38           C  
ATOM  17850  C   VAL C 595     233.669 224.308 205.587  1.00 39.22           C  
ATOM  17851  O   VAL C 595     233.537 223.137 205.968  1.00 39.08           O  
ATOM  17852  CB  VAL C 595     234.259 225.470 207.702  1.00 38.84           C  
ATOM  17853  CG1 VAL C 595     235.696 225.584 207.245  1.00 38.78           C  
ATOM  17854  CG2 VAL C 595     233.898 226.613 208.578  1.00 39.57           C  
ATOM  17855  N   SER C 596     234.120 224.643 204.388  1.00 38.58           N  
ATOM  17856  CA  SER C 596     234.474 223.635 203.417  1.00 38.19           C  
ATOM  17857  C   SER C 596     235.947 223.680 203.110  1.00 38.17           C  
ATOM  17858  O   SER C 596     236.558 224.745 203.056  1.00 39.52           O  
ATOM  17859  CB  SER C 596     233.675 223.811 202.147  1.00 38.51           C  
ATOM  17860  OG  SER C 596     232.307 223.641 202.384  1.00 38.71           O  
ATOM  17861  N   VAL C 597     236.524 222.523 202.896  1.00 38.46           N  
ATOM  17862  CA  VAL C 597     237.933 222.453 202.610  1.00 38.70           C  
ATOM  17863  C   VAL C 597     238.151 221.999 201.186  1.00 39.25           C  
ATOM  17864  O   VAL C 597     237.606 220.986 200.745  1.00 39.78           O  
ATOM  17865  CB  VAL C 597     238.624 221.513 203.604  1.00 39.25           C  
ATOM  17866  CG1 VAL C 597     240.112 221.443 203.317  1.00 39.84           C  
ATOM  17867  CG2 VAL C 597     238.374 222.014 205.018  1.00 39.77           C  
ATOM  17868  N   ILE C 598     238.937 222.779 200.468  1.00 39.12           N  
ATOM  17869  CA  ILE C 598     239.267 222.523 199.083  1.00 38.94           C  
ATOM  17870  C   ILE C 598     240.551 221.746 199.025  1.00 39.48           C  
ATOM  17871  O   ILE C 598     241.616 222.245 199.394  1.00 40.57           O  
ATOM  17872  CB  ILE C 598     239.426 223.844 198.343  1.00 38.76           C  
ATOM  17873  CG1 ILE C 598     238.115 224.589 198.406  1.00 38.49           C  
ATOM  17874  CG2 ILE C 598     239.881 223.608 196.913  1.00 39.13           C  
ATOM  17875  CD1 ILE C 598     238.213 226.021 198.035  1.00 38.74           C  
ATOM  17876  N   THR C 599     240.453 220.512 198.575  1.00 39.44           N  
ATOM  17877  CA  THR C 599     241.593 219.628 198.610  1.00 39.50           C  
ATOM  17878  C   THR C 599     241.970 219.164 197.199  1.00 41.15           C  
ATOM  17879  O   THR C 599     241.153 218.553 196.520  1.00 41.94           O  
ATOM  17880  CB  THR C 599     241.253 218.431 199.520  1.00 40.52           C  
ATOM  17881  OG1 THR C 599     240.897 218.928 200.806  1.00 40.37           O  
ATOM  17882  CG2 THR C 599     242.433 217.516 199.688  1.00 41.17           C  
ATOM  17883  N   PRO C 600     243.199 219.434 196.726  1.00 40.41           N  
ATOM  17884  CA  PRO C 600     243.767 219.004 195.453  1.00 41.06           C  
ATOM  17885  C   PRO C 600     243.843 217.493 195.323  1.00 41.62           C  
ATOM  17886  O   PRO C 600     244.030 216.961 194.233  1.00 41.99           O  
ATOM  17887  CB  PRO C 600     245.176 219.589 195.501  1.00 41.36           C  
ATOM  17888  CG  PRO C 600     245.075 220.752 196.425  1.00 40.85           C  
ATOM  17889  CD  PRO C 600     244.069 220.343 197.470  1.00 40.53           C  
ATOM  17890  N   GLY C 601     243.750 216.820 196.453  1.00 41.58           N  
ATOM  17891  CA  GLY C 601     243.848 215.378 196.556  1.00 41.69           C  
ATOM  17892  C   GLY C 601     245.165 215.064 197.234  1.00 43.16           C  
ATOM  17893  O   GLY C 601     246.222 215.515 196.779  1.00 43.80           O  
ATOM  17894  N   THR C 602     245.114 214.263 198.295  1.00 42.56           N  
ATOM  17895  CA  THR C 602     246.320 213.976 199.085  1.00 43.17           C  
ATOM  17896  C   THR C 602     247.358 213.109 198.375  1.00 43.28           C  
ATOM  17897  O   THR C 602     248.480 212.970 198.862  1.00 42.77           O  
ATOM  17898  CB  THR C 602     245.955 213.364 200.437  1.00 42.78           C  
ATOM  17899  OG1 THR C 602     245.159 212.188 200.239  1.00 42.93           O  
ATOM  17900  CG2 THR C 602     245.200 214.384 201.243  1.00 42.52           C  
ATOM  17901  N   ASN C 603     247.001 212.548 197.210  1.00 43.56           N  
ATOM  17902  CA  ASN C 603     247.924 211.808 196.362  1.00 44.07           C  
ATOM  17903  C   ASN C 603     248.936 212.749 195.677  1.00 44.51           C  
ATOM  17904  O   ASN C 603     250.014 212.318 195.283  1.00 44.66           O  
ATOM  17905  CB  ASN C 603     247.161 210.968 195.333  1.00 44.54           C  
ATOM  17906  CG  ASN C 603     247.988 209.804 194.762  1.00 45.53           C  
ATOM  17907  OD1 ASN C 603     248.484 208.959 195.526  1.00 45.97           O  
ATOM  17908  ND2 ASN C 603     248.135 209.759 193.449  1.00 46.29           N  
ATOM  17909  N   THR C 604     248.583 214.059 195.544  1.00 43.18           N  
ATOM  17910  CA  THR C 604     249.424 215.082 194.915  1.00 43.73           C  
ATOM  17911  C   THR C 604     249.946 216.093 195.930  1.00 43.19           C  
ATOM  17912  O   THR C 604     251.113 216.484 195.876  1.00 43.00           O  
ATOM  17913  CB  THR C 604     248.646 215.835 193.816  1.00 43.43           C  
ATOM  17914  OG1 THR C 604     248.247 214.913 192.797  1.00 44.22           O  
ATOM  17915  CG2 THR C 604     249.513 216.929 193.198  1.00 43.75           C  
ATOM  17916  N   SER C 605     249.084 216.542 196.838  1.00 42.68           N  
ATOM  17917  CA  SER C 605     249.478 217.571 197.795  1.00 42.11           C  
ATOM  17918  C   SER C 605     248.659 217.545 199.078  1.00 41.78           C  
ATOM  17919  O   SER C 605     247.458 217.284 199.060  1.00 41.83           O  
ATOM  17920  CB  SER C 605     249.347 218.935 197.167  1.00 41.27           C  
ATOM  17921  OG  SER C 605     249.702 219.932 198.078  1.00 40.93           O  
ATOM  17922  N   ASN C 606     249.303 217.876 200.193  1.00 40.80           N  
ATOM  17923  CA  ASN C 606     248.607 217.974 201.471  1.00 40.88           C  
ATOM  17924  C   ASN C 606     248.263 219.420 201.804  1.00 40.41           C  
ATOM  17925  O   ASN C 606     247.909 219.741 202.938  1.00 40.45           O  
ATOM  17926  CB  ASN C 606     249.426 217.349 202.574  1.00 40.65           C  
ATOM  17927  CG  ASN C 606     249.517 215.870 202.427  1.00 41.32           C  
ATOM  17928  OD1 ASN C 606     248.563 215.212 201.999  1.00 41.58           O  
ATOM  17929  ND2 ASN C 606     250.651 215.322 202.769  1.00 40.63           N  
ATOM  17930  N   GLU C 607     248.400 220.291 200.819  1.00 40.20           N  
ATOM  17931  CA  GLU C 607     248.054 221.690 200.973  1.00 39.81           C  
ATOM  17932  C   GLU C 607     246.577 221.864 200.686  1.00 39.62           C  
ATOM  17933  O   GLU C 607     246.068 221.309 199.716  1.00 40.63           O  
ATOM  17934  CB  GLU C 607     248.891 222.538 200.024  1.00 39.72           C  
ATOM  17935  CG  GLU C 607     248.702 224.020 200.147  1.00 39.62           C  
ATOM  17936  CD  GLU C 607     249.602 224.746 199.221  1.00 40.31           C  
ATOM  17937  OE1 GLU C 607     250.373 224.093 198.566  1.00 40.52           O  
ATOM  17938  OE2 GLU C 607     249.531 225.947 199.157  1.00 40.48           O  
ATOM  17939  N   VAL C 608     245.878 222.615 201.524  1.00 39.27           N  
ATOM  17940  CA  VAL C 608     244.463 222.861 201.281  1.00 39.13           C  
ATOM  17941  C   VAL C 608     244.107 224.327 201.403  1.00 39.26           C  
ATOM  17942  O   VAL C 608     244.824 225.097 202.039  1.00 39.59           O  
ATOM  17943  CB  VAL C 608     243.585 222.054 202.243  1.00 39.27           C  
ATOM  17944  CG1 VAL C 608     243.835 220.588 202.055  1.00 40.10           C  
ATOM  17945  CG2 VAL C 608     243.862 222.454 203.672  1.00 40.05           C  
ATOM  17946  N   ALA C 609     242.970 224.695 200.831  1.00 39.23           N  
ATOM  17947  CA  ALA C 609     242.423 226.040 200.984  1.00 39.32           C  
ATOM  17948  C   ALA C 609     241.094 225.935 201.708  1.00 38.69           C  
ATOM  17949  O   ALA C 609     240.385 224.942 201.563  1.00 39.89           O  
ATOM  17950  CB  ALA C 609     242.266 226.722 199.637  1.00 39.41           C  
ATOM  17951  N   VAL C 610     240.745 226.936 202.497  1.00 38.90           N  
ATOM  17952  CA  VAL C 610     239.510 226.835 203.263  1.00 38.70           C  
ATOM  17953  C   VAL C 610     238.495 227.906 202.936  1.00 38.16           C  
ATOM  17954  O   VAL C 610     238.801 229.095 202.909  1.00 39.80           O  
ATOM  17955  CB  VAL C 610     239.817 226.870 204.763  1.00 39.10           C  
ATOM  17956  CG1 VAL C 610     238.527 226.780 205.564  1.00 39.54           C  
ATOM  17957  CG2 VAL C 610     240.732 225.719 205.104  1.00 39.99           C  
ATOM  17958  N   LEU C 611     237.275 227.466 202.682  1.00 38.49           N  
ATOM  17959  CA  LEU C 611     236.170 228.356 202.395  1.00 38.38           C  
ATOM  17960  C   LEU C 611     235.227 228.495 203.571  1.00 40.30           C  
ATOM  17961  O   LEU C 611     234.627 227.518 204.025  1.00 37.81           O  
ATOM  17962  CB  LEU C 611     235.355 227.821 201.222  1.00 38.26           C  
ATOM  17963  CG  LEU C 611     234.075 228.609 200.867  1.00 38.62           C  
ATOM  17964  CD1 LEU C 611     234.444 229.973 200.273  1.00 38.74           C  
ATOM  17965  CD2 LEU C 611     233.255 227.782 199.936  1.00 38.75           C  
ATOM  17966  N   TYR C 612     235.036 229.714 204.021  1.00 38.45           N  
ATOM  17967  CA  TYR C 612     234.070 229.978 205.069  1.00 38.48           C  
ATOM  17968  C   TYR C 612     232.816 230.470 204.387  1.00 41.24           C  
ATOM  17969  O   TYR C 612     232.809 231.555 203.798  1.00 36.34           O  
ATOM  17970  CB  TYR C 612     234.636 230.990 206.046  1.00 39.07           C  
ATOM  17971  CG  TYR C 612     235.791 230.463 206.808  1.00 39.24           C  
ATOM  17972  CD1 TYR C 612     237.049 230.457 206.255  1.00 39.15           C  
ATOM  17973  CD2 TYR C 612     235.593 229.982 208.065  1.00 39.66           C  
ATOM  17974  CE1 TYR C 612     238.104 229.957 206.975  1.00 39.29           C  
ATOM  17975  CE2 TYR C 612     236.641 229.487 208.788  1.00 39.82           C  
ATOM  17976  CZ  TYR C 612     237.894 229.473 208.246  1.00 39.50           C  
ATOM  17977  OH  TYR C 612     238.949 228.979 208.969  1.00 39.65           O  
ATOM  17978  N   GLN C 613     231.774 229.655 204.412  1.00 38.49           N  
ATOM  17979  CA  GLN C 613     230.595 229.913 203.604  1.00 38.55           C  
ATOM  17980  C   GLN C 613     229.793 231.100 204.088  1.00 38.31           C  
ATOM  17981  O   GLN C 613     229.452 231.199 205.260  1.00 39.21           O  
ATOM  17982  CB  GLN C 613     229.691 228.680 203.605  1.00 38.54           C  
ATOM  17983  CG  GLN C 613     230.268 227.441 202.930  1.00 38.60           C  
ATOM  17984  CD  GLN C 613     229.396 226.223 203.205  1.00 38.40           C  
ATOM  17985  OE1 GLN C 613     228.283 226.374 203.714  1.00 37.86           O  
ATOM  17986  NE2 GLN C 613     229.885 225.025 202.901  1.00 38.33           N  
ATOM  17987  N   ASP C 614     229.443 231.968 203.150  1.00 39.15           N  
ATOM  17988  CA  ASP C 614     228.565 233.112 203.386  1.00 39.19           C  
ATOM  17989  C   ASP C 614     228.983 234.014 204.557  1.00 39.15           C  
ATOM  17990  O   ASP C 614     228.130 234.501 205.295  1.00 39.04           O  
ATOM  17991  CB  ASP C 614     227.133 232.609 203.618  1.00 39.14           C  
ATOM  17992  N   VAL C 615     230.278 234.271 204.701  1.00 39.40           N  
ATOM  17993  CA  VAL C 615     230.742 235.196 205.725  1.00 39.42           C  
ATOM  17994  C   VAL C 615     231.707 236.218 205.127  1.00 39.59           C  
ATOM  17995  O   VAL C 615     232.275 235.973 204.055  1.00 39.67           O  
ATOM  17996  CB  VAL C 615     231.442 234.469 206.900  1.00 39.43           C  
ATOM  17997  CG1 VAL C 615     230.490 233.504 207.592  1.00 39.85           C  
ATOM  17998  CG2 VAL C 615     232.640 233.749 206.383  1.00 39.49           C  
ATOM  17999  N   ASN C 616     231.897 237.355 205.835  1.00 39.94           N  
ATOM  18000  CA  ASN C 616     232.849 238.397 205.515  1.00 40.13           C  
ATOM  18001  C   ASN C 616     234.217 238.041 206.133  1.00 41.95           C  
ATOM  18002  O   ASN C 616     234.280 237.609 207.284  1.00 40.18           O  
ATOM  18003  CB  ASN C 616     232.338 239.757 206.008  1.00 40.67           C  
ATOM  18004  CG  ASN C 616     233.003 240.971 205.325  1.00 41.12           C  
ATOM  18005  OD1 ASN C 616     234.228 240.970 205.065  1.00 40.39           O  
ATOM  18006  ND2 ASN C 616     232.210 241.993 205.034  1.00 41.15           N  
ATOM  18007  N   CYS C 617     235.325 238.254 205.405  1.00 39.95           N  
ATOM  18008  CA  CYS C 617     236.672 237.922 205.836  1.00 40.63           C  
ATOM  18009  C   CYS C 617     237.131 238.664 207.103  1.00 40.63           C  
ATOM  18010  O   CYS C 617     238.107 238.246 207.734  1.00 40.52           O  
ATOM  18011  CB  CYS C 617     237.692 238.204 204.734  1.00 40.96           C  
ATOM  18012  SG  CYS C 617     237.522 237.123 203.276  1.00 40.92           S  
ATOM  18013  N   THR C 618     236.429 239.750 207.467  1.00 40.62           N  
ATOM  18014  CA  THR C 618     236.753 240.569 208.637  1.00 40.12           C  
ATOM  18015  C   THR C 618     236.424 239.855 209.951  1.00 40.81           C  
ATOM  18016  O   THR C 618     236.947 240.207 211.010  1.00 40.23           O  
ATOM  18017  CB  THR C 618     235.984 241.899 208.567  1.00 40.38           C  
ATOM  18018  OG1 THR C 618     234.603 241.630 208.650  1.00 40.47           O  
ATOM  18019  CG2 THR C 618     236.238 242.594 207.267  1.00 40.68           C  
ATOM  18020  N   GLU C 619     235.594 238.818 209.868  1.00 40.19           N  
ATOM  18021  CA  GLU C 619     235.245 238.023 211.046  1.00 40.64           C  
ATOM  18022  C   GLU C 619     236.067 236.730 211.185  1.00 40.48           C  
ATOM  18023  O   GLU C 619     236.176 236.196 212.288  1.00 40.69           O  
ATOM  18024  CB  GLU C 619     233.760 237.653 211.063  1.00 40.82           C  
ATOM  18025  CG  GLU C 619     232.798 238.741 211.563  1.00 41.40           C  
ATOM  18026  CD  GLU C 619     232.225 239.641 210.507  1.00 41.53           C  
ATOM  18027  OE1 GLU C 619     231.849 239.153 209.474  1.00 41.28           O  
ATOM  18028  OE2 GLU C 619     232.126 240.822 210.750  1.00 41.56           O  
ATOM  18029  N   VAL C 620     236.629 236.231 210.071  1.00 40.33           N  
ATOM  18030  CA  VAL C 620     237.366 234.975 210.014  1.00 40.27           C  
ATOM  18031  C   VAL C 620     238.817 235.237 210.449  1.00 39.67           C  
ATOM  18032  O   VAL C 620     239.462 234.384 211.057  1.00 39.46           O  
ATOM  18033  CB  VAL C 620     237.297 234.372 208.563  1.00 40.57           C  
ATOM  18034  CG1 VAL C 620     238.130 233.053 208.450  1.00 40.30           C  
ATOM  18035  CG2 VAL C 620     235.786 234.070 208.160  1.00 40.48           C  
ATOM  18036  N   ASN C 641     246.901 236.356 201.617  1.00 39.50           N  
ATOM  18037  CA  ASN C 641     246.437 235.432 200.585  1.00 39.40           C  
ATOM  18038  C   ASN C 641     244.968 235.042 200.858  1.00 39.46           C  
ATOM  18039  O   ASN C 641     244.637 233.860 201.033  1.00 39.47           O  
ATOM  18040  CB  ASN C 641     247.386 234.216 200.504  1.00 39.72           C  
ATOM  18041  CG  ASN C 641     247.234 233.336 199.215  1.00 39.91           C  
ATOM  18042  OD1 ASN C 641     246.750 233.795 198.170  1.00 39.59           O  
ATOM  18043  ND2 ASN C 641     247.673 232.075 199.302  1.00 40.27           N  
ATOM  18044  N   VAL C 642     244.100 236.068 200.920  1.00 39.31           N  
ATOM  18045  CA  VAL C 642     242.669 235.946 201.201  1.00 38.98           C  
ATOM  18046  C   VAL C 642     241.840 236.567 200.090  1.00 39.07           C  
ATOM  18047  O   VAL C 642     242.068 237.710 199.697  1.00 39.19           O  
ATOM  18048  CB  VAL C 642     242.336 236.629 202.533  1.00 39.56           C  
ATOM  18049  CG1 VAL C 642     240.860 236.516 202.815  1.00 39.91           C  
ATOM  18050  CG2 VAL C 642     243.153 235.992 203.636  1.00 39.38           C  
ATOM  18051  N   PHE C 643     240.876 235.812 199.594  1.00 38.87           N  
ATOM  18052  CA  PHE C 643     240.005 236.264 198.524  1.00 38.75           C  
ATOM  18053  C   PHE C 643     238.545 236.247 198.946  1.00 38.53           C  
ATOM  18054  O   PHE C 643     238.024 235.225 199.390  1.00 39.78           O  
ATOM  18055  CB  PHE C 643     240.216 235.375 197.299  1.00 38.83           C  
ATOM  18056  CG  PHE C 643     239.355 235.704 196.132  1.00 38.80           C  
ATOM  18057  CD1 PHE C 643     239.495 236.904 195.462  1.00 38.93           C  
ATOM  18058  CD2 PHE C 643     238.414 234.804 195.686  1.00 38.70           C  
ATOM  18059  CE1 PHE C 643     238.702 237.194 194.379  1.00 38.96           C  
ATOM  18060  CE2 PHE C 643     237.628 235.090 194.602  1.00 38.45           C  
ATOM  18061  CZ  PHE C 643     237.769 236.286 193.950  1.00 38.59           C  
ATOM  18062  N   GLN C 644     237.877 237.379 198.811  1.00 38.67           N  
ATOM  18063  CA  GLN C 644     236.469 237.442 199.167  1.00 38.58           C  
ATOM  18064  C   GLN C 644     235.629 237.153 197.936  1.00 38.52           C  
ATOM  18065  O   GLN C 644     235.737 237.856 196.932  1.00 39.08           O  
ATOM  18066  CB  GLN C 644     236.098 238.824 199.710  1.00 39.14           C  
ATOM  18067  CG  GLN C 644     234.633 238.969 200.153  1.00 39.34           C  
ATOM  18068  CD  GLN C 644     234.326 238.312 201.507  1.00 39.90           C  
ATOM  18069  OE1 GLN C 644     234.859 238.767 202.534  1.00 40.42           O  
ATOM  18070  NE2 GLN C 644     233.478 237.282 201.514  1.00 39.67           N  
ATOM  18071  N   THR C 645     234.780 236.141 198.015  1.00 38.59           N  
ATOM  18072  CA  THR C 645     233.898 235.804 196.910  1.00 38.58           C  
ATOM  18073  C   THR C 645     232.455 235.758 197.380  1.00 38.93           C  
ATOM  18074  O   THR C 645     232.176 235.828 198.575  1.00 39.11           O  
ATOM  18075  CB  THR C 645     234.301 234.476 196.243  1.00 38.29           C  
ATOM  18076  OG1 THR C 645     233.490 234.275 195.077  1.00 37.87           O  
ATOM  18077  CG2 THR C 645     234.159 233.296 197.185  1.00 38.36           C  
ATOM  18078  N   ARG C 646     231.524 235.632 196.446  1.00 38.49           N  
ATOM  18079  CA  ARG C 646     230.112 235.614 196.800  1.00 38.77           C  
ATOM  18080  C   ARG C 646     229.755 234.409 197.647  1.00 38.31           C  
ATOM  18081  O   ARG C 646     228.808 234.446 198.429  1.00 39.01           O  
ATOM  18082  CB  ARG C 646     229.240 235.633 195.561  1.00 38.92           C  
ATOM  18083  CG  ARG C 646     227.726 235.526 195.816  1.00 38.85           C  
ATOM  18084  CD  ARG C 646     227.181 236.709 196.559  1.00 40.79           C  
ATOM  18085  NE  ARG C 646     225.761 236.553 196.877  1.00 40.78           N  
ATOM  18086  CZ  ARG C 646     225.273 235.894 197.959  1.00 41.24           C  
ATOM  18087  NH1 ARG C 646     226.095 235.324 198.821  1.00 40.65           N  
ATOM  18088  NH2 ARG C 646     223.964 235.820 198.153  1.00 41.97           N  
ATOM  18089  N   ALA C 647     230.505 233.334 197.480  1.00 38.24           N  
ATOM  18090  CA  ALA C 647     230.247 232.099 198.191  1.00 37.97           C  
ATOM  18091  C   ALA C 647     230.798 232.115 199.608  1.00 39.02           C  
ATOM  18092  O   ALA C 647     230.561 231.175 200.367  1.00 39.10           O  
ATOM  18093  CB  ALA C 647     230.853 230.935 197.432  1.00 36.95           C  
ATOM  18094  N   GLY C 648     231.556 233.143 199.975  1.00 39.13           N  
ATOM  18095  CA  GLY C 648     232.191 233.138 201.284  1.00 38.94           C  
ATOM  18096  C   GLY C 648     233.619 233.670 201.227  1.00 38.42           C  
ATOM  18097  O   GLY C 648     234.041 234.233 200.214  1.00 40.77           O  
ATOM  18098  N   CYS C 649     234.356 233.511 202.332  1.00 39.06           N  
ATOM  18099  CA  CYS C 649     235.730 233.981 202.448  1.00 39.15           C  
ATOM  18100  C   CYS C 649     236.673 232.804 202.184  1.00 38.13           C  
ATOM  18101  O   CYS C 649     236.646 231.804 202.908  1.00 40.49           O  
ATOM  18102  CB  CYS C 649     235.979 234.605 203.832  1.00 40.03           C  
ATOM  18103  SG  CYS C 649     237.654 235.250 204.048  1.00 40.79           S  
ATOM  18104  N   LEU C 650     237.480 232.913 201.116  1.00 38.49           N  
ATOM  18105  CA  LEU C 650     238.400 231.868 200.672  1.00 38.31           C  
ATOM  18106  C   LEU C 650     239.827 232.171 201.096  1.00 38.53           C  
ATOM  18107  O   LEU C 650     240.422 233.164 200.677  1.00 39.48           O  
ATOM  18108  CB  LEU C 650     238.311 231.731 199.152  1.00 38.47           C  
ATOM  18109  CG  LEU C 650     239.247 230.739 198.501  1.00 38.44           C  
ATOM  18110  CD1 LEU C 650     238.937 229.337 198.977  1.00 38.86           C  
ATOM  18111  CD2 LEU C 650     239.084 230.842 197.004  1.00 39.72           C  
ATOM  18112  N   ILE C 651     240.381 231.313 201.938  1.00 38.68           N  
ATOM  18113  CA  ILE C 651     241.707 231.555 202.474  1.00 38.84           C  
ATOM  18114  C   ILE C 651     242.729 230.508 202.071  1.00 39.00           C  
ATOM  18115  O   ILE C 651     242.520 229.308 202.245  1.00 39.18           O  
ATOM  18116  CB  ILE C 651     241.636 231.656 204.002  1.00 38.64           C  
ATOM  18117  CG1 ILE C 651     240.710 232.822 204.368  1.00 39.33           C  
ATOM  18118  CG2 ILE C 651     243.032 231.838 204.585  1.00 39.61           C  
ATOM  18119  CD1 ILE C 651     240.388 232.946 205.811  1.00 40.12           C  
ATOM  18120  N   GLY C 652     243.862 230.970 201.550  1.00 39.24           N  
ATOM  18121  CA  GLY C 652     244.954 230.082 201.170  1.00 39.38           C  
ATOM  18122  C   GLY C 652     245.066 229.876 199.667  1.00 39.73           C  
ATOM  18123  O   GLY C 652     246.095 229.413 199.179  1.00 40.15           O  
ATOM  18124  N   ALA C 653     244.021 230.221 198.933  1.00 39.36           N  
ATOM  18125  CA  ALA C 653     244.061 230.107 197.485  1.00 39.26           C  
ATOM  18126  C   ALA C 653     244.442 231.449 196.888  1.00 39.24           C  
ATOM  18127  O   ALA C 653     243.929 232.485 197.309  1.00 39.39           O  
ATOM  18128  CB  ALA C 653     242.725 229.649 196.943  1.00 39.23           C  
ATOM  18129  N   GLU C 654     245.315 231.429 195.894  1.00 39.36           N  
ATOM  18130  CA  GLU C 654     245.725 232.653 195.221  1.00 39.00           C  
ATOM  18131  C   GLU C 654     244.774 232.979 194.092  1.00 39.31           C  
ATOM  18132  O   GLU C 654     244.489 232.126 193.257  1.00 39.06           O  
ATOM  18133  CB  GLU C 654     247.147 232.516 194.682  1.00 39.01           C  
ATOM  18134  CG  GLU C 654     247.683 233.756 193.994  1.00 38.82           C  
ATOM  18135  CD  GLU C 654     249.087 233.587 193.507  1.00 39.50           C  
ATOM  18136  OE1 GLU C 654     249.655 232.550 193.736  1.00 39.28           O  
ATOM  18137  OE2 GLU C 654     249.600 234.498 192.905  1.00 38.74           O  
ATOM  18138  N   HIS C 655     244.282 234.208 194.044  1.00 38.83           N  
ATOM  18139  CA  HIS C 655     243.393 234.568 192.950  1.00 38.26           C  
ATOM  18140  C   HIS C 655     244.197 234.847 191.697  1.00 38.32           C  
ATOM  18141  O   HIS C 655     245.182 235.584 191.731  1.00 38.66           O  
ATOM  18142  CB  HIS C 655     242.522 235.774 193.284  1.00 38.79           C  
ATOM  18143  CG  HIS C 655     241.467 236.006 192.254  1.00 38.50           C  
ATOM  18144  ND1 HIS C 655     240.414 235.137 192.067  1.00 38.68           N  
ATOM  18145  CD2 HIS C 655     241.300 236.998 191.353  1.00 39.05           C  
ATOM  18146  CE1 HIS C 655     239.646 235.584 191.094  1.00 38.35           C  
ATOM  18147  NE2 HIS C 655     240.160 236.712 190.644  1.00 39.24           N  
ATOM  18148  N   VAL C 656     243.773 234.250 190.600  1.00 38.07           N  
ATOM  18149  CA  VAL C 656     244.424 234.384 189.310  1.00 37.69           C  
ATOM  18150  C   VAL C 656     243.453 234.995 188.293  1.00 38.94           C  
ATOM  18151  O   VAL C 656     242.298 234.582 188.226  1.00 38.59           O  
ATOM  18152  CB  VAL C 656     244.926 232.993 188.863  1.00 37.50           C  
ATOM  18153  CG1 VAL C 656     245.532 233.037 187.482  1.00 37.85           C  
ATOM  18154  CG2 VAL C 656     245.962 232.512 189.860  1.00 38.63           C  
ATOM  18155  N   ASN C 657     243.929 235.996 187.519  1.00 38.15           N  
ATOM  18156  CA  ASN C 657     243.105 236.706 186.526  1.00 38.12           C  
ATOM  18157  C   ASN C 657     242.772 235.849 185.300  1.00 37.63           C  
ATOM  18158  O   ASN C 657     241.735 236.074 184.656  1.00 37.58           O  
ATOM  18159  CB  ASN C 657     243.801 238.013 186.096  1.00 38.98           C  
ATOM  18160  CG  ASN C 657     243.418 239.232 186.968  1.00 39.34           C  
ATOM  18161  OD1 ASN C 657     242.582 239.131 187.881  1.00 39.75           O  
ATOM  18162  ND2 ASN C 657     244.032 240.377 186.687  1.00 40.43           N  
ATOM  18163  N   ASN C 658     243.613 234.864 184.957  1.00 37.44           N  
ATOM  18164  CA  ASN C 658     243.401 233.964 183.825  1.00 36.97           C  
ATOM  18165  C   ASN C 658     242.205 233.054 184.064  1.00 36.30           C  
ATOM  18166  O   ASN C 658     242.025 232.535 185.163  1.00 37.09           O  
ATOM  18167  CB  ASN C 658     244.622 233.111 183.603  1.00 37.21           C  
ATOM  18168  CG  ASN C 658     245.810 233.880 183.232  1.00 37.35           C  
ATOM  18169  OD1 ASN C 658     245.738 234.936 182.593  1.00 37.53           O  
ATOM  18170  ND2 ASN C 658     246.940 233.371 183.631  1.00 36.87           N  
ATOM  18171  N   SER C 659     241.404 232.844 183.031  1.00 36.68           N  
ATOM  18172  CA  SER C 659     240.275 231.932 183.137  1.00 35.98           C  
ATOM  18173  C   SER C 659     240.721 230.523 182.799  1.00 36.24           C  
ATOM  18174  O   SER C 659     241.563 230.324 181.922  1.00 36.56           O  
ATOM  18175  CB  SER C 659     239.158 232.359 182.209  1.00 35.80           C  
ATOM  18176  OG  SER C 659     238.645 233.607 182.583  1.00 37.20           O  
ATOM  18177  N   TYR C 660     240.155 229.551 183.488  1.00 35.46           N  
ATOM  18178  CA  TYR C 660     240.480 228.147 183.240  1.00 35.57           C  
ATOM  18179  C   TYR C 660     239.236 227.291 183.283  1.00 36.93           C  
ATOM  18180  O   TYR C 660     238.244 227.668 183.897  1.00 34.72           O  
ATOM  18181  CB  TYR C 660     241.480 227.611 184.265  1.00 36.75           C  
ATOM  18182  CG  TYR C 660     242.789 228.342 184.342  1.00 37.11           C  
ATOM  18183  CD1 TYR C 660     242.933 229.393 185.219  1.00 37.89           C  
ATOM  18184  CD2 TYR C 660     243.849 227.952 183.556  1.00 37.42           C  
ATOM  18185  CE1 TYR C 660     244.124 230.054 185.314  1.00 37.76           C  
ATOM  18186  CE2 TYR C 660     245.052 228.618 183.648  1.00 37.90           C  
ATOM  18187  CZ  TYR C 660     245.192 229.666 184.525  1.00 37.84           C  
ATOM  18188  OH  TYR C 660     246.403 230.327 184.622  1.00 38.15           O  
ATOM  18189  N   GLU C 661     239.283 226.124 182.670  1.00 36.17           N  
ATOM  18190  CA  GLU C 661     238.174 225.194 182.804  1.00 36.34           C  
ATOM  18191  C   GLU C 661     238.046 224.842 184.284  1.00 36.63           C  
ATOM  18192  O   GLU C 661     239.059 224.773 184.980  1.00 37.06           O  
ATOM  18193  CB  GLU C 661     238.417 223.946 181.956  1.00 37.43           C  
ATOM  18194  N   CYS C 662     236.807 224.657 184.770  1.00 35.92           N  
ATOM  18195  CA  CYS C 662     236.528 224.372 186.180  1.00 36.18           C  
ATOM  18196  C   CYS C 662     237.024 222.978 186.580  1.00 36.62           C  
ATOM  18197  O   CYS C 662     236.831 222.006 185.850  1.00 37.02           O  
ATOM  18198  CB  CYS C 662     235.021 224.477 186.464  1.00 36.32           C  
ATOM  18199  SG  CYS C 662     234.571 224.305 188.219  1.00 36.27           S  
ATOM  18200  N   ASP C 663     237.650 222.901 187.768  1.00 36.67           N  
ATOM  18201  CA  ASP C 663     238.156 221.667 188.370  1.00 37.19           C  
ATOM  18202  C   ASP C 663     237.393 221.410 189.671  1.00 36.91           C  
ATOM  18203  O   ASP C 663     236.455 220.612 189.687  1.00 36.86           O  
ATOM  18204  CB  ASP C 663     239.668 221.757 188.601  1.00 37.66           C  
ATOM  18205  CG  ASP C 663     240.283 220.432 189.007  1.00 37.99           C  
ATOM  18206  OD1 ASP C 663     239.570 219.461 189.049  1.00 37.80           O  
ATOM  18207  OD2 ASP C 663     241.470 220.380 189.262  1.00 38.43           O  
ATOM  18208  N   ILE C 664     237.751 222.109 190.753  1.00 36.92           N  
ATOM  18209  CA  ILE C 664     237.003 221.964 191.995  1.00 36.64           C  
ATOM  18210  C   ILE C 664     236.136 223.198 192.226  1.00 35.72           C  
ATOM  18211  O   ILE C 664     236.654 224.236 192.622  1.00 36.98           O  
ATOM  18212  CB  ILE C 664     237.939 221.822 193.208  1.00 37.28           C  
ATOM  18213  CG1 ILE C 664     238.861 220.610 193.030  1.00 38.16           C  
ATOM  18214  CG2 ILE C 664     237.092 221.704 194.484  1.00 37.80           C  
ATOM  18215  CD1 ILE C 664     239.976 220.522 194.070  1.00 39.43           C  
ATOM  18216  N   PRO C 665     234.821 223.123 192.039  1.00 35.61           N  
ATOM  18217  CA  PRO C 665     233.925 224.254 192.068  1.00 34.84           C  
ATOM  18218  C   PRO C 665     233.773 224.819 193.463  1.00 35.08           C  
ATOM  18219  O   PRO C 665     233.675 224.065 194.427  1.00 35.89           O  
ATOM  18220  CB  PRO C 665     232.621 223.639 191.576  1.00 34.55           C  
ATOM  18221  CG  PRO C 665     232.713 222.186 191.956  1.00 35.40           C  
ATOM  18222  CD  PRO C 665     234.177 221.836 191.845  1.00 35.95           C  
ATOM  18223  N   ILE C 666     233.682 226.139 193.556  1.00 34.69           N  
ATOM  18224  CA  ILE C 666     233.389 226.819 194.805  1.00 34.01           C  
ATOM  18225  C   ILE C 666     231.978 227.374 194.785  1.00 33.90           C  
ATOM  18226  O   ILE C 666     231.194 227.150 195.706  1.00 35.21           O  
ATOM  18227  CB  ILE C 666     234.411 227.932 195.070  1.00 34.02           C  
ATOM  18228  CG1 ILE C 666     235.773 227.288 195.294  1.00 34.95           C  
ATOM  18229  CG2 ILE C 666     233.981 228.803 196.221  1.00 34.95           C  
ATOM  18230  CD1 ILE C 666     236.901 228.260 195.379  1.00 36.28           C  
ATOM  18231  N   GLY C 667     231.658 228.092 193.721  1.00 33.52           N  
ATOM  18232  CA  GLY C 667     230.342 228.689 193.571  1.00 31.99           C  
ATOM  18233  C   GLY C 667     230.431 230.096 193.012  1.00 32.17           C  
ATOM  18234  O   GLY C 667     231.470 230.748 193.092  1.00 33.49           O  
ATOM  18235  N   ALA C 668     229.330 230.574 192.453  1.00 31.16           N  
ATOM  18236  CA  ALA C 668     229.235 231.920 191.923  1.00 31.52           C  
ATOM  18237  C   ALA C 668     230.293 232.212 190.870  1.00 32.34           C  
ATOM  18238  O   ALA C 668     230.838 233.314 190.821  1.00 33.29           O  
ATOM  18239  CB  ALA C 668     229.347 232.931 193.047  1.00 33.51           C  
ATOM  18240  N   GLY C 669     230.575 231.237 190.018  1.00 32.00           N  
ATOM  18241  CA  GLY C 669     231.501 231.420 188.915  1.00 32.63           C  
ATOM  18242  C   GLY C 669     232.955 231.147 189.257  1.00 33.42           C  
ATOM  18243  O   GLY C 669     233.815 231.211 188.375  1.00 34.61           O  
ATOM  18244  N   ILE C 670     233.245 230.861 190.518  1.00 33.67           N  
ATOM  18245  CA  ILE C 670     234.621 230.618 190.924  1.00 33.87           C  
ATOM  18246  C   ILE C 670     234.885 229.133 191.176  1.00 33.96           C  
ATOM  18247  O   ILE C 670     234.086 228.447 191.828  1.00 34.98           O  
ATOM  18248  CB  ILE C 670     234.979 231.439 192.181  1.00 34.21           C  
ATOM  18249  CG1 ILE C 670     234.699 232.944 191.946  1.00 34.84           C  
ATOM  18250  CG2 ILE C 670     236.447 231.221 192.568  1.00 35.26           C  
ATOM  18251  CD1 ILE C 670     235.477 233.586 190.799  1.00 35.45           C  
ATOM  18252  N   CYS C 671     236.004 228.642 190.626  1.00 34.78           N  
ATOM  18253  CA  CYS C 671     236.508 227.281 190.801  1.00 34.93           C  
ATOM  18254  C   CYS C 671     237.963 227.358 191.277  1.00 37.95           C  
ATOM  18255  O   CYS C 671     238.646 228.361 191.042  1.00 35.66           O  
ATOM  18256  CB  CYS C 671     236.398 226.459 189.496  1.00 35.96           C  
ATOM  18257  SG  CYS C 671     234.700 226.216 188.904  1.00 36.44           S  
ATOM  18258  N   ALA C 672     238.426 226.301 191.959  1.00 36.36           N  
ATOM  18259  CA  ALA C 672     239.802 226.152 192.433  1.00 37.73           C  
ATOM  18260  C   ALA C 672     240.535 225.065 191.670  1.00 37.45           C  
ATOM  18261  O   ALA C 672     239.924 224.150 191.115  1.00 38.73           O  
ATOM  18262  CB  ALA C 672     239.819 225.828 193.906  1.00 38.28           C  
ATOM  18263  N   SER C 673     241.855 225.168 191.655  1.00 38.63           N  
ATOM  18264  CA  SER C 673     242.707 224.150 191.053  1.00 39.26           C  
ATOM  18265  C   SER C 673     244.094 224.203 191.653  1.00 39.72           C  
ATOM  18266  O   SER C 673     244.437 225.151 192.356  1.00 40.47           O  
ATOM  18267  CB  SER C 673     242.811 224.336 189.558  1.00 39.37           C  
ATOM  18268  OG  SER C 673     243.536 225.486 189.254  1.00 39.50           O  
ATOM  18269  N   TYR C 674     244.890 223.181 191.383  1.00 40.12           N  
ATOM  18270  CA  TYR C 674     246.265 223.142 191.853  1.00 40.36           C  
ATOM  18271  C   TYR C 674     247.196 223.223 190.654  1.00 40.48           C  
ATOM  18272  O   TYR C 674     247.145 222.376 189.761  1.00 40.73           O  
ATOM  18273  CB  TYR C 674     246.481 221.872 192.663  1.00 40.39           C  
ATOM  18274  CG  TYR C 674     247.832 221.724 193.287  1.00 40.59           C  
ATOM  18275  CD1 TYR C 674     248.153 222.447 194.417  1.00 41.53           C  
ATOM  18276  CD2 TYR C 674     248.742 220.851 192.745  1.00 41.37           C  
ATOM  18277  CE1 TYR C 674     249.386 222.294 195.003  1.00 41.09           C  
ATOM  18278  CE2 TYR C 674     249.970 220.698 193.324  1.00 41.62           C  
ATOM  18279  CZ  TYR C 674     250.295 221.409 194.449  1.00 41.47           C  
ATOM  18280  OH  TYR C 674     251.534 221.250 195.019  1.00 41.90           O  
ATOM  18281  N   GLN C 675     248.004 224.275 190.605  1.00 40.44           N  
ATOM  18282  CA  GLN C 675     248.861 224.519 189.448  1.00 41.34           C  
ATOM  18283  C   GLN C 675     250.264 224.992 189.821  1.00 41.50           C  
ATOM  18284  O   GLN C 675     250.468 225.563 190.895  1.00 41.34           O  
ATOM  18285  CB  GLN C 675     248.218 225.541 188.503  1.00 40.81           C  
ATOM  18286  CG  GLN C 675     246.924 225.082 187.868  1.00 40.80           C  
ATOM  18287  CD  GLN C 675     246.470 226.019 186.767  1.00 40.37           C  
ATOM  18288  OE1 GLN C 675     246.929 227.162 186.684  1.00 40.04           O  
ATOM  18289  NE2 GLN C 675     245.579 225.538 185.911  1.00 39.84           N  
ATOM  18290  N   THR C 676     251.225 224.770 188.901  1.00 41.93           N  
ATOM  18291  CA  THR C 676     252.616 225.218 189.017  1.00 42.26           C  
ATOM  18292  C   THR C 676     252.690 226.753 188.947  1.00 42.45           C  
ATOM  18293  O   THR C 676     252.578 227.353 187.875  1.00 42.48           O  
ATOM  18294  CB  THR C 676     253.506 224.546 187.917  1.00 42.76           C  
ATOM  18295  OG1 THR C 676     253.407 223.113 188.043  1.00 42.61           O  
ATOM  18296  CG2 THR C 676     255.021 224.950 188.055  1.00 42.74           C  
ATOM  18297  N   GLN C 690     254.370 225.137 193.068  1.00 41.20           N  
ATOM  18298  CA  GLN C 690     252.966 224.767 192.949  1.00 41.64           C  
ATOM  18299  C   GLN C 690     252.174 225.304 194.145  1.00 41.30           C  
ATOM  18300  O   GLN C 690     252.706 225.385 195.258  1.00 41.63           O  
ATOM  18301  CB  GLN C 690     252.801 223.228 192.862  1.00 41.81           C  
ATOM  18302  CG  GLN C 690     253.430 222.519 191.616  1.00 41.96           C  
ATOM  18303  CD  GLN C 690     253.283 220.953 191.646  1.00 42.18           C  
ATOM  18304  OE1 GLN C 690     253.095 220.337 192.716  1.00 42.16           O  
ATOM  18305  NE2 GLN C 690     253.372 220.312 190.439  1.00 41.20           N  
ATOM  18306  N   SER C 691     250.904 225.672 193.901  1.00 41.23           N  
ATOM  18307  CA  SER C 691     249.975 226.187 194.917  1.00 40.61           C  
ATOM  18308  C   SER C 691     248.529 226.043 194.475  1.00 41.14           C  
ATOM  18309  O   SER C 691     248.244 225.721 193.318  1.00 41.20           O  
ATOM  18310  CB  SER C 691     250.251 227.647 195.216  1.00 40.99           C  
ATOM  18311  OG  SER C 691     249.984 228.434 194.103  1.00 41.00           O  
ATOM  18312  N   ILE C 692     247.612 226.290 195.401  1.00 39.91           N  
ATOM  18313  CA  ILE C 692     246.192 226.298 195.085  1.00 39.48           C  
ATOM  18314  C   ILE C 692     245.785 227.675 194.613  1.00 39.32           C  
ATOM  18315  O   ILE C 692     246.126 228.678 195.243  1.00 40.45           O  
ATOM  18316  CB  ILE C 692     245.339 225.899 196.294  1.00 39.55           C  
ATOM  18317  CG1 ILE C 692     245.695 224.493 196.697  1.00 39.92           C  
ATOM  18318  CG2 ILE C 692     243.847 226.004 195.944  1.00 39.50           C  
ATOM  18319  CD1 ILE C 692     245.141 224.076 198.018  1.00 39.88           C  
ATOM  18320  N   ILE C 693     245.069 227.716 193.502  1.00 39.13           N  
ATOM  18321  CA  ILE C 693     244.617 228.969 192.940  1.00 38.66           C  
ATOM  18322  C   ILE C 693     243.115 228.977 192.772  1.00 39.27           C  
ATOM  18323  O   ILE C 693     242.474 227.928 192.693  1.00 39.17           O  
ATOM  18324  CB  ILE C 693     245.261 229.240 191.569  1.00 38.89           C  
ATOM  18325  CG1 ILE C 693     244.832 228.161 190.550  1.00 39.24           C  
ATOM  18326  CG2 ILE C 693     246.772 229.268 191.722  1.00 39.58           C  
ATOM  18327  CD1 ILE C 693     245.184 228.477 189.114  1.00 39.51           C  
ATOM  18328  N   ALA C 694     242.568 230.174 192.671  1.00 37.97           N  
ATOM  18329  CA  ALA C 694     241.161 230.378 192.395  1.00 37.36           C  
ATOM  18330  C   ALA C 694     241.040 231.217 191.147  1.00 40.24           C  
ATOM  18331  O   ALA C 694     241.846 232.116 190.914  1.00 37.66           O  
ATOM  18332  CB  ALA C 694     240.474 231.049 193.563  1.00 38.38           C  
ATOM  18333  N   TYR C 695     240.033 230.934 190.353  1.00 36.48           N  
ATOM  18334  CA  TYR C 695     239.850 231.631 189.098  1.00 35.80           C  
ATOM  18335  C   TYR C 695     238.409 231.636 188.666  1.00 38.53           C  
ATOM  18336  O   TYR C 695     237.616 230.797 189.096  1.00 35.42           O  
ATOM  18337  CB  TYR C 695     240.698 230.940 188.036  1.00 36.08           C  
ATOM  18338  CG  TYR C 695     240.390 229.469 187.987  1.00 35.42           C  
ATOM  18339  CD1 TYR C 695     239.427 228.960 187.151  1.00 35.42           C  
ATOM  18340  CD2 TYR C 695     241.062 228.633 188.824  1.00 37.71           C  
ATOM  18341  CE1 TYR C 695     239.141 227.614 187.167  1.00 36.55           C  
ATOM  18342  CE2 TYR C 695     240.776 227.308 188.840  1.00 37.23           C  
ATOM  18343  CZ  TYR C 695     239.824 226.791 188.025  1.00 37.62           C  
ATOM  18344  OH  TYR C 695     239.539 225.448 188.078  1.00 37.30           O  
ATOM  18345  N   THR C 696     238.073 232.547 187.772  1.00 35.20           N  
ATOM  18346  CA  THR C 696     236.767 232.498 187.162  1.00 34.81           C  
ATOM  18347  C   THR C 696     236.812 231.388 186.142  1.00 34.74           C  
ATOM  18348  O   THR C 696     237.770 231.289 185.369  1.00 36.86           O  
ATOM  18349  CB  THR C 696     236.390 233.830 186.510  1.00 35.00           C  
ATOM  18350  OG1 THR C 696     236.405 234.863 187.499  1.00 35.91           O  
ATOM  18351  CG2 THR C 696     235.007 233.746 185.897  1.00 35.39           C  
ATOM  18352  N   MET C 697     235.818 230.527 186.163  1.00 34.13           N  
ATOM  18353  CA  MET C 697     235.835 229.415 185.239  1.00 33.21           C  
ATOM  18354  C   MET C 697     235.506 229.848 183.828  1.00 33.24           C  
ATOM  18355  O   MET C 697     234.682 230.736 183.607  1.00 33.21           O  
ATOM  18356  CB  MET C 697     234.891 228.315 185.684  1.00 33.88           C  
ATOM  18357  CG  MET C 697     233.449 228.699 185.694  1.00 33.36           C  
ATOM  18358  SD  MET C 697     232.354 227.348 186.153  1.00 34.06           S  
ATOM  18359  CE  MET C 697     232.211 226.493 184.592  1.00 32.38           C  
ATOM  18360  N   SER C 698     236.148 229.194 182.879  1.00 33.96           N  
ATOM  18361  CA  SER C 698     235.875 229.373 181.471  1.00 32.13           C  
ATOM  18362  C   SER C 698     234.698 228.496 181.106  1.00 30.84           C  
ATOM  18363  O   SER C 698     234.547 227.401 181.648  1.00 31.45           O  
ATOM  18364  CB  SER C 698     237.080 229.000 180.643  1.00 32.98           C  
ATOM  18365  OG  SER C 698     236.786 229.081 179.280  1.00 31.57           O  
ATOM  18366  N   LEU C 699     233.853 228.962 180.204  1.00 29.49           N  
ATOM  18367  CA  LEU C 699     232.696 228.167 179.829  1.00 28.68           C  
ATOM  18368  C   LEU C 699     232.988 227.273 178.641  1.00 28.27           C  
ATOM  18369  O   LEU C 699     232.348 226.238 178.458  1.00 27.69           O  
ATOM  18370  CB  LEU C 699     231.523 229.068 179.487  1.00 27.75           C  
ATOM  18371  CG  LEU C 699     230.665 229.533 180.635  1.00 27.44           C  
ATOM  18372  CD1 LEU C 699     231.440 230.433 181.555  1.00 29.09           C  
ATOM  18373  CD2 LEU C 699     229.518 230.254 180.075  1.00 27.25           C  
ATOM  18374  N   GLY C 700     233.956 227.678 177.834  1.00 28.07           N  
ATOM  18375  CA  GLY C 700     234.326 226.950 176.635  1.00 26.74           C  
ATOM  18376  C   GLY C 700     235.291 227.786 175.817  1.00 26.34           C  
ATOM  18377  O   GLY C 700     235.549 228.946 176.143  1.00 26.69           O  
ATOM  18378  N   ALA C 701     235.827 227.203 174.754  1.00 25.63           N  
ATOM  18379  CA  ALA C 701     236.752 227.940 173.900  1.00 25.36           C  
ATOM  18380  C   ALA C 701     235.977 228.929 173.059  1.00 24.85           C  
ATOM  18381  O   ALA C 701     234.899 228.604 172.576  1.00 25.29           O  
ATOM  18382  CB  ALA C 701     237.530 226.997 173.004  1.00 25.62           C  
ATOM  18383  N   GLU C 702     236.520 230.112 172.835  1.00 24.79           N  
ATOM  18384  CA  GLU C 702     235.819 231.046 171.964  1.00 24.55           C  
ATOM  18385  C   GLU C 702     236.043 230.669 170.514  1.00 24.28           C  
ATOM  18386  O   GLU C 702     237.179 230.457 170.090  1.00 24.67           O  
ATOM  18387  CB  GLU C 702     236.280 232.477 172.210  1.00 24.60           C  
ATOM  18388  CG  GLU C 702     235.552 233.514 171.365  1.00 24.76           C  
ATOM  18389  CD  GLU C 702     236.007 234.911 171.641  1.00 25.66           C  
ATOM  18390  OE1 GLU C 702     236.701 235.110 172.606  1.00 24.89           O  
ATOM  18391  OE2 GLU C 702     235.674 235.785 170.873  1.00 25.20           O  
ATOM  18392  N   ASN C 703     234.963 230.582 169.751  1.00 23.99           N  
ATOM  18393  CA  ASN C 703     235.067 230.229 168.345  1.00 23.32           C  
ATOM  18394  C   ASN C 703     233.990 230.894 167.513  1.00 22.95           C  
ATOM  18395  O   ASN C 703     232.889 230.367 167.399  1.00 23.50           O  
ATOM  18396  CB  ASN C 703     234.986 228.726 168.159  1.00 23.31           C  
ATOM  18397  CG  ASN C 703     235.220 228.334 166.730  1.00 23.57           C  
ATOM  18398  OD1 ASN C 703     235.682 229.160 165.937  1.00 23.91           O  
ATOM  18399  ND2 ASN C 703     234.919 227.112 166.374  1.00 23.56           N  
ATOM  18400  N   SER C 704     234.285 232.042 166.925  1.00 22.99           N  
ATOM  18401  CA  SER C 704     233.266 232.708 166.133  1.00 22.84           C  
ATOM  18402  C   SER C 704     233.006 231.898 164.872  1.00 22.62           C  
ATOM  18403  O   SER C 704     233.903 231.219 164.376  1.00 22.67           O  
ATOM  18404  CB  SER C 704     233.708 234.111 165.785  1.00 22.67           C  
ATOM  18405  OG  SER C 704     234.840 234.087 164.965  1.00 22.29           O  
ATOM  18406  N   VAL C 705     231.801 231.995 164.323  1.00 22.41           N  
ATOM  18407  CA  VAL C 705     231.493 231.264 163.096  1.00 22.07           C  
ATOM  18408  C   VAL C 705     231.628 232.182 161.896  1.00 22.16           C  
ATOM  18409  O   VAL C 705     231.106 233.294 161.900  1.00 22.34           O  
ATOM  18410  CB  VAL C 705     230.081 230.643 163.156  1.00 22.02           C  
ATOM  18411  CG1 VAL C 705     229.744 229.938 161.833  1.00 21.91           C  
ATOM  18412  CG2 VAL C 705     230.026 229.646 164.310  1.00 22.48           C  
ATOM  18413  N   ALA C 706     232.313 231.716 160.856  1.00 21.89           N  
ATOM  18414  CA  ALA C 706     232.544 232.533 159.667  1.00 21.74           C  
ATOM  18415  C   ALA C 706     231.319 232.570 158.775  1.00 21.82           C  
ATOM  18416  O   ALA C 706     231.344 232.115 157.635  1.00 22.04           O  
ATOM  18417  CB  ALA C 706     233.718 231.987 158.883  1.00 21.60           C  
ATOM  18418  N   TYR C 707     230.255 233.139 159.308  1.00 21.98           N  
ATOM  18419  CA  TYR C 707     228.985 233.241 158.631  1.00 21.90           C  
ATOM  18420  C   TYR C 707     229.000 234.305 157.568  1.00 22.56           C  
ATOM  18421  O   TYR C 707     229.538 235.394 157.769  1.00 22.83           O  
ATOM  18422  CB  TYR C 707     227.881 233.559 159.625  1.00 22.41           C  
ATOM  18423  CG  TYR C 707     226.532 233.717 158.980  1.00 22.42           C  
ATOM  18424  CD1 TYR C 707     225.726 232.633 158.783  1.00 22.23           C  
ATOM  18425  CD2 TYR C 707     226.112 234.957 158.560  1.00 23.18           C  
ATOM  18426  CE1 TYR C 707     224.506 232.793 158.173  1.00 22.16           C  
ATOM  18427  CE2 TYR C 707     224.904 235.105 157.950  1.00 23.10           C  
ATOM  18428  CZ  TYR C 707     224.105 234.039 157.753  1.00 22.47           C  
ATOM  18429  OH  TYR C 707     222.892 234.202 157.127  1.00 23.06           O  
ATOM  18430  N   SER C 708     228.381 233.993 156.449  1.00 22.53           N  
ATOM  18431  CA  SER C 708     228.144 234.937 155.377  1.00 22.46           C  
ATOM  18432  C   SER C 708     226.937 234.423 154.617  1.00 22.52           C  
ATOM  18433  O   SER C 708     226.557 233.263 154.791  1.00 22.54           O  
ATOM  18434  CB  SER C 708     229.358 235.067 154.489  1.00 22.72           C  
ATOM  18435  OG  SER C 708     229.590 233.887 153.812  1.00 22.44           O  
ATOM  18436  N   ASN C 709     226.341 235.257 153.758  1.00 22.35           N  
ATOM  18437  CA  ASN C 709     225.124 234.900 153.031  1.00 22.19           C  
ATOM  18438  C   ASN C 709     225.373 234.039 151.778  1.00 22.29           C  
ATOM  18439  O   ASN C 709     224.413 233.594 151.139  1.00 22.35           O  
ATOM  18440  CB  ASN C 709     224.340 236.167 152.669  1.00 23.02           C  
ATOM  18441  CG  ASN C 709     225.133 237.198 151.831  1.00 23.01           C  
ATOM  18442  OD1 ASN C 709     226.369 237.131 151.720  1.00 22.82           O  
ATOM  18443  ND2 ASN C 709     224.416 238.142 151.255  1.00 23.38           N  
ATOM  18444  N   ASN C 710     226.644 233.784 151.417  1.00 22.30           N  
ATOM  18445  CA  ASN C 710     227.005 232.998 150.240  1.00 21.45           C  
ATOM  18446  C   ASN C 710     228.095 231.967 150.493  1.00 21.69           C  
ATOM  18447  O   ASN C 710     228.781 231.576 149.552  1.00 22.54           O  
ATOM  18448  CB  ASN C 710     227.429 233.915 149.120  1.00 21.78           C  
ATOM  18449  CG  ASN C 710     228.640 234.694 149.472  1.00 22.30           C  
ATOM  18450  OD1 ASN C 710     229.059 234.722 150.635  1.00 22.37           O  
ATOM  18451  ND2 ASN C 710     229.224 235.334 148.494  1.00 21.97           N  
ATOM  18452  N   SER C 711     228.258 231.497 151.725  1.00 21.54           N  
ATOM  18453  CA  SER C 711     229.315 230.514 151.973  1.00 21.18           C  
ATOM  18454  C   SER C 711     228.850 229.387 152.868  1.00 20.73           C  
ATOM  18455  O   SER C 711     228.243 229.605 153.915  1.00 21.54           O  
ATOM  18456  CB  SER C 711     230.524 231.167 152.597  1.00 21.99           C  
ATOM  18457  OG  SER C 711     231.541 230.229 152.803  1.00 21.72           O  
ATOM  18458  N   ILE C 712     229.129 228.167 152.427  1.00 20.95           N  
ATOM  18459  CA  ILE C 712     228.748 226.974 153.160  1.00 20.37           C  
ATOM  18460  C   ILE C 712     229.947 226.082 153.424  1.00 20.52           C  
ATOM  18461  O   ILE C 712     230.784 225.873 152.550  1.00 21.63           O  
ATOM  18462  CB  ILE C 712     227.682 226.181 152.379  1.00 20.87           C  
ATOM  18463  CG1 ILE C 712     227.165 225.006 153.222  1.00 21.13           C  
ATOM  18464  CG2 ILE C 712     228.271 225.664 151.067  1.00 21.18           C  
ATOM  18465  CD1 ILE C 712     225.885 224.390 152.703  1.00 21.68           C  
ATOM  18466  N   ALA C 713     230.032 225.541 154.624  1.00 20.90           N  
ATOM  18467  CA  ALA C 713     231.098 224.597 154.909  1.00 20.29           C  
ATOM  18468  C   ALA C 713     230.558 223.190 154.800  1.00 20.48           C  
ATOM  18469  O   ALA C 713     229.550 222.843 155.417  1.00 21.00           O  
ATOM  18470  CB  ALA C 713     231.712 224.844 156.264  1.00 20.82           C  
ATOM  18471  N   ILE C 714     231.213 222.394 153.988  1.00 20.69           N  
ATOM  18472  CA  ILE C 714     230.796 221.023 153.755  1.00 20.41           C  
ATOM  18473  C   ILE C 714     231.951 220.100 154.082  1.00 20.64           C  
ATOM  18474  O   ILE C 714     233.065 220.346 153.618  1.00 21.62           O  
ATOM  18475  CB  ILE C 714     230.354 220.837 152.296  1.00 20.83           C  
ATOM  18476  CG1 ILE C 714     229.196 221.773 152.024  1.00 21.45           C  
ATOM  18477  CG2 ILE C 714     229.975 219.383 152.003  1.00 20.89           C  
ATOM  18478  CD1 ILE C 714     228.841 221.904 150.608  1.00 21.85           C  
ATOM  18479  N   PRO C 715     231.745 219.062 154.896  1.00 20.36           N  
ATOM  18480  CA  PRO C 715     232.754 218.123 155.284  1.00 19.97           C  
ATOM  18481  C   PRO C 715     233.184 217.357 154.065  1.00 20.57           C  
ATOM  18482  O   PRO C 715     232.354 217.007 153.234  1.00 21.33           O  
ATOM  18483  CB  PRO C 715     232.036 217.250 156.301  1.00 19.95           C  
ATOM  18484  CG  PRO C 715     230.591 217.378 155.951  1.00 20.49           C  
ATOM  18485  CD  PRO C 715     230.427 218.773 155.427  1.00 20.69           C  
ATOM  18486  N   THR C 716     234.468 217.087 153.980  1.00 20.26           N  
ATOM  18487  CA  THR C 716     235.068 216.320 152.890  1.00 20.44           C  
ATOM  18488  C   THR C 716     235.501 214.911 153.322  1.00 20.50           C  
ATOM  18489  O   THR C 716     235.717 214.038 152.479  1.00 21.03           O  
ATOM  18490  CB  THR C 716     236.287 217.068 152.332  1.00 20.86           C  
ATOM  18491  OG1 THR C 716     237.287 217.180 153.350  1.00 20.86           O  
ATOM  18492  CG2 THR C 716     235.901 218.470 151.867  1.00 20.83           C  
ATOM  18493  N   ASN C 717     235.604 214.694 154.640  1.00 20.50           N  
ATOM  18494  CA  ASN C 717     236.017 213.445 155.267  1.00 19.87           C  
ATOM  18495  C   ASN C 717     235.202 213.272 156.547  1.00 20.03           C  
ATOM  18496  O   ASN C 717     234.492 214.182 156.959  1.00 20.65           O  
ATOM  18497  CB  ASN C 717     237.524 213.470 155.551  1.00 20.99           C  
ATOM  18498  CG  ASN C 717     238.152 212.088 155.761  1.00 20.58           C  
ATOM  18499  OD1 ASN C 717     237.455 211.062 155.776  1.00 20.76           O  
ATOM  18500  ND2 ASN C 717     239.466 212.071 155.931  1.00 21.42           N  
ATOM  18501  N   PHE C 718     235.318 212.097 157.175  1.00 19.68           N  
ATOM  18502  CA  PHE C 718     234.612 211.781 158.414  1.00 19.58           C  
ATOM  18503  C   PHE C 718     235.358 210.752 159.217  1.00 19.54           C  
ATOM  18504  O   PHE C 718     236.216 210.038 158.691  1.00 20.41           O  
ATOM  18505  CB  PHE C 718     233.238 211.218 158.114  1.00 19.65           C  
ATOM  18506  CG  PHE C 718     233.345 209.957 157.390  1.00 19.66           C  
ATOM  18507  CD1 PHE C 718     233.397 208.773 158.069  1.00 19.92           C  
ATOM  18508  CD2 PHE C 718     233.416 209.942 156.022  1.00 20.07           C  
ATOM  18509  CE1 PHE C 718     233.527 207.606 157.405  1.00 20.09           C  
ATOM  18510  CE2 PHE C 718     233.542 208.766 155.342  1.00 20.14           C  
ATOM  18511  CZ  PHE C 718     233.602 207.595 156.034  1.00 19.95           C  
ATOM  18512  N   THR C 719     234.988 210.648 160.480  1.00 19.37           N  
ATOM  18513  CA  THR C 719     235.490 209.591 161.324  1.00 19.83           C  
ATOM  18514  C   THR C 719     234.348 208.873 161.998  1.00 20.12           C  
ATOM  18515  O   THR C 719     233.270 209.434 162.198  1.00 19.82           O  
ATOM  18516  CB  THR C 719     236.448 210.129 162.394  1.00 19.89           C  
ATOM  18517  OG1 THR C 719     235.747 211.033 163.255  1.00 19.58           O  
ATOM  18518  CG2 THR C 719     237.606 210.853 161.739  1.00 20.28           C  
ATOM  18519  N   ILE C 720     234.597 207.640 162.391  1.00 20.08           N  
ATOM  18520  CA  ILE C 720     233.634 206.903 163.173  1.00 20.00           C  
ATOM  18521  C   ILE C 720     234.137 206.847 164.586  1.00 20.53           C  
ATOM  18522  O   ILE C 720     235.257 206.406 164.836  1.00 21.05           O  
ATOM  18523  CB  ILE C 720     233.430 205.475 162.645  1.00 20.17           C  
ATOM  18524  CG1 ILE C 720     233.034 205.495 161.158  1.00 20.06           C  
ATOM  18525  CG2 ILE C 720     232.387 204.739 163.489  1.00 20.65           C  
ATOM  18526  CD1 ILE C 720     231.764 206.247 160.819  1.00 20.08           C  
ATOM  18527  N   SER C 721     233.325 207.306 165.509  1.00 20.53           N  
ATOM  18528  CA  SER C 721     233.727 207.297 166.896  1.00 21.27           C  
ATOM  18529  C   SER C 721     232.804 206.428 167.703  1.00 21.49           C  
ATOM  18530  O   SER C 721     231.634 206.250 167.362  1.00 21.82           O  
ATOM  18531  CB  SER C 721     233.750 208.701 167.450  1.00 21.30           C  
ATOM  18532  OG  SER C 721     232.485 209.271 167.413  1.00 20.92           O  
ATOM  18533  N   VAL C 722     233.331 205.883 168.784  1.00 22.27           N  
ATOM  18534  CA  VAL C 722     232.537 205.075 169.678  1.00 22.18           C  
ATOM  18535  C   VAL C 722     232.598 205.683 171.053  1.00 22.78           C  
ATOM  18536  O   VAL C 722     233.679 205.964 171.565  1.00 23.18           O  
ATOM  18537  CB  VAL C 722     233.031 203.622 169.705  1.00 22.92           C  
ATOM  18538  CG1 VAL C 722     232.186 202.794 170.673  1.00 22.98           C  
ATOM  18539  CG2 VAL C 722     232.943 203.049 168.312  1.00 22.88           C  
ATOM  18540  N   THR C 723     231.442 205.908 171.642  1.00 22.61           N  
ATOM  18541  CA  THR C 723     231.402 206.487 172.969  1.00 22.84           C  
ATOM  18542  C   THR C 723     230.735 205.523 173.921  1.00 23.30           C  
ATOM  18543  O   THR C 723     229.946 204.674 173.506  1.00 23.60           O  
ATOM  18544  CB  THR C 723     230.654 207.828 172.968  1.00 22.91           C  
ATOM  18545  OG1 THR C 723     229.303 207.616 172.570  1.00 22.60           O  
ATOM  18546  CG2 THR C 723     231.307 208.810 172.018  1.00 23.26           C  
ATOM  18547  N   THR C 724     231.027 205.650 175.204  1.00 23.42           N  
ATOM  18548  CA  THR C 724     230.442 204.735 176.166  1.00 23.24           C  
ATOM  18549  C   THR C 724     229.495 205.448 177.104  1.00 23.42           C  
ATOM  18550  O   THR C 724     229.868 206.419 177.761  1.00 24.18           O  
ATOM  18551  CB  THR C 724     231.539 204.037 176.991  1.00 24.22           C  
ATOM  18552  OG1 THR C 724     232.412 203.328 176.123  1.00 24.75           O  
ATOM  18553  CG2 THR C 724     230.938 203.060 177.947  1.00 24.68           C  
ATOM  18554  N   GLU C 725     228.272 204.949 177.188  1.00 23.27           N  
ATOM  18555  CA  GLU C 725     227.295 205.531 178.088  1.00 23.18           C  
ATOM  18556  C   GLU C 725     226.839 204.531 179.131  1.00 23.92           C  
ATOM  18557  O   GLU C 725     226.315 203.466 178.809  1.00 24.54           O  
ATOM  18558  CB  GLU C 725     226.102 206.075 177.325  1.00 22.61           C  
ATOM  18559  CG  GLU C 725     225.104 206.760 178.212  1.00 23.01           C  
ATOM  18560  CD  GLU C 725     224.098 207.531 177.463  1.00 22.74           C  
ATOM  18561  OE1 GLU C 725     223.862 207.235 176.313  1.00 22.23           O  
ATOM  18562  OE2 GLU C 725     223.559 208.449 178.038  1.00 22.27           O  
ATOM  18563  N   ILE C 726     227.050 204.878 180.389  1.00 23.92           N  
ATOM  18564  CA  ILE C 726     226.736 203.986 181.493  1.00 23.98           C  
ATOM  18565  C   ILE C 726     225.494 204.419 182.250  1.00 24.09           C  
ATOM  18566  O   ILE C 726     225.422 205.551 182.730  1.00 24.90           O  
ATOM  18567  CB  ILE C 726     227.918 203.926 182.476  1.00 24.57           C  
ATOM  18568  CG1 ILE C 726     229.174 203.400 181.779  1.00 25.23           C  
ATOM  18569  CG2 ILE C 726     227.581 203.054 183.653  1.00 25.77           C  
ATOM  18570  CD1 ILE C 726     230.128 204.470 181.332  1.00 25.82           C  
ATOM  18571  N   LEU C 727     224.532 203.511 182.376  1.00 24.11           N  
ATOM  18572  CA  LEU C 727     223.314 203.797 183.119  1.00 23.97           C  
ATOM  18573  C   LEU C 727     223.052 202.709 184.162  1.00 24.56           C  
ATOM  18574  O   LEU C 727     223.190 201.525 183.856  1.00 25.63           O  
ATOM  18575  CB  LEU C 727     222.112 203.846 182.172  1.00 23.60           C  
ATOM  18576  CG  LEU C 727     222.151 204.886 181.053  1.00 23.37           C  
ATOM  18577  CD1 LEU C 727     220.985 204.652 180.144  1.00 22.36           C  
ATOM  18578  CD2 LEU C 727     222.084 206.278 181.623  1.00 23.42           C  
ATOM  18579  N   PRO C 728     222.699 203.068 185.399  1.00 24.34           N  
ATOM  18580  CA  PRO C 728     222.190 202.182 186.422  1.00 24.38           C  
ATOM  18581  C   PRO C 728     220.871 201.580 186.004  1.00 24.42           C  
ATOM  18582  O   PRO C 728     220.047 202.254 185.388  1.00 24.95           O  
ATOM  18583  CB  PRO C 728     221.994 203.110 187.612  1.00 24.69           C  
ATOM  18584  CG  PRO C 728     222.917 204.269 187.357  1.00 25.89           C  
ATOM  18585  CD  PRO C 728     222.951 204.427 185.857  1.00 24.91           C  
ATOM  18586  N   VAL C 729     220.648 200.333 186.375  1.00 24.89           N  
ATOM  18587  CA  VAL C 729     219.365 199.695 186.128  1.00 24.52           C  
ATOM  18588  C   VAL C 729     218.699 199.253 187.418  1.00 25.11           C  
ATOM  18589  O   VAL C 729     217.477 199.335 187.543  1.00 25.42           O  
ATOM  18590  CB  VAL C 729     219.511 198.523 185.153  1.00 24.83           C  
ATOM  18591  CG1 VAL C 729     218.193 197.780 185.002  1.00 24.94           C  
ATOM  18592  CG2 VAL C 729     219.938 199.074 183.803  1.00 24.62           C  
ATOM  18593  N   SER C 730     219.482 198.733 188.357  1.00 25.54           N  
ATOM  18594  CA  SER C 730     218.876 198.182 189.556  1.00 25.76           C  
ATOM  18595  C   SER C 730     219.686 198.401 190.822  1.00 26.24           C  
ATOM  18596  O   SER C 730     220.892 198.643 190.792  1.00 26.40           O  
ATOM  18597  CB  SER C 730     218.640 196.702 189.373  1.00 26.05           C  
ATOM  18598  OG  SER C 730     219.845 196.019 189.224  1.00 26.43           O  
ATOM  18599  N   MET C 731     218.985 198.304 191.938  1.00 26.44           N  
ATOM  18600  CA  MET C 731     219.526 198.395 193.281  1.00 26.89           C  
ATOM  18601  C   MET C 731     219.723 197.017 193.860  1.00 27.14           C  
ATOM  18602  O   MET C 731     219.176 196.037 193.358  1.00 27.28           O  
ATOM  18603  CB  MET C 731     218.568 199.144 194.197  1.00 27.21           C  
ATOM  18604  CG  MET C 731     218.302 200.552 193.826  1.00 27.18           C  
ATOM  18605  SD  MET C 731     217.026 201.300 194.853  1.00 27.30           S  
ATOM  18606  CE  MET C 731     217.837 201.619 196.401  1.00 27.89           C  
ATOM  18607  N   THR C 732     220.475 196.945 194.942  1.00 27.47           N  
ATOM  18608  CA  THR C 732     220.567 195.704 195.684  1.00 27.84           C  
ATOM  18609  C   THR C 732     219.211 195.428 196.319  1.00 28.19           C  
ATOM  18610  O   THR C 732     218.609 196.316 196.927  1.00 28.19           O  
ATOM  18611  CB  THR C 732     221.666 195.780 196.758  1.00 28.38           C  
ATOM  18612  OG1 THR C 732     222.940 195.969 196.130  1.00 27.59           O  
ATOM  18613  CG2 THR C 732     221.693 194.521 197.572  1.00 29.62           C  
ATOM  18614  N   LYS C 733     218.727 194.199 196.198  1.00 28.43           N  
ATOM  18615  CA  LYS C 733     217.418 193.857 196.735  1.00 28.37           C  
ATOM  18616  C   LYS C 733     217.471 193.614 198.230  1.00 29.97           C  
ATOM  18617  O   LYS C 733     217.430 192.476 198.700  1.00 31.04           O  
ATOM  18618  CB  LYS C 733     216.865 192.623 196.045  1.00 28.50           C  
ATOM  18619  CG  LYS C 733     216.482 192.819 194.603  1.00 27.68           C  
ATOM  18620  CD  LYS C 733     216.239 191.485 193.923  1.00 28.43           C  
ATOM  18621  CE  LYS C 733     215.019 190.751 194.485  1.00 28.56           C  
ATOM  18622  NZ  LYS C 733     214.762 189.485 193.770  1.00 28.25           N  
ATOM  18623  N   THR C 734     217.589 194.697 198.971  1.00 29.72           N  
ATOM  18624  CA  THR C 734     217.709 194.633 200.415  1.00 30.21           C  
ATOM  18625  C   THR C 734     216.357 194.460 201.082  1.00 30.79           C  
ATOM  18626  O   THR C 734     215.373 195.095 200.703  1.00 30.27           O  
ATOM  18627  CB  THR C 734     218.400 195.884 200.963  1.00 30.46           C  
ATOM  18628  OG1 THR C 734     219.718 195.983 200.411  1.00 30.20           O  
ATOM  18629  CG2 THR C 734     218.488 195.828 202.468  1.00 31.30           C  
ATOM  18630  N   SER C 735     216.319 193.603 202.092  1.00 31.23           N  
ATOM  18631  CA  SER C 735     215.114 193.359 202.867  1.00 31.39           C  
ATOM  18632  C   SER C 735     215.455 193.334 204.348  1.00 32.07           C  
ATOM  18633  O   SER C 735     216.420 192.694 204.769  1.00 33.26           O  
ATOM  18634  CB  SER C 735     214.479 192.051 202.459  1.00 31.60           C  
ATOM  18635  OG  SER C 735     213.342 191.788 203.227  1.00 32.79           O  
ATOM  18636  N   VAL C 736     214.701 194.080 205.140  1.00 31.95           N  
ATOM  18637  CA  VAL C 736     215.001 194.180 206.557  1.00 32.60           C  
ATOM  18638  C   VAL C 736     213.874 193.657 207.413  1.00 32.83           C  
ATOM  18639  O   VAL C 736     212.727 194.060 207.252  1.00 33.02           O  
ATOM  18640  CB  VAL C 736     215.302 195.645 206.937  1.00 32.78           C  
ATOM  18641  CG1 VAL C 736     215.579 195.756 208.426  1.00 33.26           C  
ATOM  18642  CG2 VAL C 736     216.498 196.132 206.138  1.00 32.46           C  
ATOM  18643  N   ASP C 737     214.217 192.785 208.347  1.00 33.38           N  
ATOM  18644  CA  ASP C 737     213.270 192.252 209.307  1.00 33.68           C  
ATOM  18645  C   ASP C 737     213.102 193.276 210.416  1.00 34.85           C  
ATOM  18646  O   ASP C 737     213.964 193.376 211.294  1.00 35.29           O  
ATOM  18647  CB  ASP C 737     213.810 190.925 209.873  1.00 34.63           C  
ATOM  18648  CG  ASP C 737     212.951 190.281 210.965  1.00 36.20           C  
ATOM  18649  OD1 ASP C 737     212.146 190.975 211.551  1.00 36.02           O  
ATOM  18650  OD2 ASP C 737     213.130 189.116 211.237  1.00 37.63           O  
ATOM  18651  N   CYS C 738     212.012 194.075 210.362  1.00 33.71           N  
ATOM  18652  CA  CYS C 738     211.826 195.194 211.279  1.00 33.80           C  
ATOM  18653  C   CYS C 738     211.728 194.762 212.754  1.00 35.30           C  
ATOM  18654  O   CYS C 738     212.171 195.493 213.638  1.00 35.45           O  
ATOM  18655  CB  CYS C 738     210.558 195.986 210.904  1.00 33.76           C  
ATOM  18656  SG  CYS C 738     209.005 195.041 211.030  1.00 34.54           S  
ATOM  18657  N   THR C 739     211.194 193.550 213.019  1.00 34.32           N  
ATOM  18658  CA  THR C 739     211.043 193.047 214.380  1.00 34.27           C  
ATOM  18659  C   THR C 739     212.386 192.655 214.953  1.00 35.85           C  
ATOM  18660  O   THR C 739     212.715 193.023 216.079  1.00 36.99           O  
ATOM  18661  CB  THR C 739     210.097 191.843 214.440  1.00 34.69           C  
ATOM  18662  OG1 THR C 739     208.811 192.219 213.939  1.00 34.70           O  
ATOM  18663  CG2 THR C 739     209.959 191.357 215.877  1.00 34.77           C  
ATOM  18664  N   MET C 740     213.174 191.923 214.174  1.00 34.54           N  
ATOM  18665  CA  MET C 740     214.486 191.511 214.649  1.00 34.70           C  
ATOM  18666  C   MET C 740     215.407 192.704 214.812  1.00 35.06           C  
ATOM  18667  O   MET C 740     216.239 192.735 215.718  1.00 36.22           O  
ATOM  18668  CB  MET C 740     215.114 190.493 213.717  1.00 36.42           C  
ATOM  18669  CG  MET C 740     216.443 189.944 214.210  1.00 37.41           C  
ATOM  18670  SD  MET C 740     217.080 188.639 213.155  1.00 40.71           S  
ATOM  18671  CE  MET C 740     218.693 188.373 213.868  1.00 40.88           C  
ATOM  18672  N   TYR C 741     215.269 193.682 213.926  1.00 34.23           N  
ATOM  18673  CA  TYR C 741     216.080 194.883 213.985  1.00 34.41           C  
ATOM  18674  C   TYR C 741     215.824 195.663 215.266  1.00 35.60           C  
ATOM  18675  O   TYR C 741     216.761 196.051 215.962  1.00 35.61           O  
ATOM  18676  CB  TYR C 741     215.814 195.772 212.772  1.00 34.53           C  
ATOM  18677  CG  TYR C 741     216.538 197.086 212.818  1.00 34.47           C  
ATOM  18678  CD1 TYR C 741     217.844 197.190 212.404  1.00 34.61           C  
ATOM  18679  CD2 TYR C 741     215.888 198.189 213.291  1.00 34.38           C  
ATOM  18680  CE1 TYR C 741     218.481 198.410 212.470  1.00 34.43           C  
ATOM  18681  CE2 TYR C 741     216.515 199.389 213.357  1.00 34.30           C  
ATOM  18682  CZ  TYR C 741     217.794 199.509 212.955  1.00 34.11           C  
ATOM  18683  OH  TYR C 741     218.404 200.725 213.036  1.00 34.38           O  
ATOM  18684  N   ILE C 742     214.550 195.906 215.576  1.00 35.93           N  
ATOM  18685  CA  ILE C 742     214.211 196.708 216.746  1.00 35.13           C  
ATOM  18686  C   ILE C 742     214.349 195.944 218.070  1.00 36.33           C  
ATOM  18687  O   ILE C 742     214.938 196.468 219.023  1.00 37.33           O  
ATOM  18688  CB  ILE C 742     212.768 197.243 216.648  1.00 35.47           C  
ATOM  18689  CG1 ILE C 742     212.626 198.170 215.458  1.00 34.79           C  
ATOM  18690  CG2 ILE C 742     212.431 197.998 217.930  1.00 36.62           C  
ATOM  18691  CD1 ILE C 742     211.202 198.512 215.120  1.00 34.89           C  
ATOM  18692  N   CYS C 743     213.791 194.723 218.140  1.00 36.70           N  
ATOM  18693  CA  CYS C 743     213.693 193.884 219.338  1.00 37.42           C  
ATOM  18694  C   CYS C 743     214.368 192.545 219.117  1.00 37.60           C  
ATOM  18695  O   CYS C 743     213.660 191.476 219.167  1.00 37.91           O  
ATOM  18696  CB  CYS C 743     212.243 193.720 219.768  1.00 38.08           C  
ATOM  18697  SG  CYS C 743     211.383 195.248 220.220  1.00 38.79           S  
ATOM  18698  N   GLY C 744     215.663 192.496 218.872  1.00 37.75           N  
ATOM  18699  CA  GLY C 744     216.380 191.270 218.540  1.00 38.36           C  
ATOM  18700  C   GLY C 744     216.382 190.305 219.715  1.00 39.85           C  
ATOM  18701  O   GLY C 744     216.959 190.589 220.764  1.00 40.24           O  
ATOM  18702  N   ASP C 745     215.714 189.172 219.528  1.00 40.27           N  
ATOM  18703  CA  ASP C 745     215.606 188.126 220.534  1.00 40.59           C  
ATOM  18704  C   ASP C 745     215.110 188.634 221.888  1.00 40.10           C  
ATOM  18705  O   ASP C 745     215.572 188.174 222.933  1.00 40.33           O  
ATOM  18706  CB  ASP C 745     216.953 187.428 220.706  1.00 41.50           C  
ATOM  18707  N   SER C 746     214.136 189.541 221.882  1.00 39.56           N  
ATOM  18708  CA  SER C 746     213.591 190.045 223.138  1.00 39.53           C  
ATOM  18709  C   SER C 746     212.075 190.020 223.199  1.00 39.07           C  
ATOM  18710  O   SER C 746     211.398 190.777 222.500  1.00 40.48           O  
ATOM  18711  CB  SER C 746     214.060 191.452 223.374  1.00 39.95           C  
ATOM  18712  OG  SER C 746     213.395 192.011 224.475  1.00 40.15           O  
ATOM  18713  N   THR C 747     211.543 189.156 224.059  1.00 39.29           N  
ATOM  18714  CA  THR C 747     210.100 188.993 224.203  1.00 39.40           C  
ATOM  18715  C   THR C 747     209.443 190.231 224.786  1.00 38.28           C  
ATOM  18716  O   THR C 747     208.396 190.671 224.307  1.00 40.00           O  
ATOM  18717  CB  THR C 747     209.766 187.775 225.083  1.00 39.51           C  
ATOM  18718  OG1 THR C 747     210.261 186.584 224.457  1.00 40.43           O  
ATOM  18719  CG2 THR C 747     208.259 187.655 225.273  1.00 39.70           C  
ATOM  18720  N   GLU C 748     210.057 190.797 225.816  1.00 39.15           N  
ATOM  18721  CA  GLU C 748     209.484 191.964 226.476  1.00 38.74           C  
ATOM  18722  C   GLU C 748     209.415 193.168 225.534  1.00 39.48           C  
ATOM  18723  O   GLU C 748     208.402 193.872 225.498  1.00 39.74           O  
ATOM  18724  CB  GLU C 748     210.308 192.313 227.714  1.00 40.29           C  
ATOM  18725  N   CYS C 749     210.477 193.374 224.733  1.00 38.74           N  
ATOM  18726  CA  CYS C 749     210.539 194.444 223.740  1.00 38.23           C  
ATOM  18727  C   CYS C 749     209.477 194.239 222.648  1.00 39.23           C  
ATOM  18728  O   CYS C 749     208.787 195.196 222.286  1.00 38.35           O  
ATOM  18729  CB  CYS C 749     211.950 194.529 223.147  1.00 39.92           C  
ATOM  18730  SG  CYS C 749     212.251 195.870 221.956  1.00 40.33           S  
ATOM  18731  N   SER C 750     209.324 192.995 222.137  1.00 38.27           N  
ATOM  18732  CA  SER C 750     208.346 192.671 221.094  1.00 37.78           C  
ATOM  18733  C   SER C 750     206.931 192.982 221.565  1.00 37.83           C  
ATOM  18734  O   SER C 750     206.140 193.577 220.834  1.00 39.02           O  
ATOM  18735  CB  SER C 750     208.451 191.211 220.710  1.00 38.22           C  
ATOM  18736  OG  SER C 750     207.533 190.889 219.702  1.00 38.20           O  
ATOM  18737  N   ASN C 751     206.628 192.646 222.814  1.00 38.37           N  
ATOM  18738  CA  ASN C 751     205.305 192.932 223.344  1.00 37.79           C  
ATOM  18739  C   ASN C 751     205.017 194.432 223.348  1.00 37.62           C  
ATOM  18740  O   ASN C 751     203.873 194.847 223.149  1.00 37.95           O  
ATOM  18741  CB  ASN C 751     205.157 192.353 224.731  1.00 38.35           C  
ATOM  18742  CG  ASN C 751     205.024 190.865 224.712  1.00 38.72           C  
ATOM  18743  OD1 ASN C 751     204.719 190.263 223.677  1.00 38.78           O  
ATOM  18744  ND2 ASN C 751     205.239 190.250 225.844  1.00 39.53           N  
ATOM  18745  N   LEU C 752     206.051 195.247 223.559  1.00 37.38           N  
ATOM  18746  CA  LEU C 752     205.890 196.694 223.510  1.00 36.90           C  
ATOM  18747  C   LEU C 752     205.819 197.170 222.062  1.00 38.14           C  
ATOM  18748  O   LEU C 752     205.067 198.080 221.726  1.00 37.47           O  
ATOM  18749  CB  LEU C 752     207.068 197.386 224.205  1.00 38.33           C  
ATOM  18750  CG  LEU C 752     207.217 197.162 225.718  1.00 38.88           C  
ATOM  18751  CD1 LEU C 752     208.558 197.720 226.162  1.00 39.64           C  
ATOM  18752  CD2 LEU C 752     206.087 197.857 226.463  1.00 39.63           C  
ATOM  18753  N   LEU C 753     206.579 196.526 221.184  1.00 37.09           N  
ATOM  18754  CA  LEU C 753     206.609 196.899 219.775  1.00 36.30           C  
ATOM  18755  C   LEU C 753     205.248 196.717 219.127  1.00 36.87           C  
ATOM  18756  O   LEU C 753     204.848 197.511 218.279  1.00 36.25           O  
ATOM  18757  CB  LEU C 753     207.668 196.089 219.024  1.00 37.01           C  
ATOM  18758  CG  LEU C 753     207.860 196.405 217.521  1.00 36.54           C  
ATOM  18759  CD1 LEU C 753     208.220 197.869 217.327  1.00 36.03           C  
ATOM  18760  CD2 LEU C 753     208.977 195.517 216.979  1.00 36.18           C  
ATOM  18761  N   LEU C 754     204.513 195.701 219.554  1.00 36.05           N  
ATOM  18762  CA  LEU C 754     203.191 195.415 219.006  1.00 36.52           C  
ATOM  18763  C   LEU C 754     202.204 196.550 219.247  1.00 36.20           C  
ATOM  18764  O   LEU C 754     201.171 196.636 218.582  1.00 35.91           O  
ATOM  18765  CB  LEU C 754     202.616 194.137 219.627  1.00 37.00           C  
ATOM  18766  CG  LEU C 754     203.299 192.812 219.265  1.00 37.50           C  
ATOM  18767  CD1 LEU C 754     202.711 191.711 220.131  1.00 38.27           C  
ATOM  18768  CD2 LEU C 754     203.090 192.498 217.792  1.00 37.28           C  
ATOM  18769  N   GLN C 755     202.516 197.441 220.175  1.00 36.07           N  
ATOM  18770  CA  GLN C 755     201.621 198.534 220.503  1.00 35.76           C  
ATOM  18771  C   GLN C 755     201.654 199.601 219.421  1.00 36.02           C  
ATOM  18772  O   GLN C 755     200.854 200.537 219.438  1.00 36.05           O  
ATOM  18773  CB  GLN C 755     201.996 199.135 221.852  1.00 36.32           C  
ATOM  18774  CG  GLN C 755     201.815 198.176 223.005  1.00 36.76           C  
ATOM  18775  CD  GLN C 755     202.247 198.765 224.306  1.00 37.49           C  
ATOM  18776  OE1 GLN C 755     202.542 199.956 224.386  1.00 37.27           O  
ATOM  18777  NE2 GLN C 755     202.291 197.941 225.343  1.00 38.29           N  
ATOM  18778  N   TYR C 756     202.567 199.448 218.467  1.00 35.19           N  
ATOM  18779  CA  TYR C 756     202.712 200.384 217.368  1.00 34.60           C  
ATOM  18780  C   TYR C 756     201.988 199.885 216.125  1.00 34.40           C  
ATOM  18781  O   TYR C 756     202.083 200.482 215.047  1.00 34.27           O  
ATOM  18782  CB  TYR C 756     204.189 200.628 217.101  1.00 34.72           C  
ATOM  18783  CG  TYR C 756     204.822 201.423 218.190  1.00 35.06           C  
ATOM  18784  CD1 TYR C 756     205.357 200.788 219.286  1.00 35.63           C  
ATOM  18785  CD2 TYR C 756     204.863 202.796 218.099  1.00 35.23           C  
ATOM  18786  CE1 TYR C 756     205.926 201.519 220.295  1.00 35.61           C  
ATOM  18787  CE2 TYR C 756     205.433 203.531 219.105  1.00 35.85           C  
ATOM  18788  CZ  TYR C 756     205.962 202.896 220.203  1.00 35.84           C  
ATOM  18789  OH  TYR C 756     206.529 203.631 221.214  1.00 36.93           O  
ATOM  18790  N   GLY C 757     201.227 198.810 216.290  1.00 34.74           N  
ATOM  18791  CA  GLY C 757     200.376 198.309 215.227  1.00 34.18           C  
ATOM  18792  C   GLY C 757     201.116 197.847 213.991  1.00 33.71           C  
ATOM  18793  O   GLY C 757     201.984 196.976 214.050  1.00 33.87           O  
ATOM  18794  N   SER C 758     200.747 198.430 212.858  1.00 33.20           N  
ATOM  18795  CA  SER C 758     201.294 198.069 211.561  1.00 32.81           C  
ATOM  18796  C   SER C 758     202.551 198.823 211.177  1.00 32.76           C  
ATOM  18797  O   SER C 758     203.099 198.585 210.103  1.00 32.66           O  
ATOM  18798  CB  SER C 758     200.255 198.279 210.478  1.00 32.79           C  
ATOM  18799  OG  SER C 758     199.158 197.437 210.667  1.00 33.28           O  
ATOM  18800  N   PHE C 759     203.043 199.728 212.019  1.00 32.94           N  
ATOM  18801  CA  PHE C 759     204.235 200.468 211.593  1.00 32.23           C  
ATOM  18802  C   PHE C 759     205.352 199.535 211.119  1.00 32.19           C  
ATOM  18803  O   PHE C 759     205.934 199.766 210.057  1.00 32.94           O  
ATOM  18804  CB  PHE C 759     204.786 201.364 212.709  1.00 32.43           C  
ATOM  18805  CG  PHE C 759     204.228 202.755 212.779  1.00 32.35           C  
ATOM  18806  CD1 PHE C 759     203.727 203.255 213.962  1.00 32.92           C  
ATOM  18807  CD2 PHE C 759     204.233 203.582 211.668  1.00 31.94           C  
ATOM  18808  CE1 PHE C 759     203.247 204.534 214.039  1.00 32.32           C  
ATOM  18809  CE2 PHE C 759     203.748 204.861 211.748  1.00 31.87           C  
ATOM  18810  CZ  PHE C 759     203.256 205.330 212.942  1.00 31.78           C  
ATOM  18811  N   CYS C 760     205.629 198.469 211.883  1.00 32.19           N  
ATOM  18812  CA  CYS C 760     206.678 197.497 211.571  1.00 32.26           C  
ATOM  18813  C   CYS C 760     206.353 196.761 210.234  1.00 32.33           C  
ATOM  18814  O   CYS C 760     207.203 196.678 209.336  1.00 32.47           O  
ATOM  18815  CB  CYS C 760     206.804 196.519 212.775  1.00 33.71           C  
ATOM  18816  SG  CYS C 760     208.285 195.457 212.874  1.00 35.44           S  
ATOM  18817  N   THR C 761     205.103 196.279 210.085  1.00 32.03           N  
ATOM  18818  CA  THR C 761     204.652 195.525 208.907  1.00 31.82           C  
ATOM  18819  C   THR C 761     204.694 196.317 207.607  1.00 31.34           C  
ATOM  18820  O   THR C 761     205.113 195.789 206.574  1.00 31.47           O  
ATOM  18821  CB  THR C 761     203.220 195.000 209.104  1.00 32.42           C  
ATOM  18822  OG1 THR C 761     203.190 194.090 210.209  1.00 33.62           O  
ATOM  18823  CG2 THR C 761     202.741 194.283 207.850  1.00 32.41           C  
ATOM  18824  N   GLN C 762     204.241 197.567 207.631  1.00 31.47           N  
ATOM  18825  CA  GLN C 762     204.230 198.327 206.394  1.00 30.55           C  
ATOM  18826  C   GLN C 762     205.643 198.685 205.942  1.00 30.83           C  
ATOM  18827  O   GLN C 762     205.874 198.867 204.747  1.00 31.03           O  
ATOM  18828  CB  GLN C 762     203.350 199.573 206.500  1.00 31.18           C  
ATOM  18829  CG  GLN C 762     203.862 200.662 207.381  1.00 31.29           C  
ATOM  18830  CD  GLN C 762     202.887 201.811 207.449  1.00 31.66           C  
ATOM  18831  OE1 GLN C 762     202.569 202.420 206.426  1.00 31.80           O  
ATOM  18832  NE2 GLN C 762     202.392 202.107 208.642  1.00 32.07           N  
ATOM  18833  N   LEU C 763     206.603 198.744 206.868  1.00 30.99           N  
ATOM  18834  CA  LEU C 763     207.985 198.968 206.464  1.00 30.25           C  
ATOM  18835  C   LEU C 763     208.514 197.742 205.735  1.00 30.15           C  
ATOM  18836  O   LEU C 763     209.177 197.859 204.701  1.00 30.62           O  
ATOM  18837  CB  LEU C 763     208.852 199.267 207.686  1.00 31.47           C  
ATOM  18838  CG  LEU C 763     208.589 200.607 208.380  1.00 31.63           C  
ATOM  18839  CD1 LEU C 763     209.283 200.609 209.723  1.00 32.28           C  
ATOM  18840  CD2 LEU C 763     209.113 201.747 207.526  1.00 32.01           C  
ATOM  18841  N   ASN C 764     208.163 196.555 206.232  1.00 30.73           N  
ATOM  18842  CA  ASN C 764     208.585 195.329 205.565  1.00 30.29           C  
ATOM  18843  C   ASN C 764     207.978 195.269 204.169  1.00 29.51           C  
ATOM  18844  O   ASN C 764     208.627 194.832 203.212  1.00 29.70           O  
ATOM  18845  CB  ASN C 764     208.149 194.096 206.337  1.00 31.22           C  
ATOM  18846  CG  ASN C 764     208.908 193.821 207.619  1.00 32.22           C  
ATOM  18847  OD1 ASN C 764     210.024 194.301 207.873  1.00 32.61           O  
ATOM  18848  ND2 ASN C 764     208.287 193.022 208.449  1.00 32.61           N  
ATOM  18849  N   ARG C 765     206.731 195.722 204.055  1.00 29.67           N  
ATOM  18850  CA  ARG C 765     206.023 195.727 202.785  1.00 28.91           C  
ATOM  18851  C   ARG C 765     206.650 196.684 201.787  1.00 28.44           C  
ATOM  18852  O   ARG C 765     206.787 196.350 200.609  1.00 28.65           O  
ATOM  18853  CB  ARG C 765     204.566 196.095 202.990  1.00 29.54           C  
ATOM  18854  CG  ARG C 765     203.711 196.085 201.737  1.00 29.37           C  
ATOM  18855  CD  ARG C 765     202.274 196.274 202.060  1.00 29.24           C  
ATOM  18856  NE  ARG C 765     202.015 197.578 202.662  1.00 29.95           N  
ATOM  18857  CZ  ARG C 765     200.912 197.891 203.379  1.00 30.20           C  
ATOM  18858  NH1 ARG C 765     199.974 196.988 203.572  1.00 29.43           N  
ATOM  18859  NH2 ARG C 765     200.771 199.105 203.892  1.00 30.56           N  
ATOM  18860  N   ALA C 766     207.026 197.873 202.244  1.00 28.90           N  
ATOM  18861  CA  ALA C 766     207.620 198.859 201.357  1.00 28.39           C  
ATOM  18862  C   ALA C 766     208.922 198.353 200.757  1.00 27.83           C  
ATOM  18863  O   ALA C 766     209.157 198.511 199.557  1.00 27.86           O  
ATOM  18864  CB  ALA C 766     207.873 200.147 202.113  1.00 28.48           C  
ATOM  18865  N   LEU C 767     209.752 197.703 201.568  1.00 28.39           N  
ATOM  18866  CA  LEU C 767     211.011 197.182 201.056  1.00 27.59           C  
ATOM  18867  C   LEU C 767     210.785 196.013 200.119  1.00 27.24           C  
ATOM  18868  O   LEU C 767     211.507 195.857 199.131  1.00 27.48           O  
ATOM  18869  CB  LEU C 767     211.933 196.773 202.202  1.00 28.58           C  
ATOM  18870  CG  LEU C 767     212.499 197.918 203.061  1.00 28.91           C  
ATOM  18871  CD1 LEU C 767     213.218 197.324 204.257  1.00 30.60           C  
ATOM  18872  CD2 LEU C 767     213.470 198.768 202.233  1.00 29.17           C  
ATOM  18873  N   THR C 768     209.780 195.195 200.406  1.00 27.60           N  
ATOM  18874  CA  THR C 768     209.468 194.079 199.530  1.00 26.97           C  
ATOM  18875  C   THR C 768     209.055 194.599 198.167  1.00 26.30           C  
ATOM  18876  O   THR C 768     209.477 194.065 197.138  1.00 26.61           O  
ATOM  18877  CB  THR C 768     208.351 193.197 200.105  1.00 27.73           C  
ATOM  18878  OG1 THR C 768     208.778 192.638 201.351  1.00 28.30           O  
ATOM  18879  CG2 THR C 768     208.021 192.075 199.132  1.00 26.77           C  
ATOM  18880  N   GLY C 769     208.229 195.642 198.154  1.00 26.65           N  
ATOM  18881  CA  GLY C 769     207.766 196.220 196.906  1.00 25.95           C  
ATOM  18882  C   GLY C 769     208.936 196.693 196.060  1.00 25.45           C  
ATOM  18883  O   GLY C 769     208.963 196.457 194.850  1.00 25.58           O  
ATOM  18884  N   ILE C 770     209.931 197.307 196.696  1.00 25.83           N  
ATOM  18885  CA  ILE C 770     211.097 197.757 195.956  1.00 24.78           C  
ATOM  18886  C   ILE C 770     211.864 196.586 195.390  1.00 25.34           C  
ATOM  18887  O   ILE C 770     212.258 196.615 194.228  1.00 25.70           O  
ATOM  18888  CB  ILE C 770     212.052 198.594 196.826  1.00 25.23           C  
ATOM  18889  CG1 ILE C 770     211.372 199.886 197.294  1.00 26.00           C  
ATOM  18890  CG2 ILE C 770     213.349 198.898 196.065  1.00 25.14           C  
ATOM  18891  CD1 ILE C 770     210.862 200.798 196.192  1.00 26.89           C  
ATOM  18892  N   ALA C 771     212.061 195.539 196.174  1.00 25.22           N  
ATOM  18893  CA  ALA C 771     212.811 194.406 195.661  1.00 25.44           C  
ATOM  18894  C   ALA C 771     212.169 193.866 194.383  1.00 25.41           C  
ATOM  18895  O   ALA C 771     212.866 193.563 193.410  1.00 26.41           O  
ATOM  18896  CB  ALA C 771     212.888 193.319 196.715  1.00 26.61           C  
ATOM  18897  N   VAL C 772     210.841 193.815 194.349  1.00 24.71           N  
ATOM  18898  CA  VAL C 772     210.149 193.342 193.158  1.00 24.35           C  
ATOM  18899  C   VAL C 772     210.401 194.281 191.992  1.00 24.69           C  
ATOM  18900  O   VAL C 772     210.679 193.840 190.873  1.00 25.54           O  
ATOM  18901  CB  VAL C 772     208.641 193.232 193.412  1.00 24.66           C  
ATOM  18902  CG1 VAL C 772     207.907 192.926 192.111  1.00 24.42           C  
ATOM  18903  CG2 VAL C 772     208.392 192.143 194.433  1.00 25.32           C  
ATOM  18904  N   GLU C 773     210.316 195.574 192.262  1.00 24.65           N  
ATOM  18905  CA  GLU C 773     210.563 196.596 191.264  1.00 23.77           C  
ATOM  18906  C   GLU C 773     211.945 196.471 190.643  1.00 26.61           C  
ATOM  18907  O   GLU C 773     212.112 196.732 189.452  1.00 24.92           O  
ATOM  18908  CB  GLU C 773     210.392 197.977 191.880  1.00 24.43           C  
ATOM  18909  CG  GLU C 773     210.617 199.123 190.943  1.00 24.38           C  
ATOM  18910  CD  GLU C 773     210.281 200.432 191.575  1.00 24.61           C  
ATOM  18911  OE1 GLU C 773     209.425 200.461 192.419  1.00 24.27           O  
ATOM  18912  OE2 GLU C 773     210.884 201.409 191.228  1.00 24.67           O  
ATOM  18913  N   GLN C 774     212.944 196.092 191.432  1.00 24.72           N  
ATOM  18914  CA  GLN C 774     214.292 196.010 190.896  1.00 24.56           C  
ATOM  18915  C   GLN C 774     214.417 194.894 189.864  1.00 25.66           C  
ATOM  18916  O   GLN C 774     215.151 195.039 188.881  1.00 26.08           O  
ATOM  18917  CB  GLN C 774     215.309 195.833 192.015  1.00 25.41           C  
ATOM  18918  CG  GLN C 774     215.303 196.984 192.989  1.00 25.36           C  
ATOM  18919  CD  GLN C 774     215.341 198.315 192.301  1.00 25.25           C  
ATOM  18920  OE1 GLN C 774     216.288 198.642 191.595  1.00 26.01           O  
ATOM  18921  NE2 GLN C 774     214.295 199.099 192.482  1.00 25.38           N  
ATOM  18922  N   ASP C 775     213.668 193.807 190.036  1.00 25.31           N  
ATOM  18923  CA  ASP C 775     213.696 192.766 189.014  1.00 25.27           C  
ATOM  18924  C   ASP C 775     212.945 193.234 187.790  1.00 25.13           C  
ATOM  18925  O   ASP C 775     213.328 192.925 186.662  1.00 25.89           O  
ATOM  18926  CB  ASP C 775     213.092 191.456 189.499  1.00 26.60           C  
ATOM  18927  CG  ASP C 775     213.997 190.679 190.416  1.00 27.72           C  
ATOM  18928  OD1 ASP C 775     215.167 190.551 190.117  1.00 28.37           O  
ATOM  18929  OD2 ASP C 775     213.524 190.186 191.405  1.00 28.21           O  
ATOM  18930  N   LYS C 776     211.881 193.997 188.003  1.00 25.00           N  
ATOM  18931  CA  LYS C 776     211.131 194.533 186.883  1.00 24.54           C  
ATOM  18932  C   LYS C 776     212.020 195.421 186.023  1.00 24.55           C  
ATOM  18933  O   LYS C 776     211.986 195.323 184.796  1.00 25.28           O  
ATOM  18934  CB  LYS C 776     209.919 195.319 187.357  1.00 24.70           C  
ATOM  18935  CG  LYS C 776     209.092 195.896 186.240  1.00 24.78           C  
ATOM  18936  CD  LYS C 776     207.902 196.661 186.776  1.00 25.17           C  
ATOM  18937  CE  LYS C 776     207.243 197.456 185.675  1.00 25.26           C  
ATOM  18938  NZ  LYS C 776     206.553 196.584 184.698  1.00 25.50           N  
ATOM  18939  N   ASN C 777     212.830 196.270 186.661  1.00 24.68           N  
ATOM  18940  CA  ASN C 777     213.708 197.164 185.917  1.00 24.32           C  
ATOM  18941  C   ASN C 777     214.655 196.378 185.038  1.00 24.68           C  
ATOM  18942  O   ASN C 777     214.840 196.694 183.863  1.00 24.86           O  
ATOM  18943  CB  ASN C 777     214.557 198.010 186.840  1.00 24.78           C  
ATOM  18944  CG  ASN C 777     213.851 199.076 187.576  1.00 24.56           C  
ATOM  18945  OD1 ASN C 777     212.677 199.395 187.357  1.00 24.55           O  
ATOM  18946  ND2 ASN C 777     214.590 199.670 188.468  1.00 24.78           N  
ATOM  18947  N   THR C 778     215.242 195.334 185.599  1.00 24.49           N  
ATOM  18948  CA  THR C 778     216.190 194.533 184.853  1.00 24.20           C  
ATOM  18949  C   THR C 778     215.520 193.873 183.668  1.00 24.25           C  
ATOM  18950  O   THR C 778     216.081 193.819 182.571  1.00 24.81           O  
ATOM  18951  CB  THR C 778     216.828 193.467 185.748  1.00 25.28           C  
ATOM  18952  OG1 THR C 778     217.535 194.099 186.817  1.00 26.05           O  
ATOM  18953  CG2 THR C 778     217.788 192.638 184.950  1.00 26.33           C  
ATOM  18954  N   GLN C 779     214.324 193.354 183.885  1.00 24.22           N  
ATOM  18955  CA  GLN C 779     213.621 192.655 182.833  1.00 23.45           C  
ATOM  18956  C   GLN C 779     213.277 193.583 181.678  1.00 23.67           C  
ATOM  18957  O   GLN C 779     213.481 193.230 180.519  1.00 24.43           O  
ATOM  18958  CB  GLN C 779     212.338 192.048 183.395  1.00 24.14           C  
ATOM  18959  CG  GLN C 779     211.589 191.129 182.460  1.00 23.97           C  
ATOM  18960  CD  GLN C 779     212.352 189.868 182.189  1.00 24.60           C  
ATOM  18961  OE1 GLN C 779     213.284 189.535 182.917  1.00 24.70           O  
ATOM  18962  NE2 GLN C 779     211.966 189.149 181.153  1.00 23.93           N  
ATOM  18963  N   GLU C 780     212.801 194.788 181.978  1.00 23.84           N  
ATOM  18964  CA  GLU C 780     212.435 195.722 180.918  1.00 23.54           C  
ATOM  18965  C   GLU C 780     213.632 196.236 180.131  1.00 23.42           C  
ATOM  18966  O   GLU C 780     213.516 196.493 178.929  1.00 23.41           O  
ATOM  18967  CB  GLU C 780     211.628 196.893 181.469  1.00 23.72           C  
ATOM  18968  CG  GLU C 780     210.217 196.515 181.896  1.00 24.14           C  
ATOM  18969  CD  GLU C 780     209.400 197.685 182.358  1.00 25.06           C  
ATOM  18970  OE1 GLU C 780     209.971 198.701 182.660  1.00 24.65           O  
ATOM  18971  OE2 GLU C 780     208.191 197.567 182.392  1.00 24.86           O  
ATOM  18972  N   VAL C 781     214.770 196.397 180.796  1.00 23.66           N  
ATOM  18973  CA  VAL C 781     215.953 196.876 180.105  1.00 22.91           C  
ATOM  18974  C   VAL C 781     216.587 195.818 179.229  1.00 23.02           C  
ATOM  18975  O   VAL C 781     216.993 196.124 178.119  1.00 23.41           O  
ATOM  18976  CB  VAL C 781     217.011 197.412 181.082  1.00 23.41           C  
ATOM  18977  CG1 VAL C 781     218.307 197.756 180.326  1.00 23.60           C  
ATOM  18978  CG2 VAL C 781     216.480 198.646 181.755  1.00 23.41           C  
ATOM  18979  N   PHE C 782     216.737 194.592 179.720  1.00 23.53           N  
ATOM  18980  CA  PHE C 782     217.470 193.603 178.936  1.00 23.25           C  
ATOM  18981  C   PHE C 782     216.630 192.624 178.127  1.00 23.11           C  
ATOM  18982  O   PHE C 782     217.033 192.223 177.036  1.00 23.73           O  
ATOM  18983  CB  PHE C 782     218.395 192.813 179.847  1.00 23.92           C  
ATOM  18984  CG  PHE C 782     219.496 193.629 180.401  1.00 24.17           C  
ATOM  18985  CD1 PHE C 782     219.415 194.144 181.669  1.00 24.81           C  
ATOM  18986  CD2 PHE C 782     220.617 193.887 179.655  1.00 24.38           C  
ATOM  18987  CE1 PHE C 782     220.436 194.896 182.188  1.00 25.13           C  
ATOM  18988  CE2 PHE C 782     221.641 194.639 180.169  1.00 24.74           C  
ATOM  18989  CZ  PHE C 782     221.548 195.140 181.439  1.00 25.22           C  
ATOM  18990  N   ALA C 783     215.478 192.204 178.630  1.00 23.40           N  
ATOM  18991  CA  ALA C 783     214.726 191.165 177.938  1.00 23.23           C  
ATOM  18992  C   ALA C 783     213.823 191.757 176.874  1.00 22.83           C  
ATOM  18993  O   ALA C 783     212.599 191.672 176.959  1.00 22.80           O  
ATOM  18994  CB  ALA C 783     213.909 190.364 178.925  1.00 23.88           C  
ATOM  18995  N   GLN C 784     214.436 192.358 175.864  1.00 22.64           N  
ATOM  18996  CA  GLN C 784     213.685 193.015 174.805  1.00 22.39           C  
ATOM  18997  C   GLN C 784     213.582 192.167 173.557  1.00 22.52           C  
ATOM  18998  O   GLN C 784     212.971 192.573 172.568  1.00 22.16           O  
ATOM  18999  CB  GLN C 784     214.306 194.358 174.463  1.00 22.13           C  
ATOM  19000  CG  GLN C 784     214.277 195.312 175.606  1.00 22.52           C  
ATOM  19001  CD  GLN C 784     214.647 196.690 175.214  1.00 21.87           C  
ATOM  19002  OE1 GLN C 784     215.102 196.947 174.092  1.00 21.46           O  
ATOM  19003  NE2 GLN C 784     214.440 197.608 176.141  1.00 22.11           N  
ATOM  19004  N   VAL C 785     214.195 191.001 173.595  1.00 22.80           N  
ATOM  19005  CA  VAL C 785     214.202 190.116 172.452  1.00 23.01           C  
ATOM  19006  C   VAL C 785     213.531 188.805 172.830  1.00 23.39           C  
ATOM  19007  O   VAL C 785     213.823 188.231 173.876  1.00 23.58           O  
ATOM  19008  CB  VAL C 785     215.651 189.910 171.970  1.00 23.00           C  
ATOM  19009  CG1 VAL C 785     216.505 189.246 173.048  1.00 23.18           C  
ATOM  19010  CG2 VAL C 785     215.657 189.113 170.715  1.00 23.12           C  
ATOM  19011  N   LYS C 786     212.618 188.341 171.983  1.00 23.64           N  
ATOM  19012  CA  LYS C 786     211.873 187.116 172.253  1.00 23.85           C  
ATOM  19013  C   LYS C 786     212.729 185.862 172.175  1.00 24.08           C  
ATOM  19014  O   LYS C 786     212.495 184.898 172.901  1.00 24.46           O  
ATOM  19015  CB  LYS C 786     210.704 186.986 171.284  1.00 24.15           C  
ATOM  19016  N   GLN C 787     213.690 185.861 171.268  1.00 23.94           N  
ATOM  19017  CA  GLN C 787     214.541 184.704 171.053  1.00 23.61           C  
ATOM  19018  C   GLN C 787     215.980 185.017 171.385  1.00 23.73           C  
ATOM  19019  O   GLN C 787     216.412 186.164 171.324  1.00 24.81           O  
ATOM  19020  CB  GLN C 787     214.436 184.229 169.612  1.00 23.84           C  
ATOM  19021  CG  GLN C 787     213.062 183.757 169.229  1.00 23.76           C  
ATOM  19022  CD  GLN C 787     213.008 183.285 167.809  1.00 23.79           C  
ATOM  19023  OE1 GLN C 787     213.747 183.787 166.958  1.00 23.90           O  
ATOM  19024  NE2 GLN C 787     212.135 182.324 167.531  1.00 23.12           N  
ATOM  19025  N   ILE C 788     216.736 183.992 171.711  1.00 24.12           N  
ATOM  19026  CA  ILE C 788     218.140 184.191 171.981  1.00 24.12           C  
ATOM  19027  C   ILE C 788     218.935 183.874 170.738  1.00 23.94           C  
ATOM  19028  O   ILE C 788     219.115 182.711 170.385  1.00 24.72           O  
ATOM  19029  CB  ILE C 788     218.590 183.308 173.159  1.00 25.08           C  
ATOM  19030  CG1 ILE C 788     217.698 183.588 174.404  1.00 25.72           C  
ATOM  19031  CG2 ILE C 788     220.068 183.506 173.470  1.00 25.68           C  
ATOM  19032  CD1 ILE C 788     217.694 185.044 174.896  1.00 25.77           C  
ATOM  19033  N   TYR C 789     219.416 184.914 170.080  1.00 24.17           N  
ATOM  19034  CA  TYR C 789     220.126 184.757 168.829  1.00 23.42           C  
ATOM  19035  C   TYR C 789     221.595 184.575 169.093  1.00 23.67           C  
ATOM  19036  O   TYR C 789     222.157 185.218 169.974  1.00 24.37           O  
ATOM  19037  CB  TYR C 789     219.946 185.984 167.939  1.00 23.25           C  
ATOM  19038  CG  TYR C 789     218.543 186.238 167.511  1.00 22.91           C  
ATOM  19039  CD1 TYR C 789     217.854 187.287 168.068  1.00 22.82           C  
ATOM  19040  CD2 TYR C 789     217.938 185.433 166.577  1.00 23.25           C  
ATOM  19041  CE1 TYR C 789     216.567 187.536 167.692  1.00 22.80           C  
ATOM  19042  CE2 TYR C 789     216.639 185.683 166.205  1.00 22.98           C  
ATOM  19043  CZ  TYR C 789     215.958 186.737 166.766  1.00 23.00           C  
ATOM  19044  OH  TYR C 789     214.659 187.001 166.403  1.00 23.20           O  
ATOM  19045  N   LYS C 790     222.224 183.741 168.301  1.00 23.72           N  
ATOM  19046  CA  LYS C 790     223.660 183.571 168.386  1.00 24.43           C  
ATOM  19047  C   LYS C 790     224.296 183.764 167.027  1.00 24.41           C  
ATOM  19048  O   LYS C 790     223.685 183.469 166.000  1.00 24.19           O  
ATOM  19049  CB  LYS C 790     223.973 182.201 168.980  1.00 24.84           C  
ATOM  19050  CG  LYS C 790     223.392 181.034 168.205  1.00 24.49           C  
ATOM  19051  CD  LYS C 790     223.566 179.734 168.967  1.00 24.87           C  
ATOM  19052  CE  LYS C 790     222.868 178.581 168.266  1.00 24.93           C  
ATOM  19053  NZ  LYS C 790     222.952 177.318 169.058  1.00 25.07           N  
ATOM  19054  N   THR C 791     225.520 184.269 167.018  1.00 24.70           N  
ATOM  19055  CA  THR C 791     226.240 184.452 165.775  1.00 24.47           C  
ATOM  19056  C   THR C 791     226.800 183.118 165.308  1.00 24.70           C  
ATOM  19057  O   THR C 791     226.986 182.215 166.123  1.00 24.58           O  
ATOM  19058  CB  THR C 791     227.389 185.458 165.974  1.00 24.55           C  
ATOM  19059  OG1 THR C 791     228.255 184.969 167.000  1.00 24.74           O  
ATOM  19060  CG2 THR C 791     226.846 186.824 166.353  1.00 24.47           C  
ATOM  19061  N   PRO C 792     227.088 182.975 164.013  1.00 24.48           N  
ATOM  19062  CA  PRO C 792     227.769 181.859 163.397  1.00 24.49           C  
ATOM  19063  C   PRO C 792     229.258 181.907 163.728  1.00 24.72           C  
ATOM  19064  O   PRO C 792     229.745 182.929 164.221  1.00 24.52           O  
ATOM  19065  CB  PRO C 792     227.485 182.094 161.912  1.00 24.37           C  
ATOM  19066  CG  PRO C 792     227.347 183.571 161.788  1.00 23.99           C  
ATOM  19067  CD  PRO C 792     226.640 183.998 163.051  1.00 24.30           C  
ATOM  19068  N   PRO C 793     229.991 180.819 163.472  1.00 24.09           N  
ATOM  19069  CA  PRO C 793     231.433 180.688 163.594  1.00 24.49           C  
ATOM  19070  C   PRO C 793     232.201 181.623 162.662  1.00 24.46           C  
ATOM  19071  O   PRO C 793     233.371 181.915 162.908  1.00 24.43           O  
ATOM  19072  CB  PRO C 793     231.664 179.214 163.235  1.00 25.01           C  
ATOM  19073  CG  PRO C 793     230.446 178.806 162.437  1.00 24.79           C  
ATOM  19074  CD  PRO C 793     229.315 179.582 163.044  1.00 24.56           C  
ATOM  19075  N   ILE C 794     231.546 182.100 161.610  1.00 24.56           N  
ATOM  19076  CA  ILE C 794     232.185 183.005 160.664  1.00 24.66           C  
ATOM  19077  C   ILE C 794     232.018 184.443 161.131  1.00 24.42           C  
ATOM  19078  O   ILE C 794     230.946 184.842 161.578  1.00 24.58           O  
ATOM  19079  CB  ILE C 794     231.633 182.808 159.235  1.00 24.32           C  
ATOM  19080  CG1 ILE C 794     230.098 183.064 159.191  1.00 24.29           C  
ATOM  19081  CG2 ILE C 794     231.961 181.392 158.775  1.00 24.32           C  
ATOM  19082  CD1 ILE C 794     229.502 183.137 157.800  1.00 24.16           C  
ATOM  19083  N   LYS C 795     233.094 185.211 161.047  1.00 24.18           N  
ATOM  19084  CA  LYS C 795     233.091 186.585 161.521  1.00 24.32           C  
ATOM  19085  C   LYS C 795     233.313 187.576 160.390  1.00 24.79           C  
ATOM  19086  O   LYS C 795     233.843 188.670 160.597  1.00 24.38           O  
ATOM  19087  CB  LYS C 795     234.147 186.760 162.609  1.00 24.75           C  
ATOM  19088  CG  LYS C 795     233.979 185.803 163.803  1.00 24.81           C  
ATOM  19089  CD  LYS C 795     232.683 186.052 164.582  1.00 24.49           C  
ATOM  19090  CE  LYS C 795     232.577 185.132 165.787  1.00 24.66           C  
ATOM  19091  NZ  LYS C 795     232.285 183.716 165.392  1.00 24.40           N  
ATOM  19092  N   ASP C 796     232.904 187.198 159.187  1.00 24.17           N  
ATOM  19093  CA  ASP C 796     233.092 188.034 158.017  1.00 24.21           C  
ATOM  19094  C   ASP C 796     232.041 189.128 157.945  1.00 24.04           C  
ATOM  19095  O   ASP C 796     231.171 189.142 157.074  1.00 23.52           O  
ATOM  19096  CB  ASP C 796     233.074 187.169 156.758  1.00 24.18           C  
ATOM  19097  CG  ASP C 796     231.831 186.306 156.664  1.00 24.35           C  
ATOM  19098  OD1 ASP C 796     231.263 186.023 157.696  1.00 24.00           O  
ATOM  19099  OD2 ASP C 796     231.482 185.902 155.579  1.00 24.06           O  
ATOM  19100  N   PHE C 797     232.171 190.083 158.853  1.00 23.75           N  
ATOM  19101  CA  PHE C 797     231.233 191.183 158.967  1.00 23.21           C  
ATOM  19102  C   PHE C 797     231.735 192.409 158.233  1.00 23.39           C  
ATOM  19103  O   PHE C 797     231.720 193.514 158.760  1.00 23.80           O  
ATOM  19104  CB  PHE C 797     230.977 191.526 160.426  1.00 23.07           C  
ATOM  19105  CG  PHE C 797     230.390 190.406 161.193  1.00 22.92           C  
ATOM  19106  CD1 PHE C 797     231.074 189.840 162.238  1.00 23.93           C  
ATOM  19107  CD2 PHE C 797     229.163 189.899 160.860  1.00 23.06           C  
ATOM  19108  CE1 PHE C 797     230.533 188.796 162.943  1.00 24.07           C  
ATOM  19109  CE2 PHE C 797     228.625 188.849 161.553  1.00 23.21           C  
ATOM  19110  CZ  PHE C 797     229.309 188.297 162.599  1.00 23.55           C  
ATOM  19111  N   GLY C 798     232.222 192.207 157.024  1.00 23.31           N  
ATOM  19112  CA  GLY C 798     232.615 193.317 156.166  1.00 23.12           C  
ATOM  19113  C   GLY C 798     233.934 193.949 156.574  1.00 23.48           C  
ATOM  19114  O   GLY C 798     234.291 195.016 156.077  1.00 23.56           O  
ATOM  19115  N   GLY C 799     234.659 193.296 157.470  1.00 23.60           N  
ATOM  19116  CA  GLY C 799     235.913 193.841 157.972  1.00 23.77           C  
ATOM  19117  C   GLY C 799     235.748 194.477 159.348  1.00 24.02           C  
ATOM  19118  O   GLY C 799     236.733 194.902 159.959  1.00 24.21           O  
ATOM  19119  N   PHE C 800     234.516 194.525 159.844  1.00 23.92           N  
ATOM  19120  CA  PHE C 800     234.255 195.080 161.162  1.00 23.32           C  
ATOM  19121  C   PHE C 800     234.533 194.007 162.212  1.00 24.27           C  
ATOM  19122  O   PHE C 800     233.988 192.904 162.133  1.00 24.84           O  
ATOM  19123  CB  PHE C 800     232.811 195.549 161.257  1.00 23.31           C  
ATOM  19124  CG  PHE C 800     232.522 196.765 160.443  1.00 23.13           C  
ATOM  19125  CD1 PHE C 800     232.327 196.674 159.080  1.00 23.41           C  
ATOM  19126  CD2 PHE C 800     232.416 197.998 161.036  1.00 23.24           C  
ATOM  19127  CE1 PHE C 800     232.044 197.782 158.335  1.00 22.96           C  
ATOM  19128  CE2 PHE C 800     232.132 199.112 160.293  1.00 23.01           C  
ATOM  19129  CZ  PHE C 800     231.945 198.998 158.936  1.00 22.63           C  
ATOM  19130  N   ASN C 801     235.409 194.323 163.168  1.00 25.39           N  
ATOM  19131  CA  ASN C 801     235.862 193.422 164.224  1.00 25.82           C  
ATOM  19132  C   ASN C 801     235.041 193.604 165.501  1.00 25.81           C  
ATOM  19133  O   ASN C 801     235.219 194.583 166.233  1.00 25.85           O  
ATOM  19134  CB  ASN C 801     237.352 193.628 164.484  1.00 26.97           C  
ATOM  19135  CG  ASN C 801     237.985 192.574 165.393  1.00 28.23           C  
ATOM  19136  OD1 ASN C 801     237.283 191.800 166.078  1.00 28.68           O  
ATOM  19137  ND2 ASN C 801     239.314 192.545 165.402  1.00 29.44           N  
ATOM  19138  N   PHE C 802     234.142 192.650 165.781  1.00 26.22           N  
ATOM  19139  CA  PHE C 802     233.253 192.685 166.942  1.00 26.21           C  
ATOM  19140  C   PHE C 802     233.682 191.681 167.997  1.00 27.62           C  
ATOM  19141  O   PHE C 802     232.956 191.446 168.961  1.00 28.30           O  
ATOM  19142  CB  PHE C 802     231.821 192.371 166.530  1.00 25.69           C  
ATOM  19143  CG  PHE C 802     231.261 193.319 165.559  1.00 24.69           C  
ATOM  19144  CD1 PHE C 802     230.929 192.908 164.301  1.00 24.41           C  
ATOM  19145  CD2 PHE C 802     231.072 194.625 165.889  1.00 24.66           C  
ATOM  19146  CE1 PHE C 802     230.413 193.788 163.405  1.00 24.00           C  
ATOM  19147  CE2 PHE C 802     230.558 195.498 164.993  1.00 23.91           C  
ATOM  19148  CZ  PHE C 802     230.232 195.082 163.759  1.00 23.45           C  
ATOM  19149  N   SER C 803     234.862 191.092 167.837  1.00 27.60           N  
ATOM  19150  CA  SER C 803     235.277 190.023 168.746  1.00 27.93           C  
ATOM  19151  C   SER C 803     235.485 190.490 170.176  1.00 28.41           C  
ATOM  19152  O   SER C 803     235.529 189.676 171.096  1.00 28.74           O  
ATOM  19153  CB  SER C 803     236.554 189.372 168.270  1.00 28.77           C  
ATOM  19154  OG  SER C 803     237.634 190.244 168.394  1.00 29.11           O  
ATOM  19155  N   GLN C 804     235.615 191.793 170.375  1.00 28.26           N  
ATOM  19156  CA  GLN C 804     235.848 192.326 171.704  1.00 28.15           C  
ATOM  19157  C   GLN C 804     234.556 192.691 172.423  1.00 28.27           C  
ATOM  19158  O   GLN C 804     234.573 193.026 173.611  1.00 28.88           O  
ATOM  19159  CB  GLN C 804     236.763 193.527 171.599  1.00 28.74           C  
ATOM  19160  CG  GLN C 804     238.099 193.187 170.951  1.00 29.12           C  
ATOM  19161  CD  GLN C 804     238.847 192.080 171.689  1.00 29.74           C  
ATOM  19162  OE1 GLN C 804     239.224 192.238 172.849  1.00 29.61           O  
ATOM  19163  NE2 GLN C 804     239.052 190.949 171.027  1.00 30.65           N  
ATOM  19164  N   ILE C 805     233.432 192.626 171.707  1.00 28.04           N  
ATOM  19165  CA  ILE C 805     232.137 192.905 172.317  1.00 27.54           C  
ATOM  19166  C   ILE C 805     231.255 191.655 172.322  1.00 27.97           C  
ATOM  19167  O   ILE C 805     230.297 191.573 173.094  1.00 28.72           O  
ATOM  19168  CB  ILE C 805     231.432 194.101 171.653  1.00 27.50           C  
ATOM  19169  CG1 ILE C 805     231.164 193.843 170.180  1.00 27.09           C  
ATOM  19170  CG2 ILE C 805     232.275 195.332 171.851  1.00 27.59           C  
ATOM  19171  CD1 ILE C 805     230.232 194.852 169.559  1.00 25.30           C  
ATOM  19172  N   LEU C 806     231.610 190.670 171.493  1.00 28.09           N  
ATOM  19173  CA  LEU C 806     230.941 189.376 171.470  1.00 28.36           C  
ATOM  19174  C   LEU C 806     231.442 188.527 172.638  1.00 29.55           C  
ATOM  19175  O   LEU C 806     232.584 188.697 173.064  1.00 30.48           O  
ATOM  19176  CB  LEU C 806     231.215 188.664 170.139  1.00 28.48           C  
ATOM  19177  CG  LEU C 806     230.597 189.301 168.884  1.00 27.67           C  
ATOM  19178  CD1 LEU C 806     231.209 188.682 167.642  1.00 26.90           C  
ATOM  19179  CD2 LEU C 806     229.101 189.048 168.880  1.00 26.60           C  
ATOM  19180  N   PRO C 807     230.632 187.616 173.187  1.00 30.08           N  
ATOM  19181  CA  PRO C 807     230.989 186.716 174.265  1.00 31.17           C  
ATOM  19182  C   PRO C 807     232.197 185.868 173.940  1.00 31.91           C  
ATOM  19183  O   PRO C 807     232.317 185.371 172.819  1.00 32.33           O  
ATOM  19184  CB  PRO C 807     229.752 185.834 174.387  1.00 30.92           C  
ATOM  19185  CG  PRO C 807     228.637 186.664 173.854  1.00 29.70           C  
ATOM  19186  CD  PRO C 807     229.243 187.481 172.737  1.00 29.28           C  
ATOM  19187  N   ASP C 808     233.059 185.659 174.930  1.00 32.71           N  
ATOM  19188  CA  ASP C 808     234.217 184.795 174.795  1.00 33.60           C  
ATOM  19189  C   ASP C 808     233.840 183.371 175.219  1.00 34.84           C  
ATOM  19190  O   ASP C 808     233.627 183.126 176.407  1.00 34.84           O  
ATOM  19191  CB  ASP C 808     235.372 185.312 175.652  1.00 34.85           C  
ATOM  19192  CG  ASP C 808     236.629 184.468 175.529  1.00 35.27           C  
ATOM  19193  OD1 ASP C 808     236.546 183.370 175.004  1.00 35.24           O  
ATOM  19194  OD2 ASP C 808     237.670 184.908 175.976  1.00 35.98           O  
ATOM  19195  N   PRO C 809     233.736 182.418 174.284  1.00 35.44           N  
ATOM  19196  CA  PRO C 809     233.232 181.075 174.490  1.00 35.38           C  
ATOM  19197  C   PRO C 809     234.164 180.212 175.331  1.00 36.13           C  
ATOM  19198  O   PRO C 809     233.781 179.124 175.762  1.00 35.80           O  
ATOM  19199  CB  PRO C 809     233.127 180.539 173.056  1.00 35.93           C  
ATOM  19200  CG  PRO C 809     234.176 181.304 172.282  1.00 35.60           C  
ATOM  19201  CD  PRO C 809     234.202 182.680 172.908  1.00 35.43           C  
ATOM  19202  N   SER C 810     235.402 180.666 175.518  1.00 35.32           N  
ATOM  19203  CA  SER C 810     236.386 179.870 176.236  1.00 35.93           C  
ATOM  19204  C   SER C 810     236.354 180.101 177.740  1.00 36.31           C  
ATOM  19205  O   SER C 810     237.033 179.399 178.492  1.00 35.81           O  
ATOM  19206  CB  SER C 810     237.783 180.159 175.721  1.00 35.62           C  
ATOM  19207  OG  SER C 810     238.201 181.438 176.093  1.00 35.81           O  
ATOM  19208  N   LYS C 811     235.603 181.100 178.188  1.00 35.05           N  
ATOM  19209  CA  LYS C 811     235.607 181.429 179.605  1.00 35.90           C  
ATOM  19210  C   LYS C 811     234.410 180.800 180.320  1.00 36.07           C  
ATOM  19211  O   LYS C 811     233.358 180.624 179.709  1.00 35.71           O  
ATOM  19212  CB  LYS C 811     235.606 182.944 179.783  1.00 35.71           C  
ATOM  19213  N   SER C 813     232.438 182.144 182.351  1.00 35.15           N  
ATOM  19214  CA  SER C 813     231.345 183.090 182.243  1.00 34.37           C  
ATOM  19215  C   SER C 813     231.349 183.618 180.824  1.00 34.61           C  
ATOM  19216  O   SER C 813     232.344 184.187 180.374  1.00 34.14           O  
ATOM  19217  CB  SER C 813     231.505 184.206 183.253  1.00 33.36           C  
ATOM  19218  OG  SER C 813     230.502 185.161 183.104  1.00 32.72           O  
ATOM  19219  N   LYS C 814     230.251 183.414 180.113  1.00 33.84           N  
ATOM  19220  CA  LYS C 814     230.207 183.719 178.689  1.00 33.19           C  
ATOM  19221  C   LYS C 814     230.032 185.204 178.430  1.00 32.37           C  
ATOM  19222  O   LYS C 814     228.973 185.652 177.995  1.00 31.49           O  
ATOM  19223  CB  LYS C 814     229.051 182.959 178.032  1.00 33.62           C  
ATOM  19224  N   ARG C 815     231.085 185.964 178.689  1.00 32.05           N  
ATOM  19225  CA  ARG C 815     231.051 187.410 178.547  1.00 31.45           C  
ATOM  19226  C   ARG C 815     232.162 187.885 177.634  1.00 31.66           C  
ATOM  19227  O   ARG C 815     233.137 187.174 177.403  1.00 32.17           O  
ATOM  19228  CB  ARG C 815     231.156 188.079 179.900  1.00 30.95           C  
ATOM  19229  CG  ARG C 815     230.008 187.764 180.804  1.00 31.33           C  
ATOM  19230  CD  ARG C 815     229.965 188.615 182.015  1.00 30.70           C  
ATOM  19231  NE  ARG C 815     231.196 188.545 182.795  1.00 30.61           N  
ATOM  19232  CZ  ARG C 815     231.272 188.603 184.138  1.00 30.39           C  
ATOM  19233  NH1 ARG C 815     230.182 188.683 184.877  1.00 30.20           N  
ATOM  19234  NH2 ARG C 815     232.464 188.572 184.696  1.00 30.53           N  
ATOM  19235  N   SER C 816     231.987 189.062 177.064  1.00 30.19           N  
ATOM  19236  CA  SER C 816     232.967 189.632 176.155  1.00 29.52           C  
ATOM  19237  C   SER C 816     234.146 190.192 176.911  1.00 29.25           C  
ATOM  19238  O   SER C 816     234.083 190.369 178.127  1.00 30.72           O  
ATOM  19239  CB  SER C 816     232.350 190.740 175.364  1.00 29.56           C  
ATOM  19240  OG  SER C 816     232.147 191.858 176.170  1.00 29.52           O  
ATOM  19241  N   PHE C 817     235.219 190.511 176.194  1.00 29.19           N  
ATOM  19242  CA  PHE C 817     236.376 191.099 176.845  1.00 28.96           C  
ATOM  19243  C   PHE C 817     235.975 192.387 177.542  1.00 32.59           C  
ATOM  19244  O   PHE C 817     236.284 192.589 178.717  1.00 28.95           O  
ATOM  19245  CB  PHE C 817     237.481 191.395 175.847  1.00 29.16           C  
ATOM  19246  CG  PHE C 817     238.718 191.900 176.494  1.00 29.09           C  
ATOM  19247  CD1 PHE C 817     239.659 191.011 176.954  1.00 28.98           C  
ATOM  19248  CD2 PHE C 817     238.945 193.244 176.663  1.00 29.13           C  
ATOM  19249  CE1 PHE C 817     240.806 191.455 177.559  1.00 29.66           C  
ATOM  19250  CE2 PHE C 817     240.093 193.692 177.261  1.00 29.54           C  
ATOM  19251  CZ  PHE C 817     241.023 192.798 177.709  1.00 30.27           C  
ATOM  19252  N   ILE C 818     235.258 193.253 176.830  1.00 28.62           N  
ATOM  19253  CA  ILE C 818     234.822 194.496 177.441  1.00 28.64           C  
ATOM  19254  C   ILE C 818     233.897 194.275 178.623  1.00 30.73           C  
ATOM  19255  O   ILE C 818     234.058 194.933 179.648  1.00 29.99           O  
ATOM  19256  CB  ILE C 818     234.220 195.462 176.414  1.00 28.67           C  
ATOM  19257  CG1 ILE C 818     235.369 195.986 175.529  1.00 28.74           C  
ATOM  19258  CG2 ILE C 818     233.465 196.591 177.115  1.00 28.76           C  
ATOM  19259  CD1 ILE C 818     234.950 196.735 174.300  1.00 28.65           C  
ATOM  19260  N   GLU C 819     232.957 193.347 178.531  1.00 29.00           N  
ATOM  19261  CA  GLU C 819     232.093 193.130 179.682  1.00 29.04           C  
ATOM  19262  C   GLU C 819     232.900 192.755 180.918  1.00 31.83           C  
ATOM  19263  O   GLU C 819     232.662 193.294 181.999  1.00 30.03           O  
ATOM  19264  CB  GLU C 819     231.064 192.050 179.390  1.00 29.52           C  
ATOM  19265  CG  GLU C 819     229.965 192.485 178.461  1.00 29.31           C  
ATOM  19266  CD  GLU C 819     229.024 191.388 178.103  1.00 29.30           C  
ATOM  19267  OE1 GLU C 819     229.456 190.326 177.707  1.00 30.18           O  
ATOM  19268  OE2 GLU C 819     227.845 191.608 178.244  1.00 28.57           O  
ATOM  19269  N   ASP C 820     233.913 191.909 180.767  1.00 29.52           N  
ATOM  19270  CA  ASP C 820     234.737 191.578 181.922  1.00 29.68           C  
ATOM  19271  C   ASP C 820     235.429 192.810 182.490  1.00 30.49           C  
ATOM  19272  O   ASP C 820     235.569 192.935 183.709  1.00 31.46           O  
ATOM  19273  CB  ASP C 820     235.773 190.512 181.582  1.00 30.57           C  
ATOM  19274  CG  ASP C 820     235.207 189.087 181.534  1.00 31.08           C  
ATOM  19275  OD1 ASP C 820     234.158 188.841 182.108  1.00 30.89           O  
ATOM  19276  OD2 ASP C 820     235.838 188.253 180.933  1.00 31.34           O  
ATOM  19277  N   LEU C 821     235.832 193.741 181.627  1.00 29.74           N  
ATOM  19278  CA  LEU C 821     236.472 194.950 182.123  1.00 30.05           C  
ATOM  19279  C   LEU C 821     235.491 195.745 182.958  1.00 29.99           C  
ATOM  19280  O   LEU C 821     235.866 196.351 183.958  1.00 31.30           O  
ATOM  19281  CB  LEU C 821     236.928 195.875 180.990  1.00 29.92           C  
ATOM  19282  CG  LEU C 821     238.037 195.407 180.064  1.00 29.93           C  
ATOM  19283  CD1 LEU C 821     238.204 196.468 178.971  1.00 29.86           C  
ATOM  19284  CD2 LEU C 821     239.326 195.209 180.832  1.00 31.04           C  
ATOM  19285  N   LEU C 822     234.229 195.757 182.546  1.00 29.89           N  
ATOM  19286  CA  LEU C 822     233.231 196.542 183.252  1.00 29.94           C  
ATOM  19287  C   LEU C 822     232.991 195.961 184.639  1.00 29.96           C  
ATOM  19288  O   LEU C 822     232.923 196.688 185.629  1.00 31.31           O  
ATOM  19289  CB  LEU C 822     231.913 196.545 182.458  1.00 29.63           C  
ATOM  19290  CG  LEU C 822     231.948 197.226 181.063  1.00 29.43           C  
ATOM  19291  CD1 LEU C 822     230.640 196.966 180.346  1.00 28.51           C  
ATOM  19292  CD2 LEU C 822     232.172 198.697 181.202  1.00 30.01           C  
ATOM  19293  N   PHE C 823     232.926 194.641 184.724  1.00 29.44           N  
ATOM  19294  CA  PHE C 823     232.671 193.985 185.998  1.00 29.42           C  
ATOM  19295  C   PHE C 823     233.812 194.162 186.979  1.00 30.52           C  
ATOM  19296  O   PHE C 823     233.591 194.368 188.173  1.00 30.90           O  
ATOM  19297  CB  PHE C 823     232.367 192.505 185.789  1.00 29.61           C  
ATOM  19298  CG  PHE C 823     230.915 192.239 185.483  1.00 29.63           C  
ATOM  19299  CD1 PHE C 823     230.411 192.336 184.203  1.00 29.59           C  
ATOM  19300  CD2 PHE C 823     230.048 191.885 186.494  1.00 29.47           C  
ATOM  19301  CE1 PHE C 823     229.082 192.100 183.945  1.00 28.91           C  
ATOM  19302  CE2 PHE C 823     228.717 191.646 186.239  1.00 28.97           C  
ATOM  19303  CZ  PHE C 823     228.233 191.757 184.963  1.00 28.60           C  
ATOM  19304  N   ASN C 824     235.030 194.142 186.480  1.00 31.01           N  
ATOM  19305  CA  ASN C 824     236.196 194.220 187.341  1.00 30.70           C  
ATOM  19306  C   ASN C 824     236.464 195.620 187.885  1.00 31.23           C  
ATOM  19307  O   ASN C 824     237.399 195.805 188.666  1.00 31.27           O  
ATOM  19308  CB  ASN C 824     237.409 193.712 186.600  1.00 31.01           C  
ATOM  19309  CG  ASN C 824     237.339 192.245 186.358  1.00 31.63           C  
ATOM  19310  OD1 ASN C 824     236.658 191.506 187.078  1.00 31.69           O  
ATOM  19311  ND2 ASN C 824     238.033 191.795 185.349  1.00 32.11           N  
ATOM  19312  N   LYS C 825     235.679 196.614 187.471  1.00 30.68           N  
ATOM  19313  CA  LYS C 825     235.909 197.971 187.946  1.00 30.90           C  
ATOM  19314  C   LYS C 825     234.841 198.463 188.916  1.00 31.07           C  
ATOM  19315  O   LYS C 825     234.852 199.632 189.298  1.00 31.31           O  
ATOM  19316  CB  LYS C 825     236.040 198.930 186.763  1.00 30.98           C  
ATOM  19317  CG  LYS C 825     237.201 198.608 185.820  1.00 31.22           C  
ATOM  19318  CD  LYS C 825     238.572 198.797 186.478  1.00 31.76           C  
ATOM  19319  CE  LYS C 825     239.689 198.458 185.503  1.00 32.04           C  
ATOM  19320  NZ  LYS C 825     241.045 198.608 186.115  1.00 31.15           N  
ATOM  19321  N   VAL C 826     233.926 197.588 189.329  1.00 30.95           N  
ATOM  19322  CA  VAL C 826     232.895 197.998 190.286  1.00 30.96           C  
ATOM  19323  C   VAL C 826     232.925 197.075 191.507  1.00 31.26           C  
ATOM  19324  O   VAL C 826     232.972 195.854 191.351  1.00 31.23           O  
ATOM  19325  CB  VAL C 826     231.494 197.968 189.645  1.00 30.58           C  
ATOM  19326  CG1 VAL C 826     230.420 198.427 190.647  1.00 30.44           C  
ATOM  19327  CG2 VAL C 826     231.482 198.851 188.414  1.00 29.97           C  
ATOM  19328  N   THR C 827     232.889 197.659 192.718  1.00 31.21           N  
ATOM  19329  CA  THR C 827     232.933 196.912 193.979  1.00 31.33           C  
ATOM  19330  C   THR C 827     232.034 197.573 195.033  1.00 31.15           C  
ATOM  19331  O   THR C 827     232.376 198.567 195.676  1.00 30.71           O  
ATOM  19332  CB  THR C 827     234.413 196.730 194.480  1.00 31.38           C  
ATOM  19333  OG1 THR C 827     234.408 196.043 195.748  1.00 30.90           O  
ATOM  19334  CG2 THR C 827     235.204 198.099 194.618  1.00 30.71           C  
ATOM  19335  N   ASN C 856     221.469 191.260 212.900  1.00 36.23           N  
ATOM  19336  CA  ASN C 856     220.835 192.581 212.857  1.00 35.60           C  
ATOM  19337  C   ASN C 856     219.487 192.584 212.100  1.00 35.46           C  
ATOM  19338  O   ASN C 856     218.781 193.593 212.111  1.00 35.22           O  
ATOM  19339  CB  ASN C 856     221.803 193.624 212.259  1.00 35.75           C  
ATOM  19340  CG  ASN C 856     223.037 193.964 213.178  1.00 37.48           C  
ATOM  19341  OD1 ASN C 856     222.907 194.011 214.412  1.00 36.95           O  
ATOM  19342  ND2 ASN C 856     224.211 194.190 212.574  1.00 39.07           N  
ATOM  19343  N   GLY C 857     219.133 191.464 211.440  1.00 36.24           N  
ATOM  19344  CA  GLY C 857     217.868 191.307 210.707  1.00 35.84           C  
ATOM  19345  C   GLY C 857     217.956 191.804 209.270  1.00 34.79           C  
ATOM  19346  O   GLY C 857     216.946 191.928 208.581  1.00 34.25           O  
ATOM  19347  N   LEU C 858     219.164 192.100 208.824  1.00 35.18           N  
ATOM  19348  CA  LEU C 858     219.384 192.614 207.482  1.00 34.14           C  
ATOM  19349  C   LEU C 858     219.828 191.516 206.540  1.00 34.16           C  
ATOM  19350  O   LEU C 858     220.864 190.889 206.761  1.00 34.40           O  
ATOM  19351  CB  LEU C 858     220.481 193.684 207.505  1.00 34.43           C  
ATOM  19352  CG  LEU C 858     220.088 195.119 207.877  1.00 34.36           C  
ATOM  19353  CD1 LEU C 858     219.446 195.172 209.258  1.00 34.53           C  
ATOM  19354  CD2 LEU C 858     221.336 195.954 207.859  1.00 34.13           C  
ATOM  19355  N   THR C 859     219.063 191.295 205.477  1.00 33.53           N  
ATOM  19356  CA  THR C 859     219.423 190.281 204.499  1.00 33.15           C  
ATOM  19357  C   THR C 859     219.348 190.840 203.090  1.00 32.48           C  
ATOM  19358  O   THR C 859     218.673 191.839 202.836  1.00 32.32           O  
ATOM  19359  CB  THR C 859     218.508 189.046 204.606  1.00 33.77           C  
ATOM  19360  OG1 THR C 859     217.168 189.410 204.270  1.00 33.23           O  
ATOM  19361  CG2 THR C 859     218.529 188.492 206.031  1.00 35.74           C  
ATOM  19362  N   VAL C 860     220.017 190.174 202.163  1.00 32.28           N  
ATOM  19363  CA  VAL C 860     219.961 190.568 200.766  1.00 31.41           C  
ATOM  19364  C   VAL C 860     219.468 189.440 199.890  1.00 31.65           C  
ATOM  19365  O   VAL C 860     219.979 188.323 199.943  1.00 31.95           O  
ATOM  19366  CB  VAL C 860     221.334 191.051 200.287  1.00 31.30           C  
ATOM  19367  CG1 VAL C 860     221.281 191.370 198.810  1.00 31.48           C  
ATOM  19368  CG2 VAL C 860     221.721 192.293 201.075  1.00 31.14           C  
ATOM  19369  N   LEU C 861     218.468 189.743 199.086  1.00 30.93           N  
ATOM  19370  CA  LEU C 861     217.891 188.775 198.188  1.00 30.84           C  
ATOM  19371  C   LEU C 861     218.671 188.821 196.885  1.00 30.91           C  
ATOM  19372  O   LEU C 861     219.149 189.887 196.506  1.00 30.92           O  
ATOM  19373  CB  LEU C 861     216.434 189.157 197.942  1.00 30.51           C  
ATOM  19374  CG  LEU C 861     215.546 189.258 199.187  1.00 31.21           C  
ATOM  19375  CD1 LEU C 861     214.208 189.851 198.789  1.00 30.50           C  
ATOM  19376  CD2 LEU C 861     215.361 187.878 199.807  1.00 34.34           C  
ATOM  19377  N   PRO C 862     218.835 187.705 196.185  1.00 30.80           N  
ATOM  19378  CA  PRO C 862     219.453 187.643 194.889  1.00 30.39           C  
ATOM  19379  C   PRO C 862     218.484 188.195 193.870  1.00 30.21           C  
ATOM  19380  O   PRO C 862     217.273 188.126 194.099  1.00 30.48           O  
ATOM  19381  CB  PRO C 862     219.680 186.150 194.701  1.00 31.30           C  
ATOM  19382  CG  PRO C 862     218.578 185.512 195.494  1.00 32.39           C  
ATOM  19383  CD  PRO C 862     218.370 186.425 196.699  1.00 31.92           C  
ATOM  19384  N   PRO C 863     218.980 188.689 192.738  1.00 29.77           N  
ATOM  19385  CA  PRO C 863     218.228 189.124 191.587  1.00 29.36           C  
ATOM  19386  C   PRO C 863     217.653 187.907 190.915  1.00 29.69           C  
ATOM  19387  O   PRO C 863     218.236 186.827 191.008  1.00 30.65           O  
ATOM  19388  CB  PRO C 863     219.293 189.810 190.734  1.00 29.89           C  
ATOM  19389  CG  PRO C 863     220.584 189.133 191.126  1.00 30.07           C  
ATOM  19390  CD  PRO C 863     220.429 188.803 192.591  1.00 29.91           C  
ATOM  19391  N   LEU C 864     216.546 188.073 190.214  1.00 29.31           N  
ATOM  19392  CA  LEU C 864     215.990 186.972 189.453  1.00 29.48           C  
ATOM  19393  C   LEU C 864     216.875 186.621 188.278  1.00 29.94           C  
ATOM  19394  O   LEU C 864     217.084 185.446 187.977  1.00 31.07           O  
ATOM  19395  CB  LEU C 864     214.588 187.308 188.954  1.00 29.32           C  
ATOM  19396  CG  LEU C 864     213.873 186.202 188.158  1.00 30.26           C  
ATOM  19397  CD1 LEU C 864     213.712 184.945 189.016  1.00 31.54           C  
ATOM  19398  CD2 LEU C 864     212.535 186.729 187.697  1.00 31.70           C  
ATOM  19399  N   LEU C 865     217.408 187.636 187.614  1.00 29.53           N  
ATOM  19400  CA  LEU C 865     218.255 187.397 186.465  1.00 29.12           C  
ATOM  19401  C   LEU C 865     219.709 187.485 186.872  1.00 29.16           C  
ATOM  19402  O   LEU C 865     220.197 188.548 187.257  1.00 29.34           O  
ATOM  19403  CB  LEU C 865     217.976 188.411 185.352  1.00 28.83           C  
ATOM  19404  CG  LEU C 865     216.732 188.165 184.479  1.00 28.38           C  
ATOM  19405  CD1 LEU C 865     215.477 188.545 185.242  1.00 29.00           C  
ATOM  19406  CD2 LEU C 865     216.843 188.979 183.215  1.00 27.14           C  
ATOM  19407  N   THR C 866     220.390 186.358 186.785  1.00 29.35           N  
ATOM  19408  CA  THR C 866     221.783 186.242 187.178  1.00 29.36           C  
ATOM  19409  C   THR C 866     222.675 186.872 186.136  1.00 29.47           C  
ATOM  19410  O   THR C 866     222.241 187.118 185.011  1.00 29.88           O  
ATOM  19411  CB  THR C 866     222.183 184.772 187.319  1.00 30.02           C  
ATOM  19412  OG1 THR C 866     222.060 184.130 186.043  1.00 30.01           O  
ATOM  19413  CG2 THR C 866     221.307 184.070 188.312  1.00 31.34           C  
ATOM  19414  N   ASP C 867     223.943 187.084 186.473  1.00 29.29           N  
ATOM  19415  CA  ASP C 867     224.862 187.686 185.520  1.00 29.00           C  
ATOM  19416  C   ASP C 867     224.984 186.858 184.253  1.00 28.72           C  
ATOM  19417  O   ASP C 867     225.145 187.411 183.164  1.00 29.29           O  
ATOM  19418  CB  ASP C 867     226.241 187.878 186.136  1.00 29.38           C  
ATOM  19419  N   GLU C 868     224.903 185.537 184.377  1.00 29.05           N  
ATOM  19420  CA  GLU C 868     224.983 184.691 183.197  1.00 28.82           C  
ATOM  19421  C   GLU C 868     223.783 184.928 182.298  1.00 28.39           C  
ATOM  19422  O   GLU C 868     223.909 184.964 181.074  1.00 29.04           O  
ATOM  19423  CB  GLU C 868     225.033 183.216 183.584  1.00 30.09           C  
ATOM  19424  N   MET C 869     222.615 185.098 182.904  1.00 28.28           N  
ATOM  19425  CA  MET C 869     221.405 185.327 182.133  1.00 27.44           C  
ATOM  19426  C   MET C 869     221.413 186.686 181.466  1.00 28.83           C  
ATOM  19427  O   MET C 869     220.938 186.832 180.338  1.00 27.82           O  
ATOM  19428  CB  MET C 869     220.185 185.150 183.008  1.00 28.85           C  
ATOM  19429  CG  MET C 869     219.940 183.711 183.383  1.00 29.20           C  
ATOM  19430  SD  MET C 869     218.564 183.510 184.478  1.00 31.25           S  
ATOM  19431  CE  MET C 869     218.319 181.751 184.334  1.00 32.39           C  
ATOM  19432  N   ILE C 870     221.980 187.679 182.132  1.00 27.81           N  
ATOM  19433  CA  ILE C 870     222.057 188.985 181.514  1.00 27.10           C  
ATOM  19434  C   ILE C 870     222.989 188.892 180.328  1.00 27.38           C  
ATOM  19435  O   ILE C 870     222.685 189.411 179.257  1.00 26.84           O  
ATOM  19436  CB  ILE C 870     222.552 190.070 182.477  1.00 27.94           C  
ATOM  19437  CG1 ILE C 870     221.589 190.225 183.663  1.00 28.01           C  
ATOM  19438  CG2 ILE C 870     222.694 191.387 181.724  1.00 27.18           C  
ATOM  19439  CD1 ILE C 870     220.176 190.600 183.306  1.00 27.76           C  
ATOM  19440  N   ALA C 871     224.111 188.198 180.495  1.00 27.39           N  
ATOM  19441  CA  ALA C 871     225.051 188.042 179.403  1.00 26.66           C  
ATOM  19442  C   ALA C 871     224.378 187.386 178.208  1.00 26.23           C  
ATOM  19443  O   ALA C 871     224.634 187.769 177.069  1.00 26.85           O  
ATOM  19444  CB  ALA C 871     226.241 187.217 179.847  1.00 28.54           C  
ATOM  19445  N   GLN C 872     223.494 186.423 178.448  1.00 26.48           N  
ATOM  19446  CA  GLN C 872     222.793 185.804 177.335  1.00 25.92           C  
ATOM  19447  C   GLN C 872     221.865 186.789 176.640  1.00 25.76           C  
ATOM  19448  O   GLN C 872     221.751 186.767 175.415  1.00 26.25           O  
ATOM  19449  CB  GLN C 872     222.024 184.571 177.779  1.00 26.60           C  
ATOM  19450  CG  GLN C 872     222.911 183.407 178.134  1.00 26.62           C  
ATOM  19451  CD  GLN C 872     222.140 182.199 178.592  1.00 27.22           C  
ATOM  19452  OE1 GLN C 872     221.057 181.903 178.081  1.00 26.18           O  
ATOM  19453  NE2 GLN C 872     222.692 181.485 179.562  1.00 27.65           N  
ATOM  19454  N   TYR C 873     221.228 187.680 177.394  1.00 25.64           N  
ATOM  19455  CA  TYR C 873     220.371 188.665 176.753  1.00 24.69           C  
ATOM  19456  C   TYR C 873     221.171 189.676 175.955  1.00 25.12           C  
ATOM  19457  O   TYR C 873     220.781 190.024 174.841  1.00 24.72           O  
ATOM  19458  CB  TYR C 873     219.500 189.402 177.760  1.00 25.18           C  
ATOM  19459  CG  TYR C 873     218.283 188.658 178.162  1.00 24.83           C  
ATOM  19460  CD1 TYR C 873     218.087 188.306 179.466  1.00 25.62           C  
ATOM  19461  CD2 TYR C 873     217.350 188.327 177.209  1.00 25.09           C  
ATOM  19462  CE1 TYR C 873     216.956 187.625 179.819  1.00 25.94           C  
ATOM  19463  CE2 TYR C 873     216.225 187.645 177.560  1.00 25.64           C  
ATOM  19464  CZ  TYR C 873     216.025 187.295 178.857  1.00 26.13           C  
ATOM  19465  OH  TYR C 873     214.896 186.599 179.202  1.00 26.75           O  
ATOM  19466  N   THR C 874     222.301 190.134 176.484  1.00 25.03           N  
ATOM  19467  CA  THR C 874     223.077 191.105 175.735  1.00 24.02           C  
ATOM  19468  C   THR C 874     223.742 190.424 174.556  1.00 24.41           C  
ATOM  19469  O   THR C 874     223.950 191.045 173.515  1.00 24.61           O  
ATOM  19470  CB  THR C 874     224.090 191.842 176.621  1.00 24.75           C  
ATOM  19471  OG1 THR C 874     224.950 190.908 177.260  1.00 26.61           O  
ATOM  19472  CG2 THR C 874     223.354 192.650 177.672  1.00 24.97           C  
ATOM  19473  N   SER C 875     224.019 189.131 174.685  1.00 24.76           N  
ATOM  19474  CA  SER C 875     224.555 188.366 173.576  1.00 24.23           C  
ATOM  19475  C   SER C 875     223.526 188.279 172.464  1.00 23.65           C  
ATOM  19476  O   SER C 875     223.852 188.501 171.301  1.00 24.25           O  
ATOM  19477  CB  SER C 875     224.939 186.978 174.023  1.00 25.60           C  
ATOM  19478  OG  SER C 875     225.449 186.234 172.958  1.00 26.05           O  
ATOM  19479  N   ALA C 876     222.276 187.982 172.819  1.00 23.63           N  
ATOM  19480  CA  ALA C 876     221.204 187.884 171.841  1.00 22.95           C  
ATOM  19481  C   ALA C 876     220.958 189.193 171.130  1.00 23.06           C  
ATOM  19482  O   ALA C 876     220.744 189.222 169.917  1.00 23.52           O  
ATOM  19483  CB  ALA C 876     219.923 187.465 172.519  1.00 24.22           C  
ATOM  19484  N   LEU C 877     220.985 190.284 171.878  1.00 23.16           N  
ATOM  19485  CA  LEU C 877     220.740 191.582 171.292  1.00 22.38           C  
ATOM  19486  C   LEU C 877     221.875 191.974 170.389  1.00 22.68           C  
ATOM  19487  O   LEU C 877     221.654 192.530 169.316  1.00 23.04           O  
ATOM  19488  CB  LEU C 877     220.568 192.615 172.389  1.00 22.48           C  
ATOM  19489  CG  LEU C 877     219.312 192.482 173.225  1.00 22.52           C  
ATOM  19490  CD1 LEU C 877     219.443 193.372 174.399  1.00 22.72           C  
ATOM  19491  CD2 LEU C 877     218.110 192.875 172.406  1.00 22.63           C  
ATOM  19492  N   LEU C 878     223.089 191.656 170.797  1.00 22.86           N  
ATOM  19493  CA  LEU C 878     224.244 191.955 169.986  1.00 22.13           C  
ATOM  19494  C   LEU C 878     224.267 191.112 168.725  1.00 22.78           C  
ATOM  19495  O   LEU C 878     224.555 191.623 167.644  1.00 23.15           O  
ATOM  19496  CB  LEU C 878     225.507 191.738 170.805  1.00 22.83           C  
ATOM  19497  CG  LEU C 878     226.814 191.952 170.101  1.00 23.84           C  
ATOM  19498  CD1 LEU C 878     226.869 193.313 169.532  1.00 23.07           C  
ATOM  19499  CD2 LEU C 878     227.921 191.780 171.095  1.00 25.84           C  
ATOM  19500  N   ALA C 879     223.966 189.824 168.847  1.00 22.56           N  
ATOM  19501  CA  ALA C 879     223.954 188.953 167.688  1.00 22.08           C  
ATOM  19502  C   ALA C 879     222.902 189.422 166.711  1.00 21.74           C  
ATOM  19503  O   ALA C 879     223.132 189.433 165.504  1.00 22.66           O  
ATOM  19504  CB  ALA C 879     223.681 187.519 168.100  1.00 23.59           C  
ATOM  19505  N   GLY C 880     221.758 189.853 167.231  1.00 21.96           N  
ATOM  19506  CA  GLY C 880     220.685 190.363 166.401  1.00 21.71           C  
ATOM  19507  C   GLY C 880     221.138 191.618 165.677  1.00 22.36           C  
ATOM  19508  O   GLY C 880     221.021 191.725 164.456  1.00 21.81           O  
ATOM  19509  N   THR C 881     221.703 192.556 166.425  1.00 21.91           N  
ATOM  19510  CA  THR C 881     222.138 193.826 165.875  1.00 20.99           C  
ATOM  19511  C   THR C 881     223.125 193.636 164.744  1.00 21.78           C  
ATOM  19512  O   THR C 881     223.034 194.311 163.719  1.00 22.37           O  
ATOM  19513  CB  THR C 881     222.798 194.693 166.962  1.00 21.67           C  
ATOM  19514  OG1 THR C 881     221.858 194.958 167.998  1.00 22.01           O  
ATOM  19515  CG2 THR C 881     223.276 196.014 166.385  1.00 21.75           C  
ATOM  19516  N   ILE C 882     224.081 192.740 164.928  1.00 21.98           N  
ATOM  19517  CA  ILE C 882     225.095 192.516 163.916  1.00 21.45           C  
ATOM  19518  C   ILE C 882     224.595 191.779 162.679  1.00 21.78           C  
ATOM  19519  O   ILE C 882     224.956 192.150 161.567  1.00 22.36           O  
ATOM  19520  CB  ILE C 882     226.301 191.776 164.504  1.00 22.10           C  
ATOM  19521  CG1 ILE C 882     227.011 192.683 165.505  1.00 22.61           C  
ATOM  19522  CG2 ILE C 882     227.256 191.364 163.390  1.00 22.75           C  
ATOM  19523  CD1 ILE C 882     228.019 191.971 166.366  1.00 24.13           C  
ATOM  19524  N   THR C 883     223.813 190.715 162.848  1.00 21.94           N  
ATOM  19525  CA  THR C 883     223.439 189.911 161.692  1.00 21.17           C  
ATOM  19526  C   THR C 883     222.094 190.238 161.041  1.00 21.41           C  
ATOM  19527  O   THR C 883     221.855 189.812 159.909  1.00 22.22           O  
ATOM  19528  CB  THR C 883     223.432 188.421 162.067  1.00 22.06           C  
ATOM  19529  OG1 THR C 883     222.432 188.173 163.045  1.00 22.02           O  
ATOM  19530  CG2 THR C 883     224.770 188.019 162.635  1.00 22.45           C  
ATOM  19531  N   SER C 884     221.201 190.956 161.729  1.00 21.54           N  
ATOM  19532  CA  SER C 884     219.885 191.241 161.151  1.00 20.75           C  
ATOM  19533  C   SER C 884     219.437 192.701 161.289  1.00 20.75           C  
ATOM  19534  O   SER C 884     218.293 193.046 160.982  1.00 21.21           O  
ATOM  19535  CB  SER C 884     218.860 190.324 161.764  1.00 21.11           C  
ATOM  19536  OG  SER C 884     218.749 190.545 163.127  1.00 21.64           O  
ATOM  19537  N   GLY C 885     220.321 193.563 161.757  1.00 21.52           N  
ATOM  19538  CA  GLY C 885     219.994 194.974 161.899  1.00 21.04           C  
ATOM  19539  C   GLY C 885     218.826 195.192 162.842  1.00 20.95           C  
ATOM  19540  O   GLY C 885     218.820 194.703 163.965  1.00 21.75           O  
ATOM  19541  N   TRP C 886     217.836 195.943 162.395  1.00 20.53           N  
ATOM  19542  CA  TRP C 886     216.678 196.225 163.227  1.00 20.32           C  
ATOM  19543  C   TRP C 886     215.502 195.295 163.000  1.00 20.58           C  
ATOM  19544  O   TRP C 886     214.452 195.455 163.632  1.00 20.87           O  
ATOM  19545  CB  TRP C 886     216.197 197.649 163.011  1.00 20.39           C  
ATOM  19546  CG  TRP C 886     216.141 198.067 161.596  1.00 20.32           C  
ATOM  19547  CD1 TRP C 886     215.219 197.729 160.660  1.00 20.36           C  
ATOM  19548  CD2 TRP C 886     217.046 198.977 160.956  1.00 20.14           C  
ATOM  19549  NE1 TRP C 886     215.507 198.350 159.475  1.00 20.27           N  
ATOM  19550  CE2 TRP C 886     216.621 199.123 159.644  1.00 20.25           C  
ATOM  19551  CE3 TRP C 886     218.163 199.677 161.391  1.00 19.98           C  
ATOM  19552  CZ2 TRP C 886     217.281 199.942 158.754  1.00 20.32           C  
ATOM  19553  CZ3 TRP C 886     218.819 200.500 160.506  1.00 19.89           C  
ATOM  19554  CH2 TRP C 886     218.393 200.630 159.224  1.00 19.94           C  
ATOM  19555  N   THR C 887     215.640 194.331 162.105  1.00 20.48           N  
ATOM  19556  CA  THR C 887     214.472 193.549 161.768  1.00 20.01           C  
ATOM  19557  C   THR C 887     214.133 192.555 162.863  1.00 21.29           C  
ATOM  19558  O   THR C 887     212.977 192.170 163.003  1.00 21.44           O  
ATOM  19559  CB  THR C 887     214.662 192.822 160.437  1.00 20.52           C  
ATOM  19560  OG1 THR C 887     215.660 191.815 160.571  1.00 21.61           O  
ATOM  19561  CG2 THR C 887     215.125 193.834 159.399  1.00 20.70           C  
ATOM  19562  N   PHE C 888     215.114 192.190 163.687  1.00 20.86           N  
ATOM  19563  CA  PHE C 888     214.852 191.261 164.781  1.00 20.84           C  
ATOM  19564  C   PHE C 888     213.997 191.935 165.840  1.00 20.95           C  
ATOM  19565  O   PHE C 888     213.405 191.272 166.691  1.00 21.56           O  
ATOM  19566  CB  PHE C 888     216.138 190.741 165.416  1.00 21.43           C  
ATOM  19567  CG  PHE C 888     216.800 191.671 166.348  1.00 21.18           C  
ATOM  19568  CD1 PHE C 888     216.483 191.645 167.685  1.00 21.72           C  
ATOM  19569  CD2 PHE C 888     217.733 192.562 165.914  1.00 21.30           C  
ATOM  19570  CE1 PHE C 888     217.086 192.492 168.567  1.00 21.83           C  
ATOM  19571  CE2 PHE C 888     218.342 193.419 166.796  1.00 21.26           C  
ATOM  19572  CZ  PHE C 888     218.019 193.384 168.123  1.00 21.50           C  
ATOM  19573  N   GLY C 889     213.969 193.262 165.818  1.00 21.00           N  
ATOM  19574  CA  GLY C 889     213.156 194.013 166.745  1.00 20.84           C  
ATOM  19575  C   GLY C 889     211.726 193.999 166.237  1.00 20.58           C  
ATOM  19576  O   GLY C 889     210.807 193.571 166.933  1.00 20.52           O  
ATOM  19577  N   ALA C 890     211.551 194.464 165.001  1.00 20.72           N  
ATOM  19578  CA  ALA C 890     210.235 194.587 164.384  1.00 20.12           C  
ATOM  19579  C   ALA C 890     209.498 193.255 164.248  1.00 20.11           C  
ATOM  19580  O   ALA C 890     208.272 193.208 164.345  1.00 19.90           O  
ATOM  19581  CB  ALA C 890     210.368 195.214 163.013  1.00 19.76           C  
ATOM  19582  N   GLY C 891     210.228 192.179 163.989  1.00 20.61           N  
ATOM  19583  CA  GLY C 891     209.598 190.883 163.803  1.00 20.46           C  
ATOM  19584  C   GLY C 891     210.627 189.766 163.708  1.00 20.61           C  
ATOM  19585  O   GLY C 891     211.318 189.451 164.675  1.00 20.95           O  
ATOM  19586  N   ALA C 892     210.694 189.136 162.548  1.00 20.08           N  
ATOM  19587  CA  ALA C 892     211.656 188.074 162.321  1.00 20.27           C  
ATOM  19588  C   ALA C 892     213.044 188.649 162.129  1.00 20.44           C  
ATOM  19589  O   ALA C 892     213.207 189.715 161.543  1.00 21.30           O  
ATOM  19590  CB  ALA C 892     211.261 187.261 161.101  1.00 20.36           C  
ATOM  19591  N   ALA C 893     214.060 187.920 162.560  1.00 20.92           N  
ATOM  19592  CA  ALA C 893     215.413 188.369 162.299  1.00 20.58           C  
ATOM  19593  C   ALA C 893     215.771 188.001 160.879  1.00 20.71           C  
ATOM  19594  O   ALA C 893     215.859 186.824 160.539  1.00 20.67           O  
ATOM  19595  CB  ALA C 893     216.390 187.750 163.273  1.00 21.62           C  
ATOM  19596  N   LEU C 894     215.948 189.013 160.049  1.00 20.66           N  
ATOM  19597  CA  LEU C 894     216.216 188.817 158.638  1.00 20.20           C  
ATOM  19598  C   LEU C 894     217.688 189.018 158.344  1.00 20.81           C  
ATOM  19599  O   LEU C 894     218.198 190.124 158.500  1.00 21.53           O  
ATOM  19600  CB  LEU C 894     215.393 189.824 157.841  1.00 20.23           C  
ATOM  19601  CG  LEU C 894     213.878 189.800 158.073  1.00 19.99           C  
ATOM  19602  CD1 LEU C 894     213.278 190.895 157.307  1.00 20.51           C  
ATOM  19603  CD2 LEU C 894     213.289 188.499 157.615  1.00 19.81           C  
ATOM  19604  N   GLN C 895     218.382 187.974 157.911  1.00 20.87           N  
ATOM  19605  CA  GLN C 895     219.813 188.119 157.706  1.00 20.37           C  
ATOM  19606  C   GLN C 895     220.115 189.164 156.657  1.00 21.21           C  
ATOM  19607  O   GLN C 895     219.399 189.299 155.664  1.00 21.54           O  
ATOM  19608  CB  GLN C 895     220.479 186.794 157.308  1.00 21.19           C  
ATOM  19609  CG  GLN C 895     220.180 186.287 155.916  1.00 21.70           C  
ATOM  19610  CD  GLN C 895     218.999 185.415 155.885  1.00 21.43           C  
ATOM  19611  OE1 GLN C 895     218.129 185.516 156.755  1.00 21.17           O  
ATOM  19612  NE2 GLN C 895     218.930 184.548 154.884  1.00 21.45           N  
ATOM  19613  N   ILE C 896     221.183 189.906 156.884  1.00 21.10           N  
ATOM  19614  CA  ILE C 896     221.669 190.877 155.919  1.00 20.94           C  
ATOM  19615  C   ILE C 896     223.198 190.926 156.017  1.00 21.30           C  
ATOM  19616  O   ILE C 896     223.717 190.843 157.124  1.00 22.24           O  
ATOM  19617  CB  ILE C 896     221.046 192.250 156.225  1.00 20.96           C  
ATOM  19618  CG1 ILE C 896     221.387 193.242 155.131  1.00 21.18           C  
ATOM  19619  CG2 ILE C 896     221.522 192.740 157.585  1.00 21.50           C  
ATOM  19620  CD1 ILE C 896     220.598 194.512 155.165  1.00 21.06           C  
ATOM  19621  N   PRO C 897     223.953 191.054 154.918  1.00 21.16           N  
ATOM  19622  CA  PRO C 897     225.382 191.255 154.937  1.00 21.11           C  
ATOM  19623  C   PRO C 897     225.658 192.478 155.763  1.00 21.31           C  
ATOM  19624  O   PRO C 897     224.918 193.455 155.669  1.00 21.97           O  
ATOM  19625  CB  PRO C 897     225.711 191.453 153.464  1.00 21.43           C  
ATOM  19626  CG  PRO C 897     224.632 190.705 152.754  1.00 21.38           C  
ATOM  19627  CD  PRO C 897     223.393 190.932 153.584  1.00 21.30           C  
ATOM  19628  N   PHE C 898     226.712 192.457 156.558  1.00 21.63           N  
ATOM  19629  CA  PHE C 898     226.938 193.584 157.437  1.00 21.23           C  
ATOM  19630  C   PHE C 898     227.177 194.870 156.670  1.00 21.47           C  
ATOM  19631  O   PHE C 898     226.703 195.930 157.073  1.00 22.11           O  
ATOM  19632  CB  PHE C 898     228.086 193.335 158.391  1.00 22.26           C  
ATOM  19633  CG  PHE C 898     228.103 194.357 159.433  1.00 21.81           C  
ATOM  19634  CD1 PHE C 898     227.151 194.319 160.408  1.00 21.81           C  
ATOM  19635  CD2 PHE C 898     229.022 195.360 159.449  1.00 22.32           C  
ATOM  19636  CE1 PHE C 898     227.104 195.264 161.377  1.00 21.51           C  
ATOM  19637  CE2 PHE C 898     228.977 196.313 160.425  1.00 22.10           C  
ATOM  19638  CZ  PHE C 898     228.010 196.261 161.383  1.00 21.73           C  
ATOM  19639  N   ALA C 899     227.927 194.806 155.581  1.00 21.25           N  
ATOM  19640  CA  ALA C 899     228.204 196.021 154.834  1.00 20.91           C  
ATOM  19641  C   ALA C 899     226.911 196.645 154.323  1.00 20.52           C  
ATOM  19642  O   ALA C 899     226.774 197.865 154.296  1.00 21.53           O  
ATOM  19643  CB  ALA C 899     229.139 195.730 153.680  1.00 21.60           C  
ATOM  19644  N   MET C 900     225.950 195.826 153.917  1.00 20.75           N  
ATOM  19645  CA  MET C 900     224.694 196.389 153.457  1.00 20.07           C  
ATOM  19646  C   MET C 900     223.944 196.991 154.614  1.00 20.46           C  
ATOM  19647  O   MET C 900     223.369 198.070 154.493  1.00 20.77           O  
ATOM  19648  CB  MET C 900     223.853 195.362 152.740  1.00 20.65           C  
ATOM  19649  CG  MET C 900     224.409 194.949 151.409  1.00 20.21           C  
ATOM  19650  SD  MET C 900     223.463 193.659 150.651  1.00 21.16           S  
ATOM  19651  CE  MET C 900     221.940 194.495 150.234  1.00 20.93           C  
ATOM  19652  N   GLN C 901     224.002 196.344 155.762  1.00 20.33           N  
ATOM  19653  CA  GLN C 901     223.347 196.906 156.916  1.00 19.85           C  
ATOM  19654  C   GLN C 901     223.882 198.289 157.195  1.00 20.38           C  
ATOM  19655  O   GLN C 901     223.114 199.207 157.479  1.00 21.15           O  
ATOM  19656  CB  GLN C 901     223.547 196.038 158.132  1.00 20.75           C  
ATOM  19657  CG  GLN C 901     222.925 196.578 159.351  1.00 20.61           C  
ATOM  19658  CD  GLN C 901     223.017 195.617 160.438  1.00 21.05           C  
ATOM  19659  OE1 GLN C 901     222.615 194.473 160.263  1.00 21.63           O  
ATOM  19660  NE2 GLN C 901     223.531 196.028 161.576  1.00 21.10           N  
ATOM  19661  N   MET C 902     225.195 198.449 157.091  1.00 20.27           N  
ATOM  19662  CA  MET C 902     225.785 199.754 157.307  1.00 19.86           C  
ATOM  19663  C   MET C 902     225.325 200.735 156.245  1.00 20.40           C  
ATOM  19664  O   MET C 902     225.104 201.906 156.535  1.00 20.35           O  
ATOM  19665  CB  MET C 902     227.297 199.663 157.346  1.00 20.81           C  
ATOM  19666  CG  MET C 902     227.838 199.008 158.573  1.00 21.35           C  
ATOM  19667  SD  MET C 902     227.346 199.827 160.089  1.00 21.54           S  
ATOM  19668  CE  MET C 902     228.241 201.351 159.998  1.00 21.02           C  
ATOM  19669  N   ALA C 903     225.117 200.264 155.023  1.00 20.53           N  
ATOM  19670  CA  ALA C 903     224.654 201.154 153.976  1.00 19.45           C  
ATOM  19671  C   ALA C 903     223.329 201.761 154.368  1.00 19.16           C  
ATOM  19672  O   ALA C 903     223.088 202.945 154.133  1.00 19.95           O  
ATOM  19673  CB  ALA C 903     224.510 200.416 152.665  1.00 20.45           C  
ATOM  19674  N   TYR C 904     222.479 200.974 155.012  1.00 19.33           N  
ATOM  19675  CA  TYR C 904     221.199 201.507 155.428  1.00 18.95           C  
ATOM  19676  C   TYR C 904     221.430 202.543 156.504  1.00 18.89           C  
ATOM  19677  O   TYR C 904     220.801 203.603 156.506  1.00 19.86           O  
ATOM  19678  CB  TYR C 904     220.300 200.438 156.027  1.00 19.80           C  
ATOM  19679  CG  TYR C 904     219.861 199.317 155.144  1.00 20.20           C  
ATOM  19680  CD1 TYR C 904     220.180 199.245 153.793  1.00 20.12           C  
ATOM  19681  CD2 TYR C 904     219.089 198.338 155.721  1.00 20.39           C  
ATOM  19682  CE1 TYR C 904     219.716 198.179 153.054  1.00 20.21           C  
ATOM  19683  CE2 TYR C 904     218.633 197.297 154.988  1.00 20.47           C  
ATOM  19684  CZ  TYR C 904     218.936 197.208 153.670  1.00 20.46           C  
ATOM  19685  OH  TYR C 904     218.460 196.155 152.960  1.00 20.84           O  
ATOM  19686  N   ARG C 905     222.343 202.228 157.416  1.00 18.97           N  
ATOM  19687  CA  ARG C 905     222.663 203.085 158.545  1.00 18.45           C  
ATOM  19688  C   ARG C 905     223.188 204.440 158.070  1.00 19.35           C  
ATOM  19689  O   ARG C 905     222.883 205.471 158.665  1.00 19.33           O  
ATOM  19690  CB  ARG C 905     223.693 202.393 159.422  1.00 19.46           C  
ATOM  19691  CG  ARG C 905     223.230 201.048 160.005  1.00 19.13           C  
ATOM  19692  CD  ARG C 905     222.660 201.181 161.313  1.00 19.10           C  
ATOM  19693  NE  ARG C 905     222.178 199.914 161.839  1.00 19.31           N  
ATOM  19694  CZ  ARG C 905     221.483 199.782 162.989  1.00 19.53           C  
ATOM  19695  NH1 ARG C 905     221.224 200.834 163.724  1.00 19.50           N  
ATOM  19696  NH2 ARG C 905     221.061 198.595 163.374  1.00 20.18           N  
ATOM  19697  N   PHE C 906     223.954 204.437 156.981  1.00 19.32           N  
ATOM  19698  CA  PHE C 906     224.472 205.669 156.401  1.00 18.20           C  
ATOM  19699  C   PHE C 906     223.389 206.470 155.689  1.00 21.87           C  
ATOM  19700  O   PHE C 906     223.272 207.676 155.896  1.00 17.83           O  
ATOM  19701  CB  PHE C 906     225.628 205.387 155.451  1.00 19.12           C  
ATOM  19702  CG  PHE C 906     226.972 205.357 156.116  1.00 19.21           C  
ATOM  19703  CD1 PHE C 906     227.452 204.238 156.749  1.00 20.07           C  
ATOM  19704  CD2 PHE C 906     227.769 206.466 156.079  1.00 19.56           C  
ATOM  19705  CE1 PHE C 906     228.693 204.242 157.338  1.00 20.83           C  
ATOM  19706  CE2 PHE C 906     229.004 206.470 156.659  1.00 20.10           C  
ATOM  19707  CZ  PHE C 906     229.466 205.360 157.291  1.00 20.59           C  
ATOM  19708  N   ASN C 907     222.532 205.799 154.919  1.00 18.54           N  
ATOM  19709  CA  ASN C 907     221.463 206.536 154.251  1.00 18.53           C  
ATOM  19710  C   ASN C 907     220.563 207.171 155.295  1.00 18.81           C  
ATOM  19711  O   ASN C 907     220.059 208.280 155.113  1.00 19.20           O  
ATOM  19712  CB  ASN C 907     220.640 205.639 153.349  1.00 18.64           C  
ATOM  19713  CG  ASN C 907     221.307 205.288 152.054  1.00 19.64           C  
ATOM  19714  OD1 ASN C 907     222.208 205.979 151.560  1.00 19.93           O  
ATOM  19715  ND2 ASN C 907     220.859 204.208 151.478  1.00 20.16           N  
ATOM  19716  N   GLY C 908     220.423 206.494 156.426  1.00 18.85           N  
ATOM  19717  CA  GLY C 908     219.595 206.940 157.529  1.00 18.49           C  
ATOM  19718  C   GLY C 908     220.059 208.249 158.162  1.00 18.52           C  
ATOM  19719  O   GLY C 908     219.295 208.874 158.900  1.00 18.67           O  
ATOM  19720  N   ILE C 909     221.296 208.668 157.890  1.00 18.60           N  
ATOM  19721  CA  ILE C 909     221.802 209.918 158.438  1.00 18.32           C  
ATOM  19722  C   ILE C 909     222.059 210.926 157.331  1.00 18.68           C  
ATOM  19723  O   ILE C 909     222.710 211.946 157.551  1.00 18.99           O  
ATOM  19724  CB  ILE C 909     223.089 209.727 159.258  1.00 18.21           C  
ATOM  19725  CG1 ILE C 909     224.194 209.167 158.394  1.00 18.62           C  
ATOM  19726  CG2 ILE C 909     222.808 208.789 160.416  1.00 18.85           C  
ATOM  19727  CD1 ILE C 909     225.562 209.258 159.003  1.00 18.87           C  
ATOM  19728  N   GLY C 910     221.549 210.642 156.138  1.00 18.78           N  
ATOM  19729  CA  GLY C 910     221.689 211.559 155.021  1.00 18.71           C  
ATOM  19730  C   GLY C 910     222.997 211.442 154.251  1.00 18.79           C  
ATOM  19731  O   GLY C 910     223.399 212.392 153.585  1.00 19.20           O  
ATOM  19732  N   VAL C 911     223.678 210.306 154.345  1.00 18.73           N  
ATOM  19733  CA  VAL C 911     224.910 210.119 153.598  1.00 18.64           C  
ATOM  19734  C   VAL C 911     224.703 208.962 152.642  1.00 19.33           C  
ATOM  19735  O   VAL C 911     224.443 207.843 153.067  1.00 20.09           O  
ATOM  19736  CB  VAL C 911     226.088 209.840 154.541  1.00 18.72           C  
ATOM  19737  CG1 VAL C 911     227.357 209.611 153.751  1.00 19.09           C  
ATOM  19738  CG2 VAL C 911     226.274 211.013 155.475  1.00 19.17           C  
ATOM  19739  N   THR C 912     224.807 209.227 151.354  1.00 19.46           N  
ATOM  19740  CA  THR C 912     224.495 208.228 150.352  1.00 19.42           C  
ATOM  19741  C   THR C 912     225.387 207.009 150.500  1.00 20.16           C  
ATOM  19742  O   THR C 912     226.606 207.131 150.598  1.00 20.28           O  
ATOM  19743  CB  THR C 912     224.605 208.823 148.942  1.00 19.85           C  
ATOM  19744  OG1 THR C 912     223.729 209.947 148.836  1.00 20.36           O  
ATOM  19745  CG2 THR C 912     224.216 207.813 147.892  1.00 20.72           C  
ATOM  19746  N   GLN C 913     224.764 205.838 150.436  1.00 19.75           N  
ATOM  19747  CA  GLN C 913     225.390 204.530 150.601  1.00 19.60           C  
ATOM  19748  C   GLN C 913     226.655 204.273 149.803  1.00 20.32           C  
ATOM  19749  O   GLN C 913     227.447 203.410 150.175  1.00 21.27           O  
ATOM  19750  CB  GLN C 913     224.397 203.450 150.211  1.00 20.23           C  
ATOM  19751  CG  GLN C 913     224.045 203.481 148.756  1.00 20.79           C  
ATOM  19752  CD  GLN C 913     222.937 202.560 148.397  1.00 21.51           C  
ATOM  19753  OE1 GLN C 913     223.031 201.340 148.530  1.00 21.55           O  
ATOM  19754  NE2 GLN C 913     221.859 203.146 147.908  1.00 21.87           N  
ATOM  19755  N   ASN C 914     226.863 204.980 148.706  1.00 20.27           N  
ATOM  19756  CA  ASN C 914     228.054 204.700 147.930  1.00 20.21           C  
ATOM  19757  C   ASN C 914     229.284 205.124 148.712  1.00 20.93           C  
ATOM  19758  O   ASN C 914     230.378 204.629 148.465  1.00 20.70           O  
ATOM  19759  CB  ASN C 914     228.035 205.399 146.602  1.00 20.54           C  
ATOM  19760  CG  ASN C 914     228.111 206.837 146.765  1.00 20.32           C  
ATOM  19761  OD1 ASN C 914     227.178 207.454 147.278  1.00 20.73           O  
ATOM  19762  ND2 ASN C 914     229.209 207.407 146.367  1.00 20.51           N  
ATOM  19763  N   VAL C 915     229.099 206.037 149.667  1.00 20.45           N  
ATOM  19764  CA  VAL C 915     230.200 206.526 150.472  1.00 19.96           C  
ATOM  19765  C   VAL C 915     230.738 205.392 151.303  1.00 21.17           C  
ATOM  19766  O   VAL C 915     231.947 205.239 151.441  1.00 21.66           O  
ATOM  19767  CB  VAL C 915     229.766 207.691 151.371  1.00 20.03           C  
ATOM  19768  CG1 VAL C 915     230.888 208.071 152.347  1.00 20.46           C  
ATOM  19769  CG2 VAL C 915     229.412 208.871 150.496  1.00 20.11           C  
ATOM  19770  N   LEU C 916     229.835 204.594 151.852  1.00 20.41           N  
ATOM  19771  CA  LEU C 916     230.251 203.461 152.649  1.00 20.51           C  
ATOM  19772  C   LEU C 916     231.069 202.497 151.849  1.00 21.76           C  
ATOM  19773  O   LEU C 916     232.145 202.089 152.275  1.00 21.93           O  
ATOM  19774  CB  LEU C 916     229.045 202.695 153.164  1.00 20.70           C  
ATOM  19775  CG  LEU C 916     229.340 201.327 153.806  1.00 20.74           C  
ATOM  19776  CD1 LEU C 916     230.181 201.462 155.030  1.00 21.53           C  
ATOM  19777  CD2 LEU C 916     228.088 200.706 154.121  1.00 20.84           C  
ATOM  19778  N   TYR C 917     230.580 202.110 150.690  1.00 21.13           N  
ATOM  19779  CA  TYR C 917     231.275 201.081 149.955  1.00 20.72           C  
ATOM  19780  C   TYR C 917     232.620 201.565 149.459  1.00 20.70           C  
ATOM  19781  O   TYR C 917     233.621 200.861 149.563  1.00 21.63           O  
ATOM  19782  CB  TYR C 917     230.412 200.599 148.809  1.00 21.28           C  
ATOM  19783  CG  TYR C 917     229.172 199.929 149.296  1.00 21.00           C  
ATOM  19784  CD1 TYR C 917     227.946 200.500 149.054  1.00 20.84           C  
ATOM  19785  CD2 TYR C 917     229.254 198.758 150.005  1.00 20.93           C  
ATOM  19786  CE1 TYR C 917     226.808 199.898 149.502  1.00 20.88           C  
ATOM  19787  CE2 TYR C 917     228.114 198.162 150.459  1.00 20.83           C  
ATOM  19788  CZ  TYR C 917     226.898 198.726 150.204  1.00 20.88           C  
ATOM  19789  OH  TYR C 917     225.764 198.116 150.648  1.00 21.18           O  
ATOM  19790  N   GLU C 918     232.670 202.796 148.985  1.00 20.92           N  
ATOM  19791  CA  GLU C 918     233.916 203.330 148.473  1.00 20.84           C  
ATOM  19792  C   GLU C 918     234.952 203.448 149.579  1.00 21.32           C  
ATOM  19793  O   GLU C 918     236.147 203.252 149.348  1.00 21.79           O  
ATOM  19794  CB  GLU C 918     233.672 204.666 147.785  1.00 20.95           C  
ATOM  19795  CG  GLU C 918     232.866 204.531 146.489  1.00 20.60           C  
ATOM  19796  CD  GLU C 918     232.482 205.839 145.876  1.00 20.87           C  
ATOM  19797  OE1 GLU C 918     233.062 206.833 146.230  1.00 20.34           O  
ATOM  19798  OE2 GLU C 918     231.581 205.847 145.064  1.00 21.04           O  
ATOM  19799  N   ASN C 919     234.495 203.745 150.787  1.00 21.25           N  
ATOM  19800  CA  ASN C 919     235.366 203.890 151.936  1.00 20.83           C  
ATOM  19801  C   ASN C 919     235.209 202.748 152.933  1.00 21.89           C  
ATOM  19802  O   ASN C 919     235.548 202.902 154.104  1.00 22.52           O  
ATOM  19803  CB  ASN C 919     235.085 205.207 152.624  1.00 21.03           C  
ATOM  19804  CG  ASN C 919     235.441 206.369 151.787  1.00 21.20           C  
ATOM  19805  OD1 ASN C 919     236.620 206.695 151.604  1.00 21.87           O  
ATOM  19806  ND2 ASN C 919     234.444 207.014 151.249  1.00 21.01           N  
ATOM  19807  N   GLN C 920     234.722 201.592 152.499  1.00 21.52           N  
ATOM  19808  CA  GLN C 920     234.460 200.521 153.456  1.00 20.99           C  
ATOM  19809  C   GLN C 920     235.674 200.113 154.267  1.00 21.53           C  
ATOM  19810  O   GLN C 920     235.548 199.805 155.451  1.00 22.27           O  
ATOM  19811  CB  GLN C 920     233.894 199.293 152.762  1.00 21.47           C  
ATOM  19812  CG  GLN C 920     233.513 198.173 153.710  1.00 21.53           C  
ATOM  19813  CD  GLN C 920     232.802 197.067 153.003  1.00 21.83           C  
ATOM  19814  OE1 GLN C 920     232.182 197.291 151.962  1.00 21.89           O  
ATOM  19815  NE2 GLN C 920     232.877 195.865 153.548  1.00 22.04           N  
ATOM  19816  N   LYS C 921     236.850 200.080 153.654  1.00 21.72           N  
ATOM  19817  CA  LYS C 921     238.033 199.677 154.405  1.00 21.71           C  
ATOM  19818  C   LYS C 921     238.375 200.713 155.464  1.00 22.03           C  
ATOM  19819  O   LYS C 921     238.759 200.369 156.581  1.00 22.60           O  
ATOM  19820  CB  LYS C 921     239.221 199.449 153.482  1.00 21.90           C  
ATOM  19821  CG  LYS C 921     239.102 198.209 152.617  1.00 21.82           C  
ATOM  19822  CD  LYS C 921     240.321 198.039 151.726  1.00 21.25           C  
ATOM  19823  CE  LYS C 921     240.214 196.788 150.866  1.00 20.49           C  
ATOM  19824  NZ  LYS C 921     241.395 196.626 149.973  1.00 21.56           N  
ATOM  19825  N   LEU C 922     238.223 201.984 155.118  1.00 21.93           N  
ATOM  19826  CA  LEU C 922     238.510 203.058 156.052  1.00 21.41           C  
ATOM  19827  C   LEU C 922     237.555 203.017 157.221  1.00 23.10           C  
ATOM  19828  O   LEU C 922     237.959 203.171 158.371  1.00 21.98           O  
ATOM  19829  CB  LEU C 922     238.382 204.415 155.359  1.00 21.71           C  
ATOM  19830  CG  LEU C 922     238.571 205.664 156.246  1.00 21.85           C  
ATOM  19831  CD1 LEU C 922     239.979 205.691 156.838  1.00 22.53           C  
ATOM  19832  CD2 LEU C 922     238.293 206.906 155.406  1.00 21.72           C  
ATOM  19833  N   ILE C 923     236.283 202.811 156.923  1.00 21.85           N  
ATOM  19834  CA  ILE C 923     235.256 202.803 157.941  1.00 21.16           C  
ATOM  19835  C   ILE C 923     235.454 201.647 158.892  1.00 22.68           C  
ATOM  19836  O   ILE C 923     235.369 201.824 160.107  1.00 22.90           O  
ATOM  19837  CB  ILE C 923     233.874 202.746 157.289  1.00 21.67           C  
ATOM  19838  CG1 ILE C 923     233.640 204.043 156.568  1.00 21.24           C  
ATOM  19839  CG2 ILE C 923     232.805 202.529 158.339  1.00 21.91           C  
ATOM  19840  CD1 ILE C 923     232.526 204.029 155.595  1.00 21.35           C  
ATOM  19841  N   ALA C 924     235.712 200.463 158.356  1.00 22.34           N  
ATOM  19842  CA  ALA C 924     235.932 199.314 159.208  1.00 22.33           C  
ATOM  19843  C   ALA C 924     237.158 199.522 160.081  1.00 23.17           C  
ATOM  19844  O   ALA C 924     237.143 199.176 161.262  1.00 23.74           O  
ATOM  19845  CB  ALA C 924     236.088 198.063 158.375  1.00 23.01           C  
ATOM  19846  N   ASN C 925     238.211 200.127 159.532  1.00 22.65           N  
ATOM  19847  CA  ASN C 925     239.412 200.345 160.322  1.00 22.49           C  
ATOM  19848  C   ASN C 925     239.186 201.364 161.423  1.00 23.03           C  
ATOM  19849  O   ASN C 925     239.664 201.177 162.544  1.00 24.45           O  
ATOM  19850  CB  ASN C 925     240.559 200.776 159.441  1.00 22.54           C  
ATOM  19851  CG  ASN C 925     241.106 199.656 158.628  1.00 22.65           C  
ATOM  19852  OD1 ASN C 925     240.988 198.480 158.988  1.00 22.58           O  
ATOM  19853  ND2 ASN C 925     241.717 199.990 157.525  1.00 22.76           N  
ATOM  19854  N   GLN C 926     238.428 202.418 161.135  1.00 22.53           N  
ATOM  19855  CA  GLN C 926     238.149 203.415 162.155  1.00 22.35           C  
ATOM  19856  C   GLN C 926     237.320 202.806 163.268  1.00 23.53           C  
ATOM  19857  O   GLN C 926     237.560 203.070 164.447  1.00 24.18           O  
ATOM  19858  CB  GLN C 926     237.417 204.615 161.564  1.00 21.82           C  
ATOM  19859  CG  GLN C 926     238.257 205.493 160.657  1.00 21.64           C  
ATOM  19860  CD  GLN C 926     237.417 206.551 160.005  1.00 20.86           C  
ATOM  19861  OE1 GLN C 926     236.196 206.405 159.962  1.00 21.30           O  
ATOM  19862  NE2 GLN C 926     238.038 207.614 159.516  1.00 21.07           N  
ATOM  19863  N   PHE C 927     236.366 201.961 162.903  1.00 23.21           N  
ATOM  19864  CA  PHE C 927     235.547 201.292 163.893  1.00 23.01           C  
ATOM  19865  C   PHE C 927     236.390 200.409 164.791  1.00 25.91           C  
ATOM  19866  O   PHE C 927     236.254 200.441 166.016  1.00 24.36           O  
ATOM  19867  CB  PHE C 927     234.463 200.454 163.239  1.00 23.44           C  
ATOM  19868  CG  PHE C 927     233.697 199.677 164.227  1.00 23.71           C  
ATOM  19869  CD1 PHE C 927     232.747 200.281 165.002  1.00 23.58           C  
ATOM  19870  CD2 PHE C 927     233.937 198.334 164.399  1.00 24.25           C  
ATOM  19871  CE1 PHE C 927     232.053 199.560 165.934  1.00 23.63           C  
ATOM  19872  CE2 PHE C 927     233.248 197.611 165.325  1.00 24.30           C  
ATOM  19873  CZ  PHE C 927     232.303 198.228 166.098  1.00 23.70           C  
ATOM  19874  N   ASN C 928     237.252 199.601 164.184  1.00 23.80           N  
ATOM  19875  CA  ASN C 928     238.055 198.657 164.932  1.00 23.91           C  
ATOM  19876  C   ASN C 928     238.985 199.383 165.891  1.00 24.67           C  
ATOM  19877  O   ASN C 928     239.180 198.948 167.031  1.00 25.50           O  
ATOM  19878  CB  ASN C 928     238.843 197.806 163.966  1.00 24.21           C  
ATOM  19879  CG  ASN C 928     237.943 196.931 163.176  1.00 24.32           C  
ATOM  19880  OD1 ASN C 928     236.810 196.690 163.591  1.00 24.77           O  
ATOM  19881  ND2 ASN C 928     238.398 196.466 162.045  1.00 24.31           N  
ATOM  19882  N   SER C 929     239.528 200.511 165.447  1.00 24.54           N  
ATOM  19883  CA  SER C 929     240.400 201.307 166.290  1.00 25.02           C  
ATOM  19884  C   SER C 929     239.630 201.866 167.470  1.00 25.30           C  
ATOM  19885  O   SER C 929     240.092 201.798 168.612  1.00 26.77           O  
ATOM  19886  CB  SER C 929     241.010 202.436 165.498  1.00 25.14           C  
ATOM  19887  OG  SER C 929     241.862 203.205 166.298  1.00 26.17           O  
ATOM  19888  N   ALA C 930     238.436 202.393 167.203  1.00 25.09           N  
ATOM  19889  CA  ALA C 930     237.624 202.985 168.249  1.00 25.17           C  
ATOM  19890  C   ALA C 930     237.305 201.981 169.346  1.00 25.95           C  
ATOM  19891  O   ALA C 930     237.323 202.329 170.526  1.00 26.92           O  
ATOM  19892  CB  ALA C 930     236.342 203.532 167.661  1.00 24.49           C  
ATOM  19893  N   ILE C 931     237.043 200.730 168.986  1.00 25.51           N  
ATOM  19894  CA  ILE C 931     236.751 199.752 170.024  1.00 25.75           C  
ATOM  19895  C   ILE C 931     237.980 199.537 170.892  1.00 26.55           C  
ATOM  19896  O   ILE C 931     237.877 199.512 172.120  1.00 27.98           O  
ATOM  19897  CB  ILE C 931     236.266 198.409 169.449  1.00 25.87           C  
ATOM  19898  CG1 ILE C 931     234.910 198.586 168.699  1.00 25.23           C  
ATOM  19899  CG2 ILE C 931     236.135 197.366 170.573  1.00 27.26           C  
ATOM  19900  CD1 ILE C 931     233.737 199.079 169.547  1.00 25.73           C  
ATOM  19901  N   GLY C 932     239.151 199.431 170.276  1.00 26.28           N  
ATOM  19902  CA  GLY C 932     240.370 199.266 171.057  1.00 26.77           C  
ATOM  19903  C   GLY C 932     240.546 200.421 172.045  1.00 27.18           C  
ATOM  19904  O   GLY C 932     241.015 200.226 173.168  1.00 28.35           O  
ATOM  19905  N   LYS C 933     240.154 201.624 171.635  1.00 27.01           N  
ATOM  19906  CA  LYS C 933     240.249 202.782 172.514  1.00 26.97           C  
ATOM  19907  C   LYS C 933     239.324 202.646 173.716  1.00 27.60           C  
ATOM  19908  O   LYS C 933     239.666 203.089 174.815  1.00 29.02           O  
ATOM  19909  CB  LYS C 933     239.958 204.072 171.760  1.00 27.03           C  
ATOM  19910  CG  LYS C 933     241.043 204.462 170.780  1.00 27.13           C  
ATOM  19911  CD  LYS C 933     240.699 205.743 170.052  1.00 27.26           C  
ATOM  19912  CE  LYS C 933     241.781 206.109 169.049  1.00 27.83           C  
ATOM  19913  NZ  LYS C 933     241.450 207.356 168.307  1.00 28.15           N  
ATOM  19914  N   ILE C 934     238.163 202.021 173.523  1.00 27.36           N  
ATOM  19915  CA  ILE C 934     237.227 201.832 174.624  1.00 27.45           C  
ATOM  19916  C   ILE C 934     237.858 200.944 175.674  1.00 29.12           C  
ATOM  19917  O   ILE C 934     237.731 201.204 176.872  1.00 28.95           O  
ATOM  19918  CB  ILE C 934     235.899 201.184 174.171  1.00 27.42           C  
ATOM  19919  CG1 ILE C 934     235.142 202.091 173.175  1.00 26.52           C  
ATOM  19920  CG2 ILE C 934     235.025 200.845 175.381  1.00 27.92           C  
ATOM  19921  CD1 ILE C 934     234.796 203.478 173.671  1.00 25.67           C  
ATOM  19922  N   GLN C 935     238.542 199.898 175.233  1.00 28.13           N  
ATOM  19923  CA  GLN C 935     239.170 198.992 176.178  1.00 28.40           C  
ATOM  19924  C   GLN C 935     240.230 199.695 177.002  1.00 29.20           C  
ATOM  19925  O   GLN C 935     240.303 199.501 178.218  1.00 29.96           O  
ATOM  19926  CB  GLN C 935     239.822 197.830 175.451  1.00 28.68           C  
ATOM  19927  CG  GLN C 935     238.863 196.903 174.823  1.00 28.68           C  
ATOM  19928  CD  GLN C 935     239.552 195.833 174.076  1.00 29.15           C  
ATOM  19929  OE1 GLN C 935     240.688 195.986 173.624  1.00 29.17           O  
ATOM  19930  NE2 GLN C 935     238.884 194.726 173.945  1.00 29.35           N  
ATOM  19931  N   ASP C 936     241.021 200.549 176.361  1.00 28.49           N  
ATOM  19932  CA  ASP C 936     242.066 201.258 177.080  1.00 29.03           C  
ATOM  19933  C   ASP C 936     241.478 202.250 178.063  1.00 29.82           C  
ATOM  19934  O   ASP C 936     241.994 202.414 179.171  1.00 29.93           O  
ATOM  19935  CB  ASP C 936     242.985 201.989 176.108  1.00 29.08           C  
ATOM  19936  CG  ASP C 936     243.889 201.053 175.322  1.00 29.29           C  
ATOM  19937  OD1 ASP C 936     244.033 199.915 175.704  1.00 29.09           O  
ATOM  19938  OD2 ASP C 936     244.436 201.493 174.343  1.00 28.90           O  
ATOM  19939  N   SER C 937     240.391 202.904 177.677  1.00 28.88           N  
ATOM  19940  CA  SER C 937     239.750 203.866 178.555  1.00 29.43           C  
ATOM  19941  C   SER C 937     239.206 203.185 179.799  1.00 30.44           C  
ATOM  19942  O   SER C 937     239.421 203.655 180.918  1.00 30.45           O  
ATOM  19943  CB  SER C 937     238.629 204.575 177.828  1.00 29.23           C  
ATOM  19944  OG  SER C 937     237.990 205.494 178.666  1.00 30.30           O  
ATOM  19945  N   LEU C 938     238.520 202.062 179.613  1.00 30.53           N  
ATOM  19946  CA  LEU C 938     237.938 201.353 180.740  1.00 30.17           C  
ATOM  19947  C   LEU C 938     238.999 200.753 181.644  1.00 30.22           C  
ATOM  19948  O   LEU C 938     238.834 200.732 182.864  1.00 30.45           O  
ATOM  19949  CB  LEU C 938     237.010 200.241 180.246  1.00 29.89           C  
ATOM  19950  CG  LEU C 938     235.708 200.677 179.554  1.00 30.16           C  
ATOM  19951  CD1 LEU C 938     235.045 199.445 178.988  1.00 30.15           C  
ATOM  19952  CD2 LEU C 938     234.787 201.380 180.547  1.00 29.81           C  
ATOM  19953  N   SER C 939     240.088 200.264 181.057  1.00 30.30           N  
ATOM  19954  CA  SER C 939     241.146 199.657 181.846  1.00 30.45           C  
ATOM  19955  C   SER C 939     241.908 200.701 182.654  1.00 30.73           C  
ATOM  19956  O   SER C 939     242.256 200.468 183.813  1.00 31.23           O  
ATOM  19957  CB  SER C 939     242.116 198.922 180.941  1.00 30.56           C  
ATOM  19958  OG  SER C 939     241.497 197.847 180.306  1.00 30.47           O  
ATOM  19959  N   SER C 940     242.161 201.855 182.041  1.00 30.19           N  
ATOM  19960  CA  SER C 940     242.934 202.917 182.666  1.00 30.65           C  
ATOM  19961  C   SER C 940     242.215 203.631 183.799  1.00 30.83           C  
ATOM  19962  O   SER C 940     242.790 203.824 184.873  1.00 30.60           O  
ATOM  19963  CB  SER C 940     243.334 203.935 181.621  1.00 30.64           C  
ATOM  19964  N   THR C 941     240.972 204.047 183.576  1.00 29.91           N  
ATOM  19965  CA  THR C 941     240.289 204.822 184.601  1.00 30.41           C  
ATOM  19966  C   THR C 941     239.012 204.159 185.122  1.00 30.97           C  
ATOM  19967  O   THR C 941     237.993 204.067 184.438  1.00 29.72           O  
ATOM  19968  CB  THR C 941     240.003 206.248 184.087  1.00 29.98           C  
ATOM  19969  OG1 THR C 941     239.164 206.918 185.015  1.00 30.01           O  
ATOM  19970  CG2 THR C 941     239.346 206.225 182.719  1.00 30.09           C  
ATOM  19971  N   ALA C 942     239.065 203.733 186.385  1.00 30.13           N  
ATOM  19972  CA  ALA C 942     237.945 203.046 187.033  1.00 30.37           C  
ATOM  19973  C   ALA C 942     236.731 203.958 187.151  1.00 30.17           C  
ATOM  19974  O   ALA C 942     235.589 203.502 187.069  1.00 30.01           O  
ATOM  19975  CB  ALA C 942     238.358 202.545 188.408  1.00 30.62           C  
ATOM  19976  N   SER C 943     236.985 205.258 187.304  1.00 30.02           N  
ATOM  19977  CA  SER C 943     235.941 206.262 187.481  1.00 29.93           C  
ATOM  19978  C   SER C 943     235.029 206.373 186.264  1.00 30.29           C  
ATOM  19979  O   SER C 943     233.969 207.000 186.329  1.00 29.97           O  
ATOM  19980  CB  SER C 943     236.551 207.610 187.817  1.00 29.98           C  
ATOM  19981  OG  SER C 943     237.309 208.107 186.758  1.00 29.85           O  
ATOM  19982  N   ALA C 944     235.411 205.736 185.160  1.00 29.65           N  
ATOM  19983  CA  ALA C 944     234.587 205.717 183.963  1.00 30.02           C  
ATOM  19984  C   ALA C 944     233.205 205.158 184.286  1.00 29.75           C  
ATOM  19985  O   ALA C 944     232.219 205.535 183.659  1.00 29.21           O  
ATOM  19986  CB  ALA C 944     235.246 204.877 182.881  1.00 30.16           C  
ATOM  19987  N   LEU C 945     233.135 204.254 185.267  1.00 29.51           N  
ATOM  19988  CA  LEU C 945     231.886 203.619 185.671  1.00 29.10           C  
ATOM  19989  C   LEU C 945     231.404 204.161 187.003  1.00 29.17           C  
ATOM  19990  O   LEU C 945     230.653 203.497 187.724  1.00 29.59           O  
ATOM  19991  CB  LEU C 945     232.062 202.101 185.773  1.00 29.12           C  
ATOM  19992  CG  LEU C 945     231.748 201.292 184.520  1.00 28.77           C  
ATOM  19993  CD1 LEU C 945     232.646 201.720 183.375  1.00 29.43           C  
ATOM  19994  CD2 LEU C 945     231.941 199.826 184.839  1.00 29.63           C  
ATOM  19995  N   GLY C 946     231.790 205.394 187.305  1.00 29.26           N  
ATOM  19996  CA  GLY C 946     231.444 206.030 188.564  1.00 29.17           C  
ATOM  19997  C   GLY C 946     229.952 206.001 188.849  1.00 28.75           C  
ATOM  19998  O   GLY C 946     229.551 205.926 190.006  1.00 29.04           O  
ATOM  19999  N   LYS C 947     229.119 206.056 187.820  1.00 28.76           N  
ATOM  20000  CA  LYS C 947     227.683 206.028 188.048  1.00 28.76           C  
ATOM  20001  C   LYS C 947     227.227 204.737 188.718  1.00 28.36           C  
ATOM  20002  O   LYS C 947     226.312 204.758 189.543  1.00 28.66           O  
ATOM  20003  CB  LYS C 947     226.929 206.231 186.740  1.00 28.30           C  
ATOM  20004  CG  LYS C 947     227.034 207.638 186.193  1.00 28.71           C  
ATOM  20005  CD  LYS C 947     226.273 207.794 184.894  1.00 27.76           C  
ATOM  20006  CE  LYS C 947     226.380 209.217 184.362  1.00 28.54           C  
ATOM  20007  NZ  LYS C 947     225.609 209.405 183.101  1.00 28.08           N  
ATOM  20008  N   LEU C 948     227.849 203.613 188.373  1.00 28.31           N  
ATOM  20009  CA  LEU C 948     227.420 202.346 188.943  1.00 28.47           C  
ATOM  20010  C   LEU C 948     228.033 202.184 190.312  1.00 29.15           C  
ATOM  20011  O   LEU C 948     227.408 201.645 191.229  1.00 29.17           O  
ATOM  20012  CB  LEU C 948     227.843 201.176 188.053  1.00 28.47           C  
ATOM  20013  CG  LEU C 948     227.242 201.146 186.653  1.00 27.73           C  
ATOM  20014  CD1 LEU C 948     227.873 200.005 185.868  1.00 27.96           C  
ATOM  20015  CD2 LEU C 948     225.737 200.971 186.718  1.00 26.63           C  
ATOM  20016  N   GLN C 949     229.252 202.683 190.463  1.00 29.07           N  
ATOM  20017  CA  GLN C 949     229.919 202.600 191.745  1.00 28.26           C  
ATOM  20018  C   GLN C 949     229.200 203.472 192.754  1.00 33.09           C  
ATOM  20019  O   GLN C 949     229.104 203.114 193.925  1.00 26.86           O  
ATOM  20020  CB  GLN C 949     231.382 203.009 191.636  1.00 29.57           C  
ATOM  20021  CG  GLN C 949     232.165 202.847 192.926  1.00 30.23           C  
ATOM  20022  CD  GLN C 949     232.246 201.406 193.394  1.00 30.66           C  
ATOM  20023  OE1 GLN C 949     232.587 200.517 192.607  1.00 30.87           O  
ATOM  20024  NE2 GLN C 949     231.950 201.172 194.666  1.00 30.74           N  
ATOM  20025  N   ASP C 950     228.674 204.604 192.299  1.00 29.51           N  
ATOM  20026  CA  ASP C 950     227.957 205.517 193.170  1.00 27.93           C  
ATOM  20027  C   ASP C 950     226.684 204.882 193.699  1.00 33.59           C  
ATOM  20028  O   ASP C 950     226.359 205.038 194.875  1.00 27.06           O  
ATOM  20029  CB  ASP C 950     227.620 206.810 192.440  1.00 28.64           C  
ATOM  20030  CG  ASP C 950     226.990 207.835 193.349  1.00 28.46           C  
ATOM  20031  OD1 ASP C 950     227.652 208.315 194.237  1.00 28.52           O  
ATOM  20032  OD2 ASP C 950     225.838 208.125 193.158  1.00 28.60           O  
ATOM  20033  N   VAL C 951     225.983 204.124 192.863  1.00 27.92           N  
ATOM  20034  CA  VAL C 951     224.782 203.455 193.337  1.00 28.22           C  
ATOM  20035  C   VAL C 951     225.142 202.463 194.424  1.00 28.97           C  
ATOM  20036  O   VAL C 951     224.469 202.387 195.456  1.00 29.86           O  
ATOM  20037  CB  VAL C 951     224.059 202.741 192.190  1.00 28.70           C  
ATOM  20038  CG1 VAL C 951     222.920 201.875 192.729  1.00 28.73           C  
ATOM  20039  CG2 VAL C 951     223.528 203.775 191.248  1.00 28.68           C  
ATOM  20040  N   VAL C 952     226.220 201.721 194.206  1.00 28.93           N  
ATOM  20041  CA  VAL C 952     226.678 200.764 195.193  1.00 28.65           C  
ATOM  20042  C   VAL C 952     227.077 201.464 196.484  1.00 29.05           C  
ATOM  20043  O   VAL C 952     226.744 200.995 197.574  1.00 30.46           O  
ATOM  20044  CB  VAL C 952     227.873 199.963 194.649  1.00 29.70           C  
ATOM  20045  CG1 VAL C 952     228.492 199.115 195.746  1.00 30.36           C  
ATOM  20046  CG2 VAL C 952     227.405 199.082 193.507  1.00 29.58           C  
ATOM  20047  N   ASN C 953     227.791 202.578 196.367  1.00 28.65           N  
ATOM  20048  CA  ASN C 953     228.242 203.300 197.541  1.00 28.33           C  
ATOM  20049  C   ASN C 953     227.079 203.851 198.347  1.00 29.42           C  
ATOM  20050  O   ASN C 953     227.099 203.790 199.577  1.00 30.09           O  
ATOM  20051  CB  ASN C 953     229.146 204.446 197.150  1.00 29.14           C  
ATOM  20052  CG  ASN C 953     230.479 204.017 196.636  1.00 29.62           C  
ATOM  20053  OD1 ASN C 953     230.931 202.883 196.821  1.00 30.27           O  
ATOM  20054  ND2 ASN C 953     231.148 204.931 195.987  1.00 30.49           N  
ATOM  20055  N   GLN C 954     226.058 204.383 197.677  1.00 28.87           N  
ATOM  20056  CA  GLN C 954     224.937 204.942 198.414  1.00 27.76           C  
ATOM  20057  C   GLN C 954     224.149 203.869 199.136  1.00 30.59           C  
ATOM  20058  O   GLN C 954     223.696 204.085 200.261  1.00 29.43           O  
ATOM  20059  CB  GLN C 954     223.987 205.722 197.511  1.00 27.89           C  
ATOM  20060  CG  GLN C 954     224.523 207.037 196.968  1.00 27.51           C  
ATOM  20061  CD  GLN C 954     223.443 207.803 196.204  1.00 27.66           C  
ATOM  20062  OE1 GLN C 954     222.302 207.895 196.680  1.00 27.12           O  
ATOM  20063  NE2 GLN C 954     223.769 208.349 195.041  1.00 27.55           N  
ATOM  20064  N   ASN C 955     223.984 202.711 198.512  1.00 28.41           N  
ATOM  20065  CA  ASN C 955     223.222 201.660 199.159  1.00 28.93           C  
ATOM  20066  C   ASN C 955     223.994 201.089 200.340  1.00 29.62           C  
ATOM  20067  O   ASN C 955     223.418 200.807 201.394  1.00 30.78           O  
ATOM  20068  CB  ASN C 955     222.872 200.586 198.158  1.00 29.44           C  
ATOM  20069  CG  ASN C 955     221.813 201.042 197.203  1.00 29.09           C  
ATOM  20070  OD1 ASN C 955     220.988 201.895 197.536  1.00 28.87           O  
ATOM  20071  ND2 ASN C 955     221.826 200.502 196.016  1.00 28.83           N  
ATOM  20072  N   ALA C 956     225.308 200.956 200.187  1.00 29.64           N  
ATOM  20073  CA  ALA C 956     226.128 200.450 201.270  1.00 29.81           C  
ATOM  20074  C   ALA C 956     226.127 201.419 202.438  1.00 29.86           C  
ATOM  20075  O   ALA C 956     226.042 201.004 203.595  1.00 31.45           O  
ATOM  20076  CB  ALA C 956     227.544 200.216 200.788  1.00 30.72           C  
ATOM  20077  N   GLN C 957     226.180 202.713 202.138  1.00 29.50           N  
ATOM  20078  CA  GLN C 957     226.186 203.719 203.181  1.00 29.73           C  
ATOM  20079  C   GLN C 957     224.860 203.738 203.913  1.00 32.05           C  
ATOM  20080  O   GLN C 957     224.824 203.920 205.131  1.00 31.80           O  
ATOM  20081  CB  GLN C 957     226.472 205.100 202.597  1.00 29.88           C  
ATOM  20082  CG  GLN C 957     226.641 206.200 203.635  1.00 30.50           C  
ATOM  20083  CD  GLN C 957     227.848 205.984 204.523  1.00 31.15           C  
ATOM  20084  OE1 GLN C 957     228.960 205.797 204.030  1.00 31.09           O  
ATOM  20085  NE2 GLN C 957     227.643 206.008 205.836  1.00 31.45           N  
ATOM  20086  N   ALA C 958     223.766 203.536 203.184  1.00 30.26           N  
ATOM  20087  CA  ALA C 958     222.451 203.543 203.800  1.00 30.31           C  
ATOM  20088  C   ALA C 958     222.348 202.456 204.856  1.00 30.75           C  
ATOM  20089  O   ALA C 958     221.760 202.674 205.918  1.00 32.38           O  
ATOM  20090  CB  ALA C 958     221.374 203.350 202.749  1.00 30.34           C  
ATOM  20091  N   LEU C 959     222.931 201.292 204.584  1.00 30.76           N  
ATOM  20092  CA  LEU C 959     222.881 200.220 205.562  1.00 30.74           C  
ATOM  20093  C   LEU C 959     223.888 200.395 206.670  1.00 32.16           C  
ATOM  20094  O   LEU C 959     223.598 200.072 207.821  1.00 33.38           O  
ATOM  20095  CB  LEU C 959     223.068 198.864 204.899  1.00 30.70           C  
ATOM  20096  CG  LEU C 959     221.927 198.412 204.002  1.00 31.28           C  
ATOM  20097  CD1 LEU C 959     222.314 197.109 203.332  1.00 31.85           C  
ATOM  20098  CD2 LEU C 959     220.654 198.235 204.839  1.00 32.01           C  
ATOM  20099  N   ASN C 960     225.053 200.948 206.375  1.00 31.80           N  
ATOM  20100  CA  ASN C 960     225.988 201.159 207.461  1.00 31.67           C  
ATOM  20101  C   ASN C 960     225.388 202.152 208.438  1.00 32.69           C  
ATOM  20102  O   ASN C 960     225.544 202.006 209.649  1.00 34.35           O  
ATOM  20103  CB  ASN C 960     227.329 201.633 206.951  1.00 31.66           C  
ATOM  20104  CG  ASN C 960     228.106 200.534 206.302  1.00 32.21           C  
ATOM  20105  OD1 ASN C 960     227.857 199.348 206.543  1.00 32.72           O  
ATOM  20106  ND2 ASN C 960     229.052 200.898 205.479  1.00 31.94           N  
ATOM  20107  N   THR C 961     224.658 203.136 207.920  1.00 31.98           N  
ATOM  20108  CA  THR C 961     224.023 204.116 208.780  1.00 32.35           C  
ATOM  20109  C   THR C 961     222.958 203.435 209.622  1.00 32.28           C  
ATOM  20110  O   THR C 961     222.884 203.651 210.832  1.00 34.28           O  
ATOM  20111  CB  THR C 961     223.376 205.253 207.963  1.00 32.60           C  
ATOM  20112  OG1 THR C 961     224.374 205.906 207.161  1.00 32.14           O  
ATOM  20113  CG2 THR C 961     222.743 206.281 208.905  1.00 33.12           C  
ATOM  20114  N   LEU C 962     222.149 202.588 208.990  1.00 32.38           N  
ATOM  20115  CA  LEU C 962     221.074 201.909 209.688  1.00 32.49           C  
ATOM  20116  C   LEU C 962     221.598 201.044 210.820  1.00 34.05           C  
ATOM  20117  O   LEU C 962     221.061 201.067 211.922  1.00 35.56           O  
ATOM  20118  CB  LEU C 962     220.290 201.027 208.703  1.00 32.36           C  
ATOM  20119  CG  LEU C 962     219.114 200.227 209.275  1.00 32.71           C  
ATOM  20120  CD1 LEU C 962     218.055 201.180 209.810  1.00 33.15           C  
ATOM  20121  CD2 LEU C 962     218.540 199.323 208.189  1.00 32.72           C  
ATOM  20122  N   VAL C 963     222.658 200.289 210.570  1.00 33.50           N  
ATOM  20123  CA  VAL C 963     223.196 199.426 211.608  1.00 33.77           C  
ATOM  20124  C   VAL C 963     223.834 200.227 212.725  1.00 34.36           C  
ATOM  20125  O   VAL C 963     223.672 199.893 213.895  1.00 35.55           O  
ATOM  20126  CB  VAL C 963     224.194 198.419 211.044  1.00 34.63           C  
ATOM  20127  CG1 VAL C 963     224.850 197.643 212.184  1.00 37.50           C  
ATOM  20128  CG2 VAL C 963     223.465 197.478 210.133  1.00 34.72           C  
ATOM  20129  N   LYS C 964     224.555 201.288 212.384  1.00 34.42           N  
ATOM  20130  CA  LYS C 964     225.193 202.115 213.396  1.00 34.57           C  
ATOM  20131  C   LYS C 964     224.179 202.689 214.373  1.00 34.60           C  
ATOM  20132  O   LYS C 964     224.474 202.818 215.559  1.00 35.72           O  
ATOM  20133  CB  LYS C 964     225.989 203.242 212.747  1.00 35.04           C  
ATOM  20134  CG  LYS C 964     227.284 202.796 212.066  1.00 36.54           C  
ATOM  20135  CD  LYS C 964     228.427 202.588 213.061  1.00 39.99           C  
ATOM  20136  CE  LYS C 964     229.049 203.920 213.507  1.00 39.36           C  
ATOM  20137  NZ  LYS C 964     230.227 203.707 214.394  1.00 40.00           N  
ATOM  20138  N   GLN C 965     222.972 202.992 213.899  1.00 34.44           N  
ATOM  20139  CA  GLN C 965     221.935 203.554 214.759  1.00 34.01           C  
ATOM  20140  C   GLN C 965     221.534 202.624 215.896  1.00 34.86           C  
ATOM  20141  O   GLN C 965     220.964 203.075 216.886  1.00 35.68           O  
ATOM  20142  CB  GLN C 965     220.689 203.938 213.958  1.00 33.73           C  
ATOM  20143  CG  GLN C 965     220.871 205.149 213.085  1.00 33.88           C  
ATOM  20144  CD  GLN C 965     221.183 206.378 213.878  1.00 33.88           C  
ATOM  20145  OE1 GLN C 965     222.352 206.761 213.957  1.00 34.17           O  
ATOM  20146  NE2 GLN C 965     220.177 206.995 214.473  1.00 33.98           N  
ATOM  20147  N   LEU C 966     221.828 201.335 215.785  1.00 34.80           N  
ATOM  20148  CA  LEU C 966     221.480 200.402 216.847  1.00 35.22           C  
ATOM  20149  C   LEU C 966     222.295 200.675 218.104  1.00 35.94           C  
ATOM  20150  O   LEU C 966     221.921 200.258 219.201  1.00 36.71           O  
ATOM  20151  CB  LEU C 966     221.717 198.954 216.400  1.00 35.05           C  
ATOM  20152  CG  LEU C 966     220.768 198.394 215.329  1.00 35.32           C  
ATOM  20153  CD1 LEU C 966     221.309 197.065 214.828  1.00 36.23           C  
ATOM  20154  CD2 LEU C 966     219.375 198.194 215.935  1.00 35.81           C  
ATOM  20155  N   SER C 967     223.415 201.373 217.952  1.00 35.52           N  
ATOM  20156  CA  SER C 967     224.293 201.663 219.072  1.00 35.53           C  
ATOM  20157  C   SER C 967     223.938 202.970 219.770  1.00 35.95           C  
ATOM  20158  O   SER C 967     224.577 203.340 220.756  1.00 36.53           O  
ATOM  20159  CB  SER C 967     225.731 201.719 218.605  1.00 36.30           C  
ATOM  20160  OG  SER C 967     226.149 200.477 218.116  1.00 37.42           O  
ATOM  20161  N   SER C 968     222.945 203.684 219.257  1.00 35.85           N  
ATOM  20162  CA  SER C 968     222.550 204.946 219.857  1.00 35.63           C  
ATOM  20163  C   SER C 968     221.582 204.718 221.009  1.00 36.65           C  
ATOM  20164  O   SER C 968     220.821 203.752 221.017  1.00 37.13           O  
ATOM  20165  CB  SER C 968     221.955 205.844 218.802  1.00 35.60           C  
ATOM  20166  OG  SER C 968     222.929 206.196 217.863  1.00 35.27           O  
ATOM  20167  N   ASN C 969     221.619 205.611 221.991  1.00 36.64           N  
ATOM  20168  CA  ASN C 969     220.742 205.505 223.148  1.00 36.42           C  
ATOM  20169  C   ASN C 969     219.362 206.099 222.913  1.00 37.15           C  
ATOM  20170  O   ASN C 969     218.380 205.649 223.491  1.00 37.30           O  
ATOM  20171  CB  ASN C 969     221.384 206.181 224.336  1.00 37.33           C  
ATOM  20172  CG  ASN C 969     222.562 205.435 224.866  1.00 38.38           C  
ATOM  20173  OD1 ASN C 969     222.670 204.218 224.726  1.00 38.62           O  
ATOM  20174  ND2 ASN C 969     223.466 206.150 225.476  1.00 38.25           N  
ATOM  20175  N   PHE C 970     219.285 207.148 222.115  1.00 36.22           N  
ATOM  20176  CA  PHE C 970     218.021 207.827 221.854  1.00 36.01           C  
ATOM  20177  C   PHE C 970     217.340 208.305 223.125  1.00 36.70           C  
ATOM  20178  O   PHE C 970     216.112 208.346 223.194  1.00 37.08           O  
ATOM  20179  CB  PHE C 970     217.053 206.915 221.113  1.00 36.38           C  
ATOM  20180  CG  PHE C 970     217.605 206.336 219.879  1.00 35.85           C  
ATOM  20181  CD1 PHE C 970     217.850 204.987 219.792  1.00 35.95           C  
ATOM  20182  CD2 PHE C 970     217.883 207.131 218.798  1.00 35.36           C  
ATOM  20183  CE1 PHE C 970     218.353 204.447 218.646  1.00 35.69           C  
ATOM  20184  CE2 PHE C 970     218.391 206.594 217.655  1.00 35.14           C  
ATOM  20185  CZ  PHE C 970     218.620 205.251 217.576  1.00 35.52           C  
ATOM  20186  N   GLY C 971     218.125 208.662 224.132  1.00 37.07           N  
ATOM  20187  CA  GLY C 971     217.584 209.144 225.394  1.00 37.46           C  
ATOM  20188  C   GLY C 971     217.474 208.035 226.432  1.00 37.84           C  
ATOM  20189  O   GLY C 971     217.206 208.301 227.604  1.00 37.94           O  
ATOM  20190  N   ALA C 972     217.673 206.797 226.002  1.00 38.04           N  
ATOM  20191  CA  ALA C 972     217.605 205.651 226.890  1.00 38.35           C  
ATOM  20192  C   ALA C 972     218.855 205.570 227.743  1.00 38.89           C  
ATOM  20193  O   ALA C 972     219.892 206.144 227.412  1.00 38.90           O  
ATOM  20194  CB  ALA C 972     217.427 204.361 226.105  1.00 39.34           C  
ATOM  20195  N   ILE C 973     218.743 204.841 228.840  1.00 40.05           N  
ATOM  20196  CA  ILE C 973     219.847 204.583 229.748  1.00 40.23           C  
ATOM  20197  C   ILE C 973     220.970 203.792 229.080  1.00 40.00           C  
ATOM  20198  O   ILE C 973     222.133 203.914 229.462  1.00 40.17           O  
ATOM  20199  CB  ILE C 973     219.332 203.832 230.995  1.00 41.25           C  
ATOM  20200  CG1 ILE C 973     220.379 203.881 232.112  1.00 41.68           C  
ATOM  20201  CG2 ILE C 973     218.950 202.388 230.640  1.00 41.59           C  
ATOM  20202  CD1 ILE C 973     219.875 203.394 233.466  1.00 43.36           C  
ATOM  20203  N   SER C 974     220.618 202.954 228.109  1.00 40.12           N  
ATOM  20204  CA  SER C 974     221.594 202.141 227.402  1.00 39.65           C  
ATOM  20205  C   SER C 974     221.102 201.742 226.025  1.00 40.04           C  
ATOM  20206  O   SER C 974     219.921 201.467 225.836  1.00 40.23           O  
ATOM  20207  CB  SER C 974     221.910 200.890 228.183  1.00 40.33           C  
ATOM  20208  OG  SER C 974     222.828 200.096 227.487  1.00 40.42           O  
ATOM  20209  N   SER C 975     222.027 201.644 225.076  1.00 39.48           N  
ATOM  20210  CA  SER C 975     221.727 201.172 223.725  1.00 38.26           C  
ATOM  20211  C   SER C 975     221.504 199.668 223.684  1.00 39.30           C  
ATOM  20212  O   SER C 975     221.005 199.130 222.694  1.00 39.14           O  
ATOM  20213  CB  SER C 975     222.860 201.505 222.784  1.00 38.48           C  
ATOM  20214  OG  SER C 975     224.014 200.776 223.111  1.00 38.72           O  
ATOM  20215  N   VAL C 976     221.894 198.981 224.750  1.00 40.04           N  
ATOM  20216  CA  VAL C 976     221.781 197.538 224.781  1.00 40.15           C  
ATOM  20217  C   VAL C 976     220.506 197.111 225.476  1.00 41.68           C  
ATOM  20218  O   VAL C 976     220.304 197.354 226.667  1.00 41.45           O  
ATOM  20219  CB  VAL C 976     222.995 196.922 225.482  1.00 41.13           C  
ATOM  20220  CG1 VAL C 976     222.865 195.413 225.535  1.00 41.52           C  
ATOM  20221  CG2 VAL C 976     224.248 197.321 224.740  1.00 40.80           C  
ATOM  20222  N   LEU C 977     219.662 196.438 224.721  1.00 41.03           N  
ATOM  20223  CA  LEU C 977     218.352 196.032 225.180  1.00 40.93           C  
ATOM  20224  C   LEU C 977     218.441 195.051 226.337  1.00 42.73           C  
ATOM  20225  O   LEU C 977     217.641 195.100 227.272  1.00 43.32           O  
ATOM  20226  CB  LEU C 977     217.604 195.422 223.995  1.00 41.02           C  
ATOM  20227  CG  LEU C 977     216.178 194.993 224.210  1.00 41.54           C  
ATOM  20228  CD1 LEU C 977     215.346 196.171 224.675  1.00 41.80           C  
ATOM  20229  CD2 LEU C 977     215.651 194.452 222.893  1.00 40.71           C  
ATOM  20230  N   ASN C 978     219.428 194.168 226.277  1.00 43.20           N  
ATOM  20231  CA  ASN C 978     219.611 193.161 227.310  1.00 42.40           C  
ATOM  20232  C   ASN C 978     220.069 193.769 228.629  1.00 43.49           C  
ATOM  20233  O   ASN C 978     219.751 193.242 229.697  1.00 43.80           O  
ATOM  20234  CB  ASN C 978     220.596 192.119 226.840  1.00 44.20           C  
ATOM  20235  CG  ASN C 978     220.013 191.239 225.798  1.00 45.13           C  
ATOM  20236  OD1 ASN C 978     218.806 190.979 225.790  1.00 44.18           O  
ATOM  20237  ND2 ASN C 978     220.838 190.780 224.897  1.00 47.54           N  
ATOM  20238  N   ASP C 979     220.798 194.882 228.569  1.00 42.57           N  
ATOM  20239  CA  ASP C 979     221.268 195.514 229.789  1.00 42.44           C  
ATOM  20240  C   ASP C 979     220.104 196.188 230.478  1.00 45.18           C  
ATOM  20241  O   ASP C 979     219.989 196.146 231.700  1.00 45.51           O  
ATOM  20242  CB  ASP C 979     222.368 196.527 229.498  1.00 42.66           C  
ATOM  20243  CG  ASP C 979     223.679 195.879 229.065  1.00 42.97           C  
ATOM  20244  OD1 ASP C 979     223.861 194.706 229.288  1.00 43.25           O  
ATOM  20245  OD2 ASP C 979     224.491 196.571 228.511  1.00 43.18           O  
ATOM  20246  N   ILE C 980     219.206 196.769 229.695  1.00 43.38           N  
ATOM  20247  CA  ILE C 980     218.035 197.397 230.280  1.00 43.01           C  
ATOM  20248  C   ILE C 980     217.159 196.357 230.952  1.00 45.10           C  
ATOM  20249  O   ILE C 980     216.716 196.548 232.083  1.00 45.91           O  
ATOM  20250  CB  ILE C 980     217.202 198.137 229.226  1.00 43.03           C  
ATOM  20251  CG1 ILE C 980     217.974 199.329 228.711  1.00 41.86           C  
ATOM  20252  CG2 ILE C 980     215.867 198.568 229.829  1.00 43.25           C  
ATOM  20253  CD1 ILE C 980     217.382 199.951 227.483  1.00 41.13           C  
ATOM  20254  N   LEU C 981     216.912 195.251 230.257  1.00 43.41           N  
ATOM  20255  CA  LEU C 981     216.050 194.210 230.795  1.00 44.53           C  
ATOM  20256  C   LEU C 981     216.613 193.524 232.031  1.00 45.73           C  
ATOM  20257  O   LEU C 981     215.866 193.228 232.963  1.00 46.03           O  
ATOM  20258  CB  LEU C 981     215.785 193.160 229.712  1.00 44.54           C  
ATOM  20259  CG  LEU C 981     214.882 193.602 228.554  1.00 43.54           C  
ATOM  20260  CD1 LEU C 981     214.959 192.584 227.435  1.00 42.85           C  
ATOM  20261  CD2 LEU C 981     213.444 193.714 229.046  1.00 43.27           C  
ATOM  20262  N   SER C 982     217.918 193.265 232.059  1.00 45.00           N  
ATOM  20263  CA  SER C 982     218.488 192.589 233.215  1.00 45.38           C  
ATOM  20264  C   SER C 982     218.821 193.533 234.372  1.00 46.05           C  
ATOM  20265  O   SER C 982     218.878 193.101 235.525  1.00 46.76           O  
ATOM  20266  CB  SER C 982     219.728 191.816 232.813  1.00 46.16           C  
ATOM  20267  OG  SER C 982     220.750 192.672 232.412  1.00 45.60           O  
ATOM  20268  N   ARG C 983     219.028 194.818 234.085  1.00 45.39           N  
ATOM  20269  CA  ARG C 983     219.386 195.771 235.125  1.00 46.04           C  
ATOM  20270  C   ARG C 983     218.202 196.464 235.783  1.00 47.02           C  
ATOM  20271  O   ARG C 983     218.227 196.711 236.988  1.00 47.31           O  
ATOM  20272  CB  ARG C 983     220.327 196.827 234.584  1.00 46.07           C  
ATOM  20273  CG  ARG C 983     220.771 197.859 235.597  1.00 46.09           C  
ATOM  20274  CD  ARG C 983     221.900 198.659 235.099  1.00 45.93           C  
ATOM  20275  NE  ARG C 983     221.567 199.381 233.889  1.00 45.47           N  
ATOM  20276  CZ  ARG C 983     222.452 200.079 233.155  1.00 45.33           C  
ATOM  20277  NH1 ARG C 983     223.712 200.152 233.528  1.00 45.06           N  
ATOM  20278  NH2 ARG C 983     222.059 200.692 232.061  1.00 43.55           N  
ATOM  20279  N   LEU C 984     217.190 196.840 235.010  1.00 46.65           N  
ATOM  20280  CA  LEU C 984     216.088 197.589 235.592  1.00 47.71           C  
ATOM  20281  C   LEU C 984     214.844 196.739 235.765  1.00 48.88           C  
ATOM  20282  O   LEU C 984     214.502 195.924 234.910  1.00 47.99           O  
ATOM  20283  CB  LEU C 984     215.758 198.793 234.709  1.00 47.02           C  
ATOM  20284  CG  LEU C 984     216.906 199.777 234.439  1.00 46.93           C  
ATOM  20285  CD1 LEU C 984     216.409 200.842 233.495  1.00 45.85           C  
ATOM  20286  CD2 LEU C 984     217.391 200.405 235.740  1.00 47.08           C  
ATOM  20287  N   ASP C 985     214.127 196.975 236.852  1.00 49.71           N  
ATOM  20288  CA  ASP C 985     212.862 196.302 237.078  1.00 51.62           C  
ATOM  20289  C   ASP C 985     211.914 196.671 235.935  1.00 50.66           C  
ATOM  20290  O   ASP C 985     211.898 197.832 235.526  1.00 50.10           O  
ATOM  20291  CB  ASP C 985     212.273 196.730 238.422  1.00 53.16           C  
ATOM  20292  N   PRO C 986     211.071 195.746 235.449  1.00 50.90           N  
ATOM  20293  CA  PRO C 986     210.114 195.924 234.361  1.00 50.56           C  
ATOM  20294  C   PRO C 986     209.342 197.261 234.324  1.00 50.16           C  
ATOM  20295  O   PRO C 986     209.222 197.840 233.249  1.00 48.86           O  
ATOM  20296  CB  PRO C 986     209.193 194.711 234.552  1.00 52.20           C  
ATOM  20297  CG  PRO C 986     210.115 193.648 235.102  1.00 51.74           C  
ATOM  20298  CD  PRO C 986     211.061 194.386 236.032  1.00 51.61           C  
ATOM  20299  N   PRO C 987     208.837 197.817 235.442  1.00 50.98           N  
ATOM  20300  CA  PRO C 987     208.086 199.062 235.466  1.00 51.62           C  
ATOM  20301  C   PRO C 987     208.909 200.248 234.971  1.00 49.61           C  
ATOM  20302  O   PRO C 987     208.356 201.276 234.583  1.00 48.69           O  
ATOM  20303  CB  PRO C 987     207.745 199.205 236.948  1.00 56.87           C  
ATOM  20304  CG  PRO C 987     207.859 197.803 237.495  1.00 57.01           C  
ATOM  20305  CD  PRO C 987     208.979 197.207 236.765  1.00 53.99           C  
ATOM  20306  N   GLU C 988     210.232 200.109 235.012  1.00 48.89           N  
ATOM  20307  CA  GLU C 988     211.141 201.147 234.556  1.00 47.71           C  
ATOM  20308  C   GLU C 988     211.788 200.726 233.245  1.00 47.03           C  
ATOM  20309  O   GLU C 988     212.080 201.562 232.385  1.00 46.15           O  
ATOM  20310  CB  GLU C 988     212.215 201.420 235.605  1.00 48.25           C  
ATOM  20311  N   ALA C 989     212.047 199.426 233.116  1.00 47.00           N  
ATOM  20312  CA  ALA C 989     212.709 198.888 231.939  1.00 45.69           C  
ATOM  20313  C   ALA C 989     211.868 199.138 230.709  1.00 43.73           C  
ATOM  20314  O   ALA C 989     212.400 199.442 229.646  1.00 42.94           O  
ATOM  20315  CB  ALA C 989     212.961 197.402 232.097  1.00 46.11           C  
ATOM  20316  N   GLU C 990     210.549 199.043 230.854  1.00 44.16           N  
ATOM  20317  CA  GLU C 990     209.657 199.257 229.727  1.00 42.92           C  
ATOM  20318  C   GLU C 990     209.768 200.672 229.196  1.00 40.99           C  
ATOM  20319  O   GLU C 990     209.641 200.895 227.995  1.00 43.26           O  
ATOM  20320  CB  GLU C 990     208.210 198.954 230.099  1.00 43.04           C  
ATOM  20321  CG  GLU C 990     207.904 197.476 230.290  1.00 43.33           C  
ATOM  20322  CD  GLU C 990     206.482 197.227 230.697  1.00 43.92           C  
ATOM  20323  OE1 GLU C 990     205.768 198.179 230.901  1.00 43.03           O  
ATOM  20324  OE2 GLU C 990     206.108 196.083 230.806  1.00 43.49           O  
ATOM  20325  N   VAL C 991     209.995 201.633 230.081  1.00 42.36           N  
ATOM  20326  CA  VAL C 991     210.109 203.017 229.661  1.00 41.89           C  
ATOM  20327  C   VAL C 991     211.378 203.215 228.857  1.00 41.19           C  
ATOM  20328  O   VAL C 991     211.372 203.871 227.812  1.00 42.54           O  
ATOM  20329  CB  VAL C 991     210.104 203.955 230.873  1.00 43.47           C  
ATOM  20330  CG1 VAL C 991     210.389 205.385 230.432  1.00 42.85           C  
ATOM  20331  CG2 VAL C 991     208.756 203.856 231.564  1.00 44.65           C  
ATOM  20332  N   GLN C 992     212.472 202.643 229.341  1.00 41.27           N  
ATOM  20333  CA  GLN C 992     213.734 202.780 228.638  1.00 40.37           C  
ATOM  20334  C   GLN C 992     213.664 202.075 227.291  1.00 42.19           C  
ATOM  20335  O   GLN C 992     214.230 202.549 226.302  1.00 40.43           O  
ATOM  20336  CB  GLN C 992     214.866 202.217 229.483  1.00 41.97           C  
ATOM  20337  CG  GLN C 992     215.071 202.957 230.769  1.00 42.61           C  
ATOM  20338  CD  GLN C 992     215.328 204.399 230.548  1.00 41.61           C  
ATOM  20339  OE1 GLN C 992     216.183 204.769 229.749  1.00 40.70           O  
ATOM  20340  NE2 GLN C 992     214.587 205.252 231.237  1.00 42.54           N  
ATOM  20341  N   ILE C 993     212.933 200.970 227.238  1.00 40.78           N  
ATOM  20342  CA  ILE C 993     212.766 200.254 225.990  1.00 39.07           C  
ATOM  20343  C   ILE C 993     211.932 201.070 225.027  1.00 41.91           C  
ATOM  20344  O   ILE C 993     212.273 201.157 223.852  1.00 37.78           O  
ATOM  20345  CB  ILE C 993     212.165 198.870 226.190  1.00 40.83           C  
ATOM  20346  CG1 ILE C 993     213.147 198.036 226.947  1.00 41.15           C  
ATOM  20347  CG2 ILE C 993     211.880 198.244 224.825  1.00 40.32           C  
ATOM  20348  CD1 ILE C 993     212.593 196.761 227.485  1.00 42.50           C  
ATOM  20349  N   ASP C 994     210.849 201.690 225.495  1.00 42.73           N  
ATOM  20350  CA  ASP C 994     210.055 202.507 224.590  1.00 37.97           C  
ATOM  20351  C   ASP C 994     210.922 203.559 223.916  1.00 38.05           C  
ATOM  20352  O   ASP C 994     210.738 203.846 222.731  1.00 39.05           O  
ATOM  20353  CB  ASP C 994     208.900 203.204 225.308  1.00 39.72           C  
ATOM  20354  CG  ASP C 994     207.703 202.305 225.622  1.00 40.21           C  
ATOM  20355  OD1 ASP C 994     207.610 201.231 225.081  1.00 39.69           O  
ATOM  20356  OD2 ASP C 994     206.873 202.725 226.396  1.00 40.54           O  
ATOM  20357  N   ARG C 995     211.887 204.123 224.641  1.00 38.35           N  
ATOM  20358  CA  ARG C 995     212.774 205.087 224.004  1.00 37.95           C  
ATOM  20359  C   ARG C 995     213.606 204.434 222.901  1.00 37.87           C  
ATOM  20360  O   ARG C 995     213.765 205.011 221.821  1.00 37.47           O  
ATOM  20361  CB  ARG C 995     213.681 205.763 225.012  1.00 38.33           C  
ATOM  20362  CG  ARG C 995     212.984 206.781 225.877  1.00 38.41           C  
ATOM  20363  CD  ARG C 995     213.926 207.484 226.766  1.00 38.25           C  
ATOM  20364  NE  ARG C 995     213.264 208.518 227.547  1.00 38.31           N  
ATOM  20365  CZ  ARG C 995     213.024 209.779 227.112  1.00 37.65           C  
ATOM  20366  NH1 ARG C 995     213.393 210.152 225.903  1.00 37.23           N  
ATOM  20367  NH2 ARG C 995     212.415 210.643 227.905  1.00 36.97           N  
ATOM  20368  N   LEU C 996     214.104 203.221 223.141  1.00 37.40           N  
ATOM  20369  CA  LEU C 996     214.869 202.548 222.098  1.00 36.81           C  
ATOM  20370  C   LEU C 996     213.991 202.164 220.919  1.00 37.58           C  
ATOM  20371  O   LEU C 996     214.429 202.250 219.773  1.00 37.59           O  
ATOM  20372  CB  LEU C 996     215.562 201.283 222.609  1.00 37.38           C  
ATOM  20373  CG  LEU C 996     216.712 201.452 223.605  1.00 38.10           C  
ATOM  20374  CD1 LEU C 996     217.198 200.071 224.006  1.00 39.27           C  
ATOM  20375  CD2 LEU C 996     217.848 202.258 222.987  1.00 37.77           C  
ATOM  20376  N   ILE C 997     212.753 201.757 221.177  1.00 36.52           N  
ATOM  20377  CA  ILE C 997     211.869 201.389 220.088  1.00 35.67           C  
ATOM  20378  C   ILE C 997     211.558 202.585 219.232  1.00 36.43           C  
ATOM  20379  O   ILE C 997     211.568 202.488 218.011  1.00 35.40           O  
ATOM  20380  CB  ILE C 997     210.555 200.747 220.557  1.00 36.38           C  
ATOM  20381  CG1 ILE C 997     210.839 199.362 221.152  1.00 37.23           C  
ATOM  20382  CG2 ILE C 997     209.563 200.664 219.379  1.00 36.06           C  
ATOM  20383  CD1 ILE C 997     209.660 198.749 221.878  1.00 38.25           C  
ATOM  20384  N   THR C 998     211.265 203.719 219.845  1.00 35.71           N  
ATOM  20385  CA  THR C 998     210.951 204.884 219.045  1.00 35.29           C  
ATOM  20386  C   THR C 998     212.130 205.252 218.164  1.00 34.48           C  
ATOM  20387  O   THR C 998     211.956 205.532 216.978  1.00 34.75           O  
ATOM  20388  CB  THR C 998     210.563 206.082 219.919  1.00 36.22           C  
ATOM  20389  OG1 THR C 998     209.388 205.762 220.669  1.00 36.83           O  
ATOM  20390  CG2 THR C 998     210.284 207.297 219.040  1.00 35.39           C  
ATOM  20391  N   GLY C 999     213.333 205.248 218.730  1.00 35.43           N  
ATOM  20392  CA  GLY C 999     214.525 205.599 217.970  1.00 34.50           C  
ATOM  20393  C   GLY C 999     214.811 204.619 216.836  1.00 34.19           C  
ATOM  20394  O   GLY C 999     215.155 205.027 215.725  1.00 34.41           O  
ATOM  20395  N   ARG C1000     214.688 203.327 217.114  1.00 34.21           N  
ATOM  20396  CA  ARG C1000     214.978 202.313 216.118  1.00 33.30           C  
ATOM  20397  C   ARG C1000     213.894 202.224 215.058  1.00 34.44           C  
ATOM  20398  O   ARG C1000     214.186 201.992 213.884  1.00 34.51           O  
ATOM  20399  CB  ARG C1000     215.191 200.980 216.792  1.00 34.61           C  
ATOM  20400  CG  ARG C1000     216.475 200.915 217.572  1.00 34.93           C  
ATOM  20401  CD  ARG C1000     216.632 199.654 218.280  1.00 35.34           C  
ATOM  20402  NE  ARG C1000     217.918 199.580 218.910  1.00 35.75           N  
ATOM  20403  CZ  ARG C1000     218.348 198.557 219.653  1.00 36.24           C  
ATOM  20404  NH1 ARG C1000     217.570 197.517 219.875  1.00 36.90           N  
ATOM  20405  NH2 ARG C1000     219.571 198.588 220.155  1.00 37.02           N  
ATOM  20406  N   LEU C1001     212.649 202.438 215.453  1.00 33.31           N  
ATOM  20407  CA  LEU C1001     211.551 202.422 214.509  1.00 32.68           C  
ATOM  20408  C   LEU C1001     211.671 203.630 213.602  1.00 34.54           C  
ATOM  20409  O   LEU C1001     211.468 203.532 212.391  1.00 32.53           O  
ATOM  20410  CB  LEU C1001     210.213 202.428 215.251  1.00 33.47           C  
ATOM  20411  CG  LEU C1001     208.936 202.372 214.401  1.00 32.91           C  
ATOM  20412  CD1 LEU C1001     208.919 201.099 213.547  1.00 33.17           C  
ATOM  20413  CD2 LEU C1001     207.729 202.412 215.339  1.00 33.71           C  
ATOM  20414  N   GLN C1002     212.019 204.774 214.184  1.00 32.26           N  
ATOM  20415  CA  GLN C1002     212.208 205.991 213.425  1.00 31.65           C  
ATOM  20416  C   GLN C1002     213.365 205.829 212.456  1.00 32.98           C  
ATOM  20417  O   GLN C1002     213.319 206.355 211.342  1.00 32.54           O  
ATOM  20418  CB  GLN C1002     212.455 207.165 214.362  1.00 32.59           C  
ATOM  20419  CG  GLN C1002     212.563 208.507 213.689  1.00 32.10           C  
ATOM  20420  CD  GLN C1002     212.757 209.608 214.703  1.00 32.15           C  
ATOM  20421  OE1 GLN C1002     213.098 209.344 215.860  1.00 32.81           O  
ATOM  20422  NE2 GLN C1002     212.541 210.851 214.291  1.00 31.49           N  
ATOM  20423  N   SER C1003     214.404 205.105 212.876  1.00 32.14           N  
ATOM  20424  CA  SER C1003     215.558 204.856 212.024  1.00 31.69           C  
ATOM  20425  C   SER C1003     215.162 204.044 210.804  1.00 31.25           C  
ATOM  20426  O   SER C1003     215.561 204.376 209.685  1.00 31.79           O  
ATOM  20427  CB  SER C1003     216.649 204.154 212.788  1.00 32.91           C  
ATOM  20428  OG  SER C1003     217.753 203.931 211.969  1.00 33.27           O  
ATOM  20429  N   LEU C1004     214.351 203.004 210.996  1.00 31.87           N  
ATOM  20430  CA  LEU C1004     213.881 202.234 209.853  1.00 30.93           C  
ATOM  20431  C   LEU C1004     213.025 203.081 208.942  1.00 31.08           C  
ATOM  20432  O   LEU C1004     213.128 202.969 207.726  1.00 31.14           O  
ATOM  20433  CB  LEU C1004     213.041 201.033 210.274  1.00 32.12           C  
ATOM  20434  CG  LEU C1004     213.745 199.880 210.915  1.00 32.94           C  
ATOM  20435  CD1 LEU C1004     212.709 198.946 211.485  1.00 33.59           C  
ATOM  20436  CD2 LEU C1004     214.578 199.142 209.880  1.00 33.79           C  
ATOM  20437  N   GLN C1005     212.184 203.939 209.505  1.00 30.83           N  
ATOM  20438  CA  GLN C1005     211.330 204.764 208.667  1.00 30.44           C  
ATOM  20439  C   GLN C1005     212.168 205.698 207.818  1.00 29.74           C  
ATOM  20440  O   GLN C1005     211.875 205.899 206.637  1.00 30.34           O  
ATOM  20441  CB  GLN C1005     210.341 205.548 209.523  1.00 31.19           C  
ATOM  20442  CG  GLN C1005     209.278 204.678 210.156  1.00 31.51           C  
ATOM  20443  CD  GLN C1005     208.470 205.387 211.196  1.00 31.90           C  
ATOM  20444  OE1 GLN C1005     208.739 206.543 211.549  1.00 31.66           O  
ATOM  20445  NE2 GLN C1005     207.470 204.696 211.711  1.00 31.93           N  
ATOM  20446  N   THR C1006     213.234 206.239 208.398  1.00 30.02           N  
ATOM  20447  CA  THR C1006     214.127 207.112 207.654  1.00 29.47           C  
ATOM  20448  C   THR C1006     214.797 206.342 206.529  1.00 29.61           C  
ATOM  20449  O   THR C1006     214.820 206.794 205.383  1.00 29.44           O  
ATOM  20450  CB  THR C1006     215.198 207.713 208.579  1.00 30.41           C  
ATOM  20451  OG1 THR C1006     214.564 208.513 209.580  1.00 30.77           O  
ATOM  20452  CG2 THR C1006     216.169 208.568 207.788  1.00 30.26           C  
ATOM  20453  N   TYR C1007     215.312 205.163 206.849  1.00 29.39           N  
ATOM  20454  CA  TYR C1007     215.965 204.311 205.873  1.00 28.79           C  
ATOM  20455  C   TYR C1007     215.049 203.947 204.729  1.00 33.55           C  
ATOM  20456  O   TYR C1007     215.429 204.067 203.566  1.00 27.68           O  
ATOM  20457  CB  TYR C1007     216.485 203.050 206.543  1.00 30.26           C  
ATOM  20458  CG  TYR C1007     216.925 201.998 205.592  1.00 29.75           C  
ATOM  20459  CD1 TYR C1007     218.139 202.088 204.961  1.00 30.32           C  
ATOM  20460  CD2 TYR C1007     216.098 200.925 205.355  1.00 30.08           C  
ATOM  20461  CE1 TYR C1007     218.518 201.103 204.085  1.00 30.49           C  
ATOM  20462  CE2 TYR C1007     216.476 199.948 204.489  1.00 30.05           C  
ATOM  20463  CZ  TYR C1007     217.676 200.033 203.853  1.00 30.19           C  
ATOM  20464  OH  TYR C1007     218.045 199.054 202.977  1.00 30.55           O  
ATOM  20465  N   VAL C1008     213.847 203.486 205.048  1.00 28.73           N  
ATOM  20466  CA  VAL C1008     212.924 203.056 204.022  1.00 28.08           C  
ATOM  20467  C   VAL C1008     212.527 204.214 203.132  1.00 28.31           C  
ATOM  20468  O   VAL C1008     212.469 204.059 201.915  1.00 28.80           O  
ATOM  20469  CB  VAL C1008     211.687 202.388 204.634  1.00 29.20           C  
ATOM  20470  CG1 VAL C1008     210.650 202.126 203.570  1.00 28.76           C  
ATOM  20471  CG2 VAL C1008     212.105 201.080 205.268  1.00 29.71           C  
ATOM  20472  N   THR C1009     212.261 205.379 203.709  1.00 28.45           N  
ATOM  20473  CA  THR C1009     211.898 206.517 202.886  1.00 27.40           C  
ATOM  20474  C   THR C1009     213.018 206.831 201.911  1.00 27.50           C  
ATOM  20475  O   THR C1009     212.767 207.083 200.731  1.00 28.43           O  
ATOM  20476  CB  THR C1009     211.585 207.756 203.732  1.00 28.29           C  
ATOM  20477  OG1 THR C1009     210.469 207.482 204.581  1.00 29.38           O  
ATOM  20478  CG2 THR C1009     211.252 208.930 202.826  1.00 27.95           C  
ATOM  20479  N   GLN C1010     214.257 206.801 202.388  1.00 27.56           N  
ATOM  20480  CA  GLN C1010     215.394 207.068 201.526  1.00 27.03           C  
ATOM  20481  C   GLN C1010     215.526 206.018 200.433  1.00 28.05           C  
ATOM  20482  O   GLN C1010     215.862 206.356 199.298  1.00 27.88           O  
ATOM  20483  CB  GLN C1010     216.672 207.120 202.346  1.00 27.92           C  
ATOM  20484  CG  GLN C1010     216.775 208.328 203.244  1.00 28.21           C  
ATOM  20485  CD  GLN C1010     217.901 208.187 204.241  1.00 29.28           C  
ATOM  20486  OE1 GLN C1010     218.502 207.113 204.348  1.00 29.28           O  
ATOM  20487  NE2 GLN C1010     218.186 209.250 204.982  1.00 28.78           N  
ATOM  20488  N   GLN C1011     215.249 204.753 200.748  1.00 27.43           N  
ATOM  20489  CA  GLN C1011     215.341 203.712 199.733  1.00 26.91           C  
ATOM  20490  C   GLN C1011     214.284 203.894 198.667  1.00 27.02           C  
ATOM  20491  O   GLN C1011     214.549 203.659 197.492  1.00 27.49           O  
ATOM  20492  CB  GLN C1011     215.184 202.318 200.335  1.00 27.69           C  
ATOM  20493  CG  GLN C1011     216.322 201.874 201.204  1.00 28.60           C  
ATOM  20494  CD  GLN C1011     217.612 201.745 200.460  1.00 28.85           C  
ATOM  20495  OE1 GLN C1011     218.434 202.661 200.477  1.00 28.60           O  
ATOM  20496  NE2 GLN C1011     217.816 200.609 199.807  1.00 28.99           N  
ATOM  20497  N   LEU C1012     213.091 204.322 199.058  1.00 26.53           N  
ATOM  20498  CA  LEU C1012     212.026 204.526 198.087  1.00 26.34           C  
ATOM  20499  C   LEU C1012     212.323 205.694 197.166  1.00 26.22           C  
ATOM  20500  O   LEU C1012     212.093 205.615 195.957  1.00 26.84           O  
ATOM  20501  CB  LEU C1012     210.697 204.763 198.796  1.00 26.77           C  
ATOM  20502  CG  LEU C1012     209.812 203.542 199.022  1.00 26.67           C  
ATOM  20503  CD1 LEU C1012     210.565 202.467 199.778  1.00 27.87           C  
ATOM  20504  CD2 LEU C1012     208.606 203.973 199.799  1.00 25.52           C  
ATOM  20505  N   ILE C1013     212.863 206.769 197.716  1.00 26.25           N  
ATOM  20506  CA  ILE C1013     213.189 207.910 196.887  1.00 25.88           C  
ATOM  20507  C   ILE C1013     214.350 207.563 195.971  1.00 26.10           C  
ATOM  20508  O   ILE C1013     214.322 207.878 194.780  1.00 26.39           O  
ATOM  20509  CB  ILE C1013     213.496 209.150 197.732  1.00 26.22           C  
ATOM  20510  CG1 ILE C1013     212.208 209.582 198.452  1.00 26.55           C  
ATOM  20511  CG2 ILE C1013     214.033 210.273 196.840  1.00 27.07           C  
ATOM  20512  CD1 ILE C1013     212.403 210.619 199.530  1.00 26.63           C  
ATOM  20513  N   ARG C1014     215.376 206.919 196.515  1.00 26.37           N  
ATOM  20514  CA  ARG C1014     216.509 206.516 195.702  1.00 25.61           C  
ATOM  20515  C   ARG C1014     216.053 205.558 194.616  1.00 26.15           C  
ATOM  20516  O   ARG C1014     216.526 205.629 193.482  1.00 26.71           O  
ATOM  20517  CB  ARG C1014     217.597 205.877 196.545  1.00 26.60           C  
ATOM  20518  CG  ARG C1014     218.893 205.605 195.792  1.00 26.71           C  
ATOM  20519  CD  ARG C1014     219.968 205.044 196.664  1.00 27.43           C  
ATOM  20520  NE  ARG C1014     220.411 205.981 197.702  1.00 27.61           N  
ATOM  20521  CZ  ARG C1014     220.158 205.870 199.027  1.00 27.78           C  
ATOM  20522  NH1 ARG C1014     219.448 204.868 199.491  1.00 28.07           N  
ATOM  20523  NH2 ARG C1014     220.632 206.779 199.862  1.00 27.67           N  
ATOM  20524  N   ALA C1015     215.127 204.664 194.949  1.00 25.88           N  
ATOM  20525  CA  ALA C1015     214.606 203.723 193.977  1.00 25.32           C  
ATOM  20526  C   ALA C1015     213.922 204.444 192.840  1.00 25.57           C  
ATOM  20527  O   ALA C1015     213.975 203.977 191.708  1.00 25.41           O  
ATOM  20528  CB  ALA C1015     213.638 202.760 194.622  1.00 26.15           C  
ATOM  20529  N   ALA C1016     213.263 205.563 193.121  1.00 25.63           N  
ATOM  20530  CA  ALA C1016     212.609 206.307 192.059  1.00 24.85           C  
ATOM  20531  C   ALA C1016     213.636 206.809 191.059  1.00 24.31           C  
ATOM  20532  O   ALA C1016     213.392 206.811 189.852  1.00 25.36           O  
ATOM  20533  CB  ALA C1016     211.823 207.469 192.628  1.00 25.89           C  
ATOM  20534  N   GLU C1017     214.797 207.220 191.558  1.00 24.78           N  
ATOM  20535  CA  GLU C1017     215.861 207.683 190.680  1.00 24.08           C  
ATOM  20536  C   GLU C1017     216.347 206.553 189.795  1.00 24.69           C  
ATOM  20537  O   GLU C1017     216.532 206.728 188.588  1.00 24.90           O  
ATOM  20538  CB  GLU C1017     217.032 208.234 191.481  1.00 25.11           C  
ATOM  20539  CG  GLU C1017     218.177 208.746 190.635  1.00 25.04           C  
ATOM  20540  CD  GLU C1017     219.289 209.303 191.460  1.00 25.56           C  
ATOM  20541  OE1 GLU C1017     219.124 209.401 192.652  1.00 25.27           O  
ATOM  20542  OE2 GLU C1017     220.313 209.625 190.905  1.00 24.75           O  
ATOM  20543  N   ILE C1018     216.533 205.385 190.395  1.00 24.74           N  
ATOM  20544  CA  ILE C1018     216.992 204.221 189.659  1.00 24.09           C  
ATOM  20545  C   ILE C1018     215.948 203.775 188.662  1.00 24.80           C  
ATOM  20546  O   ILE C1018     216.294 203.361 187.561  1.00 24.00           O  
ATOM  20547  CB  ILE C1018     217.367 203.067 190.592  1.00 24.93           C  
ATOM  20548  CG1 ILE C1018     218.546 203.486 191.507  1.00 25.59           C  
ATOM  20549  CG2 ILE C1018     217.714 201.816 189.781  1.00 24.95           C  
ATOM  20550  CD1 ILE C1018     219.833 203.873 190.805  1.00 26.86           C  
ATOM  20551  N   ARG C1019     214.678 203.821 189.043  1.00 24.24           N  
ATOM  20552  CA  ARG C1019     213.615 203.447 188.130  1.00 23.46           C  
ATOM  20553  C   ARG C1019     213.637 204.341 186.911  1.00 23.76           C  
ATOM  20554  O   ARG C1019     213.511 203.857 185.790  1.00 23.82           O  
ATOM  20555  CB  ARG C1019     212.253 203.547 188.785  1.00 24.12           C  
ATOM  20556  CG  ARG C1019     211.112 203.079 187.902  1.00 23.67           C  
ATOM  20557  CD  ARG C1019     209.792 203.110 188.590  1.00 23.78           C  
ATOM  20558  NE  ARG C1019     209.391 204.465 188.987  1.00 24.05           N  
ATOM  20559  CZ  ARG C1019     209.314 204.937 190.259  1.00 24.70           C  
ATOM  20560  NH1 ARG C1019     208.920 206.179 190.458  1.00 24.86           N  
ATOM  20561  NH2 ARG C1019     209.620 204.171 191.302  1.00 24.76           N  
ATOM  20562  N   ALA C1020     213.803 205.644 187.117  1.00 23.53           N  
ATOM  20563  CA  ALA C1020     213.863 206.563 185.996  1.00 22.93           C  
ATOM  20564  C   ALA C1020     215.043 206.235 185.096  1.00 22.73           C  
ATOM  20565  O   ALA C1020     214.916 206.258 183.871  1.00 22.87           O  
ATOM  20566  CB  ALA C1020     213.970 207.988 186.494  1.00 24.01           C  
ATOM  20567  N   SER C1021     216.179 205.887 185.697  1.00 23.46           N  
ATOM  20568  CA  SER C1021     217.353 205.509 184.926  1.00 22.89           C  
ATOM  20569  C   SER C1021     217.084 204.238 184.147  1.00 22.40           C  
ATOM  20570  O   SER C1021     217.452 204.135 182.980  1.00 23.20           O  
ATOM  20571  CB  SER C1021     218.557 205.333 185.823  1.00 23.79           C  
ATOM  20572  OG  SER C1021     219.692 204.986 185.080  1.00 24.09           O  
ATOM  20573  N   ALA C1022     216.443 203.265 184.781  1.00 22.66           N  
ATOM  20574  CA  ALA C1022     216.121 202.016 184.117  1.00 22.13           C  
ATOM  20575  C   ALA C1022     215.168 202.249 182.962  1.00 21.91           C  
ATOM  20576  O   ALA C1022     215.306 201.623 181.916  1.00 22.94           O  
ATOM  20577  CB  ALA C1022     215.505 201.037 185.087  1.00 23.72           C  
ATOM  20578  N   ASN C1023     214.214 203.160 183.130  1.00 22.32           N  
ATOM  20579  CA  ASN C1023     213.277 203.440 182.057  1.00 21.52           C  
ATOM  20580  C   ASN C1023     214.001 204.083 180.896  1.00 21.65           C  
ATOM  20581  O   ASN C1023     213.737 203.760 179.737  1.00 21.77           O  
ATOM  20582  CB  ASN C1023     212.153 204.329 182.530  1.00 21.71           C  
ATOM  20583  CG  ASN C1023     211.186 203.616 183.398  1.00 21.89           C  
ATOM  20584  OD1 ASN C1023     211.143 202.385 183.434  1.00 21.89           O  
ATOM  20585  ND2 ASN C1023     210.385 204.365 184.101  1.00 22.15           N  
ATOM  20586  N   LEU C1024     214.955 204.951 181.204  1.00 21.85           N  
ATOM  20587  CA  LEU C1024     215.761 205.569 180.174  1.00 20.90           C  
ATOM  20588  C   LEU C1024     216.608 204.534 179.478  1.00 21.68           C  
ATOM  20589  O   LEU C1024     216.740 204.557 178.258  1.00 20.76           O  
ATOM  20590  CB  LEU C1024     216.670 206.639 180.766  1.00 21.11           C  
ATOM  20591  CG  LEU C1024     217.628 207.314 179.794  1.00 20.69           C  
ATOM  20592  CD1 LEU C1024     216.854 208.015 178.684  1.00 20.98           C  
ATOM  20593  CD2 LEU C1024     218.487 208.293 180.566  1.00 21.43           C  
ATOM  20594  N   ALA C1025     217.202 203.636 180.251  1.00 21.41           N  
ATOM  20595  CA  ALA C1025     218.038 202.600 179.691  1.00 21.20           C  
ATOM  20596  C   ALA C1025     217.233 201.704 178.780  1.00 20.97           C  
ATOM  20597  O   ALA C1025     217.700 201.330 177.706  1.00 21.93           O  
ATOM  20598  CB  ALA C1025     218.664 201.783 180.800  1.00 22.44           C  
ATOM  20599  N   ALA C1026     216.009 201.381 179.184  1.00 21.03           N  
ATOM  20600  CA  ALA C1026     215.153 200.549 178.363  1.00 20.83           C  
ATOM  20601  C   ALA C1026     214.787 201.278 177.092  1.00 20.41           C  
ATOM  20602  O   ALA C1026     214.780 200.686 176.013  1.00 21.20           O  
ATOM  20603  CB  ALA C1026     213.899 200.159 179.120  1.00 22.23           C  
ATOM  20604  N   THR C1027     214.524 202.576 177.210  1.00 20.91           N  
ATOM  20605  CA  THR C1027     214.170 203.376 176.053  1.00 20.14           C  
ATOM  20606  C   THR C1027     215.329 203.412 175.082  1.00 20.93           C  
ATOM  20607  O   THR C1027     215.139 203.225 173.881  1.00 19.59           O  
ATOM  20608  CB  THR C1027     213.787 204.811 176.449  1.00 20.33           C  
ATOM  20609  OG1 THR C1027     212.658 204.781 177.324  1.00 21.18           O  
ATOM  20610  CG2 THR C1027     213.429 205.621 175.213  1.00 19.89           C  
ATOM  20611  N   LYS C1028     216.538 203.624 175.593  1.00 20.15           N  
ATOM  20612  CA  LYS C1028     217.687 203.657 174.717  1.00 19.29           C  
ATOM  20613  C   LYS C1028     217.907 202.318 174.076  1.00 20.73           C  
ATOM  20614  O   LYS C1028     218.165 202.239 172.885  1.00 19.94           O  
ATOM  20615  CB  LYS C1028     218.964 204.060 175.440  1.00 20.08           C  
ATOM  20616  CG  LYS C1028     219.041 205.502 175.846  1.00 19.62           C  
ATOM  20617  CD  LYS C1028     220.414 205.827 176.359  1.00 20.29           C  
ATOM  20618  CE  LYS C1028     220.471 207.190 177.021  1.00 20.69           C  
ATOM  20619  NZ  LYS C1028     220.089 208.299 176.112  1.00 20.04           N  
ATOM  20620  N   MET C1029     217.762 201.238 174.803  1.00 20.15           N  
ATOM  20621  CA  MET C1029     218.016 199.995 174.122  1.00 20.24           C  
ATOM  20622  C   MET C1029     217.026 199.806 172.984  1.00 21.38           C  
ATOM  20623  O   MET C1029     217.418 199.470 171.867  1.00 20.01           O  
ATOM  20624  CB  MET C1029     217.986 198.840 175.089  1.00 20.73           C  
ATOM  20625  CG  MET C1029     218.525 197.578 174.516  1.00 20.95           C  
ATOM  20626  SD  MET C1029     218.608 196.302 175.703  1.00 22.84           S  
ATOM  20627  CE  MET C1029     219.911 196.831 176.812  1.00 23.37           C  
ATOM  20628  N   SER C1030     215.756 200.101 173.219  1.00 19.61           N  
ATOM  20629  CA  SER C1030     214.772 199.903 172.172  1.00 19.67           C  
ATOM  20630  C   SER C1030     214.989 200.792 170.959  1.00 19.65           C  
ATOM  20631  O   SER C1030     214.868 200.340 169.824  1.00 20.33           O  
ATOM  20632  CB  SER C1030     213.393 200.178 172.703  1.00 19.85           C  
ATOM  20633  OG  SER C1030     213.002 199.222 173.644  1.00 20.61           O  
ATOM  20634  N   GLU C1031     215.319 202.053 171.183  1.00 19.22           N  
ATOM  20635  CA  GLU C1031     215.465 202.999 170.078  1.00 19.02           C  
ATOM  20636  C   GLU C1031     216.882 203.147 169.510  1.00 19.20           C  
ATOM  20637  O   GLU C1031     217.047 203.501 168.344  1.00 19.39           O  
ATOM  20638  CB  GLU C1031     214.981 204.367 170.531  1.00 19.05           C  
ATOM  20639  CG  GLU C1031     213.532 204.396 170.915  1.00 18.88           C  
ATOM  20640  CD  GLU C1031     213.084 205.733 171.362  1.00 19.07           C  
ATOM  20641  OE1 GLU C1031     213.638 206.711 170.924  1.00 19.16           O  
ATOM  20642  OE2 GLU C1031     212.176 205.792 172.150  1.00 19.09           O  
ATOM  20643  N   CYS C1032     217.897 202.905 170.344  1.00 19.50           N  
ATOM  20644  CA  CYS C1032     219.299 203.089 170.028  1.00 19.09           C  
ATOM  20645  C   CYS C1032     219.963 201.793 169.534  1.00 19.96           C  
ATOM  20646  O   CYS C1032     220.778 201.808 168.621  1.00 20.50           O  
ATOM  20647  CB  CYS C1032     220.043 203.631 171.267  1.00 20.29           C  
ATOM  20648  SG  CYS C1032     221.603 204.388 170.925  1.00 22.07           S  
ATOM  20649  N   VAL C1033     219.633 200.636 170.193  1.00 19.84           N  
ATOM  20650  CA  VAL C1033     220.197 199.315 169.849  1.00 19.93           C  
ATOM  20651  C   VAL C1033     219.341 198.538 168.860  1.00 19.97           C  
ATOM  20652  O   VAL C1033     219.847 198.046 167.855  1.00 20.40           O  
ATOM  20653  CB  VAL C1033     220.381 198.439 171.101  1.00 20.20           C  
ATOM  20654  CG1 VAL C1033     220.826 197.039 170.705  1.00 20.59           C  
ATOM  20655  CG2 VAL C1033     221.411 199.061 172.003  1.00 21.51           C  
ATOM  20656  N   LEU C1034     218.047 198.422 169.134  1.00 20.01           N  
ATOM  20657  CA  LEU C1034     217.181 197.631 168.264  1.00 19.83           C  
ATOM  20658  C   LEU C1034     216.861 198.367 166.973  1.00 19.71           C  
ATOM  20659  O   LEU C1034     216.479 197.752 165.985  1.00 20.04           O  
ATOM  20660  CB  LEU C1034     215.860 197.280 168.958  1.00 19.86           C  
ATOM  20661  CG  LEU C1034     215.823 196.016 169.830  1.00 20.46           C  
ATOM  20662  CD1 LEU C1034     216.726 196.185 171.035  1.00 20.76           C  
ATOM  20663  CD2 LEU C1034     214.398 195.768 170.276  1.00 20.40           C  
ATOM  20664  N   GLY C1035     216.998 199.683 166.990  1.00 19.42           N  
ATOM  20665  CA  GLY C1035     216.705 200.520 165.838  1.00 19.22           C  
ATOM  20666  C   GLY C1035     217.863 201.447 165.510  1.00 19.05           C  
ATOM  20667  O   GLY C1035     219.026 201.128 165.762  1.00 19.35           O  
ATOM  20668  N   GLN C1036     217.522 202.594 164.927  1.00 18.72           N  
ATOM  20669  CA  GLN C1036     218.459 203.666 164.627  1.00 18.49           C  
ATOM  20670  C   GLN C1036     217.797 204.992 164.952  1.00 18.44           C  
ATOM  20671  O   GLN C1036     216.994 205.503 164.172  1.00 18.56           O  
ATOM  20672  CB  GLN C1036     218.888 203.675 163.166  1.00 18.59           C  
ATOM  20673  CG  GLN C1036     219.890 204.778 162.863  1.00 18.41           C  
ATOM  20674  CD  GLN C1036     220.375 204.771 161.456  1.00 18.64           C  
ATOM  20675  OE1 GLN C1036     219.791 204.122 160.585  1.00 18.96           O  
ATOM  20676  NE2 GLN C1036     221.454 205.495 161.213  1.00 18.73           N  
ATOM  20677  N   SER C1037     218.116 205.532 166.111  1.00 18.54           N  
ATOM  20678  CA  SER C1037     217.518 206.766 166.582  1.00 18.03           C  
ATOM  20679  C   SER C1037     217.945 207.944 165.733  1.00 18.32           C  
ATOM  20680  O   SER C1037     219.088 208.007 165.285  1.00 18.53           O  
ATOM  20681  CB  SER C1037     217.917 207.031 168.008  1.00 18.75           C  
ATOM  20682  OG  SER C1037     217.370 208.232 168.450  1.00 18.45           O  
ATOM  20683  N   LYS C1038     217.032 208.887 165.536  1.00 17.97           N  
ATOM  20684  CA  LYS C1038     217.331 210.135 164.844  1.00 17.85           C  
ATOM  20685  C   LYS C1038     217.355 211.304 165.814  1.00 18.05           C  
ATOM  20686  O   LYS C1038     217.365 212.467 165.411  1.00 18.40           O  
ATOM  20687  CB  LYS C1038     216.324 210.391 163.733  1.00 17.52           C  
ATOM  20688  CG  LYS C1038     216.394 209.383 162.618  1.00 17.63           C  
ATOM  20689  CD  LYS C1038     215.445 209.734 161.488  1.00 16.82           C  
ATOM  20690  CE  LYS C1038     215.542 208.725 160.357  1.00 16.63           C  
ATOM  20691  NZ  LYS C1038     216.896 208.722 159.736  1.00 17.05           N  
ATOM  20692  N   ARG C1039     217.319 210.988 167.098  1.00 18.17           N  
ATOM  20693  CA  ARG C1039     217.302 211.991 168.143  1.00 17.96           C  
ATOM  20694  C   ARG C1039     218.720 212.480 168.423  1.00 18.23           C  
ATOM  20695  O   ARG C1039     219.634 211.683 168.661  1.00 18.63           O  
ATOM  20696  CB  ARG C1039     216.658 211.397 169.382  1.00 18.49           C  
ATOM  20697  CG  ARG C1039     215.170 211.067 169.215  1.00 18.46           C  
ATOM  20698  CD  ARG C1039     214.646 210.166 170.293  1.00 18.68           C  
ATOM  20699  NE  ARG C1039     214.631 210.813 171.574  1.00 18.77           N  
ATOM  20700  CZ  ARG C1039     214.277 210.249 172.734  1.00 18.90           C  
ATOM  20701  NH1 ARG C1039     213.879 208.998 172.800  1.00 19.01           N  
ATOM  20702  NH2 ARG C1039     214.344 210.983 173.819  1.00 19.03           N  
ATOM  20703  N   VAL C1040     218.910 213.788 168.372  1.00 18.32           N  
ATOM  20704  CA  VAL C1040     220.237 214.362 168.534  1.00 18.38           C  
ATOM  20705  C   VAL C1040     220.742 214.256 169.958  1.00 18.69           C  
ATOM  20706  O   VAL C1040     220.032 214.558 170.911  1.00 19.32           O  
ATOM  20707  CB  VAL C1040     220.242 215.822 168.058  1.00 18.67           C  
ATOM  20708  CG1 VAL C1040     221.574 216.484 168.352  1.00 19.05           C  
ATOM  20709  CG2 VAL C1040     219.982 215.846 166.571  1.00 19.16           C  
ATOM  20710  N   ASP C1041     221.965 213.749 170.079  1.00 18.83           N  
ATOM  20711  CA  ASP C1041     222.669 213.525 171.333  1.00 18.97           C  
ATOM  20712  C   ASP C1041     221.950 212.543 172.242  1.00 19.15           C  
ATOM  20713  O   ASP C1041     222.284 212.411 173.420  1.00 19.33           O  
ATOM  20714  CB  ASP C1041     222.952 214.834 172.054  1.00 19.16           C  
ATOM  20715  CG  ASP C1041     223.841 215.739 171.222  1.00 19.44           C  
ATOM  20716  OD1 ASP C1041     224.349 215.272 170.226  1.00 19.36           O  
ATOM  20717  OD2 ASP C1041     224.021 216.869 171.581  1.00 19.54           O  
ATOM  20718  N   PHE C1042     221.007 211.804 171.680  1.00 19.08           N  
ATOM  20719  CA  PHE C1042     220.347 210.729 172.403  1.00 18.95           C  
ATOM  20720  C   PHE C1042     221.293 209.538 172.578  1.00 19.36           C  
ATOM  20721  O   PHE C1042     221.320 208.905 173.637  1.00 20.09           O  
ATOM  20722  CB  PHE C1042     219.067 210.321 171.696  1.00 19.14           C  
ATOM  20723  CG  PHE C1042     218.286 209.265 172.390  1.00 18.76           C  
ATOM  20724  CD1 PHE C1042     217.657 209.518 173.589  1.00 18.82           C  
ATOM  20725  CD2 PHE C1042     218.164 208.015 171.835  1.00 19.18           C  
ATOM  20726  CE1 PHE C1042     216.930 208.537 174.218  1.00 19.07           C  
ATOM  20727  CE2 PHE C1042     217.439 207.034 172.455  1.00 19.84           C  
ATOM  20728  CZ  PHE C1042     216.820 207.297 173.650  1.00 19.06           C  
ATOM  20729  N   CYS C1043     222.057 209.225 171.520  1.00 19.59           N  
ATOM  20730  CA  CYS C1043     223.019 208.126 171.474  1.00 20.22           C  
ATOM  20731  C   CYS C1043     224.446 208.670 171.249  1.00 20.22           C  
ATOM  20732  O   CYS C1043     225.177 208.194 170.376  1.00 20.64           O  
ATOM  20733  CB  CYS C1043     222.628 207.125 170.375  1.00 20.69           C  
ATOM  20734  SG  CYS C1043     221.048 206.311 170.627  1.00 20.79           S  
ATOM  20735  N   GLY C1044     224.822 209.699 172.025  1.00 20.02           N  
ATOM  20736  CA  GLY C1044     226.142 210.331 171.963  1.00 19.89           C  
ATOM  20737  C   GLY C1044     226.186 211.433 170.918  1.00 19.41           C  
ATOM  20738  O   GLY C1044     225.263 211.579 170.117  1.00 19.51           O  
ATOM  20739  N   LYS C1045     227.266 212.205 170.930  1.00 19.24           N  
ATOM  20740  CA  LYS C1045     227.464 213.264 169.952  1.00 19.13           C  
ATOM  20741  C   LYS C1045     227.773 212.676 168.585  1.00 19.35           C  
ATOM  20742  O   LYS C1045     228.592 211.768 168.471  1.00 19.51           O  
ATOM  20743  CB  LYS C1045     228.603 214.190 170.382  1.00 19.14           C  
ATOM  20744  N   GLY C1046     227.144 213.218 167.550  1.00 19.37           N  
ATOM  20745  CA  GLY C1046     227.373 212.764 166.182  1.00 18.93           C  
ATOM  20746  C   GLY C1046     226.093 212.212 165.588  1.00 19.15           C  
ATOM  20747  O   GLY C1046     225.040 212.244 166.223  1.00 19.25           O  
ATOM  20748  N   TYR C1047     226.166 211.725 164.364  1.00 19.12           N  
ATOM  20749  CA  TYR C1047     224.982 211.189 163.728  1.00 18.69           C  
ATOM  20750  C   TYR C1047     224.908 209.712 164.044  1.00 18.77           C  
ATOM  20751  O   TYR C1047     225.797 208.936 163.703  1.00 20.09           O  
ATOM  20752  CB  TYR C1047     225.026 211.436 162.232  1.00 18.64           C  
ATOM  20753  CG  TYR C1047     224.956 212.879 161.879  1.00 18.52           C  
ATOM  20754  CD1 TYR C1047     226.115 213.594 161.700  1.00 18.71           C  
ATOM  20755  CD2 TYR C1047     223.741 213.494 161.741  1.00 18.55           C  
ATOM  20756  CE1 TYR C1047     226.060 214.922 161.382  1.00 18.57           C  
ATOM  20757  CE2 TYR C1047     223.682 214.828 161.424  1.00 18.27           C  
ATOM  20758  CZ  TYR C1047     224.838 215.540 161.245  1.00 18.39           C  
ATOM  20759  OH  TYR C1047     224.782 216.872 160.932  1.00 19.60           O  
ATOM  20760  N   HIS C1048     223.873 209.313 164.748  1.00 19.24           N  
ATOM  20761  CA  HIS C1048     223.806 207.944 165.213  1.00 19.18           C  
ATOM  20762  C   HIS C1048     223.719 206.939 164.100  1.00 19.21           C  
ATOM  20763  O   HIS C1048     222.868 207.072 163.224  1.00 19.16           O  
ATOM  20764  CB  HIS C1048     222.612 207.750 166.126  1.00 19.59           C  
ATOM  20765  CG  HIS C1048     222.602 206.434 166.731  1.00 19.43           C  
ATOM  20766  ND1 HIS C1048     223.634 205.987 167.480  1.00 19.81           N  
ATOM  20767  CD2 HIS C1048     221.684 205.454 166.728  1.00 19.34           C  
ATOM  20768  CE1 HIS C1048     223.368 204.794 167.921  1.00 20.39           C  
ATOM  20769  NE2 HIS C1048     222.182 204.435 167.484  1.00 19.95           N  
ATOM  20770  N   LEU C1049     224.559 205.905 164.169  1.00 19.38           N  
ATOM  20771  CA  LEU C1049     224.501 204.810 163.223  1.00 18.96           C  
ATOM  20772  C   LEU C1049     223.925 203.582 163.900  1.00 19.71           C  
ATOM  20773  O   LEU C1049     222.868 203.096 163.506  1.00 20.04           O  
ATOM  20774  CB  LEU C1049     225.897 204.482 162.683  1.00 19.09           C  
ATOM  20775  CG  LEU C1049     226.586 205.558 161.839  1.00 19.07           C  
ATOM  20776  CD1 LEU C1049     227.996 205.119 161.564  1.00 19.56           C  
ATOM  20777  CD2 LEU C1049     225.842 205.748 160.518  1.00 19.39           C  
ATOM  20778  N   MET C1050     224.607 203.097 164.932  1.00 19.55           N  
ATOM  20779  CA  MET C1050     224.209 201.871 165.621  1.00 19.64           C  
ATOM  20780  C   MET C1050     224.771 201.839 167.024  1.00 20.39           C  
ATOM  20781  O   MET C1050     225.631 202.645 167.362  1.00 21.23           O  
ATOM  20782  CB  MET C1050     224.693 200.645 164.854  1.00 20.05           C  
ATOM  20783  CG  MET C1050     226.201 200.547 164.735  1.00 20.43           C  
ATOM  20784  SD  MET C1050     226.745 199.135 163.782  1.00 21.84           S  
ATOM  20785  CE  MET C1050     228.517 199.462 163.706  1.00 22.48           C  
ATOM  20786  N   SER C1051     224.303 200.914 167.842  1.00 20.39           N  
ATOM  20787  CA  SER C1051     224.875 200.770 169.171  1.00 20.39           C  
ATOM  20788  C   SER C1051     224.862 199.334 169.622  1.00 21.01           C  
ATOM  20789  O   SER C1051     224.086 198.522 169.120  1.00 21.63           O  
ATOM  20790  CB  SER C1051     224.134 201.611 170.180  1.00 20.92           C  
ATOM  20791  OG  SER C1051     222.823 201.191 170.310  1.00 21.14           O  
ATOM  20792  N   PHE C1052     225.713 199.035 170.590  1.00 21.59           N  
ATOM  20793  CA  PHE C1052     225.788 197.697 171.131  1.00 21.77           C  
ATOM  20794  C   PHE C1052     225.689 197.745 172.651  1.00 22.52           C  
ATOM  20795  O   PHE C1052     226.371 198.551 173.278  1.00 23.52           O  
ATOM  20796  CB  PHE C1052     227.124 197.078 170.762  1.00 22.27           C  
ATOM  20797  CG  PHE C1052     227.409 197.110 169.312  1.00 21.69           C  
ATOM  20798  CD1 PHE C1052     228.403 197.926 168.826  1.00 21.65           C  
ATOM  20799  CD2 PHE C1052     226.687 196.357 168.426  1.00 21.89           C  
ATOM  20800  CE1 PHE C1052     228.670 197.968 167.488  1.00 22.01           C  
ATOM  20801  CE2 PHE C1052     226.952 196.396 167.087  1.00 22.05           C  
ATOM  20802  CZ  PHE C1052     227.944 197.199 166.620  1.00 22.09           C  
ATOM  20803  N   PRO C1053     224.839 196.936 173.273  1.00 22.61           N  
ATOM  20804  CA  PRO C1053     224.696 196.816 174.699  1.00 22.93           C  
ATOM  20805  C   PRO C1053     225.820 195.972 175.252  1.00 24.11           C  
ATOM  20806  O   PRO C1053     226.283 195.053 174.576  1.00 24.33           O  
ATOM  20807  CB  PRO C1053     223.351 196.123 174.826  1.00 23.05           C  
ATOM  20808  CG  PRO C1053     223.272 195.264 173.592  1.00 22.86           C  
ATOM  20809  CD  PRO C1053     223.985 196.055 172.511  1.00 22.40           C  
ATOM  20810  N   GLN C1054     226.184 196.224 176.496  1.00 24.46           N  
ATOM  20811  CA  GLN C1054     227.103 195.395 177.257  1.00 25.55           C  
ATOM  20812  C   GLN C1054     226.536 195.250 178.664  1.00 25.99           C  
ATOM  20813  O   GLN C1054     225.946 196.190 179.199  1.00 26.04           O  
ATOM  20814  CB  GLN C1054     228.488 196.047 177.305  1.00 25.84           C  
ATOM  20815  CG  GLN C1054     229.174 196.236 175.950  1.00 25.56           C  
ATOM  20816  CD  GLN C1054     229.810 194.980 175.408  1.00 27.29           C  
ATOM  20817  OE1 GLN C1054     230.995 194.765 175.650  1.00 28.52           O  
ATOM  20818  NE2 GLN C1054     229.057 194.158 174.691  1.00 27.46           N  
ATOM  20819  N   SER C1055     226.704 194.094 179.287  1.00 26.61           N  
ATOM  20820  CA  SER C1055     226.247 193.967 180.662  1.00 26.12           C  
ATOM  20821  C   SER C1055     227.229 194.633 181.607  1.00 26.81           C  
ATOM  20822  O   SER C1055     228.395 194.829 181.268  1.00 27.86           O  
ATOM  20823  CB  SER C1055     226.067 192.517 181.031  1.00 27.10           C  
ATOM  20824  OG  SER C1055     227.282 191.850 181.043  1.00 28.26           O  
ATOM  20825  N   ALA C1056     226.761 194.963 182.800  1.00 26.75           N  
ATOM  20826  CA  ALA C1056     227.594 195.583 183.814  1.00 26.64           C  
ATOM  20827  C   ALA C1056     226.949 195.343 185.178  1.00 27.39           C  
ATOM  20828  O   ALA C1056     225.755 195.041 185.241  1.00 27.39           O  
ATOM  20829  CB  ALA C1056     227.748 197.066 183.525  1.00 26.43           C  
ATOM  20830  N   PRO C1057     227.692 195.422 186.281  1.00 26.95           N  
ATOM  20831  CA  PRO C1057     227.168 195.303 187.618  1.00 26.81           C  
ATOM  20832  C   PRO C1057     226.042 196.284 187.849  1.00 26.45           C  
ATOM  20833  O   PRO C1057     226.239 197.493 187.756  1.00 27.03           O  
ATOM  20834  CB  PRO C1057     228.385 195.660 188.463  1.00 27.29           C  
ATOM  20835  CG  PRO C1057     229.540 195.263 187.606  1.00 28.43           C  
ATOM  20836  CD  PRO C1057     229.130 195.606 186.209  1.00 28.04           C  
ATOM  20837  N   HIS C1058     224.873 195.764 188.169  1.00 26.26           N  
ATOM  20838  CA  HIS C1058     223.708 196.576 188.481  1.00 26.08           C  
ATOM  20839  C   HIS C1058     223.358 197.605 187.412  1.00 25.51           C  
ATOM  20840  O   HIS C1058     222.744 198.633 187.727  1.00 26.30           O  
ATOM  20841  CB  HIS C1058     223.924 197.288 189.813  1.00 26.49           C  
ATOM  20842  CG  HIS C1058     224.173 196.350 190.928  1.00 26.77           C  
ATOM  20843  ND1 HIS C1058     223.210 195.488 191.398  1.00 26.56           N  
ATOM  20844  CD2 HIS C1058     225.275 196.124 191.671  1.00 27.12           C  
ATOM  20845  CE1 HIS C1058     223.707 194.774 192.384  1.00 26.73           C  
ATOM  20846  NE2 HIS C1058     224.960 195.140 192.571  1.00 27.01           N  
ATOM  20847  N   GLY C1059     223.695 197.338 186.154  1.00 25.69           N  
ATOM  20848  CA  GLY C1059     223.399 198.326 185.132  1.00 25.46           C  
ATOM  20849  C   GLY C1059     223.759 197.885 183.732  1.00 25.26           C  
ATOM  20850  O   GLY C1059     224.089 196.725 183.489  1.00 25.81           O  
ATOM  20851  N   VAL C1060     223.638 198.815 182.796  1.00 25.10           N  
ATOM  20852  CA  VAL C1060     223.895 198.535 181.394  1.00 24.77           C  
ATOM  20853  C   VAL C1060     224.836 199.563 180.818  1.00 24.38           C  
ATOM  20854  O   VAL C1060     224.763 200.748 181.147  1.00 25.07           O  
ATOM  20855  CB  VAL C1060     222.579 198.521 180.592  1.00 24.69           C  
ATOM  20856  CG1 VAL C1060     221.935 199.874 180.605  1.00 24.43           C  
ATOM  20857  CG2 VAL C1060     222.829 198.077 179.157  1.00 24.29           C  
ATOM  20858  N   VAL C1061     225.713 199.111 179.949  1.00 24.58           N  
ATOM  20859  CA  VAL C1061     226.631 199.995 179.274  1.00 23.96           C  
ATOM  20860  C   VAL C1061     226.434 199.927 177.779  1.00 24.49           C  
ATOM  20861  O   VAL C1061     226.392 198.847 177.196  1.00 25.08           O  
ATOM  20862  CB  VAL C1061     228.065 199.632 179.659  1.00 25.35           C  
ATOM  20863  CG1 VAL C1061     229.042 200.472 178.901  1.00 25.12           C  
ATOM  20864  CG2 VAL C1061     228.218 199.852 181.142  1.00 25.93           C  
ATOM  20865  N   PHE C1062     226.280 201.077 177.151  1.00 23.44           N  
ATOM  20866  CA  PHE C1062     226.092 201.089 175.717  1.00 22.62           C  
ATOM  20867  C   PHE C1062     227.312 201.626 175.016  1.00 23.42           C  
ATOM  20868  O   PHE C1062     227.907 202.615 175.441  1.00 23.70           O  
ATOM  20869  CB  PHE C1062     224.923 201.978 175.325  1.00 22.72           C  
ATOM  20870  CG  PHE C1062     223.598 201.543 175.792  1.00 22.95           C  
ATOM  20871  CD1 PHE C1062     223.082 202.034 176.964  1.00 23.05           C  
ATOM  20872  CD2 PHE C1062     222.851 200.660 175.062  1.00 22.77           C  
ATOM  20873  CE1 PHE C1062     221.841 201.650 177.395  1.00 22.93           C  
ATOM  20874  CE2 PHE C1062     221.608 200.274 175.495  1.00 22.28           C  
ATOM  20875  CZ  PHE C1062     221.104 200.773 176.663  1.00 22.32           C  
ATOM  20876  N   LEU C1063     227.642 201.017 173.896  1.00 22.83           N  
ATOM  20877  CA  LEU C1063     228.672 201.543 173.027  1.00 22.59           C  
ATOM  20878  C   LEU C1063     227.998 202.148 171.818  1.00 22.55           C  
ATOM  20879  O   LEU C1063     227.431 201.432 170.993  1.00 22.67           O  
ATOM  20880  CB  LEU C1063     229.633 200.436 172.603  1.00 23.17           C  
ATOM  20881  CG  LEU C1063     230.319 199.676 173.737  1.00 23.94           C  
ATOM  20882  CD1 LEU C1063     231.201 198.604 173.139  1.00 25.62           C  
ATOM  20883  CD2 LEU C1063     231.128 200.638 174.589  1.00 24.91           C  
ATOM  20884  N   HIS C1064     228.022 203.466 171.726  1.00 22.10           N  
ATOM  20885  CA  HIS C1064     227.315 204.138 170.652  1.00 21.01           C  
ATOM  20886  C   HIS C1064     228.250 204.440 169.516  1.00 21.67           C  
ATOM  20887  O   HIS C1064     229.265 205.109 169.707  1.00 22.11           O  
ATOM  20888  CB  HIS C1064     226.707 205.453 171.108  1.00 21.30           C  
ATOM  20889  CG  HIS C1064     225.772 205.356 172.231  1.00 21.46           C  
ATOM  20890  ND1 HIS C1064     224.730 204.471 172.261  1.00 21.66           N  
ATOM  20891  CD2 HIS C1064     225.697 206.070 173.365  1.00 21.69           C  
ATOM  20892  CE1 HIS C1064     224.043 204.653 173.373  1.00 21.85           C  
ATOM  20893  NE2 HIS C1064     224.617 205.617 174.058  1.00 21.83           N  
ATOM  20894  N   VAL C1065     227.914 203.954 168.333  1.00 20.78           N  
ATOM  20895  CA  VAL C1065     228.743 204.148 167.163  1.00 20.36           C  
ATOM  20896  C   VAL C1065     228.154 205.270 166.341  1.00 20.24           C  
ATOM  20897  O   VAL C1065     227.019 205.170 165.862  1.00 20.72           O  
ATOM  20898  CB  VAL C1065     228.770 202.870 166.327  1.00 20.71           C  
ATOM  20899  CG1 VAL C1065     229.682 203.051 165.138  1.00 20.79           C  
ATOM  20900  CG2 VAL C1065     229.180 201.709 167.191  1.00 21.43           C  
ATOM  20901  N   THR C1066     228.913 206.342 166.178  1.00 20.35           N  
ATOM  20902  CA  THR C1066     228.390 207.513 165.502  1.00 19.43           C  
ATOM  20903  C   THR C1066     229.274 208.009 164.370  1.00 19.67           C  
ATOM  20904  O   THR C1066     230.497 207.866 164.392  1.00 20.24           O  
ATOM  20905  CB  THR C1066     228.217 208.651 166.509  1.00 19.59           C  
ATOM  20906  OG1 THR C1066     229.493 208.985 167.038  1.00 20.24           O  
ATOM  20907  CG2 THR C1066     227.294 208.263 167.648  1.00 19.97           C  
ATOM  20908  N   TYR C1067     228.636 208.658 163.410  1.00 19.26           N  
ATOM  20909  CA  TYR C1067     229.304 209.281 162.284  1.00 18.73           C  
ATOM  20910  C   TYR C1067     229.571 210.739 162.581  1.00 19.33           C  
ATOM  20911  O   TYR C1067     228.654 211.513 162.855  1.00 19.73           O  
ATOM  20912  CB  TYR C1067     228.423 209.143 161.045  1.00 19.27           C  
ATOM  20913  CG  TYR C1067     228.894 209.847 159.806  1.00 19.15           C  
ATOM  20914  CD1 TYR C1067     229.667 209.195 158.887  1.00 19.40           C  
ATOM  20915  CD2 TYR C1067     228.524 211.153 159.586  1.00 19.14           C  
ATOM  20916  CE1 TYR C1067     230.062 209.847 157.749  1.00 19.39           C  
ATOM  20917  CE2 TYR C1067     228.924 211.803 158.456  1.00 19.22           C  
ATOM  20918  CZ  TYR C1067     229.689 211.153 157.537  1.00 19.23           C  
ATOM  20919  OH  TYR C1067     230.089 211.799 156.391  1.00 19.97           O  
ATOM  20920  N   VAL C1068     230.831 211.122 162.555  1.00 19.03           N  
ATOM  20921  CA  VAL C1068     231.185 212.488 162.864  1.00 18.75           C  
ATOM  20922  C   VAL C1068     231.953 213.124 161.709  1.00 19.36           C  
ATOM  20923  O   VAL C1068     233.022 212.633 161.352  1.00 20.25           O  
ATOM  20924  CB  VAL C1068     232.036 212.523 164.134  1.00 19.02           C  
ATOM  20925  CG1 VAL C1068     232.420 213.945 164.465  1.00 19.70           C  
ATOM  20926  CG2 VAL C1068     231.252 211.904 165.272  1.00 19.52           C  
ATOM  20927  N   PRO C1069     231.443 214.195 161.099  1.00 18.88           N  
ATOM  20928  CA  PRO C1069     232.076 214.947 160.036  1.00 19.18           C  
ATOM  20929  C   PRO C1069     233.453 215.390 160.493  1.00 19.54           C  
ATOM  20930  O   PRO C1069     233.610 215.765 161.657  1.00 19.91           O  
ATOM  20931  CB  PRO C1069     231.114 216.116 159.852  1.00 19.21           C  
ATOM  20932  CG  PRO C1069     229.784 215.587 160.320  1.00 19.03           C  
ATOM  20933  CD  PRO C1069     230.108 214.670 161.457  1.00 19.01           C  
ATOM  20934  N   ALA C1070     234.448 215.350 159.616  1.00 19.58           N  
ATOM  20935  CA  ALA C1070     235.809 215.693 160.009  1.00 19.72           C  
ATOM  20936  C   ALA C1070     236.765 216.723 159.427  1.00 20.26           C  
ATOM  20937  O   ALA C1070     237.342 217.525 160.160  1.00 20.31           O  
ATOM  20938  CB  ALA C1070     236.705 214.475 159.871  1.00 20.01           C  
ATOM  20939  N   GLN C1071     236.960 216.701 158.117  1.00 20.21           N  
ATOM  20940  CA  GLN C1071     237.889 217.628 157.493  1.00 20.06           C  
ATOM  20941  C   GLN C1071     236.798 218.301 156.698  1.00 20.34           C  
ATOM  20942  O   GLN C1071     235.849 217.642 156.271  1.00 21.02           O  
ATOM  20943  CB  GLN C1071     238.952 217.060 156.559  1.00 20.38           C  
ATOM  20944  CG  GLN C1071     240.137 216.461 157.281  1.00 20.55           C  
ATOM  20945  CD  GLN C1071     241.151 215.871 156.336  1.00 21.27           C  
ATOM  20946  OE1 GLN C1071     240.805 215.313 155.294  1.00 21.44           O  
ATOM  20947  NE2 GLN C1071     242.421 215.993 156.690  1.00 21.55           N  
ATOM  20948  N   GLU C1072     236.909 219.614 156.522  1.00 20.12           N  
ATOM  20949  CA  GLU C1072     235.886 220.400 155.843  1.00 20.07           C  
ATOM  20950  C   GLU C1072     236.481 221.474 154.963  1.00 20.23           C  
ATOM  20951  O   GLU C1072     237.628 221.876 155.157  1.00 20.52           O  
ATOM  20952  CB  GLU C1072     234.979 221.062 156.874  1.00 19.73           C  
ATOM  20953  CG  GLU C1072     235.715 222.069 157.721  1.00 19.47           C  
ATOM  20954  CD  GLU C1072     234.888 222.717 158.765  1.00 19.63           C  
ATOM  20955  OE1 GLU C1072     234.593 222.092 159.752  1.00 18.44           O  
ATOM  20956  OE2 GLU C1072     234.541 223.857 158.573  1.00 19.77           O  
ATOM  20957  N   LYS C1073     235.691 221.950 154.006  1.00 20.30           N  
ATOM  20958  CA  LYS C1073     236.106 223.032 153.126  1.00 20.42           C  
ATOM  20959  C   LYS C1073     235.055 224.143 153.001  1.00 21.06           C  
ATOM  20960  O   LYS C1073     233.855 223.889 153.116  1.00 21.29           O  
ATOM  20961  CB  LYS C1073     236.440 222.480 151.745  1.00 21.02           C  
ATOM  20962  CG  LYS C1073     237.783 221.794 151.639  1.00 21.25           C  
ATOM  20963  CD  LYS C1073     238.024 221.276 150.223  1.00 21.42           C  
ATOM  20964  CE  LYS C1073     238.316 222.421 149.257  1.00 21.36           C  
ATOM  20965  NZ  LYS C1073     238.841 221.936 147.959  1.00 22.09           N  
ATOM  20966  N   ASN C1074     235.538 225.378 152.737  1.00 20.80           N  
ATOM  20967  CA  ASN C1074     234.721 226.571 152.504  1.00 20.57           C  
ATOM  20968  C   ASN C1074     234.320 226.677 151.022  1.00 21.10           C  
ATOM  20969  O   ASN C1074     235.169 226.952 150.170  1.00 22.22           O  
ATOM  20970  CB  ASN C1074     235.481 227.840 152.903  1.00 20.96           C  
ATOM  20971  CG  ASN C1074     235.610 228.092 154.413  1.00 20.87           C  
ATOM  20972  OD1 ASN C1074     234.971 227.448 155.261  1.00 20.82           O  
ATOM  20973  ND2 ASN C1074     236.458 229.066 154.728  1.00 20.81           N  
ATOM  20974  N   PHE C1075     233.029 226.479 150.717  1.00 21.18           N  
ATOM  20975  CA  PHE C1075     232.499 226.542 149.347  1.00 20.79           C  
ATOM  20976  C   PHE C1075     231.582 227.737 149.188  1.00 21.38           C  
ATOM  20977  O   PHE C1075     230.918 228.147 150.137  1.00 22.48           O  
ATOM  20978  CB  PHE C1075     231.719 225.287 149.007  1.00 21.39           C  
ATOM  20979  CG  PHE C1075     232.540 224.077 148.995  1.00 21.02           C  
ATOM  20980  CD1 PHE C1075     232.582 223.261 150.094  1.00 21.18           C  
ATOM  20981  CD2 PHE C1075     233.286 223.750 147.898  1.00 21.81           C  
ATOM  20982  CE1 PHE C1075     233.352 222.133 150.098  1.00 21.39           C  
ATOM  20983  CE2 PHE C1075     234.061 222.628 147.899  1.00 21.61           C  
ATOM  20984  CZ  PHE C1075     234.094 221.818 149.005  1.00 21.21           C  
ATOM  20985  N   THR C1076     231.516 228.284 147.988  1.00 21.56           N  
ATOM  20986  CA  THR C1076     230.551 229.333 147.718  1.00 21.41           C  
ATOM  20987  C   THR C1076     229.245 228.646 147.385  1.00 21.84           C  
ATOM  20988  O   THR C1076     229.252 227.571 146.788  1.00 22.29           O  
ATOM  20989  CB  THR C1076     231.031 230.266 146.596  1.00 22.06           C  
ATOM  20990  OG1 THR C1076     232.224 230.931 147.018  1.00 22.44           O  
ATOM  20991  CG2 THR C1076     229.972 231.300 146.252  1.00 22.37           C  
ATOM  20992  N   THR C1077     228.127 229.204 147.810  1.00 21.50           N  
ATOM  20993  CA  THR C1077     226.852 228.550 147.545  1.00 21.19           C  
ATOM  20994  C   THR C1077     225.794 229.446 146.933  1.00 21.53           C  
ATOM  20995  O   THR C1077     226.001 230.643 146.742  1.00 21.87           O  
ATOM  20996  CB  THR C1077     226.304 227.913 148.816  1.00 21.19           C  
ATOM  20997  OG1 THR C1077     225.170 227.126 148.497  1.00 21.80           O  
ATOM  20998  CG2 THR C1077     225.941 228.955 149.814  1.00 21.54           C  
ATOM  20999  N   ALA C1078     224.663 228.835 146.602  1.00 21.42           N  
ATOM  21000  CA  ALA C1078     223.512 229.521 146.038  1.00 21.35           C  
ATOM  21001  C   ALA C1078     222.269 228.672 146.274  1.00 21.60           C  
ATOM  21002  O   ALA C1078     222.355 227.450 146.201  1.00 22.34           O  
ATOM  21003  CB  ALA C1078     223.706 229.763 144.553  1.00 22.16           C  
ATOM  21004  N   PRO C1079     221.109 229.279 146.545  1.00 21.53           N  
ATOM  21005  CA  PRO C1079     219.834 228.621 146.765  1.00 21.81           C  
ATOM  21006  C   PRO C1079     219.246 228.001 145.513  1.00 22.31           C  
ATOM  21007  O   PRO C1079     218.421 227.094 145.589  1.00 22.45           O  
ATOM  21008  CB  PRO C1079     218.968 229.774 147.254  1.00 21.94           C  
ATOM  21009  CG  PRO C1079     219.592 231.006 146.672  1.00 22.31           C  
ATOM  21010  CD  PRO C1079     221.064 230.731 146.648  1.00 22.00           C  
ATOM  21011  N   ALA C1080     219.665 228.499 144.363  1.00 22.62           N  
ATOM  21012  CA  ALA C1080     219.131 228.048 143.092  1.00 22.40           C  
ATOM  21013  C   ALA C1080     220.018 228.516 141.968  1.00 23.31           C  
ATOM  21014  O   ALA C1080     220.834 229.424 142.148  1.00 23.77           O  
ATOM  21015  CB  ALA C1080     217.724 228.564 142.889  1.00 23.15           C  
ATOM  21016  N   ILE C1081     219.832 227.938 140.798  1.00 23.71           N  
ATOM  21017  CA  ILE C1081     220.533 228.436 139.627  1.00 24.15           C  
ATOM  21018  C   ILE C1081     219.567 228.767 138.484  1.00 24.60           C  
ATOM  21019  O   ILE C1081     218.502 228.152 138.366  1.00 25.22           O  
ATOM  21020  CB  ILE C1081     221.584 227.419 139.174  1.00 24.39           C  
ATOM  21021  CG1 ILE C1081     220.884 226.124 138.851  1.00 24.85           C  
ATOM  21022  CG2 ILE C1081     222.657 227.241 140.253  1.00 24.31           C  
ATOM  21023  CD1 ILE C1081     221.733 225.073 138.280  1.00 26.01           C  
ATOM  21024  N   CYS C1082     219.953 229.726 137.628  1.00 25.33           N  
ATOM  21025  CA  CYS C1082     219.218 230.147 136.443  1.00 25.39           C  
ATOM  21026  C   CYS C1082     219.728 229.432 135.202  1.00 26.07           C  
ATOM  21027  O   CYS C1082     220.933 229.496 134.905  1.00 26.83           O  
ATOM  21028  CB  CYS C1082     219.331 231.662 136.215  1.00 26.32           C  
ATOM  21029  SG  CYS C1082     218.550 232.674 137.456  1.00 26.46           S  
ATOM  21030  N   HIS C1083     218.828 228.801 134.443  1.00 25.97           N  
ATOM  21031  CA  HIS C1083     219.184 228.119 133.190  1.00 26.18           C  
ATOM  21032  C   HIS C1083     218.632 228.893 131.993  1.00 26.86           C  
ATOM  21033  O   HIS C1083     219.343 229.683 131.374  1.00 26.60           O  
ATOM  21034  CB  HIS C1083     218.678 226.680 133.213  1.00 26.62           C  
ATOM  21035  CG  HIS C1083     219.050 225.886 132.024  1.00 27.16           C  
ATOM  21036  ND1 HIS C1083     220.351 225.500 131.753  1.00 27.91           N  
ATOM  21037  CD2 HIS C1083     218.297 225.384 131.033  1.00 27.51           C  
ATOM  21038  CE1 HIS C1083     220.368 224.806 130.633  1.00 28.25           C  
ATOM  21039  NE2 HIS C1083     219.137 224.722 130.180  1.00 28.40           N  
ATOM  21040  N   ASP C1084     217.343 228.729 131.718  1.00 26.61           N  
ATOM  21041  CA  ASP C1084     216.670 229.467 130.645  1.00 26.34           C  
ATOM  21042  C   ASP C1084     215.789 230.561 131.227  1.00 26.20           C  
ATOM  21043  O   ASP C1084     214.836 231.014 130.596  1.00 26.32           O  
ATOM  21044  CB  ASP C1084     215.801 228.548 129.790  1.00 26.28           C  
ATOM  21045  CG  ASP C1084     216.566 227.535 128.973  1.00 26.72           C  
ATOM  21046  OD1 ASP C1084     217.586 227.867 128.425  1.00 27.16           O  
ATOM  21047  OD2 ASP C1084     216.103 226.417 128.899  1.00 26.59           O  
ATOM  21048  N   GLY C1085     216.081 230.940 132.460  1.00 26.00           N  
ATOM  21049  CA  GLY C1085     215.276 231.897 133.206  1.00 26.18           C  
ATOM  21050  C   GLY C1085     214.492 231.135 134.259  1.00 25.69           C  
ATOM  21051  O   GLY C1085     213.962 231.712 135.212  1.00 25.46           O  
ATOM  21052  N   LYS C1086     214.462 229.819 134.083  1.00 25.57           N  
ATOM  21053  CA  LYS C1086     213.833 228.900 135.011  1.00 24.84           C  
ATOM  21054  C   LYS C1086     214.726 228.737 136.220  1.00 24.98           C  
ATOM  21055  O   LYS C1086     215.952 228.704 136.086  1.00 25.96           O  
ATOM  21056  CB  LYS C1086     213.604 227.538 134.358  1.00 25.08           C  
ATOM  21057  CG  LYS C1086     212.613 227.524 133.203  1.00 25.37           C  
ATOM  21058  CD  LYS C1086     212.344 226.086 132.735  1.00 25.07           C  
ATOM  21059  CE  LYS C1086     213.296 225.639 131.638  1.00 25.24           C  
ATOM  21060  NZ  LYS C1086     212.816 226.055 130.288  1.00 25.46           N  
ATOM  21061  N   ALA C1087     214.119 228.627 137.399  1.00 24.50           N  
ATOM  21062  CA  ALA C1087     214.890 228.425 138.621  1.00 23.57           C  
ATOM  21063  C   ALA C1087     214.977 226.952 138.984  1.00 23.77           C  
ATOM  21064  O   ALA C1087     213.968 226.302 139.265  1.00 24.25           O  
ATOM  21065  CB  ALA C1087     214.276 229.199 139.769  1.00 23.75           C  
ATOM  21066  N   HIS C1088     216.197 226.437 139.001  1.00 23.91           N  
ATOM  21067  CA  HIS C1088     216.456 225.040 139.312  1.00 23.73           C  
ATOM  21068  C   HIS C1088     216.959 224.877 140.738  1.00 23.71           C  
ATOM  21069  O   HIS C1088     217.915 225.536 141.150  1.00 24.51           O  
ATOM  21070  CB  HIS C1088     217.496 224.462 138.354  1.00 24.69           C  
ATOM  21071  CG  HIS C1088     217.055 224.335 136.946  1.00 25.05           C  
ATOM  21072  ND1 HIS C1088     216.819 223.121 136.361  1.00 25.64           N  
ATOM  21073  CD2 HIS C1088     216.801 225.260 136.002  1.00 25.47           C  
ATOM  21074  CE1 HIS C1088     216.441 223.299 135.117  1.00 26.78           C  
ATOM  21075  NE2 HIS C1088     216.416 224.585 134.872  1.00 25.86           N  
ATOM  21076  N   PHE C1089     216.318 223.994 141.489  1.00 23.36           N  
ATOM  21077  CA  PHE C1089     216.683 223.721 142.875  1.00 23.02           C  
ATOM  21078  C   PHE C1089     217.150 222.275 142.975  1.00 24.52           C  
ATOM  21079  O   PHE C1089     216.668 221.448 142.212  1.00 21.91           O  
ATOM  21080  CB  PHE C1089     215.476 223.873 143.781  1.00 22.63           C  
ATOM  21081  CG  PHE C1089     214.876 225.200 143.822  1.00 22.26           C  
ATOM  21082  CD1 PHE C1089     213.857 225.500 142.971  1.00 22.70           C  
ATOM  21083  CD2 PHE C1089     215.299 226.153 144.711  1.00 22.04           C  
ATOM  21084  CE1 PHE C1089     213.269 226.723 143.003  1.00 22.37           C  
ATOM  21085  CE2 PHE C1089     214.704 227.386 144.740  1.00 22.03           C  
ATOM  21086  CZ  PHE C1089     213.687 227.664 143.884  1.00 21.91           C  
ATOM  21087  N   PRO C1090     218.062 221.907 143.875  1.00 22.74           N  
ATOM  21088  CA  PRO C1090     218.496 220.541 144.078  1.00 22.51           C  
ATOM  21089  C   PRO C1090     217.356 219.690 144.603  1.00 22.45           C  
ATOM  21090  O   PRO C1090     216.598 220.139 145.465  1.00 22.85           O  
ATOM  21091  CB  PRO C1090     219.575 220.686 145.147  1.00 22.61           C  
ATOM  21092  CG  PRO C1090     219.968 222.131 145.114  1.00 22.87           C  
ATOM  21093  CD  PRO C1090     218.707 222.868 144.750  1.00 22.96           C  
ATOM  21094  N   ARG C1091     217.266 218.443 144.160  1.00 22.60           N  
ATOM  21095  CA  ARG C1091     216.258 217.563 144.736  1.00 22.67           C  
ATOM  21096  C   ARG C1091     216.657 217.112 146.126  1.00 22.32           C  
ATOM  21097  O   ARG C1091     215.814 216.982 147.011  1.00 22.72           O  
ATOM  21098  CB  ARG C1091     216.015 216.327 143.887  1.00 22.85           C  
ATOM  21099  CG  ARG C1091     215.247 216.546 142.606  1.00 23.19           C  
ATOM  21100  CD  ARG C1091     214.943 215.252 141.945  1.00 23.85           C  
ATOM  21101  NE  ARG C1091     214.035 215.409 140.824  1.00 23.67           N  
ATOM  21102  CZ  ARG C1091     214.408 215.737 139.578  1.00 24.68           C  
ATOM  21103  NH1 ARG C1091     215.665 215.951 139.312  1.00 24.72           N  
ATOM  21104  NH2 ARG C1091     213.507 215.848 138.621  1.00 24.16           N  
ATOM  21105  N   GLU C1092     217.939 216.852 146.313  1.00 22.06           N  
ATOM  21106  CA  GLU C1092     218.436 216.366 147.587  1.00 21.88           C  
ATOM  21107  C   GLU C1092     219.911 216.694 147.768  1.00 21.66           C  
ATOM  21108  O   GLU C1092     220.766 215.811 147.762  1.00 21.77           O  
ATOM  21109  CB  GLU C1092     218.150 214.860 147.721  1.00 21.94           C  
ATOM  21110  N   GLY C1093     220.208 217.975 147.914  1.00 21.61           N  
ATOM  21111  CA  GLY C1093     221.587 218.424 148.021  1.00 21.39           C  
ATOM  21112  C   GLY C1093     221.673 219.937 148.031  1.00 21.58           C  
ATOM  21113  O   GLY C1093     220.660 220.630 148.124  1.00 21.84           O  
ATOM  21114  N   VAL C1094     222.890 220.448 147.960  1.00 21.71           N  
ATOM  21115  CA  VAL C1094     223.125 221.882 147.961  1.00 21.58           C  
ATOM  21116  C   VAL C1094     224.056 222.277 146.828  1.00 22.23           C  
ATOM  21117  O   VAL C1094     224.985 221.539 146.502  1.00 23.29           O  
ATOM  21118  CB  VAL C1094     223.694 222.315 149.322  1.00 21.42           C  
ATOM  21119  CG1 VAL C1094     225.016 221.634 149.590  1.00 21.78           C  
ATOM  21120  CG2 VAL C1094     223.856 223.822 149.361  1.00 22.41           C  
ATOM  21121  N   PHE C1095     223.817 223.431 146.214  1.00 22.40           N  
ATOM  21122  CA  PHE C1095     224.713 223.871 145.156  1.00 22.00           C  
ATOM  21123  C   PHE C1095     225.965 224.471 145.744  1.00 22.27           C  
ATOM  21124  O   PHE C1095     225.913 225.228 146.708  1.00 23.03           O  
ATOM  21125  CB  PHE C1095     224.065 224.907 144.248  1.00 22.39           C  
ATOM  21126  CG  PHE C1095     222.991 224.389 143.374  1.00 23.00           C  
ATOM  21127  CD1 PHE C1095     221.784 225.019 143.335  1.00 23.29           C  
ATOM  21128  CD2 PHE C1095     223.177 223.275 142.585  1.00 23.80           C  
ATOM  21129  CE1 PHE C1095     220.793 224.558 142.526  1.00 23.50           C  
ATOM  21130  CE2 PHE C1095     222.173 222.815 141.784  1.00 24.01           C  
ATOM  21131  CZ  PHE C1095     220.983 223.467 141.760  1.00 23.89           C  
ATOM  21132  N   VAL C1096     227.098 224.136 145.160  1.00 22.69           N  
ATOM  21133  CA  VAL C1096     228.367 224.659 145.612  1.00 22.13           C  
ATOM  21134  C   VAL C1096     229.206 225.170 144.468  1.00 23.22           C  
ATOM  21135  O   VAL C1096     229.043 224.738 143.330  1.00 23.93           O  
ATOM  21136  CB  VAL C1096     229.155 223.572 146.346  1.00 22.44           C  
ATOM  21137  CG1 VAL C1096     228.414 223.128 147.536  1.00 22.51           C  
ATOM  21138  CG2 VAL C1096     229.378 222.402 145.437  1.00 23.01           C  
ATOM  21139  N   SER C1097     230.160 226.017 144.784  1.00 22.67           N  
ATOM  21140  CA  SER C1097     231.115 226.489 143.805  1.00 22.51           C  
ATOM  21141  C   SER C1097     232.527 226.491 144.346  1.00 23.35           C  
ATOM  21142  O   SER C1097     232.782 226.970 145.458  1.00 23.79           O  
ATOM  21143  CB  SER C1097     230.758 227.874 143.333  1.00 23.66           C  
ATOM  21144  OG  SER C1097     231.812 228.442 142.607  1.00 24.57           O  
ATOM  21145  N   ASN C1098     233.463 225.988 143.527  1.00 24.50           N  
ATOM  21146  CA  ASN C1098     234.891 225.953 143.856  1.00 24.96           C  
ATOM  21147  C   ASN C1098     235.642 227.194 143.351  1.00 25.52           C  
ATOM  21148  O   ASN C1098     236.868 227.272 143.459  1.00 26.07           O  
ATOM  21149  CB  ASN C1098     235.532 224.659 143.335  1.00 25.59           C  
ATOM  21150  CG  ASN C1098     235.703 224.577 141.796  1.00 26.24           C  
ATOM  21151  OD1 ASN C1098     235.301 225.484 141.032  1.00 26.09           O  
ATOM  21152  ND2 ASN C1098     236.315 223.473 141.354  1.00 26.50           N  
ATOM  21153  N   GLY C1099     234.901 228.192 142.832  1.00 25.47           N  
ATOM  21154  CA  GLY C1099     235.415 229.457 142.319  1.00 25.83           C  
ATOM  21155  C   GLY C1099     235.265 229.576 140.809  1.00 26.24           C  
ATOM  21156  O   GLY C1099     235.212 230.691 140.289  1.00 26.62           O  
ATOM  21157  N   THR C1100     235.170 228.453 140.101  1.00 25.92           N  
ATOM  21158  CA  THR C1100     234.974 228.537 138.655  1.00 26.10           C  
ATOM  21159  C   THR C1100     233.795 227.708 138.165  1.00 26.05           C  
ATOM  21160  O   THR C1100     233.145 228.068 137.185  1.00 25.96           O  
ATOM  21161  CB  THR C1100     236.237 228.105 137.892  1.00 26.24           C  
ATOM  21162  OG1 THR C1100     236.529 226.737 138.182  1.00 26.74           O  
ATOM  21163  CG2 THR C1100     237.420 228.963 138.302  1.00 26.45           C  
ATOM  21164  N   HIS C1101     233.500 226.612 138.854  1.00 25.73           N  
ATOM  21165  CA  HIS C1101     232.424 225.733 138.418  1.00 25.12           C  
ATOM  21166  C   HIS C1101     231.449 225.424 139.528  1.00 25.21           C  
ATOM  21167  O   HIS C1101     231.827 225.279 140.693  1.00 25.00           O  
ATOM  21168  CB  HIS C1101     232.971 224.407 137.889  1.00 25.86           C  
ATOM  21169  CG  HIS C1101     233.723 224.488 136.614  1.00 26.35           C  
ATOM  21170  ND1 HIS C1101     235.006 224.964 136.538  1.00 26.53           N  
ATOM  21171  CD2 HIS C1101     233.378 224.134 135.359  1.00 26.66           C  
ATOM  21172  CE1 HIS C1101     235.423 224.896 135.289  1.00 26.80           C  
ATOM  21173  NE2 HIS C1101     234.452 224.398 134.554  1.00 26.94           N  
ATOM  21174  N   TRP C1102     230.187 225.300 139.142  1.00 24.53           N  
ATOM  21175  CA  TRP C1102     229.122 224.950 140.059  1.00 24.31           C  
ATOM  21176  C   TRP C1102     228.793 223.476 139.994  1.00 24.55           C  
ATOM  21177  O   TRP C1102     228.679 222.908 138.909  1.00 25.23           O  
ATOM  21178  CB  TRP C1102     227.879 225.758 139.742  1.00 24.58           C  
ATOM  21179  CG  TRP C1102     227.985 227.164 140.135  1.00 24.16           C  
ATOM  21180  CD1 TRP C1102     228.433 228.188 139.379  1.00 24.56           C  
ATOM  21181  CD2 TRP C1102     227.634 227.727 141.402  1.00 23.64           C  
ATOM  21182  NE1 TRP C1102     228.394 229.347 140.094  1.00 23.78           N  
ATOM  21183  CE2 TRP C1102     227.911 229.081 141.336  1.00 23.53           C  
ATOM  21184  CE3 TRP C1102     227.123 227.196 142.574  1.00 23.71           C  
ATOM  21185  CZ2 TRP C1102     227.699 229.919 142.403  1.00 23.50           C  
ATOM  21186  CZ3 TRP C1102     226.910 228.032 143.643  1.00 23.08           C  
ATOM  21187  CH2 TRP C1102     227.193 229.359 143.561  1.00 22.85           C  
ATOM  21188  N   PHE C1103     228.617 222.886 141.161  1.00 24.08           N  
ATOM  21189  CA  PHE C1103     228.318 221.477 141.318  1.00 23.53           C  
ATOM  21190  C   PHE C1103     227.217 221.289 142.319  1.00 23.74           C  
ATOM  21191  O   PHE C1103     226.922 222.187 143.103  1.00 24.15           O  
ATOM  21192  CB  PHE C1103     229.529 220.713 141.813  1.00 24.00           C  
ATOM  21193  CG  PHE C1103     230.690 220.885 140.978  1.00 24.03           C  
ATOM  21194  CD1 PHE C1103     231.604 221.850 141.288  1.00 24.46           C  
ATOM  21195  CD2 PHE C1103     230.885 220.105 139.870  1.00 24.47           C  
ATOM  21196  CE1 PHE C1103     232.701 222.038 140.515  1.00 25.36           C  
ATOM  21197  CE2 PHE C1103     231.986 220.289 139.083  1.00 25.55           C  
ATOM  21198  CZ  PHE C1103     232.895 221.260 139.409  1.00 25.53           C  
ATOM  21199  N   VAL C1104     226.609 220.132 142.312  1.00 23.86           N  
ATOM  21200  CA  VAL C1104     225.647 219.819 143.349  1.00 22.94           C  
ATOM  21201  C   VAL C1104     226.195 218.676 144.176  1.00 23.07           C  
ATOM  21202  O   VAL C1104     226.725 217.709 143.629  1.00 24.21           O  
ATOM  21203  CB  VAL C1104     224.270 219.500 142.744  1.00 23.67           C  
ATOM  21204  CG1 VAL C1104     224.364 218.329 141.774  1.00 24.79           C  
ATOM  21205  CG2 VAL C1104     223.280 219.211 143.852  1.00 23.03           C  
ATOM  21206  N   THR C1105     226.126 218.807 145.491  1.00 22.69           N  
ATOM  21207  CA  THR C1105     226.676 217.798 146.382  1.00 22.21           C  
ATOM  21208  C   THR C1105     225.746 217.459 147.525  1.00 21.70           C  
ATOM  21209  O   THR C1105     224.964 218.301 147.979  1.00 22.39           O  
ATOM  21210  CB  THR C1105     228.034 218.259 146.936  1.00 21.83           C  
ATOM  21211  OG1 THR C1105     228.577 217.252 147.786  1.00 22.33           O  
ATOM  21212  CG2 THR C1105     227.920 219.543 147.693  1.00 22.18           C  
ATOM  21213  N   GLN C1106     225.832 216.220 148.004  1.00 21.80           N  
ATOM  21214  CA  GLN C1106     225.043 215.800 149.148  1.00 21.18           C  
ATOM  21215  C   GLN C1106     225.426 216.635 150.361  1.00 20.70           C  
ATOM  21216  O   GLN C1106     226.586 217.000 150.539  1.00 21.09           O  
ATOM  21217  CB  GLN C1106     225.196 214.300 149.402  1.00 20.81           C  
ATOM  21218  CG  GLN C1106     226.551 213.853 149.844  1.00 20.65           C  
ATOM  21219  CD  GLN C1106     226.604 212.382 150.002  1.00 20.10           C  
ATOM  21220  OE1 GLN C1106     225.725 211.801 150.641  1.00 19.91           O  
ATOM  21221  NE2 GLN C1106     227.620 211.766 149.426  1.00 20.18           N  
ATOM  21222  N   ARG C1107     224.440 216.932 151.186  1.00 20.63           N  
ATOM  21223  CA  ARG C1107     224.589 217.866 152.292  1.00 20.12           C  
ATOM  21224  C   ARG C1107     225.696 217.532 153.294  1.00 20.03           C  
ATOM  21225  O   ARG C1107     226.367 218.434 153.790  1.00 20.30           O  
ATOM  21226  CB  ARG C1107     223.277 217.930 153.053  1.00 20.25           C  
ATOM  21227  CG  ARG C1107     222.098 218.452 152.241  1.00 20.71           C  
ATOM  21228  CD  ARG C1107     220.852 218.552 153.059  1.00 20.57           C  
ATOM  21229  NE  ARG C1107     219.635 218.433 152.248  1.00 21.01           N  
ATOM  21230  CZ  ARG C1107     219.161 219.327 151.361  1.00 21.36           C  
ATOM  21231  NH1 ARG C1107     219.805 220.433 151.103  1.00 21.43           N  
ATOM  21232  NH2 ARG C1107     218.028 219.067 150.734  1.00 21.34           N  
ATOM  21233  N   ASN C1108     225.879 216.254 153.617  1.00 20.11           N  
ATOM  21234  CA  ASN C1108     226.812 215.875 154.675  1.00 19.70           C  
ATOM  21235  C   ASN C1108     228.119 215.260 154.203  1.00 19.86           C  
ATOM  21236  O   ASN C1108     228.823 214.632 154.996  1.00 19.95           O  
ATOM  21237  CB  ASN C1108     226.131 214.939 155.647  1.00 19.07           C  
ATOM  21238  CG  ASN C1108     225.075 215.625 156.433  1.00 19.33           C  
ATOM  21239  OD1 ASN C1108     225.324 216.659 157.061  1.00 19.39           O  
ATOM  21240  ND2 ASN C1108     223.891 215.082 156.418  1.00 19.18           N  
ATOM  21241  N   PHE C1109     228.444 215.405 152.930  1.00 20.49           N  
ATOM  21242  CA  PHE C1109     229.698 214.848 152.439  1.00 19.96           C  
ATOM  21243  C   PHE C1109     230.042 215.413 151.075  1.00 20.41           C  
ATOM  21244  O   PHE C1109     229.281 215.252 150.126  1.00 21.07           O  
ATOM  21245  CB  PHE C1109     229.610 213.328 152.379  1.00 20.22           C  
ATOM  21246  CG  PHE C1109     230.885 212.676 152.065  1.00 20.21           C  
ATOM  21247  CD1 PHE C1109     231.836 212.478 153.042  1.00 20.38           C  
ATOM  21248  CD2 PHE C1109     231.146 212.258 150.797  1.00 20.63           C  
ATOM  21249  CE1 PHE C1109     233.026 211.872 152.737  1.00 20.48           C  
ATOM  21250  CE2 PHE C1109     232.330 211.652 150.488  1.00 20.71           C  
ATOM  21251  CZ  PHE C1109     233.273 211.459 151.464  1.00 20.54           C  
ATOM  21252  N   TYR C1110     231.191 216.051 150.953  1.00 20.49           N  
ATOM  21253  CA  TYR C1110     231.519 216.670 149.689  1.00 20.50           C  
ATOM  21254  C   TYR C1110     231.778 215.638 148.619  1.00 20.87           C  
ATOM  21255  O   TYR C1110     232.716 214.845 148.687  1.00 21.00           O  
ATOM  21256  CB  TYR C1110     232.714 217.590 149.830  1.00 20.74           C  
ATOM  21257  CG  TYR C1110     233.042 218.313 148.577  1.00 20.92           C  
ATOM  21258  CD1 TYR C1110     232.123 219.172 148.021  1.00 21.50           C  
ATOM  21259  CD2 TYR C1110     234.262 218.130 147.982  1.00 21.26           C  
ATOM  21260  CE1 TYR C1110     232.425 219.842 146.870  1.00 21.41           C  
ATOM  21261  CE2 TYR C1110     234.567 218.807 146.830  1.00 21.30           C  
ATOM  21262  CZ  TYR C1110     233.651 219.659 146.275  1.00 21.25           C  
ATOM  21263  OH  TYR C1110     233.956 220.345 145.126  1.00 21.94           O  
ATOM  21264  N   GLU C1111     230.934 215.679 147.613  1.00 21.30           N  
ATOM  21265  CA  GLU C1111     230.960 214.755 146.509  1.00 20.86           C  
ATOM  21266  C   GLU C1111     230.320 215.422 145.307  1.00 21.50           C  
ATOM  21267  O   GLU C1111     229.156 215.166 145.017  1.00 22.53           O  
ATOM  21268  CB  GLU C1111     230.192 213.497 146.874  1.00 20.61           C  
ATOM  21269  CG  GLU C1111     230.263 212.409 145.854  1.00 20.47           C  
ATOM  21270  CD  GLU C1111     229.528 211.206 146.283  1.00 20.65           C  
ATOM  21271  OE1 GLU C1111     228.337 211.288 146.442  1.00 20.58           O  
ATOM  21272  OE2 GLU C1111     230.152 210.196 146.470  1.00 20.36           O  
ATOM  21273  N   PRO C1112     231.027 216.319 144.633  1.00 21.42           N  
ATOM  21274  CA  PRO C1112     230.495 217.200 143.628  1.00 22.07           C  
ATOM  21275  C   PRO C1112     230.064 216.421 142.411  1.00 23.14           C  
ATOM  21276  O   PRO C1112     230.808 215.580 141.907  1.00 23.48           O  
ATOM  21277  CB  PRO C1112     231.684 218.106 143.326  1.00 22.52           C  
ATOM  21278  CG  PRO C1112     232.890 217.274 143.677  1.00 21.94           C  
ATOM  21279  CD  PRO C1112     232.457 216.395 144.824  1.00 21.62           C  
ATOM  21280  N   GLN C1113     228.894 216.752 141.902  1.00 23.45           N  
ATOM  21281  CA  GLN C1113     228.368 216.149 140.700  1.00 23.65           C  
ATOM  21282  C   GLN C1113     228.026 217.222 139.700  1.00 24.61           C  
ATOM  21283  O   GLN C1113     227.741 218.361 140.068  1.00 25.33           O  
ATOM  21284  CB  GLN C1113     227.127 215.326 141.013  1.00 24.16           C  
ATOM  21285  CG  GLN C1113     227.370 214.167 141.931  1.00 23.53           C  
ATOM  21286  CD  GLN C1113     226.112 213.382 142.173  1.00 24.73           C  
ATOM  21287  OE1 GLN C1113     225.034 213.959 142.341  1.00 25.24           O  
ATOM  21288  NE2 GLN C1113     226.227 212.059 142.188  1.00 24.64           N  
ATOM  21289  N   ILE C1114     228.016 216.867 138.433  1.00 24.78           N  
ATOM  21290  CA  ILE C1114     227.592 217.816 137.428  1.00 25.55           C  
ATOM  21291  C   ILE C1114     226.122 218.088 137.636  1.00 26.09           C  
ATOM  21292  O   ILE C1114     225.348 217.169 137.902  1.00 26.67           O  
ATOM  21293  CB  ILE C1114     227.848 217.291 136.008  1.00 25.85           C  
ATOM  21294  CG1 ILE C1114     229.365 217.038 135.798  1.00 25.37           C  
ATOM  21295  CG2 ILE C1114     227.292 218.265 134.960  1.00 27.44           C  
ATOM  21296  CD1 ILE C1114     230.265 218.261 135.962  1.00 25.50           C  
ATOM  21297  N   ILE C1115     225.744 219.347 137.553  1.00 26.24           N  
ATOM  21298  CA  ILE C1115     224.357 219.704 137.730  1.00 26.55           C  
ATOM  21299  C   ILE C1115     223.594 219.377 136.474  1.00 27.85           C  
ATOM  21300  O   ILE C1115     223.930 219.859 135.390  1.00 29.39           O  
ATOM  21301  CB  ILE C1115     224.223 221.189 138.051  1.00 26.34           C  
ATOM  21302  CG1 ILE C1115     224.937 221.474 139.360  1.00 25.85           C  
ATOM  21303  CG2 ILE C1115     222.768 221.542 138.141  1.00 26.67           C  
ATOM  21304  CD1 ILE C1115     225.163 222.928 139.657  1.00 25.82           C  
ATOM  21305  N   THR C1116     222.583 218.542 136.625  1.00 27.64           N  
ATOM  21306  CA  THR C1116     221.794 218.079 135.504  1.00 28.01           C  
ATOM  21307  C   THR C1116     220.325 218.156 135.849  1.00 29.76           C  
ATOM  21308  O   THR C1116     219.954 218.362 137.010  1.00 27.13           O  
ATOM  21309  CB  THR C1116     222.111 216.620 135.134  1.00 28.96           C  
ATOM  21310  OG1 THR C1116     221.509 215.744 136.086  1.00 28.80           O  
ATOM  21311  CG2 THR C1116     223.590 216.363 135.140  1.00 29.06           C  
ATOM  21312  N   THR C1117     219.488 217.902 134.863  1.00 28.24           N  
ATOM  21313  CA  THR C1117     218.049 217.891 135.071  1.00 27.80           C  
ATOM  21314  C   THR C1117     217.611 216.714 135.939  1.00 26.91           C  
ATOM  21315  O   THR C1117     216.472 216.669 136.401  1.00 27.05           O  
ATOM  21316  CB  THR C1117     217.304 217.841 133.733  1.00 29.99           C  
ATOM  21317  OG1 THR C1117     217.682 216.655 133.023  1.00 31.18           O  
ATOM  21318  CG2 THR C1117     217.659 219.059 132.902  1.00 31.02           C  
ATOM  21319  N   ASP C1118     218.510 215.757 136.163  1.00 27.40           N  
ATOM  21320  CA  ASP C1118     218.199 214.607 136.999  1.00 27.19           C  
ATOM  21321  C   ASP C1118     218.592 214.849 138.451  1.00 27.00           C  
ATOM  21322  O   ASP C1118     218.320 214.020 139.319  1.00 26.34           O  
ATOM  21323  CB  ASP C1118     218.906 213.360 136.483  1.00 28.01           C  
ATOM  21324  CG  ASP C1118     218.391 212.889 135.137  1.00 29.12           C  
ATOM  21325  OD1 ASP C1118     217.225 213.057 134.857  1.00 28.60           O  
ATOM  21326  OD2 ASP C1118     219.179 212.373 134.389  1.00 29.85           O  
ATOM  21327  N   ASN C1119     219.246 215.981 138.714  1.00 26.42           N  
ATOM  21328  CA  ASN C1119     219.672 216.328 140.063  1.00 25.60           C  
ATOM  21329  C   ASN C1119     218.823 217.445 140.636  1.00 25.44           C  
ATOM  21330  O   ASN C1119     218.712 217.581 141.856  1.00 24.96           O  
ATOM  21331  CB  ASN C1119     221.139 216.719 140.093  1.00 26.06           C  
ATOM  21332  CG  ASN C1119     222.047 215.564 139.819  1.00 27.03           C  
ATOM  21333  OD1 ASN C1119     221.733 214.440 140.215  1.00 27.47           O  
ATOM  21334  ND2 ASN C1119     223.170 215.790 139.172  1.00 27.18           N  
ATOM  21335  N   THR C1120     218.236 218.244 139.750  1.00 24.84           N  
ATOM  21336  CA  THR C1120     217.470 219.411 140.146  1.00 23.90           C  
ATOM  21337  C   THR C1120     216.039 219.372 139.639  1.00 24.43           C  
ATOM  21338  O   THR C1120     215.693 218.574 138.771  1.00 25.75           O  
ATOM  21339  CB  THR C1120     218.134 220.679 139.604  1.00 24.13           C  
ATOM  21340  OG1 THR C1120     218.040 220.699 138.187  1.00 25.25           O  
ATOM  21341  CG2 THR C1120     219.576 220.723 139.983  1.00 24.28           C  
ATOM  21342  N   PHE C1121     215.209 220.258 140.160  1.00 23.33           N  
ATOM  21343  CA  PHE C1121     213.836 220.378 139.701  1.00 23.27           C  
ATOM  21344  C   PHE C1121     213.511 221.840 139.496  1.00 24.39           C  
ATOM  21345  O   PHE C1121     214.166 222.714 140.060  1.00 22.52           O  
ATOM  21346  CB  PHE C1121     212.866 219.755 140.695  1.00 23.30           C  
ATOM  21347  CG  PHE C1121     212.785 220.474 141.989  1.00 22.81           C  
ATOM  21348  CD1 PHE C1121     211.838 221.462 142.196  1.00 22.87           C  
ATOM  21349  CD2 PHE C1121     213.655 220.176 143.002  1.00 23.27           C  
ATOM  21350  CE1 PHE C1121     211.778 222.125 143.394  1.00 22.30           C  
ATOM  21351  CE2 PHE C1121     213.592 220.835 144.194  1.00 22.76           C  
ATOM  21352  CZ  PHE C1121     212.658 221.810 144.390  1.00 21.95           C  
ATOM  21353  N   VAL C1122     212.511 222.121 138.678  1.00 22.97           N  
ATOM  21354  CA  VAL C1122     212.181 223.504 138.384  1.00 23.01           C  
ATOM  21355  C   VAL C1122     210.932 224.005 139.053  1.00 22.86           C  
ATOM  21356  O   VAL C1122     209.885 223.359 139.005  1.00 23.08           O  
ATOM  21357  CB  VAL C1122     212.030 223.703 136.878  1.00 23.60           C  
ATOM  21358  CG1 VAL C1122     211.588 225.123 136.580  1.00 23.74           C  
ATOM  21359  CG2 VAL C1122     213.343 223.433 136.231  1.00 24.38           C  
ATOM  21360  N   SER C1123     211.042 225.179 139.654  1.00 22.66           N  
ATOM  21361  CA  SER C1123     209.883 225.835 140.225  1.00 22.34           C  
ATOM  21362  C   SER C1123     210.061 227.340 140.253  1.00 22.50           C  
ATOM  21363  O   SER C1123     210.991 227.856 140.866  1.00 22.74           O  
ATOM  21364  CB  SER C1123     209.604 225.330 141.617  1.00 21.92           C  
ATOM  21365  OG  SER C1123     208.469 225.961 142.140  1.00 21.63           O  
ATOM  21366  N   GLY C1124     209.164 228.059 139.604  1.00 22.66           N  
ATOM  21367  CA  GLY C1124     209.270 229.508 139.589  1.00 22.96           C  
ATOM  21368  C   GLY C1124     210.411 229.950 138.687  1.00 23.56           C  
ATOM  21369  O   GLY C1124     210.832 229.209 137.793  1.00 23.54           O  
ATOM  21370  N   ASN C1125     210.903 231.166 138.916  1.00 23.89           N  
ATOM  21371  CA  ASN C1125     211.913 231.733 138.039  1.00 24.34           C  
ATOM  21372  C   ASN C1125     212.885 232.667 138.781  1.00 24.27           C  
ATOM  21373  O   ASN C1125     212.756 232.900 139.994  1.00 24.60           O  
ATOM  21374  CB  ASN C1125     211.219 232.437 136.881  1.00 24.07           C  
ATOM  21375  CG  ASN C1125     210.395 233.587 137.322  1.00 24.07           C  
ATOM  21376  OD1 ASN C1125     210.911 234.550 137.904  1.00 24.24           O  
ATOM  21377  ND2 ASN C1125     209.115 233.521 137.061  1.00 24.45           N  
ATOM  21378  N   CYS C1126     213.856 233.185 138.023  1.00 24.06           N  
ATOM  21379  CA  CYS C1126     214.968 234.010 138.495  1.00 24.59           C  
ATOM  21380  C   CYS C1126     214.596 235.371 139.107  1.00 24.52           C  
ATOM  21381  O   CYS C1126     215.430 235.982 139.780  1.00 24.23           O  
ATOM  21382  CB  CYS C1126     215.944 234.244 137.326  1.00 25.89           C  
ATOM  21383  SG  CYS C1126     216.686 232.728 136.682  1.00 26.54           S  
ATOM  21384  N   ASP C1127     213.362 235.851 138.887  1.00 24.52           N  
ATOM  21385  CA  ASP C1127     212.914 237.147 139.406  1.00 24.35           C  
ATOM  21386  C   ASP C1127     212.333 237.003 140.802  1.00 24.20           C  
ATOM  21387  O   ASP C1127     211.956 237.991 141.433  1.00 24.07           O  
ATOM  21388  CB  ASP C1127     211.869 237.764 138.481  1.00 24.08           C  
ATOM  21389  CG  ASP C1127     212.432 238.159 137.123  1.00 24.52           C  
ATOM  21390  OD1 ASP C1127     213.596 238.483 137.039  1.00 24.24           O  
ATOM  21391  OD2 ASP C1127     211.688 238.126 136.174  1.00 24.15           O  
ATOM  21392  N   VAL C1128     212.244 235.768 141.276  1.00 24.27           N  
ATOM  21393  CA  VAL C1128     211.660 235.507 142.576  1.00 23.80           C  
ATOM  21394  C   VAL C1128     212.693 235.075 143.608  1.00 23.64           C  
ATOM  21395  O   VAL C1128     212.660 235.534 144.748  1.00 23.56           O  
ATOM  21396  CB  VAL C1128     210.568 234.438 142.449  1.00 24.09           C  
ATOM  21397  CG1 VAL C1128     210.007 234.109 143.808  1.00 23.63           C  
ATOM  21398  CG2 VAL C1128     209.477 234.947 141.524  1.00 24.63           C  
ATOM  21399  N   VAL C1129     213.583 234.163 143.234  1.00 23.88           N  
ATOM  21400  CA  VAL C1129     214.521 233.629 144.218  1.00 23.27           C  
ATOM  21401  C   VAL C1129     215.655 234.597 144.531  1.00 23.29           C  
ATOM  21402  O   VAL C1129     216.389 235.038 143.644  1.00 23.85           O  
ATOM  21403  CB  VAL C1129     215.113 232.303 143.725  1.00 23.51           C  
ATOM  21404  CG1 VAL C1129     216.164 231.785 144.718  1.00 23.07           C  
ATOM  21405  CG2 VAL C1129     214.005 231.295 143.547  1.00 23.81           C  
ATOM  21406  N   ILE C1130     215.820 234.888 145.813  1.00 23.25           N  
ATOM  21407  CA  ILE C1130     216.843 235.812 146.263  1.00 23.17           C  
ATOM  21408  C   ILE C1130     218.190 235.126 146.320  1.00 23.28           C  
ATOM  21409  O   ILE C1130     218.352 234.121 147.003  1.00 23.22           O  
ATOM  21410  CB  ILE C1130     216.496 236.356 147.662  1.00 22.84           C  
ATOM  21411  CG1 ILE C1130     215.170 237.133 147.605  1.00 23.45           C  
ATOM  21412  CG2 ILE C1130     217.629 237.237 148.177  1.00 23.38           C  
ATOM  21413  CD1 ILE C1130     214.579 237.464 148.971  1.00 22.72           C  
ATOM  21414  N   GLY C1131     219.170 235.681 145.624  1.00 23.41           N  
ATOM  21415  CA  GLY C1131     220.503 235.099 145.626  1.00 23.39           C  
ATOM  21416  C   GLY C1131     220.713 234.059 144.538  1.00 23.62           C  
ATOM  21417  O   GLY C1131     221.736 233.376 144.530  1.00 23.39           O  
ATOM  21418  N   ILE C1132     219.765 233.941 143.618  1.00 23.66           N  
ATOM  21419  CA  ILE C1132     219.893 232.982 142.530  1.00 23.28           C  
ATOM  21420  C   ILE C1132     221.034 233.391 141.611  1.00 24.21           C  
ATOM  21421  O   ILE C1132     221.228 234.579 141.353  1.00 24.81           O  
ATOM  21422  CB  ILE C1132     218.576 232.869 141.750  1.00 23.72           C  
ATOM  21423  CG1 ILE C1132     218.612 231.629 140.888  1.00 24.56           C  
ATOM  21424  CG2 ILE C1132     218.343 234.112 140.912  1.00 24.40           C  
ATOM  21425  CD1 ILE C1132     217.272 231.176 140.356  1.00 24.97           C  
ATOM  21426  N   VAL C1133     221.802 232.417 141.130  1.00 24.16           N  
ATOM  21427  CA  VAL C1133     222.943 232.723 140.267  1.00 24.70           C  
ATOM  21428  C   VAL C1133     222.794 232.061 138.904  1.00 26.07           C  
ATOM  21429  O   VAL C1133     222.036 231.106 138.779  1.00 26.15           O  
ATOM  21430  CB  VAL C1133     224.244 232.225 140.921  1.00 24.10           C  
ATOM  21431  CG1 VAL C1133     224.431 232.888 142.262  1.00 24.84           C  
ATOM  21432  CG2 VAL C1133     224.192 230.717 141.063  1.00 23.92           C  
ATOM  21433  N   ASN C1134     223.529 232.557 137.894  1.00 26.72           N  
ATOM  21434  CA  ASN C1134     223.525 232.004 136.541  1.00 26.64           C  
ATOM  21435  C   ASN C1134     224.406 230.760 136.441  1.00 26.52           C  
ATOM  21436  O   ASN C1134     225.524 230.742 136.964  1.00 26.15           O  
ATOM  21437  CB  ASN C1134     223.967 233.054 135.523  1.00 28.84           C  
ATOM  21438  CG  ASN C1134     222.817 233.909 135.005  1.00 30.14           C  
ATOM  21439  OD1 ASN C1134     221.870 233.378 134.400  1.00 29.94           O  
ATOM  21440  ND2 ASN C1134     222.895 235.206 135.228  1.00 32.15           N  
ATOM  21441  N   ASN C1135     223.901 229.730 135.744  1.00 26.65           N  
ATOM  21442  CA  ASN C1135     224.603 228.470 135.514  1.00 26.51           C  
ATOM  21443  C   ASN C1135     224.091 227.786 134.261  1.00 26.85           C  
ATOM  21444  O   ASN C1135     223.170 228.269 133.609  1.00 27.00           O  
ATOM  21445  CB  ASN C1135     224.414 227.550 136.696  1.00 26.38           C  
ATOM  21446  CG  ASN C1135     225.472 226.548 136.841  1.00 26.80           C  
ATOM  21447  OD1 ASN C1135     226.438 226.510 136.072  1.00 26.81           O  
ATOM  21448  ND2 ASN C1135     225.310 225.701 137.804  1.00 26.47           N  
ATOM  21449  N   THR C1136     224.668 226.640 133.944  1.00 27.11           N  
ATOM  21450  CA  THR C1136     224.161 225.822 132.859  1.00 27.55           C  
ATOM  21451  C   THR C1136     223.782 224.458 133.395  1.00 27.60           C  
ATOM  21452  O   THR C1136     224.600 223.783 134.016  1.00 27.75           O  
ATOM  21453  CB  THR C1136     225.199 225.666 131.736  1.00 27.47           C  
ATOM  21454  OG1 THR C1136     225.525 226.953 131.206  1.00 27.89           O  
ATOM  21455  CG2 THR C1136     224.644 224.797 130.624  1.00 28.92           C  
ATOM  21456  N   VAL C1137     222.551 224.043 133.136  1.00 28.23           N  
ATOM  21457  CA  VAL C1137     222.091 222.741 133.581  1.00 28.46           C  
ATOM  21458  C   VAL C1137     222.151 221.757 132.432  1.00 29.49           C  
ATOM  21459  O   VAL C1137     221.575 221.988 131.371  1.00 30.02           O  
ATOM  21460  CB  VAL C1137     220.660 222.827 134.119  1.00 27.78           C  
ATOM  21461  CG1 VAL C1137     220.184 221.457 134.560  1.00 28.65           C  
ATOM  21462  CG2 VAL C1137     220.633 223.786 135.259  1.00 27.30           C  
ATOM  21463  N   TYR C1138     222.865 220.670 132.637  1.00 30.14           N  
ATOM  21464  CA  TYR C1138     223.036 219.676 131.600  1.00 31.67           C  
ATOM  21465  C   TYR C1138     221.817 218.779 131.454  1.00 34.29           C  
ATOM  21466  O   TYR C1138     221.266 218.289 132.441  1.00 30.37           O  
ATOM  21467  CB  TYR C1138     224.286 218.860 131.893  1.00 32.34           C  
ATOM  21468  CG  TYR C1138     224.514 217.700 130.977  1.00 34.20           C  
ATOM  21469  CD1 TYR C1138     224.996 217.893 129.701  1.00 35.56           C  
ATOM  21470  CD2 TYR C1138     224.252 216.428 131.426  1.00 35.12           C  
ATOM  21471  CE1 TYR C1138     225.212 216.807 128.884  1.00 36.59           C  
ATOM  21472  CE2 TYR C1138     224.471 215.355 130.622  1.00 35.93           C  
ATOM  21473  CZ  TYR C1138     224.947 215.533 129.358  1.00 36.85           C  
ATOM  21474  OH  TYR C1138     225.165 214.442 128.557  1.00 38.24           O  
ATOM  21475  N   ASP C1139     221.409 218.560 130.211  1.00 35.11           N  
ATOM  21476  CA  ASP C1139     220.310 217.660 129.892  1.00 34.91           C  
ATOM  21477  C   ASP C1139     220.848 216.419 129.178  1.00 37.09           C  
ATOM  21478  O   ASP C1139     221.200 216.505 128.002  1.00 36.17           O  
ATOM  21479  CB  ASP C1139     219.279 218.339 128.999  1.00 36.69           C  
ATOM  21480  CG  ASP C1139     218.105 217.411 128.681  1.00 37.89           C  
ATOM  21481  OD1 ASP C1139     218.134 216.285 129.153  1.00 37.43           O  
ATOM  21482  OD2 ASP C1139     217.204 217.819 127.968  1.00 39.67           O  
ATOM  21483  N   PRO C1140     220.930 215.262 129.851  1.00 37.10           N  
ATOM  21484  CA  PRO C1140     221.452 214.000 129.353  1.00 37.48           C  
ATOM  21485  C   PRO C1140     220.745 213.512 128.097  1.00 39.08           C  
ATOM  21486  O   PRO C1140     221.284 212.688 127.359  1.00 40.61           O  
ATOM  21487  CB  PRO C1140     221.182 213.047 130.520  1.00 36.90           C  
ATOM  21488  CG  PRO C1140     221.129 213.927 131.731  1.00 34.96           C  
ATOM  21489  CD  PRO C1140     220.515 215.213 131.253  1.00 35.21           C  
ATOM  21490  N   LEU C1141     219.538 214.004 127.853  1.00 39.35           N  
ATOM  21491  CA  LEU C1141     218.786 213.578 126.692  1.00 38.32           C  
ATOM  21492  C   LEU C1141     219.226 214.239 125.401  1.00 47.95           C  
ATOM  21493  O   LEU C1141     219.090 213.647 124.330  1.00 40.19           O  
ATOM  21494  CB  LEU C1141     217.295 213.848 126.901  1.00 40.66           C  
ATOM  21495  CG  LEU C1141     216.363 213.486 125.724  1.00 41.77           C  
ATOM  21496  CD1 LEU C1141     216.482 212.011 125.367  1.00 42.41           C  
ATOM  21497  CD2 LEU C1141     214.937 213.822 126.107  1.00 42.53           C  
ATOM  21498  N   GLN C1142     219.705 215.475 125.457  1.00 40.04           N  
ATOM  21499  CA  GLN C1142     219.930 216.145 124.190  1.00 41.91           C  
ATOM  21500  C   GLN C1142     221.044 215.487 123.372  1.00 41.50           C  
ATOM  21501  O   GLN C1142     220.843 215.244 122.185  1.00 42.91           O  
ATOM  21502  CB  GLN C1142     220.162 217.651 124.374  1.00 41.44           C  
ATOM  21503  CG  GLN C1142     218.964 218.369 124.947  1.00 41.28           C  
ATOM  21504  CD  GLN C1142     217.710 218.165 124.143  1.00 42.46           C  
ATOM  21505  OE1 GLN C1142     217.718 218.273 122.914  1.00 42.83           O  
ATOM  21506  NE2 GLN C1142     216.616 217.867 124.837  1.00 41.69           N  
ATOM  21507  N   PRO C1143     222.213 215.145 123.945  1.00 42.14           N  
ATOM  21508  CA  PRO C1143     223.294 214.482 123.247  1.00 42.71           C  
ATOM  21509  C   PRO C1143     222.830 213.191 122.583  1.00 43.18           C  
ATOM  21510  O   PRO C1143     223.317 212.832 121.510  1.00 44.87           O  
ATOM  21511  CB  PRO C1143     224.289 214.204 124.375  1.00 41.42           C  
ATOM  21512  CG  PRO C1143     224.000 215.271 125.389  1.00 40.43           C  
ATOM  21513  CD  PRO C1143     222.510 215.425 125.357  1.00 40.17           C  
ATOM  21514  N   GLU C1144     221.871 212.511 123.207  1.00 42.28           N  
ATOM  21515  CA  GLU C1144     221.373 211.257 122.672  1.00 41.55           C  
ATOM  21516  C   GLU C1144     220.495 211.489 121.458  1.00 43.54           C  
ATOM  21517  O   GLU C1144     220.520 210.709 120.505  1.00 45.11           O  
ATOM  21518  CB  GLU C1144     220.584 210.510 123.737  1.00 43.44           C  
ATOM  21519  CG  GLU C1144     221.399 210.052 124.931  1.00 43.15           C  
ATOM  21520  CD  GLU C1144     222.474 209.078 124.572  1.00 44.44           C  
ATOM  21521  OE1 GLU C1144     222.213 208.189 123.802  1.00 44.55           O  
ATOM  21522  OE2 GLU C1144     223.562 209.220 125.073  1.00 43.77           O  
ATOM  21523  N   LEU C1145     219.730 212.577 121.485  1.00 43.28           N  
ATOM  21524  CA  LEU C1145     218.864 212.919 120.367  1.00 45.26           C  
ATOM  21525  C   LEU C1145     219.703 213.371 119.182  1.00 45.11           C  
ATOM  21526  O   LEU C1145     219.390 213.058 118.032  1.00 44.66           O  
ATOM  21527  CB  LEU C1145     217.897 214.038 120.768  1.00 44.15           C  
ATOM  21528  CG  LEU C1145     216.826 213.683 121.822  1.00 42.53           C  
ATOM  21529  CD1 LEU C1145     216.182 214.959 122.297  1.00 42.19           C  
ATOM  21530  CD2 LEU C1145     215.759 212.760 121.232  1.00 43.61           C  
ATOM  21531  N   ASP C1146     220.788 214.089 119.472  1.00 43.81           N  
ATOM  21532  CA  ASP C1146     221.684 214.588 118.430  1.00 45.12           C  
ATOM  21533  C   ASP C1146     222.555 213.489 117.799  1.00 45.18           C  
ATOM  21534  O   ASP C1146     222.800 213.519 116.590  1.00 45.39           O  
ATOM  21535  CB  ASP C1146     222.595 215.683 118.991  1.00 44.53           C  
ATOM  21536  N   SER C1147     223.014 212.518 118.613  1.00 45.28           N  
ATOM  21537  CA  SER C1147     223.849 211.401 118.173  1.00 45.30           C  
ATOM  21538  C   SER C1147     222.980 210.326 117.514  1.00 46.01           C  
ATOM  21539  O   SER C1147     223.349 209.745 116.489  1.00 45.86           O  
ATOM  21540  CB  SER C1147     224.627 210.826 119.360  1.00 45.57           C  
ATOM  21541  OG  SER C1147     225.386 209.709 118.987  1.00 45.95           O  
TER   21542      SER C1147                                                      
HETATM21543  C1  NAG D   1     180.518 234.754 240.820  1.00 68.53           C  
HETATM21544  C2  NAG D   1     180.844 233.215 241.025  1.00 68.82           C  
HETATM21545  C3  NAG D   1     179.779 232.390 240.254  1.00 68.89           C  
HETATM21546  C4  NAG D   1     178.362 232.744 240.782  1.00 68.80           C  
HETATM21547  C5  NAG D   1     178.121 234.272 240.601  1.00 68.10           C  
HETATM21548  C6  NAG D   1     176.775 234.712 241.182  1.00 69.18           C  
HETATM21549  C7  NAG D   1     183.295 232.932 241.259  1.00 71.50           C  
HETATM21550  C8  NAG D   1     184.591 232.587 240.589  1.00 74.71           C  
HETATM21551  N2  NAG D   1     182.191 232.901 240.517  1.00 69.75           N  
HETATM21552  O3  NAG D   1     180.024 230.987 240.457  1.00 68.79           O  
HETATM21553  O4  NAG D   1     177.386 232.054 239.978  1.00 69.07           O  
HETATM21554  O5  NAG D   1     179.170 235.030 241.309  1.00 67.60           O  
HETATM21555  O6  NAG D   1     176.474 236.068 240.870  1.00 67.96           O  
HETATM21556  O7  NAG D   1     183.262 233.252 242.453  1.00 72.00           O  
HETATM21557  C1  NAG D   2     176.571 231.054 240.747  1.00 69.78           C  
HETATM21558  C2  NAG D   2     175.290 230.660 239.943  1.00 69.93           C  
HETATM21559  C3  NAG D   2     174.427 229.716 240.829  1.00 70.21           C  
HETATM21560  C4  NAG D   2     175.268 228.470 241.213  1.00 70.21           C  
HETATM21561  C5  NAG D   2     176.540 228.940 241.982  1.00 69.30           C  
HETATM21562  C6  NAG D   2     177.469 227.785 242.323  1.00 70.36           C  
HETATM21563  C7  NAG D   2     174.274 232.301 238.377  1.00 70.18           C  
HETATM21564  C8  NAG D   2     173.457 233.555 238.243  1.00 69.42           C  
HETATM21565  N2  NAG D   2     174.513 231.867 239.609  1.00 70.00           N  
HETATM21566  O3  NAG D   2     173.262 229.313 240.099  1.00 68.80           O  
HETATM21567  O4  NAG D   2     174.480 227.611 242.032  1.00 69.76           O  
HETATM21568  O5  NAG D   2     177.317 229.872 241.141  1.00 69.84           O  
HETATM21569  O6  NAG D   2     176.968 226.993 243.395  1.00 69.09           O  
HETATM21570  O7  NAG D   2     174.696 231.697 237.380  1.00 68.80           O  
HETATM21571  C1  NAG E   1     199.173 234.110 153.139  1.00 21.08           C  
HETATM21572  C2  NAG E   1     198.977 234.994 151.851  1.00 21.38           C  
HETATM21573  C3  NAG E   1     199.787 236.299 152.042  1.00 21.62           C  
HETATM21574  C4  NAG E   1     199.305 237.041 153.317  1.00 21.70           C  
HETATM21575  C5  NAG E   1     199.478 236.085 154.538  1.00 21.59           C  
HETATM21576  C6  NAG E   1     198.982 236.702 155.841  1.00 21.94           C  
HETATM21577  C7  NAG E   1     198.700 233.614 149.811  1.00 21.89           C  
HETATM21578  C8  NAG E   1     199.381 232.890 148.688  1.00 22.06           C  
HETATM21579  N2  NAG E   1     199.476 234.242 150.686  1.00 21.32           N  
HETATM21580  O3  NAG E   1     199.601 237.143 150.896  1.00 21.68           O  
HETATM21581  O4  NAG E   1     200.162 238.184 153.510  1.00 22.23           O  
HETATM21582  O5  NAG E   1     198.721 234.841 154.314  1.00 21.12           O  
HETATM21583  O6  NAG E   1     199.217 235.842 156.949  1.00 21.88           O  
HETATM21584  O7  NAG E   1     197.469 233.617 149.918  1.00 21.66           O  
HETATM21585  C1  NAG E   2     199.417 239.484 153.631  1.00 22.44           C  
HETATM21586  C2  NAG E   2     200.376 240.622 154.128  1.00 22.50           C  
HETATM21587  C3  NAG E   2     199.526 241.901 154.364  1.00 22.78           C  
HETATM21588  C4  NAG E   2     198.817 242.287 153.035  1.00 23.08           C  
HETATM21589  C5  NAG E   2     197.911 241.103 152.580  1.00 22.86           C  
HETATM21590  C6  NAG E   2     197.235 241.375 151.243  1.00 22.99           C  
HETATM21591  C7  NAG E   2     202.327 239.849 155.460  1.00 22.67           C  
HETATM21592  C8  NAG E   2     202.854 239.433 156.804  1.00 22.74           C  
HETATM21593  N2  NAG E   2     201.042 240.194 155.377  1.00 22.74           N  
HETATM21594  O3  NAG E   2     200.385 242.975 154.777  1.00 22.86           O  
HETATM21595  O4  NAG E   2     198.035 243.462 153.244  1.00 23.12           O  
HETATM21596  O5  NAG E   2     198.736 239.889 152.411  1.00 22.46           O  
HETATM21597  O6  NAG E   2     196.128 240.504 151.034  1.00 22.95           O  
HETATM21598  O7  NAG E   2     203.062 239.852 154.462  1.00 22.39           O  
HETATM21599  C1  NAG F   1     214.819 244.295 164.568  1.00 30.16           C  
HETATM21600  C2  NAG F   1     215.484 245.402 163.662  1.00 30.61           C  
HETATM21601  C3  NAG F   1     215.878 246.592 164.574  1.00 31.11           C  
HETATM21602  C4  NAG F   1     214.615 247.136 165.297  1.00 31.91           C  
HETATM21603  C5  NAG F   1     213.978 245.982 166.128  1.00 31.30           C  
HETATM21604  C6  NAG F   1     212.684 246.407 166.818  1.00 31.62           C  
HETATM21605  C7  NAG F   1     216.691 244.318 161.789  1.00 30.39           C  
HETATM21606  C8  NAG F   1     217.999 243.785 161.285  1.00 30.28           C  
HETATM21607  N2  NAG F   1     216.677 244.841 163.008  1.00 30.43           N  
HETATM21608  O3  NAG F   1     216.467 247.623 163.767  1.00 31.99           O  
HETATM21609  O4  NAG F   1     215.015 248.172 166.221  1.00 32.48           O  
HETATM21610  O5  NAG F   1     213.650 244.850 165.240  1.00 30.34           O  
HETATM21611  O6  NAG F   1     212.350 245.520 167.873  1.00 30.90           O  
HETATM21612  O7  NAG F   1     215.668 244.262 161.097  1.00 30.15           O  
HETATM21613  C1  NAG F   2     214.468 249.527 165.872  1.00 33.27           C  
HETATM21614  C2  NAG F   2     214.534 250.497 167.103  1.00 33.86           C  
HETATM21615  C3  NAG F   2     213.848 251.832 166.703  1.00 34.24           C  
HETATM21616  C4  NAG F   2     214.567 252.423 165.460  1.00 34.69           C  
HETATM21617  C5  NAG F   2     214.490 251.397 164.290  1.00 34.29           C  
HETATM21618  C6  NAG F   2     215.243 251.877 163.058  1.00 34.68           C  
HETATM21619  C7  NAG F   2     214.439 249.354 169.302  1.00 33.63           C  
HETATM21620  C8  NAG F   2     213.567 248.773 170.376  1.00 34.07           C  
HETATM21621  N2  NAG F   2     213.833 249.888 168.246  1.00 33.63           N  
HETATM21622  O3  NAG F   2     213.936 252.759 167.795  1.00 34.42           O  
HETATM21623  O4  NAG F   2     213.933 253.645 165.087  1.00 34.96           O  
HETATM21624  O5  NAG F   2     215.106 250.124 164.712  1.00 33.59           O  
HETATM21625  O6  NAG F   2     214.933 251.087 161.916  1.00 34.69           O  
HETATM21626  O7  NAG F   2     215.674 249.322 169.395  1.00 34.03           O  
HETATM21627  C1  NAG G   1     191.810 223.793 136.691  1.00 25.99           C  
HETATM21628  C2  NAG G   1     190.691 224.813 136.258  1.00 26.30           C  
HETATM21629  C3  NAG G   1     190.819 225.048 134.731  1.00 26.34           C  
HETATM21630  C4  NAG G   1     192.226 225.609 134.397  1.00 26.72           C  
HETATM21631  C5  NAG G   1     193.297 224.592 134.910  1.00 26.09           C  
HETATM21632  C6  NAG G   1     194.715 225.127 134.703  1.00 26.59           C  
HETATM21633  C7  NAG G   1     188.548 224.726 137.493  1.00 26.39           C  
HETATM21634  C8  NAG G   1     187.240 224.020 137.674  1.00 26.44           C  
HETATM21635  N2  NAG G   1     189.372 224.253 136.570  1.00 26.13           N  
HETATM21636  O3  NAG G   1     189.798 225.966 134.308  1.00 26.35           O  
HETATM21637  O4  NAG G   1     192.314 225.691 132.957  1.00 26.92           O  
HETATM21638  O5  NAG G   1     193.119 224.351 136.361  1.00 26.03           O  
HETATM21639  O6  NAG G   1     195.709 224.279 135.255  1.00 26.78           O  
HETATM21640  O7  NAG G   1     188.843 225.717 138.175  1.00 26.37           O  
HETATM21641  C1  NAG G   2     192.909 226.972 132.442  1.00 27.01           C  
HETATM21642  C2  NAG G   2     193.410 226.783 130.967  1.00 26.96           C  
HETATM21643  C3  NAG G   2     194.146 228.081 130.532  1.00 27.15           C  
HETATM21644  C4  NAG G   2     193.166 229.280 130.654  1.00 27.55           C  
HETATM21645  C5  NAG G   2     192.681 229.385 132.129  1.00 27.34           C  
HETATM21646  C6  NAG G   2     191.675 230.511 132.328  1.00 28.19           C  
HETATM21647  C7  NAG G   2     193.974 224.438 130.382  1.00 26.71           C  
HETATM21648  C8  NAG G   2     195.008 223.350 130.400  1.00 26.82           C  
HETATM21649  N2  NAG G   2     194.311 225.617 130.900  1.00 26.90           N  
HETATM21650  O3  NAG G   2     194.584 227.949 129.169  1.00 27.42           O  
HETATM21651  O4  NAG G   2     193.840 230.475 130.268  1.00 27.96           O  
HETATM21652  O5  NAG G   2     192.025 228.122 132.537  1.00 27.11           O  
HETATM21653  O6  NAG G   2     190.576 230.419 131.427  1.00 27.79           O  
HETATM21654  O7  NAG G   2     192.847 224.235 129.905  1.00 26.61           O  
HETATM21655  C1  NAG H   1     188.926 204.246 131.553  1.00 34.22           C  
HETATM21656  C2  NAG H   1     187.579 203.800 132.248  1.00 34.51           C  
HETATM21657  C3  NAG H   1     187.297 202.327 131.854  1.00 36.12           C  
HETATM21658  C4  NAG H   1     187.201 202.201 130.306  1.00 37.14           C  
HETATM21659  C5  NAG H   1     188.548 202.690 129.695  1.00 37.21           C  
HETATM21660  C6  NAG H   1     188.541 202.656 128.172  1.00 38.18           C  
HETATM21661  C7  NAG H   1     187.162 204.830 134.473  1.00 32.87           C  
HETATM21662  C8  NAG H   1     187.475 204.793 135.942  1.00 31.21           C  
HETATM21663  N2  NAG H   1     187.746 203.914 133.707  1.00 33.68           N  
HETATM21664  O3  NAG H   1     186.062 201.925 132.456  1.00 36.52           O  
HETATM21665  O4  NAG H   1     186.997 200.817 129.919  1.00 38.53           O  
HETATM21666  O5  NAG H   1     188.806 204.084 130.109  1.00 35.22           O  
HETATM21667  O6  NAG H   1     189.784 203.077 127.624  1.00 38.33           O  
HETATM21668  O7  NAG H   1     186.394 205.682 134.000  1.00 32.92           O  
HETATM21669  C1  NAG H   2     185.551 200.418 129.714  1.00 40.10           C  
HETATM21670  C2  NAG H   2     185.356 199.659 128.352  1.00 41.03           C  
HETATM21671  C3  NAG H   2     183.837 199.384 128.160  1.00 41.69           C  
HETATM21672  C4  NAG H   2     183.308 198.557 129.362  1.00 41.98           C  
HETATM21673  C5  NAG H   2     183.565 199.353 130.671  1.00 40.93           C  
HETATM21674  C6  NAG H   2     183.112 198.602 131.913  1.00 41.97           C  
HETATM21675  C7  NAG H   2     186.619 200.026 126.242  1.00 41.49           C  
HETATM21676  C8  NAG H   2     187.027 200.998 125.169  1.00 41.50           C  
HETATM21677  N2  NAG H   2     185.847 200.481 127.227  1.00 41.60           N  
HETATM21678  O3  NAG H   2     183.626 198.650 126.943  1.00 41.63           O  
HETATM21679  O4  NAG H   2     181.913 198.319 129.189  1.00 42.69           O  
HETATM21680  O5  NAG H   2     185.009 199.635 130.812  1.00 40.64           O  
HETATM21681  O6  NAG H   2     183.662 197.290 131.987  1.00 42.85           O  
HETATM21682  O7  NAG H   2     186.990 198.842 126.202  1.00 41.84           O  
HETATM21683  C1  NAG I   1     181.901 195.911 162.312  1.00 29.99           C  
HETATM21684  C2  NAG I   1     180.687 195.819 161.310  1.00 30.22           C  
HETATM21685  C3  NAG I   1     179.400 195.579 162.145  1.00 30.76           C  
HETATM21686  C4  NAG I   1     179.545 194.274 162.981  1.00 31.66           C  
HETATM21687  C5  NAG I   1     180.796 194.424 163.905  1.00 30.91           C  
HETATM21688  C6  NAG I   1     181.081 193.177 164.733  1.00 31.52           C  
HETATM21689  C7  NAG I   1     181.102 197.286 159.361  1.00 30.21           C  
HETATM21690  C8  NAG I   1     180.900 198.636 158.741  1.00 30.54           C  
HETATM21691  N2  NAG I   1     180.574 197.081 160.562  1.00 30.12           N  
HETATM21692  O3  NAG I   1     178.278 195.470 161.257  1.00 31.34           O  
HETATM21693  O4  NAG I   1     178.364 194.125 163.807  1.00 32.17           O  
HETATM21694  O5  NAG I   1     181.994 194.685 163.090  1.00 30.32           O  
HETATM21695  O6  NAG I   1     182.119 193.396 165.681  1.00 31.30           O  
HETATM21696  O7  NAG I   1     181.724 196.397 158.767  1.00 30.08           O  
HETATM21697  C1  NAG I   2     177.638 192.817 163.622  1.00 32.87           C  
HETATM21698  C2  NAG I   2     176.797 192.460 164.899  1.00 33.50           C  
HETATM21699  C3  NAG I   2     176.175 191.052 164.697  1.00 33.86           C  
HETATM21700  C4  NAG I   2     175.301 191.059 163.415  1.00 34.56           C  
HETATM21701  C5  NAG I   2     176.189 191.445 162.196  1.00 34.13           C  
HETATM21702  C6  NAG I   2     175.385 191.534 160.905  1.00 34.35           C  
HETATM21703  C7  NAG I   2     177.725 193.417 166.993  1.00 32.95           C  
HETATM21704  C8  NAG I   2     178.667 193.231 168.148  1.00 32.56           C  
HETATM21705  N2  NAG I   2     177.661 192.442 166.092  1.00 33.17           N  
HETATM21706  O3  NAG I   2     175.360 190.720 165.831  1.00 34.07           O  
HETATM21707  O4  NAG I   2     174.729 189.764 163.229  1.00 34.96           O  
HETATM21708  O5  NAG I   2     176.802 192.771 162.433  1.00 33.35           O  
HETATM21709  O6  NAG I   2     176.225 191.450 159.758  1.00 34.34           O  
HETATM21710  O7  NAG I   2     177.035 194.441 166.890  1.00 33.26           O  
HETATM21711  C1  NAG J   1     213.846 184.710 138.142  1.00 26.25           C  
HETATM21712  C2  NAG J   1     213.487 183.228 137.749  1.00 26.54           C  
HETATM21713  C3  NAG J   1     213.429 183.148 136.201  1.00 26.96           C  
HETATM21714  C4  NAG J   1     212.367 184.136 135.656  1.00 27.09           C  
HETATM21715  C5  NAG J   1     212.741 185.573 136.142  1.00 26.42           C  
HETATM21716  C6  NAG J   1     211.702 186.613 135.733  1.00 26.86           C  
HETATM21717  C7  NAG J   1     214.394 181.488 139.260  1.00 26.56           C  
HETATM21718  C8  NAG J   1     215.592 180.670 139.628  1.00 26.36           C  
HETATM21719  N2  NAG J   1     214.535 182.337 138.256  1.00 26.48           N  
HETATM21720  O3  NAG J   1     213.116 181.803 135.810  1.00 27.02           O  
HETATM21721  O4  NAG J   1     212.477 184.109 134.219  1.00 27.66           O  
HETATM21722  O5  NAG J   1     212.831 185.613 137.617  1.00 26.45           O  
HETATM21723  O6  NAG J   1     210.386 186.265 136.157  1.00 26.91           O  
HETATM21724  O7  NAG J   1     213.321 181.372 139.863  1.00 26.71           O  
HETATM21725  C1  NAG J   2     211.163 184.002 133.500  1.00 27.62           C  
HETATM21726  C2  NAG J   2     211.341 184.389 131.991  1.00 27.60           C  
HETATM21727  C3  NAG J   2     209.942 184.405 131.322  1.00 27.55           C  
HETATM21728  C4  NAG J   2     209.291 183.003 131.484  1.00 28.00           C  
HETATM21729  C5  NAG J   2     209.177 182.667 133.002  1.00 27.88           C  
HETATM21730  C6  NAG J   2     208.615 181.275 133.243  1.00 28.53           C  
HETATM21731  C7  NAG J   2     213.232 185.924 131.511  1.00 27.33           C  
HETATM21732  C8  NAG J   2     213.725 187.341 131.496  1.00 27.25           C  
HETATM21733  N2  NAG J   2     211.978 185.716 131.907  1.00 27.61           N  
HETATM21734  O3  NAG J   2     210.089 184.712 129.926  1.00 28.27           O  
HETATM21735  O4  NAG J   2     207.996 183.020 130.882  1.00 27.96           O  
HETATM21736  O5  NAG J   2     210.520 182.705 133.619  1.00 27.89           O  
HETATM21737  O6  NAG J   2     208.168 181.122 134.586  1.00 28.08           O  
HETATM21738  O7  NAG J   2     213.972 184.987 131.176  1.00 27.26           O  
HETATM21739  C1  NAG K   1     232.627 191.539 135.058  1.00 31.35           C  
HETATM21740  C2  NAG K   1     233.766 191.007 136.005  1.00 31.96           C  
HETATM21741  C3  NAG K   1     235.119 191.579 135.503  1.00 33.10           C  
HETATM21742  C4  NAG K   1     235.354 191.140 134.030  1.00 34.16           C  
HETATM21743  C5  NAG K   1     234.170 191.674 133.165  1.00 33.49           C  
HETATM21744  C6  NAG K   1     234.262 191.249 131.703  1.00 34.36           C  
HETATM21745  C7  NAG K   1     232.788 190.778 138.272  1.00 30.04           C  
HETATM21746  C8  NAG K   1     232.582 191.419 139.610  1.00 28.85           C  
HETATM21747  N2  NAG K   1     233.480 191.470 137.371  1.00 31.30           N  
HETATM21748  O3  NAG K   1     236.177 191.083 136.338  1.00 33.64           O  
HETATM21749  O4  NAG K   1     236.580 191.729 133.541  1.00 35.30           O  
HETATM21750  O5  NAG K   1     232.898 191.140 133.685  1.00 32.13           O  
HETATM21751  O6  NAG K   1     233.432 192.058 130.880  1.00 34.38           O  
HETATM21752  O7  NAG K   1     232.340 189.653 138.021  1.00 29.80           O  
HETATM21753  C1  NAG K   2     237.671 190.726 133.285  1.00 36.17           C  
HETATM21754  C2  NAG K   2     238.717 191.275 132.253  1.00 36.86           C  
HETATM21755  C3  NAG K   2     239.740 190.146 131.955  1.00 37.49           C  
HETATM21756  C4  NAG K   2     240.413 189.698 133.283  1.00 38.08           C  
HETATM21757  C5  NAG K   2     239.315 189.196 134.266  1.00 36.96           C  
HETATM21758  C6  NAG K   2     239.895 188.824 135.624  1.00 37.09           C  
HETATM21759  C7  NAG K   2     237.787 192.927 130.649  1.00 37.09           C  
HETATM21760  C8  NAG K   2     237.090 193.156 129.338  1.00 37.64           C  
HETATM21761  N2  NAG K   2     238.042 191.671 131.001  1.00 37.05           N  
HETATM21762  O3  NAG K   2     240.745 190.638 131.054  1.00 37.81           O  
HETATM21763  O4  NAG K   2     241.351 188.660 133.012  1.00 38.21           O  
HETATM21764  O5  NAG K   2     238.329 190.272 134.496  1.00 36.21           O  
HETATM21765  O6  NAG K   2     238.951 188.112 136.418  1.00 38.19           O  
HETATM21766  O7  NAG K   2     238.107 193.881 131.376  1.00 36.89           O  
HETATM21767  C1  NAG L   1     240.202 210.772 156.100  1.00 21.68           C  
HETATM21768  C2  NAG L   1     240.959 210.434 154.760  1.00 21.93           C  
HETATM21769  C3  NAG L   1     241.753 209.124 154.971  1.00 22.40           C  
HETATM21770  C4  NAG L   1     242.735 209.280 156.160  1.00 22.80           C  
HETATM21771  C5  NAG L   1     241.906 209.643 157.431  1.00 22.53           C  
HETATM21772  C6  NAG L   1     242.763 209.863 158.671  1.00 23.18           C  
HETATM21773  C7  NAG L   1     239.743 211.062 152.692  1.00 22.32           C  
HETATM21774  C8  NAG L   1     238.653 210.687 151.732  1.00 22.07           C  
HETATM21775  N2  NAG L   1     239.951 210.240 153.708  1.00 21.75           N  
HETATM21776  O3  NAG L   1     242.489 208.827 153.774  1.00 22.36           O  
HETATM21777  O4  NAG L   1     243.372 208.005 156.365  1.00 23.51           O  
HETATM21778  O5  NAG L   1     241.153 210.888 157.194  1.00 21.81           O  
HETATM21779  O6  NAG L   1     241.958 210.060 159.828  1.00 23.41           O  
HETATM21780  O7  NAG L   1     240.408 212.094 152.538  1.00 22.11           O  
HETATM21781  C1  NAG L   2     244.861 208.093 156.542  1.00 23.71           C  
HETATM21782  C2  NAG L   2     245.417 206.749 157.128  1.00 23.97           C  
HETATM21783  C3  NAG L   2     246.924 206.944 157.439  1.00 24.26           C  
HETATM21784  C4  NAG L   2     247.657 207.341 156.126  1.00 24.42           C  
HETATM21785  C5  NAG L   2     247.034 208.657 155.571  1.00 24.13           C  
HETATM21786  C6  NAG L   2     247.647 209.066 154.239  1.00 24.51           C  
HETATM21787  C7  NAG L   2     243.720 205.439 158.384  1.00 24.19           C  
HETATM21788  C8  NAG L   2     243.024 205.199 159.692  1.00 23.77           C  
HETATM21789  N2  NAG L   2     244.652 206.393 158.341  1.00 24.13           N  
HETATM21790  O3  NAG L   2     247.470 205.717 157.945  1.00 24.45           O  
HETATM21791  O4  NAG L   2     249.045 207.523 156.400  1.00 24.49           O  
HETATM21792  O5  NAG L   2     245.586 208.459 155.336  1.00 23.87           O  
HETATM21793  O6  NAG L   2     247.324 210.413 153.909  1.00 24.03           O  
HETATM21794  O7  NAG L   2     243.419 204.783 157.376  1.00 24.24           O  
HETATM21795  C1  NAG M   1     240.050 191.561 166.264  1.00 30.62           C  
HETATM21796  C2  NAG M   1     240.419 190.265 165.437  1.00 30.77           C  
HETATM21797  C3  NAG M   1     241.168 189.299 166.386  1.00 31.51           C  
HETATM21798  C4  NAG M   1     242.434 189.987 166.962  1.00 32.41           C  
HETATM21799  C5  NAG M   1     242.001 191.290 167.701  1.00 32.20           C  
HETATM21800  C6  NAG M   1     243.182 192.107 168.214  1.00 32.38           C  
HETATM21801  C7  NAG M   1     238.691 189.797 163.722  1.00 30.52           C  
HETATM21802  C8  NAG M   1     237.418 189.077 163.386  1.00 29.87           C  
HETATM21803  N2  NAG M   1     239.186 189.628 164.944  1.00 30.56           N  
HETATM21804  O3  NAG M   1     241.554 188.133 165.640  1.00 32.01           O  
HETATM21805  O4  NAG M   1     242.991 189.083 167.942  1.00 32.97           O  
HETATM21806  O5  NAG M   1     241.261 192.173 166.782  1.00 31.02           O  
HETATM21807  O6  NAG M   1     242.763 193.106 169.134  1.00 33.10           O  
HETATM21808  O7  NAG M   1     239.253 190.524 162.894  1.00 30.63           O  
HETATM21809  C1  NAG M   2     244.456 188.816 167.771  1.00 33.82           C  
HETATM21810  C2  NAG M   2     245.102 188.367 169.131  1.00 33.95           C  
HETATM21811  C3  NAG M   2     246.635 188.227 168.913  1.00 34.83           C  
HETATM21812  C4  NAG M   2     246.900 187.199 167.781  1.00 35.39           C  
HETATM21813  C5  NAG M   2     246.203 187.698 166.480  1.00 35.03           C  
HETATM21814  C6  NAG M   2     246.362 186.724 165.324  1.00 35.84           C  
HETATM21815  C7  NAG M   2     243.796 189.346 171.006  1.00 33.85           C  
HETATM21816  C8  NAG M   2     243.684 190.449 172.019  1.00 33.90           C  
HETATM21817  N2  NAG M   2     244.844 189.369 170.185  1.00 34.24           N  
HETATM21818  O3  NAG M   2     247.256 187.775 170.125  1.00 35.04           O  
HETATM21819  O4  NAG M   2     248.304 187.075 167.579  1.00 35.18           O  
HETATM21820  O5  NAG M   2     244.754 187.861 166.719  1.00 34.32           O  
HETATM21821  O6  NAG M   2     245.764 185.465 165.613  1.00 34.43           O  
HETATM21822  O7  NAG M   2     242.940 188.452 170.944  1.00 33.50           O  
HETATM21823  C1  NAG N   1     236.623 223.295 139.893  1.00 26.54           C  
HETATM21824  C2  NAG N   1     238.122 223.702 139.614  1.00 26.92           C  
HETATM21825  C3  NAG N   1     238.388 223.523 138.097  1.00 27.20           C  
HETATM21826  C4  NAG N   1     238.105 222.068 137.674  1.00 27.27           C  
HETATM21827  C5  NAG N   1     236.640 221.697 138.047  1.00 26.90           C  
HETATM21828  C6  NAG N   1     236.336 220.228 137.754  1.00 27.24           C  
HETATM21829  C7  NAG N   1     238.994 225.538 141.035  1.00 26.76           C  
HETATM21830  C8  NAG N   1     239.054 227.018 141.254  1.00 26.73           C  
HETATM21831  N2  NAG N   1     238.303 225.111 139.989  1.00 26.66           N  
HETATM21832  O3  NAG N   1     239.768 223.820 137.822  1.00 27.31           O  
HETATM21833  O4  NAG N   1     238.192 222.055 136.240  1.00 27.89           O  
HETATM21834  O5  NAG N   1     236.410 221.909 139.489  1.00 26.73           O  
HETATM21835  O6  NAG N   1     237.248 219.342 138.399  1.00 27.43           O  
HETATM21836  O7  NAG N   1     239.562 224.750 141.800  1.00 26.81           O  
HETATM21837  C1  NAG N   2     239.164 221.052 135.710  1.00 28.12           C  
HETATM21838  C2  NAG N   2     238.955 220.849 134.176  1.00 28.02           C  
HETATM21839  C3  NAG N   2     239.882 219.695 133.707  1.00 28.08           C  
HETATM21840  C4  NAG N   2     241.355 220.063 134.050  1.00 28.55           C  
HETATM21841  C5  NAG N   2     241.480 220.288 135.589  1.00 28.38           C  
HETATM21842  C6  NAG N   2     242.882 220.705 136.007  1.00 28.74           C  
HETATM21843  C7  NAG N   2     236.674 221.372 133.356  1.00 27.59           C  
HETATM21844  C8  NAG N   2     235.261 220.899 133.184  1.00 27.49           C  
HETATM21845  N2  NAG N   2     237.538 220.533 133.922  1.00 28.03           N  
HETATM21846  O3  NAG N   2     239.743 219.522 132.290  1.00 28.64           O  
HETATM21847  O4  NAG N   2     242.209 219.000 133.633  1.00 28.70           O  
HETATM21848  O5  NAG N   2     240.551 221.360 136.009  1.00 28.16           O  
HETATM21849  O6  NAG N   2     243.088 220.500 137.401  1.00 28.52           O  
HETATM21850  O7  NAG N   2     237.020 222.500 132.974  1.00 27.32           O  
HETATM21851  C1  NAG O   1     221.814 236.132 134.762  1.00 33.66           C  
HETATM21852  C2  NAG O   1     222.019 237.538 135.442  1.00 34.22           C  
HETATM21853  C3  NAG O   1     220.932 238.504 134.899  1.00 35.77           C  
HETATM21854  C4  NAG O   1     221.052 238.600 133.348  1.00 36.74           C  
HETATM21855  C5  NAG O   1     220.868 237.169 132.757  1.00 35.81           C  
HETATM21856  C6  NAG O   1     221.004 237.138 131.239  1.00 37.03           C  
HETATM21857  C7  NAG O   1     222.929 237.194 137.723  1.00 33.23           C  
HETATM21858  C8  NAG O   1     222.622 237.029 139.182  1.00 31.40           C  
HETATM21859  N2  NAG O   1     221.898 237.375 136.899  1.00 33.97           N  
HETATM21860  O3  NAG O   1     221.119 239.793 135.503  1.00 36.04           O  
HETATM21861  O4  NAG O   1     220.019 239.461 132.802  1.00 37.79           O  
HETATM21862  O5  NAG O   1     221.892 236.269 133.316  1.00 34.50           O  
HETATM21863  O6  NAG O   1     220.844 235.825 130.716  1.00 36.69           O  
HETATM21864  O7  NAG O   1     224.095 237.169 137.307  1.00 33.30           O  
HETATM21865  C1  NAG O   2     220.438 240.900 132.608  1.00 38.94           C  
HETATM21866  C2  NAG O   2     219.964 241.450 131.214  1.00 39.50           C  
HETATM21867  C3  NAG O   2     220.523 242.893 131.044  1.00 40.38           C  
HETATM21868  C4  NAG O   2     220.019 243.781 132.215  1.00 41.01           C  
HETATM21869  C5  NAG O   2     220.496 243.158 133.559  1.00 40.14           C  
HETATM21870  C6  NAG O   2     220.006 243.936 134.775  1.00 41.11           C  
HETATM21871  C7  NAG O   2     219.720 240.072 129.164  1.00 39.74           C  
HETATM21872  C8  NAG O   2     220.404 239.226 128.126  1.00 40.29           C  
HETATM21873  N2  NAG O   2     220.474 240.597 130.125  1.00 40.13           N  
HETATM21874  O3  NAG O   2     220.071 243.441 129.793  1.00 40.60           O  
HETATM21875  O4  NAG O   2     220.546 245.099 132.065  1.00 40.68           O  
HETATM21876  O5  NAG O   2     219.988 241.776 133.678  1.00 39.57           O  
HETATM21877  O6  NAG O   2     218.593 244.111 134.773  1.00 40.90           O  
HETATM21878  O7  NAG O   2     218.497 240.270 129.119  1.00 40.31           O  
HETATM21879  C1  NAG A1301     170.484 243.581 217.363  1.00 54.42           C  
HETATM21880  C2  NAG A1301     170.297 244.288 215.959  1.00 54.81           C  
HETATM21881  C3  NAG A1301     168.907 244.981 215.956  1.00 55.06           C  
HETATM21882  C4  NAG A1301     167.801 243.923 216.208  1.00 55.52           C  
HETATM21883  C5  NAG A1301     168.065 243.236 217.579  1.00 55.39           C  
HETATM21884  C6  NAG A1301     167.050 242.137 217.875  1.00 57.22           C  
HETATM21885  C7  NAG A1301     172.461 245.109 215.050  1.00 54.27           C  
HETATM21886  C8  NAG A1301     173.428 246.253 214.984  1.00 53.23           C  
HETATM21887  N2  NAG A1301     171.355 245.294 215.766  1.00 54.20           N  
HETATM21888  O3  NAG A1301     168.696 245.620 214.687  1.00 54.74           O  
HETATM21889  O4  NAG A1301     166.528 244.565 216.215  1.00 56.08           O  
HETATM21890  O5  NAG A1301     169.408 242.618 217.573  1.00 54.72           O  
HETATM21891  O6  NAG A1301     167.141 241.698 219.226  1.00 56.21           O  
HETATM21892  O7  NAG A1301     172.684 244.040 214.464  1.00 54.09           O  
HETATM21893  C1  NAG A1302     189.471 263.335 243.323  1.00 70.79           C  
HETATM21894  C2  NAG A1302     190.178 264.650 243.847  1.00 71.66           C  
HETATM21895  C3  NAG A1302     191.262 264.239 244.885  1.00 71.79           C  
HETATM21896  C4  NAG A1302     190.601 263.456 246.049  1.00 72.35           C  
HETATM21897  C5  NAG A1302     189.903 262.195 245.465  1.00 71.11           C  
HETATM21898  C6  NAG A1302     189.158 261.397 246.527  1.00 69.94           C  
HETATM21899  C7  NAG A1302     190.357 266.409 242.098  1.00 71.10           C  
HETATM21900  C8  NAG A1302     191.187 266.974 240.984  1.00 70.78           C  
HETATM21901  N2  NAG A1302     190.840 265.343 242.728  1.00 70.25           N  
HETATM21902  O3  NAG A1302     191.906 265.416 245.398  1.00 71.23           O  
HETATM21903  O4  NAG A1302     191.609 263.066 246.979  1.00 71.28           O  
HETATM21904  O5  NAG A1302     188.906 262.604 244.456  1.00 70.89           O  
HETATM21905  O6  NAG A1302     188.699 260.152 246.012  1.00 69.01           O  
HETATM21906  O7  NAG A1302     189.274 266.918 242.418  1.00 70.94           O  
HETATM21907  C1  NAG A1305     206.416 255.125 211.642  1.00 48.02           C  
HETATM21908  C2  NAG A1305     205.395 255.311 210.452  1.00 48.37           C  
HETATM21909  C3  NAG A1305     205.928 256.431 209.518  1.00 48.45           C  
HETATM21910  C4  NAG A1305     206.080 257.741 210.336  1.00 49.39           C  
HETATM21911  C5  NAG A1305     207.067 257.490 211.512  1.00 49.43           C  
HETATM21912  C6  NAG A1305     207.228 258.716 212.403  1.00 50.38           C  
HETATM21913  C7  NAG A1305     204.118 253.423 209.481  1.00 47.21           C  
HETATM21914  C8  NAG A1305     204.177 252.120 208.740  1.00 45.93           C  
HETATM21915  N2  NAG A1305     205.271 254.038 209.726  1.00 47.95           N  
HETATM21916  O3  NAG A1305     205.005 256.632 208.437  1.00 48.81           O  
HETATM21917  O4  NAG A1305     206.571 258.779 209.487  1.00 49.41           O  
HETATM21918  O5  NAG A1305     206.557 256.390 212.356  1.00 48.60           O  
HETATM21919  O6  NAG A1305     208.344 258.576 213.277  1.00 49.92           O  
HETATM21920  O7  NAG A1305     203.035 253.906 209.844  1.00 47.74           O  
HETATM21921  C1  NAG A1306     164.529 199.465 233.442  1.00 67.88           C  
HETATM21922  C2  NAG A1306     164.694 197.887 233.511  1.00 67.54           C  
HETATM21923  C3  NAG A1306     163.492 197.248 232.756  1.00 68.15           C  
HETATM21924  C4  NAG A1306     162.163 197.714 233.410  1.00 68.58           C  
HETATM21925  C5  NAG A1306     162.087 199.266 233.341  1.00 67.91           C  
HETATM21926  C6  NAG A1306     160.834 199.818 234.014  1.00 68.15           C  
HETATM21927  C7  NAG A1306     166.986 196.943 233.449  1.00 66.62           C  
HETATM21928  C8  NAG A1306     168.186 196.604 232.614  1.00 66.77           C  
HETATM21929  N2  NAG A1306     165.943 197.500 232.836  1.00 66.89           N  
HETATM21930  O3  NAG A1306     163.585 195.815 232.832  1.00 67.77           O  
HETATM21931  O4  NAG A1306     161.064 197.139 232.700  1.00 67.99           O  
HETATM21932  O5  NAG A1306     163.253 199.853 234.026  1.00 68.09           O  
HETATM21933  O6  NAG A1306     160.753 199.457 235.390  1.00 67.93           O  
HETATM21934  O7  NAG A1306     166.980 196.710 234.667  1.00 68.19           O  
HETATM21935  C1  NAG A1307     181.775 203.529 258.531  1.00 81.34           C  
HETATM21936  C2  NAG A1307     181.187 204.148 257.202  1.00 81.61           C  
HETATM21937  C3  NAG A1307     181.339 205.695 257.288  1.00 80.96           C  
HETATM21938  C4  NAG A1307     180.582 206.220 258.538  1.00 82.11           C  
HETATM21939  C5  NAG A1307     181.175 205.540 259.807  1.00 82.34           C  
HETATM21940  C6  NAG A1307     180.437 205.948 261.076  1.00 81.45           C  
HETATM21941  C7  NAG A1307     181.365 203.042 254.980  1.00 79.73           C  
HETATM21942  C8  NAG A1307     182.270 202.604 253.864  1.00 79.28           C  
HETATM21943  N2  NAG A1307     181.928 203.644 256.029  1.00 81.29           N  
HETATM21944  O3  NAG A1307     180.801 206.297 256.099  1.00 80.68           O  
HETATM21945  O4  NAG A1307     180.731 207.635 258.620  1.00 81.14           O  
HETATM21946  O5  NAG A1307     181.059 204.072 259.682  1.00 82.43           O  
HETATM21947  O6  NAG A1307     181.154 205.554 262.241  1.00 82.10           O  
HETATM21948  O7  NAG A1307     180.140 202.859 254.918  1.00 80.49           O  
HETATM21949  C1  NAG A1308     193.262 245.120 190.580  1.00 42.30           C  
HETATM21950  C2  NAG A1308     193.931 246.475 191.037  1.00 42.49           C  
HETATM21951  C3  NAG A1308     193.856 247.475 189.848  1.00 43.35           C  
HETATM21952  C4  NAG A1308     194.591 246.866 188.626  1.00 43.52           C  
HETATM21953  C5  NAG A1308     193.919 245.512 188.250  1.00 43.21           C  
HETATM21954  C6  NAG A1308     194.631 244.817 187.093  1.00 43.26           C  
HETATM21955  C7  NAG A1308     193.627 246.860 193.467  1.00 42.46           C  
HETATM21956  C8  NAG A1308     192.772 247.455 194.544  1.00 42.94           C  
HETATM21957  N2  NAG A1308     193.214 247.004 192.209  1.00 43.28           N  
HETATM21958  O3  NAG A1308     194.479 248.714 190.225  1.00 43.35           O  
HETATM21959  O4  NAG A1308     194.501 247.779 187.532  1.00 42.63           O  
HETATM21960  O5  NAG A1308     193.965 244.598 189.414  1.00 43.19           O  
HETATM21961  O6  NAG A1308     193.785 243.857 186.470  1.00 42.56           O  
HETATM21962  O7  NAG A1308     194.680 246.266 193.741  1.00 42.00           O  
HETATM21963  C1  NAG A1309     168.961 214.388 198.981  1.00 41.91           C  
HETATM21964  C2  NAG A1309     169.272 213.373 197.810  1.00 41.88           C  
HETATM21965  C3  NAG A1309     167.995 213.235 196.936  1.00 41.89           C  
HETATM21966  C4  NAG A1309     166.825 212.723 197.820  1.00 42.35           C  
HETATM21967  C5  NAG A1309     166.596 213.734 198.984  1.00 41.97           C  
HETATM21968  C6  NAG A1309     165.522 213.272 199.962  1.00 42.05           C  
HETATM21969  C7  NAG A1309     171.655 213.427 197.122  1.00 42.01           C  
HETATM21970  C8  NAG A1309     172.687 214.061 196.238  1.00 42.18           C  
HETATM21971  N2  NAG A1309     170.405 213.875 197.014  1.00 42.14           N  
HETATM21972  O3  NAG A1309     168.246 212.308 195.868  1.00 42.06           O  
HETATM21973  O4  NAG A1309     165.652 212.617 197.015  1.00 42.04           O  
HETATM21974  O5  NAG A1309     167.838 213.887 199.768  1.00 41.63           O  
HETATM21975  O6  NAG A1309     164.214 213.410 199.420  1.00 42.01           O  
HETATM21976  O7  NAG A1309     171.957 212.521 197.913  1.00 42.10           O  
HETATM21977  C1  NAG A1310     167.810 225.508 181.484  1.00 38.31           C  
HETATM21978  C2  NAG A1310     167.350 226.067 182.892  1.00 38.77           C  
HETATM21979  C3  NAG A1310     166.042 225.339 183.303  1.00 38.52           C  
HETATM21980  C4  NAG A1310     164.956 225.584 182.223  1.00 38.99           C  
HETATM21981  C5  NAG A1310     165.475 225.042 180.859  1.00 39.18           C  
HETATM21982  C6  NAG A1310     164.485 225.293 179.726  1.00 39.82           C  
HETATM21983  C7  NAG A1310     169.263 226.699 184.332  1.00 37.54           C  
HETATM21984  C8  NAG A1310     170.265 226.246 185.350  1.00 37.07           C  
HETATM21985  N2  NAG A1310     168.393 225.798 183.888  1.00 38.50           N  
HETATM21986  O3  NAG A1310     165.595 225.845 184.571  1.00 38.32           O  
HETATM21987  O4  NAG A1310     163.758 224.909 182.601  1.00 38.10           O  
HETATM21988  O5  NAG A1310     166.743 225.722 180.509  1.00 38.71           O  
HETATM21989  O6  NAG A1310     164.788 224.495 178.587  1.00 39.05           O  
HETATM21990  O7  NAG A1310     169.253 227.867 183.915  1.00 37.95           O  
HETATM21991  C1  NAG A1311     182.372 206.869 147.335  1.00 23.69           C  
HETATM21992  C2  NAG A1311     182.625 205.871 146.143  1.00 23.82           C  
HETATM21993  C3  NAG A1311     181.476 206.037 145.115  1.00 23.87           C  
HETATM21994  C4  NAG A1311     180.121 205.753 145.816  1.00 24.09           C  
HETATM21995  C5  NAG A1311     179.948 206.745 147.003  1.00 23.91           C  
HETATM21996  C6  NAG A1311     178.659 206.502 147.778  1.00 24.66           C  
HETATM21997  C7  NAG A1311     185.075 205.620 145.871  1.00 23.80           C  
HETATM21998  C8  NAG A1311     186.313 206.088 145.169  1.00 24.14           C  
HETATM21999  N2  NAG A1311     183.925 206.202 145.537  1.00 23.72           N  
HETATM22000  O3  NAG A1311     181.669 205.110 144.035  1.00 24.10           O  
HETATM22001  O4  NAG A1311     179.064 205.923 144.875  1.00 24.29           O  
HETATM22002  O5  NAG A1311     181.078 206.588 147.945  1.00 23.66           O  
HETATM22003  O6  NAG A1311     178.311 207.633 148.571  1.00 24.17           O  
HETATM22004  O7  NAG A1311     185.126 204.731 146.730  1.00 23.36           O  
HETATM22005  C1  NAG A1316     184.758 221.817 152.596  1.00 20.83           C  
HETATM22006  C2  NAG A1316     184.814 223.343 152.997  1.00 20.83           C  
HETATM22007  C3  NAG A1316     184.163 223.506 154.399  1.00 20.80           C  
HETATM22008  C4  NAG A1316     182.696 223.007 154.339  1.00 20.70           C  
HETATM22009  C5  NAG A1316     182.698 221.514 153.901  1.00 20.75           C  
HETATM22010  C6  NAG A1316     181.292 220.953 153.736  1.00 21.10           C  
HETATM22011  C7  NAG A1316     186.668 224.868 152.395  1.00 20.81           C  
HETATM22012  C8  NAG A1316     188.127 225.170 152.531  1.00 20.68           C  
HETATM22013  N2  NAG A1316     186.215 223.789 153.026  1.00 20.79           N  
HETATM22014  O3  NAG A1316     184.193 224.891 154.780  1.00 20.85           O  
HETATM22015  O4  NAG A1316     182.105 223.156 155.630  1.00 20.45           O  
HETATM22016  O5  NAG A1316     183.365 221.378 152.592  1.00 20.87           O  
HETATM22017  O6  NAG A1316     180.644 220.758 154.988  1.00 21.27           O  
HETATM22018  O7  NAG A1316     185.921 225.598 151.727  1.00 20.83           O  
HETATM22019  C1  NAG B1301     196.544 160.617 216.008  1.00 56.99           C  
HETATM22020  C2  NAG B1301     198.042 161.043 215.737  1.00 57.15           C  
HETATM22021  C3  NAG B1301     198.619 160.112 214.635  1.00 57.06           C  
HETATM22022  C4  NAG B1301     198.527 158.636 215.105  1.00 57.22           C  
HETATM22023  C5  NAG B1301     197.036 158.292 215.392  1.00 56.94           C  
HETATM22024  C6  NAG B1301     196.857 156.877 215.932  1.00 57.33           C  
HETATM22025  C7  NAG B1301     198.336 163.486 216.076  1.00 56.58           C  
HETATM22026  C8  NAG B1301     198.340 164.843 215.441  1.00 55.78           C  
HETATM22027  N2  NAG B1301     198.090 162.446 215.285  1.00 57.04           N  
HETATM22028  O3  NAG B1301     199.992 160.459 214.386  1.00 56.74           O  
HETATM22029  O4  NAG B1301     199.043 157.787 214.084  1.00 57.00           O  
HETATM22030  O5  NAG B1301     196.504 159.216 216.415  1.00 57.28           O  
HETATM22031  O6  NAG B1301     195.515 156.430 215.769  1.00 56.50           O  
HETATM22032  O7  NAG B1301     198.570 163.342 217.286  1.00 56.53           O  
HETATM22033  C1  NAG B1302     168.322 168.144 240.193  1.00 80.89           C  
HETATM22034  C2  NAG B1302     166.939 167.662 240.826  1.00 80.85           C  
HETATM22035  C3  NAG B1302     166.744 168.424 242.168  1.00 80.53           C  
HETATM22036  C4  NAG B1302     167.911 168.132 243.142  1.00 81.18           C  
HETATM22037  C5  NAG B1302     169.223 168.595 242.455  1.00 80.60           C  
HETATM22038  C6  NAG B1302     170.454 168.361 243.316  1.00 80.37           C  
HETATM22039  C7  NAG B1302     164.677 167.394 239.811  1.00 80.09           C  
HETATM22040  C8  NAG B1302     163.681 167.918 238.822  1.00 81.42           C  
HETATM22041  N2  NAG B1302     165.843 168.011 239.894  1.00 81.00           N  
HETATM22042  O3  NAG B1302     165.498 168.063 242.773  1.00 80.54           O  
HETATM22043  O4  NAG B1302     167.706 168.863 244.353  1.00 81.87           O  
HETATM22044  O5  NAG B1302     169.400 167.890 241.158  1.00 81.44           O  
HETATM22045  O6  NAG B1302     171.552 169.156 242.879  1.00 79.93           O  
HETATM22046  O7  NAG B1302     164.418 166.423 240.513  1.00 80.61           O  
HETATM22047  C1  NAG B1303     196.603 174.312 241.363  1.00 72.89           C  
HETATM22048  C2  NAG B1303     197.657 175.440 241.713  1.00 72.63           C  
HETATM22049  C3  NAG B1303     199.061 174.949 241.268  1.00 72.24           C  
HETATM22050  C4  NAG B1303     199.397 173.622 241.998  1.00 73.66           C  
HETATM22051  C5  NAG B1303     198.312 172.563 241.647  1.00 72.54           C  
HETATM22052  C6  NAG B1303     198.538 171.246 242.390  1.00 72.40           C  
HETATM22053  C7  NAG B1303     196.740 177.738 241.573  1.00 72.67           C  
HETATM22054  C8  NAG B1303     196.463 178.923 240.699  1.00 72.80           C  
HETATM22055  N2  NAG B1303     197.315 176.684 241.005  1.00 72.43           N  
HETATM22056  O3  NAG B1303     200.042 175.948 241.592  1.00 72.50           O  
HETATM22057  O4  NAG B1303     200.684 173.171 241.584  1.00 72.95           O  
HETATM22058  O5  NAG B1303     196.980 173.073 242.042  1.00 73.22           O  
HETATM22059  O6  NAG B1303     197.846 170.166 241.775  1.00 72.06           O  
HETATM22060  O7  NAG B1303     196.441 177.747 242.778  1.00 72.57           O  
HETATM22061  C1  NAG B1304     170.497 185.970 208.251  1.00 57.44           C  
HETATM22062  C2  NAG B1304     170.943 185.029 207.064  1.00 58.34           C  
HETATM22063  C3  NAG B1304     169.790 184.973 206.026  1.00 58.05           C  
HETATM22064  C4  NAG B1304     168.511 184.432 206.718  1.00 59.28           C  
HETATM22065  C5  NAG B1304     168.141 185.372 207.904  1.00 59.12           C  
HETATM22066  C6  NAG B1304     166.930 184.868 208.680  1.00 59.29           C  
HETATM22067  C7  NAG B1304     173.294 184.888 206.296  1.00 56.01           C  
HETATM22068  C8  NAG B1304     174.451 185.609 205.670  1.00 54.68           C  
HETATM22069  N2  NAG B1304     172.168 185.574 206.458  1.00 57.74           N  
HETATM22070  O3  NAG B1304     170.163 184.111 204.941  1.00 58.32           O  
HETATM22071  O4  NAG B1304     167.445 184.391 205.771  1.00 59.20           O  
HETATM22072  O5  NAG B1304     169.275 185.443 208.851  1.00 58.13           O  
HETATM22073  O6  NAG B1304     166.447 185.854 209.587  1.00 59.44           O  
HETATM22074  O7  NAG B1304     173.387 183.703 206.649  1.00 57.72           O  
HETATM22075  C1  NAG B1305     242.607 178.502 234.503  1.00 78.65           C  
HETATM22076  C2  NAG B1305     243.784 179.142 233.659  1.00 78.29           C  
HETATM22077  C3  NAG B1305     244.171 178.151 232.530  1.00 77.96           C  
HETATM22078  C4  NAG B1305     244.586 176.790 233.147  1.00 79.46           C  
HETATM22079  C5  NAG B1305     243.394 176.234 233.979  1.00 79.15           C  
HETATM22080  C6  NAG B1305     243.741 174.924 234.676  1.00 79.26           C  
HETATM22081  C7  NAG B1305     243.576 181.616 233.531  1.00 76.56           C  
HETATM22082  C8  NAG B1305     243.015 182.784 232.774  1.00 77.35           C  
HETATM22083  N2  NAG B1305     243.325 180.402 233.053  1.00 77.07           N  
HETATM22084  O3  NAG B1305     245.277 178.695 231.790  1.00 77.80           O  
HETATM22085  O4  NAG B1305     244.928 175.876 232.107  1.00 78.77           O  
HETATM22086  O5  NAG B1305     243.030 177.209 235.029  1.00 78.10           O  
HETATM22087  O6  NAG B1305     242.575 174.270 235.163  1.00 78.94           O  
HETATM22088  O7  NAG B1305     244.246 181.781 234.562  1.00 78.73           O  
HETATM22089  C1  NAG B1306     238.459 176.582 258.089  1.00146.61           C  
HETATM22090  C2  NAG B1306     237.540 176.772 256.817  1.00146.85           C  
HETATM22091  C3  NAG B1306     236.526 175.626 256.749  1.00145.93           C  
HETATM22092  C4  NAG B1306     237.296 174.269 256.635  1.00146.07           C  
HETATM22093  C5  NAG B1306     238.276 174.137 257.852  1.00146.22           C  
HETATM22094  C6  NAG B1306     239.179 172.906 257.741  1.00148.55           C  
HETATM22095  C7  NAG B1306     237.528 179.205 256.374  1.00145.29           C  
HETATM22096  C8  NAG B1306     236.765 180.497 256.420  1.00144.34           C  
HETATM22097  N2  NAG B1306     236.904 178.093 256.794  1.00146.79           N  
HETATM22098  O3  NAG B1306     235.659 175.776 255.598  1.00147.55           O  
HETATM22099  O4  NAG B1306     236.331 173.207 256.707  1.00147.23           O  
HETATM22100  O5  NAG B1306     239.175 175.313 257.933  1.00146.73           O  
HETATM22101  O6  NAG B1306     238.577 171.780 258.353  1.00146.35           O  
HETATM22102  O7  NAG B1306     238.692 179.154 255.968  1.00147.56           O  
HETATM22103  C1  NAG B1307     187.442 179.962 190.898  1.00 49.93           C  
HETATM22104  C2  NAG B1307     186.935 179.551 189.459  1.00 50.03           C  
HETATM22105  C3  NAG B1307     185.512 180.143 189.264  1.00 50.10           C  
HETATM22106  C4  NAG B1307     184.578 179.582 190.370  1.00 51.15           C  
HETATM22107  C5  NAG B1307     185.147 179.970 191.766  1.00 50.20           C  
HETATM22108  C6  NAG B1307     184.320 179.368 192.897  1.00 50.57           C  
HETATM22109  C7  NAG B1307     188.899 179.382 187.948  1.00 50.52           C  
HETATM22110  C8  NAG B1307     189.734 180.059 186.902  1.00 50.35           C  
HETATM22111  N2  NAG B1307     187.857 180.063 188.429  1.00 50.61           N  
HETATM22112  O3  NAG B1307     185.015 179.780 187.965  1.00 50.04           O  
HETATM22113  O4  NAG B1307     183.273 180.131 190.202  1.00 50.37           O  
HETATM22114  O5  NAG B1307     186.521 179.445 191.905  1.00 50.58           O  
HETATM22115  O6  NAG B1307     184.623 179.976 194.147  1.00 51.12           O  
HETATM22116  O7  NAG B1307     189.175 178.241 188.345  1.00 48.24           O  
HETATM22117  C1  NAG B1308     225.758 174.676 202.962  1.00 43.46           C  
HETATM22118  C2  NAG B1308     225.956 173.114 203.113  1.00 43.78           C  
HETATM22119  C3  NAG B1308     227.182 172.703 202.250  1.00 43.88           C  
HETATM22120  C4  NAG B1308     226.909 173.096 200.772  1.00 44.11           C  
HETATM22121  C5  NAG B1308     226.665 174.633 200.691  1.00 43.97           C  
HETATM22122  C6  NAG B1308     226.314 175.093 199.282  1.00 44.52           C  
HETATM22123  C7  NAG B1308     225.664 171.666 205.092  1.00 43.76           C  
HETATM22124  C8  NAG B1308     225.926 171.465 206.555  1.00 44.26           C  
HETATM22125  N2  NAG B1308     226.139 172.776 204.531  1.00 43.64           N  
HETATM22126  O3  NAG B1308     227.395 171.286 202.346  1.00 44.40           O  
HETATM22127  O4  NAG B1308     228.037 172.735 199.974  1.00 43.98           O  
HETATM22128  O5  NAG B1308     225.533 175.005 201.564  1.00 43.57           O  
HETATM22129  O6  NAG B1308     226.436 176.506 199.156  1.00 43.85           O  
HETATM22130  O7  NAG B1308     225.017 170.836 204.435  1.00 43.76           O  
HETATM22131  C1  NAG B1309     219.331 165.960 184.950  1.00 39.88           C  
HETATM22132  C2  NAG B1309     218.928 165.258 186.314  1.00 40.33           C  
HETATM22133  C3  NAG B1309     220.207 164.617 186.923  1.00 40.42           C  
HETATM22134  C4  NAG B1309     220.795 163.593 185.919  1.00 40.76           C  
HETATM22135  C5  NAG B1309     221.134 164.327 184.588  1.00 40.96           C  
HETATM22136  C6  NAG B1309     221.646 163.365 183.522  1.00 41.43           C  
HETATM22137  C7  NAG B1309     217.080 166.488 187.419  1.00 39.16           C  
HETATM22138  C8  NAG B1309     216.687 167.543 188.410  1.00 38.68           C  
HETATM22139  N2  NAG B1309     218.380 166.252 187.248  1.00 40.09           N  
HETATM22140  O3  NAG B1309     219.868 163.956 188.152  1.00 40.18           O  
HETATM22141  O4  NAG B1309     221.972 163.012 186.480  1.00 39.82           O  
HETATM22142  O5  NAG B1309     219.915 164.967 184.052  1.00 40.64           O  
HETATM22143  O6  NAG B1309     222.204 164.065 182.415  1.00 40.91           O  
HETATM22144  O7  NAG B1309     216.224 165.870 186.771  1.00 39.38           O  
HETATM22145  C1  NAG B1310     232.141 185.754 150.647  1.00 23.88           C  
HETATM22146  C2  NAG B1310     233.378 186.361 149.900  1.00 23.95           C  
HETATM22147  C3  NAG B1310     233.956 185.269 148.946  1.00 24.13           C  
HETATM22148  C4  NAG B1310     234.368 184.033 149.797  1.00 24.42           C  
HETATM22149  C5  NAG B1310     233.118 183.496 150.548  1.00 24.18           C  
HETATM22150  C6  NAG B1310     233.464 182.325 151.470  1.00 24.34           C  
HETATM22151  C7  NAG B1310     232.998 188.797 149.636  1.00 23.88           C  
HETATM22152  C8  NAG B1310     232.554 189.905 148.737  1.00 23.81           C  
HETATM22153  N2  NAG B1310     232.979 187.549 149.137  1.00 23.83           N  
HETATM22154  O3  NAG B1310     235.097 185.790 148.243  1.00 24.12           O  
HETATM22155  O4  NAG B1310     234.906 183.031 148.944  1.00 24.64           O  
HETATM22156  O5  NAG B1310     232.555 184.561 151.403  1.00 23.98           O  
HETATM22157  O6  NAG B1310     232.295 181.586 151.818  1.00 24.72           O  
HETATM22158  O7  NAG B1310     233.386 189.022 150.787  1.00 23.90           O  
HETATM22159  C1  NAG B1311     199.456 186.704 152.895  1.00 18.76           C  
HETATM22160  C2  NAG B1311     199.049 186.680 151.369  1.00 18.73           C  
HETATM22161  C3  NAG B1311     197.503 186.593 151.276  1.00 18.90           C  
HETATM22162  C4  NAG B1311     197.006 185.328 152.015  1.00 18.52           C  
HETATM22163  C5  NAG B1311     197.455 185.413 153.498  1.00 18.52           C  
HETATM22164  C6  NAG B1311     197.042 184.188 154.303  1.00 19.22           C  
HETATM22165  C7  NAG B1311     200.539 188.049 149.924  1.00 19.28           C  
HETATM22166  C8  NAG B1311     200.852 189.431 149.425  1.00 19.34           C  
HETATM22167  N2  NAG B1311     199.512 187.936 150.757  1.00 18.92           N  
HETATM22168  O3  NAG B1311     197.113 186.530 149.895  1.00 18.82           O  
HETATM22169  O4  NAG B1311     195.583 185.261 151.930  1.00 19.08           O  
HETATM22170  O5  NAG B1311     198.928 185.518 153.559  1.00 18.47           O  
HETATM22171  O6  NAG B1311     196.976 184.486 155.693  1.00 19.78           O  
HETATM22172  O7  NAG B1311     201.212 187.066 149.579  1.00 19.10           O  
HETATM22173  C1  NAG B1314     217.470 180.506 154.775  1.00 20.77           C  
HETATM22174  C2  NAG B1314     216.107 179.830 155.202  1.00 20.85           C  
HETATM22175  C3  NAG B1314     216.259 179.294 156.651  1.00 20.85           C  
HETATM22176  C4  NAG B1314     217.423 178.272 156.696  1.00 20.65           C  
HETATM22177  C5  NAG B1314     218.727 178.976 156.230  1.00 20.63           C  
HETATM22178  C6  NAG B1314     219.908 178.013 156.180  1.00 20.83           C  
HETATM22179  C7  NAG B1314     213.928 180.700 154.423  1.00 20.82           C  
HETATM22180  C8  NAG B1314     212.947 181.826 154.493  1.00 20.33           C  
HETATM22181  N2  NAG B1314     215.032 180.826 155.147  1.00 20.85           N  
HETATM22182  O3  NAG B1314     215.035 178.663 157.057  1.00 21.04           O  
HETATM22183  O4  NAG B1314     217.574 177.797 158.031  1.00 20.30           O  
HETATM22184  O5  NAG B1314     218.541 179.519 154.870  1.00 20.88           O  
HETATM22185  O6  NAG B1314     221.141 178.714 156.074  1.00 21.26           O  
HETATM22186  O7  NAG B1314     213.714 179.698 153.726  1.00 20.84           O  
HETATM22187  C1  NAG B1319     185.015 174.284 256.438  1.00 80.65           C  
HETATM22188  C2  NAG B1319     185.936 173.000 256.505  1.00 80.29           C  
HETATM22189  C3  NAG B1319     186.110 172.625 258.013  1.00 80.19           C  
HETATM22190  C4  NAG B1319     186.759 173.824 258.757  1.00 80.93           C  
HETATM22191  C5  NAG B1319     185.844 175.074 258.607  1.00 81.45           C  
HETATM22192  C6  NAG B1319     186.460 176.313 259.248  1.00 81.56           C  
HETATM22193  C7  NAG B1319     185.966 170.871 255.221  1.00 79.69           C  
HETATM22194  C8  NAG B1319     185.164 169.884 254.424  1.00 79.28           C  
HETATM22195  N2  NAG B1319     185.315 171.923 255.712  1.00 79.47           N  
HETATM22196  O3  NAG B1319     186.945 171.467 258.152  1.00 79.23           O  
HETATM22197  O4  NAG B1319     186.911 173.492 260.137  1.00 80.75           O  
HETATM22198  O5  NAG B1319     185.643 175.375 257.174  1.00 82.13           O  
HETATM22199  O6  NAG B1319     185.488 177.336 259.435  1.00 80.54           O  
HETATM22200  O7  NAG B1319     187.180 170.706 255.409  1.00 78.98           O  
HETATM22201  C1  NAG C1301     254.050 226.114 221.893  1.00 52.27           C  
HETATM22202  C2  NAG C1301     255.530 226.552 221.554  1.00 52.76           C  
HETATM22203  C3  NAG C1301     255.468 227.694 220.504  1.00 52.69           C  
HETATM22204  C4  NAG C1301     254.720 227.187 219.241  1.00 53.28           C  
HETATM22205  C5  NAG C1301     253.285 226.736 219.650  1.00 53.45           C  
HETATM22206  C6  NAG C1301     252.499 226.170 218.474  1.00 53.93           C  
HETATM22207  C7  NAG C1301     257.403 226.668 223.172  1.00 51.27           C  
HETATM22208  C8  NAG C1301     257.890 227.242 224.466  1.00 51.17           C  
HETATM22209  N2  NAG C1301     256.178 227.012 222.791  1.00 52.03           N  
HETATM22210  O3  NAG C1301     256.801 228.095 220.150  1.00 52.64           O  
HETATM22211  O4  NAG C1301     254.647 228.245 218.284  1.00 53.21           O  
HETATM22212  O5  NAG C1301     253.370 225.678 220.679  1.00 53.16           O  
HETATM22213  O6  NAG C1301     251.116 226.042 218.789  1.00 52.95           O  
HETATM22214  O7  NAG C1301     258.104 225.901 222.501  1.00 51.47           O  
HETATM22215  C1  NAG C1302     261.303 196.853 246.961  1.00 73.70           C  
HETATM22216  C2  NAG C1302     262.174 195.662 247.525  1.00 75.73           C  
HETATM22217  C3  NAG C1302     261.244 194.708 248.324  1.00 74.59           C  
HETATM22218  C4  NAG C1302     260.557 195.496 249.467  1.00 74.91           C  
HETATM22219  C5  NAG C1302     259.737 196.663 248.848  1.00 74.47           C  
HETATM22220  C6  NAG C1302     259.070 197.532 249.910  1.00 74.12           C  
HETATM22221  C7  NAG C1302     264.023 195.023 246.001  1.00 74.70           C  
HETATM22222  C8  NAG C1302     264.421 194.182 244.827  1.00 74.61           C  
HETATM22223  N2  NAG C1302     262.762 194.924 246.398  1.00 73.94           N  
HETATM22224  O3  NAG C1302     262.021 193.635 248.877  1.00 74.80           O  
HETATM22225  O4  NAG C1302     259.698 194.617 250.190  1.00 74.27           O  
HETATM22226  O5  NAG C1302     260.638 197.534 248.066  1.00 74.75           O  
HETATM22227  O6  NAG C1302     258.051 198.353 249.351  1.00 73.32           O  
HETATM22228  O7  NAG C1302     264.831 195.770 246.572  1.00 74.92           O  
HETATM22229  C1  NAG C1303     236.805 213.688 245.244  1.00 62.25           C  
HETATM22230  C2  NAG C1303     236.462 212.994 246.621  1.00 62.06           C  
HETATM22231  C3  NAG C1303     234.917 212.887 246.745  1.00 62.09           C  
HETATM22232  C4  NAG C1303     234.306 214.310 246.673  1.00 62.54           C  
HETATM22233  C5  NAG C1303     234.708 214.968 245.321  1.00 62.03           C  
HETATM22234  C6  NAG C1303     234.189 216.399 245.214  1.00 61.86           C  
HETATM22235  C7  NAG C1303     237.942 211.261 247.599  1.00 61.92           C  
HETATM22236  C8  NAG C1303     238.489 209.873 247.471  1.00 62.24           C  
HETATM22237  N2  NAG C1303     237.088 211.662 246.660  1.00 62.58           N  
HETATM22238  O3  NAG C1303     234.573 212.269 247.995  1.00 61.88           O  
HETATM22239  O4  NAG C1303     232.887 214.218 246.777  1.00 62.11           O  
HETATM22240  O5  NAG C1303     236.185 215.011 245.207  1.00 62.65           O  
HETATM22241  O6  NAG C1303     234.225 216.864 243.870  1.00 61.60           O  
HETATM22242  O7  NAG C1303     238.272 211.997 248.541  1.00 61.90           O  
HETATM22243  C1  NAG C1304     251.044 190.000 211.707  1.00 50.68           C  
HETATM22244  C2  NAG C1304     251.811 190.867 210.630  1.00 51.21           C  
HETATM22245  C3  NAG C1304     252.614 189.904 209.713  1.00 51.27           C  
HETATM22246  C4  NAG C1304     253.606 189.085 210.580  1.00 51.97           C  
HETATM22247  C5  NAG C1304     252.804 188.285 211.649  1.00 52.28           C  
HETATM22248  C6  NAG C1304     253.718 187.510 212.591  1.00 52.49           C  
HETATM22249  C7  NAG C1304     250.807 192.967 209.774  1.00 50.39           C  
HETATM22250  C8  NAG C1304     249.729 193.590 208.940  1.00 49.39           C  
HETATM22251  N2  NAG C1304     250.830 191.639 209.850  1.00 51.03           N  
HETATM22252  O3  NAG C1304     253.334 190.665 208.731  1.00 51.58           O  
HETATM22253  O4  NAG C1304     254.339 188.193 209.742  1.00 51.70           O  
HETATM22254  O5  NAG C1304     252.012 189.221 212.474  1.00 51.46           O  
HETATM22255  O6  NAG C1304     252.983 186.568 213.365  1.00 52.06           O  
HETATM22256  O7  NAG C1304     251.639 193.667 210.371  1.00 50.80           O  
HETATM22257  C1  NAG C1305     218.249 254.099 236.991  1.00 61.67           C  
HETATM22258  C2  NAG C1305     216.725 254.292 237.360  1.00 62.48           C  
HETATM22259  C3  NAG C1305     216.081 255.203 236.278  1.00 62.06           C  
HETATM22260  C4  NAG C1305     216.830 256.562 236.245  1.00 62.22           C  
HETATM22261  C5  NAG C1305     218.333 256.305 235.929  1.00 61.82           C  
HETATM22262  C6  NAG C1305     219.151 257.592 235.928  1.00 62.65           C  
HETATM22263  C7  NAG C1305     215.414 252.493 238.464  1.00 61.35           C  
HETATM22264  C8  NAG C1305     214.814 251.124 238.336  1.00 61.57           C  
HETATM22265  N2  NAG C1305     216.067 252.973 237.407  1.00 62.05           N  
HETATM22266  O3  NAG C1305     214.696 255.414 236.592  1.00 62.39           O  
HETATM22267  O4  NAG C1305     216.250 257.389 235.239  1.00 61.68           O  
HETATM22268  O5  NAG C1305     218.910 255.399 236.951  1.00 61.89           O  
HETATM22269  O6  NAG C1305     220.378 257.420 235.226  1.00 63.45           O  
HETATM22270  O7  NAG C1305     215.299 253.149 239.510  1.00 62.70           O  
HETATM22271  C1  NAG C1306     212.666 235.014 259.815  1.00 84.63           C  
HETATM22272  C2  NAG C1306     213.703 235.407 258.690  1.00 84.19           C  
HETATM22273  C3  NAG C1306     214.942 234.476 258.834  1.00 83.41           C  
HETATM22274  C4  NAG C1306     215.554 234.644 260.250  1.00 84.41           C  
HETATM22275  C5  NAG C1306     214.476 234.279 261.309  1.00 84.32           C  
HETATM22276  C6  NAG C1306     214.977 234.484 262.735  1.00 84.90           C  
HETATM22277  C7  NAG C1306     213.115 236.117 256.384  1.00 81.76           C  
HETATM22278  C8  NAG C1306     212.451 235.751 255.090  1.00 81.13           C  
HETATM22279  N2  NAG C1306     213.092 235.214 257.362  1.00 83.51           N  
HETATM22280  O3  NAG C1306     215.919 234.822 257.840  1.00 83.76           O  
HETATM22281  O4  NAG C1306     216.683 233.780 260.379  1.00 84.42           O  
HETATM22282  O5  NAG C1306     213.297 235.148 261.123  1.00 84.35           O  
HETATM22283  O6  NAG C1306     214.146 233.819 263.679  1.00 84.56           O  
HETATM22284  O7  NAG C1306     213.659 237.220 256.533  1.00 81.91           O  
HETATM22285  C1  NAG C1307     248.994 208.723 192.777  1.00 46.32           C  
HETATM22286  C2  NAG C1307     250.509 209.151 192.890  1.00 46.44           C  
HETATM22287  C3  NAG C1307     251.371 208.078 192.167  1.00 46.79           C  
HETATM22288  C4  NAG C1307     251.124 206.700 192.841  1.00 47.36           C  
HETATM22289  C5  NAG C1307     249.610 206.348 192.742  1.00 47.08           C  
HETATM22290  C6  NAG C1307     249.280 205.041 193.454  1.00 47.48           C  
HETATM22291  C7  NAG C1307     251.546 211.403 192.714  1.00 46.22           C  
HETATM22292  C8  NAG C1307     251.559 212.725 192.002  1.00 45.90           C  
HETATM22293  N2  NAG C1307     250.665 210.493 192.297  1.00 46.79           N  
HETATM22294  O3  NAG C1307     252.762 208.420 192.263  1.00 47.21           O  
HETATM22295  O4  NAG C1307     251.908 205.704 192.183  1.00 46.74           O  
HETATM22296  O5  NAG C1307     248.809 207.409 193.387  1.00 47.27           O  
HETATM22297  O6  NAG C1307     247.998 204.554 193.073  1.00 46.97           O  
HETATM22298  O7  NAG C1307     252.319 211.178 193.657  1.00 46.14           O  
HETATM22299  C1  NAG C1308     232.692 243.186 204.245  1.00 42.13           C  
HETATM22300  C2  NAG C1308     231.443 244.036 203.792  1.00 42.19           C  
HETATM22301  C3  NAG C1308     231.948 245.251 202.974  1.00 42.34           C  
HETATM22302  C4  NAG C1308     232.907 246.093 203.855  1.00 42.84           C  
HETATM22303  C5  NAG C1308     234.099 245.194 204.308  1.00 42.49           C  
HETATM22304  C6  NAG C1308     235.069 245.937 205.224  1.00 43.02           C  
HETATM22305  C7  NAG C1308     229.452 242.593 203.439  1.00 42.48           C  
HETATM22306  C8  NAG C1308     228.653 241.770 202.473  1.00 43.19           C  
HETATM22307  N2  NAG C1308     230.550 243.195 202.976  1.00 42.17           N  
HETATM22308  O3  NAG C1308     230.827 246.056 202.573  1.00 42.27           O  
HETATM22309  O4  NAG C1308     233.381 247.208 203.102  1.00 42.93           O  
HETATM22310  O5  NAG C1308     233.579 244.024 205.046  1.00 42.08           O  
HETATM22311  O6  NAG C1308     236.369 245.359 205.174  1.00 42.20           O  
HETATM22312  O7  NAG C1308     229.098 242.710 204.619  1.00 42.03           O  
HETATM22313  C1  NAG C1309     243.744 241.608 187.517  1.00 40.96           C  
HETATM22314  C2  NAG C1309     244.754 241.688 188.735  1.00 40.75           C  
HETATM22315  C3  NAG C1309     244.418 242.964 189.558  1.00 41.13           C  
HETATM22316  C4  NAG C1309     244.544 244.210 188.643  1.00 41.25           C  
HETATM22317  C5  NAG C1309     243.567 244.056 187.440  1.00 41.24           C  
HETATM22318  C6  NAG C1309     243.687 245.211 186.453  1.00 41.79           C  
HETATM22319  C7  NAG C1309     245.438 239.445 189.543  1.00 40.62           C  
HETATM22320  C8  NAG C1309     245.133 238.299 190.459  1.00 39.86           C  
HETATM22321  N2  NAG C1309     244.610 240.486 189.574  1.00 40.90           N  
HETATM22322  O3  NAG C1309     245.331 243.074 190.662  1.00 41.09           O  
HETATM22323  O4  NAG C1309     244.220 245.377 189.397  1.00 40.77           O  
HETATM22324  O5  NAG C1309     243.877 242.812 186.701  1.00 40.93           O  
HETATM22325  O6  NAG C1309     242.561 245.266 185.584  1.00 42.24           O  
HETATM22326  O7  NAG C1309     246.413 239.413 188.778  1.00 40.43           O  
HETATM22327  C1  NAG C1310     225.032 239.142 150.317  1.00 23.72           C  
HETATM22328  C2  NAG C1310     223.876 239.786 149.458  1.00 23.85           C  
HETATM22329  C3  NAG C1310     224.507 240.829 148.497  1.00 23.96           C  
HETATM22330  C4  NAG C1310     225.249 241.905 149.333  1.00 24.02           C  
HETATM22331  C5  NAG C1310     226.345 241.210 150.190  1.00 23.95           C  
HETATM22332  C6  NAG C1310     227.090 242.196 151.083  1.00 24.38           C  
HETATM22333  C7  NAG C1310     222.123 238.064 149.141  1.00 23.95           C  
HETATM22334  C8  NAG C1310     221.562 236.995 148.256  1.00 24.16           C  
HETATM22335  N2  NAG C1310     223.198 238.718 148.706  1.00 23.83           N  
HETATM22336  O3  NAG C1310     223.474 241.447 147.715  1.00 24.15           O  
HETATM22337  O4  NAG C1310     225.847 242.850 148.448  1.00 24.41           O  
HETATM22338  O5  NAG C1310     225.728 240.186 151.059  1.00 23.78           O  
HETATM22339  O6  NAG C1310     226.215 242.936 151.928  1.00 24.40           O  
HETATM22340  O7  NAG C1310     221.610 238.315 150.241  1.00 23.97           O  
HETATM22341  C1  NAG C1315     236.718 229.458 156.160  1.00 20.73           C  
HETATM22342  C2  NAG C1315     237.948 228.638 156.720  1.00 20.78           C  
HETATM22343  C3  NAG C1315     238.219 229.118 158.173  1.00 20.78           C  
HETATM22344  C4  NAG C1315     238.518 230.641 158.164  1.00 20.62           C  
HETATM22345  C5  NAG C1315     237.291 231.385 157.565  1.00 20.61           C  
HETATM22346  C6  NAG C1315     237.503 232.891 157.467  1.00 21.03           C  
HETATM22347  C7  NAG C1315     238.237 226.304 155.923  1.00 20.90           C  
HETATM22348  C8  NAG C1315     237.796 224.876 156.036  1.00 20.60           C  
HETATM22349  N2  NAG C1315     237.635 227.197 156.708  1.00 20.79           N  
HETATM22350  O3  NAG C1315     239.338 228.404 158.719  1.00 20.69           O  
HETATM22351  O4  NAG C1315     238.754 231.082 159.500  1.00 20.73           O  
HETATM22352  O5  NAG C1315     237.027 230.883 156.205  1.00 20.81           O  
HETATM22353  O6  NAG C1315     236.279 233.566 157.198  1.00 21.35           O  
HETATM22354  O7  NAG C1315     239.127 226.633 155.127  1.00 21.26           O  
HETATM22355  C1  NAG C1320     244.146 206.263 259.830  1.00 78.59           C  
HETATM22356  C2  NAG C1320     245.083 207.220 260.660  1.00 78.71           C  
HETATM22357  C3  NAG C1320     244.456 207.418 262.068  1.00 78.51           C  
HETATM22358  C4  NAG C1320     243.037 208.026 261.906  1.00 79.77           C  
HETATM22359  C5  NAG C1320     242.166 207.061 261.046  1.00 79.33           C  
HETATM22360  C6  NAG C1320     240.773 207.626 260.786  1.00 77.48           C  
HETATM22361  C7  NAG C1320     247.495 207.052 260.117  1.00 76.97           C  
HETATM22362  C8  NAG C1320     248.777 206.300 260.318  1.00 79.16           C  
HETATM22363  N2  NAG C1320     246.418 206.606 260.759  1.00 79.38           N  
HETATM22364  O3  NAG C1320     245.283 208.301 262.843  1.00 77.77           O  
HETATM22365  O4  NAG C1320     242.453 208.203 263.195  1.00 78.45           O  
HETATM22366  O5  NAG C1320     242.813 206.851 259.732  1.00 78.50           O  
HETATM22367  O6  NAG C1320     239.881 206.613 260.335  1.00 78.34           O  
HETATM22368  O7  NAG C1320     247.449 208.056 259.394  1.00 76.92           O  
CONECT  29221879                                                                
CONECT  66421893                                                                
CONECT  722  817                                                                
CONECT  817  722                                                                
CONECT 126621543                                                                
CONECT 150021907                                                                
CONECT 1560 1633                                                                
CONECT 1633 1560                                                                
CONECT 187921921                                                                
CONECT 1916 2117                                                                
CONECT 196921935                                                                
CONECT 2117 1916                                                                
CONECT 2257 2655                                                                
CONECT 2347 3193                                                                
CONECT 2655 2257                                                                
CONECT 3193 2347                                                                
CONECT 3286 3675                                                                
CONECT 3675 3286                                                                
CONECT 376121949                                                                
CONECT 385921963                                                                
CONECT 3865 3946                                                                
CONECT 3946 3865                                                                
CONECT 400521977                                                                
CONECT 4042 4100                                                                
CONECT 4100 4042                                                                
CONECT 428621991                                                                
CONECT 434321571                                                                
CONECT 4499 4659                                                                
CONECT 4540 4573                                                                
CONECT 4573 4540                                                                
CONECT 4659 4499                                                                
CONECT 498021599                                                                
CONECT 6511 6597                                                                
CONECT 6597 6511                                                                
CONECT 683222005                                                                
CONECT 6888 7239                                                                
CONECT 701121627                                                                
CONECT 7239 6888                                                                
CONECT 729621655                                                                
CONECT 768322019                                                                
CONECT 805122033                                                                
CONECT 8110 8194                                                                
CONECT 818822187                                                                
CONECT 8194 8110                                                                
CONECT 859122047                                                                
CONECT 882822061                                                                
CONECT 8888 8961                                                                
CONECT 8961 8888                                                                
CONECT 920322075                                                                
CONECT 928822089                                                                
CONECT 9470 9738                                                                
CONECT 953210022                                                                
CONECT 9738 9470                                                                
CONECT10022 9532                                                                
CONECT1011110508                                                                
CONECT1050810111                                                                
CONECT1059422103                                                                
CONECT1069522117                                                                
CONECT1070110786                                                                
CONECT1078610701                                                                
CONECT1084522131                                                                
CONECT1088210940                                                                
CONECT1094010882                                                                
CONECT1113222145                                                                
CONECT1118922159                                                                
CONECT1134511508                                                                
CONECT1138611422                                                                
CONECT1142211386                                                                
CONECT1150811345                                                                
CONECT1182321683                                                                
CONECT1337313459                                                                
CONECT1345913373                                                                
CONECT1369822173                                                                
CONECT1375414108                                                                
CONECT1387721711                                                                
CONECT1410813754                                                                
CONECT1416521739                                                                
CONECT1455122201                                                                
CONECT1491222215                                                                
CONECT1496715065                                                                
CONECT1505922355                                                                
CONECT1506514967                                                                
CONECT1550022229                                                                
CONECT1572922243                                                                
CONECT1578915862                                                                
CONECT1586215789                                                                
CONECT1610422257                                                                
CONECT1614116338                                                                
CONECT1619422271                                                                
CONECT1633816141                                                                
CONECT1647416861                                                                
CONECT1656417320                                                                
CONECT1686116474                                                                
CONECT1732016564                                                                
CONECT1741717822                                                                
CONECT1782217417                                                                
CONECT1790822285                                                                
CONECT1800622299                                                                
CONECT1801218103                                                                
CONECT1810318012                                                                
CONECT1816222313                                                                
CONECT1819918257                                                                
CONECT1825718199                                                                
CONECT1844322327                                                                
CONECT1850021767                                                                
CONECT1865618816                                                                
CONECT1869718730                                                                
CONECT1873018697                                                                
CONECT1881618656                                                                
CONECT1913721795                                                                
CONECT2064820734                                                                
CONECT2073420648                                                                
CONECT2097322341                                                                
CONECT2102921383                                                                
CONECT2115221823                                                                
CONECT2138321029                                                                
CONECT2144021851                                                                
CONECT21543 12662154421554                                                      
CONECT21544215432154521551                                                      
CONECT21545215442154621552                                                      
CONECT21546215452154721553                                                      
CONECT21547215462154821554                                                      
CONECT215482154721555                                                           
CONECT21549215502155121556                                                      
CONECT2155021549                                                                
CONECT215512154421549                                                           
CONECT2155221545                                                                
CONECT215532154621557                                                           
CONECT215542154321547                                                           
CONECT2155521548                                                                
CONECT2155621549                                                                
CONECT21557215532155821568                                                      
CONECT21558215572155921565                                                      
CONECT21559215582156021566                                                      
CONECT21560215592156121567                                                      
CONECT21561215602156221568                                                      
CONECT215622156121569                                                           
CONECT21563215642156521570                                                      
CONECT2156421563                                                                
CONECT215652155821563                                                           
CONECT2156621559                                                                
CONECT2156721560                                                                
CONECT215682155721561                                                           
CONECT2156921562                                                                
CONECT2157021563                                                                
CONECT21571 43432157221582                                                      
CONECT21572215712157321579                                                      
CONECT21573215722157421580                                                      
CONECT21574215732157521581                                                      
CONECT21575215742157621582                                                      
CONECT215762157521583                                                           
CONECT21577215782157921584                                                      
CONECT2157821577                                                                
CONECT215792157221577                                                           
CONECT2158021573                                                                
CONECT215812157421585                                                           
CONECT215822157121575                                                           
CONECT2158321576                                                                
CONECT2158421577                                                                
CONECT21585215812158621596                                                      
CONECT21586215852158721593                                                      
CONECT21587215862158821594                                                      
CONECT21588215872158921595                                                      
CONECT21589215882159021596                                                      
CONECT215902158921597                                                           
CONECT21591215922159321598                                                      
CONECT2159221591                                                                
CONECT215932158621591                                                           
CONECT2159421587                                                                
CONECT2159521588                                                                
CONECT215962158521589                                                           
CONECT2159721590                                                                
CONECT2159821591                                                                
CONECT21599 49802160021610                                                      
CONECT21600215992160121607                                                      
CONECT21601216002160221608                                                      
CONECT21602216012160321609                                                      
CONECT21603216022160421610                                                      
CONECT216042160321611                                                           
CONECT21605216062160721612                                                      
CONECT2160621605                                                                
CONECT216072160021605                                                           
CONECT2160821601                                                                
CONECT216092160221613                                                           
CONECT216102159921603                                                           
CONECT2161121604                                                                
CONECT2161221605                                                                
CONECT21613216092161421624                                                      
CONECT21614216132161521621                                                      
CONECT21615216142161621622                                                      
CONECT21616216152161721623                                                      
CONECT21617216162161821624                                                      
CONECT216182161721625                                                           
CONECT21619216202162121626                                                      
CONECT2162021619                                                                
CONECT216212161421619                                                           
CONECT2162221615                                                                
CONECT2162321616                                                                
CONECT216242161321617                                                           
CONECT2162521618                                                                
CONECT2162621619                                                                
CONECT21627 70112162821638                                                      
CONECT21628216272162921635                                                      
CONECT21629216282163021636                                                      
CONECT21630216292163121637                                                      
CONECT21631216302163221638                                                      
CONECT216322163121639                                                           
CONECT21633216342163521640                                                      
CONECT2163421633                                                                
CONECT216352162821633                                                           
CONECT2163621629                                                                
CONECT216372163021641                                                           
CONECT216382162721631                                                           
CONECT2163921632                                                                
CONECT2164021633                                                                
CONECT21641216372164221652                                                      
CONECT21642216412164321649                                                      
CONECT21643216422164421650                                                      
CONECT21644216432164521651                                                      
CONECT21645216442164621652                                                      
CONECT216462164521653                                                           
CONECT21647216482164921654                                                      
CONECT2164821647                                                                
CONECT216492164221647                                                           
CONECT2165021643                                                                
CONECT2165121644                                                                
CONECT216522164121645                                                           
CONECT2165321646                                                                
CONECT2165421647                                                                
CONECT21655 72962165621666                                                      
CONECT21656216552165721663                                                      
CONECT21657216562165821664                                                      
CONECT21658216572165921665                                                      
CONECT21659216582166021666                                                      
CONECT216602165921667                                                           
CONECT21661216622166321668                                                      
CONECT2166221661                                                                
CONECT216632165621661                                                           
CONECT2166421657                                                                
CONECT216652165821669                                                           
CONECT216662165521659                                                           
CONECT2166721660                                                                
CONECT2166821661                                                                
CONECT21669216652167021680                                                      
CONECT21670216692167121677                                                      
CONECT21671216702167221678                                                      
CONECT21672216712167321679                                                      
CONECT21673216722167421680                                                      
CONECT216742167321681                                                           
CONECT21675216762167721682                                                      
CONECT2167621675                                                                
CONECT216772167021675                                                           
CONECT2167821671                                                                
CONECT2167921672                                                                
CONECT216802166921673                                                           
CONECT2168121674                                                                
CONECT2168221675                                                                
CONECT21683118232168421694                                                      
CONECT21684216832168521691                                                      
CONECT21685216842168621692                                                      
CONECT21686216852168721693                                                      
CONECT21687216862168821694                                                      
CONECT216882168721695                                                           
CONECT21689216902169121696                                                      
CONECT2169021689                                                                
CONECT216912168421689                                                           
CONECT2169221685                                                                
CONECT216932168621697                                                           
CONECT216942168321687                                                           
CONECT2169521688                                                                
CONECT2169621689                                                                
CONECT21697216932169821708                                                      
CONECT21698216972169921705                                                      
CONECT21699216982170021706                                                      
CONECT21700216992170121707                                                      
CONECT21701217002170221708                                                      
CONECT217022170121709                                                           
CONECT21703217042170521710                                                      
CONECT2170421703                                                                
CONECT217052169821703                                                           
CONECT2170621699                                                                
CONECT2170721700                                                                
CONECT217082169721701                                                           
CONECT2170921702                                                                
CONECT2171021703                                                                
CONECT21711138772171221722                                                      
CONECT21712217112171321719                                                      
CONECT21713217122171421720                                                      
CONECT21714217132171521721                                                      
CONECT21715217142171621722                                                      
CONECT217162171521723                                                           
CONECT21717217182171921724                                                      
CONECT2171821717                                                                
CONECT217192171221717                                                           
CONECT2172021713                                                                
CONECT217212171421725                                                           
CONECT217222171121715                                                           
CONECT2172321716                                                                
CONECT2172421717                                                                
CONECT21725217212172621736                                                      
CONECT21726217252172721733                                                      
CONECT21727217262172821734                                                      
CONECT21728217272172921735                                                      
CONECT21729217282173021736                                                      
CONECT217302172921737                                                           
CONECT21731217322173321738                                                      
CONECT2173221731                                                                
CONECT217332172621731                                                           
CONECT2173421727                                                                
CONECT2173521728                                                                
CONECT217362172521729                                                           
CONECT2173721730                                                                
CONECT2173821731                                                                
CONECT21739141652174021750                                                      
CONECT21740217392174121747                                                      
CONECT21741217402174221748                                                      
CONECT21742217412174321749                                                      
CONECT21743217422174421750                                                      
CONECT217442174321751                                                           
CONECT21745217462174721752                                                      
CONECT2174621745                                                                
CONECT217472174021745                                                           
CONECT2174821741                                                                
CONECT217492174221753                                                           
CONECT217502173921743                                                           
CONECT2175121744                                                                
CONECT2175221745                                                                
CONECT21753217492175421764                                                      
CONECT21754217532175521761                                                      
CONECT21755217542175621762                                                      
CONECT21756217552175721763                                                      
CONECT21757217562175821764                                                      
CONECT217582175721765                                                           
CONECT21759217602176121766                                                      
CONECT2176021759                                                                
CONECT217612175421759                                                           
CONECT2176221755                                                                
CONECT2176321756                                                                
CONECT217642175321757                                                           
CONECT2176521758                                                                
CONECT2176621759                                                                
CONECT21767185002176821778                                                      
CONECT21768217672176921775                                                      
CONECT21769217682177021776                                                      
CONECT21770217692177121777                                                      
CONECT21771217702177221778                                                      
CONECT217722177121779                                                           
CONECT21773217742177521780                                                      
CONECT2177421773                                                                
CONECT217752176821773                                                           
CONECT2177621769                                                                
CONECT217772177021781                                                           
CONECT217782176721771                                                           
CONECT2177921772                                                                
CONECT2178021773                                                                
CONECT21781217772178221792                                                      
CONECT21782217812178321789                                                      
CONECT21783217822178421790                                                      
CONECT21784217832178521791                                                      
CONECT21785217842178621792                                                      
CONECT217862178521793                                                           
CONECT21787217882178921794                                                      
CONECT2178821787                                                                
CONECT217892178221787                                                           
CONECT2179021783                                                                
CONECT2179121784                                                                
CONECT217922178121785                                                           
CONECT2179321786                                                                
CONECT2179421787                                                                
CONECT21795191372179621806                                                      
CONECT21796217952179721803                                                      
CONECT21797217962179821804                                                      
CONECT21798217972179921805                                                      
CONECT21799217982180021806                                                      
CONECT218002179921807                                                           
CONECT21801218022180321808                                                      
CONECT2180221801                                                                
CONECT218032179621801                                                           
CONECT2180421797                                                                
CONECT218052179821809                                                           
CONECT218062179521799                                                           
CONECT2180721800                                                                
CONECT2180821801                                                                
CONECT21809218052181021820                                                      
CONECT21810218092181121817                                                      
CONECT21811218102181221818                                                      
CONECT21812218112181321819                                                      
CONECT21813218122181421820                                                      
CONECT218142181321821                                                           
CONECT21815218162181721822                                                      
CONECT2181621815                                                                
CONECT218172181021815                                                           
CONECT2181821811                                                                
CONECT2181921812                                                                
CONECT218202180921813                                                           
CONECT2182121814                                                                
CONECT2182221815                                                                
CONECT21823211522182421834                                                      
CONECT21824218232182521831                                                      
CONECT21825218242182621832                                                      
CONECT21826218252182721833                                                      
CONECT21827218262182821834                                                      
CONECT218282182721835                                                           
CONECT21829218302183121836                                                      
CONECT2183021829                                                                
CONECT218312182421829                                                           
CONECT2183221825                                                                
CONECT218332182621837                                                           
CONECT218342182321827                                                           
CONECT2183521828                                                                
CONECT2183621829                                                                
CONECT21837218332183821848                                                      
CONECT21838218372183921845                                                      
CONECT21839218382184021846                                                      
CONECT21840218392184121847                                                      
CONECT21841218402184221848                                                      
CONECT218422184121849                                                           
CONECT21843218442184521850                                                      
CONECT2184421843                                                                
CONECT218452183821843                                                           
CONECT2184621839                                                                
CONECT2184721840                                                                
CONECT218482183721841                                                           
CONECT2184921842                                                                
CONECT2185021843                                                                
CONECT21851214402185221862                                                      
CONECT21852218512185321859                                                      
CONECT21853218522185421860                                                      
CONECT21854218532185521861                                                      
CONECT21855218542185621862                                                      
CONECT218562185521863                                                           
CONECT21857218582185921864                                                      
CONECT2185821857                                                                
CONECT218592185221857                                                           
CONECT2186021853                                                                
CONECT218612185421865                                                           
CONECT218622185121855                                                           
CONECT2186321856                                                                
CONECT2186421857                                                                
CONECT21865218612186621876                                                      
CONECT21866218652186721873                                                      
CONECT21867218662186821874                                                      
CONECT21868218672186921875                                                      
CONECT21869218682187021876                                                      
CONECT218702186921877                                                           
CONECT21871218722187321878                                                      
CONECT2187221871                                                                
CONECT218732186621871                                                           
CONECT2187421867                                                                
CONECT2187521868                                                                
CONECT218762186521869                                                           
CONECT2187721870                                                                
CONECT2187821871                                                                
CONECT21879  2922188021890                                                      
CONECT21880218792188121887                                                      
CONECT21881218802188221888                                                      
CONECT21882218812188321889                                                      
CONECT21883218822188421890                                                      
CONECT218842188321891                                                           
CONECT21885218862188721892                                                      
CONECT2188621885                                                                
CONECT218872188021885                                                           
CONECT2188821881                                                                
CONECT2188921882                                                                
CONECT218902187921883                                                           
CONECT2189121884                                                                
CONECT2189221885                                                                
CONECT21893  6642189421904                                                      
CONECT21894218932189521901                                                      
CONECT21895218942189621902                                                      
CONECT21896218952189721903                                                      
CONECT21897218962189821904                                                      
CONECT218982189721905                                                           
CONECT21899219002190121906                                                      
CONECT2190021899                                                                
CONECT219012189421899                                                           
CONECT2190221895                                                                
CONECT2190321896                                                                
CONECT219042189321897                                                           
CONECT2190521898                                                                
CONECT2190621899                                                                
CONECT21907 15002190821918                                                      
CONECT21908219072190921915                                                      
CONECT21909219082191021916                                                      
CONECT21910219092191121917                                                      
CONECT21911219102191221918                                                      
CONECT219122191121919                                                           
CONECT21913219142191521920                                                      
CONECT2191421913                                                                
CONECT219152190821913                                                           
CONECT2191621909                                                                
CONECT2191721910                                                                
CONECT219182190721911                                                           
CONECT2191921912                                                                
CONECT2192021913                                                                
CONECT21921 18792192221932                                                      
CONECT21922219212192321929                                                      
CONECT21923219222192421930                                                      
CONECT21924219232192521931                                                      
CONECT21925219242192621932                                                      
CONECT219262192521933                                                           
CONECT21927219282192921934                                                      
CONECT2192821927                                                                
CONECT219292192221927                                                           
CONECT2193021923                                                                
CONECT2193121924                                                                
CONECT219322192121925                                                           
CONECT2193321926                                                                
CONECT2193421927                                                                
CONECT21935 19692193621946                                                      
CONECT21936219352193721943                                                      
CONECT21937219362193821944                                                      
CONECT21938219372193921945                                                      
CONECT21939219382194021946                                                      
CONECT219402193921947                                                           
CONECT21941219422194321948                                                      
CONECT2194221941                                                                
CONECT219432193621941                                                           
CONECT2194421937                                                                
CONECT2194521938                                                                
CONECT219462193521939                                                           
CONECT2194721940                                                                
CONECT2194821941                                                                
CONECT21949 37612195021960                                                      
CONECT21950219492195121957                                                      
CONECT21951219502195221958                                                      
CONECT21952219512195321959                                                      
CONECT21953219522195421960                                                      
CONECT219542195321961                                                           
CONECT21955219562195721962                                                      
CONECT2195621955                                                                
CONECT219572195021955                                                           
CONECT2195821951                                                                
CONECT2195921952                                                                
CONECT219602194921953                                                           
CONECT2196121954                                                                
CONECT2196221955                                                                
CONECT21963 38592196421974                                                      
CONECT21964219632196521971                                                      
CONECT21965219642196621972                                                      
CONECT21966219652196721973                                                      
CONECT21967219662196821974                                                      
CONECT219682196721975                                                           
CONECT21969219702197121976                                                      
CONECT2197021969                                                                
CONECT219712196421969                                                           
CONECT2197221965                                                                
CONECT2197321966                                                                
CONECT219742196321967                                                           
CONECT2197521968                                                                
CONECT2197621969                                                                
CONECT21977 40052197821988                                                      
CONECT21978219772197921985                                                      
CONECT21979219782198021986                                                      
CONECT21980219792198121987                                                      
CONECT21981219802198221988                                                      
CONECT219822198121989                                                           
CONECT21983219842198521990                                                      
CONECT2198421983                                                                
CONECT219852197821983                                                           
CONECT2198621979                                                                
CONECT2198721980                                                                
CONECT219882197721981                                                           
CONECT2198921982                                                                
CONECT2199021983                                                                
CONECT21991 42862199222002                                                      
CONECT21992219912199321999                                                      
CONECT21993219922199422000                                                      
CONECT21994219932199522001                                                      
CONECT21995219942199622002                                                      
CONECT219962199522003                                                           
CONECT21997219982199922004                                                      
CONECT2199821997                                                                
CONECT219992199221997                                                           
CONECT2200021993                                                                
CONECT2200121994                                                                
CONECT220022199121995                                                           
CONECT2200321996                                                                
CONECT2200421997                                                                
CONECT22005 68322200622016                                                      
CONECT22006220052200722013                                                      
CONECT22007220062200822014                                                      
CONECT22008220072200922015                                                      
CONECT22009220082201022016                                                      
CONECT220102200922017                                                           
CONECT22011220122201322018                                                      
CONECT2201222011                                                                
CONECT220132200622011                                                           
CONECT2201422007                                                                
CONECT2201522008                                                                
CONECT220162200522009                                                           
CONECT2201722010                                                                
CONECT2201822011                                                                
CONECT22019 76832202022030                                                      
CONECT22020220192202122027                                                      
CONECT22021220202202222028                                                      
CONECT22022220212202322029                                                      
CONECT22023220222202422030                                                      
CONECT220242202322031                                                           
CONECT22025220262202722032                                                      
CONECT2202622025                                                                
CONECT220272202022025                                                           
CONECT2202822021                                                                
CONECT2202922022                                                                
CONECT220302201922023                                                           
CONECT2203122024                                                                
CONECT2203222025                                                                
CONECT22033 80512203422044                                                      
CONECT22034220332203522041                                                      
CONECT22035220342203622042                                                      
CONECT22036220352203722043                                                      
CONECT22037220362203822044                                                      
CONECT220382203722045                                                           
CONECT22039220402204122046                                                      
CONECT2204022039                                                                
CONECT220412203422039                                                           
CONECT2204222035                                                                
CONECT2204322036                                                                
CONECT220442203322037                                                           
CONECT2204522038                                                                
CONECT2204622039                                                                
CONECT22047 85912204822058                                                      
CONECT22048220472204922055                                                      
CONECT22049220482205022056                                                      
CONECT22050220492205122057                                                      
CONECT22051220502205222058                                                      
CONECT220522205122059                                                           
CONECT22053220542205522060                                                      
CONECT2205422053                                                                
CONECT220552204822053                                                           
CONECT2205622049                                                                
CONECT2205722050                                                                
CONECT220582204722051                                                           
CONECT2205922052                                                                
CONECT2206022053                                                                
CONECT22061 88282206222072                                                      
CONECT22062220612206322069                                                      
CONECT22063220622206422070                                                      
CONECT22064220632206522071                                                      
CONECT22065220642206622072                                                      
CONECT220662206522073                                                           
CONECT22067220682206922074                                                      
CONECT2206822067                                                                
CONECT220692206222067                                                           
CONECT2207022063                                                                
CONECT2207122064                                                                
CONECT220722206122065                                                           
CONECT2207322066                                                                
CONECT2207422067                                                                
CONECT22075 92032207622086                                                      
CONECT22076220752207722083                                                      
CONECT22077220762207822084                                                      
CONECT22078220772207922085                                                      
CONECT22079220782208022086                                                      
CONECT220802207922087                                                           
CONECT22081220822208322088                                                      
CONECT2208222081                                                                
CONECT220832207622081                                                           
CONECT2208422077                                                                
CONECT2208522078                                                                
CONECT220862207522079                                                           
CONECT2208722080                                                                
CONECT2208822081                                                                
CONECT22089 92882209022100                                                      
CONECT22090220892209122097                                                      
CONECT22091220902209222098                                                      
CONECT22092220912209322099                                                      
CONECT22093220922209422100                                                      
CONECT220942209322101                                                           
CONECT22095220962209722102                                                      
CONECT2209622095                                                                
CONECT220972209022095                                                           
CONECT2209822091                                                                
CONECT2209922092                                                                
CONECT221002208922093                                                           
CONECT2210122094                                                                
CONECT2210222095                                                                
CONECT22103105942210422114                                                      
CONECT22104221032210522111                                                      
CONECT22105221042210622112                                                      
CONECT22106221052210722113                                                      
CONECT22107221062210822114                                                      
CONECT221082210722115                                                           
CONECT22109221102211122116                                                      
CONECT2211022109                                                                
CONECT221112210422109                                                           
CONECT2211222105                                                                
CONECT2211322106                                                                
CONECT221142210322107                                                           
CONECT2211522108                                                                
CONECT2211622109                                                                
CONECT22117106952211822128                                                      
CONECT22118221172211922125                                                      
CONECT22119221182212022126                                                      
CONECT22120221192212122127                                                      
CONECT22121221202212222128                                                      
CONECT221222212122129                                                           
CONECT22123221242212522130                                                      
CONECT2212422123                                                                
CONECT221252211822123                                                           
CONECT2212622119                                                                
CONECT2212722120                                                                
CONECT221282211722121                                                           
CONECT2212922122                                                                
CONECT2213022123                                                                
CONECT22131108452213222142                                                      
CONECT22132221312213322139                                                      
CONECT22133221322213422140                                                      
CONECT22134221332213522141                                                      
CONECT22135221342213622142                                                      
CONECT221362213522143                                                           
CONECT22137221382213922144                                                      
CONECT2213822137                                                                
CONECT221392213222137                                                           
CONECT2214022133                                                                
CONECT2214122134                                                                
CONECT221422213122135                                                           
CONECT2214322136                                                                
CONECT2214422137                                                                
CONECT22145111322214622156                                                      
CONECT22146221452214722153                                                      
CONECT22147221462214822154                                                      
CONECT22148221472214922155                                                      
CONECT22149221482215022156                                                      
CONECT221502214922157                                                           
CONECT22151221522215322158                                                      
CONECT2215222151                                                                
CONECT221532214622151                                                           
CONECT2215422147                                                                
CONECT2215522148                                                                
CONECT221562214522149                                                           
CONECT2215722150                                                                
CONECT2215822151                                                                
CONECT22159111892216022170                                                      
CONECT22160221592216122167                                                      
CONECT22161221602216222168                                                      
CONECT22162221612216322169                                                      
CONECT22163221622216422170                                                      
CONECT221642216322171                                                           
CONECT22165221662216722172                                                      
CONECT2216622165                                                                
CONECT221672216022165                                                           
CONECT2216822161                                                                
CONECT2216922162                                                                
CONECT221702215922163                                                           
CONECT2217122164                                                                
CONECT2217222165                                                                
CONECT22173136982217422184                                                      
CONECT22174221732217522181                                                      
CONECT22175221742217622182                                                      
CONECT22176221752217722183                                                      
CONECT22177221762217822184                                                      
CONECT221782217722185                                                           
CONECT22179221802218122186                                                      
CONECT2218022179                                                                
CONECT221812217422179                                                           
CONECT2218222175                                                                
CONECT2218322176                                                                
CONECT221842217322177                                                           
CONECT2218522178                                                                
CONECT2218622179                                                                
CONECT22187 81882218822198                                                      
CONECT22188221872218922195                                                      
CONECT22189221882219022196                                                      
CONECT22190221892219122197                                                      
CONECT22191221902219222198                                                      
CONECT221922219122199                                                           
CONECT22193221942219522200                                                      
CONECT2219422193                                                                
CONECT221952218822193                                                           
CONECT2219622189                                                                
CONECT2219722190                                                                
CONECT221982218722191                                                           
CONECT2219922192                                                                
CONECT2220022193                                                                
CONECT22201145512220222212                                                      
CONECT22202222012220322209                                                      
CONECT22203222022220422210                                                      
CONECT22204222032220522211                                                      
CONECT22205222042220622212                                                      
CONECT222062220522213                                                           
CONECT22207222082220922214                                                      
CONECT2220822207                                                                
CONECT222092220222207                                                           
CONECT2221022203                                                                
CONECT2221122204                                                                
CONECT222122220122205                                                           
CONECT2221322206                                                                
CONECT2221422207                                                                
CONECT22215149122221622226                                                      
CONECT22216222152221722223                                                      
CONECT22217222162221822224                                                      
CONECT22218222172221922225                                                      
CONECT22219222182222022226                                                      
CONECT222202221922227                                                           
CONECT22221222222222322228                                                      
CONECT2222222221                                                                
CONECT222232221622221                                                           
CONECT2222422217                                                                
CONECT2222522218                                                                
CONECT222262221522219                                                           
CONECT2222722220                                                                
CONECT2222822221                                                                
CONECT22229155002223022240                                                      
CONECT22230222292223122237                                                      
CONECT22231222302223222238                                                      
CONECT22232222312223322239                                                      
CONECT22233222322223422240                                                      
CONECT222342223322241                                                           
CONECT22235222362223722242                                                      
CONECT2223622235                                                                
CONECT222372223022235                                                           
CONECT2223822231                                                                
CONECT2223922232                                                                
CONECT222402222922233                                                           
CONECT2224122234                                                                
CONECT2224222235                                                                
CONECT22243157292224422254                                                      
CONECT22244222432224522251                                                      
CONECT22245222442224622252                                                      
CONECT22246222452224722253                                                      
CONECT22247222462224822254                                                      
CONECT222482224722255                                                           
CONECT22249222502225122256                                                      
CONECT2225022249                                                                
CONECT222512224422249                                                           
CONECT2225222245                                                                
CONECT2225322246                                                                
CONECT222542224322247                                                           
CONECT2225522248                                                                
CONECT2225622249                                                                
CONECT22257161042225822268                                                      
CONECT22258222572225922265                                                      
CONECT22259222582226022266                                                      
CONECT22260222592226122267                                                      
CONECT22261222602226222268                                                      
CONECT222622226122269                                                           
CONECT22263222642226522270                                                      
CONECT2226422263                                                                
CONECT222652225822263                                                           
CONECT2226622259                                                                
CONECT2226722260                                                                
CONECT222682225722261                                                           
CONECT2226922262                                                                
CONECT2227022263                                                                
CONECT22271161942227222282                                                      
CONECT22272222712227322279                                                      
CONECT22273222722227422280                                                      
CONECT22274222732227522281                                                      
CONECT22275222742227622282                                                      
CONECT222762227522283                                                           
CONECT22277222782227922284                                                      
CONECT2227822277                                                                
CONECT222792227222277                                                           
CONECT2228022273                                                                
CONECT2228122274                                                                
CONECT222822227122275                                                           
CONECT2228322276                                                                
CONECT2228422277                                                                
CONECT22285179082228622296                                                      
CONECT22286222852228722293                                                      
CONECT22287222862228822294                                                      
CONECT22288222872228922295                                                      
CONECT22289222882229022296                                                      
CONECT222902228922297                                                           
CONECT22291222922229322298                                                      
CONECT2229222291                                                                
CONECT222932228622291                                                           
CONECT2229422287                                                                
CONECT2229522288                                                                
CONECT222962228522289                                                           
CONECT2229722290                                                                
CONECT2229822291                                                                
CONECT22299180062230022310                                                      
CONECT22300222992230122307                                                      
CONECT22301223002230222308                                                      
CONECT22302223012230322309                                                      
CONECT22303223022230422310                                                      
CONECT223042230322311                                                           
CONECT22305223062230722312                                                      
CONECT2230622305                                                                
CONECT223072230022305                                                           
CONECT2230822301                                                                
CONECT2230922302                                                                
CONECT223102229922303                                                           
CONECT2231122304                                                                
CONECT2231222305                                                                
CONECT22313181622231422324                                                      
CONECT22314223132231522321                                                      
CONECT22315223142231622322                                                      
CONECT22316223152231722323                                                      
CONECT22317223162231822324                                                      
CONECT223182231722325                                                           
CONECT22319223202232122326                                                      
CONECT2232022319                                                                
CONECT223212231422319                                                           
CONECT2232222315                                                                
CONECT2232322316                                                                
CONECT223242231322317                                                           
CONECT2232522318                                                                
CONECT2232622319                                                                
CONECT22327184432232822338                                                      
CONECT22328223272232922335                                                      
CONECT22329223282233022336                                                      
CONECT22330223292233122337                                                      
CONECT22331223302233222338                                                      
CONECT223322233122339                                                           
CONECT22333223342233522340                                                      
CONECT2233422333                                                                
CONECT223352232822333                                                           
CONECT2233622329                                                                
CONECT2233722330                                                                
CONECT223382232722331                                                           
CONECT2233922332                                                                
CONECT2234022333                                                                
CONECT22341209732234222352                                                      
CONECT22342223412234322349                                                      
CONECT22343223422234422350                                                      
CONECT22344223432234522351                                                      
CONECT22345223442234622352                                                      
CONECT223462234522353                                                           
CONECT22347223482234922354                                                      
CONECT2234822347                                                                
CONECT223492234222347                                                           
CONECT2235022343                                                                
CONECT2235122344                                                                
CONECT223522234122345                                                           
CONECT2235322346                                                                
CONECT2235422347                                                                
CONECT22355150592235622366                                                      
CONECT22356223552235722363                                                      
CONECT22357223562235822364                                                      
CONECT22358223572235922365                                                      
CONECT22359223582236022366                                                      
CONECT223602235922367                                                           
CONECT22361223622236322368                                                      
CONECT2236222361                                                                
CONECT223632235622361                                                           
CONECT2236422357                                                                
CONECT2236522358                                                                
CONECT223662235522359                                                           
CONECT2236722360                                                                
CONECT2236822361                                                                
MASTER     1465    0   59   66  177    0    0    622365    3  943  297          
END                                                                             
HEADER    VIRAL PROTEIN                           27-FEB-20   6VYO              
TITLE     CRYSTAL STRUCTURE OF RNA BINDING DOMAIN OF NUCLEOCAPSID PHOSPHOPROTEIN
TITLE    2 FROM SARS CORONAVIRUS 2                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NUCLEOPROTEIN;                                             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RNA BINDING DOMAIN;                                        
COMPND   5 SYNONYM: NUCLEOCAPSID PROTEIN,PROTEIN N;                             
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    CSGID, COVID-19, RNA BINDING DOMAIN, NUCLEOCAPSID PROTEIN,            
KEYWDS   2 NUCLEOPROTEIN, STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS   
KEYWDS   3 OF INFECTIOUS DISEASES, VIRAL PROTEIN                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CHANG,K.MICHALSKA,R.JEDRZEJCZAK,N.MALTSEVA,M.ENDRES,A.GODZIK,Y.KIM, 
AUTHOR   2 A.JOACHIMIAK,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES   
AUTHOR   3 (CSGID)                                                              
REVDAT   4   06-MAY-20 6VYO    1       COMPND SOURCE REMARK DBREF               
REVDAT   4 2                   1       SEQADV LINK   SITE   ATOM                
REVDAT   3   08-APR-20 6VYO    1       COMPND REMARK HET    HETNAM              
REVDAT   3 2                   1       HETSYN FORMUL LINK   SITE                
REVDAT   3 3                   1       ATOM                                     
REVDAT   2   25-MAR-20 6VYO    1       KEYWDS                                   
REVDAT   1   11-MAR-20 6VYO    0                                                
JRNL        AUTH   C.CHANG,K.MICHALSKA,R.JEDRZEJCZAK,N.MALTSEVA,M.ENDRES,       
JRNL        AUTH 2 A.GODZIK,Y.KIM,A.JOACHIMIAK                                  
JRNL        TITL   CRYSTAL STRUCTURE OF RNA BINDING DOMAIN OF NUCLEOCAPSID      
JRNL        TITL 2 PHOSPHOPROTEIN FROM SARS CORONAVIRUS 2                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.17.1_3660                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.05                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 56873                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.920                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2800                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.0500 -  4.6100    0.99     3297   179  0.1563 0.1740        
REMARK   3     2  4.6100 -  3.6600    1.00     3181   155  0.1354 0.1655        
REMARK   3     3  3.6600 -  3.2000    1.00     3166   148  0.1558 0.1923        
REMARK   3     4  3.2000 -  2.9100    1.00     3114   164  0.1670 0.2203        
REMARK   3     5  2.9100 -  2.7000    1.00     3109   166  0.1726 0.2174        
REMARK   3     6  2.7000 -  2.5400    1.00     3086   154  0.1727 0.2239        
REMARK   3     7  2.5400 -  2.4100    1.00     3115   165  0.1708 0.2219        
REMARK   3     8  2.4100 -  2.3100    0.99     3045   151  0.1643 0.2368        
REMARK   3     9  2.3100 -  2.2200    1.00     3077   152  0.1583 0.2429        
REMARK   3    10  2.2200 -  2.1400    0.99     3046   174  0.1577 0.2020        
REMARK   3    11  2.1400 -  2.0800    0.96     2954   153  0.1542 0.1996        
REMARK   3    12  2.0800 -  2.0200    0.91     2785   149  0.1547 0.2011        
REMARK   3    13  2.0200 -  1.9600    0.86     2614   141  0.1571 0.1864        
REMARK   3    14  1.9600 -  1.9100    0.82     2511   123  0.1559 0.2174        
REMARK   3    15  1.9100 -  1.8700    0.76     2352   121  0.1725 0.2086        
REMARK   3    16  1.8700 -  1.8300    0.71     2165   116  0.1792 0.3046        
REMARK   3    17  1.8300 -  1.7900    0.68     2075   100  0.1818 0.2476        
REMARK   3    18  1.7900 -  1.7600    0.63     1926   104  0.1685 0.2115        
REMARK   3    19  1.7600 -  1.7300    0.60     1848   100  0.1649 0.2585        
REMARK   3    20  1.7300 -  1.7000    0.53     1607    85  0.1505 0.2094        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.540           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6VYO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000247334.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 X 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64592                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 12.40                              
REMARK 200  R MERGE                    (I) : 0.13100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.20                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.13400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: HKL-3000                                              
REMARK 200 STARTING MODEL: 2OFZ.PDB                                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20.0% PEG6000, 0.1M MES, 10.0 MM ZINC    
REMARK 280  CHLORIDE, PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       33.11900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.01950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.71500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       57.01950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.11900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.71500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -179.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    46                                                      
REMARK 465     ASN A    47                                                      
REMARK 465     ASN A    48                                                      
REMARK 465     THR A    49                                                      
REMARK 465     GLY B    46                                                      
REMARK 465     ASN B    47                                                      
REMARK 465     ASN B    48                                                      
REMARK 465     GLY C    46                                                      
REMARK 465     ASN C    47                                                      
REMARK 465     ASN C    48                                                      
REMARK 465     GLY D    46                                                      
REMARK 465     ASN D    47                                                      
REMARK 465     ASN D    48                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A    62     O    HOH A   301              2.16            
REMARK 500   O    HOH D   312     O    HOH D   460              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  77       54.44    -91.44                                   
REMARK 500    LYS A 143       52.63   -100.40                                   
REMARK 500    LYS B 143       56.32    -99.02                                   
REMARK 500    ASN C  77       54.26    -91.23                                   
REMARK 500    LYS C 143       52.84   -100.25                                   
REMARK 500    LYS D 143       58.71    -98.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 468        DISTANCE =  6.43 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 206  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  59   NE2                                                    
REMARK 620 2 ASP B  82   OD2 106.6                                              
REMARK 620 3 HIS B 145   NE2 110.1 115.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 204  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  82   OD2                                                    
REMARK 620 2 HIS A 145   NE2 113.9                                              
REMARK 620 3 HIS D  59   ND1 105.7 110.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 203  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  59   ND1                                                    
REMARK 620 2 ASP C  82   OD2 102.9                                              
REMARK 620 3 HIS C 145   NE2 113.4 112.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 205  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  59   NE2                                                    
REMARK 620 2 ASP D  82   OD2 105.3                                              
REMARK 620 3 HIS D 145   NE2 110.8 116.9                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 205                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES C 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 205                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 202                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: CSGID-IDP51003   RELATED DB: TARGETTRACK                 
DBREF  6VYO A   47   173  UNP    P0DTC9   NCAP_SARS2      47    173             
DBREF  6VYO B   47   173  UNP    P0DTC9   NCAP_SARS2      47    173             
DBREF  6VYO C   47   173  UNP    P0DTC9   NCAP_SARS2      47    173             
DBREF  6VYO D   47   173  UNP    P0DTC9   NCAP_SARS2      47    173             
SEQADV 6VYO GLY A   46  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6VYO GLY B   46  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6VYO GLY C   46  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6VYO GLY D   46  UNP  P0DTC9              EXPRESSION TAG                 
SEQRES   1 A  128  GLY ASN ASN THR ALA SER TRP PHE THR ALA LEU THR GLN          
SEQRES   2 A  128  HIS GLY LYS GLU ASP LEU LYS PHE PRO ARG GLY GLN GLY          
SEQRES   3 A  128  VAL PRO ILE ASN THR ASN SER SER PRO ASP ASP GLN ILE          
SEQRES   4 A  128  GLY TYR TYR ARG ARG ALA THR ARG ARG ILE ARG GLY GLY          
SEQRES   5 A  128  ASP GLY LYS MET LYS ASP LEU SER PRO ARG TRP TYR PHE          
SEQRES   6 A  128  TYR TYR LEU GLY THR GLY PRO GLU ALA GLY LEU PRO TYR          
SEQRES   7 A  128  GLY ALA ASN LYS ASP GLY ILE ILE TRP VAL ALA THR GLU          
SEQRES   8 A  128  GLY ALA LEU ASN THR PRO LYS ASP HIS ILE GLY THR ARG          
SEQRES   9 A  128  ASN PRO ALA ASN ASN ALA ALA ILE VAL LEU GLN LEU PRO          
SEQRES  10 A  128  GLN GLY THR THR LEU PRO LYS GLY PHE TYR ALA                  
SEQRES   1 B  128  GLY ASN ASN THR ALA SER TRP PHE THR ALA LEU THR GLN          
SEQRES   2 B  128  HIS GLY LYS GLU ASP LEU LYS PHE PRO ARG GLY GLN GLY          
SEQRES   3 B  128  VAL PRO ILE ASN THR ASN SER SER PRO ASP ASP GLN ILE          
SEQRES   4 B  128  GLY TYR TYR ARG ARG ALA THR ARG ARG ILE ARG GLY GLY          
SEQRES   5 B  128  ASP GLY LYS MET LYS ASP LEU SER PRO ARG TRP TYR PHE          
SEQRES   6 B  128  TYR TYR LEU GLY THR GLY PRO GLU ALA GLY LEU PRO TYR          
SEQRES   7 B  128  GLY ALA ASN LYS ASP GLY ILE ILE TRP VAL ALA THR GLU          
SEQRES   8 B  128  GLY ALA LEU ASN THR PRO LYS ASP HIS ILE GLY THR ARG          
SEQRES   9 B  128  ASN PRO ALA ASN ASN ALA ALA ILE VAL LEU GLN LEU PRO          
SEQRES  10 B  128  GLN GLY THR THR LEU PRO LYS GLY PHE TYR ALA                  
SEQRES   1 C  128  GLY ASN ASN THR ALA SER TRP PHE THR ALA LEU THR GLN          
SEQRES   2 C  128  HIS GLY LYS GLU ASP LEU LYS PHE PRO ARG GLY GLN GLY          
SEQRES   3 C  128  VAL PRO ILE ASN THR ASN SER SER PRO ASP ASP GLN ILE          
SEQRES   4 C  128  GLY TYR TYR ARG ARG ALA THR ARG ARG ILE ARG GLY GLY          
SEQRES   5 C  128  ASP GLY LYS MET LYS ASP LEU SER PRO ARG TRP TYR PHE          
SEQRES   6 C  128  TYR TYR LEU GLY THR GLY PRO GLU ALA GLY LEU PRO TYR          
SEQRES   7 C  128  GLY ALA ASN LYS ASP GLY ILE ILE TRP VAL ALA THR GLU          
SEQRES   8 C  128  GLY ALA LEU ASN THR PRO LYS ASP HIS ILE GLY THR ARG          
SEQRES   9 C  128  ASN PRO ALA ASN ASN ALA ALA ILE VAL LEU GLN LEU PRO          
SEQRES  10 C  128  GLN GLY THR THR LEU PRO LYS GLY PHE TYR ALA                  
SEQRES   1 D  128  GLY ASN ASN THR ALA SER TRP PHE THR ALA LEU THR GLN          
SEQRES   2 D  128  HIS GLY LYS GLU ASP LEU LYS PHE PRO ARG GLY GLN GLY          
SEQRES   3 D  128  VAL PRO ILE ASN THR ASN SER SER PRO ASP ASP GLN ILE          
SEQRES   4 D  128  GLY TYR TYR ARG ARG ALA THR ARG ARG ILE ARG GLY GLY          
SEQRES   5 D  128  ASP GLY LYS MET LYS ASP LEU SER PRO ARG TRP TYR PHE          
SEQRES   6 D  128  TYR TYR LEU GLY THR GLY PRO GLU ALA GLY LEU PRO TYR          
SEQRES   7 D  128  GLY ALA ASN LYS ASP GLY ILE ILE TRP VAL ALA THR GLU          
SEQRES   8 D  128  GLY ALA LEU ASN THR PRO LYS ASP HIS ILE GLY THR ARG          
SEQRES   9 D  128  ASN PRO ALA ASN ASN ALA ALA ILE VAL LEU GLN LEU PRO          
SEQRES  10 D  128  GLN GLY THR THR LEU PRO LYS GLY PHE TYR ALA                  
HET    MES  A 201      12                                                       
HET     CL  A 202       1                                                       
HET    MES  A 203      12                                                       
HET     ZN  A 204       1                                                       
HET     CL  A 205       1                                                       
HET     ZN  A 206       1                                                       
HET    GOL  B 201       6                                                       
HET    MES  B 202      12                                                       
HET     ZN  B 203       1                                                       
HET     CL  C 201       1                                                       
HET     CL  C 202       1                                                       
HET    GOL  C 203       6                                                       
HET    MES  C 204      12                                                       
HET     ZN  C 205       1                                                       
HET    GOL  D 201       6                                                       
HET    GOL  D 202       6                                                       
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM      CL CHLORIDE ION                                                     
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  MES    4(C6 H13 N O4 S)                                             
FORMUL   6   CL    4(CL 1-)                                                     
FORMUL   8   ZN    4(ZN 2+)                                                     
FORMUL  11  GOL    4(C3 H8 O3)                                                  
FORMUL  21  HOH   *664(H2 O)                                                    
HELIX    1 AA1 SER A   79  ASP A   82  5                                   4    
HELIX    2 AA2 SER B   79  ASP B   82  5                                   4    
HELIX    3 AA3 SER C   79  ASP C   82  5                                   4    
HELIX    4 AA4 SER D   79  ASP D   82  5                                   4    
SHEET    1 AA1 4 LEU A  56  THR A  57  0                                        
SHEET    2 AA1 4 ARG A 107  TYR A 112 -1  O  TRP A 108   N  LEU A  56           
SHEET    3 AA1 4 ILE A  84  ALA A  90 -1  N  ALA A  90   O  ARG A 107           
SHEET    4 AA1 4 ILE A 130  ALA A 134 -1  O  VAL A 133   N  GLY A  85           
SHEET    1 AA2 2 ARG A  93  ARG A  95  0                                        
SHEET    2 AA2 2 MET A 101  ASP A 103 -1  O  LYS A 102   N  ILE A  94           
SHEET    1 AA3 5 ILE B 130  ALA B 134  0                                        
SHEET    2 AA3 5 ILE B  84  ALA B  90 -1  N  TYR B  87   O  ILE B 131           
SHEET    3 AA3 5 ARG B 107  TYR B 112 -1  O  TYR B 111   N  TYR B  86           
SHEET    4 AA3 5 LEU B  56  GLN B  58 -1  N  LEU B  56   O  TRP B 108           
SHEET    5 AA3 5 PHE B 171  TYR B 172 -1  O  TYR B 172   N  THR B  57           
SHEET    1 AA4 2 ARG B  93  ARG B  95  0                                        
SHEET    2 AA4 2 MET B 101  ASP B 103 -1  O  LYS B 102   N  ILE B  94           
SHEET    1 AA5 4 LEU C  56  THR C  57  0                                        
SHEET    2 AA5 4 ARG C 107  TYR C 112 -1  O  TRP C 108   N  LEU C  56           
SHEET    3 AA5 4 ILE C  84  ALA C  90 -1  N  ALA C  90   O  ARG C 107           
SHEET    4 AA5 4 ILE C 130  ALA C 134 -1  O  VAL C 133   N  GLY C  85           
SHEET    1 AA6 2 ARG C  93  ARG C  95  0                                        
SHEET    2 AA6 2 MET C 101  ASP C 103 -1  O  LYS C 102   N  ILE C  94           
SHEET    1 AA7 5 ILE D 130  ALA D 134  0                                        
SHEET    2 AA7 5 ILE D  84  ALA D  90 -1  N  TYR D  87   O  ILE D 131           
SHEET    3 AA7 5 ARG D 107  TYR D 112 -1  O  ARG D 107   N  ALA D  90           
SHEET    4 AA7 5 LEU D  56  GLN D  58 -1  N  LEU D  56   O  TRP D 108           
SHEET    5 AA7 5 PHE D 171  TYR D 172 -1  O  TYR D 172   N  THR D  57           
SHEET    1 AA8 2 ARG D  93  ARG D  95  0                                        
SHEET    2 AA8 2 MET D 101  ASP D 103 -1  O  LYS D 102   N  ILE D  94           
LINK         NE2 HIS A  59                ZN    ZN A 206     1555   1555  2.07  
LINK         OD2 ASP A  82                ZN    ZN A 204     1555   1555  1.99  
LINK         NE2 HIS A 145                ZN    ZN A 204     1555   1555  2.12  
LINK         ND1 HIS B  59                ZN    ZN B 203     1555   1555  2.04  
LINK         OD2 ASP B  82                ZN    ZN A 206     1555   1555  1.95  
LINK         NE2 HIS B 145                ZN    ZN A 206     1555   1555  2.09  
LINK         NE2 HIS C  59                ZN    ZN C 205     1555   1555  2.07  
LINK         OD2 ASP C  82                ZN    ZN B 203     1555   1555  1.97  
LINK         NE2 HIS C 145                ZN    ZN B 203     1555   1555  2.06  
LINK         ND1 HIS D  59                ZN    ZN A 204     1555   1555  2.00  
LINK         OD2 ASP D  82                ZN    ZN C 205     1555   1555  1.98  
LINK         NE2 HIS D 145                ZN    ZN C 205     1555   1555  2.05  
SITE     1 AC1  8 TRP A  52  ASN A  75  ASN A  77  ASN A 154                    
SITE     2 AC1  8 HOH A 303  ARG D 107  HOH D 307  HOH D 426                    
SITE     1 AC2  5 HIS A  59   ZN A 206  ASN B  77  ASP B  82                    
SITE     2 AC2  5 HIS B 145                                                     
SITE     1 AC3  8 THR A  54  ALA A  55  ARG A 107  HOH A 392                    
SITE     2 AC3  8 TRP B  52  ASN B  75  ASN B  77  ASN B 154                    
SITE     1 AC4  4 ASP A  82  HIS A 145   CL A 205  HIS D  59                    
SITE     1 AC5  5 SER A  79  ASP A  82  HIS A 145   ZN A 204                    
SITE     2 AC5  5 HIS D  59                                                     
SITE     1 AC6  4 HIS A  59   CL A 202  ASP B  82  HIS B 145                    
SITE     1 AC7  5 ASN A 140  ARG B  68  TYR B 123  HOH B 344                    
SITE     2 AC7  5 HOH B 383                                                     
SITE     1 AC8  7 ARG B  92  ARG B 107  HOH B 402  TRP C  52                    
SITE     2 AC8  7 ASN C  75  ASN C  77  ASN C 154                               
SITE     1 AC9  4 HIS B  59  ASP C  82  HIS C 145   CL C 201                    
SITE     1 AD1  5 HIS B  59   ZN B 203  SER C  79  ASP C  82                    
SITE     2 AD1  5 HIS C 145                                                     
SITE     1 AD2  5 HIS C  59   ZN C 205  ASN D  77  ASP D  82                    
SITE     2 AD2  5 HIS D 145                                                     
SITE     1 AD3  9 ASN C  75  THR C  76  SER C  78  SER C  79                    
SITE     2 AD3  9 PRO C  80  GLN C  83  HOH C 335  HOH C 371                    
SITE     3 AD3  9 ARG D  95                                                     
SITE     1 AD4 10 THR C  54  ALA C  55  ARG C 107  HOH C 305                    
SITE     2 AD4 10 HOH C 307  HOH C 374  HOH C 411  TRP D  52                    
SITE     3 AD4 10 ASN D  75  ASN D 154                                          
SITE     1 AD5  4 HIS C  59   CL C 202  ASP D  82  HIS D 145                    
SITE     1 AD6  6 ASN C 140  THR C 141  TYR D 123  TRP D 132                    
SITE     2 AD6  6 HOH D 368  HOH D 373                                          
SITE     1 AD7  4 ASN D  75  SER D  78  PRO D  80  GLN D  83                    
CRYST1   66.238   77.430  114.039  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015097  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012915  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008769        0.00000                         
ATOM      1  N   ALA A  50      -3.612   3.954  -3.007  1.00 26.73           N  
ANISOU    1  N   ALA A  50     3617   3832   2708   -591    338    -12       N  
ATOM      2  CA  ALA A  50      -4.628   3.614  -2.019  1.00 22.50           C  
ANISOU    2  CA  ALA A  50     2834   3319   2396   -339    279   -131       C  
ATOM      3  C   ALA A  50      -6.028   3.722  -2.610  1.00 18.56           C  
ANISOU    3  C   ALA A  50     2211   2662   2177   -390    432   -149       C  
ATOM      4  O   ALA A  50      -6.238   4.398  -3.616  1.00 17.90           O  
ANISOU    4  O   ALA A  50     1872   2807   2121   -381    559   -176       O  
ATOM      5  CB  ALA A  50      -4.501   4.512  -0.797  1.00 22.95           C  
ANISOU    5  CB  ALA A  50     2943   3543   2235   -189     -9    218       C  
ATOM      6  N   SER A  51      -6.982   3.045  -1.978  1.00 15.09           N  
ANISOU    6  N   SER A  51     1808   1893   2031   -648    604   -395       N  
ATOM      7  CA  SER A  51      -8.379   3.176  -2.364  1.00 14.26           C  
ANISOU    7  CA  SER A  51     2026   1585   1807   -370    468   -139       C  
ATOM      8  C   SER A  51      -8.901   4.562  -2.005  1.00 15.04           C  
ANISOU    8  C   SER A  51     2161   1884   1671     17    230    -37       C  
ATOM      9  O   SER A  51      -8.500   5.161  -1.004  1.00 16.66           O  
ANISOU    9  O   SER A  51     2379   2199   1752   -266    230    229       O  
ATOM     10  CB  SER A  51      -9.225   2.105  -1.673  1.00 13.96           C  
ANISOU   10  CB  SER A  51     1842   1760   1703   -253    304    -13       C  
ATOM     11  OG  SER A  51     -10.608   2.416  -1.735  1.00 11.93           O  
ANISOU   11  OG  SER A  51     1549   1662   1321     96    734   -321       O  
ATOM     12  N   TRP A  52      -9.807   5.074  -2.842  1.00 12.33           N  
ANISOU   12  N   TRP A  52     1426   1875   1385    -27    123    -21       N  
ATOM     13  CA  TRP A  52     -10.442   6.354  -2.551  1.00 10.58           C  
ANISOU   13  CA  TRP A  52     1629   1288   1102   -393     17    216       C  
ATOM     14  C   TRP A  52     -11.331   6.297  -1.317  1.00 12.03           C  
ANISOU   14  C   TRP A  52     1722   1699   1151   -602     36     30       C  
ATOM     15  O   TRP A  52     -11.645   7.349  -0.749  1.00 13.43           O  
ANISOU   15  O   TRP A  52     2005   1825   1273   -446    453    103       O  
ATOM     16  CB  TRP A  52     -11.270   6.826  -3.748  1.00  9.59           C  
ANISOU   16  CB  TRP A  52     1391   1037   1215   -188   -244    -74       C  
ATOM     17  CG  TRP A  52     -10.457   7.495  -4.805  1.00 10.37           C  
ANISOU   17  CG  TRP A  52     1794    937   1209   -446    -97     63       C  
ATOM     18  CD1 TRP A  52     -10.154   7.006  -6.041  1.00 10.16           C  
ANISOU   18  CD1 TRP A  52     1651   1025   1186   -363    271    471       C  
ATOM     19  CD2 TRP A  52      -9.827   8.777  -4.714  1.00 15.38           C  
ANISOU   19  CD2 TRP A  52     2683   1572   1589   -456    -17   -161       C  
ATOM     20  NE1 TRP A  52      -9.378   7.908  -6.728  1.00 13.70           N  
ANISOU   20  NE1 TRP A  52     2531   1293   1383   -723    420    115       N  
ATOM     21  CE2 TRP A  52      -9.164   9.004  -5.936  1.00 15.79           C  
ANISOU   21  CE2 TRP A  52     2598   1758   1644   -583    186     55       C  
ATOM     22  CE3 TRP A  52      -9.763   9.757  -3.719  1.00 17.84           C  
ANISOU   22  CE3 TRP A  52     3138   1791   1851   -734    -57   -294       C  
ATOM     23  CZ2 TRP A  52      -8.446  10.169  -6.190  1.00 17.62           C  
ANISOU   23  CZ2 TRP A  52     2948   1813   1933   -819     30     18       C  
ATOM     24  CZ3 TRP A  52      -9.048  10.915  -3.974  1.00 19.21           C  
ANISOU   24  CZ3 TRP A  52     3161   2092   2048   -865    106    126       C  
ATOM     25  CH2 TRP A  52      -8.396  11.107  -5.197  1.00 19.75           C  
ANISOU   25  CH2 TRP A  52     3279   2187   2038   -708    241    -72       C  
ATOM     26  N   PHE A  53     -11.735   5.106  -0.886  1.00 12.68           N  
ANISOU   26  N   PHE A  53     2103   1537   1178   -939    141    217       N  
ATOM     27  CA  PHE A  53     -12.737   4.952   0.156  1.00 11.61           C  
ANISOU   27  CA  PHE A  53     1736   1828    847   -483    226    -38       C  
ATOM     28  C   PHE A  53     -12.177   4.182   1.345  1.00 12.20           C  
ANISOU   28  C   PHE A  53     1935   1626   1073   -465    267   -100       C  
ATOM     29  O   PHE A  53     -11.204   3.430   1.230  1.00 12.51           O  
ANISOU   29  O   PHE A  53     1583   1890   1280   -116   -171    -49       O  
ATOM     30  CB  PHE A  53     -13.982   4.230  -0.383  1.00 12.02           C  
ANISOU   30  CB  PHE A  53     1873   1911    785   -139    263   -208       C  
ATOM     31  CG  PHE A  53     -14.555   4.856  -1.624  1.00 12.98           C  
ANISOU   31  CG  PHE A  53     1962   2089    883   -302    222   -120       C  
ATOM     32  CD1 PHE A  53     -15.503   5.861  -1.534  1.00 14.13           C  
ANISOU   32  CD1 PHE A  53     1934   2351   1084   -241    358     62       C  
ATOM     33  CD2 PHE A  53     -14.141   4.440  -2.882  1.00 12.59           C  
ANISOU   33  CD2 PHE A  53     1705   2065   1014   -476    217   -332       C  
ATOM     34  CE1 PHE A  53     -16.031   6.441  -2.677  1.00 14.66           C  
ANISOU   34  CE1 PHE A  53     2205   2373    992   -273    100     11       C  
ATOM     35  CE2 PHE A  53     -14.662   5.016  -4.028  1.00 11.21           C  
ANISOU   35  CE2 PHE A  53     1629   1534   1095   -399     97   -421       C  
ATOM     36  CZ  PHE A  53     -15.610   6.017  -3.926  1.00 14.45           C  
ANISOU   36  CZ  PHE A  53     2188   2071   1233   -501      8   -470       C  
ATOM     37  N   THR A  54     -12.809   4.381   2.500  1.00 12.20           N  
ANISOU   37  N   THR A  54     2316   1280   1039   -532     18   -136       N  
ATOM     38  CA  THR A  54     -12.531   3.535   3.649  1.00 12.40           C  
ANISOU   38  CA  THR A  54     2567   1143    999   -199    191   -255       C  
ATOM     39  C   THR A  54     -13.017   2.112   3.369  1.00 12.87           C  
ANISOU   39  C   THR A  54     2624   1149   1119    -40    328   -204       C  
ATOM     40  O   THR A  54     -13.774   1.857   2.428  1.00 12.95           O  
ANISOU   40  O   THR A  54     2322   1710    888     -2    419   -227       O  
ATOM     41  CB  THR A  54     -13.194   4.094   4.908  1.00 13.61           C  
ANISOU   41  CB  THR A  54     2531   1465   1177     60    -77   -423       C  
ATOM     42  OG1 THR A  54     -14.613   4.172   4.715  1.00 13.72           O  
ANISOU   42  OG1 THR A  54     2639   1233   1341     33    382   -527       O  
ATOM     43  CG2 THR A  54     -12.653   5.484   5.222  1.00 12.71           C  
ANISOU   43  CG2 THR A  54     2264   1398   1166    264    116   -646       C  
ATOM     44  N   ALA A  55     -12.577   1.178   4.201  1.00 13.08           N  
ANISOU   44  N   ALA A  55     2741   1090   1140   -153    198   -112       N  
ATOM     45  CA  ALA A  55     -12.825  -0.231   3.939  1.00 15.23           C  
ANISOU   45  CA  ALA A  55     3079   1099   1608    237    461     -3       C  
ATOM     46  C   ALA A  55     -14.150  -0.690   4.538  1.00 15.16           C  
ANISOU   46  C   ALA A  55     3142   1073   1546    280    607   -255       C  
ATOM     47  O   ALA A  55     -14.694  -0.078   5.461  1.00 18.32           O  
ANISOU   47  O   ALA A  55     3830   1561   1570    593    601   -291       O  
ATOM     48  CB  ALA A  55     -11.686  -1.087   4.493  1.00 17.74           C  
ANISOU   48  CB  ALA A  55     3017   1772   1950     61    339    195       C  
ATOM     49  N   LEU A  56     -14.671  -1.783   3.984  1.00 14.82           N  
ANISOU   49  N   LEU A  56     3061    920   1648    258    371     47       N  
ATOM     50  CA  LEU A  56     -15.746  -2.544   4.609  1.00 14.50           C  
ANISOU   50  CA  LEU A  56     2800   1335   1373    129    474     85       C  
ATOM     51  C   LEU A  56     -15.114  -3.661   5.430  1.00 15.11           C  
ANISOU   51  C   LEU A  56     2960   1299   1481     91    294    178       C  
ATOM     52  O   LEU A  56     -14.374  -4.490   4.890  1.00 17.21           O  
ANISOU   52  O   LEU A  56     2954   1791   1792   -242    674    129       O  
ATOM     53  CB  LEU A  56     -16.698  -3.121   3.561  1.00 14.24           C  
ANISOU   53  CB  LEU A  56     2227   1690   1493    871    129    -97       C  
ATOM     54  CG  LEU A  56     -17.620  -2.154   2.817  1.00 18.52           C  
ANISOU   54  CG  LEU A  56     2524   2882   1633    962   -204   -780       C  
ATOM     55  CD1 LEU A  56     -18.403  -2.882   1.732  1.00 19.19           C  
ANISOU   55  CD1 LEU A  56     2622   2759   1908    649   -248   -663       C  
ATOM     56  CD2 LEU A  56     -18.566  -1.472   3.787  1.00 21.88           C  
ANISOU   56  CD2 LEU A  56     2547   3956   1810   1540   -222   -859       C  
ATOM     57  N   THR A  57     -15.399  -3.682   6.730  1.00 14.38           N  
ANISOU   57  N   THR A  57     3228   1058   1179   -208    175    221       N  
ATOM     58  CA  THR A  57     -14.764  -4.630   7.637  1.00 15.40           C  
ANISOU   58  CA  THR A  57     3354   1186   1310   -295   -119    167       C  
ATOM     59  C   THR A  57     -15.614  -5.887   7.782  1.00 16.63           C  
ANISOU   59  C   THR A  57     3289   1608   1422   -319    247    426       C  
ATOM     60  O   THR A  57     -16.803  -5.810   8.111  1.00 15.49           O  
ANISOU   60  O   THR A  57     2604   1818   1464   -210     38    296       O  
ATOM     61  CB  THR A  57     -14.527  -3.991   9.005  1.00 15.17           C  
ANISOU   61  CB  THR A  57     3047   1329   1387   -255    -12    -11       C  
ATOM     62  OG1 THR A  57     -13.543  -2.957   8.881  1.00 17.96           O  
ANISOU   62  OG1 THR A  57     3400   1826   1596   -255    243    -45       O  
ATOM     63  CG2 THR A  57     -14.038  -5.028  10.002  1.00 16.08           C  
ANISOU   63  CG2 THR A  57     2507   1906   1697    195   -597     64       C  
ATOM     64  N   GLN A  58     -14.991  -7.041   7.545  1.00 15.77           N  
ANISOU   64  N   GLN A  58     3166   1397   1428   -282    333    520       N  
ATOM     65  CA  GLN A  58     -15.654  -8.343   7.629  1.00 15.16           C  
ANISOU   65  CA  GLN A  58     3145   1030   1584   -368    306    295       C  
ATOM     66  C   GLN A  58     -15.552  -8.853   9.063  1.00 16.21           C  
ANISOU   66  C   GLN A  58     3173   1436   1548   -299    220    445       C  
ATOM     67  O   GLN A  58     -14.508  -9.358   9.482  1.00 18.86           O  
ANISOU   67  O   GLN A  58     3306   1927   1935     51    372    720       O  
ATOM     68  CB  GLN A  58     -15.020  -9.322   6.648  1.00 17.18           C  
ANISOU   68  CB  GLN A  58     3638   1113   1775   -631     51    109       C  
ATOM     69  CG  GLN A  58     -15.556 -10.741   6.749  1.00 19.24           C  
ANISOU   69  CG  GLN A  58     3972   1283   2055   -602    307    293       C  
ATOM     70  CD  GLN A  58     -14.824 -11.710   5.839  1.00 20.05           C  
ANISOU   70  CD  GLN A  58     4373   1238   2008   -137    441    296       C  
ATOM     71  OE1 GLN A  58     -14.252 -11.317   4.821  1.00 20.65           O  
ANISOU   71  OE1 GLN A  58     4296   1549   2000    255    239    455       O  
ATOM     72  NE2 GLN A  58     -14.831 -12.985   6.207  1.00 21.90           N  
ANISOU   72  NE2 GLN A  58     4575   1641   2103   -173    327    597       N  
ATOM     73  N   HIS A  59     -16.646  -8.737   9.820  1.00 14.07           N  
ANISOU   73  N   HIS A  59     2780   1134   1432   -295    316    454       N  
ATOM     74  CA  HIS A  59     -16.627  -9.154  11.218  1.00 14.60           C  
ANISOU   74  CA  HIS A  59     3119    853   1575    -83    363    175       C  
ATOM     75  C   HIS A  59     -16.890 -10.641  11.404  1.00 18.99           C  
ANISOU   75  C   HIS A  59     3952   1427   1834   -222    104    368       C  
ATOM     76  O   HIS A  59     -16.525 -11.191  12.448  1.00 21.49           O  
ANISOU   76  O   HIS A  59     4443   1924   1798   -101   -262    317       O  
ATOM     77  CB  HIS A  59     -17.655  -8.360  12.028  1.00 11.81           C  
ANISOU   77  CB  HIS A  59     2420    659   1407    -41     43   -205       C  
ATOM     78  CG  HIS A  59     -17.313  -6.911  12.182  1.00 11.57           C  
ANISOU   78  CG  HIS A  59     1978    903   1517   -307   -182   -231       C  
ATOM     79  ND1 HIS A  59     -17.632  -5.966  11.231  1.00 13.63           N  
ANISOU   79  ND1 HIS A  59     1986   1567   1625   -487   -386   -280       N  
ATOM     80  CD2 HIS A  59     -16.678  -6.246  13.175  1.00 12.75           C  
ANISOU   80  CD2 HIS A  59     2184   1152   1507   -538   -230   -306       C  
ATOM     81  CE1 HIS A  59     -17.211  -4.780  11.634  1.00 12.58           C  
ANISOU   81  CE1 HIS A  59     1791   1444   1544   -669   -533   -274       C  
ATOM     82  NE2 HIS A  59     -16.629  -4.923  12.811  1.00 14.65           N  
ANISOU   82  NE2 HIS A  59     2385   1448   1733   -529   -201   -282       N  
ATOM     83  N   GLY A  60     -17.510 -11.301  10.428  1.00 18.48           N  
ANISOU   83  N   GLY A  60     3858   1037   2125   -312    253    130       N  
ATOM     84  CA  GLY A  60     -17.864 -12.698  10.582  1.00 19.58           C  
ANISOU   84  CA  GLY A  60     3930   1246   2264   -344    116    397       C  
ATOM     85  C   GLY A  60     -17.193 -13.617   9.582  1.00 19.80           C  
ANISOU   85  C   GLY A  60     4006   1189   2326   -417    282    329       C  
ATOM     86  O   GLY A  60     -16.155 -13.274   9.007  1.00 20.37           O  
ANISOU   86  O   GLY A  60     4020   1426   2292   -280    618    559       O  
ATOM     87  N   LYS A  61     -17.781 -14.795   9.368  1.00 21.46           N  
ANISOU   87  N   LYS A  61     4162   1441   2552   -609    409    494       N  
ATOM     88  CA  LYS A  61     -17.199 -15.778   8.463  1.00 24.41           C  
ANISOU   88  CA  LYS A  61     4594   1825   2855   -123    173    309       C  
ATOM     89  C   LYS A  61     -17.568 -15.544   7.004  1.00 23.97           C  
ANISOU   89  C   LYS A  61     4297   1963   2848   -239    206    422       C  
ATOM     90  O   LYS A  61     -16.864 -16.038   6.118  1.00 26.08           O  
ANISOU   90  O   LYS A  61     4357   2442   3111   -408     84    345       O  
ATOM     91  CB  LYS A  61     -17.630 -17.187   8.873  1.00 28.00           C  
ANISOU   91  CB  LYS A  61     5042   2406   3191    116    -42    580       C  
ATOM     92  CG  LYS A  61     -16.909 -17.731  10.094  1.00 33.13           C  
ANISOU   92  CG  LYS A  61     5509   3215   3865    308    -21    678       C  
ATOM     93  CD  LYS A  61     -17.547 -19.026  10.575  1.00 37.47           C  
ANISOU   93  CD  LYS A  61     5781   3976   4478    638   -300    800       C  
ATOM     94  CE  LYS A  61     -16.635 -19.772  11.535  1.00 41.44           C  
ANISOU   94  CE  LYS A  61     5993   4791   4961    720   -298    675       C  
ATOM     95  NZ  LYS A  61     -15.439 -20.325  10.838  1.00 44.16           N  
ANISOU   95  NZ  LYS A  61     6366   5127   5286    664   -296    554       N  
ATOM     96  N  AGLU A  62     -18.641 -14.808   6.730  0.54 23.58           N  
ANISOU   96  N  AGLU A  62     4287   1846   2826   -260    289    235       N  
ATOM     97  N  BGLU A  62     -18.647 -14.812   6.738  0.46 23.94           N  
ANISOU   97  N  BGLU A  62     4172   2040   2884   -295    240    274       N  
ATOM     98  CA AGLU A  62     -19.099 -14.624   5.359  0.54 23.79           C  
ANISOU   98  CA AGLU A  62     4175   1951   2912   -375    146    152       C  
ATOM     99  CA BGLU A  62     -19.095 -14.602   5.367  0.46 24.41           C  
ANISOU   99  CA BGLU A  62     3990   2270   3014   -441     86    186       C  
ATOM    100  C  AGLU A  62     -18.229 -13.608   4.630  0.54 22.18           C  
ANISOU  100  C  AGLU A  62     4031   1558   2839   -200    147    244       C  
ATOM    101  C  BGLU A  62     -18.185 -13.616   4.647  0.46 22.63           C  
ANISOU  101  C  BGLU A  62     3934   1748   2915   -301    145    237       C  
ATOM    102  O  AGLU A  62     -17.975 -12.511   5.139  0.54 20.92           O  
ANISOU  102  O  AGLU A  62     3784   1381   2785   -125    108    344       O  
ATOM    103  O  BGLU A  62     -17.862 -12.548   5.177  0.46 21.62           O  
ANISOU  103  O  BGLU A  62     3688   1630   2897   -330    127    271       O  
ATOM    104  CB AGLU A  62     -20.561 -14.180   5.340  0.54 26.53           C  
ANISOU  104  CB AGLU A  62     4431   2557   3094   -452    203    225       C  
ATOM    105  CB BGLU A  62     -20.537 -14.094   5.353  0.46 27.49           C  
ANISOU  105  CB BGLU A  62     4064   3113   3269   -537     31    240       C  
ATOM    106  CG AGLU A  62     -21.519 -15.208   5.918  0.54 29.60           C  
ANISOU  106  CG AGLU A  62     4900   2980   3367   -376    303    469       C  
ATOM    107  CG BGLU A  62     -21.590 -15.146   5.687  0.46 31.33           C  
ANISOU  107  CG BGLU A  62     4326   3941   3636   -471      2    424       C  
ATOM    108  CD AGLU A  62     -22.971 -14.872   5.647  0.54 31.49           C  
ANISOU  108  CD AGLU A  62     5273   3210   3483   -529    337    612       C  
ATOM    109  CD BGLU A  62     -21.696 -15.441   7.174  0.46 33.87           C  
ANISOU  109  CD BGLU A  62     4484   4530   3854   -650   -115    532       C  
ATOM    110  OE1AGLU A  62     -23.230 -13.853   4.972  0.54 31.53           O  
ANISOU  110  OE1AGLU A  62     5613   3090   3278   -677    379    862       O  
ATOM    111  OE1BGLU A  62     -20.821 -14.994   7.944  0.46 34.66           O  
ANISOU  111  OE1BGLU A  62     4367   4842   3962   -721    -62    665       O  
ATOM    112  OE2AGLU A  62     -23.854 -15.627   6.108  0.54 32.75           O  
ANISOU  112  OE2AGLU A  62     5383   3375   3684   -629    320    524       O  
ATOM    113  OE2BGLU A  62     -22.664 -16.122   7.575  0.46 34.99           O  
ANISOU  113  OE2BGLU A  62     4595   4693   4007   -837   -208    565       O  
ATOM    114  N   ASP A  63     -17.773 -13.978   3.436  1.00 21.68           N  
ANISOU  114  N   ASP A  63     3947   1413   2879   -288    309    325       N  
ATOM    115  CA  ASP A  63     -16.998 -13.072   2.606  1.00 21.57           C  
ANISOU  115  CA  ASP A  63     3476   1729   2992    196    399   -111       C  
ATOM    116  C   ASP A  63     -17.892 -11.965   2.056  1.00 17.92           C  
ANISOU  116  C   ASP A  63     2828   1369   2613     67    475   -326       C  
ATOM    117  O   ASP A  63     -19.123 -12.057   2.066  1.00 17.96           O  
ANISOU  117  O   ASP A  63     2710   1416   2696   -155    150   -304       O  
ATOM    118  CB  ASP A  63     -16.341 -13.822   1.445  1.00 25.31           C  
ANISOU  118  CB  ASP A  63     4176   1947   3495    796    382   -382       C  
ATOM    119  CG  ASP A  63     -15.254 -14.776   1.899  1.00 29.50           C  
ANISOU  119  CG  ASP A  63     4723   2516   3971   1085    393   -287       C  
ATOM    120  OD1 ASP A  63     -14.979 -14.840   3.115  1.00 32.15           O  
ANISOU  120  OD1 ASP A  63     5110   2871   4233   1239    265    -32       O  
ATOM    121  OD2 ASP A  63     -14.673 -15.462   1.033  1.00 32.01           O  
ANISOU  121  OD2 ASP A  63     4948   2841   4373    936    397   -198       O  
ATOM    122  N   LEU A  64     -17.256 -10.908   1.563  1.00 16.79           N  
ANISOU  122  N   LEU A  64     2620   1473   2286    197    133   -349       N  
ATOM    123  CA  LEU A  64     -18.006  -9.821   0.954  1.00 15.40           C  
ANISOU  123  CA  LEU A  64     2356   1408   2089    108     41   -259       C  
ATOM    124  C   LEU A  64     -18.547 -10.246  -0.405  1.00 15.55           C  
ANISOU  124  C   LEU A  64     2283   1585   2040     98    325   -232       C  
ATOM    125  O   LEU A  64     -17.860 -10.910  -1.186  1.00 16.46           O  
ANISOU  125  O   LEU A  64     2331   1621   2301   -201    162   -120       O  
ATOM    126  CB  LEU A  64     -17.127  -8.580   0.802  1.00 14.19           C  
ANISOU  126  CB  LEU A  64     2128   1503   1761      4     13     15       C  
ATOM    127  CG  LEU A  64     -17.838  -7.350   0.234  1.00 12.35           C  
ANISOU  127  CG  LEU A  64     1804   1278   1611    373    159    256       C  
ATOM    128  CD1 LEU A  64     -18.975  -6.919   1.150  1.00 13.98           C  
ANISOU  128  CD1 LEU A  64     2263   1386   1664    611    147     45       C  
ATOM    129  CD2 LEU A  64     -16.863  -6.204   0.014  1.00 13.87           C  
ANISOU  129  CD2 LEU A  64     2039   1589   1641   -306   -114    431       C  
ATOM    130  N   LYS A  65     -19.795  -9.874  -0.673  1.00 16.59           N  
ANISOU  130  N   LYS A  65     2553   1606   2146   -341    442   -232       N  
ATOM    131  CA  LYS A  65     -20.393 -10.020  -1.993  1.00 18.94           C  
ANISOU  131  CA  LYS A  65     2923   1648   2624   -800    312   -235       C  
ATOM    132  C   LYS A  65     -21.655  -9.172  -2.029  1.00 18.72           C  
ANISOU  132  C   LYS A  65     2752   1991   2371   -520    315    -25       C  
ATOM    133  O   LYS A  65     -22.211  -8.813  -0.986  1.00 19.30           O  
ANISOU  133  O   LYS A  65     2854   2127   2351   -319    278    -82       O  
ATOM    134  CB  LYS A  65     -20.707 -11.483  -2.328  1.00 24.75           C  
ANISOU  134  CB  LYS A  65     3866   2194   3342   -808    364   -217       C  
ATOM    135  CG  LYS A  65     -22.007 -12.002  -1.749  1.00 29.16           C  
ANISOU  135  CG  LYS A  65     4457   2664   3957  -1129    438   -391       C  
ATOM    136  CD  LYS A  65     -22.294 -13.409  -2.256  1.00 34.70           C  
ANISOU  136  CD  LYS A  65     5069   3697   4417  -1192    432   -434       C  
ATOM    137  CE  LYS A  65     -23.711 -13.847  -1.916  1.00 39.74           C  
ANISOU  137  CE  LYS A  65     5675   4714   4710   -850    530   -267       C  
ATOM    138  NZ  LYS A  65     -23.965 -13.835  -0.449  1.00 42.61           N  
ANISOU  138  NZ  LYS A  65     5977   5339   4873   -722    640     68       N  
ATOM    139  N   PHE A  66     -22.091  -8.843  -3.240  1.00 16.66           N  
ANISOU  139  N   PHE A  66     2612   1682   2035   -292     49    -23       N  
ATOM    140  CA  PHE A  66     -23.267  -8.014  -3.450  1.00 16.50           C  
ANISOU  140  CA  PHE A  66     2662   1668   1938   -347     38    -68       C  
ATOM    141  C   PHE A  66     -24.126  -8.617  -4.548  1.00 18.41           C  
ANISOU  141  C   PHE A  66     3038   1908   2050   -243    -38   -407       C  
ATOM    142  O   PHE A  66     -23.600  -9.218  -5.493  1.00 19.48           O  
ANISOU  142  O   PHE A  66     3329   2027   2046   -141    172   -370       O  
ATOM    143  CB  PHE A  66     -22.898  -6.576  -3.851  1.00 14.32           C  
ANISOU  143  CB  PHE A  66     2323   1437   1680   -394    311    -78       C  
ATOM    144  CG  PHE A  66     -22.258  -5.777  -2.756  1.00 13.53           C  
ANISOU  144  CG  PHE A  66     2230   1456   1454   -392    174   -150       C  
ATOM    145  CD1 PHE A  66     -23.034  -5.114  -1.819  1.00 14.62           C  
ANISOU  145  CD1 PHE A  66     2305   1577   1672    -31   -200    -17       C  
ATOM    146  CD2 PHE A  66     -20.880  -5.668  -2.676  1.00 13.26           C  
ANISOU  146  CD2 PHE A  66     1979   1693   1367   -272    263     37       C  
ATOM    147  CE1 PHE A  66     -22.447  -4.367  -0.817  1.00 14.06           C  
ANISOU  147  CE1 PHE A  66     2035   1644   1662   -192   -510      8       C  
ATOM    148  CE2 PHE A  66     -20.285  -4.923  -1.678  1.00 12.08           C  
ANISOU  148  CE2 PHE A  66     1893   1515   1183   -248    162   -105       C  
ATOM    149  CZ  PHE A  66     -21.068  -4.272  -0.745  1.00 14.23           C  
ANISOU  149  CZ  PHE A  66     2154   1433   1819    101    -25    -56       C  
ATOM    150  N   PRO A  67     -25.446  -8.467  -4.456  1.00 18.39           N  
ANISOU  150  N   PRO A  67     2731   2149   2109   -503   -268   -428       N  
ATOM    151  CA  PRO A  67     -26.303  -8.810  -5.594  1.00 20.11           C  
ANISOU  151  CA  PRO A  67     2866   2430   2344   -770   -349   -485       C  
ATOM    152  C   PRO A  67     -25.965  -7.932  -6.789  1.00 19.61           C  
ANISOU  152  C   PRO A  67     2740   2468   2243  -1098   -610   -615       C  
ATOM    153  O   PRO A  67     -25.411  -6.839  -6.651  1.00 18.24           O  
ANISOU  153  O   PRO A  67     2094   2466   2369   -883   -772   -564       O  
ATOM    154  CB  PRO A  67     -27.721  -8.531  -5.076  1.00 20.77           C  
ANISOU  154  CB  PRO A  67     2681   2821   2391   -646   -381   -296       C  
ATOM    155  CG  PRO A  67     -27.593  -8.479  -3.578  1.00 22.31           C  
ANISOU  155  CG  PRO A  67     3002   2849   2624   -541   -218   -324       C  
ATOM    156  CD  PRO A  67     -26.217  -7.966  -3.306  1.00 20.44           C  
ANISOU  156  CD  PRO A  67     3079   2272   2415   -501   -271   -486       C  
ATOM    157  N   ARG A  68     -26.297  -8.428  -7.979  1.00 21.78           N  
ANISOU  157  N   ARG A  68     3210   2632   2433  -1119   -263   -693       N  
ATOM    158  CA  ARG A  68     -26.011  -7.677  -9.195  1.00 24.66           C  
ANISOU  158  CA  ARG A  68     3606   3042   2722   -891   -531   -655       C  
ATOM    159  C   ARG A  68     -26.693  -6.315  -9.148  1.00 21.68           C  
ANISOU  159  C   ARG A  68     2578   3160   2498  -1055   -392   -399       C  
ATOM    160  O   ARG A  68     -27.894  -6.215  -8.882  1.00 20.84           O  
ANISOU  160  O   ARG A  68     1775   3605   2538   -919   -175   -221       O  
ATOM    161  CB  ARG A  68     -26.464  -8.459 -10.431  1.00 30.61           C  
ANISOU  161  CB  ARG A  68     4633   3647   3351   -867   -733   -826       C  
ATOM    162  CG  ARG A  68     -26.269  -7.693 -11.733  1.00 36.97           C  
ANISOU  162  CG  ARG A  68     5558   4413   4075   -788   -454  -1251       C  
ATOM    163  CD  ARG A  68     -26.669  -8.504 -12.957  1.00 44.55           C  
ANISOU  163  CD  ARG A  68     6503   5596   4828   -162   -153  -1169       C  
ATOM    164  NE  ARG A  68     -25.656  -9.487 -13.330  1.00 50.84           N  
ANISOU  164  NE  ARG A  68     7257   6637   5424      0    -76   -940       N  
ATOM    165  CZ  ARG A  68     -25.615 -10.106 -14.507  1.00 55.40           C  
ANISOU  165  CZ  ARG A  68     7677   7458   5916    210   -276   -474       C  
ATOM    166  NH1 ARG A  68     -24.657 -10.987 -14.765  1.00 56.14           N  
ANISOU  166  NH1 ARG A  68     7689   7574   6069    409   -354   -288       N  
ATOM    167  NH2 ARG A  68     -26.529  -9.838 -15.430  1.00 57.13           N  
ANISOU  167  NH2 ARG A  68     7823   7781   6103    306   -313   -227       N  
ATOM    168  N   GLY A  69     -25.913  -5.262  -9.385  1.00 19.24           N  
ANISOU  168  N   GLY A  69     2334   2612   2363  -1072   -224   -518       N  
ATOM    169  CA  GLY A  69     -26.412  -3.905  -9.362  1.00 17.65           C  
ANISOU  169  CA  GLY A  69     1954   2516   2236   -716    145   -220       C  
ATOM    170  C   GLY A  69     -26.090  -3.127  -8.103  1.00 15.21           C  
ANISOU  170  C   GLY A  69     1285   2550   1945   -382    -37   -193       C  
ATOM    171  O   GLY A  69     -26.251  -1.901  -8.098  1.00 17.20           O  
ANISOU  171  O   GLY A  69     1544   3013   1980    -46   -201    157       O  
ATOM    172  N   GLN A  70     -25.639  -3.794  -7.046  1.00 13.16           N  
ANISOU  172  N   GLN A  70      780   2378   1842   -480    150   -116       N  
ATOM    173  CA  GLN A  70     -25.354  -3.158  -5.768  1.00 11.76           C  
ANISOU  173  CA  GLN A  70     1034   2019   1416   -733    248   -300       C  
ATOM    174  C   GLN A  70     -23.857  -3.180  -5.480  1.00 14.12           C  
ANISOU  174  C   GLN A  70     2116   1900   1348  -1073    219    -22       C  
ATOM    175  O   GLN A  70     -23.081  -3.893  -6.122  1.00 14.92           O  
ANISOU  175  O   GLN A  70     2426   1997   1245   -922    447   -229       O  
ATOM    176  CB  GLN A  70     -26.114  -3.856  -4.632  1.00 13.05           C  
ANISOU  176  CB  GLN A  70      994   2137   1826   -697   -141   -216       C  
ATOM    177  CG  GLN A  70     -27.623  -3.908  -4.817  1.00 16.39           C  
ANISOU  177  CG  GLN A  70     1178   3048   2001   -750   -274   -174       C  
ATOM    178  CD  GLN A  70     -28.336  -4.556  -3.642  1.00 19.27           C  
ANISOU  178  CD  GLN A  70     1522   3566   2234   -582   -481     90       C  
ATOM    179  OE1 GLN A  70     -27.776  -4.686  -2.551  1.00 19.62           O  
ANISOU  179  OE1 GLN A  70     1777   3619   2058   -421   -260    334       O  
ATOM    180  NE2 GLN A  70     -29.577  -4.970  -3.862  1.00 21.70           N  
ANISOU  180  NE2 GLN A  70     1803   4073   2368   -208   -363    291       N  
ATOM    181  N   GLY A  71     -23.452  -2.374  -4.499  1.00 14.31           N  
ANISOU  181  N   GLY A  71     2061   1840   1535  -1120    283      0       N  
ATOM    182  CA  GLY A  71     -22.131  -2.454  -3.912  1.00 13.42           C  
ANISOU  182  CA  GLY A  71     1844   1726   1527   -821    260    -27       C  
ATOM    183  C   GLY A  71     -21.190  -1.317  -4.257  1.00 11.71           C  
ANISOU  183  C   GLY A  71     1888   1214   1346   -524    237   -251       C  
ATOM    184  O   GLY A  71     -20.158  -1.170  -3.590  1.00 12.71           O  
ANISOU  184  O   GLY A  71     1560   1984   1285   -182    -25   -265       O  
ATOM    185  N   VAL A  72     -21.491  -0.521  -5.274  1.00 13.36           N  
ANISOU  185  N   VAL A  72     2340   1297   1440   -306    199   -377       N  
ATOM    186  CA  VAL A  72     -20.579   0.558  -5.664  1.00 10.54           C  
ANISOU  186  CA  VAL A  72     1661    995   1350    -35    571    102       C  
ATOM    187  C   VAL A  72     -20.699   1.699  -4.657  1.00 11.46           C  
ANISOU  187  C   VAL A  72     1480   1495   1378   -219    519    -81       C  
ATOM    188  O   VAL A  72     -21.819   2.164  -4.391  1.00 13.67           O  
ANISOU  188  O   VAL A  72     1924   1847   1421   -291    805   -366       O  
ATOM    189  CB  VAL A  72     -20.881   1.039  -7.079  1.00 10.48           C  
ANISOU  189  CB  VAL A  72     1697    847   1438      8    617      1       C  
ATOM    190  CG1 VAL A  72     -19.997   2.228  -7.426  1.00  9.82           C  
ANISOU  190  CG1 VAL A  72     1308   1066   1358    500    721    453       C  
ATOM    191  CG2 VAL A  72     -20.679  -0.092  -8.077  1.00 11.30           C  
ANISOU  191  CG2 VAL A  72     1664    995   1636    184    486   -363       C  
ATOM    192  N   PRO A  73     -19.590   2.170  -4.083  1.00 11.56           N  
ANISOU  192  N   PRO A  73     1461   1247   1683     32    191   -217       N  
ATOM    193  CA  PRO A  73     -19.666   3.275  -3.118  1.00 12.56           C  
ANISOU  193  CA  PRO A  73     1606   1555   1609   -156    -59   -237       C  
ATOM    194  C   PRO A  73     -20.215   4.549  -3.745  1.00 11.80           C  
ANISOU  194  C   PRO A  73     1570   1376   1537   -316    525   -332       C  
ATOM    195  O   PRO A  73     -20.058   4.802  -4.941  1.00 13.74           O  
ANISOU  195  O   PRO A  73     1884   1823   1515     31    530   -277       O  
ATOM    196  CB  PRO A  73     -18.208   3.461  -2.678  1.00 14.04           C  
ANISOU  196  CB  PRO A  73     2246   1395   1695   -297     90   -238       C  
ATOM    197  CG  PRO A  73     -17.542   2.161  -2.982  1.00 12.85           C  
ANISOU  197  CG  PRO A  73     2083   1063   1735    -79    208   -732       C  
ATOM    198  CD  PRO A  73     -18.224   1.637  -4.213  1.00 11.92           C  
ANISOU  198  CD  PRO A  73     1643   1183   1704   -380     99   -542       C  
ATOM    199  N   ILE A  74     -20.864   5.360  -2.910  1.00 11.86           N  
ANISOU  199  N   ILE A  74     1605   1156   1745   -271    719   -172       N  
ATOM    200  CA  ILE A  74     -21.398   6.639  -3.360  1.00 12.21           C  
ANISOU  200  CA  ILE A  74     1445   1232   1962   -128    914   -179       C  
ATOM    201  C   ILE A  74     -20.253   7.618  -3.573  1.00 13.31           C  
ANISOU  201  C   ILE A  74     2035   1171   1853   -303    605     36       C  
ATOM    202  O   ILE A  74     -19.400   7.800  -2.694  1.00 16.09           O  
ANISOU  202  O   ILE A  74     2561   1632   1921   -245    645    155       O  
ATOM    203  CB  ILE A  74     -22.413   7.183  -2.344  1.00 13.04           C  
ANISOU  203  CB  ILE A  74     1712    964   2279   -116   1059   -301       C  
ATOM    204  CG1 ILE A  74     -23.610   6.237  -2.234  1.00 15.28           C  
ANISOU  204  CG1 ILE A  74     1806   1660   2342    -77   1160   -401       C  
ATOM    205  CG2 ILE A  74     -22.859   8.586  -2.731  1.00 14.14           C  
ANISOU  205  CG2 ILE A  74     1799   1066   2507   -365   1053   -453       C  
ATOM    206  CD1 ILE A  74     -24.587   6.615  -1.146  1.00 17.12           C  
ANISOU  206  CD1 ILE A  74     1753   2246   2504      8   1212   -156       C  
ATOM    207  N   ASN A  75     -20.227   8.251  -4.746  1.00 11.45           N  
ANISOU  207  N   ASN A  75     1701   1198   1452     98    650   -124       N  
ATOM    208  CA  ASN A  75     -19.211   9.252  -5.066  1.00 11.98           C  
ANISOU  208  CA  ASN A  75     1777   1127   1647     -5    673   -160       C  
ATOM    209  C   ASN A  75     -19.843  10.273  -6.002  1.00 13.36           C  
ANISOU  209  C   ASN A  75     2044   1174   1858   -274   1070   -186       C  
ATOM    210  O   ASN A  75     -20.049   9.984  -7.184  1.00 15.03           O  
ANISOU  210  O   ASN A  75     2129   1602   1980    146    961   -191       O  
ATOM    211  CB  ASN A  75     -17.981   8.605  -5.700  1.00 12.21           C  
ANISOU  211  CB  ASN A  75     2053   1109   1477   -235    442   -331       C  
ATOM    212  CG  ASN A  75     -16.911   9.617  -6.080  1.00 13.85           C  
ANISOU  212  CG  ASN A  75     2635   1331   1296    -51    552   -326       C  
ATOM    213  OD1 ASN A  75     -16.983  10.791  -5.712  1.00 15.87           O  
ANISOU  213  OD1 ASN A  75     3196   1630   1206    281    356   -282       O  
ATOM    214  ND2 ASN A  75     -15.906   9.160  -6.815  1.00 14.12           N  
ANISOU  214  ND2 ASN A  75     2295   1599   1470    -24    615    -95       N  
ATOM    215  N   THR A  76     -20.147  11.464  -5.476  1.00 14.24           N  
ANISOU  215  N   THR A  76     2195   1230   1984   -335   1184    -92       N  
ATOM    216  CA  THR A  76     -20.770  12.495  -6.298  1.00 14.14           C  
ANISOU  216  CA  THR A  76     1945   1429   1999    115   1012   -409       C  
ATOM    217  C   THR A  76     -19.852  12.982  -7.413  1.00 12.73           C  
ANISOU  217  C   THR A  76     1794   1247   1796    212    744   -330       C  
ATOM    218  O   THR A  76     -20.345  13.504  -8.420  1.00 13.83           O  
ANISOU  218  O   THR A  76     1873   1777   1605    124    814   -432       O  
ATOM    219  CB  THR A  76     -21.212  13.678  -5.429  1.00 16.18           C  
ANISOU  219  CB  THR A  76     2070   1975   2102    316    891   -691       C  
ATOM    220  OG1 THR A  76     -20.074  14.249  -4.770  1.00 19.18           O  
ANISOU  220  OG1 THR A  76     2911   2252   2123    158    762   -939       O  
ATOM    221  CG2 THR A  76     -22.222  13.226  -4.385  1.00 17.58           C  
ANISOU  221  CG2 THR A  76     2009   2495   2175    620    973   -459       C  
ATOM    222  N   ASN A  77     -18.541  12.819  -7.267  1.00 11.85           N  
ANISOU  222  N   ASN A  77     1690   1121   1693    443    664   -223       N  
ATOM    223  CA  ASN A  77     -17.604  13.209  -8.318  1.00 13.50           C  
ANISOU  223  CA  ASN A  77     1695   1547   1885    310    705   -330       C  
ATOM    224  C   ASN A  77     -17.323  12.043  -9.263  1.00 13.24           C  
ANISOU  224  C   ASN A  77     1668   1452   1910   -255    675   -665       C  
ATOM    225  O   ASN A  77     -16.182  11.651  -9.500  1.00 12.83           O  
ANISOU  225  O   ASN A  77     1927   1415   1531   -642    925   -389       O  
ATOM    226  CB  ASN A  77     -16.320  13.752  -7.702  1.00 14.36           C  
ANISOU  226  CB  ASN A  77     1833   1830   1795   -513    289   -164       C  
ATOM    227  CG  ASN A  77     -15.427  14.437  -8.724  1.00 16.36           C  
ANISOU  227  CG  ASN A  77     2408   2054   1754   -842    -72    268       C  
ATOM    228  OD1 ASN A  77     -15.775  14.534  -9.902  1.00 16.19           O  
ANISOU  228  OD1 ASN A  77     2031   2295   1828   -857   -141    362       O  
ATOM    229  ND2 ASN A  77     -14.274  14.920  -8.276  1.00 17.84           N  
ANISOU  229  ND2 ASN A  77     2997   2140   1641   -702   -221    173       N  
ATOM    230  N   SER A  78     -18.391  11.474  -9.812  1.00 12.55           N  
ANISOU  230  N   SER A  78     1478   1355   1935   -221    413   -903       N  
ATOM    231  CA  SER A  78     -18.267  10.393 -10.777  1.00 13.64           C  
ANISOU  231  CA  SER A  78     1324   1741   2120    -32    505   -728       C  
ATOM    232  C   SER A  78     -19.556  10.321 -11.581  1.00 15.36           C  
ANISOU  232  C   SER A  78     1637   1949   2249    132    543   -578       C  
ATOM    233  O   SER A  78     -20.626  10.696 -11.096  1.00 14.60           O  
ANISOU  233  O   SER A  78     1481   1843   2225    496    765   -368       O  
ATOM    234  CB  SER A  78     -17.971   9.051 -10.093  1.00 12.97           C  
ANISOU  234  CB  SER A  78     1114   1898   1918   -212    714   -559       C  
ATOM    235  OG  SER A  78     -19.014   8.671  -9.210  1.00 15.39           O  
ANISOU  235  OG  SER A  78     2121   1842   1884    285    473   -530       O  
ATOM    236  N   SER A  79     -19.438   9.846 -12.815  1.00 14.56           N  
ANISOU  236  N   SER A  79     1804   1769   1959    570    351   -564       N  
ATOM    237  CA  SER A  79     -20.562   9.751 -13.731  1.00 15.11           C  
ANISOU  237  CA  SER A  79     1853   1741   2148    343    138   -411       C  
ATOM    238  C   SER A  79     -21.220   8.383 -13.627  1.00 15.00           C  
ANISOU  238  C   SER A  79     1762   1869   2070    -79    262   -375       C  
ATOM    239  O   SER A  79     -20.644   7.446 -13.066  1.00 13.75           O  
ANISOU  239  O   SER A  79     1992   1460   1771    222    337   -670       O  
ATOM    240  CB  SER A  79     -20.087   9.990 -15.162  1.00 14.93           C  
ANISOU  240  CB  SER A  79     1947   1672   2054    353    211   -208       C  
ATOM    241  OG  SER A  79     -19.367   8.869 -15.642  1.00 16.88           O  
ANISOU  241  OG  SER A  79     2539   1584   2293   -317    151   -453       O  
ATOM    242  N   PRO A  80     -22.442   8.232 -14.149  1.00 13.91           N  
ANISOU  242  N   PRO A  80     1199   1766   2318   -125     88   -184       N  
ATOM    243  CA  PRO A  80     -23.032   6.886 -14.217  1.00 14.51           C  
ANISOU  243  CA  PRO A  80     1505   1550   2460    224   -161   -333       C  
ATOM    244  C   PRO A  80     -22.161   5.887 -14.959  1.00 14.93           C  
ANISOU  244  C   PRO A  80     1535   1914   2226    -56    263   -380       C  
ATOM    245  O   PRO A  80     -22.181   4.695 -14.625  1.00 14.43           O  
ANISOU  245  O   PRO A  80     1716   1621   2145   -334    465   -536       O  
ATOM    246  CB  PRO A  80     -24.365   7.127 -14.938  1.00 14.81           C  
ANISOU  246  CB  PRO A  80     1402   1391   2834    614   -151   -228       C  
ATOM    247  CG  PRO A  80     -24.715   8.538 -14.591  1.00 16.15           C  
ANISOU  247  CG  PRO A  80     1560   1762   2816    146   -352   -191       C  
ATOM    248  CD  PRO A  80     -23.406   9.277 -14.540  1.00 15.69           C  
ANISOU  248  CD  PRO A  80     1378   1873   2709   -144    -25   -209       C  
ATOM    249  N   ASP A  81     -21.384   6.341 -15.950  1.00 14.31           N  
ANISOU  249  N   ASP A  81     1405   2249   1782    -33     75   -251       N  
ATOM    250  CA  ASP A  81     -20.468   5.448 -16.654  1.00 14.16           C  
ANISOU  250  CA  ASP A  81     1987   1679   1712    153   -214   -378       C  
ATOM    251  C   ASP A  81     -19.414   4.862 -15.721  1.00 13.14           C  
ANISOU  251  C   ASP A  81     2283   1043   1667    142   -325   -106       C  
ATOM    252  O   ASP A  81     -18.886   3.774 -15.987  1.00 11.14           O  
ANISOU  252  O   ASP A  81     1647    864   1720   -295   -234   -375       O  
ATOM    253  CB  ASP A  81     -19.774   6.195 -17.796  1.00 15.56           C  
ANISOU  253  CB  ASP A  81     2447   1833   1632    215   -208     -4       C  
ATOM    254  CG  ASP A  81     -20.735   6.646 -18.882  1.00 21.23           C  
ANISOU  254  CG  ASP A  81     3799   2314   1953     56      6    194       C  
ATOM    255  OD1 ASP A  81     -21.906   6.212 -18.882  1.00 25.14           O  
ANISOU  255  OD1 ASP A  81     4270   2944   2337    189     23   -126       O  
ATOM    256  OD2 ASP A  81     -20.306   7.443 -19.743  1.00 23.76           O  
ANISOU  256  OD2 ASP A  81     4835   2314   1880    383   -444    236       O  
ATOM    257  N   ASP A  82     -19.097   5.560 -14.629  1.00 11.59           N  
ANISOU  257  N   ASP A  82     2202    815   1385   -338   -490    -80       N  
ATOM    258  CA  ASP A  82     -17.970   5.215 -13.771  1.00 12.79           C  
ANISOU  258  CA  ASP A  82     2228   1091   1542   -123   -431     77       C  
ATOM    259  C   ASP A  82     -18.293   4.179 -12.701  1.00 11.28           C  
ANISOU  259  C   ASP A  82     1822    998   1468   -334    163     78       C  
ATOM    260  O   ASP A  82     -17.373   3.726 -12.013  1.00 11.19           O  
ANISOU  260  O   ASP A  82     1390   1258   1605    176    348   -502       O  
ATOM    261  CB  ASP A  82     -17.435   6.469 -13.069  1.00 12.39           C  
ANISOU  261  CB  ASP A  82     2240    891   1576   -602   -155    236       C  
ATOM    262  CG  ASP A  82     -16.805   7.461 -14.027  1.00 13.37           C  
ANISOU  262  CG  ASP A  82     2343    930   1809   -376   -108    -19       C  
ATOM    263  OD1 ASP A  82     -16.331   7.045 -15.103  1.00 15.55           O  
ANISOU  263  OD1 ASP A  82     2370   1549   1989   -397    516   -440       O  
ATOM    264  OD2 ASP A  82     -16.775   8.662 -13.688  1.00 12.91           O  
ANISOU  264  OD2 ASP A  82     2368    891   1646   -435   -278     68       O  
ATOM    265  N   GLN A  83     -19.559   3.790 -12.540  1.00 11.68           N  
ANISOU  265  N   GLN A  83     1847   1161   1432   -671      2   -226       N  
ATOM    266  CA  GLN A  83     -20.000   3.068 -11.342  1.00 11.45           C  
ANISOU  266  CA  GLN A  83     1940    792   1620   -579    107    -15       C  
ATOM    267  C   GLN A  83     -19.743   1.565 -11.483  1.00 10.38           C  
ANISOU  267  C   GLN A  83     1649    844   1451    191    123   -153       C  
ATOM    268  O   GLN A  83     -20.659   0.745 -11.562  1.00 11.04           O  
ANISOU  268  O   GLN A  83     1642    967   1585    274    412   -260       O  
ATOM    269  CB  GLN A  83     -21.472   3.352 -11.078  1.00 12.33           C  
ANISOU  269  CB  GLN A  83     2096    900   1689   -608     58    -21       C  
ATOM    270  CG  GLN A  83     -21.809   4.826 -11.026  1.00 14.30           C  
ANISOU  270  CG  GLN A  83     2425   1250   1759   -333    216   -476       C  
ATOM    271  CD  GLN A  83     -20.977   5.559 -10.000  1.00 14.97           C  
ANISOU  271  CD  GLN A  83     2551   1431   1705     73     98   -598       C  
ATOM    272  OE1 GLN A  83     -20.939   5.176  -8.831  1.00 16.50           O  
ANISOU  272  OE1 GLN A  83     2916   1665   1688    632     96   -524       O  
ATOM    273  NE2 GLN A  83     -20.290   6.610 -10.433  1.00 14.14           N  
ANISOU  273  NE2 GLN A  83     2237   1293   1842   -305    102   -512       N  
ATOM    274  N   ILE A  84     -18.463   1.204 -11.475  1.00  9.78           N  
ANISOU  274  N   ILE A  84     1642    855   1220     56     76   -425       N  
ATOM    275  CA  ILE A  84     -18.073  -0.188 -11.684  1.00  8.95           C  
ANISOU  275  CA  ILE A  84     1252    967   1182   -210     72   -542       C  
ATOM    276  C   ILE A  84     -16.658  -0.379 -11.154  1.00 10.97           C  
ANISOU  276  C   ILE A  84     2085    907   1176   -154     56   -487       C  
ATOM    277  O   ILE A  84     -15.791   0.482 -11.329  1.00 11.76           O  
ANISOU  277  O   ILE A  84     2232    945   1291   -129   -181   -434       O  
ATOM    278  CB  ILE A  84     -18.200  -0.575 -13.179  1.00  8.48           C  
ANISOU  278  CB  ILE A  84     1242    885   1093   -145    443   -478       C  
ATOM    279  CG1 ILE A  84     -17.733  -2.010 -13.428  1.00 10.47           C  
ANISOU  279  CG1 ILE A  84     1708   1010   1261    -20     97   -658       C  
ATOM    280  CG2 ILE A  84     -17.451   0.411 -14.064  1.00  7.30           C  
ANISOU  280  CG2 ILE A  84      847    852   1072   -465    -80   -189       C  
ATOM    281  CD1 ILE A  84     -18.027  -2.488 -14.838  1.00 10.99           C  
ANISOU  281  CD1 ILE A  84     1513   1202   1463   -244    292   -750       C  
ATOM    282  N   GLY A  85     -16.435  -1.507 -10.493  1.00 11.58           N  
ANISOU  282  N   GLY A  85     2012   1401    988   -326    113   -535       N  
ATOM    283  CA  GLY A  85     -15.121  -1.791  -9.953  1.00 10.44           C  
ANISOU  283  CA  GLY A  85     1677   1034   1256   -512    125   -240       C  
ATOM    284  C   GLY A  85     -15.113  -3.070  -9.150  1.00 10.12           C  
ANISOU  284  C   GLY A  85     1803    864   1178   -352    289   -109       C  
ATOM    285  O   GLY A  85     -15.983  -3.929  -9.308  1.00  9.53           O  
ANISOU  285  O   GLY A  85     1641    798   1181   -116     70   -149       O  
ATOM    286  N   TYR A  86     -14.112  -3.189  -8.282  1.00 10.35           N  
ANISOU  286  N   TYR A  86     2171    691   1071    168    274    250       N  
ATOM    287  CA  TYR A  86     -13.927  -4.395  -7.491  1.00  8.79           C  
ANISOU  287  CA  TYR A  86     1592    606   1142    208    209   -282       C  
ATOM    288  C   TYR A  86     -13.561  -4.031  -6.061  1.00 11.05           C  
ANISOU  288  C   TYR A  86     1510   1282   1408    309    108   -358       C  
ATOM    289  O   TYR A  86     -13.016  -2.957  -5.793  1.00 12.00           O  
ANISOU  289  O   TYR A  86     1523   1538   1500    115     99   -203       O  
ATOM    290  CB  TYR A  86     -12.836  -5.301  -8.084  1.00  9.83           C  
ANISOU  290  CB  TYR A  86     1194   1052   1490    -57    247    -18       C  
ATOM    291  CG  TYR A  86     -11.460  -4.669  -8.126  1.00 11.28           C  
ANISOU  291  CG  TYR A  86     1325   1446   1515     97    259     23       C  
ATOM    292  CD1 TYR A  86     -11.055  -3.907  -9.216  1.00  9.21           C  
ANISOU  292  CD1 TYR A  86     1018   1152   1330    125    672    -13       C  
ATOM    293  CD2 TYR A  86     -10.563  -4.842  -7.078  1.00 11.15           C  
ANISOU  293  CD2 TYR A  86     1457   1493   1287    316     69    -73       C  
ATOM    294  CE1 TYR A  86      -9.798  -3.329  -9.257  1.00 11.16           C  
ANISOU  294  CE1 TYR A  86     1372   1462   1409    447    425   -109       C  
ATOM    295  CE2 TYR A  86      -9.305  -4.268  -7.110  1.00 12.79           C  
ANISOU  295  CE2 TYR A  86     1641   1743   1476    160    330    228       C  
ATOM    296  CZ  TYR A  86      -8.927  -3.515  -8.203  1.00 13.94           C  
ANISOU  296  CZ  TYR A  86     1617   1954   1725    310    267    137       C  
ATOM    297  OH  TYR A  86      -7.675  -2.945  -8.235  1.00 12.76           O  
ANISOU  297  OH  TYR A  86     1217   1932   1699    747    206     32       O  
ATOM    298  N   TYR A  87     -13.879  -4.940  -5.146  1.00  9.81           N  
ANISOU  298  N   TYR A  87     1190   1100   1438    334    -86   -314       N  
ATOM    299  CA  TYR A  87     -13.362  -4.908  -3.787  1.00 11.65           C  
ANISOU  299  CA  TYR A  87     1364   1529   1535    188    305   -546       C  
ATOM    300  C   TYR A  87     -12.228  -5.914  -3.662  1.00 12.04           C  
ANISOU  300  C   TYR A  87     1544   1383   1649    315    235   -582       C  
ATOM    301  O   TYR A  87     -12.304  -7.022  -4.205  1.00 12.66           O  
ANISOU  301  O   TYR A  87     1234   1603   1973    551    186   -307       O  
ATOM    302  CB  TYR A  87     -14.447  -5.236  -2.761  1.00 11.84           C  
ANISOU  302  CB  TYR A  87     1656   1450   1394    -72    619   -570       C  
ATOM    303  CG  TYR A  87     -15.457  -4.140  -2.501  1.00 10.76           C  
ANISOU  303  CG  TYR A  87     1723   1187   1178   -107    633   -463       C  
ATOM    304  CD1 TYR A  87     -16.579  -3.997  -3.307  1.00 12.37           C  
ANISOU  304  CD1 TYR A  87     2092   1342   1265    -97    899    -67       C  
ATOM    305  CD2 TYR A  87     -15.307  -3.273  -1.424  1.00  9.23           C  
ANISOU  305  CD2 TYR A  87     1716    620   1170    129    385   -230       C  
ATOM    306  CE1 TYR A  87     -17.516  -3.012  -3.059  1.00 12.94           C  
ANISOU  306  CE1 TYR A  87     2381   1143   1393    -41    445    115       C  
ATOM    307  CE2 TYR A  87     -16.238  -2.284  -1.168  1.00 10.55           C  
ANISOU  307  CE2 TYR A  87     1918    748   1343     89    153    -70       C  
ATOM    308  CZ  TYR A  87     -17.341  -2.159  -1.989  1.00 11.69           C  
ANISOU  308  CZ  TYR A  87     2068    809   1566    230    122    -99       C  
ATOM    309  OH  TYR A  87     -18.272  -1.180  -1.737  1.00 11.80           O  
ANISOU  309  OH  TYR A  87     1824    874   1786    267    402     25       O  
ATOM    310  N   ARG A  88     -11.176  -5.525  -2.949  1.00 12.37           N  
ANISOU  310  N   ARG A  88     1524   1585   1592    361    159   -292       N  
ATOM    311  CA  ARG A  88     -10.017  -6.376  -2.723  1.00 13.70           C  
ANISOU  311  CA  ARG A  88     1484   2056   1665    447    183   -119       C  
ATOM    312  C   ARG A  88      -9.837  -6.579  -1.226  1.00 12.72           C  
ANISOU  312  C   ARG A  88     1364   1783   1684    382     65    156       C  
ATOM    313  O   ARG A  88      -9.801  -5.609  -0.463  1.00 13.33           O  
ANISOU  313  O   ARG A  88     1242   2178   1645    237     67    335       O  
ATOM    314  CB  ARG A  88      -8.756  -5.764  -3.338  1.00 17.40           C  
ANISOU  314  CB  ARG A  88     1826   2801   1986    709    336    134       C  
ATOM    315  CG  ARG A  88      -7.492  -6.582  -3.114  1.00 22.90           C  
ANISOU  315  CG  ARG A  88     2610   3523   2567    937    274    226       C  
ATOM    316  CD  ARG A  88      -6.347  -6.043  -3.958  1.00 28.37           C  
ANISOU  316  CD  ARG A  88     3477   4207   3098    820    -76    271       C  
ATOM    317  NE  ARG A  88      -5.092  -6.749  -3.718  1.00 31.37           N  
ANISOU  317  NE  ARG A  88     3886   4649   3383    623   -759    244       N  
ATOM    318  CZ  ARG A  88      -4.138  -6.316  -2.902  1.00 35.91           C  
ANISOU  318  CZ  ARG A  88     4792   5152   3701    855  -1017     71       C  
ATOM    319  NH1 ARG A  88      -4.295  -5.175  -2.243  1.00 36.55           N  
ANISOU  319  NH1 ARG A  88     4995   5144   3747    816  -1237     42       N  
ATOM    320  NH2 ARG A  88      -3.026  -7.021  -2.745  1.00 39.49           N  
ANISOU  320  NH2 ARG A  88     5425   5593   3987    693   -891   -177       N  
ATOM    321  N   ARG A  89      -9.730  -7.839  -0.813  1.00 12.82           N  
ANISOU  321  N   ARG A  89     1426   1670   1774    521    306    368       N  
ATOM    322  CA  ARG A  89      -9.607  -8.163   0.599  1.00 14.78           C  
ANISOU  322  CA  ARG A  89     1908   1718   1989    497   -202    657       C  
ATOM    323  C   ARG A  89      -8.170  -7.995   1.068  1.00 19.20           C  
ANISOU  323  C   ARG A  89     2414   2622   2260    395   -409    365       C  
ATOM    324  O   ARG A  89      -7.224  -8.398   0.384  1.00 20.74           O  
ANISOU  324  O   ARG A  89     2127   3451   2302    478   -409     86       O  
ATOM    325  CB  ARG A  89     -10.073  -9.595   0.860  1.00 15.42           C  
ANISOU  325  CB  ARG A  89     2399   1517   1942    183   -140    542       C  
ATOM    326  CG  ARG A  89      -9.883 -10.057   2.301  1.00 16.23           C  
ANISOU  326  CG  ARG A  89     3045   1284   1838    228   -285    649       C  
ATOM    327  CD  ARG A  89     -10.281 -11.511   2.455  1.00 20.05           C  
ANISOU  327  CD  ARG A  89     3853   1589   2178    254   -333    598       C  
ATOM    328  NE  ARG A  89      -9.496 -12.367   1.573  1.00 22.48           N  
ANISOU  328  NE  ARG A  89     4423   1448   2670    480   -189    478       N  
ATOM    329  CZ  ARG A  89      -9.961 -13.468   0.997  1.00 26.85           C  
ANISOU  329  CZ  ARG A  89     5162   2188   2853    750   -142    269       C  
ATOM    330  NH1 ARG A  89     -11.215 -13.847   1.204  1.00 27.90           N  
ANISOU  330  NH1 ARG A  89     5247   2452   2902    686   -356    145       N  
ATOM    331  NH2 ARG A  89      -9.176 -14.185   0.205  1.00 28.19           N  
ANISOU  331  NH2 ARG A  89     5374   2488   2848   1321    242     64       N  
ATOM    332  N   ALA A  90      -8.013  -7.389   2.240  1.00 20.46           N  
ANISOU  332  N   ALA A  90     2908   2631   2233    338   -588    468       N  
ATOM    333  CA  ALA A  90      -6.726  -7.286   2.911  1.00 22.77           C  
ANISOU  333  CA  ALA A  90     2979   3046   2625    478   -547    468       C  
ATOM    334  C   ALA A  90      -6.894  -7.772   4.341  1.00 22.51           C  
ANISOU  334  C   ALA A  90     2812   2965   2776    962   -768    691       C  
ATOM    335  O   ALA A  90      -7.815  -7.341   5.041  1.00 22.00           O  
ANISOU  335  O   ALA A  90     2489   3211   2658    856   -498    420       O  
ATOM    336  CB  ALA A  90      -6.195  -5.849   2.892  1.00 23.47           C  
ANISOU  336  CB  ALA A  90     3143   3055   2718    379   -557    459       C  
ATOM    337  N   THR A  91      -6.017  -8.676   4.767  1.00 24.30           N  
ANISOU  337  N   THR A  91     2797   3345   3091   1070   -982    767       N  
ATOM    338  CA  THR A  91      -6.061  -9.236   6.110  1.00 28.25           C  
ANISOU  338  CA  THR A  91     3375   3840   3517    756   -996    890       C  
ATOM    339  C   THR A  91      -4.738  -8.962   6.806  1.00 31.82           C  
ANISOU  339  C   THR A  91     3728   4460   3904    975  -1082    644       C  
ATOM    340  O   THR A  91      -3.671  -9.242   6.250  1.00 33.55           O  
ANISOU  340  O   THR A  91     3940   4987   3819    893   -935    572       O  
ATOM    341  CB  THR A  91      -6.337 -10.743   6.076  1.00 28.98           C  
ANISOU  341  CB  THR A  91     3624   3869   3519    215   -997   1298       C  
ATOM    342  OG1 THR A  91      -7.474 -11.005   5.245  1.00 29.07           O  
ANISOU  342  OG1 THR A  91     3699   3842   3505   -348   -858   1266       O  
ATOM    343  CG2 THR A  91      -6.612 -11.266   7.482  1.00 28.44           C  
ANISOU  343  CG2 THR A  91     3514   3750   3543     60   -552   1426       C  
ATOM    344  N   ARG A  92      -4.808  -8.409   8.012  1.00 34.35           N  
ANISOU  344  N   ARG A  92     4122   4608   4321   1005  -1105    343       N  
ATOM    345  CA  ARG A  92      -3.632  -8.202   8.840  1.00 37.81           C  
ANISOU  345  CA  ARG A  92     4800   4978   4590    862  -1078    145       C  
ATOM    346  C   ARG A  92      -3.652  -9.159  10.025  1.00 37.32           C  
ANISOU  346  C   ARG A  92     4760   4792   4627    733  -1231    125       C  
ATOM    347  O   ARG A  92      -4.687  -9.736  10.371  1.00 35.09           O  
ANISOU  347  O   ARG A  92     4560   4312   4458    360  -1528     41       O  
ATOM    348  CB  ARG A  92      -3.534  -6.751   9.328  1.00 42.25           C  
ANISOU  348  CB  ARG A  92     5288   5734   5030   1104   -654    106       C  
ATOM    349  CG  ARG A  92      -4.861  -6.035   9.523  1.00 46.07           C  
ANISOU  349  CG  ARG A  92     5755   6305   5445   1081   -161      8       C  
ATOM    350  CD  ARG A  92      -4.661  -4.801  10.395  1.00 48.64           C  
ANISOU  350  CD  ARG A  92     6155   6545   5779    924     66     94       C  
ATOM    351  NE  ARG A  92      -5.720  -3.807  10.246  1.00 50.46           N  
ANISOU  351  NE  ARG A  92     6387   6891   5894    877    169    256       N  
ATOM    352  CZ  ARG A  92      -6.900  -3.868  10.855  1.00 52.04           C  
ANISOU  352  CZ  ARG A  92     6642   7259   5872    755    464     37       C  
ATOM    353  NH1 ARG A  92      -7.797  -2.911  10.666  1.00 51.81           N  
ANISOU  353  NH1 ARG A  92     6458   7412   5816    807    747   -450       N  
ATOM    354  NH2 ARG A  92      -7.193  -4.890  11.644  1.00 53.79           N  
ANISOU  354  NH2 ARG A  92     6937   7503   5997    594    615     -8       N  
ATOM    355  N   ARG A  93      -2.483  -9.324  10.641  1.00 39.23           N  
ANISOU  355  N   ARG A  93     4861   5205   4841    789  -1301    159       N  
ATOM    356  CA  ARG A  93      -2.283 -10.278  11.721  1.00 40.53           C  
ANISOU  356  CA  ARG A  93     4980   5297   5124   1052  -1351    317       C  
ATOM    357  C   ARG A  93      -1.729  -9.574  12.953  1.00 40.23           C  
ANISOU  357  C   ARG A  93     4701   5438   5145   1070  -1355    644       C  
ATOM    358  O   ARG A  93      -1.011  -8.575  12.847  1.00 41.76           O  
ANISOU  358  O   ARG A  93     5090   5538   5240    905  -1522    664       O  
ATOM    359  CB  ARG A  93      -1.315 -11.394  11.303  1.00 42.46           C  
ANISOU  359  CB  ARG A  93     5499   5237   5395   1159  -1308     31       C  
ATOM    360  CG  ARG A  93      -1.520 -11.911   9.892  1.00 44.58           C  
ANISOU  360  CG  ARG A  93     5969   5314   5655    743  -1381     63       C  
ATOM    361  CD  ARG A  93      -2.128 -13.298   9.897  1.00 46.31           C  
ANISOU  361  CD  ARG A  93     6209   5473   5912    374  -1325     57       C  
ATOM    362  NE  ARG A  93      -1.182 -14.328  10.314  1.00 48.06           N  
ANISOU  362  NE  ARG A  93     6520   5571   6171    427  -1155   -123       N  
ATOM    363  CZ  ARG A  93      -1.518 -15.589  10.568  1.00 50.10           C  
ANISOU  363  CZ  ARG A  93     6789   5833   6412    356  -1036   -261       C  
ATOM    364  NH1 ARG A  93      -2.782 -15.976  10.454  1.00 50.39           N  
ANISOU  364  NH1 ARG A  93     6764   5883   6498    289  -1049   -420       N  
ATOM    365  NH2 ARG A  93      -0.593 -16.464  10.939  1.00 50.26           N  
ANISOU  365  NH2 ARG A  93     6846   5811   6438    482   -950   -149       N  
ATOM    366  N   ILE A  94      -2.071 -10.108  14.128  1.00 38.62           N  
ANISOU  366  N   ILE A  94     4266   5319   5088   1278  -1260   1056       N  
ATOM    367  CA  ILE A  94      -1.479  -9.682  15.390  1.00 38.57           C  
ANISOU  367  CA  ILE A  94     4300   5236   5120   1434  -1187   1265       C  
ATOM    368  C   ILE A  94      -1.232 -10.916  16.247  1.00 38.42           C  
ANISOU  368  C   ILE A  94     4194   5247   5155   1766  -1392   1464       C  
ATOM    369  O   ILE A  94      -1.864 -11.961  16.074  1.00 36.28           O  
ANISOU  369  O   ILE A  94     3910   4752   5124   1777  -1440   1174       O  
ATOM    370  CB  ILE A  94      -2.352  -8.671  16.170  1.00 39.02           C  
ANISOU  370  CB  ILE A  94     4520   5124   5181   1502  -1002   1338       C  
ATOM    371  CG1 ILE A  94      -3.738  -9.255  16.452  1.00 39.26           C  
ANISOU  371  CG1 ILE A  94     4613   5175   5127   1612   -898   1262       C  
ATOM    372  CG2 ILE A  94      -2.443  -7.343  15.430  1.00 40.29           C  
ANISOU  372  CG2 ILE A  94     4679   5325   5305   1260  -1052   1285       C  
ATOM    373  CD1 ILE A  94      -4.528  -8.468  17.481  1.00 39.18           C  
ANISOU  373  CD1 ILE A  94     4621   5178   5086   1642   -738   1103       C  
ATOM    374  N   ARG A  95      -0.297 -10.781  17.185  1.00 41.13           N  
ANISOU  374  N   ARG A  95     4554   5685   5386   1127  -1475   1356       N  
ATOM    375  CA  ARG A  95       0.023 -11.876  18.092  1.00 43.77           C  
ANISOU  375  CA  ARG A  95     5150   5826   5656    507  -1331   1489       C  
ATOM    376  C   ARG A  95      -1.089 -12.032  19.123  1.00 41.39           C  
ANISOU  376  C   ARG A  95     4849   5495   5382    131  -1312   1660       C  
ATOM    377  O   ARG A  95      -1.408 -11.087  19.851  1.00 39.44           O  
ANISOU  377  O   ARG A  95     4492   5202   5290   -221  -1293   1804       O  
ATOM    378  CB  ARG A  95       1.361 -11.623  18.783  1.00 48.98           C  
ANISOU  378  CB  ARG A  95     5852   6463   6296    347  -1194   1334       C  
ATOM    379  CG  ARG A  95       1.831 -12.784  19.650  1.00 53.74           C  
ANISOU  379  CG  ARG A  95     6518   7032   6870    320  -1071   1126       C  
ATOM    380  CD  ARG A  95       2.524 -12.301  20.917  1.00 58.12           C  
ANISOU  380  CD  ARG A  95     7127   7556   7398    287   -676    945       C  
ATOM    381  NE  ARG A  95       3.831 -11.703  20.654  1.00 61.30           N  
ANISOU  381  NE  ARG A  95     7598   7951   7744    150   -354    841       N  
ATOM    382  CZ  ARG A  95       4.983 -12.362  20.738  1.00 63.34           C  
ANISOU  382  CZ  ARG A  95     8031   8148   7888    174   -143    720       C  
ATOM    383  NH1 ARG A  95       6.126 -11.739  20.484  1.00 63.54           N  
ANISOU  383  NH1 ARG A  95     8043   8178   7920    171     31    692       N  
ATOM    384  NH2 ARG A  95       4.993 -13.644  21.077  1.00 64.10           N  
ANISOU  384  NH2 ARG A  95     8242   8222   7892    218   -180    631       N  
ATOM    385  N   GLY A  96      -1.679 -13.224  19.183  1.00 41.14           N  
ANISOU  385  N   GLY A  96     5051   5376   5205     86  -1193   1631       N  
ATOM    386  CA  GLY A  96      -2.741 -13.498  20.124  1.00 42.86           C  
ANISOU  386  CA  GLY A  96     5418   5609   5257   -104   -866   1391       C  
ATOM    387  C   GLY A  96      -2.224 -13.777  21.522  1.00 44.64           C  
ANISOU  387  C   GLY A  96     5784   5836   5341   -361   -424   1294       C  
ATOM    388  O   GLY A  96      -1.026 -13.743  21.802  1.00 45.84           O  
ANISOU  388  O   GLY A  96     6321   5807   5290   -403   -239   1236       O  
ATOM    389  N   GLY A  97      -3.168 -14.066  22.420  1.00 45.80           N  
ANISOU  389  N   GLY A  97     5805   6056   5543   -517   -190   1264       N  
ATOM    390  CA  GLY A  97      -2.826 -14.348  23.804  1.00 46.55           C  
ANISOU  390  CA  GLY A  97     5751   6300   5634   -776   -112    954       C  
ATOM    391  C   GLY A  97      -2.027 -15.619  23.999  1.00 48.25           C  
ANISOU  391  C   GLY A  97     5903   6652   5777   -767   -104    657       C  
ATOM    392  O   GLY A  97      -1.433 -15.806  25.067  1.00 49.45           O  
ANISOU  392  O   GLY A  97     5995   6924   5869  -1055    197    506       O  
ATOM    393  N   ASP A  98      -2.002 -16.498  22.999  1.00 48.73           N  
ANISOU  393  N   ASP A  98     6096   6571   5847   -502   -410    473       N  
ATOM    394  CA  ASP A  98      -1.223 -17.727  23.050  1.00 49.04           C  
ANISOU  394  CA  ASP A  98     6189   6493   5951   -282   -850    485       C  
ATOM    395  C   ASP A  98       0.106 -17.607  22.314  1.00 49.98           C  
ANISOU  395  C   ASP A  98     6420   6645   5925     30  -1094    461       C  
ATOM    396  O   ASP A  98       0.810 -18.611  22.159  1.00 50.70           O  
ANISOU  396  O   ASP A  98     6629   6719   5914     44  -1244    496       O  
ATOM    397  CB  ASP A  98      -2.036 -18.891  22.476  1.00 49.47           C  
ANISOU  397  CB  ASP A  98     6262   6421   6114   -267  -1029    574       C  
ATOM    398  CG  ASP A  98      -2.465 -18.653  21.038  1.00 49.51           C  
ANISOU  398  CG  ASP A  98     6243   6303   6265   -402  -1229    580       C  
ATOM    399  OD1 ASP A  98      -2.294 -17.521  20.539  1.00 48.46           O  
ANISOU  399  OD1 ASP A  98     6148   6067   6198   -491  -1545    640       O  
ATOM    400  OD2 ASP A  98      -2.974 -19.603  20.406  1.00 49.82           O  
ANISOU  400  OD2 ASP A  98     6205   6320   6404   -444  -1093    665       O  
ATOM    401  N   GLY A  99       0.462 -16.406  21.857  1.00 49.85           N  
ANISOU  401  N   GLY A  99     6436   6616   5887    164  -1051    585       N  
ATOM    402  CA  GLY A  99       1.682 -16.192  21.110  1.00 50.30           C  
ANISOU  402  CA  GLY A  99     6603   6540   5968    468   -889    692       C  
ATOM    403  C   GLY A  99       1.592 -16.480  19.630  1.00 50.78           C  
ANISOU  403  C   GLY A  99     6761   6362   6172    769   -811    779       C  
ATOM    404  O   GLY A  99       2.442 -16.003  18.869  1.00 51.23           O  
ANISOU  404  O   GLY A  99     6891   6251   6325    624   -823    734       O  
ATOM    405  N   LYS A 100       0.595 -17.243  19.194  1.00 50.20           N  
ANISOU  405  N   LYS A 100     6635   6239   6200   1157   -928    920       N  
ATOM    406  CA  LYS A 100       0.433 -17.545  17.781  1.00 49.95           C  
ANISOU  406  CA  LYS A 100     6430   6276   6274   1449  -1228   1043       C  
ATOM    407  C   LYS A 100      -0.216 -16.371  17.059  1.00 48.53           C  
ANISOU  407  C   LYS A 100     6143   6130   6165   1630  -1266    952       C  
ATOM    408  O   LYS A 100      -1.019 -15.628  17.631  1.00 45.51           O  
ANISOU  408  O   LYS A 100     5745   5621   5926   2264  -1480    880       O  
ATOM    409  CB  LYS A 100      -0.409 -18.808  17.595  1.00 51.77           C  
ANISOU  409  CB  LYS A 100     6582   6617   6470   1463  -1212   1110       C  
ATOM    410  CG  LYS A 100       0.125 -20.016  18.347  1.00 53.96           C  
ANISOU  410  CG  LYS A 100     6849   6938   6716   1389  -1022   1157       C  
ATOM    411  CD  LYS A 100       1.589 -20.259  18.016  1.00 56.01           C  
ANISOU  411  CD  LYS A 100     7116   7233   6932   1420   -985   1168       C  
ATOM    412  CE  LYS A 100       2.217 -21.263  18.968  1.00 57.51           C  
ANISOU  412  CE  LYS A 100     7295   7474   7081   1389   -860   1215       C  
ATOM    413  NZ  LYS A 100       3.683 -21.396  18.738  1.00 58.21           N  
ANISOU  413  NZ  LYS A 100     7299   7668   7152   1383   -810   1184       N  
ATOM    414  N   MET A 101       0.147 -16.205  15.791  1.00 49.36           N  
ANISOU  414  N   MET A 101     6140   6335   6280   1267   -857    884       N  
ATOM    415  CA  MET A 101      -0.418 -15.128  14.991  1.00 49.47           C  
ANISOU  415  CA  MET A 101     6093   6288   6418    935   -500    632       C  
ATOM    416  C   MET A 101      -1.884 -15.405  14.687  1.00 48.87           C  
ANISOU  416  C   MET A 101     6142   6096   6330   1181   -420    652       C  
ATOM    417  O   MET A 101      -2.281 -16.544  14.427  1.00 49.51           O  
ANISOU  417  O   MET A 101     6203   6130   6479   1195   -350    546       O  
ATOM    418  CB  MET A 101       0.374 -14.954  13.696  1.00 50.20           C  
ANISOU  418  CB  MET A 101     6030   6406   6638    421   -266    374       C  
ATOM    419  CG  MET A 101       1.795 -14.472  13.922  1.00 51.48           C  
ANISOU  419  CG  MET A 101     6072   6553   6934   -121     57    107       C  
ATOM    420  SD  MET A 101       1.831 -12.940  14.871  1.00 53.11           S  
ANISOU  420  SD  MET A 101     6132   6768   7279   -646    231    -77       S  
ATOM    421  CE  MET A 101       3.526 -12.938  15.448  1.00 55.11           C  
ANISOU  421  CE  MET A 101     6576   7015   7350   -680    286   -114       C  
ATOM    422  N   LYS A 102      -2.690 -14.348  14.723  1.00 47.00           N  
ANISOU  422  N   LYS A 102     6048   5731   6080   1343   -468    820       N  
ATOM    423  CA  LYS A 102      -4.135 -14.447  14.588  1.00 46.01           C  
ANISOU  423  CA  LYS A 102     5902   5656   5923   1030   -615    832       C  
ATOM    424  C   LYS A 102      -4.617 -13.462  13.534  1.00 42.38           C  
ANISOU  424  C   LYS A 102     5575   5033   5497   1264  -1163    730       C  
ATOM    425  O   LYS A 102      -4.093 -12.350  13.426  1.00 43.00           O  
ANISOU  425  O   LYS A 102     5693   5104   5542   1698  -1440    784       O  
ATOM    426  CB  LYS A 102      -4.825 -14.168  15.932  1.00 49.36           C  
ANISOU  426  CB  LYS A 102     6224   6339   6193    559   -129    793       C  
ATOM    427  CG  LYS A 102      -6.342 -14.111  15.875  1.00 53.22           C  
ANISOU  427  CG  LYS A 102     6867   6888   6464    311    357    608       C  
ATOM    428  CD  LYS A 102      -6.917 -13.630  17.197  1.00 55.74           C  
ANISOU  428  CD  LYS A 102     7233   7282   6664    270    623    533       C  
ATOM    429  CE  LYS A 102      -8.430 -13.503  17.131  1.00 57.11           C  
ANISOU  429  CE  LYS A 102     7369   7510   6821    172    753    581       C  
ATOM    430  NZ  LYS A 102      -8.992 -12.947  18.394  1.00 57.89           N  
ANISOU  430  NZ  LYS A 102     7467   7588   6941     37    660    625       N  
ATOM    431  N   ASP A 103      -5.611 -13.880  12.753  1.00 39.04           N  
ANISOU  431  N   ASP A 103     5245   4543   5044    883  -1206    420       N  
ATOM    432  CA  ASP A 103      -6.211 -12.997  11.763  1.00 36.54           C  
ANISOU  432  CA  ASP A 103     4917   4405   4560    493  -1001     44       C  
ATOM    433  C   ASP A 103      -7.076 -11.943  12.442  1.00 29.67           C  
ANISOU  433  C   ASP A 103     4088   3402   3784    350   -843    188       C  
ATOM    434  O   ASP A 103      -7.937 -12.266  13.265  1.00 26.76           O  
ANISOU  434  O   ASP A 103     3807   2991   3368    109   -500    450       O  
ATOM    435  CB  ASP A 103      -7.059 -13.799  10.775  1.00 41.45           C  
ANISOU  435  CB  ASP A 103     5520   5250   4978    137   -995   -245       C  
ATOM    436  CG  ASP A 103      -6.251 -14.348   9.616  1.00 45.71           C  
ANISOU  436  CG  ASP A 103     6144   5806   5419   -376   -987   -227       C  
ATOM    437  OD1 ASP A 103      -5.072 -13.969   9.478  1.00 45.36           O  
ANISOU  437  OD1 ASP A 103     5948   5723   5565   -815   -954   -175       O  
ATOM    438  OD2 ASP A 103      -6.801 -15.157   8.838  1.00 47.79           O  
ANISOU  438  OD2 ASP A 103     6526   6063   5570   -332  -1093   -215       O  
ATOM    439  N   LEU A 104      -6.845 -10.680  12.099  1.00 25.54           N  
ANISOU  439  N   LEU A 104     3231   3086   3388    244   -725   -130       N  
ATOM    440  CA  LEU A 104      -7.814  -9.649  12.422  1.00 23.62           C  
ANISOU  440  CA  LEU A 104     3036   2798   3141    247   -679   -182       C  
ATOM    441  C   LEU A 104      -8.933  -9.659  11.384  1.00 21.30           C  
ANISOU  441  C   LEU A 104     2502   2815   2776    340   -688   -112       C  
ATOM    442  O   LEU A 104      -8.844 -10.319  10.345  1.00 20.49           O  
ANISOU  442  O   LEU A 104     2088   3095   2602    137   -518     47       O  
ATOM    443  CB  LEU A 104      -7.142  -8.279  12.489  1.00 25.38           C  
ANISOU  443  CB  LEU A 104     3287   3130   3225    255   -409   -305       C  
ATOM    444  CG  LEU A 104      -6.260  -8.051  13.716  1.00 27.05           C  
ANISOU  444  CG  LEU A 104     3687   3219   3371    306     20   -359       C  
ATOM    445  CD1 LEU A 104      -5.487  -6.751  13.592  1.00 27.99           C  
ANISOU  445  CD1 LEU A 104     3851   3325   3459    228    192   -281       C  
ATOM    446  CD2 LEU A 104      -7.111  -8.055  14.976  1.00 27.49           C  
ANISOU  446  CD2 LEU A 104     4013   3182   3249    564      6   -275       C  
ATOM    447  N   SER A 105     -10.002  -8.929  11.680  1.00 20.52           N  
ANISOU  447  N   SER A 105     2518   2803   2473    363   -587    225       N  
ATOM    448  CA  SER A 105     -11.137  -8.855  10.769  1.00 19.74           C  
ANISOU  448  CA  SER A 105     2548   2744   2210   -173   -368    159       C  
ATOM    449  C   SER A 105     -10.672  -8.363   9.403  1.00 19.16           C  
ANISOU  449  C   SER A 105     2990   2409   1883   -328   -594    101       C  
ATOM    450  O   SER A 105     -10.105  -7.264   9.311  1.00 19.56           O  
ANISOU  450  O   SER A 105     3097   2485   1849   -124   -534    168       O  
ATOM    451  CB  SER A 105     -12.214  -7.929  11.324  1.00 20.59           C  
ANISOU  451  CB  SER A 105     2429   3039   2354   -186      0    605       C  
ATOM    452  OG  SER A 105     -12.760  -8.447  12.524  1.00 24.12           O  
ANISOU  452  OG  SER A 105     3026   3461   2678   -112    489    639       O  
ATOM    453  N   PRO A 106     -10.861  -9.139   8.335  1.00 20.16           N  
ANISOU  453  N   PRO A 106     3358   2235   2067   -420   -305    275       N  
ATOM    454  CA  PRO A 106     -10.415  -8.690   7.012  1.00 18.57           C  
ANISOU  454  CA  PRO A 106     3167   1962   1928   -433   -260    216       C  
ATOM    455  C   PRO A 106     -11.112  -7.403   6.603  1.00 17.91           C  
ANISOU  455  C   PRO A 106     3129   1904   1772    -84   -120     15       C  
ATOM    456  O   PRO A 106     -12.248  -7.130   6.996  1.00 17.75           O  
ANISOU  456  O   PRO A 106     2974   2068   1702   -115    207    139       O  
ATOM    457  CB  PRO A 106     -10.805  -9.853   6.090  1.00 18.14           C  
ANISOU  457  CB  PRO A 106     3209   1732   1949    -15   -311    304       C  
ATOM    458  CG  PRO A 106     -10.934 -11.035   6.997  1.00 20.18           C  
ANISOU  458  CG  PRO A 106     3593   1828   2247    208   -250    460       C  
ATOM    459  CD  PRO A 106     -11.440 -10.492   8.297  1.00 20.34           C  
ANISOU  459  CD  PRO A 106     3651   1976   2101    106   -138    271       C  
ATOM    460  N   ARG A 107     -10.408  -6.601   5.809  1.00 16.21           N  
ANISOU  460  N   ARG A 107     2937   1724   1497    -10   -140    232       N  
ATOM    461  CA  ARG A 107     -10.931  -5.343   5.299  1.00 18.27           C  
ANISOU  461  CA  ARG A 107     3305   2006   1630     37   -370    183       C  
ATOM    462  C   ARG A 107     -10.977  -5.408   3.781  1.00 17.52           C  
ANISOU  462  C   ARG A 107     3207   1948   1503    492   -702    287       C  
ATOM    463  O   ARG A 107     -10.023  -5.867   3.145  1.00 22.26           O  
ANISOU  463  O   ARG A 107     3945   2670   1842    934   -929    175       O  
ATOM    464  CB  ARG A 107     -10.080  -4.159   5.769  1.00 21.39           C  
ANISOU  464  CB  ARG A 107     3479   2472   2175    100   -301    170       C  
ATOM    465  CG  ARG A 107     -10.009  -4.044   7.285  1.00 25.57           C  
ANISOU  465  CG  ARG A 107     3846   3078   2791   -445   -289    275       C  
ATOM    466  CD  ARG A 107      -9.705  -2.632   7.751  1.00 30.22           C  
ANISOU  466  CD  ARG A 107     4125   3780   3578   -789   -219    589       C  
ATOM    467  NE  ARG A 107      -8.292  -2.290   7.635  1.00 34.60           N  
ANISOU  467  NE  ARG A 107     4620   4297   4231   -984   -157    478       N  
ATOM    468  CZ  ARG A 107      -7.749  -1.201   8.172  1.00 38.89           C  
ANISOU  468  CZ  ARG A 107     5164   4850   4764  -1012     19     14       C  
ATOM    469  NH1 ARG A 107      -8.502  -0.359   8.866  1.00 41.54           N  
ANISOU  469  NH1 ARG A 107     5736   5068   4978   -881    372   -383       N  
ATOM    470  NH2 ARG A 107      -6.454  -0.959   8.025  1.00 39.09           N  
ANISOU  470  NH2 ARG A 107     4921   5055   4876  -1584   -398     68       N  
ATOM    471  N   TRP A 108     -12.088  -4.959   3.206  1.00 13.05           N  
ANISOU  471  N   TRP A 108     2525   1136   1299    -52   -775    330       N  
ATOM    472  CA  TRP A 108     -12.298  -4.974   1.765  1.00 12.35           C  
ANISOU  472  CA  TRP A 108     2390   1061   1240     91   -452     31       C  
ATOM    473  C   TRP A 108     -12.298  -3.537   1.258  1.00 14.06           C  
ANISOU  473  C   TRP A 108     2657   1200   1486    164    -40    295       C  
ATOM    474  O   TRP A 108     -13.081  -2.710   1.738  1.00 16.40           O  
ANISOU  474  O   TRP A 108     3252   1275   1704    526    512      5       O  
ATOM    475  CB  TRP A 108     -13.612  -5.673   1.416  1.00 11.91           C  
ANISOU  475  CB  TRP A 108     2377    797   1351   -205     16    126       C  
ATOM    476  CG  TRP A 108     -13.667  -7.127   1.802  1.00 12.55           C  
ANISOU  476  CG  TRP A 108     2416   1128   1225    114     29    216       C  
ATOM    477  CD1 TRP A 108     -13.833  -7.641   3.060  1.00 12.87           C  
ANISOU  477  CD1 TRP A 108     2433    940   1518   -181    259    150       C  
ATOM    478  CD2 TRP A 108     -13.577  -8.254   0.920  1.00 13.53           C  
ANISOU  478  CD2 TRP A 108     2468   1306   1367    135   -162    227       C  
ATOM    479  NE1 TRP A 108     -13.843  -9.015   3.013  1.00 12.69           N  
ANISOU  479  NE1 TRP A 108     2146   1236   1438      4     67    185       N  
ATOM    480  CE2 TRP A 108     -13.688  -9.416   1.712  1.00 13.45           C  
ANISOU  480  CE2 TRP A 108     2532   1268   1310   -135     56    238       C  
ATOM    481  CE3 TRP A 108     -13.410  -8.392  -0.462  1.00 14.62           C  
ANISOU  481  CE3 TRP A 108     2571   1380   1602    307   -226     18       C  
ATOM    482  CZ2 TRP A 108     -13.635 -10.699   1.167  1.00 15.26           C  
ANISOU  482  CZ2 TRP A 108     2748   1739   1312   -157    147    -76       C  
ATOM    483  CZ3 TRP A 108     -13.358  -9.668  -1.002  1.00 15.34           C  
ANISOU  483  CZ3 TRP A 108     2526   1687   1617    302   -413      3       C  
ATOM    484  CH2 TRP A 108     -13.472 -10.804  -0.189  1.00 14.97           C  
ANISOU  484  CH2 TRP A 108     2577   1609   1503    -94   -114    320       C  
ATOM    485  N   TYR A 109     -11.424  -3.242   0.296  1.00 12.76           N  
ANISOU  485  N   TYR A 109     1940   1526   1382   -288   -183    337       N  
ATOM    486  CA  TYR A 109     -11.264  -1.900  -0.250  1.00 13.40           C  
ANISOU  486  CA  TYR A 109     1794   1926   1370   -275   -252    472       C  
ATOM    487  C   TYR A 109     -11.752  -1.854  -1.692  1.00 11.79           C  
ANISOU  487  C   TYR A 109     1613   1640   1226   -312    -79     69       C  
ATOM    488  O   TYR A 109     -11.458  -2.755  -2.483  1.00 12.50           O  
ANISOU  488  O   TYR A 109     1793   1424   1534   -462      7    -87       O  
ATOM    489  CB  TYR A 109      -9.800  -1.454  -0.206  1.00 15.24           C  
ANISOU  489  CB  TYR A 109     2245   2106   1438   -790   -267    289       C  
ATOM    490  CG  TYR A 109      -9.227  -1.271   1.181  1.00 17.24           C  
ANISOU  490  CG  TYR A 109     2802   2427   1321   -510   -455    448       C  
ATOM    491  CD1 TYR A 109      -8.683  -2.345   1.878  1.00 17.38           C  
ANISOU  491  CD1 TYR A 109     2860   2592   1153   -110   -569    348       C  
ATOM    492  CD2 TYR A 109      -9.209  -0.021   1.784  1.00 17.54           C  
ANISOU  492  CD2 TYR A 109     2795   2569   1302   -364   -217    418       C  
ATOM    493  CE1 TYR A 109      -8.149  -2.178   3.142  1.00 18.92           C  
ANISOU  493  CE1 TYR A 109     2848   3016   1325   -246   -476    564       C  
ATOM    494  CE2 TYR A 109      -8.674   0.156   3.047  1.00 19.30           C  
ANISOU  494  CE2 TYR A 109     3035   3058   1242   -254   -605    657       C  
ATOM    495  CZ  TYR A 109      -8.148  -0.926   3.721  1.00 21.16           C  
ANISOU  495  CZ  TYR A 109     3264   3328   1448   -352   -718    522       C  
ATOM    496  OH  TYR A 109      -7.617  -0.755   4.979  1.00 25.39           O  
ANISOU  496  OH  TYR A 109     3988   3760   1898   -435   -879    322       O  
ATOM    497  N   PHE A 110     -12.472  -0.788  -2.041  1.00  9.63           N  
ANISOU  497  N   PHE A 110     1140   1687    833    347   -331    -77       N  
ATOM    498  CA  PHE A 110     -13.001  -0.639  -3.389  1.00  9.02           C  
ANISOU  498  CA  PHE A 110      785   1617   1026     98   -232     67       C  
ATOM    499  C   PHE A 110     -12.030   0.119  -4.286  1.00  9.61           C  
ANISOU  499  C   PHE A 110      945   1630   1078     78    -54    -66       C  
ATOM    500  O   PHE A 110     -11.466   1.145  -3.893  1.00 10.13           O  
ANISOU  500  O   PHE A 110     1075   1556   1218   -204     78    -64       O  
ATOM    501  CB  PHE A 110     -14.348   0.087  -3.382  1.00  8.46           C  
ANISOU  501  CB  PHE A 110      641   1467   1109   -275    108     39       C  
ATOM    502  CG  PHE A 110     -14.884   0.364  -4.761  1.00  7.89           C  
ANISOU  502  CG  PHE A 110      847   1154    996   -210   -192   -382       C  
ATOM    503  CD1 PHE A 110     -15.573  -0.614  -5.459  1.00  8.35           C  
ANISOU  503  CD1 PHE A 110      739   1233   1201     -8    -80   -525       C  
ATOM    504  CD2 PHE A 110     -14.687   1.597  -5.365  1.00  8.02           C  
ANISOU  504  CD2 PHE A 110      958   1395    693   -438    132    273       C  
ATOM    505  CE1 PHE A 110     -16.059  -0.367  -6.730  1.00  7.84           C  
ANISOU  505  CE1 PHE A 110     1227    834    916    294    -37     76       C  
ATOM    506  CE2 PHE A 110     -15.169   1.851  -6.642  1.00  7.99           C  
ANISOU  506  CE2 PHE A 110     1199   1191    645     14    -26   -477       C  
ATOM    507  CZ  PHE A 110     -15.857   0.870  -7.322  1.00  7.19           C  
ANISOU  507  CZ  PHE A 110     1004    801    929    352     49   -207       C  
ATOM    508  N   TYR A 111     -11.862  -0.388  -5.506  1.00  8.36           N  
ANISOU  508  N   TYR A 111      864   1395    919     30    529    -56       N  
ATOM    509  CA  TYR A 111     -11.111   0.278  -6.559  1.00  9.37           C  
ANISOU  509  CA  TYR A 111      841   1660   1059   -240    440   -359       C  
ATOM    510  C   TYR A 111     -11.953   0.318  -7.823  1.00  9.50           C  
ANISOU  510  C   TYR A 111      869   1675   1067    -16    213     77       C  
ATOM    511  O   TYR A 111     -12.613  -0.667  -8.169  1.00 10.65           O  
ANISOU  511  O   TYR A 111     1167   1842   1038     96     20   -224       O  
ATOM    512  CB  TYR A 111      -9.788  -0.440  -6.851  1.00 10.21           C  
ANISOU  512  CB  TYR A 111     1031   1662   1185    190    509   -367       C  
ATOM    513  CG  TYR A 111      -8.814  -0.425  -5.701  1.00 12.39           C  
ANISOU  513  CG  TYR A 111     1271   2065   1373    361    241   -453       C  
ATOM    514  CD1 TYR A 111      -8.820  -1.435  -4.747  1.00 13.58           C  
ANISOU  514  CD1 TYR A 111     1317   2189   1655    750    200   -360       C  
ATOM    515  CD2 TYR A 111      -7.884   0.598  -5.569  1.00 14.26           C  
ANISOU  515  CD2 TYR A 111     1511   2086   1821     16     31   -594       C  
ATOM    516  CE1 TYR A 111      -7.928  -1.424  -3.690  1.00 14.85           C  
ANISOU  516  CE1 TYR A 111     1428   2624   1593    392    275   -324       C  
ATOM    517  CE2 TYR A 111      -6.989   0.617  -4.516  1.00 15.39           C  
ANISOU  517  CE2 TYR A 111     1488   2439   1920    244   -238   -387       C  
ATOM    518  CZ  TYR A 111      -7.015  -0.395  -3.581  1.00 16.04           C  
ANISOU  518  CZ  TYR A 111     1775   2584   1735    201      8   -457       C  
ATOM    519  OH  TYR A 111      -6.123  -0.381  -2.533  1.00 19.47           O  
ANISOU  519  OH  TYR A 111     2383   3103   1910     26   -173   -533       O  
ATOM    520  N   TYR A 112     -11.930   1.455  -8.512  1.00  8.99           N  
ANISOU  520  N   TYR A 112     1047   1633    734   -217     -9    236       N  
ATOM    521  CA  TYR A 112     -12.633   1.549  -9.783  1.00  7.09           C  
ANISOU  521  CA  TYR A 112      768   1021    903    514     75    124       C  
ATOM    522  C   TYR A 112     -12.000   0.614 -10.807  1.00  9.22           C  
ANISOU  522  C   TYR A 112     1167   1587    748    615    253    -30       C  
ATOM    523  O   TYR A 112     -10.798   0.332 -10.768  1.00 10.40           O  
ANISOU  523  O   TYR A 112     1381   1810    761    705    155   -161       O  
ATOM    524  CB  TYR A 112     -12.628   2.990 -10.294  1.00  7.64           C  
ANISOU  524  CB  TYR A 112      549   1280   1075    335    203     51       C  
ATOM    525  CG  TYR A 112     -13.583   3.885  -9.533  1.00 10.02           C  
ANISOU  525  CG  TYR A 112     1224   1240   1342    499    322     26       C  
ATOM    526  CD1 TYR A 112     -14.941   3.884  -9.826  1.00  9.51           C  
ANISOU  526  CD1 TYR A 112     1005   1314   1293    655    181     20       C  
ATOM    527  CD2 TYR A 112     -13.132   4.714  -8.513  1.00 10.01           C  
ANISOU  527  CD2 TYR A 112     1478   1004   1321   -114    371   -167       C  
ATOM    528  CE1 TYR A 112     -15.821   4.691  -9.134  1.00  9.80           C  
ANISOU  528  CE1 TYR A 112     1474   1050   1199    432    455    -37       C  
ATOM    529  CE2 TYR A 112     -14.008   5.527  -7.814  1.00 10.53           C  
ANISOU  529  CE2 TYR A 112     1332   1279   1392     39    312    154       C  
ATOM    530  CZ  TYR A 112     -15.350   5.509  -8.129  1.00 10.45           C  
ANISOU  530  CZ  TYR A 112     1652    968   1351    218    417    -57       C  
ATOM    531  OH  TYR A 112     -16.228   6.310  -7.442  1.00 10.86           O  
ANISOU  531  OH  TYR A 112     1828    912   1387    -39    350   -465       O  
ATOM    532  N   LEU A 113     -12.839   0.108 -11.711  1.00  6.84           N  
ANISOU  532  N   LEU A 113      812   1043    743    419    230   -101       N  
ATOM    533  CA  LEU A 113     -12.387  -0.786 -12.770  1.00  9.66           C  
ANISOU  533  CA  LEU A 113     1481   1275    913     64    229   -406       C  
ATOM    534  C   LEU A 113     -11.187  -0.201 -13.503  1.00 12.15           C  
ANISOU  534  C   LEU A 113     1588   2064    965    179    267   -249       C  
ATOM    535  O   LEU A 113     -11.175   0.980 -13.865  1.00 11.79           O  
ANISOU  535  O   LEU A 113     1567   1868   1044    -68    436    -69       O  
ATOM    536  CB  LEU A 113     -13.535  -1.043 -13.749  1.00  9.20           C  
ANISOU  536  CB  LEU A 113     1470   1077    949    261     84   -212       C  
ATOM    537  CG  LEU A 113     -13.241  -1.883 -14.993  1.00 10.27           C  
ANISOU  537  CG  LEU A 113     1730    907   1266    621    -82   -251       C  
ATOM    538  CD1 LEU A 113     -12.886  -3.317 -14.617  1.00 14.21           C  
ANISOU  538  CD1 LEU A 113     2372   1185   1842    836    -47   -277       C  
ATOM    539  CD2 LEU A 113     -14.430  -1.847 -15.945  1.00 11.90           C  
ANISOU  539  CD2 LEU A 113     2198   1221   1103    701    -19   -319       C  
ATOM    540  N   GLY A 114     -10.167  -1.032 -13.701  1.00 13.50           N  
ANISOU  540  N   GLY A 114     1862   2139   1129    258   -281   -419       N  
ATOM    541  CA  GLY A 114      -8.968  -0.604 -14.393  1.00 14.69           C  
ANISOU  541  CA  GLY A 114     1741   2401   1438    131   -346    -89       C  
ATOM    542  C   GLY A 114      -7.990   0.196 -13.563  1.00 16.17           C  
ANISOU  542  C   GLY A 114     2049   2290   1803   -105   -145    -81       C  
ATOM    543  O   GLY A 114      -7.026   0.734 -14.121  1.00 18.45           O  
ANISOU  543  O   GLY A 114     2501   2350   2158    -81   -217     22       O  
ATOM    544  N   THR A 115      -8.207   0.298 -12.255  1.00 12.67           N  
ANISOU  544  N   THR A 115     1480   1817   1518    133    -34    -12       N  
ATOM    545  CA  THR A 115      -7.319   1.008 -11.346  1.00 11.75           C  
ANISOU  545  CA  THR A 115     1314   1656   1494    -71    366   -177       C  
ATOM    546  C   THR A 115      -6.881   0.075 -10.224  1.00 11.65           C  
ANISOU  546  C   THR A 115     1294   1492   1639    238    -41   -216       C  
ATOM    547  O   THR A 115      -7.424  -1.017 -10.043  1.00 13.95           O  
ANISOU  547  O   THR A 115     1832   1730   1738   -119    113   -194       O  
ATOM    548  CB  THR A 115      -8.003   2.245 -10.745  1.00 12.55           C  
ANISOU  548  CB  THR A 115     1554   1881   1334    141    408    -83       C  
ATOM    549  OG1 THR A 115      -8.891   1.834  -9.699  1.00 13.10           O  
ANISOU  549  OG1 THR A 115     1685   1886   1407   -187    487   -138       O  
ATOM    550  CG2 THR A 115      -8.799   2.999 -11.805  1.00 13.37           C  
ANISOU  550  CG2 THR A 115     1629   1929   1522    578   -174   -368       C  
ATOM    551  N   GLY A 116      -5.888   0.524  -9.462  1.00 14.95           N  
ANISOU  551  N   GLY A 116     1555   1950   2173    108    -86    -45       N  
ATOM    552  CA  GLY A 116      -5.502  -0.143  -8.240  1.00 15.79           C  
ANISOU  552  CA  GLY A 116     1609   2143   2246    234    314     83       C  
ATOM    553  C   GLY A 116      -4.647  -1.379  -8.444  1.00 17.88           C  
ANISOU  553  C   GLY A 116     1271   2934   2589    510    594    145       C  
ATOM    554  O   GLY A 116      -4.070  -1.601  -9.513  1.00 18.40           O  
ANISOU  554  O   GLY A 116     1387   3040   2562   -108    961    297       O  
ATOM    555  N   PRO A 117      -4.562  -2.214  -7.403  1.00 18.55           N  
ANISOU  555  N   PRO A 117     1633   2801   2614   1038     57    -38       N  
ATOM    556  CA  PRO A 117      -3.672  -3.388  -7.466  1.00 20.16           C  
ANISOU  556  CA  PRO A 117     1969   3075   2617   1050   -346   -296       C  
ATOM    557  C   PRO A 117      -4.033  -4.377  -8.558  1.00 20.95           C  
ANISOU  557  C   PRO A 117     1977   3152   2831   1019   -168   -328       C  
ATOM    558  O   PRO A 117      -3.143  -5.055  -9.086  1.00 23.33           O  
ANISOU  558  O   PRO A 117     2270   3500   3097   1006    -96   -721       O  
ATOM    559  CB  PRO A 117      -3.825  -4.017  -6.072  1.00 21.15           C  
ANISOU  559  CB  PRO A 117     2091   3256   2690   1025   -617   -415       C  
ATOM    560  CG  PRO A 117      -4.354  -2.924  -5.206  1.00 21.04           C  
ANISOU  560  CG  PRO A 117     1970   3319   2705   1331   -558   -246       C  
ATOM    561  CD  PRO A 117      -5.213  -2.079  -6.091  1.00 19.32           C  
ANISOU  561  CD  PRO A 117     1714   3182   2444   1115   -499     42       C  
ATOM    562  N   GLU A 118      -5.311  -4.497  -8.904  1.00 19.10           N  
ANISOU  562  N   GLU A 118     1446   3176   2635    997   -329   -176       N  
ATOM    563  CA  GLU A 118      -5.758  -5.385  -9.971  1.00 20.58           C  
ANISOU  563  CA  GLU A 118     1863   3324   2632    969     51   -140       C  
ATOM    564  C   GLU A 118      -6.255  -4.591 -11.175  1.00 20.44           C  
ANISOU  564  C   GLU A 118     1962   3542   2262   1294    386   -232       C  
ATOM    565  O   GLU A 118      -7.281  -4.917 -11.776  1.00 21.32           O  
ANISOU  565  O   GLU A 118     2300   3714   2085   1166    433   -672       O  
ATOM    566  CB  GLU A 118      -6.840  -6.335  -9.467  1.00 21.04           C  
ANISOU  566  CB  GLU A 118     2032   2995   2969    711     47    -81       C  
ATOM    567  CG  GLU A 118      -6.406  -7.220  -8.306  1.00 23.44           C  
ANISOU  567  CG  GLU A 118     2491   3108   3308    635    -92     10       C  
ATOM    568  CD  GLU A 118      -5.369  -8.260  -8.701  1.00 30.70           C  
ANISOU  568  CD  GLU A 118     3714   4126   3823     90   -583    269       C  
ATOM    569  OE1 GLU A 118      -5.114  -8.437  -9.913  1.00 33.77           O  
ANISOU  569  OE1 GLU A 118     4315   4362   4154    234   -622     56       O  
ATOM    570  OE2 GLU A 118      -4.808  -8.908  -7.792  1.00 32.83           O  
ANISOU  570  OE2 GLU A 118     3866   4542   4064   -134   -650    585       O  
ATOM    571  N   ALA A 119      -5.520  -3.534 -11.539  1.00 20.48           N  
ANISOU  571  N   ALA A 119     2249   3488   2044   1056    386    -69       N  
ATOM    572  CA  ALA A 119      -5.923  -2.692 -12.660  1.00 19.41           C  
ANISOU  572  CA  ALA A 119     2622   3098   1653    628    351    -91       C  
ATOM    573  C   ALA A 119      -5.993  -3.477 -13.963  1.00 20.69           C  
ANISOU  573  C   ALA A 119     2888   3355   1619    879    194   -151       C  
ATOM    574  O   ALA A 119      -6.770  -3.126 -14.857  1.00 19.60           O  
ANISOU  574  O   ALA A 119     2867   3374   1205   1252   -145   -162       O  
ATOM    575  CB  ALA A 119      -4.960  -1.514 -12.804  1.00 20.61           C  
ANISOU  575  CB  ALA A 119     3204   3084   1543    615    480    -10       C  
ATOM    576  N   GLY A 120      -5.198  -4.537 -14.088  1.00 22.56           N  
ANISOU  576  N   GLY A 120     3144   3487   1942    893    319   -448       N  
ATOM    577  CA  GLY A 120      -5.198  -5.350 -15.287  1.00 23.50           C  
ANISOU  577  CA  GLY A 120     3358   3417   2154    704    667   -812       C  
ATOM    578  C   GLY A 120      -6.233  -6.449 -15.334  1.00 23.82           C  
ANISOU  578  C   GLY A 120     3229   3545   2279    753    832   -680       C  
ATOM    579  O   GLY A 120      -6.359  -7.122 -16.361  1.00 25.56           O  
ANISOU  579  O   GLY A 120     3562   3833   2318    717   1329   -665       O  
ATOM    580  N   LEU A 121      -6.973  -6.656 -14.253  1.00 22.68           N  
ANISOU  580  N   LEU A 121     3032   3239   2347    869    637   -327       N  
ATOM    581  CA  LEU A 121      -8.005  -7.686 -14.246  1.00 23.33           C  
ANISOU  581  CA  LEU A 121     3275   3118   2470    882    624   -506       C  
ATOM    582  C   LEU A 121      -9.217  -7.220 -15.044  1.00 22.10           C  
ANISOU  582  C   LEU A 121     2800   3139   2457    866    560   -865       C  
ATOM    583  O   LEU A 121      -9.755  -6.140 -14.770  1.00 23.79           O  
ANISOU  583  O   LEU A 121     2970   3411   2658   1078    598  -1001       O  
ATOM    584  CB  LEU A 121      -8.429  -8.022 -12.817  1.00 24.04           C  
ANISOU  584  CB  LEU A 121     3781   3036   2317    873    912   -422       C  
ATOM    585  CG  LEU A 121      -7.667  -9.118 -12.072  1.00 26.81           C  
ANISOU  585  CG  LEU A 121     4665   2982   2540    758   1205   -440       C  
ATOM    586  CD1 LEU A 121      -8.330  -9.409 -10.732  1.00 26.21           C  
ANISOU  586  CD1 LEU A 121     4706   2656   2597    408   1538   -405       C  
ATOM    587  CD2 LEU A 121      -7.591 -10.375 -12.914  1.00 28.26           C  
ANISOU  587  CD2 LEU A 121     5175   2902   2659    510    915   -551       C  
ATOM    588  N   PRO A 122      -9.677  -7.993 -16.026  1.00 19.97           N  
ANISOU  588  N   PRO A 122     2512   3016   2059    611    698   -984       N  
ATOM    589  CA  PRO A 122     -10.932  -7.652 -16.700  1.00 19.31           C  
ANISOU  589  CA  PRO A 122     2513   2896   1928    558    559  -1036       C  
ATOM    590  C   PRO A 122     -12.106  -7.815 -15.751  1.00 18.97           C  
ANISOU  590  C   PRO A 122     2656   2672   1882    746    440   -958       C  
ATOM    591  O   PRO A 122     -12.066  -8.615 -14.813  1.00 19.69           O  
ANISOU  591  O   PRO A 122     2710   2845   1925    589    252   -870       O  
ATOM    592  CB  PRO A 122     -11.010  -8.661 -17.855  1.00 18.19           C  
ANISOU  592  CB  PRO A 122     2213   2886   1811    256    497  -1096       C  
ATOM    593  CG  PRO A 122      -9.649  -9.305 -17.929  1.00 20.80           C  
ANISOU  593  CG  PRO A 122     2713   3164   2026     91    194  -1068       C  
ATOM    594  CD  PRO A 122      -9.089  -9.236 -16.547  1.00 20.46           C  
ANISOU  594  CD  PRO A 122     2732   3052   1989    432    594  -1059       C  
ATOM    595  N   TYR A 123     -13.161  -7.042 -16.003  1.00 17.85           N  
ANISOU  595  N   TYR A 123     2660   2060   2062    712    388   -931       N  
ATOM    596  CA  TYR A 123     -14.347  -7.118 -15.161  1.00 16.90           C  
ANISOU  596  CA  TYR A 123     2698   1522   2202    447    362   -820       C  
ATOM    597  C   TYR A 123     -14.904  -8.535 -15.160  1.00 17.91           C  
ANISOU  597  C   TYR A 123     3127   1430   2248    100    120   -381       C  
ATOM    598  O   TYR A 123     -15.048  -9.161 -16.214  1.00 20.29           O  
ANISOU  598  O   TYR A 123     3500   1988   2222   -110    395   -202       O  
ATOM    599  CB  TYR A 123     -15.417  -6.139 -15.641  1.00 18.64           C  
ANISOU  599  CB  TYR A 123     2877   1610   2595    178    560  -1012       C  
ATOM    600  CG  TYR A 123     -16.651  -6.148 -14.767  1.00 20.70           C  
ANISOU  600  CG  TYR A 123     2842   1895   3128    229    552   -538       C  
ATOM    601  CD1 TYR A 123     -16.663  -5.479 -13.552  1.00 22.36           C  
ANISOU  601  CD1 TYR A 123     3067   2259   3171    540    489     22       C  
ATOM    602  CD2 TYR A 123     -17.798  -6.835 -15.148  1.00 22.66           C  
ANISOU  602  CD2 TYR A 123     3098   2130   3382   -249    614   -691       C  
ATOM    603  CE1 TYR A 123     -17.780  -5.485 -12.742  1.00 24.30           C  
ANISOU  603  CE1 TYR A 123     3244   2432   3559    531    524    147       C  
ATOM    604  CE2 TYR A 123     -18.925  -6.847 -14.340  1.00 23.62           C  
ANISOU  604  CE2 TYR A 123     3315   2011   3647    -31    647   -654       C  
ATOM    605  CZ  TYR A 123     -18.908  -6.169 -13.138  1.00 25.88           C  
ANISOU  605  CZ  TYR A 123     3503   2383   3946    455    732    -33       C  
ATOM    606  OH  TYR A 123     -20.018  -6.170 -12.322  1.00 30.23           O  
ANISOU  606  OH  TYR A 123     4357   2549   4580    731    743     38       O  
ATOM    607  N   GLY A 124     -15.210  -9.042 -13.967  1.00 17.41           N  
ANISOU  607  N   GLY A 124     3118   1354   2144    122    -23   -314       N  
ATOM    608  CA  GLY A 124     -15.734 -10.381 -13.814  1.00 17.41           C  
ANISOU  608  CA  GLY A 124     3238   1230   2147      3     97   -107       C  
ATOM    609  C   GLY A 124     -14.694 -11.474 -13.704  1.00 19.28           C  
ANISOU  609  C   GLY A 124     3550   1639   2138     73     40    -63       C  
ATOM    610  O   GLY A 124     -15.068 -12.646 -13.564  1.00 22.79           O  
ANISOU  610  O   GLY A 124     4313   2015   2333    523      3   -196       O  
ATOM    611  N   ALA A 125     -13.409 -11.137 -13.764  1.00 19.80           N  
ANISOU  611  N   ALA A 125     3436   1832   2256    551     27    126       N  
ATOM    612  CA  ALA A 125     -12.366 -12.147 -13.662  1.00 21.98           C  
ANISOU  612  CA  ALA A 125     3610   2138   2604    918    129     -5       C  
ATOM    613  C   ALA A 125     -12.392 -12.802 -12.288  1.00 22.57           C  
ANISOU  613  C   ALA A 125     3711   2029   2834   1224    -55   -277       C  
ATOM    614  O   ALA A 125     -12.611 -12.141 -11.269  1.00 21.38           O  
ANISOU  614  O   ALA A 125     3434   2061   2627   1296     80   -599       O  
ATOM    615  CB  ALA A 125     -10.994 -11.528 -13.924  1.00 23.22           C  
ANISOU  615  CB  ALA A 125     3579   2530   2715   1100    394     81       C  
ATOM    616  N   ASN A 126     -12.167 -14.112 -12.265  1.00 23.84           N  
ANISOU  616  N   ASN A 126     3891   2008   3160   1155   -117     61       N  
ATOM    617  CA  ASN A 126     -12.209 -14.886 -11.032  1.00 26.33           C  
ANISOU  617  CA  ASN A 126     4113   2502   3388   1262   -172     -6       C  
ATOM    618  C   ASN A 126     -10.837 -14.861 -10.369  1.00 26.65           C  
ANISOU  618  C   ASN A 126     4258   2717   3149   1305     99   -198       C  
ATOM    619  O   ASN A 126      -9.844 -15.290 -10.967  1.00 28.79           O  
ANISOU  619  O   ASN A 126     4468   3351   3121   1207     75   -371       O  
ATOM    620  CB  ASN A 126     -12.647 -16.322 -11.319  1.00 30.24           C  
ANISOU  620  CB  ASN A 126     4595   2990   3905   1018   -197    -56       C  
ATOM    621  CG  ASN A 126     -12.808 -17.146 -10.059  1.00 37.11           C  
ANISOU  621  CG  ASN A 126     5265   4260   4576    595    142   -277       C  
ATOM    622  OD1 ASN A 126     -13.011 -16.606  -8.971  1.00 41.19           O  
ANISOU  622  OD1 ASN A 126     5657   5031   4962    683    131    -72       O  
ATOM    623  ND2 ASN A 126     -12.719 -18.464 -10.199  1.00 40.44           N  
ANISOU  623  ND2 ASN A 126     5509   5030   4825    407    281   -178       N  
ATOM    624  N   LYS A 127     -10.784 -14.354  -9.139  1.00 24.07           N  
ANISOU  624  N   LYS A 127     3985   2314   2845   1369    266   -233       N  
ATOM    625  CA  LYS A 127      -9.552 -14.338  -8.365  1.00 24.48           C  
ANISOU  625  CA  LYS A 127     3949   2375   2976   1139    386   -245       C  
ATOM    626  C   LYS A 127      -9.911 -14.266  -6.888  1.00 23.11           C  
ANISOU  626  C   LYS A 127     3833   2086   2862   1183    100     -7       C  
ATOM    627  O   LYS A 127     -10.788 -13.490  -6.498  1.00 22.85           O  
ANISOU  627  O   LYS A 127     3871   1958   2853   1395    -45   -395       O  
ATOM    628  CB  LYS A 127      -8.655 -13.158  -8.758  1.00 25.85           C  
ANISOU  628  CB  LYS A 127     3966   2629   3228   1215    501   -271       C  
ATOM    629  CG  LYS A 127      -7.311 -13.148  -8.048  1.00 27.56           C  
ANISOU  629  CG  LYS A 127     3855   3080   3537    856    344   -292       C  
ATOM    630  CD  LYS A 127      -6.358 -12.140  -8.664  1.00 28.49           C  
ANISOU  630  CD  LYS A 127     3681   3328   3815    297    341   -132       C  
ATOM    631  CE  LYS A 127      -4.976 -12.252  -8.044  1.00 31.22           C  
ANISOU  631  CE  LYS A 127     3875   3811   4178    103    465    162       C  
ATOM    632  NZ  LYS A 127      -4.007 -11.315  -8.674  1.00 33.37           N  
ANISOU  632  NZ  LYS A 127     4164   4064   4452    -61    547    328       N  
ATOM    633  N   ASP A 128      -9.235 -15.078  -6.076  1.00 22.40           N  
ANISOU  633  N   ASP A 128     3789   1914   2806   1065   -222    120       N  
ATOM    634  CA  ASP A 128      -9.539 -15.117  -4.652  1.00 25.12           C  
ANISOU  634  CA  ASP A 128     4148   2428   2970   1190   -804    334       C  
ATOM    635  C   ASP A 128      -9.227 -13.774  -4.006  1.00 21.99           C  
ANISOU  635  C   ASP A 128     3423   2164   2767    826   -445    117       C  
ATOM    636  O   ASP A 128      -8.174 -13.179  -4.254  1.00 21.37           O  
ANISOU  636  O   ASP A 128     3118   2262   2740    358    -55     62       O  
ATOM    637  CB  ASP A 128      -8.749 -16.232  -3.968  1.00 30.90           C  
ANISOU  637  CB  ASP A 128     4845   3460   3435   1403   -956    505       C  
ATOM    638  CG  ASP A 128      -9.105 -16.380  -2.500  1.00 38.86           C  
ANISOU  638  CG  ASP A 128     5782   4727   4254    856  -1040    483       C  
ATOM    639  OD1 ASP A 128     -10.260 -16.757  -2.202  1.00 41.86           O  
ANISOU  639  OD1 ASP A 128     6055   5271   4579    763  -1028    486       O  
ATOM    640  OD2 ASP A 128      -8.233 -16.117  -1.644  1.00 41.05           O  
ANISOU  640  OD2 ASP A 128     6081   5094   4422    649  -1096    449       O  
ATOM    641  N   GLY A 129     -10.152 -13.295  -3.176  1.00 18.96           N  
ANISOU  641  N   GLY A 129     2786   1887   2532    889    -80     71       N  
ATOM    642  CA  GLY A 129     -10.020 -11.999  -2.549  1.00 17.67           C  
ANISOU  642  CA  GLY A 129     2501   1745   2467    687     88     64       C  
ATOM    643  C   GLY A 129     -10.516 -10.836  -3.379  1.00 17.60           C  
ANISOU  643  C   GLY A 129     2568   1997   2121    531    109    158       C  
ATOM    644  O   GLY A 129     -10.392  -9.686  -2.939  1.00 17.94           O  
ANISOU  644  O   GLY A 129     2690   1994   2130    267    304    -82       O  
ATOM    645  N   ILE A 130     -11.072 -11.095  -4.560  1.00 16.93           N  
ANISOU  645  N   ILE A 130     2499   2077   1855    734    -34    116       N  
ATOM    646  CA  ILE A 130     -11.585 -10.064  -5.454  1.00 15.13           C  
ANISOU  646  CA  ILE A 130     2003   1834   1911    548    165    329       C  
ATOM    647  C   ILE A 130     -13.051 -10.363  -5.727  1.00 13.58           C  
ANISOU  647  C   ILE A 130     1543   1759   1859    470     16    342       C  
ATOM    648  O   ILE A 130     -13.395 -11.486  -6.114  1.00 14.14           O  
ANISOU  648  O   ILE A 130     1105   1907   2359    114    142   -147       O  
ATOM    649  CB  ILE A 130     -10.792 -10.014  -6.774  1.00 14.90           C  
ANISOU  649  CB  ILE A 130     1998   1448   2214    398    144    445       C  
ATOM    650  CG1 ILE A 130      -9.303  -9.776  -6.507  1.00 15.09           C  
ANISOU  650  CG1 ILE A 130     1846   1424   2466    129    263    205       C  
ATOM    651  CG2 ILE A 130     -11.360  -8.951  -7.705  1.00 13.92           C  
ANISOU  651  CG2 ILE A 130     1863   1036   2391     86    114    352       C  
ATOM    652  CD1 ILE A 130      -8.998  -8.424  -5.910  1.00 16.10           C  
ANISOU  652  CD1 ILE A 130     2406   1185   2526    -58    141    173       C  
ATOM    653  N   ILE A 131     -13.911  -9.366  -5.523  1.00 12.12           N  
ANISOU  653  N   ILE A 131     1849   1296   1461    340    215    177       N  
ATOM    654  CA  ILE A 131     -15.313  -9.455  -5.911  1.00 12.06           C  
ANISOU  654  CA  ILE A 131     1697   1209   1677    319    345    149       C  
ATOM    655  C   ILE A 131     -15.662  -8.221  -6.730  1.00 13.05           C  
ANISOU  655  C   ILE A 131     1405   1688   1867    457    148   -236       C  
ATOM    656  O   ILE A 131     -15.096  -7.142  -6.533  1.00 13.63           O  
ANISOU  656  O   ILE A 131     1331   1799   2049    -99    250     61       O  
ATOM    657  CB  ILE A 131     -16.255  -9.596  -4.694  1.00 14.13           C  
ANISOU  657  CB  ILE A 131     2195   1128   2047    324    551   -188       C  
ATOM    658  CG1 ILE A 131     -16.064  -8.432  -3.723  1.00 15.08           C  
ANISOU  658  CG1 ILE A 131     2150   1336   2246    230    425   -609       C  
ATOM    659  CG2 ILE A 131     -16.028 -10.930  -3.996  1.00 16.56           C  
ANISOU  659  CG2 ILE A 131     2724   1277   2291    -84    660   -305       C  
ATOM    660  CD1 ILE A 131     -17.251  -7.502  -3.660  1.00 18.31           C  
ANISOU  660  CD1 ILE A 131     2471   1938   2549    460    111   -481       C  
ATOM    661  N   TRP A 132     -16.598  -8.387  -7.661  1.00 12.11           N  
ANISOU  661  N   TRP A 132     1239   1725   1639    179    -95   -345       N  
ATOM    662  CA  TRP A 132     -16.925  -7.357  -8.638  1.00 11.30           C  
ANISOU  662  CA  TRP A 132     1412   1452   1431    -53   -229   -204       C  
ATOM    663  C   TRP A 132     -18.286  -6.740  -8.347  1.00 12.32           C  
ANISOU  663  C   TRP A 132     1534   1376   1770   -173   -361    -18       C  
ATOM    664  O   TRP A 132     -19.214  -7.432  -7.915  1.00 13.39           O  
ANISOU  664  O   TRP A 132     1402   1405   2279   -465   -543    -16       O  
ATOM    665  CB  TRP A 132     -16.905  -7.936 -10.054  1.00 14.26           C  
ANISOU  665  CB  TRP A 132     2034   1808   1575    500    -35   -242       C  
ATOM    666  CG  TRP A 132     -15.544  -8.374 -10.471  1.00 14.73           C  
ANISOU  666  CG  TRP A 132     2242   1891   1464    770    109   -534       C  
ATOM    667  CD1 TRP A 132     -15.044  -9.643 -10.444  1.00 14.47           C  
ANISOU  667  CD1 TRP A 132     2072   1858   1567   1062    201   -270       C  
ATOM    668  CD2 TRP A 132     -14.492  -7.536 -10.957  1.00 15.47           C  
ANISOU  668  CD2 TRP A 132     2517   2015   1348    575    251   -403       C  
ATOM    669  NE1 TRP A 132     -13.746  -9.648 -10.896  1.00 16.96           N  
ANISOU  669  NE1 TRP A 132     2470   2195   1781    780     38   -232       N  
ATOM    670  CE2 TRP A 132     -13.384  -8.366 -11.217  1.00 17.18           C  
ANISOU  670  CE2 TRP A 132     2698   2262   1568    305     15   -255       C  
ATOM    671  CE3 TRP A 132     -14.380  -6.164 -11.203  1.00 15.60           C  
ANISOU  671  CE3 TRP A 132     2457   2208   1264     68    167   -467       C  
ATOM    672  CZ2 TRP A 132     -12.181  -7.869 -11.711  1.00 17.52           C  
ANISOU  672  CZ2 TRP A 132     2762   2479   1416     90   -106   -470       C  
ATOM    673  CZ3 TRP A 132     -13.188  -5.673 -11.694  1.00 15.88           C  
ANISOU  673  CZ3 TRP A 132     2434   2522   1079    -69    156   -362       C  
ATOM    674  CH2 TRP A 132     -12.103  -6.523 -11.944  1.00 17.01           C  
ANISOU  674  CH2 TRP A 132     2702   2400   1360     77   -175   -443       C  
ATOM    675  N   VAL A 133     -18.394  -5.430  -8.585  1.00 11.21           N  
ANISOU  675  N   VAL A 133     1484   1229   1546     48   -209   -171       N  
ATOM    676  CA  VAL A 133     -19.640  -4.691  -8.423  1.00 11.68           C  
ANISOU  676  CA  VAL A 133     1779   1473   1186    -25     11   -388       C  
ATOM    677  C   VAL A 133     -19.797  -3.729  -9.594  1.00 12.55           C  
ANISOU  677  C   VAL A 133     1581   1783   1405    115    -16   -268       C  
ATOM    678  O   VAL A 133     -18.813  -3.223 -10.146  1.00 12.04           O  
ANISOU  678  O   VAL A 133     1378   1919   1278    -47    -29     -8       O  
ATOM    679  CB  VAL A 133     -19.696  -3.917  -7.082  1.00 11.35           C  
ANISOU  679  CB  VAL A 133     1908   1529    877   -580    213   -187       C  
ATOM    680  CG1 VAL A 133     -19.733  -4.873  -5.898  1.00 11.12           C  
ANISOU  680  CG1 VAL A 133     1896   1188   1142   -332    379    460       C  
ATOM    681  CG2 VAL A 133     -18.518  -2.959  -6.969  1.00 11.53           C  
ANISOU  681  CG2 VAL A 133     1634   1629   1119   -872     20   -310       C  
ATOM    682  N   ALA A 134     -21.049  -3.481  -9.976  1.00 10.87           N  
ANISOU  682  N   ALA A 134     1297   1504   1329    258   -109    -12       N  
ATOM    683  CA  ALA A 134     -21.346  -2.523 -11.034  1.00 13.49           C  
ANISOU  683  CA  ALA A 134     1696   1799   1631    355    157    -67       C  
ATOM    684  C   ALA A 134     -22.788  -2.064 -10.900  1.00 13.04           C  
ANISOU  684  C   ALA A 134     1511   1494   1952    227    343      7       C  
ATOM    685  O   ALA A 134     -23.688  -2.888 -10.715  1.00 15.94           O  
ANISOU  685  O   ALA A 134     2089   1770   2199    224    351    132       O  
ATOM    686  CB  ALA A 134     -21.110  -3.129 -12.423  1.00 15.06           C  
ANISOU  686  CB  ALA A 134     2276   1911   1535    237    125    -92       C  
ATOM    687  N   THR A 135     -22.999  -0.755 -10.992  1.00 10.22           N  
ANISOU  687  N   THR A 135      938   1266   1680    629    109    -71       N  
ATOM    688  CA  THR A 135     -24.337  -0.190 -11.011  1.00 10.80           C  
ANISOU  688  CA  THR A 135     1022   1344   1737     -8     35   -382       C  
ATOM    689  C   THR A 135     -24.901  -0.252 -12.426  1.00 13.10           C  
ANISOU  689  C   THR A 135     1252   1529   2197     71   -115   -133       C  
ATOM    690  O   THR A 135     -24.157  -0.257 -13.410  1.00 12.14           O  
ANISOU  690  O   THR A 135      985   1538   2088   -344    -82   -264       O  
ATOM    691  CB  THR A 135     -24.307   1.258 -10.512  1.00 12.33           C  
ANISOU  691  CB  THR A 135     1219   1636   1830    -72    204   -293       C  
ATOM    692  OG1 THR A 135     -23.631   1.311  -9.249  1.00 12.70           O  
ANISOU  692  OG1 THR A 135     1233   2068   1526   -354    301   -191       O  
ATOM    693  CG2 THR A 135     -25.714   1.827 -10.346  1.00 15.10           C  
ANISOU  693  CG2 THR A 135     1916   1825   1999    116   -191     56       C  
ATOM    694  N   GLU A 136     -26.228  -0.333 -12.517  1.00 13.62           N  
ANISOU  694  N   GLU A 136     1049   1770   2357    335   -442   -244       N  
ATOM    695  CA  GLU A 136     -26.904  -0.262 -13.805  1.00 18.05           C  
ANISOU  695  CA  GLU A 136     1946   2340   2572    217   -609    -94       C  
ATOM    696  C   GLU A 136     -26.443   0.966 -14.578  1.00 17.81           C  
ANISOU  696  C   GLU A 136     1936   2361   2471      5   -506     43       C  
ATOM    697  O   GLU A 136     -26.397   2.074 -14.038  1.00 17.49           O  
ANISOU  697  O   GLU A 136     1973   2350   2323   -513   -828   -118       O  
ATOM    698  CB  GLU A 136     -28.419  -0.220 -13.593  1.00 23.02           C  
ANISOU  698  CB  GLU A 136     2680   3120   2949    -62   -738     -6       C  
ATOM    699  CG  GLU A 136     -29.237  -0.316 -14.869  1.00 30.86           C  
ANISOU  699  CG  GLU A 136     4049   4054   3621    -79   -447     70       C  
ATOM    700  CD  GLU A 136     -28.993  -1.611 -15.619  1.00 38.66           C  
ANISOU  700  CD  GLU A 136     5342   5117   4232   -247   -143    296       C  
ATOM    701  OE1 GLU A 136     -28.715  -1.552 -16.836  1.00 41.95           O  
ANISOU  701  OE1 GLU A 136     5767   5675   4497   -124    168    322       O  
ATOM    702  OE2 GLU A 136     -29.073  -2.687 -14.989  1.00 41.87           O  
ANISOU  702  OE2 GLU A 136     5830   5573   4507   -345   -350    379       O  
ATOM    703  N   GLY A 137     -26.085   0.760 -15.846  1.00 16.61           N  
ANISOU  703  N   GLY A 137     1642   2325   2344    -19    -93     90       N  
ATOM    704  CA  GLY A 137     -25.643   1.840 -16.701  1.00 15.93           C  
ANISOU  704  CA  GLY A 137     1657   2080   2316   -142    -82    -54       C  
ATOM    705  C   GLY A 137     -24.147   2.070 -16.734  1.00 14.51           C  
ANISOU  705  C   GLY A 137     1781   1761   1972     92   -161     90       C  
ATOM    706  O   GLY A 137     -23.674   2.831 -17.589  1.00 14.53           O  
ANISOU  706  O   GLY A 137     1915   1697   1908    263   -301    396       O  
ATOM    707  N   ALA A 138     -23.389   1.447 -15.837  1.00 11.90           N  
ANISOU  707  N   ALA A 138     1490   1650   1380    540   -393   -203       N  
ATOM    708  CA  ALA A 138     -21.941   1.592 -15.854  1.00 13.02           C  
ANISOU  708  CA  ALA A 138     1607   1891   1451    555   -492     11       C  
ATOM    709  C   ALA A 138     -21.352   0.975 -17.118  1.00 13.58           C  
ANISOU  709  C   ALA A 138     1997   1594   1567    113   -400   -516       C  
ATOM    710  O   ALA A 138     -21.914   0.048 -17.708  1.00 14.81           O  
ANISOU  710  O   ALA A 138     1950   1509   2167   -295   -487   -710       O  
ATOM    711  CB  ALA A 138     -21.322   0.940 -14.620  1.00 12.89           C  
ANISOU  711  CB  ALA A 138     1503   1946   1448    895   -228    246       C  
ATOM    712  N   LEU A 139     -20.200   1.498 -17.530  1.00 11.87           N  
ANISOU  712  N   LEU A 139     2113   1230   1167    192    -51   -491       N  
ATOM    713  CA  LEU A 139     -19.526   1.053 -18.741  1.00 12.43           C  
ANISOU  713  CA  LEU A 139     2297   1217   1208    295    113   -369       C  
ATOM    714  C   LEU A 139     -18.295   0.230 -18.387  1.00 13.44           C  
ANISOU  714  C   LEU A 139     2628   1172   1306   -107     96   -548       C  
ATOM    715  O   LEU A 139     -17.539   0.585 -17.476  1.00 13.91           O  
ANISOU  715  O   LEU A 139     2882    876   1527   -128    173   -341       O  
ATOM    716  CB  LEU A 139     -19.116   2.242 -19.613  1.00 13.56           C  
ANISOU  716  CB  LEU A 139     2384   1519   1251    153     -3      5       C  
ATOM    717  CG  LEU A 139     -20.236   3.153 -20.115  1.00 13.37           C  
ANISOU  717  CG  LEU A 139     2211   1625   1244    236     24    110       C  
ATOM    718  CD1 LEU A 139     -19.683   4.180 -21.092  1.00 11.88           C  
ANISOU  718  CD1 LEU A 139     1915   1388   1211   -353    479    -64       C  
ATOM    719  CD2 LEU A 139     -21.346   2.334 -20.756  1.00 14.89           C  
ANISOU  719  CD2 LEU A 139     2516   2021   1120     80    135    168       C  
ATOM    720  N   ASN A 140     -18.101  -0.867 -19.122  1.00 13.56           N  
ANISOU  720  N   ASN A 140     2460   1347   1346   -169    296   -531       N  
ATOM    721  CA  ASN A 140     -16.939  -1.740 -18.952  1.00 13.66           C  
ANISOU  721  CA  ASN A 140     2690   1383   1118   -113    211   -534       C  
ATOM    722  C   ASN A 140     -15.756  -1.141 -19.716  1.00 14.91           C  
ANISOU  722  C   ASN A 140     2892   1620   1154    -39    485   -503       C  
ATOM    723  O   ASN A 140     -15.353  -1.604 -20.785  1.00 17.50           O  
ANISOU  723  O   ASN A 140     3725   1609   1317    -25    188   -500       O  
ATOM    724  CB  ASN A 140     -17.264  -3.153 -19.421  1.00 13.31           C  
ANISOU  724  CB  ASN A 140     2700   1351   1009   -127   -302   -405       C  
ATOM    725  CG  ASN A 140     -16.166  -4.151 -19.094  1.00 15.21           C  
ANISOU  725  CG  ASN A 140     2913   1612   1257   -306   -481   -486       C  
ATOM    726  OD1 ASN A 140     -15.060  -3.778 -18.700  1.00 17.72           O  
ANISOU  726  OD1 ASN A 140     3206   1960   1568   -527   -388   -691       O  
ATOM    727  ND2 ASN A 140     -16.469  -5.433 -19.264  1.00 16.25           N  
ANISOU  727  ND2 ASN A 140     3375   1445   1356   -300   -275   -473       N  
ATOM    728  N   THR A 141     -15.208  -0.074 -19.143  1.00 13.92           N  
ANISOU  728  N   THR A 141     2885   1421    985   -240    173   -363       N  
ATOM    729  CA  THR A 141     -14.040   0.634 -19.646  1.00 13.60           C  
ANISOU  729  CA  THR A 141     2577   1464   1127    131     62   -211       C  
ATOM    730  C   THR A 141     -13.179   1.030 -18.458  1.00 14.28           C  
ANISOU  730  C   THR A 141     2710   1599   1115   -214    372   -537       C  
ATOM    731  O   THR A 141     -13.707   1.275 -17.367  1.00 15.80           O  
ANISOU  731  O   THR A 141     3069   1465   1471    331    449   -531       O  
ATOM    732  CB  THR A 141     -14.420   1.895 -20.441  1.00 14.73           C  
ANISOU  732  CB  THR A 141     2896   1565   1134    515   -276   -133       C  
ATOM    733  OG1 THR A 141     -15.193   2.773 -19.611  1.00 16.75           O  
ANISOU  733  OG1 THR A 141     3300   1886   1178    451      6   -410       O  
ATOM    734  CG2 THR A 141     -15.220   1.539 -21.688  1.00 16.47           C  
ANISOU  734  CG2 THR A 141     3152   1739   1366    233   -408   -406       C  
ATOM    735  N   PRO A 142     -11.859   1.098 -18.631  1.00 15.19           N  
ANISOU  735  N   PRO A 142     2519   2027   1224   -392    648   -623       N  
ATOM    736  CA  PRO A 142     -10.993   1.448 -17.497  1.00 14.03           C  
ANISOU  736  CA  PRO A 142     2195   1893   1245   -188    706   -583       C  
ATOM    737  C   PRO A 142     -11.218   2.882 -17.043  1.00 13.74           C  
ANISOU  737  C   PRO A 142     2388   1703   1130    286    716   -233       C  
ATOM    738  O   PRO A 142     -11.441   3.785 -17.853  1.00 14.37           O  
ANISOU  738  O   PRO A 142     2706   1392   1362    385    506     19       O  
ATOM    739  CB  PRO A 142      -9.579   1.252 -18.055  1.00 14.76           C  
ANISOU  739  CB  PRO A 142     1920   2286   1403      4    893   -363       C  
ATOM    740  CG  PRO A 142      -9.734   1.421 -19.528  1.00 17.77           C  
ANISOU  740  CG  PRO A 142     2431   2782   1538   -362    935   -565       C  
ATOM    741  CD  PRO A 142     -11.087   0.857 -19.862  1.00 17.07           C  
ANISOU  741  CD  PRO A 142     2487   2406   1594   -343    992   -612       C  
ATOM    742  N   LYS A 143     -11.155   3.083 -15.731  1.00 10.62           N  
ANISOU  742  N   LYS A 143     1617   1272   1145    228    522   -447       N  
ATOM    743  CA  LYS A 143     -11.402   4.394 -15.131  1.00 11.01           C  
ANISOU  743  CA  LYS A 143     1305   1691   1187     59    696   -261       C  
ATOM    744  C   LYS A 143     -10.095   5.099 -14.783  1.00 14.72           C  
ANISOU  744  C   LYS A 143     2002   1920   1672    -74   1078    108       C  
ATOM    745  O   LYS A 143      -9.886   5.553 -13.657  1.00 13.29           O  
ANISOU  745  O   LYS A 143     1700   1555   1796    305   1016    350       O  
ATOM    746  CB  LYS A 143     -12.293   4.245 -13.903  1.00  7.47           C  
ANISOU  746  CB  LYS A 143      685   1253    898     99    446    -50       C  
ATOM    747  CG  LYS A 143     -13.528   3.377 -14.136  1.00  9.19           C  
ANISOU  747  CG  LYS A 143     1007   1384   1102   -345    181   -165       C  
ATOM    748  CD  LYS A 143     -14.296   3.795 -15.391  1.00  8.37           C  
ANISOU  748  CD  LYS A 143     1041   1027   1113   -360   -310   -374       C  
ATOM    749  CE  LYS A 143     -15.556   2.952 -15.566  1.00  8.60           C  
ANISOU  749  CE  LYS A 143     1041   1116   1112     96   -323   -605       C  
ATOM    750  NZ  LYS A 143     -16.121   3.034 -16.944  1.00 11.04           N  
ANISOU  750  NZ  LYS A 143     1451   1380   1365   -136   -156   -786       N  
ATOM    751  N   ASP A 144      -9.201   5.200 -15.772  1.00 17.51           N  
ANISOU  751  N   ASP A 144     2356   2030   2267   -469   1253    125       N  
ATOM    752  CA  ASP A 144      -7.912   5.848 -15.553  1.00 20.32           C  
ANISOU  752  CA  ASP A 144     2663   2437   2619   -164    957   -103       C  
ATOM    753  C   ASP A 144      -8.069   7.311 -15.162  1.00 16.52           C  
ANISOU  753  C   ASP A 144     2241   1831   2204   -160    663     42       C  
ATOM    754  O   ASP A 144      -7.222   7.854 -14.443  1.00 17.89           O  
ANISOU  754  O   ASP A 144     2562   1887   2347     71    239    -65       O  
ATOM    755  CB  ASP A 144      -7.047   5.737 -16.809  1.00 27.71           C  
ANISOU  755  CB  ASP A 144     3679   3247   3602    199   1016   -318       C  
ATOM    756  CG  ASP A 144      -6.769   4.300 -17.201  1.00 34.95           C  
ANISOU  756  CG  ASP A 144     4711   4224   4345     -6    860   -260       C  
ATOM    757  OD1 ASP A 144      -6.437   3.491 -16.310  1.00 38.81           O  
ANISOU  757  OD1 ASP A 144     5183   4669   4895    275    871   -344       O  
ATOM    758  OD2 ASP A 144      -6.887   3.980 -18.401  1.00 38.36           O  
ANISOU  758  OD2 ASP A 144     5099   4759   4715   -344    291   -135       O  
ATOM    759  N   HIS A 145      -9.138   7.969 -15.620  1.00 13.49           N  
ANISOU  759  N   HIS A 145     1806   1536   1782   -128    850     71       N  
ATOM    760  CA  HIS A 145      -9.308   9.381 -15.306  1.00 11.93           C  
ANISOU  760  CA  HIS A 145     1850   1257   1425    228    860   -168       C  
ATOM    761  C   HIS A 145      -9.658   9.607 -13.841  1.00 12.16           C  
ANISOU  761  C   HIS A 145     2076   1191   1355    169    458   -170       C  
ATOM    762  O   HIS A 145      -9.540  10.738 -13.358  1.00 13.36           O  
ANISOU  762  O   HIS A 145     2587   1155   1336   -483    206    149       O  
ATOM    763  CB  HIS A 145     -10.371  10.006 -16.216  1.00 12.84           C  
ANISOU  763  CB  HIS A 145     2243   1285   1349     64    747   -160       C  
ATOM    764  CG  HIS A 145     -11.757   9.489 -15.984  1.00 14.06           C  
ANISOU  764  CG  HIS A 145     2704   1229   1408    144    541   -161       C  
ATOM    765  ND1 HIS A 145     -12.182   8.262 -16.445  1.00 14.80           N  
ANISOU  765  ND1 HIS A 145     2800   1252   1572   -168    441   -230       N  
ATOM    766  CD2 HIS A 145     -12.822  10.044 -15.358  1.00 14.68           C  
ANISOU  766  CD2 HIS A 145     2897   1303   1379    114    544   -141       C  
ATOM    767  CE1 HIS A 145     -13.445   8.078 -16.103  1.00 15.37           C  
ANISOU  767  CE1 HIS A 145     2848   1270   1720     -9    431   -424       C  
ATOM    768  NE2 HIS A 145     -13.858   9.145 -15.445  1.00 14.34           N  
ANISOU  768  NE2 HIS A 145     2852   1129   1469     46    185   -544       N  
ATOM    769  N   ILE A 146     -10.080   8.565 -13.129  1.00 11.23           N  
ANISOU  769  N   ILE A 146     1894   1110   1264    233    392     -3       N  
ATOM    770  CA  ILE A 146     -10.277   8.647 -11.684  1.00 13.03           C  
ANISOU  770  CA  ILE A 146     1958   1478   1516     -8    301    -30       C  
ATOM    771  C   ILE A 146      -9.028   8.209 -10.934  1.00 12.47           C  
ANISOU  771  C   ILE A 146     1908   1240   1591     62    371    -77       C  
ATOM    772  O   ILE A 146      -8.583   8.879  -9.999  1.00 12.92           O  
ANISOU  772  O   ILE A 146     1768   1359   1783   -272    389   -281       O  
ATOM    773  CB  ILE A 146     -11.504   7.808 -11.264  1.00 13.39           C  
ANISOU  773  CB  ILE A 146     2554   1227   1307   -324    149    219       C  
ATOM    774  CG1 ILE A 146     -12.779   8.363 -11.903  1.00 14.25           C  
ANISOU  774  CG1 ILE A 146     2422   1370   1623   -244    349    594       C  
ATOM    775  CG2 ILE A 146     -11.636   7.776  -9.748  1.00 14.08           C  
ANISOU  775  CG2 ILE A 146     2809   1492   1048    108     44     42       C  
ATOM    776  CD1 ILE A 146     -14.041   7.625 -11.511  1.00 15.35           C  
ANISOU  776  CD1 ILE A 146     2507   1520   1803   -258    712    299       C  
ATOM    777  N   GLY A 147      -8.448   7.079 -11.336  1.00 12.35           N  
ANISOU  777  N   GLY A 147     1779   1484   1428    229    609    106       N  
ATOM    778  CA  GLY A 147      -7.232   6.562 -10.745  1.00 13.71           C  
ANISOU  778  CA  GLY A 147     1929   1859   1422    150    259    -60       C  
ATOM    779  C   GLY A 147      -7.410   6.167  -9.286  1.00 14.07           C  
ANISOU  779  C   GLY A 147     1806   2063   1477    278    307   -237       C  
ATOM    780  O   GLY A 147      -8.510   5.885  -8.807  1.00 12.16           O  
ANISOU  780  O   GLY A 147      994   2071   1553     75    473   -192       O  
ATOM    781  N   THR A 148      -6.286   6.150  -8.578  1.00 15.06           N  
ANISOU  781  N   THR A 148     1903   2396   1425    304   -217   -460       N  
ATOM    782  CA  THR A 148      -6.247   5.827  -7.160  1.00 15.93           C  
ANISOU  782  CA  THR A 148     2129   2277   1645    120   -156   -457       C  
ATOM    783  C   THR A 148      -5.937   7.078  -6.349  1.00 17.07           C  
ANISOU  783  C   THR A 148     2429   2467   1591   -296    143   -201       C  
ATOM    784  O   THR A 148      -5.561   8.125  -6.882  1.00 18.30           O  
ANISOU  784  O   THR A 148     2507   2817   1629   -526     74   -169       O  
ATOM    785  CB  THR A 148      -5.209   4.735  -6.874  1.00 18.00           C  
ANISOU  785  CB  THR A 148     2259   2311   2267    -20    -44   -457       C  
ATOM    786  OG1 THR A 148      -3.929   5.146  -7.373  1.00 20.25           O  
ANISOU  786  OG1 THR A 148     2466   2790   2438   -123    100    -58       O  
ATOM    787  CG2 THR A 148      -5.613   3.427  -7.538  1.00 20.34           C  
ANISOU  787  CG2 THR A 148     2158   2914   2658    270      4   -404       C  
ATOM    788  N   ARG A 149      -6.096   6.953  -5.036  1.00 17.11           N  
ANISOU  788  N   ARG A 149     2170   2790   1543   -458    207   -292       N  
ATOM    789  CA  ARG A 149      -5.929   8.076  -4.126  1.00 20.57           C  
ANISOU  789  CA  ARG A 149     2395   3568   1853   -630     35   -562       C  
ATOM    790  C   ARG A 149      -4.482   8.189  -3.670  1.00 25.62           C  
ANISOU  790  C   ARG A 149     2851   4391   2490   -657    189   -417       C  
ATOM    791  O   ARG A 149      -3.839   7.188  -3.344  1.00 28.47           O  
ANISOU  791  O   ARG A 149     3114   4936   2767   -129   -171   -492       O  
ATOM    792  CB  ARG A 149      -6.848   7.917  -2.913  1.00 20.46           C  
ANISOU  792  CB  ARG A 149     2406   3568   1801   -743     32   -767       C  
ATOM    793  CG  ARG A 149      -6.669   8.988  -1.849  1.00 18.26           C  
ANISOU  793  CG  ARG A 149     2318   2958   1664   -703   -172   -922       C  
ATOM    794  CD  ARG A 149      -7.684   8.835  -0.725  1.00 19.09           C  
ANISOU  794  CD  ARG A 149     2696   2733   1825   -971   -409   -751       C  
ATOM    795  NE  ARG A 149      -7.507   7.592   0.020  1.00 18.42           N  
ANISOU  795  NE  ARG A 149     2817   2428   1752   -954   -522   -606       N  
ATOM    796  CZ  ARG A 149      -6.764   7.473   1.116  1.00 20.14           C  
ANISOU  796  CZ  ARG A 149     3235   2600   1818   -574   -154   -329       C  
ATOM    797  NH1 ARG A 149      -6.122   8.526   1.606  1.00 19.84           N  
ANISOU  797  NH1 ARG A 149     3069   2760   1711   -695   -173      2       N  
ATOM    798  NH2 ARG A 149      -6.665   6.299   1.726  1.00 20.66           N  
ANISOU  798  NH2 ARG A 149     3332   2635   1883    -95    100   -221       N  
ATOM    799  N   ASN A 150      -3.971   9.420  -3.658  1.00 27.56           N  
ANISOU  799  N   ASN A 150     2906   4730   2836  -1248    491   -217       N  
ATOM    800  CA  ASN A 150      -2.669   9.702  -3.076  1.00 30.61           C  
ANISOU  800  CA  ASN A 150     2870   5337   3424  -1660    153   -250       C  
ATOM    801  C   ASN A 150      -2.887  10.211  -1.661  1.00 32.18           C  
ANISOU  801  C   ASN A 150     2991   5316   3921  -1707   -212   -613       C  
ATOM    802  O   ASN A 150      -3.445  11.306  -1.489  1.00 30.81           O  
ANISOU  802  O   ASN A 150     2710   5080   3918  -1784    -36  -1116       O  
ATOM    803  CB  ASN A 150      -1.910  10.735  -3.909  1.00 35.37           C  
ANISOU  803  CB  ASN A 150     3388   6213   3838  -1562   -232    -16       C  
ATOM    804  CG  ASN A 150      -0.452  10.869  -3.495  1.00 40.66           C  
ANISOU  804  CG  ASN A 150     4429   6782   4239  -1351   -270     69       C  
ATOM    805  OD1 ASN A 150      -0.128  10.910  -2.307  1.00 41.30           O  
ANISOU  805  OD1 ASN A 150     4581   6737   4374  -1426   -592    -47       O  
ATOM    806  ND2 ASN A 150       0.436  10.935  -4.481  1.00 42.83           N  
ANISOU  806  ND2 ASN A 150     4772   7082   4420  -1046   -131     55       N  
ATOM    807  N   PRO A 151      -2.481   9.468  -0.628  1.00 34.31           N  
ANISOU  807  N   PRO A 151     3460   5426   4152  -1474   -627   -444       N  
ATOM    808  CA  PRO A 151      -2.774   9.899   0.750  1.00 36.04           C  
ANISOU  808  CA  PRO A 151     3894   5429   4371  -1545   -820   -566       C  
ATOM    809  C   PRO A 151      -2.179  11.248   1.113  1.00 38.99           C  
ANISOU  809  C   PRO A 151     4373   5716   4726  -1668   -885   -772       C  
ATOM    810  O   PRO A 151      -2.657  11.881   2.063  1.00 40.50           O  
ANISOU  810  O   PRO A 151     4614   5960   4816  -1786  -1056  -1143       O  
ATOM    811  CB  PRO A 151      -2.171   8.775   1.604  1.00 35.08           C  
ANISOU  811  CB  PRO A 151     3702   5334   4294  -1309   -742   -286       C  
ATOM    812  CG  PRO A 151      -2.104   7.594   0.690  1.00 34.34           C  
ANISOU  812  CG  PRO A 151     3498   5352   4200  -1309   -632   -219       C  
ATOM    813  CD  PRO A 151      -1.818   8.155  -0.670  1.00 34.54           C  
ANISOU  813  CD  PRO A 151     3584   5394   4147  -1151   -722   -259       C  
ATOM    814  N   ALA A 152      -1.157  11.711   0.391  1.00 39.54           N  
ANISOU  814  N   ALA A 152     4549   5550   4925  -1760   -658   -580       N  
ATOM    815  CA  ALA A 152      -0.570  13.010   0.699  1.00 40.37           C  
ANISOU  815  CA  ALA A 152     4930   5291   5117  -1450   -191   -402       C  
ATOM    816  C   ALA A 152      -1.503  14.155   0.327  1.00 40.42           C  
ANISOU  816  C   ALA A 152     5403   4869   5084  -1655   -293   -401       C  
ATOM    817  O   ALA A 152      -1.495  15.198   0.989  1.00 41.71           O  
ANISOU  817  O   ALA A 152     5506   4958   5383  -1900   -508   -727       O  
ATOM    818  CB  ALA A 152       0.769  13.165  -0.020  1.00 40.82           C  
ANISOU  818  CB  ALA A 152     4964   5394   5153  -1587    -20   -412       C  
ATOM    819  N   ASN A 153      -2.317  13.981  -0.714  1.00 37.99           N  
ANISOU  819  N   ASN A 153     5296   4417   4720  -1753   -322   -109       N  
ATOM    820  CA  ASN A 153      -3.169  15.057  -1.200  1.00 37.49           C  
ANISOU  820  CA  ASN A 153     5286   4522   4437  -1538   -178    -82       C  
ATOM    821  C   ASN A 153      -4.634  14.896  -0.823  1.00 35.10           C  
ANISOU  821  C   ASN A 153     5384   4068   3886  -1535   -169     65       C  
ATOM    822  O   ASN A 153      -5.366  15.892  -0.827  1.00 36.15           O  
ANISOU  822  O   ASN A 153     5540   4133   4063  -1900    -87    338       O  
ATOM    823  CB  ASN A 153      -3.059  15.170  -2.725  1.00 41.01           C  
ANISOU  823  CB  ASN A 153     5671   5150   4761  -1196    -92   -219       C  
ATOM    824  CG  ASN A 153      -1.628  15.315  -3.196  1.00 44.85           C  
ANISOU  824  CG  ASN A 153     6266   5662   5111  -1026      6   -243       C  
ATOM    825  OD1 ASN A 153      -1.152  14.535  -4.022  1.00 46.98           O  
ANISOU  825  OD1 ASN A 153     6440   6151   5261   -944    -71     -3       O  
ATOM    826  ND2 ASN A 153      -0.929  16.313  -2.667  1.00 46.13           N  
ANISOU  826  ND2 ASN A 153     6691   5564   5271  -1138    198   -369       N  
ATOM    827  N   ASN A 154      -5.081  13.684  -0.503  1.00 30.93           N  
ANISOU  827  N   ASN A 154     4956   3623   3173  -1764   -259     58       N  
ATOM    828  CA  ASN A 154      -6.493  13.440  -0.242  1.00 28.55           C  
ANISOU  828  CA  ASN A 154     4702   3275   2870  -1512     53    446       C  
ATOM    829  C   ASN A 154      -6.653  12.409   0.862  1.00 26.56           C  
ANISOU  829  C   ASN A 154     4678   3024   2390  -1590     81    463       C  
ATOM    830  O   ASN A 154      -6.003  11.360   0.836  1.00 26.42           O  
ANISOU  830  O   ASN A 154     4890   2897   2253  -1900    -54    178       O  
ATOM    831  CB  ASN A 154      -7.214  12.956  -1.506  1.00 28.28           C  
ANISOU  831  CB  ASN A 154     4528   3090   3126  -1562    273    390       C  
ATOM    832  CG  ASN A 154      -7.163  13.969  -2.632  1.00 31.12           C  
ANISOU  832  CG  ASN A 154     4827   3384   3612  -1254    603    564       C  
ATOM    833  OD1 ASN A 154      -6.296  13.902  -3.503  1.00 33.40           O  
ANISOU  833  OD1 ASN A 154     5131   3670   3888  -1645    829    579       O  
ATOM    834  ND2 ASN A 154      -8.095  14.914  -2.619  1.00 32.80           N  
ANISOU  834  ND2 ASN A 154     4943   3677   3843   -976    470    428       N  
ATOM    835  N   ALA A 155      -7.519  12.710   1.824  1.00 25.06           N  
ANISOU  835  N   ALA A 155     4746   2715   2062  -1684     -7    329       N  
ATOM    836  CA  ALA A 155      -7.951  11.707   2.780  1.00 22.39           C  
ANISOU  836  CA  ALA A 155     4460   2367   1681  -1756   -228    146       C  
ATOM    837  C   ALA A 155      -9.002  10.804   2.143  1.00 19.89           C  
ANISOU  837  C   ALA A 155     4265   1940   1353  -1439    -90     -1       C  
ATOM    838  O   ALA A 155      -9.608  11.136   1.121  1.00 19.00           O  
ANISOU  838  O   ALA A 155     4218   1652   1349  -1185    -75    -32       O  
ATOM    839  CB  ALA A 155      -8.513  12.364   4.041  1.00 23.18           C  
ANISOU  839  CB  ALA A 155     4718   2444   1644  -1485   -149   -142       C  
ATOM    840  N   ALA A 156      -9.214   9.647   2.761  1.00 17.96           N  
ANISOU  840  N   ALA A 156     3860   1772   1191  -1297   -202     54       N  
ATOM    841  CA  ALA A 156     -10.173   8.691   2.230  1.00 17.87           C  
ANISOU  841  CA  ALA A 156     3900   1663   1229   -606    177   -184       C  
ATOM    842  C   ALA A 156     -11.598   9.218   2.364  1.00 17.17           C  
ANISOU  842  C   ALA A 156     3647   1575   1300   -392    428   -199       C  
ATOM    843  O   ALA A 156     -11.934   9.941   3.306  1.00 20.27           O  
ANISOU  843  O   ALA A 156     4250   1863   1590   -501    592   -290       O  
ATOM    844  CB  ALA A 156     -10.042   7.349   2.948  1.00 18.39           C  
ANISOU  844  CB  ALA A 156     3846   1844   1297    -64    105   -171       C  
ATOM    845  N   ILE A 157     -12.431   8.859   1.394  1.00 17.54           N  
ANISOU  845  N   ILE A 157     3329   1705   1631   -216    155   -106       N  
ATOM    846  CA  ILE A 157     -13.864   9.120   1.465  1.00 16.11           C  
ANISOU  846  CA  ILE A 157     2502   2176   1443   -337    218     62       C  
ATOM    847  C   ILE A 157     -14.507   8.038   2.320  1.00 15.44           C  
ANISOU  847  C   ILE A 157     2369   2205   1294    -12    284    277       C  
ATOM    848  O   ILE A 157     -14.228   6.849   2.140  1.00 14.79           O  
ANISOU  848  O   ILE A 157     2198   2134   1285    261     70    256       O  
ATOM    849  CB  ILE A 157     -14.482   9.145   0.058  1.00 16.86           C  
ANISOU  849  CB  ILE A 157     2406   2500   1499   -171    289    385       C  
ATOM    850  CG1 ILE A 157     -13.809  10.206  -0.812  1.00 16.63           C  
ANISOU  850  CG1 ILE A 157     2138   2886   1295   -101    459    262       C  
ATOM    851  CG2 ILE A 157     -15.986   9.374   0.131  1.00 17.97           C  
ANISOU  851  CG2 ILE A 157     2663   2507   1657    198     25    466       C  
ATOM    852  CD1 ILE A 157     -14.161  10.094  -2.282  1.00 17.16           C  
ANISOU  852  CD1 ILE A 157     1669   3335   1514    313    424    167       C  
ATOM    853  N   VAL A 158     -15.367   8.441   3.255  1.00 17.08           N  
ANISOU  853  N   VAL A 158     2838   2347   1304    -38    609    -21       N  
ATOM    854  CA  VAL A 158     -16.094   7.453   4.046  1.00 16.07           C  
ANISOU  854  CA  VAL A 158     2157   2323   1625   -389    434   -306       C  
ATOM    855  C   VAL A 158     -17.003   6.662   3.117  1.00 15.40           C  
ANISOU  855  C   VAL A 158     1870   2153   1828     66    352   -266       C  
ATOM    856  O   VAL A 158     -17.829   7.236   2.396  1.00 15.84           O  
ANISOU  856  O   VAL A 158     1686   2445   1887    563    347   -239       O  
ATOM    857  CB  VAL A 158     -16.879   8.127   5.174  1.00 17.17           C  
ANISOU  857  CB  VAL A 158     1698   2887   1938   -298    639   -250       C  
ATOM    858  CG1 VAL A 158     -17.777   7.113   5.876  1.00 18.09           C  
ANISOU  858  CG1 VAL A 158     1892   3099   1882   -206    604   -143       C  
ATOM    859  CG2 VAL A 158     -15.925   8.767   6.168  1.00 17.56           C  
ANISOU  859  CG2 VAL A 158     1487   3223   1961    -18    582   -458       C  
ATOM    860  N   LEU A 159     -16.842   5.341   3.116  1.00 12.78           N  
ANISOU  860  N   LEU A 159     1510   1644   1703   -554    177   -234       N  
ATOM    861  CA  LEU A 159     -17.608   4.495   2.210  1.00 13.42           C  
ANISOU  861  CA  LEU A 159     2078   1409   1611   -576    -66   -407       C  
ATOM    862  C   LEU A 159     -19.073   4.490   2.626  1.00 14.85           C  
ANISOU  862  C   LEU A 159     2472   1622   1550   -412    146   -180       C  
ATOM    863  O   LEU A 159     -19.405   4.127   3.759  1.00 17.17           O  
ANISOU  863  O   LEU A 159     2917   2048   1558    -49    305    265       O  
ATOM    864  CB  LEU A 159     -17.041   3.076   2.196  1.00 14.65           C  
ANISOU  864  CB  LEU A 159     2065   1542   1958   -345   -212   -755       C  
ATOM    865  CG  LEU A 159     -17.552   2.127   1.103  1.00 17.58           C  
ANISOU  865  CG  LEU A 159     2225   1854   2602     69     58   -542       C  
ATOM    866  CD1 LEU A 159     -16.475   1.119   0.714  1.00 15.92           C  
ANISOU  866  CD1 LEU A 159     2036   1811   2204    650    281   -797       C  
ATOM    867  CD2 LEU A 159     -18.820   1.401   1.538  1.00 20.73           C  
ANISOU  867  CD2 LEU A 159     2213   2457   3205    209    -34   -465       C  
ATOM    868  N   GLN A 160     -19.947   4.900   1.711  1.00 16.83           N  
ANISOU  868  N   GLN A 160     2622   1990   1784   -324    201   -383       N  
ATOM    869  CA  GLN A 160     -21.384   4.874   1.924  1.00 17.43           C  
ANISOU  869  CA  GLN A 160     2427   2019   2177   -247    467   -686       C  
ATOM    870  C   GLN A 160     -22.044   4.110   0.787  1.00 15.75           C  
ANISOU  870  C   GLN A 160     2074   1906   2003   -287    444   -379       C  
ATOM    871  O   GLN A 160     -21.581   4.144  -0.357  1.00 15.72           O  
ANISOU  871  O   GLN A 160     2214   1963   1795   -273    448     34       O  
ATOM    872  CB  GLN A 160     -21.978   6.289   2.008  1.00 20.09           C  
ANISOU  872  CB  GLN A 160     2767   1996   2870   -164    499   -822       C  
ATOM    873  CG  GLN A 160     -21.420   7.142   3.137  1.00 22.93           C  
ANISOU  873  CG  GLN A 160     3131   2175   3408    598    739  -1185       C  
ATOM    874  CD  GLN A 160     -22.128   8.478   3.256  1.00 31.21           C  
ANISOU  874  CD  GLN A 160     4236   3259   4364    151    488   -866       C  
ATOM    875  OE1 GLN A 160     -21.493   9.533   3.237  1.00 35.39           O  
ANISOU  875  OE1 GLN A 160     5228   3548   4671    -25     98   -628       O  
ATOM    876  NE2 GLN A 160     -23.450   8.439   3.385  1.00 32.75           N  
ANISOU  876  NE2 GLN A 160     4168   3673   4604    603    732   -951       N  
ATOM    877  N   LEU A 161     -23.130   3.417   1.112  1.00 13.86           N  
ANISOU  877  N   LEU A 161     1524   1833   1908    113    751   -349       N  
ATOM    878  CA  LEU A 161     -23.888   2.675   0.121  1.00 16.62           C  
ANISOU  878  CA  LEU A 161     2218   1986   2110    130    704   -375       C  
ATOM    879  C   LEU A 161     -25.332   3.160   0.098  1.00 19.37           C  
ANISOU  879  C   LEU A 161     2656   2277   2426    134    812   -320       C  
ATOM    880  O   LEU A 161     -25.851   3.617   1.122  1.00 20.07           O  
ANISOU  880  O   LEU A 161     2701   2341   2582    354   1079   -143       O  
ATOM    881  CB  LEU A 161     -23.849   1.169   0.412  1.00 16.36           C  
ANISOU  881  CB  LEU A 161     2414   1789   2014   -109    742   -242       C  
ATOM    882  CG  LEU A 161     -22.458   0.531   0.327  1.00 16.28           C  
ANISOU  882  CG  LEU A 161     2196   1947   2041   -164    803    -49       C  
ATOM    883  CD1 LEU A 161     -22.452  -0.852   0.960  1.00 15.25           C  
ANISOU  883  CD1 LEU A 161     1996   1576   2223   -645    901     48       C  
ATOM    884  CD2 LEU A 161     -21.987   0.457  -1.119  1.00 16.56           C  
ANISOU  884  CD2 LEU A 161     1793   2318   2179    -61    739    138       C  
ATOM    885  N   PRO A 162     -25.998   3.097  -1.056  1.00 21.66           N  
ANISOU  885  N   PRO A 162     2715   2598   2917    157    708     19       N  
ATOM    886  CA  PRO A 162     -27.396   3.536  -1.121  1.00 23.13           C  
ANISOU  886  CA  PRO A 162     2828   2767   3194     54   1116    -16       C  
ATOM    887  C   PRO A 162     -28.271   2.734  -0.171  1.00 26.61           C  
ANISOU  887  C   PRO A 162     3109   3038   3965    418   1467   -140       C  
ATOM    888  O   PRO A 162     -27.989   1.575   0.142  1.00 26.40           O  
ANISOU  888  O   PRO A 162     3148   3044   3839    -18   1683    -10       O  
ATOM    889  CB  PRO A 162     -27.783   3.284  -2.583  1.00 22.77           C  
ANISOU  889  CB  PRO A 162     2742   2893   3017     53    777     42       C  
ATOM    890  CG  PRO A 162     -26.487   3.292  -3.322  1.00 22.39           C  
ANISOU  890  CG  PRO A 162     2630   2888   2988    301    598     28       C  
ATOM    891  CD  PRO A 162     -25.480   2.705  -2.378  1.00 21.40           C  
ANISOU  891  CD  PRO A 162     2651   2700   2778    222    594    -15       C  
ATOM    892  N   GLN A 163     -29.336   3.374   0.300  1.00 29.07           N  
ANISOU  892  N   GLN A 163     3005   3290   4749    815   1475     96       N  
ATOM    893  CA  GLN A 163     -30.259   2.705   1.203  1.00 33.54           C  
ANISOU  893  CA  GLN A 163     3407   3870   5465    682   1348    245       C  
ATOM    894  C   GLN A 163     -30.916   1.524   0.503  1.00 32.29           C  
ANISOU  894  C   GLN A 163     2745   3800   5723    614   1041    645       C  
ATOM    895  O   GLN A 163     -31.213   1.574  -0.694  1.00 32.40           O  
ANISOU  895  O   GLN A 163     2433   3904   5972    447    761    913       O  
ATOM    896  CB  GLN A 163     -31.314   3.690   1.704  1.00 40.18           C  
ANISOU  896  CB  GLN A 163     4890   4547   5831    127   1364     70       C  
ATOM    897  CG  GLN A 163     -30.751   4.739   2.642  1.00 44.94           C  
ANISOU  897  CG  GLN A 163     5852   5122   6102     22   1304    151       C  
ATOM    898  CD  GLN A 163     -30.266   4.144   3.950  1.00 48.31           C  
ANISOU  898  CD  GLN A 163     6502   5455   6398     15   1363    372       C  
ATOM    899  OE1 GLN A 163     -30.884   3.227   4.494  1.00 49.68           O  
ANISOU  899  OE1 GLN A 163     6676   5671   6529     82   1505    329       O  
ATOM    900  NE2 GLN A 163     -29.152   4.658   4.458  1.00 49.88           N  
ANISOU  900  NE2 GLN A 163     6854   5561   6539    -54   1427    568       N  
ATOM    901  N   GLY A 164     -31.130   0.450   1.258  1.00 31.52           N  
ANISOU  901  N   GLY A 164     2608   3700   5668   1101   1039    734       N  
ATOM    902  CA  GLY A 164     -31.638  -0.782   0.699  1.00 30.81           C  
ANISOU  902  CA  GLY A 164     2606   3586   5515    659    971    445       C  
ATOM    903  C   GLY A 164     -30.580  -1.731   0.185  1.00 29.55           C  
ANISOU  903  C   GLY A 164     2476   3522   5230    530   1021    213       C  
ATOM    904  O   GLY A 164     -30.930  -2.801  -0.329  1.00 32.96           O  
ANISOU  904  O   GLY A 164     2792   4138   5593    260   1136     94       O  
ATOM    905  N   THR A 165     -29.301  -1.378   0.300  1.00 24.78           N  
ANISOU  905  N   THR A 165     1967   2934   4515    403    566    388       N  
ATOM    906  CA  THR A 165     -28.234  -2.265  -0.144  1.00 20.85           C  
ANISOU  906  CA  THR A 165     1608   2739   3575    210    663    243       C  
ATOM    907  C   THR A 165     -28.108  -3.448   0.807  1.00 21.08           C  
ANISOU  907  C   THR A 165     1841   2954   3213   -330    707    253       C  
ATOM    908  O   THR A 165     -28.037  -3.273   2.028  1.00 23.01           O  
ANISOU  908  O   THR A 165     2159   3380   3205   -532    831    273       O  
ATOM    909  CB  THR A 165     -26.906  -1.512  -0.223  1.00 17.67           C  
ANISOU  909  CB  THR A 165     1017   2647   3048    245    422    222       C  
ATOM    910  OG1 THR A 165     -27.003  -0.457  -1.187  1.00 17.29           O  
ANISOU  910  OG1 THR A 165      926   2641   3003    199    270    146       O  
ATOM    911  CG2 THR A 165     -25.781  -2.456  -0.622  1.00 15.75           C  
ANISOU  911  CG2 THR A 165      929   2603   2453   -107    656     74       C  
ATOM    912  N   THR A 166     -28.083  -4.653   0.247  1.00 18.09           N  
ANISOU  912  N   THR A 166     1523   2433   2917   -673    647    216       N  
ATOM    913  CA  THR A 166     -27.944  -5.859   1.049  1.00 20.51           C  
ANISOU  913  CA  THR A 166     2051   2714   3027   -728    580     90       C  
ATOM    914  C   THR A 166     -26.471  -6.131   1.322  1.00 21.27           C  
ANISOU  914  C   THR A 166     2578   2862   2642   -621    403     56       C  
ATOM    915  O   THR A 166     -25.650  -6.152   0.399  1.00 22.87           O  
ANISOU  915  O   THR A 166     2758   3440   2492   -555    403    401       O  
ATOM    916  CB  THR A 166     -28.582  -7.053   0.340  1.00 23.01           C  
ANISOU  916  CB  THR A 166     2125   3018   3600  -1278    377    351       C  
ATOM    917  OG1 THR A 166     -29.992  -6.832   0.201  1.00 24.97           O  
ANISOU  917  OG1 THR A 166     2251   3383   3852  -1564   -204    251       O  
ATOM    918  CG2 THR A 166     -28.351  -8.331   1.131  1.00 22.33           C  
ANISOU  918  CG2 THR A 166     2210   2640   3633  -1329    463    388       C  
ATOM    919  N   LEU A 167     -26.139  -6.327   2.592  1.00 20.36           N  
ANISOU  919  N   LEU A 167     2720   2566   2448   -886    380    -37       N  
ATOM    920  CA  LEU A 167     -24.794  -6.676   3.011  1.00 20.09           C  
ANISOU  920  CA  LEU A 167     2783   2453   2396   -860     33    -76       C  
ATOM    921  C   LEU A 167     -24.773  -8.077   3.609  1.00 19.28           C  
ANISOU  921  C   LEU A 167     2634   2320   2373  -1081    233     64       C  
ATOM    922  O   LEU A 167     -25.759  -8.513   4.211  1.00 21.20           O  
ANISOU  922  O   LEU A 167     2420   2934   2700  -1277    -15     -1       O  
ATOM    923  CB  LEU A 167     -24.261  -5.681   4.050  1.00 19.41           C  
ANISOU  923  CB  LEU A 167     2947   2198   2230  -1027   -420   -200       C  
ATOM    924  CG  LEU A 167     -23.902  -4.275   3.565  1.00 18.53           C  
ANISOU  924  CG  LEU A 167     2975   1891   2175  -1122   -533    -75       C  
ATOM    925  CD1 LEU A 167     -23.749  -3.335   4.749  1.00 18.10           C  
ANISOU  925  CD1 LEU A 167     3032   1914   1931  -1122   -872     89       C  
ATOM    926  CD2 LEU A 167     -22.628  -4.306   2.739  1.00 16.62           C  
ANISOU  926  CD2 LEU A 167     2297   1978   2038  -1212   -467    125       C  
ATOM    927  N   PRO A 168     -23.674  -8.810   3.459  1.00 18.22           N  
ANISOU  927  N   PRO A 168     2907   2039   1978   -667    540     80       N  
ATOM    928  CA  PRO A 168     -23.557 -10.100   4.144  1.00 17.95           C  
ANISOU  928  CA  PRO A 168     2889   2201   1731   -441    491     71       C  
ATOM    929  C   PRO A 168     -23.509  -9.907   5.652  1.00 18.47           C  
ANISOU  929  C   PRO A 168     2877   2358   1784   -508    521    119       C  
ATOM    930  O   PRO A 168     -23.295  -8.804   6.160  1.00 19.50           O  
ANISOU  930  O   PRO A 168     3016   2544   1848   -311    956     86       O  
ATOM    931  CB  PRO A 168     -22.237 -10.675   3.616  1.00 16.45           C  
ANISOU  931  CB  PRO A 168     2415   2078   1756   -309    366    188       C  
ATOM    932  CG  PRO A 168     -21.936  -9.891   2.369  1.00 17.84           C  
ANISOU  932  CG  PRO A 168     2770   2054   1955   -271    407    248       C  
ATOM    933  CD  PRO A 168     -22.506  -8.528   2.608  1.00 17.97           C  
ANISOU  933  CD  PRO A 168     2961   1927   1939   -402    547     84       C  
ATOM    934  N   LYS A 169     -23.726 -11.008   6.368  1.00 17.77           N  
ANISOU  934  N   LYS A 169     2701   2225   1826   -928    326    735       N  
ATOM    935  CA  LYS A 169     -23.597 -10.993   7.819  1.00 20.39           C  
ANISOU  935  CA  LYS A 169     2957   2508   2281  -1180    462    708       C  
ATOM    936  C   LYS A 169     -22.208 -10.516   8.218  1.00 20.92           C  
ANISOU  936  C   LYS A 169     3347   2296   2305   -991    400    451       C  
ATOM    937  O   LYS A 169     -21.204 -10.893   7.608  1.00 21.22           O  
ANISOU  937  O   LYS A 169     3223   2403   2436   -476     61    191       O  
ATOM    938  CB  LYS A 169     -23.846 -12.388   8.390  1.00 25.13           C  
ANISOU  938  CB  LYS A 169     3342   3200   3008  -1243    359   1053       C  
ATOM    939  CG  LYS A 169     -25.163 -13.017   7.983  1.00 33.26           C  
ANISOU  939  CG  LYS A 169     4140   4766   3732   -470    623    838       C  
ATOM    940  CD  LYS A 169     -26.294 -12.556   8.879  1.00 38.93           C  
ANISOU  940  CD  LYS A 169     4844   5618   4330    175    619    534       C  
ATOM    941  CE  LYS A 169     -27.424 -13.571   8.889  1.00 42.20           C  
ANISOU  941  CE  LYS A 169     5252   6070   4714    284    734    678       C  
ATOM    942  NZ  LYS A 169     -28.467 -13.211   9.884  1.00 44.41           N  
ANISOU  942  NZ  LYS A 169     5549   6419   4905    559    653    647       N  
ATOM    943  N   GLY A 170     -22.152  -9.676   9.248  1.00 19.80           N  
ANISOU  943  N   GLY A 170     3400   2011   2111  -1036    429    129       N  
ATOM    944  CA  GLY A 170     -20.893  -9.166   9.742  1.00 20.02           C  
ANISOU  944  CA  GLY A 170     3341   2068   2196  -1263    334    441       C  
ATOM    945  C   GLY A 170     -20.372  -7.932   9.038  1.00 18.38           C  
ANISOU  945  C   GLY A 170     3152   1772   2059  -1045    385    427       C  
ATOM    946  O   GLY A 170     -19.264  -7.485   9.356  1.00 19.70           O  
ANISOU  946  O   GLY A 170     3377   2040   2069  -1067    -75    404       O  
ATOM    947  N   PHE A 171     -21.125  -7.376   8.092  1.00 16.58           N  
ANISOU  947  N   PHE A 171     2922   1845   1533   -634    528    125       N  
ATOM    948  CA  PHE A 171     -20.767  -6.138   7.411  1.00 13.18           C  
ANISOU  948  CA  PHE A 171     2433   1344   1230   -378    778    124       C  
ATOM    949  C   PHE A 171     -21.755  -5.042   7.784  1.00 13.88           C  
ANISOU  949  C   PHE A 171     2520   1274   1479   -291    487    -71       C  
ATOM    950  O   PHE A 171     -22.964  -5.285   7.858  1.00 16.84           O  
ANISOU  950  O   PHE A 171     2742   1637   2021   -140    253   -377       O  
ATOM    951  CB  PHE A 171     -20.760  -6.322   5.892  1.00 13.26           C  
ANISOU  951  CB  PHE A 171     2584   1391   1064   -276    747   -223       C  
ATOM    952  CG  PHE A 171     -19.608  -7.132   5.382  1.00 15.51           C  
ANISOU  952  CG  PHE A 171     2831   1757   1306   -124    372    -41       C  
ATOM    953  CD1 PHE A 171     -18.406  -6.525   5.059  1.00 14.42           C  
ANISOU  953  CD1 PHE A 171     2430   1627   1421   -389    477     40       C  
ATOM    954  CD2 PHE A 171     -19.732  -8.500   5.208  1.00 16.50           C  
ANISOU  954  CD2 PHE A 171     3160   1652   1456    130    329    -54       C  
ATOM    955  CE1 PHE A 171     -17.343  -7.271   4.582  1.00 14.17           C  
ANISOU  955  CE1 PHE A 171     2363   1506   1514    144    221     35       C  
ATOM    956  CE2 PHE A 171     -18.674  -9.251   4.733  1.00 17.04           C  
ANISOU  956  CE2 PHE A 171     2855   2009   1608     87    370     22       C  
ATOM    957  CZ  PHE A 171     -17.481  -8.635   4.416  1.00 15.38           C  
ANISOU  957  CZ  PHE A 171     2449   1816   1579    176     93     83       C  
ATOM    958  N   TYR A 172     -21.240  -3.833   8.007  1.00 14.32           N  
ANISOU  958  N   TYR A 172     2789   1221   1431    148    230   -173       N  
ATOM    959  CA  TYR A 172     -22.062  -2.714   8.443  1.00 16.35           C  
ANISOU  959  CA  TYR A 172     2931   1641   1638    115     69   -165       C  
ATOM    960  C   TYR A 172     -21.647  -1.451   7.705  1.00 19.38           C  
ANISOU  960  C   TYR A 172     3267   2199   1898    243   -114   -186       C  
ATOM    961  O   TYR A 172     -20.454  -1.185   7.535  1.00 21.04           O  
ANISOU  961  O   TYR A 172     3657   2320   2017    204   -259   -148       O  
ATOM    962  CB  TYR A 172     -21.948  -2.506   9.959  1.00 17.39           C  
ANISOU  962  CB  TYR A 172     2985   1819   1803     53    250   -235       C  
ATOM    963  CG  TYR A 172     -22.237  -3.762  10.746  1.00 16.73           C  
ANISOU  963  CG  TYR A 172     2581   2035   1742   -398    188   -125       C  
ATOM    964  CD1 TYR A 172     -21.223  -4.662  11.047  1.00 15.24           C  
ANISOU  964  CD1 TYR A 172     2144   2019   1629   -134    219     26       C  
ATOM    965  CD2 TYR A 172     -23.525  -4.060  11.167  1.00 17.53           C  
ANISOU  965  CD2 TYR A 172     2571   2467   1621   -230    510   -158       C  
ATOM    966  CE1 TYR A 172     -21.483  -5.819  11.749  1.00 16.29           C  
ANISOU  966  CE1 TYR A 172     2364   2328   1498   -590    282    144       C  
ATOM    967  CE2 TYR A 172     -23.793  -5.215  11.874  1.00 18.52           C  
ANISOU  967  CE2 TYR A 172     2943   2401   1692   -225     94     64       C  
ATOM    968  CZ  TYR A 172     -22.766  -6.089  12.164  1.00 18.57           C  
ANISOU  968  CZ  TYR A 172     2775   2619   1663   -580    205     -8       C  
ATOM    969  OH  TYR A 172     -23.022  -7.241  12.868  1.00 21.77           O  
ANISOU  969  OH  TYR A 172     3150   3145   1979   -773    477    114       O  
ATOM    970  N   ALA A 173     -22.639  -0.679   7.271  1.00 20.66           N  
ANISOU  970  N   ALA A 173     3360   2593   1896    440    -98   -164       N  
ATOM    971  CA  ALA A 173     -22.389   0.577   6.572  1.00 21.07           C  
ANISOU  971  CA  ALA A 173     3096   2952   1958    753    330    -24       C  
ATOM    972  C   ALA A 173     -23.582   1.519   6.703  1.00 26.59           C  
ANISOU  972  C   ALA A 173     3162   4658   2282    754    682    -19       C  
ATOM    973  O   ALA A 173     -24.582   1.183   7.339  1.00 28.83           O  
ANISOU  973  O   ALA A 173     3085   5302   2568   1220    582    111       O  
ATOM    974  CB  ALA A 173     -22.074   0.318   5.105  1.00 17.58           C  
ANISOU  974  CB  ALA A 173     2850   1942   1888    890    741   -135       C  
TER     975      ALA A 173                                                      
ATOM    976  N   THR B  49      -2.802   7.122  15.636  1.00 35.44           N  
ANISOU  976  N   THR B  49     3759   5357   4349    795    654   -521       N  
ATOM    977  CA  THR B  49      -2.451   7.983  16.760  1.00 36.76           C  
ANISOU  977  CA  THR B  49     4061   5527   4380    879    896   -627       C  
ATOM    978  C   THR B  49      -3.681   8.668  17.347  1.00 31.46           C  
ANISOU  978  C   THR B  49     3524   4897   3531   1212    713   -553       C  
ATOM    979  O   THR B  49      -3.938   8.588  18.549  1.00 31.54           O  
ANISOU  979  O   THR B  49     3555   5103   3325   1094    173   -360       O  
ATOM    980  CB  THR B  49      -1.434   9.070  16.347  1.00 41.81           C  
ANISOU  980  CB  THR B  49     4773   6070   5044    774    869   -698       C  
ATOM    981  OG1 THR B  49      -0.233   8.453  15.869  1.00 45.83           O  
ANISOU  981  OG1 THR B  49     5332   6658   5422    581    933   -671       O  
ATOM    982  CG2 THR B  49      -1.104   9.968  17.531  1.00 42.84           C  
ANISOU  982  CG2 THR B  49     5014   6032   5232    549    534   -608       C  
ATOM    983  N   ALA B  50      -4.442   9.332  16.485  1.00 24.76           N  
ANISOU  983  N   ALA B  50     2841   3800   2768   1238    630   -424       N  
ATOM    984  CA  ALA B  50      -5.524  10.205  16.910  1.00 19.68           C  
ANISOU  984  CA  ALA B  50     2473   2847   2155    711    478    -68       C  
ATOM    985  C   ALA B  50      -6.826   9.432  17.115  1.00 14.22           C  
ANISOU  985  C   ALA B  50     1973   1887   1543    610    228     16       C  
ATOM    986  O   ALA B  50      -6.984   8.286  16.688  1.00 13.71           O  
ANISOU  986  O   ALA B  50     2153   1705   1352    429    393    336       O  
ATOM    987  CB  ALA B  50      -5.732  11.321  15.886  1.00 20.87           C  
ANISOU  987  CB  ALA B  50     2776   3012   2140   -157    410     61       C  
ATOM    988  N   SER B  51      -7.765  10.086  17.792  1.00  9.30           N  
ANISOU  988  N   SER B  51      907   1534   1092    129    159    -80       N  
ATOM    989  CA  SER B  51      -9.122   9.576  17.897  1.00 10.14           C  
ANISOU  989  CA  SER B  51     1255   1542   1056    324    -52   -248       C  
ATOM    990  C   SER B  51      -9.804   9.600  16.534  1.00 10.35           C  
ANISOU  990  C   SER B  51     1452   1263   1219   -169    -82   -127       C  
ATOM    991  O   SER B  51      -9.534  10.462  15.693  1.00 10.13           O  
ANISOU  991  O   SER B  51     1767    822   1258   -404   -135    146       O  
ATOM    992  CB  SER B  51      -9.926  10.411  18.896  1.00 10.17           C  
ANISOU  992  CB  SER B  51     1233   1475   1158    426   -510   -312       C  
ATOM    993  OG  SER B  51     -11.312  10.125  18.815  1.00 10.29           O  
ANISOU  993  OG  SER B  51     1335   1411   1164    340   -577    286       O  
ATOM    994  N   TRP B  52     -10.700   8.634  16.318  1.00 10.05           N  
ANISOU  994  N   TRP B  52      811   1835   1173    -45   -231    -61       N  
ATOM    995  CA  TRP B  52     -11.480   8.611  15.087  1.00  9.28           C  
ANISOU  995  CA  TRP B  52     1205   1144   1178    -98   -227   -270       C  
ATOM    996  C   TRP B  52     -12.494   9.745  15.024  1.00 10.21           C  
ANISOU  996  C   TRP B  52     1166   1382   1333    -33   -435     -4       C  
ATOM    997  O   TRP B  52     -13.007  10.039  13.939  1.00 12.14           O  
ANISOU  997  O   TRP B  52     1948   1345   1319    278   -685    172       O  
ATOM    998  CB  TRP B  52     -12.195   7.265  14.935  1.00  8.50           C  
ANISOU  998  CB  TRP B  52     1004    993   1234    -84    -18     67       C  
ATOM    999  CG  TRP B  52     -11.300   6.181  14.424  1.00  9.57           C  
ANISOU  999  CG  TRP B  52     1249   1162   1226    247     27   -119       C  
ATOM   1000  CD1 TRP B  52     -10.781   5.135  15.135  1.00 11.13           C  
ANISOU 1000  CD1 TRP B  52     1561   1176   1492    271    135   -714       C  
ATOM   1001  CD2 TRP B  52     -10.797   6.048  13.090  1.00 11.77           C  
ANISOU 1001  CD2 TRP B  52     1708   1586   1180    177   -143   -267       C  
ATOM   1002  NE1 TRP B  52      -9.994   4.355  14.321  1.00 14.62           N  
ANISOU 1002  NE1 TRP B  52     2080   1819   1656    218    -59   -518       N  
ATOM   1003  CE2 TRP B  52      -9.987   4.895  13.061  1.00 14.88           C  
ANISOU 1003  CE2 TRP B  52     2249   2040   1364      9     60   -556       C  
ATOM   1004  CE3 TRP B  52     -10.958   6.790  11.916  1.00 13.78           C  
ANISOU 1004  CE3 TRP B  52     2224   1789   1223      8   -101   -206       C  
ATOM   1005  CZ2 TRP B  52      -9.339   4.468  11.905  1.00 16.34           C  
ANISOU 1005  CZ2 TRP B  52     2506   2376   1327    104    297   -639       C  
ATOM   1006  CZ3 TRP B  52     -10.313   6.364  10.768  1.00 15.98           C  
ANISOU 1006  CZ3 TRP B  52     2662   1985   1425    -57    -70   -121       C  
ATOM   1007  CH2 TRP B  52      -9.513   5.215  10.772  1.00 17.12           C  
ANISOU 1007  CH2 TRP B  52     2697   2152   1657   -115    140   -412       C  
ATOM   1008  N   PHE B  53     -12.776  10.397  16.148  1.00  9.34           N  
ANISOU 1008  N   PHE B  53     1220    907   1423     90   -333   -174       N  
ATOM   1009  CA  PHE B  53     -13.837  11.386  16.232  1.00 10.29           C  
ANISOU 1009  CA  PHE B  53     1509    886   1516   -190     33    228       C  
ATOM   1010  C   PHE B  53     -13.291  12.725  16.709  1.00 11.59           C  
ANISOU 1010  C   PHE B  53     1820   1332   1253   -119   -243    231       C  
ATOM   1011  O   PHE B  53     -12.227  12.804  17.332  1.00 10.56           O  
ANISOU 1011  O   PHE B  53     1509   1182   1323   -239   -430    408       O  
ATOM   1012  CB  PHE B  53     -14.953  10.920  17.179  1.00  8.39           C  
ANISOU 1012  CB  PHE B  53      967    741   1482   -249    125    370       C  
ATOM   1013  CG  PHE B  53     -15.519   9.576  16.828  1.00  9.84           C  
ANISOU 1013  CG  PHE B  53     1242    933   1564   -368   -416    110       C  
ATOM   1014  CD1 PHE B  53     -16.557   9.464  15.918  1.00 11.88           C  
ANISOU 1014  CD1 PHE B  53     1314   1342   1857    -23   -511     65       C  
ATOM   1015  CD2 PHE B  53     -15.009   8.424  17.403  1.00  9.49           C  
ANISOU 1015  CD2 PHE B  53     1218    862   1524   -347   -425    291       C  
ATOM   1016  CE1 PHE B  53     -17.078   8.226  15.587  1.00 12.27           C  
ANISOU 1016  CE1 PHE B  53     1501   1335   1825    134   -381     66       C  
ATOM   1017  CE2 PHE B  53     -15.525   7.182  17.078  1.00 11.57           C  
ANISOU 1017  CE2 PHE B  53     1536   1283   1579    -73   -628    210       C  
ATOM   1018  CZ  PHE B  53     -16.561   7.083  16.169  1.00 12.59           C  
ANISOU 1018  CZ  PHE B  53     1378   1761   1646    239   -541    240       C  
ATOM   1019  N   THR B  54     -14.039  13.783  16.399  1.00 10.93           N  
ANISOU 1019  N   THR B  54     1621   1465   1068   -125   -383    118       N  
ATOM   1020  CA  THR B  54     -13.772  15.088  16.977  1.00 11.04           C  
ANISOU 1020  CA  THR B  54     1831   1317   1048     71   -292    570       C  
ATOM   1021  C   THR B  54     -14.060  15.058  18.478  1.00 10.81           C  
ANISOU 1021  C   THR B  54     1805   1315    989   -199   -101    502       C  
ATOM   1022  O   THR B  54     -14.684  14.131  19.001  1.00 10.62           O  
ANISOU 1022  O   THR B  54     1868   1266    901   -196    -87    341       O  
ATOM   1023  CB  THR B  54     -14.612  16.165  16.292  1.00 12.76           C  
ANISOU 1023  CB  THR B  54     2065   1648   1137    -58   -524    520       C  
ATOM   1024  OG1 THR B  54     -16.001  15.833  16.403  1.00 12.72           O  
ANISOU 1024  OG1 THR B  54     2179   1569   1085     -2   -771    216       O  
ATOM   1025  CG2 THR B  54     -14.239  16.277  14.821  1.00 13.29           C  
ANISOU 1025  CG2 THR B  54     2235   1594   1221    303   -780    222       C  
ATOM   1026  N   ALA B  55     -13.607  16.096  19.171  1.00 10.76           N  
ANISOU 1026  N   ALA B  55     1345   1737   1008   -371   -433    333       N  
ATOM   1027  CA  ALA B  55     -13.644  16.120  20.625  1.00 10.68           C  
ANISOU 1027  CA  ALA B  55     1297   1532   1228   -544   -616    172       C  
ATOM   1028  C   ALA B  55     -14.901  16.805  21.154  1.00 12.81           C  
ANISOU 1028  C   ALA B  55     2024   1506   1339   -566   -544    256       C  
ATOM   1029  O   ALA B  55     -15.585  17.555  20.450  1.00 13.06           O  
ANISOU 1029  O   ALA B  55     1915   1403   1646   -545   -789    100       O  
ATOM   1030  CB  ALA B  55     -12.406  16.826  21.178  1.00 12.57           C  
ANISOU 1030  CB  ALA B  55     1555   1642   1577   -255   -456    144       C  
ATOM   1031  N   LEU B  56     -15.199  16.525  22.419  1.00 13.44           N  
ANISOU 1031  N   LEU B  56     2190   1417   1500   -389   -184    -61       N  
ATOM   1032  CA  LEU B  56     -16.165  17.286  23.199  1.00 13.56           C  
ANISOU 1032  CA  LEU B  56     2033   1333   1784   -502   -380    255       C  
ATOM   1033  C   LEU B  56     -15.395  18.241  24.099  1.00 12.44           C  
ANISOU 1033  C   LEU B  56     2082    766   1880   -420   -492    114       C  
ATOM   1034  O   LEU B  56     -14.439  17.833  24.767  1.00 15.85           O  
ANISOU 1034  O   LEU B  56     2790   1147   2086    135  -1051    -10       O  
ATOM   1035  CB  LEU B  56     -17.051  16.363  24.037  1.00 13.39           C  
ANISOU 1035  CB  LEU B  56     1501   1481   2106   -506   -418    -67       C  
ATOM   1036  CG  LEU B  56     -17.878  15.339  23.262  1.00 16.09           C  
ANISOU 1036  CG  LEU B  56     1726   1889   2499   -642   -434    -66       C  
ATOM   1037  CD1 LEU B  56     -18.688  14.476  24.217  1.00 18.01           C  
ANISOU 1037  CD1 LEU B  56     1980   2103   2759   -596   -314   -156       C  
ATOM   1038  CD2 LEU B  56     -18.781  16.039  22.260  1.00 15.57           C  
ANISOU 1038  CD2 LEU B  56     1439   1800   2678   -290   -581   -373       C  
ATOM   1039  N   THR B  57     -15.802  19.505  24.114  1.00  9.91           N  
ANISOU 1039  N   THR B  57     1373    546   1848   -262    -98    -14       N  
ATOM   1040  CA  THR B  57     -15.063  20.546  24.814  1.00  9.93           C  
ANISOU 1040  CA  THR B  57     1342    667   1764     13    184   -150       C  
ATOM   1041  C   THR B  57     -15.759  20.905  26.121  1.00 12.40           C  
ANISOU 1041  C   THR B  57     1870   1128   1714     61   -317   -217       C  
ATOM   1042  O   THR B  57     -16.950  21.237  26.127  1.00 13.39           O  
ANISOU 1042  O   THR B  57     1654   1633   1801      9   -198   -119       O  
ATOM   1043  CB  THR B  57     -14.913  21.784  23.932  1.00 11.03           C  
ANISOU 1043  CB  THR B  57     1756    712   1723    -10    270   -107       C  
ATOM   1044  OG1 THR B  57     -14.140  21.445  22.773  1.00 12.89           O  
ANISOU 1044  OG1 THR B  57     1952   1120   1827    262    477   -105       O  
ATOM   1045  CG2 THR B  57     -14.214  22.896  24.692  1.00 10.24           C  
ANISOU 1045  CG2 THR B  57     1236    714   1939     32    200    163       C  
ATOM   1046  N   GLN B  58     -15.010  20.846  27.221  1.00 12.17           N  
ANISOU 1046  N   GLN B  58     1995   1067   1561    132   -456   -396       N  
ATOM   1047  CA  GLN B  58     -15.547  21.097  28.557  1.00 12.86           C  
ANISOU 1047  CA  GLN B  58     2166   1297   1424    149   -427   -306       C  
ATOM   1048  C   GLN B  58     -15.399  22.579  28.881  1.00 16.14           C  
ANISOU 1048  C   GLN B  58     2549   1636   1945    300   -496   -215       C  
ATOM   1049  O   GLN B  58     -14.305  23.054  29.200  1.00 18.94           O  
ANISOU 1049  O   GLN B  58     3407   1484   2306   -118   -633   -232       O  
ATOM   1050  CB  GLN B  58     -14.838  20.235  29.596  1.00 13.29           C  
ANISOU 1050  CB  GLN B  58     2515   1394   1141    282   -422    -86       C  
ATOM   1051  CG  GLN B  58     -15.335  20.466  31.018  1.00 14.56           C  
ANISOU 1051  CG  GLN B  58     2841   1636   1057     -5      0    -61       C  
ATOM   1052  CD  GLN B  58     -14.507  19.739  32.063  1.00 17.11           C  
ANISOU 1052  CD  GLN B  58     3244   1907   1348    319     -8   -257       C  
ATOM   1053  OE1 GLN B  58     -13.831  18.755  31.765  1.00 15.37           O  
ANISOU 1053  OE1 GLN B  58     2814   1562   1465    688   -334   -365       O  
ATOM   1054  NE2 GLN B  58     -14.555  20.226  33.298  1.00 19.53           N  
ANISOU 1054  NE2 GLN B  58     3797   2133   1493    316     62   -324       N  
ATOM   1055  N   HIS B  59     -16.507  23.314  28.803  1.00 14.38           N  
ANISOU 1055  N   HIS B  59     2230   1316   1920    575   -439   -283       N  
ATOM   1056  CA  HIS B  59     -16.525  24.701  29.247  1.00 13.87           C  
ANISOU 1056  CA  HIS B  59     1995   1436   1839    202   -396   -380       C  
ATOM   1057  C   HIS B  59     -16.895  24.835  30.716  1.00 16.47           C  
ANISOU 1057  C   HIS B  59     2677   1658   1923   -254   -203   -568       C  
ATOM   1058  O   HIS B  59     -16.485  25.805  31.365  1.00 17.56           O  
ANISOU 1058  O   HIS B  59     3035   1599   2038   -772   -351   -460       O  
ATOM   1059  CB  HIS B  59     -17.505  25.518  28.401  1.00  9.54           C  
ANISOU 1059  CB  HIS B  59     1056    968   1602    296   -260     89       C  
ATOM   1060  CG  HIS B  59     -17.029  25.783  27.007  1.00  9.72           C  
ANISOU 1060  CG  HIS B  59      852   1027   1815    -48   -156   -307       C  
ATOM   1061  ND1 HIS B  59     -16.620  27.029  26.585  1.00 11.35           N  
ANISOU 1061  ND1 HIS B  59     1485   1017   1812    -65   -301   -314       N  
ATOM   1062  CD2 HIS B  59     -16.901  24.963  25.937  1.00 12.81           C  
ANISOU 1062  CD2 HIS B  59     1106   1648   2112   -409   -100   -204       C  
ATOM   1063  CE1 HIS B  59     -16.259  26.966  25.316  1.00 12.35           C  
ANISOU 1063  CE1 HIS B  59     1769    891   2033   -258   -140   -415       C  
ATOM   1064  NE2 HIS B  59     -16.421  25.723  24.898  1.00 12.34           N  
ANISOU 1064  NE2 HIS B  59     1549    958   2180   -234    -80   -123       N  
ATOM   1065  N   GLY B  60     -17.656  23.882  31.254  1.00 17.47           N  
ANISOU 1065  N   GLY B  60     2654   1828   2154     70    -19   -319       N  
ATOM   1066  CA  GLY B  60     -18.097  23.928  32.631  1.00 18.61           C  
ANISOU 1066  CA  GLY B  60     2778   2108   2186     36    148   -331       C  
ATOM   1067  C   GLY B  60     -17.087  23.319  33.583  1.00 19.67           C  
ANISOU 1067  C   GLY B  60     3001   2239   2235   -186   -157   -501       C  
ATOM   1068  O   GLY B  60     -15.957  22.986  33.219  1.00 18.97           O  
ANISOU 1068  O   GLY B  60     3053   1894   2263   -274   -450   -509       O  
ATOM   1069  N   LYS B  61     -17.520  23.164  34.835  1.00 21.67           N  
ANISOU 1069  N   LYS B  61     3432   2400   2401   -165    440   -706       N  
ATOM   1070  CA  LYS B  61     -16.655  22.695  35.909  1.00 21.85           C  
ANISOU 1070  CA  LYS B  61     3531   2265   2506   -213    279   -887       C  
ATOM   1071  C   LYS B  61     -16.739  21.194  36.155  1.00 23.25           C  
ANISOU 1071  C   LYS B  61     3975   2405   2455     36    -66   -340       C  
ATOM   1072  O   LYS B  61     -15.962  20.676  36.962  1.00 27.08           O  
ANISOU 1072  O   LYS B  61     4554   2912   2824    560   -739   -300       O  
ATOM   1073  CB  LYS B  61     -16.989  23.429  37.215  1.00 24.08           C  
ANISOU 1073  CB  LYS B  61     3832   2205   3112   -572    348  -1062       C  
ATOM   1074  CG  LYS B  61     -16.887  24.942  37.124  1.00 28.19           C  
ANISOU 1074  CG  LYS B  61     4144   2794   3771   -513    644   -924       C  
ATOM   1075  CD  LYS B  61     -15.491  25.374  36.706  1.00 32.08           C  
ANISOU 1075  CD  LYS B  61     4481   3365   4342   -668    665  -1037       C  
ATOM   1076  CE  LYS B  61     -15.386  26.887  36.624  1.00 35.10           C  
ANISOU 1076  CE  LYS B  61     4616   3988   4732   -876    850  -1023       C  
ATOM   1077  NZ  LYS B  61     -14.048  27.321  36.137  1.00 38.17           N  
ANISOU 1077  NZ  LYS B  61     4954   4560   4988   -733   1004   -977       N  
ATOM   1078  N   GLU B  62     -17.647  20.488  35.490  1.00 23.11           N  
ANISOU 1078  N   GLU B  62     3635   2771   2374   -510     87    -42       N  
ATOM   1079  CA  GLU B  62     -17.890  19.076  35.754  1.00 25.56           C  
ANISOU 1079  CA  GLU B  62     4256   2967   2487     76    448    253       C  
ATOM   1080  C   GLU B  62     -17.162  18.199  34.743  1.00 23.54           C  
ANISOU 1080  C   GLU B  62     4086   2739   2118    261    595    282       C  
ATOM   1081  O   GLU B  62     -17.123  18.510  33.549  1.00 23.79           O  
ANISOU 1081  O   GLU B  62     4239   2893   1906    114    441    372       O  
ATOM   1082  CB  GLU B  62     -19.388  18.769  35.717  1.00 31.87           C  
ANISOU 1082  CB  GLU B  62     5233   3671   3203   -138    652    306       C  
ATOM   1083  CG  GLU B  62     -20.201  19.527  36.752  1.00 39.21           C  
ANISOU 1083  CG  GLU B  62     6238   4621   4039     71    781    338       C  
ATOM   1084  CD  GLU B  62     -19.883  19.093  38.169  1.00 47.67           C  
ANISOU 1084  CD  GLU B  62     7306   5764   5042    396    679    196       C  
ATOM   1085  OE1 GLU B  62     -19.554  17.903  38.367  1.00 51.18           O  
ANISOU 1085  OE1 GLU B  62     7817   6196   5435    430    570    357       O  
ATOM   1086  OE2 GLU B  62     -19.957  19.941  39.085  1.00 50.35           O  
ANISOU 1086  OE2 GLU B  62     7611   6136   5383    594    653    -53       O  
ATOM   1087  N   ASP B  63     -16.592  17.097  35.228  1.00 22.06           N  
ANISOU 1087  N   ASP B  63     3742   2709   1929    650    497     75       N  
ATOM   1088  CA  ASP B  63     -15.989  16.115  34.341  1.00 21.48           C  
ANISOU 1088  CA  ASP B  63     3510   2412   2240    637     77     43       C  
ATOM   1089  C   ASP B  63     -17.055  15.466  33.461  1.00 19.52           C  
ANISOU 1089  C   ASP B  63     3116   1994   2306    435    381   -368       C  
ATOM   1090  O   ASP B  63     -18.242  15.428  33.797  1.00 21.86           O  
ANISOU 1090  O   ASP B  63     3100   2574   2633    108    548   -730       O  
ATOM   1091  CB  ASP B  63     -15.256  15.037  35.141  1.00 24.29           C  
ANISOU 1091  CB  ASP B  63     3747   2945   2539    319   -144    288       C  
ATOM   1092  CG  ASP B  63     -13.962  15.537  35.749  1.00 29.25           C  
ANISOU 1092  CG  ASP B  63     4201   3734   3180     -1     -8    639       C  
ATOM   1093  OD1 ASP B  63     -13.629  16.725  35.552  1.00 33.21           O  
ANISOU 1093  OD1 ASP B  63     4450   4837   3330   -170    232    754       O  
ATOM   1094  OD2 ASP B  63     -13.276  14.739  36.424  1.00 31.79           O  
ANISOU 1094  OD2 ASP B  63     4531   3968   3579   -232    235    488       O  
ATOM   1095  N   LEU B  64     -16.612  14.948  32.318  1.00 16.67           N  
ANISOU 1095  N   LEU B  64     3137   1319   1875    351    175    104       N  
ATOM   1096  CA  LEU B  64     -17.520  14.262  31.409  1.00 15.00           C  
ANISOU 1096  CA  LEU B  64     2482   1511   1706   -181    -30    103       C  
ATOM   1097  C   LEU B  64     -18.069  12.998  32.057  1.00 15.55           C  
ANISOU 1097  C   LEU B  64     2705   1630   1575   -292    164    261       C  
ATOM   1098  O   LEU B  64     -17.361  12.289  32.777  1.00 16.23           O  
ANISOU 1098  O   LEU B  64     2723   1778   1667     85    374    215       O  
ATOM   1099  CB  LEU B  64     -16.807  13.915  30.103  1.00 12.95           C  
ANISOU 1099  CB  LEU B  64     1960   1413   1548    243    -81    171       C  
ATOM   1100  CG  LEU B  64     -17.678  13.311  29.001  1.00 13.51           C  
ANISOU 1100  CG  LEU B  64     1839   1517   1776    385    -77    343       C  
ATOM   1101  CD1 LEU B  64     -18.817  14.251  28.645  1.00 13.86           C  
ANISOU 1101  CD1 LEU B  64     2032   1566   1668    408   -258    366       C  
ATOM   1102  CD2 LEU B  64     -16.843  12.993  27.771  1.00 13.48           C  
ANISOU 1102  CD2 LEU B  64     1627   1751   1743    710    -44    186       C  
ATOM   1103  N   LYS B  65     -19.343  12.721  31.796  1.00 16.97           N  
ANISOU 1103  N   LYS B  65     2899   2000   1549   -706    617     87       N  
ATOM   1104  CA  LYS B  65     -19.996  11.546  32.351  1.00 22.05           C  
ANISOU 1104  CA  LYS B  65     3517   2986   1875   -979    826    105       C  
ATOM   1105  C   LYS B  65     -21.264  11.281  31.553  1.00 22.22           C  
ANISOU 1105  C   LYS B  65     3540   2712   2192   -995    832   -118       C  
ATOM   1106  O   LYS B  65     -21.956  12.220  31.155  1.00 23.09           O  
ANISOU 1106  O   LYS B  65     3590   2602   2582  -1120    808     13       O  
ATOM   1107  CB  LYS B  65     -20.315  11.746  33.840  1.00 28.95           C  
ANISOU 1107  CB  LYS B  65     4342   4255   2403   -864    719    313       C  
ATOM   1108  CG  LYS B  65     -20.827  10.510  34.554  1.00 33.98           C  
ANISOU 1108  CG  LYS B  65     4969   4961   2982   -735    618    208       C  
ATOM   1109  CD  LYS B  65     -20.600  10.610  36.060  1.00 36.75           C  
ANISOU 1109  CD  LYS B  65     5220   5379   3366   -504    605     30       C  
ATOM   1110  CE  LYS B  65     -21.191  11.887  36.637  1.00 38.74           C  
ANISOU 1110  CE  LYS B  65     5199   5797   3723   -533    468    -37       C  
ATOM   1111  NZ  LYS B  65     -22.667  11.956  36.450  1.00 40.19           N  
ANISOU 1111  NZ  LYS B  65     5217   6123   3929   -543    428     -2       N  
ATOM   1112  N   PHE B  66     -21.550  10.006  31.311  1.00 19.95           N  
ANISOU 1112  N   PHE B  66     3268   2281   2032   -701   1034   -432       N  
ATOM   1113  CA  PHE B  66     -22.754   9.604  30.604  1.00 21.50           C  
ANISOU 1113  CA  PHE B  66     3399   2482   2289   -635   1137   -159       C  
ATOM   1114  C   PHE B  66     -23.507   8.560  31.411  1.00 24.30           C  
ANISOU 1114  C   PHE B  66     3542   3013   2679   -297   1146    -65       C  
ATOM   1115  O   PHE B  66     -22.891   7.727  32.084  1.00 26.14           O  
ANISOU 1115  O   PHE B  66     3788   3469   2676   -146   1034    274       O  
ATOM   1116  CB  PHE B  66     -22.432   9.025  29.219  1.00 19.69           C  
ANISOU 1116  CB  PHE B  66     3103   2240   2138   -220    983    -60       C  
ATOM   1117  CG  PHE B  66     -22.046  10.057  28.199  1.00 17.94           C  
ANISOU 1117  CG  PHE B  66     2874   1815   2128   -220    988     30       C  
ATOM   1118  CD1 PHE B  66     -23.017  10.778  27.524  1.00 17.43           C  
ANISOU 1118  CD1 PHE B  66     2709   1835   2080   -221    730     97       C  
ATOM   1119  CD2 PHE B  66     -20.714  10.292  27.899  1.00 18.16           C  
ANISOU 1119  CD2 PHE B  66     2817   1733   2348   -224    635   -117       C  
ATOM   1120  CE1 PHE B  66     -22.666  11.722  26.578  1.00 18.31           C  
ANISOU 1120  CE1 PHE B  66     2800   2074   2082   -561    298    -58       C  
ATOM   1121  CE2 PHE B  66     -20.357  11.236  26.951  1.00 17.45           C  
ANISOU 1121  CE2 PHE B  66     2827   1628   2174      8    633    -97       C  
ATOM   1122  CZ  PHE B  66     -21.334  11.951  26.291  1.00 18.00           C  
ANISOU 1122  CZ  PHE B  66     2777   1993   2071   -162    432     54       C  
ATOM   1123  N   PRO B  67     -24.839   8.581  31.366  1.00 25.65           N  
ANISOU 1123  N   PRO B  67     3611   2980   3157   -228   1237   -110       N  
ATOM   1124  CA  PRO B  67     -25.606   7.481  31.958  1.00 25.76           C  
ANISOU 1124  CA  PRO B  67     3469   3017   3302    -73   1479   -200       C  
ATOM   1125  C   PRO B  67     -25.253   6.164  31.285  1.00 24.71           C  
ANISOU 1125  C   PRO B  67     3220   2925   3243   -325   1434   -282       C  
ATOM   1126  O   PRO B  67     -24.836   6.127  30.125  1.00 22.98           O  
ANISOU 1126  O   PRO B  67     2920   2943   2869    -97   1674   -512       O  
ATOM   1127  CB  PRO B  67     -27.064   7.876  31.692  1.00 28.23           C  
ANISOU 1127  CB  PRO B  67     3955   3219   3553   -218   1479   -165       C  
ATOM   1128  CG  PRO B  67     -27.027   9.357  31.490  1.00 28.77           C  
ANISOU 1128  CG  PRO B  67     4013   3311   3607   -136   1447     38       C  
ATOM   1129  CD  PRO B  67     -25.709   9.641  30.831  1.00 27.50           C  
ANISOU 1129  CD  PRO B  67     3808   3178   3462   -350   1452     -7       C  
ATOM   1130  N   ARG B  68     -25.414   5.075  32.033  1.00 24.29           N  
ANISOU 1130  N   ARG B  68     2898   2834   3497   -527   1313   -161       N  
ATOM   1131  CA  ARG B  68     -25.074   3.760  31.509  1.00 25.23           C  
ANISOU 1131  CA  ARG B  68     2821   3007   3759   -434   1196     45       C  
ATOM   1132  C   ARG B  68     -25.909   3.452  30.273  1.00 23.91           C  
ANISOU 1132  C   ARG B  68     2116   2970   3999   -598   1402    -60       C  
ATOM   1133  O   ARG B  68     -27.140   3.524  30.304  1.00 27.85           O  
ANISOU 1133  O   ARG B  68     2487   3639   4455   -733   1482   -444       O  
ATOM   1134  CB  ARG B  68     -25.291   2.694  32.584  1.00 30.48           C  
ANISOU 1134  CB  ARG B  68     3668   3836   4075   -144    798    128       C  
ATOM   1135  CG  ARG B  68     -24.729   1.327  32.227  1.00 35.14           C  
ANISOU 1135  CG  ARG B  68     4601   4489   4260    245    362    158       C  
ATOM   1136  CD  ARG B  68     -24.374   0.526  33.477  1.00 39.89           C  
ANISOU 1136  CD  ARG B  68     5319   5304   4534    547    -79    123       C  
ATOM   1137  NE  ARG B  68     -23.274   1.135  34.223  1.00 43.19           N  
ANISOU 1137  NE  ARG B  68     5837   5892   4680    672   -441    338       N  
ATOM   1138  CZ  ARG B  68     -23.427   1.879  35.315  1.00 46.05           C  
ANISOU 1138  CZ  ARG B  68     6117   6274   5106    855   -588    700       C  
ATOM   1139  NH1 ARG B  68     -22.365   2.394  35.923  1.00 46.46           N  
ANISOU 1139  NH1 ARG B  68     6144   6382   5125    756   -939    746       N  
ATOM   1140  NH2 ARG B  68     -24.639   2.105  35.804  1.00 46.48           N  
ANISOU 1140  NH2 ARG B  68     5998   6371   5293   1014   -448    808       N  
ATOM   1141  N   GLY B  69     -25.230   3.130  29.174  1.00 22.79           N  
ANISOU 1141  N   GLY B  69     2118   2647   3894   -509    828    -44       N  
ATOM   1142  CA  GLY B  69     -25.881   2.855  27.912  1.00 19.39           C  
ANISOU 1142  CA  GLY B  69     1399   2426   3541   -394    554   -286       C  
ATOM   1143  C   GLY B  69     -25.771   3.961  26.884  1.00 19.24           C  
ANISOU 1143  C   GLY B  69     1498   2397   3417    -76    319   -203       C  
ATOM   1144  O   GLY B  69     -26.103   3.729  25.715  1.00 21.35           O  
ANISOU 1144  O   GLY B  69     2206   2534   3372   -255    257   -521       O  
ATOM   1145  N   GLN B  70     -25.317   5.147  27.276  1.00 17.72           N  
ANISOU 1145  N   GLN B  70     1183   2208   3340     38    351    -88       N  
ATOM   1146  CA  GLN B  70     -25.200   6.289  26.380  1.00 17.65           C  
ANISOU 1146  CA  GLN B  70     1318   2112   3275    407    835     73       C  
ATOM   1147  C   GLN B  70     -23.741   6.717  26.268  1.00 16.48           C  
ANISOU 1147  C   GLN B  70     1639   1797   2827    324   1114    -29       C  
ATOM   1148  O   GLN B  70     -22.883   6.302  27.051  1.00 16.38           O  
ANISOU 1148  O   GLN B  70     1629   1755   2841    116    954   -115       O  
ATOM   1149  CB  GLN B  70     -26.058   7.463  26.871  1.00 20.28           C  
ANISOU 1149  CB  GLN B  70     1519   2802   3384    320   1085      1       C  
ATOM   1150  CG  GLN B  70     -27.522   7.121  27.082  1.00 26.49           C  
ANISOU 1150  CG  GLN B  70     2404   3425   4236    359   1415     30       C  
ATOM   1151  CD  GLN B  70     -28.297   8.250  27.739  1.00 31.35           C  
ANISOU 1151  CD  GLN B  70     2988   4146   4776    237   1579     34       C  
ATOM   1152  OE1 GLN B  70     -27.854   9.400  27.755  1.00 32.46           O  
ANISOU 1152  OE1 GLN B  70     3313   4084   4938    633   1794   -107       O  
ATOM   1153  NE2 GLN B  70     -29.458   7.925  28.292  1.00 33.59           N  
ANISOU 1153  NE2 GLN B  70     3131   4589   5044    324   1485     35       N  
ATOM   1154  N   GLY B  71     -23.463   7.557  25.272  1.00 16.27           N  
ANISOU 1154  N   GLY B  71     1650   2047   2486    525    968   -152       N  
ATOM   1155  CA  GLY B  71     -22.174   8.208  25.144  1.00 16.02           C  
ANISOU 1155  CA  GLY B  71     2099   1798   2189    121    567    -43       C  
ATOM   1156  C   GLY B  71     -21.291   7.714  24.018  1.00 14.28           C  
ANISOU 1156  C   GLY B  71     2087   1594   1745   -151    204    -15       C  
ATOM   1157  O   GLY B  71     -20.310   8.393  23.692  1.00 13.40           O  
ANISOU 1157  O   GLY B  71     1939   1436   1716    118     31    135       O  
ATOM   1158  N   VAL B  72     -21.584   6.567  23.418  1.00 13.89           N  
ANISOU 1158  N   VAL B  72     2338   1295   1646    -94     84    -84       N  
ATOM   1159  CA  VAL B  72     -20.736   6.057  22.337  1.00 12.83           C  
ANISOU 1159  CA  VAL B  72     1933   1267   1676    -89    -79     56       C  
ATOM   1160  C   VAL B  72     -21.058   6.822  21.056  1.00 12.31           C  
ANISOU 1160  C   VAL B  72     1396   1309   1973     23   -398    -42       C  
ATOM   1161  O   VAL B  72     -22.234   6.891  20.665  1.00 12.52           O  
ANISOU 1161  O   VAL B  72      848   1670   2239   -135   -437   -104       O  
ATOM   1162  CB  VAL B  72     -20.939   4.557  22.148  1.00 11.47           C  
ANISOU 1162  CB  VAL B  72     1932   1158   1269    281    192    -21       C  
ATOM   1163  CG1 VAL B  72     -20.076   4.054  21.000  1.00 10.65           C  
ANISOU 1163  CG1 VAL B  72     1992    848   1205    190    138   -117       C  
ATOM   1164  CG2 VAL B  72     -20.606   3.807  23.432  1.00 12.83           C  
ANISOU 1164  CG2 VAL B  72     2232   1225   1418    225     34    103       C  
ATOM   1165  N   PRO B  73     -20.064   7.410  20.389  1.00 12.07           N  
ANISOU 1165  N   PRO B  73     1422   1417   1746    210   -397    122       N  
ATOM   1166  CA  PRO B  73     -20.342   8.160  19.158  1.00 13.62           C  
ANISOU 1166  CA  PRO B  73     1892   1414   1870   -511   -433    -30       C  
ATOM   1167  C   PRO B  73     -20.916   7.270  18.065  1.00 16.64           C  
ANISOU 1167  C   PRO B  73     2347   1932   2044   -281   -514    134       C  
ATOM   1168  O   PRO B  73     -20.624   6.074  17.985  1.00 17.95           O  
ANISOU 1168  O   PRO B  73     2578   1985   2256   -662  -1070    187       O  
ATOM   1169  CB  PRO B  73     -18.968   8.710  18.761  1.00 12.38           C  
ANISOU 1169  CB  PRO B  73     1635   1313   1758   -367   -310     47       C  
ATOM   1170  CG  PRO B  73     -18.198   8.756  20.037  1.00 11.49           C  
ANISOU 1170  CG  PRO B  73     1725   1367   1274   -135   -136    600       C  
ATOM   1171  CD  PRO B  73     -18.667   7.567  20.829  1.00 11.66           C  
ANISOU 1171  CD  PRO B  73     1625   1301   1506    360   -526    413       C  
ATOM   1172  N   ILE B  74     -21.742   7.878  17.214  1.00 14.58           N  
ANISOU 1172  N   ILE B  74     1642   1846   2053    163   -351      9       N  
ATOM   1173  CA  ILE B  74     -22.344   7.156  16.101  1.00 13.40           C  
ANISOU 1173  CA  ILE B  74     1439   1846   1806    205   -220   -312       C  
ATOM   1174  C   ILE B  74     -21.269   6.798  15.086  1.00 14.06           C  
ANISOU 1174  C   ILE B  74     1742   1777   1821    -76   -467    101       C  
ATOM   1175  O   ILE B  74     -20.448   7.641  14.698  1.00 16.48           O  
ANISOU 1175  O   ILE B  74     1838   2309   2116   -443   -296    -14       O  
ATOM   1176  CB  ILE B  74     -23.461   7.992  15.458  1.00 14.92           C  
ANISOU 1176  CB  ILE B  74     1493   2316   1861    571   -553   -634       C  
ATOM   1177  CG1 ILE B  74     -24.605   8.208  16.452  1.00 18.36           C  
ANISOU 1177  CG1 ILE B  74     1762   2882   2332    883   -505   -486       C  
ATOM   1178  CG2 ILE B  74     -23.970   7.322  14.184  1.00 17.00           C  
ANISOU 1178  CG2 ILE B  74     2301   2070   2088     63   -701   -267       C  
ATOM   1179  CD1 ILE B  74     -25.679   9.150  15.951  1.00 19.61           C  
ANISOU 1179  CD1 ILE B  74     1727   3118   2605    668   -501   -146       C  
ATOM   1180  N   ASN B  75     -21.266   5.539  14.652  1.00 13.65           N  
ANISOU 1180  N   ASN B  75     1950   1573   1663    -98   -639     85       N  
ATOM   1181  CA  ASN B  75     -20.333   5.069  13.627  1.00 15.05           C  
ANISOU 1181  CA  ASN B  75     2283   1632   1801    -31   -719   -144       C  
ATOM   1182  C   ASN B  75     -21.008   3.884  12.933  1.00 17.34           C  
ANISOU 1182  C   ASN B  75     2769   1888   1929   -181   -672   -373       C  
ATOM   1183  O   ASN B  75     -20.862   2.735  13.355  1.00 18.46           O  
ANISOU 1183  O   ASN B  75     3234   1697   2082   -667   -285   -564       O  
ATOM   1184  CB  ASN B  75     -18.985   4.692  14.226  1.00 14.94           C  
ANISOU 1184  CB  ASN B  75     2471   1402   1803    296   -679   -200       C  
ATOM   1185  CG  ASN B  75     -17.995   4.210  13.184  1.00 15.91           C  
ANISOU 1185  CG  ASN B  75     2803   1541   1700     46   -369    -21       C  
ATOM   1186  OD1 ASN B  75     -18.238   4.309  11.980  1.00 17.96           O  
ANISOU 1186  OD1 ASN B  75     3287   1826   1712   -108   -487   -470       O  
ATOM   1187  ND2 ASN B  75     -16.866   3.689  13.643  1.00 16.54           N  
ANISOU 1187  ND2 ASN B  75     3051   1474   1758     69   -302   -140       N  
ATOM   1188  N   THR B  76     -21.746   4.184  11.861  1.00 16.75           N  
ANISOU 1188  N   THR B  76     2109   2166   2090    461   -944   -166       N  
ATOM   1189  CA  THR B  76     -22.516   3.168  11.153  1.00 19.23           C  
ANISOU 1189  CA  THR B  76     2569   2540   2197    305   -747   -183       C  
ATOM   1190  C   THR B  76     -21.644   2.162  10.410  1.00 18.28           C  
ANISOU 1190  C   THR B  76     2359   2535   2052     -9   -507   -164       C  
ATOM   1191  O   THR B  76     -22.176   1.174   9.892  1.00 18.57           O  
ANISOU 1191  O   THR B  76     2641   2328   2088   -390   -406   -451       O  
ATOM   1192  CB  THR B  76     -23.484   3.832  10.172  1.00 22.14           C  
ANISOU 1192  CB  THR B  76     2823   3162   2427    244   -781    -77       C  
ATOM   1193  OG1 THR B  76     -22.744   4.593   9.209  1.00 20.66           O  
ANISOU 1193  OG1 THR B  76     2632   3222   1998   -377   -704    650       O  
ATOM   1194  CG2 THR B  76     -24.437   4.755  10.916  1.00 25.16           C  
ANISOU 1194  CG2 THR B  76     3263   3521   2778    513   -844   -206       C  
ATOM   1195  N  AASN B  77     -20.333   2.388  10.330  0.54 17.91           N  
ANISOU 1195  N  AASN B  77     2450   2497   1858     14   -566    100       N  
ATOM   1196  N  BASN B  77     -20.333   2.384  10.354  0.46 18.31           N  
ANISOU 1196  N  BASN B  77     2583   2533   1840    -34   -695    -44       N  
ATOM   1197  CA AASN B  77     -19.420   1.434   9.717  0.54 17.45           C  
ANISOU 1197  CA AASN B  77     2285   2517   1829     58   -373    221       C  
ATOM   1198  CA BASN B  77     -19.402   1.461   9.723  0.46 18.22           C  
ANISOU 1198  CA BASN B  77     2584   2578   1760    -48   -664      1       C  
ATOM   1199  C  AASN B  77     -18.728   0.551  10.749  0.54 18.72           C  
ANISOU 1199  C  AASN B  77     2583   2618   1910    143   -236     57       C  
ATOM   1200  C  BASN B  77     -18.787   0.478  10.712  0.46 19.18           C  
ANISOU 1200  C  BASN B  77     2718   2708   1862    135   -411     -6       C  
ATOM   1201  O  AASN B  77     -17.642   0.025  10.481  0.54 20.37           O  
ANISOU 1201  O  AASN B  77     2782   2940   2016    259   -154    258       O  
ATOM   1202  O  BASN B  77     -17.810  -0.197  10.373  0.46 20.97           O  
ANISOU 1202  O  BASN B  77     2947   3061   1961    365   -389    248       O  
ATOM   1203  CB AASN B  77     -18.391   2.162   8.853  0.54 17.81           C  
ANISOU 1203  CB AASN B  77     2109   2636   2022    -91   -408    419       C  
ATOM   1204  CB BASN B  77     -18.298   2.244   9.009  0.46 18.91           C  
ANISOU 1204  CB BASN B  77     2698   2643   1844   -373   -951     -8       C  
ATOM   1205  CG AASN B  77     -18.997   2.725   7.582  0.54 18.64           C  
ANISOU 1205  CG AASN B  77     2045   2832   2207   -271   -121    599       C  
ATOM   1206  CG BASN B  77     -18.844   3.187   7.956  0.46 20.62           C  
ANISOU 1206  CG BASN B  77     3084   2736   2013   -755   -977    -66       C  
ATOM   1207  OD1AASN B  77     -20.191   3.022   7.532  0.54 20.74           O  
ANISOU 1207  OD1AASN B  77     2288   3302   2288     26    365    665       O  
ATOM   1208  OD1BASN B  77     -19.617   2.785   7.086  0.46 22.78           O  
ANISOU 1208  OD1BASN B  77     3563   2923   2170   -603  -1113   -174       O  
ATOM   1209  ND2AASN B  77     -18.179   2.866   6.545  0.54 15.93           N  
ANISOU 1209  ND2AASN B  77     1536   2363   2153   -431    -87    734       N  
ATOM   1210  ND2BASN B  77     -18.454   4.454   8.037  0.46 18.73           N  
ANISOU 1210  ND2BASN B  77     2923   2243   1952  -1021   -868     53       N  
ATOM   1211  N   SER B  78     -19.335   0.381  11.921  1.00 17.54           N  
ANISOU 1211  N   SER B  78     2482   2406   1777      3    -84    -71       N  
ATOM   1212  CA  SER B  78     -18.832  -0.517  12.948  1.00 15.68           C  
ANISOU 1212  CA  SER B  78     2023   2039   1897      8   -395   -178       C  
ATOM   1213  C   SER B  78     -19.963  -1.424  13.416  1.00 14.92           C  
ANISOU 1213  C   SER B  78     1963   1630   2074     -9    -26   -139       C  
ATOM   1214  O   SER B  78     -21.142  -1.164  13.158  1.00 14.47           O  
ANISOU 1214  O   SER B  78     1746   1556   2195   -128    145    229       O  
ATOM   1215  CB  SER B  78     -18.241   0.260  14.134  1.00 15.93           C  
ANISOU 1215  CB  SER B  78     1810   2190   2053    351   -724     57       C  
ATOM   1216  OG  SER B  78     -19.200   1.131  14.708  1.00 15.07           O  
ANISOU 1216  OG  SER B  78     1747   1776   2205    139   -480    381       O  
ATOM   1217  N   SER B  79     -19.590  -2.499  14.112  1.00 13.52           N  
ANISOU 1217  N   SER B  79     1915   1376   1845     86     -8    160       N  
ATOM   1218  CA  SER B  79     -20.540  -3.519  14.526  1.00 16.08           C  
ANISOU 1218  CA  SER B  79     2331   1798   1981    -24    -24    -36       C  
ATOM   1219  C   SER B  79     -21.139  -3.184  15.884  1.00 14.61           C  
ANISOU 1219  C   SER B  79     2106   1557   1888    114    140    -41       C  
ATOM   1220  O   SER B  79     -20.570  -2.401  16.651  1.00 15.34           O  
ANISOU 1220  O   SER B  79     2420   1631   1778    265     36     62       O  
ATOM   1221  CB  SER B  79     -19.851  -4.880  14.591  1.00 17.29           C  
ANISOU 1221  CB  SER B  79     2652   1999   1919    466   -284   -244       C  
ATOM   1222  OG  SER B  79     -18.984  -4.955  15.706  1.00 21.84           O  
ANISOU 1222  OG  SER B  79     3793   2385   2119    747     84     87       O  
ATOM   1223  N   PRO B  80     -22.304  -3.754  16.207  1.00 15.70           N  
ANISOU 1223  N   PRO B  80     1871   2084   2011   -261     53   -121       N  
ATOM   1224  CA  PRO B  80     -22.845  -3.576  17.565  1.00 17.01           C  
ANISOU 1224  CA  PRO B  80     2146   2273   2045   -351    -99     74       C  
ATOM   1225  C   PRO B  80     -21.897  -4.043  18.656  1.00 16.45           C  
ANISOU 1225  C   PRO B  80     2281   1842   2126   -643     58    113       C  
ATOM   1226  O   PRO B  80     -21.870  -3.441  19.736  1.00 16.33           O  
ANISOU 1226  O   PRO B  80     2222   2077   1907  -1158    -70    -84       O  
ATOM   1227  CB  PRO B  80     -24.133  -4.410  17.538  1.00 17.69           C  
ANISOU 1227  CB  PRO B  80     1889   2839   1994   -340   -161     53       C  
ATOM   1228  CG  PRO B  80     -24.542  -4.414  16.104  1.00 18.78           C  
ANISOU 1228  CG  PRO B  80     2019   3004   2114   -377     -2   -189       C  
ATOM   1229  CD  PRO B  80     -23.260  -4.436  15.315  1.00 17.61           C  
ANISOU 1229  CD  PRO B  80     1818   2759   2113   -220    335   -115       C  
ATOM   1230  N   ASP B  81     -21.110  -5.094  18.404  1.00 14.15           N  
ANISOU 1230  N   ASP B  81     2265    785   2328   -425    235    187       N  
ATOM   1231  CA  ASP B  81     -20.133  -5.549  19.387  1.00 14.32           C  
ANISOU 1231  CA  ASP B  81     2467    852   2123   -271    427    155       C  
ATOM   1232  C   ASP B  81     -19.047  -4.513  19.651  1.00 14.44           C  
ANISOU 1232  C   ASP B  81     2793    859   1835   -181    310    -82       C  
ATOM   1233  O   ASP B  81     -18.412  -4.559  20.711  1.00 16.63           O  
ANISOU 1233  O   ASP B  81     3154   1315   1851   -353    370    316       O  
ATOM   1234  CB  ASP B  81     -19.479  -6.854  18.928  1.00 18.97           C  
ANISOU 1234  CB  ASP B  81     3116   1444   2650   -657    875    140       C  
ATOM   1235  CG  ASP B  81     -20.470  -7.994  18.783  1.00 25.43           C  
ANISOU 1235  CG  ASP B  81     3938   2493   3230   -440   1032   -471       C  
ATOM   1236  OD1 ASP B  81     -21.488  -8.011  19.507  1.00 27.44           O  
ANISOU 1236  OD1 ASP B  81     3944   2923   3558   -629   1398    -41       O  
ATOM   1237  OD2 ASP B  81     -20.220  -8.883  17.944  1.00 27.19           O  
ANISOU 1237  OD2 ASP B  81     4303   2451   3575   -589    971   -631       O  
ATOM   1238  N   ASP B  82     -18.819  -3.587  18.717  1.00 14.82           N  
ANISOU 1238  N   ASP B  82     2786   1368   1476    -24    342     47       N  
ATOM   1239  CA  ASP B  82     -17.741  -2.609  18.826  1.00 13.25           C  
ANISOU 1239  CA  ASP B  82     2281   1342   1410   -164    110    -70       C  
ATOM   1240  C   ASP B  82     -18.076  -1.416  19.716  1.00 12.47           C  
ANISOU 1240  C   ASP B  82     1848   1384   1504    596    112   -222       C  
ATOM   1241  O   ASP B  82     -17.176  -0.623  20.009  1.00 13.63           O  
ANISOU 1241  O   ASP B  82     1409   2017   1751    379      0    -10       O  
ATOM   1242  CB  ASP B  82     -17.362  -2.060  17.444  1.00 13.71           C  
ANISOU 1242  CB  ASP B  82     2338   1835   1037     11    372     61       C  
ATOM   1243  CG  ASP B  82     -16.772  -3.108  16.517  1.00 13.99           C  
ANISOU 1243  CG  ASP B  82     2255   1903   1158   -207    119    152       C  
ATOM   1244  OD1 ASP B  82     -16.280  -4.153  16.992  1.00 14.18           O  
ANISOU 1244  OD1 ASP B  82     2074   2020   1296    332    262    264       O  
ATOM   1245  OD2 ASP B  82     -16.790  -2.866  15.291  1.00 13.34           O  
ANISOU 1245  OD2 ASP B  82     2332   1578   1160   -340    115    -38       O  
ATOM   1246  N   GLN B  83     -19.330  -1.256  20.143  1.00 13.28           N  
ANISOU 1246  N   GLN B  83     1927   1495   1622     73    146    104       N  
ATOM   1247  CA  GLN B  83     -19.812   0.020  20.682  1.00 11.82           C  
ANISOU 1247  CA  GLN B  83     1760   1359   1374    286      0   -357       C  
ATOM   1248  C   GLN B  83     -19.449   0.169  22.162  1.00 12.90           C  
ANISOU 1248  C   GLN B  83     2018   1352   1530   -199   -429     -2       C  
ATOM   1249  O   GLN B  83     -20.301   0.170  23.053  1.00 14.74           O  
ANISOU 1249  O   GLN B  83     2473   1534   1594   -195   -705    165       O  
ATOM   1250  CB  GLN B  83     -21.315   0.135  20.472  1.00 11.88           C  
ANISOU 1250  CB  GLN B  83     1764   1554   1195    612   -301   -249       C  
ATOM   1251  CG  GLN B  83     -21.744  -0.066  19.032  1.00 14.29           C  
ANISOU 1251  CG  GLN B  83     2117   1820   1495     42     56   -408       C  
ATOM   1252  CD  GLN B  83     -21.056   0.900  18.093  1.00 15.04           C  
ANISOU 1252  CD  GLN B  83     2468   1808   1439   -248    371    -61       C  
ATOM   1253  OE1 GLN B  83     -21.080   2.113  18.305  1.00 16.78           O  
ANISOU 1253  OE1 GLN B  83     2862   2119   1396    -61    142     54       O  
ATOM   1254  NE2 GLN B  83     -20.425   0.367  17.054  1.00 15.15           N  
ANISOU 1254  NE2 GLN B  83     2358   1767   1630   -354    341   -265       N  
ATOM   1255  N   ILE B  84     -18.155   0.348  22.414  1.00 11.28           N  
ANISOU 1255  N   ILE B  84     1895   1054   1338   -232   -675    -51       N  
ATOM   1256  CA  ILE B  84     -17.656   0.427  23.784  1.00 11.84           C  
ANISOU 1256  CA  ILE B  84     2210   1103   1184   -512   -182     -1       C  
ATOM   1257  C   ILE B  84     -16.269   1.058  23.762  1.00 13.87           C  
ANISOU 1257  C   ILE B  84     3023   1094   1152    -80   -165    -68       C  
ATOM   1258  O   ILE B  84     -15.453   0.769  22.882  1.00 15.08           O  
ANISOU 1258  O   ILE B  84     3297   1153   1282   -258    -30    329       O  
ATOM   1259  CB  ILE B  84     -17.657  -0.973  24.448  1.00 11.81           C  
ANISOU 1259  CB  ILE B  84     2224   1243   1018   -578    148     72       C  
ATOM   1260  CG1 ILE B  84     -17.120  -0.913  25.880  1.00 11.36           C  
ANISOU 1260  CG1 ILE B  84     2185   1207    926   -425    290    299       C  
ATOM   1261  CG2 ILE B  84     -16.868  -1.967  23.612  1.00 12.83           C  
ANISOU 1261  CG2 ILE B  84     2313   1528   1034   -772    474     49       C  
ATOM   1262  CD1 ILE B  84     -17.273  -2.220  26.631  1.00 10.85           C  
ANISOU 1262  CD1 ILE B  84     1747   1452    925   -180    554    316       C  
ATOM   1263  N   GLY B  85     -16.011   1.931  24.732  1.00 13.44           N  
ANISOU 1263  N   GLY B  85     2787    921   1399   -229    -21    239       N  
ATOM   1264  CA  GLY B  85     -14.717   2.582  24.816  1.00 12.03           C  
ANISOU 1264  CA  GLY B  85     2555    785   1230     95    346    111       C  
ATOM   1265  C   GLY B  85     -14.705   3.629  25.911  1.00 12.48           C  
ANISOU 1265  C   GLY B  85     2808   1054    881    347    392     93       C  
ATOM   1266  O   GLY B  85     -15.541   3.609  26.817  1.00 15.50           O  
ANISOU 1266  O   GLY B  85     3334   1495   1058    255    299   -297       O  
ATOM   1267  N   TYR B  86     -13.744   4.548  25.809  1.00 10.43           N  
ANISOU 1267  N   TYR B  86     2117    983    862    297    237   -188       N  
ATOM   1268  CA  TYR B  86     -13.540   5.561  26.834  1.00 10.65           C  
ANISOU 1268  CA  TYR B  86     2044   1252    749    383   -165    288       C  
ATOM   1269  C   TYR B  86     -13.322   6.927  26.199  1.00 10.52           C  
ANISOU 1269  C   TYR B  86     2075   1033    889    156   -277    163       C  
ATOM   1270  O   TYR B  86     -12.881   7.037  25.051  1.00 11.87           O  
ANISOU 1270  O   TYR B  86     2508   1021    980    239   -261     94       O  
ATOM   1271  CB  TYR B  86     -12.340   5.216  27.738  1.00 10.87           C  
ANISOU 1271  CB  TYR B  86     1771   1517    843    483    -48    286       C  
ATOM   1272  CG  TYR B  86     -11.009   5.142  27.016  1.00  8.74           C  
ANISOU 1272  CG  TYR B  86      982   1379    958    186     31    382       C  
ATOM   1273  CD1 TYR B  86     -10.602   3.972  26.387  1.00  9.16           C  
ANISOU 1273  CD1 TYR B  86      674   1616   1192    293   -128    177       C  
ATOM   1274  CD2 TYR B  86     -10.154   6.236  26.974  1.00  9.88           C  
ANISOU 1274  CD2 TYR B  86     1038   1622   1094    334    143    465       C  
ATOM   1275  CE1 TYR B  86      -9.388   3.896  25.727  1.00 10.65           C  
ANISOU 1275  CE1 TYR B  86      925   1632   1488     -5   -343    464       C  
ATOM   1276  CE2 TYR B  86      -8.934   6.169  26.316  1.00 10.82           C  
ANISOU 1276  CE2 TYR B  86     1274   1525   1313    612   -167    468       C  
ATOM   1277  CZ  TYR B  86      -8.557   4.997  25.694  1.00 12.54           C  
ANISOU 1277  CZ  TYR B  86     1227   1914   1623    596   -163    496       C  
ATOM   1278  OH  TYR B  86      -7.346   4.920  25.036  1.00 12.24           O  
ANISOU 1278  OH  TYR B  86      851   2076   1724    487    106    282       O  
ATOM   1279  N   TYR B  87     -13.649   7.969  26.960  1.00  8.41           N  
ANISOU 1279  N   TYR B  87     1844    757    593    306   -204    -16       N  
ATOM   1280  CA  TYR B  87     -13.234   9.329  26.653  1.00 10.74           C  
ANISOU 1280  CA  TYR B  87     2027   1064    991    108   -443   -282       C  
ATOM   1281  C   TYR B  87     -12.021   9.678  27.503  1.00 12.52           C  
ANISOU 1281  C   TYR B  87     2122   1433   1200   -107   -582    204       C  
ATOM   1282  O   TYR B  87     -11.991   9.393  28.703  1.00 12.47           O  
ANISOU 1282  O   TYR B  87     2049   1643   1046   -517   -669    159       O  
ATOM   1283  CB  TYR B  87     -14.347  10.342  26.926  1.00 11.14           C  
ANISOU 1283  CB  TYR B  87     1962   1199   1070    332   -463    -80       C  
ATOM   1284  CG  TYR B  87     -15.485  10.346  25.934  1.00 11.04           C  
ANISOU 1284  CG  TYR B  87     2286    985    924    272   -365    228       C  
ATOM   1285  CD1 TYR B  87     -16.543   9.456  26.057  1.00 10.83           C  
ANISOU 1285  CD1 TYR B  87     1952   1211    952    339   -407    -19       C  
ATOM   1286  CD2 TYR B  87     -15.520  11.267  24.894  1.00 10.00           C  
ANISOU 1286  CD2 TYR B  87     2050    962    788     43   -550   -103       C  
ATOM   1287  CE1 TYR B  87     -17.594   9.470  25.163  1.00 11.17           C  
ANISOU 1287  CE1 TYR B  87     2117   1231    898     91   -548   -298       C  
ATOM   1288  CE2 TYR B  87     -16.568  11.291  23.996  1.00 10.68           C  
ANISOU 1288  CE2 TYR B  87     2123    973    964   -196   -589   -148       C  
ATOM   1289  CZ  TYR B  87     -17.601  10.389  24.134  1.00 11.67           C  
ANISOU 1289  CZ  TYR B  87     2130   1398    907   -337   -468   -259       C  
ATOM   1290  OH  TYR B  87     -18.645  10.411  23.240  1.00 12.05           O  
ANISOU 1290  OH  TYR B  87     2021   1565    993    235   -388   -167       O  
ATOM   1291  N   ARG B  88     -11.025  10.300  26.878  1.00 13.55           N  
ANISOU 1291  N   ARG B  88     2006   1485   1657     91   -337    129       N  
ATOM   1292  CA  ARG B  88      -9.803  10.709  27.557  1.00 13.70           C  
ANISOU 1292  CA  ARG B  88     1996   1532   1676    467   -579    153       C  
ATOM   1293  C   ARG B  88      -9.672  12.223  27.492  1.00 13.90           C  
ANISOU 1293  C   ARG B  88     2117   1581   1585    -76   -825    -35       C  
ATOM   1294  O   ARG B  88      -9.769  12.814  26.411  1.00 15.03           O  
ANISOU 1294  O   ARG B  88     2937   1206   1568   -150   -901     92       O  
ATOM   1295  CB  ARG B  88      -8.572  10.049  26.934  1.00 16.15           C  
ANISOU 1295  CB  ARG B  88     1860   1997   2277    887   -713    162       C  
ATOM   1296  CG  ARG B  88      -7.261  10.470  27.577  1.00 18.77           C  
ANISOU 1296  CG  ARG B  88     2439   1902   2792    394   -788    -49       C  
ATOM   1297  CD  ARG B  88      -6.082   9.767  26.928  1.00 21.84           C  
ANISOU 1297  CD  ARG B  88     2627   2457   3212    231   -881     69       C  
ATOM   1298  NE  ARG B  88      -4.811  10.165  27.523  1.00 24.93           N  
ANISOU 1298  NE  ARG B  88     3198   2741   3534     75   -718     91       N  
ATOM   1299  CZ  ARG B  88      -4.097  11.209  27.120  1.00 28.17           C  
ANISOU 1299  CZ  ARG B  88     3425   3580   3697   -295   -814    547       C  
ATOM   1300  NH1 ARG B  88      -4.532  11.966  26.123  1.00 28.35           N  
ANISOU 1300  NH1 ARG B  88     3357   3819   3598   -153   -887    849       N  
ATOM   1301  NH2 ARG B  88      -2.949  11.498  27.717  1.00 30.07           N  
ANISOU 1301  NH2 ARG B  88     3425   4094   3908   -205   -914    616       N  
ATOM   1302  N   ARG B  89      -9.447  12.842  28.647  1.00 12.55           N  
ANISOU 1302  N   ARG B  89     1824   1403   1541   -217   -922   -164       N  
ATOM   1303  CA  ARG B  89      -9.319  14.289  28.731  1.00 13.85           C  
ANISOU 1303  CA  ARG B  89     1984   1597   1682   -280  -1042    -36       C  
ATOM   1304  C   ARG B  89      -7.917  14.721  28.319  1.00 15.75           C  
ANISOU 1304  C   ARG B  89     2366   1819   1799   -207   -890    251       C  
ATOM   1305  O   ARG B  89      -6.922  14.135  28.757  1.00 16.76           O  
ANISOU 1305  O   ARG B  89     2284   2107   1977    -82  -1240    298       O  
ATOM   1306  CB  ARG B  89      -9.622  14.761  30.152  1.00 13.26           C  
ANISOU 1306  CB  ARG B  89     2001   1286   1751   -328   -970     49       C  
ATOM   1307  CG  ARG B  89      -9.562  16.267  30.347  1.00 14.90           C  
ANISOU 1307  CG  ARG B  89     2469   1287   1906   -168  -1120   -248       C  
ATOM   1308  CD  ARG B  89      -9.801  16.615  31.804  1.00 18.33           C  
ANISOU 1308  CD  ARG B  89     3261   1513   2189      5  -1388   -238       C  
ATOM   1309  NE  ARG B  89      -8.817  15.968  32.665  1.00 21.86           N  
ANISOU 1309  NE  ARG B  89     3859   2310   2135    236  -1551   -298       N  
ATOM   1310  CZ  ARG B  89      -9.042  15.599  33.921  1.00 23.11           C  
ANISOU 1310  CZ  ARG B  89     3939   2759   2081     70  -1530   -224       C  
ATOM   1311  NH1 ARG B  89     -10.229  15.805  34.476  1.00 24.77           N  
ANISOU 1311  NH1 ARG B  89     3997   3347   2065    -29  -1492   -221       N  
ATOM   1312  NH2 ARG B  89      -8.080  15.014  34.618  1.00 22.65           N  
ANISOU 1312  NH2 ARG B  89     3643   2598   2365    174  -1631    242       N  
ATOM   1313  N   ALA B  90      -7.843  15.744  27.471  1.00 14.86           N  
ANISOU 1313  N   ALA B  90     2294   1584   1766   -166   -714     -2       N  
ATOM   1314  CA  ALA B  90      -6.585  16.368  27.086  1.00 14.90           C  
ANISOU 1314  CA  ALA B  90     2175   1505   1983     27   -597   -283       C  
ATOM   1315  C   ALA B  90      -6.656  17.847  27.432  1.00 16.50           C  
ANISOU 1315  C   ALA B  90     2068   1745   2458    121   -716   -235       C  
ATOM   1316  O   ALA B  90      -7.601  18.534  27.035  1.00 15.71           O  
ANISOU 1316  O   ALA B  90     1853   1517   2600    386   -577   -139       O  
ATOM   1317  CB  ALA B  90      -6.299  16.179  25.594  1.00 12.79           C  
ANISOU 1317  CB  ALA B  90     1875   1267   1719    684   -457   -635       C  
ATOM   1318  N   THR B  91      -5.663  18.332  28.172  1.00 18.94           N  
ANISOU 1318  N   THR B  91     2088   2350   2760    449   -982    133       N  
ATOM   1319  CA  THR B  91      -5.650  19.702  28.664  1.00 23.02           C  
ANISOU 1319  CA  THR B  91     2517   3055   3174    564   -897    162       C  
ATOM   1320  C   THR B  91      -4.473  20.459  28.065  1.00 23.30           C  
ANISOU 1320  C   THR B  91     2500   2794   3559    258   -826    634       C  
ATOM   1321  O   THR B  91      -3.350  19.945  28.032  1.00 25.59           O  
ANISOU 1321  O   THR B  91     2805   3146   3772   -118   -657   1168       O  
ATOM   1322  CB  THR B  91      -5.577  19.730  30.192  1.00 26.97           C  
ANISOU 1322  CB  THR B  91     3155   3659   3434    284   -765    100       C  
ATOM   1323  OG1 THR B  91      -4.469  18.934  30.634  1.00 31.03           O  
ANISOU 1323  OG1 THR B  91     3986   3928   3878    387   -835    370       O  
ATOM   1324  CG2 THR B  91      -6.863  19.183  30.794  1.00 24.96           C  
ANISOU 1324  CG2 THR B  91     2634   3487   3362   -605   -749   -508       C  
ATOM   1325  N   ARG B  92      -4.736  21.672  27.589  1.00 23.18           N  
ANISOU 1325  N   ARG B  92     2238   2762   3808     89   -480    118       N  
ATOM   1326  CA  ARG B  92      -3.711  22.565  27.072  1.00 23.44           C  
ANISOU 1326  CA  ARG B  92     2432   2671   3803    224   -298   -238       C  
ATOM   1327  C   ARG B  92      -3.608  23.786  27.973  1.00 21.74           C  
ANISOU 1327  C   ARG B  92     1926   2550   3786    -95   -103   -409       C  
ATOM   1328  O   ARG B  92      -4.616  24.263  28.503  1.00 20.67           O  
ANISOU 1328  O   ARG B  92     1676   2462   3717   -156   -126   -546       O  
ATOM   1329  CB  ARG B  92      -4.027  23.001  25.639  1.00 25.82           C  
ANISOU 1329  CB  ARG B  92     3033   2974   3802    346   -412   -569       C  
ATOM   1330  CG  ARG B  92      -3.979  21.884  24.611  1.00 27.21           C  
ANISOU 1330  CG  ARG B  92     3239   3224   3875    645   -366   -607       C  
ATOM   1331  CD  ARG B  92      -4.439  22.388  23.253  1.00 28.12           C  
ANISOU 1331  CD  ARG B  92     3602   3269   3812    757    -80   -304       C  
ATOM   1332  NE  ARG B  92      -5.815  22.874  23.302  1.00 32.23           N  
ANISOU 1332  NE  ARG B  92     4698   3524   4025    212     64   -185       N  
ATOM   1333  CZ  ARG B  92      -6.463  23.400  22.267  1.00 31.98           C  
ANISOU 1333  CZ  ARG B  92     4604   3542   4005     52    314   -428       C  
ATOM   1334  NH1 ARG B  92      -5.859  23.514  21.092  1.00 32.96           N  
ANISOU 1334  NH1 ARG B  92     4717   3834   3974   -110    431   -638       N  
ATOM   1335  NH2 ARG B  92      -7.715  23.814  22.407  1.00 30.21           N  
ANISOU 1335  NH2 ARG B  92     4106   3395   3976    186    820   -530       N  
ATOM   1336  N   ARG B  93      -2.392  24.294  28.142  1.00 23.36           N  
ANISOU 1336  N   ARG B  93     1933   2915   4028    520   -216   -334       N  
ATOM   1337  CA  ARG B  93      -2.154  25.445  28.999  1.00 27.26           C  
ANISOU 1337  CA  ARG B  93     2412   3592   4352    -42   -359   -255       C  
ATOM   1338  C   ARG B  93      -1.270  26.455  28.284  1.00 28.54           C  
ANISOU 1338  C   ARG B  93     2580   3742   4522   -243   -169   -414       C  
ATOM   1339  O   ARG B  93      -0.352  26.083  27.548  1.00 28.85           O  
ANISOU 1339  O   ARG B  93     2507   3830   4624   -132    175   -203       O  
ATOM   1340  CB  ARG B  93      -1.528  25.015  30.328  1.00 31.52           C  
ANISOU 1340  CB  ARG B  93     3080   4271   4627   -296   -381     51       C  
ATOM   1341  CG  ARG B  93      -2.499  24.240  31.196  1.00 36.18           C  
ANISOU 1341  CG  ARG B  93     3632   5200   4915   -191   -543    267       C  
ATOM   1342  CD  ARG B  93      -1.804  23.419  32.258  1.00 40.22           C  
ANISOU 1342  CD  ARG B  93     4379   5688   5216   -239   -696    361       C  
ATOM   1343  NE  ARG B  93      -2.743  22.513  32.913  1.00 43.40           N  
ANISOU 1343  NE  ARG B  93     5089   5992   5410   -535   -994    197       N  
ATOM   1344  CZ  ARG B  93      -3.004  21.278  32.498  1.00 44.48           C  
ANISOU 1344  CZ  ARG B  93     5400   6064   5436   -692  -1275     58       C  
ATOM   1345  NH1 ARG B  93      -2.395  20.794  31.423  1.00 44.79           N  
ANISOU 1345  NH1 ARG B  93     5513   6039   5465   -700  -1249    -20       N  
ATOM   1346  NH2 ARG B  93      -3.875  20.525  33.157  1.00 44.16           N  
ANISOU 1346  NH2 ARG B  93     5329   6069   5380   -756  -1519    -58       N  
ATOM   1347  N   ILE B  94      -1.563  27.734  28.504  1.00 30.19           N  
ANISOU 1347  N   ILE B  94     2963   3866   4641   -600   -291   -617       N  
ATOM   1348  CA  ILE B  94      -0.883  28.840  27.841  1.00 32.49           C  
ANISOU 1348  CA  ILE B  94     3498   3934   4911  -1019   -153   -788       C  
ATOM   1349  C   ILE B  94      -0.543  29.890  28.888  1.00 33.98           C  
ANISOU 1349  C   ILE B  94     3551   3981   5379  -1000    179   -972       C  
ATOM   1350  O   ILE B  94      -1.394  30.254  29.707  1.00 32.42           O  
ANISOU 1350  O   ILE B  94     3051   3805   5462  -1115    252   -929       O  
ATOM   1351  CB  ILE B  94      -1.752  29.451  26.724  1.00 35.21           C  
ANISOU 1351  CB  ILE B  94     4139   4322   4919   -833   -138   -600       C  
ATOM   1352  CG1 ILE B  94      -1.829  28.501  25.527  1.00 38.46           C  
ANISOU 1352  CG1 ILE B  94     4648   4792   5171   -695   -163   -398       C  
ATOM   1353  CG2 ILE B  94      -1.223  30.814  26.307  1.00 36.85           C  
ANISOU 1353  CG2 ILE B  94     4607   4475   4920   -339   -127   -625       C  
ATOM   1354  CD1 ILE B  94      -2.660  29.032  24.378  1.00 40.38           C  
ANISOU 1354  CD1 ILE B  94     4978   5013   5350   -419    -41   -303       C  
ATOM   1355  N   ARG B  95       0.699  30.369  28.869  1.00 35.59           N  
ANISOU 1355  N   ARG B  95     3812   4091   5622  -1075    264  -1097       N  
ATOM   1356  CA  ARG B  95       1.110  31.437  29.771  1.00 38.24           C  
ANISOU 1356  CA  ARG B  95     4103   4548   5877   -830    130   -830       C  
ATOM   1357  C   ARG B  95       0.544  32.759  29.265  1.00 39.29           C  
ANISOU 1357  C   ARG B  95     4335   4480   6113   -790    228   -383       C  
ATOM   1358  O   ARG B  95       0.868  33.196  28.155  1.00 40.19           O  
ANISOU 1358  O   ARG B  95     4661   4536   6073   -832    703    -47       O  
ATOM   1359  CB  ARG B  95       2.632  31.495  29.879  1.00 38.91           C  
ANISOU 1359  CB  ARG B  95     4001   4980   5804   -379   -167  -1046       C  
ATOM   1360  CG  ARG B  95       3.126  32.292  31.075  1.00 40.20           C  
ANISOU 1360  CG  ARG B  95     4133   5311   5830   -357   -325   -964       C  
ATOM   1361  CD  ARG B  95       4.600  32.042  31.352  1.00 40.43           C  
ANISOU 1361  CD  ARG B  95     4104   5516   5743   -490   -374   -791       C  
ATOM   1362  NE  ARG B  95       5.000  32.590  32.645  1.00 40.38           N  
ANISOU 1362  NE  ARG B  95     4070   5602   5669   -368   -258   -406       N  
ATOM   1363  CZ  ARG B  95       5.403  33.843  32.832  1.00 39.53           C  
ANISOU 1363  CZ  ARG B  95     3834   5673   5513   -271   -222    122       C  
ATOM   1364  NH1 ARG B  95       5.465  34.680  31.805  1.00 39.79           N  
ANISOU 1364  NH1 ARG B  95     4120   5588   5410    203   -112    476       N  
ATOM   1365  NH2 ARG B  95       5.744  34.260  34.045  1.00 36.53           N  
ANISOU 1365  NH2 ARG B  95     3057   5546   5276   -428   -609    229       N  
ATOM   1366  N   GLY B  96      -0.305  33.390  30.073  1.00 38.22           N  
ANISOU 1366  N   GLY B  96     3971   4254   6297   -880   -233   -424       N  
ATOM   1367  CA  GLY B  96      -0.994  34.592  29.660  1.00 37.06           C  
ANISOU 1367  CA  GLY B  96     3726   3995   6359   -723   -537   -321       C  
ATOM   1368  C   GLY B  96      -0.114  35.826  29.695  1.00 37.80           C  
ANISOU 1368  C   GLY B  96     3836   4122   6404   -468   -660   -242       C  
ATOM   1369  O   GLY B  96       1.063  35.792  30.054  1.00 36.69           O  
ANISOU 1369  O   GLY B  96     3584   3965   6392  -1039   -609   -231       O  
ATOM   1370  N   GLY B  97      -0.718  36.951  29.304  1.00 38.06           N  
ANISOU 1370  N   GLY B  97     3842   4277   6341     21   -829   -112       N  
ATOM   1371  CA  GLY B  97      -0.018  38.222  29.331  1.00 39.33           C  
ANISOU 1371  CA  GLY B  97     4211   4354   6380    -97   -937   -220       C  
ATOM   1372  C   GLY B  97       0.353  38.686  30.723  1.00 41.41           C  
ANISOU 1372  C   GLY B  97     4704   4511   6520   -310   -995   -179       C  
ATOM   1373  O   GLY B  97       1.265  39.507  30.872  1.00 41.24           O  
ANISOU 1373  O   GLY B  97     4501   4505   6662   -841  -1437   -150       O  
ATOM   1374  N   ASP B  98      -0.333  38.183  31.747  1.00 42.13           N  
ANISOU 1374  N   ASP B  98     5088   4434   6486   -425   -704   -301       N  
ATOM   1375  CA  ASP B  98      -0.017  38.496  33.133  1.00 43.81           C  
ANISOU 1375  CA  ASP B  98     5370   4792   6485   -498   -430   -531       C  
ATOM   1376  C   ASP B  98       0.973  37.513  33.746  1.00 42.25           C  
ANISOU 1376  C   ASP B  98     5090   4570   6394   -612   -469   -505       C  
ATOM   1377  O   ASP B  98       1.186  37.542  34.962  1.00 41.96           O  
ANISOU 1377  O   ASP B  98     5179   4423   6343   -538   -474   -701       O  
ATOM   1378  CB  ASP B  98      -1.297  38.532  33.973  1.00 46.43           C  
ANISOU 1378  CB  ASP B  98     5779   5286   6578   -723   -229   -725       C  
ATOM   1379  CG  ASP B  98      -2.037  37.205  33.974  1.00 49.49           C  
ANISOU 1379  CG  ASP B  98     6267   5882   6655   -769    -75   -748       C  
ATOM   1380  OD1 ASP B  98      -1.703  36.330  33.147  1.00 50.82           O  
ANISOU 1380  OD1 ASP B  98     6508   6016   6783  -1103   -186   -737       O  
ATOM   1381  OD2 ASP B  98      -2.952  37.037  34.807  1.00 50.44           O  
ANISOU 1381  OD2 ASP B  98     6424   6137   6603   -583    -12   -748       O  
ATOM   1382  N   GLY B  99       1.577  36.645  32.937  1.00 40.49           N  
ANISOU 1382  N   GLY B  99     4750   4254   6381   -933   -521   -325       N  
ATOM   1383  CA  GLY B  99       2.492  35.645  33.440  1.00 40.43           C  
ANISOU 1383  CA  GLY B  99     4833   4148   6382  -1042   -407   -227       C  
ATOM   1384  C   GLY B  99       1.840  34.462  34.120  1.00 41.04           C  
ANISOU 1384  C   GLY B  99     4864   4380   6351   -691   -182   -603       C  
ATOM   1385  O   GLY B  99       2.555  33.555  34.566  1.00 41.99           O  
ANISOU 1385  O   GLY B  99     5017   4402   6534   -287    -38   -899       O  
ATOM   1386  N   LYS B 100       0.514  34.439  34.219  1.00 38.87           N  
ANISOU 1386  N   LYS B 100     4440   4320   6010   -808   -130   -693       N  
ATOM   1387  CA  LYS B 100      -0.196  33.327  34.832  1.00 37.33           C  
ANISOU 1387  CA  LYS B 100     4319   4241   5623  -1193   -304  -1098       C  
ATOM   1388  C   LYS B 100      -0.485  32.254  33.791  1.00 33.00           C  
ANISOU 1388  C   LYS B 100     3527   3785   5224   -815   -596  -1225       C  
ATOM   1389  O   LYS B 100      -0.755  32.558  32.625  1.00 29.11           O  
ANISOU 1389  O   LYS B 100     2362   3679   5021   -703   -627   -846       O  
ATOM   1390  CB  LYS B 100      -1.505  33.804  35.466  1.00 40.03           C  
ANISOU 1390  CB  LYS B 100     4990   4638   5582  -1373    -31  -1139       C  
ATOM   1391  CG  LYS B 100      -1.332  34.781  36.619  1.00 43.24           C  
ANISOU 1391  CG  LYS B 100     5598   5190   5640  -1209    291  -1118       C  
ATOM   1392  CD  LYS B 100      -0.652  34.120  37.808  1.00 46.48           C  
ANISOU 1392  CD  LYS B 100     6207   5646   5808  -1220    604  -1162       C  
ATOM   1393  CE  LYS B 100      -1.509  34.216  39.063  1.00 47.33           C  
ANISOU 1393  CE  LYS B 100     6201   5831   5953  -1261    812  -1107       C  
ATOM   1394  NZ  LYS B 100      -1.793  35.627  39.448  1.00 47.06           N  
ANISOU 1394  NZ  LYS B 100     6114   5790   5978  -1183    894  -1201       N  
ATOM   1395  N   MET B 101      -0.418  30.997  34.218  1.00 31.78           N  
ANISOU 1395  N   MET B 101     3687   3385   5004  -1073  -1066  -1499       N  
ATOM   1396  CA  MET B 101      -0.787  29.893  33.343  1.00 32.38           C  
ANISOU 1396  CA  MET B 101     3607   3696   4998   -712  -1305  -1342       C  
ATOM   1397  C   MET B 101      -2.298  29.864  33.161  1.00 31.25           C  
ANISOU 1397  C   MET B 101     3614   3564   4695   -783  -1218  -1145       C  
ATOM   1398  O   MET B 101      -3.052  29.859  34.139  1.00 32.73           O  
ANISOU 1398  O   MET B 101     3971   3902   4561   -969  -1257  -1298       O  
ATOM   1399  CB  MET B 101      -0.292  28.568  33.918  1.00 35.24           C  
ANISOU 1399  CB  MET B 101     3740   4324   5324   -503  -1095  -1248       C  
ATOM   1400  CG  MET B 101       1.221  28.437  33.948  1.00 39.54           C  
ANISOU 1400  CG  MET B 101     4206   5214   5602   -122  -1118  -1163       C  
ATOM   1401  SD  MET B 101       1.956  28.612  32.310  1.00 42.29           S  
ANISOU 1401  SD  MET B 101     4257   6056   5756    198  -1197  -1194       S  
ATOM   1402  CE  MET B 101       1.213  27.226  31.454  1.00 41.70           C  
ANISOU 1402  CE  MET B 101     4256   5906   5682   -190  -1178  -1198       C  
ATOM   1403  N   LYS B 102      -2.738  29.857  31.905  1.00 27.77           N  
ANISOU 1403  N   LYS B 102     3161   3086   4305   -624  -1485  -1084       N  
ATOM   1404  CA  LYS B 102      -4.152  29.835  31.558  1.00 26.89           C  
ANISOU 1404  CA  LYS B 102     3164   2974   4078  -1108  -1113   -955       C  
ATOM   1405  C   LYS B 102      -4.501  28.477  30.970  1.00 24.32           C  
ANISOU 1405  C   LYS B 102     2703   2893   3645  -1015  -1126   -656       C  
ATOM   1406  O   LYS B 102      -3.774  27.962  30.116  1.00 24.40           O  
ANISOU 1406  O   LYS B 102     2295   3251   3726   -784   -626   -517       O  
ATOM   1407  CB  LYS B 102      -4.491  30.942  30.556  1.00 29.14           C  
ANISOU 1407  CB  LYS B 102     3429   3257   4386  -1070  -1013   -972       C  
ATOM   1408  CG  LYS B 102      -4.088  32.337  31.001  1.00 32.17           C  
ANISOU 1408  CG  LYS B 102     4217   3493   4514   -854   -388  -1230       C  
ATOM   1409  CD  LYS B 102      -4.817  32.751  32.268  1.00 34.87           C  
ANISOU 1409  CD  LYS B 102     4736   3861   4651   -650     64  -1479       C  
ATOM   1410  CE  LYS B 102      -4.363  34.126  32.733  1.00 36.45           C  
ANISOU 1410  CE  LYS B 102     4953   4126   4772   -366    421  -1569       C  
ATOM   1411  NZ  LYS B 102      -5.036  34.538  33.995  1.00 38.18           N  
ANISOU 1411  NZ  LYS B 102     5058   4441   5007   -173    477  -1726       N  
ATOM   1412  N   ASP B 103      -5.611  27.904  31.423  1.00 22.10           N  
ANISOU 1412  N   ASP B 103     2893   2521   2983  -1084  -1082   -195       N  
ATOM   1413  CA  ASP B 103      -6.078  26.622  30.914  1.00 22.06           C  
ANISOU 1413  CA  ASP B 103     2611   2954   2818   -537  -1240    379       C  
ATOM   1414  C   ASP B 103      -7.040  26.849  29.757  1.00 19.54           C  
ANISOU 1414  C   ASP B 103     1996   2827   2602    -91   -966   -144       C  
ATOM   1415  O   ASP B 103      -8.087  27.483  29.931  1.00 19.58           O  
ANISOU 1415  O   ASP B 103     1779   3004   2658    469   -688   -614       O  
ATOM   1416  CB  ASP B 103      -6.761  25.817  32.018  1.00 27.14           C  
ANISOU 1416  CB  ASP B 103     3479   3492   3341   -315  -1522   1013       C  
ATOM   1417  CG  ASP B 103      -5.778  25.029  32.855  1.00 35.13           C  
ANISOU 1417  CG  ASP B 103     5106   4268   3974   -375  -1500   1261       C  
ATOM   1418  OD1 ASP B 103      -4.754  25.609  33.271  1.00 38.77           O  
ANISOU 1418  OD1 ASP B 103     5496   5043   4191   -362  -1686   1277       O  
ATOM   1419  OD2 ASP B 103      -6.034  23.833  33.102  1.00 39.08           O  
ANISOU 1419  OD2 ASP B 103     6093   4391   4363   -397  -1184   1272       O  
ATOM   1420  N   LEU B 104      -6.686  26.343  28.579  1.00 16.60           N  
ANISOU 1420  N   LEU B 104     1560   2439   2307    215  -1006   -291       N  
ATOM   1421  CA  LEU B 104      -7.684  26.195  27.533  1.00 14.73           C  
ANISOU 1421  CA  LEU B 104     1440   2045   2111    201   -532   -752       C  
ATOM   1422  C   LEU B 104      -8.680  25.122  27.955  1.00 14.71           C  
ANISOU 1422  C   LEU B 104     1677   1962   1950    312   -810   -375       C  
ATOM   1423  O   LEU B 104      -8.369  24.246  28.766  1.00 15.85           O  
ANISOU 1423  O   LEU B 104     1927   2200   1896    304  -1102     68       O  
ATOM   1424  CB  LEU B 104      -7.029  25.830  26.201  1.00 16.48           C  
ANISOU 1424  CB  LEU B 104     1755   2094   2412    590   -414   -343       C  
ATOM   1425  CG  LEU B 104      -6.071  26.874  25.617  1.00 16.86           C  
ANISOU 1425  CG  LEU B 104     1867   1783   2756    961    -21   -380       C  
ATOM   1426  CD1 LEU B 104      -5.512  26.411  24.284  1.00 17.84           C  
ANISOU 1426  CD1 LEU B 104     1616   2124   3037   1076     80    -51       C  
ATOM   1427  CD2 LEU B 104      -6.767  28.221  25.465  1.00 18.91           C  
ANISOU 1427  CD2 LEU B 104     2516   1750   2921   1026    364   -574       C  
ATOM   1428  N   SER B 105      -9.891  25.208  27.418  1.00 13.61           N  
ANISOU 1428  N   SER B 105     1603   1639   1927    -30   -808    -29       N  
ATOM   1429  CA  SER B 105     -10.937  24.274  27.809  1.00 13.59           C  
ANISOU 1429  CA  SER B 105     1562   1365   2235     37   -851   -131       C  
ATOM   1430  C   SER B 105     -10.479  22.842  27.556  1.00 13.32           C  
ANISOU 1430  C   SER B 105     1523   1589   1949    253   -886   -389       C  
ATOM   1431  O   SER B 105      -9.955  22.546  26.472  1.00 15.06           O  
ANISOU 1431  O   SER B 105     2154   1494   2076    370   -683   -510       O  
ATOM   1432  CB  SER B 105     -12.227  24.554  27.043  1.00 16.41           C  
ANISOU 1432  CB  SER B 105     1859   1444   2931    307   -547   -249       C  
ATOM   1433  OG  SER B 105     -12.782  25.804  27.407  1.00 16.62           O  
ANISOU 1433  OG  SER B 105     2084    913   3316     67   -411   -316       O  
ATOM   1434  N   PRO B 106     -10.626  21.941  28.525  1.00 11.27           N  
ANISOU 1434  N   PRO B 106     1216   1410   1654    362   -775   -276       N  
ATOM   1435  CA  PRO B 106     -10.258  20.541  28.287  1.00 12.83           C  
ANISOU 1435  CA  PRO B 106     1701   1548   1627    -36   -893   -234       C  
ATOM   1436  C   PRO B 106     -11.065  19.957  27.139  1.00 12.35           C  
ANISOU 1436  C   PRO B 106     1785   1260   1646   -214   -816   -130       C  
ATOM   1437  O   PRO B 106     -12.237  20.285  26.948  1.00 13.81           O  
ANISOU 1437  O   PRO B 106     2199   1362   1686    279   -480    116       O  
ATOM   1438  CB  PRO B 106     -10.592  19.852  29.616  1.00 13.11           C  
ANISOU 1438  CB  PRO B 106     1527   1869   1584    125   -909   -239       C  
ATOM   1439  CG  PRO B 106     -10.557  20.946  30.629  1.00 14.23           C  
ANISOU 1439  CG  PRO B 106     1806   1819   1783    424   -628   -297       C  
ATOM   1440  CD  PRO B 106     -11.047  22.177  29.916  1.00 12.40           C  
ANISOU 1440  CD  PRO B 106     1345   1740   1624    564   -745   -317       C  
ATOM   1441  N   ARG B 107     -10.419  19.092  26.364  1.00 13.41           N  
ANISOU 1441  N   ARG B 107     1818   1455   1821   -103   -289    -97       N  
ATOM   1442  CA  ARG B 107     -11.062  18.395  25.261  1.00 13.03           C  
ANISOU 1442  CA  ARG B 107     1616   1377   1959   -183   -418    -35       C  
ATOM   1443  C   ARG B 107     -11.065  16.904  25.561  1.00 11.01           C  
ANISOU 1443  C   ARG B 107      833   1246   2103   -395   -212     68       C  
ATOM   1444  O   ARG B 107     -10.031  16.340  25.935  1.00 14.17           O  
ANISOU 1444  O   ARG B 107     1121   1611   2652   -275    -62    -14       O  
ATOM   1445  CB  ARG B 107     -10.351  18.683  23.938  1.00 14.25           C  
ANISOU 1445  CB  ARG B 107     1998   1407   2009   -103   -302    101       C  
ATOM   1446  CG  ARG B 107     -10.415  20.145  23.518  1.00 17.35           C  
ANISOU 1446  CG  ARG B 107     2312   2122   2160    -22   -127    526       C  
ATOM   1447  CD  ARG B 107      -9.716  20.373  22.187  1.00 22.51           C  
ANISOU 1447  CD  ARG B 107     3090   2798   2666    126    -32    230       C  
ATOM   1448  NE  ARG B 107      -8.313  19.974  22.231  1.00 27.15           N  
ANISOU 1448  NE  ARG B 107     3934   3303   3077     90    443   -264       N  
ATOM   1449  CZ  ARG B 107      -7.457  20.140  21.228  1.00 30.30           C  
ANISOU 1449  CZ  ARG B 107     4404   3637   3471    170    276   -685       C  
ATOM   1450  NH1 ARG B 107      -7.858  20.703  20.096  1.00 30.28           N  
ANISOU 1450  NH1 ARG B 107     4855   3147   3505   -156    533   -917       N  
ATOM   1451  NH2 ARG B 107      -6.198  19.743  21.357  1.00 32.09           N  
ANISOU 1451  NH2 ARG B 107     4211   4204   3778    621    117   -944       N  
ATOM   1452  N   TRP B 108     -12.225  16.273  25.413  1.00  8.57           N  
ANISOU 1452  N   TRP B 108      498   1090   1668   -107    228    114       N  
ATOM   1453  CA  TRP B 108     -12.395  14.850  25.678  1.00  7.39           C  
ANISOU 1453  CA  TRP B 108      887    669   1253   -176    -19    127       C  
ATOM   1454  C   TRP B 108     -12.529  14.119  24.347  1.00  8.98           C  
ANISOU 1454  C   TRP B 108     1392    874   1145     -2   -335   -183       C  
ATOM   1455  O   TRP B 108     -13.412  14.445  23.546  1.00 10.34           O  
ANISOU 1455  O   TRP B 108     1446   1327   1154     -7   -197    209       O  
ATOM   1456  CB  TRP B 108     -13.619  14.602  26.560  1.00  9.09           C  
ANISOU 1456  CB  TRP B 108     1244   1113   1095    135   -316   -128       C  
ATOM   1457  CG  TRP B 108     -13.515  15.190  27.946  1.00  9.59           C  
ANISOU 1457  CG  TRP B 108     1422   1149   1074   -160   -448   -346       C  
ATOM   1458  CD1 TRP B 108     -13.588  16.511  28.287  1.00 11.39           C  
ANISOU 1458  CD1 TRP B 108     1470   1882    976    217   -605   -294       C  
ATOM   1459  CD2 TRP B 108     -13.340  14.469  29.172  1.00 10.35           C  
ANISOU 1459  CD2 TRP B 108     1419   1425   1089     98   -562     86       C  
ATOM   1460  NE1 TRP B 108     -13.459  16.655  29.649  1.00 11.69           N  
ANISOU 1460  NE1 TRP B 108     1438   1711   1293    526   -681    -77       N  
ATOM   1461  CE2 TRP B 108     -13.308  15.418  30.215  1.00 11.39           C  
ANISOU 1461  CE2 TRP B 108     1408   1704   1218    127   -733    236       C  
ATOM   1462  CE3 TRP B 108     -13.204  13.113  29.490  1.00  9.75           C  
ANISOU 1462  CE3 TRP B 108     1371   1190   1143     38   -364    599       C  
ATOM   1463  CZ2 TRP B 108     -13.144  15.055  31.552  1.00 13.43           C  
ANISOU 1463  CZ2 TRP B 108     1894   1687   1521    449   -562    632       C  
ATOM   1464  CZ3 TRP B 108     -13.041  12.754  30.819  1.00 11.86           C  
ANISOU 1464  CZ3 TRP B 108     1642   1610   1255     83   -676    332       C  
ATOM   1465  CH2 TRP B 108     -13.014  13.721  31.833  1.00 14.04           C  
ANISOU 1465  CH2 TRP B 108     1920   1744   1670   -274   -551    434       C  
ATOM   1466  N   TYR B 109     -11.657  13.139  24.116  1.00  9.89           N  
ANISOU 1466  N   TYR B 109     1484   1033   1243    457   -588     52       N  
ATOM   1467  CA  TYR B 109     -11.632  12.369  22.877  1.00  9.87           C  
ANISOU 1467  CA  TYR B 109     1650    845   1254    183   -349     23       C  
ATOM   1468  C   TYR B 109     -12.037  10.925  23.142  1.00 10.05           C  
ANISOU 1468  C   TYR B 109     1630    982   1206    106   -219     45       C  
ATOM   1469  O   TYR B 109     -11.615  10.327  24.137  1.00 10.70           O  
ANISOU 1469  O   TYR B 109     1741   1134   1190    288   -218    111       O  
ATOM   1470  CB  TYR B 109     -10.239  12.384  22.240  1.00  9.66           C  
ANISOU 1470  CB  TYR B 109     1539    758   1371    269    152    165       C  
ATOM   1471  CG  TYR B 109      -9.777  13.730  21.728  1.00 11.81           C  
ANISOU 1471  CG  TYR B 109     2026    887   1573     16    -93    244       C  
ATOM   1472  CD1 TYR B 109      -9.112  14.621  22.560  1.00 12.18           C  
ANISOU 1472  CD1 TYR B 109     2002    836   1787    -67    -96    234       C  
ATOM   1473  CD2 TYR B 109      -9.981  14.097  20.404  1.00 14.94           C  
ANISOU 1473  CD2 TYR B 109     2513   1234   1928    -94   -306    403       C  
ATOM   1474  CE1 TYR B 109      -8.677  15.845  22.093  1.00 14.58           C  
ANISOU 1474  CE1 TYR B 109     2246   1332   1961   -180   -168    296       C  
ATOM   1475  CE2 TYR B 109      -9.549  15.318  19.927  1.00 16.59           C  
ANISOU 1475  CE2 TYR B 109     2671   1506   2126     73   -331    332       C  
ATOM   1476  CZ  TYR B 109      -8.900  16.189  20.776  1.00 16.16           C  
ANISOU 1476  CZ  TYR B 109     2536   1558   2048   -236   -130    284       C  
ATOM   1477  OH  TYR B 109      -8.471  17.406  20.306  1.00 16.85           O  
ANISOU 1477  OH  TYR B 109     2454   1745   2202   -420    -17    368       O  
ATOM   1478  N   PHE B 110     -12.827  10.355  22.234  1.00  9.20           N  
ANISOU 1478  N   PHE B 110     1367    875   1254   -336   -337     26       N  
ATOM   1479  CA  PHE B 110     -13.285   8.980  22.376  1.00  8.81           C  
ANISOU 1479  CA  PHE B 110     1185    779   1385   -530   -158    -11       C  
ATOM   1480  C   PHE B 110     -12.324   8.006  21.706  1.00  9.84           C  
ANISOU 1480  C   PHE B 110     1701    701   1335    -13   -344    118       C  
ATOM   1481  O   PHE B 110     -11.872   8.229  20.578  1.00 10.93           O  
ANISOU 1481  O   PHE B 110     1981    912   1258    243   -409    375       O  
ATOM   1482  CB  PHE B 110     -14.684   8.799  21.782  1.00  9.49           C  
ANISOU 1482  CB  PHE B 110     1315    892   1400    -56    122    173       C  
ATOM   1483  CG  PHE B 110     -15.153   7.367  21.785  1.00  8.67           C  
ANISOU 1483  CG  PHE B 110     1233    668   1393   -359   -139     52       C  
ATOM   1484  CD1 PHE B 110     -15.733   6.817  22.917  1.00  9.84           C  
ANISOU 1484  CD1 PHE B 110     1241    956   1540   -406     81    -31       C  
ATOM   1485  CD2 PHE B 110     -14.990   6.565  20.665  1.00  9.86           C  
ANISOU 1485  CD2 PHE B 110     1495    749   1501   -449   -493    154       C  
ATOM   1486  CE1 PHE B 110     -16.153   5.498  22.931  1.00 10.87           C  
ANISOU 1486  CE1 PHE B 110     1582    939   1609   -133   -193     27       C  
ATOM   1487  CE2 PHE B 110     -15.406   5.242  20.670  1.00 10.49           C  
ANISOU 1487  CE2 PHE B 110     1786    827   1373   -329   -202    479       C  
ATOM   1488  CZ  PHE B 110     -15.990   4.708  21.805  1.00  9.91           C  
ANISOU 1488  CZ  PHE B 110     1500    991   1274   -342   -342    333       C  
ATOM   1489  N   TYR B 111     -12.034   6.910  22.405  1.00 10.06           N  
ANISOU 1489  N   TYR B 111     1745    775   1300    391   -277   -256       N  
ATOM   1490  CA  TYR B 111     -11.247   5.807  21.873  1.00 10.03           C  
ANISOU 1490  CA  TYR B 111     1444    972   1394     17   -394    -93       C  
ATOM   1491  C   TYR B 111     -11.965   4.497  22.156  1.00 10.22           C  
ANISOU 1491  C   TYR B 111     1638   1012   1233    173   -258   -336       C  
ATOM   1492  O   TYR B 111     -12.456   4.278  23.268  1.00 10.61           O  
ANISOU 1492  O   TYR B 111     1722   1269   1042   -242    275    277       O  
ATOM   1493  CB  TYR B 111      -9.841   5.762  22.487  1.00 10.08           C  
ANISOU 1493  CB  TYR B 111     1030   1311   1489     35   -678     69       C  
ATOM   1494  CG  TYR B 111      -8.984   6.959  22.152  1.00 12.48           C  
ANISOU 1494  CG  TYR B 111     1739   1372   1632   -318   -607    502       C  
ATOM   1495  CD1 TYR B 111      -8.236   6.994  20.982  1.00 12.70           C  
ANISOU 1495  CD1 TYR B 111     1613   1502   1710   -635   -377    457       C  
ATOM   1496  CD2 TYR B 111      -8.918   8.052  23.006  1.00 12.76           C  
ANISOU 1496  CD2 TYR B 111     1822   1419   1607   -162   -503     51       C  
ATOM   1497  CE1 TYR B 111      -7.449   8.088  20.669  1.00 14.73           C  
ANISOU 1497  CE1 TYR B 111     1713   1846   2036   -213   -630    764       C  
ATOM   1498  CE2 TYR B 111      -8.134   9.150  22.701  1.00 15.55           C  
ANISOU 1498  CE2 TYR B 111     1779   2115   2016     34   -556    151       C  
ATOM   1499  CZ  TYR B 111      -7.402   9.162  21.532  1.00 15.74           C  
ANISOU 1499  CZ  TYR B 111     1871   1893   2217   -244   -562    689       C  
ATOM   1500  OH  TYR B 111      -6.619  10.249  21.226  1.00 18.18           O  
ANISOU 1500  OH  TYR B 111     2152   2132   2624   -298   -777    839       O  
ATOM   1501  N   TYR B 112     -12.022   3.627  21.153  1.00 10.26           N  
ANISOU 1501  N   TYR B 112     1844    882   1173    -78   -538   -241       N  
ATOM   1502  CA  TYR B 112     -12.608   2.312  21.364  1.00 10.58           C  
ANISOU 1502  CA  TYR B 112     1832   1000   1187   -185   -533   -152       C  
ATOM   1503  C   TYR B 112     -11.794   1.526  22.385  1.00 11.11           C  
ANISOU 1503  C   TYR B 112     1950    935   1337    -63   -362     69       C  
ATOM   1504  O   TYR B 112     -10.581   1.712  22.525  1.00 11.06           O  
ANISOU 1504  O   TYR B 112     1634    995   1573    212   -375     98       O  
ATOM   1505  CB  TYR B 112     -12.695   1.545  20.043  1.00  9.43           C  
ANISOU 1505  CB  TYR B 112     1704    786   1094   -129   -471   -226       C  
ATOM   1506  CG  TYR B 112     -13.751   2.093  19.115  1.00 10.22           C  
ANISOU 1506  CG  TYR B 112     1763   1059   1061    102   -360    -14       C  
ATOM   1507  CD1 TYR B 112     -15.079   1.706  19.241  1.00  9.48           C  
ANISOU 1507  CD1 TYR B 112     1318   1257   1028    712    165   -116       C  
ATOM   1508  CD2 TYR B 112     -13.426   3.013  18.125  1.00 10.44           C  
ANISOU 1508  CD2 TYR B 112     1866   1434    666    179   -327    250       C  
ATOM   1509  CE1 TYR B 112     -16.051   2.210  18.402  1.00 10.21           C  
ANISOU 1509  CE1 TYR B 112     1697   1410    772    355   -249    301       C  
ATOM   1510  CE2 TYR B 112     -14.394   3.522  17.278  1.00 11.13           C  
ANISOU 1510  CE2 TYR B 112     1657   1544   1029    143    -99    121       C  
ATOM   1511  CZ  TYR B 112     -15.705   3.118  17.423  1.00 11.99           C  
ANISOU 1511  CZ  TYR B 112     2008   1571    979   -154   -493      4       C  
ATOM   1512  OH  TYR B 112     -16.673   3.623  16.588  1.00 13.91           O  
ANISOU 1512  OH  TYR B 112     2645   1526   1113    216   -506     40       O  
ATOM   1513  N   LEU B 113     -12.489   0.661  23.120  1.00  9.64           N  
ANISOU 1513  N   LEU B 113     1754    739   1169    -44   -386    380       N  
ATOM   1514  CA  LEU B 113     -11.857  -0.176  24.131  1.00 11.16           C  
ANISOU 1514  CA  LEU B 113     1949   1010   1282    293   -222    524       C  
ATOM   1515  C   LEU B 113     -10.661  -0.921  23.551  1.00 13.76           C  
ANISOU 1515  C   LEU B 113     2180   1463   1586    746      5    516       C  
ATOM   1516  O   LEU B 113     -10.740  -1.501  22.465  1.00 14.08           O  
ANISOU 1516  O   LEU B 113     2458   1416   1476    695     42    471       O  
ATOM   1517  CB  LEU B 113     -12.882  -1.167  24.681  1.00  9.84           C  
ANISOU 1517  CB  LEU B 113     1446   1340    953    -13   -229    621       C  
ATOM   1518  CG  LEU B 113     -12.363  -2.244  25.629  1.00 10.14           C  
ANISOU 1518  CG  LEU B 113     1681   1084   1088    136   -144    628       C  
ATOM   1519  CD1 LEU B 113     -11.911  -1.619  26.940  1.00 11.78           C  
ANISOU 1519  CD1 LEU B 113     1864   1476   1135    143    -25    346       C  
ATOM   1520  CD2 LEU B 113     -13.436  -3.296  25.860  1.00 12.59           C  
ANISOU 1520  CD2 LEU B 113     2222    969   1594    189   -295    555       C  
ATOM   1521  N   GLY B 114      -9.545  -0.888  24.278  1.00 13.73           N  
ANISOU 1521  N   GLY B 114     1983   1650   1585    797     49    510       N  
ATOM   1522  CA  GLY B 114      -8.338  -1.559  23.840  1.00 12.85           C  
ANISOU 1522  CA  GLY B 114     1513   1570   1797    585    297    479       C  
ATOM   1523  C   GLY B 114      -7.529  -0.823  22.796  1.00 13.04           C  
ANISOU 1523  C   GLY B 114     1237   2004   1715    713    192     90       C  
ATOM   1524  O   GLY B 114      -6.601  -1.412  22.229  1.00 14.23           O  
ANISOU 1524  O   GLY B 114     1363   2129   1915    383    109    381       O  
ATOM   1525  N   THR B 115      -7.853   0.439  22.517  1.00 10.79           N  
ANISOU 1525  N   THR B 115     1202   1298   1598    713    188    244       N  
ATOM   1526  CA  THR B 115      -7.123   1.266  21.568  1.00 11.53           C  
ANISOU 1526  CA  THR B 115     1459   1498   1423    490    -42    476       C  
ATOM   1527  C   THR B 115      -6.736   2.578  22.237  1.00 11.41           C  
ANISOU 1527  C   THR B 115     1602   1451   1281     41     21    618       C  
ATOM   1528  O   THR B 115      -7.252   2.936  23.299  1.00 11.78           O  
ANISOU 1528  O   THR B 115     1598   1828   1052    398     22    202       O  
ATOM   1529  CB  THR B 115      -7.952   1.575  20.312  1.00 11.44           C  
ANISOU 1529  CB  THR B 115     1466   1444   1437    557   -241    171       C  
ATOM   1530  OG1 THR B 115      -8.932   2.573  20.629  1.00 10.50           O  
ANISOU 1530  OG1 THR B 115     1343   1246   1399    178    351    103       O  
ATOM   1531  CG2 THR B 115      -8.655   0.329  19.793  1.00 12.20           C  
ANISOU 1531  CG2 THR B 115     1609   1624   1404    203   -464    179       C  
ATOM   1532  N   GLY B 116      -5.826   3.306  21.594  1.00 12.43           N  
ANISOU 1532  N   GLY B 116     1433   1687   1601   -527    -22    678       N  
ATOM   1533  CA  GLY B 116      -5.517   4.659  21.992  1.00 13.86           C  
ANISOU 1533  CA  GLY B 116     1432   1964   1869   -434    -58    504       C  
ATOM   1534  C   GLY B 116      -4.507   4.751  23.116  1.00 15.93           C  
ANISOU 1534  C   GLY B 116     1910   2074   2069    157   -371    479       C  
ATOM   1535  O   GLY B 116      -3.826   3.778  23.457  1.00 17.21           O  
ANISOU 1535  O   GLY B 116     2597   1878   2064    554   -282    618       O  
ATOM   1536  N   PRO B 117      -4.396   5.941  23.717  1.00 15.59           N  
ANISOU 1536  N   PRO B 117     1790   2089   2046     58   -380    224       N  
ATOM   1537  CA  PRO B 117      -3.374   6.148  24.757  1.00 17.38           C  
ANISOU 1537  CA  PRO B 117     2266   2203   2135     34   -228    238       C  
ATOM   1538  C   PRO B 117      -3.537   5.239  25.961  1.00 17.19           C  
ANISOU 1538  C   PRO B 117     2063   2294   2176    390   -243    327       C  
ATOM   1539  O   PRO B 117      -2.549   4.952  26.648  1.00 19.40           O  
ANISOU 1539  O   PRO B 117     1960   2734   2676    601   -111    206       O  
ATOM   1540  CB  PRO B 117      -3.557   7.625  25.138  1.00 16.48           C  
ANISOU 1540  CB  PRO B 117     2384   1952   1925   -160   -609    543       C  
ATOM   1541  CG  PRO B 117      -4.263   8.243  23.967  1.00 18.04           C  
ANISOU 1541  CG  PRO B 117     2412   2274   2170   -365   -605    207       C  
ATOM   1542  CD  PRO B 117      -5.151   7.170  23.425  1.00 15.31           C  
ANISOU 1542  CD  PRO B 117     2006   1707   2103   -563   -430    -55       C  
ATOM   1543  N   GLU B 118      -4.750   4.777  26.240  1.00 15.13           N  
ANISOU 1543  N   GLU B 118     1887   1971   1891    300    114     79       N  
ATOM   1544  CA  GLU B 118      -5.016   3.866  27.346  1.00 15.91           C  
ANISOU 1544  CA  GLU B 118     2136   2135   1773    276   -272    287       C  
ATOM   1545  C   GLU B 118      -5.505   2.518  26.829  1.00 15.60           C  
ANISOU 1545  C   GLU B 118     2000   2148   1781    212   -529    382       C  
ATOM   1546  O   GLU B 118      -6.448   1.930  27.363  1.00 15.22           O  
ANISOU 1546  O   GLU B 118     1918   1987   1880     51   -405    444       O  
ATOM   1547  CB  GLU B 118      -6.021   4.475  28.320  1.00 17.08           C  
ANISOU 1547  CB  GLU B 118     2188   2540   1761    380   -320    237       C  
ATOM   1548  CG  GLU B 118      -5.543   5.758  28.985  1.00 19.15           C  
ANISOU 1548  CG  GLU B 118     2654   2587   2035    646   -406    215       C  
ATOM   1549  CD  GLU B 118      -4.407   5.528  29.970  1.00 26.79           C  
ANISOU 1549  CD  GLU B 118     4256   3032   2891     56   -519     70       C  
ATOM   1550  OE1 GLU B 118      -4.161   4.362  30.348  1.00 28.42           O  
ANISOU 1550  OE1 GLU B 118     4584   3306   2909      1  -1011    160       O  
ATOM   1551  OE2 GLU B 118      -3.758   6.519  30.370  1.00 31.33           O  
ANISOU 1551  OE2 GLU B 118     5119   3392   3392   -235   -540    124       O  
ATOM   1552  N   ALA B 119      -4.853   2.013  25.778  1.00 15.79           N  
ANISOU 1552  N   ALA B 119     2154   2075   1773    214   -499    310       N  
ATOM   1553  CA  ALA B 119      -5.264   0.754  25.167  1.00 15.49           C  
ANISOU 1553  CA  ALA B 119     2319   1739   1828    189   -458    334       C  
ATOM   1554  C   ALA B 119      -5.143  -0.425  26.121  1.00 15.11           C  
ANISOU 1554  C   ALA B 119     1819   1720   2203    351   -611    535       C  
ATOM   1555  O   ALA B 119      -5.812  -1.443  25.919  1.00 15.76           O  
ANISOU 1555  O   ALA B 119     1362   2179   2447   -113   -437    340       O  
ATOM   1556  CB  ALA B 119      -4.436   0.487  23.909  1.00 15.74           C  
ANISOU 1556  CB  ALA B 119     2514   1749   1719    308   -347    525       C  
ATOM   1557  N   GLY B 120      -4.311  -0.314  27.155  1.00 15.40           N  
ANISOU 1557  N   GLY B 120     1636   1812   2404    495   -589    691       N  
ATOM   1558  CA  GLY B 120      -4.136  -1.401  28.096  1.00 17.49           C  
ANISOU 1558  CA  GLY B 120     1887   2222   2537    701   -503    821       C  
ATOM   1559  C   GLY B 120      -5.128  -1.453  29.232  1.00 19.38           C  
ANISOU 1559  C   GLY B 120     2239   2459   2665    653   -272    730       C  
ATOM   1560  O   GLY B 120      -5.158  -2.444  29.966  1.00 21.17           O  
ANISOU 1560  O   GLY B 120     2569   2398   3078    778    -96    791       O  
ATOM   1561  N   LEU B 121      -5.948  -0.413  29.400  1.00 17.99           N  
ANISOU 1561  N   LEU B 121     2256   2237   2344    655    -61    165       N  
ATOM   1562  CA  LEU B 121      -6.894  -0.395  30.508  1.00 17.94           C  
ANISOU 1562  CA  LEU B 121     2298   2404   2114    604   -411    195       C  
ATOM   1563  C   LEU B 121      -8.098  -1.283  30.198  1.00 15.89           C  
ANISOU 1563  C   LEU B 121     1985   2132   1921    391   -538    192       C  
ATOM   1564  O   LEU B 121      -8.602  -1.276  29.071  1.00 17.54           O  
ANISOU 1564  O   LEU B 121     2290   2309   2066    786   -400    323       O  
ATOM   1565  CB  LEU B 121      -7.372   1.028  30.792  1.00 17.68           C  
ANISOU 1565  CB  LEU B 121     2293   2516   1908    627   -620     97       C  
ATOM   1566  CG  LEU B 121      -6.358   2.048  31.310  1.00 19.87           C  
ANISOU 1566  CG  LEU B 121     2710   2963   1878    477   -510    256       C  
ATOM   1567  CD1 LEU B 121      -7.048   3.371  31.598  1.00 19.46           C  
ANISOU 1567  CD1 LEU B 121     2493   3156   1744    577     -4    122       C  
ATOM   1568  CD2 LEU B 121      -5.660   1.527  32.553  1.00 19.25           C  
ANISOU 1568  CD2 LEU B 121     2551   3119   1645    203   -848    643       C  
ATOM   1569  N   PRO B 122      -8.571  -2.055  31.172  1.00 16.28           N  
ANISOU 1569  N   PRO B 122     2170   2109   1905    436   -702    457       N  
ATOM   1570  CA  PRO B 122      -9.850  -2.749  31.007  1.00 15.58           C  
ANISOU 1570  CA  PRO B 122     2339   1765   1818    275   -370    485       C  
ATOM   1571  C   PRO B 122     -11.008  -1.779  31.172  1.00 15.52           C  
ANISOU 1571  C   PRO B 122     2464   1622   1811    -72   -118    574       C  
ATOM   1572  O   PRO B 122     -10.876  -0.708  31.769  1.00 15.79           O  
ANISOU 1572  O   PRO B 122     2930   1248   1822     73      6    445       O  
ATOM   1573  CB  PRO B 122      -9.835  -3.781  32.136  1.00 17.09           C  
ANISOU 1573  CB  PRO B 122     2616   2166   1713     31   -486    614       C  
ATOM   1574  CG  PRO B 122      -9.042  -3.110  33.208  1.00 18.57           C  
ANISOU 1574  CG  PRO B 122     2838   2346   1873   -111   -350    649       C  
ATOM   1575  CD  PRO B 122      -7.968  -2.323  32.489  1.00 18.15           C  
ANISOU 1575  CD  PRO B 122     2566   2375   1955    -92   -788    752       C  
ATOM   1576  N   TYR B 123     -12.161  -2.175  30.635  1.00 13.33           N  
ANISOU 1576  N   TYR B 123     1726   1916   1423   -317    -83    243       N  
ATOM   1577  CA  TYR B 123     -13.350  -1.342  30.745  1.00 13.49           C  
ANISOU 1577  CA  TYR B 123     2091   1752   1284     10   -256    231       C  
ATOM   1578  C   TYR B 123     -13.688  -1.085  32.208  1.00 15.05           C  
ANISOU 1578  C   TYR B 123     2554   1727   1439    300     13    229       C  
ATOM   1579  O   TYR B 123     -13.704  -2.007  33.027  1.00 15.00           O  
ANISOU 1579  O   TYR B 123     2420   1567   1713     63    202    596       O  
ATOM   1580  CB  TYR B 123     -14.537  -2.000  30.045  1.00 13.92           C  
ANISOU 1580  CB  TYR B 123     1791   2156   1343    146   -206    306       C  
ATOM   1581  CG  TYR B 123     -15.775  -1.135  30.073  1.00 14.16           C  
ANISOU 1581  CG  TYR B 123     1857   2046   1478     43   -284    583       C  
ATOM   1582  CD1 TYR B 123     -15.975  -0.155  29.114  1.00 13.64           C  
ANISOU 1582  CD1 TYR B 123     1885   1991   1305    196   -617    636       C  
ATOM   1583  CD2 TYR B 123     -16.732  -1.283  31.071  1.00 16.07           C  
ANISOU 1583  CD2 TYR B 123     2139   2309   1657    253   -247    695       C  
ATOM   1584  CE1 TYR B 123     -17.095   0.646  29.134  1.00 16.57           C  
ANISOU 1584  CE1 TYR B 123     1971   2739   1587    -58   -522    413       C  
ATOM   1585  CE2 TYR B 123     -17.860  -0.481  31.101  1.00 16.85           C  
ANISOU 1585  CE2 TYR B 123     2030   2646   1725     20   -411    515       C  
ATOM   1586  CZ  TYR B 123     -18.033   0.481  30.127  1.00 17.98           C  
ANISOU 1586  CZ  TYR B 123     1986   2927   1917    -84   -511    245       C  
ATOM   1587  OH  TYR B 123     -19.148   1.286  30.141  1.00 19.31           O  
ANISOU 1587  OH  TYR B 123     2078   3104   2154    -52   -261   -310       O  
ATOM   1588  N   GLY B 124     -13.964   0.176  32.532  1.00 13.41           N  
ANISOU 1588  N   GLY B 124     2897   1231    965    365    192    -81       N  
ATOM   1589  CA  GLY B 124     -14.296   0.559  33.886  1.00 14.18           C  
ANISOU 1589  CA  GLY B 124     2818   1479   1090    371    317     78       C  
ATOM   1590  C   GLY B 124     -13.117   0.925  34.758  1.00 15.61           C  
ANISOU 1590  C   GLY B 124     3235   1589   1105    114    509    362       C  
ATOM   1591  O   GLY B 124     -13.323   1.280  35.927  1.00 17.99           O  
ANISOU 1591  O   GLY B 124     3550   1903   1381    223    460    172       O  
ATOM   1592  N   ALA B 125     -11.893   0.849  34.233  1.00 15.53           N  
ANISOU 1592  N   ALA B 125     3355   1369   1178    507    131    367       N  
ATOM   1593  CA  ALA B 125     -10.710   1.209  35.003  1.00 16.19           C  
ANISOU 1593  CA  ALA B 125     3292   1616   1243    390     64   -142       C  
ATOM   1594  C   ALA B 125     -10.853   2.609  35.586  1.00 17.45           C  
ANISOU 1594  C   ALA B 125     3429   1797   1403    302   -176    -37       C  
ATOM   1595  O   ALA B 125     -11.282   3.545  34.904  1.00 15.50           O  
ANISOU 1595  O   ALA B 125     3209   1499   1181     51    -25    434       O  
ATOM   1596  CB  ALA B 125      -9.459   1.127  34.126  1.00 15.91           C  
ANISOU 1596  CB  ALA B 125     3143   1602   1300    971     30   -207       C  
ATOM   1597  N   ASN B 126     -10.491   2.738  36.861  1.00 18.81           N  
ANISOU 1597  N   ASN B 126     3650   2135   1361     51   -734   -341       N  
ATOM   1598  CA  ASN B 126     -10.702   3.959  37.636  1.00 19.64           C  
ANISOU 1598  CA  ASN B 126     3637   2052   1775    524   -827   -420       C  
ATOM   1599  C   ASN B 126      -9.457   4.830  37.519  1.00 21.53           C  
ANISOU 1599  C   ASN B 126     3835   2115   2230    431  -1180     62       C  
ATOM   1600  O   ASN B 126      -8.462   4.609  38.215  1.00 24.20           O  
ANISOU 1600  O   ASN B 126     4211   2358   2626    -24  -1213    188       O  
ATOM   1601  CB  ASN B 126     -11.006   3.607  39.089  1.00 21.72           C  
ANISOU 1601  CB  ASN B 126     4066   2494   1691    645   -544   -465       C  
ATOM   1602  CG  ASN B 126     -11.537   4.783  39.882  1.00 25.72           C  
ANISOU 1602  CG  ASN B 126     4779   3240   1755    808   -213    -84       C  
ATOM   1603  OD1 ASN B 126     -12.074   5.738  39.320  1.00 27.75           O  
ANISOU 1603  OD1 ASN B 126     4835   3754   1954    978   -162    125       O  
ATOM   1604  ND2 ASN B 126     -11.396   4.714  41.203  1.00 25.88           N  
ANISOU 1604  ND2 ASN B 126     4906   3238   1688    596    277     59       N  
ATOM   1605  N   LYS B 127      -9.509   5.831  36.642  1.00 20.76           N  
ANISOU 1605  N   LYS B 127     3647   1980   2260    384  -1332    274       N  
ATOM   1606  CA  LYS B 127      -8.364   6.700  36.417  1.00 22.32           C  
ANISOU 1606  CA  LYS B 127     3845   2226   2408    655  -1173    202       C  
ATOM   1607  C   LYS B 127      -8.851   8.107  36.102  1.00 21.41           C  
ANISOU 1607  C   LYS B 127     3688   2171   2276     24   -950    140       C  
ATOM   1608  O   LYS B 127      -9.801   8.285  35.335  1.00 19.25           O  
ANISOU 1608  O   LYS B 127     3124   1978   2214     89   -741    204       O  
ATOM   1609  CB  LYS B 127      -7.481   6.171  35.279  1.00 24.42           C  
ANISOU 1609  CB  LYS B 127     3910   2586   2782   1126  -1002    218       C  
ATOM   1610  CG  LYS B 127      -6.222   6.990  35.042  1.00 28.12           C  
ANISOU 1610  CG  LYS B 127     4218   3328   3139   1430   -790    100       C  
ATOM   1611  CD  LYS B 127      -5.299   6.326  34.035  1.00 29.97           C  
ANISOU 1611  CD  LYS B 127     4389   3565   3435   1646   -312   -201       C  
ATOM   1612  CE  LYS B 127      -3.996   7.100  33.897  1.00 32.50           C  
ANISOU 1612  CE  LYS B 127     4777   3992   3580   1749    194   -379       C  
ATOM   1613  NZ  LYS B 127      -2.996   6.374  33.068  1.00 34.66           N  
ANISOU 1613  NZ  LYS B 127     5106   4450   3615   1610    448   -452       N  
ATOM   1614  N   ASP B 128      -8.195   9.101  36.700  1.00 22.19           N  
ANISOU 1614  N   ASP B 128     4148   2160   2125   -257   -986     30       N  
ATOM   1615  CA  ASP B 128      -8.580  10.488  36.478  1.00 22.43           C  
ANISOU 1615  CA  ASP B 128     4079   2516   1926   -378  -1172   -201       C  
ATOM   1616  C   ASP B 128      -8.377  10.876  35.018  1.00 20.62           C  
ANISOU 1616  C   ASP B 128     3516   2561   1756   -358  -1282      4       C  
ATOM   1617  O   ASP B 128      -7.354  10.558  34.405  1.00 20.52           O  
ANISOU 1617  O   ASP B 128     3226   2846   1725    -70  -1274    -97       O  
ATOM   1618  CB  ASP B 128      -7.773  11.415  37.387  1.00 28.08           C  
ANISOU 1618  CB  ASP B 128     4791   3462   2416   -241   -838   -416       C  
ATOM   1619  CG  ASP B 128      -8.075  12.881  37.139  1.00 34.08           C  
ANISOU 1619  CG  ASP B 128     5384   4578   2988   -829   -401   -438       C  
ATOM   1620  OD1 ASP B 128      -9.246  13.287  37.301  1.00 34.80           O  
ANISOU 1620  OD1 ASP B 128     5311   4896   3017   -770   -146   -458       O  
ATOM   1621  OD2 ASP B 128      -7.140  13.628  36.784  1.00 37.88           O  
ANISOU 1621  OD2 ASP B 128     5877   5091   3424  -1025   -521   -526       O  
ATOM   1622  N   GLY B 129      -9.365  11.573  34.462  1.00 17.53           N  
ANISOU 1622  N   GLY B 129     2865   2167   1629   -236  -1187    122       N  
ATOM   1623  CA  GLY B 129      -9.345  11.938  33.062  1.00 15.82           C  
ANISOU 1623  CA  GLY B 129     2840   1855   1314    130   -980      3       C  
ATOM   1624  C   GLY B 129      -9.822  10.860  32.114  1.00 14.79           C  
ANISOU 1624  C   GLY B 129     2590   1754   1277    100   -954    -21       C  
ATOM   1625  O   GLY B 129      -9.805  11.081  30.897  1.00 14.40           O  
ANISOU 1625  O   GLY B 129     2572   1569   1331     63   -600   -152       O  
ATOM   1626  N   ILE B 130     -10.239   9.703  32.628  1.00 14.70           N  
ANISOU 1626  N   ILE B 130     2702   1568   1314   -102   -846    149       N  
ATOM   1627  CA  ILE B 130     -10.757   8.599  31.829  1.00 13.85           C  
ANISOU 1627  CA  ILE B 130     2801   1034   1429    398   -539    219       C  
ATOM   1628  C   ILE B 130     -12.165   8.284  32.313  1.00 14.87           C  
ANISOU 1628  C   ILE B 130     3079   1233   1336      4   -448    217       C  
ATOM   1629  O   ILE B 130     -12.371   8.036  33.507  1.00 16.15           O  
ANISOU 1629  O   ILE B 130     3312   1649   1175   -104   -161    524       O  
ATOM   1630  CB  ILE B 130      -9.862   7.349  31.936  1.00 14.92           C  
ANISOU 1630  CB  ILE B 130     2897   1274   1497    311   -770    -41       C  
ATOM   1631  CG1 ILE B 130      -8.425   7.670  31.522  1.00 15.15           C  
ANISOU 1631  CG1 ILE B 130     2425   1782   1548    573   -561    349       C  
ATOM   1632  CG2 ILE B 130     -10.432   6.206  31.098  1.00 14.44           C  
ANISOU 1632  CG2 ILE B 130     3210   1016   1260    534   -289   -202       C  
ATOM   1633  CD1 ILE B 130      -8.284   8.100  30.086  1.00 16.50           C  
ANISOU 1633  CD1 ILE B 130     2527   2026   1717    487   -915    273       C  
ATOM   1634  N   ILE B 131     -13.131   8.297  31.395  1.00 14.50           N  
ANISOU 1634  N   ILE B 131     3043   1223   1243   -124   -221   -166       N  
ATOM   1635  CA  ILE B 131     -14.493   7.879  31.702  1.00 13.08           C  
ANISOU 1635  CA  ILE B 131     2321   1375   1272     -3   -229    -53       C  
ATOM   1636  C   ILE B 131     -14.948   6.899  30.631  1.00 12.72           C  
ANISOU 1636  C   ILE B 131     2146   1401   1285    361     59     67       C  
ATOM   1637  O   ILE B 131     -14.518   6.971  29.475  1.00 12.75           O  
ANISOU 1637  O   ILE B 131     2083   1434   1328    273    300    327       O  
ATOM   1638  CB  ILE B 131     -15.469   9.073  31.816  1.00 13.47           C  
ANISOU 1638  CB  ILE B 131     2332   1534   1251    471   -191   -104       C  
ATOM   1639  CG1 ILE B 131     -15.528   9.866  30.509  1.00 15.62           C  
ANISOU 1639  CG1 ILE B 131     2601   1905   1429    566   -249    187       C  
ATOM   1640  CG2 ILE B 131     -15.081   9.968  32.987  1.00 16.04           C  
ANISOU 1640  CG2 ILE B 131     2632   1863   1600    823   -332    -42       C  
ATOM   1641  CD1 ILE B 131     -16.754   9.569  29.679  1.00 16.41           C  
ANISOU 1641  CD1 ILE B 131     2614   2183   1438    173     18     68       C  
ATOM   1642  N   TRP B 132     -15.826   5.977  31.019  1.00 12.40           N  
ANISOU 1642  N   TRP B 132     2209   1227   1275   -166   -119     14       N  
ATOM   1643  CA  TRP B 132     -16.173   4.833  30.187  1.00 12.31           C  
ANISOU 1643  CA  TRP B 132     2187   1092   1400    230     10    494       C  
ATOM   1644  C   TRP B 132     -17.619   4.905  29.715  1.00 13.15           C  
ANISOU 1644  C   TRP B 132     2130   1500   1365    134     66    466       C  
ATOM   1645  O   TRP B 132     -18.504   5.359  30.448  1.00 16.04           O  
ANISOU 1645  O   TRP B 132     2474   2168   1453    297     78    308       O  
ATOM   1646  CB  TRP B 132     -15.926   3.528  30.950  1.00 11.78           C  
ANISOU 1646  CB  TRP B 132     1858   1148   1471    543   -141    527       C  
ATOM   1647  CG  TRP B 132     -14.477   3.331  31.259  1.00 12.22           C  
ANISOU 1647  CG  TRP B 132     2084   1136   1423    246   -391    569       C  
ATOM   1648  CD1 TRP B 132     -13.825   3.691  32.404  1.00 12.75           C  
ANISOU 1648  CD1 TRP B 132     2101   1146   1598    331   -366    521       C  
ATOM   1649  CD2 TRP B 132     -13.490   2.751  30.399  1.00 13.55           C  
ANISOU 1649  CD2 TRP B 132     2371   1386   1391    199    -60    206       C  
ATOM   1650  NE1 TRP B 132     -12.493   3.360  32.313  1.00 14.29           N  
ANISOU 1650  NE1 TRP B 132     2721   1185   1524    410   -290    337       N  
ATOM   1651  CE2 TRP B 132     -12.263   2.783  31.091  1.00 14.27           C  
ANISOU 1651  CE2 TRP B 132     2747   1301   1375    560    -33    330       C  
ATOM   1652  CE3 TRP B 132     -13.526   2.206  29.111  1.00 13.29           C  
ANISOU 1652  CE3 TRP B 132     2575   1059   1416    182    302     87       C  
ATOM   1653  CZ2 TRP B 132     -11.082   2.289  30.540  1.00 12.19           C  
ANISOU 1653  CZ2 TRP B 132     2444    918   1268    507    337    318       C  
ATOM   1654  CZ3 TRP B 132     -12.353   1.715  28.565  1.00 12.69           C  
ANISOU 1654  CZ3 TRP B 132     2723    729   1371   -164    279     71       C  
ATOM   1655  CH2 TRP B 132     -11.148   1.759  29.280  1.00 12.34           C  
ANISOU 1655  CH2 TRP B 132     2544    856   1288    230    367    242       C  
ATOM   1656  N   VAL B 133     -17.848   4.458  28.478  1.00 12.79           N  
ANISOU 1656  N   VAL B 133     2312   1275   1272    305   -380    404       N  
ATOM   1657  CA  VAL B 133     -19.173   4.418  27.871  1.00 13.18           C  
ANISOU 1657  CA  VAL B 133     2479   1182   1347    146     14     48       C  
ATOM   1658  C   VAL B 133     -19.324   3.107  27.111  1.00 13.76           C  
ANISOU 1658  C   VAL B 133     2529   1310   1389    137     66     17       C  
ATOM   1659  O   VAL B 133     -18.355   2.564  26.571  1.00 12.26           O  
ANISOU 1659  O   VAL B 133     2561    761   1335    412    170    -10       O  
ATOM   1660  CB  VAL B 133     -19.424   5.616  26.924  1.00 11.68           C  
ANISOU 1660  CB  VAL B 133     2328   1040   1070    594    374     -7       C  
ATOM   1661  CG1 VAL B 133     -19.465   6.927  27.701  1.00 11.21           C  
ANISOU 1661  CG1 VAL B 133     2089   1139   1031    756    473    123       C  
ATOM   1662  CG2 VAL B 133     -18.363   5.670  25.826  1.00  9.72           C  
ANISOU 1662  CG2 VAL B 133     2010    855    827    403     61    260       C  
ATOM   1663  N   ALA B 134     -20.553   2.599  27.065  1.00 13.72           N  
ANISOU 1663  N   ALA B 134     2250   1570   1395   -240   -188   -257       N  
ATOM   1664  CA  ALA B 134     -20.822   1.369  26.334  1.00 13.49           C  
ANISOU 1664  CA  ALA B 134     1954   1516   1655    102     68     21       C  
ATOM   1665  C   ALA B 134     -22.297   1.311  25.971  1.00 16.55           C  
ANISOU 1665  C   ALA B 134     2224   2110   1953   -112    434   -170       C  
ATOM   1666  O   ALA B 134     -23.161   1.605  26.802  1.00 19.02           O  
ANISOU 1666  O   ALA B 134     2230   2930   2068   -587    469   -501       O  
ATOM   1667  CB  ALA B 134     -20.430   0.131  27.150  1.00 13.73           C  
ANISOU 1667  CB  ALA B 134     1974   1593   1651    537     36    518       C  
ATOM   1668  N   THR B 135     -22.572   0.936  24.726  1.00 15.68           N  
ANISOU 1668  N   THR B 135     1941   1735   2283   -330    594    128       N  
ATOM   1669  CA  THR B 135     -23.936   0.705  24.282  1.00 18.99           C  
ANISOU 1669  CA  THR B 135     2082   2264   2869   -602    603     77       C  
ATOM   1670  C   THR B 135     -24.367  -0.709  24.653  1.00 20.71           C  
ANISOU 1670  C   THR B 135     1970   2421   3476   -359    596   -101       C  
ATOM   1671  O   THR B 135     -23.550  -1.632  24.715  1.00 21.10           O  
ANISOU 1671  O   THR B 135     1809   2456   3753   -213    236   -153       O  
ATOM   1672  CB  THR B 135     -24.045   0.916  22.769  1.00 20.01           C  
ANISOU 1672  CB  THR B 135     1747   2853   3002   -930    859    -12       C  
ATOM   1673  OG1 THR B 135     -23.492   2.193  22.429  1.00 18.38           O  
ANISOU 1673  OG1 THR B 135     1524   2569   2890   -779    819   -218       O  
ATOM   1674  CG2 THR B 135     -25.497   0.870  22.306  1.00 21.22           C  
ANISOU 1674  CG2 THR B 135     1792   3158   3112   -982    612   -168       C  
ATOM   1675  N   GLU B 136     -25.662  -0.867  24.923  1.00 20.58           N  
ANISOU 1675  N   GLU B 136     1621   2529   3668   -618   1001   -284       N  
ATOM   1676  CA  GLU B 136     -26.214  -2.185  25.202  1.00 24.96           C  
ANISOU 1676  CA  GLU B 136     2162   2990   4331  -1064   1088   -537       C  
ATOM   1677  C   GLU B 136     -25.912  -3.139  24.052  1.00 26.65           C  
ANISOU 1677  C   GLU B 136     2533   3116   4477  -1352    706   -602       C  
ATOM   1678  O   GLU B 136     -26.114  -2.805  22.880  1.00 28.01           O  
ANISOU 1678  O   GLU B 136     2939   3227   4478  -1500    574   -572       O  
ATOM   1679  CB  GLU B 136     -27.722  -2.084  25.434  1.00 31.49           C  
ANISOU 1679  CB  GLU B 136     3331   3777   4858  -1265   1025   -532       C  
ATOM   1680  CG  GLU B 136     -28.436  -3.423  25.521  1.00 37.57           C  
ANISOU 1680  CG  GLU B 136     3982   5025   5269  -1314    967   -724       C  
ATOM   1681  CD  GLU B 136     -29.873  -3.285  25.984  1.00 45.43           C  
ANISOU 1681  CD  GLU B 136     5412   6203   5647  -1122    525   -793       C  
ATOM   1682  OE1 GLU B 136     -30.089  -2.944  27.167  1.00 48.31           O  
ANISOU 1682  OE1 GLU B 136     6038   6527   5788  -1186    446   -808       O  
ATOM   1683  OE2 GLU B 136     -30.787  -3.508  25.162  1.00 48.32           O  
ANISOU 1683  OE2 GLU B 136     5925   6682   5754   -855    358   -818       O  
ATOM   1684  N   GLY B 137     -25.407  -4.323  24.391  1.00 25.30           N  
ANISOU 1684  N   GLY B 137     2468   2777   4367  -1322    726   -639       N  
ATOM   1685  CA  GLY B 137     -25.043  -5.318  23.407  1.00 23.95           C  
ANISOU 1685  CA  GLY B 137     2641   2490   3970  -1281    624   -936       C  
ATOM   1686  C   GLY B 137     -23.577  -5.335  23.029  1.00 23.14           C  
ANISOU 1686  C   GLY B 137     3075   2168   3548   -956    501   -801       C  
ATOM   1687  O   GLY B 137     -23.143  -6.273  22.348  1.00 24.66           O  
ANISOU 1687  O   GLY B 137     3648   1866   3855  -1140    110   -801       O  
ATOM   1688  N   ALA B 138     -22.806  -4.332  23.440  1.00 18.94           N  
ANISOU 1688  N   ALA B 138     2807   1688   2701   -487    482   -351       N  
ATOM   1689  CA  ALA B 138     -21.384  -4.312  23.133  1.00 19.12           C  
ANISOU 1689  CA  ALA B 138     3358   1635   2274   -110    -68   -132       C  
ATOM   1690  C   ALA B 138     -20.659  -5.430  23.873  1.00 17.54           C  
ANISOU 1690  C   ALA B 138     2881   1713   2069    223    215    149       C  
ATOM   1691  O   ALA B 138     -21.072  -5.861  24.954  1.00 18.10           O  
ANISOU 1691  O   ALA B 138     2540   2269   2066    147    907    530       O  
ATOM   1692  CB  ALA B 138     -20.771  -2.960  23.499  1.00 17.40           C  
ANISOU 1692  CB  ALA B 138     3501   1121   1989    391   -291   -441       C  
ATOM   1693  N   LEU B 139     -19.570  -5.904  23.276  1.00 15.62           N  
ANISOU 1693  N   LEU B 139     2586   1394   1953    210    100     42       N  
ATOM   1694  CA  LEU B 139     -18.764  -6.971  23.852  1.00 16.60           C  
ANISOU 1694  CA  LEU B 139     2698   1619   1991   -135   -150    -12       C  
ATOM   1695  C   LEU B 139     -17.526  -6.376  24.506  1.00 14.87           C  
ANISOU 1695  C   LEU B 139     2539   1346   1766   -216    -41     23       C  
ATOM   1696  O   LEU B 139     -16.858  -5.517  23.920  1.00 11.81           O  
ANISOU 1696  O   LEU B 139     2046    920   1519   -482    -30    150       O  
ATOM   1697  CB  LEU B 139     -18.361  -7.994  22.789  1.00 19.54           C  
ANISOU 1697  CB  LEU B 139     3237   1940   2247   -125   -170   -212       C  
ATOM   1698  CG  LEU B 139     -19.493  -8.805  22.154  1.00 23.54           C  
ANISOU 1698  CG  LEU B 139     4183   2201   2562    145    104   -159       C  
ATOM   1699  CD1 LEU B 139     -18.926  -9.887  21.246  1.00 24.21           C  
ANISOU 1699  CD1 LEU B 139     4670   1994   2534    396    -21   -511       C  
ATOM   1700  CD2 LEU B 139     -20.398  -9.408  23.221  1.00 24.03           C  
ANISOU 1700  CD2 LEU B 139     4083   2469   2577     84    305    -36       C  
ATOM   1701  N   ASN B 140     -17.225  -6.841  25.721  1.00 14.85           N  
ANISOU 1701  N   ASN B 140     2751   1468   1422    323    166    302       N  
ATOM   1702  CA  ASN B 140     -16.083  -6.353  26.494  1.00 16.53           C  
ANISOU 1702  CA  ASN B 140     3082   1712   1488    300    194    273       C  
ATOM   1703  C   ASN B 140     -14.819  -7.087  26.040  1.00 17.29           C  
ANISOU 1703  C   ASN B 140     3042   1829   1698    632      5    282       C  
ATOM   1704  O   ASN B 140     -14.262  -7.943  26.729  1.00 17.95           O  
ANISOU 1704  O   ASN B 140     2894   2175   1750    965   -284    390       O  
ATOM   1705  CB  ASN B 140     -16.343  -6.530  27.985  1.00 16.61           C  
ANISOU 1705  CB  ASN B 140     3183   1827   1302   -219    201    562       C  
ATOM   1706  CG  ASN B 140     -15.292  -5.861  28.850  1.00 17.81           C  
ANISOU 1706  CG  ASN B 140     3261   2241   1265   -567    204    602       C  
ATOM   1707  OD1 ASN B 140     -14.448  -5.114  28.361  1.00 20.72           O  
ANISOU 1707  OD1 ASN B 140     4077   2474   1323   -490    -39    277       O  
ATOM   1708  ND2 ASN B 140     -15.346  -6.123  30.150  1.00 20.44           N  
ANISOU 1708  ND2 ASN B 140     3360   2846   1561   -597    296    930       N  
ATOM   1709  N   THR B 141     -14.381  -6.738  24.834  1.00 16.62           N  
ANISOU 1709  N   THR B 141     3056   1459   1801    -21    407     -3       N  
ATOM   1710  CA  THR B 141     -13.180  -7.266  24.206  1.00 16.73           C  
ANISOU 1710  CA  THR B 141     2702   1577   2080    -80    202     84       C  
ATOM   1711  C   THR B 141     -12.460  -6.117  23.519  1.00 17.07           C  
ANISOU 1711  C   THR B 141     2626   1739   2122    239     13    194       C  
ATOM   1712  O   THR B 141     -13.104  -5.162  23.069  1.00 16.50           O  
ANISOU 1712  O   THR B 141     2337   1786   2146    633    -38    304       O  
ATOM   1713  CB  THR B 141     -13.498  -8.364  23.175  1.00 18.74           C  
ANISOU 1713  CB  THR B 141     3257   1566   2298      5    299    171       C  
ATOM   1714  OG1 THR B 141     -14.394  -7.848  22.181  1.00 19.43           O  
ANISOU 1714  OG1 THR B 141     3752   1742   1889   -221    532    -49       O  
ATOM   1715  CG2 THR B 141     -14.132  -9.576  23.848  1.00 18.62           C  
ANISOU 1715  CG2 THR B 141     3175   1308   2591   -102    429   -247       C  
ATOM   1716  N   PRO B 142     -11.130  -6.172  23.429  1.00 16.17           N  
ANISOU 1716  N   PRO B 142     2211   1904   2030    411   -154    410       N  
ATOM   1717  CA  PRO B 142     -10.394  -5.071  22.795  1.00 16.32           C  
ANISOU 1717  CA  PRO B 142     2394   1890   1916    674   -257    529       C  
ATOM   1718  C   PRO B 142     -10.702  -4.974  21.309  1.00 15.76           C  
ANISOU 1718  C   PRO B 142     2563   1822   1604    872   -129    466       C  
ATOM   1719  O   PRO B 142     -10.862  -5.984  20.620  1.00 17.66           O  
ANISOU 1719  O   PRO B 142     3137   1986   1586    655   -243    720       O  
ATOM   1720  CB  PRO B 142      -8.925  -5.434  23.042  1.00 18.44           C  
ANISOU 1720  CB  PRO B 142     2766   1960   2281    409   -167    554       C  
ATOM   1721  CG  PRO B 142      -8.934  -6.916  23.270  1.00 19.29           C  
ANISOU 1721  CG  PRO B 142     2798   2166   2363    184   -118    664       C  
ATOM   1722  CD  PRO B 142     -10.229  -7.207  23.963  1.00 18.01           C  
ANISOU 1722  CD  PRO B 142     2462   2027   2354    342     53    539       C  
ATOM   1723  N   LYS B 143     -10.775  -3.739  20.819  1.00 13.25           N  
ANISOU 1723  N   LYS B 143     1936   1781   1318    860    370    398       N  
ATOM   1724  CA  LYS B 143     -11.145  -3.469  19.428  1.00 12.84           C  
ANISOU 1724  CA  LYS B 143     1934   1694   1250    633    147    304       C  
ATOM   1725  C   LYS B 143      -9.899  -3.218  18.579  1.00 13.25           C  
ANISOU 1725  C   LYS B 143     2254   1301   1481    244    -21    351       C  
ATOM   1726  O   LYS B 143      -9.754  -2.188  17.918  1.00 12.85           O  
ANISOU 1726  O   LYS B 143     2524   1188   1170    358   -261    111       O  
ATOM   1727  CB  LYS B 143     -12.111  -2.289  19.359  1.00 11.27           C  
ANISOU 1727  CB  LYS B 143     1485   1630   1165    274    404    206       C  
ATOM   1728  CG  LYS B 143     -13.313  -2.410  20.288  1.00 11.74           C  
ANISOU 1728  CG  LYS B 143     1517   1662   1284    -98    414    208       C  
ATOM   1729  CD  LYS B 143     -13.981  -3.771  20.170  1.00 11.47           C  
ANISOU 1729  CD  LYS B 143     1712   1283   1363    -29    638    535       C  
ATOM   1730  CE  LYS B 143     -15.168  -3.884  21.122  1.00 11.72           C  
ANISOU 1730  CE  LYS B 143     1773   1353   1326   -125    373    701       C  
ATOM   1731  NZ  LYS B 143     -15.528  -5.301  21.415  1.00 12.71           N  
ANISOU 1731  NZ  LYS B 143     1778   1705   1344     66    401    815       N  
ATOM   1732  N   ASP B 144      -8.997  -4.203  18.603  1.00 15.61           N  
ANISOU 1732  N   ASP B 144     2485   1761   1685    254   -129    458       N  
ATOM   1733  CA  ASP B 144      -7.734  -4.092  17.880  1.00 17.43           C  
ANISOU 1733  CA  ASP B 144     2193   2370   2058    841   -598    246       C  
ATOM   1734  C   ASP B 144      -7.949  -3.813  16.397  1.00 17.68           C  
ANISOU 1734  C   ASP B 144     1972   2526   2219    552   -294     43       C  
ATOM   1735  O   ASP B 144      -7.158  -3.089  15.780  1.00 17.54           O  
ANISOU 1735  O   ASP B 144     1852   2666   2148    426   -293    -91       O  
ATOM   1736  CB  ASP B 144      -6.922  -5.375  18.063  1.00 22.07           C  
ANISOU 1736  CB  ASP B 144     3183   2807   2396    701   -881    315       C  
ATOM   1737  CG  ASP B 144      -6.695  -5.718  19.523  1.00 27.57           C  
ANISOU 1737  CG  ASP B 144     4255   3240   2980    596   -512     48       C  
ATOM   1738  OD1 ASP B 144      -6.061  -4.910  20.232  1.00 29.55           O  
ANISOU 1738  OD1 ASP B 144     4588   3533   3109    550   -389   -342       O  
ATOM   1739  OD2 ASP B 144      -7.165  -6.787  19.967  1.00 30.39           O  
ANISOU 1739  OD2 ASP B 144     4777   3525   3247    453   -283    259       O  
ATOM   1740  N   HIS B 145      -9.011  -4.367  15.807  1.00 16.01           N  
ANISOU 1740  N   HIS B 145     1878   2184   2020    396   -232   -302       N  
ATOM   1741  CA  HIS B 145      -9.224  -4.199  14.374  1.00 14.68           C  
ANISOU 1741  CA  HIS B 145     2116   1862   1600    285     47    -77       C  
ATOM   1742  C   HIS B 145      -9.626  -2.775  14.005  1.00 13.90           C  
ANISOU 1742  C   HIS B 145     2039   1766   1478    461    290    108       C  
ATOM   1743  O   HIS B 145      -9.463  -2.383  12.844  1.00 16.02           O  
ANISOU 1743  O   HIS B 145     2528   1911   1647    282    651   -130       O  
ATOM   1744  CB  HIS B 145     -10.272  -5.198  13.875  1.00 14.67           C  
ANISOU 1744  CB  HIS B 145     2279   1940   1355     25    355   -276       C  
ATOM   1745  CG  HIS B 145     -11.668  -4.898  14.323  1.00 13.76           C  
ANISOU 1745  CG  HIS B 145     2477   1751    999    146    687   -167       C  
ATOM   1746  ND1 HIS B 145     -12.148  -5.263  15.563  1.00 16.73           N  
ANISOU 1746  ND1 HIS B 145     2800   2047   1511    263    678    332       N  
ATOM   1747  CD2 HIS B 145     -12.696  -4.288  13.687  1.00 14.41           C  
ANISOU 1747  CD2 HIS B 145     2615   1800   1059    333    567   -206       C  
ATOM   1748  CE1 HIS B 145     -13.408  -4.880  15.676  1.00 15.44           C  
ANISOU 1748  CE1 HIS B 145     2755   1767   1345    447    694    375       C  
ATOM   1749  NE2 HIS B 145     -13.764  -4.286  14.551  1.00 14.75           N  
ANISOU 1749  NE2 HIS B 145     2766   1743   1096    653    302    170       N  
ATOM   1750  N   ILE B 146     -10.131  -1.994  14.954  1.00 11.69           N  
ANISOU 1750  N   ILE B 146     1552   1451   1439    565    365    326       N  
ATOM   1751  CA  ILE B 146     -10.466  -0.597  14.687  1.00 12.57           C  
ANISOU 1751  CA  ILE B 146     1702   1547   1525    613    341    272       C  
ATOM   1752  C   ILE B 146      -9.250   0.302  14.855  1.00 14.57           C  
ANISOU 1752  C   ILE B 146     2332   1691   1515    820    -72    117       C  
ATOM   1753  O   ILE B 146      -8.963   1.142  13.997  1.00 14.75           O  
ANISOU 1753  O   ILE B 146     2740   1538   1326    848   -337     74       O  
ATOM   1754  CB  ILE B 146     -11.630  -0.143  15.592  1.00 14.45           C  
ANISOU 1754  CB  ILE B 146     2278   1466   1746    316    253    476       C  
ATOM   1755  CG1 ILE B 146     -12.874  -0.989  15.320  1.00 17.37           C  
ANISOU 1755  CG1 ILE B 146     2430   2250   1920     30    536    211       C  
ATOM   1756  CG2 ILE B 146     -11.929   1.336  15.371  1.00 14.54           C  
ANISOU 1756  CG2 ILE B 146     2077   1642   1804    357   -211    784       C  
ATOM   1757  CD1 ILE B 146     -14.083  -0.585  16.138  1.00 18.45           C  
ANISOU 1757  CD1 ILE B 146     2520   2496   1994    219    813     54       C  
ATOM   1758  N   GLY B 147      -8.519   0.137  15.954  1.00 15.49           N  
ANISOU 1758  N   GLY B 147     2061   2080   1745    689    -65   -132       N  
ATOM   1759  CA  GLY B 147      -7.318   0.911  16.181  1.00 13.49           C  
ANISOU 1759  CA  GLY B 147     1400   2123   1604    736   -136    -13       C  
ATOM   1760  C   GLY B 147      -7.610   2.394  16.297  1.00 13.62           C  
ANISOU 1760  C   GLY B 147     1348   2192   1634    861     18    127       C  
ATOM   1761  O   GLY B 147      -8.706   2.821  16.682  1.00 14.84           O  
ANISOU 1761  O   GLY B 147     1702   2310   1625    831    -93   -100       O  
ATOM   1762  N   THR B 148      -6.612   3.196  15.951  1.00 13.35           N  
ANISOU 1762  N   THR B 148     1310   1989   1775    746     10    214       N  
ATOM   1763  CA  THR B 148      -6.716   4.648  15.961  1.00 11.73           C  
ANISOU 1763  CA  THR B 148     1248   1659   1548    422   -192    309       C  
ATOM   1764  C   THR B 148      -6.555   5.186  14.541  1.00 12.01           C  
ANISOU 1764  C   THR B 148     1309   1743   1510     98   -221     85       C  
ATOM   1765  O   THR B 148      -6.292   4.442  13.592  1.00 12.67           O  
ANISOU 1765  O   THR B 148     1142   1937   1733   -163    -41   -231       O  
ATOM   1766  CB  THR B 148      -5.678   5.261  16.903  1.00 16.17           C  
ANISOU 1766  CB  THR B 148     1859   2403   1884    281   -525    374       C  
ATOM   1767  OG1 THR B 148      -4.383   4.731  16.596  1.00 19.82           O  
ANISOU 1767  OG1 THR B 148     1974   2983   2576    351   -739    -38       O  
ATOM   1768  CG2 THR B 148      -6.026   4.944  18.351  1.00 18.15           C  
ANISOU 1768  CG2 THR B 148     2476   2603   1820   -102   -624    571       C  
ATOM   1769  N   ARG B 149      -6.707   6.501  14.411  1.00 12.77           N  
ANISOU 1769  N   ARG B 149     1780   1670   1400   -110   -229    146       N  
ATOM   1770  CA  ARG B 149      -6.770   7.172  13.120  1.00 14.15           C  
ANISOU 1770  CA  ARG B 149     1790   1992   1595     77   -531    314       C  
ATOM   1771  C   ARG B 149      -5.443   7.837  12.781  1.00 16.88           C  
ANISOU 1771  C   ARG B 149     2111   2545   1759     34   -310     38       C  
ATOM   1772  O   ARG B 149      -4.810   8.461  13.638  1.00 18.40           O  
ANISOU 1772  O   ARG B 149     2381   2892   1717    -88   -285   -202       O  
ATOM   1773  CB  ARG B 149      -7.884   8.224  13.119  1.00 13.35           C  
ANISOU 1773  CB  ARG B 149     1718   1778   1576    312   -409    359       C  
ATOM   1774  CG  ARG B 149      -7.947   9.081  11.861  1.00 12.39           C  
ANISOU 1774  CG  ARG B 149     1644   1620   1442     30   -224    326       C  
ATOM   1775  CD  ARG B 149      -9.125  10.041  11.903  1.00 12.56           C  
ANISOU 1775  CD  ARG B 149     1552   1734   1487     -3    -28     70       C  
ATOM   1776  NE  ARG B 149      -9.020  10.993  13.005  1.00 12.43           N  
ANISOU 1776  NE  ARG B 149     1444   1813   1466   -350    321    177       N  
ATOM   1777  CZ  ARG B 149      -8.497  12.211  12.896  1.00 13.59           C  
ANISOU 1777  CZ  ARG B 149     2067   1719   1378   -271    532    222       C  
ATOM   1778  NH1 ARG B 149      -8.026  12.636  11.729  1.00 14.63           N  
ANISOU 1778  NH1 ARG B 149     2301   1821   1436   -341    546     26       N  
ATOM   1779  NH2 ARG B 149      -8.445  13.005  13.956  1.00 14.80           N  
ANISOU 1779  NH2 ARG B 149     2322   1784   1516   -434    224     75       N  
ATOM   1780  N   ASN B 150      -5.030   7.699  11.519  1.00 17.09           N  
ANISOU 1780  N   ASN B 150     2183   2370   1941    -80   -259    234       N  
ATOM   1781  CA  ASN B 150      -3.918   8.472  10.982  1.00 18.90           C  
ANISOU 1781  CA  ASN B 150     1867   2856   2459    -38   -162    324       C  
ATOM   1782  C   ASN B 150      -4.490   9.740  10.364  1.00 18.49           C  
ANISOU 1782  C   ASN B 150     1730   2905   2390   -388   -101    507       C  
ATOM   1783  O   ASN B 150      -5.186   9.654   9.340  1.00 20.76           O  
ANISOU 1783  O   ASN B 150     2139   3314   2433   -377    245    511       O  
ATOM   1784  CB  ASN B 150      -3.153   7.665   9.939  1.00 20.33           C  
ANISOU 1784  CB  ASN B 150     1618   3011   3095    -35    231    -97       C  
ATOM   1785  CG  ASN B 150      -1.902   8.377   9.436  1.00 25.88           C  
ANISOU 1785  CG  ASN B 150     2541   3466   3826      6    404   -428       C  
ATOM   1786  OD1 ASN B 150      -1.760   9.594   9.565  1.00 25.91           O  
ANISOU 1786  OD1 ASN B 150     2392   3278   4173  -1200    275    217       O  
ATOM   1787  ND2 ASN B 150      -0.989   7.612   8.851  1.00 29.75           N  
ANISOU 1787  ND2 ASN B 150     3027   4265   4014    324    932   -908       N  
ATOM   1788  N   PRO B 151      -4.233  10.921  10.932  1.00 18.84           N  
ANISOU 1788  N   PRO B 151     1868   3133   2158   -373      7    214       N  
ATOM   1789  CA  PRO B 151      -4.812  12.152  10.367  1.00 20.10           C  
ANISOU 1789  CA  PRO B 151     2157   3225   2257   -583    171    162       C  
ATOM   1790  C   PRO B 151      -4.407  12.417   8.928  1.00 22.78           C  
ANISOU 1790  C   PRO B 151     2586   3566   2505   -671    249    612       C  
ATOM   1791  O   PRO B 151      -5.138  13.116   8.215  1.00 25.51           O  
ANISOU 1791  O   PRO B 151     3142   3841   2711   -416    470   1046       O  
ATOM   1792  CB  PRO B 151      -4.290  13.249  11.306  1.00 20.31           C  
ANISOU 1792  CB  PRO B 151     2296   3079   2342   -572     69     50       C  
ATOM   1793  CG  PRO B 151      -3.962  12.539  12.577  1.00 21.58           C  
ANISOU 1793  CG  PRO B 151     2434   3369   2398   -469   -181    -53       C  
ATOM   1794  CD  PRO B 151      -3.471  11.182  12.164  1.00 19.83           C  
ANISOU 1794  CD  PRO B 151     2083   3247   2204   -413   -146   -167       C  
ATOM   1795  N   ALA B 152      -3.270  11.886   8.474  1.00 22.11           N  
ANISOU 1795  N   ALA B 152     2405   3597   2397   -987    739    366       N  
ATOM   1796  CA  ALA B 152      -2.874  12.068   7.084  1.00 24.59           C  
ANISOU 1796  CA  ALA B 152     2728   3892   2723  -1067    859    121       C  
ATOM   1797  C   ALA B 152      -3.696  11.211   6.131  1.00 25.70           C  
ANISOU 1797  C   ALA B 152     3076   3894   2795   -904    751    259       C  
ATOM   1798  O   ALA B 152      -3.739  11.508   4.932  1.00 32.18           O  
ANISOU 1798  O   ALA B 152     4323   4542   3362  -1190    886    346       O  
ATOM   1799  CB  ALA B 152      -1.388  11.753   6.915  1.00 26.38           C  
ANISOU 1799  CB  ALA B 152     2898   4256   2868  -1169    825   -118       C  
ATOM   1800  N   ASN B 153      -4.349  10.163   6.631  1.00 20.77           N  
ANISOU 1800  N   ASN B 153     2166   3193   2532   -606    702    162       N  
ATOM   1801  CA  ASN B 153      -5.113   9.253   5.787  1.00 20.83           C  
ANISOU 1801  CA  ASN B 153     2654   2889   2374   -456    561    121       C  
ATOM   1802  C   ASN B 153      -6.619   9.392   5.936  1.00 20.61           C  
ANISOU 1802  C   ASN B 153     2925   2824   2081   -443    246     84       C  
ATOM   1803  O   ASN B 153      -7.342   9.159   4.966  1.00 22.86           O  
ANISOU 1803  O   ASN B 153     3460   3186   2038    137     16   -117       O  
ATOM   1804  CB  ASN B 153      -4.718   7.799   6.078  1.00 21.44           C  
ANISOU 1804  CB  ASN B 153     2836   2708   2604   -549    242    283       C  
ATOM   1805  CG  ASN B 153      -5.337   6.819   5.099  1.00 22.58           C  
ANISOU 1805  CG  ASN B 153     2814   2910   2857   -502    233    208       C  
ATOM   1806  OD1 ASN B 153      -4.983   6.796   3.920  1.00 22.43           O  
ANISOU 1806  OD1 ASN B 153     2750   2938   2835   -721    117     78       O  
ATOM   1807  ND2 ASN B 153      -6.259   5.996   5.585  1.00 23.88           N  
ANISOU 1807  ND2 ASN B 153     2859   3097   3118   -374    229    337       N  
ATOM   1808  N   ASN B 154      -7.109   9.765   7.117  1.00 18.64           N  
ANISOU 1808  N   ASN B 154     2795   2630   1656   -941    529   -161       N  
ATOM   1809  CA  ASN B 154      -8.540   9.897   7.353  1.00 18.15           C  
ANISOU 1809  CA  ASN B 154     2969   2325   1602   -874    197   -306       C  
ATOM   1810  C   ASN B 154      -8.823  11.179   8.117  1.00 17.59           C  
ANISOU 1810  C   ASN B 154     3012   1945   1724  -1208     74    129       C  
ATOM   1811  O   ASN B 154      -8.115  11.513   9.071  1.00 19.49           O  
ANISOU 1811  O   ASN B 154     3235   2333   1839  -1278   -135    239       O  
ATOM   1812  CB  ASN B 154      -9.098   8.710   8.150  1.00 18.25           C  
ANISOU 1812  CB  ASN B 154     3081   2359   1496  -1281    -40   -484       C  
ATOM   1813  CG  ASN B 154      -8.966   7.397   7.412  1.00 21.53           C  
ANISOU 1813  CG  ASN B 154     3553   2867   1759   -879    125   -585       C  
ATOM   1814  OD1 ASN B 154      -7.946   6.717   7.510  1.00 26.44           O  
ANISOU 1814  OD1 ASN B 154     4390   3413   2241    -38    409   -446       O  
ATOM   1815  ND2 ASN B 154     -10.003   7.030   6.671  1.00 21.28           N  
ANISOU 1815  ND2 ASN B 154     2940   3202   1943  -1588     45   -692       N  
ATOM   1816  N   ALA B 155      -9.867  11.886   7.699  1.00 17.31           N  
ANISOU 1816  N   ALA B 155     3045   1962   1572   -627    298    -16       N  
ATOM   1817  CA  ALA B 155     -10.358  13.005   8.483  1.00 17.19           C  
ANISOU 1817  CA  ALA B 155     3081   1987   1464   -280    171    303       C  
ATOM   1818  C   ALA B 155     -11.110  12.492   9.709  1.00 15.36           C  
ANISOU 1818  C   ALA B 155     2473   2152   1212     -1     14   -181       C  
ATOM   1819  O   ALA B 155     -11.605  11.362   9.742  1.00 12.14           O  
ANISOU 1819  O   ALA B 155     1422   2265    926     30   -202   -120       O  
ATOM   1820  CB  ALA B 155     -11.269  13.896   7.638  1.00 17.52           C  
ANISOU 1820  CB  ALA B 155     3312   1807   1538   -314   -134    552       C  
ATOM   1821  N   ALA B 156     -11.181  13.334  10.733  1.00 16.35           N  
ANISOU 1821  N   ALA B 156     2608   2361   1244    -95     64   -231       N  
ATOM   1822  CA  ALA B 156     -11.927  12.974  11.928  1.00 17.09           C  
ANISOU 1822  CA  ALA B 156     2508   2534   1452    180   -476     58       C  
ATOM   1823  C   ALA B 156     -13.419  12.930  11.627  1.00 16.68           C  
ANISOU 1823  C   ALA B 156     2210   2449   1679    200   -559    684       C  
ATOM   1824  O   ALA B 156     -13.951  13.781  10.910  1.00 19.66           O  
ANISOU 1824  O   ALA B 156     2327   3035   2107     52   -324   1303       O  
ATOM   1825  CB  ALA B 156     -11.647  13.968  13.055  1.00 19.50           C  
ANISOU 1825  CB  ALA B 156     2920   2886   1604    339   -318   -359       C  
ATOM   1826  N   ILE B 157     -14.090  11.914  12.163  1.00 14.42           N  
ANISOU 1826  N   ILE B 157     1828   2111   1539   -191   -546    228       N  
ATOM   1827  CA  ILE B 157     -15.544  11.856  12.102  1.00 12.88           C  
ANISOU 1827  CA  ILE B 157     1785   1712   1395     75   -929   -111       C  
ATOM   1828  C   ILE B 157     -16.116  12.848  13.102  1.00 14.01           C  
ANISOU 1828  C   ILE B 157     2052   1607   1663    248  -1079    -78       C  
ATOM   1829  O   ILE B 157     -15.716  12.869  14.273  1.00 15.05           O  
ANISOU 1829  O   ILE B 157     2352   1738   1630   -433  -1008   -137       O  
ATOM   1830  CB  ILE B 157     -16.041  10.431  12.391  1.00 14.16           C  
ANISOU 1830  CB  ILE B 157     1772   2070   1539    -79   -923   -289       C  
ATOM   1831  CG1 ILE B 157     -15.465   9.445  11.374  1.00 14.83           C  
ANISOU 1831  CG1 ILE B 157     2009   1741   1886     42   -649   -795       C  
ATOM   1832  CG2 ILE B 157     -17.561  10.389  12.384  1.00 15.10           C  
ANISOU 1832  CG2 ILE B 157     1961   2214   1562    -37   -683   -104       C  
ATOM   1833  CD1 ILE B 157     -15.716   8.000  11.729  1.00 17.59           C  
ANISOU 1833  CD1 ILE B 157     2399   2108   2177    -91   -350   -790       C  
ATOM   1834  N   VAL B 158     -17.050  13.680  12.649  1.00 16.26           N  
ANISOU 1834  N   VAL B 158     2274   1968   1934    540   -502     44       N  
ATOM   1835  CA  VAL B 158     -17.703  14.615  13.558  1.00 16.30           C  
ANISOU 1835  CA  VAL B 158     2383   1927   1882    831   -230    132       C  
ATOM   1836  C   VAL B 158     -18.520  13.821  14.568  1.00 15.79           C  
ANISOU 1836  C   VAL B 158     2097   2237   1665    408   -338   -197       C  
ATOM   1837  O   VAL B 158     -19.404  13.041  14.194  1.00 18.66           O  
ANISOU 1837  O   VAL B 158     2320   2943   1826   -153   -232   -638       O  
ATOM   1838  CB  VAL B 158     -18.582  15.611  12.794  1.00 18.78           C  
ANISOU 1838  CB  VAL B 158     2709   2333   2093   1057   -305    638       C  
ATOM   1839  CG1 VAL B 158     -19.358  16.475  13.775  1.00 19.71           C  
ANISOU 1839  CG1 VAL B 158     3012   2264   2211    812   -530    514       C  
ATOM   1840  CG2 VAL B 158     -17.728  16.469  11.872  1.00 18.00           C  
ANISOU 1840  CG2 VAL B 158     2673   2348   1819   1200    -73    625       C  
ATOM   1841  N   LEU B 159     -18.227  14.015  15.851  1.00 12.30           N  
ANISOU 1841  N   LEU B 159     1649   1949   1076    194   -392    189       N  
ATOM   1842  CA  LEU B 159     -18.875  13.235  16.897  1.00 11.11           C  
ANISOU 1842  CA  LEU B 159     1124   1779   1319     87   -424     22       C  
ATOM   1843  C   LEU B 159     -20.362  13.562  16.944  1.00 13.34           C  
ANISOU 1843  C   LEU B 159     1608   1648   1811     88   -513      1       C  
ATOM   1844  O   LEU B 159     -20.746  14.727  17.098  1.00 14.72           O  
ANISOU 1844  O   LEU B 159     2049   1680   1864    431   -190   -373       O  
ATOM   1845  CB  LEU B 159     -18.215  13.508  18.248  1.00  9.85           C  
ANISOU 1845  CB  LEU B 159      809   1850   1083    116   -414    100       C  
ATOM   1846  CG  LEU B 159     -18.429  12.488  19.373  1.00 12.44           C  
ANISOU 1846  CG  LEU B 159     1247   2232   1245   -114   -156    464       C  
ATOM   1847  CD1 LEU B 159     -17.311  12.586  20.395  1.00 13.63           C  
ANISOU 1847  CD1 LEU B 159     1556   2215   1409   -186   -435    550       C  
ATOM   1848  CD2 LEU B 159     -19.773  12.675  20.060  1.00 16.38           C  
ANISOU 1848  CD2 LEU B 159     2081   2572   1571    368    -26    646       C  
ATOM   1849  N   GLN B 160     -21.194  12.534  16.804  1.00 15.50           N  
ANISOU 1849  N   GLN B 160     1736   1858   2296   -169   -535    154       N  
ATOM   1850  CA  GLN B 160     -22.638  12.664  16.914  1.00 17.35           C  
ANISOU 1850  CA  GLN B 160     1997   1884   2710    -10   -473     51       C  
ATOM   1851  C   GLN B 160     -23.155  11.631  17.902  1.00 17.29           C  
ANISOU 1851  C   GLN B 160     1646   2394   2529    219   -167     79       C  
ATOM   1852  O   GLN B 160     -22.680  10.492  17.931  1.00 17.86           O  
ANISOU 1852  O   GLN B 160     1910   2341   2534    260   -127    176       O  
ATOM   1853  CB  GLN B 160     -23.329  12.478  15.555  1.00 18.63           C  
ANISOU 1853  CB  GLN B 160     2215   1646   3218    562   -594    288       C  
ATOM   1854  CG  GLN B 160     -23.017  13.566  14.543  1.00 24.29           C  
ANISOU 1854  CG  GLN B 160     2640   2484   4104    317   -446     90       C  
ATOM   1855  CD  GLN B 160     -23.617  14.904  14.926  1.00 33.04           C  
ANISOU 1855  CD  GLN B 160     3651   3945   4957    -56   -242     88       C  
ATOM   1856  OE1 GLN B 160     -24.795  14.992  15.276  1.00 38.12           O  
ANISOU 1856  OE1 GLN B 160     4456   4713   5314    -69   -288   -123       O  
ATOM   1857  NE2 GLN B 160     -22.806  15.954  14.869  1.00 34.94           N  
ANISOU 1857  NE2 GLN B 160     3881   4182   5215   -375    -69    327       N  
ATOM   1858  N   LEU B 161     -24.117  12.034  18.711  1.00 19.54           N  
ANISOU 1858  N   LEU B 161     1819   2770   2835    601   -535     40       N  
ATOM   1859  CA  LEU B 161     -24.755  11.121  19.638  1.00 22.53           C  
ANISOU 1859  CA  LEU B 161     2281   3085   3194    306   -527     74       C  
ATOM   1860  C   LEU B 161     -26.208  10.896  19.234  1.00 26.63           C  
ANISOU 1860  C   LEU B 161     2789   3618   3712     55   -414   -111       C  
ATOM   1861  O   LEU B 161     -26.801  11.738  18.552  1.00 28.07           O  
ANISOU 1861  O   LEU B 161     2857   3928   3881    -51   -576   -138       O  
ATOM   1862  CB  LEU B 161     -24.691  11.665  21.070  1.00 23.59           C  
ANISOU 1862  CB  LEU B 161     2415   3340   3208    278   -832    413       C  
ATOM   1863  CG  LEU B 161     -23.278  11.806  21.640  1.00 23.32           C  
ANISOU 1863  CG  LEU B 161     2185   3360   3314    432   -948    516       C  
ATOM   1864  CD1 LEU B 161     -23.299  12.547  22.968  1.00 25.29           C  
ANISOU 1864  CD1 LEU B 161     2609   3654   3347    136  -1002    710       C  
ATOM   1865  CD2 LEU B 161     -22.629  10.438  21.796  1.00 23.02           C  
ANISOU 1865  CD2 LEU B 161     1701   3694   3352    613  -1099    318       C  
ATOM   1866  N   PRO B 162     -26.800   9.763  19.614  1.00 29.78           N  
ANISOU 1866  N   PRO B 162     3128   3990   4195   -420   -333   -542       N  
ATOM   1867  CA  PRO B 162     -28.211   9.522  19.291  1.00 34.30           C  
ANISOU 1867  CA  PRO B 162     3659   4708   4666   -246    -98   -696       C  
ATOM   1868  C   PRO B 162     -29.111  10.629  19.823  1.00 40.21           C  
ANISOU 1868  C   PRO B 162     4142   5862   5276    109    193   -743       C  
ATOM   1869  O   PRO B 162     -28.752  11.380  20.732  1.00 40.16           O  
ANISOU 1869  O   PRO B 162     3664   6222   5374      8    278   -943       O  
ATOM   1870  CB  PRO B 162     -28.507   8.183  19.974  1.00 32.10           C  
ANISOU 1870  CB  PRO B 162     3371   4297   4528   -675   -251   -696       C  
ATOM   1871  CG  PRO B 162     -27.185   7.494  20.011  1.00 31.41           C  
ANISOU 1871  CG  PRO B 162     3384   4171   4377   -906   -372   -668       C  
ATOM   1872  CD  PRO B 162     -26.165   8.581  20.224  1.00 30.05           C  
ANISOU 1872  CD  PRO B 162     3253   3936   4229   -799   -414   -625       C  
ATOM   1873  N   GLN B 163     -30.308  10.716  19.234  1.00 46.32           N  
ANISOU 1873  N   GLN B 163     5286   6601   5713    533    164   -450       N  
ATOM   1874  CA  GLN B 163     -31.209  11.826  19.532  1.00 51.00           C  
ANISOU 1874  CA  GLN B 163     6042   7150   6186    823    175   -137       C  
ATOM   1875  C   GLN B 163     -31.610  11.846  21.002  1.00 51.75           C  
ANISOU 1875  C   GLN B 163     5763   7309   6590   1152    203     84       C  
ATOM   1876  O   GLN B 163     -31.704  12.918  21.613  1.00 53.73           O  
ANISOU 1876  O   GLN B 163     6129   7517   6768   1376    193     89       O  
ATOM   1877  CB  GLN B 163     -32.450  11.744  18.641  1.00 54.71           C  
ANISOU 1877  CB  GLN B 163     7021   7383   6384    357    230    -37       C  
ATOM   1878  CG  GLN B 163     -32.155  11.637  17.148  1.00 57.82           C  
ANISOU 1878  CG  GLN B 163     7825   7495   6649   -103     89     80       C  
ATOM   1879  CD  GLN B 163     -31.722  12.955  16.525  1.00 59.63           C  
ANISOU 1879  CD  GLN B 163     8269   7477   6910   -429     30    140       C  
ATOM   1880  OE1 GLN B 163     -30.798  13.613  17.005  1.00 60.48           O  
ANISOU 1880  OE1 GLN B 163     8408   7538   7032   -623    111    126       O  
ATOM   1881  NE2 GLN B 163     -32.393  13.345  15.447  1.00 59.68           N  
ANISOU 1881  NE2 GLN B 163     8317   7422   6938   -415   -147    163       N  
ATOM   1882  N   GLY B 164     -31.845  10.673  21.591  1.00 49.68           N  
ANISOU 1882  N   GLY B 164     5140   7037   6700    882    261    288       N  
ATOM   1883  CA  GLY B 164     -32.243  10.603  22.987  1.00 49.47           C  
ANISOU 1883  CA  GLY B 164     5199   6776   6822    806    255    197       C  
ATOM   1884  C   GLY B 164     -31.185  11.058  23.972  1.00 49.74           C  
ANISOU 1884  C   GLY B 164     5583   6355   6961    764    380     40       C  
ATOM   1885  O   GLY B 164     -31.498  11.218  25.157  1.00 50.57           O  
ANISOU 1885  O   GLY B 164     5790   6385   7038    736    623   -128       O  
ATOM   1886  N   THR B 165     -29.953  11.271  23.517  1.00 48.03           N  
ANISOU 1886  N   THR B 165     5502   5772   6976    664     36     78       N  
ATOM   1887  CA  THR B 165     -28.851  11.681  24.376  1.00 45.59           C  
ANISOU 1887  CA  THR B 165     5183   5202   6937    327   -117      0       C  
ATOM   1888  C   THR B 165     -28.505  13.140  24.108  1.00 46.14           C  
ANISOU 1888  C   THR B 165     5446   5331   6755     59   -129   -392       C  
ATOM   1889  O   THR B 165     -28.394  13.555  22.950  1.00 46.69           O  
ANISOU 1889  O   THR B 165     5754   5220   6767   -360   -165   -261       O  
ATOM   1890  CB  THR B 165     -27.619  10.802  24.146  1.00 43.44           C  
ANISOU 1890  CB  THR B 165     4766   4736   7003    398   -271    279       C  
ATOM   1891  OG1 THR B 165     -27.990   9.422  24.239  1.00 43.14           O  
ANISOU 1891  OG1 THR B 165     4497   4773   7123    514   -285    340       O  
ATOM   1892  CG2 THR B 165     -26.548  11.100  25.184  1.00 41.91           C  
ANISOU 1892  CG2 THR B 165     4588   4385   6951    310   -349    381       C  
ATOM   1893  N   THR B 166     -28.346  13.912  25.178  1.00 45.58           N  
ANISOU 1893  N   THR B 166     5299   5504   6517    314    -82   -726       N  
ATOM   1894  CA  THR B 166     -27.885  15.289  25.095  1.00 45.40           C  
ANISOU 1894  CA  THR B 166     5394   5584   6274    139   -109   -769       C  
ATOM   1895  C   THR B 166     -26.536  15.409  25.790  1.00 41.54           C  
ANISOU 1895  C   THR B 166     4826   5022   5934   -325   -105   -627       C  
ATOM   1896  O   THR B 166     -26.208  14.620  26.681  1.00 42.49           O  
ANISOU 1896  O   THR B 166     5006   5219   5919   -741    -81   -667       O  
ATOM   1897  CB  THR B 166     -28.886  16.263  25.731  1.00 49.59           C  
ANISOU 1897  CB  THR B 166     6350   6159   6335    280   -327   -911       C  
ATOM   1898  OG1 THR B 166     -29.186  15.839  27.067  1.00 51.58           O  
ANISOU 1898  OG1 THR B 166     6899   6406   6293    317   -274  -1203       O  
ATOM   1899  CG2 THR B 166     -30.170  16.318  24.915  1.00 51.56           C  
ANISOU 1899  CG2 THR B 166     6755   6396   6438    369   -419   -781       C  
ATOM   1900  N   LEU B 167     -25.756  16.400  25.370  1.00 37.57           N  
ANISOU 1900  N   LEU B 167     4369   4267   5640   -368    -63   -323       N  
ATOM   1901  CA  LEU B 167     -24.443  16.600  25.962  1.00 35.44           C  
ANISOU 1901  CA  LEU B 167     4195   3822   5450   -603    -84   -226       C  
ATOM   1902  C   LEU B 167     -24.586  16.920  27.447  1.00 33.38           C  
ANISOU 1902  C   LEU B 167     3857   3652   5174   -493    -91    150       C  
ATOM   1903  O   LEU B 167     -25.504  17.652  27.839  1.00 33.63           O  
ANISOU 1903  O   LEU B 167     3678   3958   5143   -250    -24    251       O  
ATOM   1904  CB  LEU B 167     -23.691  17.731  25.254  1.00 35.74           C  
ANISOU 1904  CB  LEU B 167     4100   3886   5593   -531   -285   -362       C  
ATOM   1905  CG  LEU B 167     -22.920  17.409  23.969  1.00 38.00           C  
ANISOU 1905  CG  LEU B 167     4312   4346   5780   -558   -525   -470       C  
ATOM   1906  CD1 LEU B 167     -23.856  17.079  22.816  1.00 40.66           C  
ANISOU 1906  CD1 LEU B 167     4698   4788   5962   -401   -569   -406       C  
ATOM   1907  CD2 LEU B 167     -21.998  18.561  23.594  1.00 38.54           C  
ANISOU 1907  CD2 LEU B 167     4351   4510   5782   -323   -527   -572       C  
ATOM   1908  N   PRO B 168     -23.718  16.378  28.300  1.00 31.92           N  
ANISOU 1908  N   PRO B 168     3757   3395   4977   -221     -5    406       N  
ATOM   1909  CA  PRO B 168     -23.758  16.735  29.721  1.00 30.57           C  
ANISOU 1909  CA  PRO B 168     3664   3303   4647     93    136    499       C  
ATOM   1910  C   PRO B 168     -23.544  18.228  29.919  1.00 27.15           C  
ANISOU 1910  C   PRO B 168     3010   3155   4150    -42    333    507       C  
ATOM   1911  O   PRO B 168     -23.009  18.927  29.056  1.00 25.73           O  
ANISOU 1911  O   PRO B 168     2931   2908   3936    340    387    723       O  
ATOM   1912  CB  PRO B 168     -22.609  15.919  30.327  1.00 33.05           C  
ANISOU 1912  CB  PRO B 168     4244   3457   4856    -36     86    449       C  
ATOM   1913  CG  PRO B 168     -22.409  14.786  29.371  1.00 34.61           C  
ANISOU 1913  CG  PRO B 168     4445   3750   4955    -91     33    517       C  
ATOM   1914  CD  PRO B 168     -22.713  15.341  28.013  1.00 34.09           C  
ANISOU 1914  CD  PRO B 168     4261   3688   5005   -316    -44    489       C  
ATOM   1915  N   LYS B 169     -23.974  18.713  31.083  1.00 26.95           N  
ANISOU 1915  N   LYS B 169     2834   3588   3815   -647    597    276       N  
ATOM   1916  CA  LYS B 169     -23.939  20.143  31.359  1.00 28.35           C  
ANISOU 1916  CA  LYS B 169     3331   3834   3607   -437    631     -5       C  
ATOM   1917  C   LYS B 169     -22.516  20.677  31.263  1.00 25.31           C  
ANISOU 1917  C   LYS B 169     3290   3201   3124   -514    600     60       C  
ATOM   1918  O   LYS B 169     -21.576  20.082  31.799  1.00 24.62           O  
ANISOU 1918  O   LYS B 169     3207   3153   2993   -988    369     85       O  
ATOM   1919  CB  LYS B 169     -24.521  20.431  32.744  1.00 34.05           C  
ANISOU 1919  CB  LYS B 169     4297   4732   3909   -245    792    -59       C  
ATOM   1920  CG  LYS B 169     -24.762  21.910  33.005  1.00 40.38           C  
ANISOU 1920  CG  LYS B 169     5372   5786   4185   -143    922    -58       C  
ATOM   1921  CD  LYS B 169     -25.387  22.160  34.371  1.00 45.58           C  
ANISOU 1921  CD  LYS B 169     6262   6611   4448   -260    941    137       C  
ATOM   1922  CE  LYS B 169     -24.393  21.917  35.495  1.00 48.38           C  
ANISOU 1922  CE  LYS B 169     6774   7011   4597   -258   1105    212       C  
ATOM   1923  NZ  LYS B 169     -24.907  22.411  36.804  1.00 50.05           N  
ANISOU 1923  NZ  LYS B 169     7159   7133   4725   -266   1168    159       N  
ATOM   1924  N   GLY B 170     -22.359  21.796  30.562  1.00 22.83           N  
ANISOU 1924  N   GLY B 170     3253   2700   2721    232    660   -117       N  
ATOM   1925  CA  GLY B 170     -21.066  22.424  30.402  1.00 19.16           C  
ANISOU 1925  CA  GLY B 170     2676   2340   2264    560    553   -410       C  
ATOM   1926  C   GLY B 170     -20.231  21.909  29.252  1.00 17.12           C  
ANISOU 1926  C   GLY B 170     2262   2157   2085    433   -216   -293       C  
ATOM   1927  O   GLY B 170     -19.068  22.311  29.127  1.00 17.49           O  
ANISOU 1927  O   GLY B 170     2393   2195   2056    717   -509   -538       O  
ATOM   1928  N   PHE B 171     -20.776  21.039  28.409  1.00 14.92           N  
ANISOU 1928  N   PHE B 171     1906   1677   2087    -24    -64    -94       N  
ATOM   1929  CA  PHE B 171     -20.040  20.484  27.283  1.00 13.90           C  
ANISOU 1929  CA  PHE B 171     1916   1147   2219     44   -169   -170       C  
ATOM   1930  C   PHE B 171     -20.612  20.995  25.969  1.00 15.29           C  
ANISOU 1930  C   PHE B 171     1874   1508   2428   -362   -173    -17       C  
ATOM   1931  O   PHE B 171     -21.833  21.080  25.800  1.00 15.49           O  
ANISOU 1931  O   PHE B 171     1578   1498   2808   -261    297      2       O  
ATOM   1932  CB  PHE B 171     -20.056  18.956  27.324  1.00 14.33           C  
ANISOU 1932  CB  PHE B 171     2370    896   2177    133   -101     71       C  
ATOM   1933  CG  PHE B 171     -19.058  18.388  28.281  1.00 14.49           C  
ANISOU 1933  CG  PHE B 171     2458    876   2172    385   -260    396       C  
ATOM   1934  CD1 PHE B 171     -19.374  18.235  29.621  1.00 16.33           C  
ANISOU 1934  CD1 PHE B 171     3022    966   2217    302   -285    410       C  
ATOM   1935  CD2 PHE B 171     -17.785  18.054  27.853  1.00 15.52           C  
ANISOU 1935  CD2 PHE B 171     2834    795   2267    328   -182    104       C  
ATOM   1936  CE1 PHE B 171     -18.446  17.733  30.510  1.00 16.13           C  
ANISOU 1936  CE1 PHE B 171     3066    897   2166    186   -356    302       C  
ATOM   1937  CE2 PHE B 171     -16.855  17.547  28.737  1.00 17.47           C  
ANISOU 1937  CE2 PHE B 171     3200    987   2451    167   -352    443       C  
ATOM   1938  CZ  PHE B 171     -17.184  17.394  30.067  1.00 16.87           C  
ANISOU 1938  CZ  PHE B 171     3216    885   2307    -83   -292    289       C  
ATOM   1939  N   TYR B 172     -19.714  21.347  25.050  1.00 13.19           N  
ANISOU 1939  N   TYR B 172     1679   1331   2001    -76    177    214       N  
ATOM   1940  CA  TYR B 172     -20.074  21.946  23.774  1.00 13.89           C  
ANISOU 1940  CA  TYR B 172     1969   1232   2078    202   -159    -16       C  
ATOM   1941  C   TYR B 172     -19.164  21.389  22.690  1.00 15.21           C  
ANISOU 1941  C   TYR B 172     2011   1575   2195    674   -465    -92       C  
ATOM   1942  O   TYR B 172     -18.111  20.809  22.969  1.00 13.90           O  
ANISOU 1942  O   TYR B 172     1645   1570   2067    409   -337     22       O  
ATOM   1943  CB  TYR B 172     -19.961  23.479  23.813  1.00 12.35           C  
ANISOU 1943  CB  TYR B 172     1467    889   2335    191   -351     58       C  
ATOM   1944  CG  TYR B 172     -20.817  24.144  24.867  1.00 14.81           C  
ANISOU 1944  CG  TYR B 172     1549   1278   2799   -215   -155   -383       C  
ATOM   1945  CD1 TYR B 172     -20.378  24.251  26.183  1.00 16.22           C  
ANISOU 1945  CD1 TYR B 172     1703   1391   3068   -351   -185   -453       C  
ATOM   1946  CD2 TYR B 172     -22.060  24.673  24.547  1.00 16.52           C  
ANISOU 1946  CD2 TYR B 172     1844   1368   3067    158   -302   -345       C  
ATOM   1947  CE1 TYR B 172     -21.158  24.857  27.153  1.00 16.76           C  
ANISOU 1947  CE1 TYR B 172     1768   1391   3210   -520   -148   -661       C  
ATOM   1948  CE2 TYR B 172     -22.848  25.286  25.512  1.00 19.23           C  
ANISOU 1948  CE2 TYR B 172     2508   1464   3336    260   -126   -666       C  
ATOM   1949  CZ  TYR B 172     -22.391  25.373  26.812  1.00 18.90           C  
ANISOU 1949  CZ  TYR B 172     2448   1334   3398     33     45   -862       C  
ATOM   1950  OH  TYR B 172     -23.167  25.978  27.776  1.00 20.13           O  
ANISOU 1950  OH  TYR B 172     2627   1338   3683    -34    390   -436       O  
ATOM   1951  N   ALA B 173     -19.581  21.580  21.443  1.00 15.96           N  
ANISOU 1951  N   ALA B 173     2094   1840   2131    994   -659   -398       N  
ATOM   1952  CA  ALA B 173     -18.798  21.152  20.291  1.00 16.98           C  
ANISOU 1952  CA  ALA B 173     1798   2092   2560   1067   -494   -331       C  
ATOM   1953  C   ALA B 173     -19.098  22.042  19.092  1.00 18.99           C  
ANISOU 1953  C   ALA B 173     1927   2489   2800    776   -596   -372       C  
ATOM   1954  O   ALA B 173     -20.176  22.628  19.008  1.00 17.46           O  
ANISOU 1954  O   ALA B 173     1675   2306   2654    421  -1001   -484       O  
ATOM   1955  CB  ALA B 173     -19.084  19.696  19.958  1.00 18.51           C  
ANISOU 1955  CB  ALA B 173     1856   2343   2833   1099   -502   -674       C  
ATOM   1956  OXT ALA B 173     -18.281  22.193  18.183  1.00 21.24           O  
ANISOU 1956  OXT ALA B 173     1988   3135   2945    501   -422     15       O  
TER    1957      ALA B 173                                                      
ATOM   1958  N   THR C  49      -3.216  36.242  19.168  1.00 43.09           N  
ANISOU 1958  N   THR C  49     4618   7116   4640  -1031   -601     44       N  
ATOM   1959  CA  THR C  49      -2.503  36.407  17.906  1.00 42.40           C  
ANISOU 1959  CA  THR C  49     4579   6730   4800   -226   -970    145       C  
ATOM   1960  C   THR C  49      -3.471  36.557  16.730  1.00 37.84           C  
ANISOU 1960  C   THR C  49     3722   6141   4513     82  -1133     93       C  
ATOM   1961  O   THR C  49      -3.768  37.674  16.299  1.00 39.17           O  
ANISOU 1961  O   THR C  49     3781   6410   4691     57  -1226     42       O  
ATOM   1962  CB  THR C  49      -1.550  35.221  17.641  1.00 43.72           C  
ANISOU 1962  CB  THR C  49     4684   6723   5203    188  -1133    351       C  
ATOM   1963  OG1 THR C  49      -2.117  34.016  18.172  1.00 43.74           O  
ANISOU 1963  OG1 THR C  49     4595   6634   5391    167  -1003    805       O  
ATOM   1964  CG2 THR C  49      -0.194  35.470  18.287  1.00 44.54           C  
ANISOU 1964  CG2 THR C  49     4929   6780   5212    292  -1308     38       C  
ATOM   1965  N   ALA C  50      -3.961  35.434  16.212  1.00 30.94           N  
ANISOU 1965  N   ALA C  50     2669   5233   3852    573   -837    -99       N  
ATOM   1966  CA  ALA C  50      -4.886  35.435  15.089  1.00 22.98           C  
ANISOU 1966  CA  ALA C  50     1321   4197   3214    365   -482   -450       C  
ATOM   1967  C   ALA C  50      -6.314  35.240  15.580  1.00 18.07           C  
ANISOU 1967  C   ALA C  50     1079   3210   2577    -21   -627   -328       C  
ATOM   1968  O   ALA C  50      -6.559  34.503  16.540  1.00 17.57           O  
ANISOU 1968  O   ALA C  50      942   3273   2462   -140   -320   -392       O  
ATOM   1969  CB  ALA C  50      -4.529  34.340  14.082  1.00 23.13           C  
ANISOU 1969  CB  ALA C  50     1182   4348   3260    408    134   -304       C  
ATOM   1970  N   SER C  51      -7.252  35.910  14.919  1.00 13.57           N  
ANISOU 1970  N   SER C  51      809   2177   2171    459   -326   -107       N  
ATOM   1971  CA  SER C  51      -8.661  35.707  15.215  1.00 11.62           C  
ANISOU 1971  CA  SER C  51      798   1885   1730    298   -285   -323       C  
ATOM   1972  C   SER C  51      -9.085  34.294  14.834  1.00 12.36           C  
ANISOU 1972  C   SER C  51     1013   2114   1571    201    -17   -285       C  
ATOM   1973  O   SER C  51      -8.587  33.709  13.868  1.00 13.11           O  
ANISOU 1973  O   SER C  51     1136   2132   1714    265    197   -175       O  
ATOM   1974  CB  SER C  51      -9.518  36.728  14.464  1.00 11.52           C  
ANISOU 1974  CB  SER C  51      734   1897   1748    -34   -431   -290       C  
ATOM   1975  OG  SER C  51     -10.892  36.376  14.505  1.00  9.73           O  
ANISOU 1975  OG  SER C  51      707   1555   1436    148   -414   -455       O  
ATOM   1976  N   TRP C  52     -10.020  33.746  15.612  1.00 10.80           N  
ANISOU 1976  N   TRP C  52     1071   1971   1061    177   -297   -141       N  
ATOM   1977  CA  TRP C  52     -10.586  32.443  15.288  1.00  9.86           C  
ANISOU 1977  CA  TRP C  52      964   1900    882    323   -124   -234       C  
ATOM   1978  C   TRP C  52     -11.401  32.461  14.004  1.00 11.21           C  
ANISOU 1978  C   TRP C  52      750   2371   1140     60    -14   -542       C  
ATOM   1979  O   TRP C  52     -11.614  31.399  13.408  1.00 11.28           O  
ANISOU 1979  O   TRP C  52      728   2350   1206    -18    238   -367       O  
ATOM   1980  CB  TRP C  52     -11.464  31.949  16.437  1.00 10.89           C  
ANISOU 1980  CB  TRP C  52     1102   1729   1306    488    102   -349       C  
ATOM   1981  CG  TRP C  52     -10.702  31.232  17.489  1.00 11.61           C  
ANISOU 1981  CG  TRP C  52     1250   1701   1459    371   -116   -245       C  
ATOM   1982  CD1 TRP C  52     -10.452  31.661  18.761  1.00 10.91           C  
ANISOU 1982  CD1 TRP C  52     1351   1503   1291   -146    -15   -133       C  
ATOM   1983  CD2 TRP C  52     -10.070  29.953  17.364  1.00 14.50           C  
ANISOU 1983  CD2 TRP C  52     2025   1740   1744    996   -272   -559       C  
ATOM   1984  NE1 TRP C  52      -9.709  30.724  19.436  1.00 11.85           N  
ANISOU 1984  NE1 TRP C  52     1818   1041   1643    716   -185    -91       N  
ATOM   1985  CE2 TRP C  52      -9.461  29.666  18.601  1.00 15.10           C  
ANISOU 1985  CE2 TRP C  52     2078   1804   1855   1008   -430   -264       C  
ATOM   1986  CE3 TRP C  52      -9.962  29.022  16.326  1.00 16.57           C  
ANISOU 1986  CE3 TRP C  52     2343   1925   2026   1215   -314   -428       C  
ATOM   1987  CZ2 TRP C  52      -8.754  28.487  18.830  1.00 18.02           C  
ANISOU 1987  CZ2 TRP C  52     2639   1967   2240    607   -582   -405       C  
ATOM   1988  CZ3 TRP C  52      -9.259  27.849  16.556  1.00 20.00           C  
ANISOU 1988  CZ3 TRP C  52     3087   2189   2323    798   -375   -384       C  
ATOM   1989  CH2 TRP C  52      -8.664  27.594  17.797  1.00 19.66           C  
ANISOU 1989  CH2 TRP C  52     2811   2319   2340   1036   -692   -289       C  
ATOM   1990  N   PHE C  53     -11.851  33.632  13.561  1.00 11.02           N  
ANISOU 1990  N   PHE C  53      799   2126   1262    236    211   -512       N  
ATOM   1991  CA  PHE C  53     -12.797  33.745  12.462  1.00  9.80           C  
ANISOU 1991  CA  PHE C  53      770   1838   1114    240    295   -331       C  
ATOM   1992  C   PHE C  53     -12.212  34.558  11.315  1.00  9.97           C  
ANISOU 1992  C   PHE C  53      865   1652   1270     44    -19   -420       C  
ATOM   1993  O   PHE C  53     -11.294  35.363  11.495  1.00 10.36           O  
ANISOU 1993  O   PHE C  53      579   1826   1530   -234    189   -298       O  
ATOM   1994  CB  PHE C  53     -14.109  34.393  12.930  1.00  9.17           C  
ANISOU 1994  CB  PHE C  53      618   1805   1060    272     49   -439       C  
ATOM   1995  CG  PHE C  53     -14.704  33.742  14.147  1.00 10.87           C  
ANISOU 1995  CG  PHE C  53      699   2113   1318    297    141   -369       C  
ATOM   1996  CD1 PHE C  53     -15.552  32.652  14.023  1.00 11.84           C  
ANISOU 1996  CD1 PHE C  53      662   2338   1500   -213    -56   -360       C  
ATOM   1997  CD2 PHE C  53     -14.412  34.219  15.416  1.00 10.14           C  
ANISOU 1997  CD2 PHE C  53      561   1941   1350     66    170   -288       C  
ATOM   1998  CE1 PHE C  53     -16.097  32.047  15.143  1.00 12.56           C  
ANISOU 1998  CE1 PHE C  53      984   2229   1558   -506   -253   -238       C  
ATOM   1999  CE2 PHE C  53     -14.954  33.619  16.542  1.00  8.98           C  
ANISOU 1999  CE2 PHE C  53      436   1549   1426     27   -145   -151       C  
ATOM   2000  CZ  PHE C  53     -15.799  32.532  16.404  1.00  9.53           C  
ANISOU 2000  CZ  PHE C  53      673   1489   1459    -78   -385   -362       C  
ATOM   2001  N   THR C  54     -12.763  34.335  10.123  1.00  9.61           N  
ANISOU 2001  N   THR C  54     1185   1433   1032    136   -135    -76       N  
ATOM   2002  CA  THR C  54     -12.475  35.206   8.995  1.00  8.10           C  
ANISOU 2002  CA  THR C  54     1008   1223    846     42    -78    -40       C  
ATOM   2003  C   THR C  54     -13.027  36.607   9.269  1.00  9.56           C  
ANISOU 2003  C   THR C  54     1206   1362   1064     78    -39    -16       C  
ATOM   2004  O   THR C  54     -13.824  36.825  10.186  1.00 10.58           O  
ANISOU 2004  O   THR C  54     1169   1744   1107   -197     63   -528       O  
ATOM   2005  CB  THR C  54     -13.072  34.639   7.707  1.00 10.98           C  
ANISOU 2005  CB  THR C  54     1380   1494   1297    570   -125   -267       C  
ATOM   2006  OG1 THR C  54     -14.498  34.578   7.827  1.00 11.33           O  
ANISOU 2006  OG1 THR C  54     1084   1689   1532    427   -646   -386       O  
ATOM   2007  CG2 THR C  54     -12.530  33.235   7.436  1.00 12.96           C  
ANISOU 2007  CG2 THR C  54     2244   1427   1255    433   -507   -114       C  
ATOM   2008  N   ALA C  55     -12.601  37.565   8.455  1.00 10.01           N  
ANISOU 2008  N   ALA C  55     1225   1240   1339    338     10    160       N  
ATOM   2009  CA  ALA C  55     -12.922  38.964   8.694  1.00 11.25           C  
ANISOU 2009  CA  ALA C  55     1400   1331   1543   -392     38    132       C  
ATOM   2010  C   ALA C  55     -14.202  39.383   7.977  1.00 10.66           C  
ANISOU 2010  C   ALA C  55     1357   1306   1385   -359   -102   -103       C  
ATOM   2011  O   ALA C  55     -14.631  38.769   6.996  1.00 12.86           O  
ANISOU 2011  O   ALA C  55     1525   1883   1476   -438   -441   -303       O  
ATOM   2012  CB  ALA C  55     -11.767  39.862   8.248  1.00 13.13           C  
ANISOU 2012  CB  ALA C  55     1693   1550   1747   -213    -13    279       C  
ATOM   2013  N   LEU C  56     -14.814  40.448   8.491  1.00 11.32           N  
ANISOU 2013  N   LEU C  56     1293   1439   1569    -74    -67   -111       N  
ATOM   2014  CA  LEU C  56     -15.873  41.162   7.787  1.00 11.33           C  
ANISOU 2014  CA  LEU C  56      986   1688   1631   -175     22   -157       C  
ATOM   2015  C   LEU C  56     -15.237  42.318   7.023  1.00 10.91           C  
ANISOU 2015  C   LEU C  56      991   1486   1668   -112    104    -56       C  
ATOM   2016  O   LEU C  56     -14.563  43.164   7.620  1.00 10.87           O  
ANISOU 2016  O   LEU C  56      646   1435   2049   -346     64      2       O  
ATOM   2017  CB  LEU C  56     -16.933  41.682   8.759  1.00 13.63           C  
ANISOU 2017  CB  LEU C  56     1225   2040   1914   -624    144   -446       C  
ATOM   2018  CG  LEU C  56     -17.751  40.682   9.580  1.00 16.35           C  
ANISOU 2018  CG  LEU C  56     1361   2733   2119   -534    286   -685       C  
ATOM   2019  CD1 LEU C  56     -18.692  41.417  10.529  1.00 12.80           C  
ANISOU 2019  CD1 LEU C  56      595   2165   2102    -31    271    -28       C  
ATOM   2020  CD2 LEU C  56     -18.527  39.740   8.674  1.00 21.81           C  
ANISOU 2020  CD2 LEU C  56     2041   3633   2613   -708     51   -232       C  
ATOM   2021  N   THR C  57     -15.448  42.353   5.710  1.00 10.66           N  
ANISOU 2021  N   THR C  57     1426   1352   1271    148    219   -132       N  
ATOM   2022  CA  THR C  57     -14.812  43.346   4.853  1.00 11.29           C  
ANISOU 2022  CA  THR C  57     1793   1276   1219    143    432     -1       C  
ATOM   2023  C   THR C  57     -15.701  44.575   4.709  1.00 11.58           C  
ANISOU 2023  C   THR C  57     1632   1409   1358   -175    369   -102       C  
ATOM   2024  O   THR C  57     -16.887  44.461   4.382  1.00 10.98           O  
ANISOU 2024  O   THR C  57      995   1536   1641   -211    395   -180       O  
ATOM   2025  CB  THR C  57     -14.506  42.747   3.480  1.00 14.28           C  
ANISOU 2025  CB  THR C  57     2202   1984   1238    316    575   -105       C  
ATOM   2026  OG1 THR C  57     -13.546  41.693   3.628  1.00 15.35           O  
ANISOU 2026  OG1 THR C  57     2258   2540   1036    -42    241   -517       O  
ATOM   2027  CG2 THR C  57     -13.950  43.808   2.535  1.00 15.31           C  
ANISOU 2027  CG2 THR C  57     1863   2541   1413    493    815    123       C  
ATOM   2028  N   GLN C  58     -15.119  45.748   4.950  1.00 10.20           N  
ANISOU 2028  N   GLN C  58     1797    869   1209   -300    150   -295       N  
ATOM   2029  CA  GLN C  58     -15.821  47.026   4.842  1.00  9.99           C  
ANISOU 2029  CA  GLN C  58     1764    736   1297     -3    221   -167       C  
ATOM   2030  C   GLN C  58     -15.694  47.530   3.409  1.00 12.22           C  
ANISOU 2030  C   GLN C  58     1964   1424   1255    187    342   -158       C  
ATOM   2031  O   GLN C  58     -14.649  48.050   3.011  1.00 13.93           O  
ANISOU 2031  O   GLN C  58     2069   1804   1420    214    321     36       O  
ATOM   2032  CB  GLN C  58     -15.248  48.031   5.836  1.00 11.87           C  
ANISOU 2032  CB  GLN C  58     2000    879   1629    295    474   -203       C  
ATOM   2033  CG  GLN C  58     -15.923  49.390   5.805  1.00 12.85           C  
ANISOU 2033  CG  GLN C  58     2271    679   1931    171    304   -216       C  
ATOM   2034  CD  GLN C  58     -15.233  50.411   6.690  1.00 13.93           C  
ANISOU 2034  CD  GLN C  58     2316    890   2088    110     98    -86       C  
ATOM   2035  OE1 GLN C  58     -14.598  50.065   7.689  1.00 15.22           O  
ANISOU 2035  OE1 GLN C  58     2103   1505   2173    133     29   -330       O  
ATOM   2036  NE2 GLN C  58     -15.352  51.681   6.324  1.00 15.67           N  
ANISOU 2036  NE2 GLN C  58     2735    881   2337   -535   -168    117       N  
ATOM   2037  N   HIS C  59     -16.765  47.389   2.627  1.00 11.76           N  
ANISOU 2037  N   HIS C  59     1905   1467   1095    358    231    224       N  
ATOM   2038  CA  HIS C  59     -16.737  47.797   1.226  1.00 13.06           C  
ANISOU 2038  CA  HIS C  59     2023   1502   1436    132    178    -22       C  
ATOM   2039  C   HIS C  59     -17.071  49.267   1.013  1.00 15.38           C  
ANISOU 2039  C   HIS C  59     2560   1475   1810     74     33    211       C  
ATOM   2040  O   HIS C  59     -16.797  49.793  -0.072  1.00 17.62           O  
ANISOU 2040  O   HIS C  59     3132   1474   2090   -169    365    315       O  
ATOM   2041  CB  HIS C  59     -17.702  46.944   0.396  1.00 10.43           C  
ANISOU 2041  CB  HIS C  59     1729    846   1386    264    198   -303       C  
ATOM   2042  CG  HIS C  59     -17.268  45.520   0.237  1.00 11.42           C  
ANISOU 2042  CG  HIS C  59     1901    997   1441    226    250   -334       C  
ATOM   2043  ND1 HIS C  59     -17.569  44.541   1.158  1.00 13.84           N  
ANISOU 2043  ND1 HIS C  59     2062   1652   1546    525    242   -130       N  
ATOM   2044  CD2 HIS C  59     -16.552  44.911  -0.738  1.00 11.02           C  
ANISOU 2044  CD2 HIS C  59     1635   1192   1361    336    217   -392       C  
ATOM   2045  CE1 HIS C  59     -17.061  43.389   0.756  1.00 12.99           C  
ANISOU 2045  CE1 HIS C  59     1909   1574   1454    126    637   -176       C  
ATOM   2046  NE2 HIS C  59     -16.439  43.586  -0.392  1.00 11.28           N  
ANISOU 2046  NE2 HIS C  59     1698   1269   1318    132    359    -67       N  
ATOM   2047  N   GLY C  60     -17.655  49.939   2.004  1.00 15.47           N  
ANISOU 2047  N   GLY C  60     2711   1148   2020    644    184    205       N  
ATOM   2048  CA  GLY C  60     -18.039  51.329   1.845  1.00 16.91           C  
ANISOU 2048  CA  GLY C  60     2883   1363   2181    472      8    322       C  
ATOM   2049  C   GLY C  60     -17.435  52.256   2.880  1.00 17.30           C  
ANISOU 2049  C   GLY C  60     2992   1318   2263    601     54    439       C  
ATOM   2050  O   GLY C  60     -16.455  51.904   3.543  1.00 17.93           O  
ANISOU 2050  O   GLY C  60     3009   1428   2375    517   -369    784       O  
ATOM   2051  N   LYS C  61     -18.019  53.447   3.029  1.00 19.75           N  
ANISOU 2051  N   LYS C  61     3423   1685   2395    372    350    566       N  
ATOM   2052  CA  LYS C  61     -17.501  54.437   3.966  1.00 22.22           C  
ANISOU 2052  CA  LYS C  61     3700   1946   2795   -130    468    427       C  
ATOM   2053  C   LYS C  61     -17.931  54.185   5.405  1.00 21.33           C  
ANISOU 2053  C   LYS C  61     3564   1853   2689     53    327    349       C  
ATOM   2054  O   LYS C  61     -17.269  54.674   6.326  1.00 22.60           O  
ANISOU 2054  O   LYS C  61     3645   2130   2810   -561    304     44       O  
ATOM   2055  CB  LYS C  61     -17.948  55.842   3.552  1.00 27.42           C  
ANISOU 2055  CB  LYS C  61     4221   2888   3308   -333    356    642       C  
ATOM   2056  CG  LYS C  61     -17.139  56.450   2.420  1.00 33.13           C  
ANISOU 2056  CG  LYS C  61     4632   4045   3910   -335     72    212       C  
ATOM   2057  CD  LYS C  61     -15.715  56.755   2.865  1.00 37.86           C  
ANISOU 2057  CD  LYS C  61     5024   4839   4522   -245    -50    -61       C  
ATOM   2058  CE  LYS C  61     -15.686  57.802   3.972  1.00 40.58           C  
ANISOU 2058  CE  LYS C  61     5374   5133   4913    114    -76    -83       C  
ATOM   2059  NZ  LYS C  61     -16.147  59.138   3.501  1.00 41.76           N  
ANISOU 2059  NZ  LYS C  61     5560   5114   5194    385   -236    -12       N  
ATOM   2060  N  AGLU C  62     -19.012  53.441   5.622  0.46 21.14           N  
ANISOU 2060  N  AGLU C  62     3412   1963   2656    475    482    388       N  
ATOM   2061  N  BGLU C  62     -19.013  53.442   5.620  0.54 21.16           N  
ANISOU 2061  N  BGLU C  62     3340   2005   2694    540    488    240       N  
ATOM   2062  CA AGLU C  62     -19.514  53.216   6.970  0.46 21.79           C  
ANISOU 2062  CA AGLU C  62     3393   2047   2838    461    416    438       C  
ATOM   2063  CA BGLU C  62     -19.520  53.206   6.965  0.54 21.93           C  
ANISOU 2063  CA BGLU C  62     3249   2146   2936    496    390    151       C  
ATOM   2064  C  AGLU C  62     -18.647  52.202   7.703  0.46 21.14           C  
ANISOU 2064  C  AGLU C  62     3386   1881   2765    -17    507    207       C  
ATOM   2065  C  BGLU C  62     -18.640  52.202   7.700  0.54 21.26           C  
ANISOU 2065  C  BGLU C  62     3351   1917   2809     -2    499     44       C  
ATOM   2066  O  AGLU C  62     -18.341  51.129   7.172  0.46 20.66           O  
ANISOU 2066  O  AGLU C  62     3198   1890   2764   -260    513    143       O  
ATOM   2067  O  BGLU C  62     -18.320  51.135   7.168  0.54 20.82           O  
ANISOU 2067  O  BGLU C  62     3197   1911   2801   -244    496    -52       O  
ATOM   2068  CB AGLU C  62     -20.965  52.739   6.930  0.46 23.76           C  
ANISOU 2068  CB AGLU C  62     3577   2366   3085    554    317    696       C  
ATOM   2069  CB BGLU C  62     -20.962  52.703   6.910  0.54 24.20           C  
ANISOU 2069  CB BGLU C  62     3280   2617   3298    513    231    143       C  
ATOM   2070  CG AGLU C  62     -21.950  53.815   6.510  0.46 26.25           C  
ANISOU 2070  CG AGLU C  62     3867   2694   3414    550    200   1012       C  
ATOM   2071  CG BGLU C  62     -21.945  53.702   6.320  0.54 27.44           C  
ANISOU 2071  CG BGLU C  62     3406   3254   3768    357     68    198       C  
ATOM   2072  CD AGLU C  62     -23.337  53.583   7.072  0.46 28.58           C  
ANISOU 2072  CD AGLU C  62     4275   2884   3702    556    160   1367       C  
ATOM   2073  CD BGLU C  62     -22.058  54.970   7.146  0.54 30.56           C  
ANISOU 2073  CD BGLU C  62     3647   3777   4188    180      0    381       C  
ATOM   2074  OE1AGLU C  62     -23.609  52.458   7.545  0.46 29.84           O  
ANISOU 2074  OE1AGLU C  62     4664   2873   3801    688     17   1495       O  
ATOM   2075  OE1BGLU C  62     -21.907  54.892   8.384  0.54 31.40           O  
ANISOU 2075  OE1BGLU C  62     3646   3983   4303    -87    122    358       O  
ATOM   2076  OE2AGLU C  62     -24.155  54.527   7.051  0.46 29.44           O  
ANISOU 2076  OE2AGLU C  62     4344   2990   3853    561    346   1460       O  
ATOM   2077  OE2BGLU C  62     -22.294  56.047   6.557  0.54 32.15           O  
ANISOU 2077  OE2BGLU C  62     3855   3903   4458    425   -133    513       O  
ATOM   2078  N   ASP C  63     -18.252  52.546   8.925  1.00 20.57           N  
ANISOU 2078  N   ASP C  63     3397   1722   2698   -128    387     99       N  
ATOM   2079  CA  ASP C  63     -17.484  51.638   9.758  1.00 19.10           C  
ANISOU 2079  CA  ASP C  63     2978   1650   2628   -321    336    -50       C  
ATOM   2080  C   ASP C  63     -18.388  50.539  10.314  1.00 17.17           C  
ANISOU 2080  C   ASP C  63     2752   1373   2399   -269    287    -43       C  
ATOM   2081  O   ASP C  63     -19.619  50.625  10.278  1.00 14.99           O  
ANISOU 2081  O   ASP C  63     2292   1047   2355     25    799    126       O  
ATOM   2082  CB  ASP C  63     -16.813  52.396  10.902  1.00 21.92           C  
ANISOU 2082  CB  ASP C  63     3405   1737   3187   -931    316      6       C  
ATOM   2083  CG  ASP C  63     -15.829  53.439  10.416  1.00 26.59           C  
ANISOU 2083  CG  ASP C  63     4090   2399   3613  -1188     24   -113       C  
ATOM   2084  OD1 ASP C  63     -15.593  53.518   9.191  1.00 27.09           O  
ANISOU 2084  OD1 ASP C  63     4025   2450   3817  -1120    -21    -14       O  
ATOM   2085  OD2 ASP C  63     -15.292  54.184  11.262  1.00 32.07           O  
ANISOU 2085  OD2 ASP C  63     4873   3371   3941  -1509    -75    258       O  
ATOM   2086  N   LEU C  64     -17.761  49.492  10.842  1.00 14.99           N  
ANISOU 2086  N   LEU C  64     2539   1100   2056   -666    481    183       N  
ATOM   2087  CA  LEU C  64     -18.521  48.407  11.443  1.00 14.55           C  
ANISOU 2087  CA  LEU C  64     2447   1095   1986     21    493   -113       C  
ATOM   2088  C   LEU C  64     -19.130  48.850  12.769  1.00 14.75           C  
ANISOU 2088  C   LEU C  64     2429   1129   2044   -250    626   -179       C  
ATOM   2089  O   LEU C  64     -18.511  49.588  13.542  1.00 15.29           O  
ANISOU 2089  O   LEU C  64     2428   1337   2044   -102    786   -194       O  
ATOM   2090  CB  LEU C  64     -17.630  47.183  11.656  1.00 13.54           C  
ANISOU 2090  CB  LEU C  64     2004   1503   1637    224     51   -249       C  
ATOM   2091  CG  LEU C  64     -18.338  45.924  12.156  1.00 11.46           C  
ANISOU 2091  CG  LEU C  64     1581   1226   1548    301     86    -12       C  
ATOM   2092  CD1 LEU C  64     -19.412  45.479  11.168  1.00 13.28           C  
ANISOU 2092  CD1 LEU C  64     2277   1230   1539   -413    539   -126       C  
ATOM   2093  CD2 LEU C  64     -17.341  44.806  12.402  1.00 12.50           C  
ANISOU 2093  CD2 LEU C  64     1642   1271   1836     58    268    182       C  
ATOM   2094  N   LYS C  65     -20.364  48.414  13.012  1.00 14.31           N  
ANISOU 2094  N   LYS C  65     2368    804   2265     35    787    157       N  
ATOM   2095  CA  LYS C  65     -21.031  48.552  14.301  1.00 17.73           C  
ANISOU 2095  CA  LYS C  65     2695   1113   2929    333    425     58       C  
ATOM   2096  C   LYS C  65     -22.284  47.689  14.273  1.00 17.79           C  
ANISOU 2096  C   LYS C  65     2703   1481   2573    -19    719    138       C  
ATOM   2097  O   LYS C  65     -22.781  47.325  13.203  1.00 16.63           O  
ANISOU 2097  O   LYS C  65     2566   1167   2586    120    572    112       O  
ATOM   2098  CB  LYS C  65     -21.382  50.010  14.622  1.00 22.51           C  
ANISOU 2098  CB  LYS C  65     3177   1587   3789    646    257    117       C  
ATOM   2099  CG  LYS C  65     -22.465  50.610  13.749  1.00 26.34           C  
ANISOU 2099  CG  LYS C  65     3865   1738   4404   1213    253    232       C  
ATOM   2100  CD  LYS C  65     -22.841  51.996  14.248  1.00 32.63           C  
ANISOU 2100  CD  LYS C  65     4684   2490   5223   1439    410     29       C  
ATOM   2101  CE  LYS C  65     -23.951  52.606  13.413  1.00 36.90           C  
ANISOU 2101  CE  LYS C  65     5141   3126   5753   1876    286   -182       C  
ATOM   2102  NZ  LYS C  65     -24.335  53.956  13.913  1.00 40.69           N  
ANISOU 2102  NZ  LYS C  65     5762   3551   6149   1765    304   -471       N  
ATOM   2103  N   PHE C  66     -22.781  47.361  15.462  1.00 16.35           N  
ANISOU 2103  N   PHE C  66     2652   1505   2055    130    973    -88       N  
ATOM   2104  CA  PHE C  66     -23.943  46.500  15.621  1.00 14.60           C  
ANISOU 2104  CA  PHE C  66     2099   1353   2096    458    631   -355       C  
ATOM   2105  C   PHE C  66     -24.870  47.070  16.683  1.00 15.59           C  
ANISOU 2105  C   PHE C  66     2169   1737   2018    501    791   -322       C  
ATOM   2106  O   PHE C  66     -24.403  47.649  17.671  1.00 16.27           O  
ANISOU 2106  O   PHE C  66     2505   1533   2142    495    510   -610       O  
ATOM   2107  CB  PHE C  66     -23.547  45.073  16.030  1.00 11.90           C  
ANISOU 2107  CB  PHE C  66     1602    911   2009    231    -63   -245       C  
ATOM   2108  CG  PHE C  66     -22.848  44.304  14.954  1.00 11.28           C  
ANISOU 2108  CG  PHE C  66     1505    943   1836    247     66   -247       C  
ATOM   2109  CD1 PHE C  66     -23.572  43.665  13.962  1.00 11.87           C  
ANISOU 2109  CD1 PHE C  66     1432   1253   1825    206     -6   -104       C  
ATOM   2110  CD2 PHE C  66     -21.467  44.207  14.941  1.00 11.02           C  
ANISOU 2110  CD2 PHE C  66     1209   1296   1682    149   -244   -243       C  
ATOM   2111  CE1 PHE C  66     -22.932  42.946  12.974  1.00 12.89           C  
ANISOU 2111  CE1 PHE C  66     1444   1723   1731    163     37     -2       C  
ATOM   2112  CE2 PHE C  66     -20.820  43.492  13.955  1.00 12.50           C  
ANISOU 2112  CE2 PHE C  66     1444   1521   1785     90   -303    -69       C  
ATOM   2113  CZ  PHE C  66     -21.553  42.862  12.968  1.00 13.68           C  
ANISOU 2113  CZ  PHE C  66     1569   1812   1817    167   -274     60       C  
ATOM   2114  N   PRO C  67     -26.182  46.915  16.509  1.00 15.89           N  
ANISOU 2114  N   PRO C  67     1742   2241   2056    965    520   -244       N  
ATOM   2115  CA  PRO C  67     -27.106  47.235  17.603  1.00 16.44           C  
ANISOU 2115  CA  PRO C  67     1834   2390   2022    895    469   -169       C  
ATOM   2116  C   PRO C  67     -26.825  46.351  18.807  1.00 16.40           C  
ANISOU 2116  C   PRO C  67     2056   2262   1911    734    731   -328       C  
ATOM   2117  O   PRO C  67     -26.299  45.242  18.679  1.00 15.73           O  
ANISOU 2117  O   PRO C  67     1793   2225   1957    606    642   -207       O  
ATOM   2118  CB  PRO C  67     -28.488  46.944  17.004  1.00 16.91           C  
ANISOU 2118  CB  PRO C  67     1411   2877   2137    899    206   -117       C  
ATOM   2119  CG  PRO C  67     -28.287  46.975  15.524  1.00 17.44           C  
ANISOU 2119  CG  PRO C  67     1559   2903   2163   1105    190   -206       C  
ATOM   2120  CD  PRO C  67     -26.888  46.486  15.291  1.00 17.70           C  
ANISOU 2120  CD  PRO C  67     1993   2484   2247   1216    346   -239       C  
ATOM   2121  N   ARG C  68     -27.179  46.858  19.987  1.00 18.45           N  
ANISOU 2121  N   ARG C  68     2622   2399   1989    338    960   -144       N  
ATOM   2122  CA  ARG C  68     -26.925  46.130  21.224  1.00 19.64           C  
ANISOU 2122  CA  ARG C  68     2604   2731   2126    796    909    -71       C  
ATOM   2123  C   ARG C  68     -27.549  44.743  21.157  1.00 17.24           C  
ANISOU 2123  C   ARG C  68     1839   2669   2042    933    788     50       C  
ATOM   2124  O   ARG C  68     -28.712  44.587  20.774  1.00 19.02           O  
ANISOU 2124  O   ARG C  68     1956   2814   2458    744    909    206       O  
ATOM   2125  CB  ARG C  68     -27.478  46.910  22.417  1.00 27.12           C  
ANISOU 2125  CB  ARG C  68     3860   3806   2640   1124    919      7       C  
ATOM   2126  CG  ARG C  68     -26.796  46.588  23.741  1.00 33.98           C  
ANISOU 2126  CG  ARG C  68     4828   4726   3358   1373   1004   -444       C  
ATOM   2127  CD  ARG C  68     -27.205  47.564  24.838  1.00 40.55           C  
ANISOU 2127  CD  ARG C  68     5581   5704   4122   1203   1156   -440       C  
ATOM   2128  NE  ARG C  68     -28.466  47.192  25.475  1.00 45.26           N  
ANISOU 2128  NE  ARG C  68     6270   6219   4709   1165   1095   -514       N  
ATOM   2129  CZ  ARG C  68     -28.554  46.485  26.598  1.00 48.82           C  
ANISOU 2129  CZ  ARG C  68     6649   6609   5293    807    657   -468       C  
ATOM   2130  NH1 ARG C  68     -27.453  46.070  27.210  1.00 50.35           N  
ANISOU 2130  NH1 ARG C  68     6810   6787   5533    956    374   -377       N  
ATOM   2131  NH2 ARG C  68     -29.743  46.193  27.110  1.00 49.13           N  
ANISOU 2131  NH2 ARG C  68     6533   6673   5463    500    583   -643       N  
ATOM   2132  N   GLY C  69     -26.759  43.730  21.501  1.00 14.33           N  
ANISOU 2132  N   GLY C  69     1591   2182   1672   1017    215   -200       N  
ATOM   2133  CA  GLY C  69     -27.211  42.358  21.486  1.00 14.76           C  
ANISOU 2133  CA  GLY C  69     1674   2162   1772    931    -72   -212       C  
ATOM   2134  C   GLY C  69     -26.862  41.581  20.234  1.00 13.55           C  
ANISOU 2134  C   GLY C  69     1554   1968   1626    684    265   -279       C  
ATOM   2135  O   GLY C  69     -27.011  40.352  20.231  1.00 14.90           O  
ANISOU 2135  O   GLY C  69     1627   2146   1887   1023    389      9       O  
ATOM   2136  N   GLN C  70     -26.405  42.250  19.179  1.00 11.81           N  
ANISOU 2136  N   GLN C  70     1459   1489   1540    181    168    -23       N  
ATOM   2137  CA  GLN C  70     -26.099  41.616  17.904  1.00 12.29           C  
ANISOU 2137  CA  GLN C  70     1688   1627   1356    435    -78     21       C  
ATOM   2138  C   GLN C  70     -24.598  41.626  17.642  1.00 12.07           C  
ANISOU 2138  C   GLN C  70     1583   1655   1346    787    312    -16       C  
ATOM   2139  O   GLN C  70     -23.825  42.309  18.317  1.00 12.06           O  
ANISOU 2139  O   GLN C  70     1442   1611   1532    723    259    -96       O  
ATOM   2140  CB  GLN C  70     -26.827  42.326  16.755  1.00 13.20           C  
ANISOU 2140  CB  GLN C  70     1931   1812   1271    312     75    143       C  
ATOM   2141  CG  GLN C  70     -28.342  42.327  16.855  1.00 16.89           C  
ANISOU 2141  CG  GLN C  70     2132   2613   1672    634   -155    284       C  
ATOM   2142  CD  GLN C  70     -29.003  42.826  15.582  1.00 18.89           C  
ANISOU 2142  CD  GLN C  70     2405   2833   1940    634    200    455       C  
ATOM   2143  OE1 GLN C  70     -28.327  43.167  14.611  1.00 19.05           O  
ANISOU 2143  OE1 GLN C  70     2950   2476   1813    983    438    363       O  
ATOM   2144  NE2 GLN C  70     -30.329  42.868  15.580  1.00 22.33           N  
ANISOU 2144  NE2 GLN C  70     2516   3572   2394    714    148    419       N  
ATOM   2145  N   GLY C  71     -24.189  40.846  16.640  1.00 12.69           N  
ANISOU 2145  N   GLY C  71     1756   1860   1207    872    341    101       N  
ATOM   2146  CA  GLY C  71     -22.852  40.935  16.092  1.00 12.42           C  
ANISOU 2146  CA  GLY C  71     1711   1900   1109    559    258     52       C  
ATOM   2147  C   GLY C  71     -21.872  39.868  16.537  1.00 10.27           C  
ANISOU 2147  C   GLY C  71     1439   1270   1191    291     32    -96       C  
ATOM   2148  O   GLY C  71     -20.756  39.826  16.005  1.00 10.79           O  
ANISOU 2148  O   GLY C  71     1395   1370   1336     33    539     20       O  
ATOM   2149  N   VAL C  72     -22.233  39.012  17.482  1.00 10.02           N  
ANISOU 2149  N   VAL C  72     1314   1213   1281    310   -168     -4       N  
ATOM   2150  CA  VAL C  72     -21.293  37.989  17.948  1.00  8.94           C  
ANISOU 2150  CA  VAL C  72     1493    651   1253     19   -313    125       C  
ATOM   2151  C   VAL C  72     -21.281  36.835  16.949  1.00  8.29           C  
ANISOU 2151  C   VAL C  72      847   1107   1197    388   -266     93       C  
ATOM   2152  O   VAL C  72     -22.352  36.298  16.624  1.00  9.03           O  
ANISOU 2152  O   VAL C  72      717   1644   1069    185   -276    158       O  
ATOM   2153  CB  VAL C  72     -21.667  37.506  19.345  1.00  8.25           C  
ANISOU 2153  CB  VAL C  72     1481    439   1213    200     85    123       C  
ATOM   2154  CG1 VAL C  72     -20.720  36.398  19.788  1.00  9.01           C  
ANISOU 2154  CG1 VAL C  72     1323    785   1313    -48     18    210       C  
ATOM   2155  CG2 VAL C  72     -21.626  38.666  20.335  1.00 10.84           C  
ANISOU 2155  CG2 VAL C  72     1943    839   1338    544    398    -15       C  
ATOM   2156  N   PRO C  73     -20.113  36.431  16.446  1.00  9.13           N  
ANISOU 2156  N   PRO C  73      784   1122   1562   -226     91   -391       N  
ATOM   2157  CA  PRO C  73     -20.065  35.333  15.470  1.00 10.69           C  
ANISOU 2157  CA  PRO C  73      818   1623   1622   -101    406   -515       C  
ATOM   2158  C   PRO C  73     -20.609  34.031  16.041  1.00 11.17           C  
ANISOU 2158  C   PRO C  73     1145   1388   1711   -110    324   -473       C  
ATOM   2159  O   PRO C  73     -20.473  33.739  17.231  1.00 11.34           O  
ANISOU 2159  O   PRO C  73     1143   1423   1741     55    126   -317       O  
ATOM   2160  CB  PRO C  73     -18.571  35.212  15.146  1.00  9.19           C  
ANISOU 2160  CB  PRO C  73      753   1351   1386   -106    412   -559       C  
ATOM   2161  CG  PRO C  73     -17.998  36.546  15.484  1.00  9.25           C  
ANISOU 2161  CG  PRO C  73      845   1112   1559   -181    351   -729       C  
ATOM   2162  CD  PRO C  73     -18.790  37.040  16.662  1.00  7.42           C  
ANISOU 2162  CD  PRO C  73      613    793   1413    -31    205   -541       C  
ATOM   2163  N   ILE C  74     -21.221  33.238  15.162  1.00 11.06           N  
ANISOU 2163  N   ILE C  74     1085   1204   1913   -317     94   -192       N  
ATOM   2164  CA  ILE C  74     -21.768  31.947  15.558  1.00 10.96           C  
ANISOU 2164  CA  ILE C  74      880   1357   1927   -185   -169    -72       C  
ATOM   2165  C   ILE C  74     -20.629  30.983  15.856  1.00  9.88           C  
ANISOU 2165  C   ILE C  74      838   1327   1590     -6   -346    122       C  
ATOM   2166  O   ILE C  74     -19.706  30.815  15.047  1.00 10.71           O  
ANISOU 2166  O   ILE C  74      977   1694   1399   -367   -394    147       O  
ATOM   2167  CB  ILE C  74     -22.691  31.398  14.460  1.00  9.12           C  
ANISOU 2167  CB  ILE C  74      595   1012   1859   -173   -247   -121       C  
ATOM   2168  CG1 ILE C  74     -23.875  32.343  14.246  1.00  9.64           C  
ANISOU 2168  CG1 ILE C  74      644   1244   1776     82   -399   -358       C  
ATOM   2169  CG2 ILE C  74     -23.172  29.990  14.809  1.00  9.47           C  
ANISOU 2169  CG2 ILE C  74      583    960   2057   -133    -82   -227       C  
ATOM   2170  CD1 ILE C  74     -24.739  31.981  13.055  1.00 11.40           C  
ANISOU 2170  CD1 ILE C  74      860   1566   1907    159   -514   -633       C  
ATOM   2171  N   ASN C  75     -20.687  30.343  17.024  1.00  7.93           N  
ANISOU 2171  N   ASN C  75      630    973   1409    -48   -467    -14       N  
ATOM   2172  CA  ASN C  75     -19.680  29.359  17.419  1.00  6.90           C  
ANISOU 2172  CA  ASN C  75      516    950   1156   -112   -349   -102       C  
ATOM   2173  C   ASN C  75     -20.354  28.388  18.386  1.00  9.10           C  
ANISOU 2173  C   ASN C  75      991    921   1544    -48   -638   -241       C  
ATOM   2174  O   ASN C  75     -20.520  28.704  19.567  1.00 10.45           O  
ANISOU 2174  O   ASN C  75     1074   1240   1658    241   -727   -373       O  
ATOM   2175  CB  ASN C  75     -18.468  30.034  18.051  1.00  5.92           C  
ANISOU 2175  CB  ASN C  75      394    750   1105     57   -134   -468       C  
ATOM   2176  CG  ASN C  75     -17.437  29.039  18.551  1.00  9.27           C  
ANISOU 2176  CG  ASN C  75      979   1252   1292     25   -418   -597       C  
ATOM   2177  OD1 ASN C  75     -17.491  27.852  18.228  1.00 11.78           O  
ANISOU 2177  OD1 ASN C  75     1469   1495   1512   -372   -392   -567       O  
ATOM   2178  ND2 ASN C  75     -16.482  29.523  19.342  1.00 10.63           N  
ANISOU 2178  ND2 ASN C  75     1047   1471   1522     92   -667   -397       N  
ATOM   2179  N   THR C  76     -20.733  27.210  17.881  1.00 13.21           N  
ANISOU 2179  N   THR C  76     1766   1310   1943    -97   -627   -239       N  
ATOM   2180  CA  THR C  76     -21.409  26.240  18.734  1.00 13.73           C  
ANISOU 2180  CA  THR C  76     1987   1165   2066   -282   -677   -333       C  
ATOM   2181  C   THR C  76     -20.503  25.706  19.837  1.00 12.47           C  
ANISOU 2181  C   THR C  76     1679   1081   1977   -111   -591   -393       C  
ATOM   2182  O   THR C  76     -21.008  25.150  20.817  1.00 12.86           O  
ANISOU 2182  O   THR C  76     1502   1288   2094   -538   -418   -247       O  
ATOM   2183  CB  THR C  76     -21.960  25.077  17.902  1.00 14.28           C  
ANISOU 2183  CB  THR C  76     1905   1466   2053   -114   -877   -447       C  
ATOM   2184  OG1 THR C  76     -20.899  24.463  17.159  1.00 14.77           O  
ANISOU 2184  OG1 THR C  76     2286   1309   2016    319   -431   -844       O  
ATOM   2185  CG2 THR C  76     -23.034  25.568  16.941  1.00 16.27           C  
ANISOU 2185  CG2 THR C  76     1710   2086   2385   -679   -900   -123       C  
ATOM   2186  N   ASN C  77     -19.187  25.867  19.710  1.00 11.64           N  
ANISOU 2186  N   ASN C  77     1643    920   1861   -104   -475   -315       N  
ATOM   2187  CA  ASN C  77     -18.255  25.455  20.759  1.00 10.02           C  
ANISOU 2187  CA  ASN C  77     1022   1063   1722    470   -467   -170       C  
ATOM   2188  C   ASN C  77     -17.980  26.598  21.733  1.00  9.65           C  
ANISOU 2188  C   ASN C  77     1069   1020   1577    383   -663   -335       C  
ATOM   2189  O   ASN C  77     -16.838  26.981  21.984  1.00 11.91           O  
ANISOU 2189  O   ASN C  77     1473   1517   1536    618   -787   -515       O  
ATOM   2190  CB  ASN C  77     -16.961  24.930  20.145  1.00 10.76           C  
ANISOU 2190  CB  ASN C  77      870   1455   1763    295   -497    250       C  
ATOM   2191  CG  ASN C  77     -16.080  24.229  21.163  1.00 14.17           C  
ANISOU 2191  CG  ASN C  77     1377   1824   2184    327   -232    294       C  
ATOM   2192  OD1 ASN C  77     -16.465  24.071  22.323  1.00 13.76           O  
ANISOU 2192  OD1 ASN C  77     1382   1704   2141    552   -317    343       O  
ATOM   2193  ND2 ASN C  77     -14.894  23.804  20.736  1.00 16.94           N  
ANISOU 2193  ND2 ASN C  77     2011   2169   2256    198   -420    139       N  
ATOM   2194  N   SER C  78     -19.052  27.156  22.287  1.00 10.35           N  
ANISOU 2194  N   SER C  78     1305   1051   1578    369   -805   -457       N  
ATOM   2195  CA  SER C  78     -18.953  28.216  23.279  1.00 10.66           C  
ANISOU 2195  CA  SER C  78     1414   1139   1497    162   -418   -351       C  
ATOM   2196  C   SER C  78     -20.276  28.292  24.022  1.00 12.43           C  
ANISOU 2196  C   SER C  78     1704   1570   1450    -67   -421   -330       C  
ATOM   2197  O   SER C  78     -21.318  27.889  23.500  1.00 13.99           O  
ANISOU 2197  O   SER C  78     1421   2209   1688   -121   -275   -469       O  
ATOM   2198  CB  SER C  78     -18.606  29.570  22.642  1.00 13.15           C  
ANISOU 2198  CB  SER C  78     1748   1580   1667   -235   -212   -640       C  
ATOM   2199  OG  SER C  78     -19.622  30.017  21.760  1.00 14.08           O  
ANISOU 2199  OG  SER C  78     2378   1479   1493   -584    241   -714       O  
ATOM   2200  N   SER C  79     -20.218  28.803  25.244  1.00 12.54           N  
ANISOU 2200  N   SER C  79     1929   1623   1212   -407    -45   -216       N  
ATOM   2201  CA  SER C  79     -21.365  28.884  26.128  1.00 12.21           C  
ANISOU 2201  CA  SER C  79     1771   1614   1255   -313   -469   -426       C  
ATOM   2202  C   SER C  79     -22.019  30.252  26.031  1.00 11.60           C  
ANISOU 2202  C   SER C  79     1421   1418   1568     -7   -407     87       C  
ATOM   2203  O   SER C  79     -21.423  31.201  25.514  1.00 11.67           O  
ANISOU 2203  O   SER C  79     1706   1170   1559    -50   -118    510       O  
ATOM   2204  CB  SER C  79     -20.927  28.624  27.573  1.00 13.25           C  
ANISOU 2204  CB  SER C  79     1909   1811   1313    -39   -746   -517       C  
ATOM   2205  OG  SER C  79     -20.192  29.724  28.077  1.00 13.96           O  
ANISOU 2205  OG  SER C  79     1759   2119   1426     95   -549   -568       O  
ATOM   2206  N   PRO C  80     -23.257  30.391  26.513  1.00 11.77           N  
ANISOU 2206  N   PRO C  80     1305   1108   2060   -383   -277     74       N  
ATOM   2207  CA  PRO C  80     -23.859  31.734  26.591  1.00 10.99           C  
ANISOU 2207  CA  PRO C  80     1111    939   2128    -10   -157    236       C  
ATOM   2208  C   PRO C  80     -23.000  32.742  27.338  1.00  9.80           C  
ANISOU 2208  C   PRO C  80      895   1098   1732    131   -289   -147       C  
ATOM   2209  O   PRO C  80     -23.023  33.933  27.000  1.00  9.63           O  
ANISOU 2209  O   PRO C  80     1045    915   1700    -63   -131   -226       O  
ATOM   2210  CB  PRO C  80     -25.186  31.472  27.313  1.00 14.75           C  
ANISOU 2210  CB  PRO C  80     2104   1051   2448   -259    -27    229       C  
ATOM   2211  CG  PRO C  80     -25.530  30.065  26.944  1.00 15.25           C  
ANISOU 2211  CG  PRO C  80     2148   1147   2501    251    327    -33       C  
ATOM   2212  CD  PRO C  80     -24.219  29.331  26.868  1.00 13.62           C  
ANISOU 2212  CD  PRO C  80     1506   1328   2342     51     -1     -2       C  
ATOM   2213  N   ASP C  81     -22.231  32.298  28.339  1.00 10.35           N  
ANISOU 2213  N   ASP C  81      744   1698   1492   -185   -524    -93       N  
ATOM   2214  CA  ASP C  81     -21.341  33.207  29.056  1.00 12.60           C  
ANISOU 2214  CA  ASP C  81     1719   1505   1563   -543   -450     60       C  
ATOM   2215  C   ASP C  81     -20.279  33.806  28.141  1.00  9.87           C  
ANISOU 2215  C   ASP C  81     1113   1198   1439   -358   -137     90       C  
ATOM   2216  O   ASP C  81     -19.794  34.914  28.401  1.00 11.57           O  
ANISOU 2216  O   ASP C  81     1447   1423   1524     67   -275   -496       O  
ATOM   2217  CB  ASP C  81     -20.657  32.478  30.216  1.00 15.31           C  
ANISOU 2217  CB  ASP C  81     2430   1809   1580   -710   -301    265       C  
ATOM   2218  CG  ASP C  81     -21.629  32.037  31.295  1.00 20.48           C  
ANISOU 2218  CG  ASP C  81     3377   2503   1900   -896   -207    147       C  
ATOM   2219  OD1 ASP C  81     -22.819  32.413  31.230  1.00 22.14           O  
ANISOU 2219  OD1 ASP C  81     3100   3117   2195  -1103    390    181       O  
ATOM   2220  OD2 ASP C  81     -21.196  31.310  32.213  1.00 23.29           O  
ANISOU 2220  OD2 ASP C  81     4246   2703   1902  -1231   -112     75       O  
ATOM   2221  N   ASP C  82     -19.909  33.098  27.071  1.00  8.88           N  
ANISOU 2221  N   ASP C  82     1198   1137   1039    -93   -170    -21       N  
ATOM   2222  CA  ASP C  82     -18.758  33.450  26.245  1.00  9.63           C  
ANISOU 2222  CA  ASP C  82     1234   1098   1329     76    114     54       C  
ATOM   2223  C   ASP C  82     -19.054  34.479  25.159  1.00  7.74           C  
ANISOU 2223  C   ASP C  82     1031    856   1054    138     -1    332       C  
ATOM   2224  O   ASP C  82     -18.114  34.931  24.497  1.00  9.49           O  
ANISOU 2224  O   ASP C  82     1089   1043   1474   -173   -104     83       O  
ATOM   2225  CB  ASP C  82     -18.190  32.199  25.563  1.00 10.65           C  
ANISOU 2225  CB  ASP C  82     1352   1025   1669    589    -91   -339       C  
ATOM   2226  CG  ASP C  82     -17.599  31.207  26.541  1.00 11.55           C  
ANISOU 2226  CG  ASP C  82     1344   1347   1698    171   -516   -577       C  
ATOM   2227  OD1 ASP C  82     -17.187  31.621  27.644  1.00 11.49           O  
ANISOU 2227  OD1 ASP C  82      844   1718   1802    197   -541   -455       O  
ATOM   2228  OD2 ASP C  82     -17.534  30.006  26.195  1.00 11.87           O  
ANISOU 2228  OD2 ASP C  82     1591   1240   1678      4   -632   -488       O  
ATOM   2229  N   GLN C  83     -20.315  34.858  24.953  1.00  8.82           N  
ANISOU 2229  N   GLN C  83      960   1264   1125    -38    381      1       N  
ATOM   2230  CA  GLN C  83     -20.724  35.563  23.732  1.00  9.38           C  
ANISOU 2230  CA  GLN C  83     1355   1016   1194   -159    125    -89       C  
ATOM   2231  C   GLN C  83     -20.499  37.071  23.865  1.00  8.87           C  
ANISOU 2231  C   GLN C  83     1090   1113   1165   -480    231   -115       C  
ATOM   2232  O   GLN C  83     -21.432  37.878  23.900  1.00  7.68           O  
ANISOU 2232  O   GLN C  83      883    866   1170   -170   -174    -66       O  
ATOM   2233  CB  GLN C  83     -22.180  35.251  23.414  1.00  9.27           C  
ANISOU 2233  CB  GLN C  83     1337    793   1392   -154   -293   -390       C  
ATOM   2234  CG  GLN C  83     -22.500  33.768  23.382  1.00  9.26           C  
ANISOU 2234  CG  GLN C  83     1511    697   1312    216   -466   -393       C  
ATOM   2235  CD  GLN C  83     -21.677  33.033  22.354  1.00  9.64           C  
ANISOU 2235  CD  GLN C  83     1182   1158   1325    -38   -370   -446       C  
ATOM   2236  OE1 GLN C  83     -21.641  33.415  21.185  1.00 11.49           O  
ANISOU 2236  OE1 GLN C  83     1656   1467   1242     30    -70   -714       O  
ATOM   2237  NE2 GLN C  83     -20.998  31.976  22.785  1.00 10.37           N  
ANISOU 2237  NE2 GLN C  83      975   1583   1382    113   -277     82       N  
ATOM   2238  N   ILE C  84     -19.225  37.453  23.896  1.00  6.46           N  
ANISOU 2238  N   ILE C  84      609    828   1017   -337    -21   -269       N  
ATOM   2239  CA  ILE C  84     -18.863  38.855  24.093  1.00  8.41           C  
ANISOU 2239  CA  ILE C  84      937   1307    950   -577     28   -318       C  
ATOM   2240  C   ILE C  84     -17.436  39.060  23.600  1.00  8.84           C  
ANISOU 2240  C   ILE C  84     1309   1148    902   -249    378   -136       C  
ATOM   2241  O   ILE C  84     -16.561  38.218  23.820  1.00  9.43           O  
ANISOU 2241  O   ILE C  84     1295   1221   1067   -220    294   -284       O  
ATOM   2242  CB  ILE C  84     -19.039  39.262  25.577  1.00  9.25           C  
ANISOU 2242  CB  ILE C  84     1076   1612    825   -188     55   -338       C  
ATOM   2243  CG1 ILE C  84     -18.657  40.723  25.803  1.00 10.20           C  
ANISOU 2243  CG1 ILE C  84     1651   1237    988    169    222   -603       C  
ATOM   2244  CG2 ILE C  84     -18.248  38.333  26.492  1.00  7.92           C  
ANISOU 2244  CG2 ILE C  84      429   1633    947     45     92    -69       C  
ATOM   2245  CD1 ILE C  84     -19.027  41.224  27.188  1.00 11.78           C  
ANISOU 2245  CD1 ILE C  84     1961   1290   1224     50    173   -723       C  
ATOM   2246  N   GLY C  85     -17.210  40.178  22.922  1.00  8.23           N  
ANISOU 2246  N   GLY C  85     1123   1179    827   -240    467   -146       N  
ATOM   2247  CA  GLY C  85     -15.886  40.467  22.407  1.00  9.69           C  
ANISOU 2247  CA  GLY C  85     1516   1083   1084    277    489    -94       C  
ATOM   2248  C   GLY C  85     -15.861  41.754  21.615  1.00  9.18           C  
ANISOU 2248  C   GLY C  85     1338    931   1221    348    249   -342       C  
ATOM   2249  O   GLY C  85     -16.751  42.597  21.739  1.00 10.58           O  
ANISOU 2249  O   GLY C  85     1419    959   1641    147   -288   -541       O  
ATOM   2250  N   TYR C  86     -14.822  41.900  20.795  1.00  8.51           N  
ANISOU 2250  N   TYR C  86     1559    765    910    -38    -92     -2       N  
ATOM   2251  CA  TYR C  86     -14.632  43.108  20.007  1.00  8.30           C  
ANISOU 2251  CA  TYR C  86     1357    952    845   -198   -120   -357       C  
ATOM   2252  C   TYR C  86     -14.215  42.746  18.591  1.00  8.63           C  
ANISOU 2252  C   TYR C  86     1164   1068   1048     23    -60   -287       C  
ATOM   2253  O   TYR C  86     -13.629  41.687  18.345  1.00  9.95           O  
ANISOU 2253  O   TYR C  86     1557   1140   1084   -401    141   -151       O  
ATOM   2254  CB  TYR C  86     -13.578  44.038  20.631  1.00  9.89           C  
ANISOU 2254  CB  TYR C  86     1352   1228   1178   -242   -186      7       C  
ATOM   2255  CG  TYR C  86     -12.195  43.432  20.736  1.00 10.97           C  
ANISOU 2255  CG  TYR C  86     1015   1855   1298   -530   -424    -40       C  
ATOM   2256  CD1 TYR C  86     -11.829  42.681  21.848  1.00 10.38           C  
ANISOU 2256  CD1 TYR C  86      855   1656   1434   -274   -546   -171       C  
ATOM   2257  CD2 TYR C  86     -11.253  43.615  19.729  1.00 10.59           C  
ANISOU 2257  CD2 TYR C  86     1010   1643   1371   -416   -535   -138       C  
ATOM   2258  CE1 TYR C  86     -10.567  42.124  21.950  1.00 10.44           C  
ANISOU 2258  CE1 TYR C  86      799   1683   1483   -460   -234   -296       C  
ATOM   2259  CE2 TYR C  86      -9.988  43.062  19.823  1.00 11.16           C  
ANISOU 2259  CE2 TYR C  86      890   1908   1443   -269   -271   -280       C  
ATOM   2260  CZ  TYR C  86      -9.651  42.318  20.937  1.00 11.75           C  
ANISOU 2260  CZ  TYR C  86      755   2109   1598   -296   -245   -395       C  
ATOM   2261  OH  TYR C  86      -8.396  41.762  21.043  1.00 11.84           O  
ANISOU 2261  OH  TYR C  86      628   2151   1720   -280      9   -256       O  
ATOM   2262  N   TYR C  87     -14.534  43.640  17.662  1.00  8.16           N  
ANISOU 2262  N   TYR C  87      900   1128   1071   -446    -99   -374       N  
ATOM   2263  CA  TYR C  87     -13.985  43.610  16.317  1.00  9.24           C  
ANISOU 2263  CA  TYR C  87      913   1440   1158   -512   -240   -251       C  
ATOM   2264  C   TYR C  87     -12.868  44.639  16.220  1.00 11.91           C  
ANISOU 2264  C   TYR C  87     1353   1843   1330   -436   -247   -537       C  
ATOM   2265  O   TYR C  87     -12.994  45.758  16.729  1.00 14.51           O  
ANISOU 2265  O   TYR C  87     1793   1930   1789   -461    172   -185       O  
ATOM   2266  CB  TYR C  87     -15.055  43.914  15.269  1.00  9.59           C  
ANISOU 2266  CB  TYR C  87      912   1498   1234   -321   -490   -236       C  
ATOM   2267  CG  TYR C  87     -16.046  42.804  14.997  1.00  9.16           C  
ANISOU 2267  CG  TYR C  87     1076   1272   1132   -151   -133   -448       C  
ATOM   2268  CD1 TYR C  87     -17.189  42.656  15.775  1.00  9.93           C  
ANISOU 2268  CD1 TYR C  87     1405   1248   1122    -37     98   -202       C  
ATOM   2269  CD2 TYR C  87     -15.861  41.930  13.931  1.00  8.89           C  
ANISOU 2269  CD2 TYR C  87     1228    883   1267   -237   -138     55       C  
ATOM   2270  CE1 TYR C  87     -18.109  41.655  15.513  1.00  8.73           C  
ANISOU 2270  CE1 TYR C  87     1019    959   1340    244    157     47       C  
ATOM   2271  CE2 TYR C  87     -16.773  40.927  13.661  1.00 10.28           C  
ANISOU 2271  CE2 TYR C  87     1112   1320   1473   -252    -97    238       C  
ATOM   2272  CZ  TYR C  87     -17.897  40.795  14.455  1.00  9.27           C  
ANISOU 2272  CZ  TYR C  87     1070   1051   1401   -479    273    120       C  
ATOM   2273  OH  TYR C  87     -18.806  39.799  14.185  1.00  9.68           O  
ANISOU 2273  OH  TYR C  87     1067   1147   1465   -239    253    -68       O  
ATOM   2274  N   ARG C  88     -11.773  44.257  15.571  1.00 12.55           N  
ANISOU 2274  N   ARG C  88     1226   2240   1301   -392    146   -266       N  
ATOM   2275  CA  ARG C  88     -10.615  45.122  15.404  1.00 13.73           C  
ANISOU 2275  CA  ARG C  88     1318   2420   1480   -621   -165     60       C  
ATOM   2276  C   ARG C  88     -10.380  45.358  13.919  1.00 12.84           C  
ANISOU 2276  C   ARG C  88     1107   2281   1491   -654    225     32       C  
ATOM   2277  O   ARG C  88     -10.246  44.402  13.146  1.00 11.44           O  
ANISOU 2277  O   ARG C  88      727   2154   1467   -481     43   -109       O  
ATOM   2278  CB  ARG C  88      -9.373  44.511  16.056  1.00 15.30           C  
ANISOU 2278  CB  ARG C  88     1332   2708   1773   -959   -270    376       C  
ATOM   2279  CG  ARG C  88      -8.117  45.355  15.928  1.00 17.75           C  
ANISOU 2279  CG  ARG C  88     1401   3129   2214  -1037     16    186       C  
ATOM   2280  CD  ARG C  88      -7.011  44.797  16.810  1.00 24.97           C  
ANISOU 2280  CD  ARG C  88     2279   4260   2947  -1659    262     25       C  
ATOM   2281  NE  ARG C  88      -5.750  45.515  16.649  1.00 30.08           N  
ANISOU 2281  NE  ARG C  88     2993   4954   3482  -1678    715     65       N  
ATOM   2282  CZ  ARG C  88      -4.740  45.089  15.898  1.00 34.74           C  
ANISOU 2282  CZ  ARG C  88     3943   5267   3989  -1553    839   -120       C  
ATOM   2283  NH1 ARG C  88      -4.840  43.945  15.236  1.00 37.00           N  
ANISOU 2283  NH1 ARG C  88     4361   5458   4240  -1353    984    -30       N  
ATOM   2284  NH2 ARG C  88      -3.629  45.807  15.812  1.00 37.24           N  
ANISOU 2284  NH2 ARG C  88     4372   5502   4275  -1423    936   -236       N  
ATOM   2285  N   ARG C  89     -10.333  46.628  13.527  1.00 13.05           N  
ANISOU 2285  N   ARG C  89     1423   1962   1573   -718     59     46       N  
ATOM   2286  CA  ARG C  89     -10.122  46.987  12.133  1.00 14.62           C  
ANISOU 2286  CA  ARG C  89     1727   2184   1645   -754    316    189       C  
ATOM   2287  C   ARG C  89      -8.659  46.811  11.748  1.00 16.38           C  
ANISOU 2287  C   ARG C  89     1687   2652   1885   -988    282    -67       C  
ATOM   2288  O   ARG C  89      -7.754  47.171  12.504  1.00 18.52           O  
ANISOU 2288  O   ARG C  89     1785   3437   1816   -923    137   -202       O  
ATOM   2289  CB  ARG C  89     -10.553  48.432  11.885  1.00 16.71           C  
ANISOU 2289  CB  ARG C  89     2327   2242   1780   -718    274    499       C  
ATOM   2290  CG  ARG C  89     -10.275  48.930  10.469  1.00 17.57           C  
ANISOU 2290  CG  ARG C  89     2490   2163   2022   -977    415    661       C  
ATOM   2291  CD  ARG C  89     -10.715  50.369  10.302  1.00 21.90           C  
ANISOU 2291  CD  ARG C  89     3230   2634   2458   -984    210    458       C  
ATOM   2292  NE  ARG C  89     -10.058  51.244  11.265  1.00 24.92           N  
ANISOU 2292  NE  ARG C  89     3939   2568   2961   -976   -257    457       N  
ATOM   2293  CZ  ARG C  89     -10.573  52.386  11.706  1.00 26.95           C  
ANISOU 2293  CZ  ARG C  89     4213   2830   3198  -1351   -454    631       C  
ATOM   2294  NH1 ARG C  89     -11.760  52.791  11.272  1.00 26.64           N  
ANISOU 2294  NH1 ARG C  89     3801   3119   3202  -1305   -791    642       N  
ATOM   2295  NH2 ARG C  89      -9.905  53.117  12.587  1.00 27.61           N  
ANISOU 2295  NH2 ARG C  89     4216   3070   3204  -1778   -565    595       N  
ATOM   2296  N   ALA C  90      -8.436  46.249  10.562  1.00 17.28           N  
ANISOU 2296  N   ALA C  90     1940   2544   2082   -572    252     15       N  
ATOM   2297  CA  ALA C  90      -7.107  46.119   9.983  1.00 21.34           C  
ANISOU 2297  CA  ALA C  90     2571   3046   2491   -375    282     19       C  
ATOM   2298  C   ALA C  90      -7.157  46.606   8.544  1.00 23.15           C  
ANISOU 2298  C   ALA C  90     2801   3283   2713   -564    249     54       C  
ATOM   2299  O   ALA C  90      -8.077  46.258   7.797  1.00 21.29           O  
ANISOU 2299  O   ALA C  90     2590   2936   2562   -586     75   -219       O  
ATOM   2300  CB  ALA C  90      -6.608  44.671  10.042  1.00 22.06           C  
ANISOU 2300  CB  ALA C  90     2593   3069   2720    -64    215     46       C  
ATOM   2301  N  ATHR C  91      -6.166  47.407   8.161  0.51 23.83           N  
ANISOU 2301  N  ATHR C  91     2664   3593   2796   -462    366    -13       N  
ATOM   2302  N  BTHR C  91      -6.176  47.418   8.157  0.49 24.53           N  
ANISOU 2302  N  BTHR C  91     2773   3651   2895   -431    417     69       N  
ATOM   2303  CA ATHR C  91      -6.099  48.007   6.837  0.51 25.15           C  
ANISOU 2303  CA ATHR C  91     2858   3773   2927   -494    489    -79       C  
ATOM   2304  CA BTHR C  91      -6.120  48.002   6.824  0.49 26.57           C  
ANISOU 2304  CA BTHR C  91     3056   3921   3119   -420    600     86       C  
ATOM   2305  C  ATHR C  91      -4.811  47.578   6.151  0.51 26.69           C  
ANISOU 2305  C  ATHR C  91     3041   4093   3007   -504    258   -294       C  
ATOM   2306  C  BTHR C  91      -4.820  47.599   6.145  0.49 27.40           C  
ANISOU 2306  C  BTHR C  91     3160   4144   3108   -462    333   -186       C  
ATOM   2307  O  ATHR C  91      -3.733  47.641   6.751  0.51 25.91           O  
ANISOU 2307  O  ATHR C  91     2666   4206   2972   -514   -183   -545       O  
ATOM   2308  O  BTHR C  91      -3.745  47.699   6.744  0.49 26.77           O  
ANISOU 2308  O  BTHR C  91     2848   4234   3088   -465    -67   -394       O  
ATOM   2309  CB ATHR C  91      -6.165  49.534   6.920  0.51 26.09           C  
ANISOU 2309  CB ATHR C  91     3072   3851   2991   -518    583     14       C  
ATOM   2310  CB BTHR C  91      -6.234  49.529   6.881  0.49 29.02           C  
ANISOU 2310  CB BTHR C  91     3447   4201   3379   -332    824    336       C  
ATOM   2311  OG1ATHR C  91      -5.101  50.015   7.752  0.51 24.83           O  
ANISOU 2311  OG1ATHR C  91     2942   3580   2912   -684    552     23       O  
ATOM   2312  OG1BTHR C  91      -7.455  49.895   7.537  0.49 29.17           O  
ANISOU 2312  OG1BTHR C  91     3313   4319   3451   -108    886    450       O  
ATOM   2313  CG2ATHR C  91      -7.497  49.974   7.506  0.51 26.42           C  
ANISOU 2313  CG2ATHR C  91     3004   3987   3047   -329    636    145       C  
ATOM   2314  CG2BTHR C  91      -6.225  50.121   5.476  0.49 29.88           C  
ANISOU 2314  CG2BTHR C  91     3641   4212   3498   -440    923    500       C  
ATOM   2315  N   ARG C  92      -4.925  47.144   4.900  1.00 27.98           N  
ANISOU 2315  N   ARG C  92     3355   4224   3052   -492    648   -137       N  
ATOM   2316  CA  ARG C  92      -3.779  46.746   4.101  1.00 27.62           C  
ANISOU 2316  CA  ARG C  92     3201   4110   3185   -576   1070    -31       C  
ATOM   2317  C   ARG C  92      -3.497  47.790   3.031  1.00 25.92           C  
ANISOU 2317  C   ARG C  92     2864   3934   3051   -293    940   -221       C  
ATOM   2318  O   ARG C  92      -4.406  48.471   2.546  1.00 22.60           O  
ANISOU 2318  O   ARG C  92     1967   3944   2675     52    749   -319       O  
ATOM   2319  CB  ARG C  92      -4.012  45.394   3.425  1.00 30.16           C  
ANISOU 2319  CB  ARG C  92     3561   4474   3426   -639   1121    151       C  
ATOM   2320  CG  ARG C  92      -3.905  44.190   4.331  1.00 32.49           C  
ANISOU 2320  CG  ARG C  92     3978   4724   3643   -355    475    144       C  
ATOM   2321  CD  ARG C  92      -4.286  42.945   3.555  1.00 34.70           C  
ANISOU 2321  CD  ARG C  92     4349   5159   3676   -458   -134     40       C  
ATOM   2322  NE  ARG C  92      -5.633  43.064   3.000  1.00 35.35           N  
ANISOU 2322  NE  ARG C  92     4466   5317   3647   -555   -607    167       N  
ATOM   2323  CZ  ARG C  92      -6.150  42.240   2.095  1.00 35.70           C  
ANISOU 2323  CZ  ARG C  92     4457   5399   3708   -695  -1121    260       C  
ATOM   2324  NH1 ARG C  92      -5.431  41.229   1.625  1.00 37.77           N  
ANISOU 2324  NH1 ARG C  92     4762   5633   3957   -590   -760     91       N  
ATOM   2325  NH2 ARG C  92      -7.386  42.431   1.654  1.00 32.58           N  
ANISOU 2325  NH2 ARG C  92     3793   5183   3402  -1178  -1888    482       N  
ATOM   2326  N   ARG C  93      -2.222  47.906   2.670  1.00 26.31           N  
ANISOU 2326  N   ARG C  93     2716   3939   3344   -527   1016   -392       N  
ATOM   2327  CA  ARG C  93      -1.787  48.695   1.527  1.00 29.66           C  
ANISOU 2327  CA  ARG C  93     3133   4366   3772   -600    943   -573       C  
ATOM   2328  C   ARG C  93      -0.947  47.800   0.633  1.00 30.35           C  
ANISOU 2328  C   ARG C  93     2981   4737   3812   -149   1006   -547       C  
ATOM   2329  O   ARG C  93      -0.039  47.115   1.114  1.00 32.60           O  
ANISOU 2329  O   ARG C  93     3642   4969   3776     21    945   -163       O  
ATOM   2330  CB  ARG C  93      -0.985  49.925   1.962  1.00 33.92           C  
ANISOU 2330  CB  ARG C  93     4133   4489   4267   -927    945   -559       C  
ATOM   2331  CG  ARG C  93      -1.834  51.054   2.523  1.00 38.74           C  
ANISOU 2331  CG  ARG C  93     4937   5131   4651  -1203    802   -321       C  
ATOM   2332  CD  ARG C  93      -0.976  52.243   2.921  1.00 41.18           C  
ANISOU 2332  CD  ARG C  93     5334   5412   4900  -1198    552   -182       C  
ATOM   2333  NE  ARG C  93      -0.039  52.617   1.866  1.00 42.71           N  
ANISOU 2333  NE  ARG C  93     5402   5625   5201  -1129    467    135       N  
ATOM   2334  CZ  ARG C  93      -0.331  53.435   0.859  1.00 44.62           C  
ANISOU 2334  CZ  ARG C  93     5621   5843   5490   -711    360    319       C  
ATOM   2335  NH1 ARG C  93      -1.541  53.969   0.763  1.00 44.91           N  
ANISOU 2335  NH1 ARG C  93     5596   5794   5674   -576    411    172       N  
ATOM   2336  NH2 ARG C  93       0.588  53.718  -0.055  1.00 45.19           N  
ANISOU 2336  NH2 ARG C  93     5734   5925   5512   -675    143    615       N  
ATOM   2337  N   ILE C  94      -1.263  47.786  -0.661  1.00 30.31           N  
ANISOU 2337  N   ILE C  94     2910   4722   3884    139   1162   -861       N  
ATOM   2338  CA  ILE C  94      -0.557  46.962  -1.633  1.00 33.72           C  
ANISOU 2338  CA  ILE C  94     3643   5071   4098     97   1172   -866       C  
ATOM   2339  C   ILE C  94      -0.285  47.796  -2.876  1.00 36.84           C  
ANISOU 2339  C   ILE C  94     4095   5585   4318     85   1271   -531       C  
ATOM   2340  O   ILE C  94      -0.830  48.886  -3.058  1.00 36.58           O  
ANISOU 2340  O   ILE C  94     3927   5587   4386    637   1440   -300       O  
ATOM   2341  CB  ILE C  94      -1.344  45.692  -2.021  1.00 34.53           C  
ANISOU 2341  CB  ILE C  94     3776   5052   4291    191    963  -1172       C  
ATOM   2342  CG1 ILE C  94      -2.625  46.075  -2.766  1.00 33.78           C  
ANISOU 2342  CG1 ILE C  94     3437   4997   4400    452    635  -1427       C  
ATOM   2343  CG2 ILE C  94      -1.645  44.840  -0.795  1.00 35.64           C  
ANISOU 2343  CG2 ILE C  94     4077   5027   4439    496    801  -1199       C  
ATOM   2344  CD1 ILE C  94      -3.271  44.921  -3.498  1.00 33.80           C  
ANISOU 2344  CD1 ILE C  94     3391   5009   4443    581    663  -1501       C  
ATOM   2345  N   ARG C  95       0.572  47.259  -3.738  1.00 39.31           N  
ANISOU 2345  N   ARG C  95     4332   6218   4388   -256   1335   -496       N  
ATOM   2346  CA  ARG C  95       0.795  47.817  -5.064  1.00 42.61           C  
ANISOU 2346  CA  ARG C  95     4635   6882   4672   -591   1273   -384       C  
ATOM   2347  C   ARG C  95      -0.098  47.074  -6.050  1.00 44.55           C  
ANISOU 2347  C   ARG C  95     4851   7279   4797   -856    973   -526       C  
ATOM   2348  O   ARG C  95       0.021  45.853  -6.203  1.00 44.36           O  
ANISOU 2348  O   ARG C  95     4842   7385   4628  -1179    496   -707       O  
ATOM   2349  CB  ARG C  95       2.264  47.701  -5.466  1.00 42.30           C  
ANISOU 2349  CB  ARG C  95     4223   7057   4792   -301   1426   -113       C  
ATOM   2350  CG  ARG C  95       2.615  48.441  -6.748  1.00 43.35           C  
ANISOU 2350  CG  ARG C  95     4315   7223   4935   -281   1517     43       C  
ATOM   2351  CD  ARG C  95       4.095  48.314  -7.080  1.00 42.69           C  
ANISOU 2351  CD  ARG C  95     4170   7140   4908   -559   1647     99       C  
ATOM   2352  NE  ARG C  95       4.940  48.568  -5.916  1.00 41.67           N  
ANISOU 2352  NE  ARG C  95     3961   6871   4998   -581   1469    321       N  
ATOM   2353  CZ  ARG C  95       5.249  49.779  -5.464  1.00 39.62           C  
ANISOU 2353  CZ  ARG C  95     3772   6371   4913   -333   1570    452       C  
ATOM   2354  NH1 ARG C  95       6.026  49.911  -4.397  1.00 38.93           N  
ANISOU 2354  NH1 ARG C  95     3694   6185   4913    132   1762    236       N  
ATOM   2355  NH2 ARG C  95       4.778  50.859  -6.072  1.00 37.80           N  
ANISOU 2355  NH2 ARG C  95     3495   6112   4754   -371   1538   1007       N  
ATOM   2356  N   GLY C  96      -0.996  47.803  -6.703  1.00 47.04           N  
ANISOU 2356  N   GLY C  96     5125   7568   5182   -620   1064   -483       N  
ATOM   2357  CA  GLY C  96      -1.923  47.188  -7.628  1.00 51.26           C  
ANISOU 2357  CA  GLY C  96     5958   7902   5616   -509    841   -444       C  
ATOM   2358  C   GLY C  96      -1.234  46.635  -8.861  1.00 55.06           C  
ANISOU 2358  C   GLY C  96     6681   8177   6063   -475    370   -361       C  
ATOM   2359  O   GLY C  96      -0.054  46.872  -9.124  1.00 56.04           O  
ANISOU 2359  O   GLY C  96     7010   8195   6087   -427    297   -273       O  
ATOM   2360  N   GLY C  97      -2.006  45.868  -9.635  1.00 57.68           N  
ANISOU 2360  N   GLY C  97     6986   8431   6498   -512     91   -282       N  
ATOM   2361  CA  GLY C  97      -1.502  45.321 -10.882  1.00 60.25           C  
ANISOU 2361  CA  GLY C  97     7411   8585   6895   -465    -11   -215       C  
ATOM   2362  C   GLY C  97      -1.036  46.374 -11.864  1.00 62.90           C  
ANISOU 2362  C   GLY C  97     7861   8778   7261   -281     -4   -142       C  
ATOM   2363  O   GLY C  97      -0.191  46.085 -12.719  1.00 63.48           O  
ANISOU 2363  O   GLY C  97     7948   8880   7293   -153    -25   -102       O  
ATOM   2364  N   ASP C  98      -1.566  47.592 -11.762  1.00 64.54           N  
ANISOU 2364  N   ASP C  98     8121   8831   7572   -154     68    -87       N  
ATOM   2365  CA  ASP C  98      -1.109  48.713 -12.571  1.00 66.61           C  
ANISOU 2365  CA  ASP C  98     8414   9038   7856     14    233     57       C  
ATOM   2366  C   ASP C  98       0.158  49.358 -12.025  1.00 66.36           C  
ANISOU 2366  C   ASP C  98     8318   9074   7823   -165    531    147       C  
ATOM   2367  O   ASP C  98       0.643  50.329 -12.616  1.00 67.29           O  
ANISOU 2367  O   ASP C  98     8436   9290   7842   -278    633    361       O  
ATOM   2368  CB  ASP C  98      -2.214  49.767 -12.679  1.00 68.85           C  
ANISOU 2368  CB  ASP C  98     8775   9264   8123    411    147    171       C  
ATOM   2369  CG  ASP C  98      -2.616  50.328 -11.328  1.00 70.83           C  
ANISOU 2369  CG  ASP C  98     9156   9426   8329    750    119    356       C  
ATOM   2370  OD1 ASP C  98      -2.603  49.566 -10.337  1.00 71.63           O  
ANISOU 2370  OD1 ASP C  98     9266   9520   8430    871    105    379       O  
ATOM   2371  OD2 ASP C  98      -2.943  51.532 -11.255  1.00 71.20           O  
ANISOU 2371  OD2 ASP C  98     9348   9350   8354    827    132    470       O  
ATOM   2372  N   GLY C  99       0.697  48.854 -10.918  1.00 64.85           N  
ANISOU 2372  N   GLY C  99     8066   8825   7749   -154    691     -4       N  
ATOM   2373  CA  GLY C  99       1.910  49.402 -10.346  1.00 63.93           C  
ANISOU 2373  CA  GLY C  99     7965   8671   7654    -23    941    -91       C  
ATOM   2374  C   GLY C  99       1.703  50.713  -9.617  1.00 62.72           C  
ANISOU 2374  C   GLY C  99     7808   8523   7498    -56   1221   -129       C  
ATOM   2375  O   GLY C  99       2.435  51.680  -9.849  1.00 64.00           O  
ANISOU 2375  O   GLY C  99     7924   8671   7722   -247   1216   -294       O  
ATOM   2376  N   LYS C 100       0.701  50.766  -8.741  1.00 59.21           N  
ANISOU 2376  N   LYS C 100     7301   8186   7011    255   1465     81       N  
ATOM   2377  CA  LYS C 100       0.434  51.942  -7.925  1.00 54.61           C  
ANISOU 2377  CA  LYS C 100     6551   7587   6610    507   1623    345       C  
ATOM   2378  C   LYS C 100      -0.008  51.490  -6.542  1.00 48.47           C  
ANISOU 2378  C   LYS C 100     5378   7102   5935    599   2209    576       C  
ATOM   2379  O   LYS C 100      -0.760  50.520  -6.411  1.00 45.27           O  
ANISOU 2379  O   LYS C 100     4658   7034   5507    230   2790    624       O  
ATOM   2380  CB  LYS C 100      -0.642  52.843  -8.554  1.00 56.16           C  
ANISOU 2380  CB  LYS C 100     7005   7455   6880    329   1330    396       C  
ATOM   2381  CG  LYS C 100      -0.296  53.369  -9.943  1.00 57.31           C  
ANISOU 2381  CG  LYS C 100     7191   7439   7145    179    978    312       C  
ATOM   2382  CD  LYS C 100      -1.381  54.287 -10.483  1.00 57.95           C  
ANISOU 2382  CD  LYS C 100     7228   7456   7334    117    753    196       C  
ATOM   2383  CE  LYS C 100      -1.381  55.628  -9.768  1.00 58.97           C  
ANISOU 2383  CE  LYS C 100     7317   7591   7499    -62    685    143       C  
ATOM   2384  NZ  LYS C 100      -0.127  56.391 -10.022  1.00 59.24           N  
ANISOU 2384  NZ  LYS C 100     7325   7608   7574   -193    651    178       N  
ATOM   2385  N   MET C 101       0.467  52.189  -5.513  1.00 46.29           N  
ANISOU 2385  N   MET C 101     5067   6657   5863    736   2133    790       N  
ATOM   2386  CA  MET C 101       0.105  51.843  -4.145  1.00 44.37           C  
ANISOU 2386  CA  MET C 101     4722   6323   5812    757   1850    992       C  
ATOM   2387  C   MET C 101      -1.333  52.261  -3.859  1.00 45.17           C  
ANISOU 2387  C   MET C 101     5076   6253   5834    333   2043   1235       C  
ATOM   2388  O   MET C 101      -1.746  53.376  -4.191  1.00 46.47           O  
ANISOU 2388  O   MET C 101     5365   6232   6060    625   1994   1403       O  
ATOM   2389  CB  MET C 101       1.059  52.509  -3.154  1.00 41.62           C  
ANISOU 2389  CB  MET C 101     4100   6036   5679   1057   1457   1101       C  
ATOM   2390  CG  MET C 101       2.495  52.007  -3.228  1.00 38.24           C  
ANISOU 2390  CG  MET C 101     3294   5800   5435    835   1261   1472       C  
ATOM   2391  SD  MET C 101       2.666  50.252  -2.835  1.00 34.87           S  
ANISOU 2391  SD  MET C 101     2527   5657   5067    530    858   1925       S  
ATOM   2392  CE  MET C 101       2.123  50.220  -1.127  1.00 33.92           C  
ANISOU 2392  CE  MET C 101     2513   5400   4974    900    939   1786       C  
ATOM   2393  N   LYS C 102      -2.094  51.362  -3.238  1.00 43.24           N  
ANISOU 2393  N   LYS C 102     4898   6106   5425   -406   2355   1446       N  
ATOM   2394  CA  LYS C 102      -3.500  51.599  -2.951  1.00 42.21           C  
ANISOU 2394  CA  LYS C 102     4745   6013   5280   -499   1941   1194       C  
ATOM   2395  C   LYS C 102      -3.846  51.019  -1.588  1.00 37.60           C  
ANISOU 2395  C   LYS C 102     3749   5357   5181   -975   1864   1156       C  
ATOM   2396  O   LYS C 102      -3.245  50.038  -1.142  1.00 35.58           O  
ANISOU 2396  O   LYS C 102     3289   5000   5228  -1494   1419   1102       O  
ATOM   2397  CB  LYS C 102      -4.407  50.978  -4.024  1.00 43.61           C  
ANISOU 2397  CB  LYS C 102     5220   6252   5098   -180   1770    886       C  
ATOM   2398  CG  LYS C 102      -4.241  49.471  -4.164  1.00 44.74           C  
ANISOU 2398  CG  LYS C 102     5410   6592   4999   -463   1839    795       C  
ATOM   2399  CD  LYS C 102      -5.046  48.910  -5.327  1.00 44.96           C  
ANISOU 2399  CD  LYS C 102     5303   6872   4907   -482   1912    803       C  
ATOM   2400  CE  LYS C 102      -6.540  48.976  -5.062  1.00 45.46           C  
ANISOU 2400  CE  LYS C 102     5413   7034   4826   -420   2063    852       C  
ATOM   2401  NZ  LYS C 102      -7.316  48.261  -6.115  1.00 45.87           N  
ANISOU 2401  NZ  LYS C 102     5518   7138   4774   -402   2131    780       N  
ATOM   2402  N   ASP C 103      -4.819  51.640  -0.927  1.00 35.68           N  
ANISOU 2402  N   ASP C 103     3791   4921   4844   -177   1664    529       N  
ATOM   2403  CA  ASP C 103      -5.372  51.108   0.310  1.00 34.50           C  
ANISOU 2403  CA  ASP C 103     4031   4580   4497     78   1220    -72       C  
ATOM   2404  C   ASP C 103      -6.527  50.172  -0.021  1.00 27.61           C  
ANISOU 2404  C   ASP C 103     3207   3650   3633   -106   1198   -197       C  
ATOM   2405  O   ASP C 103      -7.439  50.542  -0.765  1.00 28.23           O  
ANISOU 2405  O   ASP C 103     3393   3682   3652   -236    846   -116       O  
ATOM   2406  CB  ASP C 103      -5.845  52.235   1.228  1.00 41.27           C  
ANISOU 2406  CB  ASP C 103     5181   5383   5117     -1    800   -143       C  
ATOM   2407  CG  ASP C 103      -4.696  52.989   1.867  1.00 46.90           C  
ANISOU 2407  CG  ASP C 103     6179   6052   5591   -157    679    108       C  
ATOM   2408  OD1 ASP C 103      -3.909  53.616   1.126  1.00 49.61           O  
ANISOU 2408  OD1 ASP C 103     6631   6393   5826   -150    860    198       O  
ATOM   2409  OD2 ASP C 103      -4.580  52.956   3.111  1.00 48.87           O  
ANISOU 2409  OD2 ASP C 103     6562   6244   5761   -199    459    234       O  
ATOM   2410  N   LEU C 104      -6.479  48.962   0.523  1.00 21.98           N  
ANISOU 2410  N   LEU C 104     2578   2825   2949   -542   1156   -483       N  
ATOM   2411  CA  LEU C 104      -7.541  48.000   0.287  1.00 20.04           C  
ANISOU 2411  CA  LEU C 104     2416   2613   2587   -413    755   -668       C  
ATOM   2412  C   LEU C 104      -8.692  48.225   1.266  1.00 17.87           C  
ANISOU 2412  C   LEU C 104     1859   2393   2539   -717    746   -538       C  
ATOM   2413  O   LEU C 104      -8.577  48.967   2.245  1.00 16.86           O  
ANISOU 2413  O   LEU C 104     1525   2405   2476   -819    761   -447       O  
ATOM   2414  CB  LEU C 104      -7.004  46.574   0.400  1.00 19.08           C  
ANISOU 2414  CB  LEU C 104     2361   2484   2405    -97    696   -975       C  
ATOM   2415  CG  LEU C 104      -5.910  46.202  -0.602  1.00 18.98           C  
ANISOU 2415  CG  LEU C 104     2178   2578   2456     86   1091   -849       C  
ATOM   2416  CD1 LEU C 104      -5.393  44.794  -0.342  1.00 21.31           C  
ANISOU 2416  CD1 LEU C 104     2478   2953   2667     67   1071   -733       C  
ATOM   2417  CD2 LEU C 104      -6.431  46.330  -2.023  1.00 19.35           C  
ANISOU 2417  CD2 LEU C 104     2072   2874   2405     72   1122   -762       C  
ATOM   2418  N   SER C 105      -9.816  47.575   0.984  1.00 18.58           N  
ANISOU 2418  N   SER C 105     1802   2764   2494   -804    813   -339       N  
ATOM   2419  CA  SER C 105     -10.974  47.675   1.861  1.00 19.29           C  
ANISOU 2419  CA  SER C 105     2185   2872   2271   -468    607   -156       C  
ATOM   2420  C   SER C 105     -10.607  47.176   3.255  1.00 17.11           C  
ANISOU 2420  C   SER C 105     2224   2350   1925   -279    732     24       C  
ATOM   2421  O   SER C 105     -10.021  46.093   3.385  1.00 15.87           O  
ANISOU 2421  O   SER C 105     2011   2185   1834     51    833     44       O  
ATOM   2422  CB  SER C 105     -12.145  46.866   1.303  1.00 20.02           C  
ANISOU 2422  CB  SER C 105     1959   3464   2183   -917    348    270       C  
ATOM   2423  OG  SER C 105     -12.529  47.335   0.021  1.00 23.65           O  
ANISOU 2423  OG  SER C 105     2318   4230   2438   -843    205    -42       O  
ATOM   2424  N   PRO C 106     -10.910  47.932   4.310  1.00 16.98           N  
ANISOU 2424  N   PRO C 106     2431   2172   1850   -436    544     98       N  
ATOM   2425  CA  PRO C 106     -10.559  47.482   5.661  1.00 17.00           C  
ANISOU 2425  CA  PRO C 106     2453   2163   1844   -391    472    -25       C  
ATOM   2426  C   PRO C 106     -11.261  46.180   6.014  1.00 16.93           C  
ANISOU 2426  C   PRO C 106     2438   2174   1820    106    529   -187       C  
ATOM   2427  O   PRO C 106     -12.355  45.883   5.527  1.00 17.61           O  
ANISOU 2427  O   PRO C 106     2566   2378   1745    181    401   -326       O  
ATOM   2428  CB  PRO C 106     -11.036  48.633   6.556  1.00 16.43           C  
ANISOU 2428  CB  PRO C 106     2545   1949   1750   -402      4    158       C  
ATOM   2429  CG  PRO C 106     -11.110  49.819   5.650  1.00 17.53           C  
ANISOU 2429  CG  PRO C 106     2713   2159   1787   -602    244    312       C  
ATOM   2430  CD  PRO C 106     -11.510  49.277   4.311  1.00 16.66           C  
ANISOU 2430  CD  PRO C 106     2453   2117   1761   -648    268     96       C  
ATOM   2431  N   ARG C 107     -10.611  45.397   6.870  1.00 14.93           N  
ANISOU 2431  N   ARG C 107     1950   2115   1608   -417    602   -155       N  
ATOM   2432  CA  ARG C 107     -11.163  44.148   7.370  1.00 15.80           C  
ANISOU 2432  CA  ARG C 107     1876   2465   1664   -564    653   -122       C  
ATOM   2433  C   ARG C 107     -11.282  44.223   8.884  1.00 15.47           C  
ANISOU 2433  C   ARG C 107     1712   2565   1600   -635    522   -219       C  
ATOM   2434  O   ARG C 107     -10.402  44.765   9.559  1.00 19.56           O  
ANISOU 2434  O   ARG C 107     2093   3363   1977  -1222    344   -231       O  
ATOM   2435  CB  ARG C 107     -10.296  42.952   6.961  1.00 16.41           C  
ANISOU 2435  CB  ARG C 107     1893   2356   1987   -636    474    -83       C  
ATOM   2436  CG  ARG C 107     -10.273  42.709   5.459  1.00 19.41           C  
ANISOU 2436  CG  ARG C 107     2045   2868   2461   -402    695    210       C  
ATOM   2437  CD  ARG C 107      -9.563  41.414   5.087  1.00 22.46           C  
ANISOU 2437  CD  ARG C 107     2151   3315   3067    169    626    457       C  
ATOM   2438  NE  ARG C 107      -8.132  41.453   5.370  1.00 27.67           N  
ANISOU 2438  NE  ARG C 107     3185   3937   3390    741    695    352       N  
ATOM   2439  CZ  ARG C 107      -7.260  40.557   4.918  1.00 31.50           C  
ANISOU 2439  CZ  ARG C 107     3704   4629   3636    344    966    195       C  
ATOM   2440  NH1 ARG C 107      -7.671  39.555   4.152  1.00 31.53           N  
ANISOU 2440  NH1 ARG C 107     3737   4629   3615    102   1042   -281       N  
ATOM   2441  NH2 ARG C 107      -5.975  40.663   5.226  1.00 33.35           N  
ANISOU 2441  NH2 ARG C 107     3942   4988   3740    555    930    336       N  
ATOM   2442  N   TRP C 108     -12.378  43.683   9.410  1.00 10.94           N  
ANISOU 2442  N   TRP C 108     1264   1707   1185   -285    682    -32       N  
ATOM   2443  CA  TRP C 108     -12.664  43.704  10.840  1.00  9.41           C  
ANISOU 2443  CA  TRP C 108     1064   1512   1000   -139    565   -251       C  
ATOM   2444  C   TRP C 108     -12.654  42.273  11.359  1.00 10.04           C  
ANISOU 2444  C   TRP C 108     1129   1552   1135   -107    174    -79       C  
ATOM   2445  O   TRP C 108     -13.394  41.422  10.853  1.00 12.74           O  
ANISOU 2445  O   TRP C 108     1996   1507   1339   -294    -73    -74       O  
ATOM   2446  CB  TRP C 108     -14.011  44.373  11.117  1.00  8.49           C  
ANISOU 2446  CB  TRP C 108     1111    770   1344    137     84   -167       C  
ATOM   2447  CG  TRP C 108     -14.069  45.829  10.743  1.00 10.41           C  
ANISOU 2447  CG  TRP C 108     1390   1105   1459   -235   -172   -194       C  
ATOM   2448  CD1 TRP C 108     -14.157  46.351   9.484  1.00 11.55           C  
ANISOU 2448  CD1 TRP C 108     1764    909   1716   -446   -257   -109       C  
ATOM   2449  CD2 TRP C 108     -14.062  46.946  11.641  1.00 11.41           C  
ANISOU 2449  CD2 TRP C 108     1405   1323   1610   -623   -106   -221       C  
ATOM   2450  NE1 TRP C 108     -14.196  47.727   9.543  1.00 12.76           N  
ANISOU 2450  NE1 TRP C 108     1596   1522   1730   -534   -431   -313       N  
ATOM   2451  CE2 TRP C 108     -14.141  48.115  10.855  1.00 12.47           C  
ANISOU 2451  CE2 TRP C 108     1534   1505   1698   -695     -7   -612       C  
ATOM   2452  CE3 TRP C 108     -13.993  47.071  13.032  1.00 11.97           C  
ANISOU 2452  CE3 TRP C 108     1523   1451   1573   -640   -223   -528       C  
ATOM   2453  CZ2 TRP C 108     -14.153  49.391  11.415  1.00 14.45           C  
ANISOU 2453  CZ2 TRP C 108     1851   2000   1641   -615   -133   -739       C  
ATOM   2454  CZ3 TRP C 108     -14.006  48.340  13.586  1.00 14.20           C  
ANISOU 2454  CZ3 TRP C 108     1797   1823   1775   -564   -136   -159       C  
ATOM   2455  CH2 TRP C 108     -14.085  49.482  12.780  1.00 13.81           C  
ANISOU 2455  CH2 TRP C 108     1861   1770   1616   -200    -22    -40       C  
ATOM   2456  N   TYR C 109     -11.819  42.012  12.364  1.00  9.82           N  
ANISOU 2456  N   TYR C 109     1015   1767    950    -62     -4   -270       N  
ATOM   2457  CA  TYR C 109     -11.630  40.680  12.924  1.00  9.90           C  
ANISOU 2457  CA  TYR C 109      905   1688   1168    -33    419     -8       C  
ATOM   2458  C   TYR C 109     -12.183  40.618  14.341  1.00 11.36           C  
ANISOU 2458  C   TYR C 109     1218   1881   1217      9    299   -196       C  
ATOM   2459  O   TYR C 109     -11.941  41.522  15.149  1.00 12.73           O  
ANISOU 2459  O   TYR C 109     1369   2158   1310   -713    232   -197       O  
ATOM   2460  CB  TYR C 109     -10.147  40.296  12.954  1.00 10.46           C  
ANISOU 2460  CB  TYR C 109     1045   1745   1183    469    424   -193       C  
ATOM   2461  CG  TYR C 109      -9.497  40.115  11.605  1.00 12.46           C  
ANISOU 2461  CG  TYR C 109     1569   1978   1187   -237    131   -167       C  
ATOM   2462  CD1 TYR C 109      -8.925  41.190  10.936  1.00 16.23           C  
ANISOU 2462  CD1 TYR C 109     2361   2479   1329   -544    -30   -222       C  
ATOM   2463  CD2 TYR C 109      -9.430  38.862  11.009  1.00 15.50           C  
ANISOU 2463  CD2 TYR C 109     2172   2491   1226   -296    212    -15       C  
ATOM   2464  CE1 TYR C 109      -8.316  41.024   9.707  1.00 17.38           C  
ANISOU 2464  CE1 TYR C 109     2174   2920   1510   -601    328    150       C  
ATOM   2465  CE2 TYR C 109      -8.823  38.686   9.782  1.00 18.60           C  
ANISOU 2465  CE2 TYR C 109     2546   3023   1498   -305    532     27       C  
ATOM   2466  CZ  TYR C 109      -8.269  39.771   9.135  1.00 18.67           C  
ANISOU 2466  CZ  TYR C 109     2292   3213   1589   -473    579     67       C  
ATOM   2467  OH  TYR C 109      -7.666  39.594   7.911  1.00 22.00           O  
ANISOU 2467  OH  TYR C 109     2405   3864   2090   -570   1017    104       O  
ATOM   2468  N   PHE C 110     -12.898  39.537  14.653  1.00  9.72           N  
ANISOU 2468  N   PHE C 110     1102   1500   1089   -174    466   -347       N  
ATOM   2469  CA  PHE C 110     -13.484  39.369  15.978  1.00 10.03           C  
ANISOU 2469  CA  PHE C 110      855   1663   1294     52    363    -45       C  
ATOM   2470  C   PHE C 110     -12.530  38.651  16.925  1.00  9.99           C  
ANISOU 2470  C   PHE C 110     1334   1415   1046    103    -48   -127       C  
ATOM   2471  O   PHE C 110     -11.887  37.662  16.557  1.00  9.52           O  
ANISOU 2471  O   PHE C 110     1193   1364   1061    650   -289   -174       O  
ATOM   2472  CB  PHE C 110     -14.802  38.593  15.909  1.00  9.24           C  
ANISOU 2472  CB  PHE C 110      925   1272   1314    185    432    220       C  
ATOM   2473  CG  PHE C 110     -15.401  38.305  17.264  1.00  7.80           C  
ANISOU 2473  CG  PHE C 110      734   1066   1165   -189    448    110       C  
ATOM   2474  CD1 PHE C 110     -16.166  39.260  17.914  1.00  7.40           C  
ANISOU 2474  CD1 PHE C 110      655   1049   1109   -363    288     88       C  
ATOM   2475  CD2 PHE C 110     -15.186  37.086  17.890  1.00  7.59           C  
ANISOU 2475  CD2 PHE C 110      698   1177   1008     81    225     58       C  
ATOM   2476  CE1 PHE C 110     -16.713  39.004  19.162  1.00  6.57           C  
ANISOU 2476  CE1 PHE C 110      665    901    930   -423     11    184       C  
ATOM   2477  CE2 PHE C 110     -15.726  36.823  19.140  1.00  8.21           C  
ANISOU 2477  CE2 PHE C 110     1036   1038   1046   -234    155   -483       C  
ATOM   2478  CZ  PHE C 110     -16.492  37.783  19.775  1.00  6.22           C  
ANISOU 2478  CZ  PHE C 110      666    568   1128   -260    195   -165       C  
ATOM   2479  N   TYR C 111     -12.465  39.151  18.157  1.00  8.05           N  
ANISOU 2479  N   TYR C 111      904   1215    938    -33   -416      0       N  
ATOM   2480  CA  TYR C 111     -11.741  38.516  19.248  1.00  9.80           C  
ANISOU 2480  CA  TYR C 111      981   1634   1108   -140    -81   -129       C  
ATOM   2481  C   TYR C 111     -12.641  38.462  20.470  1.00  9.86           C  
ANISOU 2481  C   TYR C 111     1017   1535   1193   -102   -156    178       C  
ATOM   2482  O   TYR C 111     -13.312  39.445  20.797  1.00  8.79           O  
ANISOU 2482  O   TYR C 111      718   1539   1082    147     60   -227       O  
ATOM   2483  CB  TYR C 111     -10.460  39.280  19.601  1.00 10.22           C  
ANISOU 2483  CB  TYR C 111      593   2182   1110   -187     16   -301       C  
ATOM   2484  CG  TYR C 111      -9.415  39.277  18.515  1.00 12.56           C  
ANISOU 2484  CG  TYR C 111      859   2532   1381   -274    339   -458       C  
ATOM   2485  CD1 TYR C 111      -8.452  38.280  18.458  1.00 14.38           C  
ANISOU 2485  CD1 TYR C 111     1064   2853   1547   -228    230   -788       C  
ATOM   2486  CD2 TYR C 111      -9.391  40.272  17.546  1.00 12.70           C  
ANISOU 2486  CD2 TYR C 111      982   2460   1383   -407    249   -551       C  
ATOM   2487  CE1 TYR C 111      -7.490  38.272  17.466  1.00 16.08           C  
ANISOU 2487  CE1 TYR C 111     1398   3069   1642   -297    586   -771       C  
ATOM   2488  CE2 TYR C 111      -8.435  40.272  16.548  1.00 13.74           C  
ANISOU 2488  CE2 TYR C 111     1084   2627   1511   -653    394   -461       C  
ATOM   2489  CZ  TYR C 111      -7.486  39.270  16.514  1.00 16.28           C  
ANISOU 2489  CZ  TYR C 111     1451   3135   1600   -424    565   -624       C  
ATOM   2490  OH  TYR C 111      -6.530  39.266  15.524  1.00 17.71           O  
ANISOU 2490  OH  TYR C 111     1411   3609   1711   -407    554   -655       O  
ATOM   2491  N   TYR C 112     -12.651  37.316  21.145  1.00  7.83           N  
ANISOU 2491  N   TYR C 112      664   1359    953     76    -14    284       N  
ATOM   2492  CA  TYR C 112     -13.386  37.214  22.395  1.00  7.70           C  
ANISOU 2492  CA  TYR C 112      864   1056   1007     44   -104    -82       C  
ATOM   2493  C   TYR C 112     -12.792  38.156  23.437  1.00  9.86           C  
ANISOU 2493  C   TYR C 112     1115   1596   1037   -157   -126   -239       C  
ATOM   2494  O   TYR C 112     -11.593  38.451  23.430  1.00 10.14           O  
ANISOU 2494  O   TYR C 112      911   1892   1051    -68   -149   -380       O  
ATOM   2495  CB  TYR C 112     -13.376  35.774  22.903  1.00  7.54           C  
ANISOU 2495  CB  TYR C 112      703    984   1177    290     95   -423       C  
ATOM   2496  CG  TYR C 112     -14.275  34.866  22.099  1.00  7.23           C  
ANISOU 2496  CG  TYR C 112      692    965   1091   -192    -21   -432       C  
ATOM   2497  CD1 TYR C 112     -15.645  34.846  22.322  1.00  8.21           C  
ANISOU 2497  CD1 TYR C 112     1041    917   1160   -570    123   -128       C  
ATOM   2498  CD2 TYR C 112     -13.760  34.044  21.105  1.00  6.39           C  
ANISOU 2498  CD2 TYR C 112      681    672   1074     42   -270   -373       C  
ATOM   2499  CE1 TYR C 112     -16.477  34.024  21.586  1.00  8.13           C  
ANISOU 2499  CE1 TYR C 112     1221    768   1100   -448   -146   -255       C  
ATOM   2500  CE2 TYR C 112     -14.584  33.218  20.363  1.00  8.78           C  
ANISOU 2500  CE2 TYR C 112     1033   1152   1151    236   -274    -94       C  
ATOM   2501  CZ  TYR C 112     -15.941  33.213  20.609  1.00  9.17           C  
ANISOU 2501  CZ  TYR C 112     1500    758   1226   -112   -225   -298       C  
ATOM   2502  OH  TYR C 112     -16.767  32.395  19.876  1.00  9.44           O  
ANISOU 2502  OH  TYR C 112     1674    642   1272    -81   -365   -309       O  
ATOM   2503  N   LEU C 113     -13.660  38.647  24.321  1.00  8.87           N  
ANISOU 2503  N   LEU C 113      975   1300   1095    -31   -266   -498       N  
ATOM   2504  CA  LEU C 113     -13.250  39.563  25.379  1.00  8.69           C  
ANISOU 2504  CA  LEU C 113     1012   1212   1079   -110   -263   -579       C  
ATOM   2505  C   LEU C 113     -12.066  39.005  26.158  1.00 11.33           C  
ANISOU 2505  C   LEU C 113     1093   1899   1313   -389   -351   -500       C  
ATOM   2506  O   LEU C 113     -12.055  37.833  26.547  1.00  9.87           O  
ANISOU 2506  O   LEU C 113      602   1829   1319     99   -268   -362       O  
ATOM   2507  CB  LEU C 113     -14.427  39.821  26.321  1.00  9.33           C  
ANISOU 2507  CB  LEU C 113     1291   1161   1092   -313    -31   -540       C  
ATOM   2508  CG  LEU C 113     -14.185  40.735  27.524  1.00  9.51           C  
ANISOU 2508  CG  LEU C 113     1293    994   1328   -609      0   -280       C  
ATOM   2509  CD1 LEU C 113     -13.869  42.156  27.072  1.00 10.22           C  
ANISOU 2509  CD1 LEU C 113     1153   1079   1651   -641     81   -163       C  
ATOM   2510  CD2 LEU C 113     -15.392  40.716  28.446  1.00 14.22           C  
ANISOU 2510  CD2 LEU C 113     2529   1573   1300   -661    129   -416       C  
ATOM   2511  N   GLY C 114     -11.059  39.849  26.368  1.00 12.34           N  
ANISOU 2511  N   GLY C 114     1476   1942   1269   -442    -56   -596       N  
ATOM   2512  CA  GLY C 114      -9.882  39.450  27.109  1.00 12.18           C  
ANISOU 2512  CA  GLY C 114     1008   2291   1330   -154   -223   -158       C  
ATOM   2513  C   GLY C 114      -8.875  38.633  26.335  1.00 13.71           C  
ANISOU 2513  C   GLY C 114      997   2807   1407    254   -128    -55       C  
ATOM   2514  O   GLY C 114      -7.953  38.081  26.947  1.00 17.77           O  
ANISOU 2514  O   GLY C 114     2030   3429   1292    386   -268   -271       O  
ATOM   2515  N   THR C 115      -9.022  38.529  25.015  1.00 13.33           N  
ANISOU 2515  N   THR C 115      824   2795   1445     44    -71   -224       N  
ATOM   2516  CA  THR C 115      -8.069  37.837  24.159  1.00 14.07           C  
ANISOU 2516  CA  THR C 115     1409   2445   1491    123   -181   -384       C  
ATOM   2517  C   THR C 115      -7.608  38.781  23.056  1.00 14.98           C  
ANISOU 2517  C   THR C 115     1510   2569   1614   -156   -155   -656       C  
ATOM   2518  O   THR C 115      -8.197  39.840  22.826  1.00 14.69           O  
ANISOU 2518  O   THR C 115     1585   2284   1712   -463   -235   -563       O  
ATOM   2519  CB  THR C 115      -8.674  36.571  23.533  1.00 13.47           C  
ANISOU 2519  CB  THR C 115     1711   2146   1262    397   -495   -233       C  
ATOM   2520  OG1 THR C 115      -9.566  36.941  22.472  1.00 12.86           O  
ANISOU 2520  OG1 THR C 115     1633   1825   1426    349   -162   -265       O  
ATOM   2521  CG2 THR C 115      -9.439  35.764  24.572  1.00 13.33           C  
ANISOU 2521  CG2 THR C 115     1904   1968   1192    264     50   -325       C  
ATOM   2522  N   GLY C 116      -6.536  38.388  22.372  1.00 14.59           N  
ANISOU 2522  N   GLY C 116      947   2802   1793   -125    130   -768       N  
ATOM   2523  CA  GLY C 116      -6.115  39.060  21.165  1.00 16.74           C  
ANISOU 2523  CA  GLY C 116      978   3216   2168   -376     62   -746       C  
ATOM   2524  C   GLY C 116      -5.304  40.319  21.399  1.00 18.25           C  
ANISOU 2524  C   GLY C 116     1196   3493   2245   -579   -106   -764       C  
ATOM   2525  O   GLY C 116      -4.769  40.556  22.487  1.00 19.38           O  
ANISOU 2525  O   GLY C 116     1345   3816   2202   -681     26   -996       O  
ATOM   2526  N   PRO C 117      -5.201  41.155  20.361  1.00 18.29           N  
ANISOU 2526  N   PRO C 117     1350   3428   2171   -554   -285   -509       N  
ATOM   2527  CA  PRO C 117      -4.339  42.346  20.456  1.00 19.04           C  
ANISOU 2527  CA  PRO C 117     1566   3424   2246   -817   -344   -363       C  
ATOM   2528  C   PRO C 117      -4.789  43.344  21.505  1.00 20.08           C  
ANISOU 2528  C   PRO C 117     1711   3570   2348  -1143   -201   -455       C  
ATOM   2529  O   PRO C 117      -3.954  44.080  22.044  1.00 24.13           O  
ANISOU 2529  O   PRO C 117     2266   4341   2563  -1146    -10   -684       O  
ATOM   2530  CB  PRO C 117      -4.412  42.945  19.043  1.00 19.93           C  
ANISOU 2530  CB  PRO C 117     1763   3439   2369   -593   -127   -398       C  
ATOM   2531  CG  PRO C 117      -4.891  41.830  18.167  1.00 20.00           C  
ANISOU 2531  CG  PRO C 117     1738   3545   2315   -201   -118   -306       C  
ATOM   2532  CD  PRO C 117      -5.797  41.006  19.024  1.00 18.87           C  
ANISOU 2532  CD  PRO C 117     1382   3530   2256   -146    -83   -378       C  
ATOM   2533  N   GLU C 118      -6.083  43.404  21.806  1.00 20.20           N  
ANISOU 2533  N   GLU C 118     2111   3241   2323  -1062      0   -264       N  
ATOM   2534  CA  GLU C 118      -6.619  44.284  22.838  1.00 18.93           C  
ANISOU 2534  CA  GLU C 118     1713   3164   2316  -1111   -186   -559       C  
ATOM   2535  C   GLU C 118      -7.151  43.481  24.021  1.00 17.45           C  
ANISOU 2535  C   GLU C 118     1355   3150   2127   -780   -277   -540       C  
ATOM   2536  O   GLU C 118      -8.208  43.785  24.576  1.00 19.82           O  
ANISOU 2536  O   GLU C 118     1542   3555   2435   -770   -285   -695       O  
ATOM   2537  CB  GLU C 118      -7.708  45.188  22.266  1.00 20.74           C  
ANISOU 2537  CB  GLU C 118     2009   3228   2642   -901     82   -598       C  
ATOM   2538  CG  GLU C 118      -7.238  46.091  21.133  1.00 23.87           C  
ANISOU 2538  CG  GLU C 118     2213   3943   2913  -1209     82   -731       C  
ATOM   2539  CD  GLU C 118      -6.286  47.180  21.600  1.00 29.38           C  
ANISOU 2539  CD  GLU C 118     3134   4892   3137  -1372    443   -606       C  
ATOM   2540  OE1 GLU C 118      -6.230  47.452  22.818  1.00 31.13           O  
ANISOU 2540  OE1 GLU C 118     3468   5018   3342  -1900    116   -961       O  
ATOM   2541  OE2 GLU C 118      -5.593  47.767  20.744  1.00 31.99           O  
ANISOU 2541  OE2 GLU C 118     3406   5417   3331  -1284    939   -427       O  
ATOM   2542  N   ALA C 119      -6.411  42.440  24.415  1.00 14.56           N  
ANISOU 2542  N   ALA C 119     1026   2760   1747   -416   -371   -368       N  
ATOM   2543  CA  ALA C 119      -6.845  41.590  25.519  1.00 16.50           C  
ANISOU 2543  CA  ALA C 119     1521   3086   1662   -101   -283   -283       C  
ATOM   2544  C   ALA C 119      -6.935  42.363  26.828  1.00 18.93           C  
ANISOU 2544  C   ALA C 119     1974   3271   1947   -331   -417   -531       C  
ATOM   2545  O   ALA C 119      -7.745  42.019  27.697  1.00 19.84           O  
ANISOU 2545  O   ALA C 119     2252   3567   1719   -492   -297   -444       O  
ATOM   2546  CB  ALA C 119      -5.895  40.402  25.669  1.00 18.15           C  
ANISOU 2546  CB  ALA C 119     2396   2823   1678   -137   -150    -65       C  
ATOM   2547  N   GLY C 120      -6.118  43.400  26.992  1.00 20.19           N  
ANISOU 2547  N   GLY C 120     2244   3108   2319   -244   -352   -613       N  
ATOM   2548  CA  GLY C 120      -6.157  44.206  28.193  1.00 21.76           C  
ANISOU 2548  CA  GLY C 120     2585   3211   2472   -401   -141   -822       C  
ATOM   2549  C   GLY C 120      -7.198  45.298  28.203  1.00 23.79           C  
ANISOU 2549  C   GLY C 120     3259   3317   2462   -720    -75   -945       C  
ATOM   2550  O   GLY C 120      -7.340  46.002  29.206  1.00 26.19           O  
ANISOU 2550  O   GLY C 120     3809   3686   2456   -784    -91  -1074       O  
ATOM   2551  N   LEU C 121      -7.937  45.455  27.115  1.00 21.64           N  
ANISOU 2551  N   LEU C 121     2683   3238   2301   -989     25   -857       N  
ATOM   2552  CA  LEU C 121      -8.926  46.520  27.015  1.00 21.45           C  
ANISOU 2552  CA  LEU C 121     2403   3319   2428   -885    168   -839       C  
ATOM   2553  C   LEU C 121     -10.214  46.100  27.717  1.00 21.55           C  
ANISOU 2553  C   LEU C 121     2504   3255   2429   -926    474   -902       C  
ATOM   2554  O   LEU C 121     -10.756  45.033  27.415  1.00 22.68           O  
ANISOU 2554  O   LEU C 121     2839   3313   2466  -1192    606   -936       O  
ATOM   2555  CB  LEU C 121      -9.206  46.842  25.549  1.00 22.09           C  
ANISOU 2555  CB  LEU C 121     2661   3190   2541   -414   -520   -733       C  
ATOM   2556  CG  LEU C 121      -9.689  48.250  25.202  1.00 24.52           C  
ANISOU 2556  CG  LEU C 121     3211   3327   2780  -1351   -859   -341       C  
ATOM   2557  CD1 LEU C 121      -8.643  49.282  25.591  1.00 25.20           C  
ANISOU 2557  CD1 LEU C 121     3287   3348   2939  -1338  -1150   -411       C  
ATOM   2558  CD2 LEU C 121     -10.022  48.349  23.720  1.00 25.23           C  
ANISOU 2558  CD2 LEU C 121     3575   3235   2776  -1521   -610     37       C  
ATOM   2559  N   PRO C 122     -10.723  46.895  28.656  1.00 19.08           N  
ANISOU 2559  N   PRO C 122     1888   3045   2316   -654    485   -792       N  
ATOM   2560  CA  PRO C 122     -11.996  46.550  29.295  1.00 17.57           C  
ANISOU 2560  CA  PRO C 122     1801   2809   2066   -430    318   -800       C  
ATOM   2561  C   PRO C 122     -13.142  46.646  28.304  1.00 15.91           C  
ANISOU 2561  C   PRO C 122     1693   2566   1788   -552    326   -837       C  
ATOM   2562  O   PRO C 122     -13.109  47.438  27.359  1.00 17.03           O  
ANISOU 2562  O   PRO C 122     2024   2550   1897   -680    109   -571       O  
ATOM   2563  CB  PRO C 122     -12.138  47.598  30.407  1.00 16.88           C  
ANISOU 2563  CB  PRO C 122     1575   2836   2003   -330    194  -1068       C  
ATOM   2564  CG  PRO C 122     -10.775  48.207  30.557  1.00 19.21           C  
ANISOU 2564  CG  PRO C 122     1924   3077   2297   -361    345   -824       C  
ATOM   2565  CD  PRO C 122     -10.147  48.131  29.208  1.00 18.15           C  
ANISOU 2565  CD  PRO C 122     1893   2819   2185   -586    255  -1018       C  
ATOM   2566  N   TYR C 123     -14.163  45.822  28.529  1.00 14.79           N  
ANISOU 2566  N   TYR C 123     1737   2061   1821   -948     54   -659       N  
ATOM   2567  CA  TYR C 123     -15.336  45.834  27.666  1.00 15.17           C  
ANISOU 2567  CA  TYR C 123     2120   1685   1958   -882    -66   -641       C  
ATOM   2568  C   TYR C 123     -15.948  47.227  27.612  1.00 13.78           C  
ANISOU 2568  C   TYR C 123     1874   1563   1798   -356    102   -479       C  
ATOM   2569  O   TYR C 123     -16.143  47.876  28.643  1.00 14.41           O  
ANISOU 2569  O   TYR C 123     1843   1826   1806   -588     89   -352       O  
ATOM   2570  CB  TYR C 123     -16.376  44.829  28.159  1.00 15.00           C  
ANISOU 2570  CB  TYR C 123     1932   1520   2246   -785   -274   -584       C  
ATOM   2571  CG  TYR C 123     -17.645  44.849  27.337  1.00 19.79           C  
ANISOU 2571  CG  TYR C 123     2596   1751   3173   -704   -292   -478       C  
ATOM   2572  CD1 TYR C 123     -17.669  44.309  26.058  1.00 21.35           C  
ANISOU 2572  CD1 TYR C 123     2795   2014   3305   -826   -156    -60       C  
ATOM   2573  CD2 TYR C 123     -18.814  45.413  27.833  1.00 22.36           C  
ANISOU 2573  CD2 TYR C 123     3052   1834   3608   -408   -745   -586       C  
ATOM   2574  CE1 TYR C 123     -18.820  44.328  25.295  1.00 23.64           C  
ANISOU 2574  CE1 TYR C 123     2908   2355   3719  -1029   -101    133       C  
ATOM   2575  CE2 TYR C 123     -19.973  45.435  27.075  1.00 25.21           C  
ANISOU 2575  CE2 TYR C 123     3384   2149   4046   -347   -815   -510       C  
ATOM   2576  CZ  TYR C 123     -19.967  44.891  25.807  1.00 26.73           C  
ANISOU 2576  CZ  TYR C 123     3386   2603   4166   -568   -751     34       C  
ATOM   2577  OH  TYR C 123     -21.110  44.905  25.042  1.00 31.07           O  
ANISOU 2577  OH  TYR C 123     4100   2825   4882   -589  -1025    355       O  
ATOM   2578  N   GLY C 124     -16.242  47.688  26.398  1.00 14.52           N  
ANISOU 2578  N   GLY C 124     2156   1711   1648   -147    353   -109       N  
ATOM   2579  CA  GLY C 124     -16.859  48.980  26.199  1.00 16.03           C  
ANISOU 2579  CA  GLY C 124     2446   1777   1869   -277    420   -521       C  
ATOM   2580  C   GLY C 124     -15.904  50.150  26.126  1.00 19.19           C  
ANISOU 2580  C   GLY C 124     2918   2193   2180   -346    410   -256       C  
ATOM   2581  O   GLY C 124     -16.359  51.283  25.917  1.00 22.68           O  
ANISOU 2581  O   GLY C 124     3439   2594   2586   -279    291    -15       O  
ATOM   2582  N   ALA C 125     -14.604  49.921  26.293  1.00 17.50           N  
ANISOU 2582  N   ALA C 125     2494   2119   2037   -488    -35   -272       N  
ATOM   2583  CA  ALA C 125     -13.641  51.012  26.236  1.00 19.77           C  
ANISOU 2583  CA  ALA C 125     2728   2489   2295   -696    -76   -298       C  
ATOM   2584  C   ALA C 125     -13.617  51.633  24.845  1.00 20.03           C  
ANISOU 2584  C   ALA C 125     3072   2210   2328  -1018    396   -283       C  
ATOM   2585  O   ALA C 125     -13.676  50.932  23.832  1.00 20.55           O  
ANISOU 2585  O   ALA C 125     3551   2254   2003   -977    183   -277       O  
ATOM   2586  CB  ALA C 125     -12.247  50.510  26.613  1.00 19.65           C  
ANISOU 2586  CB  ALA C 125     2363   2619   2485   -478   -384   -391       C  
ATOM   2587  N   ASN C 126     -13.532  52.960  24.802  1.00 21.90           N  
ANISOU 2587  N   ASN C 126     3489   2268   2562  -1095    716     -6       N  
ATOM   2588  CA  ASN C 126     -13.514  53.684  23.537  1.00 24.22           C  
ANISOU 2588  CA  ASN C 126     3919   2500   2785   -976    815   -220       C  
ATOM   2589  C   ASN C 126     -12.099  53.684  22.967  1.00 23.53           C  
ANISOU 2589  C   ASN C 126     3696   2572   2671  -1583    810   -316       C  
ATOM   2590  O   ASN C 126     -11.156  54.134  23.627  1.00 24.95           O  
ANISOU 2590  O   ASN C 126     3563   3202   2715  -1777    918   -373       O  
ATOM   2591  CB  ASN C 126     -14.019  55.112  23.734  1.00 28.04           C  
ANISOU 2591  CB  ASN C 126     4716   2631   3305   -596   1094   -300       C  
ATOM   2592  CG  ASN C 126     -14.240  55.839  22.420  1.00 35.40           C  
ANISOU 2592  CG  ASN C 126     5662   3518   4269   -760   1113   -536       C  
ATOM   2593  OD1 ASN C 126     -14.433  55.216  21.375  1.00 37.92           O  
ANISOU 2593  OD1 ASN C 126     5765   3975   4669  -1161   1179   -202       O  
ATOM   2594  ND2 ASN C 126     -14.215  57.167  22.468  1.00 39.66           N  
ANISOU 2594  ND2 ASN C 126     6267   4237   4564   -789   1119   -517       N  
ATOM   2595  N   LYS C 127     -11.954  53.175  21.745  1.00 22.71           N  
ANISOU 2595  N   LYS C 127     3560   2411   2656  -1608    820   -394       N  
ATOM   2596  CA  LYS C 127     -10.666  53.150  21.065  1.00 22.46           C  
ANISOU 2596  CA  LYS C 127     3491   2356   2687  -1590    453   -554       C  
ATOM   2597  C   LYS C 127     -10.920  53.041  19.569  1.00 21.56           C  
ANISOU 2597  C   LYS C 127     3241   2226   2726  -1498    607   -418       C  
ATOM   2598  O   LYS C 127     -11.709  52.195  19.136  1.00 18.84           O  
ANISOU 2598  O   LYS C 127     2672   1973   2511  -1240    482   -624       O  
ATOM   2599  CB  LYS C 127      -9.800  51.983  21.556  1.00 24.02           C  
ANISOU 2599  CB  LYS C 127     3542   2668   2917  -1664    132   -703       C  
ATOM   2600  CG  LYS C 127      -8.415  51.932  20.936  1.00 28.10           C  
ANISOU 2600  CG  LYS C 127     4128   3050   3500  -1828   -106   -611       C  
ATOM   2601  CD  LYS C 127      -7.573  50.827  21.549  1.00 32.85           C  
ANISOU 2601  CD  LYS C 127     4792   3782   3908  -1459     12   -619       C  
ATOM   2602  CE  LYS C 127      -6.134  50.906  21.070  1.00 35.28           C  
ANISOU 2602  CE  LYS C 127     5161   4063   4181  -1486      8   -708       C  
ATOM   2603  NZ  LYS C 127      -5.514  52.214  21.414  1.00 39.77           N  
ANISOU 2603  NZ  LYS C 127     5913   4790   4407   -786    -93   -520       N  
ATOM   2604  N   ASP C 128     -10.261  53.897  18.791  1.00 22.74           N  
ANISOU 2604  N   ASP C 128     3283   2607   2749  -1543    911   -147       N  
ATOM   2605  CA  ASP C 128     -10.486  53.927  17.351  1.00 23.66           C  
ANISOU 2605  CA  ASP C 128     3278   2931   2781  -1553   1039   -166       C  
ATOM   2606  C   ASP C 128     -10.120  52.587  16.726  1.00 21.72           C  
ANISOU 2606  C   ASP C 128     2897   2895   2462  -1582    854   -369       C  
ATOM   2607  O   ASP C 128      -9.071  52.011  17.027  1.00 22.51           O  
ANISOU 2607  O   ASP C 128     3097   3045   2412  -1667   1034   -672       O  
ATOM   2608  CB  ASP C 128      -9.674  55.054  16.714  1.00 30.13           C  
ANISOU 2608  CB  ASP C 128     4068   3986   3392   -826    665    -49       C  
ATOM   2609  CG  ASP C 128      -9.981  55.231  15.239  1.00 37.80           C  
ANISOU 2609  CG  ASP C 128     4911   5132   4318    -11   1078   -160       C  
ATOM   2610  OD1 ASP C 128     -11.148  55.535  14.905  1.00 40.58           O  
ANISOU 2610  OD1 ASP C 128     5225   5556   4637    950    889   -154       O  
ATOM   2611  OD2 ASP C 128      -9.058  55.071  14.414  1.00 41.53           O  
ANISOU 2611  OD2 ASP C 128     5387   5641   4750    168   1259   -105       O  
ATOM   2612  N   GLY C 129     -10.996  52.090  15.858  1.00 19.60           N  
ANISOU 2612  N   GLY C 129     2574   2530   2343  -1461    503   -625       N  
ATOM   2613  CA  GLY C 129     -10.810  50.789  15.253  1.00 18.77           C  
ANISOU 2613  CA  GLY C 129     2234   2612   2287  -1355    177   -602       C  
ATOM   2614  C   GLY C 129     -11.295  49.624  16.085  1.00 16.53           C  
ANISOU 2614  C   GLY C 129     1996   2358   1927  -1057    325   -420       C  
ATOM   2615  O   GLY C 129     -11.124  48.473  15.665  1.00 17.05           O  
ANISOU 2615  O   GLY C 129     2421   2226   1832   -184    391   -449       O  
ATOM   2616  N   ILE C 130     -11.889  49.878  17.248  1.00 15.06           N  
ANISOU 2616  N   ILE C 130     1546   2481   1694   -817    606   -472       N  
ATOM   2617  CA  ILE C 130     -12.427  48.837  18.116  1.00 14.30           C  
ANISOU 2617  CA  ILE C 130     1604   2144   1685   -775    410   -183       C  
ATOM   2618  C   ILE C 130     -13.909  49.113  18.329  1.00 12.81           C  
ANISOU 2618  C   ILE C 130     1585   1556   1726   -325    409   -225       C  
ATOM   2619  O   ILE C 130     -14.286  50.219  18.732  1.00 14.80           O  
ANISOU 2619  O   ILE C 130     2078   1521   2026   -615    238   -454       O  
ATOM   2620  CB  ILE C 130     -11.687  48.783  19.467  1.00 13.16           C  
ANISOU 2620  CB  ILE C 130     1253   1928   1819   -781    374    135       C  
ATOM   2621  CG1 ILE C 130     -10.197  48.504  19.260  1.00 14.39           C  
ANISOU 2621  CG1 ILE C 130     1412   2038   2017   -362    473    -41       C  
ATOM   2622  CG2 ILE C 130     -12.309  47.730  20.379  1.00 13.11           C  
ANISOU 2622  CG2 ILE C 130     1301   1905   1776   -864    244   -183       C  
ATOM   2623  CD1 ILE C 130      -9.906  47.144  18.670  1.00 17.70           C  
ANISOU 2623  CD1 ILE C 130     2192   2062   2471   -142    276   -202       C  
ATOM   2624  N   ILE C 131     -14.746  48.114  18.050  1.00 12.25           N  
ANISOU 2624  N   ILE C 131     1559   1487   1608     45    122   -460       N  
ATOM   2625  CA  ILE C 131     -16.163  48.162  18.386  1.00 12.03           C  
ANISOU 2625  CA  ILE C 131     1688   1053   1829   -501    111   -228       C  
ATOM   2626  C   ILE C 131     -16.505  46.906  19.172  1.00 11.72           C  
ANISOU 2626  C   ILE C 131     1754   1119   1578    -60    340   -113       C  
ATOM   2627  O   ILE C 131     -15.893  45.850  18.988  1.00 12.04           O  
ANISOU 2627  O   ILE C 131     1380   1372   1824    466    390    -51       O  
ATOM   2628  CB  ILE C 131     -17.064  48.300  17.137  1.00 12.41           C  
ANISOU 2628  CB  ILE C 131     2141    741   1833   -261     65   -230       C  
ATOM   2629  CG1 ILE C 131     -16.858  47.126  16.176  1.00 12.65           C  
ANISOU 2629  CG1 ILE C 131     2034    700   2071   -207    384    -96       C  
ATOM   2630  CG2 ILE C 131     -16.801  49.621  16.435  1.00 16.58           C  
ANISOU 2630  CG2 ILE C 131     2720   1398   2180   -625    368   -466       C  
ATOM   2631  CD1 ILE C 131     -17.970  46.102  16.219  1.00 15.04           C  
ANISOU 2631  CD1 ILE C 131     1907   1457   2351   -474    633   -101       C  
ATOM   2632  N   TRP C 132     -17.490  47.025  20.058  1.00 10.30           N  
ANISOU 2632  N   TRP C 132     1425   1126   1362   -204    487   -163       N  
ATOM   2633  CA  TRP C 132     -17.814  45.973  21.010  1.00 10.50           C  
ANISOU 2633  CA  TRP C 132     1811   1061   1117   -538    440     15       C  
ATOM   2634  C   TRP C 132     -19.156  45.331  20.679  1.00 11.45           C  
ANISOU 2634  C   TRP C 132     1895   1177   1279   -380    313    -66       C  
ATOM   2635  O   TRP C 132     -20.077  45.991  20.188  1.00 12.40           O  
ANISOU 2635  O   TRP C 132     2017   1183   1513     45    249     66       O  
ATOM   2636  CB  TRP C 132     -17.842  46.523  22.441  1.00 13.15           C  
ANISOU 2636  CB  TRP C 132     2026   1756   1213   -648     69   -104       C  
ATOM   2637  CG  TRP C 132     -16.504  46.999  22.913  1.00 13.34           C  
ANISOU 2637  CG  TRP C 132     2163   1729   1177   -768     70    -88       C  
ATOM   2638  CD1 TRP C 132     -16.045  48.285  22.926  1.00 13.46           C  
ANISOU 2638  CD1 TRP C 132     2278   1797   1039   -768   -159   -252       C  
ATOM   2639  CD2 TRP C 132     -15.442  46.189  23.431  1.00 14.55           C  
ANISOU 2639  CD2 TRP C 132     2238   2147   1142   -486     48   -151       C  
ATOM   2640  NE1 TRP C 132     -14.766  48.326  23.425  1.00 14.14           N  
ANISOU 2640  NE1 TRP C 132     2441   1794   1138   -770     96   -179       N  
ATOM   2641  CE2 TRP C 132     -14.372  47.052  23.740  1.00 15.31           C  
ANISOU 2641  CE2 TRP C 132     2488   2192   1137   -697     -6    -22       C  
ATOM   2642  CE3 TRP C 132     -15.293  44.818  23.661  1.00 13.21           C  
ANISOU 2642  CE3 TRP C 132     1925   2099    996   -251    209   -132       C  
ATOM   2643  CZ2 TRP C 132     -13.169  46.589  24.270  1.00 17.53           C  
ANISOU 2643  CZ2 TRP C 132     2677   2603   1381   -525    263   -117       C  
ATOM   2644  CZ3 TRP C 132     -14.098  44.360  24.188  1.00 14.83           C  
ANISOU 2644  CZ3 TRP C 132     2061   2560   1014   -395    113   -450       C  
ATOM   2645  CH2 TRP C 132     -13.053  45.243  24.488  1.00 17.37           C  
ANISOU 2645  CH2 TRP C 132     2679   2594   1328   -157    259   -521       C  
ATOM   2646  N   VAL C 133     -19.253  44.028  20.950  1.00  9.82           N  
ANISOU 2646  N   VAL C 133     1558    974   1201   -448     65    -68       N  
ATOM   2647  CA  VAL C 133     -20.486  43.271  20.769  1.00 10.61           C  
ANISOU 2647  CA  VAL C 133     1628   1153   1251   -176    353   -294       C  
ATOM   2648  C   VAL C 133     -20.667  42.333  21.955  1.00 11.19           C  
ANISOU 2648  C   VAL C 133     1322   1522   1409   -387    218   -206       C  
ATOM   2649  O   VAL C 133     -19.696  41.843  22.542  1.00 10.19           O  
ANISOU 2649  O   VAL C 133      981   1618   1272   -444     81     76       O  
ATOM   2650  CB  VAL C 133     -20.498  42.467  19.446  1.00  9.32           C  
ANISOU 2650  CB  VAL C 133     1630    964    947    392     95   -385       C  
ATOM   2651  CG1 VAL C 133     -20.572  43.397  18.242  1.00 10.38           C  
ANISOU 2651  CG1 VAL C 133     2120    779   1043    517    138    -70       C  
ATOM   2652  CG2 VAL C 133     -19.277  41.564  19.360  1.00 10.24           C  
ANISOU 2652  CG2 VAL C 133     1587   1324    980    238    304   -562       C  
ATOM   2653  N   ALA C 134     -21.926  42.081  22.306  1.00  9.79           N  
ANISOU 2653  N   ALA C 134     1275   1128   1316   -580    278    -99       N  
ATOM   2654  CA  ALA C 134     -22.234  41.145  23.379  1.00  8.99           C  
ANISOU 2654  CA  ALA C 134     1136   1222   1058    -26    317   -262       C  
ATOM   2655  C   ALA C 134     -23.660  40.649  23.210  1.00  9.96           C  
ANISOU 2655  C   ALA C 134     1370   1170   1244   -121    125   -187       C  
ATOM   2656  O   ALA C 134     -24.583  41.454  23.056  1.00 11.38           O  
ANISOU 2656  O   ALA C 134     1531   1207   1587      1    265   -179       O  
ATOM   2657  CB  ALA C 134     -22.059  41.797  24.757  1.00 10.31           C  
ANISOU 2657  CB  ALA C 134     1574   1244   1098    453     50   -552       C  
ATOM   2658  N   THR C 135     -23.831  39.331  23.238  1.00  8.14           N  
ANISOU 2658  N   THR C 135     1072    795   1226   -433    218   -124       N  
ATOM   2659  CA  THR C 135     -25.154  38.732  23.272  1.00 10.95           C  
ANISOU 2659  CA  THR C 135     1331   1263   1566   -140    279   -320       C  
ATOM   2660  C   THR C 135     -25.719  38.830  24.684  1.00 10.40           C  
ANISOU 2660  C   THR C 135     1021   1405   1526   -350    282   -168       C  
ATOM   2661  O   THR C 135     -24.976  38.834  25.670  1.00 10.77           O  
ANISOU 2661  O   THR C 135     1041   1863   1189   -236   -386   -151       O  
ATOM   2662  CB  THR C 135     -25.088  37.267  22.825  1.00 10.73           C  
ANISOU 2662  CB  THR C 135     1115   1253   1708   -440    470   -633       C  
ATOM   2663  OG1 THR C 135     -24.468  37.186  21.535  1.00 10.17           O  
ANISOU 2663  OG1 THR C 135      646   1556   1662   -195    212   -393       O  
ATOM   2664  CG2 THR C 135     -26.480  36.642  22.750  1.00 11.98           C  
ANISOU 2664  CG2 THR C 135     1430   1282   1840   -237    667   -361       C  
ATOM   2665  N   GLU C 136     -27.043  38.943  24.775  1.00  9.91           N  
ANISOU 2665  N   GLU C 136      884   1133   1749   -129    644   -242       N  
ATOM   2666  CA  GLU C 136     -27.703  38.936  26.075  1.00 13.33           C  
ANISOU 2666  CA  GLU C 136     1092   2142   1831   -135    732   -318       C  
ATOM   2667  C   GLU C 136     -27.307  37.688  26.853  1.00 12.43           C  
ANISOU 2667  C   GLU C 136     1171   1985   1568   -696     78   -372       C  
ATOM   2668  O   GLU C 136     -27.308  36.578  26.313  1.00 12.82           O  
ANISOU 2668  O   GLU C 136     1757   1702   1411   -612   -337   -319       O  
ATOM   2669  CB  GLU C 136     -29.221  38.997  25.896  1.00 16.74           C  
ANISOU 2669  CB  GLU C 136     1539   2615   2207    593    882   -151       C  
ATOM   2670  CG  GLU C 136     -29.993  39.389  27.153  1.00 25.85           C  
ANISOU 2670  CG  GLU C 136     2382   4383   3058    630   1222   -430       C  
ATOM   2671  CD  GLU C 136     -30.169  38.239  28.129  1.00 35.55           C  
ANISOU 2671  CD  GLU C 136     3898   5907   3703    749    893  -1020       C  
ATOM   2672  OE1 GLU C 136     -30.158  37.071  27.684  1.00 38.38           O  
ANISOU 2672  OE1 GLU C 136     4218   6403   3964    674    917  -1358       O  
ATOM   2673  OE2 GLU C 136     -30.315  38.504  29.342  1.00 39.50           O  
ANISOU 2673  OE2 GLU C 136     4449   6669   3889    828    475  -1005       O  
ATOM   2674  N   GLY C 137     -26.951  37.875  28.124  1.00 10.67           N  
ANISOU 2674  N   GLY C 137      936   1771   1347   -590    235   -271       N  
ATOM   2675  CA  GLY C 137     -26.533  36.786  28.980  1.00 11.94           C  
ANISOU 2675  CA  GLY C 137      930   2077   1528   -357    370   -153       C  
ATOM   2676  C   GLY C 137     -25.035  36.572  29.064  1.00 11.08           C  
ANISOU 2676  C   GLY C 137      823   1923   1464   -265    101   -129       C  
ATOM   2677  O   GLY C 137     -24.583  35.835  29.951  1.00 11.62           O  
ANISOU 2677  O   GLY C 137     1013   1900   1502   -196    473     80       O  
ATOM   2678  N   ALA C 138     -24.256  37.184  28.176  1.00  9.23           N  
ANISOU 2678  N   ALA C 138      600   1715   1190   -350     80   -370       N  
ATOM   2679  CA  ALA C 138     -22.808  37.042  28.230  1.00  9.49           C  
ANISOU 2679  CA  ALA C 138      539   1797   1271    -67    239   -186       C  
ATOM   2680  C   ALA C 138     -22.246  37.701  29.485  1.00 10.06           C  
ANISOU 2680  C   ALA C 138     1048   1461   1312    -11    165   -554       C  
ATOM   2681  O   ALA C 138     -22.808  38.665  30.015  1.00 11.32           O  
ANISOU 2681  O   ALA C 138     1152   1405   1744   -276    340   -387       O  
ATOM   2682  CB  ALA C 138     -22.162  37.651  26.986  1.00  9.47           C  
ANISOU 2682  CB  ALA C 138      528   1796   1274    -85    210   -211       C  
ATOM   2683  N   LEU C 139     -21.120  37.174  29.958  1.00  9.41           N  
ANISOU 2683  N   LEU C 139     1502    980   1092    221     59   -539       N  
ATOM   2684  CA  LEU C 139     -20.484  37.650  31.178  1.00 10.10           C  
ANISOU 2684  CA  LEU C 139     1651   1135   1050    187     -9   -171       C  
ATOM   2685  C   LEU C 139     -19.251  38.481  30.848  1.00  9.32           C  
ANISOU 2685  C   LEU C 139     1182   1183   1175    153    -23   -331       C  
ATOM   2686  O   LEU C 139     -18.469  38.126  29.959  1.00  9.35           O  
ANISOU 2686  O   LEU C 139     1632    901   1022    202    -42   -125       O  
ATOM   2687  CB  LEU C 139     -20.091  36.482  32.085  1.00 12.41           C  
ANISOU 2687  CB  LEU C 139     2027   1466   1222    483    -78      8       C  
ATOM   2688  CG  LEU C 139     -21.228  35.580  32.566  1.00 12.06           C  
ANISOU 2688  CG  LEU C 139     1989   1409   1183    410     75   -214       C  
ATOM   2689  CD1 LEU C 139     -20.685  34.512  33.497  1.00 10.69           C  
ANISOU 2689  CD1 LEU C 139     1928   1050   1086    578   -311   -254       C  
ATOM   2690  CD2 LEU C 139     -22.318  36.396  33.252  1.00 12.76           C  
ANISOU 2690  CD2 LEU C 139     2151   1511   1186    -48    377   -399       C  
ATOM   2691  N   ASN C 140     -19.085  39.591  31.569  1.00  8.16           N  
ANISOU 2691  N   ASN C 140      627   1156   1319   -337    152   -477       N  
ATOM   2692  CA  ASN C 140     -17.928  40.474  31.408  1.00  9.74           C  
ANISOU 2692  CA  ASN C 140      916   1350   1437   -364    -76   -584       C  
ATOM   2693  C   ASN C 140     -16.765  39.884  32.204  1.00  9.76           C  
ANISOU 2693  C   ASN C 140     1033   1267   1408    158   -301   -682       C  
ATOM   2694  O   ASN C 140     -16.401  40.346  33.289  1.00 12.52           O  
ANISOU 2694  O   ASN C 140     1376   1821   1559   -463   -296   -522       O  
ATOM   2695  CB  ASN C 140     -18.272  41.891  31.854  1.00  9.00           C  
ANISOU 2695  CB  ASN C 140      998   1163   1261    -88    163   -412       C  
ATOM   2696  CG  ASN C 140     -17.138  42.884  31.620  1.00 12.17           C  
ANISOU 2696  CG  ASN C 140     1871   1588   1165    132    337   -538       C  
ATOM   2697  OD1 ASN C 140     -16.049  42.521  31.169  1.00 14.90           O  
ANISOU 2697  OD1 ASN C 140     2188   1788   1684     82    515   -527       O  
ATOM   2698  ND2 ASN C 140     -17.400  44.152  31.916  1.00 10.75           N  
ANISOU 2698  ND2 ASN C 140     1751   1451    881   -331    481   -299       N  
ATOM   2699  N   THR C 141     -16.187  38.823  31.647  1.00 10.90           N  
ANISOU 2699  N   THR C 141     1521   1237   1385    684    145   -352       N  
ATOM   2700  CA  THR C 141     -15.025  38.123  32.175  1.00 11.60           C  
ANISOU 2700  CA  THR C 141     1813   1360   1234    182     -1   -587       C  
ATOM   2701  C   THR C 141     -14.138  37.730  31.004  1.00 11.62           C  
ANISOU 2701  C   THR C 141     1686   1519   1209   -262   -177   -567       C  
ATOM   2702  O   THR C 141     -14.643  37.483  29.903  1.00 12.17           O  
ANISOU 2702  O   THR C 141     1834   1411   1380   -490   -416   -537       O  
ATOM   2703  CB  THR C 141     -15.419  36.857  32.955  1.00 14.28           C  
ANISOU 2703  CB  THR C 141     2264   1781   1378   -166     69   -492       C  
ATOM   2704  OG1 THR C 141     -16.155  35.978  32.094  1.00 14.92           O  
ANISOU 2704  OG1 THR C 141     2497   1776   1398   -555   -301   -438       O  
ATOM   2705  CG2 THR C 141     -16.267  37.202  34.172  1.00 15.55           C  
ANISOU 2705  CG2 THR C 141     2700   1652   1557    -56    222   -890       C  
ATOM   2706  N   PRO C 142     -12.821  37.658  31.205  1.00 12.09           N  
ANISOU 2706  N   PRO C 142     1630   1732   1232   -278   -521   -582       N  
ATOM   2707  CA  PRO C 142     -11.935  37.294  30.091  1.00 11.45           C  
ANISOU 2707  CA  PRO C 142     1628   1591   1131   -246   -443   -590       C  
ATOM   2708  C   PRO C 142     -12.149  35.853  29.649  1.00 12.32           C  
ANISOU 2708  C   PRO C 142     1792   1671   1219      2   -550   -578       C  
ATOM   2709  O   PRO C 142     -12.387  34.959  30.465  1.00 15.32           O  
ANISOU 2709  O   PRO C 142     2385   1744   1694     32   -227   -833       O  
ATOM   2710  CB  PRO C 142     -10.529  37.504  30.667  1.00 13.59           C  
ANISOU 2710  CB  PRO C 142     1942   1947   1276   -496   -551   -504       C  
ATOM   2711  CG  PRO C 142     -10.704  37.416  32.142  1.00 14.95           C  
ANISOU 2711  CG  PRO C 142     2019   2321   1340   -226   -496   -655       C  
ATOM   2712  CD  PRO C 142     -12.066  37.981  32.428  1.00 13.14           C  
ANISOU 2712  CD  PRO C 142     1292   2231   1470    105   -628   -603       C  
ATOM   2713  N   LYS C 143     -12.061  35.634  28.341  1.00 12.03           N  
ANISOU 2713  N   LYS C 143     1765   1620   1185    148   -560   -628       N  
ATOM   2714  CA  LYS C 143     -12.291  34.313  27.752  1.00 12.48           C  
ANISOU 2714  CA  LYS C 143     1700   1663   1379    261   -804   -502       C  
ATOM   2715  C   LYS C 143     -10.978  33.607  27.440  1.00 13.21           C  
ANISOU 2715  C   LYS C 143     1311   2048   1660    104   -782   -454       C  
ATOM   2716  O   LYS C 143     -10.750  33.141  26.321  1.00 10.86           O  
ANISOU 2716  O   LYS C 143      695   1824   1608    231   -359   -427       O  
ATOM   2717  CB  LYS C 143     -13.152  34.437  26.501  1.00 11.35           C  
ANISOU 2717  CB  LYS C 143     1375   1674   1263    560   -672   -366       C  
ATOM   2718  CG  LYS C 143     -14.397  35.290  26.684  1.00 10.18           C  
ANISOU 2718  CG  LYS C 143     1248   1317   1301    639    141   -354       C  
ATOM   2719  CD  LYS C 143     -15.209  34.857  27.897  1.00 10.29           C  
ANISOU 2719  CD  LYS C 143     1118   1627   1164    660   -184   -561       C  
ATOM   2720  CE  LYS C 143     -16.422  35.756  28.076  1.00 10.81           C  
ANISOU 2720  CE  LYS C 143     1361   1524   1224    496   -321   -739       C  
ATOM   2721  NZ  LYS C 143     -17.010  35.676  29.444  1.00  9.91           N  
ANISOU 2721  NZ  LYS C 143     1140   1496   1128    548   -448   -682       N  
ATOM   2722  N   ASP C 144     -10.103  33.514  28.446  1.00 15.40           N  
ANISOU 2722  N   ASP C 144     1698   1917   2236    129  -1072   -520       N  
ATOM   2723  CA  ASP C 144      -8.805  32.874  28.255  1.00 17.83           C  
ANISOU 2723  CA  ASP C 144     2215   1994   2567    274  -1066   -496       C  
ATOM   2724  C   ASP C 144      -8.946  31.420  27.828  1.00 16.29           C  
ANISOU 2724  C   ASP C 144     2300   1607   2282    369  -1165   -374       C  
ATOM   2725  O   ASP C 144      -8.109  30.914  27.070  1.00 17.58           O  
ANISOU 2725  O   ASP C 144     2388   1585   2708   -225   -744   -140       O  
ATOM   2726  CB  ASP C 144      -7.981  32.962  29.540  1.00 22.75           C  
ANISOU 2726  CB  ASP C 144     2870   2696   3076    186  -1209   -660       C  
ATOM   2727  CG  ASP C 144      -7.598  34.386  29.892  1.00 30.30           C  
ANISOU 2727  CG  ASP C 144     3972   3922   3618     90   -836   -329       C  
ATOM   2728  OD1 ASP C 144      -6.886  35.029  29.093  1.00 33.94           O  
ANISOU 2728  OD1 ASP C 144     4189   4473   4231   -655   -475   -315       O  
ATOM   2729  OD2 ASP C 144      -8.019  34.866  30.965  1.00 32.08           O  
ANISOU 2729  OD2 ASP C 144     4255   4300   3633   1121   -667   -304       O  
ATOM   2730  N   HIS C 145      -9.994  30.732  28.293  1.00 15.34           N  
ANISOU 2730  N   HIS C 145     2419   1553   1858    489  -1004   -296       N  
ATOM   2731  CA  HIS C 145     -10.155  29.322  27.957  1.00 15.64           C  
ANISOU 2731  CA  HIS C 145     2384   1643   1916    452   -706   -401       C  
ATOM   2732  C   HIS C 145     -10.456  29.110  26.479  1.00 14.69           C  
ANISOU 2732  C   HIS C 145     1929   1822   1832    204   -848   -428       C  
ATOM   2733  O   HIS C 145     -10.296  27.989  25.984  1.00 15.17           O  
ANISOU 2733  O   HIS C 145     1662   1991   2109    268   -767   -202       O  
ATOM   2734  CB  HIS C 145     -11.249  28.687  28.819  1.00 15.08           C  
ANISOU 2734  CB  HIS C 145     2025   1573   2133    371   -624   -420       C  
ATOM   2735  CG  HIS C 145     -12.626  29.201  28.535  1.00 15.88           C  
ANISOU 2735  CG  HIS C 145     2644   1387   2001    591   -987   -244       C  
ATOM   2736  ND1 HIS C 145     -13.078  30.419  28.996  1.00 15.42           N  
ANISOU 2736  ND1 HIS C 145     2493   1374   1992    782   -613   -311       N  
ATOM   2737  CD2 HIS C 145     -13.658  28.651  27.852  1.00 15.49           C  
ANISOU 2737  CD2 HIS C 145     2597   1498   1791    463   -825   -171       C  
ATOM   2738  CE1 HIS C 145     -14.325  30.603  28.598  1.00 14.94           C  
ANISOU 2738  CE1 HIS C 145     2386   1378   1914    330   -927   -621       C  
ATOM   2739  NE2 HIS C 145     -14.700  29.544  27.903  1.00 14.23           N  
ANISOU 2739  NE2 HIS C 145     2240   1351   1818    767   -851   -179       N  
ATOM   2740  N   ILE C 146     -10.879  30.152  25.767  1.00 12.02           N  
ANISOU 2740  N   ILE C 146     1484   1488   1594    741   -627   -294       N  
ATOM   2741  CA  ILE C 146     -11.002  30.090  24.313  1.00 13.29           C  
ANISOU 2741  CA  ILE C 146     1816   1518   1716    554   -557   -143       C  
ATOM   2742  C   ILE C 146      -9.728  30.575  23.634  1.00 14.35           C  
ANISOU 2742  C   ILE C 146     2011   1652   1789    345   -394   -306       C  
ATOM   2743  O   ILE C 146      -9.204  29.921  22.728  1.00 13.65           O  
ANISOU 2743  O   ILE C 146     1845   1734   1609    677   -527   -522       O  
ATOM   2744  CB  ILE C 146     -12.231  30.897  23.844  1.00 13.28           C  
ANISOU 2744  CB  ILE C 146     1550   1951   1543    457   -648   -122       C  
ATOM   2745  CG1 ILE C 146     -13.518  30.289  24.403  1.00 14.84           C  
ANISOU 2745  CG1 ILE C 146     1696   1890   2053    236  -1051    111       C  
ATOM   2746  CG2 ILE C 146     -12.284  30.961  22.319  1.00 12.18           C  
ANISOU 2746  CG2 ILE C 146     1081   2211   1337    648   -422   -510       C  
ATOM   2747  CD1 ILE C 146     -14.772  31.031  23.990  1.00 13.94           C  
ANISOU 2747  CD1 ILE C 146     1639   1574   2084     69  -1093    -50       C  
ATOM   2748  N   GLY C 147      -9.214  31.725  24.064  1.00 15.98           N  
ANISOU 2748  N   GLY C 147     2309   2029   1732    -64   -329    113       N  
ATOM   2749  CA  GLY C 147      -7.968  32.237  23.532  1.00 16.17           C  
ANISOU 2749  CA  GLY C 147     1939   2518   1686     53   -446   -268       C  
ATOM   2750  C   GLY C 147      -8.070  32.649  22.070  1.00 15.85           C  
ANISOU 2750  C   GLY C 147     1712   2513   1797    164   -451   -402       C  
ATOM   2751  O   GLY C 147      -9.142  32.964  21.541  1.00 13.65           O  
ANISOU 2751  O   GLY C 147      923   2306   1956    508   -433   -159       O  
ATOM   2752  N   THR C 148      -6.914  32.641  21.417  1.00 15.71           N  
ANISOU 2752  N   THR C 148     1663   2640   1668     20   -428   -476       N  
ATOM   2753  CA  THR C 148      -6.793  32.998  20.013  1.00 16.43           C  
ANISOU 2753  CA  THR C 148     1615   2757   1871     80   -681   -310       C  
ATOM   2754  C   THR C 148      -6.369  31.781  19.201  1.00 17.44           C  
ANISOU 2754  C   THR C 148     1589   3075   1963    400   -895   -324       C  
ATOM   2755  O   THR C 148      -6.065  30.713  19.742  1.00 19.13           O  
ANISOU 2755  O   THR C 148     2180   3038   2051    863   -910   -260       O  
ATOM   2756  CB  THR C 148      -5.793  34.145  19.825  1.00 20.48           C  
ANISOU 2756  CB  THR C 148     2118   3361   2304    459   -570   -337       C  
ATOM   2757  OG1 THR C 148      -4.559  33.816  20.474  1.00 23.60           O  
ANISOU 2757  OG1 THR C 148     2407   4095   2464    436   -895    -99       O  
ATOM   2758  CG2 THR C 148      -6.345  35.432  20.419  1.00 22.19           C  
ANISOU 2758  CG2 THR C 148     2695   3062   2673    209   -366   -589       C  
ATOM   2759  N   ARG C 149      -6.341  31.960  17.884  1.00 17.78           N  
ANISOU 2759  N   ARG C 149     1382   3369   2004    579   -632   -727       N  
ATOM   2760  CA  ARG C 149      -6.099  30.862  16.960  1.00 21.94           C  
ANISOU 2760  CA  ARG C 149     1835   4085   2418    849   -831   -827       C  
ATOM   2761  C   ARG C 149      -4.624  30.781  16.590  1.00 27.68           C  
ANISOU 2761  C   ARG C 149     2858   4728   2933   1092   -757   -730       C  
ATOM   2762  O   ARG C 149      -3.987  31.803  16.317  1.00 28.44           O  
ANISOU 2762  O   ARG C 149     3111   4659   3036    783   -746   -669       O  
ATOM   2763  CB  ARG C 149      -6.946  31.032  15.698  1.00 19.05           C  
ANISOU 2763  CB  ARG C 149     1693   3411   2137    464   -826   -916       C  
ATOM   2764  CG  ARG C 149      -6.705  29.966  14.636  1.00 19.56           C  
ANISOU 2764  CG  ARG C 149     2017   3444   1970   1110   -798   -942       C  
ATOM   2765  CD  ARG C 149      -7.668  30.111  13.469  1.00 18.69           C  
ANISOU 2765  CD  ARG C 149     1889   3230   1983   1112   -414   -805       C  
ATOM   2766  NE  ARG C 149      -7.515  31.385  12.773  1.00 17.22           N  
ANISOU 2766  NE  ARG C 149     1471   3099   1974    774    -85   -714       N  
ATOM   2767  CZ  ARG C 149      -6.740  31.573  11.709  1.00 17.97           C  
ANISOU 2767  CZ  ARG C 149     1410   3192   2227    687    254   -485       C  
ATOM   2768  NH1 ARG C 149      -6.035  30.566  11.209  1.00 18.54           N  
ANISOU 2768  NH1 ARG C 149     1499   3248   2298    965    400   -226       N  
ATOM   2769  NH2 ARG C 149      -6.670  32.770  11.144  1.00 17.29           N  
ANISOU 2769  NH2 ARG C 149     1080   3169   2321    592    289   -275       N  
ATOM   2770  N   ASN C 150      -4.087  29.559  16.590  1.00 31.44           N  
ANISOU 2770  N   ASN C 150     3196   5433   3318   1563   -686   -501       N  
ATOM   2771  CA  ASN C 150      -2.762  29.298  16.052  1.00 33.23           C  
ANISOU 2771  CA  ASN C 150     3164   5650   3811   1870   -363   -292       C  
ATOM   2772  C   ASN C 150      -2.929  28.788  14.630  1.00 32.78           C  
ANISOU 2772  C   ASN C 150     2887   5388   4179   2140     75    -93       C  
ATOM   2773  O   ASN C 150      -3.446  27.675  14.441  1.00 31.88           O  
ANISOU 2773  O   ASN C 150     2969   4974   4169   2161     -9    -52       O  
ATOM   2774  CB  ASN C 150      -2.020  28.272  16.906  1.00 36.98           C  
ANISOU 2774  CB  ASN C 150     3532   6226   4292   1805   -104    -35       C  
ATOM   2775  CG  ASN C 150      -0.560  28.124  16.512  1.00 41.51           C  
ANISOU 2775  CG  ASN C 150     4196   6904   4674   1632     23    432       C  
ATOM   2776  OD1 ASN C 150      -0.168  28.439  15.387  1.00 43.13           O  
ANISOU 2776  OD1 ASN C 150     4567   7082   4739   1592     18    454       O  
ATOM   2777  ND2 ASN C 150       0.253  27.637  17.442  1.00 41.96           N  
ANISOU 2777  ND2 ASN C 150     4001   7091   4852   1781    -75    840       N  
ATOM   2778  N   PRO C 151      -2.523  29.547  13.609  1.00 32.90           N  
ANISOU 2778  N   PRO C 151     3049   5196   4257   1423    704     62       N  
ATOM   2779  CA  PRO C 151      -2.730  29.088  12.225  1.00 35.39           C  
ANISOU 2779  CA  PRO C 151     3668   5292   4489   1295    814     43       C  
ATOM   2780  C   PRO C 151      -2.065  27.759  11.913  1.00 38.74           C  
ANISOU 2780  C   PRO C 151     4259   5659   4804   1455    880    -20       C  
ATOM   2781  O   PRO C 151      -2.475  27.089  10.957  1.00 40.53           O  
ANISOU 2781  O   PRO C 151     4555   5828   5018   1459    894    -11       O  
ATOM   2782  CB  PRO C 151      -2.131  30.226  11.385  1.00 35.27           C  
ANISOU 2782  CB  PRO C 151     3777   5168   4455   1004    781    106       C  
ATOM   2783  CG  PRO C 151      -2.185  31.423  12.279  1.00 34.25           C  
ANISOU 2783  CG  PRO C 151     3574   5016   4422    969    901    127       C  
ATOM   2784  CD  PRO C 151      -1.946  30.901  13.664  1.00 33.55           C  
ANISOU 2784  CD  PRO C 151     3285   5095   4369   1170    732     38       C  
ATOM   2785  N   ALA C 152      -1.060  27.351  12.692  1.00 39.13           N  
ANISOU 2785  N   ALA C 152     4287   5673   4907   1687    844    -70       N  
ATOM   2786  CA  ALA C 152      -0.403  26.074  12.439  1.00 39.96           C  
ANISOU 2786  CA  ALA C 152     4598   5553   5030   1904    500   -126       C  
ATOM   2787  C   ALA C 152      -1.292  24.895  12.817  1.00 39.45           C  
ANISOU 2787  C   ALA C 152     4622   5397   4970   2227    677   -397       C  
ATOM   2788  O   ALA C 152      -1.120  23.795  12.280  1.00 41.62           O  
ANISOU 2788  O   ALA C 152     5083   5705   5026   1986    710   -519       O  
ATOM   2789  CB  ALA C 152       0.920  26.005  13.202  1.00 39.84           C  
ANISOU 2789  CB  ALA C 152     4410   5617   5110   1954     33    -57       C  
ATOM   2790  N   ASN C 153      -2.240  25.099  13.730  1.00 35.47           N  
ANISOU 2790  N   ASN C 153     3817   4788   4871   2435    516   -358       N  
ATOM   2791  CA  ASN C 153      -3.092  24.022  14.214  1.00 36.21           C  
ANISOU 2791  CA  ASN C 153     4024   4945   4790   2610     45   -476       C  
ATOM   2792  C   ASN C 153      -4.533  24.115  13.743  1.00 35.78           C  
ANISOU 2792  C   ASN C 153     4590   4691   4313   2399   -226   -283       C  
ATOM   2793  O   ASN C 153      -5.210  23.088  13.676  1.00 37.18           O  
ANISOU 2793  O   ASN C 153     4919   4829   4381   2110   -378     11       O  
ATOM   2794  CB  ASN C 153      -3.080  23.981  15.747  1.00 38.89           C  
ANISOU 2794  CB  ASN C 153     4103   5531   5142   2586   -271   -411       C  
ATOM   2795  CG  ASN C 153      -1.726  23.600  16.308  1.00 42.44           C  
ANISOU 2795  CG  ASN C 153     4472   6154   5501   2296   -220   -572       C  
ATOM   2796  OD1 ASN C 153      -1.046  22.725  15.773  1.00 44.73           O  
ANISOU 2796  OD1 ASN C 153     4657   6563   5775   1988   -314   -638       O  
ATOM   2797  ND2 ASN C 153      -1.326  24.257  17.391  1.00 42.51           N  
ANISOU 2797  ND2 ASN C 153     4500   6200   5452   2206   -227   -679       N  
ATOM   2798  N   ASN C 154      -5.021  25.311  13.420  1.00 32.19           N  
ANISOU 2798  N   ASN C 154     4309   4174   3749   2506     27   -382       N  
ATOM   2799  CA  ASN C 154      -6.415  25.490  13.039  1.00 30.00           C  
ANISOU 2799  CA  ASN C 154     4150   3889   3359   2404     30     63       C  
ATOM   2800  C   ASN C 154      -6.527  26.533  11.940  1.00 26.43           C  
ANISOU 2800  C   ASN C 154     3721   3655   2666   1997    356      1       C  
ATOM   2801  O   ASN C 154      -5.971  27.629  12.059  1.00 26.92           O  
ANISOU 2801  O   ASN C 154     3982   3673   2574   1610    526   -159       O  
ATOM   2802  CB  ASN C 154      -7.269  25.914  14.240  1.00 32.04           C  
ANISOU 2802  CB  ASN C 154     4790   3810   3573   2142   -284    173       C  
ATOM   2803  CG  ASN C 154      -7.333  24.852  15.317  1.00 35.00           C  
ANISOU 2803  CG  ASN C 154     5233   3989   4074   1897   -693    553       C  
ATOM   2804  OD1 ASN C 154      -6.521  24.839  16.242  1.00 36.54           O  
ANISOU 2804  OD1 ASN C 154     5412   4179   4294   2261  -1106    745       O  
ATOM   2805  ND2 ASN C 154      -8.305  23.954  15.204  1.00 36.54           N  
ANISOU 2805  ND2 ASN C 154     5433   4208   4244   1230   -623    612       N  
ATOM   2806  N   ALA C 155      -7.245  26.188  10.877  1.00 22.20           N  
ANISOU 2806  N   ALA C 155     3186   3025   2224   1855    218    203       N  
ATOM   2807  CA  ALA C 155      -7.636  27.187   9.900  1.00 18.72           C  
ANISOU 2807  CA  ALA C 155     2826   2622   1664   1614    118    239       C  
ATOM   2808  C   ALA C 155      -8.729  28.079  10.484  1.00 15.96           C  
ANISOU 2808  C   ALA C 155     2703   2014   1347   1359    133    186       C  
ATOM   2809  O   ALA C 155      -9.389  27.734  11.469  1.00 16.42           O  
ANISOU 2809  O   ALA C 155     3061   1958   1219    769     42    116       O  
ATOM   2810  CB  ALA C 155      -8.123  26.522   8.613  1.00 18.56           C  
ANISOU 2810  CB  ALA C 155     2733   2754   1564   1569    182   -123       C  
ATOM   2811  N   ALA C 156      -8.911  29.243   9.872  1.00 14.84           N  
ANISOU 2811  N   ALA C 156     2250   1853   1537   1198    134    -43       N  
ATOM   2812  CA  ALA C 156      -9.929  30.167  10.347  1.00 11.77           C  
ANISOU 2812  CA  ALA C 156     1473   1516   1484    842    -59   -339       C  
ATOM   2813  C   ALA C 156     -11.324  29.587  10.146  1.00 12.66           C  
ANISOU 2813  C   ALA C 156     1847   1485   1478    492   -339   -531       C  
ATOM   2814  O   ALA C 156     -11.586  28.846   9.194  1.00 15.29           O  
ANISOU 2814  O   ALA C 156     2541   1719   1549    221   -405   -483       O  
ATOM   2815  CB  ALA C 156      -9.810  31.512   9.631  1.00 10.44           C  
ANISOU 2815  CB  ALA C 156      869   1728   1370    370    298   -285       C  
ATOM   2816  N   ILE C 157     -12.215  29.917  11.074  1.00 10.71           N  
ANISOU 2816  N   ILE C 157     1098   1490   1483    361     36   -223       N  
ATOM   2817  CA  ILE C 157     -13.630  29.582  10.975  1.00 13.53           C  
ANISOU 2817  CA  ILE C 157     1509   1925   1705     10     94     43       C  
ATOM   2818  C   ILE C 157     -14.320  30.673  10.169  1.00 13.67           C  
ANISOU 2818  C   ILE C 157     1162   2263   1770    158     46    127       C  
ATOM   2819  O   ILE C 157     -14.125  31.863  10.435  1.00 13.22           O  
ANISOU 2819  O   ILE C 157      918   2246   1857    163    319    -19       O  
ATOM   2820  CB  ILE C 157     -14.258  29.454  12.373  1.00 16.61           C  
ANISOU 2820  CB  ILE C 157     1925   2390   1995   -831    357    347       C  
ATOM   2821  CG1 ILE C 157     -13.568  28.349  13.175  1.00 19.84           C  
ANISOU 2821  CG1 ILE C 157     2661   3053   1824   -654    597    500       C  
ATOM   2822  CG2 ILE C 157     -15.764  29.221  12.278  1.00 18.37           C  
ANISOU 2822  CG2 ILE C 157     2283   2517   2180   -695    395    142       C  
ATOM   2823  CD1 ILE C 157     -13.935  28.344  14.642  1.00 23.39           C  
ANISOU 2823  CD1 ILE C 157     3387   3492   2009   -473    827    709       C  
ATOM   2824  N   VAL C 158     -15.123  30.278   9.180  1.00 12.26           N  
ANISOU 2824  N   VAL C 158      901   2030   1728     53   -373   -302       N  
ATOM   2825  CA  VAL C 158     -15.846  31.269   8.388  1.00 13.46           C  
ANISOU 2825  CA  VAL C 158     1286   2011   1816     78   -523   -432       C  
ATOM   2826  C   VAL C 158     -16.813  32.017   9.295  1.00 13.31           C  
ANISOU 2826  C   VAL C 158     1202   1902   1951   -203    -88   -185       C  
ATOM   2827  O   VAL C 158     -17.659  31.408   9.961  1.00 17.26           O  
ANISOU 2827  O   VAL C 158     1838   2312   2408   -213    131   -123       O  
ATOM   2828  CB  VAL C 158     -16.573  30.604   7.217  1.00 17.41           C  
ANISOU 2828  CB  VAL C 158     1964   2570   2081    424   -675   -478       C  
ATOM   2829  CG1 VAL C 158     -17.500  31.602   6.538  1.00 16.82           C  
ANISOU 2829  CG1 VAL C 158     2194   2194   2003    139   -414   -269       C  
ATOM   2830  CG2 VAL C 158     -15.565  30.052   6.223  1.00 19.31           C  
ANISOU 2830  CG2 VAL C 158     2412   2769   2157    503   -576   -780       C  
ATOM   2831  N   LEU C 159     -16.686  33.342   9.337  1.00 10.80           N  
ANISOU 2831  N   LEU C 159      895   1640   1568    -91     92   -330       N  
ATOM   2832  CA  LEU C 159     -17.534  34.141  10.213  1.00  9.56           C  
ANISOU 2832  CA  LEU C 159      907   1212   1512    -25     47   -464       C  
ATOM   2833  C   LEU C 159     -18.971  34.098   9.709  1.00 10.52           C  
ANISOU 2833  C   LEU C 159     1231   1582   1184    -28   -233   -136       C  
ATOM   2834  O   LEU C 159     -19.256  34.506   8.579  1.00 12.59           O  
ANISOU 2834  O   LEU C 159     1178   2215   1389    240   -346    360       O  
ATOM   2835  CB  LEU C 159     -17.028  35.582  10.289  1.00 11.44           C  
ANISOU 2835  CB  LEU C 159     1180   1194   1974     28    247   -820       C  
ATOM   2836  CG  LEU C 159     -17.459  36.400  11.517  1.00 15.72           C  
ANISOU 2836  CG  LEU C 159     1413   1726   2834    255    511   -862       C  
ATOM   2837  CD1 LEU C 159     -16.535  37.590  11.734  1.00 15.59           C  
ANISOU 2837  CD1 LEU C 159     1262   1834   2828   -241    672  -1104       C  
ATOM   2838  CD2 LEU C 159     -18.905  36.876  11.417  1.00 19.16           C  
ANISOU 2838  CD2 LEU C 159     1682   2305   3294    280    718   -990       C  
ATOM   2839  N   GLN C 160     -19.872  33.598  10.547  1.00 10.20           N  
ANISOU 2839  N   GLN C 160      922   1749   1202   -461   -171   -315       N  
ATOM   2840  CA  GLN C 160     -21.295  33.566  10.257  1.00 12.36           C  
ANISOU 2840  CA  GLN C 160     1282   1929   1485    229    -77   -552       C  
ATOM   2841  C   GLN C 160     -22.044  34.379  11.300  1.00 11.96           C  
ANISOU 2841  C   GLN C 160      912   1967   1666    334    174   -324       C  
ATOM   2842  O   GLN C 160     -21.688  34.371  12.483  1.00 12.03           O  
ANISOU 2842  O   GLN C 160     1295   1701   1575    -30    298   -109       O  
ATOM   2843  CB  GLN C 160     -21.834  32.136  10.243  1.00 15.74           C  
ANISOU 2843  CB  GLN C 160     1898   2007   2075   -127    191   -544       C  
ATOM   2844  CG  GLN C 160     -21.273  31.264   9.141  1.00 20.84           C  
ANISOU 2844  CG  GLN C 160     2816   2354   2748   -543     77   -347       C  
ATOM   2845  CD  GLN C 160     -21.896  29.885   9.137  1.00 26.71           C  
ANISOU 2845  CD  GLN C 160     3713   3030   3405   -507    -19      1       C  
ATOM   2846  OE1 GLN C 160     -21.329  28.935   9.676  1.00 29.64           O  
ANISOU 2846  OE1 GLN C 160     4140   3217   3904   -338     52    289       O  
ATOM   2847  NE2 GLN C 160     -23.075  29.770   8.535  1.00 28.13           N  
ANISOU 2847  NE2 GLN C 160     4056   3299   3333   -851   -180   -140       N  
ATOM   2848  N   LEU C 161     -23.075  35.082  10.851  1.00 10.68           N  
ANISOU 2848  N   LEU C 161      505   1764   1789    -81     92   -193       N  
ATOM   2849  CA  LEU C 161     -23.973  35.823  11.716  1.00 11.04           C  
ANISOU 2849  CA  LEU C 161      672   1623   1899   -142   -280   -429       C  
ATOM   2850  C   LEU C 161     -25.401  35.353  11.479  1.00 12.23           C  
ANISOU 2850  C   LEU C 161      644   1952   2052    -21    -70   -550       C  
ATOM   2851  O   LEU C 161     -25.744  34.952  10.362  1.00 14.55           O  
ANISOU 2851  O   LEU C 161      890   2471   2166   -200   -465   -381       O  
ATOM   2852  CB  LEU C 161     -23.868  37.332  11.456  1.00 12.49           C  
ANISOU 2852  CB  LEU C 161      814   1893   2037   -104   -579   -107       C  
ATOM   2853  CG  LEU C 161     -22.511  37.942  11.815  1.00 11.35           C  
ANISOU 2853  CG  LEU C 161      586   1913   1814    -76   -367    -17       C  
ATOM   2854  CD1 LEU C 161     -22.361  39.330  11.218  1.00 10.85           C  
ANISOU 2854  CD1 LEU C 161      513   1782   1827   -247    114     18       C  
ATOM   2855  CD2 LEU C 161     -22.341  37.989  13.328  1.00 14.69           C  
ANISOU 2855  CD2 LEU C 161      987   2455   2141    264   -682     86       C  
ATOM   2856  N   PRO C 162     -26.247  35.359  12.507  1.00 14.48           N  
ANISOU 2856  N   PRO C 162     1232   1862   2408    225    -74   -650       N  
ATOM   2857  CA  PRO C 162     -27.622  34.884  12.327  1.00 15.73           C  
ANISOU 2857  CA  PRO C 162     1165   2239   2573    -81   -172   -282       C  
ATOM   2858  C   PRO C 162     -28.380  35.734  11.319  1.00 17.33           C  
ANISOU 2858  C   PRO C 162     1065   2499   3021   -342   -647     72       C  
ATOM   2859  O   PRO C 162     -28.056  36.899  11.076  1.00 15.82           O  
ANISOU 2859  O   PRO C 162      824   2342   2846   -233   -360     66       O  
ATOM   2860  CB  PRO C 162     -28.230  34.997  13.730  1.00 15.35           C  
ANISOU 2860  CB  PRO C 162     1657   1956   2219    -37    178   -453       C  
ATOM   2861  CG  PRO C 162     -27.332  35.928  14.476  1.00 14.49           C  
ANISOU 2861  CG  PRO C 162     1382   1839   2286    136    337   -711       C  
ATOM   2862  CD  PRO C 162     -25.965  35.727  13.904  1.00 13.48           C  
ANISOU 2862  CD  PRO C 162     1352   1726   2043    499    376   -672       C  
ATOM   2863  N  AGLN C 163     -29.418  35.130  10.732  0.36 19.03           N  
ANISOU 2863  N  AGLN C 163     1406   2720   3104   -582   -852    -10       N  
ATOM   2864  N  BGLN C 163     -29.395  35.119  10.718  0.64 18.57           N  
ANISOU 2864  N  BGLN C 163     1460   2647   2949   -433   -980   -140       N  
ATOM   2865  CA AGLN C 163     -30.077  35.721   9.569  0.36 20.88           C  
ANISOU 2865  CA AGLN C 163     1711   3032   3191   -786   -823   -135       C  
ATOM   2866  CA BGLN C 163     -30.318  35.864   9.877  0.64 21.02           C  
ANISOU 2866  CA BGLN C 163     1865   2986   3137   -530  -1184   -341       C  
ATOM   2867  C  AGLN C 163     -30.660  37.101   9.858  0.36 19.76           C  
ANISOU 2867  C  AGLN C 163     1483   2939   3085   -894   -651   -117       C  
ATOM   2868  C  BGLN C 163     -31.057  36.895  10.719  0.64 20.58           C  
ANISOU 2868  C  BGLN C 163     1672   2939   3208   -143  -1123   -343       C  
ATOM   2869  O  AGLN C 163     -30.759  37.931   8.947  0.36 19.83           O  
ANISOU 2869  O  AGLN C 163     1301   2991   3242   -866   -446   -181       O  
ATOM   2870  O  BGLN C 163     -31.424  36.636  11.868  0.64 20.81           O  
ANISOU 2870  O  BGLN C 163     1420   3014   3475    270   -686   -233       O  
ATOM   2871  CB AGLN C 163     -31.174  34.784   9.058  0.36 23.81           C  
ANISOU 2871  CB AGLN C 163     2478   3260   3310   -596   -568   -233       C  
ATOM   2872  CB BGLN C 163     -31.306  34.915   9.198  0.64 24.97           C  
ANISOU 2872  CB BGLN C 163     2767   3230   3490   -748  -1083   -390       C  
ATOM   2873  CG AGLN C 163     -30.654  33.576   8.295  0.36 26.95           C  
ANISOU 2873  CG AGLN C 163     3172   3621   3448   -316   -369   -209       C  
ATOM   2874  CG BGLN C 163     -30.650  33.939   8.236  0.64 29.27           C  
ANISOU 2874  CG BGLN C 163     3767   3688   3664   -537   -875   -263       C  
ATOM   2875  CD AGLN C 163     -30.077  33.945   6.941  0.36 29.32           C  
ANISOU 2875  CD AGLN C 163     3657   3902   3582    -13   -249   -303       C  
ATOM   2876  CD BGLN C 163     -29.854  34.641   7.152  0.64 32.54           C  
ANISOU 2876  CD BGLN C 163     4484   4050   3829   -227   -842   -243       C  
ATOM   2877  OE1AGLN C 163     -30.708  34.654   6.156  0.36 29.54           O  
ANISOU 2877  OE1AGLN C 163     3615   4035   3576    -59   -488   -306       O  
ATOM   2878  OE1BGLN C 163     -30.334  35.588   6.526  0.64 33.53           O  
ANISOU 2878  OE1BGLN C 163     4820   4105   3815     72  -1012    -44       O  
ATOM   2879  NE2AGLN C 163     -28.868  33.469   6.662  0.36 30.45           N  
ANISOU 2879  NE2AGLN C 163     3897   3997   3677    170    -52   -394       N  
ATOM   2880  NE2BGLN C 163     -28.626  34.184   6.929  0.64 32.04           N  
ANISOU 2880  NE2BGLN C 163     4211   4111   3853   -327   -909   -419       N  
ATOM   2881  N  AGLY C 164     -31.048  37.370  11.102  0.36 19.96           N  
ANISOU 2881  N  AGLY C 164     1637   2880   3068   -975   -719    126       N  
ATOM   2882  N  BGLY C 164     -31.263  38.076  10.144  0.64 21.17           N  
ANISOU 2882  N  BGLY C 164     2052   2914   3077    228  -1131   -306       N  
ATOM   2883  CA AGLY C 164     -31.679  38.638  11.423  0.36 19.97           C  
ANISOU 2883  CA AGLY C 164     1898   2725   2966   -662   -816    435       C  
ATOM   2884  CA BGLY C 164     -31.830  39.187  10.869  0.64 21.70           C  
ANISOU 2884  CA BGLY C 164     2031   3101   3114    200  -1044   -146       C  
ATOM   2885  C  AGLY C 164     -30.741  39.681  11.997  0.36 19.99           C  
ANISOU 2885  C  AGLY C 164     1935   2766   2893   -409   -660    508       C  
ATOM   2886  C  BGLY C 164     -30.814  40.114  11.498  0.64 20.33           C  
ANISOU 2886  C  BGLY C 164     1598   3075   3054    274   -726    -20       C  
ATOM   2887  O  AGLY C 164     -31.115  40.420  12.913  0.36 21.58           O  
ANISOU 2887  O  AGLY C 164     2276   2998   2927   -359   -491    762       O  
ATOM   2888  O  BGLY C 164     -31.205  41.160  12.034  0.64 20.43           O  
ANISOU 2888  O  BGLY C 164     1348   3303   3114    969   -227    -28       O  
ATOM   2889  N   THR C 165     -29.529  39.766  11.458  1.00 19.00           N  
ANISOU 2889  N   THR C 165     1565   2780   2874     54   -497    340       N  
ATOM   2890  CA  THR C 165     -28.499  40.663  11.969  1.00 15.45           C  
ANISOU 2890  CA  THR C 165      952   2224   2695   -391   -390    386       C  
ATOM   2891  C   THR C 165     -28.420  41.912  11.103  1.00 16.06           C  
ANISOU 2891  C   THR C 165     1116   2528   2457     86   -266    357       C  
ATOM   2892  O   THR C 165     -28.307  41.822   9.876  1.00 18.06           O  
ANISOU 2892  O   THR C 165     1728   2701   2435    363     18    196       O  
ATOM   2893  CB  THR C 165     -27.135  39.970  12.001  1.00 13.20           C  
ANISOU 2893  CB  THR C 165      833   1915   2269   -560     96    143       C  
ATOM   2894  OG1 THR C 165     -27.177  38.853  12.898  1.00 16.63           O  
ANISOU 2894  OG1 THR C 165     1301   2389   2627   -556    -38    252       O  
ATOM   2895  CG2 THR C 165     -26.058  40.945  12.466  1.00 11.94           C  
ANISOU 2895  CG2 THR C 165      574   1811   2149   -192     -7    101       C  
ATOM   2896  N   THR C 166     -28.478  43.077  11.744  1.00 14.79           N  
ANISOU 2896  N   THR C 166      962   2307   2350    523   -189    163       N  
ATOM   2897  CA  THR C 166     -28.353  44.348  11.041  1.00 17.82           C  
ANISOU 2897  CA  THR C 166     1580   2733   2459    407    192     57       C  
ATOM   2898  C   THR C 166     -26.885  44.611  10.727  1.00 17.14           C  
ANISOU 2898  C   THR C 166     1706   2651   2156    164    548   -178       C  
ATOM   2899  O   THR C 166     -26.046  44.641  11.634  1.00 18.78           O  
ANISOU 2899  O   THR C 166     1886   3032   2216    216    751   -253       O  
ATOM   2900  CB  THR C 166     -28.930  45.487  11.879  1.00 19.89           C  
ANISOU 2900  CB  THR C 166     2086   2762   2711    129    416     -9       C  
ATOM   2901  OG1 THR C 166     -30.334  45.279  12.072  1.00 22.09           O  
ANISOU 2901  OG1 THR C 166     2187   3303   2903    222    571   -141       O  
ATOM   2902  CG2 THR C 166     -28.713  46.823  11.183  1.00 22.10           C  
ANISOU 2902  CG2 THR C 166     2707   2701   2990    119    109     50       C  
ATOM   2903  N   LEU C 167     -26.575  44.790   9.447  1.00 15.70           N  
ANISOU 2903  N   LEU C 167     1990   2019   1956    346    425    215       N  
ATOM   2904  CA  LEU C 167     -25.227  45.139   9.036  1.00 15.52           C  
ANISOU 2904  CA  LEU C 167     1990   2039   1867    653    427    -75       C  
ATOM   2905  C   LEU C 167     -25.203  46.537   8.436  1.00 15.21           C  
ANISOU 2905  C   LEU C 167     1737   2193   1849   1052    246     88       C  
ATOM   2906  O   LEU C 167     -26.151  46.929   7.746  1.00 18.08           O  
ANISOU 2906  O   LEU C 167     2258   2590   2021   1417     66    311       O  
ATOM   2907  CB  LEU C 167     -24.679  44.144   8.004  1.00 17.29           C  
ANISOU 2907  CB  LEU C 167     2513   2077   1981    578    568   -187       C  
ATOM   2908  CG  LEU C 167     -24.282  42.755   8.504  1.00 17.93           C  
ANISOU 2908  CG  LEU C 167     2883   2016   1913    570    547   -142       C  
ATOM   2909  CD1 LEU C 167     -23.951  41.847   7.332  1.00 18.66           C  
ANISOU 2909  CD1 LEU C 167     3116   2033   1940    543    560   -381       C  
ATOM   2910  CD2 LEU C 167     -23.098  42.850   9.449  1.00 17.81           C  
ANISOU 2910  CD2 LEU C 167     3032   2054   1683    550    275    116       C  
ATOM   2911  N   PRO C 168     -24.147  47.312   8.678  1.00 13.92           N  
ANISOU 2911  N   PRO C 168     1567   1943   1778    533    274    -13       N  
ATOM   2912  CA  PRO C 168     -24.017  48.603   7.998  1.00 15.45           C  
ANISOU 2912  CA  PRO C 168     1880   2141   1849    606    260     85       C  
ATOM   2913  C   PRO C 168     -23.871  48.404   6.498  1.00 15.84           C  
ANISOU 2913  C   PRO C 168     1995   2019   2006    870    100    270       C  
ATOM   2914  O   PRO C 168     -23.456  47.344   6.023  1.00 14.29           O  
ANISOU 2914  O   PRO C 168     1457   1995   1977    529    196    346       O  
ATOM   2915  CB  PRO C 168     -22.743  49.208   8.606  1.00 14.82           C  
ANISOU 2915  CB  PRO C 168     1940   1878   1811    234     36     76       C  
ATOM   2916  CG  PRO C 168     -22.480  48.414   9.852  1.00 15.20           C  
ANISOU 2916  CG  PRO C 168     2013   1812   1950    235    321    104       C  
ATOM   2917  CD  PRO C 168     -23.015  47.044   9.579  1.00 14.29           C  
ANISOU 2917  CD  PRO C 168     1635   1927   1868     85    171    156       C  
ATOM   2918  N   LYS C 169     -24.231  49.443   5.748  1.00 17.77           N  
ANISOU 2918  N   LYS C 169     2508   1962   2283   1166    -75    543       N  
ATOM   2919  CA  LYS C 169     -24.080  49.401   4.300  1.00 21.02           C  
ANISOU 2919  CA  LYS C 169     2927   2456   2605   1519    -58    434       C  
ATOM   2920  C   LYS C 169     -22.628  49.130   3.930  1.00 19.01           C  
ANISOU 2920  C   LYS C 169     2755   2052   2415   1380    195    262       C  
ATOM   2921  O   LYS C 169     -21.710  49.755   4.468  1.00 19.25           O  
ANISOU 2921  O   LYS C 169     2902   2037   2376   1092    503   -105       O  
ATOM   2922  CB  LYS C 169     -24.553  50.715   3.679  1.00 26.19           C  
ANISOU 2922  CB  LYS C 169     3643   3118   3191   1888   -305    440       C  
ATOM   2923  CG  LYS C 169     -26.047  50.965   3.833  1.00 33.57           C  
ANISOU 2923  CG  LYS C 169     4841   4027   3886   2317   -468    362       C  
ATOM   2924  CD  LYS C 169     -26.473  52.254   3.146  1.00 39.08           C  
ANISOU 2924  CD  LYS C 169     5410   5005   4435   2317   -653    519       C  
ATOM   2925  CE  LYS C 169     -27.967  52.502   3.316  1.00 42.59           C  
ANISOU 2925  CE  LYS C 169     5732   5547   4903   2452   -535    612       C  
ATOM   2926  NZ  LYS C 169     -28.409  53.752   2.634  1.00 45.36           N  
ANISOU 2926  NZ  LYS C 169     6139   5991   5106   2406   -406    625       N  
ATOM   2927  N   GLY C 170     -22.422  48.179   3.023  1.00 17.45           N  
ANISOU 2927  N   GLY C 170     2474   1947   2209   1169   -110    281       N  
ATOM   2928  CA  GLY C 170     -21.097  47.791   2.596  1.00 15.95           C  
ANISOU 2928  CA  GLY C 170     2198   1789   2074   1168    -54    122       C  
ATOM   2929  C   GLY C 170     -20.555  46.542   3.258  1.00 13.65           C  
ANISOU 2929  C   GLY C 170     1733   1624   1830    746    -64   -104       C  
ATOM   2930  O   GLY C 170     -19.470  46.085   2.880  1.00 15.26           O  
ANISOU 2930  O   GLY C 170     2131   1899   1766    562    117   -181       O  
ATOM   2931  N   PHE C 171     -21.267  45.985   4.234  1.00 12.22           N  
ANISOU 2931  N   PHE C 171     1116   2012   1514    395    265   -139       N  
ATOM   2932  CA  PHE C 171     -20.879  44.741   4.886  1.00 12.04           C  
ANISOU 2932  CA  PHE C 171     1458   1764   1354    313    128    -31       C  
ATOM   2933  C   PHE C 171     -21.813  43.622   4.452  1.00 12.90           C  
ANISOU 2933  C   PHE C 171     1660   1645   1596    339    182   -237       C  
ATOM   2934  O   PHE C 171     -23.022  43.832   4.303  1.00 13.71           O  
ANISOU 2934  O   PHE C 171     1709   1518   1983    -63    445   -384       O  
ATOM   2935  CB  PHE C 171     -20.911  44.875   6.410  1.00 10.89           C  
ANISOU 2935  CB  PHE C 171     1493   1757    888    580    328    -96       C  
ATOM   2936  CG  PHE C 171     -19.799  45.712   6.971  1.00 12.44           C  
ANISOU 2936  CG  PHE C 171     1593   1903   1231    436    399      6       C  
ATOM   2937  CD1 PHE C 171     -18.578  45.140   7.288  1.00 12.05           C  
ANISOU 2937  CD1 PHE C 171     1515   1767   1295    963    146     20       C  
ATOM   2938  CD2 PHE C 171     -19.978  47.069   7.192  1.00 11.95           C  
ANISOU 2938  CD2 PHE C 171     1701   1571   1268     43    401     56       C  
ATOM   2939  CE1 PHE C 171     -17.550  45.907   7.811  1.00 12.22           C  
ANISOU 2939  CE1 PHE C 171     1405   1838   1401    531    270    122       C  
ATOM   2940  CE2 PHE C 171     -18.955  47.841   7.716  1.00 12.91           C  
ANISOU 2940  CE2 PHE C 171     1391   2063   1450    184     28    185       C  
ATOM   2941  CZ  PHE C 171     -17.742  47.258   8.028  1.00 12.25           C  
ANISOU 2941  CZ  PHE C 171     1167   1970   1519    264    191     97       C  
ATOM   2942  N   TYR C 172     -21.250  42.432   4.255  1.00 11.51           N  
ANISOU 2942  N   TYR C 172     1721   1018   1636    499    109   -254       N  
ATOM   2943  CA  TYR C 172     -22.002  41.292   3.749  1.00 13.69           C  
ANISOU 2943  CA  TYR C 172     1723   1902   1577    350   -226   -510       C  
ATOM   2944  C   TYR C 172     -21.626  40.046   4.530  1.00 15.74           C  
ANISOU 2944  C   TYR C 172     2290   1838   1854    -75      4   -418       C  
ATOM   2945  O   TYR C 172     -20.444  39.804   4.793  1.00 16.42           O  
ANISOU 2945  O   TYR C 172     2529   1810   1900    107     26   -114       O  
ATOM   2946  CB  TYR C 172     -21.740  41.086   2.251  1.00 13.13           C  
ANISOU 2946  CB  TYR C 172     1624   1949   1417    409   -196   -461       C  
ATOM   2947  CG  TYR C 172     -22.064  42.317   1.445  1.00 14.34           C  
ANISOU 2947  CG  TYR C 172     1849   2168   1430    678     54   -352       C  
ATOM   2948  CD1 TYR C 172     -23.345  42.534   0.960  1.00 15.24           C  
ANISOU 2948  CD1 TYR C 172     1664   2734   1390    524      6   -469       C  
ATOM   2949  CD2 TYR C 172     -21.096  43.283   1.200  1.00 14.54           C  
ANISOU 2949  CD2 TYR C 172     1520   2434   1570    156    206     -6       C  
ATOM   2950  CE1 TYR C 172     -23.650  43.672   0.237  1.00 17.94           C  
ANISOU 2950  CE1 TYR C 172     2184   3005   1629    238    337   -252       C  
ATOM   2951  CE2 TYR C 172     -21.392  44.422   0.483  1.00 16.55           C  
ANISOU 2951  CE2 TYR C 172     1852   2735   1700    -74    181    -59       C  
ATOM   2952  CZ  TYR C 172     -22.668  44.611   0.001  1.00 17.91           C  
ANISOU 2952  CZ  TYR C 172     2288   2798   1721    -62     71    -55       C  
ATOM   2953  OH  TYR C 172     -22.961  45.745  -0.717  1.00 19.58           O  
ANISOU 2953  OH  TYR C 172     2674   2835   1931    197   -253    309       O  
ATOM   2954  N   ALA C 173     -22.634  39.263   4.897  1.00 17.97           N  
ANISOU 2954  N   ALA C 173     2648   2055   2126   -344    160   -417       N  
ATOM   2955  CA  ALA C 173     -22.426  38.022   5.629  1.00 22.90           C  
ANISOU 2955  CA  ALA C 173     3558   2467   2674   -881   -399    -48       C  
ATOM   2956  C   ALA C 173     -23.643  37.117   5.472  1.00 29.63           C  
ANISOU 2956  C   ALA C 173     4659   3108   3490  -1301   -585    607       C  
ATOM   2957  O   ALA C 173     -24.691  37.547   4.985  1.00 31.47           O  
ANISOU 2957  O   ALA C 173     4756   3498   3705  -1644   -511    803       O  
ATOM   2958  CB  ALA C 173     -22.151  38.305   7.098  1.00 21.56           C  
ANISOU 2958  CB  ALA C 173     3529   2123   2542   -843   -850   -285       C  
ATOM   2959  OXT ALA C 173     -23.611  35.937   5.821  1.00 32.33           O  
ANISOU 2959  OXT ALA C 173     5348   3135   3801  -1686   -950    891       O  
TER    2960      ALA C 173                                                      
ATOM   2961  N   THR D  49      -1.045  30.324  -3.127  1.00 41.41           N  
ANISOU 2961  N   THR D  49     4965   6406   4363  -1371    -32  -1435       N  
ATOM   2962  CA  THR D  49      -1.786  30.991  -4.193  1.00 42.31           C  
ANISOU 2962  CA  THR D  49     5008   6421   4646  -1049    418  -1253       C  
ATOM   2963  C   THR D  49      -2.883  30.091  -4.747  1.00 36.57           C  
ANISOU 2963  C   THR D  49     4324   5486   4086   -677    529  -1226       C  
ATOM   2964  O   THR D  49      -2.928  29.814  -5.948  1.00 38.90           O  
ANISOU 2964  O   THR D  49     4675   5685   4420   -156    985  -1110       O  
ATOM   2965  CB  THR D  49      -0.863  31.412  -5.348  1.00 47.60           C  
ANISOU 2965  CB  THR D  49     5732   7017   5338  -1035    784  -1008       C  
ATOM   2966  OG1 THR D  49      -0.120  30.275  -5.807  1.00 51.39           O  
ANISOU 2966  OG1 THR D  49     6334   7500   5692   -806   1016   -814       O  
ATOM   2967  CG2 THR D  49       0.092  32.499  -4.899  1.00 48.56           C  
ANISOU 2967  CG2 THR D  49     5956   6973   5522  -1187    825   -971       C  
ATOM   2968  N   ALA D  50      -3.768  29.640  -3.869  1.00 26.30           N  
ANISOU 2968  N   ALA D  50     2881   4063   3051   -432    413  -1050       N  
ATOM   2969  CA  ALA D  50      -4.822  28.710  -4.235  1.00 17.73           C  
ANISOU 2969  CA  ALA D  50     1394   2988   2353     89    137   -390       C  
ATOM   2970  C   ALA D  50      -6.135  29.444  -4.482  1.00 10.98           C  
ANISOU 2970  C   ALA D  50      661   1914   1597    406   -117   -236       C  
ATOM   2971  O   ALA D  50      -6.323  30.593  -4.075  1.00  9.86           O  
ANISOU 2971  O   ALA D  50      715   1803   1229    513    -20   -159       O  
ATOM   2972  CB  ALA D  50      -5.010  27.655  -3.143  1.00 18.25           C  
ANISOU 2972  CB  ALA D  50     1862   2687   2384    554     88    -73       C  
ATOM   2973  N   SER D  51      -7.040  28.761  -5.177  1.00  8.54           N  
ANISOU 2973  N   SER D  51      588   1401   1254    132   -421     59       N  
ATOM   2974  CA  SER D  51      -8.404  29.246  -5.309  1.00  7.56           C  
ANISOU 2974  CA  SER D  51      401   1497    976    -45   -120     -5       C  
ATOM   2975  C   SER D  51      -9.091  29.249  -3.950  1.00  9.07           C  
ANISOU 2975  C   SER D  51      570   1737   1138    263   -207     42       C  
ATOM   2976  O   SER D  51      -8.820  28.407  -3.089  1.00  9.54           O  
ANISOU 2976  O   SER D  51      815   1622   1187    382   -381    135       O  
ATOM   2977  CB  SER D  51      -9.186  28.367  -6.287  1.00  7.23           C  
ANISOU 2977  CB  SER D  51      428   1474    846   -143    106   -241       C  
ATOM   2978  OG  SER D  51     -10.576  28.650  -6.238  1.00  7.89           O  
ANISOU 2978  OG  SER D  51      626   1344   1028    -15    433     77       O  
ATOM   2979  N   TRP D  52      -9.994  30.211  -3.758  1.00  9.38           N  
ANISOU 2979  N   TRP D  52      652   1675   1238    183    383   -103       N  
ATOM   2980  CA  TRP D  52     -10.807  30.219  -2.548  1.00  8.22           C  
ANISOU 2980  CA  TRP D  52     1006    875   1243    456     -9     73       C  
ATOM   2981  C   TRP D  52     -11.809  29.075  -2.501  1.00 10.25           C  
ANISOU 2981  C   TRP D  52     1271   1190   1434    312     36     27       C  
ATOM   2982  O   TRP D  52     -12.355  28.802  -1.426  1.00 11.65           O  
ANISOU 2982  O   TRP D  52     1924   1158   1342   -283    124    151       O  
ATOM   2983  CB  TRP D  52     -11.545  31.553  -2.414  1.00  8.14           C  
ANISOU 2983  CB  TRP D  52     1104    805   1182    100    -45     15       C  
ATOM   2984  CG  TRP D  52     -10.682  32.636  -1.864  1.00  9.41           C  
ANISOU 2984  CG  TRP D  52     1404    813   1358    203   -308    -57       C  
ATOM   2985  CD1 TRP D  52     -10.117  33.668  -2.555  1.00  9.61           C  
ANISOU 2985  CD1 TRP D  52     1459    705   1488     90    -96   -515       C  
ATOM   2986  CD2 TRP D  52     -10.261  32.783  -0.504  1.00 10.02           C  
ANISOU 2986  CD2 TRP D  52     1426   1096   1284    158   -397   -179       C  
ATOM   2987  NE1 TRP D  52      -9.378  34.456  -1.704  1.00 11.52           N  
ANISOU 2987  NE1 TRP D  52     1399   1305   1675    220    -97   -567       N  
ATOM   2988  CE2 TRP D  52      -9.450  33.932  -0.439  1.00 12.44           C  
ANISOU 2988  CE2 TRP D  52     1665   1565   1495    195   -391   -368       C  
ATOM   2989  CE3 TRP D  52     -10.496  32.057   0.667  1.00 11.59           C  
ANISOU 2989  CE3 TRP D  52     1552   1389   1463    293   -454   -140       C  
ATOM   2990  CZ2 TRP D  52      -8.871  34.371   0.750  1.00 13.77           C  
ANISOU 2990  CZ2 TRP D  52     1964   1713   1555    387   -284   -178       C  
ATOM   2991  CZ3 TRP D  52      -9.922  32.495   1.847  1.00 11.97           C  
ANISOU 2991  CZ3 TRP D  52     1846    961   1742    456   -483   -485       C  
ATOM   2992  CH2 TRP D  52      -9.118  33.640   1.879  1.00 14.03           C  
ANISOU 2992  CH2 TRP D  52     1949   1435   1946    583   -293   -191       C  
ATOM   2993  N   PHE D  53     -12.049  28.392  -3.618  1.00  9.36           N  
ANISOU 2993  N   PHE D  53     1406    791   1358    212   -208   -160       N  
ATOM   2994  CA  PHE D  53     -13.108  27.402  -3.714  1.00 10.58           C  
ANISOU 2994  CA  PHE D  53     1096   1431   1491    726     26   -143       C  
ATOM   2995  C   PHE D  53     -12.559  26.051  -4.158  1.00  9.80           C  
ANISOU 2995  C   PHE D  53     1220   1214   1290    705    -24    183       C  
ATOM   2996  O   PHE D  53     -11.475  25.954  -4.740  1.00  9.72           O  
ANISOU 2996  O   PHE D  53      884   1499   1308    514    -39    448       O  
ATOM   2997  CB  PHE D  53     -14.200  27.861  -4.690  1.00  7.65           C  
ANISOU 2997  CB  PHE D  53      709   1115   1081    484    165     64       C  
ATOM   2998  CG  PHE D  53     -14.749  29.225  -4.385  1.00  9.22           C  
ANISOU 2998  CG  PHE D  53      785   1418   1298    370    118   -190       C  
ATOM   2999  CD1 PHE D  53     -15.826  29.377  -3.526  1.00 11.34           C  
ANISOU 2999  CD1 PHE D  53     1212   1591   1505     19    304   -321       C  
ATOM   3000  CD2 PHE D  53     -14.182  30.356  -4.950  1.00  8.29           C  
ANISOU 3000  CD2 PHE D  53      536   1319   1297    291   -225   -229       C  
ATOM   3001  CE1 PHE D  53     -16.332  30.633  -3.239  1.00 13.62           C  
ANISOU 3001  CE1 PHE D  53     1680   1981   1515    -27      8   -435       C  
ATOM   3002  CE2 PHE D  53     -14.681  31.616  -4.670  1.00  9.31           C  
ANISOU 3002  CE2 PHE D  53      783   1461   1294    533   -189   -316       C  
ATOM   3003  CZ  PHE D  53     -15.758  31.755  -3.811  1.00 12.20           C  
ANISOU 3003  CZ  PHE D  53     1579   1725   1332    279     10    -79       C  
ATOM   3004  N   THR D  54     -13.330  25.004  -3.869  1.00  8.17           N  
ANISOU 3004  N   THR D  54     1237    808   1061    203    300     57       N  
ATOM   3005  CA  THR D  54     -13.052  23.688  -4.422  1.00  7.83           C  
ANISOU 3005  CA  THR D  54     1068    988    920   -296    332    348       C  
ATOM   3006  C   THR D  54     -13.319  23.694  -5.927  1.00  9.39           C  
ANISOU 3006  C   THR D  54     1310   1331    929   -429    174     66       C  
ATOM   3007  O   THR D  54     -13.936  24.613  -6.473  1.00  8.40           O  
ANISOU 3007  O   THR D  54      861   1294   1038   -165    434    144       O  
ATOM   3008  CB  THR D  54     -13.899  22.621  -3.728  1.00 10.04           C  
ANISOU 3008  CB  THR D  54     1259   1662    892    118   -163    415       C  
ATOM   3009  OG1 THR D  54     -15.289  22.944  -3.865  1.00 10.36           O  
ANISOU 3009  OG1 THR D  54     1189   1813    934    232    -15    490       O  
ATOM   3010  CG2 THR D  54     -13.538  22.536  -2.249  1.00 12.62           C  
ANISOU 3010  CG2 THR D  54     1705   1928   1163     41    368    758       C  
ATOM   3011  N   ALA D  55     -12.849  22.649  -6.601  1.00 12.46           N  
ANISOU 3011  N   ALA D  55     2030   1757    947    -84     11    -46       N  
ATOM   3012  CA  ALA D  55     -12.847  22.627  -8.056  1.00 10.71           C  
ANISOU 3012  CA  ALA D  55     1370   1699   1001    290    403    164       C  
ATOM   3013  C   ALA D  55     -14.082  21.933  -8.620  1.00  9.63           C  
ANISOU 3013  C   ALA D  55     1325   1189   1146     85    433   -126       C  
ATOM   3014  O   ALA D  55     -14.792  21.196  -7.930  1.00 11.40           O  
ANISOU 3014  O   ALA D  55     1261   1557   1514    163    518    -15       O  
ATOM   3015  CB  ALA D  55     -11.592  21.932  -8.583  1.00  9.86           C  
ANISOU 3015  CB  ALA D  55     1209   1416   1122    496     26   -127       C  
ATOM   3016  N   LEU D  56     -14.329  22.187  -9.902  1.00  8.50           N  
ANISOU 3016  N   LEU D  56      869   1095   1265     68    198   -381       N  
ATOM   3017  CA  LEU D  56     -15.264  21.408 -10.700  1.00 10.93           C  
ANISOU 3017  CA  LEU D  56     1301   1279   1572    360    268   -119       C  
ATOM   3018  C   LEU D  56     -14.461  20.438 -11.554  1.00 10.31           C  
ANISOU 3018  C   LEU D  56     1295    989   1632    278    404   -193       C  
ATOM   3019  O   LEU D  56     -13.463  20.828 -12.168  1.00 11.98           O  
ANISOU 3019  O   LEU D  56     1681   1153   1720   -234    762   -231       O  
ATOM   3020  CB  LEU D  56     -16.126  22.310 -11.587  1.00 10.43           C  
ANISOU 3020  CB  LEU D  56     1029   1140   1792    504    148     74       C  
ATOM   3021  CG  LEU D  56     -16.996  23.359 -10.891  1.00 11.32           C  
ANISOU 3021  CG  LEU D  56     1238   1221   1842    632    350    401       C  
ATOM   3022  CD1 LEU D  56     -17.754  24.194 -11.923  1.00 12.90           C  
ANISOU 3022  CD1 LEU D  56      962   1756   2183    636    165    236       C  
ATOM   3023  CD2 LEU D  56     -17.956  22.701  -9.906  1.00 14.08           C  
ANISOU 3023  CD2 LEU D  56     1694   1367   2289    416    615    445       C  
ATOM   3024  N   THR D  57     -14.886  19.180 -11.585  1.00  8.04           N  
ANISOU 3024  N   THR D  57      767    788   1501    190    -62    381       N  
ATOM   3025  CA  THR D  57     -14.146  18.131 -12.274  1.00  8.41           C  
ANISOU 3025  CA  THR D  57     1288    629   1278    420   -188    108       C  
ATOM   3026  C   THR D  57     -14.804  17.804 -13.610  1.00 11.65           C  
ANISOU 3026  C   THR D  57     1911   1067   1447    413    -24     89       C  
ATOM   3027  O   THR D  57     -16.003  17.511 -13.665  1.00 10.58           O  
ANISOU 3027  O   THR D  57     1320   1239   1461     98    -28    166       O  
ATOM   3028  CB  THR D  57     -14.055  16.879 -11.402  1.00  9.64           C  
ANISOU 3028  CB  THR D  57     1570    722   1370    527   -151    -69       C  
ATOM   3029  OG1 THR D  57     -13.345  17.195 -10.198  1.00 12.70           O  
ANISOU 3029  OG1 THR D  57     2137   1143   1546    638   -282    -65       O  
ATOM   3030  CG2 THR D  57     -13.319  15.775 -12.135  1.00 12.25           C  
ANISOU 3030  CG2 THR D  57     2015    774   1864    407   -273   -344       C  
ATOM   3031  N   GLN D  58     -14.010  17.851 -14.680  1.00 10.77           N  
ANISOU 3031  N   GLN D  58     2040   1169    883    145    149    -89       N  
ATOM   3032  CA  GLN D  58     -14.496  17.611 -16.039  1.00 10.32           C  
ANISOU 3032  CA  GLN D  58     1872   1151    898     60    -70    -26       C  
ATOM   3033  C   GLN D  58     -14.365  16.128 -16.362  1.00 13.05           C  
ANISOU 3033  C   GLN D  58     2062   1425   1470     42    -24     52       C  
ATOM   3034  O   GLN D  58     -13.279  15.648 -16.696  1.00 13.93           O  
ANISOU 3034  O   GLN D  58     2029   1548   1717     84    141     90       O  
ATOM   3035  CB  GLN D  58     -13.722  18.456 -17.045  1.00 10.32           C  
ANISOU 3035  CB  GLN D  58     2084   1014    822    336    -97   -110       C  
ATOM   3036  CG  GLN D  58     -14.202  18.277 -18.482  1.00 12.51           C  
ANISOU 3036  CG  GLN D  58     2309   1765    678   -183     25   -313       C  
ATOM   3037  CD  GLN D  58     -13.304  18.951 -19.505  1.00 15.53           C  
ANISOU 3037  CD  GLN D  58     3046   1873    980    -99   -120   -235       C  
ATOM   3038  OE1 GLN D  58     -12.617  19.927 -19.202  1.00 14.22           O  
ANISOU 3038  OE1 GLN D  58     2801   1617    986   -138   -162   -235       O  
ATOM   3039  NE2 GLN D  58     -13.304  18.425 -20.728  1.00 16.87           N  
ANISOU 3039  NE2 GLN D  58     3224   1931   1257    199     51   -388       N  
ATOM   3040  N   HIS D  59     -15.476  15.397 -16.270  1.00 14.11           N  
ANISOU 3040  N   HIS D  59     2495   1256   1611   -448   -327   -201       N  
ATOM   3041  CA  HIS D  59     -15.505  14.014 -16.731  1.00 12.61           C  
ANISOU 3041  CA  HIS D  59     2225   1128   1438   -236    -53    -99       C  
ATOM   3042  C   HIS D  59     -15.817  13.902 -18.216  1.00 14.73           C  
ANISOU 3042  C   HIS D  59     2636   1456   1504    290   -258   -432       C  
ATOM   3043  O   HIS D  59     -15.373  12.948 -18.864  1.00 17.02           O  
ANISOU 3043  O   HIS D  59     3006   1786   1675    197   -262   -376       O  
ATOM   3044  CB  HIS D  59     -16.537  13.205 -15.942  1.00 10.31           C  
ANISOU 3044  CB  HIS D  59     1877    796   1243   -402     49    189       C  
ATOM   3045  CG  HIS D  59     -16.123  12.897 -14.538  1.00 11.05           C  
ANISOU 3045  CG  HIS D  59     1679    935   1584   -314    118     12       C  
ATOM   3046  ND1 HIS D  59     -15.741  11.636 -14.135  1.00  9.31           N  
ANISOU 3046  ND1 HIS D  59     1269    767   1504   -325    417    -64       N  
ATOM   3047  CD2 HIS D  59     -16.032  13.686 -13.442  1.00 13.41           C  
ANISOU 3047  CD2 HIS D  59     1770   1444   1882    -49    208   -120       C  
ATOM   3048  CE1 HIS D  59     -15.436  11.660 -12.851  1.00 10.89           C  
ANISOU 3048  CE1 HIS D  59     1371    804   1962   -304    315   -322       C  
ATOM   3049  NE2 HIS D  59     -15.603  12.892 -12.406  1.00 12.32           N  
ANISOU 3049  NE2 HIS D  59     1593   1050   2037    -38    313    -22       N  
ATOM   3050  N   GLY D  60     -16.571  14.851 -18.765  1.00 16.66           N  
ANISOU 3050  N   GLY D  60     3096   1461   1774    403   -175   -200       N  
ATOM   3051  CA  GLY D  60     -16.946  14.827 -20.162  1.00 16.87           C  
ANISOU 3051  CA  GLY D  60     2912   1751   1746    223   -278   -349       C  
ATOM   3052  C   GLY D  60     -15.865  15.400 -21.057  1.00 18.44           C  
ANISOU 3052  C   GLY D  60     2949   2239   1819    427   -573   -467       C  
ATOM   3053  O   GLY D  60     -14.750  15.707 -20.633  1.00 16.22           O  
ANISOU 3053  O   GLY D  60     2066   2189   1907    466   -556   -483       O  
ATOM   3054  N   LYS D  61     -16.217  15.551 -22.332  1.00 20.93           N  
ANISOU 3054  N   LYS D  61     3401   2355   2195    258   -900   -551       N  
ATOM   3055  CA  LYS D  61     -15.272  16.005 -23.343  1.00 24.11           C  
ANISOU 3055  CA  LYS D  61     4030   2624   2505    414   -523   -307       C  
ATOM   3056  C   LYS D  61     -15.398  17.487 -23.672  1.00 23.68           C  
ANISOU 3056  C   LYS D  61     3944   2470   2583    567   -179   -202       C  
ATOM   3057  O   LYS D  61     -14.609  17.996 -24.473  1.00 25.62           O  
ANISOU 3057  O   LYS D  61     4310   2564   2858    594     29    189       O  
ATOM   3058  CB  LYS D  61     -15.438  15.178 -24.623  1.00 28.80           C  
ANISOU 3058  CB  LYS D  61     4802   2911   3229    764   -333     40       C  
ATOM   3059  CG  LYS D  61     -15.157  13.696 -24.430  1.00 33.64           C  
ANISOU 3059  CG  LYS D  61     5231   3627   3922    972   -333    335       C  
ATOM   3060  CD  LYS D  61     -13.851  13.497 -23.676  1.00 38.43           C  
ANISOU 3060  CD  LYS D  61     5616   4336   4649   1702    -33    652       C  
ATOM   3061  CE  LYS D  61     -13.676  12.058 -23.220  1.00 41.38           C  
ANISOU 3061  CE  LYS D  61     5825   4842   5054   2095     -4    960       C  
ATOM   3062  NZ  LYS D  61     -12.562  11.928 -22.238  1.00 42.57           N  
ANISOU 3062  NZ  LYS D  61     5820   5114   5241   2261   -110    918       N  
ATOM   3063  N  AGLU D  62     -16.356  18.190 -23.075  0.59 25.01           N  
ANISOU 3063  N  AGLU D  62     4047   2826   2630    372   -375   -226       N  
ATOM   3064  N  BGLU D  62     -16.357  18.190 -23.077  0.41 24.45           N  
ANISOU 3064  N  BGLU D  62     3937   2750   2602    297   -317   -144       N  
ATOM   3065  CA AGLU D  62     -16.597  19.596 -23.370  0.59 24.48           C  
ANISOU 3065  CA AGLU D  62     3862   2800   2641    168   -356   -204       C  
ATOM   3066  CA BGLU D  62     -16.593  19.596 -23.371  0.41 23.89           C  
ANISOU 3066  CA BGLU D  62     3752   2737   2588     28   -289    -14       C  
ATOM   3067  C  AGLU D  62     -15.923  20.485 -22.332  0.59 21.98           C  
ANISOU 3067  C  AGLU D  62     3570   2486   2296    -32   -171    104       C  
ATOM   3068  C  BGLU D  62     -15.911  20.480 -22.335  0.41 21.94           C  
ANISOU 3068  C  BGLU D  62     3497   2481   2358    -67   -148    162       C  
ATOM   3069  O  AGLU D  62     -15.927  20.178 -21.136  0.59 20.03           O  
ANISOU 3069  O  AGLU D  62     3397   2396   1818   -278     56     86       O  
ATOM   3070  O  BGLU D  62     -15.899  20.162 -21.142  0.41 20.72           O  
ANISOU 3070  O  BGLU D  62     3353   2438   2082   -229    -18    163       O  
ATOM   3071  CB AGLU D  62     -18.098  19.894 -23.409  0.59 27.43           C  
ANISOU 3071  CB AGLU D  62     3971   3308   3144    421   -594   -543       C  
ATOM   3072  CB BGLU D  62     -18.091  19.909 -23.405  0.41 26.00           C  
ANISOU 3072  CB BGLU D  62     3849   3121   2910     76   -463    -88       C  
ATOM   3073  CG AGLU D  62     -18.861  19.117 -24.470  0.59 31.50           C  
ANISOU 3073  CG AGLU D  62     4408   3945   3617    595   -647   -858       C  
ATOM   3074  CG BGLU D  62     -18.886  19.107 -24.425  0.41 29.00           C  
ANISOU 3074  CG BGLU D  62     4208   3611   3198     90   -525   -131       C  
ATOM   3075  CD AGLU D  62     -20.358  19.363 -24.413  0.59 35.84           C  
ANISOU 3075  CD AGLU D  62     5014   4607   3997    587   -747  -1057       C  
ATOM   3076  CD BGLU D  62     -19.281  17.734 -23.914  0.41 32.13           C  
ANISOU 3076  CD BGLU D  62     4723   4096   3390    -17   -644    -36       C  
ATOM   3077  OE1AGLU D  62     -20.797  20.193 -23.588  0.59 37.48           O  
ANISOU 3077  OE1AGLU D  62     5304   4834   4102    649   -790  -1141       O  
ATOM   3078  OE1BGLU D  62     -19.014  17.438 -22.730  0.41 33.52           O  
ANISOU 3078  OE1BGLU D  62     5000   4292   3443    -24   -651   -194       O  
ATOM   3079  OE2AGLU D  62     -21.096  18.723 -25.193  0.59 37.18           O  
ANISOU 3079  OE2AGLU D  62     5100   4825   4200    500   -710   -990       O  
ATOM   3080  OE2BGLU D  62     -19.860  16.951 -24.697  0.41 33.16           O  
ANISOU 3080  OE2BGLU D  62     4803   4333   3462    -93   -740    208       O  
ATOM   3081  N   ASP D  63     -15.346  21.591 -22.800  1.00 20.72           N  
ANISOU 3081  N   ASP D  63     3313   2222   2338    -38     14    160       N  
ATOM   3082  CA  ASP D  63     -14.772  22.578 -21.899  1.00 20.69           C  
ANISOU 3082  CA  ASP D  63     3082   2296   2482     -7    197    304       C  
ATOM   3083  C   ASP D  63     -15.867  23.213 -21.046  1.00 18.15           C  
ANISOU 3083  C   ASP D  63     2794   1681   2423    -99   -210      8       C  
ATOM   3084  O   ASP D  63     -17.041  23.260 -21.424  1.00 18.95           O  
ANISOU 3084  O   ASP D  63     2915   1749   2534    -77   -450   -155       O  
ATOM   3085  CB  ASP D  63     -14.039  23.670 -22.682  1.00 24.14           C  
ANISOU 3085  CB  ASP D  63     3327   3086   2758    357    630    482       C  
ATOM   3086  CG  ASP D  63     -12.685  23.220 -23.197  1.00 28.22           C  
ANISOU 3086  CG  ASP D  63     3771   3812   3138    448    639    911       C  
ATOM   3087  OD1 ASP D  63     -12.251  22.099 -22.858  1.00 31.81           O  
ANISOU 3087  OD1 ASP D  63     4125   4579   3380    824    325   1145       O  
ATOM   3088  OD2 ASP D  63     -12.051  23.997 -23.944  1.00 28.42           O  
ANISOU 3088  OD2 ASP D  63     3713   3928   3156    670    695    829       O  
ATOM   3089  N   LEU D  64     -15.468  23.710 -19.880  1.00 15.32           N  
ANISOU 3089  N   LEU D  64     2370   1310   2140     57   -350    103       N  
ATOM   3090  CA  LEU D  64     -16.407  24.400 -19.007  1.00 12.82           C  
ANISOU 3090  CA  LEU D  64     2102    972   1796   -110   -483    203       C  
ATOM   3091  C   LEU D  64     -16.896  25.686 -19.659  1.00 13.52           C  
ANISOU 3091  C   LEU D  64     2225   1213   1699     33   -690    325       C  
ATOM   3092  O   LEU D  64     -16.124  26.414 -20.290  1.00 15.06           O  
ANISOU 3092  O   LEU D  64     2280   1914   1527    -63   -306    525       O  
ATOM   3093  CB  LEU D  64     -15.748  24.712 -17.664  1.00 10.49           C  
ANISOU 3093  CB  LEU D  64     1668    893   1425   -538   -306   -206       C  
ATOM   3094  CG  LEU D  64     -16.607  25.388 -16.594  1.00 11.82           C  
ANISOU 3094  CG  LEU D  64     1768   1020   1704   -485   -409   -268       C  
ATOM   3095  CD1 LEU D  64     -17.787  24.510 -16.224  1.00 13.22           C  
ANISOU 3095  CD1 LEU D  64     2036   1035   1951   -111      6   -410       C  
ATOM   3096  CD2 LEU D  64     -15.765  25.703 -15.367  1.00 10.95           C  
ANISOU 3096  CD2 LEU D  64     1745   1020   1396   -107   -702   -128       C  
ATOM   3097  N   LYS D  65     -18.191  25.953 -19.520  1.00 12.87           N  
ANISOU 3097  N   LYS D  65     1841   1326   1723    498   -807    138       N  
ATOM   3098  CA  LYS D  65     -18.747  27.243 -19.899  1.00 16.25           C  
ANISOU 3098  CA  LYS D  65     2119   2217   1839    487  -1018    261       C  
ATOM   3099  C   LYS D  65     -20.082  27.414 -19.194  1.00 14.79           C  
ANISOU 3099  C   LYS D  65     1817   1904   1897     -2   -944    333       C  
ATOM   3100  O   LYS D  65     -20.773  26.436 -18.894  1.00 15.10           O  
ANISOU 3100  O   LYS D  65     2055   1777   1907   -216   -790    486       O  
ATOM   3101  CB  LYS D  65     -18.915  27.384 -21.420  1.00 22.82           C  
ANISOU 3101  CB  LYS D  65     2919   3692   2059    576   -637   -144       C  
ATOM   3102  CG  LYS D  65     -20.136  26.690 -21.996  1.00 26.90           C  
ANISOU 3102  CG  LYS D  65     3727   4281   2213    750   -393   -429       C  
ATOM   3103  CD  LYS D  65     -20.541  27.305 -23.332  1.00 30.55           C  
ANISOU 3103  CD  LYS D  65     4374   4527   2705   1358   -314   -695       C  
ATOM   3104  CE  LYS D  65     -19.503  27.046 -24.409  1.00 34.52           C  
ANISOU 3104  CE  LYS D  65     5084   4924   3108   1602   -625   -816       C  
ATOM   3105  NZ  LYS D  65     -19.451  25.605 -24.784  1.00 38.28           N  
ANISOU 3105  NZ  LYS D  65     5651   5451   3443   1131   -922  -1106       N  
ATOM   3106  N   PHE D  66     -20.421  28.667 -18.912  1.00 15.16           N  
ANISOU 3106  N   PHE D  66     1743   2068   1951    -76   -657    255       N  
ATOM   3107  CA  PHE D  66     -21.681  29.029 -18.294  1.00 16.56           C  
ANISOU 3107  CA  PHE D  66     2119   2162   2013     82   -887    333       C  
ATOM   3108  C   PHE D  66     -22.395  30.065 -19.149  1.00 17.09           C  
ANISOU 3108  C   PHE D  66     2166   2399   1929   -109  -1147    431       C  
ATOM   3109  O   PHE D  66     -21.745  30.896 -19.791  1.00 19.02           O  
ANISOU 3109  O   PHE D  66     2681   2616   1931    298  -1164    319       O  
ATOM   3110  CB  PHE D  66     -21.481  29.610 -16.888  1.00 15.53           C  
ANISOU 3110  CB  PHE D  66     2172   1791   1938    -32   -933    119       C  
ATOM   3111  CG  PHE D  66     -21.033  28.607 -15.865  1.00 14.54           C  
ANISOU 3111  CG  PHE D  66     2123   1476   1926   -131   -883    144       C  
ATOM   3112  CD1 PHE D  66     -21.959  27.847 -15.169  1.00 15.20           C  
ANISOU 3112  CD1 PHE D  66     2360   1371   2044   -450   -648     73       C  
ATOM   3113  CD2 PHE D  66     -19.688  28.439 -15.585  1.00 14.52           C  
ANISOU 3113  CD2 PHE D  66     2121   1337   2059   -254   -790   -335       C  
ATOM   3114  CE1 PHE D  66     -21.549  26.931 -14.218  1.00 14.01           C  
ANISOU 3114  CE1 PHE D  66     1883   1299   2142   -187   -683     35       C  
ATOM   3115  CE2 PHE D  66     -19.273  27.525 -14.634  1.00 14.15           C  
ANISOU 3115  CE2 PHE D  66     2063   1088   2227   -276   -695   -218       C  
ATOM   3116  CZ  PHE D  66     -20.204  26.770 -13.951  1.00 14.60           C  
ANISOU 3116  CZ  PHE D  66     1940   1428   2178   -300   -463    -13       C  
ATOM   3117  N   PRO D  67     -23.724  30.043 -19.180  1.00 17.92           N  
ANISOU 3117  N   PRO D  67     2039   2343   2426   -262  -1117    362       N  
ATOM   3118  CA  PRO D  67     -24.454  31.154 -19.794  1.00 20.03           C  
ANISOU 3118  CA  PRO D  67     2241   2824   2543   -544  -1052    221       C  
ATOM   3119  C   PRO D  67     -24.116  32.462 -19.096  1.00 20.07           C  
ANISOU 3119  C   PRO D  67     2294   2682   2650    -33   -858    468       C  
ATOM   3120  O   PRO D  67     -23.826  32.496 -17.897  1.00 16.92           O  
ANISOU 3120  O   PRO D  67     1463   2499   2466     49   -447    236       O  
ATOM   3121  CB  PRO D  67     -25.925  30.771 -19.592  1.00 19.97           C  
ANISOU 3121  CB  PRO D  67     2107   2765   2715   -369  -1022    108       C  
ATOM   3122  CG  PRO D  67     -25.907  29.285 -19.440  1.00 21.85           C  
ANISOU 3122  CG  PRO D  67     2472   2976   2855    -61  -1264    419       C  
ATOM   3123  CD  PRO D  67     -24.624  28.968 -18.729  1.00 20.04           C  
ANISOU 3123  CD  PRO D  67     2204   2663   2749     20  -1198    592       C  
ATOM   3124  N   ARG D  68     -24.136  33.541 -19.873  1.00 22.62           N  
ANISOU 3124  N   ARG D  68     2957   2931   2705   -174  -1181   1109       N  
ATOM   3125  CA  ARG D  68     -23.843  34.870 -19.352  1.00 24.01           C  
ANISOU 3125  CA  ARG D  68     3028   3066   3029   -255  -1147   1087       C  
ATOM   3126  C   ARG D  68     -24.742  35.187 -18.167  1.00 21.42           C  
ANISOU 3126  C   ARG D  68     2162   2960   3018    -54  -1357    725       C  
ATOM   3127  O   ARG D  68     -25.971  35.159 -18.282  1.00 22.27           O  
ANISOU 3127  O   ARG D  68     2140   3226   3097   -558  -1392      5       O  
ATOM   3128  CB  ARG D  68     -24.030  35.903 -20.466  1.00 28.75           C  
ANISOU 3128  CB  ARG D  68     3947   3433   3544   -648   -983   1312       C  
ATOM   3129  CG  ARG D  68     -23.394  37.256 -20.211  1.00 33.08           C  
ANISOU 3129  CG  ARG D  68     4727   3832   4010   -620   -797   1203       C  
ATOM   3130  CD  ARG D  68     -23.444  38.102 -21.478  1.00 38.21           C  
ANISOU 3130  CD  ARG D  68     5675   4402   4442   -672   -366   1099       C  
ATOM   3131  NE  ARG D  68     -22.757  39.381 -21.328  1.00 44.77           N  
ANISOU 3131  NE  ARG D  68     6653   5353   5004   -267   -144    793       N  
ATOM   3132  CZ  ARG D  68     -23.368  40.532 -21.067  1.00 48.81           C  
ANISOU 3132  CZ  ARG D  68     7071   5928   5548   -305    -79    259       C  
ATOM   3133  NH1 ARG D  68     -22.660  41.648 -20.950  1.00 49.22           N  
ANISOU 3133  NH1 ARG D  68     7181   5813   5710   -625   -141     41       N  
ATOM   3134  NH2 ARG D  68     -24.687  40.571 -20.926  1.00 50.27           N  
ANISOU 3134  NH2 ARG D  68     7047   6301   5753   -293    -97    156       N  
ATOM   3135  N   GLY D  69     -24.126  35.462 -17.019  1.00 18.89           N  
ANISOU 3135  N   GLY D  69     1700   2444   3033   -214  -1032    799       N  
ATOM   3136  CA  GLY D  69     -24.847  35.731 -15.790  1.00 16.59           C  
ANISOU 3136  CA  GLY D  69     1303   2121   2879     39   -857    579       C  
ATOM   3137  C   GLY D  69     -24.785  34.621 -14.764  1.00 16.98           C  
ANISOU 3137  C   GLY D  69     1515   1994   2943      8   -345    442       C  
ATOM   3138  O   GLY D  69     -25.190  34.843 -13.614  1.00 18.59           O  
ANISOU 3138  O   GLY D  69     1769   2031   3263    251   -167    130       O  
ATOM   3139  N   GLN D  70     -24.293  33.439 -15.130  1.00 13.54           N  
ANISOU 3139  N   GLN D  70      989   1394   2762    126   -415    226       N  
ATOM   3140  CA  GLN D  70     -24.220  32.299 -14.229  1.00 14.96           C  
ANISOU 3140  CA  GLN D  70     1218   1765   2701   -213   -378    227       C  
ATOM   3141  C   GLN D  70     -22.771  31.870 -14.033  1.00 14.98           C  
ANISOU 3141  C   GLN D  70     1745   1660   2286     18   -191     67       C  
ATOM   3142  O   GLN D  70     -21.874  32.264 -14.784  1.00 14.37           O  
ANISOU 3142  O   GLN D  70     1481   1769   2210   -373   -233    267       O  
ATOM   3143  CB  GLN D  70     -25.038  31.111 -14.763  1.00 19.23           C  
ANISOU 3143  CB  GLN D  70     1470   2637   3201   -495   -616    127       C  
ATOM   3144  CG  GLN D  70     -26.525  31.392 -14.939  1.00 21.94           C  
ANISOU 3144  CG  GLN D  70     1363   3179   3794   -657   -654   -155       C  
ATOM   3145  CD  GLN D  70     -27.290  30.193 -15.481  1.00 27.63           C  
ANISOU 3145  CD  GLN D  70     1841   3994   4662   -171   -891   -211       C  
ATOM   3146  OE1 GLN D  70     -26.750  29.091 -15.588  1.00 27.89           O  
ANISOU 3146  OE1 GLN D  70     1860   3889   4848   -720  -1095    -85       O  
ATOM   3147  NE2 GLN D  70     -28.555  30.406 -15.829  1.00 29.58           N  
ANISOU 3147  NE2 GLN D  70     2057   4320   4860    -32   -925   -330       N  
ATOM   3148  N   GLY D  71     -22.549  31.056 -13.003  1.00 14.35           N  
ANISOU 3148  N   GLY D  71     1715   1616   2123     91   -237   -219       N  
ATOM   3149  CA  GLY D  71     -21.277  30.390 -12.799  1.00 13.05           C  
ANISOU 3149  CA  GLY D  71     1613   1430   1914     59   -252   -517       C  
ATOM   3150  C   GLY D  71     -20.429  30.911 -11.658  1.00 11.69           C  
ANISOU 3150  C   GLY D  71     1499   1479   1464   -109   -252   -309       C  
ATOM   3151  O   GLY D  71     -19.461  30.237 -11.283  1.00  9.96           O  
ANISOU 3151  O   GLY D  71      733   1539   1514   -330    101   -256       O  
ATOM   3152  N   VAL D  72     -20.736  32.074 -11.099  1.00 12.17           N  
ANISOU 3152  N   VAL D  72     1887   1392   1346    -87     86     44       N  
ATOM   3153  CA  VAL D  72     -19.919  32.611 -10.007  1.00 10.57           C  
ANISOU 3153  CA  VAL D  72     1377   1225   1415   -112    372    105       C  
ATOM   3154  C   VAL D  72     -20.261  31.862  -8.721  1.00  9.65           C  
ANISOU 3154  C   VAL D  72      802   1340   1526     37    564    256       C  
ATOM   3155  O   VAL D  72     -21.441  31.814  -8.340  1.00 10.85           O  
ANISOU 3155  O   VAL D  72      856   1567   1701     84    631    106       O  
ATOM   3156  CB  VAL D  72     -20.146  34.110  -9.845  1.00 11.13           C  
ANISOU 3156  CB  VAL D  72     1524   1443   1263    -99    207    249       C  
ATOM   3157  CG1 VAL D  72     -19.327  34.636  -8.675  1.00 10.67           C  
ANISOU 3157  CG1 VAL D  72     1389   1326   1338    -23    332    163       C  
ATOM   3158  CG2 VAL D  72     -19.792  34.852 -11.134  1.00 11.73           C  
ANISOU 3158  CG2 VAL D  72     1625   1666   1166    -44     92    435       C  
ATOM   3159  N   PRO D  73     -19.279  31.274  -8.035  1.00 10.21           N  
ANISOU 3159  N   PRO D  73     1089   1413   1376    354    654    130       N  
ATOM   3160  CA  PRO D  73     -19.575  30.544  -6.797  1.00 10.52           C  
ANISOU 3160  CA  PRO D  73     1248   1319   1430    533    609    101       C  
ATOM   3161  C   PRO D  73     -20.168  31.450  -5.729  1.00 12.34           C  
ANISOU 3161  C   PRO D  73     1587   1321   1781    519    555    234       C  
ATOM   3162  O   PRO D  73     -19.865  32.643  -5.652  1.00 13.82           O  
ANISOU 3162  O   PRO D  73     1812   1596   1842    261    628    245       O  
ATOM   3163  CB  PRO D  73     -18.206  30.005  -6.366  1.00 10.37           C  
ANISOU 3163  CB  PRO D  73     1318   1328   1295    664    505    168       C  
ATOM   3164  CG  PRO D  73     -17.392  29.983  -7.619  1.00 10.04           C  
ANISOU 3164  CG  PRO D  73     1423   1295   1097    -91    596    342       C  
ATOM   3165  CD  PRO D  73     -17.863  31.159  -8.421  1.00  9.90           C  
ANISOU 3165  CD  PRO D  73     1147   1350   1266    -62    534    229       C  
ATOM   3166  N   ILE D  74     -21.024  30.859  -4.894  1.00 11.40           N  
ANISOU 3166  N   ILE D  74     1162   1564   1605    225    770    239       N  
ATOM   3167  CA  ILE D  74     -21.646  31.593  -3.798  1.00 13.39           C  
ANISOU 3167  CA  ILE D  74     1466   1649   1972    252    722    124       C  
ATOM   3168  C   ILE D  74     -20.590  31.946  -2.762  1.00 13.99           C  
ANISOU 3168  C   ILE D  74     1472   1951   1895    102    852    209       C  
ATOM   3169  O   ILE D  74     -19.800  31.092  -2.339  1.00 14.20           O  
ANISOU 3169  O   ILE D  74      877   2478   2039    258    514    184       O  
ATOM   3170  CB  ILE D  74     -22.782  30.768  -3.173  1.00 15.13           C  
ANISOU 3170  CB  ILE D  74     1381   2043   2324     46    820   -155       C  
ATOM   3171  CG1 ILE D  74     -23.915  30.558  -4.178  1.00 18.51           C  
ANISOU 3171  CG1 ILE D  74     1476   2841   2716   -293    548    205       C  
ATOM   3172  CG2 ILE D  74     -23.305  31.439  -1.907  1.00 16.21           C  
ANISOU 3172  CG2 ILE D  74     1591   2183   2386    179    862    -60       C  
ATOM   3173  CD1 ILE D  74     -24.974  29.582  -3.705  1.00 20.07           C  
ANISOU 3173  CD1 ILE D  74     1293   3275   3057   -541    548    194       C  
ATOM   3174  N   ASN D  75     -20.573  33.211  -2.347  1.00 13.88           N  
ANISOU 3174  N   ASN D  75     1862   1686   1723     17    989    236       N  
ATOM   3175  CA  ASN D  75     -19.660  33.680  -1.302  1.00 15.52           C  
ANISOU 3175  CA  ASN D  75     2199   1788   1908    289    872    -19       C  
ATOM   3176  C   ASN D  75     -20.394  34.795  -0.553  1.00 17.11           C  
ANISOU 3176  C   ASN D  75     2436   1951   2116    445   1179   -247       C  
ATOM   3177  O   ASN D  75     -20.246  35.976  -0.875  1.00 16.94           O  
ANISOU 3177  O   ASN D  75     2191   1877   2370    595   1171    167       O  
ATOM   3178  CB  ASN D  75     -18.338  34.155  -1.887  1.00 13.91           C  
ANISOU 3178  CB  ASN D  75     1755   1502   2029    137    818     94       C  
ATOM   3179  CG  ASN D  75     -17.367  34.645  -0.827  1.00 15.86           C  
ANISOU 3179  CG  ASN D  75     2197   1869   1959     -1    821    343       C  
ATOM   3180  OD1 ASN D  75     -17.628  34.544   0.371  1.00 17.81           O  
ANISOU 3180  OD1 ASN D  75     2533   2472   1762   -175   1000    368       O  
ATOM   3181  ND2 ASN D  75     -16.233  35.174  -1.269  1.00 14.79           N  
ANISOU 3181  ND2 ASN D  75     1689   1759   2171     48    975    253       N  
ATOM   3182  N   THR D  76     -21.181  34.399   0.451  1.00 19.03           N  
ANISOU 3182  N   THR D  76     2744   2331   2157   -184   1263   -251       N  
ATOM   3183  CA  THR D  76     -22.067  35.331   1.143  1.00 19.94           C  
ANISOU 3183  CA  THR D  76     2767   2833   1977   -243   1342   -252       C  
ATOM   3184  C   THR D  76     -21.320  36.438   1.874  1.00 17.16           C  
ANISOU 3184  C   THR D  76     2061   2669   1788    -82    739   -206       C  
ATOM   3185  O   THR D  76     -21.957  37.402   2.314  1.00 17.80           O  
ANISOU 3185  O   THR D  76     2301   2659   1805    715   -225   -439       O  
ATOM   3186  CB  THR D  76     -22.958  34.581   2.136  1.00 24.81           C  
ANISOU 3186  CB  THR D  76     3597   3584   2246   -693   1378    -95       C  
ATOM   3187  OG1 THR D  76     -22.140  33.907   3.101  1.00 24.39           O  
ANISOU 3187  OG1 THR D  76     3723   3740   1803   -378   1181    364       O  
ATOM   3188  CG2 THR D  76     -23.829  33.564   1.410  1.00 28.42           C  
ANISOU 3188  CG2 THR D  76     3957   4279   2563   -618   1746   -227       C  
ATOM   3189  N   ASN D  77     -20.001  36.335   2.013  1.00 17.92           N  
ANISOU 3189  N   ASN D  77     2286   2618   1904    -19    571    143       N  
ATOM   3190  CA  ASN D  77     -19.208  37.358   2.677  1.00 19.41           C  
ANISOU 3190  CA  ASN D  77     2497   2865   2014     -6    724    472       C  
ATOM   3191  C   ASN D  77     -18.568  38.333   1.696  1.00 18.69           C  
ANISOU 3191  C   ASN D  77     2250   2770   2083   -105    429    160       C  
ATOM   3192  O   ASN D  77     -17.688  39.105   2.089  1.00 23.15           O  
ANISOU 3192  O   ASN D  77     2632   3792   2370   -862    365    640       O  
ATOM   3193  CB  ASN D  77     -18.139  36.702   3.550  1.00 25.51           C  
ANISOU 3193  CB  ASN D  77     3684   3449   2558    204   1323    525       C  
ATOM   3194  CG  ASN D  77     -18.724  35.697   4.521  1.00 30.87           C  
ANISOU 3194  CG  ASN D  77     5045   3714   2970    375   1807    482       C  
ATOM   3195  OD1 ASN D  77     -19.352  36.070   5.510  1.00 34.71           O  
ANISOU 3195  OD1 ASN D  77     5830   4136   3223    136   2336    439       O  
ATOM   3196  ND2 ASN D  77     -18.525  34.414   4.242  1.00 32.30           N  
ANISOU 3196  ND2 ASN D  77     5428   3636   3208    450   1604    627       N  
ATOM   3197  N   SER D  78     -18.991  38.320   0.438  1.00 16.12           N  
ANISOU 3197  N   SER D  78     1884   2304   1938    525    432    -24       N  
ATOM   3198  CA  SER D  78     -18.487  39.229  -0.581  1.00 15.82           C  
ANISOU 3198  CA  SER D  78     2117   2008   1887    474    532   -148       C  
ATOM   3199  C   SER D  78     -19.618  40.126  -1.068  1.00 16.75           C  
ANISOU 3199  C   SER D  78     2417   2135   1814    187    323   -145       C  
ATOM   3200  O   SER D  78     -20.798  39.867  -0.822  1.00 16.52           O  
ANISOU 3200  O   SER D  78     2330   2233   1712    139    -50    -86       O  
ATOM   3201  CB  SER D  78     -17.873  38.457  -1.755  1.00 15.30           C  
ANISOU 3201  CB  SER D  78     2014   1955   1842     74    405   -234       C  
ATOM   3202  OG  SER D  78     -18.836  37.620  -2.366  1.00 14.79           O  
ANISOU 3202  OG  SER D  78     1990   1702   1928     39    496    135       O  
ATOM   3203  N   SER D  79     -19.243  41.193  -1.772  1.00 17.46           N  
ANISOU 3203  N   SER D  79     2619   2200   1814    168    624    -90       N  
ATOM   3204  CA  SER D  79     -20.188  42.195  -2.237  1.00 16.05           C  
ANISOU 3204  CA  SER D  79     2081   2268   1749   -135    382   -179       C  
ATOM   3205  C   SER D  79     -20.703  41.854  -3.630  1.00 14.47           C  
ANISOU 3205  C   SER D  79     1549   2232   1715    -15    -18   -212       C  
ATOM   3206  O   SER D  79     -20.063  41.110  -4.379  1.00 14.51           O  
ANISOU 3206  O   SER D  79     1583   2321   1610   -177   -470   -168       O  
ATOM   3207  CB  SER D  79     -19.523  43.570  -2.255  1.00 16.78           C  
ANISOU 3207  CB  SER D  79     2286   2118   1973   -344    566   -465       C  
ATOM   3208  OG  SER D  79     -18.605  43.673  -3.326  1.00 20.35           O  
ANISOU 3208  OG  SER D  79     2789   2447   2495   -804     67   -176       O  
ATOM   3209  N   PRO D  80     -21.872  42.382  -4.006  1.00 14.57           N  
ANISOU 3209  N   PRO D  80     1049   2840   1648    437     12   -296       N  
ATOM   3210  CA  PRO D  80     -22.345  42.196  -5.388  1.00 14.54           C  
ANISOU 3210  CA  PRO D  80     1075   2728   1719    503    -23   -271       C  
ATOM   3211  C   PRO D  80     -21.369  42.707  -6.432  1.00 14.78           C  
ANISOU 3211  C   PRO D  80     1374   2285   1955    431   -373   -126       C  
ATOM   3212  O   PRO D  80     -21.300  42.141  -7.531  1.00 14.63           O  
ANISOU 3212  O   PRO D  80     1520   2165   1875    349   -647     19       O  
ATOM   3213  CB  PRO D  80     -23.663  42.981  -5.414  1.00 15.22           C  
ANISOU 3213  CB  PRO D  80     1086   3201   1496    362    327   -266       C  
ATOM   3214  CG  PRO D  80     -24.125  42.980  -3.997  1.00 17.54           C  
ANISOU 3214  CG  PRO D  80     1434   3592   1637    747    212   -259       C  
ATOM   3215  CD  PRO D  80     -22.877  43.056  -3.164  1.00 15.32           C  
ANISOU 3215  CD  PRO D  80     1148   3049   1621    815    -42   -221       C  
ATOM   3216  N   ASP D  81     -20.610  43.762  -6.123  1.00 14.11           N  
ANISOU 3216  N   ASP D  81     1316   1739   2305    666   -248    -42       N  
ATOM   3217  CA  ASP D  81     -19.595  44.242  -7.053  1.00 14.81           C  
ANISOU 3217  CA  ASP D  81     1920   1472   2235    682    -48   -322       C  
ATOM   3218  C   ASP D  81     -18.511  43.201  -7.311  1.00 12.18           C  
ANISOU 3218  C   ASP D  81     1532   1205   1890    682   -135   -465       C  
ATOM   3219  O   ASP D  81     -17.865  43.245  -8.363  1.00 14.15           O  
ANISOU 3219  O   ASP D  81     2017   1639   1722    202   -544    234       O  
ATOM   3220  CB  ASP D  81     -18.947  45.525  -6.523  1.00 16.48           C  
ANISOU 3220  CB  ASP D  81     2367   1406   2490    874    -13   -541       C  
ATOM   3221  CG  ASP D  81     -19.916  46.691  -6.450  1.00 24.64           C  
ANISOU 3221  CG  ASP D  81     3639   2561   3160    482    -41   -817       C  
ATOM   3222  OD1 ASP D  81     -20.934  46.682  -7.174  1.00 27.30           O  
ANISOU 3222  OD1 ASP D  81     3885   3109   3380   1150   -126   -327       O  
ATOM   3223  OD2 ASP D  81     -19.651  47.626  -5.669  1.00 27.08           O  
ANISOU 3223  OD2 ASP D  81     4036   2661   3594    405    -48   -770       O  
ATOM   3224  N   ASP D  82     -18.302  42.266  -6.378  1.00 10.80           N  
ANISOU 3224  N   ASP D  82     1557   1250   1296    374   -255   -116       N  
ATOM   3225  CA  ASP D  82     -17.203  41.306  -6.450  1.00  9.38           C  
ANISOU 3225  CA  ASP D  82     1109   1251   1204    293    -99   -164       C  
ATOM   3226  C   ASP D  82     -17.467  40.122  -7.375  1.00 11.25           C  
ANISOU 3226  C   ASP D  82     1290   1489   1496   -287      1    -78       C  
ATOM   3227  O   ASP D  82     -16.531  39.365  -7.653  1.00 13.66           O  
ANISOU 3227  O   ASP D  82     1476   2035   1680   -397   -312    -75       O  
ATOM   3228  CB  ASP D  82     -16.887  40.740  -5.059  1.00  9.61           C  
ANISOU 3228  CB  ASP D  82     1193   1550    908     55     57   -264       C  
ATOM   3229  CG  ASP D  82     -16.381  41.787  -4.083  1.00 12.11           C  
ANISOU 3229  CG  ASP D  82     1656   2026    921    484     18    -53       C  
ATOM   3230  OD1 ASP D  82     -15.880  42.846  -4.515  1.00 13.81           O  
ANISOU 3230  OD1 ASP D  82     2019   2144   1084    250   -126    244       O  
ATOM   3231  OD2 ASP D  82     -16.477  41.530  -2.865  1.00 12.67           O  
ANISOU 3231  OD2 ASP D  82     1739   2073   1001    -30   -685   -246       O  
ATOM   3232  N   GLN D  83     -18.699  39.929  -7.849  1.00 11.22           N  
ANISOU 3232  N   GLN D  83     1386   1365   1513    109   -134    139       N  
ATOM   3233  CA  GLN D  83     -19.121  38.639  -8.407  1.00 11.27           C  
ANISOU 3233  CA  GLN D  83     1452   1585   1245     36    589   -222       C  
ATOM   3234  C   GLN D  83     -18.702  38.503  -9.872  1.00 11.18           C  
ANISOU 3234  C   GLN D  83     1408   1433   1406    281    810    290       C  
ATOM   3235  O   GLN D  83     -19.523  38.483 -10.791  1.00 11.22           O  
ANISOU 3235  O   GLN D  83     1231   1419   1615    569    647    271       O  
ATOM   3236  CB  GLN D  83     -20.627  38.478  -8.255  1.00 12.28           C  
ANISOU 3236  CB  GLN D  83     1439   1939   1289     35    807   -110       C  
ATOM   3237  CG  GLN D  83     -21.121  38.701  -6.839  1.00 12.71           C  
ANISOU 3237  CG  GLN D  83     1782   1864   1183    -85    833    -50       C  
ATOM   3238  CD  GLN D  83     -20.442  37.777  -5.857  1.00 12.31           C  
ANISOU 3238  CD  GLN D  83     1492   1844   1342     76    651    222       C  
ATOM   3239  OE1 GLN D  83     -20.451  36.559  -6.029  1.00 14.00           O  
ANISOU 3239  OE1 GLN D  83     2229   1615   1476    184    727    -73       O  
ATOM   3240  NE2 GLN D  83     -19.831  38.351  -4.830  1.00  9.43           N  
ANISOU 3240  NE2 GLN D  83      577   1735   1271     20    300    231       N  
ATOM   3241  N   ILE D  84     -17.396  38.352 -10.083  1.00 10.48           N  
ANISOU 3241  N   ILE D  84     1438   1201   1341    437    597     61       N  
ATOM   3242  CA  ILE D  84     -16.857  38.290 -11.439  1.00 10.26           C  
ANISOU 3242  CA  ILE D  84     1274   1224   1401    348    289    231       C  
ATOM   3243  C   ILE D  84     -15.470  37.659 -11.388  1.00  9.51           C  
ANISOU 3243  C   ILE D  84     1393   1004   1217    286    294     66       C  
ATOM   3244  O   ILE D  84     -14.666  37.964 -10.504  1.00  9.42           O  
ANISOU 3244  O   ILE D  84      979   1365   1235    -70    109      9       O  
ATOM   3245  CB  ILE D  84     -16.837  39.697 -12.087  1.00 10.14           C  
ANISOU 3245  CB  ILE D  84     1341   1103   1408    384    -24    159       C  
ATOM   3246  CG1 ILE D  84     -16.268  39.648 -13.506  1.00  9.09           C  
ANISOU 3246  CG1 ILE D  84     1264    928   1262   -117    466    435       C  
ATOM   3247  CG2 ILE D  84     -16.061  40.680 -11.228  1.00  7.91           C  
ANISOU 3247  CG2 ILE D  84      823    760   1425    337    286    -46       C  
ATOM   3248  CD1 ILE D  84     -16.394  40.971 -14.243  1.00 12.19           C  
ANISOU 3248  CD1 ILE D  84     1821   1363   1446    -46    276    477       C  
ATOM   3249  N   GLY D  85     -15.199  36.774 -12.339  1.00  8.01           N  
ANISOU 3249  N   GLY D  85     1145    876   1021     97    354    249       N  
ATOM   3250  CA  GLY D  85     -13.908  36.117 -12.378  1.00  6.72           C  
ANISOU 3250  CA  GLY D  85     1031    651    872    105    206   -190       C  
ATOM   3251  C   GLY D  85     -13.827  35.093 -13.486  1.00  9.66           C  
ANISOU 3251  C   GLY D  85     1599   1185    885     98    -20    156       C  
ATOM   3252  O   GLY D  85     -14.600  35.129 -14.446  1.00  9.77           O  
ANISOU 3252  O   GLY D  85     1683   1238    790   -604     24   -247       O  
ATOM   3253  N   TYR D  86     -12.878  34.171 -13.340  1.00  9.30           N  
ANISOU 3253  N   TYR D  86     1847    813    873    -19   -139    181       N  
ATOM   3254  CA  TYR D  86     -12.625  33.158 -14.351  1.00  8.12           C  
ANISOU 3254  CA  TYR D  86     1426    833    826    -54    209    334       C  
ATOM   3255  C   TYR D  86     -12.411  31.803 -13.694  1.00  9.29           C  
ANISOU 3255  C   TYR D  86     1439    968   1124    -74    241    166       C  
ATOM   3256  O   TYR D  86     -11.966  31.715 -12.546  1.00 10.75           O  
ANISOU 3256  O   TYR D  86     1400   1460   1225   -176    229    -73       O  
ATOM   3257  CB  TYR D  86     -11.399  33.511 -15.214  1.00  7.67           C  
ANISOU 3257  CB  TYR D  86      799   1271    843   -287    -80    328       C  
ATOM   3258  CG  TYR D  86     -10.095  33.598 -14.446  1.00  8.56           C  
ANISOU 3258  CG  TYR D  86      635   1757    861   -383   -106    443       C  
ATOM   3259  CD1 TYR D  86      -9.726  34.767 -13.794  1.00  9.15           C  
ANISOU 3259  CD1 TYR D  86      817   1709    950   -382    175    347       C  
ATOM   3260  CD2 TYR D  86      -9.227  32.513 -14.384  1.00  7.97           C  
ANISOU 3260  CD2 TYR D  86      599   1578    850   -299   -211    469       C  
ATOM   3261  CE1 TYR D  86      -8.533  34.851 -13.091  1.00  9.17           C  
ANISOU 3261  CE1 TYR D  86      612   1940    934   -186    -57    448       C  
ATOM   3262  CE2 TYR D  86      -8.034  32.588 -13.683  1.00  9.45           C  
ANISOU 3262  CE2 TYR D  86      681   1950    960   -114     25    388       C  
ATOM   3263  CZ  TYR D  86      -7.691  33.759 -13.042  1.00  9.85           C  
ANISOU 3263  CZ  TYR D  86      727   1941   1075     84     92    372       C  
ATOM   3264  OH  TYR D  86      -6.505  33.836 -12.344  1.00  9.50           O  
ANISOU 3264  OH  TYR D  86      751   1549   1309    511    178    269       O  
ATOM   3265  N   TYR D  87     -12.743  30.748 -14.434  1.00  7.20           N  
ANISOU 3265  N   TYR D  87      779    824   1132   -153    356    -20       N  
ATOM   3266  CA  TYR D  87     -12.325  29.394 -14.102  1.00  6.51           C  
ANISOU 3266  CA  TYR D  87      377    819   1277     63    194     36       C  
ATOM   3267  C   TYR D  87     -11.091  29.051 -14.926  1.00  8.11           C  
ANISOU 3267  C   TYR D  87      618   1268   1194    124    416    219       C  
ATOM   3268  O   TYR D  87     -11.035  29.345 -16.124  1.00  8.95           O  
ANISOU 3268  O   TYR D  87      506   1511   1383    173    197    301       O  
ATOM   3269  CB  TYR D  87     -13.424  28.369 -14.388  1.00  7.17           C  
ANISOU 3269  CB  TYR D  87      413   1132   1181    -20   -164    331       C  
ATOM   3270  CG  TYR D  87     -14.588  28.344 -13.417  1.00  7.40           C  
ANISOU 3270  CG  TYR D  87      655   1171    986   -109   -158    419       C  
ATOM   3271  CD1 TYR D  87     -15.650  29.228 -13.549  1.00  8.06           C  
ANISOU 3271  CD1 TYR D  87      549   1395   1117   -241     33    127       C  
ATOM   3272  CD2 TYR D  87     -14.642  27.407 -12.391  1.00  6.86           C  
ANISOU 3272  CD2 TYR D  87      872    930    803    177    266    -19       C  
ATOM   3273  CE1 TYR D  87     -16.724  29.194 -12.676  1.00  9.02           C  
ANISOU 3273  CE1 TYR D  87     1092   1387    947   -378    283     -5       C  
ATOM   3274  CE2 TYR D  87     -15.711  27.364 -11.514  1.00  6.54           C  
ANISOU 3274  CE2 TYR D  87      817    984    683    182    180   -164       C  
ATOM   3275  CZ  TYR D  87     -16.748  28.260 -11.661  1.00  8.12           C  
ANISOU 3275  CZ  TYR D  87      954   1365    765    129    379      2       C  
ATOM   3276  OH  TYR D  87     -17.814  28.218 -10.791  1.00  9.11           O  
ANISOU 3276  OH  TYR D  87      937   1220   1304   -503    219   -221       O  
ATOM   3277  N   ARG D  88     -10.107  28.425 -14.285  1.00  9.23           N  
ANISOU 3277  N   ARG D  88      967   1174   1367    221    294    138       N  
ATOM   3278  CA  ARG D  88      -8.865  28.033 -14.940  1.00  7.37           C  
ANISOU 3278  CA  ARG D  88      625    809   1366   -175    397     17       C  
ATOM   3279  C   ARG D  88      -8.698  26.523 -14.858  1.00  9.91           C  
ANISOU 3279  C   ARG D  88     1237   1202   1327    108    444     61       C  
ATOM   3280  O   ARG D  88      -8.795  25.939 -13.772  1.00 10.88           O  
ANISOU 3280  O   ARG D  88     1335   1339   1460   -104    462    165       O  
ATOM   3281  CB  ARG D  88      -7.660  28.729 -14.306  1.00  9.66           C  
ANISOU 3281  CB  ARG D  88      649   1278   1744   -373    176    100       C  
ATOM   3282  CG  ARG D  88      -6.325  28.305 -14.903  1.00 13.04           C  
ANISOU 3282  CG  ARG D  88      674   1858   2423   -271     89     81       C  
ATOM   3283  CD  ARG D  88      -5.170  29.052 -14.256  1.00 15.73           C  
ANISOU 3283  CD  ARG D  88      868   1965   3143   -246   -230    126       C  
ATOM   3284  NE  ARG D  88      -3.881  28.642 -14.806  1.00 21.74           N  
ANISOU 3284  NE  ARG D  88     1610   2949   3702    138   -404    584       N  
ATOM   3285  CZ  ARG D  88      -3.146  27.648 -14.320  1.00 28.24           C  
ANISOU 3285  CZ  ARG D  88     2355   4161   4216   -205   -172    786       C  
ATOM   3286  NH1 ARG D  88      -3.571  26.959 -13.269  1.00 30.11           N  
ANISOU 3286  NH1 ARG D  88     2589   4499   4352   -203   -249   1003       N  
ATOM   3287  NH2 ARG D  88      -1.985  27.340 -14.884  1.00 29.03           N  
ANISOU 3287  NH2 ARG D  88     2082   4539   4408   -397    -24    880       N  
ATOM   3288  N   ARG D  89      -8.439  25.899 -16.005  1.00  9.75           N  
ANISOU 3288  N   ARG D  89     1211   1216   1276    221    516   -266       N  
ATOM   3289  CA  ARG D  89      -8.285  24.453 -16.074  1.00 11.53           C  
ANISOU 3289  CA  ARG D  89     1496   1491   1392    227    143   -300       C  
ATOM   3290  C   ARG D  89      -6.915  24.036 -15.556  1.00 13.24           C  
ANISOU 3290  C   ARG D  89     1566   1700   1764    396    360    231       C  
ATOM   3291  O   ARG D  89      -5.896  24.630 -15.921  1.00 15.33           O  
ANISOU 3291  O   ARG D  89     1645   1973   2207    580    387    357       O  
ATOM   3292  CB  ARG D  89      -8.470  23.966 -17.510  1.00 11.89           C  
ANISOU 3292  CB  ARG D  89     1623   1365   1530     18    512   -717       C  
ATOM   3293  CG  ARG D  89      -8.298  22.465 -17.686  1.00 14.05           C  
ANISOU 3293  CG  ARG D  89     2129   1418   1790    230    280   -872       C  
ATOM   3294  CD  ARG D  89      -8.498  22.074 -19.137  1.00 18.59           C  
ANISOU 3294  CD  ARG D  89     2843   1835   2383    356    472   -995       C  
ATOM   3295  NE  ARG D  89      -7.521  22.728 -20.002  1.00 22.63           N  
ANISOU 3295  NE  ARG D  89     3425   2668   2507    220    895  -1117       N  
ATOM   3296  CZ  ARG D  89      -7.771  23.135 -21.241  1.00 23.77           C  
ANISOU 3296  CZ  ARG D  89     3268   3145   2619    252    798   -940       C  
ATOM   3297  NH1 ARG D  89      -8.975  22.966 -21.770  1.00 23.71           N  
ANISOU 3297  NH1 ARG D  89     2777   3626   2605    423    603  -1045       N  
ATOM   3298  NH2 ARG D  89      -6.817  23.722 -21.949  1.00 23.15           N  
ANISOU 3298  NH2 ARG D  89     3118   2839   2839   -170   1019   -299       N  
ATOM   3299  N   ALA D  90      -6.895  23.012 -14.707  1.00 12.37           N  
ANISOU 3299  N   ALA D  90     1532   1469   1698    617    231    369       N  
ATOM   3300  CA  ALA D  90      -5.662  22.411 -14.214  1.00 14.89           C  
ANISOU 3300  CA  ALA D  90     1912   1656   2090    601    684     88       C  
ATOM   3301  C   ALA D  90      -5.665  20.942 -14.602  1.00 16.86           C  
ANISOU 3301  C   ALA D  90     1948   1916   2542    575    892   -159       C  
ATOM   3302  O   ALA D  90      -6.569  20.196 -14.211  1.00 16.66           O  
ANISOU 3302  O   ALA D  90     2119   1570   2641    406    980   -122       O  
ATOM   3303  CB  ALA D  90      -5.530  22.570 -12.699  1.00 15.54           C  
ANISOU 3303  CB  ALA D  90     1986   2075   1842    886    204     -8       C  
ATOM   3304  N   THR D  91      -4.661  20.530 -15.370  1.00 17.61           N  
ANISOU 3304  N   THR D  91     1647   2324   2718    513   1002   -250       N  
ATOM   3305  CA  THR D  91      -4.564  19.169 -15.872  1.00 20.79           C  
ANISOU 3305  CA  THR D  91     2047   2698   3155    677    675    -17       C  
ATOM   3306  C   THR D  91      -3.491  18.403 -15.111  1.00 19.43           C  
ANISOU 3306  C   THR D  91     1553   2408   3421    371    283     59       C  
ATOM   3307  O   THR D  91      -2.451  18.963 -14.750  1.00 19.96           O  
ANISOU 3307  O   THR D  91     1451   2387   3748     48    290    116       O  
ATOM   3308  CB  THR D  91      -4.244  19.155 -17.369  1.00 27.35           C  
ANISOU 3308  CB  THR D  91     3085   3697   3611   1067    402      0       C  
ATOM   3309  OG1 THR D  91      -3.005  19.839 -17.601  1.00 27.44           O  
ANISOU 3309  OG1 THR D  91     2973   3634   3821   1280    537    -55       O  
ATOM   3310  CG2 THR D  91      -5.354  19.840 -18.155  1.00 28.66           C  
ANISOU 3310  CG2 THR D  91     3153   4156   3582   1359    -40     -1       C  
ATOM   3311  N   ARG D  92      -3.756  17.124 -14.863  1.00 18.17           N  
ANISOU 3311  N   ARG D  92     1459   2226   3218    479     36     -3       N  
ATOM   3312  CA  ARG D  92      -2.806  16.233 -14.217  1.00 19.17           C  
ANISOU 3312  CA  ARG D  92     2129   2054   3100    212    469   -328       C  
ATOM   3313  C   ARG D  92      -2.695  14.950 -15.022  1.00 19.53           C  
ANISOU 3313  C   ARG D  92     2174   2216   3032    351    579   -126       C  
ATOM   3314  O   ARG D  92      -3.667  14.495 -15.631  1.00 19.56           O  
ANISOU 3314  O   ARG D  92     2100   2260   3073    203    449   -174       O  
ATOM   3315  CB  ARG D  92      -3.219  15.899 -12.779  1.00 20.11           C  
ANISOU 3315  CB  ARG D  92     2297   2291   3052   -354    844   -460       C  
ATOM   3316  CG  ARG D  92      -3.179  17.072 -11.817  1.00 23.16           C  
ANISOU 3316  CG  ARG D  92     2714   2895   3192   -467    544   -264       C  
ATOM   3317  CD  ARG D  92      -3.656  16.642 -10.438  1.00 24.48           C  
ANISOU 3317  CD  ARG D  92     2888   3194   3220   -209      4     72       C  
ATOM   3318  NE  ARG D  92      -5.021  16.123 -10.481  1.00 24.18           N  
ANISOU 3318  NE  ARG D  92     2757   3191   3238   -243   -541     24       N  
ATOM   3319  CZ  ARG D  92      -5.624  15.507  -9.470  1.00 22.29           C  
ANISOU 3319  CZ  ARG D  92     2666   2897   2907    -97   -761      3       C  
ATOM   3320  NH1 ARG D  92      -4.984  15.321  -8.323  1.00 24.56           N  
ANISOU 3320  NH1 ARG D  92     2800   3451   3082      9  -1481     31       N  
ATOM   3321  NH2 ARG D  92      -6.869  15.072  -9.608  1.00 19.09           N  
ANISOU 3321  NH2 ARG D  92     2338   2147   2771   -118   -315   -197       N  
ATOM   3322  N   ARG D  93      -1.501  14.369 -15.019  1.00 19.44           N  
ANISOU 3322  N   ARG D  93     2030   2317   3038    556    509    377       N  
ATOM   3323  CA  ARG D  93      -1.249  13.108 -15.697  1.00 20.94           C  
ANISOU 3323  CA  ARG D  93     2182   2648   3125    711    542    296       C  
ATOM   3324  C   ARG D  93      -0.537  12.158 -14.747  1.00 18.63           C  
ANISOU 3324  C   ARG D  93     1582   2638   2858    559    292     17       C  
ATOM   3325  O   ARG D  93       0.277  12.584 -13.922  1.00 18.94           O  
ANISOU 3325  O   ARG D  93     1716   2729   2752     79     39   -280       O  
ATOM   3326  CB  ARG D  93      -0.412  13.307 -16.962  1.00 25.75           C  
ANISOU 3326  CB  ARG D  93     2891   3441   3450    567    957    681       C  
ATOM   3327  CG  ARG D  93      -1.030  14.247 -17.978  1.00 29.88           C  
ANISOU 3327  CG  ARG D  93     3349   4137   3866    611   1315   1043       C  
ATOM   3328  CD  ARG D  93      -0.311  14.145 -19.308  1.00 35.21           C  
ANISOU 3328  CD  ARG D  93     4006   5141   4231    566   1655   1122       C  
ATOM   3329  NE  ARG D  93       1.125  14.361 -19.167  1.00 41.09           N  
ANISOU 3329  NE  ARG D  93     5010   5932   4669    739   1715   1171       N  
ATOM   3330  CZ  ARG D  93       2.009  14.159 -20.138  1.00 43.70           C  
ANISOU 3330  CZ  ARG D  93     5283   6428   4893    655   1978   1298       C  
ATOM   3331  NH1 ARG D  93       1.606  13.730 -21.326  1.00 43.99           N  
ANISOU 3331  NH1 ARG D  93     5553   6445   4718    969   2105   1367       N  
ATOM   3332  NH2 ARG D  93       3.298  14.381 -19.919  1.00 44.12           N  
ANISOU 3332  NH2 ARG D  93     4977   6615   5172    429   1852   1376       N  
ATOM   3333  N   ILE D  94      -0.853  10.870 -14.865  1.00 16.16           N  
ANISOU 3333  N   ILE D  94     1048   2292   2800    381    613     44       N  
ATOM   3334  CA  ILE D  94      -0.260   9.828 -14.037  1.00 19.58           C  
ANISOU 3334  CA  ILE D  94     1958   2559   2924    576   1009     54       C  
ATOM   3335  C   ILE D  94       0.319   8.761 -14.953  1.00 19.04           C  
ANISOU 3335  C   ILE D  94     1692   2762   2781    497    857   -209       C  
ATOM   3336  O   ILE D  94      -0.362   8.287 -15.869  1.00 19.17           O  
ANISOU 3336  O   ILE D  94     1799   2638   2846    192    407   -580       O  
ATOM   3337  CB  ILE D  94      -1.287   9.206 -13.071  1.00 23.86           C  
ANISOU 3337  CB  ILE D  94     2684   3056   3325    852   1399    323       C  
ATOM   3338  CG1 ILE D  94      -1.869  10.278 -12.147  1.00 28.08           C  
ANISOU 3338  CG1 ILE D  94     3341   3592   3735   1091    864     32       C  
ATOM   3339  CG2 ILE D  94      -0.646   8.090 -12.259  1.00 25.96           C  
ANISOU 3339  CG2 ILE D  94     2955   3437   3473    702   1587    462       C  
ATOM   3340  CD1 ILE D  94      -0.836  10.961 -11.281  1.00 29.03           C  
ANISOU 3340  CD1 ILE D  94     3498   3630   3904   1160    755   -245       C  
ATOM   3341  N   ARG D  95       1.570   8.385 -14.706  1.00 16.84           N  
ANISOU 3341  N   ARG D  95     1226   2666   2508    299    854   -188       N  
ATOM   3342  CA  ARG D  95       2.212   7.339 -15.486  1.00 17.16           C  
ANISOU 3342  CA  ARG D  95     1141   2793   2584    431    736   -186       C  
ATOM   3343  C   ARG D  95       1.694   5.976 -15.042  1.00 16.31           C  
ANISOU 3343  C   ARG D  95     1105   2510   2581    410    714    -33       C  
ATOM   3344  O   ARG D  95       1.685   5.663 -13.846  1.00 16.42           O  
ANISOU 3344  O   ARG D  95     1359   2302   2580    124   1000    168       O  
ATOM   3345  CB  ARG D  95       3.730   7.415 -15.326  1.00 19.38           C  
ANISOU 3345  CB  ARG D  95     1530   2996   2838    674    871   -367       C  
ATOM   3346  CG  ARG D  95       4.506   6.555 -16.307  1.00 21.07           C  
ANISOU 3346  CG  ARG D  95     1592   3288   3127    868    798   -190       C  
ATOM   3347  CD  ARG D  95       6.005   6.680 -16.071  1.00 24.13           C  
ANISOU 3347  CD  ARG D  95     1896   3949   3323    382    734    213       C  
ATOM   3348  NE  ARG D  95       6.464   8.065 -16.154  1.00 24.19           N  
ANISOU 3348  NE  ARG D  95     2230   3648   3314    365    363    284       N  
ATOM   3349  CZ  ARG D  95       6.935   8.632 -17.261  1.00 24.96           C  
ANISOU 3349  CZ  ARG D  95     2836   3505   3143    297    120    410       C  
ATOM   3350  NH1 ARG D  95       7.011   7.932 -18.385  1.00 27.02           N  
ANISOU 3350  NH1 ARG D  95     3398   3672   3197   -436    378    113       N  
ATOM   3351  NH2 ARG D  95       7.332   9.897 -17.245  1.00 24.82           N  
ANISOU 3351  NH2 ARG D  95     2868   3449   3111    452   -267    620       N  
ATOM   3352  N   GLY D  96       1.251   5.168 -16.011  1.00 15.61           N  
ANISOU 3352  N   GLY D  96     1171   2164   2598    129    382   -277       N  
ATOM   3353  CA  GLY D  96       0.737   3.848 -15.711  1.00 17.17           C  
ANISOU 3353  CA  GLY D  96     1520   2055   2950    281    140   -379       C  
ATOM   3354  C   GLY D  96       1.817   2.779 -15.725  1.00 18.06           C  
ANISOU 3354  C   GLY D  96     1700   2107   3055    264     40   -121       C  
ATOM   3355  O   GLY D  96       2.967   3.029 -16.080  1.00 16.41           O  
ANISOU 3355  O   GLY D  96     1048   2056   3130    183   -184   -180       O  
ATOM   3356  N   GLY D  97       1.415   1.565 -15.336  1.00 18.80           N  
ANISOU 3356  N   GLY D  97     1908   2176   3061    208    299   -184       N  
ATOM   3357  CA  GLY D  97       2.363   0.464 -15.258  1.00 18.30           C  
ANISOU 3357  CA  GLY D  97     1722   2286   2944    392    293   -214       C  
ATOM   3358  C   GLY D  97       3.013   0.131 -16.586  1.00 18.95           C  
ANISOU 3358  C   GLY D  97     1567   2497   3137    526   -129   -624       C  
ATOM   3359  O   GLY D  97       4.131  -0.390 -16.620  1.00 17.47           O  
ANISOU 3359  O   GLY D  97     1050   2380   3206    306   -449   -753       O  
ATOM   3360  N   ASP D  98       2.337   0.431 -17.692  1.00 18.58           N  
ANISOU 3360  N   ASP D  98     1340   2788   2932    -25   -543   -680       N  
ATOM   3361  CA  ASP D  98       2.895   0.237 -19.024  1.00 19.58           C  
ANISOU 3361  CA  ASP D  98     1323   3101   3017     78    -95   -468       C  
ATOM   3362  C   ASP D  98       3.810   1.379 -19.454  1.00 17.99           C  
ANISOU 3362  C   ASP D  98     1128   2603   3105   -329    124   -509       C  
ATOM   3363  O   ASP D  98       4.231   1.411 -20.616  1.00 21.25           O  
ANISOU 3363  O   ASP D  98     1795   2865   3414   -362    476   -726       O  
ATOM   3364  CB  ASP D  98       1.767   0.058 -20.046  1.00 21.31           C  
ANISOU 3364  CB  ASP D  98     1422   3647   3028    443   -282   -114       C  
ATOM   3365  CG  ASP D  98       0.845   1.266 -20.124  1.00 25.62           C  
ANISOU 3365  CG  ASP D  98     2119   4372   3243    430    -79    -28       C  
ATOM   3366  OD1 ASP D  98       1.037   2.232 -19.354  1.00 25.09           O  
ANISOU 3366  OD1 ASP D  98     1860   4208   3464    455   -198    -36       O  
ATOM   3367  OD2 ASP D  98      -0.081   1.244 -20.961  1.00 29.47           O  
ANISOU 3367  OD2 ASP D  98     2940   4929   3327    173   -176    -23       O  
ATOM   3368  N   GLY D  99       4.111   2.316 -18.558  1.00 16.58           N  
ANISOU 3368  N   GLY D  99      914   2391   2994     54     55   -213       N  
ATOM   3369  CA  GLY D  99       4.999   3.414 -18.866  1.00 17.05           C  
ANISOU 3369  CA  GLY D  99     1372   2173   2932    157    568     43       C  
ATOM   3370  C   GLY D  99       4.355   4.601 -19.545  1.00 18.44           C  
ANISOU 3370  C   GLY D  99     1681   2219   3109    576   1069    130       C  
ATOM   3371  O   GLY D  99       5.037   5.610 -19.763  1.00 19.63           O  
ANISOU 3371  O   GLY D  99     1825   2423   3210    467   1126   -364       O  
ATOM   3372  N   LYS D 100       3.072   4.521 -19.882  1.00 18.10           N  
ANISOU 3372  N   LYS D 100     1555   2330   2991    713    898    364       N  
ATOM   3373  CA  LYS D 100       2.390   5.582 -20.608  1.00 21.90           C  
ANISOU 3373  CA  LYS D 100     2318   2711   3294   1232    959    264       C  
ATOM   3374  C   LYS D 100       1.666   6.520 -19.648  1.00 22.50           C  
ANISOU 3374  C   LYS D 100     2640   2688   3220    930   1149    120       C  
ATOM   3375  O   LYS D 100       1.169   6.106 -18.597  1.00 20.26           O  
ANISOU 3375  O   LYS D 100     1901   2695   3101    625   1190    -80       O  
ATOM   3376  CB  LYS D 100       1.390   4.994 -21.607  1.00 24.09           C  
ANISOU 3376  CB  LYS D 100     2728   3099   3326   1501    897     -6       C  
ATOM   3377  CG  LYS D 100       2.008   4.070 -22.647  1.00 26.23           C  
ANISOU 3377  CG  LYS D 100     3126   3347   3493   1432   1294    -94       C  
ATOM   3378  CD  LYS D 100       2.983   4.816 -23.541  1.00 29.26           C  
ANISOU 3378  CD  LYS D 100     3614   3870   3633   1254   1649   -425       C  
ATOM   3379  CE  LYS D 100       3.551   3.903 -24.617  1.00 32.37           C  
ANISOU 3379  CE  LYS D 100     4073   4211   4015   1566   1729   -379       C  
ATOM   3380  NZ  LYS D 100       4.481   4.627 -25.524  1.00 35.44           N  
ANISOU 3380  NZ  LYS D 100     4535   4691   4239   1829   1861   -244       N  
ATOM   3381  N   MET D 101       1.605   7.795 -20.028  1.00 24.95           N  
ANISOU 3381  N   MET D 101     3101   3026   3351    846   1357    -37       N  
ATOM   3382  CA  MET D 101       0.908   8.792 -19.227  1.00 24.98           C  
ANISOU 3382  CA  MET D 101     2992   3014   3484   1025   1492   -228       C  
ATOM   3383  C   MET D 101      -0.593   8.731 -19.482  1.00 27.02           C  
ANISOU 3383  C   MET D 101     3540   3180   3545   1004   1332   -414       C  
ATOM   3384  O   MET D 101      -1.041   8.644 -20.629  1.00 28.17           O  
ANISOU 3384  O   MET D 101     3681   3514   3509    982   1253   -293       O  
ATOM   3385  CB  MET D 101       1.431  10.195 -19.540  1.00 26.91           C  
ANISOU 3385  CB  MET D 101     3228   3183   3812   1327   1571    193       C  
ATOM   3386  CG  MET D 101       2.928  10.371 -19.338  1.00 31.50           C  
ANISOU 3386  CG  MET D 101     3719   3806   4442    823   1480    556       C  
ATOM   3387  SD  MET D 101       3.448  10.220 -17.618  1.00 39.02           S  
ANISOU 3387  SD  MET D 101     4834   4623   5370    363    873    502       S  
ATOM   3388  CE  MET D 101       2.819  11.742 -16.922  1.00 40.00           C  
ANISOU 3388  CE  MET D 101     5154   4697   5346    576    943    200       C  
ATOM   3389  N   LYS D 102      -1.369   8.775 -18.400  1.00 25.20           N  
ANISOU 3389  N   LYS D 102     3100   2973   3501    885   1496   -524       N  
ATOM   3390  CA  LYS D 102      -2.824   8.795 -18.461  1.00 26.32           C  
ANISOU 3390  CA  LYS D 102     3403   3043   3554    998   1171   -912       C  
ATOM   3391  C   LYS D 102      -3.337  10.088 -17.845  1.00 23.97           C  
ANISOU 3391  C   LYS D 102     3322   2719   3067   1216    917   -726       C  
ATOM   3392  O   LYS D 102      -2.837  10.532 -16.807  1.00 23.96           O  
ANISOU 3392  O   LYS D 102     3341   2692   3070   1387    662   -712       O  
ATOM   3393  CB  LYS D 102      -3.431   7.593 -17.726  1.00 30.12           C  
ANISOU 3393  CB  LYS D 102     3911   3715   3819    613   1285  -1171       C  
ATOM   3394  CG  LYS D 102      -3.120   6.236 -18.347  1.00 36.01           C  
ANISOU 3394  CG  LYS D 102     4720   4745   4219    -65   1075  -1138       C  
ATOM   3395  CD  LYS D 102      -3.972   5.965 -19.582  1.00 41.19           C  
ANISOU 3395  CD  LYS D 102     5488   5737   4425   -467    947  -1183       C  
ATOM   3396  CE  LYS D 102      -3.203   6.215 -20.871  1.00 45.95           C  
ANISOU 3396  CE  LYS D 102     6063   6630   4766   -860    587  -1069       C  
ATOM   3397  NZ  LYS D 102      -4.061   6.031 -22.076  1.00 48.18           N  
ANISOU 3397  NZ  LYS D 102     6333   7015   4959  -1046    483  -1096       N  
ATOM   3398  N   ASP D 103      -4.339  10.687 -18.484  1.00 21.65           N  
ANISOU 3398  N   ASP D 103     3029   2567   2629    911    987   -364       N  
ATOM   3399  CA  ASP D 103      -4.889  11.955 -18.022  1.00 21.30           C  
ANISOU 3399  CA  ASP D 103     2687   2967   2441    767   1276    151       C  
ATOM   3400  C   ASP D 103      -5.906  11.716 -16.915  1.00 17.80           C  
ANISOU 3400  C   ASP D 103     2511   2189   2061    223    862   -258       C  
ATOM   3401  O   ASP D 103      -6.893  11.001 -17.117  1.00 19.95           O  
ANISOU 3401  O   ASP D 103     3063   2316   2200   -152    865   -308       O  
ATOM   3402  CB  ASP D 103      -5.548  12.709 -19.176  1.00 28.49           C  
ANISOU 3402  CB  ASP D 103     3302   4460   3064   1201   1512    970       C  
ATOM   3403  CG  ASP D 103      -4.548  13.229 -20.185  1.00 36.08           C  
ANISOU 3403  CG  ASP D 103     4475   5801   3434   1058   1620   1907       C  
ATOM   3404  OD1 ASP D 103      -3.331  13.124 -19.933  1.00 38.32           O  
ANISOU 3404  OD1 ASP D 103     4794   6064   3703    917   1793   1980       O  
ATOM   3405  OD2 ASP D 103      -4.984  13.746 -21.234  1.00 41.76           O  
ANISOU 3405  OD2 ASP D 103     5348   6566   3952    745   1430   2014       O  
ATOM   3406  N   LEU D 104      -5.675  12.313 -15.750  1.00 12.19           N  
ANISOU 3406  N   LEU D 104     1468   1501   1664    514    620   -327       N  
ATOM   3407  CA  LEU D 104      -6.765  12.450 -14.801  1.00 11.78           C  
ANISOU 3407  CA  LEU D 104     1587   1377   1514    713    307   -330       C  
ATOM   3408  C   LEU D 104      -7.747  13.495 -15.323  1.00 12.07           C  
ANISOU 3408  C   LEU D 104     1475   1648   1463    283    402    -15       C  
ATOM   3409  O   LEU D 104      -7.406  14.335 -16.160  1.00 13.14           O  
ANISOU 3409  O   LEU D 104     1548   1866   1578   -437    694    453       O  
ATOM   3410  CB  LEU D 104      -6.244  12.851 -13.420  1.00 12.01           C  
ANISOU 3410  CB  LEU D 104     1527   1487   1550    203    350     14       C  
ATOM   3411  CG  LEU D 104      -5.318  11.858 -12.709  1.00 13.42           C  
ANISOU 3411  CG  LEU D 104     1734   1539   1825   -225   -203     24       C  
ATOM   3412  CD1 LEU D 104      -4.860  12.416 -11.369  1.00 13.57           C  
ANISOU 3412  CD1 LEU D 104     1566   1731   1860    207    -69    232       C  
ATOM   3413  CD2 LEU D 104      -6.007  10.515 -12.522  1.00 16.56           C  
ANISOU 3413  CD2 LEU D 104     1965   2018   2309   -662   -489    -73       C  
ATOM   3414  N   SER D 105      -8.980  13.429 -14.835  1.00  8.96           N  
ANISOU 3414  N   SER D 105      717   1223   1466    411    143    193       N  
ATOM   3415  CA  SER D 105      -9.980  14.402 -15.249  1.00 10.27           C  
ANISOU 3415  CA  SER D 105      934   1192   1776    508     23    158       C  
ATOM   3416  C   SER D 105      -9.477  15.815 -14.969  1.00 10.57           C  
ANISOU 3416  C   SER D 105     1041   1374   1603    192    -57    -87       C  
ATOM   3417  O   SER D 105      -8.968  16.081 -13.870  1.00 11.87           O  
ANISOU 3417  O   SER D 105     1330   1503   1678    -31    131   -301       O  
ATOM   3418  CB  SER D 105     -11.303  14.169 -14.523  1.00 13.02           C  
ANISOU 3418  CB  SER D 105     1316   1304   2328    282      9    140       C  
ATOM   3419  OG  SER D 105     -11.867  12.915 -14.861  1.00 14.29           O  
ANISOU 3419  OG  SER D 105     1424   1302   2704     30    -14      2       O  
ATOM   3420  N   PRO D 106      -9.573  16.732 -15.929  1.00 10.45           N  
ANISOU 3420  N   PRO D 106     1313   1271   1385   -215    148   -158       N  
ATOM   3421  CA  PRO D 106      -9.199  18.123 -15.652  1.00  9.38           C  
ANISOU 3421  CA  PRO D 106     1120   1079   1365   -134    304    -25       C  
ATOM   3422  C   PRO D 106     -10.057  18.707 -14.542  1.00 11.10           C  
ANISOU 3422  C   PRO D 106     1466   1464   1289   -389      9     19       C  
ATOM   3423  O   PRO D 106     -11.238  18.382 -14.401  1.00 10.57           O  
ANISOU 3423  O   PRO D 106     1450   1313   1253   -264    379     72       O  
ATOM   3424  CB  PRO D 106      -9.454  18.833 -16.987  1.00 11.25           C  
ANISOU 3424  CB  PRO D 106     1297   1415   1562   -193    514   -229       C  
ATOM   3425  CG  PRO D 106      -9.396  17.747 -18.014  1.00 12.69           C  
ANISOU 3425  CG  PRO D 106     2132   1104   1586   -272    593    -37       C  
ATOM   3426  CD  PRO D 106      -9.935  16.519 -17.340  1.00 12.29           C  
ANISOU 3426  CD  PRO D 106     1931   1352   1387   -305    600     96       C  
ATOM   3427  N   ARG D 107      -9.443  19.570 -13.738  1.00 11.16           N  
ANISOU 3427  N   ARG D 107     1335   1512   1391   -629   -123     54       N  
ATOM   3428  CA  ARG D 107     -10.134  20.287 -12.677  1.00  9.68           C  
ANISOU 3428  CA  ARG D 107      908   1310   1461     98    105    360       C  
ATOM   3429  C   ARG D 107     -10.118  21.775 -12.986  1.00 10.42           C  
ANISOU 3429  C   ARG D 107      834   1255   1868    312     22    -40       C  
ATOM   3430  O   ARG D 107      -9.089  22.322 -13.395  1.00 13.02           O  
ANISOU 3430  O   ARG D 107      756   1783   2407    386    195     20       O  
ATOM   3431  CB  ARG D 107      -9.491  20.022 -11.311  1.00 13.23           C  
ANISOU 3431  CB  ARG D 107     1966   1577   1483    398    429    683       C  
ATOM   3432  CG  ARG D 107      -9.644  18.589 -10.830  1.00 16.05           C  
ANISOU 3432  CG  ARG D 107     2329   2193   1576    385     34   1035       C  
ATOM   3433  CD  ARG D 107      -9.106  18.415  -9.421  1.00 22.46           C  
ANISOU 3433  CD  ARG D 107     2981   3627   1925    626   -318    908       C  
ATOM   3434  NE  ARG D 107      -7.683  18.732  -9.329  1.00 26.44           N  
ANISOU 3434  NE  ARG D 107     3392   4307   2345    885   -214    359       N  
ATOM   3435  CZ  ARG D 107      -6.930  18.483  -8.261  1.00 30.24           C  
ANISOU 3435  CZ  ARG D 107     3892   4910   2688    845    -55   -173       C  
ATOM   3436  NH1 ARG D 107      -5.643  18.806  -8.266  1.00 31.12           N  
ANISOU 3436  NH1 ARG D 107     3776   5107   2939    558    -76   -688       N  
ATOM   3437  NH2 ARG D 107      -7.462  17.909  -7.190  1.00 31.70           N  
ANISOU 3437  NH2 ARG D 107     4359   4941   2745   1282   -201    103       N  
ATOM   3438  N   TRP D 108     -11.263  22.425 -12.801  1.00  8.23           N  
ANISOU 3438  N   TRP D 108      916    897   1314    469   -274     34       N  
ATOM   3439  CA  TRP D 108     -11.417  23.847 -13.073  1.00  7.17           C  
ANISOU 3439  CA  TRP D 108      874    746   1106    295    -81     95       C  
ATOM   3440  C   TRP D 108     -11.613  24.595 -11.760  1.00  6.66           C  
ANISOU 3440  C   TRP D 108      557    868   1107     73     92   -342       C  
ATOM   3441  O   TRP D 108     -12.511  24.260 -10.980  1.00  8.54           O  
ANISOU 3441  O   TRP D 108      580   1246   1417    -11    -84   -146       O  
ATOM   3442  CB  TRP D 108     -12.596  24.097 -14.016  1.00  6.99           C  
ANISOU 3442  CB  TRP D 108      825   1044    786    272   -365   -168       C  
ATOM   3443  CG  TRP D 108     -12.414  23.518 -15.396  1.00  9.30           C  
ANISOU 3443  CG  TRP D 108     1572   1114    846    705   -247   -158       C  
ATOM   3444  CD1 TRP D 108     -12.486  22.199 -15.752  1.00  9.30           C  
ANISOU 3444  CD1 TRP D 108     1603   1215    714    709    138    -90       C  
ATOM   3445  CD2 TRP D 108     -12.151  24.244 -16.605  1.00  8.73           C  
ANISOU 3445  CD2 TRP D 108     1178   1148    990    687    168    127       C  
ATOM   3446  NE1 TRP D 108     -12.276  22.061 -17.104  1.00 10.62           N  
ANISOU 3446  NE1 TRP D 108     2132   1149    755    410    396    255       N  
ATOM   3447  CE2 TRP D 108     -12.068  23.300 -17.650  1.00  9.84           C  
ANISOU 3447  CE2 TRP D 108     1595   1188    958    506    536    456       C  
ATOM   3448  CE3 TRP D 108     -11.970  25.599 -16.904  1.00  8.46           C  
ANISOU 3448  CE3 TRP D 108      802   1313   1098    546    211    104       C  
ATOM   3449  CZ2 TRP D 108     -11.816  23.668 -18.972  1.00 11.87           C  
ANISOU 3449  CZ2 TRP D 108     1766   1237   1508    399    626    575       C  
ATOM   3450  CZ3 TRP D 108     -11.722  25.964 -18.216  1.00  9.47           C  
ANISOU 3450  CZ3 TRP D 108     1086   1264   1247    560    341   -161       C  
ATOM   3451  CH2 TRP D 108     -11.645  25.001 -19.234  1.00 11.56           C  
ANISOU 3451  CH2 TRP D 108     1942    920   1531    328    636    220       C  
ATOM   3452  N   TYR D 109     -10.774  25.603 -11.524  1.00  6.77           N  
ANISOU 3452  N   TYR D 109      995    442   1137   -123     83   -292       N  
ATOM   3453  CA  TYR D 109     -10.772  26.383 -10.292  1.00  8.18           C  
ANISOU 3453  CA  TYR D 109     1163    850   1096    267    138   -227       C  
ATOM   3454  C   TYR D 109     -11.168  27.825 -10.581  1.00  8.64           C  
ANISOU 3454  C   TYR D 109     1087   1104   1092     88     71     71       C  
ATOM   3455  O   TYR D 109     -10.709  28.417 -11.563  1.00 10.59           O  
ANISOU 3455  O   TYR D 109     1203   1326   1495    379     -1    224       O  
ATOM   3456  CB  TYR D 109      -9.387  26.371  -9.632  1.00  7.08           C  
ANISOU 3456  CB  TYR D 109      766    709   1216    -86    107     98       C  
ATOM   3457  CG  TYR D 109      -8.951  25.036  -9.077  1.00  9.04           C  
ANISOU 3457  CG  TYR D 109     1008    925   1503     -2    531     25       C  
ATOM   3458  CD1 TYR D 109      -8.294  24.110  -9.876  1.00  9.72           C  
ANISOU 3458  CD1 TYR D 109      739    970   1984    286    304    130       C  
ATOM   3459  CD2 TYR D 109      -9.178  24.711  -7.745  1.00 12.29           C  
ANISOU 3459  CD2 TYR D 109     1576   1434   1658   -159    278    356       C  
ATOM   3460  CE1 TYR D 109      -7.885  22.891  -9.367  1.00 11.30           C  
ANISOU 3460  CE1 TYR D 109      817   1388   2090    409    347    180       C  
ATOM   3461  CE2 TYR D 109      -8.772  23.497  -7.227  1.00 12.17           C  
ANISOU 3461  CE2 TYR D 109     1082   1555   1987    316     88    253       C  
ATOM   3462  CZ  TYR D 109      -8.128  22.591  -8.044  1.00 13.40           C  
ANISOU 3462  CZ  TYR D 109      984   1779   2327    554    -23    319       C  
ATOM   3463  OH  TYR D 109      -7.726  21.383  -7.532  1.00 16.18           O  
ANISOU 3463  OH  TYR D 109     1153   2400   2595    666     41    500       O  
ATOM   3464  N   PHE D 110     -11.993  28.401  -9.708  1.00  7.30           N  
ANISOU 3464  N   PHE D 110      892    738   1143    335    543    409       N  
ATOM   3465  CA  PHE D 110     -12.435  29.780  -9.871  1.00  7.89           C  
ANISOU 3465  CA  PHE D 110      685   1081   1231    437    226    119       C  
ATOM   3466  C   PHE D 110     -11.484  30.753  -9.184  1.00  6.76           C  
ANISOU 3466  C   PHE D 110      491   1112    966    225    271    197       C  
ATOM   3467  O   PHE D 110     -11.072  30.542  -8.038  1.00  7.19           O  
ANISOU 3467  O   PHE D 110      367   1343   1023    -37     27    219       O  
ATOM   3468  CB  PHE D 110     -13.847  29.981  -9.316  1.00  6.65           C  
ANISOU 3468  CB  PHE D 110      484    986   1057    315    176     21       C  
ATOM   3469  CG  PHE D 110     -14.307  31.417  -9.348  1.00  7.09           C  
ANISOU 3469  CG  PHE D 110      540    927   1226    357    106     47       C  
ATOM   3470  CD1 PHE D 110     -14.848  31.958 -10.506  1.00  7.56           C  
ANISOU 3470  CD1 PHE D 110      693    850   1327    409     54    132       C  
ATOM   3471  CD2 PHE D 110     -14.183  32.229  -8.227  1.00  6.85           C  
ANISOU 3471  CD2 PHE D 110      432   1029   1143    163    235    206       C  
ATOM   3472  CE1 PHE D 110     -15.266  33.281 -10.545  1.00  7.79           C  
ANISOU 3472  CE1 PHE D 110      736    677   1546    268    312    232       C  
ATOM   3473  CE2 PHE D 110     -14.595  33.556  -8.259  1.00  5.77           C  
ANISOU 3473  CE2 PHE D 110      473    723    998    182    209    472       C  
ATOM   3474  CZ  PHE D 110     -15.139  34.081  -9.420  1.00  7.07           C  
ANISOU 3474  CZ  PHE D 110      589    897   1201    213    385    267       C  
ATOM   3475  N   TYR D 111     -11.163  31.836  -9.889  1.00  5.71           N  
ANISOU 3475  N   TYR D 111      343    925    903   -125     62    257       N  
ATOM   3476  CA  TYR D 111     -10.403  32.954  -9.351  1.00  6.06           C  
ANISOU 3476  CA  TYR D 111      294   1032    977    -13    152     23       C  
ATOM   3477  C   TYR D 111     -11.137  34.249  -9.658  1.00  6.51           C  
ANISOU 3477  C   TYR D 111      435   1107    932     42    202   -297       C  
ATOM   3478  O   TYR D 111     -11.610  34.452 -10.782  1.00  8.12           O  
ANISOU 3478  O   TYR D 111      675   1355   1055     56    -10   -312       O  
ATOM   3479  CB  TYR D 111      -8.991  33.020  -9.944  1.00  7.36           C  
ANISOU 3479  CB  TYR D 111      430   1215   1152     59    256    158       C  
ATOM   3480  CG  TYR D 111      -8.106  31.861  -9.558  1.00  8.04           C  
ANISOU 3480  CG  TYR D 111      712   1070   1272    375    357    458       C  
ATOM   3481  CD1 TYR D 111      -7.337  31.908  -8.404  1.00  9.64           C  
ANISOU 3481  CD1 TYR D 111      830   1581   1254    447    381    771       C  
ATOM   3482  CD2 TYR D 111      -8.033  30.723 -10.352  1.00  9.71           C  
ANISOU 3482  CD2 TYR D 111     1148   1113   1428    510    616    398       C  
ATOM   3483  CE1 TYR D 111      -6.522  30.854  -8.046  1.00 12.49           C  
ANISOU 3483  CE1 TYR D 111     1336   2009   1401    375    205    758       C  
ATOM   3484  CE2 TYR D 111      -7.221  29.660 -10.000  1.00 11.47           C  
ANISOU 3484  CE2 TYR D 111     1356   1294   1706    585    438    281       C  
ATOM   3485  CZ  TYR D 111      -6.467  29.733  -8.847  1.00 12.71           C  
ANISOU 3485  CZ  TYR D 111     1565   1608   1656    467    207    619       C  
ATOM   3486  OH  TYR D 111      -5.654  28.685  -8.492  1.00 14.23           O  
ANISOU 3486  OH  TYR D 111     1601   1984   1822    572   -241    704       O  
ATOM   3487  N   TYR D 112     -11.224  35.126  -8.663  1.00  6.15           N  
ANISOU 3487  N   TYR D 112      744    583   1010    -90    266   -163       N  
ATOM   3488  CA  TYR D 112     -11.844  36.422  -8.891  1.00  7.62           C  
ANISOU 3488  CA  TYR D 112     1257    727    913     65    280   -268       C  
ATOM   3489  C   TYR D 112     -11.035  37.219  -9.907  1.00  7.69           C  
ANISOU 3489  C   TYR D 112     1015    757   1149   -283    322    286       C  
ATOM   3490  O   TYR D 112      -9.816  37.060 -10.026  1.00  8.09           O  
ANISOU 3490  O   TYR D 112      861   1094   1119   -119    379    278       O  
ATOM   3491  CB  TYR D 112     -11.972  37.197  -7.577  1.00  7.07           C  
ANISOU 3491  CB  TYR D 112      943    961    782    240    343   -278       C  
ATOM   3492  CG  TYR D 112     -13.055  36.652  -6.678  1.00  9.02           C  
ANISOU 3492  CG  TYR D 112     1128   1245   1055    427    284     35       C  
ATOM   3493  CD1 TYR D 112     -14.383  37.029  -6.849  1.00  8.71           C  
ANISOU 3493  CD1 TYR D 112      959   1299   1051    109    298   -122       C  
ATOM   3494  CD2 TYR D 112     -12.756  35.747  -5.668  1.00  8.12           C  
ANISOU 3494  CD2 TYR D 112      977   1147    959    381    113   -109       C  
ATOM   3495  CE1 TYR D 112     -15.378  36.526  -6.034  1.00  9.18           C  
ANISOU 3495  CE1 TYR D 112      974   1358   1157    -64    274   -323       C  
ATOM   3496  CE2 TYR D 112     -13.742  35.238  -4.850  1.00 10.03           C  
ANISOU 3496  CE2 TYR D 112      976   1467   1368    327    163   -171       C  
ATOM   3497  CZ  TYR D 112     -15.051  35.629  -5.037  1.00  9.54           C  
ANISOU 3497  CZ  TYR D 112      802   1479   1346    303     67     -7       C  
ATOM   3498  OH  TYR D 112     -16.032  35.118  -4.219  1.00 12.31           O  
ANISOU 3498  OH  TYR D 112     1165   1810   1702    170    -33   -149       O  
ATOM   3499  N   LEU D 113     -11.738  38.060 -10.663  1.00  6.96           N  
ANISOU 3499  N   LEU D 113      730    780   1136   -285    182    299       N  
ATOM   3500  CA  LEU D 113     -11.099  38.919 -11.653  1.00  8.10           C  
ANISOU 3500  CA  LEU D 113      896    867   1315   -241    -96    560       C  
ATOM   3501  C   LEU D 113      -9.936  39.686 -11.037  1.00 10.55           C  
ANISOU 3501  C   LEU D 113     1358   1083   1566   -353     75    284       C  
ATOM   3502  O   LEU D 113     -10.054  40.248  -9.945  1.00 10.37           O  
ANISOU 3502  O   LEU D 113     1504   1028   1408   -215    242     43       O  
ATOM   3503  CB  LEU D 113     -12.128  39.891 -12.226  1.00  8.19           C  
ANISOU 3503  CB  LEU D 113      917    702   1493    -41    124    492       C  
ATOM   3504  CG  LEU D 113     -11.585  40.947 -13.182  1.00  9.25           C  
ANISOU 3504  CG  LEU D 113     1407    569   1538      3    157    307       C  
ATOM   3505  CD1 LEU D 113     -11.106  40.291 -14.470  1.00 11.68           C  
ANISOU 3505  CD1 LEU D 113     1620    909   1911   -377   -152    -40       C  
ATOM   3506  CD2 LEU D 113     -12.652  41.997 -13.458  1.00  9.57           C  
ANISOU 3506  CD2 LEU D 113     1650    530   1454    145    428    -49       C  
ATOM   3507  N   GLY D 114      -8.804  39.695 -11.738  1.00  9.07           N  
ANISOU 3507  N   GLY D 114      862   1212   1373    -95   -110    213       N  
ATOM   3508  CA  GLY D 114      -7.624  40.381 -11.255  1.00  9.95           C  
ANISOU 3508  CA  GLY D 114      760   1491   1531   -341   -333    -96       C  
ATOM   3509  C   GLY D 114      -6.839  39.651 -10.189  1.00 10.97           C  
ANISOU 3509  C   GLY D 114      780   1642   1747   -481   -319   -156       C  
ATOM   3510  O   GLY D 114      -5.958  40.260  -9.569  1.00 12.63           O  
ANISOU 3510  O   GLY D 114      991   1808   2000   -607   -400   -128       O  
ATOM   3511  N   THR D 115      -7.129  38.373  -9.947  1.00  8.38           N  
ANISOU 3511  N   THR D 115      467   1291   1425   -269    104   -100       N  
ATOM   3512  CA  THR D 115      -6.402  37.565  -8.978  1.00  9.91           C  
ANISOU 3512  CA  THR D 115      784   1614   1366    -53    160    -99       C  
ATOM   3513  C   THR D 115      -5.944  36.271  -9.634  1.00 11.07           C  
ANISOU 3513  C   THR D 115      937   1738   1531    171    166    348       C  
ATOM   3514  O   THR D 115      -6.411  35.888 -10.710  1.00 10.89           O  
ANISOU 3514  O   THR D 115     1115   1576   1448    256    152    329       O  
ATOM   3515  CB  THR D 115      -7.255  37.221  -7.744  1.00  9.15           C  
ANISOU 3515  CB  THR D 115      586   1637   1252   -156    302   -309       C  
ATOM   3516  OG1 THR D 115      -8.228  36.229  -8.095  1.00  8.78           O  
ANISOU 3516  OG1 THR D 115      595   1798    941     39    184   -211       O  
ATOM   3517  CG2 THR D 115      -7.958  38.455  -7.194  1.00 10.09           C  
ANISOU 3517  CG2 THR D 115      779   1803   1252    193    419   -236       C  
ATOM   3518  N   GLY D 116      -5.020  35.590  -8.962  1.00 12.40           N  
ANISOU 3518  N   GLY D 116     1014   1955   1742   -387   -157    375       N  
ATOM   3519  CA  GLY D 116      -4.652  34.244  -9.328  1.00 13.39           C  
ANISOU 3519  CA  GLY D 116     1347   1996   1747   -443   -172      5       C  
ATOM   3520  C   GLY D 116      -3.616  34.163 -10.428  1.00 12.67           C  
ANISOU 3520  C   GLY D 116     1025   2072   1716   -764    -36    -59       C  
ATOM   3521  O   GLY D 116      -2.949  35.146 -10.770  1.00 12.22           O  
ANISOU 3521  O   GLY D 116      969   2189   1485   -355     49    111       O  
ATOM   3522  N   PRO D 117      -3.462  32.967 -11.002  1.00 13.78           N  
ANISOU 3522  N   PRO D 117     1023   2368   1846   -394     43    -22       N  
ATOM   3523  CA  PRO D 117      -2.443  32.777 -12.047  1.00 14.89           C  
ANISOU 3523  CA  PRO D 117     1153   2541   1965    -35     67     84       C  
ATOM   3524  C   PRO D 117      -2.636  33.670 -13.260  1.00 15.00           C  
ANISOU 3524  C   PRO D 117     1167   2549   1985    240    234    130       C  
ATOM   3525  O   PRO D 117      -1.652  34.004 -13.931  1.00 17.45           O  
ANISOU 3525  O   PRO D 117     1157   3027   2447    -19    410    181       O  
ATOM   3526  CB  PRO D 117      -2.594  31.294 -12.413  1.00 15.43           C  
ANISOU 3526  CB  PRO D 117     1389   2553   1922    248     41     51       C  
ATOM   3527  CG  PRO D 117      -3.242  30.667 -11.225  1.00 17.08           C  
ANISOU 3527  CG  PRO D 117     1796   2691   2003    541     99   -137       C  
ATOM   3528  CD  PRO D 117      -4.154  31.713 -10.662  1.00 14.77           C  
ANISOU 3528  CD  PRO D 117     1437   2368   1806    385    326     24       C  
ATOM   3529  N   GLU D 118      -3.867  34.066 -13.569  1.00 12.70           N  
ANISOU 3529  N   GLU D 118     1124   2049   1652    552   -146    191       N  
ATOM   3530  CA  GLU D 118      -4.144  34.960 -14.687  1.00 13.64           C  
ANISOU 3530  CA  GLU D 118     1458   1976   1747    232   -134    111       C  
ATOM   3531  C   GLU D 118      -4.681  36.305 -14.205  1.00 12.81           C  
ANISOU 3531  C   GLU D 118     1367   1864   1638    138     23    -76       C  
ATOM   3532  O   GLU D 118      -5.609  36.870 -14.789  1.00 12.73           O  
ANISOU 3532  O   GLU D 118     1498   1811   1527   -130   -281   -102       O  
ATOM   3533  CB  GLU D 118      -5.113  34.311 -15.672  1.00 15.97           C  
ANISOU 3533  CB  GLU D 118     1812   2131   2123   -249     27     -6       C  
ATOM   3534  CG  GLU D 118      -4.549  33.080 -16.379  1.00 19.05           C  
ANISOU 3534  CG  GLU D 118     2178   2461   2597   -915    101   -125       C  
ATOM   3535  CD  GLU D 118      -3.403  33.404 -17.327  1.00 22.80           C  
ANISOU 3535  CD  GLU D 118     2895   2639   3129   -332    231   -426       C  
ATOM   3536  OE1 GLU D 118      -3.165  34.596 -17.615  1.00 25.17           O  
ANISOU 3536  OE1 GLU D 118     3309   3013   3243   -171    468   -459       O  
ATOM   3537  OE2 GLU D 118      -2.737  32.458 -17.792  1.00 24.84           O  
ANISOU 3537  OE2 GLU D 118     3118   2865   3453    -90    421   -213       O  
ATOM   3538  N   ALA D 119      -4.080  36.836 -13.135  1.00 11.32           N  
ANISOU 3538  N   ALA D 119     1314   1605   1383   -226    226   -191       N  
ATOM   3539  CA  ALA D 119      -4.533  38.103 -12.568  1.00 13.18           C  
ANISOU 3539  CA  ALA D 119     1790   1742   1474   -618    -15   -295       C  
ATOM   3540  C   ALA D 119      -4.413  39.250 -13.563  1.00 14.11           C  
ANISOU 3540  C   ALA D 119     1852   1735   1775   -568    114    -42       C  
ATOM   3541  O   ALA D 119      -5.150  40.237 -13.462  1.00 14.09           O  
ANISOU 3541  O   ALA D 119     1651   1708   1995   -418    496    221       O  
ATOM   3542  CB  ALA D 119      -3.738  38.423 -11.302  1.00 16.46           C  
ANISOU 3542  CB  ALA D 119     2317   2276   1660   -239    -72   -414       C  
ATOM   3543  N   GLY D 120      -3.495  39.144 -14.523  1.00 14.79           N  
ANISOU 3543  N   GLY D 120     1916   2162   1543   -959    -52    343       N  
ATOM   3544  CA  GLY D 120      -3.292  40.211 -15.484  1.00 16.89           C  
ANISOU 3544  CA  GLY D 120     1864   2687   1867   -929   -234    405       C  
ATOM   3545  C   GLY D 120      -4.265  40.242 -16.643  1.00 17.23           C  
ANISOU 3545  C   GLY D 120     1969   2699   1877   -962   -200    219       C  
ATOM   3546  O   GLY D 120      -4.274  41.225 -17.391  1.00 20.06           O  
ANISOU 3546  O   GLY D 120     2460   2977   2184  -1528   -244    641       O  
ATOM   3547  N   LEU D 121      -5.091  39.200 -16.811  1.00 14.31           N  
ANISOU 3547  N   LEU D 121     1347   2289   1800   -903    -42      9       N  
ATOM   3548  CA  LEU D 121      -5.989  39.153 -17.959  1.00 13.58           C  
ANISOU 3548  CA  LEU D 121     1593   1882   1684   -560     90   -385       C  
ATOM   3549  C   LEU D 121      -7.219  40.024 -17.713  1.00 13.51           C  
ANISOU 3549  C   LEU D 121     1724   1859   1550   -250    352   -341       C  
ATOM   3550  O   LEU D 121      -7.782  40.011 -16.614  1.00 15.46           O  
ANISOU 3550  O   LEU D 121     2131   2025   1717   -184    547   -342       O  
ATOM   3551  CB  LEU D 121      -6.433  37.719 -18.248  1.00 13.47           C  
ANISOU 3551  CB  LEU D 121     1494   1814   1811   -318    197   -370       C  
ATOM   3552  CG  LEU D 121      -5.371  36.722 -18.714  1.00 15.44           C  
ANISOU 3552  CG  LEU D 121     1579   2088   2200    -38    481   -684       C  
ATOM   3553  CD1 LEU D 121      -6.007  35.379 -19.044  1.00 15.90           C  
ANISOU 3553  CD1 LEU D 121     1390   2140   2510    175    264   -535       C  
ATOM   3554  CD2 LEU D 121      -4.615  37.271 -19.914  1.00 17.69           C  
ANISOU 3554  CD2 LEU D 121     1742   2696   2283     95    766   -443       C  
ATOM   3555  N   PRO D 122      -7.658  40.782 -18.714  1.00 11.40           N  
ANISOU 3555  N   PRO D 122     1208   1784   1340   -300    331    157       N  
ATOM   3556  CA  PRO D 122      -8.938  41.483 -18.597  1.00 13.87           C  
ANISOU 3556  CA  PRO D 122     1703   1946   1619   -464    301    410       C  
ATOM   3557  C   PRO D 122     -10.093  40.510 -18.767  1.00 12.75           C  
ANISOU 3557  C   PRO D 122     1675   1500   1668   -621    257    566       C  
ATOM   3558  O   PRO D 122      -9.955  39.439 -19.364  1.00 12.66           O  
ANISOU 3558  O   PRO D 122     2089   1305   1415   -501    -41    119       O  
ATOM   3559  CB  PRO D 122      -8.891  42.491 -19.746  1.00 13.50           C  
ANISOU 3559  CB  PRO D 122     1468   2009   1651   -253    441    433       C  
ATOM   3560  CG  PRO D 122      -8.068  41.800 -20.783  1.00 14.18           C  
ANISOU 3560  CG  PRO D 122     1676   2102   1608    -92    121    416       C  
ATOM   3561  CD  PRO D 122      -7.026  41.003 -20.026  1.00 12.13           C  
ANISOU 3561  CD  PRO D 122     1311   1925   1374   -175    -87    611       C  
ATOM   3562  N   TYR D 123     -11.247  40.897 -18.225  1.00 10.10           N  
ANISOU 3562  N   TYR D 123      991   1373   1475    103    182    592       N  
ATOM   3563  CA  TYR D 123     -12.434  40.060 -18.345  1.00 10.04           C  
ANISOU 3563  CA  TYR D 123     1005   1653   1156   -581    156    326       C  
ATOM   3564  C   TYR D 123     -12.753  39.798 -19.811  1.00 10.39           C  
ANISOU 3564  C   TYR D 123     1171   1680   1097   -291     42    149       C  
ATOM   3565  O   TYR D 123     -12.790  40.723 -20.626  1.00 11.20           O  
ANISOU 3565  O   TYR D 123     1297   1750   1209   -610     20    518       O  
ATOM   3566  CB  TYR D 123     -13.635  40.716 -17.666  1.00 10.54           C  
ANISOU 3566  CB  TYR D 123     1010   1877   1116   -680    167    118       C  
ATOM   3567  CG  TYR D 123     -14.861  39.831 -17.681  1.00 11.54           C  
ANISOU 3567  CG  TYR D 123     1018   2036   1330   -556    236      2       C  
ATOM   3568  CD1 TYR D 123     -15.043  38.857 -16.711  1.00 10.85           C  
ANISOU 3568  CD1 TYR D 123     1092   1713   1318   -364    571    241       C  
ATOM   3569  CD2 TYR D 123     -15.825  39.952 -18.677  1.00 14.23           C  
ANISOU 3569  CD2 TYR D 123     1240   2349   1818   -279    446    104       C  
ATOM   3570  CE1 TYR D 123     -16.152  38.035 -16.719  1.00 11.37           C  
ANISOU 3570  CE1 TYR D 123      946   1908   1466   -318    568    114       C  
ATOM   3571  CE2 TYR D 123     -16.941  39.130 -18.695  1.00 15.28           C  
ANISOU 3571  CE2 TYR D 123     1234   2744   1829   -374    639    298       C  
ATOM   3572  CZ  TYR D 123     -17.098  38.173 -17.710  1.00 14.39           C  
ANISOU 3572  CZ  TYR D 123     1189   2623   1657   -407    573    254       C  
ATOM   3573  OH  TYR D 123     -18.201  37.348 -17.710  1.00 16.02           O  
ANISOU 3573  OH  TYR D 123     1527   2983   1577   -359    593    131       O  
ATOM   3574  N   GLY D 124     -12.988  38.530 -20.141  1.00  9.77           N  
ANISOU 3574  N   GLY D 124     1291   1493    930   -289   -272    225       N  
ATOM   3575  CA  GLY D 124     -13.283  38.140 -21.503  1.00 10.42           C  
ANISOU 3575  CA  GLY D 124     1607   1414    940    620      7    197       C  
ATOM   3576  C   GLY D 124     -12.081  37.762 -22.338  1.00 10.42           C  
ANISOU 3576  C   GLY D 124     1841   1162    955    487     84    454       C  
ATOM   3577  O   GLY D 124     -12.255  37.406 -23.511  1.00 12.36           O  
ANISOU 3577  O   GLY D 124     1822   1720   1156    219    288    531       O  
ATOM   3578  N   ALA D 125     -10.874  37.822 -21.776  1.00 10.32           N  
ANISOU 3578  N   ALA D 125     1847   1097    977    765    239     68       N  
ATOM   3579  CA  ALA D 125      -9.673  37.477 -22.525  1.00 12.03           C  
ANISOU 3579  CA  ALA D 125     2197   1248   1123    277    -87   -312       C  
ATOM   3580  C   ALA D 125      -9.779  36.070 -23.100  1.00 13.04           C  
ANISOU 3580  C   ALA D 125     2378   1478   1100    -85    127    163       C  
ATOM   3581  O   ALA D 125     -10.210  35.130 -22.426  1.00 12.95           O  
ANISOU 3581  O   ALA D 125     2208   1641   1073     89    386    634       O  
ATOM   3582  CB  ALA D 125      -8.438  37.588 -21.632  1.00 12.98           C  
ANISOU 3582  CB  ALA D 125     2028   1568   1334     12   -302   -359       C  
ATOM   3583  N   ASN D 126      -9.380  35.939 -24.362  1.00 13.95           N  
ANISOU 3583  N   ASN D 126     2516   1682   1101    -30    199   -241       N  
ATOM   3584  CA  ASN D 126      -9.499  34.695 -25.112  1.00 17.18           C  
ANISOU 3584  CA  ASN D 126     3168   1919   1441    -21    574   -200       C  
ATOM   3585  C   ASN D 126      -8.217  33.891 -24.920  1.00 19.13           C  
ANISOU 3585  C   ASN D 126     3470   1907   1890     84    942     31       C  
ATOM   3586  O   ASN D 126      -7.175  34.229 -25.490  1.00 21.41           O  
ANISOU 3586  O   ASN D 126     3854   1754   2525    405   1025    325       O  
ATOM   3587  CB  ASN D 126      -9.754  35.004 -26.586  1.00 19.92           C  
ANISOU 3587  CB  ASN D 126     3865   2231   1474   -520    604   -665       C  
ATOM   3588  CG  ASN D 126     -10.283  33.815 -27.356  1.00 25.35           C  
ANISOU 3588  CG  ASN D 126     4655   3249   1729   -742    245   -424       C  
ATOM   3589  OD1 ASN D 126     -10.700  32.814 -26.773  1.00 28.59           O  
ANISOU 3589  OD1 ASN D 126     5039   3772   2052  -1068    309   -416       O  
ATOM   3590  ND2 ASN D 126     -10.280  33.923 -28.681  1.00 25.77           N  
ANISOU 3590  ND2 ASN D 126     4659   3260   1874   -488     46   -364       N  
ATOM   3591  N   LYS D 127      -8.292  32.832 -24.114  1.00 17.91           N  
ANISOU 3591  N   LYS D 127     3137   2045   1623   -412    860    -42       N  
ATOM   3592  CA  LYS D 127      -7.119  32.028 -23.790  1.00 18.28           C  
ANISOU 3592  CA  LYS D 127     3113   2135   1698   -446    971   -346       C  
ATOM   3593  C   LYS D 127      -7.558  30.607 -23.472  1.00 17.07           C  
ANISOU 3593  C   LYS D 127     3075   1761   1652     12   1166   -179       C  
ATOM   3594  O   LYS D 127      -8.515  30.410 -22.717  1.00 16.67           O  
ANISOU 3594  O   LYS D 127     2869   1593   1871   -346   1213    122       O  
ATOM   3595  CB  LYS D 127      -6.354  32.622 -22.600  1.00 20.52           C  
ANISOU 3595  CB  LYS D 127     3126   2826   1844   -564    975   -263       C  
ATOM   3596  CG  LYS D 127      -4.991  31.988 -22.351  1.00 22.27           C  
ANISOU 3596  CG  LYS D 127     3275   3007   2178   -300    879   -163       C  
ATOM   3597  CD  LYS D 127      -4.344  32.547 -21.091  1.00 24.22           C  
ANISOU 3597  CD  LYS D 127     3502   3038   2661   -354    907     -6       C  
ATOM   3598  CE  LYS D 127      -2.835  32.353 -21.108  1.00 27.71           C  
ANISOU 3598  CE  LYS D 127     4147   3240   3141   -293    736    157       C  
ATOM   3599  NZ  LYS D 127      -2.449  30.944 -21.385  1.00 30.40           N  
ANISOU 3599  NZ  LYS D 127     4418   3619   3513   -442    627    383       N  
ATOM   3600  N   ASP D 128      -6.856  29.627 -24.038  1.00 16.86           N  
ANISOU 3600  N   ASP D 128     3085   1723   1597    191   1102   -209       N  
ATOM   3601  CA  ASP D 128      -7.202  28.232 -23.797  1.00 18.57           C  
ANISOU 3601  CA  ASP D 128     3129   2218   1708    304    979     72       C  
ATOM   3602  C   ASP D 128      -7.074  27.898 -22.316  1.00 14.49           C  
ANISOU 3602  C   ASP D 128     2076   2104   1327    363    613     73       C  
ATOM   3603  O   ASP D 128      -6.107  28.285 -21.654  1.00 14.72           O  
ANISOU 3603  O   ASP D 128     1737   2268   1589    798    620    284       O  
ATOM   3604  CB  ASP D 128      -6.308  27.310 -24.625  1.00 22.83           C  
ANISOU 3604  CB  ASP D 128     3883   2689   2101    691    975     68       C  
ATOM   3605  CG  ASP D 128      -6.661  25.843 -24.450  1.00 29.11           C  
ANISOU 3605  CG  ASP D 128     4627   3893   2542    880    607    176       C  
ATOM   3606  OD1 ASP D 128      -7.835  25.478 -24.678  1.00 29.65           O  
ANISOU 3606  OD1 ASP D 128     4624   4150   2491    741    410     78       O  
ATOM   3607  OD2 ASP D 128      -5.764  25.052 -24.087  1.00 33.37           O  
ANISOU 3607  OD2 ASP D 128     5396   4309   2975    729    619    311       O  
ATOM   3608  N   GLY D 129      -8.064  27.175 -21.796  1.00 11.75           N  
ANISOU 3608  N   GLY D 129     1283   2158   1023    -45    508   -226       N  
ATOM   3609  CA  GLY D 129      -8.099  26.826 -20.392  1.00 11.71           C  
ANISOU 3609  CA  GLY D 129     1462   2044    942    -62    371   -142       C  
ATOM   3610  C   GLY D 129      -8.642  27.900 -19.476  1.00 10.92           C  
ANISOU 3610  C   GLY D 129     1623   1582    945     -6    599   -184       C  
ATOM   3611  O   GLY D 129      -8.645  27.703 -18.255  1.00 11.25           O  
ANISOU 3611  O   GLY D 129     1741   1498   1036    -88    553    -67       O  
ATOM   3612  N   ILE D 130      -9.103  29.025 -20.020  1.00 11.51           N  
ANISOU 3612  N   ILE D 130     1882   1414   1078     62    618    132       N  
ATOM   3613  CA  ILE D 130      -9.650  30.127 -19.241  1.00 11.45           C  
ANISOU 3613  CA  ILE D 130     1696   1309   1346   -108    392    246       C  
ATOM   3614  C   ILE D 130     -11.051  30.424 -19.754  1.00 11.33           C  
ANISOU 3614  C   ILE D 130     1729   1222   1353   -330    573    -25       C  
ATOM   3615  O   ILE D 130     -11.238  30.654 -20.953  1.00 11.73           O  
ANISOU 3615  O   ILE D 130     1727   1596   1132   -151    158     67       O  
ATOM   3616  CB  ILE D 130      -8.771  31.389 -19.339  1.00 11.86           C  
ANISOU 3616  CB  ILE D 130     1698   1477   1331    -39    543     97       C  
ATOM   3617  CG1 ILE D 130      -7.351  31.098 -18.849  1.00 10.61           C  
ANISOU 3617  CG1 ILE D 130     1421   1464   1146   -121    440    185       C  
ATOM   3618  CG2 ILE D 130      -9.394  32.537 -18.555  1.00 13.35           C  
ANISOU 3618  CG2 ILE D 130     2121   1867   1085   -139    630    -88       C  
ATOM   3619  CD1 ILE D 130      -7.264  30.819 -17.369  1.00  9.85           C  
ANISOU 3619  CD1 ILE D 130     1537   1397    810   -126    362    -12       C  
ATOM   3620  N   ILE D 131     -12.032  30.422 -18.854  1.00  9.66           N  
ANISOU 3620  N   ILE D 131     1700    887   1083   -546    555   -302       N  
ATOM   3621  CA  ILE D 131     -13.396  30.801 -19.199  1.00 10.52           C  
ANISOU 3621  CA  ILE D 131     1432   1236   1330   -398    644   -217       C  
ATOM   3622  C   ILE D 131     -13.900  31.781 -18.150  1.00  9.14           C  
ANISOU 3622  C   ILE D 131      918   1230   1327   -413    426    187       C  
ATOM   3623  O   ILE D 131     -13.503  31.727 -16.983  1.00 11.02           O  
ANISOU 3623  O   ILE D 131     1147   1347   1695   -163    192    312       O  
ATOM   3624  CB  ILE D 131     -14.333  29.576 -19.329  1.00  9.99           C  
ANISOU 3624  CB  ILE D 131     1470   1106   1219   -107    587   -358       C  
ATOM   3625  CG1 ILE D 131     -14.439  28.811 -18.007  1.00  9.64           C  
ANISOU 3625  CG1 ILE D 131     1145   1132   1385    156    484    130       C  
ATOM   3626  CG2 ILE D 131     -13.853  28.657 -20.444  1.00 13.93           C  
ANISOU 3626  CG2 ILE D 131     2472   1592   1227   -318    542   -213       C  
ATOM   3627  CD1 ILE D 131     -15.706  29.101 -17.238  1.00 11.80           C  
ANISOU 3627  CD1 ILE D 131     1206   1514   1765    491    451    483       C  
ATOM   3628  N   TRP D 132     -14.774  32.689 -18.576  1.00  9.26           N  
ANISOU 3628  N   TRP D 132      746   1350   1421   -269    330    100       N  
ATOM   3629  CA  TRP D 132     -15.165  33.837 -17.769  1.00  9.02           C  
ANISOU 3629  CA  TRP D 132      909   1032   1488   -321    200    199       C  
ATOM   3630  C   TRP D 132     -16.617  33.734 -17.318  1.00 10.51           C  
ANISOU 3630  C   TRP D 132     1362   1270   1362    -96    250    221       C  
ATOM   3631  O   TRP D 132     -17.474  33.228 -18.052  1.00 11.87           O  
ANISOU 3631  O   TRP D 132     1664   1450   1396   -252   -185    288       O  
ATOM   3632  CB  TRP D 132     -14.946  35.136 -18.550  1.00  9.73           C  
ANISOU 3632  CB  TRP D 132     1139    843   1716   -346    196    304       C  
ATOM   3633  CG  TRP D 132     -13.503  35.371 -18.855  1.00  8.50           C  
ANISOU 3633  CG  TRP D 132     1208    700   1322   -318    246    319       C  
ATOM   3634  CD1 TRP D 132     -12.840  35.041 -20.002  1.00  9.22           C  
ANISOU 3634  CD1 TRP D 132     1270    742   1489   -482    139    234       C  
ATOM   3635  CD2 TRP D 132     -12.531  35.956 -17.983  1.00  9.76           C  
ANISOU 3635  CD2 TRP D 132     1615    805   1288    -95   -211   -111       C  
ATOM   3636  NE1 TRP D 132     -11.515  35.399 -19.902  1.00 10.39           N  
ANISOU 3636  NE1 TRP D 132     1559    930   1457   -676    -44      8       N  
ATOM   3637  CE2 TRP D 132     -11.301  35.963 -18.671  1.00  9.68           C  
ANISOU 3637  CE2 TRP D 132     1452    937   1289   -662    -96     98       C  
ATOM   3638  CE3 TRP D 132     -12.583  36.482 -16.687  1.00  9.76           C  
ANISOU 3638  CE3 TRP D 132     1813    774   1121    -14   -594   -149       C  
ATOM   3639  CZ2 TRP D 132     -10.136  36.472 -18.108  1.00 11.07           C  
ANISOU 3639  CZ2 TRP D 132     1958    908   1341   -631   -351    240       C  
ATOM   3640  CZ3 TRP D 132     -11.424  36.989 -16.130  1.00 10.20           C  
ANISOU 3640  CZ3 TRP D 132     1924    589   1364     54   -186     26       C  
ATOM   3641  CH2 TRP D 132     -10.217  36.983 -16.841  1.00 11.32           C  
ANISOU 3641  CH2 TRP D 132     2021    903   1378   -151   -158    302       C  
ATOM   3642  N   VAL D 133     -16.880  34.218 -16.101  1.00  8.50           N  
ANISOU 3642  N   VAL D 133      960   1124   1145    125    547    374       N  
ATOM   3643  CA  VAL D 133     -18.220  34.263 -15.526  1.00  7.82           C  
ANISOU 3643  CA  VAL D 133      760   1061   1152   -137    520     -3       C  
ATOM   3644  C   VAL D 133     -18.390  35.582 -14.782  1.00  9.38           C  
ANISOU 3644  C   VAL D 133      781   1379   1404    -46    504    312       C  
ATOM   3645  O   VAL D 133     -17.431  36.143 -14.244  1.00  7.61           O  
ANISOU 3645  O   VAL D 133      519   1195   1176   -254   -268    223       O  
ATOM   3646  CB  VAL D 133     -18.495  33.073 -14.576  1.00  7.00           C  
ANISOU 3646  CB  VAL D 133      580    918   1162   -411    -54    -42       C  
ATOM   3647  CG1 VAL D 133     -18.484  31.756 -15.337  1.00  6.24           C  
ANISOU 3647  CG1 VAL D 133      442    905   1025   -283   -161    -71       C  
ATOM   3648  CG2 VAL D 133     -17.477  33.045 -13.438  1.00  8.30           C  
ANISOU 3648  CG2 VAL D 133      917   1197   1038   -602   -165    162       C  
ATOM   3649  N   ALA D 134     -19.627  36.076 -14.750  1.00  9.93           N  
ANISOU 3649  N   ALA D 134     1048   1371   1354    361    612     38       N  
ATOM   3650  CA  ALA D 134     -19.928  37.312 -14.038  1.00 10.45           C  
ANISOU 3650  CA  ALA D 134     1007   1315   1650   -169    472    323       C  
ATOM   3651  C   ALA D 134     -21.418  37.371 -13.746  1.00 13.08           C  
ANISOU 3651  C   ALA D 134     1017   2093   1859    218    104    -90       C  
ATOM   3652  O   ALA D 134     -22.235  37.081 -14.625  1.00 15.45           O  
ANISOU 3652  O   ALA D 134     1479   2250   2140      5    483   -143       O  
ATOM   3653  CB  ALA D 134     -19.495  38.542 -14.846  1.00 11.18           C  
ANISOU 3653  CB  ALA D 134     1424   1113   1711    432    -64    621       C  
ATOM   3654  N   THR D 135     -21.761  37.741 -12.515  1.00 13.57           N  
ANISOU 3654  N   THR D 135      913   2214   2028    166     58     59       N  
ATOM   3655  CA  THR D 135     -23.144  37.971 -12.133  1.00 15.35           C  
ANISOU 3655  CA  THR D 135     1296   2208   2329    442    -89    232       C  
ATOM   3656  C   THR D 135     -23.563  39.381 -12.533  1.00 19.53           C  
ANISOU 3656  C   THR D 135     1813   2509   3099    549    -88    213       C  
ATOM   3657  O   THR D 135     -22.743  40.303 -12.574  1.00 20.46           O  
ANISOU 3657  O   THR D 135     1870   2266   3640    304    -66    295       O  
ATOM   3658  CB  THR D 135     -23.319  37.784 -10.622  1.00 15.38           C  
ANISOU 3658  CB  THR D 135     1075   2404   2366    277      3    351       C  
ATOM   3659  OG1 THR D 135     -22.760  36.527 -10.226  1.00 15.11           O  
ANISOU 3659  OG1 THR D 135     1162   2117   2462     45     91    375       O  
ATOM   3660  CG2 THR D 135     -24.791  37.817 -10.225  1.00 15.66           C  
ANISOU 3660  CG2 THR D 135      867   2553   2529    487    326     -1       C  
ATOM   3661  N   GLU D 136     -24.849  39.536 -12.846  1.00 21.58           N  
ANISOU 3661  N   GLU D 136     1943   2937   3321    997   -904    301       N  
ATOM   3662  CA  GLU D 136     -25.403  40.852 -13.141  1.00 26.38           C  
ANISOU 3662  CA  GLU D 136     2649   3590   3783   1174   -821   -168       C  
ATOM   3663  C   GLU D 136     -25.099  41.829 -12.015  1.00 24.06           C  
ANISOU 3663  C   GLU D 136     2312   3221   3610    949   -733   -470       C  
ATOM   3664  O   GLU D 136     -25.320  41.530 -10.838  1.00 25.93           O  
ANISOU 3664  O   GLU D 136     2958   3265   3631    888   -529   -567       O  
ATOM   3665  CB  GLU D 136     -26.915  40.757 -13.350  1.00 32.42           C  
ANISOU 3665  CB  GLU D 136     3355   4622   4341    826  -1034   -112       C  
ATOM   3666  CG  GLU D 136     -27.358  40.845 -14.800  1.00 40.72           C  
ANISOU 3666  CG  GLU D 136     4546   5832   5094    933   -757   -178       C  
ATOM   3667  CD  GLU D 136     -28.764  41.398 -14.937  1.00 47.92           C  
ANISOU 3667  CD  GLU D 136     5776   6742   5688    947   -448   -350       C  
ATOM   3668  OE1 GLU D 136     -29.131  42.288 -14.139  1.00 49.20           O  
ANISOU 3668  OE1 GLU D 136     6093   6774   5826   1224    -31   -519       O  
ATOM   3669  OE2 GLU D 136     -29.501  40.942 -15.837  1.00 51.15           O  
ANISOU 3669  OE2 GLU D 136     6241   7238   5956    591   -588   -380       O  
ATOM   3670  N   GLY D 137     -24.589  43.000 -12.384  1.00 21.39           N  
ANISOU 3670  N   GLY D 137     1717   2984   3426    994   -565   -413       N  
ATOM   3671  CA  GLY D 137     -24.256  44.025 -11.421  1.00 21.86           C  
ANISOU 3671  CA  GLY D 137     2101   2869   3336    731   -474   -620       C  
ATOM   3672  C   GLY D 137     -22.818  44.027 -10.952  1.00 19.42           C  
ANISOU 3672  C   GLY D 137     1987   2409   2981    685   -538   -325       C  
ATOM   3673  O   GLY D 137     -22.403  44.988 -10.291  1.00 23.44           O  
ANISOU 3673  O   GLY D 137     2626   2822   3461    533   -293   -314       O  
ATOM   3674  N   ALA D 138     -22.047  42.987 -11.263  1.00 14.34           N  
ANISOU 3674  N   ALA D 138     1712   1390   2346    605   -281     68       N  
ATOM   3675  CA  ALA D 138     -20.644  42.965 -10.877  1.00 11.95           C  
ANISOU 3675  CA  ALA D 138     1480   1106   1956    729   -109    169       C  
ATOM   3676  C   ALA D 138     -19.882  44.080 -11.583  1.00 14.10           C  
ANISOU 3676  C   ALA D 138     2061   1420   1876    471   -285    467       C  
ATOM   3677  O   ALA D 138     -20.219  44.486 -12.698  1.00 17.25           O  
ANISOU 3677  O   ALA D 138     2213   2095   2246    683   -255    766       O  
ATOM   3678  CB  ALA D 138     -20.015  41.611 -11.208  1.00 11.95           C  
ANISOU 3678  CB  ALA D 138     1708   1192   1641    816   -194    -54       C  
ATOM   3679  N   LEU D 139     -18.848  44.581 -10.917  1.00 14.64           N  
ANISOU 3679  N   LEU D 139     2285   1535   1743    408   -231    297       N  
ATOM   3680  CA  LEU D 139     -18.018  45.645 -11.459  1.00 14.99           C  
ANISOU 3680  CA  LEU D 139     2490   1414   1791    166   -222    -56       C  
ATOM   3681  C   LEU D 139     -16.763  45.055 -12.085  1.00 12.99           C  
ANISOU 3681  C   LEU D 139     2324   1115   1498    487   -188     53       C  
ATOM   3682  O   LEU D 139     -16.123  44.172 -11.507  1.00 12.05           O  
ANISOU 3682  O   LEU D 139     2110   1035   1433    481   -397    336       O  
ATOM   3683  CB  LEU D 139     -17.638  46.655 -10.375  1.00 18.77           C  
ANISOU 3683  CB  LEU D 139     3183   1903   2048    773    100   -749       C  
ATOM   3684  CG  LEU D 139     -18.794  47.433  -9.746  1.00 22.96           C  
ANISOU 3684  CG  LEU D 139     3805   2373   2545    604   -235   -386       C  
ATOM   3685  CD1 LEU D 139     -18.260  48.543  -8.847  1.00 22.77           C  
ANISOU 3685  CD1 LEU D 139     3898   2241   2512    319   -363   -296       C  
ATOM   3686  CD2 LEU D 139     -19.724  47.991 -10.820  1.00 25.19           C  
ANISOU 3686  CD2 LEU D 139     4103   2729   2739    427   -197   -333       C  
ATOM   3687  N   ASN D 140     -16.418  45.552 -13.273  1.00 13.75           N  
ANISOU 3687  N   ASN D 140     2169   1576   1480    288     53    134       N  
ATOM   3688  CA  ASN D 140     -15.255  45.071 -14.018  1.00 14.89           C  
ANISOU 3688  CA  ASN D 140     2474   1918   1264     84    392    195       C  
ATOM   3689  C   ASN D 140     -13.998  45.779 -13.505  1.00 15.85           C  
ANISOU 3689  C   ASN D 140     2506   1932   1583    -93    520    313       C  
ATOM   3690  O   ASN D 140     -13.401  46.634 -14.162  1.00 19.18           O  
ANISOU 3690  O   ASN D 140     2842   2339   2105   -397    325    359       O  
ATOM   3691  CB  ASN D 140     -15.467  45.289 -15.510  1.00 15.89           C  
ANISOU 3691  CB  ASN D 140     2745   2015   1276    461    302    727       C  
ATOM   3692  CG  ASN D 140     -14.376  44.667 -16.357  1.00 17.65           C  
ANISOU 3692  CG  ASN D 140     3150   2125   1431    686    250    570       C  
ATOM   3693  OD1 ASN D 140     -13.519  43.945 -15.855  1.00 19.04           O  
ANISOU 3693  OD1 ASN D 140     3305   2246   1683   1153    274    609       O  
ATOM   3694  ND2 ASN D 140     -14.407  44.944 -17.655  1.00 20.08           N  
ANISOU 3694  ND2 ASN D 140     3446   2562   1620     65      5    560       N  
ATOM   3695  N   THR D 141     -13.607  45.408 -12.288  1.00 15.82           N  
ANISOU 3695  N   THR D 141     2653   1743   1615    368    -47    -36       N  
ATOM   3696  CA  THR D 141     -12.439  45.945 -11.602  1.00 16.91           C  
ANISOU 3696  CA  THR D 141     2584   1703   2137     90    302     94       C  
ATOM   3697  C   THR D 141     -11.722  44.806 -10.893  1.00 15.27           C  
ANISOU 3697  C   THR D 141     2345   1606   1851    290    545    176       C  
ATOM   3698  O   THR D 141     -12.360  43.821 -10.501  1.00 15.43           O  
ANISOU 3698  O   THR D 141     2391   1998   1475    429    475     26       O  
ATOM   3699  CB  THR D 141     -12.820  47.028 -10.576  1.00 16.87           C  
ANISOU 3699  CB  THR D 141     2556   1354   2499    125    536     86       C  
ATOM   3700  OG1 THR D 141     -13.715  46.479  -9.600  1.00 15.86           O  
ANISOU 3700  OG1 THR D 141     2167   1315   2545    195    300   -306       O  
ATOM   3701  CG2 THR D 141     -13.482  48.220 -11.257  1.00 18.67           C  
ANISOU 3701  CG2 THR D 141     2977   1395   2724    -28    939    201       C  
ATOM   3702  N   PRO D 142     -10.402  44.905 -10.714  1.00 13.75           N  
ANISOU 3702  N   PRO D 142     1749   1552   1923    175    999    237       N  
ATOM   3703  CA  PRO D 142      -9.668  43.817 -10.054  1.00 13.48           C  
ANISOU 3703  CA  PRO D 142     1674   1429   2019   -149   1069     53       C  
ATOM   3704  C   PRO D 142     -10.072  43.682  -8.594  1.00 13.84           C  
ANISOU 3704  C   PRO D 142     2279   1073   1906   -537    444    157       C  
ATOM   3705  O   PRO D 142     -10.284  44.676  -7.894  1.00 17.33           O  
ANISOU 3705  O   PRO D 142     2932   1506   2145   -421    433    354       O  
ATOM   3706  CB  PRO D 142      -8.199  44.240 -10.185  1.00 16.25           C  
ANISOU 3706  CB  PRO D 142     1787   2122   2264   -243   1095    325       C  
ATOM   3707  CG  PRO D 142      -8.182  45.338 -11.205  1.00 19.08           C  
ANISOU 3707  CG  PRO D 142     2097   2356   2795    337   1058    264       C  
ATOM   3708  CD  PRO D 142      -9.511  46.008 -11.109  1.00 15.51           C  
ANISOU 3708  CD  PRO D 142     1604   1961   2329    461   1007     11       C  
ATOM   3709  N   LYS D 143     -10.169  42.437  -8.135  1.00 12.56           N  
ANISOU 3709  N   LYS D 143     2157    963   1651   -305   -125     71       N  
ATOM   3710  CA  LYS D 143     -10.597  42.149  -6.765  1.00 12.15           C  
ANISOU 3710  CA  LYS D 143     2110    933   1572   -282    -52    217       C  
ATOM   3711  C   LYS D 143      -9.386  41.900  -5.868  1.00 14.74           C  
ANISOU 3711  C   LYS D 143     2298   1501   1803   -293    130    -63       C  
ATOM   3712  O   LYS D 143      -9.233  40.847  -5.247  1.00 13.78           O  
ANISOU 3712  O   LYS D 143     2021   1361   1853    206    204     35       O  
ATOM   3713  CB  LYS D 143     -11.555  40.960  -6.747  1.00 12.51           C  
ANISOU 3713  CB  LYS D 143     2071   1187   1496   -175    114    189       C  
ATOM   3714  CG  LYS D 143     -12.720  41.075  -7.721  1.00 11.49           C  
ANISOU 3714  CG  LYS D 143     1710   1222   1434    155    -79    224       C  
ATOM   3715  CD  LYS D 143     -13.420  42.421  -7.623  1.00 10.65           C  
ANISOU 3715  CD  LYS D 143     1121   1551   1372    195   -326    441       C  
ATOM   3716  CE  LYS D 143     -14.511  42.540  -8.680  1.00  9.08           C  
ANISOU 3716  CE  LYS D 143      950   1133   1367    213   -417    276       C  
ATOM   3717  NZ  LYS D 143     -14.963  43.946  -8.885  1.00 11.24           N  
ANISOU 3717  NZ  LYS D 143     1591   1098   1581   -286    -49    522       N  
ATOM   3718  N   ASP D 144      -8.519  42.914  -5.806  1.00 16.29           N  
ANISOU 3718  N   ASP D 144     2149   2269   1770  -1037    -77    -57       N  
ATOM   3719  CA  ASP D 144      -7.295  42.804  -5.018  1.00 17.82           C  
ANISOU 3719  CA  ASP D 144     1895   2864   2010  -1045     34      3       C  
ATOM   3720  C   ASP D 144      -7.584  42.537  -3.546  1.00 16.45           C  
ANISOU 3720  C   ASP D 144     1429   2870   1951   -609   -240    -87       C  
ATOM   3721  O   ASP D 144      -6.814  41.830  -2.885  1.00 14.53           O  
ANISOU 3721  O   ASP D 144      845   2704   1973   -130   -444    127       O  
ATOM   3722  CB  ASP D 144      -6.461  44.077  -5.173  1.00 21.73           C  
ANISOU 3722  CB  ASP D 144     2626   3279   2354  -1503    188    -10       C  
ATOM   3723  CG  ASP D 144      -5.878  44.227  -6.566  1.00 27.28           C  
ANISOU 3723  CG  ASP D 144     3390   3976   2999  -1172    399    172       C  
ATOM   3724  OD1 ASP D 144      -5.307  43.243  -7.083  1.00 31.36           O  
ANISOU 3724  OD1 ASP D 144     3845   4892   3179  -1389    501    172       O  
ATOM   3725  OD2 ASP D 144      -5.996  45.325  -7.148  1.00 30.21           O  
ANISOU 3725  OD2 ASP D 144     3695   4334   3451   -552    315    291       O  
ATOM   3726  N   HIS D 145      -8.684  43.078  -3.013  1.00 14.68           N  
ANISOU 3726  N   HIS D 145     1490   2357   1731   -397   -180   -590       N  
ATOM   3727  CA  HIS D 145      -8.962  42.900  -1.592  1.00 14.03           C  
ANISOU 3727  CA  HIS D 145     1562   2115   1654   -193   -112   -604       C  
ATOM   3728  C   HIS D 145      -9.361  41.469  -1.254  1.00 13.10           C  
ANISOU 3728  C   HIS D 145     1584   1868   1525   -263    125   -466       C  
ATOM   3729  O   HIS D 145      -9.251  41.069  -0.090  1.00 15.73           O  
ANISOU 3729  O   HIS D 145     2284   2084   1608   -716   -226    -97       O  
ATOM   3730  CB  HIS D 145     -10.040  43.885  -1.125  1.00 12.74           C  
ANISOU 3730  CB  HIS D 145     1343   1748   1748    -82   -192   -865       C  
ATOM   3731  CG  HIS D 145     -11.414  43.586  -1.640  1.00 11.01           C  
ANISOU 3731  CG  HIS D 145     1053   1554   1577   -493    -18   -478       C  
ATOM   3732  ND1 HIS D 145     -11.838  43.965  -2.895  1.00 13.36           N  
ANISOU 3732  ND1 HIS D 145     1129   2129   1817   -795    -69   -280       N  
ATOM   3733  CD2 HIS D 145     -12.470  42.970  -1.057  1.00 11.98           C  
ANISOU 3733  CD2 HIS D 145     1495   1464   1591   -389    201   -481       C  
ATOM   3734  CE1 HIS D 145     -13.091  43.583  -3.069  1.00 12.64           C  
ANISOU 3734  CE1 HIS D 145     1306   1918   1580   -850    317     -7       C  
ATOM   3735  NE2 HIS D 145     -13.498  42.978  -1.968  1.00 11.95           N  
ANISOU 3735  NE2 HIS D 145     1502   1613   1427   -643    406   -380       N  
ATOM   3736  N   ILE D 146      -9.804  40.688  -2.235  1.00 12.36           N  
ANISOU 3736  N   ILE D 146     1536   1596   1564     87    300   -297       N  
ATOM   3737  CA  ILE D 146     -10.090  39.273  -2.013  1.00 12.48           C  
ANISOU 3737  CA  ILE D 146     1612   1493   1636   -389    -37    161       C  
ATOM   3738  C   ILE D 146      -8.846  38.419  -2.217  1.00 14.91           C  
ANISOU 3738  C   ILE D 146     2228   1789   1649   -368   -183    199       C  
ATOM   3739  O   ILE D 146      -8.529  37.555  -1.393  1.00 13.81           O  
ANISOU 3739  O   ILE D 146     2649   1086   1513   -213   -569    127       O  
ATOM   3740  CB  ILE D 146     -11.242  38.813  -2.932  1.00 12.08           C  
ANISOU 3740  CB  ILE D 146     1505   1247   1839   -652   -483   -138       C  
ATOM   3741  CG1 ILE D 146     -12.532  39.556  -2.580  1.00 13.90           C  
ANISOU 3741  CG1 ILE D 146     1446   1724   2110   -640   -721    -28       C  
ATOM   3742  CG2 ILE D 146     -11.441  37.308  -2.823  1.00 13.55           C  
ANISOU 3742  CG2 ILE D 146     1821   1442   1886   -533    -41   -101       C  
ATOM   3743  CD1 ILE D 146     -13.712  39.188  -3.463  1.00 12.44           C  
ANISOU 3743  CD1 ILE D 146     1032   1729   1968   -388   -667    154       C  
ATOM   3744  N   GLY D 147      -8.125  38.649  -3.312  1.00 14.92           N  
ANISOU 3744  N   GLY D 147     1983   1927   1758   -495    -13     54       N  
ATOM   3745  CA  GLY D 147      -6.893  37.940  -3.593  1.00 13.85           C  
ANISOU 3745  CA  GLY D 147     1541   1712   2011    -23    -78    -78       C  
ATOM   3746  C   GLY D 147      -7.101  36.442  -3.712  1.00 13.97           C  
ANISOU 3746  C   GLY D 147     1358   1797   2152     82    145    -29       C  
ATOM   3747  O   GLY D 147      -8.177  35.955  -4.077  1.00 12.23           O  
ANISOU 3747  O   GLY D 147      932   1414   2299    161     76    -58       O  
ATOM   3748  N   THR D 148      -6.047  35.698  -3.400  1.00 13.42           N  
ANISOU 3748  N   THR D 148     1419   1686   1993    195    -27     -1       N  
ATOM   3749  CA  THR D 148      -6.079  34.244  -3.396  1.00 12.32           C  
ANISOU 3749  CA  THR D 148     1179   1703   1798     18   -109     76       C  
ATOM   3750  C   THR D 148      -6.015  33.730  -1.964  1.00 11.67           C  
ANISOU 3750  C   THR D 148     1332   1537   1566    -51   -242    -44       C  
ATOM   3751  O   THR D 148      -5.817  34.487  -1.010  1.00 10.61           O  
ANISOU 3751  O   THR D 148      850   1392   1789     -6     75    -73       O  
ATOM   3752  CB  THR D 148      -4.927  33.664  -4.226  1.00 12.30           C  
ANISOU 3752  CB  THR D 148      857   2211   1606     87    170   -357       C  
ATOM   3753  OG1 THR D 148      -3.678  34.131  -3.702  1.00 14.90           O  
ANISOU 3753  OG1 THR D 148     1003   2659   1999   -155     83   -188       O  
ATOM   3754  CG2 THR D 148      -5.052  34.085  -5.687  1.00 13.07           C  
ANISOU 3754  CG2 THR D 148      844   2607   1516    152    289   -294       C  
ATOM   3755  N   ARG D 149      -6.178  32.419  -1.827  1.00 11.40           N  
ANISOU 3755  N   ARG D 149     1480   1346   1508    -14   -196    308       N  
ATOM   3756  CA  ARG D 149      -6.276  31.772  -0.527  1.00 12.59           C  
ANISOU 3756  CA  ARG D 149     1406   1844   1534    344    -87    545       C  
ATOM   3757  C   ARG D 149      -4.926  31.213  -0.097  1.00 14.89           C  
ANISOU 3757  C   ARG D 149     1574   2445   1639    838    -64    208       C  
ATOM   3758  O   ARG D 149      -4.215  30.590  -0.893  1.00 16.07           O  
ANISOU 3758  O   ARG D 149     1646   3197   1263    724    177    -94       O  
ATOM   3759  CB  ARG D 149      -7.314  30.649  -0.560  1.00 12.18           C  
ANISOU 3759  CB  ARG D 149     1268   1767   1592    -43    335    587       C  
ATOM   3760  CG  ARG D 149      -7.426  29.863   0.739  1.00 11.41           C  
ANISOU 3760  CG  ARG D 149     1131   1614   1592    395    552    549       C  
ATOM   3761  CD  ARG D 149      -8.548  28.835   0.669  1.00 11.63           C  
ANISOU 3761  CD  ARG D 149     1374   1492   1552     28    740     44       C  
ATOM   3762  NE  ARG D 149      -8.336  27.869  -0.406  1.00 11.39           N  
ANISOU 3762  NE  ARG D 149     1397   1671   1261    420    610    231       N  
ATOM   3763  CZ  ARG D 149      -7.727  26.699  -0.251  1.00 12.70           C  
ANISOU 3763  CZ  ARG D 149     1725   1930   1169    480    241     41       C  
ATOM   3764  NH1 ARG D 149      -7.267  26.338   0.940  1.00 13.38           N  
ANISOU 3764  NH1 ARG D 149     1702   2206   1174    636     11      8       N  
ATOM   3765  NH2 ARG D 149      -7.575  25.889  -1.290  1.00 12.60           N  
ANISOU 3765  NH2 ARG D 149     1879   1777   1132    927    225    -51       N  
ATOM   3766  N   ASN D 150      -4.579  31.446   1.168  1.00 14.04           N  
ANISOU 3766  N   ASN D 150     1414   2390   1532    447   -445    317       N  
ATOM   3767  CA  ASN D 150      -3.419  30.816   1.781  1.00 18.65           C  
ANISOU 3767  CA  ASN D 150     2129   2963   1994    472   -452    175       C  
ATOM   3768  C   ASN D 150      -3.884  29.534   2.460  1.00 19.04           C  
ANISOU 3768  C   ASN D 150     2373   2932   1927    883   -444    313       C  
ATOM   3769  O   ASN D 150      -4.582  29.610   3.483  1.00 18.71           O  
ANISOU 3769  O   ASN D 150     2546   2856   1706    647   -544    241       O  
ATOM   3770  CB  ASN D 150      -2.771  31.752   2.792  1.00 21.91           C  
ANISOU 3770  CB  ASN D 150     2219   3724   2383    222  -1045    -77       C  
ATOM   3771  CG  ASN D 150      -1.456  31.219   3.335  1.00 26.20           C  
ANISOU 3771  CG  ASN D 150     2754   4303   2899   -175  -1468   -557       C  
ATOM   3772  OD1 ASN D 150      -1.129  30.040   3.183  1.00 25.79           O  
ANISOU 3772  OD1 ASN D 150     2634   4203   2962   -259  -1408   -625       O  
ATOM   3773  ND2 ASN D 150      -0.696  32.092   3.988  1.00 29.10           N  
ANISOU 3773  ND2 ASN D 150     2916   4813   3327   -220  -1636   -445       N  
ATOM   3774  N   PRO D 151      -3.535  28.353   1.942  1.00 20.34           N  
ANISOU 3774  N   PRO D 151     2700   3156   1871   1539   -149     80       N  
ATOM   3775  CA  PRO D 151      -4.055  27.110   2.537  1.00 22.30           C  
ANISOU 3775  CA  PRO D 151     3089   3404   1980   1372    -85    201       C  
ATOM   3776  C   PRO D 151      -3.664  26.915   3.992  1.00 23.59           C  
ANISOU 3776  C   PRO D 151     3282   3610   2071   1335    -18    148       C  
ATOM   3777  O   PRO D 151      -4.377  26.220   4.725  1.00 25.11           O  
ANISOU 3777  O   PRO D 151     3824   3784   1932   1155    231    678       O  
ATOM   3778  CB  PRO D 151      -3.453  26.017   1.641  1.00 22.41           C  
ANISOU 3778  CB  PRO D 151     3222   3379   1914   1415    111     99       C  
ATOM   3779  CG  PRO D 151      -3.149  26.707   0.351  1.00 22.10           C  
ANISOU 3779  CG  PRO D 151     2854   3582   1960   1484    519   -129       C  
ATOM   3780  CD  PRO D 151      -2.740  28.098   0.730  1.00 20.38           C  
ANISOU 3780  CD  PRO D 151     2572   3274   1899   1480    247   -321       C  
ATOM   3781  N   ALA D 152      -2.555  27.509   4.436  1.00 23.26           N  
ANISOU 3781  N   ALA D 152     2935   3671   2232   1870   -441   -299       N  
ATOM   3782  CA  ALA D 152      -2.155  27.393   5.832  1.00 25.16           C  
ANISOU 3782  CA  ALA D 152     3449   3878   2234   1567   -596   -489       C  
ATOM   3783  C   ALA D 152      -3.034  28.211   6.767  1.00 26.91           C  
ANISOU 3783  C   ALA D 152     3897   3960   2369   1435   -905   -142       C  
ATOM   3784  O   ALA D 152      -2.960  28.016   7.986  1.00 30.92           O  
ANISOU 3784  O   ALA D 152     4736   4398   2615   1397  -1409   -518       O  
ATOM   3785  CB  ALA D 152      -0.694  27.815   5.996  1.00 26.21           C  
ANISOU 3785  CB  ALA D 152     3542   4073   2345   1436   -420   -650       C  
ATOM   3786  N   ASN D 153      -3.858  29.110   6.237  1.00 23.07           N  
ANISOU 3786  N   ASN D 153     3075   3471   2218   1343   -512    101       N  
ATOM   3787  CA  ASN D 153      -4.723  29.945   7.058  1.00 20.44           C  
ANISOU 3787  CA  ASN D 153     2396   3251   2119    850   -196    -17       C  
ATOM   3788  C   ASN D 153      -6.207  29.704   6.831  1.00 19.03           C  
ANISOU 3788  C   ASN D 153     2243   3120   1869    673     39    -80       C  
ATOM   3789  O   ASN D 153      -6.986  29.839   7.776  1.00 19.75           O  
ANISOU 3789  O   ASN D 153     2411   3393   1701   -141    355    188       O  
ATOM   3790  CB  ASN D 153      -4.421  31.433   6.815  1.00 19.50           C  
ANISOU 3790  CB  ASN D 153     1933   3212   2265    527     57   -101       C  
ATOM   3791  CG  ASN D 153      -5.170  32.342   7.769  1.00 20.96           C  
ANISOU 3791  CG  ASN D 153     1869   3401   2694    -25   -258   -283       C  
ATOM   3792  OD1 ASN D 153      -4.841  32.422   8.952  1.00 20.76           O  
ANISOU 3792  OD1 ASN D 153     1481   3468   2940   -375   -648   -249       O  
ATOM   3793  ND2 ASN D 153      -6.181  33.036   7.258  1.00 20.77           N  
ANISOU 3793  ND2 ASN D 153     1464   3636   2790    -51    152   -396       N  
ATOM   3794  N   ASN D 154      -6.619  29.350   5.615  1.00 17.49           N  
ANISOU 3794  N   ASN D 154     2147   2967   1531   1010   -638   -254       N  
ATOM   3795  CA  ASN D 154      -8.022  29.140   5.289  1.00 17.39           C  
ANISOU 3795  CA  ASN D 154     2521   2433   1653   1203   -392   -389       C  
ATOM   3796  C   ASN D 154      -8.195  27.842   4.520  1.00 16.64           C  
ANISOU 3796  C   ASN D 154     2550   2307   1467   1010   -175    -54       C  
ATOM   3797  O   ASN D 154      -7.425  27.546   3.601  1.00 17.16           O  
ANISOU 3797  O   ASN D 154     3098   2330   1091    567    101   -334       O  
ATOM   3798  CB  ASN D 154      -8.585  30.287   4.443  1.00 17.27           C  
ANISOU 3798  CB  ASN D 154     2782   2299   1481   1111   -515   -392       C  
ATOM   3799  CG  ASN D 154      -8.574  31.608   5.171  1.00 20.98           C  
ANISOU 3799  CG  ASN D 154     3278   2804   1889    876   -264   -975       C  
ATOM   3800  OD1 ASN D 154      -7.582  32.337   5.141  1.00 26.03           O  
ANISOU 3800  OD1 ASN D 154     3793   3663   2436    258   -367  -1075       O  
ATOM   3801  ND2 ASN D 154      -9.684  31.931   5.825  1.00 18.75           N  
ANISOU 3801  ND2 ASN D 154     2443   2885   1797   1513   -146   -484       N  
ATOM   3802  N   ALA D 155      -9.217  27.079   4.892  1.00 14.65           N  
ANISOU 3802  N   ALA D 155     1926   2422   1218    484   -249    312       N  
ATOM   3803  CA  ALA D 155      -9.631  25.952   4.078  1.00 16.24           C  
ANISOU 3803  CA  ALA D 155     2415   2450   1306    114   -354    530       C  
ATOM   3804  C   ALA D 155     -10.426  26.448   2.876  1.00 15.34           C  
ANISOU 3804  C   ALA D 155     2575   2113   1140   -112    -59    275       C  
ATOM   3805  O   ALA D 155     -10.959  27.560   2.866  1.00 12.85           O  
ANISOU 3805  O   ALA D 155     2040   1905    938    209    133    211       O  
ATOM   3806  CB  ALA D 155     -10.470  24.970   4.895  1.00 18.56           C  
ANISOU 3806  CB  ALA D 155     2870   2803   1381   -447    -50    639       C  
ATOM   3807  N   ALA D 156     -10.500  25.605   1.851  1.00 15.67           N  
ANISOU 3807  N   ALA D 156     2796   1979   1177   -142     20     63       N  
ATOM   3808  CA  ALA D 156     -11.255  25.961   0.660  1.00 14.76           C  
ANISOU 3808  CA  ALA D 156     2381   1978   1250   -147     41     95       C  
ATOM   3809  C   ALA D 156     -12.748  25.997   0.963  1.00 15.61           C  
ANISOU 3809  C   ALA D 156     2442   1971   1520   -630    170    487       C  
ATOM   3810  O   ALA D 156     -13.261  25.193   1.746  1.00 19.70           O  
ANISOU 3810  O   ALA D 156     2853   2422   2212   -933    204    756       O  
ATOM   3811  CB  ALA D 156     -10.971  24.970  -0.467  1.00 16.24           C  
ANISOU 3811  CB  ALA D 156     2261   2564   1344    413   -130   -112       C  
ATOM   3812  N   ILE D 157     -13.438  26.955   0.356  1.00 14.94           N  
ANISOU 3812  N   ILE D 157     2147   2144   1386   -143    180   -243       N  
ATOM   3813  CA  ILE D 157     -14.894  27.010   0.412  1.00 12.29           C  
ANISOU 3813  CA  ILE D 157     1518   1679   1473   -317    495    -53       C  
ATOM   3814  C   ILE D 157     -15.452  26.001  -0.579  1.00 11.84           C  
ANISOU 3814  C   ILE D 157     1738   1296   1464   -560    494    341       C  
ATOM   3815  O   ILE D 157     -15.036  25.967  -1.742  1.00 11.61           O  
ANISOU 3815  O   ILE D 157     1973   1492    946    127    189    226       O  
ATOM   3816  CB  ILE D 157     -15.395  28.428   0.095  1.00 14.56           C  
ANISOU 3816  CB  ILE D 157     1305   2362   1864    -49    482   -554       C  
ATOM   3817  CG1 ILE D 157     -14.847  29.429   1.113  1.00 14.94           C  
ANISOU 3817  CG1 ILE D 157     1456   1982   2241   -149    483   -766       C  
ATOM   3818  CG2 ILE D 157     -16.915  28.465   0.060  1.00 17.34           C  
ANISOU 3818  CG2 ILE D 157     1462   3087   2040    108    510   -471       C  
ATOM   3819  CD1 ILE D 157     -15.111  30.866   0.743  1.00 16.42           C  
ANISOU 3819  CD1 ILE D 157     1634   2084   2520   -210    608   -755       C  
ATOM   3820  N   VAL D 158     -16.388  25.168  -0.127  1.00 14.71           N  
ANISOU 3820  N   VAL D 158     2081   1798   1708   -534    257    505       N  
ATOM   3821  CA  VAL D 158     -17.016  24.216  -1.037  1.00 14.75           C  
ANISOU 3821  CA  VAL D 158     1956   1827   1820   -491     -6    272       C  
ATOM   3822  C   VAL D 158     -17.787  24.993  -2.096  1.00 14.79           C  
ANISOU 3822  C   VAL D 158     1769   2176   1676     77    558     52       C  
ATOM   3823  O   VAL D 158     -18.670  25.797  -1.774  1.00 16.25           O  
ANISOU 3823  O   VAL D 158     1907   2492   1776    447    528   -188       O  
ATOM   3824  CB  VAL D 158     -17.930  23.245  -0.282  1.00 16.12           C  
ANISOU 3824  CB  VAL D 158     2182   1935   2007   -633   -108    355       C  
ATOM   3825  CG1 VAL D 158     -18.695  22.375  -1.266  1.00 17.44           C  
ANISOU 3825  CG1 VAL D 158     2532   1902   2192   -416    339    468       C  
ATOM   3826  CG2 VAL D 158     -17.114  22.383   0.670  1.00 16.32           C  
ANISOU 3826  CG2 VAL D 158     1934   2070   2197   -857   -785    166       C  
ATOM   3827  N   LEU D 159     -17.444  24.770  -3.364  1.00 11.75           N  
ANISOU 3827  N   LEU D 159     1346   1882   1236   -100    402    235       N  
ATOM   3828  CA  LEU D 159     -18.075  25.510  -4.449  1.00 11.16           C  
ANISOU 3828  CA  LEU D 159      976   1798   1467     68    329    406       C  
ATOM   3829  C   LEU D 159     -19.555  25.166  -4.522  1.00 13.12           C  
ANISOU 3829  C   LEU D 159     1290   1682   2015   -143     94    284       C  
ATOM   3830  O   LEU D 159     -19.928  23.998  -4.673  1.00 14.99           O  
ANISOU 3830  O   LEU D 159     1584   1650   2463     16    105    131       O  
ATOM   3831  CB  LEU D 159     -17.381  25.205  -5.779  1.00 10.46           C  
ANISOU 3831  CB  LEU D 159      765   1808   1401    238    249    452       C  
ATOM   3832  CG  LEU D 159     -17.569  26.215  -6.923  1.00 10.86           C  
ANISOU 3832  CG  LEU D 159      735   1997   1393    477    -45    260       C  
ATOM   3833  CD1 LEU D 159     -16.517  26.013  -8.001  1.00  9.90           C  
ANISOU 3833  CD1 LEU D 159      751   1750   1262    499    230     55       C  
ATOM   3834  CD2 LEU D 159     -18.963  26.156  -7.543  1.00 12.79           C  
ANISOU 3834  CD2 LEU D 159     1237   2157   1466    150   -274    496       C  
ATOM   3835  N   GLN D 160     -20.395  26.191  -4.412  1.00 15.43           N  
ANISOU 3835  N   GLN D 160     1587   2183   2092   -297    483    229       N  
ATOM   3836  CA  GLN D 160     -21.840  26.053  -4.506  1.00 17.42           C  
ANISOU 3836  CA  GLN D 160     1717   2239   2662    132    608    693       C  
ATOM   3837  C   GLN D 160     -22.362  27.082  -5.494  1.00 18.51           C  
ANISOU 3837  C   GLN D 160     1872   2265   2898    370    509    592       C  
ATOM   3838  O   GLN D 160     -22.008  28.262  -5.409  1.00 19.33           O  
ANISOU 3838  O   GLN D 160     2367   1893   3084    554    279    743       O  
ATOM   3839  CB  GLN D 160     -22.508  26.249  -3.141  1.00 20.48           C  
ANISOU 3839  CB  GLN D 160     1974   2764   3045     11   1088    827       C  
ATOM   3840  CG  GLN D 160     -22.080  25.245  -2.083  1.00 28.34           C  
ANISOU 3840  CG  GLN D 160     3103   3894   3769     97    808    616       C  
ATOM   3841  CD  GLN D 160     -23.046  24.084  -1.957  1.00 35.10           C  
ANISOU 3841  CD  GLN D 160     4182   4860   4294    396    551    412       C  
ATOM   3842  OE1 GLN D 160     -22.729  22.953  -2.327  1.00 36.51           O  
ANISOU 3842  OE1 GLN D 160     4638   4768   4467    479    126    163       O  
ATOM   3843  NE2 GLN D 160     -24.232  24.358  -1.424  1.00 38.72           N  
ANISOU 3843  NE2 GLN D 160     4544   5670   4499    596    604    527       N  
ATOM   3844  N   LEU D 161     -23.177  26.639  -6.424  1.00 17.13           N  
ANISOU 3844  N   LEU D 161     1326   2084   3101     14    614    234       N  
ATOM   3845  CA  LEU D 161     -23.880  27.544  -7.314  1.00 19.18           C  
ANISOU 3845  CA  LEU D 161     1312   2553   3424   -102    495    131       C  
ATOM   3846  C   LEU D 161     -25.305  27.746  -6.818  1.00 23.94           C  
ANISOU 3846  C   LEU D 161     2003   3178   3913    293    710      4       C  
ATOM   3847  O   LEU D 161     -25.824  26.926  -6.055  1.00 24.82           O  
ANISOU 3847  O   LEU D 161     1733   3623   4076    292    742   -107       O  
ATOM   3848  CB  LEU D 161     -23.881  26.986  -8.741  1.00 18.34           C  
ANISOU 3848  CB  LEU D 161     1288   2404   3277   -169    633    240       C  
ATOM   3849  CG  LEU D 161     -22.486  26.760  -9.331  1.00 19.70           C  
ANISOU 3849  CG  LEU D 161     1670   2582   3232   -289    121    118       C  
ATOM   3850  CD1 LEU D 161     -22.569  26.118 -10.705  1.00 22.59           C  
ANISOU 3850  CD1 LEU D 161     1882   3400   3300     59    109   -188       C  
ATOM   3851  CD2 LEU D 161     -21.708  28.066  -9.397  1.00 22.51           C  
ANISOU 3851  CD2 LEU D 161     2046   3178   3327    -91    153    152       C  
ATOM   3852  N   PRO D 162     -25.961  28.843  -7.203  1.00 29.35           N  
ANISOU 3852  N   PRO D 162     2910   3790   4451    585    552   -169       N  
ATOM   3853  CA  PRO D 162     -27.327  29.093  -6.724  1.00 33.44           C  
ANISOU 3853  CA  PRO D 162     3565   4201   4940    726    358   -196       C  
ATOM   3854  C   PRO D 162     -28.253  27.913  -6.991  1.00 38.89           C  
ANISOU 3854  C   PRO D 162     3975   5233   5567    569    234   -269       C  
ATOM   3855  O   PRO D 162     -28.047  27.133  -7.923  1.00 38.06           O  
ANISOU 3855  O   PRO D 162     3588   5156   5716    681    128   -391       O  
ATOM   3856  CB  PRO D 162     -27.755  30.334  -7.515  1.00 31.40           C  
ANISOU 3856  CB  PRO D 162     3400   3829   4702   1394    165     15       C  
ATOM   3857  CG  PRO D 162     -26.478  31.055  -7.766  1.00 31.22           C  
ANISOU 3857  CG  PRO D 162     3360   3804   4699   1398    317   -105       C  
ATOM   3858  CD  PRO D 162     -25.434  29.985  -7.973  1.00 31.38           C  
ANISOU 3858  CD  PRO D 162     3433   3832   4657    943    322    -59       C  
ATOM   3859  N   GLN D 163     -29.286  27.795  -6.150  1.00 44.33           N  
ANISOU 3859  N   GLN D 163     4792   6092   5960    184    179   -167       N  
ATOM   3860  CA  GLN D 163     -30.194  26.653  -6.203  1.00 49.83           C  
ANISOU 3860  CA  GLN D 163     5548   6990   6393      0     84    101       C  
ATOM   3861  C   GLN D 163     -30.814  26.449  -7.579  1.00 51.26           C  
ANISOU 3861  C   GLN D 163     5438   7407   6631   -267   -225    242       C  
ATOM   3862  O   GLN D 163     -31.296  25.349  -7.873  1.00 52.10           O  
ANISOU 3862  O   GLN D 163     5439   7548   6809   -224   -198    563       O  
ATOM   3863  CB  GLN D 163     -31.301  26.819  -5.157  1.00 53.35           C  
ANISOU 3863  CB  GLN D 163     6279   7422   6568   -251     44    141       C  
ATOM   3864  CG  GLN D 163     -30.855  26.570  -3.724  1.00 56.49           C  
ANISOU 3864  CG  GLN D 163     6930   7763   6769   -459     92     70       C  
ATOM   3865  CD  GLN D 163     -30.722  25.094  -3.402  1.00 59.77           C  
ANISOU 3865  CD  GLN D 163     7508   8180   7022   -650     73   -109       C  
ATOM   3866  OE1 GLN D 163     -31.225  24.239  -4.132  1.00 61.13           O  
ANISOU 3866  OE1 GLN D 163     7692   8387   7147   -949     25   -157       O  
ATOM   3867  NE2 GLN D 163     -30.040  24.786  -2.304  1.00 60.65           N  
ANISOU 3867  NE2 GLN D 163     7697   8285   7063   -553    122   -152       N  
ATOM   3868  N   GLY D 164     -30.810  27.472  -8.429  1.00 53.26           N  
ANISOU 3868  N   GLY D 164     5677   7812   6746   -331   -329    144       N  
ATOM   3869  CA  GLY D 164     -31.358  27.378  -9.763  1.00 56.04           C  
ANISOU 3869  CA  GLY D 164     6335   8085   6875   -315   -281     38       C  
ATOM   3870  C   GLY D 164     -30.363  27.124 -10.873  1.00 57.67           C  
ANISOU 3870  C   GLY D 164     6643   8257   7012   -173   -358    -37       C  
ATOM   3871  O   GLY D 164     -30.766  27.052 -12.038  1.00 59.57           O  
ANISOU 3871  O   GLY D 164     6880   8585   7170   -216   -451    -49       O  
ATOM   3872  N   THR D 165     -29.078  26.984 -10.558  1.00 56.58           N  
ANISOU 3872  N   THR D 165     6642   7905   6949    -67   -350    -49       N  
ATOM   3873  CA  THR D 165     -28.043  26.741 -11.555  1.00 53.30           C  
ANISOU 3873  CA  THR D 165     6050   7398   6805     53   -419    -34       C  
ATOM   3874  C   THR D 165     -27.490  25.333 -11.380  1.00 51.55           C  
ANISOU 3874  C   THR D 165     5754   7324   6507    346   -448    203       C  
ATOM   3875  O   THR D 165     -27.116  24.943 -10.270  1.00 52.94           O  
ANISOU 3875  O   THR D 165     6010   7654   6452    330   -292    435       O  
ATOM   3876  CB  THR D 165     -26.913  27.768 -11.442  1.00 51.62           C  
ANISOU 3876  CB  THR D 165     5838   6913   6863   -150   -668   -230       C  
ATOM   3877  OG1 THR D 165     -27.446  29.089 -11.600  1.00 51.05           O  
ANISOU 3877  OG1 THR D 165     5782   6677   6936   -607   -744   -354       O  
ATOM   3878  CG2 THR D 165     -25.861  27.524 -12.515  1.00 50.83           C  
ANISOU 3878  CG2 THR D 165     5790   6695   6829    -55   -733   -259       C  
ATOM   3879  N   THR D 166     -27.441  24.579 -12.474  1.00 48.77           N  
ANISOU 3879  N   THR D 166     5283   6985   6261    310   -612    159       N  
ATOM   3880  CA  THR D 166     -26.905  23.227 -12.477  1.00 45.82           C  
ANISOU 3880  CA  THR D 166     4879   6562   5970    188   -645    360       C  
ATOM   3881  C   THR D 166     -25.584  23.190 -13.235  1.00 40.00           C  
ANISOU 3881  C   THR D 166     4044   5631   5525    611   -543    461       C  
ATOM   3882  O   THR D 166     -25.306  24.037 -14.088  1.00 39.17           O  
ANISOU 3882  O   THR D 166     3763   5734   5384   1466   -759    644       O  
ATOM   3883  CB  THR D 166     -27.895  22.241 -13.106  1.00 48.65           C  
ANISOU 3883  CB  THR D 166     5390   7046   6048   -253   -396    571       C  
ATOM   3884  OG1 THR D 166     -28.049  22.541 -14.498  1.00 50.30           O  
ANISOU 3884  OG1 THR D 166     5705   7313   6093   -528   -476    621       O  
ATOM   3885  CG2 THR D 166     -29.248  22.342 -12.420  1.00 50.58           C  
ANISOU 3885  CG2 THR D 166     5907   7204   6108    -67   -106    573       C  
ATOM   3886  N   LEU D 167     -24.769  22.189 -12.910  1.00 35.40           N  
ANISOU 3886  N   LEU D 167     3789   4454   5209    214   -398    340       N  
ATOM   3887  CA  LEU D 167     -23.448  22.081 -13.513  1.00 31.26           C  
ANISOU 3887  CA  LEU D 167     3501   3570   4806    469   -313    239       C  
ATOM   3888  C   LEU D 167     -23.568  21.780 -15.005  1.00 27.90           C  
ANISOU 3888  C   LEU D 167     2921   3251   4427    217   -425    535       C  
ATOM   3889  O   LEU D 167     -24.474  21.051 -15.423  1.00 26.86           O  
ANISOU 3889  O   LEU D 167     2602   3374   4230   -442   -821    897       O  
ATOM   3890  CB  LEU D 167     -22.627  20.987 -12.830  1.00 29.39           C  
ANISOU 3890  CB  LEU D 167     3400   2928   4841    635   -199    236       C  
ATOM   3891  CG  LEU D 167     -22.160  21.260 -11.399  1.00 30.45           C  
ANISOU 3891  CG  LEU D 167     3492   3109   4969    414     61    349       C  
ATOM   3892  CD1 LEU D 167     -21.311  20.111 -10.879  1.00 30.06           C  
ANISOU 3892  CD1 LEU D 167     3235   3397   4791    593    291    446       C  
ATOM   3893  CD2 LEU D 167     -21.390  22.568 -11.334  1.00 31.20           C  
ANISOU 3893  CD2 LEU D 167     3417   3313   5124   -322    166    355       C  
ATOM   3894  N   PRO D 168     -22.677  22.329 -15.830  1.00 25.63           N  
ANISOU 3894  N   PRO D 168     2636   2788   4315    278    -47    353       N  
ATOM   3895  CA  PRO D 168     -22.693  22.001 -17.260  1.00 26.12           C  
ANISOU 3895  CA  PRO D 168     2949   2807   4168    173    -69     89       C  
ATOM   3896  C   PRO D 168     -22.460  20.515 -17.494  1.00 25.83           C  
ANISOU 3896  C   PRO D 168     2973   2918   3922    247   -530   -329       C  
ATOM   3897  O   PRO D 168     -21.928  19.797 -16.644  1.00 23.16           O  
ANISOU 3897  O   PRO D 168     2493   2456   3850    553   -580   -226       O  
ATOM   3898  CB  PRO D 168     -21.547  22.845 -17.831  1.00 25.56           C  
ANISOU 3898  CB  PRO D 168     2746   2712   4252   -256    283    145       C  
ATOM   3899  CG  PRO D 168     -21.382  23.968 -16.851  1.00 26.00           C  
ANISOU 3899  CG  PRO D 168     2615   2989   4275   -204    329    438       C  
ATOM   3900  CD  PRO D 168     -21.686  23.370 -15.509  1.00 25.53           C  
ANISOU 3900  CD  PRO D 168     2534   2885   4282    166    188    297       C  
ATOM   3901  N   LYS D 169     -22.870  20.061 -18.678  1.00 27.97           N  
ANISOU 3901  N   LYS D 169     3171   3742   3714    374   -989   -452       N  
ATOM   3902  CA  LYS D 169     -22.851  18.637 -18.993  1.00 29.16           C  
ANISOU 3902  CA  LYS D 169     3616   3906   3559    376  -1322   -353       C  
ATOM   3903  C   LYS D 169     -21.439  18.074 -18.900  1.00 26.68           C  
ANISOU 3903  C   LYS D 169     3535   3504   3096    244  -1506   -250       C  
ATOM   3904  O   LYS D 169     -20.491  18.639 -19.453  1.00 26.33           O  
ANISOU 3904  O   LYS D 169     3782   3357   2865    225  -1714     -1       O  
ATOM   3905  CB  LYS D 169     -23.423  18.402 -20.392  1.00 34.30           C  
ANISOU 3905  CB  LYS D 169     4528   4617   3889    428  -1237   -266       C  
ATOM   3906  CG  LYS D 169     -23.574  16.935 -20.762  1.00 38.83           C  
ANISOU 3906  CG  LYS D 169     5116   5472   4165    488  -1140    -57       C  
ATOM   3907  CD  LYS D 169     -24.255  16.770 -22.114  1.00 43.06           C  
ANISOU 3907  CD  LYS D 169     5603   6220   4537    664   -771    151       C  
ATOM   3908  CE  LYS D 169     -23.365  17.244 -23.251  1.00 45.27           C  
ANISOU 3908  CE  LYS D 169     5780   6634   4785    945   -693    125       C  
ATOM   3909  NZ  LYS D 169     -22.165  16.376 -23.414  1.00 46.28           N  
ANISOU 3909  NZ  LYS D 169     5817   6829   4938   1099   -631     46       N  
ATOM   3910  N   GLY D 170     -21.305  16.956 -18.193  1.00 24.62           N  
ANISOU 3910  N   GLY D 170     3246   3213   2896    142  -1434   -339       N  
ATOM   3911  CA  GLY D 170     -20.022  16.311 -18.011  1.00 21.51           C  
ANISOU 3911  CA  GLY D 170     2796   2834   2543    -17  -1302   -439       C  
ATOM   3912  C   GLY D 170     -19.208  16.808 -16.839  1.00 16.91           C  
ANISOU 3912  C   GLY D 170     2202   2048   2174    -74   -737   -252       C  
ATOM   3913  O   GLY D 170     -18.059  16.379 -16.680  1.00 15.03           O  
ANISOU 3913  O   GLY D 170     1817   1857   2039     10   -803   -422       O  
ATOM   3914  N   PHE D 171     -19.756  17.695 -16.016  1.00 13.91           N  
ANISOU 3914  N   PHE D 171     1741   1484   2062   -417   -512     80       N  
ATOM   3915  CA  PHE D 171     -19.043  18.235 -14.869  1.00 11.73           C  
ANISOU 3915  CA  PHE D 171     1429   1024   2005   -298    -50   -113       C  
ATOM   3916  C   PHE D 171     -19.661  17.725 -13.577  1.00 13.63           C  
ANISOU 3916  C   PHE D 171     1509   1388   2282    112    -82    158       C  
ATOM   3917  O   PHE D 171     -20.886  17.615 -13.459  1.00 13.77           O  
ANISOU 3917  O   PHE D 171     1470   1338   2423   -162   -104    283       O  
ATOM   3918  CB  PHE D 171     -19.033  19.763 -14.900  1.00 12.76           C  
ANISOU 3918  CB  PHE D 171     1257   1543   2047   -535    148   -123       C  
ATOM   3919  CG  PHE D 171     -18.028  20.319 -15.855  1.00 12.34           C  
ANISOU 3919  CG  PHE D 171     1551   1158   1979   -400    573    191       C  
ATOM   3920  CD1 PHE D 171     -18.338  20.471 -17.196  1.00 12.84           C  
ANISOU 3920  CD1 PHE D 171     1834   1305   1741   -193    367    100       C  
ATOM   3921  CD2 PHE D 171     -16.754  20.642 -15.423  1.00 12.29           C  
ANISOU 3921  CD2 PHE D 171     1644   1026   2000   -175    537    -42       C  
ATOM   3922  CE1 PHE D 171     -17.403  20.963 -18.082  1.00 13.68           C  
ANISOU 3922  CE1 PHE D 171     2195   1204   1798   -276    146    243       C  
ATOM   3923  CE2 PHE D 171     -15.815  21.137 -16.305  1.00 11.06           C  
ANISOU 3923  CE2 PHE D 171     1344    941   1917     15    667    470       C  
ATOM   3924  CZ  PHE D 171     -16.138  21.290 -17.636  1.00 11.77           C  
ANISOU 3924  CZ  PHE D 171     1451   1096   1925     40    151    169       C  
ATOM   3925  N   TYR D 172     -18.796  17.396 -12.621  1.00 11.63           N  
ANISOU 3925  N   TYR D 172     1127   1257   2034    229   -596    257       N  
ATOM   3926  CA  TYR D 172     -19.201  16.804 -11.357  1.00 12.46           C  
ANISOU 3926  CA  TYR D 172     1361   1211   2161    289    -44    211       C  
ATOM   3927  C   TYR D 172     -18.348  17.392 -10.245  1.00 13.69           C  
ANISOU 3927  C   TYR D 172     1734   1471   1996     29     39     76       C  
ATOM   3928  O   TYR D 172     -17.317  18.025 -10.488  1.00 14.55           O  
ANISOU 3928  O   TYR D 172     1684   1978   1866   -186     64    194       O  
ATOM   3929  CB  TYR D 172     -19.062  15.275 -11.383  1.00 12.57           C  
ANISOU 3929  CB  TYR D 172     1300   1359   2117    800      5     -3       C  
ATOM   3930  CG  TYR D 172     -19.874  14.601 -12.466  1.00 15.07           C  
ANISOU 3930  CG  TYR D 172     1312   1444   2971    422    -98   -500       C  
ATOM   3931  CD1 TYR D 172     -19.371  14.461 -13.756  1.00 16.21           C  
ANISOU 3931  CD1 TYR D 172     1294   1671   3192    280     18   -585       C  
ATOM   3932  CD2 TYR D 172     -21.144  14.105 -12.202  1.00 18.98           C  
ANISOU 3932  CD2 TYR D 172     2074   1855   3284     -5   -130   -333       C  
ATOM   3933  CE1 TYR D 172     -20.112  13.847 -14.750  1.00 18.74           C  
ANISOU 3933  CE1 TYR D 172     1734   2085   3303    344      5   -374       C  
ATOM   3934  CE2 TYR D 172     -21.892  13.489 -13.191  1.00 20.84           C  
ANISOU 3934  CE2 TYR D 172     2349   2102   3468    495   -167   -254       C  
ATOM   3935  CZ  TYR D 172     -21.371  13.363 -14.462  1.00 20.28           C  
ANISOU 3935  CZ  TYR D 172     2043   2215   3449    664   -254   -603       C  
ATOM   3936  OH  TYR D 172     -22.111  12.750 -15.449  1.00 22.28           O  
ANISOU 3936  OH  TYR D 172     2212   2540   3714    315   -334   -765       O  
ATOM   3937  N   ALA D 173     -18.787  17.170  -9.012  1.00 14.87           N  
ANISOU 3937  N   ALA D 173     1983   1692   1976   -367    -34   -230       N  
ATOM   3938  CA  ALA D 173     -18.034  17.598  -7.843  1.00 19.37           C  
ANISOU 3938  CA  ALA D 173     2965   2111   2285   -431    -14   -413       C  
ATOM   3939  C   ALA D 173     -18.331  16.675  -6.671  1.00 22.27           C  
ANISOU 3939  C   ALA D 173     3557   2376   2529   -209    140   -317       C  
ATOM   3940  O   ALA D 173     -19.380  16.034  -6.638  1.00 23.74           O  
ANISOU 3940  O   ALA D 173     3764   2665   2592    -10    713   -491       O  
ATOM   3941  CB  ALA D 173     -18.366  19.038  -7.488  1.00 19.60           C  
ANISOU 3941  CB  ALA D 173     3235   1814   2398   -169   -320   -720       C  
ATOM   3942  OXT ALA D 173     -17.540  16.547  -5.737  1.00 25.12           O  
ANISOU 3942  OXT ALA D 173     4074   2861   2609    200     72   -128       O  
TER    3943      ALA D 173                                                      
HETATM 3944  O1  MES A 201     -13.182  10.346  -7.319  0.70 33.93           O  
ANISOU 3944  O1  MES A 201     3974   3172   5748  -1388    227    271       O  
HETATM 3945  C2  MES A 201     -13.471  11.624  -7.875  0.70 36.25           C  
ANISOU 3945  C2  MES A 201     4266   3622   5885  -1001    -37    389       C  
HETATM 3946  C3  MES A 201     -12.167  12.368  -8.139  0.70 37.52           C  
ANISOU 3946  C3  MES A 201     4543   3758   5953   -994    -72    544       C  
HETATM 3947  N4  MES A 201     -11.436  12.381  -6.882  0.70 41.01           N  
ANISOU 3947  N4  MES A 201     5117   4355   6112   -770   -165    625       N  
HETATM 3948  C5  MES A 201     -12.033  11.804  -5.686  0.70 38.49           C  
ANISOU 3948  C5  MES A 201     4804   3871   5950  -1022   -135    552       C  
HETATM 3949  C6  MES A 201     -12.509  10.401  -6.059  0.70 36.18           C  
ANISOU 3949  C6  MES A 201     4328   3587   5831  -1189      5    346       C  
HETATM 3950  C7  MES A 201     -10.377  13.367  -6.722  0.70 47.76           C  
ANISOU 3950  C7  MES A 201     6301   5472   6375   -201   -215    809       C  
HETATM 3951  C8  MES A 201     -11.050  14.632  -6.206  0.70 53.46           C  
ANISOU 3951  C8  MES A 201     7369   6388   6555    174   -317    991       C  
HETATM 3952  S   MES A 201      -9.881  15.752  -5.828  0.70 59.39           S  
ANISOU 3952  S   MES A 201     8535   7341   6687    670   -402   1286       S  
HETATM 3953  O1S MES A 201      -8.540  15.132  -5.920  0.70 59.34           O  
ANISOU 3953  O1S MES A 201     8493   7362   6693    935   -572   1281       O  
HETATM 3954  O2S MES A 201      -9.983  16.885  -6.774  0.70 60.04           O  
ANISOU 3954  O2S MES A 201     8672   7486   6655    884   -307   1515       O  
HETATM 3955  O3S MES A 201     -10.101  16.260  -4.454  0.70 60.34           O  
ANISOU 3955  O3S MES A 201     8714   7621   6593    768   -448   1397       O  
HETATM 3956 CL    CL A 202     -15.236  -1.874  12.348  1.00 14.59          CL  
ANISOU 3956 CL    CL A 202     2002   1770   1770   -197    -79    539      CL  
HETATM 3957  O1  MES A 203     -14.527   2.937  12.210  1.00 22.48           O  
ANISOU 3957  O1  MES A 203     3765   2033   2744     62    816   -641       O  
HETATM 3958  C2  MES A 203     -14.683   1.731  11.467  1.00 20.90           C  
ANISOU 3958  C2  MES A 203     3375   1664   2901   -254    429  -1129       C  
HETATM 3959  C3  MES A 203     -13.357   1.274  10.864  1.00 22.18           C  
ANISOU 3959  C3  MES A 203     3083   2241   3103   -198    786   -682       C  
HETATM 3960  N4  MES A 203     -12.711   2.398  10.192  1.00 24.11           N  
ANISOU 3960  N4  MES A 203     3408   2735   3017   -102   1125   -464       N  
HETATM 3961  C5  MES A 203     -12.654   3.686  10.871  1.00 21.86           C  
ANISOU 3961  C5  MES A 203     3263   2174   2867   -352   1398   -631       C  
HETATM 3962  C6  MES A 203     -14.054   3.997  11.383  1.00 23.55           C  
ANISOU 3962  C6  MES A 203     3765   2064   3119   -223    976   -567       C  
HETATM 3963  C7  MES A 203     -11.555   2.058   9.368  1.00 26.81           C  
ANISOU 3963  C7  MES A 203     3841   3419   2924   -120   1112   -317       C  
HETATM 3964  C8  MES A 203     -11.596   2.964   8.142  1.00 28.41           C  
ANISOU 3964  C8  MES A 203     3966   3751   3078    -70   1506   -142       C  
HETATM 3965  S   MES A 203     -10.335   2.580   7.121  1.00 30.71           S  
ANISOU 3965  S   MES A 203     4581   3723   3364    -24   1569     14       S  
HETATM 3966  O1S MES A 203     -10.866   1.799   5.984  1.00 33.41           O  
ANISOU 3966  O1S MES A 203     5118   3922   3654     -2   1306   -199       O  
HETATM 3967  O2S MES A 203      -9.723   3.821   6.596  1.00 32.79           O  
ANISOU 3967  O2S MES A 203     4415   4340   3704   -444   1446   -649       O  
HETATM 3968  O3S MES A 203      -9.306   1.795   7.835  1.00 33.49           O  
ANISOU 3968  O3S MES A 203     4496   4453   3774   -122   1065   -239       O  
HETATM 3969 ZN    ZN A 204     -15.810   9.821 -14.980  0.97 13.17          ZN  
ANISOU 3969 ZN    ZN A 204     2284   1180   1539   -184    166   -238      ZN  
HETATM 3970 CL    CL A 205     -16.989   9.766 -16.990  1.00 20.57          CL  
ANISOU 3970 CL    CL A 205     3249   1753   2814   -115   -589   -110      CL  
HETATM 3971 ZN    ZN A 206     -15.586  -3.498  13.892  1.00 14.39          ZN  
ANISOU 3971 ZN    ZN A 206     2338   1713   1417     77    -43    -44      ZN  
HETATM 3972  C1  GOL B 201     -18.962   3.702  34.178  1.00 41.25           C  
ANISOU 3972  C1  GOL B 201     5131   5218   5323    -14   -261   3152       C  
HETATM 3973  O1  GOL B 201     -17.590   3.495  34.300  1.00 36.64           O  
ANISOU 3973  O1  GOL B 201     3968   4935   5018    229   -454   2891       O  
HETATM 3974  C2  GOL B 201     -19.542   2.454  33.470  1.00 45.56           C  
ANISOU 3974  C2  GOL B 201     5867   5866   5576    -10    159   3404       C  
HETATM 3975  O2  GOL B 201     -20.117   1.556  34.364  1.00 48.25           O  
ANISOU 3975  O2  GOL B 201     6262   6294   5776     79    219   3294       O  
HETATM 3976  C3  GOL B 201     -20.566   3.014  32.475  1.00 45.84           C  
ANISOU 3976  C3  GOL B 201     5823   5950   5646    -26    547   3154       C  
HETATM 3977  O3  GOL B 201     -21.514   3.707  33.222  1.00 45.42           O  
ANISOU 3977  O3  GOL B 201     5613   5881   5766     -7    879   2863       O  
HETATM 3978  O1  MES B 202     -13.822  28.429  19.785  0.86 29.41           O  
ANISOU 3978  O1  MES B 202     3207   3333   4635   1160   -897   -174       O  
HETATM 3979  C2  MES B 202     -13.940  27.465  20.826  0.86 30.88           C  
ANISOU 3979  C2  MES B 202     3207   3622   4903   1284   -595   -193       C  
HETATM 3980  C3  MES B 202     -12.621  26.741  21.060  0.86 32.64           C  
ANISOU 3980  C3  MES B 202     3392   3933   5076   1474   -452   -147       C  
HETATM 3981  N4  MES B 202     -12.092  26.292  19.779  0.86 35.26           N  
ANISOU 3981  N4  MES B 202     3955   4190   5252   1806   -504    -89       N  
HETATM 3982  C5  MES B 202     -12.076  27.213  18.651  0.86 32.48           C  
ANISOU 3982  C5  MES B 202     3435   3913   4991   1817   -664    -25       C  
HETATM 3983  C6  MES B 202     -13.465  27.822  18.549  0.86 30.94           C  
ANISOU 3983  C6  MES B 202     3287   3657   4814   1782   -698      2       C  
HETATM 3984  C7  MES B 202     -10.967  25.370  19.856  0.86 43.96           C  
ANISOU 3984  C7  MES B 202     5566   5349   5787   1672   -235    -91       C  
HETATM 3985  C8  MES B 202     -11.260  24.219  18.903  0.86 49.99           C  
ANISOU 3985  C8  MES B 202     6696   6092   6204   2049   -101      4       C  
HETATM 3986  S   MES B 202      -9.859  23.349  18.694  0.86 56.27           S  
ANISOU 3986  S   MES B 202     7950   6870   6561   2119     11    138       S  
HETATM 3987  O1S MES B 202     -10.045  21.987  19.245  0.86 57.03           O  
ANISOU 3987  O1S MES B 202     8014   7019   6637   1937     41    390       O  
HETATM 3988  O2S MES B 202      -9.553  23.247  17.248  0.86 57.42           O  
ANISOU 3988  O2S MES B 202     8286   7061   6469   1881    342    245       O  
HETATM 3989  O3S MES B 202      -8.741  24.032  19.385  0.86 56.49           O  
ANISOU 3989  O3S MES B 202     7878   6910   6677   2158   -328    190       O  
HETATM 3990 ZN    ZN B 203     -16.597  28.860  27.492  0.92 11.86          ZN  
ANISOU 3990 ZN    ZN B 203     1907   1291   1308    249   -387    -34      ZN  
HETATM 3991 CL    CL C 201     -17.746  28.957  29.452  1.00 17.74          CL  
ANISOU 3991 CL    CL C 201     2230   1788   2724     15   -179    156      CL  
HETATM 3992 CL    CL C 202     -15.012  40.608   0.116  1.00 14.34          CL  
ANISOU 3992 CL    CL C 202     1753   1942   1753    110     56   -141      CL  
HETATM 3993  C1  GOL C 203     -23.568  28.370  21.154  1.00 33.22           C  
ANISOU 3993  C1  GOL C 203     4679   4883   3060    809   -733   -498       C  
HETATM 3994  O1  GOL C 203     -24.165  28.130  19.917  1.00 34.66           O  
ANISOU 3994  O1  GOL C 203     4760   5103   3306   1133   -546   -659       O  
HETATM 3995  C2  GOL C 203     -23.819  29.858  21.488  1.00 31.04           C  
ANISOU 3995  C2  GOL C 203     4350   4475   2968    741  -1131   -335       C  
HETATM 3996  O2  GOL C 203     -25.003  30.320  20.936  1.00 32.83           O  
ANISOU 3996  O2  GOL C 203     4655   4781   3038    778  -1472   -346       O  
HETATM 3997  C3  GOL C 203     -23.815  29.953  23.042  1.00 28.56           C  
ANISOU 3997  C3  GOL C 203     4114   3968   2769    446  -1111      7       C  
HETATM 3998  O3  GOL C 203     -23.960  28.661  23.552  1.00 28.57           O  
ANISOU 3998  O3  GOL C 203     4145   4050   2661    337  -1046   -101       O  
HETATM 3999  O1  MES C 204     -14.070  35.726   0.382  1.00 24.55           O  
ANISOU 3999  O1  MES C 204     2521   3524   3283     95  -1191  -1080       O  
HETATM 4000  C2  MES C 204     -12.802  35.104   0.594  1.00 24.90           C  
ANISOU 4000  C2  MES C 204     2891   3301   3270    388   -873  -1001       C  
HETATM 4001  C3  MES C 204     -12.484  35.062   2.085  1.00 25.16           C  
ANISOU 4001  C3  MES C 204     3293   3279   2986    308   -927  -1000       C  
HETATM 4002  N4  MES C 204     -12.672  36.408   2.615  1.00 25.12           N  
ANISOU 4002  N4  MES C 204     3231   3368   2945    146   -786   -802       N  
HETATM 4003  C5  MES C 204     -12.946  37.495   1.684  1.00 23.61           C  
ANISOU 4003  C5  MES C 204     2792   3299   2880    168  -1179   -901       C  
HETATM 4004  C6  MES C 204     -14.167  37.067   0.871  1.00 21.60           C  
ANISOU 4004  C6  MES C 204     2194   2944   3070    215  -1213  -1003       C  
HETATM 4005  C7  MES C 204     -12.082  36.761   3.906  1.00 26.46           C  
ANISOU 4005  C7  MES C 204     3211   3914   2928     11   -814   -699       C  
HETATM 4006  C8  MES C 204     -11.041  35.705   4.272  1.00 25.74           C  
ANISOU 4006  C8  MES C 204     3196   3701   2885   -215   -817   -846       C  
HETATM 4007  S   MES C 204     -10.061  36.256   5.502  1.00 26.36           S  
ANISOU 4007  S   MES C 204     3669   3331   3016   -659   -263   -289       S  
HETATM 4008  O1S MES C 204      -8.864  36.887   4.907  1.00 28.44           O  
ANISOU 4008  O1S MES C 204     3715   4104   2985   -954    174   -135       O  
HETATM 4009  O2S MES C 204     -10.781  37.242   6.337  1.00 24.97           O  
ANISOU 4009  O2S MES C 204     3493   3293   2701   -673    361   -100       O  
HETATM 4010  O3S MES C 204      -9.625  35.119   6.346  1.00 27.00           O  
ANISOU 4010  O3S MES C 204     3552   3630   3078   -698   -201   -444       O  
HETATM 4011 ZN    ZN C 205     -15.307  42.188  -1.415  1.00 13.26          ZN  
ANISOU 4011 ZN    ZN C 205     2140   1539   1359    133     88    -18      ZN  
HETATM 4012  C1  GOL D 201     -17.942  34.948 -21.674  1.00 33.72           C  
ANISOU 4012  C1  GOL D 201     5051   3930   3830    675   -158   2061       C  
HETATM 4013  O1  GOL D 201     -16.598  35.272 -21.840  1.00 29.02           O  
ANISOU 4013  O1  GOL D 201     4420   3399   3207   1013     18   1742       O  
HETATM 4014  C2  GOL D 201     -18.659  36.227 -21.174  1.00 38.69           C  
ANISOU 4014  C2  GOL D 201     5505   4853   4341    212   -297   2228       C  
HETATM 4015  O2  GOL D 201     -19.056  37.052 -22.218  1.00 40.96           O  
ANISOU 4015  O2  GOL D 201     5967   4923   4675    270   -355   2378       O  
HETATM 4016  C3  GOL D 201     -19.853  35.710 -20.354  1.00 40.84           C  
ANISOU 4016  C3  GOL D 201     5734   5184   4600    108   -433   2216       C  
HETATM 4017  O3  GOL D 201     -20.374  34.619 -21.046  1.00 42.20           O  
ANISOU 4017  O3  GOL D 201     5999   5245   4791    200   -534   2196       O  
HETATM 4018  C1  GOL D 202     -23.010  35.581  -2.627  1.00 47.62           C  
ANISOU 4018  C1  GOL D 202     5481   5969   6645    966   1063    990       C  
HETATM 4019  O1  GOL D 202     -22.398  35.387  -3.866  1.00 47.19           O  
ANISOU 4019  O1  GOL D 202     5494   5893   6544   1122   1080    975       O  
HETATM 4020  C2  GOL D 202     -23.723  36.957  -2.671  1.00 46.82           C  
ANISOU 4020  C2  GOL D 202     5217   5821   6754   1013    988    960       C  
HETATM 4021  O2  GOL D 202     -24.138  37.368  -1.411  1.00 47.51           O  
ANISOU 4021  O2  GOL D 202     5299   5960   6792   1199    936    812       O  
HETATM 4022  C3  GOL D 202     -22.691  37.924  -3.284  1.00 44.87           C  
ANISOU 4022  C3  GOL D 202     4614   5640   6795    721   1046   1020       C  
HETATM 4023  O3  GOL D 202     -23.384  39.074  -3.655  1.00 44.90           O  
ANISOU 4023  O3  GOL D 202     4659   5600   6803    321   1018   1174       O  
HETATM 4024  O   HOH A 301     -20.770 -13.442   9.441  1.00 53.59           O  
HETATM 4025  O   HOH A 302     -25.333 -13.283   4.584  1.00 36.92           O  
HETATM 4026  O   HOH A 303     -11.927  17.987  -6.894  1.00 56.54           O  
HETATM 4027  O   HOH A 304     -10.623  10.271  -0.686  1.00 76.79           O  
HETATM 4028  O   HOH A 305      -8.850 -14.454   7.872  1.00 53.36           O  
HETATM 4029  O   HOH A 306     -31.086  -4.944  -1.434  1.00 34.45           O  
HETATM 4030  O   HOH A 307     -11.699  -2.651  10.432  1.00 36.25           O  
HETATM 4031  O   HOH A 308     -27.024   1.342   7.258  1.00 33.39           O  
HETATM 4032  O   HOH A 309      -6.921   1.526   5.658  1.00 39.39           O  
HETATM 4033  O   HOH A 310     -24.022  -0.668 -18.841  1.00 17.05           O  
HETATM 4034  O   HOH A 311      -9.234  -4.116 -16.148  1.00 33.10           O  
HETATM 4035  O   HOH A 312     -23.728 -13.591   2.048  1.00 37.32           O  
HETATM 4036  O   HOH A 313     -20.883 -13.852   1.680  1.00 26.45           O  
HETATM 4037  O   HOH A 314      -9.660  12.327 -11.358  1.00 23.96           O  
HETATM 4038  O   HOH A 315     -24.585  -8.528  -0.077  1.00 20.45           O  
HETATM 4039  O   HOH A 316      -5.696   1.701 -18.691  1.00 40.67           O  
HETATM 4040  O   HOH A 317     -24.265   5.643 -17.970  1.00 37.35           O  
HETATM 4041  O   HOH A 318     -18.380  -3.881   8.829  1.00 15.83           O  
HETATM 4042  O   HOH A 319      -5.140  -9.102  -5.218  1.00 32.71           O  
HETATM 4043  O   HOH A 320      -8.039 -10.522  18.422  1.00 43.95           O  
HETATM 4044  O   HOH A 321     -18.630 -11.310   7.728  1.00 19.32           O  
HETATM 4045  O   HOH A 322      -5.971  -2.146  -0.607  1.00 35.88           O  
HETATM 4046  O   HOH A 323     -14.220 -12.051  10.286  1.00 33.66           O  
HETATM 4047  O   HOH A 324     -18.774   5.657  -7.332  1.00 11.55           O  
HETATM 4048  O   HOH A 325     -10.559   7.051 -18.138  1.00 21.63           O  
HETATM 4049  O   HOH A 326     -21.209   4.895   5.532  1.00 32.07           O  
HETATM 4050  O   HOH A 327     -28.064  -3.908 -12.870  1.00 30.89           O  
HETATM 4051  O   HOH A 328     -24.068  -0.356  -7.234  1.00 18.34           O  
HETATM 4052  O   HOH A 329     -25.484  -7.679  13.753  1.00 41.07           O  
HETATM 4053  O   HOH A 330      -9.690  -4.941  10.532  1.00 23.68           O  
HETATM 4054  O   HOH A 331     -19.051  -5.989 -19.562  1.00 38.39           O  
HETATM 4055  O   HOH A 332      -4.936  11.620  -4.799  1.00 27.88           O  
HETATM 4056  O   HOH A 333     -12.910  -5.283 -18.233  1.00 19.49           O  
HETATM 4057  O   HOH A 334      -2.626  13.523  -6.005  1.00 62.26           O  
HETATM 4058  O   HOH A 335     -13.525 -14.040  -5.341  1.00 33.12           O  
HETATM 4059  O   HOH A 336     -15.594 -13.628 -11.118  1.00 58.30           O  
HETATM 4060  O   HOH A 337     -12.818 -13.296   3.627  1.00 25.14           O  
HETATM 4061  O   HOH A 338     -25.465  -4.299   8.180  1.00 46.97           O  
HETATM 4062  O   HOH A 339      -6.826  -5.498   6.764  1.00 34.88           O  
HETATM 4063  O   HOH A 340     -16.320   5.806 -17.515  1.00 13.20           O  
HETATM 4064  O   HOH A 341     -23.444   3.784  -8.138  1.00 17.02           O  
HETATM 4065  O   HOH A 342      -6.855 -12.800  -0.177  1.00 39.12           O  
HETATM 4066  O   HOH A 343      -0.386  -8.395   9.157  1.00 45.22           O  
HETATM 4067  O   HOH A 344     -23.864   3.477  -5.654  1.00 29.25           O  
HETATM 4068  O   HOH A 345     -17.728 -13.517  -2.023  1.00 23.44           O  
HETATM 4069  O   HOH A 346     -18.899   6.480  -0.344  1.00 21.17           O  
HETATM 4070  O   HOH A 347      -9.704   3.514  -7.690  1.00 11.06           O  
HETATM 4071  O   HOH A 348     -14.852  -0.588   8.428  1.00 33.14           O  
HETATM 4072  O   HOH A 349     -25.651  -0.753  -3.558  1.00 16.62           O  
HETATM 4073  O   HOH A 350      -9.183  11.440  -9.212  1.00 25.51           O  
HETATM 4074  O   HOH A 351      -0.925  -8.391  20.099  1.00 30.24           O  
HETATM 4075  O   HOH A 352      -3.643 -16.468  18.381  1.00 54.90           O  
HETATM 4076  O   HOH A 353     -20.895  -8.845  13.604  1.00 29.26           O  
HETATM 4077  O   HOH A 354     -13.140 -12.885  -8.495  1.00 25.28           O  
HETATM 4078  O   HOH A 355     -12.493   1.135   0.072  1.00 15.39           O  
HETATM 4079  O   HOH A 356     -19.010   9.701   1.901  1.00 25.30           O  
HETATM 4080  O   HOH A 357     -22.917  -5.332  -8.493  1.00 12.66           O  
HETATM 4081  O   HOH A 358     -15.750   5.101 -21.023  1.00 16.99           O  
HETATM 4082  O   HOH A 359     -13.367 -11.159  12.542  1.00 47.26           O  
HETATM 4083  O   HOH A 360     -11.492   4.712 -20.477  1.00 33.84           O  
HETATM 4084  O   HOH A 361     -25.953  -1.841 -17.036  1.00 21.62           O  
HETATM 4085  O   HOH A 362     -23.697  -5.580 -11.436  1.00 33.44           O  
HETATM 4086  O   HOH A 363     -27.794  -0.894 -10.189  1.00 18.77           O  
HETATM 4087  O   HOH A 364      -5.745   9.701  -9.175  1.00 27.11           O  
HETATM 4088  O   HOH A 365     -24.310   3.770 -13.046  1.00 15.00           O  
HETATM 4089  O   HOH A 366     -14.871  -8.087 -18.803  1.00 20.52           O  
HETATM 4090  O   HOH A 367     -10.774   3.632  -5.064  1.00 10.51           O  
HETATM 4091  O   HOH A 368     -14.045 -11.533 -17.402  1.00 24.84           O  
HETATM 4092  O   HOH A 369      -6.782 -10.427  -1.554  1.00 30.26           O  
HETATM 4093  O   HOH A 370     -23.693  -2.573 -15.002  1.00 24.23           O  
HETATM 4094  O   HOH A 371       7.096 -10.434  22.834  1.00 39.59           O  
HETATM 4095  O   HOH A 372     -17.705 -10.973  -8.184  1.00 16.82           O  
HETATM 4096  O   HOH A 373      -5.878   0.206 -16.690  1.00 34.43           O  
HETATM 4097  O   HOH A 374     -19.712   9.915  -0.787  1.00 32.87           O  
HETATM 4098  O   HOH A 375      -9.791  -3.773 -12.886  1.00 14.00           O  
HETATM 4099  O   HOH A 376      -6.578 -10.792  -3.974  1.00 39.08           O  
HETATM 4100  O   HOH A 377     -30.208   5.615  -1.295  1.00 45.59           O  
HETATM 4101  O   HOH A 378     -18.576 -16.544   2.384  1.00 35.24           O  
HETATM 4102  O   HOH A 379     -27.490 -11.065  -7.978  1.00 31.12           O  
HETATM 4103  O   HOH A 380     -12.713 -14.561  -2.709  1.00 38.82           O  
HETATM 4104  O   HOH A 381      -5.492 -14.022  -4.953  1.00 41.18           O  
HETATM 4105  O   HOH A 382     -12.365 -15.713 -14.685  1.00 32.27           O  
HETATM 4106  O   HOH A 383     -15.162 -14.676  -1.729  1.00 47.41           O  
HETATM 4107  O   HOH A 384     -28.160  -6.247   4.689  1.00 32.58           O  
HETATM 4108  O   HOH A 385      -8.371   3.760   1.826  1.00 21.24           O  
HETATM 4109  O   HOH A 386     -26.590   6.082   2.495  1.00 45.08           O  
HETATM 4110  O   HOH A 387     -23.893   3.626   3.939  1.00 22.09           O  
HETATM 4111  O   HOH A 388     -13.449   5.891 -18.293  1.00 21.68           O  
HETATM 4112  O   HOH A 389     -24.476   1.286  -5.319  1.00 36.11           O  
HETATM 4113  O   HOH A 390      -6.286   1.934   0.665  1.00 24.58           O  
HETATM 4114  O   HOH A 391      -5.603   0.437  10.482  1.00 49.87           O  
HETATM 4115  O   HOH A 392      -7.820   3.809   4.336  1.00 30.71           O  
HETATM 4116  O   HOH A 393      -4.229   2.673 -10.641  1.00 27.00           O  
HETATM 4117  O   HOH A 394     -24.885   3.709 -20.149  1.00 42.64           O  
HETATM 4118  O   HOH A 395     -22.046   7.235  -6.867  1.00 26.57           O  
HETATM 4119  O   HOH A 396     -16.007  11.334   3.506  1.00 29.92           O  
HETATM 4120  O   HOH A 397     -15.106  12.672  -4.372  1.00 35.77           O  
HETATM 4121  O   HOH A 398     -19.159  11.963  -2.713  1.00 25.98           O  
HETATM 4122  O   HOH A 399     -20.199  -8.979  -5.558  1.00 20.07           O  
HETATM 4123  O   HOH A 400     -22.216  -7.756  -7.707  1.00 21.83           O  
HETATM 4124  O   HOH A 401     -14.113  14.685  -5.296  1.00 26.97           O  
HETATM 4125  O   HOH A 402     -19.741 -15.610  11.479  1.00 35.31           O  
HETATM 4126  O   HOH A 403     -22.447   9.227  -8.843  1.00 41.63           O  
HETATM 4127  O   HOH A 404     -11.117  13.397  -0.192  1.00 37.03           O  
HETATM 4128  O   HOH A 405      -4.003   7.062 -10.361  1.00 21.80           O  
HETATM 4129  O   HOH A 406       0.769  -8.009  17.823  1.00 38.01           O  
HETATM 4130  O   HOH A 407      -3.319   8.936  -8.771  1.00 51.13           O  
HETATM 4131  O   HOH A 408     -25.368  -1.710   8.147  1.00 42.42           O  
HETATM 4132  O   HOH A 409      -4.664   6.726 -13.221  1.00 21.80           O  
HETATM 4133  O   HOH A 410     -23.667  10.392 -11.219  1.00 39.54           O  
HETATM 4134  O   HOH A 411     -22.935   6.429 -21.759  1.00 36.44           O  
HETATM 4135  O   HOH A 412      -4.020  -9.869   2.769  1.00 36.37           O  
HETATM 4136  O   HOH A 413     -24.655  -8.923  10.856  1.00 45.23           O  
HETATM 4137  O   HOH A 414      -7.051 -16.915  -7.206  1.00 36.35           O  
HETATM 4138  O   HOH A 415     -26.098  -7.533   7.102  1.00 38.52           O  
HETATM 4139  O   HOH A 416     -10.749  -8.821  14.830  1.00 18.57           O  
HETATM 4140  O   HOH A 417      -2.908  -5.597 -12.245  1.00 34.67           O  
HETATM 4141  O   HOH A 418     -22.112   9.040 -17.567  1.00 30.25           O  
HETATM 4142  O   HOH A 419      -7.040  -4.198  -0.912  1.00 29.73           O  
HETATM 4143  O   HOH A 420     -14.219  -8.033  15.277  1.00 45.34           O  
HETATM 4144  O   HOH A 421     -29.780  -4.541   4.320  1.00 49.24           O  
HETATM 4145  O   HOH A 422      -9.140 -13.696   5.258  1.00 41.45           O  
HETATM 4146  O   HOH A 423      -5.607  -0.310   0.731  1.00 41.11           O  
HETATM 4147  O   HOH A 424     -16.997   7.097 -19.766  1.00 17.16           O  
HETATM 4148  O   HOH A 425     -25.049  -4.447 -13.367  1.00 39.61           O  
HETATM 4149  O   HOH A 426     -15.034   3.786   8.171  1.00 26.95           O  
HETATM 4150  O   HOH A 427     -10.605  -1.985 -17.559  1.00 38.76           O  
HETATM 4151  O   HOH A 428     -30.512  -0.563  -3.388  1.00 46.28           O  
HETATM 4152  O   HOH A 429     -13.461   8.483 -19.710  1.00 29.22           O  
HETATM 4153  O   HOH A 430     -25.457 -11.013   1.052  1.00 34.90           O  
HETATM 4154  O   HOH A 431     -23.769   8.206 -10.819  1.00 34.35           O  
HETATM 4155  O   HOH A 432      -1.634   5.209 -10.129  1.00 35.05           O  
HETATM 4156  O   HOH A 433      -3.884  -1.822 -16.727  1.00 44.31           O  
HETATM 4157  O   HOH A 434     -28.619   6.991   0.056  1.00 46.12           O  
HETATM 4158  O   HOH A 435      -2.603   0.719  -6.252  1.00 32.94           O  
HETATM 4159  O   HOH A 436     -18.281  -8.678 -19.769  1.00 29.50           O  
HETATM 4160  O   HOH A 437     -15.747 -13.146  -8.626  1.00 27.84           O  
HETATM 4161  O   HOH A 438     -32.700  -0.115  -3.845  1.00 66.87           O  
HETATM 4162  O   HOH A 439     -13.417   5.590 -21.668  1.00 40.14           O  
HETATM 4163  O   HOH A 440     -16.190  -9.021  15.801  1.00 43.53           O  
HETATM 4164  O   HOH A 441     -21.420 -16.569  -1.903  1.00 49.32           O  
HETATM 4165  O   HOH A 442      -5.298   4.264 -12.518  1.00 24.88           O  
HETATM 4166  O   HOH A 443     -25.419   1.014 -20.759  1.00 25.30           O  
HETATM 4167  O   HOH A 444     -12.827  19.093  -3.362  1.00 39.35           O  
HETATM 4168  O   HOH A 445     -16.205  -9.281 -20.661  1.00 33.61           O  
HETATM 4169  O   HOH A 446     -19.677 -15.204  -0.531  1.00 27.94           O  
HETATM 4170  O   HOH A 447     -20.877   6.550 -23.758  1.00 25.79           O  
HETATM 4171  O   HOH A 448     -22.252  -9.380 -10.023  1.00 38.60           O  
HETATM 4172  O   HOH A 449     -19.961 -10.891 -10.151  1.00 40.76           O  
HETATM 4173  O   HOH A 450     -12.845  -7.046 -20.667  1.00 28.02           O  
HETATM 4174  O   HOH A 451     -19.134 -21.477  12.613  1.00 65.65           O  
HETATM 4175  O   HOH A 452     -29.825  -2.816 -10.695  1.00 34.93           O  
HETATM 4176  O   HOH A 453     -25.239   5.610  -9.080  1.00 26.32           O  
HETATM 4177  O   HOH A 454     -16.202 -14.785  -6.066  1.00 29.59           O  
HETATM 4178  O   HOH A 455     -12.965 -11.327  17.564  1.00 58.57           O  
HETATM 4179  O   HOH A 456     -25.569   5.687 -11.723  1.00 28.96           O  
HETATM 4180  O   HOH A 457     -18.513 -13.721  -4.600  1.00 26.68           O  
HETATM 4181  O   HOH A 458     -28.169   1.967  -6.836  1.00 38.47           O  
HETATM 4182  O   HOH A 459     -29.946  -0.817  -5.608  1.00 48.08           O  
HETATM 4183  O   HOH A 460     -28.960   1.590  -9.261  1.00 34.21           O  
HETATM 4184  O   HOH A 461      -3.850   2.035   1.260  1.00 43.05           O  
HETATM 4185  O   HOH A 462     -19.257 -11.788  -6.008  1.00 21.34           O  
HETATM 4186  O   HOH A 463      -1.692   3.904   1.231  1.00 47.88           O  
HETATM 4187  O   HOH A 464     -24.624   6.098  -5.715  1.00 37.82           O  
HETATM 4188  O   HOH A 465     -14.266   3.835 -24.266  1.00 40.64           O  
HETATM 4189  O   HOH A 466     -16.060  13.026   1.582  1.00 34.39           O  
HETATM 4190  O   HOH A 467     -27.620   7.318 -13.110  1.00 40.04           O  
HETATM 4191  O   HOH A 468     -21.042 -13.318  -9.748  1.00 50.03           O  
HETATM 4192  O   HOH B 301      -4.294   9.843  20.328  1.00 31.33           O  
HETATM 4193  O   HOH B 302     -28.139  13.786  20.693  1.00 51.75           O  
HETATM 4194  O   HOH B 303     -20.380  15.504  32.898  1.00 28.92           O  
HETATM 4195  O   HOH B 304     -23.386  -0.986  13.790  1.00 40.40           O  
HETATM 4196  O   HOH B 305      -0.444  21.081  30.108  1.00 45.66           O  
HETATM 4197  O   HOH B 306      -7.085  22.510  29.763  1.00 50.51           O  
HETATM 4198  O   HOH B 307     -17.618   5.882   9.789  1.00 22.91           O  
HETATM 4199  O   HOH B 308     -23.543  -6.833  19.999  1.00 39.21           O  
HETATM 4200  O   HOH B 309      -7.592  22.070  32.505  1.00 46.66           O  
HETATM 4201  O   HOH B 310      -5.471  21.757  34.600  1.00 56.17           O  
HETATM 4202  O   HOH B 311     -15.908  21.365  18.232  1.00 26.04           O  
HETATM 4203  O   HOH B 312      -8.768  -8.391  18.852  1.00 30.34           O  
HETATM 4204  O   HOH B 313     -20.632   2.231  37.762  1.00 30.47           O  
HETATM 4205  O   HOH B 314     -15.764   2.190   6.049  1.00 26.84           O  
HETATM 4206  O   HOH B 315     -19.086   3.761  17.451  1.00 15.70           O  
HETATM 4207  O   HOH B 316      -5.883  -8.096  21.782  1.00 30.14           O  
HETATM 4208  O   HOH B 317      -6.297   5.929   9.330  1.00 15.61           O  
HETATM 4209  O   HOH B 318     -24.437   0.209  10.685  1.00 34.96           O  
HETATM 4210  O   HOH B 319     -12.036  -4.768  29.219  1.00 18.12           O  
HETATM 4211  O   HOH B 320     -14.104  26.548  33.672  1.00 41.13           O  
HETATM 4212  O   HOH B 321     -24.166   5.410  19.795  1.00 35.29           O  
HETATM 4213  O   HOH B 322     -21.677  17.754  32.946  1.00 32.67           O  
HETATM 4214  O   HOH B 323     -19.844  17.022  17.973  1.00 15.88           O  
HETATM 4215  O   HOH B 324     -12.159   6.048  35.202  1.00 24.53           O  
HETATM 4216  O   HOH B 325     -13.713  23.898  32.184  1.00 23.56           O  
HETATM 4217  O   HOH B 326      -3.321  30.898  36.549  1.00 51.13           O  
HETATM 4218  O   HOH B 327      -8.855  29.622  31.273  1.00 39.18           O  
HETATM 4219  O   HOH B 328     -15.389  -9.489  20.350  1.00 30.83           O  
HETATM 4220  O   HOH B 329     -17.085  17.530  18.164  1.00 13.24           O  
HETATM 4221  O   HOH B 330     -13.267  10.061   8.093  1.00 24.09           O  
HETATM 4222  O   HOH B 331     -16.693  11.896  35.348  1.00 34.19           O  
HETATM 4223  O   HOH B 332      -6.380  12.692  22.320  1.00 43.47           O  
HETATM 4224  O   HOH B 333     -21.495   0.337  31.048  1.00 60.35           O  
HETATM 4225  O   HOH B 334     -20.488  12.843  11.727  1.00 24.83           O  
HETATM 4226  O   HOH B 335     -24.133   9.831  35.649  1.00 48.90           O  
HETATM 4227  O   HOH B 336     -13.987  -4.640  32.461  1.00 13.87           O  
HETATM 4228  O   HOH B 337     -24.036  -2.061  20.599  1.00 19.12           O  
HETATM 4229  O   HOH B 338     -12.957  25.955  30.111  1.00 21.11           O  
HETATM 4230  O   HOH B 339      -7.407  21.994  25.716  1.00 22.34           O  
HETATM 4231  O   HOH B 340     -10.052   4.185  18.751  1.00 12.89           O  
HETATM 4232  O   HOH B 341     -15.216  20.247  20.537  1.00 16.93           O  
HETATM 4233  O   HOH B 342     -22.351   4.282  28.791  1.00 18.75           O  
HETATM 4234  O   HOH B 343     -20.135  10.245  15.414  1.00 15.40           O  
HETATM 4235  O   HOH B 344     -16.344   5.883  33.890  1.00 13.85           O  
HETATM 4236  O   HOH B 345      -3.691  16.600  28.938  1.00 45.25           O  
HETATM 4237  O   HOH B 346     -25.591   8.002  23.600  1.00 23.40           O  
HETATM 4238  O   HOH B 347     -13.168  11.943  20.024  1.00 11.47           O  
HETATM 4239  O   HOH B 348     -11.980  18.051  33.666  1.00 27.76           O  
HETATM 4240  O   HOH B 349     -22.560   7.760  34.811  1.00 31.27           O  
HETATM 4241  O   HOH B 350      -6.986  12.318  24.936  1.00 25.14           O  
HETATM 4242  O   HOH B 351     -12.464   9.687  35.711  1.00 26.27           O  
HETATM 4243  O   HOH B 352     -10.698  -8.734  20.806  1.00 25.67           O  
HETATM 4244  O   HOH B 353     -18.659  20.622  32.632  1.00 22.02           O  
HETATM 4245  O   HOH B 354     -15.992  -6.243  18.786  1.00 14.89           O  
HETATM 4246  O   HOH B 355      -4.634  10.765  34.896  1.00 44.16           O  
HETATM 4247  O   HOH B 356     -27.467   1.407  25.048  1.00 24.28           O  
HETATM 4248  O   HOH B 357     -10.137  23.678  23.943  1.00 16.53           O  
HETATM 4249  O   HOH B 358     -24.030  21.918  27.284  1.00 41.51           O  
HETATM 4250  O   HOH B 359     -13.601  19.545  36.021  1.00 38.30           O  
HETATM 4251  O   HOH B 360     -18.905  -8.736  26.882  1.00 27.00           O  
HETATM 4252  O   HOH B 361     -26.033  12.798  28.784  1.00 35.81           O  
HETATM 4253  O   HOH B 362     -16.987  27.310  33.660  1.00 31.37           O  
HETATM 4254  O   HOH B 363     -23.480   2.880  19.722  1.00 23.90           O  
HETATM 4255  O   HOH B 364     -11.671   9.199   6.105  1.00 31.07           O  
HETATM 4256  O   HOH B 365      -9.715  13.740  16.531  1.00 14.35           O  
HETATM 4257  O   HOH B 366     -23.917   4.529  23.918  1.00 20.94           O  
HETATM 4258  O   HOH B 367     -24.496  23.048  29.249  1.00 36.41           O  
HETATM 4259  O   HOH B 368      -1.119   3.065  23.306  1.00 41.80           O  
HETATM 4260  O   HOH B 369     -23.761  21.692  23.855  1.00 32.18           O  
HETATM 4261  O   HOH B 370      -9.175  18.184  17.702  1.00 41.55           O  
HETATM 4262  O   HOH B 371     -11.372   6.664  18.293  1.00 12.10           O  
HETATM 4263  O   HOH B 372      -8.475  -3.281  27.098  1.00 23.80           O  
HETATM 4264  O   HOH B 373     -15.479 -10.441  27.186  1.00 48.86           O  
HETATM 4265  O   HOH B 374     -18.543  -7.736  15.624  1.00 30.64           O  
HETATM 4266  O   HOH B 375      -6.270  12.705  31.099  1.00 30.32           O  
HETATM 4267  O   HOH B 376     -10.293  -6.902  16.916  1.00 16.59           O  
HETATM 4268  O   HOH B 377     -21.723   6.820  10.840  1.00 25.80           O  
HETATM 4269  O   HOH B 378     -11.896  23.056  22.159  1.00 20.01           O  
HETATM 4270  O   HOH B 379      -8.793   0.435  26.807  1.00 13.34           O  
HETATM 4271  O   HOH B 380      -6.631  19.513  24.530  1.00 22.87           O  
HETATM 4272  O   HOH B 381      -3.070   6.652  20.466  1.00 29.49           O  
HETATM 4273  O   HOH B 382     -10.023  15.953  10.748  1.00 24.64           O  
HETATM 4274  O   HOH B 383     -21.644   5.417  30.890  1.00 22.92           O  
HETATM 4275  O   HOH B 384     -21.813  -7.239  16.162  1.00 40.91           O  
HETATM 4276  O   HOH B 385      -0.372  22.509  27.054  1.00 46.35           O  
HETATM 4277  O   HOH B 386     -18.391  13.182  10.118  1.00 24.87           O  
HETATM 4278  O   HOH B 387     -19.141  14.451  36.386  1.00 31.69           O  
HETATM 4279  O   HOH B 388     -14.554  27.945  30.964  1.00 22.45           O  
HETATM 4280  O   HOH B 389     -19.240   7.880  31.717  1.00 20.92           O  
HETATM 4281  O   HOH B 390     -17.182  -1.456   7.791  1.00 20.12           O  
HETATM 4282  O   HOH B 391      -6.541   1.545  12.372  1.00 40.31           O  
HETATM 4283  O   HOH B 392     -28.851  12.292  27.586  1.00 49.80           O  
HETATM 4284  O   HOH B 393      -7.299  12.952  18.294  1.00 18.64           O  
HETATM 4285  O   HOH B 394      -4.451   2.039  19.305  1.00 30.66           O  
HETATM 4286  O   HOH B 395     -12.120  12.210  35.421  1.00 31.47           O  
HETATM 4287  O   HOH B 396     -11.974  18.057  17.650  1.00 18.11           O  
HETATM 4288  O   HOH B 397     -20.675   8.578  11.870  1.00 36.25           O  
HETATM 4289  O   HOH B 398     -25.984  26.155  26.777  1.00 43.01           O  
HETATM 4290  O   HOH B 399     -22.820  14.202  34.473  1.00 39.44           O  
HETATM 4291  O   HOH B 400     -21.799  26.059  30.453  1.00 32.24           O  
HETATM 4292  O   HOH B 401     -16.134  16.546  38.154  1.00 33.29           O  
HETATM 4293  O   HOH B 402      -8.721  20.408  16.663  1.00 32.76           O  
HETATM 4294  O   HOH B 403     -25.882  20.638  27.501  1.00 44.10           O  
HETATM 4295  O   HOH B 404      -4.561  18.261  23.446  1.00 29.21           O  
HETATM 4296  O   HOH B 405     -22.894   3.309  15.969  1.00 31.81           O  
HETATM 4297  O   HOH B 406     -12.856  26.417  24.406  1.00 34.91           O  
HETATM 4298  O   HOH B 407     -13.324  16.796  10.877  1.00 31.15           O  
HETATM 4299  O   HOH B 408     -12.959  -6.758  18.136  1.00 24.66           O  
HETATM 4300  O   HOH B 409      -4.432   9.537  30.575  1.00 40.65           O  
HETATM 4301  O   HOH B 410      -5.787   8.316  38.492  1.00 32.51           O  
HETATM 4302  O   HOH B 411      -6.481  15.416  13.878  1.00 32.92           O  
HETATM 4303  O   HOH B 412      -2.712   1.738  28.901  1.00 30.61           O  
HETATM 4304  O   HOH B 413      -3.957   1.815  14.955  1.00 32.81           O  
HETATM 4305  O   HOH B 414     -10.572  26.000  31.196  1.00 25.53           O  
HETATM 4306  O   HOH B 415     -22.713  21.984  21.550  1.00 28.80           O  
HETATM 4307  O   HOH B 416     -23.459   1.268  14.477  1.00 38.41           O  
HETATM 4308  O   HOH B 417      -6.133  26.627  20.296  1.00 40.90           O  
HETATM 4309  O   HOH B 418      -7.304   6.566  40.534  1.00 49.03           O  
HETATM 4310  O   HOH B 419     -24.083  15.398  19.359  1.00 36.56           O  
HETATM 4311  O   HOH B 420     -21.083  -1.634  33.520  1.00 38.57           O  
HETATM 4312  O   HOH B 421     -21.428  10.697  12.557  1.00 36.49           O  
HETATM 4313  O   HOH B 422     -16.669  -8.715  18.028  1.00 37.41           O  
HETATM 4314  O   HOH B 423     -10.500  -5.291  26.879  1.00 28.93           O  
HETATM 4315  O   HOH B 424     -25.907   5.351  22.415  1.00 45.28           O  
HETATM 4316  O   HOH B 425     -12.871 -10.112  19.705  1.00 39.97           O  
HETATM 4317  O   HOH B 426     -16.159  19.513  16.549  1.00 23.48           O  
HETATM 4318  O   HOH B 427     -22.204  15.324  11.286  1.00 40.20           O  
HETATM 4319  O   HOH B 428     -16.626  -5.077  33.459  1.00 22.76           O  
HETATM 4320  O   HOH B 429      -9.746  24.019  32.856  1.00 27.28           O  
HETATM 4321  O   HOH B 430     -10.988  20.153  34.426  1.00 38.11           O  
HETATM 4322  O   HOH B 431     -11.839  22.799  33.681  1.00 29.29           O  
HETATM 4323  O   HOH B 432     -22.893  25.135  32.267  1.00 50.17           O  
HETATM 4324  O   HOH B 433     -15.445  11.614   8.132  1.00 24.03           O  
HETATM 4325  O   HOH B 434     -24.127  -0.368  15.881  1.00 41.82           O  
HETATM 4326  O   HOH B 435     -22.336  17.058  19.769  1.00 28.44           O  
HETATM 4327  O   HOH B 436     -18.630   8.059   9.533  1.00 21.17           O  
HETATM 4328  O   HOH B 437      -8.556  19.771  33.597  1.00 37.69           O  
HETATM 4329  O   HOH B 438      -6.282  14.106  20.184  1.00 37.06           O  
HETATM 4330  O   HOH B 439     -20.769  19.137  16.420  1.00 31.83           O  
HETATM 4331  O   HOH B 440     -12.884  -9.137  16.748  1.00 64.89           O  
HETATM 4332  O   HOH B 441     -20.998  13.425  39.927  1.00 44.88           O  
HETATM 4333  O   HOH B 442     -10.092  16.355  15.865  1.00 19.55           O  
HETATM 4334  O   HOH B 443     -12.673  23.127  35.861  1.00 41.80           O  
HETATM 4335  O   HOH B 444     -17.004  -8.113  33.489  1.00 39.57           O  
HETATM 4336  O   HOH B 445     -11.204  -6.771  30.804  1.00 31.26           O  
HETATM 4337  O   HOH B 446     -23.186  19.721  19.749  1.00 46.15           O  
HETATM 4338  O   HOH B 447     -18.223   7.716  34.399  1.00 22.76           O  
HETATM 4339  O   HOH B 448     -16.499  29.649  33.499  1.00 33.71           O  
HETATM 4340  O   HOH B 449     -25.239  -1.061  18.551  1.00 33.04           O  
HETATM 4341  O   HOH B 450     -28.743   1.543  22.935  1.00 43.44           O  
HETATM 4342  O   HOH B 451     -28.110   4.299  21.724  1.00 41.41           O  
HETATM 4343  O   HOH B 452     -11.614  -9.301  30.186  1.00 53.20           O  
HETATM 4344  O   HOH B 453     -10.941 -10.681  24.955  1.00 43.24           O  
HETATM 4345  O   HOH B 454     -10.215  17.269  13.269  1.00 31.73           O  
HETATM 4346  O   HOH B 455     -10.030 -10.628  22.430  1.00 38.79           O  
HETATM 4347  O   HOH B 456     -13.202  19.639  15.778  1.00 35.32           O  
HETATM 4348  O   HOH B 457     -17.952  10.580   8.524  1.00 18.67           O  
HETATM 4349  O   HOH C 301     -22.300  55.381  10.528  1.00 71.09           O  
HETATM 4350  O   HOH C 302     -25.722  51.717   7.186  1.00 27.85           O  
HETATM 4351  O   HOH C 303     -23.530  34.699   7.922  1.00 22.37           O  
HETATM 4352  O   HOH C 304      -5.618  46.083  13.070  1.00 46.69           O  
HETATM 4353  O   HOH C 305      -6.943  37.341   7.194  1.00 30.04           O  
HETATM 4354  O   HOH C 306     -31.638  43.494  13.236  1.00 32.22           O  
HETATM 4355  O   HOH C 307      -8.114  34.950   8.344  1.00 26.56           O  
HETATM 4356  O   HOH C 308     -25.051  33.103  30.282  1.00 30.46           O  
HETATM 4357  O   HOH C 309     -25.083  47.116  12.186  1.00 21.00           O  
HETATM 4358  O   HOH C 310      -9.556  43.687   2.130  1.00 21.87           O  
HETATM 4359  O   HOH C 311     -15.401  36.453   6.226  1.00 22.71           O  
HETATM 4360  O   HOH C 312     -11.185  56.256  12.435  1.00 52.42           O  
HETATM 4361  O   HOH C 313      -6.425  41.013  13.625  1.00 41.46           O  
HETATM 4362  O   HOH C 314     -14.326  51.515  20.967  1.00 25.19           O  
HETATM 4363  O   HOH C 315      -1.457  54.789  -1.696  1.00 54.36           O  
HETATM 4364  O   HOH C 316     -24.997  39.411  31.241  1.00 13.16           O  
HETATM 4365  O   HOH C 317     -11.399  41.520   2.126  1.00 45.34           O  
HETATM 4366  O   HOH C 318     -13.139  51.923   8.839  1.00 23.27           O  
HETATM 4367  O   HOH C 319     -13.970  44.093  30.750  1.00 17.23           O  
HETATM 4368  O   HOH C 320      -9.600  27.480  21.802  1.00 26.43           O  
HETATM 4369  O   HOH C 321     -26.550  46.260   5.193  1.00 32.16           O  
HETATM 4370  O   HOH C 322      -5.900  47.984  18.100  1.00 32.57           O  
HETATM 4371  O   HOH C 323     -14.759  39.349   4.046  1.00 22.35           O  
HETATM 4372  O   HOH C 324     -18.618  52.184  14.175  1.00 21.15           O  
HETATM 4373  O   HOH C 325     -10.274  26.452  23.793  1.00 22.99           O  
HETATM 4374  O   HOH C 326     -18.972  32.055  12.788  1.00 14.36           O  
HETATM 4375  O   HOH C 327     -19.355  33.060  19.653  1.00 12.46           O  
HETATM 4376  O   HOH C 328     -25.001  38.636  19.328  1.00 15.67           O  
HETATM 4377  O   HOH C 329     -26.350  39.045  15.456  1.00 12.72           O  
HETATM 4378  O   HOH C 330     -17.165  32.954  29.991  1.00 11.91           O  
HETATM 4379  O   HOH C 331       2.612  52.327   1.410  1.00 52.67           O  
HETATM 4380  O   HOH C 332       2.424  47.436   2.187  1.00 39.36           O  
HETATM 4381  O   HOH C 333     -21.576  52.461  10.625  1.00 25.91           O  
HETATM 4382  O   HOH C 334     -10.157  42.977  29.079  1.00 31.23           O  
HETATM 4383  O   HOH C 335     -25.801  32.879  21.350  1.00 19.16           O  
HETATM 4384  O   HOH C 336     -24.090  34.745  20.403  1.00 11.64           O  
HETATM 4385  O   HOH C 337     -12.538  34.232  33.089  1.00 30.29           O  
HETATM 4386  O   HOH C 338      -7.516  45.263   4.091  1.00 32.10           O  
HETATM 4387  O   HOH C 339     -20.995  33.786   6.597  1.00 25.86           O  
HETATM 4388  O   HOH C 340     -26.181  53.381  15.845  1.00 54.75           O  
HETATM 4389  O   HOH C 341     -24.695  44.096  23.770  1.00 35.99           O  
HETATM 4390  O   HOH C 342     -10.342  35.225  20.482  1.00  9.83           O  
HETATM 4391  O   HOH C 343     -11.355  31.624  30.753  1.00 26.20           O  
HETATM 4392  O   HOH C 344      -2.764  41.385  24.162  1.00 52.63           O  
HETATM 4393  O   HOH C 345     -18.566  42.452   3.570  1.00 17.23           O  
HETATM 4394  O   HOH C 346     -14.444  24.036  18.041  1.00 27.03           O  
HETATM 4395  O   HOH C 347     -28.010  48.947   7.871  1.00 38.78           O  
HETATM 4396  O   HOH C 348     -18.717  28.873  10.546  1.00 28.93           O  
HETATM 4397  O   HOH C 349       1.923  44.988  -2.962  1.00 33.25           O  
HETATM 4398  O   HOH C 350     -12.769  37.667  12.587  1.00 12.30           O  
HETATM 4399  O   HOH C 351     -20.920  47.507  -1.281  1.00 25.94           O  
HETATM 4400  O   HOH C 352     -10.433  25.534  12.760  1.00 29.33           O  
HETATM 4401  O   HOH C 353     -23.825  43.715  20.693  1.00 11.68           O  
HETATM 4402  O   HOH C 354       2.141  54.270  -6.214  1.00 38.47           O  
HETATM 4403  O   HOH C 355     -14.703  52.736  17.648  1.00 34.50           O  
HETATM 4404  O   HOH C 356      -7.792  51.342  12.871  1.00 41.48           O  
HETATM 4405  O   HOH C 357     -25.145  34.867  25.476  1.00 13.25           O  
HETATM 4406  O   HOH C 358     -16.782  33.704  33.576  1.00 20.97           O  
HETATM 4407  O   HOH C 359      -6.283  29.214  22.082  1.00 38.17           O  
HETATM 4408  O   HOH C 360     -11.232  35.132  17.706  1.00 10.50           O  
HETATM 4409  O   HOH C 361     -24.640  41.081  27.290  1.00 21.50           O  
HETATM 4410  O   HOH C 362      -7.399  49.217  14.374  1.00 29.69           O  
HETATM 4411  O   HOH C 363     -18.921  49.875   4.667  1.00 19.86           O  
HETATM 4412  O   HOH C 364      -5.678  32.017  26.165  1.00 22.00           O  
HETATM 4413  O   HOH C 365      -4.333  44.709  25.245  1.00 32.34           O  
HETATM 4414  O   HOH C 366     -10.608  42.672  25.571  1.00 13.99           O  
HETATM 4415  O   HOH C 367     -16.199  46.846  31.279  1.00 17.86           O  
HETATM 4416  O   HOH C 368     -25.118  45.447   3.278  1.00 34.33           O  
HETATM 4417  O   HOH C 369     -15.671  26.111  16.911  1.00 27.01           O  
HETATM 4418  O   HOH C 370     -26.772  40.443  29.346  1.00 17.02           O  
HETATM 4419  O   HOH C 371     -26.221  27.293  24.628  1.00 37.59           O  
HETATM 4420  O   HOH C 372      -8.486  35.133  11.018  1.00 16.79           O  
HETATM 4421  O   HOH C 373     -18.598  49.624  20.490  1.00 15.11           O  
HETATM 4422  O   HOH C 374      -6.969  36.488   2.796  1.00 38.95           O  
HETATM 4423  O   HOH C 375     -15.343  50.385  29.782  1.00 29.12           O  
HETATM 4424  O   HOH C 376     -28.310  49.507  19.965  1.00 27.90           O  
HETATM 4425  O   HOH C 377     -13.643  53.068  15.252  1.00 34.34           O  
HETATM 4426  O   HOH C 378     -25.636  42.640   3.987  1.00 57.52           O  
HETATM 4427  O   HOH C 379     -23.866  32.542  33.921  1.00 34.98           O  
HETATM 4428  O   HOH C 380     -19.937  26.634  15.160  1.00 21.18           O  
HETATM 4429  O   HOH C 381      -7.356  49.681  16.970  1.00 37.78           O  
HETATM 4430  O   HOH C 382     -22.494  31.492  18.972  1.00 12.39           O  
HETATM 4431  O   HOH C 383     -13.223  50.145  -0.031  1.00 44.54           O  
HETATM 4432  O   HOH C 384      -8.482  55.842  20.006  1.00 35.41           O  
HETATM 4433  O   HOH C 385     -30.483  42.376  20.139  1.00 33.93           O  
HETATM 4434  O   HOH C 386     -14.095  50.782   2.199  1.00 31.92           O  
HETATM 4435  O   HOH C 387      -5.238  27.102  17.631  1.00 29.39           O  
HETATM 4436  O   HOH C 388     -15.729  27.455   8.754  1.00 31.13           O  
HETATM 4437  O   HOH C 389      -6.669  37.142  12.332  1.00 20.82           O  
HETATM 4438  O   HOH C 390     -13.350  54.511  27.277  1.00 36.23           O  
HETATM 4439  O   HOH C 391     -26.457  32.319   9.301  1.00 25.52           O  
HETATM 4440  O   HOH C 392     -13.569  41.032  31.669  1.00 28.61           O  
HETATM 4441  O   HOH C 393     -20.858  52.643   3.480  1.00 43.84           O  
HETATM 4442  O   HOH C 394     -23.067  46.243  19.883  1.00 22.27           O  
HETATM 4443  O   HOH C 395     -24.589  47.140   1.298  1.00 39.62           O  
HETATM 4444  O   HOH C 396     -25.286  40.140   3.686  1.00 36.82           O  
HETATM 4445  O   HOH C 397     -19.215  55.173   9.899  1.00 27.48           O  
HETATM 4446  O   HOH C 398     -23.023  29.763  29.921  1.00 34.19           O  
HETATM 4447  O   HOH C 399     -13.594  46.828  -2.702  1.00 49.61           O  
HETATM 4448  O   HOH C 400     -25.168  37.108  17.107  1.00 21.20           O  
HETATM 4449  O   HOH C 401      -4.970  36.054  23.370  1.00 33.57           O  
HETATM 4450  O   HOH C 402     -10.184  39.527   2.545  1.00 44.48           O  
HETATM 4451  O   HOH C 403     -20.893  47.655  17.836  1.00 21.41           O  
HETATM 4452  O   HOH C 404      -0.244  46.347   4.306  1.00 42.19           O  
HETATM 4453  O   HOH C 405     -23.914  24.466  21.190  1.00 42.81           O  
HETATM 4454  O   HOH C 406      -6.754  43.927   6.419  1.00 27.49           O  
HETATM 4455  O   HOH C 407     -28.556  44.435   7.203  1.00 35.46           O  
HETATM 4456  O   HOH C 408     -19.772  45.000  33.586  1.00 30.57           O  
HETATM 4457  O   HOH C 409      -4.732  31.590  23.252  1.00 27.13           O  
HETATM 4458  O   HOH C 410     -31.994  41.668  17.830  1.00 34.77           O  
HETATM 4459  O   HOH C 411     -14.845  35.087   4.297  1.00 28.32           O  
HETATM 4460  O   HOH C 412     -25.690  34.768  32.587  1.00 34.52           O  
HETATM 4461  O   HOH C 413     -18.147  31.583  32.267  1.00 16.95           O  
HETATM 4462  O   HOH C 414     -31.561  47.551  13.746  1.00 45.54           O  
HETATM 4463  O   HOH C 415      -7.528  43.020  13.676  1.00 25.22           O  
HETATM 4464  O   HOH C 416     -10.239  47.405  -2.081  1.00 16.96           O  
HETATM 4465  O   HOH C 417     -14.538  32.753  30.947  1.00 21.86           O  
HETATM 4466  O   HOH C 418     -27.835  39.256   8.113  1.00 45.38           O  
HETATM 4467  O   HOH C 419     -15.795  53.245  14.246  1.00 40.27           O  
HETATM 4468  O   HOH C 420     -24.266  34.007  17.709  1.00 25.02           O  
HETATM 4469  O   HOH C 421     -26.502  36.770   7.795  1.00 40.55           O  
HETATM 4470  O   HOH C 422      -9.191  52.688   7.142  1.00 44.86           O  
HETATM 4471  O   HOH C 423     -20.436  53.964   0.776  1.00 33.64           O  
HETATM 4472  O   HOH C 424     -25.876  43.115  25.660  1.00 46.44           O  
HETATM 4473  O   HOH C 425       5.663  50.858  -1.191  1.00 44.58           O  
HETATM 4474  O   HOH C 426     -21.000  28.137  31.069  1.00 47.31           O  
HETATM 4475  O   HOH C 427      -5.182  42.110  12.127  1.00 42.74           O  
HETATM 4476  O   HOH C 428     -14.460  30.191  32.400  1.00 29.62           O  
HETATM 4477  O   HOH C 429      -4.943  37.109   5.165  1.00 41.33           O  
HETATM 4478  O   HOH C 430      -6.161  34.670  25.471  1.00 35.45           O  
HETATM 4479  O   HOH C 431     -11.564  40.984  30.106  1.00 34.35           O  
HETATM 4480  O   HOH C 432     -26.130  50.682  15.885  1.00 39.53           O  
HETATM 4481  O   HOH C 433     -19.495  47.342  32.122  1.00 31.17           O  
HETATM 4482  O   HOH C 434     -16.854  51.865  21.059  1.00 23.96           O  
HETATM 4483  O   HOH C 435     -11.481  53.062   7.454  1.00 33.49           O  
HETATM 4484  O   HOH C 436     -26.013  37.547  33.156  1.00 20.22           O  
HETATM 4485  O   HOH C 437     -25.400  25.066  22.992  1.00 51.51           O  
HETATM 4486  O   HOH C 438     -15.653  47.629  -3.130  1.00 48.76           O  
HETATM 4487  O   HOH C 439     -11.094  44.161  31.518  1.00 44.18           O  
HETATM 4488  O   HOH C 440      -8.309  52.571   4.536  1.00 50.44           O  
HETATM 4489  O   HOH C 441     -14.634  33.000   3.488  1.00 40.57           O  
HETATM 4490  O   HOH C 442     -14.081  46.038  33.216  1.00 24.61           O  
HETATM 4491  O   HOH C 443     -28.551  42.781  25.126  1.00 34.39           O  
HETATM 4492  O   HOH C 444     -22.042  32.071  36.106  1.00 23.99           O  
HETATM 4493  O   HOH C 445     -21.508  48.865  25.983  1.00 53.09           O  
HETATM 4494  O   HOH C 446     -23.273  47.512  22.344  1.00 36.78           O  
HETATM 4495  O   HOH C 447     -17.024  53.311  18.344  1.00 47.58           O  
HETATM 4496  O   HOH C 448     -20.408  50.654  25.108  1.00 63.92           O  
HETATM 4497  O   HOH C 449      -5.059  44.679 -12.255  1.00 49.68           O  
HETATM 4498  O   HOH C 450     -17.550  48.153  33.212  1.00 29.17           O  
HETATM 4499  O   HOH C 451     -16.022  46.589  35.107  1.00 17.03           O  
HETATM 4500  O   HOH C 452     -20.180  53.923  12.937  1.00 28.36           O  
HETATM 4501  O   HOH C 453     -20.448  49.387  22.872  1.00 31.94           O  
HETATM 4502  O   HOH C 454     -19.294  52.397  16.891  1.00 28.14           O  
HETATM 4503  O   HOH C 455     -30.652  41.101  22.806  1.00 26.85           O  
HETATM 4504  O   HOH C 456     -24.590  21.962  17.626  1.00 43.94           O  
HETATM 4505  O   HOH C 457     -26.834  43.528  -1.487  1.00 46.01           O  
HETATM 4506  O   HOH C 458     -20.275  50.382  18.292  1.00 19.42           O  
HETATM 4507  O   HOH C 459     -22.995  26.620  13.420  1.00 31.05           O  
HETATM 4508  O   HOH C 460     -28.416  38.485  33.938  1.00 45.89           O  
HETATM 4509  O   HOH C 461       1.125  56.005 -14.981  1.00 50.96           O  
HETATM 4510  O   HOH C 462       3.044  54.777 -15.060  1.00 52.15           O  
HETATM 4511  O   HOH D 301     -17.653  24.311 -24.003  1.00 34.84           O  
HETATM 4512  O   HOH D 302      -4.794  46.105  -9.145  1.00 39.64           O  
HETATM 4513  O   HOH D 303     -17.271  32.969   2.691  1.00 30.81           O  
HETATM 4514  O   HOH D 304      -8.773  37.647   1.082  1.00 36.33           O  
HETATM 4515  O   HOH D 305     -14.520  25.006   3.909  1.00 38.50           O  
HETATM 4516  O   HOH D 306     -19.371  23.114 -20.419  1.00 21.10           O  
HETATM 4517  O   HOH D 307      -7.405  13.147  -8.009  1.00 30.39           O  
HETATM 4518  O   HOH D 308     -11.195  43.503 -16.857  1.00 15.97           O  
HETATM 4519  O   HOH D 309     -10.850  32.643 -22.758  1.00 15.67           O  
HETATM 4520  O   HOH D 310     -23.311  40.794  -8.457  1.00 18.89           O  
HETATM 4521  O   HOH D 311     -24.753  25.886 -15.834  1.00 45.71           O  
HETATM 4522  O   HOH D 312      -7.170  41.764 -14.773  1.00 29.90           O  
HETATM 4523  O   HOH D 313      -8.290  20.741  -5.060  1.00 37.14           O  
HETATM 4524  O   HOH D 314     -14.150  48.262  -7.736  1.00 31.65           O  
HETATM 4525  O   HOH D 315     -18.544  34.998  -5.150  1.00 14.52           O  
HETATM 4526  O   HOH D 316     -20.300  38.483 -18.828  1.00 63.54           O  
HETATM 4527  O   HOH D 317     -12.520  19.091 -23.295  1.00 42.63           O  
HETATM 4528  O   HOH D 318      -6.091  16.535 -16.781  1.00 26.67           O  
HETATM 4529  O   HOH D 319     -24.379  38.217   1.648  1.00 27.13           O  
HETATM 4530  O   HOH D 320     -20.001  26.284   0.457  1.00 26.47           O  
HETATM 4531  O   HOH D 321     -20.564  20.823 -20.944  1.00 35.57           O  
HETATM 4532  O   HOH D 322     -22.253  37.776 -17.179  1.00 42.50           O  
HETATM 4533  O   HOH D 323     -15.607  44.830  -6.249  1.00 15.73           O  
HETATM 4534  O   HOH D 324     -19.091  21.614  -5.475  1.00 17.17           O  
HETATM 4535  O   HOH D 325       4.482  -0.543 -22.401  1.00 15.78           O  
HETATM 4536  O   HOH D 326     -12.467  14.767 -19.619  1.00 26.23           O  
HETATM 4537  O   HOH D 327     -23.401  21.929 -20.509  1.00 46.86           O  
HETATM 4538  O   HOH D 328     -10.811  20.781 -20.973  1.00 25.13           O  
HETATM 4539  O   HOH D 329     -21.776  20.472  -1.953  1.00 42.91           O  
HETATM 4540  O   HOH D 330      -1.032   3.893 -18.947  1.00 36.02           O  
HETATM 4541  O   HOH D 331     -20.187  40.092 -20.946  1.00 24.10           O  
HETATM 4542  O   HOH D 332     -10.393  47.368  -7.999  1.00 36.23           O  
HETATM 4543  O   HOH D 333     -16.273  21.171  -5.670  1.00 12.75           O  
HETATM 4544  O   HOH D 334      -2.711  36.481  -4.632  1.00 36.43           O  
HETATM 4545  O   HOH D 335     -17.097  40.127   4.525  1.00 25.36           O  
HETATM 4546  O   HOH D 336      -5.888  33.234   3.224  1.00 15.26           O  
HETATM 4547  O   HOH D 337      -9.279  34.538  -6.246  1.00 10.43           O  
HETATM 4548  O   HOH D 338     -19.060  14.730 -22.975  1.00 42.62           O  
HETATM 4549  O   HOH D 339      -6.505  16.773 -12.944  1.00 20.52           O  
HETATM 4550  O   HOH D 340     -20.997  12.726 -17.932  1.00 44.59           O  
HETATM 4551  O   HOH D 341     -12.699  28.960   4.437  1.00 21.91           O  
HETATM 4552  O   HOH D 342      -6.613  23.787   1.676  1.00 35.95           O  
HETATM 4553  O   HOH D 343      -7.952   9.140 -18.825  1.00 28.42           O  
HETATM 4554  O   HOH D 344     -19.286  28.508  -3.092  1.00 15.22           O  
HETATM 4555  O   HOH D 345      -5.397  26.178  -9.569  1.00 30.05           O  
HETATM 4556  O   HOH D 346     -17.457  18.074 -20.271  1.00 17.05           O  
HETATM 4557  O   HOH D 347     -15.889  26.973 -22.968  1.00 34.68           O  
HETATM 4558  O   HOH D 348       2.882  12.728 -13.049  1.00 46.15           O  
HETATM 4559  O   HOH D 349     -22.979  17.036 -11.766  1.00 36.88           O  
HETATM 4560  O   HOH D 350     -21.254  30.837 -22.501  1.00 22.71           O  
HETATM 4561  O   HOH D 351     -12.489  26.725  -7.502  1.00  9.98           O  
HETATM 4562  O   HOH D 352     -14.481  18.447  -8.004  1.00 12.74           O  
HETATM 4563  O   HOH D 353     -18.199  46.417  -3.186  1.00 28.70           O  
HETATM 4564  O   HOH D 354     -10.519  32.080  -5.749  1.00  9.33           O  
HETATM 4565  O   HOH D 355       6.247   9.715 -13.920  1.00 26.23           O  
HETATM 4566  O   HOH D 356       3.206   6.318 -11.605  1.00 20.51           O  
HETATM 4567  O   HOH D 357     -21.342  34.434 -16.461  1.00 16.45           O  
HETATM 4568  O   HOH D 358      -9.337  15.030 -11.308  1.00 16.68           O  
HETATM 4569  O   HOH D 359     -24.795  30.560 -11.404  1.00 23.14           O  
HETATM 4570  O   HOH D 360     -22.773  35.872  -7.501  1.00 22.93           O  
HETATM 4571  O   HOH D 361      -8.931  25.150  -3.872  1.00 14.84           O  
HETATM 4572  O   HOH D 362     -13.166  43.431 -19.985  1.00 15.59           O  
HETATM 4573  O   HOH D 363     -11.160  29.123 -23.308  1.00 17.91           O  
HETATM 4574  O   HOH D 364     -26.654  37.186 -13.098  1.00 24.76           O  
HETATM 4575  O   HOH D 365      -9.278  23.071   1.907  1.00 27.19           O  
HETATM 4576  O   HOH D 366      -1.423  34.988 -19.797  1.00 54.06           O  
HETATM 4577  O   HOH D 367     -23.124  34.088 -11.593  1.00 17.44           O  
HETATM 4578  O   HOH D 368     -20.241  33.173 -18.610  1.00 17.93           O  
HETATM 4579  O   HOH D 369     -24.714  12.437 -14.396  1.00 31.66           O  
HETATM 4580  O   HOH D 370      -0.098   4.324 -12.107  1.00 31.25           O  
HETATM 4581  O   HOH D 371     -13.591  10.749 -18.699  1.00 25.71           O  
HETATM 4582  O   HOH D 372      -0.966  17.892 -17.905  1.00 43.39           O  
HETATM 4583  O   HOH D 373     -15.316  32.779 -21.410  1.00 11.13           O  
HETATM 4584  O   HOH D 374     -14.819  17.352  -5.648  1.00 33.72           O  
HETATM 4585  O   HOH D 375      -5.028  26.151 -18.156  1.00 19.07           O  
HETATM 4586  O   HOH D 376      -0.486   0.539 -17.395  1.00 40.93           O  
HETATM 4587  O   HOH D 377      -4.685  42.755 -10.094  1.00 31.36           O  
HETATM 4588  O   HOH D 378       7.579  11.593 -14.966  1.00 24.61           O  
HETATM 4589  O   HOH D 379      -8.032  38.350 -14.303  1.00 11.56           O  
HETATM 4590  O   HOH D 380      -9.760  26.690 -26.409  1.00 41.48           O  
HETATM 4591  O   HOH D 381     -11.908  12.743 -17.716  1.00 16.97           O  
HETATM 4592  O   HOH D 382      -1.297  37.356 -14.929  1.00 30.43           O  
HETATM 4593  O   HOH D 383      -5.923  19.255 -11.572  1.00 27.10           O  
HETATM 4594  O   HOH D 384     -23.979  32.430  -9.548  1.00 35.93           O  
HETATM 4595  O   HOH D 385     -10.986  15.657  -9.516  1.00 23.36           O  
HETATM 4596  O   HOH D 386      -7.539  13.827 -22.603  1.00 53.11           O  
HETATM 4597  O   HOH D 387       3.304   9.872 -12.907  1.00 22.28           O  
HETATM 4598  O   HOH D 388      -6.234  26.445 -12.217  1.00 22.58           O  
HETATM 4599  O   HOH D 389     -11.784  12.289 -12.021  1.00 28.77           O  
HETATM 4600  O   HOH D 390      -5.906  23.505  -1.204  1.00 35.02           O  
HETATM 4601  O   HOH D 391      -4.840  28.356 -19.032  1.00 29.66           O  
HETATM 4602  O   HOH D 392     -18.127  30.753 -19.458  1.00 15.32           O  
HETATM 4603  O   HOH D 393      -3.585  29.565 -17.563  1.00 34.00           O  
HETATM 4604  O   HOH D 394     -21.592  16.345  -9.030  1.00 29.86           O  
HETATM 4605  O   HOH D 395     -10.713  26.507 -22.848  1.00 27.44           O  
HETATM 4606  O   HOH D 396     -22.721  33.739  -6.535  1.00 32.76           O  
HETATM 4607  O   HOH D 397     -17.692  25.668   2.455  1.00 28.84           O  
HETATM 4608  O   HOH D 398     -18.053  47.679 -14.470  1.00 24.41           O  
HETATM 4609  O   HOH D 399      -4.808  23.723 -19.437  1.00 40.52           O  
HETATM 4610  O   HOH D 400     -16.169  11.424 -21.256  1.00 38.15           O  
HETATM 4611  O   HOH D 401     -23.587  25.490 -18.919  1.00 39.01           O  
HETATM 4612  O   HOH D 402      -6.502  25.870  -5.604  1.00 17.55           O  
HETATM 4613  O   HOH D 403      -1.133   1.156 -13.860  1.00 46.11           O  
HETATM 4614  O   HOH D 404       6.757   5.901 -24.073  1.00 20.17           O  
HETATM 4615  O   HOH D 405      -4.608  30.389 -25.862  1.00 25.38           O  
HETATM 4616  O   HOH D 406      -5.989  37.336   0.198  1.00 39.84           O  
HETATM 4617  O   HOH D 407      -3.156  22.151 -19.520  1.00 40.89           O  
HETATM 4618  O   HOH D 408       3.103   8.430 -22.564  1.00 37.10           O  
HETATM 4619  O   HOH D 409     -20.743  31.491   1.126  1.00 23.58           O  
HETATM 4620  O   HOH D 410     -21.228  14.609 -21.151  1.00 48.31           O  
HETATM 4621  O   HOH D 411     -11.171  20.659  -5.066  1.00 19.92           O  
HETATM 4622  O   HOH D 412     -14.706  21.873 -25.740  1.00 27.25           O  
HETATM 4623  O   HOH D 413       0.720  16.081 -13.886  1.00 31.97           O  
HETATM 4624  O   HOH D 414     -21.470  45.837  -4.037  1.00 28.75           O  
HETATM 4625  O   HOH D 415      -5.565  10.152 -21.220  1.00 50.08           O  
HETATM 4626  O   HOH D 416      -3.873  15.803 -18.589  1.00 53.01           O  
HETATM 4627  O   HOH D 417     -19.178  24.827 -27.730  1.00 35.30           O  
HETATM 4628  O   HOH D 418      -3.598  37.212  -2.249  1.00 33.08           O  
HETATM 4629  O   HOH D 419      -9.727  45.689  -4.375  1.00 11.63           O  
HETATM 4630  O   HOH D 420     -15.012  49.211 -14.870  1.00 40.42           O  
HETATM 4631  O   HOH D 421      -3.596  37.284  -6.754  1.00 19.60           O  
HETATM 4632  O   HOH D 422      -2.491  32.206  -7.924  1.00 29.53           O  
HETATM 4633  O   HOH D 423     -21.484  18.056  -5.472  1.00 43.57           O  
HETATM 4634  O   HOH D 424       5.619  16.219 -21.081  1.00 42.28           O  
HETATM 4635  O   HOH D 425      -5.073  35.943 -23.827  1.00 41.86           O  
HETATM 4636  O   HOH D 426     -13.287  11.285 -10.929  0.17 47.91           O  
HETATM 4637  O   HOH D 427     -10.018  29.862 -25.473  1.00 34.40           O  
HETATM 4638  O   HOH D 428     -16.463  47.554  -5.742  1.00 32.90           O  
HETATM 4639  O   HOH D 429     -12.620  45.452  -5.620  1.00 27.76           O  
HETATM 4640  O   HOH D 430     -23.602  23.461  -6.551  1.00 26.83           O  
HETATM 4641  O   HOH D 431     -25.475  33.418 -22.799  1.00 37.27           O  
HETATM 4642  O   HOH D 432      -9.377  12.603 -18.463  1.00 22.29           O  
HETATM 4643  O   HOH D 433      -6.513  43.611 -17.246  1.00 45.90           O  
HETATM 4644  O   HOH D 434     -24.831  39.850  -6.547  1.00 34.53           O  
HETATM 4645  O   HOH D 435      -3.905  40.174  -3.292  1.00 36.84           O  
HETATM 4646  O   HOH D 436     -21.021  28.787  -0.134  1.00 36.12           O  
HETATM 4647  O   HOH D 437      -6.209  16.484 -19.553  1.00 35.90           O  
HETATM 4648  O   HOH D 438      -2.553  27.433 -18.287  1.00 51.59           O  
HETATM 4649  O   HOH D 439       4.762   7.909 -24.415  1.00 41.68           O  
HETATM 4650  O   HOH D 440     -12.672  31.736   4.057  1.00 34.83           O  
HETATM 4651  O   HOH D 441      -5.401  11.961  -7.520  1.00 34.52           O  
HETATM 4652  O   HOH D 442      -8.251  14.597 -20.171  1.00 24.66           O  
HETATM 4653  O   HOH D 443     -14.566  27.324   4.269  1.00 28.97           O  
HETATM 4654  O   HOH D 444     -10.887  14.961 -23.273  1.00 42.21           O  
HETATM 4655  O   HOH D 445     -15.541  43.910 -21.005  1.00 23.39           O  
HETATM 4656  O   HOH D 446     -22.897  32.903 -23.292  1.00 41.71           O  
HETATM 4657  O   HOH D 447      -2.010  42.029 -12.635  1.00 41.71           O  
HETATM 4658  O   HOH D 448     -15.303  19.233  -3.953  1.00 24.16           O  
HETATM 4659  O   HOH D 449      -2.477  17.319 -20.277  1.00 47.74           O  
HETATM 4660  O   HOH D 450      -9.719  18.539 -21.752  1.00 30.67           O  
HETATM 4661  O   HOH D 451      -5.332  25.112  -7.462  1.00 39.77           O  
HETATM 4662  O   HOH D 452     -19.714  12.982 -19.798  1.00 57.74           O  
HETATM 4663  O   HOH D 453     -23.337  28.798 -22.754  1.00 38.61           O  
HETATM 4664  O   HOH D 454     -21.299  21.662  -7.376  1.00 29.54           O  
HETATM 4665  O   HOH D 455     -28.050  37.418 -15.315  1.00 41.85           O  
HETATM 4666  O   HOH D 456     -10.559  15.741 -21.043  1.00 30.87           O  
HETATM 4667  O   HOH D 457      -9.770  44.292 -14.965  1.00 65.17           O  
HETATM 4668  O   HOH D 458     -26.009  40.881  -1.415  1.00 33.14           O  
HETATM 4669  O   HOH D 459     -18.319  30.690   2.849  1.00 22.45           O  
HETATM 4670  O   HOH D 460      -8.173  43.355 -13.691  1.00 45.64           O  
HETATM 4671  O   HOH D 461      -7.065  18.799 -20.773  1.00 35.56           O  
HETATM 4672  O   HOH D 462     -16.609  50.179  -4.604  1.00 54.42           O  
HETATM 4673  O   HOH D 463     -15.702  46.788 -21.147  1.00 37.54           O  
HETATM 4674  O   HOH D 464     -22.356  18.842  -7.463  1.00 44.98           O  
HETATM 4675  O   HOH D 465     -15.398   8.897 -21.213  1.00 30.61           O  
HETATM 4676  O   HOH D 466      -3.827  23.913  -2.047  1.00 55.10           O  
HETATM 4677  O   HOH D 467      -9.378  22.429  -3.124  1.00 17.61           O  
HETATM 4678  O   HOH D 468     -10.099  45.657 -18.362  1.00 29.74           O  
HETATM 4679  O   HOH D 469     -18.714  11.924 -21.767  1.00 45.57           O  
HETATM 4680  O   HOH D 470     -20.072  19.628  -3.625  1.00 29.79           O  
HETATM 4681  O   HOH D 471     -10.172  49.452  -9.596  1.00 43.15           O  
HETATM 4682  O   HOH D 472      -1.946  35.561 -21.987  1.00 48.23           O  
HETATM 4683  O   HOH D 473     -18.017  42.478 -19.850  1.00 37.13           O  
HETATM 4684  O   HOH D 474      -9.695  21.525  -0.671  1.00 27.56           O  
HETATM 4685  O   HOH D 475      -7.875  45.662 -17.406  1.00 43.04           O  
HETATM 4686  O   HOH D 476     -17.394  28.222   3.874  1.00 21.40           O  
HETATM 4687  O   HOH D 477     -12.041  19.936  -0.215  1.00 39.99           O  
CONECT   82 3971                                                                
CONECT  264 3969                                                                
CONECT  768 3969                                                                
CONECT 1061 3990                                                                
CONECT 1245 3971                                                                
CONECT 1749 3971                                                                
CONECT 2046 4011                                                                
CONECT 2228 3990                                                                
CONECT 2739 3990                                                                
CONECT 3046 3969                                                                
CONECT 3231 4011                                                                
CONECT 3735 4011                                                                
CONECT 3944 3945 3949                                                           
CONECT 3945 3944 3946                                                           
CONECT 3946 3945 3947                                                           
CONECT 3947 3946 3948 3950                                                      
CONECT 3948 3947 3949                                                           
CONECT 3949 3944 3948                                                           
CONECT 3950 3947 3951                                                           
CONECT 3951 3950 3952                                                           
CONECT 3952 3951 3953 3954 3955                                                 
CONECT 3953 3952                                                                
CONECT 3954 3952                                                                
CONECT 3955 3952                                                                
CONECT 3957 3958 3962                                                           
CONECT 3958 3957 3959                                                           
CONECT 3959 3958 3960                                                           
CONECT 3960 3959 3961 3963                                                      
CONECT 3961 3960 3962                                                           
CONECT 3962 3957 3961                                                           
CONECT 3963 3960 3964                                                           
CONECT 3964 3963 3965                                                           
CONECT 3965 3964 3966 3967 3968                                                 
CONECT 3966 3965                                                                
CONECT 3967 3965                                                                
CONECT 3968 3965                                                                
CONECT 3969  264  768 3046                                                      
CONECT 3971   82 1245 1749                                                      
CONECT 3972 3973 3974                                                           
CONECT 3973 3972                                                                
CONECT 3974 3972 3975 3976                                                      
CONECT 3975 3974                                                                
CONECT 3976 3974 3977                                                           
CONECT 3977 3976                                                                
CONECT 3978 3979 3983                                                           
CONECT 3979 3978 3980                                                           
CONECT 3980 3979 3981                                                           
CONECT 3981 3980 3982 3984                                                      
CONECT 3982 3981 3983                                                           
CONECT 3983 3978 3982                                                           
CONECT 3984 3981 3985                                                           
CONECT 3985 3984 3986                                                           
CONECT 3986 3985 3987 3988 3989                                                 
CONECT 3987 3986                                                                
CONECT 3988 3986                                                                
CONECT 3989 3986                                                                
CONECT 3990 1061 2228 2739                                                      
CONECT 3993 3994 3995                                                           
CONECT 3994 3993                                                                
CONECT 3995 3993 3996 3997                                                      
CONECT 3996 3995                                                                
CONECT 3997 3995 3998                                                           
CONECT 3998 3997                                                                
CONECT 3999 4000 4004                                                           
CONECT 4000 3999 4001                                                           
CONECT 4001 4000 4002                                                           
CONECT 4002 4001 4003 4005                                                      
CONECT 4003 4002 4004                                                           
CONECT 4004 3999 4003                                                           
CONECT 4005 4002 4006                                                           
CONECT 4006 4005 4007                                                           
CONECT 4007 4006 4008 4009 4010                                                 
CONECT 4008 4007                                                                
CONECT 4009 4007                                                                
CONECT 4010 4007                                                                
CONECT 4011 2046 3231 3735                                                      
CONECT 4012 4013 4014                                                           
CONECT 4013 4012                                                                
CONECT 4014 4012 4015 4016                                                      
CONECT 4015 4014                                                                
CONECT 4016 4014 4017                                                           
CONECT 4017 4016                                                                
CONECT 4018 4019 4020                                                           
CONECT 4019 4018                                                                
CONECT 4020 4018 4021 4022                                                      
CONECT 4021 4020                                                                
CONECT 4022 4020 4023                                                           
CONECT 4023 4022                                                                
MASTER      382    0   16    4   26    0   29    6 4628    4   88   40          
END                                                                             
HEADER    VIRUS                                   09-MAR-20   6W37              
TITLE     STRUCTURE OF THE SARS-COV-2 ORF7A ENCODED ACCESSORY PROTEIN           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN 7A;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: H-2KB RESIDUES 1-277;                                      
COMPND   5 SYNONYM: SARS-COV-2 ACCESSORY PROTEIN 7A,PROTEIN U122,PROTEIN X4;    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: ECTODOMAIN, THE FIRST AND LAST RESIDUE WERE DISORDERED
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 GENE: 7A;                                                            
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: RIL;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET21                                     
KEYWDS    VIRAL PROTEIN, STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF 
KEYWDS   2 INFECTIOUS DISEASES, CSGID, VIRUS                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.A.NELSON,G.MINASOV,L.SHUVALOVA,D.H.FREMONT,CENTER FOR STRUCTURAL    
AUTHOR   2 GENOMICS OF INFECTIOUS DISEASES (CSGID)                              
REVDAT   3   20-MAY-20 6W37    1       AUTHOR JRNL                              
REVDAT   2   06-MAY-20 6W37    1       COMPND SOURCE DBREF                      
REVDAT   1   29-APR-20 6W37    0                                                
JRNL        AUTH   C.A.NELSON,G.MINASOV,L.SHUVALOVA,D.H.FREMONT                 
JRNL        TITL   STRUCTURE OF THE SARS-COV-2 ORF7A ENCODED ACCESSORY PROTEIN  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.17.1_3660                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.15                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 2541                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.255                           
REMARK   3   R VALUE            (WORKING SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.310                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 262                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.1500 -  2.9000    1.00     2541     0  0.0000 0.0000        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: 0.4800                                                   
REMARK   3   OPERATOR: -H,-K,L                                                  
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.001            537                                  
REMARK   3   ANGLE     :  0.413            728                                  
REMARK   3   CHIRALITY :  0.039             77                                  
REMARK   3   PLANARITY :  0.002             95                                  
REMARK   3   DIHEDRAL  :  7.638            191                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6W37 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000247519.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-FEB-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97857                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.7.4                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 2553                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.150                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.900                              
REMARK 200  R MERGE                    (I) : 0.24900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.70                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.04200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.8.3                                          
REMARK 200 STARTING MODEL: 1XAK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: LONG THIN NEEDLES.                                           
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.2 M CACL2, 0.1M TRIS     
REMARK 280  -HCL PH8.5, PH 5.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       18.63933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       37.27867            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       37.27867            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       18.63933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     VAL A    67                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A   6      143.25   -170.22                                   
REMARK 500    SER A  22      -86.92   -103.16                                   
REMARK 500    PHE A  44      135.11   -174.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1XAK   RELATED DB: PDB                                   
REMARK 900 SARS-COV ORF7A                                                       
REMARK 900 RELATED ID: IDP51001   RELATED DB: TARGETTRACK                       
REMARK 900 CSGID DATABASE                                                       
REMARK 900 RELATED ID: 1YO4   RELATED DB: PDB                                   
REMARK 900 SARS-COV ORF7A                                                       
DBREF  6W37 A    1    67  UNP    P0DTC7   NS7A_SARS2      16     82             
SEQRES   1 A   67  GLU LEU TYR HIS TYR GLN GLU CYS VAL ARG GLY THR THR          
SEQRES   2 A   67  VAL LEU LEU LYS GLU PRO CYS SER SER GLY THR TYR GLU          
SEQRES   3 A   67  GLY ASN SER PRO PHE HIS PRO LEU ALA ASP ASN LYS PHE          
SEQRES   4 A   67  ALA LEU THR CYS PHE SER THR GLN PHE ALA PHE ALA CYS          
SEQRES   5 A   67  PRO ASP GLY VAL LYS HIS VAL TYR GLN LEU ARG ALA ARG          
SEQRES   6 A   67  SER VAL                                                      
FORMUL   2  HOH   *3(H2 O)                                                      
SHEET    1 AA1 4 GLN A   6  VAL A   9  0                                        
SHEET    2 AA1 4 LYS A  57  ARG A  65  1  O  ARG A  63   N  CYS A   8           
SHEET    3 AA1 4 THR A  46  ALA A  51 -1  N  PHE A  48   O  TYR A  60           
SHEET    4 AA1 4 THR A  24  GLU A  26 -1  N  THR A  24   O  ALA A  51           
SHEET    1 AA2 3 THR A  13  LYS A  17  0                                        
SHEET    2 AA2 3 LYS A  38  THR A  42 -1  O  PHE A  39   N  LEU A  16           
SHEET    3 AA2 3 HIS A  32  LEU A  34 -1  N  LEU A  34   O  LYS A  38           
SSBOND   1 CYS A    8    CYS A   43                          1555   1555  2.03  
SSBOND   2 CYS A   20    CYS A   52                          1555   1555  2.03  
CRYST1   57.393   57.393   55.918  90.00  90.00 120.00 P 31 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017424  0.010060  0.000000        0.00000                         
SCALE2      0.000000  0.020119  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017883        0.00000                         
ATOM      1  N   GLU A   1     -35.002  23.721  10.106  1.00 31.16           N  
ATOM      2  CA  GLU A   1     -34.808  22.363  10.600  1.00 38.49           C  
ATOM      3  C   GLU A   1     -34.161  21.487   9.532  1.00 33.79           C  
ATOM      4  O   GLU A   1     -34.848  20.775   8.799  1.00 30.23           O  
ATOM      5  CB  GLU A   1     -36.142  21.759  11.042  1.00 35.36           C  
ATOM      6  CG  GLU A   1     -36.798  22.497  12.198  1.00 51.28           C  
ATOM      7  CD  GLU A   1     -38.121  21.881  12.609  1.00 45.59           C  
ATOM      8  OE1 GLU A   1     -38.662  21.061  11.838  1.00 45.91           O  
ATOM      9  OE2 GLU A   1     -38.618  22.216  13.705  1.00 66.17           O1-
ATOM     10  N   LEU A   2     -32.834  21.542   9.452  1.00 25.08           N  
ATOM     11  CA  LEU A   2     -32.081  20.794   8.453  1.00 28.95           C  
ATOM     12  C   LEU A   2     -31.782  19.399   8.990  1.00 29.65           C  
ATOM     13  O   LEU A   2     -31.148  19.255  10.040  1.00 39.99           O  
ATOM     14  CB  LEU A   2     -30.788  21.526   8.099  1.00 30.68           C  
ATOM     15  CG  LEU A   2     -30.950  23.002   7.727  1.00 38.41           C  
ATOM     16  CD1 LEU A   2     -29.599  23.636   7.434  1.00 29.08           C  
ATOM     17  CD2 LEU A   2     -31.890  23.165   6.542  1.00 53.76           C  
ATOM     18  N   TYR A   3     -32.234  18.379   8.268  1.00 28.35           N  
ATOM     19  CA  TYR A   3     -32.049  16.997   8.681  1.00 28.12           C  
ATOM     20  C   TYR A   3     -30.782  16.417   8.064  1.00 32.27           C  
ATOM     21  O   TYR A   3     -30.323  16.858   7.007  1.00 28.31           O  
ATOM     22  CB  TYR A   3     -33.256  16.149   8.277  1.00 31.24           C  
ATOM     23  CG  TYR A   3     -34.566  16.633   8.857  1.00 36.67           C  
ATOM     24  CD1 TYR A   3     -35.121  16.025   9.974  1.00 27.41           C  
ATOM     25  CD2 TYR A   3     -35.246  17.701   8.287  1.00 49.25           C  
ATOM     26  CE1 TYR A   3     -36.318  16.464  10.506  1.00 36.03           C  
ATOM     27  CE2 TYR A   3     -36.443  18.148   8.813  1.00 47.08           C  
ATOM     28  CZ  TYR A   3     -36.974  17.527   9.922  1.00 34.98           C  
ATOM     29  OH  TYR A   3     -38.166  17.970  10.447  1.00 35.89           O  
ATOM     30  N   HIS A   4     -30.219  15.420   8.743  1.00 27.80           N  
ATOM     31  CA  HIS A   4     -29.024  14.732   8.281  1.00 19.35           C  
ATOM     32  C   HIS A   4     -29.259  13.228   8.327  1.00 26.14           C  
ATOM     33  O   HIS A   4     -30.118  12.733   9.061  1.00 27.94           O  
ATOM     34  CB  HIS A   4     -27.794  15.090   9.130  1.00 15.38           C  
ATOM     35  CG  HIS A   4     -27.427  16.541   9.088  1.00 20.19           C  
ATOM     36  ND1 HIS A   4     -26.191  16.983   8.669  1.00 18.69           N  
ATOM     37  CD2 HIS A   4     -28.132  17.650   9.415  1.00 23.59           C  
ATOM     38  CE1 HIS A   4     -26.150  18.301   8.738  1.00 19.88           C  
ATOM     39  NE2 HIS A   4     -27.315  18.731   9.188  1.00 24.85           N  
ATOM     40  N   TYR A   5     -28.477  12.504   7.529  1.00 38.79           N  
ATOM     41  CA  TYR A   5     -28.554  11.052   7.486  1.00 27.99           C  
ATOM     42  C   TYR A   5     -27.200  10.510   7.057  1.00 25.23           C  
ATOM     43  O   TYR A   5     -26.478  11.146   6.284  1.00 22.78           O  
ATOM     44  CB  TYR A   5     -29.652  10.570   6.529  1.00 24.87           C  
ATOM     45  CG  TYR A   5     -29.814   9.065   6.476  1.00 30.43           C  
ATOM     46  CD1 TYR A   5     -29.040   8.292   5.619  1.00 28.55           C  
ATOM     47  CD2 TYR A   5     -30.744   8.419   7.279  1.00 32.46           C  
ATOM     48  CE1 TYR A   5     -29.185   6.919   5.568  1.00 36.68           C  
ATOM     49  CE2 TYR A   5     -30.896   7.046   7.234  1.00 31.65           C  
ATOM     50  CZ  TYR A   5     -30.115   6.301   6.377  1.00 34.48           C  
ATOM     51  OH  TYR A   5     -30.263   4.934   6.328  1.00 44.33           O  
ATOM     52  N   GLN A   6     -26.861   9.328   7.567  1.00 34.47           N  
ATOM     53  CA  GLN A   6     -25.574   8.717   7.271  1.00 33.16           C  
ATOM     54  C   GLN A   6     -25.574   7.287   7.787  1.00 34.04           C  
ATOM     55  O   GLN A   6     -26.147   7.003   8.843  1.00 33.71           O  
ATOM     56  CB  GLN A   6     -24.427   9.516   7.907  1.00 34.50           C  
ATOM     57  CG  GLN A   6     -23.051   8.884   7.750  1.00 52.88           C  
ATOM     58  CD  GLN A   6     -21.949   9.748   8.334  1.00 54.62           C  
ATOM     59  OE1 GLN A   6     -22.196  10.869   8.779  1.00 32.80           O  
ATOM     60  NE2 GLN A   6     -20.726   9.230   8.336  1.00 45.23           N  
ATOM     61  N   GLU A   7     -24.930   6.398   7.036  1.00 34.16           N  
ATOM     62  CA  GLU A   7     -24.786   5.000   7.412  1.00 35.09           C  
ATOM     63  C   GLU A   7     -23.351   4.723   7.838  1.00 45.21           C  
ATOM     64  O   GLU A   7     -22.400   5.145   7.170  1.00 41.88           O  
ATOM     65  CB  GLU A   7     -25.170   4.072   6.259  1.00 36.68           C  
ATOM     66  CG  GLU A   7     -26.594   4.253   5.768  1.00 51.43           C  
ATOM     67  CD  GLU A   7     -27.027   3.157   4.813  1.00 55.52           C  
ATOM     68  OE1 GLU A   7     -26.202   2.269   4.512  1.00 39.63           O  
ATOM     69  OE2 GLU A   7     -28.193   3.183   4.367  1.00 65.11           O1-
ATOM     70  N   CYS A   8     -23.203   4.007   8.949  1.00 44.23           N  
ATOM     71  CA  CYS A   8     -21.892   3.692   9.496  1.00 33.22           C  
ATOM     72  C   CYS A   8     -21.856   2.230   9.914  1.00 36.82           C  
ATOM     73  O   CYS A   8     -22.893   1.593  10.116  1.00 32.94           O  
ATOM     74  CB  CYS A   8     -21.549   4.593  10.692  1.00 49.21           C  
ATOM     75  SG  CYS A   8     -22.763   4.563  12.032  1.00 44.42           S  
ATOM     76  N   VAL A   9     -20.639   1.709  10.052  1.00 26.95           N  
ATOM     77  CA  VAL A   9     -20.433   0.324  10.458  1.00 32.79           C  
ATOM     78  C   VAL A   9     -20.492   0.232  11.976  1.00 39.33           C  
ATOM     79  O   VAL A   9     -19.955   1.090  12.688  1.00 35.69           O  
ATOM     80  CB  VAL A   9     -19.091  -0.203   9.918  1.00 29.77           C  
ATOM     81  CG1 VAL A   9     -18.950  -1.691  10.204  1.00 29.92           C  
ATOM     82  CG2 VAL A   9     -18.969   0.076   8.428  1.00 31.87           C  
ATOM     83  N   ARG A  10     -21.145  -0.815  12.477  1.00 35.01           N  
ATOM     84  CA  ARG A  10     -21.294  -0.987  13.917  1.00 33.43           C  
ATOM     85  C   ARG A  10     -19.932  -1.016  14.598  1.00 35.84           C  
ATOM     86  O   ARG A  10     -19.007  -1.694  14.141  1.00 33.69           O  
ATOM     87  CB  ARG A  10     -22.060  -2.276  14.218  1.00 37.86           C  
ATOM     88  CG  ARG A  10     -23.500  -2.273  13.733  1.00 48.77           C  
ATOM     89  CD  ARG A  10     -24.249  -3.514  14.190  1.00 33.84           C  
ATOM     90  NE  ARG A  10     -25.575  -3.610  13.583  1.00 24.35           N  
ATOM     91  CZ  ARG A  10     -26.639  -2.918  13.982  1.00 18.91           C  
ATOM     92  NH1 ARG A  10     -26.551  -2.064  14.994  1.00 43.51           N  
ATOM     93  NH2 ARG A  10     -27.800  -3.080  13.362  1.00 23.67           N  
ATOM     94  N   GLY A  11     -19.813  -0.275  15.694  1.00 55.52           N  
ATOM     95  CA  GLY A  11     -18.600  -0.239  16.495  1.00 59.77           C  
ATOM     96  C   GLY A  11     -17.596   0.817  16.085  1.00 54.98           C  
ATOM     97  O   GLY A  11     -17.025   1.496  16.941  1.00 71.18           O  
ATOM     98  N   THR A  12     -17.368   0.968  14.783  1.00 48.29           N  
ATOM     99  CA  THR A  12     -16.383   1.928  14.305  1.00 48.71           C  
ATOM    100  C   THR A  12     -16.783   3.345  14.696  1.00 40.84           C  
ATOM    101  O   THR A  12     -17.967   3.690  14.723  1.00 39.83           O  
ATOM    102  CB  THR A  12     -16.235   1.826  12.787  1.00 63.95           C  
ATOM    103  OG1 THR A  12     -17.498   2.082  12.161  1.00 42.24           O  
ATOM    104  CG2 THR A  12     -15.744   0.439  12.388  1.00 50.24           C  
ATOM    105  N   THR A  13     -15.782   4.164  15.005  1.00 40.95           N  
ATOM    106  CA  THR A  13     -16.028   5.549  15.373  1.00 41.94           C  
ATOM    107  C   THR A  13     -16.453   6.355  14.148  1.00 47.33           C  
ATOM    108  O   THR A  13     -16.211   5.969  13.001  1.00 63.22           O  
ATOM    109  CB  THR A  13     -14.775   6.165  15.999  1.00 51.58           C  
ATOM    110  OG1 THR A  13     -14.245   5.273  16.989  1.00 58.38           O  
ATOM    111  CG2 THR A  13     -15.095   7.502  16.653  1.00 39.75           C  
ATOM    112  N   VAL A  14     -17.099   7.492  14.404  1.00 52.39           N  
ATOM    113  CA  VAL A  14     -17.555   8.388  13.349  1.00 52.73           C  
ATOM    114  C   VAL A  14     -17.292   9.815  13.808  1.00 40.07           C  
ATOM    115  O   VAL A  14     -17.784  10.230  14.864  1.00 42.11           O  
ATOM    116  CB  VAL A  14     -19.048   8.197  13.027  1.00 36.55           C  
ATOM    117  CG1 VAL A  14     -19.470   9.114  11.886  1.00 43.43           C  
ATOM    118  CG2 VAL A  14     -19.339   6.743  12.687  1.00 35.73           C  
ATOM    119  N   LEU A  15     -16.508  10.554  13.028  1.00 34.43           N  
ATOM    120  CA  LEU A  15     -16.244  11.964  13.275  1.00 41.42           C  
ATOM    121  C   LEU A  15     -17.067  12.804  12.307  1.00 39.05           C  
ATOM    122  O   LEU A  15     -17.227  12.441  11.138  1.00 71.88           O  
ATOM    123  CB  LEU A  15     -14.757  12.286  13.106  1.00 36.97           C  
ATOM    124  CG  LEU A  15     -13.792  11.752  14.169  1.00 53.94           C  
ATOM    125  CD1 LEU A  15     -13.766  10.231  14.189  1.00 46.05           C  
ATOM    126  CD2 LEU A  15     -12.393  12.307  13.942  1.00 45.03           C  
ATOM    127  N   LEU A  16     -17.585  13.929  12.797  1.00 31.17           N  
ATOM    128  CA  LEU A  16     -18.436  14.792  11.993  1.00 36.73           C  
ATOM    129  C   LEU A  16     -18.136  16.247  12.320  1.00 33.43           C  
ATOM    130  O   LEU A  16     -17.582  16.572  13.375  1.00 47.28           O  
ATOM    131  CB  LEU A  16     -19.922  14.492  12.229  1.00 43.84           C  
ATOM    132  CG  LEU A  16     -20.378  13.063  11.922  1.00 36.74           C  
ATOM    133  CD1 LEU A  16     -21.799  12.843  12.413  1.00 32.05           C  
ATOM    134  CD2 LEU A  16     -20.276  12.765  10.433  1.00 44.63           C  
ATOM    135  N   LYS A  17     -18.512  17.122  11.392  1.00 39.80           N  
ATOM    136  CA  LYS A  17     -18.315  18.555  11.546  1.00 48.68           C  
ATOM    137  C   LYS A  17     -19.476  19.159  12.324  1.00 42.24           C  
ATOM    138  O   LYS A  17     -20.625  18.728  12.185  1.00 50.57           O  
ATOM    139  CB  LYS A  17     -18.195  19.228  10.176  1.00 47.99           C  
ATOM    140  CG  LYS A  17     -17.874  20.716  10.224  1.00 41.86           C  
ATOM    141  CD  LYS A  17     -16.445  20.968  10.677  1.00 48.56           C  
ATOM    142  CE  LYS A  17     -16.157  22.456  10.801  1.00 61.08           C  
ATOM    143  NZ  LYS A  17     -14.740  22.723  11.174  1.00 47.97           N  
ATOM    144  N   GLU A  18     -19.171  20.157  13.140  1.00 60.85           N  
ATOM    145  CA  GLU A  18     -20.207  20.827  13.914  1.00 61.04           C  
ATOM    146  C   GLU A  18     -21.027  21.730  12.998  1.00 32.95           C  
ATOM    147  O   GLU A  18     -20.452  22.492  12.214  1.00 35.94           O  
ATOM    148  CB  GLU A  18     -19.587  21.647  15.043  1.00 52.92           C  
ATOM    149  CG  GLU A  18     -18.830  20.822  16.069  1.00 42.02           C  
ATOM    150  CD  GLU A  18     -18.228  21.674  17.170  1.00 53.13           C  
ATOM    151  OE1 GLU A  18     -18.404  22.910  17.130  1.00 55.47           O  
ATOM    152  OE2 GLU A  18     -17.579  21.108  18.074  1.00 47.76           O1-
ATOM    153  N   PRO A  19     -22.362  21.680  13.061  1.00 29.71           N  
ATOM    154  CA  PRO A  19     -23.160  22.587  12.222  1.00 29.52           C  
ATOM    155  C   PRO A  19     -23.037  24.044  12.629  1.00 29.46           C  
ATOM    156  O   PRO A  19     -23.361  24.924  11.822  1.00 30.45           O  
ATOM    157  CB  PRO A  19     -24.593  22.071  12.405  1.00 27.55           C  
ATOM    158  CG  PRO A  19     -24.585  21.405  13.734  1.00 41.38           C  
ATOM    159  CD  PRO A  19     -23.210  20.822  13.909  1.00 42.01           C  
ATOM    160  N   CYS A  20     -22.584  24.325  13.848  1.00 45.28           N  
ATOM    161  CA  CYS A  20     -22.340  25.691  14.287  1.00 56.04           C  
ATOM    162  C   CYS A  20     -21.210  25.679  15.306  1.00 41.46           C  
ATOM    163  O   CYS A  20     -20.757  24.622  15.753  1.00 35.57           O  
ATOM    164  CB  CYS A  20     -23.601  26.330  14.877  1.00 45.60           C  
ATOM    165  SG  CYS A  20     -24.547  25.260  15.981  1.00 44.35           S  
ATOM    166  N   SER A  21     -20.755  26.877  15.670  1.00 35.19           N  
ATOM    167  CA  SER A  21     -19.642  27.024  16.598  1.00 46.54           C  
ATOM    168  C   SER A  21     -19.962  26.386  17.945  1.00 44.57           C  
ATOM    169  O   SER A  21     -19.336  25.393  18.329  1.00 35.44           O  
ATOM    170  CB  SER A  21     -19.295  28.503  16.779  1.00 50.71           C  
ATOM    171  OG  SER A  21     -20.425  29.245  17.204  1.00 60.93           O  
ATOM    172  N   SER A  22     -20.932  26.947  18.666  1.00 35.35           N  
ATOM    173  CA  SER A  22     -21.295  26.437  19.983  1.00 32.62           C  
ATOM    174  C   SER A  22     -22.584  25.627  19.912  1.00 38.68           C  
ATOM    175  O   SER A  22     -22.544  24.403  19.750  1.00 33.37           O  
ATOM    176  CB  SER A  22     -21.441  27.590  20.979  1.00 40.07           C  
ATOM    177  OG  SER A  22     -22.455  28.492  20.570  1.00 41.24           O  
ATOM    178  N   GLY A  23     -23.729  26.296  20.028  1.00 26.21           N  
ATOM    179  CA  GLY A  23     -25.009  25.614  20.000  1.00 29.82           C  
ATOM    180  C   GLY A  23     -25.199  24.672  21.171  1.00 35.18           C  
ATOM    181  O   GLY A  23     -24.302  24.524  22.006  1.00 42.12           O  
ATOM    182  N   THR A  24     -26.362  24.028  21.242  1.00 31.94           N  
ATOM    183  CA  THR A  24     -26.686  23.097  22.315  1.00 26.87           C  
ATOM    184  C   THR A  24     -26.986  21.730  21.715  1.00 28.36           C  
ATOM    185  O   THR A  24     -27.813  21.617  20.806  1.00 30.58           O  
ATOM    186  CB  THR A  24     -27.882  23.592  23.135  1.00 26.11           C  
ATOM    187  OG1 THR A  24     -29.081  23.479  22.359  1.00 22.52           O  
ATOM    188  CG2 THR A  24     -27.686  25.046  23.543  1.00 28.41           C  
ATOM    189  N   TYR A  25     -26.315  20.702  22.224  1.00 30.69           N  
ATOM    190  CA  TYR A  25     -26.441  19.346  21.711  1.00 26.05           C  
ATOM    191  C   TYR A  25     -27.405  18.534  22.568  1.00 27.33           C  
ATOM    192  O   TYR A  25     -27.547  18.772  23.770  1.00 26.84           O  
ATOM    193  CB  TYR A  25     -25.068  18.668  21.671  1.00 23.29           C  
ATOM    194  CG  TYR A  25     -25.107  17.158  21.612  1.00 38.86           C  
ATOM    195  CD1 TYR A  25     -25.002  16.396  22.768  1.00 33.96           C  
ATOM    196  CD2 TYR A  25     -25.240  16.495  20.401  1.00 40.83           C  
ATOM    197  CE1 TYR A  25     -25.032  15.016  22.719  1.00 28.14           C  
ATOM    198  CE2 TYR A  25     -25.272  15.115  20.342  1.00 37.59           C  
ATOM    199  CZ  TYR A  25     -25.167  14.381  21.504  1.00 38.55           C  
ATOM    200  OH  TYR A  25     -25.197  13.007  21.451  1.00 54.40           O  
ATOM    201  N   GLU A  26     -28.073  17.570  21.933  1.00 32.20           N  
ATOM    202  CA  GLU A  26     -29.014  16.699  22.635  1.00 26.99           C  
ATOM    203  C   GLU A  26     -29.027  15.352  21.929  1.00 28.80           C  
ATOM    204  O   GLU A  26     -29.515  15.250  20.800  1.00 31.32           O  
ATOM    205  CB  GLU A  26     -30.410  17.315  22.666  1.00 25.49           C  
ATOM    206  CG  GLU A  26     -31.497  16.393  23.201  1.00 27.99           C  
ATOM    207  CD  GLU A  26     -32.857  17.061  23.234  1.00 37.69           C  
ATOM    208  OE1 GLU A  26     -32.911  18.307  23.171  1.00 50.05           O  
ATOM    209  OE2 GLU A  26     -33.873  16.339  23.317  1.00 27.69           O1-
ATOM    210  N   GLY A  27     -28.505  14.322  22.591  1.00 32.78           N  
ATOM    211  CA  GLY A  27     -28.444  12.999  22.010  1.00 40.43           C  
ATOM    212  C   GLY A  27     -28.528  11.928  23.075  1.00 30.90           C  
ATOM    213  O   GLY A  27     -28.692  12.212  24.263  1.00 38.01           O  
ATOM    214  N   ASN A  28     -28.410  10.678  22.629  1.00 33.08           N  
ATOM    215  CA  ASN A  28     -28.477   9.515  23.502  1.00 38.88           C  
ATOM    216  C   ASN A  28     -27.095   9.012  23.906  1.00 32.36           C  
ATOM    217  O   ASN A  28     -26.955   7.848  24.296  1.00 24.04           O  
ATOM    218  CB  ASN A  28     -29.258   8.392  22.818  1.00 35.03           C  
ATOM    219  CG  ASN A  28     -30.632   8.833  22.353  1.00 41.95           C  
ATOM    220  OD1 ASN A  28     -31.601   8.783  23.111  1.00 30.37           O  
ATOM    221  ND2 ASN A  28     -30.724   9.261  21.099  1.00 50.84           N  
ATOM    222  N   SER A  29     -26.072   9.860  23.813  1.00 33.25           N  
ATOM    223  CA  SER A  29     -24.715   9.477  24.174  1.00 33.06           C  
ATOM    224  C   SER A  29     -23.922  10.744  24.440  1.00 38.34           C  
ATOM    225  O   SER A  29     -24.263  11.804  23.903  1.00 36.06           O  
ATOM    226  CB  SER A  29     -24.055   8.650  23.061  1.00 37.05           C  
ATOM    227  OG  SER A  29     -24.002   9.379  21.847  1.00 65.69           O  
ATOM    228  N   PRO A  30     -22.869  10.677  25.255  1.00 50.75           N  
ATOM    229  CA  PRO A  30     -22.118  11.895  25.576  1.00 38.97           C  
ATOM    230  C   PRO A  30     -21.505  12.524  24.334  1.00 44.89           C  
ATOM    231  O   PRO A  30     -21.214  11.851  23.343  1.00 35.92           O  
ATOM    232  CB  PRO A  30     -21.039  11.406  26.552  1.00 39.26           C  
ATOM    233  CG  PRO A  30     -20.938   9.937  26.317  1.00 51.70           C  
ATOM    234  CD  PRO A  30     -22.309   9.489  25.922  1.00 56.22           C  
ATOM    235  N   PHE A  31     -21.314  13.839  24.403  1.00 42.79           N  
ATOM    236  CA  PHE A  31     -20.755  14.610  23.300  1.00 35.82           C  
ATOM    237  C   PHE A  31     -19.236  14.621  23.419  1.00 40.43           C  
ATOM    238  O   PHE A  31     -18.692  15.091  24.425  1.00 45.48           O  
ATOM    239  CB  PHE A  31     -21.319  16.030  23.315  1.00 34.16           C  
ATOM    240  CG  PHE A  31     -20.827  16.897  22.192  1.00 43.94           C  
ATOM    241  CD1 PHE A  31     -21.327  16.745  20.910  1.00 40.02           C  
ATOM    242  CD2 PHE A  31     -19.876  17.876  22.423  1.00 53.31           C  
ATOM    243  CE1 PHE A  31     -20.879  17.546  19.877  1.00 37.41           C  
ATOM    244  CE2 PHE A  31     -19.425  18.680  21.395  1.00 36.24           C  
ATOM    245  CZ  PHE A  31     -19.927  18.515  20.121  1.00 32.72           C  
ATOM    246  N   HIS A  32     -18.553  14.101  22.396  1.00 42.35           N  
ATOM    247  CA  HIS A  32     -17.097  13.981  22.391  1.00 40.74           C  
ATOM    248  C   HIS A  32     -16.508  14.996  21.419  1.00 36.19           C  
ATOM    249  O   HIS A  32     -16.304  14.684  20.236  1.00 45.98           O  
ATOM    250  CB  HIS A  32     -16.671  12.561  22.009  1.00 37.84           C  
ATOM    251  CG  HIS A  32     -17.386  11.488  22.769  1.00 43.87           C  
ATOM    252  ND1 HIS A  32     -18.498  10.842  22.274  1.00 46.90           N  
ATOM    253  CD2 HIS A  32     -17.147  10.947  23.986  1.00 59.04           C  
ATOM    254  CE1 HIS A  32     -18.913   9.948  23.154  1.00 43.84           C  
ATOM    255  NE2 HIS A  32     -18.111   9.992  24.202  1.00 56.63           N  
ATOM    256  N   PRO A  33     -16.214  16.217  21.858  1.00 32.12           N  
ATOM    257  CA  PRO A  33     -15.606  17.197  20.955  1.00 38.26           C  
ATOM    258  C   PRO A  33     -14.118  16.956  20.761  1.00 51.25           C  
ATOM    259  O   PRO A  33     -13.417  16.459  21.646  1.00 36.09           O  
ATOM    260  CB  PRO A  33     -15.858  18.532  21.665  1.00 33.62           C  
ATOM    261  CG  PRO A  33     -15.908  18.175  23.107  1.00 39.48           C  
ATOM    262  CD  PRO A  33     -16.506  16.794  23.183  1.00 48.05           C  
ATOM    263  N   LEU A  34     -13.643  17.320  19.572  1.00 41.31           N  
ATOM    264  CA  LEU A  34     -12.234  17.250  19.217  1.00 40.73           C  
ATOM    265  C   LEU A  34     -11.808  18.603  18.660  1.00 35.77           C  
ATOM    266  O   LEU A  34     -12.606  19.540  18.566  1.00 37.53           O  
ATOM    267  CB  LEU A  34     -11.972  16.130  18.201  1.00 39.90           C  
ATOM    268  CG  LEU A  34     -12.307  14.707  18.654  1.00 43.19           C  
ATOM    269  CD1 LEU A  34     -12.115  13.724  17.509  1.00 55.78           C  
ATOM    270  CD2 LEU A  34     -11.458  14.306  19.851  1.00 62.47           C  
ATOM    271  N   ALA A  35     -10.537  18.704  18.285  1.00 42.24           N  
ATOM    272  CA  ALA A  35     -10.017  19.947  17.740  1.00 61.41           C  
ATOM    273  C   ALA A  35     -10.598  20.206  16.351  1.00 55.31           C  
ATOM    274  O   ALA A  35     -11.198  19.331  15.719  1.00 51.89           O  
ATOM    275  CB  ALA A  35      -8.491  19.906  17.679  1.00 63.48           C  
ATOM    276  N   ASP A  36     -10.416  21.439  15.879  1.00 58.01           N  
ATOM    277  CA  ASP A  36     -10.860  21.850  14.547  1.00 59.85           C  
ATOM    278  C   ASP A  36     -12.380  21.797  14.412  1.00 57.48           C  
ATOM    279  O   ASP A  36     -12.909  21.572  13.320  1.00 61.22           O  
ATOM    280  CB  ASP A  36     -10.200  20.996  13.460  1.00 71.53           C  
ATOM    281  CG  ASP A  36      -8.686  21.061  13.506  1.00 76.55           C  
ATOM    282  OD1 ASP A  36      -8.147  22.101  13.941  1.00 84.11           O  
ATOM    283  OD2 ASP A  36      -8.034  20.073  13.108  1.00 63.26           O1-
ATOM    284  N   ASN A  37     -13.093  22.007  15.518  1.00 58.24           N  
ATOM    285  CA  ASN A  37     -14.554  22.062  15.520  1.00 51.74           C  
ATOM    286  C   ASN A  37     -15.154  20.793  14.907  1.00 49.02           C  
ATOM    287  O   ASN A  37     -15.832  20.822  13.878  1.00 48.92           O  
ATOM    288  CB  ASN A  37     -15.050  23.314  14.788  1.00 51.02           C  
ATOM    289  CG  ASN A  37     -14.663  24.596  15.499  1.00 54.84           C  
ATOM    290  OD1 ASN A  37     -14.507  24.619  16.720  1.00 77.82           O  
ATOM    291  ND2 ASN A  37     -14.509  25.672  14.737  1.00 57.57           N  
ATOM    292  N   LYS A  38     -14.891  19.670  15.569  1.00 45.61           N  
ATOM    293  CA  LYS A  38     -15.433  18.379  15.173  1.00 46.30           C  
ATOM    294  C   LYS A  38     -15.951  17.658  16.409  1.00 57.91           C  
ATOM    295  O   LYS A  38     -15.578  17.978  17.540  1.00 48.38           O  
ATOM    296  CB  LYS A  38     -14.379  17.508  14.473  1.00 45.22           C  
ATOM    297  CG  LYS A  38     -13.686  18.170  13.293  1.00 55.24           C  
ATOM    298  CD  LYS A  38     -12.523  17.319  12.802  1.00 58.20           C  
ATOM    299  CE  LYS A  38     -11.753  18.001  11.682  1.00 73.16           C  
ATOM    300  NZ  LYS A  38     -12.548  18.109  10.430  1.00 94.39           N  
ATOM    301  N   PHE A  39     -16.811  16.667  16.186  1.00 36.80           N  
ATOM    302  CA  PHE A  39     -17.291  15.825  17.272  1.00 27.99           C  
ATOM    303  C   PHE A  39     -17.355  14.380  16.803  1.00 33.66           C  
ATOM    304  O   PHE A  39     -17.784  14.099  15.681  1.00 38.38           O  
ATOM    305  CB  PHE A  39     -18.664  16.285  17.787  1.00 36.79           C  
ATOM    306  CG  PHE A  39     -19.786  16.088  16.808  1.00 35.06           C  
ATOM    307  CD1 PHE A  39     -20.111  17.079  15.897  1.00 41.85           C  
ATOM    308  CD2 PHE A  39     -20.530  14.920  16.815  1.00 29.29           C  
ATOM    309  CE1 PHE A  39     -21.149  16.902  15.002  1.00 42.37           C  
ATOM    310  CE2 PHE A  39     -21.568  14.738  15.922  1.00 27.09           C  
ATOM    311  CZ  PHE A  39     -21.879  15.730  15.016  1.00 35.46           C  
ATOM    312  N   ALA A  40     -16.919  13.472  17.669  1.00 50.33           N  
ATOM    313  CA  ALA A  40     -16.868  12.051  17.367  1.00 33.66           C  
ATOM    314  C   ALA A  40     -17.877  11.294  18.219  1.00 36.99           C  
ATOM    315  O   ALA A  40     -18.326  11.772  19.265  1.00 55.62           O  
ATOM    316  CB  ALA A  40     -15.462  11.491  17.608  1.00 28.91           C  
ATOM    317  N   LEU A  41     -18.235  10.100  17.755  1.00 35.16           N  
ATOM    318  CA  LEU A  41     -19.150   9.251  18.508  1.00 33.24           C  
ATOM    319  C   LEU A  41     -19.140   7.850  17.914  1.00 33.54           C  
ATOM    320  O   LEU A  41     -18.771   7.648  16.754  1.00 31.71           O  
ATOM    321  CB  LEU A  41     -20.571   9.829  18.515  1.00 43.80           C  
ATOM    322  CG  LEU A  41     -21.241  10.060  17.158  1.00 42.59           C  
ATOM    323  CD1 LEU A  41     -21.891   8.787  16.638  1.00 31.19           C  
ATOM    324  CD2 LEU A  41     -22.263  11.184  17.252  1.00 32.29           C  
ATOM    325  N   THR A  42     -19.555   6.885  18.729  1.00 32.37           N  
ATOM    326  CA  THR A  42     -19.615   5.498  18.296  1.00 32.79           C  
ATOM    327  C   THR A  42     -20.818   5.275  17.387  1.00 36.50           C  
ATOM    328  O   THR A  42     -21.850   5.939  17.509  1.00 31.63           O  
ATOM    329  CB  THR A  42     -19.690   4.562  19.503  1.00 32.19           C  
ATOM    330  OG1 THR A  42     -18.504   4.704  20.296  1.00 39.02           O  
ATOM    331  CG2 THR A  42     -19.827   3.112  19.058  1.00 33.48           C  
ATOM    332  N   CYS A  43     -20.673   4.323  16.468  1.00 38.81           N  
ATOM    333  CA  CYS A  43     -21.717   4.039  15.495  1.00 38.24           C  
ATOM    334  C   CYS A  43     -22.807   3.174  16.115  1.00 31.99           C  
ATOM    335  O   CYS A  43     -22.523   2.127  16.706  1.00 32.40           O  
ATOM    336  CB  CYS A  43     -21.127   3.338  14.273  1.00 41.94           C  
ATOM    337  SG  CYS A  43     -22.354   2.849  13.040  1.00 49.63           S  
ATOM    338  N   PHE A  44     -24.055   3.615  15.974  1.00 30.51           N  
ATOM    339  CA  PHE A  44     -25.212   2.848  16.413  1.00 32.05           C  
ATOM    340  C   PHE A  44     -26.466   3.582  15.964  1.00 27.36           C  
ATOM    341  O   PHE A  44     -26.553   4.804  16.104  1.00 26.07           O  
ATOM    342  CB  PHE A  44     -25.218   2.651  17.936  1.00 28.28           C  
ATOM    343  CG  PHE A  44     -25.347   3.927  18.718  1.00 26.99           C  
ATOM    344  CD1 PHE A  44     -26.549   4.270  19.313  1.00 22.49           C  
ATOM    345  CD2 PHE A  44     -24.266   4.781  18.861  1.00 25.16           C  
ATOM    346  CE1 PHE A  44     -26.670   5.442  20.036  1.00 22.71           C  
ATOM    347  CE2 PHE A  44     -24.383   5.955  19.581  1.00 27.31           C  
ATOM    348  CZ  PHE A  44     -25.587   6.285  20.169  1.00 22.55           C  
ATOM    349  N   SER A  45     -27.423   2.832  15.414  1.00 30.47           N  
ATOM    350  CA  SER A  45     -28.655   3.415  14.894  1.00 29.79           C  
ATOM    351  C   SER A  45     -29.285   4.339  15.929  1.00 22.07           C  
ATOM    352  O   SER A  45     -29.721   3.878  16.988  1.00 28.10           O  
ATOM    353  CB  SER A  45     -29.641   2.314  14.496  1.00 37.06           C  
ATOM    354  OG  SER A  45     -29.076   1.445  13.529  1.00 47.07           O  
ATOM    355  N   THR A  46     -29.341   5.638  15.643  1.00 23.15           N  
ATOM    356  CA  THR A  46     -29.802   6.596  16.644  1.00 30.50           C  
ATOM    357  C   THR A  46     -30.117   7.923  15.967  1.00 26.04           C  
ATOM    358  O   THR A  46     -29.871   8.111  14.773  1.00 37.32           O  
ATOM    359  CB  THR A  46     -28.756   6.789  17.747  1.00 39.11           C  
ATOM    360  OG1 THR A  46     -29.304   7.583  18.807  1.00 31.07           O  
ATOM    361  CG2 THR A  46     -27.514   7.478  17.192  1.00 28.60           C  
ATOM    362  N   GLN A  47     -30.673   8.843  16.757  1.00 31.42           N  
ATOM    363  CA  GLN A  47     -30.968  10.196  16.308  1.00 35.74           C  
ATOM    364  C   GLN A  47     -30.636  11.178  17.422  1.00 30.32           C  
ATOM    365  O   GLN A  47     -30.887  10.901  18.599  1.00 48.75           O  
ATOM    366  CB  GLN A  47     -32.442  10.351  15.908  1.00 44.50           C  
ATOM    367  CG  GLN A  47     -32.886   9.441  14.776  1.00 52.04           C  
ATOM    368  CD  GLN A  47     -34.303   9.733  14.320  1.00 42.39           C  
ATOM    369  OE1 GLN A  47     -34.894  10.742  14.704  1.00 26.94           O  
ATOM    370  NE2 GLN A  47     -34.856   8.849  13.497  1.00 41.98           N  
ATOM    371  N   PHE A  48     -30.073  12.324  17.044  1.00 19.32           N  
ATOM    372  CA  PHE A  48     -29.777  13.399  17.985  1.00 27.85           C  
ATOM    373  C   PHE A  48     -30.012  14.735  17.287  1.00 26.24           C  
ATOM    374  O   PHE A  48     -30.456  14.787  16.136  1.00 25.19           O  
ATOM    375  CB  PHE A  48     -28.350  13.279  18.539  1.00 32.96           C  
ATOM    376  CG  PHE A  48     -27.286  13.177  17.483  1.00 39.99           C  
ATOM    377  CD1 PHE A  48     -26.995  11.961  16.888  1.00 34.88           C  
ATOM    378  CD2 PHE A  48     -26.562  14.294  17.100  1.00 36.72           C  
ATOM    379  CE1 PHE A  48     -26.011  11.863  15.922  1.00 22.04           C  
ATOM    380  CE2 PHE A  48     -25.575  14.201  16.136  1.00 22.66           C  
ATOM    381  CZ  PHE A  48     -25.300  12.984  15.547  1.00 20.92           C  
ATOM    382  N   ALA A  49     -29.718  15.829  17.988  1.00 22.98           N  
ATOM    383  CA  ALA A  49     -30.066  17.149  17.487  1.00 26.96           C  
ATOM    384  C   ALA A  49     -29.102  18.203  18.012  1.00 26.00           C  
ATOM    385  O   ALA A  49     -28.494  18.048  19.076  1.00 21.35           O  
ATOM    386  CB  ALA A  49     -31.502  17.525  17.874  1.00 19.88           C  
ATOM    387  N   PHE A  50     -28.975  19.280  17.235  1.00 30.89           N  
ATOM    388  CA  PHE A  50     -28.226  20.470  17.607  1.00 27.06           C  
ATOM    389  C   PHE A  50     -29.121  21.687  17.430  1.00 35.99           C  
ATOM    390  O   PHE A  50     -29.812  21.815  16.414  1.00 32.48           O  
ATOM    391  CB  PHE A  50     -26.968  20.645  16.743  1.00 24.04           C  
ATOM    392  CG  PHE A  50     -25.851  19.705  17.087  1.00 22.13           C  
ATOM    393  CD1 PHE A  50     -25.955  18.352  16.820  1.00 24.35           C  
ATOM    394  CD2 PHE A  50     -24.683  20.183  17.658  1.00 24.70           C  
ATOM    395  CE1 PHE A  50     -24.922  17.490  17.130  1.00 34.17           C  
ATOM    396  CE2 PHE A  50     -23.647  19.326  17.970  1.00 25.87           C  
ATOM    397  CZ  PHE A  50     -23.766  17.978  17.705  1.00 29.92           C  
ATOM    398  N   ALA A  51     -29.106  22.579  18.416  1.00 25.96           N  
ATOM    399  CA  ALA A  51     -29.809  23.856  18.342  1.00 23.09           C  
ATOM    400  C   ALA A  51     -28.759  24.950  18.206  1.00 28.71           C  
ATOM    401  O   ALA A  51     -27.994  25.204  19.143  1.00 29.32           O  
ATOM    402  CB  ALA A  51     -30.687  24.077  19.571  1.00 19.12           C  
ATOM    403  N   CYS A  52     -28.720  25.589  17.043  1.00 25.73           N  
ATOM    404  CA  CYS A  52     -27.695  26.570  16.730  1.00 31.49           C  
ATOM    405  C   CYS A  52     -28.203  27.985  16.964  1.00 22.30           C  
ATOM    406  O   CYS A  52     -29.413  28.227  16.999  1.00 15.04           O  
ATOM    407  CB  CYS A  52     -27.243  26.416  15.275  1.00 25.46           C  
ATOM    408  SG  CYS A  52     -26.272  24.923  14.965  1.00 17.61           S  
ATOM    409  N   PRO A  53     -27.297  28.953  17.128  1.00 21.95           N  
ATOM    410  CA  PRO A  53     -27.745  30.331  17.389  1.00 18.46           C  
ATOM    411  C   PRO A  53     -28.555  30.930  16.254  1.00 29.70           C  
ATOM    412  O   PRO A  53     -29.439  31.758  16.506  1.00 22.06           O  
ATOM    413  CB  PRO A  53     -26.429  31.096  17.602  1.00 15.91           C  
ATOM    414  CG  PRO A  53     -25.403  30.051  17.893  1.00 33.37           C  
ATOM    415  CD  PRO A  53     -25.828  28.839  17.134  1.00 23.50           C  
ATOM    416  N   ASP A  54     -28.282  30.536  15.009  1.00 32.94           N  
ATOM    417  CA  ASP A  54     -28.977  31.108  13.862  1.00 40.93           C  
ATOM    418  C   ASP A  54     -30.453  30.733  13.811  1.00 30.91           C  
ATOM    419  O   ASP A  54     -31.177  31.265  12.962  1.00 38.70           O  
ATOM    420  CB  ASP A  54     -28.293  30.665  12.566  1.00 38.48           C  
ATOM    421  CG  ASP A  54     -28.260  29.156  12.410  1.00 38.21           C  
ATOM    422  OD1 ASP A  54     -28.769  28.451  13.306  1.00 32.10           O  
ATOM    423  OD2 ASP A  54     -27.723  28.675  11.390  1.00 31.51           O1-
ATOM    424  N   GLY A  55     -30.916  29.845  14.686  1.00 26.13           N  
ATOM    425  CA  GLY A  55     -32.294  29.404  14.659  1.00 26.47           C  
ATOM    426  C   GLY A  55     -32.548  28.186  13.805  1.00 43.38           C  
ATOM    427  O   GLY A  55     -33.707  27.910  13.475  1.00 28.01           O  
ATOM    428  N   VAL A  56     -31.505  27.448  13.437  1.00 31.08           N  
ATOM    429  CA  VAL A  56     -31.621  26.267  12.590  1.00 25.63           C  
ATOM    430  C   VAL A  56     -31.373  25.042  13.458  1.00 30.39           C  
ATOM    431  O   VAL A  56     -30.302  24.908  14.064  1.00 46.09           O  
ATOM    432  CB  VAL A  56     -30.635  26.318  11.413  1.00 38.53           C  
ATOM    433  CG1 VAL A  56     -30.755  25.064  10.562  1.00 31.02           C  
ATOM    434  CG2 VAL A  56     -30.874  27.565  10.573  1.00 45.26           C  
ATOM    435  N   LYS A  57     -32.359  24.151  13.518  1.00 24.56           N  
ATOM    436  CA  LYS A  57     -32.252  22.919  14.292  1.00 24.98           C  
ATOM    437  C   LYS A  57     -31.708  21.821  13.384  1.00 24.88           C  
ATOM    438  O   LYS A  57     -32.413  21.336  12.493  1.00 23.33           O  
ATOM    439  CB  LYS A  57     -33.607  22.530  14.877  1.00 39.64           C  
ATOM    440  CG  LYS A  57     -33.580  21.258  15.711  1.00 29.95           C  
ATOM    441  CD  LYS A  57     -34.950  20.941  16.287  1.00 41.06           C  
ATOM    442  CE  LYS A  57     -34.920  19.670  17.119  1.00 52.94           C  
ATOM    443  NZ  LYS A  57     -36.253  19.353  17.703  1.00 46.57           N  
ATOM    444  N   HIS A  58     -30.459  21.427  13.614  1.00 25.71           N  
ATOM    445  CA  HIS A  58     -29.806  20.404  12.803  1.00 25.74           C  
ATOM    446  C   HIS A  58     -30.079  19.040  13.427  1.00 22.53           C  
ATOM    447  O   HIS A  58     -29.502  18.696  14.462  1.00 20.48           O  
ATOM    448  CB  HIS A  58     -28.307  20.675  12.703  1.00 22.28           C  
ATOM    449  CG  HIS A  58     -27.970  21.980  12.052  1.00 24.88           C  
ATOM    450  ND1 HIS A  58     -27.494  22.067  10.762  1.00 26.71           N  
ATOM    451  CD2 HIS A  58     -28.042  23.251  12.513  1.00 35.40           C  
ATOM    452  CE1 HIS A  58     -27.286  23.336  10.456  1.00 38.03           C  
ATOM    453  NE2 HIS A  58     -27.610  24.075  11.502  1.00 43.78           N  
ATOM    454  N   VAL A  59     -30.964  18.271  12.807  1.00 24.11           N  
ATOM    455  CA  VAL A  59     -31.284  16.926  13.269  1.00 20.29           C  
ATOM    456  C   VAL A  59     -30.369  15.937  12.564  1.00 19.22           C  
ATOM    457  O   VAL A  59     -30.138  16.037  11.353  1.00 28.12           O  
ATOM    458  CB  VAL A  59     -32.767  16.596  13.013  1.00 24.26           C  
ATOM    459  CG1 VAL A  59     -33.108  15.216  13.560  1.00 26.13           C  
ATOM    460  CG2 VAL A  59     -33.661  17.659  13.633  1.00 24.42           C  
ATOM    461  N   TYR A  60     -29.843  14.977  13.321  1.00 20.87           N  
ATOM    462  CA  TYR A  60     -28.923  13.974  12.810  1.00 15.93           C  
ATOM    463  C   TYR A  60     -29.487  12.587  13.073  1.00 21.80           C  
ATOM    464  O   TYR A  60     -30.055  12.332  14.139  1.00 34.83           O  
ATOM    465  CB  TYR A  60     -27.548  14.097  13.470  1.00 22.29           C  
ATOM    466  CG  TYR A  60     -26.773  15.335  13.084  1.00 20.75           C  
ATOM    467  CD1 TYR A  60     -27.207  16.598  13.461  1.00 19.06           C  
ATOM    468  CD2 TYR A  60     -25.595  15.238  12.356  1.00 19.61           C  
ATOM    469  CE1 TYR A  60     -26.497  17.730  13.113  1.00 21.78           C  
ATOM    470  CE2 TYR A  60     -24.878  16.363  12.004  1.00 22.57           C  
ATOM    471  CZ  TYR A  60     -25.332  17.607  12.386  1.00 23.37           C  
ATOM    472  OH  TYR A  60     -24.620  18.730  12.037  1.00 44.82           O  
ATOM    473  N   GLN A  61     -29.317  11.693  12.101  1.00 36.00           N  
ATOM    474  CA  GLN A  61     -29.764  10.310  12.224  1.00 38.18           C  
ATOM    475  C   GLN A  61     -28.699   9.404  11.630  1.00 35.30           C  
ATOM    476  O   GLN A  61     -28.335   9.556  10.460  1.00 30.67           O  
ATOM    477  CB  GLN A  61     -31.106  10.095  11.518  1.00 31.35           C  
ATOM    478  CG  GLN A  61     -31.554   8.641  11.466  1.00 34.25           C  
ATOM    479  CD  GLN A  61     -32.958   8.481  10.918  1.00 48.20           C  
ATOM    480  OE1 GLN A  61     -33.623   9.463  10.587  1.00 47.12           O  
ATOM    481  NE2 GLN A  61     -33.417   7.239  10.820  1.00 35.96           N  
ATOM    482  N   LEU A  62     -28.201   8.468  12.433  1.00 29.28           N  
ATOM    483  CA  LEU A  62     -27.227   7.486  11.983  1.00 28.26           C  
ATOM    484  C   LEU A  62     -27.878   6.113  11.898  1.00 35.30           C  
ATOM    485  O   LEU A  62     -28.658   5.728  12.778  1.00 54.41           O  
ATOM    486  CB  LEU A  62     -26.020   7.421  12.923  1.00 31.11           C  
ATOM    487  CG  LEU A  62     -25.030   8.587  12.881  1.00 35.47           C  
ATOM    488  CD1 LEU A  62     -23.842   8.283  13.773  1.00 35.48           C  
ATOM    489  CD2 LEU A  62     -24.568   8.871  11.462  1.00 53.74           C  
ATOM    490  N   ARG A  63     -27.553   5.388  10.830  1.00 34.53           N  
ATOM    491  CA  ARG A  63     -28.006   4.018  10.625  1.00 32.18           C  
ATOM    492  C   ARG A  63     -26.801   3.089  10.699  1.00 37.92           C  
ATOM    493  O   ARG A  63     -25.828   3.266   9.957  1.00 40.28           O  
ATOM    494  CB  ARG A  63     -28.712   3.869   9.275  1.00 38.26           C  
ATOM    495  CG  ARG A  63     -29.179   2.452   8.958  1.00 61.06           C  
ATOM    496  CD  ARG A  63     -30.417   2.070   9.752  1.00 58.78           C  
ATOM    497  NE  ARG A  63     -31.646   2.414   9.041  1.00 73.90           N  
ATOM    498  CZ  ARG A  63     -32.176   1.686   8.060  1.00 75.16           C  
ATOM    499  NH1 ARG A  63     -31.590   0.565   7.659  1.00 67.62           N  
ATOM    500  NH2 ARG A  63     -33.298   2.083   7.475  1.00 66.76           N  
ATOM    501  N   ALA A  64     -26.875   2.096  11.578  1.00 39.03           N  
ATOM    502  CA  ALA A  64     -25.768   1.184  11.818  1.00 41.62           C  
ATOM    503  C   ALA A  64     -25.941  -0.090  11.002  1.00 31.95           C  
ATOM    504  O   ALA A  64     -27.035  -0.658  10.939  1.00 32.08           O  
ATOM    505  CB  ALA A  64     -25.662   0.841  13.304  1.00 39.73           C  
ATOM    506  N   ARG A  65     -24.851  -0.531  10.376  1.00 31.04           N  
ATOM    507  CA  ARG A  65     -24.833  -1.761   9.599  1.00 31.83           C  
ATOM    508  C   ARG A  65     -23.609  -2.581   9.981  1.00 31.27           C  
ATOM    509  O   ARG A  65     -22.592  -2.040  10.422  1.00 25.89           O  
ATOM    510  CB  ARG A  65     -24.825  -1.476   8.089  1.00 39.41           C  
ATOM    511  CG  ARG A  65     -23.741  -0.506   7.640  1.00 43.27           C  
ATOM    512  CD  ARG A  65     -23.806  -0.261   6.139  1.00 33.57           C  
ATOM    513  NE  ARG A  65     -22.884   0.788   5.709  1.00 35.96           N  
ATOM    514  CZ  ARG A  65     -21.601   0.595   5.410  1.00 45.38           C  
ATOM    515  NH1 ARG A  65     -21.060  -0.615   5.491  1.00 33.30           N  
ATOM    516  NH2 ARG A  65     -20.854   1.621   5.029  1.00 35.71           N  
ATOM    517  N   SER A  66     -23.720  -3.894   9.811  1.00 31.50           N  
ATOM    518  CA  SER A  66     -22.636  -4.806  10.158  1.00 43.18           C  
ATOM    519  C   SER A  66     -21.925  -5.309   8.907  1.00 43.29           C  
ATOM    520  O   SER A  66     -21.017  -6.136   8.988  1.00 57.40           O  
ATOM    521  CB  SER A  66     -23.170  -5.987  10.969  1.00 52.52           C  
ATOM    522  OG  SER A  66     -24.139  -6.712  10.233  1.00 32.86           O  
TER     523      SER A  66                                                      
HETATM  524  O   HOH A 101     -15.156   1.771  18.304  1.00 28.67           O  
HETATM  525  O   HOH A 102     -34.358  25.671  13.835  1.00 28.71           O  
HETATM  526  O   HOH A 103     -21.221  22.900   8.980  1.00 22.51           O  
CONECT   75  337                                                                
CONECT  165  408                                                                
CONECT  337   75                                                                
CONECT  408  165                                                                
MASTER      234    0    0    0    7    0    0    6  525    1    4    6          
END                                                                             
HEADER    VIRAL PROTEIN                           10-MAR-20   6W4H              
TITLE     1.80 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF NSP16 - NSP10 COMPLEX   
TITLE    2 FROM SARS-COV-2                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SARS-COV-2 NSP16;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 6799-7096;                                    
COMPND   5 SYNONYM: 2'-O-METHYLTRANSFERASE;                                     
COMPND   6 EC: 2.1.1.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SARS-COV-2 NSP10;                                          
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 4254-4392;                                    
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 GENE: REP, 1A-1B;                                                    
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: MAGIC;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMCSG53;                                  
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE  14 2;                                                                   
SOURCE  15 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE  16 ORGANISM_TAXID: 2697049;                                             
SOURCE  17 GENE: REP, 1A-1B;                                                    
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  20 EXPRESSION_SYSTEM_VARIANT: MAGIC;                                    
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PMCSG53                                   
KEYWDS    STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS     
KEYWDS   2 DISEASES, CSGID, NSP16, NSP10, COMPLEX, VIRAL PROTEIN                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.MINASOV,L.SHUVALOVA,M.ROSAS-LEMUS,O.KIRYUKHINA,G.WIERSUM,A.GODZIK,  
AUTHOR   2 L.JAROSZEWSKI,P.J.STOGIOS,T.SKARINA,K.J.F.SATCHELL,CENTER FOR        
AUTHOR   3 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)                   
REVDAT   4   29-JUL-20 6W4H    1       COMPND REMARK HETNAM SITE                
REVDAT   3   06-MAY-20 6W4H    1       COMPND SOURCE DBREF  SEQADV              
REVDAT   2   01-APR-20 6W4H    1       COMPND                                   
REVDAT   1   18-MAR-20 6W4H    0                                                
JRNL        AUTH   G.MINASOV,L.SHUVALOVA,M.ROSAS-LEMUS,O.KIRYUKHINA,G.WIERSUM,  
JRNL        AUTH 2 A.GODZIK,L.JAROSZEWSKI,P.J.STOGIOS,T.SKARINA,K.J.F.SATCHELL  
JRNL        TITL   1.80 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF NSP16 - NSP10  
JRNL        TITL 2 COMPLEX FROM SARS-COV-2                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0258                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 73752                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.150                           
REMARK   3   R VALUE            (WORKING SET) : 0.149                           
REMARK   3   FREE R VALUE                     : 0.163                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3821                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5432                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 282                          
REMARK   3   BIN FREE R VALUE                    : 0.2390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3201                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 65                                      
REMARK   3   SOLVENT ATOMS            : 442                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.18000                                              
REMARK   3    B12 (A**2) : -0.03000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.073         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.070         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.047         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.962         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.966                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3697 ; 0.004 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  3336 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5072 ; 1.183 ; 1.640       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7788 ; 0.321 ; 1.578       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   485 ; 3.282 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   166 ;27.951 ;23.614       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   617 ; 8.695 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ; 6.592 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   495 ; 0.052 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4271 ; 0.055 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   754 ; 0.051 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  6798        A  6827                          
REMARK   3    ORIGIN FOR THE GROUP (A):  92.7106  37.5769  33.6726              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1121 T22:   0.0521                                     
REMARK   3      T33:   0.1420 T12:  -0.0205                                     
REMARK   3      T13:  -0.0123 T23:  -0.0755                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8328 L22:   1.4376                                     
REMARK   3      L33:   2.2037 L12:   0.1141                                     
REMARK   3      L13:   0.6504 L23:   0.2818                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0530 S12:  -0.1785 S13:   0.4034                       
REMARK   3      S21:   0.1046 S22:   0.0545 S23:  -0.1822                       
REMARK   3      S31:  -0.1433 S32:   0.1214 S33:  -0.0016                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  6828        A  6932                          
REMARK   3    ORIGIN FOR THE GROUP (A):  84.8509  20.0354  18.6950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1163 T22:   0.0192                                     
REMARK   3      T33:   0.0180 T12:  -0.0232                                     
REMARK   3      T13:  -0.0076 T23:  -0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1583 L22:   1.9178                                     
REMARK   3      L33:   0.7927 L12:  -0.0499                                     
REMARK   3      L13:   0.1649 L23:   0.3623                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0148 S12:   0.0719 S13:  -0.0399                       
REMARK   3      S21:  -0.2093 S22:   0.1018 S23:   0.0202                       
REMARK   3      S31:   0.0562 S32:   0.0147 S33:  -0.0869                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  6933        A  6956                          
REMARK   3    ORIGIN FOR THE GROUP (A):  93.6483  16.9856  35.6139              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1389 T22:   0.0527                                     
REMARK   3      T33:   0.0288 T12:   0.0043                                     
REMARK   3      T13:  -0.0455 T23:   0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5538 L22:   3.8901                                     
REMARK   3      L33:   5.7842 L12:  -0.6515                                     
REMARK   3      L13:  -1.2383 L23:   2.9366                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1011 S12:  -0.1924 S13:  -0.1545                       
REMARK   3      S21:   0.4604 S22:   0.0523 S23:  -0.1975                       
REMARK   3      S31:   0.4097 S32:  -0.1119 S33:  -0.1534                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  6957        A  7048                          
REMARK   3    ORIGIN FOR THE GROUP (A):  94.2818  28.8532  26.9016              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0744 T22:   0.0393                                     
REMARK   3      T33:   0.0617 T12:  -0.0207                                     
REMARK   3      T13:   0.0071 T23:  -0.0421                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0247 L22:   1.4906                                     
REMARK   3      L33:   1.0888 L12:   0.2122                                     
REMARK   3      L13:   0.0595 L23:   0.3060                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0319 S12:  -0.0547 S13:   0.1098                       
REMARK   3      S21:  -0.0019 S22:   0.1340 S23:  -0.2202                       
REMARK   3      S31:  -0.0136 S32:   0.1503 S33:  -0.1021                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  7049        A  7065                          
REMARK   3    ORIGIN FOR THE GROUP (A): 101.8656  23.0792   6.3974              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0863 T22:   0.0346                                     
REMARK   3      T33:   0.0477 T12:  -0.0461                                     
REMARK   3      T13:   0.0435 T23:  -0.0257                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7604 L22:   2.5286                                     
REMARK   3      L33:   1.0699 L12:  -2.7017                                     
REMARK   3      L13:  -0.6614 L23:   0.4493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0197 S12:   0.1631 S13:   0.2645                       
REMARK   3      S21:  -0.1341 S22:   0.0870 S23:  -0.3117                       
REMARK   3      S31:  -0.0419 S32:   0.0750 S33:  -0.0674                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  7066        A  7096                          
REMARK   3    ORIGIN FOR THE GROUP (A): 100.7636  15.4269  12.2787              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1440 T22:   0.1119                                     
REMARK   3      T33:   0.1198 T12:  -0.0228                                     
REMARK   3      T13:   0.0944 T23:  -0.0856                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9004 L22:   5.7587                                     
REMARK   3      L33:   1.2851 L12:   1.3876                                     
REMARK   3      L13:  -0.0168 L23:  -1.3622                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0027 S12:   0.0893 S13:  -0.1138                       
REMARK   3      S21:  -0.2651 S22:   0.0967 S23:  -0.4347                       
REMARK   3      S31:   0.0410 S32:   0.2319 S33:  -0.0940                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  4271        B  4288                          
REMARK   3    ORIGIN FOR THE GROUP (A):  56.0951   4.7767  15.2986              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0820 T22:   0.0845                                     
REMARK   3      T33:   0.3435 T12:  -0.0624                                     
REMARK   3      T13:  -0.0536 T23:   0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2654 L22:  11.9433                                     
REMARK   3      L33:   1.3971 L12:  -1.7056                                     
REMARK   3      L13:  -0.2773 L23:   0.8343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0488 S12:   0.0327 S13:  -0.1424                       
REMARK   3      S21:  -0.4528 S22:  -0.2131 S23:   0.7220                       
REMARK   3      S31:   0.1344 S32:  -0.1350 S33:   0.1643                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  4289        B  4344                          
REMARK   3    RESIDUE RANGE :   S     1        S     1                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.0475  17.8217  10.6894              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1397 T22:   0.0577                                     
REMARK   3      T33:   0.1077 T12:  -0.0322                                     
REMARK   3      T13:  -0.1024 T23:  -0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2104 L22:   3.6373                                     
REMARK   3      L33:   1.6256 L12:  -0.0143                                     
REMARK   3      L13:  -0.0847 L23:  -0.5394                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0243 S12:   0.3024 S13:  -0.1843                       
REMARK   3      S21:  -0.4276 S22:   0.0520 S23:   0.4007                       
REMARK   3      S31:   0.1414 S32:  -0.1435 S33:  -0.0277                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  4345        B  4386                          
REMARK   3    RESIDUE RANGE :   S     2        S     2                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.4718  19.8901   4.2832              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2508 T22:   0.1631                                     
REMARK   3      T33:   0.2055 T12:  -0.0525                                     
REMARK   3      T13:  -0.1997 T23:  -0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3852 L22:   2.7319                                     
REMARK   3      L33:   2.7697 L12:  -0.3080                                     
REMARK   3      L13:  -0.6470 L23:  -1.2904                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0449 S12:   0.5496 S13:  -0.2003                       
REMARK   3      S21:  -0.5509 S22:   0.0720 S23:   0.6134                       
REMARK   3      S31:   0.2313 S32:  -0.3482 S33:  -0.1169                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 6W4H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000247613.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAR-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : DIAMOND(111)                       
REMARK 200  OPTICS                         : C(111)                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 77886                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : 0.06000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.76500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.76500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3R24                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5.3 MG/ML 1:1 NSP16/NSP10 IN 0.15 M      
REMARK 280  SODIUM CHLORIDE, 0.01 M TRIS, PH 7.5, 2 MM SAM, 1 MM TCEP, 5%       
REMARK 280  GLYCEROL AGAINST COMPAS SCREEN A7 (0.2 M CALCIUM ACETATE, 0.1 M     
REMARK 280  HEPES, PH 7.5, 18% W/V PEG 8000), CRYOPROTECTANT: 1:1 SCREEN +      
REMARK 280  50% SUCROSE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       17.31400            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       34.62800            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       34.62800            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       17.31400            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A  6796                                                      
REMARK 465     ASN A  6797                                                      
REMARK 465     SER B  4251                                                      
REMARK 465     ASN B  4252                                                      
REMARK 465     ALA B  4253                                                      
REMARK 465     ALA B  4254                                                      
REMARK 465     GLY B  4255                                                      
REMARK 465     ASN B  4256                                                      
REMARK 465     ALA B  4257                                                      
REMARK 465     THR B  4258                                                      
REMARK 465     GLU B  4259                                                      
REMARK 465     VAL B  4260                                                      
REMARK 465     PRO B  4261                                                      
REMARK 465     ALA B  4262                                                      
REMARK 465     ASN B  4263                                                      
REMARK 465     SER B  4264                                                      
REMARK 465     THR B  4265                                                      
REMARK 465     VAL B  4266                                                      
REMARK 465     LEU B  4267                                                      
REMARK 465     SER B  4268                                                      
REMARK 465     PHE B  4269                                                      
REMARK 465     CYS B  4270                                                      
REMARK 465     ARG B  4387                                                      
REMARK 465     GLU B  4388                                                      
REMARK 465     PRO B  4389                                                      
REMARK 465     MET B  4390                                                      
REMARK 465     LEU B  4391                                                      
REMARK 465     GLN B  4392                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A6945     -109.86   -100.79                                   
REMARK 500    GLU A6945     -108.41    -99.92                                   
REMARK 500    ASN A7008       87.84     73.73                                   
REMARK 500    ASP B4275       79.68   -107.97                                   
REMARK 500    ASN B4338      154.34    179.41                                   
REMARK 500    LYS B4340      -15.07     84.03                                   
REMARK 500    TYR B4379       46.38   -141.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B4401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B4327   SG                                                     
REMARK 620 2 CYS B4330   SG  114.5                                              
REMARK 620 3 HIS B4336   NE2 104.9 111.6                                        
REMARK 620 4 CYS B4343   SG  110.4 114.0 100.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B4402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B4370   SG                                                     
REMARK 620 2 CYS B4373   SG  105.7                                              
REMARK 620 3 CYS B4381   SG  102.9 111.5                                        
REMARK 620 4 CYS B4383   SG  110.8 117.2 107.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: CSGID-IDP51000   RELATED DB: TARGETTRACK                 
REMARK 900 RELATED ID: SCGID-IDP51000   RELATED DB: TARGETTRACK                 
DBREF  6W4H A 6799  7096  UNP    P0DTD1   R1AB_SARS2    6799   7096             
DBREF  6W4H B 4254  4392  UNP    P0DTD1   R1AB_SARS2    4254   4392             
SEQADV 6W4H SER A 6796  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6W4H ASN A 6797  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6W4H ALA A 6798  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6W4H SER B 4251  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6W4H ASN B 4252  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6W4H ALA B 4253  UNP  P0DTD1              EXPRESSION TAG                 
SEQRES   1 A  301  SER ASN ALA SER SER GLN ALA TRP GLN PRO GLY VAL ALA          
SEQRES   2 A  301  MET PRO ASN LEU TYR LYS MET GLN ARG MET LEU LEU GLU          
SEQRES   3 A  301  LYS CYS ASP LEU GLN ASN TYR GLY ASP SER ALA THR LEU          
SEQRES   4 A  301  PRO LYS GLY ILE MET MET ASN VAL ALA LYS TYR THR GLN          
SEQRES   5 A  301  LEU CYS GLN TYR LEU ASN THR LEU THR LEU ALA VAL PRO          
SEQRES   6 A  301  TYR ASN MET ARG VAL ILE HIS PHE GLY ALA GLY SER ASP          
SEQRES   7 A  301  LYS GLY VAL ALA PRO GLY THR ALA VAL LEU ARG GLN TRP          
SEQRES   8 A  301  LEU PRO THR GLY THR LEU LEU VAL ASP SER ASP LEU ASN          
SEQRES   9 A  301  ASP PHE VAL SER ASP ALA ASP SER THR LEU ILE GLY ASP          
SEQRES  10 A  301  CYS ALA THR VAL HIS THR ALA ASN LYS TRP ASP LEU ILE          
SEQRES  11 A  301  ILE SER ASP MET TYR ASP PRO LYS THR LYS ASN VAL THR          
SEQRES  12 A  301  LYS GLU ASN ASP SER LYS GLU GLY PHE PHE THR TYR ILE          
SEQRES  13 A  301  CYS GLY PHE ILE GLN GLN LYS LEU ALA LEU GLY GLY SER          
SEQRES  14 A  301  VAL ALA ILE LYS ILE THR GLU HIS SER TRP ASN ALA ASP          
SEQRES  15 A  301  LEU TYR LYS LEU MET GLY HIS PHE ALA TRP TRP THR ALA          
SEQRES  16 A  301  PHE VAL THR ASN VAL ASN ALA SER SER SER GLU ALA PHE          
SEQRES  17 A  301  LEU ILE GLY CYS ASN TYR LEU GLY LYS PRO ARG GLU GLN          
SEQRES  18 A  301  ILE ASP GLY TYR VAL MET HIS ALA ASN TYR ILE PHE TRP          
SEQRES  19 A  301  ARG ASN THR ASN PRO ILE GLN LEU SER SER TYR SER LEU          
SEQRES  20 A  301  PHE ASP MET SER LYS PHE PRO LEU LYS LEU ARG GLY THR          
SEQRES  21 A  301  ALA VAL MET SER LEU LYS GLU GLY GLN ILE ASN ASP MET          
SEQRES  22 A  301  ILE LEU SER LEU LEU SER LYS GLY ARG LEU ILE ILE ARG          
SEQRES  23 A  301  GLU ASN ASN ARG VAL VAL ILE SER SER ASP VAL LEU VAL          
SEQRES  24 A  301  ASN ASN                                                      
SEQRES   1 B  142  SER ASN ALA ALA GLY ASN ALA THR GLU VAL PRO ALA ASN          
SEQRES   2 B  142  SER THR VAL LEU SER PHE CYS ALA PHE ALA VAL ASP ALA          
SEQRES   3 B  142  ALA LYS ALA TYR LYS ASP TYR LEU ALA SER GLY GLY GLN          
SEQRES   4 B  142  PRO ILE THR ASN CYS VAL LYS MET LEU CYS THR HIS THR          
SEQRES   5 B  142  GLY THR GLY GLN ALA ILE THR VAL THR PRO GLU ALA ASN          
SEQRES   6 B  142  MET ASP GLN GLU SER PHE GLY GLY ALA SER CYS CYS LEU          
SEQRES   7 B  142  TYR CYS ARG CYS HIS ILE ASP HIS PRO ASN PRO LYS GLY          
SEQRES   8 B  142  PHE CYS ASP LEU LYS GLY LYS TYR VAL GLN ILE PRO THR          
SEQRES   9 B  142  THR CYS ALA ASN ASP PRO VAL GLY PHE THR LEU LYS ASN          
SEQRES  10 B  142  THR VAL CYS THR VAL CYS GLY MET TRP LYS GLY TYR GLY          
SEQRES  11 B  142  CYS SER CYS ASP GLN LEU ARG GLU PRO MET LEU GLN              
HET    SO3  A7101       4                                                       
HET    SAM  A7102      27                                                       
HET    ACT  A7103       4                                                       
HET    ACT  A7104       4                                                       
HET    BDF  A7105      12                                                       
HET     ZN  B4401       1                                                       
HET     ZN  B4402       1                                                       
HET    BDF  B4403      12                                                       
HETNAM     SO3 SULFITE ION                                                      
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     ACT ACETATE ION                                                      
HETNAM     BDF BETA-D-FRUCTOPYRANOSE                                            
HETNAM      ZN ZINC ION                                                         
FORMUL   3  SO3    O3 S 2-                                                      
FORMUL   4  SAM    C15 H22 N6 O5 S                                              
FORMUL   5  ACT    2(C2 H3 O2 1-)                                               
FORMUL   7  BDF    2(C6 H12 O6)                                                 
FORMUL   8   ZN    2(ZN 2+)                                                     
FORMUL  11  HOH   *442(H2 O)                                                    
HELIX    1 AA1 SER A 6799  GLN A 6804  5                                   6    
HELIX    2 AA2 PRO A 6810  MET A 6815  1                                   6    
HELIX    3 AA3 MET A 6839  ASN A 6853  1                                  15    
HELIX    4 AA4 ALA A 6877  LEU A 6887  1                                  11    
HELIX    5 AA5 ASP A 6912  ALA A 6914  5                                   3    
HELIX    6 AA6 ASP A 6931  LYS A 6935  5                                   5    
HELIX    7 AA7 GLY A 6946  LYS A 6958  1                                  13    
HELIX    8 AA8 ASN A 6975  GLY A 6983  1                                   9    
HELIX    9 AA9 ASP A 7018  ASN A 7033  1                                  16    
HELIX   10 AB1 SER A 7039  ASP A 7044  5                                   6    
HELIX   11 AB2 LYS A 7061  ILE A 7065  5                                   5    
HELIX   12 AB3 ASN A 7066  LYS A 7075  1                                  10    
HELIX   13 AB4 ASP B 4275  SER B 4286  1                                  12    
HELIX   14 AB5 ALA B 4324  CYS B 4326  5                                   3    
HELIX   15 AB6 CYS B 4327  HIS B 4333  1                                   7    
HELIX   16 AB7 ASN B 4338  PHE B 4342  5                                   5    
HELIX   17 AB8 THR B 4355  ALA B 4357  5                                   3    
HELIX   18 AB9 ASP B 4359  ASN B 4367  1                                   9    
SHEET    1 AA1 8 GLY A6806  ALA A6808  0                                        
SHEET    2 AA1 8 PHE A6985  THR A6993 -1  O  VAL A6992   N  VAL A6807           
SHEET    3 AA1 8 ALA A7002  TYR A7009 -1  O  CYS A7007   N  TRP A6987           
SHEET    4 AA1 8 LEU A6959  ILE A6969 -1  N  ILE A6967   O  LEU A7004           
SHEET    5 AA1 8 TRP A6922  SER A6927  1  N  TRP A6922   O  ALA A6960           
SHEET    6 AA1 8 ARG A6864  PHE A6868  1  N  PHE A6868   O  ILE A6926           
SHEET    7 AA1 8 LEU A6892  ASP A6897  1  O  LEU A6892   N  VAL A6865           
SHEET    8 AA1 8 SER A6907  ILE A6910  1  O  LEU A6909   N  ASP A6895           
SHEET    1 AA2 2 VAL A6916  THR A6918  0                                        
SHEET    2 AA2 2 ILE A7088  SER A7090 -1  O  SER A7089   N  HIS A6917           
SHEET    1 AA3 2 ALA A7056  MET A7058  0                                        
SHEET    2 AA3 2 LEU A7078  ILE A7080  1  O  ILE A7079   N  MET A7058           
SHEET    1 AA4 3 ILE B4308  THR B4309  0                                        
SHEET    2 AA4 3 TYR B4349  PRO B4353 -1  O  TYR B4349   N  THR B4309           
SHEET    3 AA4 3 GLN B4318  GLY B4322 -1  N  GLU B4319   O  ILE B4352           
SHEET    1 AA5 2 TRP B4376  LYS B4377  0                                        
SHEET    2 AA5 2 GLY B4380  CYS B4381  1  O  CYS B4381   N  TRP B4376           
LINK         SG  CYS B4327                ZN    ZN B4401     1555   1555  2.30  
LINK         SG  CYS B4330                ZN    ZN B4401     1555   1555  2.32  
LINK         NE2 HIS B4336                ZN    ZN B4401     1555   1555  2.01  
LINK         SG  CYS B4343                ZN    ZN B4401     1555   1555  2.32  
LINK         SG  CYS B4370                ZN    ZN B4402     1555   1555  2.32  
LINK         SG  CYS B4373                ZN    ZN B4402     1555   1555  2.33  
LINK         SG  CYS B4381                ZN    ZN B4402     1555   1555  2.33  
LINK         SG  CYS B4383                ZN    ZN B4402     1555   1555  2.33  
CRYST1  167.740  167.740   51.942  90.00  90.00 120.00 P 31 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005962  0.003442  0.000000        0.00000                         
SCALE2      0.000000  0.006884  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019252        0.00000                         
ATOM      1  N   ALA A6798      78.228  47.055  27.186  1.00 69.03           N  
ANISOU    1  N   ALA A6798     8734   7385  10105    700   -466   -340       N  
ATOM      2  CA  ALA A6798      78.868  48.293  27.743  1.00 69.84           C  
ANISOU    2  CA  ALA A6798     8891   7246  10398    730   -514   -417       C  
ATOM      3  C   ALA A6798      80.391  48.218  27.568  1.00 67.02           C  
ANISOU    3  C   ALA A6798     8622   6818  10024    566   -488   -339       C  
ATOM      4  O   ALA A6798      80.957  49.127  26.929  1.00 70.05           O  
ANISOU    4  O   ALA A6798     9073   7001  10541    526   -552   -212       O  
ATOM      5  CB  ALA A6798      78.486  48.468  29.194  1.00 70.45           C  
ANISOU    5  CB  ALA A6798     8907   7356  10503    826   -482   -677       C  
ATOM      6  N   SER A6799      81.018  47.176  28.129  1.00 63.31           N  
ANISOU    6  N   SER A6799     8145   6508   9401    472   -400   -407       N  
ATOM      7  CA  SER A6799      82.489  46.961  28.038  1.00 59.29           C  
ANISOU    7  CA  SER A6799     7692   5971   8862    323   -368   -354       C  
ATOM      8  C   SER A6799      82.897  46.725  26.577  1.00 54.21           C  
ANISOU    8  C   SER A6799     7088   5344   8165    229   -370   -120       C  
ATOM      9  O   SER A6799      82.172  45.996  25.887  1.00 49.75           O  
ANISOU    9  O   SER A6799     6499   4921   7482    249   -357    -43       O  
ATOM     10  CB  SER A6799      82.902  45.798  28.915  1.00 61.81           C  
ANISOU   10  CB  SER A6799     7987   6474   9023    272   -287   -468       C  
ATOM     11  OG  SER A6799      84.296  45.541  28.812  1.00 64.28           O  
ANISOU   11  OG  SER A6799     8336   6778   9308    145   -262   -423       O  
ATOM     12  N   SER A6800      84.017  47.313  26.132  1.00 50.71           N  
ANISOU   12  N   SER A6800     6696   4773   7797    123   -385    -18       N  
ATOM     13  CA  SER A6800      84.516  47.129  24.737  1.00 48.15           C  
ANISOU   13  CA  SER A6800     6404   4489   7402     21   -373    205       C  
ATOM     14  C   SER A6800      84.720  45.634  24.444  1.00 42.54           C  
ANISOU   14  C   SER A6800     5666   4022   6473    -30   -288    206       C  
ATOM     15  O   SER A6800      84.446  45.178  23.293  1.00 41.45           O  
ANISOU   15  O   SER A6800     5535   3990   6223    -52   -281    347       O  
ATOM     16  CB  SER A6800      85.790  47.903  24.516  1.00 52.04           C  
ANISOU   16  CB  SER A6800     6934   4837   7999   -104   -381    290       C  
ATOM     17  OG  SER A6800      86.307  47.656  23.217  1.00 55.12           O  
ANISOU   17  OG  SER A6800     7342   5309   8290   -210   -350    499       O  
ATOM     18  N   GLN A6801      85.170  44.892  25.453  1.00 36.35           N  
ANISOU   18  N   GLN A6801     4857   3321   5631    -44   -235     51       N  
ATOM     19  CA  GLN A6801      85.385  43.429  25.326  1.00 32.80           C  
ANISOU   19  CA  GLN A6801     4390   3072   5000    -83   -165     33       C  
ATOM     20  C   GLN A6801      84.056  42.712  25.061  1.00 28.48           C  
ANISOU   20  C   GLN A6801     3820   2644   4357    -10   -169     31       C  
ATOM     21  O   GLN A6801      84.106  41.593  24.544  1.00 26.22           O  
ANISOU   21  O   GLN A6801     3531   2499   3931    -48   -130     58       O  
ATOM     22  CB  GLN A6801      86.011  42.879  26.607  1.00 33.50           C  
ANISOU   22  CB  GLN A6801     4460   3202   5064    -94   -130   -126       C  
ATOM     23  CG  GLN A6801      87.392  43.439  26.883  1.00 37.89           C  
ANISOU   23  CG  GLN A6801     5022   3672   5703   -178   -129   -137       C  
ATOM     24  CD  GLN A6801      88.004  42.876  28.142  1.00 38.55           C  
ANISOU   24  CD  GLN A6801     5083   3813   5750   -182   -110   -291       C  
ATOM     25  OE1 GLN A6801      89.220  42.732  28.236  1.00 44.29           O  
ANISOU   25  OE1 GLN A6801     5794   4554   6477   -257    -93   -296       O  
ATOM     26  NE2 GLN A6801      87.165  42.540  29.112  1.00 38.88           N  
ANISOU   26  NE2 GLN A6801     5116   3906   5750   -102   -112   -411       N  
ATOM     27  N   ALA A6802      82.923  43.340  25.392  1.00 27.50           N  
ANISOU   27  N   ALA A6802     3671   2464   4313     92   -218     -9       N  
ATOM     28  CA  ALA A6802      81.597  42.687  25.247  1.00 26.67           C  
ANISOU   28  CA  ALA A6802     3519   2486   4128    158   -223    -26       C  
ATOM     29  C   ALA A6802      81.266  42.397  23.777  1.00 25.98           C  
ANISOU   29  C   ALA A6802     3441   2469   3957    132   -248    132       C  
ATOM     30  O   ALA A6802      80.425  41.505  23.540  1.00 25.04           O  
ANISOU   30  O   ALA A6802     3285   2491   3735    145   -242    117       O  
ATOM     31  CB  ALA A6802      80.525  43.540  25.877  1.00 27.48           C  
ANISOU   31  CB  ALA A6802     3574   2519   4347    283   -271   -109       C  
ATOM     32  N   TRP A6803      81.892  43.111  22.836  1.00 26.34           N  
ANISOU   32  N   TRP A6803     3535   2432   4039     87   -276    280       N  
ATOM     33  CA  TRP A6803      81.601  42.899  21.391  1.00 27.40           C  
ANISOU   33  CA  TRP A6803     3683   2656   4070     61   -304    440       C  
ATOM     34  C   TRP A6803      82.545  41.848  20.796  1.00 26.04           C  
ANISOU   34  C   TRP A6803     3532   2619   3739    -45   -232    463       C  
ATOM     35  O   TRP A6803      82.341  41.447  19.636  1.00 27.84           O  
ANISOU   35  O   TRP A6803     3770   2964   3844    -72   -242    561       O  
ATOM     36  CB  TRP A6803      81.605  44.225  20.631  1.00 30.83           C  
ANISOU   36  CB  TRP A6803     4155   2947   4610     76   -380    611       C  
ATOM     37  CG  TRP A6803      80.385  45.028  20.960  1.00 32.47           C  
ANISOU   37  CG  TRP A6803     4329   3057   4950    213   -468    587       C  
ATOM     38  CD1 TRP A6803      79.173  44.933  20.352  1.00 33.93           C  
ANISOU   38  CD1 TRP A6803     4471   3325   5094    295   -534    639       C  
ATOM     39  CD2 TRP A6803      80.221  45.985  22.019  1.00 34.53           C  
ANISOU   39  CD2 TRP A6803     4580   3135   5402    299   -501    479       C  
ATOM     40  NE1 TRP A6803      78.271  45.773  20.939  1.00 35.18           N  
ANISOU   40  NE1 TRP A6803     4587   3368   5412    432   -604    578       N  
ATOM     41  CE2 TRP A6803      78.885  46.437  21.960  1.00 35.50           C  
ANISOU   41  CE2 TRP A6803     4652   3240   5597    441   -583    473       C  
ATOM     42  CE3 TRP A6803      81.063  46.508  23.005  1.00 35.56           C  
ANISOU   42  CE3 TRP A6803     4736   3124   5652    273   -475    374       C  
ATOM     43  CZ2 TRP A6803      78.378  47.388  22.840  1.00 37.40           C  
ANISOU   43  CZ2 TRP A6803     4864   3321   6023    568   -633    358       C  
ATOM     44  CZ3 TRP A6803      80.561  47.449  23.875  1.00 37.31           C  
ANISOU   44  CZ3 TRP A6803     4940   3186   6050    388   -529    257       C  
ATOM     45  CH2 TRP A6803      79.238  47.887  23.787  1.00 38.34           C  
ANISOU   45  CH2 TRP A6803     5020   3296   6251    538   -603    246       C  
ATOM     46  N  AGLN A6804      83.534  41.407  21.571  0.60 24.33           N  
ANISOU   46  N  AGLN A6804     3321   2398   3526    -95   -166    364       N  
ATOM     47  N  BGLN A6804      83.532  41.411  21.583  0.40 24.26           N  
ANISOU   47  N  BGLN A6804     3311   2387   3517    -94   -166    362       N  
ATOM     48  CA AGLN A6804      84.469  40.353  21.100  0.60 23.52           C  
ANISOU   48  CA AGLN A6804     3227   2421   3289   -175    -98    357       C  
ATOM     49  CA BGLN A6804      84.483  40.351  21.158  0.40 23.16           C  
ANISOU   49  CA BGLN A6804     3181   2372   3247   -174    -97    352       C  
ATOM     50  C  AGLN A6804      83.845  38.998  21.430  0.60 21.57           C  
ANISOU   50  C  AGLN A6804     2962   2291   2943   -152    -80    244       C  
ATOM     51  C  BGLN A6804      83.837  38.995  21.431  0.40 21.49           C  
ANISOU   51  C  BGLN A6804     2951   2281   2933   -151    -81    244       C  
ATOM     52  O  AGLN A6804      82.866  38.928  22.170  0.60 20.54           O  
ANISOU   52  O  AGLN A6804     2804   2148   2850    -93   -106    172       O  
ATOM     53  O  BGLN A6804      82.838  38.923  22.145  0.40 20.70           O  
ANISOU   53  O  BGLN A6804     2825   2171   2869    -93   -107    174       O  
ATOM     54  CB AGLN A6804      85.847  40.546  21.742  0.60 23.96           C  
ANISOU   54  CB AGLN A6804     3284   2414   3404   -232    -50    312       C  
ATOM     55  CB BGLN A6804      85.787  40.458  21.953  0.40 22.98           C  
ANISOU   55  CB BGLN A6804     3157   2288   3285   -223    -50    287       C  
ATOM     56  CG AGLN A6804      86.540  41.833  21.308  0.60 26.39           C  
ANISOU   56  CG AGLN A6804     3607   2605   3811   -288    -66    439       C  
ATOM     57  CG BGLN A6804      86.437  41.834  21.902  0.40 24.64           C  
ANISOU   57  CG BGLN A6804     3381   2352   3630   -263    -72    373       C  
ATOM     58  CD AGLN A6804      86.791  41.869  19.820  0.60 28.04           C  
ANISOU   58  CD AGLN A6804     3832   2909   3913   -351    -51    605       C  
ATOM     59  CD BGLN A6804      87.676  41.910  22.760  0.40 24.63           C  
ANISOU   59  CD BGLN A6804     3363   2303   3692   -317    -36    289       C  
ATOM     60  OE1AGLN A6804      87.231  40.889  19.221  0.60 29.55           O  
ANISOU   60  OE1AGLN A6804     4010   3259   3956   -386      6    591       O  
ATOM     61  OE1BGLN A6804      88.074  40.940  23.405  0.40 24.51           O  
ANISOU   61  OE1BGLN A6804     3327   2367   3617   -312      1    173       O  
ATOM     62  NE2AGLN A6804      86.524  43.011  19.211  0.60 30.67           N  
ANISOU   62  NE2AGLN A6804     4193   3144   4316   -362   -105    764       N  
ATOM     63  NE2BGLN A6804      88.296  43.077  22.783  0.40 25.98           N  
ANISOU   63  NE2BGLN A6804     3540   2336   3993   -371    -57    352       N  
ATOM     64  N   PRO A6805      84.343  37.886  20.845  1.00 20.76           N  
ANISOU   64  N   PRO A6805     2868   2304   2713   -198    -39    226       N  
ATOM     65  CA  PRO A6805      83.818  36.558  21.176  1.00 19.92           C  
ANISOU   65  CA  PRO A6805     2756   2277   2533   -190    -30    122       C  
ATOM     66  C   PRO A6805      84.213  36.140  22.603  1.00 18.67           C  
ANISOU   66  C   PRO A6805     2595   2067   2429   -182     -3      9       C  
ATOM     67  O   PRO A6805      83.589  35.265  23.177  1.00 18.49           O  
ANISOU   67  O   PRO A6805     2567   2079   2379   -174     -5    -60       O  
ATOM     68  CB  PRO A6805      84.469  35.645  20.127  1.00 19.89           C  
ANISOU   68  CB  PRO A6805     2771   2383   2400   -235      1    125       C  
ATOM     69  CG  PRO A6805      85.723  36.390  19.697  1.00 20.99           C  
ANISOU   69  CG  PRO A6805     2914   2507   2554   -274     41    199       C  
ATOM     70  CD  PRO A6805      85.359  37.859  19.781  1.00 21.43           C  
ANISOU   70  CD  PRO A6805     2968   2455   2718   -261      0    304       C  
ATOM     71  N   GLY A6806      85.239  36.791  23.146  1.00 19.06           N  
ANISOU   71  N   GLY A6806     2645   2041   2552   -193     17      3       N  
ATOM     72  CA  GLY A6806      85.731  36.478  24.497  1.00 18.78           C  
ANISOU   72  CA  GLY A6806     2608   1971   2557   -185     33    -97       C  
ATOM     73  C   GLY A6806      86.968  37.285  24.824  1.00 19.29           C  
ANISOU   73  C   GLY A6806     2665   1965   2700   -210     45    -96       C  
ATOM     74  O   GLY A6806      87.266  38.236  24.081  1.00 19.97           O  
ANISOU   74  O   GLY A6806     2749   2008   2831   -238     40     -6       O  
ATOM     75  N   VAL A6807      87.687  36.882  25.868  1.00 18.96           N  
ANISOU   75  N   VAL A6807     2617   1917   2670   -211     55   -182       N  
ATOM     76  CA  VAL A6807      88.874  37.645  26.334  1.00 19.71           C  
ANISOU   76  CA  VAL A6807     2690   1950   2846   -241     55   -201       C  
ATOM     77  C   VAL A6807      90.054  36.689  26.493  1.00 18.93           C  
ANISOU   77  C   VAL A6807     2574   1917   2701   -259     80   -245       C  
ATOM     78  O   VAL A6807      89.888  35.622  27.120  1.00 18.99           O  
ANISOU   78  O   VAL A6807     2598   1966   2651   -226     74   -305       O  
ATOM     79  CB  VAL A6807      88.552  38.376  27.652  1.00 20.61           C  
ANISOU   79  CB  VAL A6807     2801   1988   3040   -209     21   -286       C  
ATOM     80  CG1 VAL A6807      89.703  39.257  28.104  1.00 21.69           C  
ANISOU   80  CG1 VAL A6807     2915   2051   3275   -250      7   -317       C  
ATOM     81  CG2 VAL A6807      87.281  39.197  27.529  1.00 21.67           C  
ANISOU   81  CG2 VAL A6807     2943   2065   3225   -164     -5   -265       C  
ATOM     82  N   ALA A6808      91.188  37.064  25.910  1.00 19.13           N  
ANISOU   82  N   ALA A6808     2561   1953   2753   -309    105   -208       N  
ATOM     83  CA  ALA A6808      92.444  36.298  26.028  1.00 19.52           C  
ANISOU   83  CA  ALA A6808     2568   2071   2777   -316    127   -257       C  
ATOM     84  C   ALA A6808      93.264  36.865  27.193  1.00 19.69           C  
ANISOU   84  C   ALA A6808     2551   2043   2884   -331     95   -324       C  
ATOM     85  O   ALA A6808      93.267  38.095  27.390  1.00 20.14           O  
ANISOU   85  O   ALA A6808     2601   2014   3035   -372     75   -307       O  
ATOM     86  CB  ALA A6808      93.216  36.383  24.740  1.00 20.56           C  
ANISOU   86  CB  ALA A6808     2656   2275   2878   -366    182   -188       C  
ATOM     87  N   MET A6809      93.939  35.989  27.924  1.00 19.72           N  
ANISOU   87  N   MET A6809     2534   2095   2861   -296     78   -399       N  
ATOM     88  CA  MET A6809      94.798  36.388  29.066  1.00 20.39           C  
ANISOU   88  CA  MET A6809     2576   2163   3008   -306     35   -473       C  
ATOM     89  C   MET A6809      95.847  37.394  28.586  1.00 22.04           C  
ANISOU   89  C   MET A6809     2708   2360   3307   -391     52   -445       C  
ATOM     90  O   MET A6809      96.656  37.071  27.717  1.00 22.81           O  
ANISOU   90  O   MET A6809     2745   2536   3386   -417    100   -410       O  
ATOM     91  CB  MET A6809      95.481  35.141  29.617  1.00 20.45           C  
ANISOU   91  CB  MET A6809     2565   2243   2961   -249     12   -529       C  
ATOM     92  CG  MET A6809      96.320  35.367  30.840  1.00 20.96           C  
ANISOU   92  CG  MET A6809     2584   2315   3063   -247    -48   -606       C  
ATOM     93  SD  MET A6809      96.899  33.768  31.398  1.00 21.17           S  
ANISOU   93  SD  MET A6809     2609   2414   3019   -157    -90   -641       S  
ATOM     94  CE  MET A6809      97.969  34.279  32.746  1.00 22.55           C  
ANISOU   94  CE  MET A6809     2713   2618   3236   -166   -174   -724       C  
ATOM     95  N   PRO A6810      95.847  38.648  29.093  1.00 23.26           N  
ANISOU   95  N   PRO A6810     2858   2415   3563   -443     17   -461       N  
ATOM     96  CA  PRO A6810      96.829  39.646  28.663  1.00 25.08           C  
ANISOU   96  CA  PRO A6810     3016   2614   3896   -549     28   -422       C  
ATOM     97  C   PRO A6810      98.272  39.200  28.953  1.00 25.65           C  
ANISOU   97  C   PRO A6810     2980   2788   3975   -573     25   -479       C  
ATOM     98  O   PRO A6810      98.508  38.567  29.963  1.00 25.31           O  
ANISOU   98  O   PRO A6810     2929   2787   3901   -509    -23   -574       O  
ATOM     99  CB  PRO A6810      96.436  40.908  29.438  1.00 26.12           C  
ANISOU   99  CB  PRO A6810     3182   2597   4145   -579    -33   -468       C  
ATOM    100  CG  PRO A6810      94.977  40.700  29.770  1.00 25.12           C  
ANISOU  100  CG  PRO A6810     3146   2433   3963   -485    -47   -488       C  
ATOM    101  CD  PRO A6810      94.853  39.213  30.020  1.00 23.69           C  
ANISOU  101  CD  PRO A6810     2975   2380   3646   -408    -30   -517       C  
ATOM    102  N   ASN A6811      99.189  39.553  28.052  1.00 27.02           N  
ANISOU  102  N   ASN A6811     3067   3013   4187   -664     78   -411       N  
ATOM    103  CA  ASN A6811     100.618  39.144  28.128  1.00 27.46           C  
ANISOU  103  CA  ASN A6811     2987   3193   4253   -688     89   -460       C  
ATOM    104  C   ASN A6811     101.230  39.483  29.494  1.00 26.80           C  
ANISOU  104  C   ASN A6811     2857   3079   4246   -698     -3   -577       C  
ATOM    105  O   ASN A6811     101.989  38.637  30.014  1.00 26.54           O  
ANISOU  105  O   ASN A6811     2751   3152   4177   -635    -32   -654       O  
ATOM    106  CB  ASN A6811     101.430  39.754  26.983  1.00 29.82           C  
ANISOU  106  CB  ASN A6811     3187   3550   4590   -816    168   -359       C  
ATOM    107  CG  ASN A6811     101.146  39.102  25.645  1.00 30.61           C  
ANISOU  107  CG  ASN A6811     3300   3758   4571   -789    263   -273       C  
ATOM    108  OD1 ASN A6811     100.514  38.049  25.587  1.00 30.82           O  
ANISOU  108  OD1 ASN A6811     3392   3820   4497   -671    264   -310       O  
ATOM    109  ND2 ASN A6811     101.634  39.699  24.570  1.00 32.73           N  
ANISOU  109  ND2 ASN A6811     3504   4087   4844   -907    340   -160       N  
ATOM    110  N   LEU A6812     100.913  40.641  30.079  1.00 26.48           N  
ANISOU  110  N   LEU A6812     2855   2899   4305   -762    -57   -600       N  
ATOM    111  CA  LEU A6812     101.612  40.982  31.350  1.00 26.74           C  
ANISOU  111  CA  LEU A6812     2833   2925   4402   -782   -151   -731       C  
ATOM    112  C   LEU A6812     101.239  39.976  32.447  1.00 25.66           C  
ANISOU  112  C   LEU A6812     2746   2849   4153   -644   -210   -827       C  
ATOM    113  O   LEU A6812     102.108  39.697  33.288  1.00 26.21           O  
ANISOU  113  O   LEU A6812     2739   2998   4221   -630   -277   -916       O  
ATOM    114  CB  LEU A6812     101.307  42.427  31.764  1.00 27.61           C  
ANISOU  114  CB  LEU A6812     2983   2859   4647   -872   -205   -762       C  
ATOM    115  CG  LEU A6812     102.124  42.947  32.945  1.00 28.84           C  
ANISOU  115  CG  LEU A6812     3070   3006   4881   -920   -305   -907       C  
ATOM    116  CD1 LEU A6812     103.624  42.820  32.690  1.00 29.67           C  
ANISOU  116  CD1 LEU A6812     3006   3234   5032  -1011   -298   -904       C  
ATOM    117  CD2 LEU A6812     101.771  44.391  33.251  1.00 30.24           C  
ANISOU  117  CD2 LEU A6812     3299   2982   5208  -1007   -359   -951       C  
ATOM    118  N   TYR A6813     100.020  39.419  32.420  1.00 24.69           N  
ANISOU  118  N   TYR A6813     2741   2702   3938   -553   -189   -798       N  
ATOM    119  CA  TYR A6813      99.616  38.418  33.448  1.00 24.20           C  
ANISOU  119  CA  TYR A6813     2733   2700   3761   -440   -239   -861       C  
ATOM    120  C   TYR A6813     100.439  37.134  33.277  1.00 23.91           C  
ANISOU  120  C   TYR A6813     2634   2787   3662   -375   -237   -849       C  
ATOM    121  O   TYR A6813     100.756  36.490  34.284  1.00 23.81           O  
ANISOU  121  O   TYR A6813     2616   2835   3594   -310   -311   -908       O  
ATOM    122  CB  TYR A6813      98.109  38.146  33.401  1.00 23.54           C  
ANISOU  122  CB  TYR A6813     2773   2566   3602   -379   -209   -824       C  
ATOM    123  CG  TYR A6813      97.280  39.289  33.925  1.00 23.99           C  
ANISOU  123  CG  TYR A6813     2884   2516   3712   -401   -233   -876       C  
ATOM    124  CD1 TYR A6813      97.102  39.467  35.286  1.00 25.14           C  
ANISOU  124  CD1 TYR A6813     3051   2679   3821   -369   -301   -994       C  
ATOM    125  CD2 TYR A6813      96.712  40.216  33.070  1.00 24.62           C  
ANISOU  125  CD2 TYR A6813     2991   2483   3878   -448   -195   -813       C  
ATOM    126  CE1 TYR A6813      96.367  40.530  35.785  1.00 25.74           C  
ANISOU  126  CE1 TYR A6813     3169   2661   3950   -374   -323  -1072       C  
ATOM    127  CE2 TYR A6813      95.972  41.284  33.552  1.00 25.85           C  
ANISOU  127  CE2 TYR A6813     3193   2523   4104   -449   -227   -875       C  
ATOM    128  CZ  TYR A6813      95.796  41.439  34.916  1.00 26.15           C  
ANISOU  128  CZ  TYR A6813     3246   2579   4109   -408   -288  -1017       C  
ATOM    129  OH  TYR A6813      95.075  42.491  35.407  1.00 27.44           O  
ANISOU  129  OH  TYR A6813     3448   2634   4344   -394   -318  -1107       O  
ATOM    130  N   LYS A6814     100.790  36.790  32.039  1.00 24.50           N  
ANISOU  130  N   LYS A6814     2661   2901   3744   -387   -160   -778       N  
ATOM    131  CA  LYS A6814     101.601  35.570  31.771  1.00 25.19           C  
ANISOU  131  CA  LYS A6814     2680   3101   3788   -308   -154   -787       C  
ATOM    132  C   LYS A6814     103.017  35.714  32.335  1.00 26.87           C  
ANISOU  132  C   LYS A6814     2747   3399   4062   -326   -214   -859       C  
ATOM    133  O   LYS A6814     103.648  34.674  32.599  1.00 27.51           O  
ANISOU  133  O   LYS A6814     2778   3563   4111   -228   -254   -892       O  
ATOM    134  CB  LYS A6814     101.723  35.335  30.264  1.00 26.09           C  
ANISOU  134  CB  LYS A6814     2759   3261   3893   -326    -49   -719       C  
ATOM    135  CG  LYS A6814     100.407  35.178  29.519  1.00 25.36           C  
ANISOU  135  CG  LYS A6814     2791   3106   3738   -314      6   -647       C  
ATOM    136  CD  LYS A6814     100.594  35.112  28.023  1.00 26.56           C  
ANISOU  136  CD  LYS A6814     2900   3325   3864   -347    105   -585       C  
ATOM    137  CE  LYS A6814      99.285  35.029  27.271  1.00 26.55           C  
ANISOU  137  CE  LYS A6814     3016   3273   3797   -341    145   -514       C  
ATOM    138  NZ  LYS A6814      99.487  35.191  25.813  1.00 28.08           N  
ANISOU  138  NZ  LYS A6814     3167   3547   3952   -392    239   -445       N  
ATOM    139  N   MET A6815     103.483  36.951  32.540  1.00 27.14           N  
ANISOU  139  N   MET A6815     2715   3405   4192   -446   -231   -884       N  
ATOM    140  CA  MET A6815     104.887  37.221  32.953  1.00 28.78           C  
ANISOU  140  CA  MET A6815     2756   3704   4474   -493   -284   -953       C  
ATOM    141  C   MET A6815     105.011  37.347  34.475  1.00 28.81           C  
ANISOU  141  C   MET A6815     2774   3706   4466   -465   -416  -1055       C  
ATOM    142  O   MET A6815     106.129  37.628  34.942  1.00 29.63           O  
ANISOU  142  O   MET A6815     2739   3886   4630   -508   -482  -1125       O  
ATOM    143  CB  MET A6815     105.378  38.516  32.300  1.00 30.28           C  
ANISOU  143  CB  MET A6815     2859   3860   4784   -665   -235   -920       C  
ATOM    144  CG  MET A6815     105.257  38.500  30.789  1.00 30.56           C  
ANISOU  144  CG  MET A6815     2881   3918   4809   -709   -103   -805       C  
ATOM    145  SD  MET A6815     105.781  40.056  30.045  1.00 32.85           S  
ANISOU  145  SD  MET A6815     3086   4157   5238   -932    -48   -726       S  
ATOM    146  CE  MET A6815     107.537  40.005  30.388  1.00 34.55           C  
ANISOU  146  CE  MET A6815     3058   4542   5528   -991    -81   -810       C  
ATOM    147  N   GLN A6816     103.928  37.105  35.218  1.00 27.44           N  
ANISOU  147  N   GLN A6816     2748   3471   4204   -398   -453  -1065       N  
ATOM    148  CA  GLN A6816     103.973  37.249  36.697  1.00 28.36           C  
ANISOU  148  CA  GLN A6816     2886   3611   4277   -373   -574  -1163       C  
ATOM    149  C   GLN A6816     104.446  35.941  37.341  1.00 29.40           C  
ANISOU  149  C   GLN A6816     2999   3856   4314   -245   -651  -1166       C  
ATOM    150  O   GLN A6816     104.695  34.955  36.611  1.00 28.42           O  
ANISOU  150  O   GLN A6816     2850   3767   4178   -171   -609  -1104       O  
ATOM    151  CB  GLN A6816     102.604  37.678  37.233  1.00 27.22           C  
ANISOU  151  CB  GLN A6816     2894   3372   4074   -367   -571  -1178       C  
ATOM    152  CG  GLN A6816     102.109  38.981  36.620  1.00 27.05           C  
ANISOU  152  CG  GLN A6816     2897   3215   4164   -474   -513  -1174       C  
ATOM    153  CD  GLN A6816     103.145  40.072  36.740  1.00 28.19           C  
ANISOU  153  CD  GLN A6816     2926   3338   4445   -596   -561  -1247       C  
ATOM    154  OE1 GLN A6816     103.623  40.383  37.830  1.00 29.32           O  
ANISOU  154  OE1 GLN A6816     3031   3521   4586   -608   -663  -1368       O  
ATOM    155  NE2 GLN A6816     103.499  40.667  35.610  1.00 27.86           N  
ANISOU  155  NE2 GLN A6816     2826   3240   4520   -699   -489  -1171       N  
ATOM    156  N   ARG A6817     104.605  35.964  38.663  1.00 31.22           N  
ANISOU  156  N   ARG A6817     3239   4142   4480   -219   -768  -1241       N  
ATOM    157  CA  ARG A6817     104.999  34.760  39.434  1.00 33.76           C  
ANISOU  157  CA  ARG A6817     3561   4564   4702    -95   -866  -1226       C  
ATOM    158  C   ARG A6817     104.085  34.714  40.658  1.00 33.42           C  
ANISOU  158  C   ARG A6817     3652   4529   4515    -67   -926  -1244       C  
ATOM    159  O   ARG A6817     104.572  34.842  41.792  1.00 34.27           O  
ANISOU  159  O   ARG A6817     3727   4731   4561    -57  -1045  -1317       O  
ATOM    160  CB  ARG A6817     106.495  34.785  39.763  1.00 38.03           C  
ANISOU  160  CB  ARG A6817     3922   5222   5303    -92   -965  -1295       C  
ATOM    161  CG  ARG A6817     107.000  33.467  40.327  1.00 42.16           C  
ANISOU  161  CG  ARG A6817     4431   5836   5749     55  -1068  -1257       C  
ATOM    162  CD  ARG A6817     108.505  33.381  40.472  1.00 46.66           C  
ANISOU  162  CD  ARG A6817     4800   6533   6394     80  -1162  -1319       C  
ATOM    163  NE  ARG A6817     108.860  32.058  40.966  1.00 50.95           N  
ANISOU  163  NE  ARG A6817     5351   7136   6869    246  -1267  -1266       N  
ATOM    164  CZ  ARG A6817     109.011  30.973  40.208  1.00 52.23           C  
ANISOU  164  CZ  ARG A6817     5506   7273   7064    363  -1229  -1200       C  
ATOM    165  NH1 ARG A6817     109.328  29.820  40.771  1.00 55.17           N  
ANISOU  165  NH1 ARG A6817     5898   7675   7389    516  -1348  -1151       N  
ATOM    166  NH2 ARG A6817     108.847  31.034  38.896  1.00 51.89           N  
ANISOU  166  NH2 ARG A6817     5442   7172   7100    332  -1081  -1185       N  
ATOM    167  N   MET A6818     102.785  34.567  40.401  1.00 31.83           N  
ANISOU  167  N   MET A6818     3587   4248   4258    -61   -841  -1182       N  
ATOM    168  CA  MET A6818     101.754  34.579  41.464  1.00 32.35           C  
ANISOU  168  CA  MET A6818     3774   4336   4179    -46   -866  -1196       C  
ATOM    169  C   MET A6818     101.684  33.221  42.163  1.00 32.84           C  
ANISOU  169  C   MET A6818     3901   4473   4102     51   -935  -1105       C  
ATOM    170  O   MET A6818     102.108  32.211  41.569  1.00 32.04           O  
ANISOU  170  O   MET A6818     3785   4353   4036    118   -937  -1020       O  
ATOM    171  CB  MET A6818     100.380  34.895  40.863  1.00 31.47           C  
ANISOU  171  CB  MET A6818     3764   4123   4070    -75   -747  -1158       C  
ATOM    172  CG  MET A6818     100.351  36.179  40.051  1.00 31.43           C  
ANISOU  172  CG  MET A6818     3714   4016   4212   -165   -682  -1212       C  
ATOM    173  SD  MET A6818     101.013  37.594  40.955  1.00 33.86           S  
ANISOU  173  SD  MET A6818     3947   4336   4579   -243   -771  -1388       S  
ATOM    174  CE  MET A6818      99.817  37.730  42.283  1.00 35.06           C  
ANISOU  174  CE  MET A6818     4215   4544   4563   -202   -794  -1466       C  
ATOM    175  N   LEU A6819     101.209  33.228  43.410  1.00 34.62           N  
ANISOU  175  N   LEU A6819     4195   4785   4174     59   -995  -1129       N  
ATOM    176  CA  LEU A6819     100.950  31.966  44.144  1.00 35.81           C  
ANISOU  176  CA  LEU A6819     4432   5000   4171    134  -1056  -1010       C  
ATOM    177  C   LEU A6819      99.501  31.577  43.850  1.00 33.07           C  
ANISOU  177  C   LEU A6819     4209   4589   3764    119   -947   -920       C  
ATOM    178  O   LEU A6819      98.687  32.493  43.596  1.00 30.85           O  
ANISOU  178  O   LEU A6819     3943   4271   3507     60   -856   -988       O  
ATOM    179  CB  LEU A6819     101.187  32.163  45.642  1.00 38.79           C  
ANISOU  179  CB  LEU A6819     4814   5534   4387    139  -1174  -1070       C  
ATOM    180  CG  LEU A6819     102.632  32.454  46.045  1.00 42.19           C  
ANISOU  180  CG  LEU A6819     5114   6050   4864    155  -1306  -1159       C  
ATOM    181  CD1 LEU A6819     102.741  32.610  47.551  1.00 44.60           C  
ANISOU  181  CD1 LEU A6819     5439   6529   4978    160  -1428  -1217       C  
ATOM    182  CD2 LEU A6819     103.573  31.361  45.556  1.00 43.18           C  
ANISOU  182  CD2 LEU A6819     5182   6155   5066    246  -1368  -1056       C  
ATOM    183  N   LEU A6820      99.205  30.280  43.877  1.00 33.30           N  
ANISOU  183  N   LEU A6820     4319   4601   3731    169   -962   -774       N  
ATOM    184  CA  LEU A6820      97.840  29.803  43.547  1.00 32.97           C  
ANISOU  184  CA  LEU A6820     4384   4498   3642    141   -863   -679       C  
ATOM    185  C   LEU A6820      96.863  30.216  44.648  1.00 33.04           C  
ANISOU  185  C   LEU A6820     4451   4623   3479     95   -843   -701       C  
ATOM    186  O   LEU A6820      97.136  29.953  45.829  1.00 34.26           O  
ANISOU  186  O   LEU A6820     4626   4905   3484    111   -934   -681       O  
ATOM    187  CB  LEU A6820      97.850  28.280  43.376  1.00 34.42           C  
ANISOU  187  CB  LEU A6820     4641   4620   3816    197   -904   -520       C  
ATOM    188  CG  LEU A6820      96.501  27.660  43.013  1.00 34.45           C  
ANISOU  188  CG  LEU A6820     4749   4555   3783    154   -814   -415       C  
ATOM    189  CD1 LEU A6820      95.965  28.254  41.725  1.00 33.44           C  
ANISOU  189  CD1 LEU A6820     4592   4335   3778    117   -694   -475       C  
ATOM    190  CD2 LEU A6820      96.602  26.148  42.888  1.00 36.15           C  
ANISOU  190  CD2 LEU A6820     5043   4681   4010    203   -875   -265       C  
ATOM    191  N  AGLU A6821      95.763  30.862  44.251  0.50 31.93           N  
ANISOU  191  N  AGLU A6821     4327   4451   3353     45   -727   -744       N  
ATOM    192  N  BGLU A6821      95.756  30.847  44.254  0.50 31.98           N  
ANISOU  192  N  BGLU A6821     4334   4457   3358     45   -728   -742       N  
ATOM    193  CA AGLU A6821      94.686  31.288  45.182  0.50 32.92           C  
ANISOU  193  CA AGLU A6821     4490   4695   3321      8   -682   -784       C  
ATOM    194  CA BGLU A6821      94.700  31.271  45.207  0.50 33.02           C  
ANISOU  194  CA BGLU A6821     4504   4711   3330      8   -684   -782       C  
ATOM    195  C  AGLU A6821      93.382  30.625  44.744  0.50 31.41           C  
ANISOU  195  C  AGLU A6821     4366   4466   3101    -24   -584   -667       C  
ATOM    196  C  BGLU A6821      93.367  30.699  44.724  0.50 31.49           C  
ANISOU  196  C  BGLU A6821     4373   4475   3115    -24   -580   -676       C  
ATOM    197  O  AGLU A6821      93.344  30.073  43.622  0.50 29.06           O  
ANISOU  197  O  AGLU A6821     4081   4033   2927    -20   -552   -591       O  
ATOM    198  O  BGLU A6821      93.299  30.248  43.560  0.50 29.06           O  
ANISOU  198  O  BGLU A6821     4073   4030   2937    -22   -543   -609       O  
ATOM    199  CB AGLU A6821      94.450  32.800  45.146  0.50 33.92           C  
ANISOU  199  CB AGLU A6821     4559   4821   3507    -13   -635   -970       C  
ATOM    200  CB BGLU A6821      94.646  32.797  45.314  0.50 34.27           C  
ANISOU  200  CB BGLU A6821     4598   4883   3538     -9   -656   -978       C  
ATOM    201  CG AGLU A6821      95.672  33.645  45.440  0.50 35.94           C  
ANISOU  201  CG AGLU A6821     4737   5089   3827     -6   -725  -1109       C  
ATOM    202  CG BGLU A6821      95.907  33.413  45.898  0.50 36.34           C  
ANISOU  202  CG BGLU A6821     4793   5197   3815      2   -767  -1099       C  
ATOM    203  CD AGLU A6821      95.352  35.126  45.545  0.50 37.17           C  
ANISOU  203  CD AGLU A6821     4853   5225   4043    -32   -691  -1297       C  
ATOM    204  CD BGLU A6821      96.183  33.060  47.349  0.50 39.24           C  
ANISOU  204  CD BGLU A6821     5184   5755   3971     19   -864  -1102       C  
ATOM    205  OE1AGLU A6821      96.158  35.946  45.065  0.50 38.60           O  
ANISOU  205  OE1AGLU A6821     4967   5315   4382    -53   -722  -1387       O  
ATOM    206  OE1BGLU A6821      95.271  32.524  48.008  0.50 41.35           O  
ANISOU  206  OE1BGLU A6821     5520   6128   4061     10   -827  -1025       O  
ATOM    207  OE2AGLU A6821      94.297  35.456  46.121  0.50 39.58           O  
ANISOU  207  OE2AGLU A6821     5190   5607   4241    -32   -636  -1354       O  
ATOM    208  OE2BGLU A6821      97.313  33.321  47.819  0.50 41.15           O  
ANISOU  208  OE2BGLU A6821     5367   6050   4217     34   -977  -1178       O  
ATOM    209  N  ALYS A6822      92.359  30.678  45.595  0.50 31.61           N  
ANISOU  209  N  ALYS A6822     4423   4622   2963    -58   -536   -662       N  
ATOM    210  N  BLYS A6822      92.364  30.690  45.600  0.50 31.75           N  
ANISOU  210  N  BLYS A6822     4440   4640   2981    -58   -536   -664       N  
ATOM    211  CA ALYS A6822      91.038  30.152  45.180  0.50 31.31           C  
ANISOU  211  CA ALYS A6822     4425   4564   2906   -105   -435   -564       C  
ATOM    212  CA BLYS A6822      91.016  30.205  45.217  0.50 31.49           C  
ANISOU  212  CA BLYS A6822     4445   4593   2923   -105   -433   -571       C  
ATOM    213  C  ALYS A6822      90.483  31.119  44.134  0.50 29.94           C  
ANISOU  213  C  ALYS A6822     4199   4293   2884   -104   -348   -669       C  
ATOM    214  C  BLYS A6822      90.456  31.144  44.146  0.50 30.05           C  
ANISOU  214  C  BLYS A6822     4211   4308   2895   -105   -346   -672       C  
ATOM    215  O  ALYS A6822      90.759  32.336  44.245  0.50 29.11           O  
ANISOU  215  O  ALYS A6822     4038   4193   2828    -81   -351   -828       O  
ATOM    216  O  BLYS A6822      90.704  32.368  44.247  0.50 29.18           O  
ANISOU  216  O  BLYS A6822     4045   4204   2835    -82   -346   -832       O  
ATOM    217  CB ALYS A6822      90.077  30.037  46.367  0.50 33.31           C  
ANISOU  217  CB ALYS A6822     4702   5013   2940   -148   -393   -540       C  
ATOM    218  CB BLYS A6822      90.110  30.160  46.451  0.50 33.58           C  
ANISOU  218  CB BLYS A6822     4730   5060   2967   -145   -395   -559       C  
ATOM    219  CG ALYS A6822      90.535  29.122  47.493  0.50 35.68           C  
ANISOU  219  CG ALYS A6822     5064   5433   3059   -159   -481   -412       C  
ATOM    220  CG BLYS A6822      88.645  29.859  46.174  0.50 34.19           C  
ANISOU  220  CG BLYS A6822     4815   5162   3012   -204   -279   -491       C  
ATOM    221  CD ALYS A6822      89.510  28.987  48.598  0.50 37.89           C  
ANISOU  221  CD ALYS A6822     5362   5931   3103   -219   -420   -371       C  
ATOM    222  CD BLYS A6822      87.808  29.705  47.428  0.50 36.58           C  
ANISOU  222  CD BLYS A6822     5124   5696   3076   -254   -232   -463       C  
ATOM    223  CE ALYS A6822      89.095  30.319  49.188  0.50 39.21           C  
ANISOU  223  CE ALYS A6822     5455   6251   3190   -200   -360   -592       C  
ATOM    224  CE BLYS A6822      86.354  29.420  47.119  0.50 36.86           C  
ANISOU  224  CE BLYS A6822     5141   5771   3092   -322   -112   -400       C  
ATOM    225  NZ ALYS A6822      90.233  31.022  49.828  0.50 40.49           N  
ANISOU  225  NZ ALYS A6822     5591   6470   3320   -144   -465   -737       N  
ATOM    226  NZ BLYS A6822      86.209  28.232  46.245  0.50 36.19           N  
ANISOU  226  NZ BLYS A6822     5116   5524   3110   -374   -124   -215       N  
ATOM    227  N   CYS A6823      89.767  30.591  43.143  1.00 28.88           N  
ANISOU  227  N   CYS A6823     4084   4062   2826   -129   -287   -580       N  
ATOM    228  CA  CYS A6823      89.145  31.434  42.098  1.00 29.05           C  
ANISOU  228  CA  CYS A6823     4060   3997   2979   -127   -213   -653       C  
ATOM    229  C   CYS A6823      87.839  31.974  42.687  1.00 31.08           C  
ANISOU  229  C   CYS A6823     4288   4376   3141   -144   -134   -713       C  
ATOM    230  O   CYS A6823      87.043  31.164  43.217  1.00 32.73           O  
ANISOU  230  O   CYS A6823     4525   4688   3222   -191   -100   -617       O  
ATOM    231  CB  CYS A6823      88.909  30.658  40.808  1.00 28.83           C  
ANISOU  231  CB  CYS A6823     4058   3842   3055   -144   -189   -548       C  
ATOM    232  SG  CYS A6823      88.430  31.727  39.428  1.00 28.91           S  
ANISOU  232  SG  CYS A6823     4012   3746   3223   -133   -125   -620       S  
ATOM    233  N   ASP A6824      87.681  33.295  42.682  1.00 31.04           N  
ANISOU  233  N   ASP A6824     4227   4366   3197   -107   -112   -868       N  
ATOM    234  CA  ASP A6824      86.474  33.955  43.240  1.00 32.84           C  
ANISOU  234  CA  ASP A6824     4410   4713   3353    -96    -38   -965       C  
ATOM    235  C   ASP A6824      86.009  34.981  42.208  1.00 31.62           C  
ANISOU  235  C   ASP A6824     4209   4430   3374    -57     -4  -1042       C  
ATOM    236  O   ASP A6824      86.494  36.124  42.252  1.00 31.80           O  
ANISOU  236  O   ASP A6824     4207   4386   3488    -14    -36  -1179       O  
ATOM    237  CB  ASP A6824      86.795  34.586  44.598  1.00 35.74           C  
ANISOU  237  CB  ASP A6824     4761   5224   3592    -69    -66  -1108       C  
ATOM    238  CG  ASP A6824      85.619  35.272  45.269  1.00 39.32           C  
ANISOU  238  CG  ASP A6824     5157   5825   3956    -41     12  -1238       C  
ATOM    239  OD1 ASP A6824      84.478  35.043  44.836  1.00 42.07           O  
ANISOU  239  OD1 ASP A6824     5474   6197   4312    -54     92  -1186       O  
ATOM    240  OD2 ASP A6824      85.859  36.031  46.226  1.00 44.21           O  
ANISOU  240  OD2 ASP A6824     5755   6543   4499     -3     -9  -1405       O  
ATOM    241  N   LEU A6825      85.127  34.573  41.297  1.00 30.49           N  
ANISOU  241  N   LEU A6825     4057   4245   3282    -76     46   -950       N  
ATOM    242  CA  LEU A6825      84.623  35.440  40.203  1.00 30.91           C  
ANISOU  242  CA  LEU A6825     4070   4178   3494    -38     68   -988       C  
ATOM    243  C   LEU A6825      83.473  36.314  40.709  1.00 33.78           C  
ANISOU  243  C   LEU A6825     4363   4632   3839     15    121  -1116       C  
ATOM    244  O   LEU A6825      82.498  35.773  41.254  1.00 33.59           O  
ANISOU  244  O   LEU A6825     4307   4766   3690     -6    182  -1094       O  
ATOM    245  CB  LEU A6825      84.191  34.558  39.030  1.00 29.20           C  
ANISOU  245  CB  LEU A6825     3870   3900   3321    -81     87   -842       C  
ATOM    246  CG  LEU A6825      85.292  33.664  38.467  1.00 28.56           C  
ANISOU  246  CG  LEU A6825     3852   3731   3266   -117     38   -738       C  
ATOM    247  CD1 LEU A6825      84.777  32.833  37.305  1.00 28.16           C  
ANISOU  247  CD1 LEU A6825     3818   3626   3254   -154     56   -626       C  
ATOM    248  CD2 LEU A6825      86.492  34.496  38.039  1.00 28.43           C  
ANISOU  248  CD2 LEU A6825     3835   3600   3367    -87     -8   -794       C  
ATOM    249  N  AGLN A6826      83.652  37.631  40.598  0.60 35.53           N  
ANISOU  249  N  AGLN A6826     4559   4755   4183     83     96  -1252       N  
ATOM    250  N  BGLN A6826      83.547  37.616  40.417  0.40 36.02           N  
ANISOU  250  N  BGLN A6826     4619   4805   4261     83     99  -1237       N  
ATOM    251  CA AGLN A6826      82.643  38.639  41.020  0.60 39.11           C  
ANISOU  251  CA AGLN A6826     4941   5260   4658    167    132  -1408       C  
ATOM    252  CA BGLN A6826      82.499  38.585  40.837  0.40 39.61           C  
ANISOU  252  CA BGLN A6826     4999   5315   4732    166    138  -1388       C  
ATOM    253  C  AGLN A6826      81.291  38.328  40.373  0.60 39.76           C  
ANISOU  253  C  AGLN A6826     4965   5391   4751    176    193  -1337       C  
ATOM    254  C  BGLN A6826      81.172  38.302  40.120  0.40 40.12           C  
ANISOU  254  C  BGLN A6826     5007   5418   4818    176    195  -1315       C  
ATOM    255  O  AGLN A6826      80.258  38.513  41.040  0.60 40.81           O  
ANISOU  255  O  AGLN A6826     5021   5678   4807    219    254  -1428       O  
ATOM    256  O  BGLN A6826      80.123  38.554  40.741  0.40 40.97           O  
ANISOU  256  O  BGLN A6826     5035   5669   4861    224    252  -1410       O  
ATOM    257  CB AGLN A6826      83.119  40.031  40.595  0.60 40.15           C  
ANISOU  257  CB AGLN A6826     5075   5197   4983    230     74  -1520       C  
ATOM    258  CB BGLN A6826      82.962  40.022  40.592  0.40 41.50           C  
ANISOU  258  CB BGLN A6826     5238   5379   5149    235     81  -1521       C  
ATOM    259  CG AGLN A6826      82.032  41.097  40.619  0.60 41.78           C  
ANISOU  259  CG AGLN A6826     5211   5386   5277    338     95  -1658       C  
ATOM    260  CG BGLN A6826      84.009  40.489  41.592  0.40 43.33           C  
ANISOU  260  CG BGLN A6826     5497   5618   5348    234     29  -1656       C  
ATOM    261  CD AGLN A6826      82.548  42.430  40.138  0.60 41.81           C  
ANISOU  261  CD AGLN A6826     5235   5156   5494    389     22  -1741       C  
ATOM    262  CD BGLN A6826      84.249  41.975  41.508  0.40 44.74           C  
ANISOU  262  CD BGLN A6826     5667   5625   5708    300    -25  -1816       C  
ATOM    263  OE1AGLN A6826      83.249  43.141  40.854  0.60 43.50           O  
ANISOU  263  OE1AGLN A6826     5466   5323   5737    404    -23  -1890       O  
ATOM    264  OE1BGLN A6826      84.132  42.584  40.447  0.40 45.96           O  
ANISOU  264  OE1BGLN A6826     5824   5595   6042    320    -47  -1765       O  
ATOM    265  NE2AGLN A6826      82.169  42.794  38.924  0.60 40.45           N  
ANISOU  265  NE2AGLN A6826     5059   4835   5473    412      6  -1644       N  
ATOM    266  NE2BGLN A6826      84.587  42.573  42.638  0.40 46.92           N  
ANISOU  266  NE2BGLN A6826     5936   5956   5934    331    -54  -2011       N  
ATOM    267  N  AASN A6827      81.325  37.847  39.119  0.50 38.87           N  
ANISOU  267  N  AASN A6827     4879   5168   4722    136    178  -1186       N  
ATOM    268  N  BASN A6827      81.192  37.799  38.878  0.50 38.97           N  
ANISOU  268  N  BASN A6827     4887   5168   4750    134    180  -1165       N  
ATOM    269  CA AASN A6827      80.117  37.580  38.286  0.50 39.84           C  
ANISOU  269  CA AASN A6827     4945   5316   4876    139    214  -1113       C  
ATOM    270  CA BASN A6827      79.894  37.522  38.210  0.50 40.17           C  
ANISOU  270  CA BASN A6827     4974   5371   4915    139    222  -1104       C  
ATOM    271  C  AASN A6827      79.691  36.102  38.351  0.50 41.05           C  
ANISOU  271  C  AASN A6827     5105   5594   4896     37    255   -980       C  
ATOM    272  C  BASN A6827      79.540  36.042  38.393  0.50 41.20           C  
ANISOU  272  C  BASN A6827     5116   5634   4905     34    263   -978       C  
ATOM    273  O  AASN A6827      78.875  35.699  37.503  0.50 41.17           O  
ANISOU  273  O  AASN A6827     5085   5613   4943     13    269   -899       O  
ATOM    274  O  BASN A6827      78.631  35.576  37.682  0.50 41.10           O  
ANISOU  274  O  BASN A6827     5060   5649   4907      5    285   -901       O  
ATOM    275  CB AASN A6827      80.369  37.997  36.832  0.50 38.17           C  
ANISOU  275  CB AASN A6827     4759   4917   4825    154    164  -1035       C  
ATOM    276  CB BASN A6827      79.909  37.939  36.739  0.50 38.68           C  
ANISOU  276  CB BASN A6827     4798   5013   4885    161    177  -1029       C  
ATOM    277  CG AASN A6827      80.787  39.448  36.694  0.50 38.01           C  
ANISOU  277  CG AASN A6827     4741   4743   4955    237    115  -1136       C  
ATOM    278  CG BASN A6827      81.032  37.293  35.966  0.50 36.15           C  
ANISOU  278  CG BASN A6827     4565   4586   4582     87    139   -907       C  
ATOM    279  OD1AASN A6827      80.693  40.223  37.641  0.50 37.87           O  
ANISOU  279  OD1AASN A6827     4694   4752   4941    301    117  -1293       O  
ATOM    280  OD1BASN A6827      81.882  36.624  36.550  0.50 35.47           O  
ANISOU  280  OD1BASN A6827     4531   4529   4416     35    134   -889       O  
ATOM    281  ND2AASN A6827      81.254  39.829  35.516  0.50 37.50           N  
ANISOU  281  ND2AASN A6827     4715   4517   5017    230     68  -1049       N  
ATOM    282  ND2BASN A6827      81.043  37.491  34.658  0.50 35.30           N  
ANISOU  282  ND2BASN A6827     4470   4369   4573     89    110   -825       N  
ATOM    283  N   TYR A6828      80.202  35.342  39.325  1.00 41.72           N  
ANISOU  283  N   TYR A6828     5681   5270   4900    392    335   -738       N  
ATOM    284  CA  TYR A6828      79.875  33.901  39.516  1.00 46.77           C  
ANISOU  284  CA  TYR A6828     6356   5964   5450    370    378   -649       C  
ATOM    285  C   TYR A6828      78.377  33.749  39.808  1.00 49.91           C  
ANISOU  285  C   TYR A6828     6716   6385   5860    375    496   -627       C  
ATOM    286  O   TYR A6828      77.831  34.562  40.579  1.00 51.95           O  
ANISOU  286  O   TYR A6828     6969   6654   6112    416    557   -705       O  
ATOM    287  CB  TYR A6828      80.699  33.289  40.653  1.00 51.63           C  
ANISOU  287  CB  TYR A6828     7076   6633   5907    391    355   -671       C  
ATOM    288  CG  TYR A6828      80.417  31.830  40.913  1.00 57.46           C  
ANISOU  288  CG  TYR A6828     7865   7414   6551    370    396   -576       C  
ATOM    289  CD1 TYR A6828      81.029  30.840  40.159  1.00 61.36           C  
ANISOU  289  CD1 TYR A6828     8361   7894   7057    335    335   -499       C  
ATOM    290  CD2 TYR A6828      79.540  31.433  41.911  1.00 62.30           C  
ANISOU  290  CD2 TYR A6828     8525   8079   7066    383    503   -564       C  
ATOM    291  CE1 TYR A6828      80.776  29.497  40.386  1.00 63.66           C  
ANISOU  291  CE1 TYR A6828     8701   8212   7274    315    368   -412       C  
ATOM    292  CE2 TYR A6828      79.277  30.093  42.153  1.00 64.37           C  
ANISOU  292  CE2 TYR A6828     8837   8370   7247    357    544   -469       C  
ATOM    293  CZ  TYR A6828      79.898  29.121  41.387  1.00 65.73           C  
ANISOU  293  CZ  TYR A6828     9013   8519   7442    324    471   -392       C  
ATOM    294  OH  TYR A6828      79.651  27.797  41.613  1.00 69.26           O  
ANISOU  294  OH  TYR A6828     9512   8983   7821    298    506   -299       O  
ATOM    295  N   GLY A6829      77.737  32.740  39.209  1.00 50.77           N  
ANISOU  295  N   GLY A6829     6794   6500   5996    334    528   -529       N  
ATOM    296  CA  GLY A6829      76.294  32.507  39.425  1.00 54.33           C  
ANISOU  296  CA  GLY A6829     7190   6969   6480    330    642   -504       C  
ATOM    297  C   GLY A6829      75.438  33.177  38.360  1.00 55.23           C  
ANISOU  297  C   GLY A6829     7189   7029   6766    324    633   -499       C  
ATOM    298  O   GLY A6829      74.300  32.705  38.144  1.00 59.05           O  
ANISOU  298  O   GLY A6829     7605   7517   7312    305    699   -454       O  
ATOM    299  N   ASP A6830      75.951  34.246  37.735  1.00 53.24           N  
ANISOU  299  N   ASP A6830     6914   6721   6593    340    552   -543       N  
ATOM    300  CA  ASP A6830      75.222  34.960  36.650  1.00 50.71           C  
ANISOU  300  CA  ASP A6830     6498   6337   6433    340    521   -532       C  
ATOM    301  C   ASP A6830      75.305  34.133  35.361  1.00 47.78           C  
ANISOU  301  C   ASP A6830     6110   5942   6100    286    456   -433       C  
ATOM    302  O   ASP A6830      76.327  33.449  35.159  1.00 42.76           O  
ANISOU  302  O   ASP A6830     5539   5319   5389    258    409   -399       O  
ATOM    303  CB  ASP A6830      75.792  36.359  36.406  1.00 50.68           C  
ANISOU  303  CB  ASP A6830     6490   6270   6494    370    457   -601       C  
ATOM    304  CG  ASP A6830      75.677  37.299  37.595  1.00 54.86           C  
ANISOU  304  CG  ASP A6830     7032   6811   7001    427    511   -714       C  
ATOM    305  OD1 ASP A6830      74.995  36.927  38.573  1.00 57.75           O  
ANISOU  305  OD1 ASP A6830     7402   7234   7303    446    612   -738       O  
ATOM    306  OD2 ASP A6830      76.270  38.398  37.531  1.00 51.65           O  
ANISOU  306  OD2 ASP A6830     6633   6350   6639    449    456   -779       O  
ATOM    307  N   SER A6831      74.261  34.200  34.532  1.00 47.10           N  
ANISOU  307  N   SER A6831     5941   5823   6132    277    450   -396       N  
ATOM    308  CA  SER A6831      74.207  33.465  33.241  1.00 46.79           C  
ANISOU  308  CA  SER A6831     5887   5758   6132    229    381   -310       C  
ATOM    309  C   SER A6831      73.925  34.455  32.107  1.00 43.69           C  
ANISOU  309  C   SER A6831     5448   5291   5860    239    301   -304       C  
ATOM    310  O   SER A6831      73.089  35.352  32.305  1.00 45.85           O  
ANISOU  310  O   SER A6831     5655   5537   6228    281    321   -347       O  
ATOM    311  CB  SER A6831      73.171  32.367  33.274  1.00 49.90           C  
ANISOU  311  CB  SER A6831     6233   6181   6544    200    435   -258       C  
ATOM    312  OG  SER A6831      73.531  31.352  34.200  1.00 53.52           O  
ANISOU  312  OG  SER A6831     6754   6698   6882    183    500   -243       O  
ATOM    313  N   ALA A6832      74.619  34.302  30.975  1.00 39.87           N  
ANISOU  313  N   ALA A6832     5004   4774   5370    205    216   -254       N  
ATOM    314  CA  ALA A6832      74.393  35.181  29.804  1.00 37.36           C  
ANISOU  314  CA  ALA A6832     4663   4381   5148    209    134   -232       C  
ATOM    315  C   ALA A6832      73.044  34.827  29.165  1.00 35.35           C  
ANISOU  315  C   ALA A6832     4331   4113   4986    206    111   -189       C  
ATOM    316  O   ALA A6832      72.595  33.667  29.300  1.00 36.45           O  
ANISOU  316  O   ALA A6832     4451   4297   5102    177    144   -159       O  
ATOM    317  CB  ALA A6832      75.510  35.017  28.801  1.00 37.31           C  
ANISOU  317  CB  ALA A6832     4731   4352   5091    168     68   -188       C  
ATOM    318  N  ATHR A6833      72.401  35.805  28.525  0.50 34.30           N  
ANISOU  318  N  ATHR A6833     4152   3914   4965    236     51   -189       N  
ATOM    319  N  BTHR A6833      72.427  35.808  28.504  0.50 35.25           N  
ANISOU  319  N  BTHR A6833     4276   4034   5084    235     50   -188       N  
ATOM    320  CA ATHR A6833      71.115  35.545  27.823  0.50 34.63           C  
ANISOU  320  CA ATHR A6833     4112   3933   5111    238      4   -152       C  
ATOM    321  CA BTHR A6833      71.143  35.599  27.786  0.50 36.27           C  
ANISOU  321  CA BTHR A6833     4322   4137   5319    239      0   -152       C  
ATOM    322  C  ATHR A6833      71.449  35.059  26.409  0.50 32.24           C  
ANISOU  322  C  ATHR A6833     3869   3604   4776    193    -98    -76       C  
ATOM    323  C  BTHR A6833      71.473  35.060  26.390  0.50 33.03           C  
ANISOU  323  C  BTHR A6833     3971   3704   4874    193   -100    -75       C  
ATOM    324  O  ATHR A6833      71.941  35.866  25.604  0.50 32.02           O  
ANISOU  324  O  ATHR A6833     3895   3518   4750    198   -171    -54       O  
ATOM    325  O  BTHR A6833      71.986  35.837  25.568  0.50 32.66           O  
ANISOU  325  O  BTHR A6833     3981   3600   4827    195   -172    -52       O  
ATOM    326  CB ATHR A6833      70.200  36.774  27.844  0.50 35.95           C  
ANISOU  326  CB ATHR A6833     4197   4039   5421    301    -20   -191       C  
ATOM    327  CB BTHR A6833      70.328  36.896  27.730  0.50 38.83           C  
ANISOU  327  CB BTHR A6833     4574   4395   5782    301    -32   -188       C  
ATOM    328  OG1ATHR A6833      69.852  37.009  29.209  0.50 36.71           O  
ANISOU  328  OG1ATHR A6833     4240   4173   5532    338     94   -269       O  
ATOM    329  OG1BTHR A6833      71.074  37.853  26.976  0.50 40.59           O  
ANISOU  329  OG1BTHR A6833     4871   4549   6003    306   -112   -168       O  
ATOM    330  CG2ATHR A6833      68.946  36.590  27.018  0.50 36.30           C  
ANISOU  330  CG2ATHR A6833     4153   4050   5586    308    -95   -155       C  
ATOM    331  CG2BTHR A6833      70.019  37.454  29.102  0.50 39.92           C  
ANISOU  331  CG2BTHR A6833     4659   4556   5951    350     74   -277       C  
ATOM    332  N   LEU A6834      71.205  33.777  26.145  1.00 31.03           N  
ANISOU  332  N   LEU A6834     3711   3490   4589    150    -98    -39       N  
ATOM    333  CA  LEU A6834      71.529  33.166  24.828  1.00 28.75           C  
ANISOU  333  CA  LEU A6834     3486   3183   4252    106   -190     22       C  
ATOM    334  C   LEU A6834      70.422  33.459  23.823  1.00 27.56           C  
ANISOU  334  C   LEU A6834     3283   2980   4208    120   -298     52       C  
ATOM    335  O   LEU A6834      69.272  33.655  24.206  1.00 26.93           O  
ANISOU  335  O   LEU A6834     3092   2893   4247    151   -291     28       O  
ATOM    336  CB  LEU A6834      71.683  31.656  25.017  1.00 28.84           C  
ANISOU  336  CB  LEU A6834     3512   3250   4194     57   -150     40       C  
ATOM    337  CG  LEU A6834      72.783  31.225  25.984  1.00 29.23           C  
ANISOU  337  CG  LEU A6834     3619   3350   4135     46    -60     17       C  
ATOM    338  CD1 LEU A6834      72.795  29.717  26.162  1.00 30.14           C  
ANISOU  338  CD1 LEU A6834     3745   3506   4198      3    -29     42       C  
ATOM    339  CD2 LEU A6834      74.133  31.720  25.504  1.00 29.00           C  
ANISOU  339  CD2 LEU A6834     3684   3303   4029     40    -89     19       C  
ATOM    340  N   PRO A6835      70.745  33.509  22.511  1.00 25.67           N  
ANISOU  340  N   PRO A6835     3122   2702   3929     99   -402    103       N  
ATOM    341  CA  PRO A6835      69.721  33.625  21.479  1.00 26.06           C  
ANISOU  341  CA  PRO A6835     3138   2704   4060    111   -527    137       C  
ATOM    342  C   PRO A6835      68.718  32.484  21.698  1.00 25.89           C  
ANISOU  342  C   PRO A6835     3018   2717   4100     90   -520    127       C  
ATOM    343  O   PRO A6835      69.121  31.409  22.128  1.00 24.75           O  
ANISOU  343  O   PRO A6835     2891   2625   3886     47   -448    124       O  
ATOM    344  CB  PRO A6835      70.497  33.514  20.161  1.00 25.97           C  
ANISOU  344  CB  PRO A6835     3259   2668   3938     76   -610    193       C  
ATOM    345  CG  PRO A6835      71.909  33.937  20.524  1.00 25.06           C  
ANISOU  345  CG  PRO A6835     3231   2564   3726     63   -528    184       C  
ATOM    346  CD  PRO A6835      72.105  33.486  21.952  1.00 24.59           C  
ANISOU  346  CD  PRO A6835     3112   2565   3666     66   -405    129       C  
ATOM    347  N   LYS A6836      67.447  32.746  21.400  1.00 26.81           N  
ANISOU  347  N   LYS A6836     3031   2798   4355    119   -597    124       N  
ATOM    348  CA  LYS A6836      66.345  31.786  21.649  1.00 27.81           C  
ANISOU  348  CA  LYS A6836     3037   2948   4580     99   -589    108       C  
ATOM    349  C   LYS A6836      66.676  30.393  21.093  1.00 26.57           C  
ANISOU  349  C   LYS A6836     2942   2819   4333     31   -612    137       C  
ATOM    350  O   LYS A6836      67.024  30.285  19.898  1.00 25.33           O  
ANISOU  350  O   LYS A6836     2880   2636   4105     14   -725    173       O  
ATOM    351  CB  LYS A6836      65.056  32.334  21.030  1.00 30.65           C  
ANISOU  351  CB  LYS A6836     3291   3250   5103    141   -715    105       C  
ATOM    352  CG  LYS A6836      63.805  31.541  21.347  1.00 33.45           C  
ANISOU  352  CG  LYS A6836     3489   3619   5600    125   -703     78       C  
ATOM    353  CD  LYS A6836      62.546  32.179  20.799  1.00 36.73           C  
ANISOU  353  CD  LYS A6836     3782   3974   6197    176   -833     65       C  
ATOM    354  CE  LYS A6836      61.299  31.409  21.167  1.00 39.91           C  
ANISOU  354  CE  LYS A6836     4007   4390   6764    155   -809     30       C  
ATOM    355  NZ  LYS A6836      61.337  30.030  20.630  1.00 41.77           N  
ANISOU  355  NZ  LYS A6836     4277   4647   6947     78   -849     55       N  
ATOM    356  N   GLY A6837      66.582  29.372  21.954  1.00 25.74           N  
ANISOU  356  N   GLY A6837     2790   2763   4227     -6   -503    121       N  
ATOM    357  CA  GLY A6837      66.761  27.961  21.558  1.00 25.37           C  
ANISOU  357  CA  GLY A6837     2783   2733   4121    -70   -517    141       C  
ATOM    358  C   GLY A6837      68.200  27.561  21.280  1.00 24.14           C  
ANISOU  358  C   GLY A6837     2779   2598   3793    -96   -498    161       C  
ATOM    359  O   GLY A6837      68.395  26.431  20.789  1.00 24.14           O  
ANISOU  359  O   GLY A6837     2824   2603   3745   -144   -526    175       O  
ATOM    360  N   ILE A6838      69.174  28.432  21.561  1.00 22.54           N  
ANISOU  360  N   ILE A6838     2649   2402   3512    -67   -454    158       N  
ATOM    361  CA  ILE A6838      70.604  28.082  21.319  1.00 21.57           C  
ANISOU  361  CA  ILE A6838     2656   2298   3240    -92   -429    170       C  
ATOM    362  C   ILE A6838      71.200  27.482  22.598  1.00 21.28           C  
ANISOU  362  C   ILE A6838     2620   2311   3155   -102   -300    151       C  
ATOM    363  O   ILE A6838      71.050  28.082  23.675  1.00 21.76           O  
ANISOU  363  O   ILE A6838     2630   2389   3248    -70   -221    125       O  
ATOM    364  CB  ILE A6838      71.393  29.308  20.816  1.00 21.11           C  
ANISOU  364  CB  ILE A6838     2677   2212   3129    -64   -460    178       C  
ATOM    365  CG1 ILE A6838      70.870  29.776  19.453  1.00 21.46           C  
ANISOU  365  CG1 ILE A6838     2752   2205   3196    -58   -598    211       C  
ATOM    366  CG2 ILE A6838      72.888  29.028  20.779  1.00 20.48           C  
ANISOU  366  CG2 ILE A6838     2705   2156   2919    -88   -409    179       C  
ATOM    367  CD1 ILE A6838      71.053  28.779  18.329  1.00 21.68           C  
ANISOU  367  CD1 ILE A6838     2858   2232   3147   -102   -672    233       C  
ATOM    368  N   MET A6839      71.845  26.328  22.457  1.00 21.30           N  
ANISOU  368  N   MET A6839     2683   2330   3078   -141   -286    161       N  
ATOM    369  CA  MET A6839      72.502  25.635  23.593  1.00 21.09           C  
ANISOU  369  CA  MET A6839     2675   2344   2994   -150   -182    152       C  
ATOM    370  C   MET A6839      73.767  26.386  24.017  1.00 20.08           C  
ANISOU  370  C   MET A6839     2613   2233   2783   -122   -140    132       C  
ATOM    371  O   MET A6839      74.470  26.934  23.148  1.00 17.93           O  
ANISOU  371  O   MET A6839     2403   1941   2469   -120   -190    135       O  
ATOM    372  CB  MET A6839      72.914  24.221  23.186  1.00 21.63           C  
ANISOU  372  CB  MET A6839     2796   2412   3009   -194   -197    168       C  
ATOM    373  CG  MET A6839      71.760  23.315  22.870  1.00 23.74           C  
ANISOU  373  CG  MET A6839     2999   2658   3360   -231   -233    182       C  
ATOM    374  SD  MET A6839      72.384  21.769  22.169  1.00 24.55           S  
ANISOU  374  SD  MET A6839     3183   2746   3399   -279   -270    191       S  
ATOM    375  CE  MET A6839      70.859  20.837  22.045  1.00 25.96           C  
ANISOU  375  CE  MET A6839     3261   2893   3707   -325   -304    202       C  
ATOM    376  N   MET A6840      74.073  26.346  25.312  1.00 20.39           N  
ANISOU  376  N   MET A6840     2645   2307   2795   -106    -51    113       N  
ATOM    377  CA  MET A6840      75.313  26.976  25.828  1.00 20.77           C  
ANISOU  377  CA  MET A6840     2749   2371   2770    -81    -19     84       C  
ATOM    378  C   MET A6840      76.529  26.484  25.032  1.00 19.57           C  
ANISOU  378  C   MET A6840     2678   2212   2543   -103    -54     91       C  
ATOM    379  O   MET A6840      77.369  27.323  24.675  1.00 18.72           O  
ANISOU  379  O   MET A6840     2607   2093   2411    -93    -68     75       O  
ATOM    380  CB  MET A6840      75.516  26.623  27.306  1.00 22.69           C  
ANISOU  380  CB  MET A6840     2993   2656   2972    -65     67     67       C  
ATOM    381  CG  MET A6840      76.883  27.006  27.835  1.00 24.11           C  
ANISOU  381  CG  MET A6840     3233   2853   3074    -43     82     33       C  
ATOM    382  SD  MET A6840      77.235  28.784  27.674  1.00 28.52           S  
ANISOU  382  SD  MET A6840     3783   3386   3665     -9     62     -9       S  
ATOM    383  CE  MET A6840      76.076  29.457  28.857  1.00 30.52           C  
ANISOU  383  CE  MET A6840     3966   3656   3972     29    128    -40       C  
ATOM    384  N   ASN A6841      76.633  25.176  24.768  1.00 19.06           N  
ANISOU  384  N   ASN A6841     2639   2151   2450   -134    -63    111       N  
ATOM    385  CA  ASN A6841      77.863  24.668  24.100  1.00 19.61           C  
ANISOU  385  CA  ASN A6841     2781   2216   2452   -149    -83    105       C  
ATOM    386  C   ASN A6841      77.904  25.083  22.625  1.00 18.51           C  
ANISOU  386  C   ASN A6841     2675   2047   2310   -166   -147    114       C  
ATOM    387  O   ASN A6841      79.024  25.201  22.105  1.00 18.65           O  
ANISOU  387  O   ASN A6841     2748   2062   2274   -171   -145    100       O  
ATOM    388  CB  ASN A6841      78.082  23.187  24.388  1.00 21.02           C  
ANISOU  388  CB  ASN A6841     2982   2401   2602   -168    -69    115       C  
ATOM    389  CG  ASN A6841      78.549  22.999  25.819  1.00 23.52           C  
ANISOU  389  CG  ASN A6841     3301   2747   2886   -142     -9    105       C  
ATOM    390  OD1 ASN A6841      78.923  23.970  26.479  1.00 27.38           O  
ANISOU  390  OD1 ASN A6841     3784   3255   3363   -112     15     79       O  
ATOM    391  ND2 ASN A6841      78.512  21.778  26.317  1.00 24.26           N  
ANISOU  391  ND2 ASN A6841     3411   2840   2964   -154      7    126       N  
ATOM    392  N   VAL A6842      76.758  25.297  21.974  1.00 17.90           N  
ANISOU  392  N   VAL A6842     2567   1947   2286   -174   -202    136       N  
ATOM    393  CA  VAL A6842      76.830  25.853  20.589  1.00 17.91           C  
ANISOU  393  CA  VAL A6842     2619   1917   2266   -185   -270    151       C  
ATOM    394  C   VAL A6842      77.390  27.281  20.694  1.00 17.61           C  
ANISOU  394  C   VAL A6842     2595   1869   2227   -161   -251    145       C  
ATOM    395  O   VAL A6842      78.287  27.639  19.906  1.00 17.72           O  
ANISOU  395  O   VAL A6842     2677   1869   2184   -175   -254    148       O  
ATOM    396  CB  VAL A6842      75.463  25.817  19.878  1.00 18.38           C  
ANISOU  396  CB  VAL A6842     2644   1950   2388   -192   -354    174       C  
ATOM    397  CG1 VAL A6842      75.429  26.702  18.639  1.00 18.78           C  
ANISOU  397  CG1 VAL A6842     2752   1966   2417   -190   -431    197       C  
ATOM    398  CG2 VAL A6842      75.065  24.390  19.537  1.00 18.46           C  
ANISOU  398  CG2 VAL A6842     2654   1959   2397   -226   -384    175       C  
ATOM    399  N   ALA A6843      76.895  28.062  21.655  1.00 18.05           N  
ANISOU  399  N   ALA A6843     2587   1927   2344   -129   -224    133       N  
ATOM    400  CA  ALA A6843      77.352  29.458  21.828  1.00 17.55           C  
ANISOU  400  CA  ALA A6843     2529   1842   2294   -105   -210    120       C  
ATOM    401  C   ALA A6843      78.847  29.478  22.177  1.00 17.14           C  
ANISOU  401  C   ALA A6843     2521   1809   2182   -112   -154     91       C  
ATOM    402  O   ALA A6843      79.594  30.278  21.588  1.00 16.99           O  
ANISOU  402  O   ALA A6843     2545   1762   2146   -121   -156     94       O  
ATOM    403  CB  ALA A6843      76.522  30.130  22.893  1.00 18.03           C  
ANISOU  403  CB  ALA A6843     2511   1906   2434    -66   -184     99       C  
ATOM    404  N   LYS A6844      79.262  28.595  23.084  1.00 16.97           N  
ANISOU  404  N   LYS A6844     2487   1827   2132   -109   -109     66       N  
ATOM    405  CA  LYS A6844      80.664  28.525  23.571  1.00 16.68           C  
ANISOU  405  CA  LYS A6844     2476   1809   2051   -108    -67     30       C  
ATOM    406  C   LYS A6844      81.612  28.143  22.428  1.00 16.46           C  
ANISOU  406  C   LYS A6844     2506   1770   1976   -141    -75     36       C  
ATOM    407  O   LYS A6844      82.615  28.854  22.216  1.00 15.70           O  
ANISOU  407  O   LYS A6844     2429   1661   1875   -148    -53     17       O  
ATOM    408  CB  LYS A6844      80.738  27.515  24.714  1.00 17.09           C  
ANISOU  408  CB  LYS A6844     2511   1901   2078    -94    -35     14       C  
ATOM    409  CG  LYS A6844      82.113  27.325  25.327  1.00 17.87           C  
ANISOU  409  CG  LYS A6844     2630   2019   2139    -83    -11    -26       C  
ATOM    410  CD  LYS A6844      82.162  26.185  26.312  1.00 18.36           C  
ANISOU  410  CD  LYS A6844     2696   2113   2167    -69      5    -27       C  
ATOM    411  CE  LYS A6844      81.163  26.322  27.437  1.00 18.93           C  
ANISOU  411  CE  LYS A6844     2739   2206   2247    -47     33    -22       C  
ATOM    412  NZ  LYS A6844      81.359  25.259  28.446  1.00 18.68           N  
ANISOU  412  NZ  LYS A6844     2730   2201   2166    -35     53    -16       N  
ATOM    413  N   TYR A6845      81.324  27.045  21.730  1.00 16.08           N  
ANISOU  413  N   TYR A6845     2484   1726   1900   -163    -98     57       N  
ATOM    414  CA  TYR A6845      82.195  26.663  20.589  1.00 16.36           C  
ANISOU  414  CA  TYR A6845     2580   1752   1882   -193    -97     55       C  
ATOM    415  C   TYR A6845      82.156  27.732  19.497  1.00 16.47           C  
ANISOU  415  C   TYR A6845     2638   1732   1888   -211   -115     83       C  
ATOM    416  O   TYR A6845      83.182  27.934  18.846  1.00 16.75           O  
ANISOU  416  O   TYR A6845     2717   1759   1886   -233    -81     73       O  
ATOM    417  CB  TYR A6845      81.787  25.311  20.020  1.00 16.74           C  
ANISOU  417  CB  TYR A6845     2652   1803   1903   -210   -126     65       C  
ATOM    418  CG  TYR A6845      82.356  24.129  20.749  1.00 17.05           C  
ANISOU  418  CG  TYR A6845     2680   1864   1933   -201    -99     38       C  
ATOM    419  CD1 TYR A6845      81.907  23.781  22.013  1.00 17.49           C  
ANISOU  419  CD1 TYR A6845     2691   1936   2018   -179    -88     41       C  
ATOM    420  CD2 TYR A6845      83.309  23.322  20.151  1.00 17.83           C  
ANISOU  420  CD2 TYR A6845     2818   1961   1993   -213    -84     12       C  
ATOM    421  CE1 TYR A6845      82.405  22.668  22.669  1.00 17.75           C  
ANISOU  421  CE1 TYR A6845     2726   1979   2037   -169    -73     27       C  
ATOM    422  CE2 TYR A6845      83.816  22.205  20.793  1.00 17.67           C  
ANISOU  422  CE2 TYR A6845     2789   1949   1974   -199    -72    -10       C  
ATOM    423  CZ  TYR A6845      83.357  21.875  22.055  1.00 18.23           C  
ANISOU  423  CZ  TYR A6845     2824   2032   2070   -177    -72      2       C  
ATOM    424  OH  TYR A6845      83.821  20.758  22.691  1.00 18.99           O  
ANISOU  424  OH  TYR A6845     2923   2127   2162   -161    -68     -8       O  
ATOM    425  N   THR A6846      81.007  28.379  19.282  1.00 16.59           N  
ANISOU  425  N   THR A6846     2641   1722   1938   -202   -167    118       N  
ATOM    426  CA  THR A6846      80.965  29.435  18.235  1.00 17.14           C  
ANISOU  426  CA  THR A6846     2767   1750   1995   -215   -195    154       C  
ATOM    427  C   THR A6846      81.959  30.543  18.612  1.00 16.91           C  
ANISOU  427  C   THR A6846     2735   1703   1986   -216   -140    137       C  
ATOM    428  O   THR A6846      82.732  30.973  17.737  1.00 17.30           O  
ANISOU  428  O   THR A6846     2848   1730   1995   -247   -115    152       O  
ATOM    429  CB  THR A6846      79.544  29.970  18.038  1.00 18.07           C  
ANISOU  429  CB  THR A6846     2861   1837   2165   -195   -274    191       C  
ATOM    430  OG1 THR A6846      78.760  28.885  17.534  1.00 18.81           O  
ANISOU  430  OG1 THR A6846     2960   1943   2241   -205   -329    202       O  
ATOM    431  CG2 THR A6846      79.479  31.151  17.093  1.00 19.14           C  
ANISOU  431  CG2 THR A6846     3059   1919   2293   -201   -313    236       C  
ATOM    432  N   GLN A6847      81.968  30.956  19.879  1.00 16.42           N  
ANISOU  432  N   GLN A6847     2604   1650   1982   -185   -116    102       N  
ATOM    433  CA  GLN A6847      82.888  32.043  20.313  1.00 16.52           C  
ANISOU  433  CA  GLN A6847     2608   1641   2028   -185    -73     74       C  
ATOM    434  C   GLN A6847      84.340  31.551  20.258  1.00 16.74           C  
ANISOU  434  C   GLN A6847     2647   1690   2020   -212    -15     37       C  
ATOM    435  O   GLN A6847      85.205  32.358  19.868  1.00 17.36           O  
ANISOU  435  O   GLN A6847     2746   1737   2111   -239     19     34       O  
ATOM    436  CB  GLN A6847      82.455  32.598  21.670  1.00 16.92           C  
ANISOU  436  CB  GLN A6847     2588   1696   2141   -142    -71     37       C  
ATOM    437  CG  GLN A6847      81.231  33.490  21.550  1.00 17.31           C  
ANISOU  437  CG  GLN A6847     2622   1704   2250   -117   -119     67       C  
ATOM    438  CD  GLN A6847      80.839  34.143  22.848  1.00 17.69           C  
ANISOU  438  CD  GLN A6847     2605   1754   2361    -73   -104     19       C  
ATOM    439  OE1 GLN A6847      81.093  33.615  23.929  1.00 17.39           O  
ANISOU  439  OE1 GLN A6847     2535   1764   2307    -56    -68    -26       O  
ATOM    440  NE2 GLN A6847      80.210  35.306  22.742  1.00 17.62           N  
ANISOU  440  NE2 GLN A6847     2584   1689   2420    -50   -134     30       N  
ATOM    441  N   LEU A6848      84.603  30.293  20.619  1.00 16.36           N  
ANISOU  441  N   LEU A6848     2586   1689   1941   -205     -5     11       N  
ATOM    442  CA  LEU A6848      85.990  29.755  20.513  1.00 17.19           C  
ANISOU  442  CA  LEU A6848     2693   1810   2026   -224     44    -29       C  
ATOM    443  C   LEU A6848      86.452  29.832  19.048  1.00 17.82           C  
ANISOU  443  C   LEU A6848     2840   1868   2060   -270     72     -2       C  
ATOM    444  O   LEU A6848      87.575  30.317  18.803  1.00 18.66           O  
ANISOU  444  O   LEU A6848     2946   1961   2182   -296    129    -26       O  
ATOM    445  CB  LEU A6848      86.024  28.315  21.031  1.00 16.99           C  
ANISOU  445  CB  LEU A6848     2652   1827   1976   -204     36    -51       C  
ATOM    446  CG  LEU A6848      87.347  27.575  20.835  1.00 17.89           C  
ANISOU  446  CG  LEU A6848     2764   1954   2077   -214     76    -95       C  
ATOM    447  CD1 LEU A6848      88.484  28.299  21.538  1.00 18.06           C  
ANISOU  447  CD1 LEU A6848     2737   1973   2149   -208    105   -148       C  
ATOM    448  CD2 LEU A6848      87.244  26.138  21.324  1.00 17.66           C  
ANISOU  448  CD2 LEU A6848     2727   1951   2028   -190     55   -108       C  
ATOM    449  N   CYS A6849      85.612  29.376  18.115  1.00 17.93           N  
ANISOU  449  N   CYS A6849     2911   1878   2022   -281     34     42       N  
ATOM    450  CA  CYS A6849      85.960  29.392  16.669  1.00 18.65           C  
ANISOU  450  CA  CYS A6849     3088   1952   2044   -323     58     69       C  
ATOM    451  C   CYS A6849      86.110  30.836  16.170  1.00 19.10           C  
ANISOU  451  C   CYS A6849     3183   1960   2113   -348     76    110       C  
ATOM    452  O   CYS A6849      87.032  31.096  15.371  1.00 19.48           O  
ANISOU  452  O   CYS A6849     3280   1994   2126   -390    144    113       O  
ATOM    453  CB  CYS A6849      84.922  28.618  15.871  1.00 19.31           C  
ANISOU  453  CB  CYS A6849     3228   2040   2068   -323     -6    103       C  
ATOM    454  SG  CYS A6849      84.972  26.839  16.216  1.00 19.66           S  
ANISOU  454  SG  CYS A6849     3245   2126   2097   -308    -12     56       S  
ATOM    455  N   GLN A6850      85.243  31.741  16.626  1.00 19.06           N  
ANISOU  455  N   GLN A6850     3155   1924   2161   -324     22    139       N  
ATOM    456  CA  GLN A6850      85.357  33.174  16.242  1.00 20.14           C  
ANISOU  456  CA  GLN A6850     3327   1999   2324   -343     31    180       C  
ATOM    457  C   GLN A6850      86.721  33.712  16.691  1.00 19.87           C  
ANISOU  457  C   GLN A6850     3253   1955   2340   -368    117    134       C  
ATOM    458  O   GLN A6850      87.322  34.512  15.949  1.00 20.41           O  
ANISOU  458  O   GLN A6850     3373   1977   2402   -413    166    165       O  
ATOM    459  CB  GLN A6850      84.211  33.990  16.837  1.00 20.43           C  
ANISOU  459  CB  GLN A6850     3328   2003   2432   -301    -41    201       C  
ATOM    460  CG  GLN A6850      82.884  33.758  16.134  1.00 21.07           C  
ANISOU  460  CG  GLN A6850     3451   2073   2480   -284   -132    256       C  
ATOM    461  CD  GLN A6850      81.751  34.489  16.808  1.00 21.86           C  
ANISOU  461  CD  GLN A6850     3493   2143   2669   -236   -198    264       C  
ATOM    462  OE1 GLN A6850      81.731  34.653  18.031  1.00 21.62           O  
ANISOU  462  OE1 GLN A6850     3377   2128   2707   -206   -176    213       O  
ATOM    463  NE2 GLN A6850      80.798  34.946  16.006  1.00 22.41           N  
ANISOU  463  NE2 GLN A6850     3609   2168   2737   -226   -281    325       N  
ATOM    464  N   TYR A6851      87.196  33.276  17.856  1.00 19.63           N  
ANISOU  464  N   TYR A6851     3136   1962   2358   -343    132     64       N  
ATOM    465  CA  TYR A6851      88.520  33.734  18.342  1.00 19.96           C  
ANISOU  465  CA  TYR A6851     3126   1996   2460   -363    198      8       C  
ATOM    466  C   TYR A6851      89.636  33.056  17.530  1.00 20.17           C  
ANISOU  466  C   TYR A6851     3174   2042   2445   -406    276     -9       C  
ATOM    467  O   TYR A6851      90.591  33.752  17.123  1.00 20.54           O  
ANISOU  467  O   TYR A6851     3223   2056   2525   -453    349    -15       O  
ATOM    468  CB  TYR A6851      88.674  33.486  19.843  1.00 19.88           C  
ANISOU  468  CB  TYR A6851     3027   2020   2506   -317    174    -62       C  
ATOM    469  CG  TYR A6851      90.013  33.942  20.353  1.00 20.04           C  
ANISOU  469  CG  TYR A6851     2988   2030   2596   -335    221   -127       C  
ATOM    470  CD1 TYR A6851      90.311  35.292  20.434  1.00 21.34           C  
ANISOU  470  CD1 TYR A6851     3141   2132   2832   -359    236   -130       C  
ATOM    471  CD2 TYR A6851      91.003  33.034  20.694  1.00 20.20           C  
ANISOU  471  CD2 TYR A6851     2961   2092   2621   -330    246   -188       C  
ATOM    472  CE1 TYR A6851      91.552  35.732  20.862  1.00 21.96           C  
ANISOU  472  CE1 TYR A6851     3157   2195   2990   -383    276   -195       C  
ATOM    473  CE2 TYR A6851      92.246  33.458  21.131  1.00 20.52           C  
ANISOU  473  CE2 TYR A6851     2935   2120   2742   -347    280   -254       C  
ATOM    474  CZ  TYR A6851      92.522  34.809  21.208  1.00 21.79           C  
ANISOU  474  CZ  TYR A6851     3079   2221   2975   -376    296   -259       C  
ATOM    475  OH  TYR A6851      93.744  35.233  21.638  1.00 22.89           O  
ANISOU  475  OH  TYR A6851     3145   2344   3208   -397    323   -330       O  
ATOM    476  N   LEU A6852      89.518  31.748  17.287  1.00 19.76           N  
ANISOU  476  N   LEU A6852     3137   2039   2332   -392    269    -21       N  
ATOM    477  CA  LEU A6852      90.558  31.026  16.501  1.00 20.55           C  
ANISOU  477  CA  LEU A6852     3254   2158   2395   -425    348    -50       C  
ATOM    478  C   LEU A6852      90.690  31.656  15.105  1.00 21.38           C  
ANISOU  478  C   LEU A6852     3457   2228   2439   -483    406      7       C  
ATOM    479  O   LEU A6852      91.799  31.596  14.542  1.00 21.72           O  
ANISOU  479  O   LEU A6852     3501   2270   2479   -525    505    -19       O  
ATOM    480  CB  LEU A6852      90.211  29.532  16.445  1.00 20.37           C  
ANISOU  480  CB  LEU A6852     3241   2180   2316   -396    315    -70       C  
ATOM    481  CG  LEU A6852      90.299  28.785  17.778  1.00 20.18           C  
ANISOU  481  CG  LEU A6852     3133   2190   2344   -344    274   -123       C  
ATOM    482  CD1 LEU A6852      89.861  27.340  17.625  1.00 19.98           C  
ANISOU  482  CD1 LEU A6852     3129   2193   2267   -321    241   -129       C  
ATOM    483  CD2 LEU A6852      91.706  28.848  18.363  1.00 21.42           C  
ANISOU  483  CD2 LEU A6852     3210   2352   2576   -344    325   -196       C  
ATOM    484  N   ASN A6853      89.619  32.273  14.589  1.00 21.69           N  
ANISOU  484  N   ASN A6853     3573   2233   2433   -485    348     84       N  
ATOM    485  CA  ASN A6853      89.657  32.948  13.261  1.00 23.00           C  
ANISOU  485  CA  ASN A6853     3855   2358   2526   -538    390    155       C  
ATOM    486  C   ASN A6853      90.669  34.104  13.263  1.00 24.54           C  
ANISOU  486  C   ASN A6853     4030   2503   2790   -588    481    157       C  
ATOM    487  O   ASN A6853      91.142  34.460  12.174  1.00 25.45           O  
ANISOU  487  O   ASN A6853     4232   2592   2844   -645    561    200       O  
ATOM    488  CB  ASN A6853      88.292  33.520  12.867  1.00 23.03           C  
ANISOU  488  CB  ASN A6853     3935   2324   2492   -520    287    237       C  
ATOM    489  CG  ASN A6853      87.348  32.488  12.296  1.00 23.35           C  
ANISOU  489  CG  ASN A6853     4034   2399   2439   -496    211    253       C  
ATOM    490  OD1 ASN A6853      87.787  31.437  11.840  1.00 23.08           O  
ANISOU  490  OD1 ASN A6853     4022   2407   2340   -507    251    216       O  
ATOM    491  ND2 ASN A6853      86.057  32.792  12.291  1.00 22.91           N  
ANISOU  491  ND2 ASN A6853     3998   2320   2385   -464     98    303       N  
ATOM    492  N   THR A6854      91.001  34.643  14.440  1.00 23.48           N  
ANISOU  492  N   THR A6854     3789   2356   2777   -570    471    109       N  
ATOM    493  CA  THR A6854      91.892  35.830  14.569  1.00 24.73           C  
ANISOU  493  CA  THR A6854     3914   2454   3027   -618    542    105       C  
ATOM    494  C   THR A6854      93.359  35.411  14.693  1.00 25.01           C  
ANISOU  494  C   THR A6854     3869   2517   3117   -651    647     24       C  
ATOM    495  O   THR A6854      94.219  36.316  14.672  1.00 25.49           O  
ANISOU  495  O   THR A6854     3897   2528   3261   -704    722     16       O  
ATOM    496  CB  THR A6854      91.494  36.703  15.768  1.00 25.02           C  
ANISOU  496  CB  THR A6854     3878   2455   3171   -581    469     83       C  
ATOM    497  OG1 THR A6854      91.873  36.058  16.987  1.00 23.53           O  
ANISOU  497  OG1 THR A6854     3578   2319   3041   -537    445     -9       O  
ATOM    498  CG2 THR A6854      90.018  37.037  15.778  1.00 25.29           C  
ANISOU  498  CG2 THR A6854     3965   2467   3174   -537    363    146       C  
ATOM    499  N   LEU A6855      93.638  34.107  14.765  1.00 24.40           N  
ANISOU  499  N   LEU A6855     3760   2507   3004   -624    655    -30       N  
ATOM    500  CA  LEU A6855      95.025  33.610  14.968  1.00 25.88           C  
ANISOU  500  CA  LEU A6855     3851   2720   3260   -641    742   -119       C  
ATOM    501  C   LEU A6855      95.607  33.124  13.637  1.00 27.73           C  
ANISOU  501  C   LEU A6855     4154   2968   3413   -692    860   -108       C  
ATOM    502  O   LEU A6855      94.849  33.036  12.650  1.00 31.33           O  
ANISOU  502  O   LEU A6855     4739   3421   3742   -705    854    -34       O  
ATOM    503  CB  LEU A6855      95.005  32.477  16.000  1.00 25.15           C  
ANISOU  503  CB  LEU A6855     3677   2685   3192   -570    668   -192       C  
ATOM    504  CG  LEU A6855      94.319  32.798  17.329  1.00 24.41           C  
ANISOU  504  CG  LEU A6855     3535   2591   3149   -514    555   -203       C  
ATOM    505  CD1 LEU A6855      94.463  31.635  18.295  1.00 24.20           C  
ANISOU  505  CD1 LEU A6855     3439   2617   3137   -451    498   -270       C  
ATOM    506  CD2 LEU A6855      94.873  34.073  17.949  1.00 25.38           C  
ANISOU  506  CD2 LEU A6855     3593   2663   3386   -538    565   -229       C  
ATOM    507  N   THR A6856      96.900  32.802  13.628  1.00 27.92           N  
ANISOU  507  N   THR A6856     4091   3006   3509   -717    961   -185       N  
ATOM    508  CA  THR A6856      97.584  32.318  12.400  1.00 28.83           C  
ANISOU  508  CA  THR A6856     4259   3138   3556   -766   1098   -192       C  
ATOM    509  C   THR A6856      97.461  30.792  12.317  1.00 27.79           C  
ANISOU  509  C   THR A6856     4128   3067   3361   -710   1069   -245       C  
ATOM    510  O   THR A6856      98.505  30.111  12.250  1.00 28.07           O  
ANISOU  510  O   THR A6856     4086   3128   3451   -711   1151   -330       O  
ATOM    511  CB  THR A6856      99.038  32.803  12.371  1.00 30.39           C  
ANISOU  511  CB  THR A6856     4352   3313   3879   -825   1234   -251       C  
ATOM    512  OG1 THR A6856      99.681  32.366  13.569  1.00 30.16           O  
ANISOU  512  OG1 THR A6856     4164   3305   3988   -776   1181   -353       O  
ATOM    513  CG2 THR A6856      99.138  34.308  12.263  1.00 31.93           C  
ANISOU  513  CG2 THR A6856     4566   3435   4129   -893   1276   -189       C  
ATOM    514  N   LEU A6857      96.234  30.267  12.337  1.00 26.97           N  
ANISOU  514  N   LEU A6857     4103   2982   3161   -664    954   -202       N  
ATOM    515  CA  LEU A6857      96.075  28.796  12.202  1.00 27.15           C  
ANISOU  515  CA  LEU A6857     4135   3052   3127   -616    925   -250       C  
ATOM    516  C   LEU A6857      96.503  28.360  10.801  1.00 27.48           C  
ANISOU  516  C   LEU A6857     4268   3106   3064   -659   1046   -257       C  
ATOM    517  O   LEU A6857      96.170  29.074   9.837  1.00 27.47           O  
ANISOU  517  O   LEU A6857     4389   3083   2965   -710   1089   -181       O  
ATOM    518  CB  LEU A6857      94.615  28.377  12.397  1.00 28.22           C  
ANISOU  518  CB  LEU A6857     4340   3197   3186   -571    785   -198       C  
ATOM    519  CG  LEU A6857      94.005  28.584  13.778  1.00 29.71           C  
ANISOU  519  CG  LEU A6857     4452   3382   3453   -520    667   -194       C  
ATOM    520  CD1 LEU A6857      92.658  27.880  13.848  1.00 29.92           C  
ANISOU  520  CD1 LEU A6857     4534   3423   3408   -479    554   -157       C  
ATOM    521  CD2 LEU A6857      94.924  28.073  14.875  1.00 30.90           C  
ANISOU  521  CD2 LEU A6857     4470   3551   3718   -483    665   -282       C  
ATOM    522  N   ALA A6858      97.220  27.238  10.719  1.00 26.80           N  
ANISOU  522  N   ALA A6858     4131   3052   2999   -635   1095   -347       N  
ATOM    523  CA  ALA A6858      97.533  26.604   9.423  1.00 27.72           C  
ANISOU  523  CA  ALA A6858     4340   3188   3004   -662   1203   -370       C  
ATOM    524  C   ALA A6858      96.247  25.908   8.968  1.00 27.08           C  
ANISOU  524  C   ALA A6858     4386   3119   2783   -631   1092   -328       C  
ATOM    525  O   ALA A6858      95.617  25.232   9.813  1.00 25.78           O  
ANISOU  525  O   ALA A6858     4175   2962   2657   -572    965   -341       O  
ATOM    526  CB  ALA A6858      98.674  25.633   9.576  1.00 28.37           C  
ANISOU  526  CB  ALA A6858     4313   3293   3173   -635   1281   -489       C  
ATOM    527  N   VAL A6859      95.835  26.122   7.718  1.00 27.43           N  
ANISOU  527  N   VAL A6859     4586   3162   2673   -673   1132   -275       N  
ATOM    528  CA  VAL A6859      94.573  25.512   7.211  1.00 27.41           C  
ANISOU  528  CA  VAL A6859     4707   3167   2539   -648   1012   -238       C  
ATOM    529  C   VAL A6859      94.863  24.878   5.856  1.00 28.77           C  
ANISOU  529  C   VAL A6859     5004   3360   2565   -673   1107   -273       C  
ATOM    530  O   VAL A6859      94.625  25.479   4.809  1.00 29.48           O  
ANISOU  530  O   VAL A6859     5240   3443   2518   -720   1148   -209       O  
ATOM    531  CB  VAL A6859      93.435  26.546   7.138  1.00 27.44           C  
ANISOU  531  CB  VAL A6859     4793   3140   2490   -662    910   -122       C  
ATOM    532  CG1 VAL A6859      92.115  25.891   6.770  1.00 27.45           C  
ANISOU  532  CG1 VAL A6859     4890   3148   2392   -630    767    -94       C  
ATOM    533  CG2 VAL A6859      93.291  27.321   8.442  1.00 26.61           C  
ANISOU  533  CG2 VAL A6859     4566   3012   2530   -642    845    -97       C  
ATOM    534  N   PRO A6860      95.440  23.660   5.846  1.00 29.38           N  
ANISOU  534  N   PRO A6860     5031   3460   2669   -640   1148   -380       N  
ATOM    535  CA  PRO A6860      95.738  22.971   4.597  1.00 31.44           C  
ANISOU  535  CA  PRO A6860     5408   3743   2793   -657   1242   -433       C  
ATOM    536  C   PRO A6860      94.486  22.342   3.982  1.00 31.71           C  
ANISOU  536  C   PRO A6860     5583   3780   2685   -637   1108   -409       C  
ATOM    537  O   PRO A6860      93.440  22.318   4.626  1.00 29.08           O  
ANISOU  537  O   PRO A6860     5230   3432   2386   -607    946   -360       O  
ATOM    538  CB  PRO A6860      96.716  21.868   5.030  1.00 31.44           C  
ANISOU  538  CB  PRO A6860     5279   3757   2910   -614   1305   -562       C  
ATOM    539  CG  PRO A6860      96.338  21.571   6.464  1.00 30.07           C  
ANISOU  539  CG  PRO A6860     4971   3569   2885   -556   1161   -561       C  
ATOM    540  CD  PRO A6860      95.844  22.887   7.029  1.00 28.76           C  
ANISOU  540  CD  PRO A6860     4791   3386   2750   -582   1105   -456       C  
ATOM    541  N   TYR A6861      94.609  21.901   2.730  1.00 33.63           N  
ANISOU  541  N   TYR A6861     5967   4040   2770   -658   1180   -444       N  
ATOM    542  CA  TYR A6861      93.514  21.111   2.125  1.00 34.98           C  
ANISOU  542  CA  TYR A6861     6264   4212   2814   -635   1046   -448       C  
ATOM    543  C   TYR A6861      93.457  19.794   2.894  1.00 34.19           C  
ANISOU  543  C   TYR A6861     6050   4107   2831   -574    971   -540       C  
ATOM    544  O   TYR A6861      94.522  19.366   3.373  1.00 34.13           O  
ANISOU  544  O   TYR A6861     5920   4104   2941   -554   1071   -621       O  
ATOM    545  CB  TYR A6861      93.774  20.851   0.641  1.00 37.26           C  
ANISOU  545  CB  TYR A6861     6732   4523   2903   -667   1147   -485       C  
ATOM    546  CG  TYR A6861      93.660  22.065  -0.237  1.00 38.87           C  
ANISOU  546  CG  TYR A6861     7088   4725   2955   -728   1202   -380       C  
ATOM    547  CD1 TYR A6861      92.423  22.504  -0.675  1.00 40.20           C  
ANISOU  547  CD1 TYR A6861     7392   4877   3004   -732   1045   -284       C  
ATOM    548  CD2 TYR A6861      94.783  22.757  -0.659  1.00 41.58           C  
ANISOU  548  CD2 TYR A6861     7442   5078   3278   -782   1409   -376       C  
ATOM    549  CE1 TYR A6861      92.300  23.611  -1.499  1.00 42.48           C  
ANISOU  549  CE1 TYR A6861     7835   5155   3149   -784   1082   -179       C  
ATOM    550  CE2 TYR A6861      94.679  23.864  -1.484  1.00 43.37           C  
ANISOU  550  CE2 TYR A6861     7823   5294   3360   -843   1464   -269       C  
ATOM    551  CZ  TYR A6861      93.432  24.296  -1.900  1.00 43.61           C  
ANISOU  551  CZ  TYR A6861     7999   5305   3264   -841   1295   -167       C  
ATOM    552  OH  TYR A6861      93.313  25.385  -2.713  1.00 46.81           O  
ANISOU  552  OH  TYR A6861     8568   5692   3525   -895   1336    -53       O  
ATOM    553  N   ASN A6862      92.275  19.184   3.002  1.00 35.43           N  
ANISOU  553  N   ASN A6862     6243   4249   2967   -545    800   -526       N  
ATOM    554  CA  ASN A6862      92.137  17.891   3.726  1.00 36.09           C  
ANISOU  554  CA  ASN A6862     6231   4317   3163   -492    723   -602       C  
ATOM    555  C   ASN A6862      92.735  18.043   5.123  1.00 33.26           C  
ANISOU  555  C   ASN A6862     5690   3951   2994   -464    740   -603       C  
ATOM    556  O   ASN A6862      93.485  17.152   5.567  1.00 33.06           O  
ANISOU  556  O   ASN A6862     5573   3919   3067   -427    781   -691       O  
ATOM    557  CB  ASN A6862      92.783  16.746   2.950  1.00 39.49           C  
ANISOU  557  CB  ASN A6862     6710   4753   3540   -477    804   -726       C  
ATOM    558  CG  ASN A6862      92.192  16.611   1.567  1.00 44.15           C  
ANISOU  558  CG  ASN A6862     7496   5353   3925   -504    780   -732       C  
ATOM    559  OD1 ASN A6862      90.980  16.724   1.396  1.00 49.93           O  
ANISOU  559  OD1 ASN A6862     8302   6072   4596   -509    627   -669       O  
ATOM    560  ND2 ASN A6862      93.038  16.380   0.582  1.00 46.26           N  
ANISOU  560  ND2 ASN A6862     7845   5642   4087   -519    929   -810       N  
ATOM    561  N   MET A6863      92.416  19.163   5.764  1.00 31.14           N  
ANISOU  561  N   MET A6863     5377   3681   2772   -480    705   -509       N  
ATOM    562  CA  MET A6863      92.868  19.457   7.140  1.00 29.38           C  
ANISOU  562  CA  MET A6863     4994   3452   2716   -454    703   -502       C  
ATOM    563  C   MET A6863      92.381  18.333   8.068  1.00 28.06           C  
ANISOU  563  C   MET A6863     4753   3267   2641   -401    589   -532       C  
ATOM    564  O   MET A6863      91.290  17.792   7.826  1.00 29.50           O  
ANISOU  564  O   MET A6863     5001   3436   2772   -396    479   -512       O  
ATOM    565  CB  MET A6863      92.288  20.801   7.570  1.00 28.85           C  
ANISOU  565  CB  MET A6863     4921   3380   2660   -478    656   -396       C  
ATOM    566  CG  MET A6863      92.693  21.235   8.935  1.00 28.61           C  
ANISOU  566  CG  MET A6863     4745   3345   2781   -455    649   -389       C  
ATOM    567  SD  MET A6863      92.015  22.871   9.228  1.00 29.23           S  
ANISOU  567  SD  MET A6863     4836   3410   2859   -485    606   -275       S  
ATOM    568  CE  MET A6863      92.683  23.205  10.853  1.00 28.06           C  
ANISOU  568  CE  MET A6863     4515   3259   2884   -454    607   -299       C  
ATOM    569  N   ARG A6864      93.183  17.988   9.071  1.00 27.06           N  
ANISOU  569  N   ARG A6864     4498   3135   2648   -364    613   -577       N  
ATOM    570  CA  ARG A6864      92.866  16.881  10.008  1.00 25.86           C  
ANISOU  570  CA  ARG A6864     4280   2959   2586   -313    516   -601       C  
ATOM    571  C   ARG A6864      92.580  17.468  11.387  1.00 23.52           C  
ANISOU  571  C   ARG A6864     3890   2661   2383   -295    450   -539       C  
ATOM    572  O   ARG A6864      93.509  18.052  11.994  1.00 23.32           O  
ANISOU  572  O   ARG A6864     3777   2646   2436   -287    507   -554       O  
ATOM    573  CB  ARG A6864      94.035  15.902  10.076  1.00 27.51           C  
ANISOU  573  CB  ARG A6864     4425   3156   2868   -273    583   -708       C  
ATOM    574  CG  ARG A6864      94.403  15.300   8.731  1.00 29.88           C  
ANISOU  574  CG  ARG A6864     4816   3459   3078   -286    665   -787       C  
ATOM    575  CD  ARG A6864      95.719  14.583   8.860  1.00 31.98           C  
ANISOU  575  CD  ARG A6864     4993   3715   3442   -245    753   -896       C  
ATOM    576  NE  ARG A6864      96.052  13.842   7.662  1.00 33.92           N  
ANISOU  576  NE  ARG A6864     5319   3959   3610   -247    832   -987       N  
ATOM    577  CZ  ARG A6864      97.126  13.081   7.542  1.00 35.74           C  
ANISOU  577  CZ  ARG A6864     5487   4176   3916   -208    915  -1099       C  
ATOM    578  NH1 ARG A6864      97.982  12.979   8.548  1.00 36.65           N  
ANISOU  578  NH1 ARG A6864     5457   4278   4190   -163    919  -1129       N  
ATOM    579  NH2 ARG A6864      97.345  12.436   6.414  1.00 36.87           N  
ANISOU  579  NH2 ARG A6864     5715   4319   3975   -210    989  -1186       N  
ATOM    580  N   VAL A6865      91.350  17.285  11.861  1.00 21.40           N  
ANISOU  580  N   VAL A6865     3638   2381   2112   -289    335   -479       N  
ATOM    581  CA  VAL A6865      90.934  17.854  13.170  1.00 20.45           C  
ANISOU  581  CA  VAL A6865     3442   2263   2066   -273    276   -419       C  
ATOM    582  C   VAL A6865      90.406  16.726  14.049  1.00 19.89           C  
ANISOU  582  C   VAL A6865     3338   2166   2052   -236    191   -418       C  
ATOM    583  O   VAL A6865      89.571  15.936  13.568  1.00 19.97           O  
ANISOU  583  O   VAL A6865     3405   2155   2026   -245    135   -415       O  
ATOM    584  CB  VAL A6865      89.873  18.952  12.984  1.00 19.93           C  
ANISOU  584  CB  VAL A6865     3420   2205   1948   -306    233   -334       C  
ATOM    585  CG1 VAL A6865      89.430  19.537  14.317  1.00 19.07           C  
ANISOU  585  CG1 VAL A6865     3235   2098   1911   -287    183   -284       C  
ATOM    586  CG2 VAL A6865      90.367  20.042  12.045  1.00 21.01           C  
ANISOU  586  CG2 VAL A6865     3607   2354   2018   -347    316   -323       C  
ATOM    587  N   ILE A6866      90.895  16.657  15.287  1.00 19.35           N  
ANISOU  587  N   ILE A6866     3185   2096   2069   -199    180   -421       N  
ATOM    588  CA  ILE A6866      90.375  15.642  16.244  1.00 18.92           C  
ANISOU  588  CA  ILE A6866     3110   2014   2064   -166    102   -404       C  
ATOM    589  C   ILE A6866      89.802  16.395  17.450  1.00 18.15           C  
ANISOU  589  C   ILE A6866     2969   1932   1992   -160     63   -336       C  
ATOM    590  O   ILE A6866      90.432  17.385  17.927  1.00 17.89           O  
ANISOU  590  O   ILE A6866     2890   1925   1982   -154     96   -338       O  
ATOM    591  CB  ILE A6866      91.424  14.569  16.596  1.00 19.89           C  
ANISOU  591  CB  ILE A6866     3193   2110   2254   -118    112   -471       C  
ATOM    592  CG1 ILE A6866      90.795  13.450  17.431  1.00 20.14           C  
ANISOU  592  CG1 ILE A6866     3227   2100   2324    -92     31   -442       C  
ATOM    593  CG2 ILE A6866      92.644  15.175  17.265  1.00 20.13           C  
ANISOU  593  CG2 ILE A6866     3143   2159   2345    -89    152   -504       C  
ATOM    594  CD1 ILE A6866      91.601  12.167  17.446  1.00 21.40           C  
ANISOU  594  CD1 ILE A6866     3376   2213   2541    -47     25   -508       C  
ATOM    595  N   HIS A6867      88.615  15.963  17.866  1.00 17.35           N  
ANISOU  595  N   HIS A6867     2885   1817   1891   -166      0   -283       N  
ATOM    596  CA  HIS A6867      87.835  16.616  18.940  1.00 17.37           C  
ANISOU  596  CA  HIS A6867     2855   1835   1909   -164    -30   -219       C  
ATOM    597  C   HIS A6867      87.554  15.630  20.080  1.00 17.12           C  
ANISOU  597  C   HIS A6867     2808   1780   1917   -136    -71   -195       C  
ATOM    598  O   HIS A6867      86.718  14.734  19.898  1.00 18.26           O  
ANISOU  598  O   HIS A6867     2978   1892   2066   -152   -107   -174       O  
ATOM    599  CB  HIS A6867      86.578  17.217  18.305  1.00 17.27           C  
ANISOU  599  CB  HIS A6867     2873   1827   1859   -204    -55   -172       C  
ATOM    600  CG  HIS A6867      85.669  17.890  19.274  1.00 17.12           C  
ANISOU  600  CG  HIS A6867     2817   1823   1862   -202    -77   -115       C  
ATOM    601  ND1 HIS A6867      84.299  17.914  19.102  1.00 17.44           N  
ANISOU  601  ND1 HIS A6867     2863   1855   1905   -227   -121    -70       N  
ATOM    602  CD2 HIS A6867      85.920  18.514  20.445  1.00 17.05           C  
ANISOU  602  CD2 HIS A6867     2764   1835   1877   -177    -63   -103       C  
ATOM    603  CE1 HIS A6867      83.752  18.561  20.113  1.00 17.34           C  
ANISOU  603  CE1 HIS A6867     2807   1859   1920   -216   -119    -33       C  
ATOM    604  NE2 HIS A6867      84.723  18.939  20.949  1.00 16.92           N  
ANISOU  604  NE2 HIS A6867     2729   1825   1872   -186    -84    -53       N  
ATOM    605  N   PHE A6868      88.226  15.830  21.216  1.00 17.43           N  
ANISOU  605  N   PHE A6868     2808   1831   1982    -97    -69   -198       N  
ATOM    606  CA  PHE A6868      88.064  14.982  22.423  1.00 17.69           C  
ANISOU  606  CA  PHE A6868     2839   1842   2038    -66   -107   -166       C  
ATOM    607  C   PHE A6868      87.019  15.605  23.350  1.00 17.19           C  
ANISOU  607  C   PHE A6868     2768   1803   1959    -77   -112   -101       C  
ATOM    608  O   PHE A6868      86.913  16.846  23.402  1.00 16.96           O  
ANISOU  608  O   PHE A6868     2716   1810   1915    -85    -91    -99       O  
ATOM    609  CB  PHE A6868      89.400  14.811  23.147  1.00 18.47           C  
ANISOU  609  CB  PHE A6868     2910   1940   2167    -12   -114   -208       C  
ATOM    610  CG  PHE A6868      90.435  14.039  22.370  1.00 19.53           C  
ANISOU  610  CG  PHE A6868     3039   2044   2335      7   -106   -278       C  
ATOM    611  CD1 PHE A6868      90.387  12.656  22.310  1.00 20.51           C  
ANISOU  611  CD1 PHE A6868     3193   2113   2485     23   -139   -281       C  
ATOM    612  CD2 PHE A6868      91.467  14.696  21.715  1.00 20.25           C  
ANISOU  612  CD2 PHE A6868     3093   2157   2441      8    -58   -344       C  
ATOM    613  CE1 PHE A6868      91.345  11.943  21.603  1.00 21.17           C  
ANISOU  613  CE1 PHE A6868     3269   2166   2608     48   -128   -356       C  
ATOM    614  CE2 PHE A6868      92.428  13.980  21.018  1.00 20.83           C  
ANISOU  614  CE2 PHE A6868     3155   2205   2553     28    -37   -416       C  
ATOM    615  CZ  PHE A6868      92.363  12.609  20.961  1.00 21.07           C  
ANISOU  615  CZ  PHE A6868     3214   2182   2608     52    -73   -426       C  
ATOM    616  N   GLY A6869      86.282  14.757  24.071  1.00 17.27           N  
ANISOU  616  N   GLY A6869     2797   1789   1976    -78   -134    -51       N  
ATOM    617  CA  GLY A6869      85.228  15.225  24.988  1.00 17.03           C  
ANISOU  617  CA  GLY A6869     2758   1780   1932    -90   -123      8       C  
ATOM    618  C   GLY A6869      84.079  15.834  24.214  1.00 17.11           C  
ANISOU  618  C   GLY A6869     2751   1800   1947   -136   -114     26       C  
ATOM    619  O   GLY A6869      83.538  16.858  24.666  1.00 17.06           O  
ANISOU  619  O   GLY A6869     2719   1828   1935   -138    -94     45       O  
ATOM    620  N   ALA A6870      83.727  15.221  23.080  1.00 16.96           N  
ANISOU  620  N   ALA A6870     2749   1749   1942   -167   -135     15       N  
ATOM    621  CA  ALA A6870      82.691  15.747  22.158  1.00 17.41           C  
ANISOU  621  CA  ALA A6870     2797   1811   2006   -208   -149     26       C  
ATOM    622  C   ALA A6870      81.274  15.318  22.555  1.00 18.59           C  
ANISOU  622  C   ALA A6870     2923   1943   2197   -239   -161     78       C  
ATOM    623  O   ALA A6870      80.317  15.863  21.976  1.00 19.03           O  
ANISOU  623  O   ALA A6870     2955   2004   2271   -266   -181     89       O  
ATOM    624  CB  ALA A6870      83.007  15.279  20.762  1.00 17.83           C  
ANISOU  624  CB  ALA A6870     2889   1841   2044   -225   -173    -16       C  
ATOM    625  N   GLY A6871      81.140  14.357  23.467  1.00 19.17           N  
ANISOU  625  N   GLY A6871     3002   1990   2290   -237   -151    109       N  
ATOM    626  CA  GLY A6871      79.809  13.886  23.882  1.00 20.90           C  
ANISOU  626  CA  GLY A6871     3193   2188   2561   -276   -146    160       C  
ATOM    627  C   GLY A6871      79.178  14.813  24.907  1.00 22.87           C  
ANISOU  627  C   GLY A6871     3398   2480   2809   -268    -97    195       C  
ATOM    628  O   GLY A6871      79.782  15.835  25.262  1.00 23.18           O  
ANISOU  628  O   GLY A6871     3436   2564   2807   -233    -77    176       O  
ATOM    629  N   SER A6872      77.993  14.457  25.380  1.00 24.59           N  
ANISOU  629  N   SER A6872     3580   2684   3079   -304    -73    240       N  
ATOM    630  CA  SER A6872      77.285  15.293  26.379  1.00 24.94           C  
ANISOU  630  CA  SER A6872     3577   2768   3127   -298    -11    267       C  
ATOM    631  C   SER A6872      76.206  14.439  27.028  1.00 25.97           C  
ANISOU  631  C   SER A6872     3682   2870   3314   -342     32    321       C  
ATOM    632  O   SER A6872      75.895  13.362  26.473  1.00 24.25           O  
ANISOU  632  O   SER A6872     3470   2596   3148   -382     -1    332       O  
ATOM    633  CB  SER A6872      76.678  16.523  25.753  1.00 25.14           C  
ANISOU  633  CB  SER A6872     3545   2822   3182   -297    -27    243       C  
ATOM    634  OG  SER A6872      75.586  16.184  24.914  1.00 26.66           O  
ANISOU  634  OG  SER A6872     3691   2982   3455   -342    -68    248       O  
ATOM    635  N   ASP A6873      75.651  14.928  28.135  1.00 28.20           N  
ANISOU  635  N   ASP A6873     3936   3187   3589   -337    110    350       N  
ATOM    636  CA  ASP A6873      74.555  14.211  28.834  1.00 31.81           C  
ANISOU  636  CA  ASP A6873     4362   3621   4103   -385    178    405       C  
ATOM    637  C   ASP A6873      73.314  14.215  27.932  1.00 31.88           C  
ANISOU  637  C   ASP A6873     4275   3604   4233   -436    149    395       C  
ATOM    638  O   ASP A6873      72.369  13.480  28.243  1.00 34.83           O  
ANISOU  638  O   ASP A6873     4606   3943   4683   -490    193    435       O  
ATOM    639  CB  ASP A6873      74.285  14.825  30.212  1.00 35.23           C  
ANISOU  639  CB  ASP A6873     4793   4105   4488   -365    280    429       C  
ATOM    640  CG  ASP A6873      73.908  16.298  30.206  1.00 39.11           C  
ANISOU  640  CG  ASP A6873     5218   4650   4990   -334    298    385       C  
ATOM    641  OD1 ASP A6873      73.724  16.870  29.108  1.00 40.95           O  
ANISOU  641  OD1 ASP A6873     5402   4879   5279   -334    229    346       O  
ATOM    642  OD2 ASP A6873      73.803  16.869  31.312  1.00 46.30           O  
ANISOU  642  OD2 ASP A6873     6135   5605   5850   -309    378    389       O  
ATOM    643  N   LYS A6874      73.342  14.996  26.845  1.00 30.73           N  
ANISOU  643  N   LYS A6874     4100   3470   4105   -420     74    346       N  
ATOM    644  CA  LYS A6874      72.203  15.095  25.888  1.00 31.23           C  
ANISOU  644  CA  LYS A6874     4076   3509   4279   -458     18    330       C  
ATOM    645  C   LYS A6874      72.276  13.956  24.857  1.00 29.40           C  
ANISOU  645  C   LYS A6874     3874   3215   4079   -497    -66    320       C  
ATOM    646  O   LYS A6874      71.285  13.762  24.134  1.00 30.49           O  
ANISOU  646  O   LYS A6874     3945   3322   4315   -538   -121    309       O  
ATOM    647  CB  LYS A6874      72.240  16.432  25.135  1.00 32.76           C  
ANISOU  647  CB  LYS A6874     4246   3736   4465   -420    -37    288       C  
ATOM    648  CG  LYS A6874      72.205  17.702  25.980  1.00 35.20           C  
ANISOU  648  CG  LYS A6874     4525   4098   4751   -375     28    282       C  
ATOM    649  CD  LYS A6874      72.347  18.959  25.135  1.00 37.22           C  
ANISOU  649  CD  LYS A6874     4771   4368   5001   -339    -37    246       C  
ATOM    650  CE  LYS A6874      72.430  20.242  25.938  1.00 39.23           C  
ANISOU  650  CE  LYS A6874     5004   4665   5236   -291     20    230       C  
ATOM    651  NZ  LYS A6874      71.192  20.494  26.711  1.00 42.29           N  
ANISOU  651  NZ  LYS A6874     5291   5062   5712   -298     90    238       N  
ATOM    652  N   GLY A6875      73.417  13.263  24.765  1.00 25.84           N  
ANISOU  652  N   GLY A6875     3518   2746   3553   -482    -83    316       N  
ATOM    653  CA  GLY A6875      73.611  12.177  23.784  1.00 25.45           C  
ANISOU  653  CA  GLY A6875     3508   2634   3525   -511   -160    293       C  
ATOM    654  C   GLY A6875      73.902  12.704  22.383  1.00 24.06           C  
ANISOU  654  C   GLY A6875     3353   2468   3319   -495   -253    235       C  
ATOM    655  O   GLY A6875      73.891  11.891  21.433  1.00 24.20           O  
ANISOU  655  O   GLY A6875     3399   2437   3356   -521   -325    205       O  
ATOM    656  N   VAL A6876      74.144  14.013  22.259  1.00 22.29           N  
ANISOU  656  N   VAL A6876     3121   2298   3047   -455   -251    221       N  
ATOM    657  CA  VAL A6876      74.469  14.665  20.953  1.00 22.00           C  
ANISOU  657  CA  VAL A6876     3119   2274   2966   -440   -329    177       C  
ATOM    658  C   VAL A6876      75.795  15.428  21.117  1.00 21.25           C  
ANISOU  658  C   VAL A6876     3082   2221   2770   -389   -291    162       C  
ATOM    659  O   VAL A6876      76.322  15.467  22.243  1.00 21.59           O  
ANISOU  659  O   VAL A6876     3128   2284   2788   -365   -220    181       O  
ATOM    660  CB  VAL A6876      73.312  15.562  20.468  1.00 22.18           C  
ANISOU  660  CB  VAL A6876     3069   2305   3051   -448   -380    178       C  
ATOM    661  CG1 VAL A6876      72.070  14.739  20.154  1.00 24.01           C  
ANISOU  661  CG1 VAL A6876     3237   2490   3396   -501   -433    180       C  
ATOM    662  CG2 VAL A6876      72.979  16.662  21.461  1.00 22.21           C  
ANISOU  662  CG2 VAL A6876     3009   2351   3075   -420   -310    202       C  
ATOM    663  N   ALA A6877      76.315  16.008  20.034  1.00 20.51           N  
ANISOU  663  N   ALA A6877     3035   2138   2619   -376   -336    129       N  
ATOM    664  CA  ALA A6877      77.632  16.685  20.053  1.00 19.64           C  
ANISOU  664  CA  ALA A6877     2975   2060   2426   -338   -298    109       C  
ATOM    665  C   ALA A6877      77.495  18.103  19.508  1.00 19.52           C  
ANISOU  665  C   ALA A6877     2956   2071   2390   -324   -317    109       C  
ATOM    666  O   ALA A6877      77.779  18.352  18.335  1.00 18.58           O  
ANISOU  666  O   ALA A6877     2892   1947   2222   -330   -360     89       O  
ATOM    667  CB  ALA A6877      78.610  15.870  19.244  1.00 19.94           C  
ANISOU  667  CB  ALA A6877     3087   2078   2411   -339   -314     67       C  
ATOM    668  N   PRO A6878      77.021  19.059  20.338  1.00 19.47           N  
ANISOU  668  N   PRO A6878     2890   2087   2418   -306   -285    132       N  
ATOM    669  CA  PRO A6878      76.855  20.446  19.907  1.00 19.74           C  
ANISOU  669  CA  PRO A6878     2918   2133   2447   -289   -305    136       C  
ATOM    670  C   PRO A6878      78.172  21.049  19.391  1.00 18.59           C  
ANISOU  670  C   PRO A6878     2841   2000   2220   -274   -285    115       C  
ATOM    671  O   PRO A6878      78.173  21.657  18.325  1.00 18.18           O  
ANISOU  671  O   PRO A6878     2832   1938   2136   -280   -328    116       O  
ATOM    672  CB  PRO A6878      76.361  21.169  21.172  1.00 20.54           C  
ANISOU  672  CB  PRO A6878     2946   2257   2600   -265   -252    151       C  
ATOM    673  CG  PRO A6878      75.766  20.079  22.030  1.00 21.42           C  
ANISOU  673  CG  PRO A6878     3017   2364   2758   -284   -219    167       C  
ATOM    674  CD  PRO A6878      76.579  18.840  21.725  1.00 20.49           C  
ANISOU  674  CD  PRO A6878     2962   2228   2594   -300   -225    156       C  
ATOM    675  N   GLY A6879      79.266  20.846  20.135  1.00 17.78           N  
ANISOU  675  N   GLY A6879     2751   1916   2088   -256   -223     96       N  
ATOM    676  CA  GLY A6879      80.577  21.373  19.718  1.00 17.47           C  
ANISOU  676  CA  GLY A6879     2759   1887   1992   -247   -193     69       C  
ATOM    677  C   GLY A6879      81.008  20.808  18.376  1.00 17.52           C  
ANISOU  677  C   GLY A6879     2835   1876   1944   -270   -218     48       C  
ATOM    678  O   GLY A6879      81.508  21.583  17.534  1.00 17.17           O  
ANISOU  678  O   GLY A6879     2835   1832   1854   -276   -212     44       O  
ATOM    679  N   THR A6880      80.803  19.506  18.157  1.00 17.24           N  
ANISOU  679  N   THR A6880     2814   1823   1912   -284   -243     36       N  
ATOM    680  CA  THR A6880      81.201  18.918  16.851  1.00 17.70           C  
ANISOU  680  CA  THR A6880     2947   1866   1913   -303   -265      4       C  
ATOM    681  C   THR A6880      80.384  19.569  15.732  1.00 18.23           C  
ANISOU  681  C   THR A6880     3052   1924   1950   -323   -330     24       C  
ATOM    682  O   THR A6880      80.954  19.823  14.668  1.00 18.83           O  
ANISOU  682  O   THR A6880     3204   2001   1949   -333   -326      7       O  
ATOM    683  CB  THR A6880      81.022  17.397  16.829  1.00 18.19           C  
ANISOU  683  CB  THR A6880     3016   1898   1995   -314   -290    -17       C  
ATOM    684  OG1 THR A6880      81.972  16.827  17.727  1.00 18.63           O  
ANISOU  684  OG1 THR A6880     3055   1957   2067   -289   -236    -36       O  
ATOM    685  CG2 THR A6880      81.220  16.806  15.452  1.00 18.94           C  
ANISOU  685  CG2 THR A6880     3190   1975   2031   -334   -323    -59       C  
ATOM    686  N   ALA A6881      79.091  19.801  15.963  1.00 18.25           N  
ANISOU  686  N   ALA A6881     3005   1917   2013   -328   -389     59       N  
ATOM    687  CA  ALA A6881      78.246  20.450  14.934  1.00 18.95           C  
ANISOU  687  CA  ALA A6881     3125   1992   2084   -339   -473     80       C  
ATOM    688  C   ALA A6881      78.822  21.837  14.601  1.00 18.69           C  
ANISOU  688  C   ALA A6881     3131   1969   2000   -327   -444    101       C  
ATOM    689  O   ALA A6881      78.852  22.207  13.401  1.00 19.15           O  
ANISOU  689  O   ALA A6881     3276   2016   1982   -339   -487    109       O  
ATOM    690  CB  ALA A6881      76.820  20.519  15.422  1.00 19.28           C  
ANISOU  690  CB  ALA A6881     3079   2020   2226   -339   -532    108       C  
ATOM    691  N   VAL A6882      79.282  22.579  15.611  1.00 18.16           N  
ANISOU  691  N   VAL A6882     3012   1917   1968   -305   -376    109       N  
ATOM    692  CA  VAL A6882      79.879  23.923  15.350  1.00 18.19           C  
ANISOU  692  CA  VAL A6882     3050   1921   1940   -298   -344    127       C  
ATOM    693  C   VAL A6882      81.208  23.747  14.599  1.00 18.37           C  
ANISOU  693  C   VAL A6882     3153   1952   1874   -316   -283     99       C  
ATOM    694  O   VAL A6882      81.444  24.510  13.639  1.00 18.44           O  
ANISOU  694  O   VAL A6882     3238   1948   1820   -331   -286    121       O  
ATOM    695  CB  VAL A6882      80.068  24.724  16.653  1.00 17.63           C  
ANISOU  695  CB  VAL A6882     2902   1862   1935   -272   -290    129       C  
ATOM    696  CG1 VAL A6882      80.850  26.005  16.421  1.00 18.05           C  
ANISOU  696  CG1 VAL A6882     2986   1905   1965   -271   -250    139       C  
ATOM    697  CG2 VAL A6882      78.734  25.020  17.323  1.00 17.40           C  
ANISOU  697  CG2 VAL A6882     2793   1825   1991   -253   -335    152       C  
ATOM    698  N   LEU A6883      82.047  22.787  15.009  1.00 18.01           N  
ANISOU  698  N   LEU A6883     3093   1921   1826   -314   -228     54       N  
ATOM    699  CA  LEU A6883      83.352  22.603  14.307  1.00 18.82           C  
ANISOU  699  CA  LEU A6883     3257   2032   1860   -329   -158     17       C  
ATOM    700  C   LEU A6883      83.103  22.246  12.836  1.00 20.12           C  
ANISOU  700  C   LEU A6883     3525   2185   1932   -355   -197     15       C  
ATOM    701  O   LEU A6883      83.843  22.742  11.968  1.00 20.68           O  
ANISOU  701  O   LEU A6883     3671   2258   1927   -374   -146     12       O  
ATOM    702  CB  LEU A6883      84.189  21.522  15.001  1.00 18.60           C  
ANISOU  702  CB  LEU A6883     3188   2016   1861   -313   -110    -35       C  
ATOM    703  CG  LEU A6883      84.706  21.862  16.398  1.00 18.22           C  
ANISOU  703  CG  LEU A6883     3058   1982   1882   -285    -69    -41       C  
ATOM    704  CD1 LEU A6883      85.405  20.668  17.022  1.00 18.58           C  
ANISOU  704  CD1 LEU A6883     3075   2031   1953   -264    -47    -86       C  
ATOM    705  CD2 LEU A6883      85.644  23.055  16.361  1.00 18.80           C  
ANISOU  705  CD2 LEU A6883     3128   2062   1953   -290     -7    -46       C  
ATOM    706  N  AARG A6884      82.098  21.399  12.575  0.50 20.71           N  
ANISOU  706  N  AARG A6884     3608   2248   2013   -358   -283     13       N  
ATOM    707  N  BARG A6884      82.088  21.413  12.586  0.50 20.87           N  
ANISOU  707  N  BARG A6884     3627   2268   2033   -358   -283     14       N  
ATOM    708  CA AARG A6884      81.745  20.967  11.191  0.50 22.17           C  
ANISOU  708  CA AARG A6884     3897   2421   2104   -380   -342      2       C  
ATOM    709  CA BARG A6884      81.714  20.961  11.219  0.50 22.44           C  
ANISOU  709  CA BARG A6884     3928   2454   2141   -379   -344      3       C  
ATOM    710  C  AARG A6884      81.283  22.189  10.387  0.50 22.21           C  
ANISOU  710  C  AARG A6884     3971   2416   2052   -389   -389     59       C  
ATOM    711  C  BARG A6884      81.272  22.177  10.395  0.50 22.37           C  
ANISOU  711  C  BARG A6884     3990   2436   2073   -389   -390     59       C  
ATOM    712  O  AARG A6884      81.576  22.253   9.179  0.50 22.87           O  
ANISOU  712  O  AARG A6884     4172   2498   2019   -408   -390     55       O  
ATOM    713  O  BARG A6884      81.570  22.226   9.187  0.50 23.04           O  
ANISOU  713  O  BARG A6884     4192   2519   2041   -408   -391     54       O  
ATOM    714  CB AARG A6884      80.652  19.893  11.240  0.50 23.26           C  
ANISOU  714  CB AARG A6884     4007   2539   2289   -382   -439    -11       C  
ATOM    715  CB BARG A6884      80.597  19.919  11.337  0.50 23.74           C  
ANISOU  715  CB BARG A6884     4059   2600   2359   -381   -441     -8       C  
ATOM    716  CG AARG A6884      80.138  19.433   9.882  0.50 25.71           C  
ANISOU  716  CG AARG A6884     4421   2834   2512   -402   -527    -30       C  
ATOM    717  CG BARG A6884      80.220  19.219  10.042  0.50 26.33           C  
ANISOU  717  CG BARG A6884     4486   2912   2603   -401   -517    -38       C  
ATOM    718  CD AARG A6884      81.020  18.383   9.238  0.50 27.09           C  
ANISOU  718  CD AARG A6884     4668   3011   2613   -412   -478   -102       C  
ATOM    719  CD BARG A6884      81.315  18.264   9.640  0.50 27.72           C  
ANISOU  719  CD BARG A6884     4717   3095   2721   -406   -443   -109       C  
ATOM    720  NE AARG A6884      82.369  18.877   9.020  0.50 27.90           N  
ANISOU  720  NE AARG A6884     4812   3138   2649   -411   -354   -116       N  
ATOM    721  NE BARG A6884      80.903  17.285   8.651  0.50 29.17           N  
ANISOU  721  NE BARG A6884     4977   3257   2846   -421   -517   -157       N  
ATOM    722  CZ AARG A6884      83.401  18.115   8.685  0.50 28.51           C  
ANISOU  722  CZ AARG A6884     4925   3221   2684   -411   -274   -185       C  
ATOM    723  CZ BARG A6884      81.698  16.321   8.220  0.50 31.06           C  
ANISOU  723  CZ BARG A6884     5267   3494   3041   -422   -467   -231       C  
ATOM    724  NH1AARG A6884      83.239  16.813   8.538  0.50 28.97           N  
ANISOU  724  NH1AARG A6884     4991   3260   2756   -408   -311   -244       N  
ATOM    725  NH1BARG A6884      81.274  15.450   7.320  0.50 32.24           N  
ANISOU  725  NH1BARG A6884     5490   3620   3137   -435   -542   -283       N  
ATOM    726  NH2AARG A6884      84.594  18.656   8.520  0.50 28.31           N  
ANISOU  726  NH2AARG A6884     4921   3218   2617   -413   -156   -197       N  
ATOM    727  NH2BARG A6884      82.925  16.238   8.704  0.50 31.26           N  
ANISOU  727  NH2BARG A6884     5262   3535   3081   -407   -346   -259       N  
ATOM    728  N   GLN A6885      80.592  23.125  11.043  1.00 21.52           N  
ANISOU  728  N   GLN A6885     3817   2319   2041   -373   -425    109       N  
ATOM    729  CA  GLN A6885      80.106  24.360  10.372  1.00 21.73           C  
ANISOU  729  CA  GLN A6885     3902   2322   2030   -373   -481    170       C  
ATOM    730  C   GLN A6885      81.290  25.290  10.063  1.00 21.50           C  
ANISOU  730  C   GLN A6885     3934   2294   1938   -388   -377    186       C  
ATOM    731  O   GLN A6885      81.332  25.889   8.979  1.00 21.36           O  
ANISOU  731  O   GLN A6885     4031   2260   1823   -406   -396    225       O  
ATOM    732  CB  GLN A6885      79.116  25.060  11.303  1.00 21.30           C  
ANISOU  732  CB  GLN A6885     3742   2253   2097   -345   -534    206       C  
ATOM    733  CG  GLN A6885      78.680  26.430  10.822  1.00 21.94           C  
ANISOU  733  CG  GLN A6885     3866   2301   2169   -336   -589    268       C  
ATOM    734  CD  GLN A6885      77.811  27.137  11.832  1.00 21.87           C  
ANISOU  734  CD  GLN A6885     3740   2276   2293   -302   -623    289       C  
ATOM    735  OE1 GLN A6885      77.687  26.712  12.977  1.00 22.09           O  
ANISOU  735  OE1 GLN A6885     3660   2324   2406   -289   -582    259       O  
ATOM    736  NE2 GLN A6885      77.213  28.238  11.409  1.00 22.23           N  
ANISOU  736  NE2 GLN A6885     3812   2282   2351   -285   -696    342       N  
ATOM    737  N   TRP A6886      82.220  25.380  11.007  1.00 20.18           N  
ANISOU  737  N   TRP A6886     3693   2144   1828   -383   -273    159       N  
ATOM    738  CA  TRP A6886      83.390  26.296  10.959  1.00 20.38           C  
ANISOU  738  CA  TRP A6886     3740   2168   1834   -400   -166    166       C  
ATOM    739  C   TRP A6886      84.458  25.844   9.956  1.00 21.04           C  
ANISOU  739  C   TRP A6886     3917   2266   1811   -433    -79    134       C  
ATOM    740  O   TRP A6886      84.923  26.683   9.157  1.00 21.58           O  
ANISOU  740  O   TRP A6886     4072   2318   1807   -462    -31    170       O  
ATOM    741  CB  TRP A6886      83.966  26.369  12.377  1.00 19.61           C  
ANISOU  741  CB  TRP A6886     3521   2085   1844   -380   -103    133       C  
ATOM    742  CG  TRP A6886      85.172  27.236  12.527  1.00 19.56           C  
ANISOU  742  CG  TRP A6886     3506   2074   1850   -397      0    126       C  
ATOM    743  CD1 TRP A6886      85.258  28.572  12.268  1.00 20.38           C  
ANISOU  743  CD1 TRP A6886     3643   2144   1956   -413     14    176       C  
ATOM    744  CD2 TRP A6886      86.442  26.852  13.083  1.00 19.72           C  
ANISOU  744  CD2 TRP A6886     3470   2117   1905   -398     94     64       C  
ATOM    745  NE1 TRP A6886      86.507  29.033  12.578  1.00 20.33           N  
ANISOU  745  NE1 TRP A6886     3603   2137   1982   -432    119    147       N  
ATOM    746  CE2 TRP A6886      87.254  28.005  13.082  1.00 19.98           C  
ANISOU  746  CE2 TRP A6886     3498   2129   1960   -422    167     76       C  
ATOM    747  CE3 TRP A6886      86.974  25.654  13.571  1.00 19.47           C  
ANISOU  747  CE3 TRP A6886     3387   2113   1894   -381    119      1       C  
ATOM    748  CZ2 TRP A6886      88.566  27.992  13.552  1.00 20.32           C  
ANISOU  748  CZ2 TRP A6886     3480   2186   2055   -430    260     20       C  
ATOM    749  CZ3 TRP A6886      88.274  25.641  14.029  1.00 19.88           C  
ANISOU  749  CZ3 TRP A6886     3383   2176   1991   -381    205    -51       C  
ATOM    750  CH2 TRP A6886      89.059  26.794  14.011  1.00 20.05           C  
ANISOU  750  CH2 TRP A6886     3392   2183   2040   -406    274    -45       C  
ATOM    751  N   LEU A6887      84.833  24.567  10.013  1.00 21.58           N  
ANISOU  751  N   LEU A6887     3968   2359   1872   -428    -55     67       N  
ATOM    752  CA  LEU A6887      85.955  24.038   9.194  1.00 22.27           C  
ANISOU  752  CA  LEU A6887     4123   2463   1875   -452     45     16       C  
ATOM    753  C   LEU A6887      85.600  23.992   7.713  1.00 24.27           C  
ANISOU  753  C   LEU A6887     4529   2709   1981   -478     12     35       C  
ATOM    754  O   LEU A6887      84.461  23.729   7.331  1.00 25.13           O  
ANISOU  754  O   LEU A6887     4681   2807   2059   -470   -111     58       O  
ATOM    755  CB  LEU A6887      86.331  22.654   9.720  1.00 21.48           C  
ANISOU  755  CB  LEU A6887     3957   2379   1822   -430     61    -62       C  
ATOM    756  CG  LEU A6887      86.872  22.637  11.148  1.00 20.89           C  
ANISOU  756  CG  LEU A6887     3750   2312   1873   -403     98    -84       C  
ATOM    757  CD1 LEU A6887      86.837  21.230  11.716  1.00 20.84           C  
ANISOU  757  CD1 LEU A6887     3693   2310   1915   -375     71   -138       C  
ATOM    758  CD2 LEU A6887      88.276  23.220  11.207  1.00 20.84           C  
ANISOU  758  CD2 LEU A6887     3718   2316   1884   -417    223   -112       C  
ATOM    759  N   PRO A6888      86.592  24.235   6.834  1.00 26.01           N  
ANISOU  759  N   PRO A6888     4837   2939   2106   -511    126     23       N  
ATOM    760  CA  PRO A6888      86.362  24.185   5.393  1.00 27.82           C  
ANISOU  760  CA  PRO A6888     5233   3167   2169   -537    108     39       C  
ATOM    761  C   PRO A6888      85.821  22.821   4.937  1.00 29.10           C  
ANISOU  761  C   PRO A6888     5435   3339   2280   -521     28    -23       C  
ATOM    762  O   PRO A6888      86.192  21.807   5.515  1.00 27.78           O  
ANISOU  762  O   PRO A6888     5183   3183   2186   -502     56    -97       O  
ATOM    763  CB  PRO A6888      87.752  24.408   4.780  1.00 29.04           C  
ANISOU  763  CB  PRO A6888     5441   3336   2254   -574    285     12       C  
ATOM    764  CG  PRO A6888      88.582  25.033   5.871  1.00 28.03           C  
ANISOU  764  CG  PRO A6888     5174   3205   2269   -574    375      9       C  
ATOM    765  CD  PRO A6888      87.985  24.560   7.178  1.00 26.01           C  
ANISOU  765  CD  PRO A6888     4779   2949   2152   -527    278     -9       C  
ATOM    766  N   THR A6889      84.961  22.822   3.915  1.00 32.00           N  
ANISOU  766  N   THR A6889     5933   3696   2527   -529    -76      5       N  
ATOM    767  CA  THR A6889      84.442  21.544   3.360  1.00 33.56           C  
ANISOU  767  CA  THR A6889     6182   3897   2668   -519   -160    -62       C  
ATOM    768  C   THR A6889      85.661  20.705   2.955  1.00 32.90           C  
ANISOU  768  C   THR A6889     6131   3839   2529   -529    -17   -157       C  
ATOM    769  O   THR A6889      86.635  21.292   2.438  1.00 33.87           O  
ANISOU  769  O   THR A6889     6318   3977   2573   -556    121   -150       O  
ATOM    770  CB  THR A6889      83.462  21.807   2.208  1.00 38.03           C  
ANISOU  770  CB  THR A6889     6903   4450   3096   -528   -296    -18       C  
ATOM    771  OG1 THR A6889      82.473  22.729   2.671  1.00 40.78           O  
ANISOU  771  OG1 THR A6889     7201   4771   3522   -513   -412     69       O  
ATOM    772  CG2 THR A6889      82.787  20.551   1.703  1.00 39.02           C  
ANISOU  772  CG2 THR A6889     7071   4572   3182   -518   -409    -91       C  
ATOM    773  N   GLY A6890      85.635  19.399   3.226  1.00 32.22           N  
ANISOU  773  N   GLY A6890     5993   3752   2497   -508    -41   -243       N  
ATOM    774  CA  GLY A6890      86.781  18.527   2.900  1.00 32.21           C  
ANISOU  774  CA  GLY A6890     6006   3767   2464   -507     89   -345       C  
ATOM    775  C   GLY A6890      87.644  18.268   4.124  1.00 30.51           C  
ANISOU  775  C   GLY A6890     5625   3553   2411   -484    179   -379       C  
ATOM    776  O   GLY A6890      88.467  17.331   4.094  1.00 30.33           O  
ANISOU  776  O   GLY A6890     5578   3533   2410   -469    258   -473       O  
ATOM    777  N   THR A6891      87.479  19.084   5.164  1.00 27.87           N  
ANISOU  777  N   THR A6891     5185   3215   2188   -478    162   -309       N  
ATOM    778  CA  THR A6891      88.253  18.867   6.410  1.00 26.84           C  
ANISOU  778  CA  THR A6891     4902   3085   2208   -452    227   -339       C  
ATOM    779  C   THR A6891      87.832  17.535   7.031  1.00 26.21           C  
ANISOU  779  C   THR A6891     4759   2986   2214   -419    147   -390       C  
ATOM    780  O   THR A6891      86.616  17.271   7.120  1.00 25.54           O  
ANISOU  780  O   THR A6891     4683   2882   2139   -417     18   -357       O  
ATOM    781  CB  THR A6891      88.033  20.001   7.416  1.00 25.64           C  
ANISOU  781  CB  THR A6891     4661   2931   2147   -450    209   -259       C  
ATOM    782  OG1 THR A6891      88.498  21.218   6.833  1.00 25.97           O  
ANISOU  782  OG1 THR A6891     4764   2982   2122   -484    289   -212       O  
ATOM    783  CG2 THR A6891      88.749  19.768   8.726  1.00 25.14           C  
ANISOU  783  CG2 THR A6891     4454   2871   2227   -420    253   -290       C  
ATOM    784  N  ALEU A6892      88.809  16.704   7.406  0.50 25.98           N  
ANISOU  784  N  ALEU A6892     4666   2953   2249   -393    221   -468       N  
ATOM    785  N  BLEU A6892      88.812  16.731   7.444  0.50 26.74           N  
ANISOU  785  N  BLEU A6892     4759   3050   2349   -393    222   -466       N  
ATOM    786  CA ALEU A6892      88.501  15.422   8.092  0.50 25.51           C  
ANISOU  786  CA ALEU A6892     4546   2862   2283   -360    151   -510       C  
ATOM    787  CA BLEU A6892      88.522  15.429   8.091  0.50 26.81           C  
ANISOU  787  CA BLEU A6892     4710   3027   2448   -360    153   -510       C  
ATOM    788  C  ALEU A6892      88.327  15.730   9.582  0.50 24.15           C  
ANISOU  788  C  ALEU A6892     4249   2686   2239   -339    117   -454       C  
ATOM    789  C  BLEU A6892      88.342  15.696   9.590  0.50 24.90           C  
ANISOU  789  C  BLEU A6892     4344   2780   2336   -338    118   -456       C  
ATOM    790  O  ALEU A6892      89.269  16.285  10.181  0.50 23.74           O  
ANISOU  790  O  ALEU A6892     4127   2651   2241   -327    197   -456       O  
ATOM    791  O  BLEU A6892      89.308  16.175  10.216  0.50 24.57           O  
ANISOU  791  O  BLEU A6892     4228   2754   2352   -324    197   -462       O  
ATOM    792  CB ALEU A6892      89.621  14.408   7.844  0.50 26.65           C  
ANISOU  792  CB ALEU A6892     4681   2996   2446   -335    236   -617       C  
ATOM    793  CB BLEU A6892      89.684  14.474   7.813  0.50 29.06           C  
ANISOU  793  CB BLEU A6892     4988   3305   2748   -336    245   -617       C  
ATOM    794  CG ALEU A6892      89.800  13.983   6.387  0.50 28.21           C  
ANISOU  794  CG ALEU A6892     5008   3199   2510   -353    278   -688       C  
ATOM    795  CG BLEU A6892      89.307  12.999   7.748  0.50 30.98           C  
ANISOU  795  CG BLEU A6892     5244   3504   3021   -314    173   -681       C  
ATOM    796  CD1ALEU A6892      90.918  12.962   6.249  0.50 29.28           C  
ANISOU  796  CD1ALEU A6892     5116   3321   2688   -319    367   -804       C  
ATOM    797  CD1BLEU A6892      88.293  12.761   6.637  0.50 32.21           C  
ANISOU  797  CD1BLEU A6892     5526   3652   3061   -344     90   -685       C  
ATOM    798  CD2ALEU A6892      88.503  13.426   5.825  0.50 29.21           C  
ANISOU  798  CD2ALEU A6892     5221   3301   2574   -367    141   -680       C  
ATOM    799  CD2BLEU A6892      90.539  12.135   7.533  0.50 32.38           C  
ANISOU  799  CD2BLEU A6892     5403   3669   3231   -281    269   -792       C  
ATOM    800  N   LEU A6893      87.147  15.423  10.125  1.00 23.15           N  
ANISOU  800  N   LEU A6893     4100   2538   2157   -337      6   -408       N  
ATOM    801  CA  LEU A6893      86.826  15.701  11.550  1.00 21.91           C  
ANISOU  801  CA  LEU A6893     3839   2379   2106   -318    -24   -353       C  
ATOM    802  C   LEU A6893      86.512  14.392  12.269  1.00 21.12           C  
ANISOU  802  C   LEU A6893     3697   2240   2087   -297    -78   -372       C  
ATOM    803  O   LEU A6893      85.567  13.681  11.860  1.00 21.77           O  
ANISOU  803  O   LEU A6893     3816   2293   2162   -313   -157   -374       O  
ATOM    804  CB  LEU A6893      85.639  16.668  11.609  1.00 21.93           C  
ANISOU  804  CB  LEU A6893     3847   2390   2095   -340    -94   -271       C  
ATOM    805  CG  LEU A6893      85.123  17.038  12.999  1.00 21.13           C  
ANISOU  805  CG  LEU A6893     3649   2290   2088   -324   -122   -214       C  
ATOM    806  CD1 LEU A6893      86.202  17.697  13.847  1.00 20.70           C  
ANISOU  806  CD1 LEU A6893     3531   2257   2074   -302    -42   -218       C  
ATOM    807  CD2 LEU A6893      83.911  17.953  12.873  1.00 21.60           C  
ANISOU  807  CD2 LEU A6893     3714   2353   2140   -342   -190   -147       C  
ATOM    808  N   VAL A6894      87.296  14.104  13.302  1.00 20.65           N  
ANISOU  808  N   VAL A6894     3563   2176   2105   -261    -41   -385       N  
ATOM    809  CA  VAL A6894      87.120  12.882  14.129  1.00 20.07           C  
ANISOU  809  CA  VAL A6894     3454   2058   2112   -237    -87   -391       C  
ATOM    810  C   VAL A6894      86.777  13.351  15.539  1.00 19.54           C  
ANISOU  810  C   VAL A6894     3315   2003   2106   -224   -105   -321       C  
ATOM    811  O   VAL A6894      87.395  14.333  15.999  1.00 18.49           O  
ANISOU  811  O   VAL A6894     3144   1906   1974   -211    -59   -309       O  
ATOM    812  CB  VAL A6894      88.388  12.008  14.108  1.00 20.74           C  
ANISOU  812  CB  VAL A6894     3527   2121   2233   -198    -38   -472       C  
ATOM    813  CG1 VAL A6894      88.346  10.923  15.174  1.00 21.35           C  
ANISOU  813  CG1 VAL A6894     3564   2147   2399   -164    -85   -463       C  
ATOM    814  CG2 VAL A6894      88.623  11.412  12.730  1.00 22.10           C  
ANISOU  814  CG2 VAL A6894     3775   2277   2342   -209    -17   -552       C  
ATOM    815  N   ASP A6895      85.815  12.701  16.185  1.00 19.32           N  
ANISOU  815  N   ASP A6895     3272   1943   2124   -230   -165   -278       N  
ATOM    816  CA  ASP A6895      85.513  13.116  17.574  1.00 18.96           C  
ANISOU  816  CA  ASP A6895     3168   1912   2123   -216   -168   -214       C  
ATOM    817  C   ASP A6895      85.477  11.876  18.464  1.00 19.41           C  
ANISOU  817  C   ASP A6895     3214   1919   2241   -196   -195   -202       C  
ATOM    818  O   ASP A6895      85.489  10.728  17.948  1.00 19.66           O  
ANISOU  818  O   ASP A6895     3279   1899   2292   -200   -220   -239       O  
ATOM    819  CB  ASP A6895      84.294  14.037  17.668  1.00 19.17           C  
ANISOU  819  CB  ASP A6895     3179   1963   2141   -247   -194   -152       C  
ATOM    820  CG  ASP A6895      82.969  13.412  17.306  1.00 19.89           C  
ANISOU  820  CG  ASP A6895     3282   2021   2255   -284   -258   -129       C  
ATOM    821  OD1 ASP A6895      82.941  12.189  17.015  1.00 20.82           O  
ANISOU  821  OD1 ASP A6895     3425   2089   2394   -290   -285   -158       O  
ATOM    822  OD2 ASP A6895      81.970  14.165  17.307  1.00 20.43           O  
ANISOU  822  OD2 ASP A6895     3327   2106   2328   -305   -283    -86       O  
ATOM    823  N   SER A6896      85.438  12.118  19.770  1.00 19.12           N  
ANISOU  823  N   SER A6896     3139   1895   2230   -176   -189   -152       N  
ATOM    824  CA  SER A6896      85.557  11.010  20.730  1.00 19.87           C  
ANISOU  824  CA  SER A6896     3236   1942   2372   -152   -210   -129       C  
ATOM    825  C   SER A6896      84.996  11.427  22.084  1.00 19.56           C  
ANISOU  825  C   SER A6896     3170   1924   2335   -149   -204    -55       C  
ATOM    826  O   SER A6896      84.954  12.647  22.377  1.00 19.22           O  
ANISOU  826  O   SER A6896     3099   1937   2264   -146   -178    -43       O  
ATOM    827  CB  SER A6896      87.003  10.614  20.843  1.00 21.32           C  
ANISOU  827  CB  SER A6896     3417   2112   2570    -98   -199   -186       C  
ATOM    828  OG  SER A6896      87.141   9.391  21.552  1.00 24.55           O  
ANISOU  828  OG  SER A6896     3843   2459   3026    -72   -233   -168       O  
ATOM    829  N   ASP A6897      84.568  10.435  22.850  1.00 19.74           N  
ANISOU  829  N   ASP A6897     3208   1898   2391   -151   -222     -8       N  
ATOM    830  CA  ASP A6897      84.070  10.663  24.227  1.00 20.52           C  
ANISOU  830  CA  ASP A6897     3299   2014   2482   -147   -205     65       C  
ATOM    831  C   ASP A6897      84.036   9.316  24.937  1.00 21.00           C  
ANISOU  831  C   ASP A6897     3398   2004   2575   -140   -226    108       C  
ATOM    832  O   ASP A6897      83.954   8.277  24.260  1.00 20.92           O  
ANISOU  832  O   ASP A6897     3410   1928   2609   -156   -255     88       O  
ATOM    833  CB  ASP A6897      82.689  11.320  24.253  1.00 20.72           C  
ANISOU  833  CB  ASP A6897     3292   2067   2511   -196   -184    109       C  
ATOM    834  CG  ASP A6897      82.355  11.967  25.587  1.00 21.70           C  
ANISOU  834  CG  ASP A6897     3402   2233   2608   -184   -146    162       C  
ATOM    835  OD1 ASP A6897      81.967  11.236  26.536  1.00 22.99           O  
ANISOU  835  OD1 ASP A6897     3588   2367   2779   -189   -132    221       O  
ATOM    836  OD2 ASP A6897      82.544  13.193  25.690  1.00 20.88           O  
ANISOU  836  OD2 ASP A6897     3272   2188   2474   -167   -126    144       O  
ATOM    837  N   LEU A6898      84.094   9.364  26.259  1.00 21.96           N  
ANISOU  837  N   LEU A6898     3536   2136   2670   -116   -213    164       N  
ATOM    838  CA  LEU A6898      84.006   8.159  27.114  1.00 23.73           C  
ANISOU  838  CA  LEU A6898     3812   2291   2911   -110   -229    227       C  
ATOM    839  C   LEU A6898      82.629   7.509  26.923  1.00 23.71           C  
ANISOU  839  C   LEU A6898     3807   2241   2959   -183   -211    280       C  
ATOM    840  O   LEU A6898      82.548   6.269  26.924  1.00 23.16           O  
ANISOU  840  O   LEU A6898     3776   2085   2938   -196   -236    304       O  
ATOM    841  CB  LEU A6898      84.195   8.647  28.554  1.00 25.21           C  
ANISOU  841  CB  LEU A6898     4023   2520   3033    -75   -210    279       C  
ATOM    842  CG  LEU A6898      84.152   7.599  29.657  1.00 28.52           C  
ANISOU  842  CG  LEU A6898     4515   2879   3442    -63   -222    361       C  
ATOM    843  CD1 LEU A6898      85.289   6.600  29.506  1.00 30.21           C  
ANISOU  843  CD1 LEU A6898     4766   3021   3690     -9   -293    332       C  
ATOM    844  CD2 LEU A6898      84.213   8.276  31.021  1.00 29.92           C  
ANISOU  844  CD2 LEU A6898     4723   3113   3529    -33   -197    407       C  
ATOM    845  N   ASN A6899      81.600   8.336  26.726  1.00 23.38           N  
ANISOU  845  N   ASN A6899     3717   2249   2918   -228   -173    290       N  
ATOM    846  CA  ASN A6899      80.185   7.886  26.659  1.00 24.93           C  
ANISOU  846  CA  ASN A6899     3887   2409   3174   -301   -151    340       C  
ATOM    847  C   ASN A6899      79.637   7.985  25.234  1.00 25.09           C  
ANISOU  847  C   ASN A6899     3866   2422   3245   -341   -187    282       C  
ATOM    848  O   ASN A6899      80.053   8.882  24.484  1.00 23.11           O  
ANISOU  848  O   ASN A6899     3597   2223   2958   -320   -202    223       O  
ATOM    849  CB  ASN A6899      79.331   8.706  27.624  1.00 26.11           C  
ANISOU  849  CB  ASN A6899     4005   2617   3299   -319    -80    395       C  
ATOM    850  CG  ASN A6899      79.841   8.616  29.044  1.00 27.08           C  
ANISOU  850  CG  ASN A6899     4186   2750   3351   -279    -47    451       C  
ATOM    851  OD1 ASN A6899      80.112   7.523  29.535  1.00 27.27           O  
ANISOU  851  OD1 ASN A6899     4272   2707   3380   -276    -60    497       O  
ATOM    852  ND2 ASN A6899      79.987   9.758  29.699  1.00 27.26           N  
ANISOU  852  ND2 ASN A6899     4197   2853   3307   -247    -12    445       N  
ATOM    853  N  AASP A6900      78.714   7.082  24.893  0.60 25.80           N  
ANISOU  853  N  AASP A6900     3945   2444   3413   -401   -203    302       N  
ATOM    854  N  BASP A6900      78.697   7.089  24.906  0.40 25.87           N  
ANISOU  854  N  BASP A6900     3953   2453   3422   -402   -202    303       N  
ATOM    855  CA AASP A6900      78.126   7.031  23.530  0.60 26.41           C  
ANISOU  855  CA AASP A6900     3991   2503   3538   -441   -257    244       C  
ATOM    856  CA BASP A6900      78.028   7.030  23.578  0.40 26.46           C  
ANISOU  856  CA BASP A6900     3994   2509   3549   -445   -254    249       C  
ATOM    857  C  AASP A6900      77.364   8.334  23.243  0.60 25.34           C  
ANISOU  857  C  AASP A6900     3790   2443   3393   -455   -245    238       C  
ATOM    858  C  BASP A6900      77.349   8.365  23.255  0.40 25.26           C  
ANISOU  858  C  BASP A6900     3779   2435   3383   -455   -244    239       C  
ATOM    859  O  AASP A6900      76.789   8.922  24.181  0.60 25.47           O  
ANISOU  859  O  AASP A6900     3767   2498   3412   -462   -186    291       O  
ATOM    860  O  BASP A6900      76.816   9.006  24.184  0.40 25.13           O  
ANISOU  860  O  BASP A6900     3722   2460   3364   -459   -185    289       O  
ATOM    861  CB AASP A6900      77.235   5.795  23.379  0.60 29.03           C  
ANISOU  861  CB AASP A6900     4317   2741   3971   -506   -280    267       C  
ATOM    862  CB BASP A6900      76.965   5.926  23.540  0.40 28.85           C  
ANISOU  862  CB BASP A6900     4279   2726   3956   -516   -268    282       C  
ATOM    863  CG AASP A6900      76.888   5.458  21.941  0.60 30.11           C  
ANISOU  863  CG AASP A6900     4447   2842   4150   -537   -359    193       C  
ATOM    864  CG BASP A6900      77.524   4.516  23.543  0.40 30.46           C  
ANISOU  864  CG BASP A6900     4548   2830   4195   -513   -298    280       C  
ATOM    865  OD1AASP A6900      77.591   5.947  21.039  0.60 30.06           O  
ANISOU  865  OD1AASP A6900     4467   2874   4081   -501   -392    122       O  
ATOM    866  OD1BASP A6900      78.623   4.325  22.992  0.40 31.69           O  
ANISOU  866  OD1BASP A6900     4750   2978   4310   -462   -335    218       O  
ATOM    867  OD2AASP A6900      75.915   4.707  21.736  0.60 34.61           O  
ANISOU  867  OD2AASP A6900     4988   3344   4815   -601   -385    204       O  
ATOM    868  OD2BASP A6900      76.852   3.620  24.094  0.40 32.84           O  
ANISOU  868  OD2BASP A6900     4849   3058   4571   -563   -280    341       O  
ATOM    869  N   PHE A6901      77.395   8.773  21.985  1.00 24.18           N  
ANISOU  869  N   PHE A6901     3640   2314   3232   -456   -300    174       N  
ATOM    870  CA  PHE A6901      76.693  10.001  21.542  1.00 23.15           C  
ANISOU  870  CA  PHE A6901     3455   2241   3096   -465   -310    166       C  
ATOM    871  C   PHE A6901      76.542   9.945  20.023  1.00 23.76           C  
ANISOU  871  C   PHE A6901     3552   2303   3170   -481   -394    103       C  
ATOM    872  O   PHE A6901      77.249   9.152  19.373  1.00 24.27           O  
ANISOU  872  O   PHE A6901     3678   2329   3212   -474   -425     55       O  
ATOM    873  CB  PHE A6901      77.436  11.265  21.983  1.00 21.74           C  
ANISOU  873  CB  PHE A6901     3280   2139   2839   -412   -265    166       C  
ATOM    874  CG  PHE A6901      78.788  11.468  21.348  1.00 20.78           C  
ANISOU  874  CG  PHE A6901     3217   2035   2642   -369   -278    110       C  
ATOM    875  CD1 PHE A6901      79.896  10.776  21.805  1.00 20.89           C  
ANISOU  875  CD1 PHE A6901     3274   2027   2633   -334   -260    100       C  
ATOM    876  CD2 PHE A6901      78.957  12.366  20.306  1.00 20.63           C  
ANISOU  876  CD2 PHE A6901     3208   2051   2579   -363   -304     70       C  
ATOM    877  CE1 PHE A6901      81.142  10.965  21.230  1.00 20.24           C  
ANISOU  877  CE1 PHE A6901     3229   1961   2499   -295   -262     42       C  
ATOM    878  CE2 PHE A6901      80.205  12.558  19.734  1.00 19.84           C  
ANISOU  878  CE2 PHE A6901     3156   1967   2414   -330   -296     20       C  
ATOM    879  CZ  PHE A6901      81.295  11.860  20.198  1.00 20.18           C  
ANISOU  879  CZ  PHE A6901     3227   1991   2448   -297   -271      1       C  
ATOM    880  N  AVAL A6902      75.608  10.726  19.476  0.50 24.40           N  
ANISOU  880  N  AVAL A6902     3586   2409   3274   -502   -433    100       N  
ATOM    881  N  BVAL A6902      75.640  10.789  19.511  0.50 23.94           N  
ANISOU  881  N  BVAL A6902     3528   2355   3213   -499   -429    101       N  
ATOM    882  CA AVAL A6902      75.421  10.774  17.995  0.50 25.24           C  
ANISOU  882  CA AVAL A6902     3726   2505   3358   -515   -525     43       C  
ATOM    883  CA BVAL A6902      75.305  10.959  18.066  0.50 24.61           C  
ANISOU  883  CA BVAL A6902     3634   2433   3281   -515   -522     49       C  
ATOM    884  C  AVAL A6902      76.127  12.040  17.509  0.50 24.05           C  
ANISOU  884  C  AVAL A6902     3611   2418   3107   -473   -516     26       C  
ATOM    885  C  BVAL A6902      76.165  12.106  17.533  0.50 23.67           C  
ANISOU  885  C  BVAL A6902     3563   2373   3055   -471   -513     27       C  
ATOM    886  O  AVAL A6902      75.922  13.103  18.117  0.50 23.24           O  
ANISOU  886  O  AVAL A6902     3462   2361   3004   -455   -478     63       O  
ATOM    887  O  BVAL A6902      76.132  13.178  18.162  0.50 23.01           O  
ANISOU  887  O  BVAL A6902     3441   2338   2962   -448   -468     61       O  
ATOM    888  CB AVAL A6902      73.937  10.712  17.586  0.50 26.58           C  
ANISOU  888  CB AVAL A6902     3826   2648   3625   -564   -599     47       C  
ATOM    889  CB BVAL A6902      73.806  11.275  17.900  0.50 25.12           C  
ANISOU  889  CB BVAL A6902     3614   2490   3439   -554   -576     68       C  
ATOM    890  CG1AVAL A6902      73.300   9.418  18.062  0.50 28.47           C  
ANISOU  890  CG1AVAL A6902     4028   2816   3974   -615   -598     64       C  
ATOM    891  CG1BVAL A6902      73.461  11.659  16.475  0.50 25.52           C  
ANISOU  891  CG1BVAL A6902     3694   2542   3459   -560   -685     21       C  
ATOM    892  CG2AVAL A6902      73.152  11.910  18.083  0.50 27.00           C  
ANISOU  892  CG2AVAL A6902     3794   2748   3713   -557   -578     89       C  
ATOM    893  CG2BVAL A6902      72.921  10.145  18.390  0.50 26.48           C  
ANISOU  893  CG2BVAL A6902     3729   2598   3733   -609   -578     89       C  
ATOM    894  N   SER A6903      76.897  11.902  16.431  1.00 23.90           N  
ANISOU  894  N   SER A6903     3674   2398   3009   -461   -546    -29       N  
ATOM    895  CA  SER A6903      77.794  12.972  15.935  1.00 23.59           C  
ANISOU  895  CA  SER A6903     3683   2411   2868   -427   -519    -45       C  
ATOM    896  C   SER A6903      77.689  13.247  14.436  1.00 23.43           C  
ANISOU  896  C   SER A6903     3734   2392   2774   -438   -590    -85       C  
ATOM    897  O   SER A6903      77.339  12.331  13.677  1.00 23.92           O  
ANISOU  897  O   SER A6903     3831   2412   2842   -463   -657   -127       O  
ATOM    898  CB  SER A6903      79.202  12.551  16.259  1.00 24.24           C  
ANISOU  898  CB  SER A6903     3805   2496   2908   -394   -449    -73       C  
ATOM    899  OG  SER A6903      80.141  13.449  15.712  1.00 24.16           O  
ANISOU  899  OG  SER A6903     3838   2528   2811   -370   -414    -96       O  
ATOM    900  N   ASP A6904      78.082  14.467  14.056  1.00 22.27           N  
ANISOU  900  N   ASP A6904     3616   2290   2555   -418   -571    -74       N  
ATOM    901  CA  ASP A6904      78.186  14.903  12.641  1.00 23.22           C  
ANISOU  901  CA  ASP A6904     3828   2419   2574   -424   -621   -102       C  
ATOM    902  C   ASP A6904      79.633  14.717  12.166  1.00 23.12           C  
ANISOU  902  C   ASP A6904     3895   2421   2468   -408   -544   -152       C  
ATOM    903  O   ASP A6904      79.917  15.062  11.011  1.00 24.65           O  
ANISOU  903  O   ASP A6904     4180   2627   2558   -413   -558   -176       O  
ATOM    904  CB  ASP A6904      77.708  16.347  12.488  1.00 23.16           C  
ANISOU  904  CB  ASP A6904     3810   2440   2549   -416   -645    -53       C  
ATOM    905  CG  ASP A6904      76.220  16.492  12.744  1.00 23.81           C  
ANISOU  905  CG  ASP A6904     3811   2504   2732   -430   -732    -18       C  
ATOM    906  OD1 ASP A6904      75.437  15.838  12.018  1.00 24.59           O  
ANISOU  906  OD1 ASP A6904     3924   2569   2846   -454   -833    -43       O  
ATOM    907  OD2 ASP A6904      75.859  17.208  13.704  1.00 23.43           O  
ANISOU  907  OD2 ASP A6904     3678   2470   2752   -415   -698     24       O  
ATOM    908  N   ALA A6905      80.513  14.180  13.021  1.00 22.32           N  
ANISOU  908  N   ALA A6905     3761   2317   2401   -387   -466   -167       N  
ATOM    909  CA  ALA A6905      81.924  13.968  12.624  1.00 21.78           C  
ANISOU  909  CA  ALA A6905     3746   2260   2268   -368   -389   -223       C  
ATOM    910  C   ALA A6905      82.019  12.873  11.550  1.00 22.65           C  
ANISOU  910  C   ALA A6905     3935   2336   2334   -380   -424   -296       C  
ATOM    911  O   ALA A6905      81.085  12.052  11.428  1.00 23.07           O  
ANISOU  911  O   ALA A6905     3984   2348   2434   -401   -507   -304       O  
ATOM    912  CB  ALA A6905      82.749  13.605  13.836  1.00 21.30           C  
ANISOU  912  CB  ALA A6905     3624   2198   2270   -337   -321   -223       C  
ATOM    913  N   ASP A6906      83.122  12.873  10.801  1.00 23.08           N  
ANISOU  913  N   ASP A6906     4056   2407   2306   -368   -357   -354       N  
ATOM    914  CA  ASP A6906      83.404  11.834   9.775  1.00 24.49           C  
ANISOU  914  CA  ASP A6906     4316   2556   2431   -372   -370   -442       C  
ATOM    915  C   ASP A6906      83.540  10.473  10.466  1.00 24.33           C  
ANISOU  915  C   ASP A6906     4250   2480   2514   -356   -380   -477       C  
ATOM    916  O   ASP A6906      83.116   9.458   9.895  1.00 24.93           O  
ANISOU  916  O   ASP A6906     4369   2508   2595   -370   -442   -529       O  
ATOM    917  CB  ASP A6906      84.653  12.210   8.982  1.00 25.54           C  
ANISOU  917  CB  ASP A6906     4515   2724   2465   -360   -267   -495       C  
ATOM    918  CG  ASP A6906      84.430  13.462   8.156  1.00 26.93           C  
ANISOU  918  CG  ASP A6906     4762   2942   2528   -384   -266   -454       C  
ATOM    919  OD1 ASP A6906      83.514  13.436   7.311  1.00 28.32           O  
ANISOU  919  OD1 ASP A6906     5012   3109   2639   -407   -360   -451       O  
ATOM    920  OD2 ASP A6906      85.103  14.474   8.425  1.00 26.96           O  
ANISOU  920  OD2 ASP A6906     4743   2981   2520   -379   -183   -419       O  
ATOM    921  N  ASER A6907      84.110  10.463  11.671  0.60 23.15           N  
ANISOU  921  N  ASER A6907     4021   2331   2443   -328   -327   -447       N  
ATOM    922  N  BSER A6907      84.132  10.466  11.663  0.40 23.22           N  
ANISOU  922  N  BSER A6907     4031   2341   2451   -327   -325   -448       N  
ATOM    923  CA ASER A6907      84.257   9.199  12.433  0.60 23.35           C  
ANISOU  923  CA ASER A6907     4010   2296   2567   -309   -340   -465       C  
ATOM    924  CA BSER A6907      84.318   9.222  12.453  0.40 23.30           C  
ANISOU  924  CA BSER A6907     4002   2291   2560   -307   -335   -465       C  
ATOM    925  C  ASER A6907      84.240   9.530  13.926  0.60 22.30           C  
ANISOU  925  C  ASER A6907     3791   2172   2508   -292   -320   -387       C  
ATOM    926  C  BSER A6907      84.228   9.553  13.941  0.40 22.29           C  
ANISOU  926  C  BSER A6907     3789   2172   2508   -292   -320   -385       C  
ATOM    927  O  ASER A6907      84.773  10.594  14.298  0.60 21.16           O  
ANISOU  927  O  ASER A6907     3618   2082   2339   -275   -265   -360       O  
ATOM    928  O  BSER A6907      84.703  10.638  14.329  0.40 21.33           O  
ANISOU  928  O  BSER A6907     3638   2105   2361   -277   -267   -355       O  
ATOM    929  CB ASER A6907      85.503   8.456  12.024  0.60 24.41           C  
ANISOU  929  CB ASER A6907     4173   2408   2692   -272   -283   -557       C  
ATOM    930  CB BSER A6907      85.627   8.553  12.127  0.40 24.07           C  
ANISOU  930  CB BSER A6907     4123   2371   2651   -268   -273   -554       C  
ATOM    931  OG ASER A6907      85.435   7.098  12.430  0.60 25.06           O  
ANISOU  931  OG ASER A6907     4246   2412   2863   -259   -322   -583       O  
ATOM    932  OG BSER A6907      85.641   8.103  10.783  0.40 25.21           O  
ANISOU  932  OG BSER A6907     4354   2502   2722   -282   -284   -636       O  
ATOM    933  N   THR A6908      83.616   8.658  14.720  1.00 22.11           N  
ANISOU  933  N   THR A6908     3735   2093   2570   -299   -363   -352       N  
ATOM    934  CA  THR A6908      83.478   8.845  16.184  1.00 21.88           C  
ANISOU  934  CA  THR A6908     3642   2070   2601   -286   -346   -274       C  
ATOM    935  C   THR A6908      84.037   7.617  16.901  1.00 22.58           C  
ANISOU  935  C   THR A6908     3727   2092   2757   -256   -346   -284       C  
ATOM    936  O   THR A6908      83.722   6.487  16.466  1.00 22.87           O  
ANISOU  936  O   THR A6908     3796   2059   2835   -272   -390   -317       O  
ATOM    937  CB  THR A6908      82.008   9.079  16.556  1.00 22.03           C  
ANISOU  937  CB  THR A6908     3624   2086   2658   -331   -390   -203       C  
ATOM    938  OG1 THR A6908      81.581  10.258  15.877  1.00 21.36           O  
ANISOU  938  OG1 THR A6908     3543   2056   2514   -348   -399   -197       O  
ATOM    939  CG2 THR A6908      81.780   9.229  18.044  1.00 21.86           C  
ANISOU  939  CG2 THR A6908     3548   2071   2685   -322   -361   -126       C  
ATOM    940  N   LEU A6909      84.862   7.838  17.924  1.00 22.00           N  
ANISOU  940  N   LEU A6909     3623   2036   2697   -211   -308   -260       N  
ATOM    941  CA  LEU A6909      85.400   6.722  18.746  1.00 23.63           C  
ANISOU  941  CA  LEU A6909     3832   2177   2969   -174   -320   -254       C  
ATOM    942  C   LEU A6909      84.839   6.852  20.159  1.00 23.09           C  
ANISOU  942  C   LEU A6909     3737   2110   2924   -178   -321   -154       C  
ATOM    943  O   LEU A6909      84.954   7.946  20.734  1.00 21.52           O  
ANISOU  943  O   LEU A6909     3507   1980   2687   -167   -289   -122       O  
ATOM    944  CB  LEU A6909      86.926   6.765  18.770  1.00 24.81           C  
ANISOU  944  CB  LEU A6909     3972   2338   3115   -110   -286   -317       C  
ATOM    945  CG  LEU A6909      87.618   6.434  17.453  1.00 26.78           C  
ANISOU  945  CG  LEU A6909     4251   2576   3347    -99   -267   -425       C  
ATOM    946  CD1 LEU A6909      89.120   6.572  17.611  1.00 28.50           C  
ANISOU  946  CD1 LEU A6909     4435   2811   3582    -36   -223   -485       C  
ATOM    947  CD2 LEU A6909      87.259   5.039  16.980  1.00 28.78           C  
ANISOU  947  CD2 LEU A6909     4547   2737   3649   -109   -315   -462       C  
ATOM    948  N   ILE A6910      84.258   5.771  20.679  1.00 23.37           N  
ANISOU  948  N   ILE A6910     3790   2070   3020   -196   -351   -109       N  
ATOM    949  CA  ILE A6910      83.681   5.801  22.050  1.00 23.64           C  
ANISOU  949  CA  ILE A6910     3811   2102   3067   -205   -339     -8       C  
ATOM    950  C   ILE A6910      84.606   5.024  22.980  1.00 24.18           C  
ANISOU  950  C   ILE A6910     3908   2120   3157   -148   -352     10       C  
ATOM    951  O   ILE A6910      84.899   3.856  22.685  1.00 24.32           O  
ANISOU  951  O   ILE A6910     3959   2050   3230   -136   -387    -17       O  
ATOM    952  CB  ILE A6910      82.248   5.240  22.083  1.00 24.55           C  
ANISOU  952  CB  ILE A6910     3921   2168   3236   -277   -353     45       C  
ATOM    953  CG1 ILE A6910      81.334   5.957  21.086  1.00 24.24           C  
ANISOU  953  CG1 ILE A6910     3851   2172   3187   -326   -363     18       C  
ATOM    954  CG2 ILE A6910      81.696   5.295  23.500  1.00 24.67           C  
ANISOU  954  CG2 ILE A6910     3928   2187   3257   -288   -318    148       C  
ATOM    955  CD1 ILE A6910      81.269   7.454  21.275  1.00 23.57           C  
ANISOU  955  CD1 ILE A6910     3728   2186   3041   -316   -327     34       C  
ATOM    956  N   GLY A6911      85.009   5.665  24.075  1.00 23.84           N  
ANISOU  956  N   GLY A6911     3857   2126   3073   -112   -331     55       N  
ATOM    957  CA  GLY A6911      85.866   5.031  25.089  1.00 24.36           C  
ANISOU  957  CA  GLY A6911     3957   2149   3150    -51   -358     83       C  
ATOM    958  C   GLY A6911      86.773   6.046  25.745  1.00 23.83           C  
ANISOU  958  C   GLY A6911     3866   2159   3028      3   -349     70       C  
ATOM    959  O   GLY A6911      86.793   7.217  25.302  1.00 22.05           O  
ANISOU  959  O   GLY A6911     3598   2014   2766     -7   -315     33       O  
ATOM    960  N  AASP A6912      87.491   5.626  26.789  0.60 24.21           N  
ANISOU  960  N  AASP A6912     3945   2178   3073     62   -385    101       N  
ATOM    961  N  BASP A6912      87.489   5.624  26.789  0.40 24.05           N  
ANISOU  961  N  BASP A6912     3925   2158   3053     62   -385    102       N  
ATOM    962  CA AASP A6912      88.441   6.543  27.470  0.60 24.41           C  
ANISOU  962  CA AASP A6912     3947   2271   3055    120   -394     79       C  
ATOM    963  CA BASP A6912      88.456   6.522  27.474  0.40 24.04           C  
ANISOU  963  CA BASP A6912     3901   2223   3009    121   -395     79       C  
ATOM    964  C  AASP A6912      89.435   7.048  26.418  0.60 23.71           C  
ANISOU  964  C  AASP A6912     3798   2215   2995    144   -386    -32       C  
ATOM    965  C  BASP A6912      89.435   7.047  26.417  0.40 23.54           C  
ANISOU  965  C  BASP A6912     3776   2192   2973    144   -386    -32       C  
ATOM    966  O  AASP A6912      89.837   6.244  25.548  0.60 23.75           O  
ANISOU  966  O  AASP A6912     3801   2163   3058    154   -400    -91       O  
ATOM    967  O  BASP A6912      89.830   6.249  25.539  0.40 23.68           O  
ANISOU  967  O  BASP A6912     3792   2154   3049    154   -399    -91       O  
ATOM    968  CB AASP A6912      89.124   5.847  28.647  0.60 25.80           C  
ANISOU  968  CB AASP A6912     4174   2399   3230    186   -458    123       C  
ATOM    969  CB BASP A6912      89.185   5.779  28.593  0.40 25.05           C  
ANISOU  969  CB BASP A6912     4078   2298   3140    188   -461    118       C  
ATOM    970  CG AASP A6912      89.936   6.785  29.519  0.60 26.22           C  
ANISOU  970  CG AASP A6912     4210   2520   3231    241   -481    108       C  
ATOM    971  CG BASP A6912      90.132   6.661  29.382  0.40 25.08           C  
ANISOU  971  CG BASP A6912     4060   2366   3102    249   -489     93       C  
ATOM    972  OD1AASP A6912      90.825   7.484  28.981  0.60 25.03           O  
ANISOU  972  OD1AASP A6912     3991   2412   3104    267   -480     18       O  
ATOM    973  OD1BASP A6912      89.709   7.763  29.788  0.40 24.71           O  
ANISOU  973  OD1BASP A6912     3999   2398   2990    226   -449    111       O  
ATOM    974  OD2AASP A6912      89.635   6.848  30.719  0.60 28.18           O  
ANISOU  974  OD2AASP A6912     4514   2779   3414    251   -493    186       O  
ATOM    975  OD2BASP A6912      91.292   6.255  29.549  0.40 25.64           O  
ANISOU  975  OD2BASP A6912     4121   2402   3216    321   -554     49       O  
ATOM    976  N   CYS A6913      89.806   8.330  26.485  1.00 22.89           N  
ANISOU  976  N   CYS A6913     3648   2194   2855    150   -359    -64       N  
ATOM    977  CA  CYS A6913      90.729   8.902  25.464  1.00 23.16           C  
ANISOU  977  CA  CYS A6913     3622   2260   2915    162   -333   -165       C  
ATOM    978  C   CYS A6913      92.043   8.109  25.422  1.00 23.51           C  
ANISOU  978  C   CYS A6913     3648   2253   3030    232   -376   -232       C  
ATOM    979  O   CYS A6913      92.644   8.047  24.335  1.00 23.79           O  
ANISOU  979  O   CYS A6913     3648   2285   3105    234   -344   -318       O  
ATOM    980  CB  CYS A6913      90.997  10.383  25.696  1.00 23.60           C  
ANISOU  980  CB  CYS A6913     3632   2400   2933    159   -301   -182       C  
ATOM    981  SG  CYS A6913      91.728  10.733  27.311  1.00 25.06           S  
ANISOU  981  SG  CYS A6913     3813   2605   3100    225   -359   -161       S  
ATOM    982  N   ALA A6914      92.432   7.485  26.538  1.00 23.61           N  
ANISOU  982  N   ALA A6914     3688   2225   3058    289   -445   -193       N  
ATOM    983  CA  ALA A6914      93.705   6.729  26.607  1.00 25.06           C  
ANISOU  983  CA  ALA A6914     3845   2352   3323    368   -504   -256       C  
ATOM    984  C   ALA A6914      93.663   5.519  25.663  1.00 25.37           C  
ANISOU  984  C   ALA A6914     3902   2308   3426    366   -502   -294       C  
ATOM    985  O   ALA A6914      94.741   4.989  25.354  1.00 26.94           O  
ANISOU  985  O   ALA A6914     4062   2465   3708    427   -528   -375       O  
ATOM    986  CB  ALA A6914      93.982   6.296  28.026  1.00 26.57           C  
ANISOU  986  CB  ALA A6914     4080   2509   3503    428   -594   -191       C  
ATOM    987  N   THR A6915      92.467   5.111  25.228  1.00 24.60           N  
ANISOU  987  N   THR A6915     3858   2185   3301    300   -475   -245       N  
ATOM    988  CA  THR A6915      92.313   3.940  24.322  1.00 25.54           C  
ANISOU  988  CA  THR A6915     4004   2219   3480    292   -480   -285       C  
ATOM    989  C   THR A6915      92.427   4.386  22.862  1.00 26.00           C  
ANISOU  989  C   THR A6915     4026   2318   3531    257   -409   -382       C  
ATOM    990  O   THR A6915      92.518   3.499  21.984  1.00 26.61           O  
ANISOU  990  O   THR A6915     4120   2333   3655    260   -408   -445       O  
ATOM    991  CB  THR A6915      90.962   3.234  24.506  1.00 25.32           C  
ANISOU  991  CB  THR A6915     4046   2135   3437    232   -491   -193       C  
ATOM    992  OG1 THR A6915      89.923   4.106  24.053  1.00 24.61           O  
ANISOU  992  OG1 THR A6915     3949   2116   3283    153   -434   -169       O  
ATOM    993  CG2 THR A6915      90.707   2.791  25.930  1.00 26.02           C  
ANISOU  993  CG2 THR A6915     4189   2182   3514    252   -543    -81       C  
ATOM    994  N   VAL A6916      92.438   5.699  22.619  1.00 25.81           N  
ANISOU  994  N   VAL A6916     3964   2392   3450    228   -354   -394       N  
ATOM    995  CA  VAL A6916      92.433   6.234  21.224  1.00 26.06           C  
ANISOU  995  CA  VAL A6916     3981   2467   3452    186   -281   -469       C  
ATOM    996  C   VAL A6916      93.857   6.265  20.669  1.00 27.62           C  
ANISOU  996  C   VAL A6916     4120   2671   3703    237   -245   -582       C  
ATOM    997  O   VAL A6916      94.739   6.888  21.293  1.00 27.32           O  
ANISOU  997  O   VAL A6916     4020   2669   3691    277   -246   -597       O  
ATOM    998  CB  VAL A6916      91.766   7.618  21.144  1.00 25.18           C  
ANISOU  998  CB  VAL A6916     3862   2445   3261    128   -237   -425       C  
ATOM    999  CG1 VAL A6916      91.887   8.222  19.751  1.00 25.00           C  
ANISOU  999  CG1 VAL A6916     3835   2464   3198     91   -167   -494       C  
ATOM   1000  CG2 VAL A6916      90.309   7.553  21.580  1.00 24.57           C  
ANISOU 1000  CG2 VAL A6916     3829   2361   3146     77   -263   -326       C  
ATOM   1001  N   HIS A6917      94.046   5.607  19.524  1.00 28.55           N  
ANISOU 1001  N   HIS A6917     4253   2752   3839    234   -212   -665       N  
ATOM   1002  CA  HIS A6917      95.346   5.579  18.815  1.00 31.66           C  
ANISOU 1002  CA  HIS A6917     4591   3152   4286    277   -153   -786       C  
ATOM   1003  C   HIS A6917      95.117   6.042  17.376  1.00 31.68           C  
ANISOU 1003  C   HIS A6917     4623   3199   4212    218    -62   -842       C  
ATOM   1004  O   HIS A6917      94.024   5.805  16.829  1.00 29.90           O  
ANISOU 1004  O   HIS A6917     4472   2962   3923    166    -76   -811       O  
ATOM   1005  CB  HIS A6917      95.982   4.187  18.928  1.00 35.64           C  
ANISOU 1005  CB  HIS A6917     5088   3557   4895    349   -203   -844       C  
ATOM   1006  CG  HIS A6917      96.269   3.813  20.342  1.00 39.05           C  
ANISOU 1006  CG  HIS A6917     5501   3945   5389    409   -299   -781       C  
ATOM   1007  ND1 HIS A6917      97.468   4.114  20.957  1.00 43.98           N  
ANISOU 1007  ND1 HIS A6917     6041   4583   6085    477   -317   -821       N  
ATOM   1008  CD2 HIS A6917      95.502   3.219  21.280  1.00 41.70           C  
ANISOU 1008  CD2 HIS A6917     5896   4226   5719    409   -383   -678       C  
ATOM   1009  CE1 HIS A6917      97.435   3.700  22.209  1.00 44.49           C  
ANISOU 1009  CE1 HIS A6917     6123   4603   6176    522   -420   -745       C  
ATOM   1010  NE2 HIS A6917      96.241   3.145  22.430  1.00 44.72           N  
ANISOU 1010  NE2 HIS A6917     6245   4590   6154    480   -453   -652       N  
ATOM   1011  N  ATHR A6918      96.097   6.748  16.802  0.70 31.85           N  
ANISOU 1011  N  ATHR A6918     4589   3273   4237    224     27   -918       N  
ATOM   1012  N  BTHR A6918      96.126   6.689  16.800  0.30 32.41           N  
ANISOU 1012  N  BTHR A6918     4660   3341   4313    226     26   -922       N  
ATOM   1013  CA ATHR A6918      96.006   7.223  15.394  0.70 32.54           C  
ANISOU 1013  CA ATHR A6918     4718   3404   4238    170    127   -972       C  
ATOM   1014  CA BTHR A6918      96.039   7.188  15.408  0.30 33.31           C  
ANISOU 1014  CA BTHR A6918     4814   3500   4340    172    126   -974       C  
ATOM   1015  C  ATHR A6918      97.368   7.002  14.725  0.70 34.32           C  
ANISOU 1015  C  ATHR A6918     4885   3628   4526    210    220  -1101       C  
ATOM   1016  C  BTHR A6918      97.388   6.981  14.727  0.30 34.74           C  
ANISOU 1016  C  BTHR A6918     4936   3679   4581    212    220  -1103       C  
ATOM   1017  O  ATHR A6918      98.396   7.216  15.397  0.70 35.45           O  
ANISOU 1017  O  ATHR A6918     4926   3775   4765    259    226  -1130       O  
ATOM   1018  O  BTHR A6918      98.424   7.207  15.384  0.30 35.34           O  
ANISOU 1018  O  BTHR A6918     4912   3761   4754    260    227  -1133       O  
ATOM   1019  CB ATHR A6918      95.547   8.688  15.299  0.70 32.15           C  
ANISOU 1019  CB ATHR A6918     4678   3437   4100    106    167   -904       C  
ATOM   1020  CB BTHR A6918      95.640   8.664  15.373  0.30 32.94           C  
ANISOU 1020  CB BTHR A6918     4770   3535   4209    112    166   -907       C  
ATOM   1021  OG1ATHR A6918      96.557   9.557  15.811  0.70 30.76           O  
ANISOU 1021  OG1ATHR A6918     4409   3301   3976    126    211   -919       O  
ATOM   1022  OG1BTHR A6918      95.727   9.066  14.006  0.30 33.63           O  
ANISOU 1022  OG1BTHR A6918     4904   3658   4213     68    264   -960       O  
ATOM   1023  CG2ATHR A6918      94.252   8.962  16.036  0.70 30.85           C  
ANISOU 1023  CG2ATHR A6918     4552   3276   3890     73     83   -785       C  
ATOM   1024  CG2BTHR A6918      96.527   9.523  16.247  0.30 32.55           C  
ANISOU 1024  CG2BTHR A6918     4622   3522   4222    138    181   -900       C  
ATOM   1025  N   ALA A6919      97.361   6.546  13.470  1.00 35.76           N  
ANISOU 1025  N   ALA A6919     5127   3801   4658    193    286  -1182       N  
ATOM   1026  CA  ALA A6919      98.600   6.326  12.697  1.00 38.09           C  
ANISOU 1026  CA  ALA A6919     5372   4099   5003    226    399  -1315       C  
ATOM   1027  C   ALA A6919      99.105   7.680  12.181  1.00 39.39           C  
ANISOU 1027  C   ALA A6919     5506   4348   5109    176    525  -1320       C  
ATOM   1028  O   ALA A6919     100.327   7.831  12.006  1.00 42.47           O  
ANISOU 1028  O   ALA A6919     5804   4752   5580    204    621  -1409       O  
ATOM   1029  CB  ALA A6919      98.311   5.370  11.565  1.00 38.93           C  
ANISOU 1029  CB  ALA A6919     5568   4164   5057    223    424  -1398       C  
ATOM   1030  N   ASN A6920      98.188   8.641  12.023  1.00 38.44           N  
ANISOU 1030  N   ASN A6920     5455   4279   4871    105    519  -1224       N  
ATOM   1031  CA  ASN A6920      98.496   9.959  11.408  1.00 36.84           C  
ANISOU 1031  CA  ASN A6920     5253   4149   4595     46    636  -1213       C  
ATOM   1032  C   ASN A6920      98.678  11.070  12.444  1.00 34.49           C  
ANISOU 1032  C   ASN A6920     4871   3883   4347     37    613  -1137       C  
ATOM   1033  O   ASN A6920      98.318  10.879  13.630  1.00 32.22           O  
ANISOU 1033  O   ASN A6920     4550   3573   4118     69    496  -1077       O  
ATOM   1034  CB  ASN A6920      97.387  10.395  10.443  1.00 38.19           C  
ANISOU 1034  CB  ASN A6920     5564   4349   4597    -24    643  -1158       C  
ATOM   1035  CG  ASN A6920      96.021  10.511  11.094  1.00 39.03           C  
ANISOU 1035  CG  ASN A6920     5718   4446   4666    -44    507  -1042       C  
ATOM   1036  OD1 ASN A6920      95.418   9.505  11.470  1.00 39.31           O  
ANISOU 1036  OD1 ASN A6920     5773   4429   4732    -18    407  -1034       O  
ATOM   1037  ND2 ASN A6920      95.500  11.727  11.182  1.00 37.18           N  
ANISOU 1037  ND2 ASN A6920     5501   4256   4367    -94    507   -953       N  
ATOM   1038  N   LYS A6921      99.253  12.186  11.983  1.00 32.26           N  
ANISOU 1038  N   LYS A6921     4563   3652   4042     -7    728  -1144       N  
ATOM   1039  CA  LYS A6921      99.378  13.415  12.804  1.00 30.60           C  
ANISOU 1039  CA  LYS A6921     4286   3473   3868    -30    716  -1076       C  
ATOM   1040  C   LYS A6921      98.176  14.302  12.481  1.00 27.94           C  
ANISOU 1040  C   LYS A6921     4056   3165   3396    -96    694   -969       C  
ATOM   1041  O   LYS A6921      97.535  14.080  11.431  1.00 27.52           O  
ANISOU 1041  O   LYS A6921     4116   3114   3222   -130    717   -965       O  
ATOM   1042  CB  LYS A6921     100.726  14.103  12.588  1.00 32.09           C  
ANISOU 1042  CB  LYS A6921     4369   3685   4139    -41    846  -1146       C  
ATOM   1043  CG  LYS A6921     101.903  13.302  13.116  1.00 34.62           C  
ANISOU 1043  CG  LYS A6921     4557   3973   4623     34    843  -1249       C  
ATOM   1044  CD  LYS A6921     103.129  14.116  13.393  1.00 36.78           C  
ANISOU 1044  CD  LYS A6921     4689   4265   5018     28    922  -1300       C  
ATOM   1045  CE  LYS A6921     104.236  13.272  13.984  1.00 39.04           C  
ANISOU 1045  CE  LYS A6921     4836   4514   5481    114    891  -1403       C  
ATOM   1046  NZ  LYS A6921     105.308  14.118  14.550  1.00 41.35           N  
ANISOU 1046  NZ  LYS A6921     4976   4821   5913    112    922  -1441       N  
ATOM   1047  N   TRP A6922      97.903  15.269  13.358  1.00 26.02           N  
ANISOU 1047  N   TRP A6922     3774   2938   3173   -110    644   -893       N  
ATOM   1048  CA  TRP A6922      96.706  16.144  13.267  1.00 24.93           C  
ANISOU 1048  CA  TRP A6922     3720   2819   2932   -161    603   -788       C  
ATOM   1049  C   TRP A6922      97.133  17.602  13.125  1.00 24.23           C  
ANISOU 1049  C   TRP A6922     3604   2758   2841   -210    684   -760       C  
ATOM   1050  O   TRP A6922      98.245  17.939  13.557  1.00 24.94           O  
ANISOU 1050  O   TRP A6922     3587   2852   3036   -198    735   -811       O  
ATOM   1051  CB  TRP A6922      95.815  15.899  14.493  1.00 24.32           C  
ANISOU 1051  CB  TRP A6922     3631   2727   2883   -129    465   -720       C  
ATOM   1052  CG  TRP A6922      95.375  14.473  14.505  1.00 24.69           C  
ANISOU 1052  CG  TRP A6922     3714   2735   2931    -93    397   -740       C  
ATOM   1053  CD1 TRP A6922      96.078  13.402  14.971  1.00 26.18           C  
ANISOU 1053  CD1 TRP A6922     3847   2887   3210    -32    373   -804       C  
ATOM   1054  CD2 TRP A6922      94.188  13.945  13.895  1.00 24.63           C  
ANISOU 1054  CD2 TRP A6922     3808   2713   2837   -116    347   -706       C  
ATOM   1055  NE1 TRP A6922      95.394  12.245  14.715  1.00 26.81           N  
ANISOU 1055  NE1 TRP A6922     3991   2926   3266    -19    316   -807       N  
ATOM   1056  CE2 TRP A6922      94.231  12.543  14.057  1.00 25.60           C  
ANISOU 1056  CE2 TRP A6922     3931   2787   3007    -73    299   -751       C  
ATOM   1057  CE3 TRP A6922      93.091  14.515  13.243  1.00 24.50           C  
ANISOU 1057  CE3 TRP A6922     3879   2714   2717   -168    328   -643       C  
ATOM   1058  CZ2 TRP A6922      93.217  11.708  13.593  1.00 25.29           C  
ANISOU 1058  CZ2 TRP A6922     3974   2716   2918    -86    237   -739       C  
ATOM   1059  CZ3 TRP A6922      92.092  13.687  12.778  1.00 24.73           C  
ANISOU 1059  CZ3 TRP A6922     3984   2716   2696   -177    261   -634       C  
ATOM   1060  CH2 TRP A6922      92.153  12.306  12.959  1.00 24.73           C  
ANISOU 1060  CH2 TRP A6922     3979   2667   2747   -140    218   -682       C  
ATOM   1061  N   ASP A6923      96.268  18.408  12.521  1.00 23.47           N  
ANISOU 1061  N   ASP A6923     3603   2676   2637   -263    687   -685       N  
ATOM   1062  CA  ASP A6923      96.544  19.847  12.277  1.00 23.79           C  
ANISOU 1062  CA  ASP A6923     3641   2732   2666   -318    761   -645       C  
ATOM   1063  C   ASP A6923      95.911  20.682  13.389  1.00 22.34           C  
ANISOU 1063  C   ASP A6923     3421   2545   2520   -312    668   -571       C  
ATOM   1064  O   ASP A6923      96.365  21.811  13.607  1.00 22.40           O  
ANISOU 1064  O   ASP A6923     3384   2555   2571   -342    713   -555       O  
ATOM   1065  CB  ASP A6923      96.019  20.252  10.903  1.00 24.63           C  
ANISOU 1065  CB  ASP A6923     3885   2846   2626   -375    818   -604       C  
ATOM   1066  CG  ASP A6923      96.621  19.420   9.785  1.00 26.51           C  
ANISOU 1066  CG  ASP A6923     4173   3091   2808   -380    918   -685       C  
ATOM   1067  OD1 ASP A6923      97.833  19.114   9.871  1.00 27.12           O  
ANISOU 1067  OD1 ASP A6923     4157   3170   2977   -363   1009   -772       O  
ATOM   1068  OD2 ASP A6923      95.861  19.033   8.871  1.00 27.12           O  
ANISOU 1068  OD2 ASP A6923     4377   3169   2756   -394    896   -669       O  
ATOM   1069  N   LEU A6924      94.875  20.149  14.036  1.00 21.51           N  
ANISOU 1069  N   LEU A6924     3336   2434   2402   -280    549   -530       N  
ATOM   1070  CA  LEU A6924      94.165  20.887  15.106  1.00 20.68           C  
ANISOU 1070  CA  LEU A6924     3203   2329   2324   -271    466   -465       C  
ATOM   1071  C   LEU A6924      93.584  19.874  16.086  1.00 20.48           C  
ANISOU 1071  C   LEU A6924     3158   2295   2327   -219    363   -458       C  
ATOM   1072  O   LEU A6924      92.956  18.903  15.634  1.00 19.74           O  
ANISOU 1072  O   LEU A6924     3122   2190   2187   -214    328   -456       O  
ATOM   1073  CB  LEU A6924      93.059  21.744  14.480  1.00 21.21           C  
ANISOU 1073  CB  LEU A6924     3360   2396   2302   -315    447   -383       C  
ATOM   1074  CG  LEU A6924      92.221  22.588  15.442  1.00 21.31           C  
ANISOU 1074  CG  LEU A6924     3348   2406   2340   -307    372   -319       C  
ATOM   1075  CD1 LEU A6924      93.074  23.629  16.162  1.00 21.99           C  
ANISOU 1075  CD1 LEU A6924     3353   2492   2508   -310    409   -336       C  
ATOM   1076  CD2 LEU A6924      91.071  23.264  14.705  1.00 21.46           C  
ANISOU 1076  CD2 LEU A6924     3456   2417   2278   -340    341   -243       C  
ATOM   1077  N   ILE A6925      93.848  20.085  17.371  1.00 19.90           N  
ANISOU 1077  N   ILE A6925     3008   2224   2327   -185    318   -460       N  
ATOM   1078  CA  ILE A6925      93.285  19.226  18.447  1.00 19.85           C  
ANISOU 1078  CA  ILE A6925     2991   2208   2340   -138    225   -440       C  
ATOM   1079  C   ILE A6925      92.405  20.111  19.321  1.00 19.13           C  
ANISOU 1079  C   ILE A6925     2898   2130   2239   -141    176   -375       C  
ATOM   1080  O   ILE A6925      92.919  21.127  19.827  1.00 18.95           O  
ANISOU 1080  O   ILE A6925     2826   2118   2254   -143    191   -385       O  
ATOM   1081  CB  ILE A6925      94.390  18.568  19.290  1.00 20.85           C  
ANISOU 1081  CB  ILE A6925     3042   2326   2552    -83    206   -501       C  
ATOM   1082  CG1 ILE A6925      95.323  17.708  18.441  1.00 21.80           C  
ANISOU 1082  CG1 ILE A6925     3150   2431   2702    -72    262   -578       C  
ATOM   1083  CG2 ILE A6925      93.772  17.781  20.438  1.00 20.67           C  
ANISOU 1083  CG2 ILE A6925     3028   2291   2534    -39    112   -464       C  
ATOM   1084  CD1 ILE A6925      96.594  17.314  19.150  1.00 23.49           C  
ANISOU 1084  CD1 ILE A6925     3269   2633   3020    -18    250   -650       C  
ATOM   1085  N   ILE A6926      91.130  19.748  19.446  1.00 18.62           N  
ANISOU 1085  N   ILE A6926     2880   2060   2132   -145    122   -317       N  
ATOM   1086  CA  ILE A6926      90.183  20.454  20.351  1.00 18.14           C  
ANISOU 1086  CA  ILE A6926     2812   2011   2067   -142     80   -260       C  
ATOM   1087  C   ILE A6926      89.830  19.473  21.471  1.00 17.71           C  
ANISOU 1087  C   ILE A6926     2750   1951   2027   -103     24   -245       C  
ATOM   1088  O   ILE A6926      89.538  18.306  21.160  1.00 17.71           O  
ANISOU 1088  O   ILE A6926     2780   1928   2018   -100      4   -242       O  
ATOM   1089  CB  ILE A6926      88.908  20.917  19.615  1.00 18.86           C  
ANISOU 1089  CB  ILE A6926     2955   2100   2110   -180     68   -204       C  
ATOM   1090  CG1 ILE A6926      89.203  21.727  18.348  1.00 20.03           C  
ANISOU 1090  CG1 ILE A6926     3140   2247   2224   -220    118   -207       C  
ATOM   1091  CG2 ILE A6926      87.988  21.662  20.572  1.00 18.69           C  
ANISOU 1091  CG2 ILE A6926     2911   2088   2099   -171     35   -157       C  
ATOM   1092  CD1 ILE A6926      89.922  23.017  18.587  1.00 20.77           C  
ANISOU 1092  CD1 ILE A6926     3195   2344   2349   -229    161   -217       C  
ATOM   1093  N   SER A6927      89.923  19.909  22.727  1.00 17.17           N  
ANISOU 1093  N   SER A6927     2648   1897   1976    -73      1   -238       N  
ATOM   1094  CA  SER A6927      89.472  19.050  23.846  1.00 17.31           C  
ANISOU 1094  CA  SER A6927     2676   1909   1989    -40    -45   -208       C  
ATOM   1095  C   SER A6927      88.515  19.821  24.749  1.00 17.58           C  
ANISOU 1095  C   SER A6927     2710   1966   2002    -41    -53   -163       C  
ATOM   1096  O   SER A6927      88.864  20.944  25.165  1.00 17.41           O  
ANISOU 1096  O   SER A6927     2659   1964   1990    -34    -44   -184       O  
ATOM   1097  CB  SER A6927      90.613  18.510  24.664  1.00 18.25           C  
ANISOU 1097  CB  SER A6927     2771   2023   2140      9    -74   -249       C  
ATOM   1098  OG  SER A6927      90.110  17.885  25.841  1.00 18.30           O  
ANISOU 1098  OG  SER A6927     2803   2025   2123     39   -117   -206       O  
ATOM   1099  N   ASP A6928      87.347  19.232  25.011  1.00 16.92           N  
ANISOU 1099  N   ASP A6928     2652   1875   1900    -51    -66   -108       N  
ATOM   1100  CA  ASP A6928      86.399  19.769  26.014  1.00 17.55           C  
ANISOU 1100  CA  ASP A6928     2727   1976   1963    -46    -63    -69       C  
ATOM   1101  C   ASP A6928      86.266  18.717  27.123  1.00 17.09           C  
ANISOU 1101  C   ASP A6928     2696   1911   1885    -20    -82    -38       C  
ATOM   1102  O   ASP A6928      85.275  18.766  27.871  1.00 17.09           O  
ANISOU 1102  O   ASP A6928     2704   1922   1866    -25    -66      5       O  
ATOM   1103  CB  ASP A6928      85.059  20.140  25.384  1.00 18.60           C  
ANISOU 1103  CB  ASP A6928     2858   2107   2102    -85    -51    -29       C  
ATOM   1104  CG  ASP A6928      84.206  21.028  26.271  1.00 20.58           C  
ANISOU 1104  CG  ASP A6928     3085   2381   2350    -78    -34     -8       C  
ATOM   1105  OD1 ASP A6928      84.800  21.824  27.031  1.00 21.26           O  
ANISOU 1105  OD1 ASP A6928     3160   2489   2427    -49    -27    -38       O  
ATOM   1106  OD2 ASP A6928      82.955  20.915  26.197  1.00 21.49           O  
ANISOU 1106  OD2 ASP A6928     3191   2493   2481   -100    -27     31       O  
ATOM   1107  N   MET A6929      87.228  17.791  27.216  1.00 17.03           N  
ANISOU 1107  N   MET A6929     2704   1881   1884      6   -111    -59       N  
ATOM   1108  CA  MET A6929      87.165  16.758  28.283  1.00 17.48           C  
ANISOU 1108  CA  MET A6929     2802   1921   1918     34   -137    -20       C  
ATOM   1109  C   MET A6929      87.149  17.445  29.648  1.00 17.94           C  
ANISOU 1109  C   MET A6929     2869   2016   1928     65   -138    -12       C  
ATOM   1110  O   MET A6929      87.885  18.428  29.850  1.00 17.86           O  
ANISOU 1110  O   MET A6929     2831   2033   1920     87   -147    -64       O  
ATOM   1111  CB  MET A6929      88.312  15.749  28.194  1.00 18.39           C  
ANISOU 1111  CB  MET A6929     2928   1999   2058     71   -181    -51       C  
ATOM   1112  CG  MET A6929      88.156  14.838  26.987  1.00 18.77           C  
ANISOU 1112  CG  MET A6929     2983   2004   2144     42   -177    -57       C  
ATOM   1113  SD  MET A6929      89.370  13.517  26.914  1.00 20.43           S  
ANISOU 1113  SD  MET A6929     3205   2159   2398     91   -226    -95       S  
ATOM   1114  CE  MET A6929      90.861  14.445  26.560  1.00 20.27           C  
ANISOU 1114  CE  MET A6929     3119   2170   2413    121   -221   -190       C  
ATOM   1115  N   TYR A6930      86.318  16.914  30.536  1.00 18.42           N  
ANISOU 1115  N   TYR A6930     2973   2075   1948     64   -125     50       N  
ATOM   1116  CA  TYR A6930      86.110  17.522  31.865  1.00 19.75           C  
ANISOU 1116  CA  TYR A6930     3168   2283   2052     90   -113     61       C  
ATOM   1117  C   TYR A6930      85.313  16.557  32.731  1.00 22.12           C  
ANISOU 1117  C   TYR A6930     3530   2567   2304     83    -91    141       C  
ATOM   1118  O   TYR A6930      84.437  15.859  32.205  1.00 21.90           O  
ANISOU 1118  O   TYR A6930     3499   2509   2312     38    -61    187       O  
ATOM   1119  CB  TYR A6930      85.342  18.837  31.702  1.00 20.32           C  
ANISOU 1119  CB  TYR A6930     3195   2392   2132     66    -63     44       C  
ATOM   1120  CG  TYR A6930      85.026  19.535  32.994  1.00 21.30           C  
ANISOU 1120  CG  TYR A6930     3343   2557   2190     92    -39     44       C  
ATOM   1121  CD1 TYR A6930      86.035  20.114  33.740  1.00 21.40           C  
ANISOU 1121  CD1 TYR A6930     3371   2593   2167    139    -82     -9       C  
ATOM   1122  CD2 TYR A6930      83.725  19.644  33.460  1.00 22.78           C  
ANISOU 1122  CD2 TYR A6930     3536   2761   2358     68     28     88       C  
ATOM   1123  CE1 TYR A6930      85.770  20.752  34.942  1.00 23.04           C  
ANISOU 1123  CE1 TYR A6930     3612   2840   2302    166    -64    -20       C  
ATOM   1124  CE2 TYR A6930      83.438  20.300  34.649  1.00 24.55           C  
ANISOU 1124  CE2 TYR A6930     3787   3026   2514     94     62     79       C  
ATOM   1125  CZ  TYR A6930      84.466  20.856  35.393  1.00 24.48           C  
ANISOU 1125  CZ  TYR A6930     3806   3040   2453    144     13     23       C  
ATOM   1126  OH  TYR A6930      84.206  21.496  36.575  1.00 26.40           O  
ANISOU 1126  OH  TYR A6930     4088   3325   2618    172     42      4       O  
ATOM   1127  N   ASP A6931      85.631  16.540  34.019  1.00 24.29           N  
ANISOU 1127  N   ASP A6931     3864   2862   2501    124   -108    154       N  
ATOM   1128  CA  ASP A6931      84.889  15.742  35.023  1.00 27.76           C  
ANISOU 1128  CA  ASP A6931     4380   3291   2873    117    -73    237       C  
ATOM   1129  C   ASP A6931      84.519  16.724  36.128  1.00 28.04           C  
ANISOU 1129  C   ASP A6931     4440   3388   2825    135    -30    227       C  
ATOM   1130  O   ASP A6931      85.410  17.242  36.787  1.00 27.07           O  
ANISOU 1130  O   ASP A6931     4343   3291   2648    187    -84    180       O  
ATOM   1131  CB  ASP A6931      85.732  14.572  35.519  1.00 30.65           C  
ANISOU 1131  CB  ASP A6931     4821   3612   3210    157   -146    270       C  
ATOM   1132  CG  ASP A6931      85.037  13.731  36.576  1.00 34.40           C  
ANISOU 1132  CG  ASP A6931     5393   4069   3606    148   -109    367       C  
ATOM   1133  OD1 ASP A6931      83.892  14.074  36.953  1.00 36.68           O  
ANISOU 1133  OD1 ASP A6931     5683   4388   3865    108    -14    404       O  
ATOM   1134  OD2 ASP A6931      85.652  12.755  37.017  1.00 38.58           O  
ANISOU 1134  OD2 ASP A6931     5996   4553   4110    181   -172    406       O  
ATOM   1135  N   PRO A6932      83.225  17.077  36.309  1.00 29.63           N  
ANISOU 1135  N   PRO A6932     4623   3612   3021     95     65    258       N  
ATOM   1136  CA  PRO A6932      82.838  18.056  37.328  1.00 31.89           C  
ANISOU 1136  CA  PRO A6932     4930   3956   3230    115    118    236       C  
ATOM   1137  C   PRO A6932      83.245  17.640  38.749  1.00 34.61           C  
ANISOU 1137  C   PRO A6932     5393   4316   3439    158    102    268       C  
ATOM   1138  O   PRO A6932      83.251  18.501  39.618  1.00 35.32           O  
ANISOU 1138  O   PRO A6932     5511   4456   3449    189    121    227       O  
ATOM   1139  CB  PRO A6932      81.309  18.177  37.200  1.00 33.21           C  
ANISOU 1139  CB  PRO A6932     5049   4131   3435     60    229    274       C  
ATOM   1140  CG  PRO A6932      80.882  16.958  36.399  1.00 34.25           C  
ANISOU 1140  CG  PRO A6932     5167   4204   3642     10    230    339       C  
ATOM   1141  CD  PRO A6932      82.074  16.579  35.543  1.00 31.65           C  
ANISOU 1141  CD  PRO A6932     4832   3838   3353     31    125    306       C  
ATOM   1142  N   LYS A6933      83.600  16.365  38.938  1.00 39.58           N  
ANISOU 1142  N   LYS A6933     5266   5836   3933  -1095    667   -312       N  
ATOM   1143  CA  LYS A6933      84.023  15.855  40.272  1.00 42.87           C  
ANISOU 1143  CA  LYS A6933     6039   6045   4203  -1237    751   -169       C  
ATOM   1144  C   LYS A6933      85.444  16.341  40.588  1.00 41.81           C  
ANISOU 1144  C   LYS A6933     6110   5724   4052   -995    542     -4       C  
ATOM   1145  O   LYS A6933      85.861  16.237  41.757  1.00 40.99           O  
ANISOU 1145  O   LYS A6933     6278   5500   3793  -1019    555     97       O  
ATOM   1146  CB  LYS A6933      83.908  14.328  40.330  1.00 46.47           C  
ANISOU 1146  CB  LYS A6933     6722   6306   4626  -1521    874   -130       C  
ATOM   1147  CG  LYS A6933      82.478  13.800  40.297  1.00 50.98           C  
ANISOU 1147  CG  LYS A6933     7111   7061   5198  -1853   1145   -335       C  
ATOM   1148  CD  LYS A6933      82.370  12.294  40.376  1.00 55.49           C  
ANISOU 1148  CD  LYS A6933     7964   7383   5735  -2179   1315   -305       C  
ATOM   1149  CE  LYS A6933      80.934  11.813  40.411  1.00 60.42           C  
ANISOU 1149  CE  LYS A6933     8381   8207   6369  -2573   1632   -559       C  
ATOM   1150  NZ  LYS A6933      80.846  10.337  40.522  1.00 64.63           N  
ANISOU 1150  NZ  LYS A6933     9254   8435   6866  -2935   1846   -532       N  
ATOM   1151  N  ATHR A6934      86.146  16.914  39.603  0.60 39.28           N  
ANISOU 1151  N  ATHR A6934     5657   5401   3867   -773    366     -3       N  
ATOM   1152  N  BTHR A6934      86.162  16.807  39.558  0.40 39.76           N  
ANISOU 1152  N  BTHR A6934     5725   5450   3932   -783    365      0       N  
ATOM   1153  CA ATHR A6934      87.517  17.448  39.851  0.60 39.01           C  
ANISOU 1153  CA ATHR A6934     5752   5224   3844   -576    191     90       C  
ATOM   1154  CA BTHR A6934      87.547  17.324  39.715  0.40 39.50           C  
ANISOU 1154  CA BTHR A6934     5812   5276   3920   -580    184     93       C  
ATOM   1155  C  ATHR A6934      87.432  18.692  40.747  0.60 40.15           C  
ANISOU 1155  C  ATHR A6934     5880   5463   3910   -491    219     55       C  
ATOM   1156  C  BTHR A6934      87.519  18.492  40.704  0.40 40.63           C  
ANISOU 1156  C  BTHR A6934     5963   5498   3973   -503    208     68       C  
ATOM   1157  O  ATHR A6934      88.438  19.010  41.411  0.60 42.20           O  
ANISOU 1157  O  ATHR A6934     6283   5624   4124   -401    109    102       O  
ATOM   1158  O  BTHR A6934      88.480  18.631  41.486  0.40 42.83           O  
ANISOU 1158  O  BTHR A6934     6418   5670   4184   -434    105    128       O  
ATOM   1159  CB ATHR A6934      88.249  17.794  38.548  0.60 37.60           C  
ANISOU 1159  CB ATHR A6934     5438   5018   3828   -409     59     75       C  
ATOM   1160  CB BTHR A6934      88.121  17.776  38.366  0.40 38.10           C  
ANISOU 1160  CB BTHR A6934     5471   5101   3905   -412     68     63       C  
ATOM   1161  OG1ATHR A6934      87.478  18.785  37.865  0.60 37.90           O  
ANISOU 1161  OG1ATHR A6934     5251   5238   3911   -316    112    -19       O  
ATOM   1162  OG1BTHR A6934      89.538  17.911  38.477  0.40 36.76           O  
ANISOU 1162  OG1BTHR A6934     5409   4780   3775   -289    -79    120       O  
ATOM   1163  CG2ATHR A6934      88.480  16.587  37.664  0.60 35.89           C  
ANISOU 1163  CG2ATHR A6934     5251   4698   3688   -471     17     96       C  
ATOM   1164  CG2BTHR A6934      87.515  19.080  37.894  0.40 37.25           C  
ANISOU 1164  CG2BTHR A6934     5157   5166   3830   -280    109    -24       C  
ATOM   1165  N  ALYS A6935      86.280  19.369  40.757  0.60 41.61           N  
ANISOU 1165  N  ALYS A6935     5880   5848   4081   -504    354    -55       N  
ATOM   1166  N  BLYS A6935      86.451  19.294  40.654  0.40 41.71           N  
ANISOU 1166  N  BLYS A6935     5905   5833   4107   -494    330    -41       N  
ATOM   1167  CA ALYS A6935      86.114  20.597  41.579  0.60 44.30           C  
ANISOU 1167  CA ALYS A6935     6208   6271   4352   -409    400   -112       C  
ATOM   1168  CA BLYS A6935      86.273  20.461  41.555  0.40 43.57           C  
ANISOU 1168  CA BLYS A6935     6141   6150   4263   -415    381    -94       C  
ATOM   1169  C  ALYS A6935      85.927  20.200  43.048  0.60 47.31           C  
ANISOU 1169  C  ALYS A6935     6798   6641   4537   -566    501    -80       C  
ATOM   1170  C  BLYS A6935      86.087  19.956  42.989  0.40 46.38           C  
ANISOU 1170  C  BLYS A6935     6715   6485   4422   -580    479    -54       C  
ATOM   1171  O  ALYS A6935      84.777  19.905  43.440  0.60 47.87           O  
ANISOU 1171  O  ALYS A6935     6809   6851   4528   -730    695   -153       O  
ATOM   1172  O  BLYS A6935      85.058  19.304  43.264  0.40 46.48           O  
ANISOU 1172  O  BLYS A6935     6710   6588   4360   -778    659    -94       O  
ATOM   1173  CB ALYS A6935      84.936  21.439  41.078  0.60 46.67           C  
ANISOU 1173  CB ALYS A6935     6245   6792   4694   -314    497   -255       C  
ATOM   1174  CB BLYS A6935      85.084  21.317  41.104  0.40 45.22           C  
ANISOU 1174  CB BLYS A6935     6091   6579   4509   -328    484   -236       C  
ATOM   1175  CG ALYS A6935      84.703  22.732  41.849  0.60 49.16           C  
ANISOU 1175  CG ALYS A6935     6557   7173   4949   -188    558   -332       C  
ATOM   1176  CG BLYS A6935      84.864  22.591  41.911  0.40 47.07           C  
ANISOU 1176  CG BLYS A6935     6326   6879   4679   -211    545   -311       C  
ATOM   1177  CD ALYS A6935      83.601  23.594  41.275  0.60 51.93           C  
ANISOU 1177  CD ALYS A6935     6662   7727   5340    -11    620   -478       C  
ATOM   1178  CD BLYS A6935      83.771  23.483  41.357  0.40 49.10           C  
ANISOU 1178  CD BLYS A6935     6340   7336   4977    -37    612   -455       C  
ATOM   1179  CE ALYS A6935      83.404  24.885  42.042  0.60 54.84           C  
ANISOU 1179  CE ALYS A6935     7061   8121   5653    137    688   -560       C  
ATOM   1180  CE BLYS A6935      83.615  24.777  42.129  0.40 51.15           C  
ANISOU 1180  CE BLYS A6935     6635   7616   5181    107    675   -535       C  
ATOM   1181  NZ ALYS A6935      82.334  25.716  41.442  0.60 57.09           N  
ANISOU 1181  NZ ALYS A6935     7125   8596   5968    380    724   -706       N  
ATOM   1182  NZ BLYS A6935      82.572  25.646  41.534  0.40 53.10           N  
ANISOU 1182  NZ BLYS A6935     6668   8044   5462    349    715   -676       N  
ATOM   1183  N  AASN A6936      87.027  20.188  43.809  0.60 48.06           N  
ANISOU 1183  N  AASN A6936     7124   6591   4544   -515    376      3       N  
ATOM   1184  N  BASN A6936      87.073  20.227  43.846  0.40 47.32           N  
ANISOU 1184  N  BASN A6936     7036   6494   4447   -508    370      3       N  
ATOM   1185  CA AASN A6936      87.011  19.849  45.258  0.60 50.36           C  
ANISOU 1185  CA AASN A6936     7686   6855   4591   -615    437     53       C  
ATOM   1186  CA BASN A6936      87.031  19.832  45.279  0.40 50.09           C  
ANISOU 1186  CA BASN A6936     7660   6818   4554   -615    434     56       C  
ATOM   1187  C  AASN A6936      87.704  20.986  46.018  0.60 50.06           C  
ANISOU 1187  C  AASN A6936     7690   6838   4493   -469    339     -6       C  
ATOM   1188  C  BASN A6936      87.710  20.944  46.083  0.40 50.31           C  
ANISOU 1188  C  BASN A6936     7737   6866   4511   -474    340     -2       C  
ATOM   1189  O  AASN A6936      88.948  21.064  45.966  0.60 48.92           O  
ANISOU 1189  O  AASN A6936     7606   6591   4389   -345    130     14       O  
ATOM   1190  O  BASN A6936      88.956  20.960  46.129  0.40 49.71           O  
ANISOU 1190  O  BASN A6936     7744   6686   4454   -355    130     25       O  
ATOM   1191  CB AASN A6936      87.663  18.491  45.533  0.60 51.41           C  
ANISOU 1191  CB AASN A6936     8123   6792   4618   -673    352    208       C  
ATOM   1192  CB BASN A6936      87.692  18.473  45.521  0.40 51.17           C  
ANISOU 1192  CB BASN A6936     8095   6757   4588   -670    346    210       C  
ATOM   1193  CG AASN A6936      87.614  18.092  46.994  0.60 55.62           C  
ANISOU 1193  CG AASN A6936     9009   7277   4846   -751    419    285       C  
ATOM   1194  CG BASN A6936      87.593  18.025  46.964  0.40 54.95           C  
ANISOU 1194  CG BASN A6936     8928   7185   4763   -759    424    290       C  
ATOM   1195  OD1AASN A6936      87.038  18.798  47.820  0.60 56.09           O  
ANISOU 1195  OD1AASN A6936     9064   7470   4776   -796    553    209       O  
ATOM   1196  OD1BASN A6936      86.929  18.670  47.773  0.40 56.02           O  
ANISOU 1196  OD1BASN A6936     9059   7457   4768   -823    577    215       O  
ATOM   1197  ND2AASN A6936      88.215  16.959  47.322  0.60 57.58           N  
ANISOU 1197  ND2AASN A6936     9595   7323   4957   -744    332    436       N  
ATOM   1198  ND2BASN A6936      88.247  16.923  47.294  0.40 56.69           N  
ANISOU 1198  ND2BASN A6936     9486   7203   4848   -740    325    440       N  
ATOM   1199  N   VAL A6937      86.913  21.832  46.685  1.00 52.62           N  
ANISOU 1199  N   VAL A6937     7959   7302   4731   -489    493   -113       N  
ATOM   1200  CA  VAL A6937      87.434  23.003  47.458  1.00 54.00           C  
ANISOU 1200  CA  VAL A6937     8174   7499   4843   -374    435   -211       C  
ATOM   1201  C   VAL A6937      87.880  22.559  48.858  1.00 55.48           C  
ANISOU 1201  C   VAL A6937     8672   7663   4745   -420    387   -160       C  
ATOM   1202  O   VAL A6937      88.337  23.433  49.619  1.00 59.37           O  
ANISOU 1202  O   VAL A6937     9213   8191   5151   -343    327   -265       O  
ATOM   1203  CB  VAL A6937      86.379  24.125  47.541  1.00 55.25           C  
ANISOU 1203  CB  VAL A6937     8155   7806   5029   -339    621   -363       C  
ATOM   1204  CG1 VAL A6937      85.941  24.591  46.160  1.00 54.47           C  
ANISOU 1204  CG1 VAL A6937     7796   7733   5166   -225    636   -406       C  
ATOM   1205  CG2 VAL A6937      85.169  23.717  48.373  1.00 57.71           C  
ANISOU 1205  CG2 VAL A6937     8503   8268   5154   -503    857   -397       C  
ATOM   1206  N   THR A6938      87.786  21.262  49.174  1.00 56.24           N  
ANISOU 1206  N   THR A6938     9001   7684   4684   -531    409    -12       N  
ATOM   1207  CA  THR A6938      88.147  20.750  50.528  1.00 58.14           C  
ANISOU 1207  CA  THR A6938     9622   7882   4586   -543    368     67       C  
ATOM   1208  C   THR A6938      89.562  20.157  50.516  1.00 56.28           C  
ANISOU 1208  C   THR A6938     9553   7509   4320   -368     49    155       C  
ATOM   1209  O   THR A6938      90.020  19.725  51.587  1.00 58.85           O  
ANISOU 1209  O   THR A6938    10215   7800   4344   -301    -53    224       O  
ATOM   1210  CB  THR A6938      87.145  19.699  51.028  1.00 61.24           C  
ANISOU 1210  CB  THR A6938    10260   8239   4768   -772    631    180       C  
ATOM   1211  OG1 THR A6938      87.363  18.472  50.331  1.00 62.30           O  
ANISOU 1211  OG1 THR A6938    10505   8194   4973   -818    585    328       O  
ATOM   1212  CG2 THR A6938      85.703  20.134  50.877  1.00 61.77           C  
ANISOU 1212  CG2 THR A6938    10078   8483   4908   -956    952     48       C  
ATOM   1213  N   LYS A6939      90.223  20.133  49.356  1.00 51.52           N  
ANISOU 1213  N   LYS A6939     8728   6847   3999   -277   -101    141       N  
ATOM   1214  CA  LYS A6939      91.598  19.570  49.268  1.00 50.01           C  
ANISOU 1214  CA  LYS A6939     8631   6559   3811    -89   -407    179       C  
ATOM   1215  C   LYS A6939      92.443  20.510  48.400  1.00 43.53           C  
ANISOU 1215  C   LYS A6939     7464   5788   3286      8   -540     13       C  
ATOM   1216  O   LYS A6939      91.853  21.331  47.674  1.00 39.25           O  
ANISOU 1216  O   LYS A6939     6682   5290   2942    -68   -379    -59       O  
ATOM   1217  CB  LYS A6939      91.517  18.123  48.763  1.00 55.28           C  
ANISOU 1217  CB  LYS A6939     9482   7046   4473   -120   -401    361       C  
ATOM   1218  CG  LYS A6939      92.836  17.362  48.665  1.00 59.32           C  
ANISOU 1218  CG  LYS A6939    10119   7445   4973    111   -709    407       C  
ATOM   1219  CD  LYS A6939      93.585  17.588  47.365  1.00 59.04           C  
ANISOU 1219  CD  LYS A6939     9734   7414   5281    191   -832    306       C  
ATOM   1220  CE  LYS A6939      94.950  16.932  47.336  1.00 61.63           C  
ANISOU 1220  CE  LYS A6939    10125   7683   5606    447  -1146    291       C  
ATOM   1221  NZ  LYS A6939      95.662  17.225  46.070  1.00 58.63           N  
ANISOU 1221  NZ  LYS A6939     9384   7329   5562    490  -1217    163       N  
ATOM   1222  N   GLU A6940      93.770  20.408  48.502  1.00 41.37           N  
ANISOU 1222  N   GLU A6940     7177   5513   3026    178   -815    -58       N  
ATOM   1223  CA  GLU A6940      94.681  21.289  47.728  1.00 39.48           C  
ANISOU 1223  CA  GLU A6940     6616   5318   3065    225   -906   -250       C  
ATOM   1224  C   GLU A6940      94.380  21.162  46.229  1.00 34.20           C  
ANISOU 1224  C   GLU A6940     5755   4564   2676    158   -781   -195       C  
ATOM   1225  O   GLU A6940      94.059  20.049  45.766  1.00 32.54           O  
ANISOU 1225  O   GLU A6940     5642   4259   2461    148   -766    -39       O  
ATOM   1226  CB  GLU A6940      96.139  20.948  48.023  1.00 44.31           C  
ANISOU 1226  CB  GLU A6940     7209   5974   3652    415  -1223   -363       C  
ATOM   1227  CG  GLU A6940      97.126  21.789  47.233  1.00 47.09           C  
ANISOU 1227  CG  GLU A6940     7216   6379   4297    411  -1275   -597       C  
ATOM   1228  CD  GLU A6940      98.582  21.617  47.632  1.00 54.44           C  
ANISOU 1228  CD  GLU A6940     8040   7430   5213    588  -1588   -802       C  
ATOM   1229  OE1 GLU A6940      99.456  21.827  46.763  1.00 59.23           O  
ANISOU 1229  OE1 GLU A6940     8366   8057   6079    584  -1625   -965       O  
ATOM   1230  OE2 GLU A6940      98.842  21.299  48.814  1.00 59.30           O  
ANISOU 1230  OE2 GLU A6940     8846   8138   5546    735  -1791   -818       O  
ATOM   1231  N   ASN A6941      94.485  22.276  45.508  1.00 30.20           N  
ANISOU 1231  N   ASN A6941     5018   4074   2383    114   -685   -326       N  
ATOM   1232  CA  ASN A6941      94.237  22.289  44.043  1.00 28.07           C  
ANISOU 1232  CA  ASN A6941     4588   3732   2343     78   -571   -283       C  
ATOM   1233  C   ASN A6941      95.567  21.976  43.347  1.00 28.25           C  
ANISOU 1233  C   ASN A6941     4480   3719   2532    148   -727   -365       C  
ATOM   1234  O   ASN A6941      96.298  22.917  42.992  1.00 28.85           O  
ANISOU 1234  O   ASN A6941     4398   3804   2760    126   -704   -535       O  
ATOM   1235  CB  ASN A6941      93.636  23.624  43.607  1.00 26.74           C  
ANISOU 1235  CB  ASN A6941     4314   3567   2278     30   -373   -358       C  
ATOM   1236  CG  ASN A6941      93.340  23.667  42.128  1.00 24.90           C  
ANISOU 1236  CG  ASN A6941     3966   3269   2223     34   -271   -304       C  
ATOM   1237  OD1 ASN A6941      93.376  22.631  41.460  1.00 23.04           O  
ANISOU 1237  OD1 ASN A6941     3718   3006   2029     40   -324   -209       O  
ATOM   1238  ND2 ASN A6941      93.040  24.852  41.619  1.00 24.07           N  
ANISOU 1238  ND2 ASN A6941     3815   3128   2203     46   -124   -364       N  
ATOM   1239  N  AASP A6942      95.861  20.684  43.171  0.70 29.26           N  
ANISOU 1239  N  AASP A6942     4685   3798   2631    222   -858   -263       N  
ATOM   1240  N  BASP A6942      95.867  20.686  43.177  0.30 28.69           N  
ANISOU 1240  N  BASP A6942     4613   3727   2559    222   -859   -264       N  
ATOM   1241  CA AASP A6942      97.133  20.231  42.549  0.70 30.41           C  
ANISOU 1241  CA AASP A6942     4695   3930   2927    323  -1020   -360       C  
ATOM   1242  CA BASP A6942      97.145  20.249  42.556  0.30 29.18           C  
ANISOU 1242  CA BASP A6942     4537   3776   2773    323  -1021   -363       C  
ATOM   1243  C  AASP A6942      96.930  19.944  41.060  0.70 27.43           C  
ANISOU 1243  C  AASP A6942     4209   3471   2740    275   -899   -302       C  
ATOM   1244  C  BASP A6942      96.935  19.973  41.065  0.30 26.88           C  
ANISOU 1244  C  BASP A6942     4137   3403   2672    274   -897   -306       C  
ATOM   1245  O  AASP A6942      95.766  19.807  40.622  0.70 25.85           O  
ANISOU 1245  O  AASP A6942     4071   3232   2518    192   -743   -168       O  
ATOM   1246  O  BASP A6942      95.768  19.875  40.633  0.30 25.57           O  
ANISOU 1246  O  BASP A6942     4031   3199   2484    190   -738   -173       O  
ATOM   1247  CB AASP A6942      97.682  18.988  43.259  0.70 34.23           C  
ANISOU 1247  CB AASP A6942     5357   4394   3251    497  -1262   -300       C  
ATOM   1248  CB BASP A6942      97.689  18.997  43.245  0.30 31.75           C  
ANISOU 1248  CB BASP A6942     5040   4081   2942    496  -1261   -302       C  
ATOM   1249  CG AASP A6942      98.297  19.270  44.620  0.70 38.56           C  
ANISOU 1249  CG AASP A6942     5978   5062   3608    614  -1460   -416       C  
ATOM   1250  CG BASP A6942      96.735  17.817  43.184  0.30 32.29           C  
ANISOU 1250  CG BASP A6942     5369   4009   2889    469  -1191    -63       C  
ATOM   1251  OD1AASP A6942      98.890  20.356  44.783  0.70 41.62           O  
ANISOU 1251  OD1AASP A6942     6156   5571   4084    574  -1473   -641       O  
ATOM   1252  OD1BASP A6942      95.545  18.042  42.887  0.30 31.42           O  
ANISOU 1252  OD1BASP A6942     5275   3880   2781    301   -968     26       O  
ATOM   1253  OD2AASP A6942      98.176  18.404  45.508  0.70 42.92           O  
ANISOU 1253  OD2AASP A6942     6821   5576   3909    739  -1590   -287       O  
ATOM   1254  OD2BASP A6942      97.190  16.683  43.430  0.30 35.17           O  
ANISOU 1254  OD2BASP A6942     5920   4283   3158    620  -1355     10       O  
ATOM   1255  N   SER A6943      98.040  19.862  40.323  1.00 26.67           N  
ANISOU 1255  N   SER A6943     3938   3378   2816    328   -970   -432       N  
ATOM   1256  CA  SER A6943      98.011  19.534  38.880  1.00 24.73           C  
ANISOU 1256  CA  SER A6943     3601   3062   2732    298   -866   -398       C  
ATOM   1257  C   SER A6943      97.285  18.193  38.711  1.00 24.50           C  
ANISOU 1257  C   SER A6943     3745   2944   2618    328   -896   -212       C  
ATOM   1258  O   SER A6943      97.564  17.262  39.493  1.00 25.02           O  
ANISOU 1258  O   SER A6943     3969   2972   2565    437  -1063   -163       O  
ATOM   1259  CB  SER A6943      99.412  19.501  38.327  1.00 25.62           C  
ANISOU 1259  CB  SER A6943     3507   3211   3016    354   -945   -593       C  
ATOM   1260  OG  SER A6943      99.412  19.087  36.978  1.00 23.71           O  
ANISOU 1260  OG  SER A6943     3206   2903   2899    334   -846   -560       O  
ATOM   1261  N   LYS A6944      96.383  18.099  37.736  1.00 22.88           N  
ANISOU 1261  N   LYS A6944     3533   2703   2457    240   -740   -125       N  
ATOM   1262  CA  LYS A6944      95.590  16.856  37.548  1.00 23.71           C  
ANISOU 1262  CA  LYS A6944     3788   2726   2494    209   -730      9       C  
ATOM   1263  C   LYS A6944      96.224  16.004  36.445  1.00 25.02           C  
ANISOU 1263  C   LYS A6944     3898   2816   2791    269   -777    -23       C  
ATOM   1264  O   LYS A6944      96.784  16.566  35.485  1.00 25.36           O  
ANISOU 1264  O   LYS A6944     3763   2899   2972    279   -727   -123       O  
ATOM   1265  CB  LYS A6944      94.136  17.195  37.201  1.00 22.75           C  
ANISOU 1265  CB  LYS A6944     3654   2660   2330     77   -548     72       C  
ATOM   1266  CG  LYS A6944      93.397  18.054  38.222  1.00 22.68           C  
ANISOU 1266  CG  LYS A6944     3682   2737   2198     25   -473     84       C  
ATOM   1267  CD  LYS A6944      93.393  17.479  39.625  1.00 23.92           C  
ANISOU 1267  CD  LYS A6944     4053   2856   2177     17   -543    148       C  
ATOM   1268  CE  LYS A6944      92.532  18.259  40.601  1.00 24.15           C  
ANISOU 1268  CE  LYS A6944     4122   2983   2069    -53   -434    148       C  
ATOM   1269  NZ  LYS A6944      92.972  19.667  40.718  1.00 23.40           N  
ANISOU 1269  NZ  LYS A6944     3896   2961   2031      4   -433     36       N  
ATOM   1270  N  AGLU A6945      96.120  14.684  36.585  0.70 26.27           N  
ANISOU 1270  N  AGLU A6945     4239   2849   2894    298   -844     55       N  
ATOM   1271  N  BGLU A6945      96.146  14.679  36.589  0.30 26.30           N  
ANISOU 1271  N  BGLU A6945     4241   2851   2898    301   -848     53       N  
ATOM   1272  CA AGLU A6945      96.672  13.745  35.575  0.70 27.26           C  
ANISOU 1272  CA AGLU A6945     4341   2879   3136    367   -887     14       C  
ATOM   1273  CA BGLU A6945      96.685  13.756  35.556  0.30 26.91           C  
ANISOU 1273  CA BGLU A6945     4292   2837   3094    368   -887     12       C  
ATOM   1274  C  AGLU A6945      95.498  13.273  34.713  0.70 26.14           C  
ANISOU 1274  C  AGLU A6945     4227   2708   2996    205   -734     67       C  
ATOM   1275  C  BGLU A6945      95.504  13.274  34.705  0.30 25.98           C  
ANISOU 1275  C  BGLU A6945     4205   2688   2977    206   -734     67       C  
ATOM   1276  O  AGLU A6945      94.954  14.111  33.968  0.70 24.95           O  
ANISOU 1276  O  AGLU A6945     3910   2682   2885    128   -617     32       O  
ATOM   1277  O  BGLU A6945      94.964  14.105  33.948  0.30 24.67           O  
ANISOU 1277  O  BGLU A6945     3874   2647   2852    129   -617     31       O  
ATOM   1278  CB AGLU A6945      97.452  12.629  36.273  0.70 30.59           C  
ANISOU 1278  CB AGLU A6945     4967   3159   3497    550  -1077     39       C  
ATOM   1279  CB BGLU A6945      97.494  12.635  36.211  0.30 29.74           C  
ANISOU 1279  CB BGLU A6945     4847   3053   3400    553  -1078     31       C  
ATOM   1280  CG AGLU A6945      98.655  13.152  37.036  0.70 33.01           C  
ANISOU 1280  CG AGLU A6945     5173   3566   3803    740  -1266    -75       C  
ATOM   1281  CG BGLU A6945      98.770  13.132  36.870  0.30 31.50           C  
ANISOU 1281  CG BGLU A6945     4950   3376   3639    749  -1268    -94       C  
ATOM   1282  CD AGLU A6945      99.466  12.106  37.777  0.70 37.08           C  
ANISOU 1282  CD AGLU A6945     5895   3970   4223   1007  -1506    -63       C  
ATOM   1283  CD BGLU A6945      99.730  13.852  35.935  0.30 31.47           C  
ANISOU 1283  CD BGLU A6945     4607   3505   3842    771  -1249   -298       C  
ATOM   1284  OE1AGLU A6945      99.311  10.911  37.476  0.70 40.69           O  
ANISOU 1284  OE1AGLU A6945     6574   4226   4660   1063  -1515     22       O  
ATOM   1285  OE1BGLU A6945      99.444  13.915  34.724  0.30 31.80           O  
ANISOU 1285  OE1BGLU A6945     4550   3539   3993    663  -1094   -312       O  
ATOM   1286  OE2AGLU A6945     100.240  12.495  38.667  0.70 41.44           O  
ANISOU 1286  OE2AGLU A6945     6402   4634   4709   1172  -1689   -152       O  
ATOM   1287  OE2BGLU A6945     100.765  14.349  36.420  0.30 33.56           O  
ANISOU 1287  OE2BGLU A6945     4711   3892   4148    884  -1377   -461       O  
ATOM   1288  N   GLY A6946      95.101  12.007  34.842  1.00 27.02           N  
ANISOU 1288  N   GLY A6946     4556   2657   3051    160   -732    136       N  
ATOM   1289  CA  GLY A6946      93.970  11.479  34.053  1.00 26.76           C  
ANISOU 1289  CA  GLY A6946     4524   2616   3027    -29   -584    132       C  
ATOM   1290  C   GLY A6946      94.101  11.812  32.577  1.00 24.93           C  
ANISOU 1290  C   GLY A6946     4060   2491   2920    -11   -551     24       C  
ATOM   1291  O   GLY A6946      95.193  11.602  32.022  1.00 24.73           O  
ANISOU 1291  O   GLY A6946     3987   2414   2994    128   -632    -39       O  
ATOM   1292  N   PHE A6947      93.052  12.382  31.970  1.00 23.35           N  
ANISOU 1292  N   PHE A6947     3716   2455   2699   -124   -440     -9       N  
ATOM   1293  CA  PHE A6947      93.082  12.644  30.507  1.00 22.09           C  
ANISOU 1293  CA  PHE A6947     3393   2396   2603    -88   -411   -100       C  
ATOM   1294  C   PHE A6947      94.156  13.681  30.147  1.00 20.82           C  
ANISOU 1294  C   PHE A6947     3128   2278   2505     57   -431   -124       C  
ATOM   1295  O   PHE A6947      94.573  13.693  28.986  1.00 20.38           O  
ANISOU 1295  O   PHE A6947     3002   2243   2499    104   -404   -193       O  
ATOM   1296  CB  PHE A6947      91.699  13.032  29.974  1.00 22.06           C  
ANISOU 1296  CB  PHE A6947     3265   2586   2528   -184   -326   -146       C  
ATOM   1297  CG  PHE A6947      91.117  14.303  30.536  1.00 21.73           C  
ANISOU 1297  CG  PHE A6947     3144   2695   2417   -152   -287   -109       C  
ATOM   1298  CD1 PHE A6947      91.617  15.539  30.155  1.00 21.20           C  
ANISOU 1298  CD1 PHE A6947     3018   2679   2355     -7   -281    -95       C  
ATOM   1299  CD2 PHE A6947      90.039  14.265  31.406  1.00 23.12           C  
ANISOU 1299  CD2 PHE A6947     3317   2948   2518   -277   -228   -104       C  
ATOM   1300  CE1 PHE A6947      91.073  16.711  30.662  1.00 21.14           C  
ANISOU 1300  CE1 PHE A6947     2974   2774   2282     40   -237    -68       C  
ATOM   1301  CE2 PHE A6947      89.497  15.439  31.911  1.00 23.40           C  
ANISOU 1301  CE2 PHE A6947     3274   3124   2491   -222   -189    -91       C  
ATOM   1302  CZ  PHE A6947      90.023  16.655  31.547  1.00 21.71           C  
ANISOU 1302  CZ  PHE A6947     3025   2936   2287    -49   -204    -68       C  
ATOM   1303  N   PHE A6948      94.602  14.522  31.089  1.00 20.82           N  
ANISOU 1303  N   PHE A6948     3125   2289   2496    102   -454    -89       N  
ATOM   1304  CA  PHE A6948      95.660  15.504  30.728  1.00 20.94           C  
ANISOU 1304  CA  PHE A6948     3036   2332   2588    184   -430   -154       C  
ATOM   1305  C   PHE A6948      96.967  14.788  30.374  1.00 22.37           C  
ANISOU 1305  C   PHE A6948     3177   2434   2887    265   -502   -251       C  
ATOM   1306  O   PHE A6948      97.689  15.294  29.505  1.00 22.43           O  
ANISOU 1306  O   PHE A6948     3079   2473   2969    285   -423   -343       O  
ATOM   1307  CB  PHE A6948      95.889  16.524  31.843  1.00 20.61           C  
ANISOU 1307  CB  PHE A6948     2988   2320   2523    190   -437   -143       C  
ATOM   1308  CG  PHE A6948      94.788  17.539  31.968  1.00 19.88           C  
ANISOU 1308  CG  PHE A6948     2902   2313   2337    151   -336    -86       C  
ATOM   1309  CD1 PHE A6948      94.626  18.510  30.994  1.00 19.52           C  
ANISOU 1309  CD1 PHE A6948     2825   2304   2286    184   -217   -100       C  
ATOM   1310  CD2 PHE A6948      93.940  17.551  33.065  1.00 19.90           C  
ANISOU 1310  CD2 PHE A6948     2967   2351   2242    105   -351    -25       C  
ATOM   1311  CE1 PHE A6948      93.628  19.463  31.103  1.00 19.53           C  
ANISOU 1311  CE1 PHE A6948     2851   2376   2193    212   -144    -55       C  
ATOM   1312  CE2 PHE A6948      92.938  18.503  33.167  1.00 19.61           C  
ANISOU 1312  CE2 PHE A6948     2908   2411   2129    103   -260     -5       C  
ATOM   1313  CZ  PHE A6948      92.789  19.461  32.194  1.00 19.34           C  
ANISOU 1313  CZ  PHE A6948     2837   2411   2098    177   -172    -21       C  
ATOM   1314  N   THR A6949      97.276  13.682  31.055  1.00 23.95           N  
ANISOU 1314  N   THR A6949     3479   2530   3092    324   -636   -237       N  
ATOM   1315  CA  THR A6949      98.505  12.909  30.742  1.00 26.56           C  
ANISOU 1315  CA  THR A6949     3766   2791   3532    461   -732   -351       C  
ATOM   1316  C   THR A6949      98.421  12.473  29.276  1.00 25.42           C  
ANISOU 1316  C   THR A6949     3577   2639   3442    430   -635   -414       C  
ATOM   1317  O   THR A6949      99.415  12.620  28.540  1.00 25.26           O  
ANISOU 1317  O   THR A6949     3414   2656   3526    491   -600   -551       O  
ATOM   1318  CB  THR A6949      98.647  11.699  31.673  1.00 29.23           C  
ANISOU 1318  CB  THR A6949     4310   2975   3822    572   -895   -293       C  
ATOM   1319  OG1 THR A6949      98.585  12.187  33.016  1.00 31.65           O  
ANISOU 1319  OG1 THR A6949     4686   3311   4027    593   -973   -225       O  
ATOM   1320  CG2 THR A6949      99.932  10.930  31.452  1.00 31.94           C  
ANISOU 1320  CG2 THR A6949     4607   3256   4271    785  -1028   -427       C  
ATOM   1321  N   TYR A6950      97.244  11.998  28.874  1.00 24.05           N  
ANISOU 1321  N   TYR A6950     3503   2442   3190    322   -579   -343       N  
ATOM   1322  CA  TYR A6950      97.041  11.532  27.481  1.00 24.03           C  
ANISOU 1322  CA  TYR A6950     3471   2453   3206    291   -504   -420       C  
ATOM   1323  C   TYR A6950      97.201  12.700  26.501  1.00 22.99           C  
ANISOU 1323  C   TYR A6950     3209   2464   3060    286   -377   -463       C  
ATOM   1324  O   TYR A6950      97.918  12.557  25.493  1.00 22.41           O  
ANISOU 1324  O   TYR A6950     3077   2397   3039    328   -318   -570       O  
ATOM   1325  CB  TYR A6950      95.663  10.887  27.329  1.00 24.24           C  
ANISOU 1325  CB  TYR A6950     3593   2471   3144    151   -474   -379       C  
ATOM   1326  CG  TYR A6950      95.333  10.537  25.903  1.00 24.48           C  
ANISOU 1326  CG  TYR A6950     3575   2564   3161    116   -413   -483       C  
ATOM   1327  CD1 TYR A6950      95.804   9.367  25.328  1.00 26.24           C  
ANISOU 1327  CD1 TYR A6950     3862   2653   3452    141   -433   -582       C  
ATOM   1328  CD2 TYR A6950      94.582  11.395  25.118  1.00 23.81           C  
ANISOU 1328  CD2 TYR A6950     3396   2673   2975     91   -346   -492       C  
ATOM   1329  CE1 TYR A6950      95.524   9.053  24.006  1.00 26.69           C  
ANISOU 1329  CE1 TYR A6950     3878   2783   3480    108   -378   -701       C  
ATOM   1330  CE2 TYR A6950      94.291  11.093  23.798  1.00 24.75           C  
ANISOU 1330  CE2 TYR A6950     3484   2876   3042     87   -312   -598       C  
ATOM   1331  CZ  TYR A6950      94.761   9.918  23.242  1.00 26.14           C  
ANISOU 1331  CZ  TYR A6950     3711   2932   3289     79   -324   -709       C  
ATOM   1332  OH  TYR A6950      94.464   9.612  21.943  1.00 27.95           O  
ANISOU 1332  OH  TYR A6950     3913   3256   3447     70   -293   -834       O  
ATOM   1333  N  AILE A6951      96.548  13.832  26.784  0.70 22.39           N  
ANISOU 1333  N  AILE A6951     3123   2484   2900    245   -320   -381       N  
ATOM   1334  N  BILE A6951      96.542  13.821  26.818  0.30 21.95           N  
ANISOU 1334  N  BILE A6951     3069   2426   2845    245   -323   -379       N  
ATOM   1335  CA AILE A6951      96.608  15.003  25.858  0.70 22.82           C  
ANISOU 1335  CA AILE A6951     3145   2623   2900    259   -178   -390       C  
ATOM   1336  CA BILE A6951      96.567  15.069  25.997  0.30 21.82           C  
ANISOU 1336  CA BILE A6951     3020   2497   2772    257   -183   -381       C  
ATOM   1337  C  AILE A6951      98.053  15.488  25.705  0.70 22.80           C  
ANISOU 1337  C  AILE A6951     3066   2584   3012    277    -97   -491       C  
ATOM   1338  C  BILE A6951      98.016  15.487  25.734  0.30 22.41           C  
ANISOU 1338  C  BILE A6951     3019   2535   2960    277   -100   -487       C  
ATOM   1339  O  AILE A6951      98.431  15.810  24.564  0.70 22.70           O  
ANISOU 1339  O  AILE A6951     3056   2589   2977    275     44   -548       O  
ATOM   1340  O  BILE A6951      98.351  15.746  24.563  0.30 22.68           O  
ANISOU 1340  O  BILE A6951     3059   2588   2970    277     34   -543       O  
ATOM   1341  CB AILE A6951      95.656  16.125  26.316  0.70 23.65           C  
ANISOU 1341  CB AILE A6951     3287   2802   2895    253   -141   -287       C  
ATOM   1342  CB BILE A6951      95.783  16.192  26.706  0.30 21.37           C  
ANISOU 1342  CB BILE A6951     2992   2497   2627    246   -156   -280       C  
ATOM   1343  CG1AILE A6951      94.193  15.734  26.094  0.70 24.42           C  
ANISOU 1343  CG1AILE A6951     3395   3006   2875    238   -189   -255       C  
ATOM   1344  CG1BILE A6951      94.274  15.937  26.672  0.30 21.36           C  
ANISOU 1344  CG1BILE A6951     3009   2597   2507    228   -198   -229       C  
ATOM   1345  CG2AILE A6951      95.987  17.439  25.619  0.70 24.73           C  
ANISOU 1345  CG2AILE A6951     3470   2945   2979    291     17   -278       C  
ATOM   1346  CG2BILE A6951      96.131  17.550  26.116  0.30 21.75           C  
ANISOU 1346  CG2BILE A6951     3077   2549   2635    275      1   -274       C  
ATOM   1347  CD1AILE A6951      93.794  15.589  24.631  0.70 25.87           C  
ANISOU 1347  CD1AILE A6951     3585   3283   2961    290   -156   -308       C  
ATOM   1348  CD1BILE A6951      93.455  17.002  27.367  0.30 20.93           C  
ANISOU 1348  CD1BILE A6951     2964   2617   2370    249   -173   -157       C  
ATOM   1349  N   CYS A6952      98.827  15.552  26.793  1.00 22.99           N  
ANISOU 1349  N   CYS A6952     3019   2577   3138    289   -173   -533       N  
ATOM   1350  CA  CYS A6952     100.240  16.002  26.670  1.00 24.40           C  
ANISOU 1350  CA  CYS A6952     3054   2767   3447    283    -93   -699       C  
ATOM   1351  C   CYS A6952     101.008  15.060  25.736  1.00 24.79           C  
ANISOU 1351  C   CYS A6952     3026   2809   3582    336    -81   -839       C  
ATOM   1352  O   CYS A6952     101.734  15.557  24.853  1.00 25.10           O  
ANISOU 1352  O   CYS A6952     2992   2880   3663    281    107   -959       O  
ATOM   1353  CB  CYS A6952     100.913  16.105  28.032  1.00 25.83           C  
ANISOU 1353  CB  CYS A6952     3140   2964   3711    318   -231   -764       C  
ATOM   1354  SG  CYS A6952     100.287  17.489  29.020  1.00 26.93           S  
ANISOU 1354  SG  CYS A6952     3345   3119   3766    231   -183   -665       S  
ATOM   1355  N   GLY A6953     100.822  13.750  25.899  1.00 24.65           N  
ANISOU 1355  N   GLY A6953     3053   2732   3579    429   -245   -828       N  
ATOM   1356  CA  GLY A6953     101.536  12.791  25.037  1.00 25.78           C  
ANISOU 1356  CA  GLY A6953     3136   2852   3807    506   -240   -977       C  
ATOM   1357  C   GLY A6953     101.023  12.849  23.608  1.00 25.69           C  
ANISOU 1357  C   GLY A6953     3194   2866   3698    435    -75   -970       C  
ATOM   1358  O   GLY A6953     101.837  12.711  22.677  1.00 27.09           O  
ANISOU 1358  O   GLY A6953     3287   3073   3932    447     43  -1125       O  
ATOM   1359  N   PHE A6954      99.716  13.069  23.446  1.00 24.89           N  
ANISOU 1359  N   PHE A6954     3230   2781   3444    376    -71   -817       N  
ATOM   1360  CA  PHE A6954      99.094  13.102  22.097  1.00 25.03           C  
ANISOU 1360  CA  PHE A6954     3327   2859   3322    350     36   -816       C  
ATOM   1361  C   PHE A6954      99.622  14.316  21.326  1.00 26.04           C  
ANISOU 1361  C   PHE A6954     3467   3037   3389    318    258   -835       C  
ATOM   1362  O   PHE A6954      99.924  14.179  20.127  1.00 27.38           O  
ANISOU 1362  O   PHE A6954     3671   3235   3497    321    387   -918       O  
ATOM   1363  CB  PHE A6954      97.568  13.079  22.209  1.00 24.75           C  
ANISOU 1363  CB  PHE A6954     3386   2877   3141    319    -42   -692       C  
ATOM   1364  CG  PHE A6954      96.861  12.849  20.897  1.00 24.84           C  
ANISOU 1364  CG  PHE A6954     3455   2984   2996    328     -4   -733       C  
ATOM   1365  CD1 PHE A6954      96.525  13.913  20.077  1.00 25.85           C  
ANISOU 1365  CD1 PHE A6954     3661   3215   2946    375    103   -681       C  
ATOM   1366  CD2 PHE A6954      96.549  11.569  20.475  1.00 26.05           C  
ANISOU 1366  CD2 PHE A6954     3615   3116   3165    302    -79   -835       C  
ATOM   1367  CE1 PHE A6954      95.889  13.703  18.864  1.00 26.66           C  
ANISOU 1367  CE1 PHE A6954     3828   3434   2865    424    106   -730       C  
ATOM   1368  CE2 PHE A6954      95.907  11.360  19.263  1.00 27.25           C  
ANISOU 1368  CE2 PHE A6954     3802   3388   3160    310    -62   -911       C  
ATOM   1369  CZ  PHE A6954      95.578  12.427  18.461  1.00 27.05           C  
ANISOU 1369  CZ  PHE A6954     3836   3503   2937    385     14   -860       C  
ATOM   1370  N   ILE A6955      99.752  15.463  21.999  1.00 26.24           N  
ANISOU 1370  N   ILE A6955     3493   3054   3422    275    324   -768       N  
ATOM   1371  CA  ILE A6955     100.297  16.682  21.334  1.00 28.66           C  
ANISOU 1371  CA  ILE A6955     3869   3349   3671    208    587   -785       C  
ATOM   1372  C   ILE A6955     101.740  16.408  20.888  1.00 30.83           C  
ANISOU 1372  C   ILE A6955     3990   3625   4099    150    730  -1004       C  
ATOM   1373  O   ILE A6955     102.058  16.660  19.710  1.00 32.93           O  
ANISOU 1373  O   ILE A6955     4344   3894   4273    107    952  -1055       O  
ATOM   1374  CB  ILE A6955     100.207  17.899  22.276  1.00 28.22           C  
ANISOU 1374  CB  ILE A6955     3847   3249   3623    154    635   -703       C  
ATOM   1375  CG1 ILE A6955      98.752  18.318  22.506  1.00 27.39           C  
ANISOU 1375  CG1 ILE A6955     3897   3165   3344    234    540   -510       C  
ATOM   1376  CG2 ILE A6955     101.047  19.053  21.745  1.00 30.81           C  
ANISOU 1376  CG2 ILE A6955     4248   3510   3946     32    945   -768       C  
ATOM   1377  CD1 ILE A6955      98.558  19.355  23.592  1.00 27.34           C  
ANISOU 1377  CD1 ILE A6955     3920   3113   3356    203    550   -439       C  
ATOM   1378  N   GLN A6956     102.561  15.867  21.789  1.00 31.45           N  
ANISOU 1378  N   GLN A6956     3846   3717   4384    170    600  -1142       N  
ATOM   1379  CA  GLN A6956     104.006  15.653  21.512  1.00 34.40           C  
ANISOU 1379  CA  GLN A6956     3994   4140   4934    138    715  -1409       C  
ATOM   1380  C   GLN A6956     104.224  14.566  20.449  1.00 34.74           C  
ANISOU 1380  C   GLN A6956     4025   4201   4973    215    730  -1517       C  
ATOM   1381  O   GLN A6956     105.222  14.666  19.717  1.00 36.64           O  
ANISOU 1381  O   GLN A6956     4144   4495   5283    150    946  -1723       O  
ATOM   1382  CB  GLN A6956     104.731  15.321  22.816  1.00 36.97           C  
ANISOU 1382  CB  GLN A6956     4084   4509   5452    212    504  -1539       C  
ATOM   1383  CG  GLN A6956     104.875  16.523  23.738  1.00 39.92           C  
ANISOU 1383  CG  GLN A6956     4416   4896   5855     95    554  -1532       C  
ATOM   1384  CD  GLN A6956     105.545  16.171  25.042  1.00 43.69           C  
ANISOU 1384  CD  GLN A6956     4670   5449   6479    202    305  -1670       C  
ATOM   1385  OE1 GLN A6956     105.003  15.431  25.861  1.00 47.59           O  
ANISOU 1385  OE1 GLN A6956     5243   5906   6933    359     32  -1542       O  
ATOM   1386  NE2 GLN A6956     106.715  16.742  25.263  1.00 47.52           N  
ANISOU 1386  NE2 GLN A6956     4890   6047   7118    110    409  -1945       N  
ATOM   1387  N   GLN A6957     103.325  13.587  20.348  1.00 31.85           N  
ANISOU 1387  N   GLN A6957     3947   3659   4493    375    301   -974       N  
ATOM   1388  CA  GLN A6957     103.516  12.465  19.387  1.00 33.50           C  
ANISOU 1388  CA  GLN A6957     4188   3818   4719    406    366  -1037       C  
ATOM   1389  C   GLN A6957     102.662  12.615  18.121  1.00 31.21           C  
ANISOU 1389  C   GLN A6957     4000   3534   4325    303    463  -1025       C  
ATOM   1390  O   GLN A6957     103.119  12.133  17.069  1.00 30.76           O  
ANISOU 1390  O   GLN A6957     3937   3468   4280    302    558  -1106       O  
ATOM   1391  CB  GLN A6957     103.146  11.145  20.067  1.00 35.81           C  
ANISOU 1391  CB  GLN A6957     4557   4022   5024    494    269  -1004       C  
ATOM   1392  CG  GLN A6957     103.956  10.856  21.321  1.00 39.46           C  
ANISOU 1392  CG  GLN A6957     4940   4470   5581    605    156  -1008       C  
ATOM   1393  CD  GLN A6957     103.372   9.719  22.124  1.00 43.45           C  
ANISOU 1393  CD  GLN A6957     5550   4886   6071    673     50   -943       C  
ATOM   1394  OE1 GLN A6957     102.757   8.801  21.583  1.00 47.84           O  
ANISOU 1394  OE1 GLN A6957     6209   5372   6594    667     74   -936       O  
ATOM   1395  NE2 GLN A6957     103.563   9.773  23.434  1.00 45.88           N  
ANISOU 1395  NE2 GLN A6957     5839   5194   6400    732    -68   -894       N  
ATOM   1396  N   LYS A6958     101.498  13.270  18.195  1.00 28.72           N  
ANISOU 1396  N   LYS A6958     3769   3234   3910    222    440   -935       N  
ATOM   1397  CA  LYS A6958     100.566  13.241  17.032  1.00 29.07           C  
ANISOU 1397  CA  LYS A6958     3921   3274   3850    134    506   -917       C  
ATOM   1398  C   LYS A6958     100.162  14.630  16.525  1.00 27.75           C  
ANISOU 1398  C   LYS A6958     3760   3169   3612     29    554   -876       C  
ATOM   1399  O   LYS A6958      99.306  14.675  15.618  1.00 28.67           O  
ANISOU 1399  O   LYS A6958     3972   3285   3635    -43    590   -848       O  
ATOM   1400  CB  LYS A6958      99.328  12.423  17.415  1.00 29.34           C  
ANISOU 1400  CB  LYS A6958     4072   3246   3827    137    427   -846       C  
ATOM   1401  CG  LYS A6958      99.625  10.980  17.796  1.00 31.69           C  
ANISOU 1401  CG  LYS A6958     4391   3464   4186    232    382   -879       C  
ATOM   1402  CD  LYS A6958     100.239  10.199  16.660  1.00 34.43           C  
ANISOU 1402  CD  LYS A6958     4742   3783   4556    250    471   -981       C  
ATOM   1403  CE  LYS A6958     100.614   8.778  17.016  1.00 37.65           C  
ANISOU 1403  CE  LYS A6958     5167   4098   5039    354    427  -1021       C  
ATOM   1404  NZ  LYS A6958     101.073   8.048  15.813  1.00 39.23           N  
ANISOU 1404  NZ  LYS A6958     5383   4269   5251    362    524  -1127       N  
ATOM   1405  N   LEU A6959     100.723  15.716  17.059  1.00 26.22           N  
ANISOU 1405  N   LEU A6959     3476   3023   3461     19    551   -871       N  
ATOM   1406  CA  LEU A6959     100.367  17.043  16.490  1.00 25.23           C  
ANISOU 1406  CA  LEU A6959     3366   2943   3274    -81    602   -831       C  
ATOM   1407  C   LEU A6959     101.408  17.420  15.429  1.00 25.41           C  
ANISOU 1407  C   LEU A6959     3332   3005   3318   -123    730   -910       C  
ATOM   1408  O   LEU A6959     102.612  17.370  15.728  1.00 26.32           O  
ANISOU 1408  O   LEU A6959     3329   3137   3534    -76    754   -983       O  
ATOM   1409  CB  LEU A6959     100.310  18.097  17.598  1.00 24.53           C  
ANISOU 1409  CB  LEU A6959     3226   2879   3214    -83    536   -782       C  
ATOM   1410  CG  LEU A6959      99.914  19.501  17.147  1.00 24.51           C  
ANISOU 1410  CG  LEU A6959     3243   2909   3161   -179    576   -736       C  
ATOM   1411  CD1 LEU A6959      98.506  19.517  16.571  1.00 24.22           C  
ANISOU 1411  CD1 LEU A6959     3330   2855   3017   -232    562   -661       C  
ATOM   1412  CD2 LEU A6959     100.022  20.478  18.305  1.00 24.31           C  
ANISOU 1412  CD2 LEU A6959     3156   2900   3179   -171    513   -708       C  
ATOM   1413  N   ALA A6960     100.949  17.777  14.232  1.00 25.02           N  
ANISOU 1413  N   ALA A6960     3363   2969   3173   -211    807   -894       N  
ATOM   1414  CA  ALA A6960     101.867  18.199  13.150  1.00 26.32           C  
ANISOU 1414  CA  ALA A6960     3489   3172   3336   -268    943   -961       C  
ATOM   1415  C   ALA A6960     102.570  19.496  13.552  1.00 26.58           C  
ANISOU 1415  C   ALA A6960     3423   3245   3428   -306    966   -956       C  
ATOM   1416  O   ALA A6960     101.931  20.324  14.239  1.00 25.66           O  
ANISOU 1416  O   ALA A6960     3323   3126   3298   -326    890   -878       O  
ATOM   1417  CB  ALA A6960     101.089  18.406  11.880  1.00 26.34           C  
ANISOU 1417  CB  ALA A6960     3620   3180   3204   -360   1001   -926       C  
ATOM   1418  N   LEU A6961     103.840  19.654  13.172  1.00 27.66           N  
ANISOU 1418  N   LEU A6961     3455   3416   3636   -315   1068  -1044       N  
ATOM   1419  CA  LEU A6961     104.487  20.969  13.408  1.00 28.39           C  
ANISOU 1419  CA  LEU A6961     3461   3545   3780   -375   1103  -1040       C  
ATOM   1420  C   LEU A6961     103.659  21.990  12.625  1.00 27.29           C  
ANISOU 1420  C   LEU A6961     3438   3407   3521   -487   1141   -954       C  
ATOM   1421  O   LEU A6961     103.252  21.672  11.485  1.00 27.66           O  
ANISOU 1421  O   LEU A6961     3589   3453   3465   -535   1208   -948       O  
ATOM   1422  CB  LEU A6961     105.947  20.949  12.950  1.00 30.47           C  
ANISOU 1422  CB  LEU A6961     3593   3848   4133   -383   1226  -1151       C  
ATOM   1423  CG  LEU A6961     106.831  19.876  13.583  1.00 32.30           C  
ANISOU 1423  CG  LEU A6961     3703   4077   4492   -262   1193  -1245       C  
ATOM   1424  CD1 LEU A6961     108.255  19.985  13.062  1.00 34.86           C  
ANISOU 1424  CD1 LEU A6961     3882   4447   4912   -279   1326  -1359       C  
ATOM   1425  CD2 LEU A6961     106.818  19.967  15.100  1.00 31.99           C  
ANISOU 1425  CD2 LEU A6961     3597   4024   4532   -184   1040  -1216       C  
ATOM   1426  N   GLY A6962     103.406  23.154  13.220  1.00 26.63           N  
ANISOU 1426  N   GLY A6962     3343   3321   3451   -526   1092   -891       N  
ATOM   1427  CA  GLY A6962     102.547  24.181  12.605  1.00 26.37           C  
ANISOU 1427  CA  GLY A6962     3423   3277   3317   -620   1105   -798       C  
ATOM   1428  C   GLY A6962     101.107  24.036  13.062  1.00 25.26           C  
ANISOU 1428  C   GLY A6962     3382   3103   3112   -588    982   -709       C  
ATOM   1429  O   GLY A6962     100.333  24.993  12.875  1.00 25.58           O  
ANISOU 1429  O   GLY A6962     3495   3127   3095   -645    960   -626       O  
ATOM   1430  N   GLY A6963     100.763  22.880  13.644  1.00 24.66           N  
ANISOU 1430  N   GLY A6963     3305   3011   3050   -500    907   -725       N  
ATOM   1431  CA  GLY A6963      99.397  22.609  14.128  1.00 23.58           C  
ANISOU 1431  CA  GLY A6963     3252   2845   2860   -471    798   -648       C  
ATOM   1432  C   GLY A6963      99.060  23.415  15.372  1.00 22.60           C  
ANISOU 1432  C   GLY A6963     3090   2713   2784   -449    709   -602       C  
ATOM   1433  O   GLY A6963      99.974  24.025  15.967  1.00 22.97           O  
ANISOU 1433  O   GLY A6963     3038   2774   2912   -445    720   -640       O  
ATOM   1434  N   SER A6964      97.785  23.407  15.764  1.00 21.56           N  
ANISOU 1434  N   SER A6964     3028   2560   2604   -437    626   -529       N  
ATOM   1435  CA  SER A6964      97.331  24.200  16.933  1.00 20.84           C  
ANISOU 1435  CA  SER A6964     2911   2461   2546   -417    548   -486       C  
ATOM   1436  C   SER A6964      96.428  23.358  17.834  1.00 20.02           C  
ANISOU 1436  C   SER A6964     2834   2341   2431   -353    456   -457       C  
ATOM   1437  O   SER A6964      95.965  22.278  17.399  1.00 19.80           O  
ANISOU 1437  O   SER A6964     2860   2301   2360   -338    450   -455       O  
ATOM   1438  CB  SER A6964      96.646  25.469  16.485  1.00 20.90           C  
ANISOU 1438  CB  SER A6964     2972   2457   2512   -485    555   -419       C  
ATOM   1439  OG  SER A6964      97.570  26.342  15.838  1.00 21.73           O  
ANISOU 1439  OG  SER A6964     3048   2570   2636   -549    640   -442       O  
ATOM   1440  N   VAL A6965      96.225  23.828  19.062  1.00 19.16           N  
ANISOU 1440  N   VAL A6965     2690   2230   2357   -321    391   -441       N  
ATOM   1441  CA  VAL A6965      95.354  23.108  20.029  1.00 18.81           C  
ANISOU 1441  CA  VAL A6965     2674   2174   2297   -267    311   -408       C  
ATOM   1442  C   VAL A6965      94.494  24.119  20.788  1.00 17.96           C  
ANISOU 1442  C   VAL A6965     2575   2064   2182   -277    267   -358       C  
ATOM   1443  O   VAL A6965      94.886  25.295  20.904  1.00 18.25           O  
ANISOU 1443  O   VAL A6965     2577   2105   2251   -304    283   -366       O  
ATOM   1444  CB  VAL A6965      96.174  22.265  21.029  1.00 19.26           C  
ANISOU 1444  CB  VAL A6965     2676   2235   2408   -193    272   -457       C  
ATOM   1445  CG1 VAL A6965      97.152  21.336  20.328  1.00 20.31           C  
ANISOU 1445  CG1 VAL A6965     2782   2365   2569   -172    319   -519       C  
ATOM   1446  CG2 VAL A6965      96.903  23.132  22.046  1.00 20.01           C  
ANISOU 1446  CG2 VAL A6965     2693   2348   2560   -176    243   -485       C  
ATOM   1447  N   ALA A6966      93.345  23.650  21.254  1.00 17.06           N  
ANISOU 1447  N   ALA A6966     2508   1941   2032   -258    218   -312       N  
ATOM   1448  CA  ALA A6966      92.467  24.406  22.175  1.00 16.67           C  
ANISOU 1448  CA  ALA A6966     2460   1892   1979   -252    175   -274       C  
ATOM   1449  C   ALA A6966      91.987  23.369  23.192  1.00 16.90           C  
ANISOU 1449  C   ALA A6966     2507   1921   1993   -204    125   -263       C  
ATOM   1450  O   ALA A6966      91.206  22.469  22.801  1.00 17.15           O  
ANISOU 1450  O   ALA A6966     2587   1941   1988   -210    119   -233       O  
ATOM   1451  CB  ALA A6966      91.349  25.089  21.429  1.00 16.45           C  
ANISOU 1451  CB  ALA A6966     2477   1854   1919   -297    181   -219       C  
ATOM   1452  N   ILE A6967      92.504  23.453  24.422  1.00 17.36           N  
ANISOU 1452  N   ILE A6967     2529   1990   2075   -162     91   -288       N  
ATOM   1453  CA  ILE A6967      92.251  22.445  25.488  1.00 17.50           C  
ANISOU 1453  CA  ILE A6967     2570   2006   2072   -115     43   -276       C  
ATOM   1454  C   ILE A6967      91.501  23.116  26.635  1.00 17.36           C  
ANISOU 1454  C   ILE A6967     2558   2002   2034   -109     16   -255       C  
ATOM   1455  O   ILE A6967      92.054  24.059  27.233  1.00 16.70           O  
ANISOU 1455  O   ILE A6967     2434   1934   1976   -102      6   -287       O  
ATOM   1456  CB  ILE A6967      93.577  21.824  25.976  1.00 18.35           C  
ANISOU 1456  CB  ILE A6967     2640   2116   2216    -63     16   -326       C  
ATOM   1457  CG1 ILE A6967      94.460  21.346  24.820  1.00 19.02           C  
ANISOU 1457  CG1 ILE A6967     2701   2190   2334    -66     58   -366       C  
ATOM   1458  CG2 ILE A6967      93.303  20.713  26.980  1.00 18.44           C  
ANISOU 1458  CG2 ILE A6967     2693   2114   2197    -15    -37   -301       C  
ATOM   1459  CD1 ILE A6967      93.840  20.256  23.970  1.00 19.09           C  
ANISOU 1459  CD1 ILE A6967     2772   2171   2310    -77     78   -341       C  
ATOM   1460  N   LYS A6968      90.315  22.608  26.949  1.00 17.16           N  
ANISOU 1460  N   LYS A6968     2578   1972   1968   -114      7   -208       N  
ATOM   1461  CA  LYS A6968      89.505  23.226  28.022  1.00 17.49           C  
ANISOU 1461  CA  LYS A6968     2625   2031   1987   -111     -3   -192       C  
ATOM   1462  C   LYS A6968      90.105  22.909  29.392  1.00 17.84           C  
ANISOU 1462  C   LYS A6968     2674   2090   2012    -67    -44   -212       C  
ATOM   1463  O   LYS A6968      90.461  21.738  29.657  1.00 17.10           O  
ANISOU 1463  O   LYS A6968     2609   1983   1901    -40    -72   -202       O  
ATOM   1464  CB  LYS A6968      88.047  22.775  27.932  1.00 18.53           C  
ANISOU 1464  CB  LYS A6968     2792   2159   2086   -136      8   -139       C  
ATOM   1465  CG  LYS A6968      87.098  23.606  28.781  1.00 19.73           C  
ANISOU 1465  CG  LYS A6968     2936   2332   2227   -139     16   -130       C  
ATOM   1466  CD  LYS A6968      86.830  23.057  30.156  1.00 21.82           C  
ANISOU 1466  CD  LYS A6968     3231   2613   2445   -119      4   -121       C  
ATOM   1467  CE  LYS A6968      85.735  22.013  30.154  1.00 22.51           C  
ANISOU 1467  CE  LYS A6968     3355   2694   2501   -143     16    -71       C  
ATOM   1468  NZ  LYS A6968      84.443  22.577  29.678  1.00 22.95           N  
ANISOU 1468  NZ  LYS A6968     3384   2758   2576   -177     46    -51       N  
ATOM   1469  N   ILE A6969      90.214  23.953  30.211  1.00 17.39           N  
ANISOU 1469  N   ILE A6969     2594   2053   1957    -61    -53   -239       N  
ATOM   1470  CA  ILE A6969      90.681  23.854  31.621  1.00 17.60           C  
ANISOU 1470  CA  ILE A6969     2633   2102   1950    -25    -99   -261       C  
ATOM   1471  C   ILE A6969      89.697  24.634  32.491  1.00 17.17           C  
ANISOU 1471  C   ILE A6969     2596   2067   1860    -36    -81   -257       C  
ATOM   1472  O   ILE A6969      88.854  25.359  31.940  1.00 16.38           O  
ANISOU 1472  O   ILE A6969     2481   1960   1781    -64    -39   -247       O  
ATOM   1473  CB  ILE A6969      92.112  24.397  31.803  1.00 18.39           C  
ANISOU 1473  CB  ILE A6969     2680   2212   2094     -4   -133   -324       C  
ATOM   1474  CG1 ILE A6969      92.198  25.891  31.474  1.00 19.26           C  
ANISOU 1474  CG1 ILE A6969     2745   2323   2250    -37   -103   -361       C  
ATOM   1475  CG2 ILE A6969      93.109  23.572  31.005  1.00 18.70           C  
ANISOU 1475  CG2 ILE A6969     2692   2235   2176     13   -143   -336       C  
ATOM   1476  CD1 ILE A6969      93.446  26.556  31.984  1.00 21.12           C  
ANISOU 1476  CD1 ILE A6969     2928   2573   2523    -26   -140   -428       C  
ATOM   1477  N   THR A6970      89.813  24.463  33.807  1.00 17.64           N  
ANISOU 1477  N   THR A6970     2689   2150   1864    -11   -114   -267       N  
ATOM   1478  CA  THR A6970      89.020  25.227  34.799  1.00 17.62           C  
ANISOU 1478  CA  THR A6970     2704   2172   1818    -18    -93   -280       C  
ATOM   1479  C   THR A6970      89.950  25.503  35.979  1.00 18.15           C  
ANISOU 1479  C   THR A6970     2782   2265   1848     10   -150   -329       C  
ATOM   1480  O   THR A6970      91.134  25.104  35.914  1.00 17.86           O  
ANISOU 1480  O   THR A6970     2726   2225   1832     35   -207   -348       O  
ATOM   1481  CB  THR A6970      87.771  24.469  35.272  1.00 18.19           C  
ANISOU 1481  CB  THR A6970     2831   2253   1827    -31    -60   -226       C  
ATOM   1482  OG1 THR A6970      88.199  23.316  36.000  1.00 18.25           O  
ANISOU 1482  OG1 THR A6970     2898   2264   1772    -10   -104   -198       O  
ATOM   1483  CG2 THR A6970      86.848  24.063  34.143  1.00 18.31           C  
ANISOU 1483  CG2 THR A6970     2833   2246   1876    -62    -17   -179       C  
ATOM   1484  N   GLU A6971      89.434  26.128  37.029  1.00 18.91           N  
ANISOU 1484  N   GLU A6971     2905   2387   1891      8   -137   -354       N  
ATOM   1485  CA  GLU A6971      90.269  26.347  38.231  1.00 19.65           C  
ANISOU 1485  CA  GLU A6971     3021   2510   1932     32   -200   -402       C  
ATOM   1486  C   GLU A6971      90.856  25.010  38.704  1.00 19.93           C  
ANISOU 1486  C   GLU A6971     3108   2552   1913     63   -267   -362       C  
ATOM   1487  O   GLU A6971      92.067  24.963  38.999  1.00 21.05           O  
ANISOU 1487  O   GLU A6971     3229   2700   2065     93   -346   -397       O  
ATOM   1488  CB  GLU A6971      89.418  26.947  39.344  1.00 20.34           C  
ANISOU 1488  CB  GLU A6971     3154   2628   1945     23   -165   -426       C  
ATOM   1489  CG  GLU A6971      90.121  26.984  40.685  1.00 21.66           C  
ANISOU 1489  CG  GLU A6971     3370   2831   2026     43   -233   -467       C  
ATOM   1490  CD  GLU A6971      89.248  27.481  41.820  1.00 22.73           C  
ANISOU 1490  CD  GLU A6971     3564   3002   2071     32   -187   -493       C  
ATOM   1491  OE1 GLU A6971      88.011  27.552  41.628  1.00 23.18           O  
ANISOU 1491  OE1 GLU A6971     3623   3055   2127     11    -99   -467       O  
ATOM   1492  OE2 GLU A6971      89.803  27.800  42.887  1.00 23.66           O  
ANISOU 1492  OE2 GLU A6971     3720   3150   2117     43   -239   -544       O  
ATOM   1493  N   HIS A6972      90.027  23.960  38.744  1.00 19.90           N  
ANISOU 1493  N   HIS A6972     3163   2539   1858     56   -239   -290       N  
ATOM   1494  CA  HIS A6972      90.447  22.648  39.307  1.00 20.28           C  
ANISOU 1494  CA  HIS A6972     3280   2579   1844     87   -302   -241       C  
ATOM   1495  C   HIS A6972      90.823  21.637  38.220  1.00 20.00           C  
ANISOU 1495  C   HIS A6972     3225   2498   1875    101   -315   -203       C  
ATOM   1496  O   HIS A6972      91.541  20.681  38.557  1.00 20.31           O  
ANISOU 1496  O   HIS A6972     3301   2520   1894    141   -386   -179       O  
ATOM   1497  CB  HIS A6972      89.354  22.092  40.222  1.00 21.51           C  
ANISOU 1497  CB  HIS A6972     3530   2749   1890     64   -263   -186       C  
ATOM   1498  CG  HIS A6972      89.138  22.925  41.440  1.00 22.42           C  
ANISOU 1498  CG  HIS A6972     3681   2914   1923     58   -256   -229       C  
ATOM   1499  ND1 HIS A6972      89.834  22.706  42.612  1.00 25.26           N  
ANISOU 1499  ND1 HIS A6972     4108   3299   2190     86   -336   -237       N  
ATOM   1500  CD2 HIS A6972      88.324  23.976  41.670  1.00 22.51           C  
ANISOU 1500  CD2 HIS A6972     3672   2951   1927     29   -183   -271       C  
ATOM   1501  CE1 HIS A6972      89.463  23.597  43.513  1.00 24.87           C  
ANISOU 1501  CE1 HIS A6972     4083   3293   2072     70   -308   -286       C  
ATOM   1502  NE2 HIS A6972      88.528  24.381  42.961  1.00 24.19           N  
ANISOU 1502  NE2 HIS A6972     3943   3206   2042     37   -209   -310       N  
ATOM   1503  N   SER A6973      90.366  21.833  36.984  1.00 19.04           N  
ANISOU 1503  N   SER A6973     3052   2354   1826     71   -254   -199       N  
ATOM   1504  CA  SER A6973      90.701  20.866  35.907  1.00 18.82           C  
ANISOU 1504  CA  SER A6973     3013   2284   1855     81   -259   -172       C  
ATOM   1505  C   SER A6973      91.842  21.460  35.078  1.00 18.55           C  
ANISOU 1505  C   SER A6973     2890   2246   1909     96   -276   -233       C  
ATOM   1506  O   SER A6973      91.567  22.198  34.121  1.00 17.97           O  
ANISOU 1506  O   SER A6973     2768   2170   1888     62   -222   -250       O  
ATOM   1507  CB  SER A6973      89.494  20.537  35.067  1.00 18.62           C  
ANISOU 1507  CB  SER A6973     2998   2236   1838     34   -188   -128       C  
ATOM   1508  OG  SER A6973      89.789  19.494  34.146  1.00 18.19           O  
ANISOU 1508  OG  SER A6973     2949   2138   1823     42   -196   -105       O  
ATOM   1509  N   TRP A6974      93.078  21.150  35.464  1.00 18.91           N  
ANISOU 1509  N   TRP A6974     2918   2294   1972    145   -351   -262       N  
ATOM   1510  CA  TRP A6974      94.272  21.724  34.801  1.00 18.91           C  
ANISOU 1510  CA  TRP A6974     2822   2299   2062    157   -365   -328       C  
ATOM   1511  C   TRP A6974      95.463  20.799  35.019  1.00 19.66           C  
ANISOU 1511  C   TRP A6974     2901   2382   2185    222   -446   -341       C  
ATOM   1512  O   TRP A6974      95.387  19.919  35.912  1.00 20.03           O  
ANISOU 1512  O   TRP A6974     3021   2419   2168    260   -505   -299       O  
ATOM   1513  CB  TRP A6974      94.566  23.124  35.347  1.00 19.09           C  
ANISOU 1513  CB  TRP A6974     2801   2359   2091    139   -373   -387       C  
ATOM   1514  CG  TRP A6974      95.022  23.100  36.772  1.00 19.94           C  
ANISOU 1514  CG  TRP A6974     2941   2497   2137    175   -458   -404       C  
ATOM   1515  CD1 TRP A6974      94.237  22.961  37.879  1.00 20.61           C  
ANISOU 1515  CD1 TRP A6974     3113   2599   2117    174   -469   -371       C  
ATOM   1516  CD2 TRP A6974      96.375  23.194  37.249  1.00 20.75           C  
ANISOU 1516  CD2 TRP A6974     2990   2619   2274    215   -548   -460       C  
ATOM   1517  NE1 TRP A6974      95.005  22.973  39.011  1.00 21.15           N  
ANISOU 1517  NE1 TRP A6974     3199   2696   2140    210   -562   -399       N  
ATOM   1518  CE2 TRP A6974      96.321  23.119  38.657  1.00 21.52           C  
ANISOU 1518  CE2 TRP A6974     3155   2745   2274    238   -620   -455       C  
ATOM   1519  CE3 TRP A6974      97.620  23.352  36.631  1.00 21.05           C  
ANISOU 1519  CE3 TRP A6974     2925   2658   2415    231   -574   -518       C  
ATOM   1520  CZ2 TRP A6974      97.466  23.183  39.449  1.00 22.49           C  
ANISOU 1520  CZ2 TRP A6974     3248   2896   2399    279   -730   -503       C  
ATOM   1521  CZ3 TRP A6974      98.750  23.423  37.414  1.00 22.01           C  
ANISOU 1521  CZ3 TRP A6974     3003   2808   2552    271   -676   -569       C  
ATOM   1522  CH2 TRP A6974      98.672  23.343  38.805  1.00 23.11           C  
ANISOU 1522  CH2 TRP A6974     3213   2975   2593    296   -760   -561       C  
ATOM   1523  N   ASN A6975      96.527  21.045  34.260  1.00 19.89           N  
ANISOU 1523  N   ASN A6975     2838   2412   2306    233   -446   -397       N  
ATOM   1524  CA  ASN A6975      97.747  20.205  34.302  1.00 20.86           C  
ANISOU 1524  CA  ASN A6975     2919   2523   2483    301   -517   -423       C  
ATOM   1525  C   ASN A6975      98.967  21.098  34.064  1.00 21.24           C  
ANISOU 1525  C   ASN A6975     2844   2603   2620    300   -531   -509       C  
ATOM   1526  O   ASN A6975      98.963  21.879  33.090  1.00 20.50           O  
ANISOU 1526  O   ASN A6975     2696   2513   2577    246   -449   -538       O  
ATOM   1527  CB  ASN A6975      97.627  19.042  33.314  1.00 21.12           C  
ANISOU 1527  CB  ASN A6975     2971   2504   2547    318   -481   -394       C  
ATOM   1528  CG  ASN A6975      98.899  18.235  33.199  1.00 22.59           C  
ANISOU 1528  CG  ASN A6975     3101   2673   2810    394   -541   -431       C  
ATOM   1529  OD1 ASN A6975      99.817  18.620  32.479  1.00 23.78           O  
ANISOU 1529  OD1 ASN A6975     3146   2837   3049    395   -516   -498       O  
ATOM   1530  ND2 ASN A6975      98.944  17.095  33.866  1.00 24.81           N  
ANISOU 1530  ND2 ASN A6975     3448   2916   3059    457   -616   -387       N  
ATOM   1531  N   ALA A6976      99.979  20.959  34.918  1.00 22.28           N  
ANISOU 1531  N   ALA A6976     2936   2756   2771    357   -633   -545       N  
ATOM   1532  CA  ALA A6976     101.194  21.804  34.839  1.00 23.48           C  
ANISOU 1532  CA  ALA A6976     2961   2944   3014    352   -658   -633       C  
ATOM   1533  C   ALA A6976     101.969  21.511  33.551  1.00 24.06           C  
ANISOU 1533  C   ALA A6976     2938   3002   3199    357   -598   -674       C  
ATOM   1534  O   ALA A6976     102.476  22.472  32.944  1.00 24.18           O  
ANISOU 1534  O   ALA A6976     2864   3039   3284    304   -542   -733       O  
ATOM   1535  CB  ALA A6976     102.047  21.580  36.063  1.00 24.32           C  
ANISOU 1535  CB  ALA A6976     3050   3078   3113    417   -796   -659       C  
ATOM   1536  N   ASP A6977     102.054  20.237  33.153  1.00 24.83           N  
ANISOU 1536  N   ASP A6977     3060   3062   3313    413   -603   -647       N  
ATOM   1537  CA  ASP A6977     102.808  19.850  31.927  1.00 26.46           C  
ANISOU 1537  CA  ASP A6977     3177   3253   3621    424   -540   -695       C  
ATOM   1538  C   ASP A6977     102.134  20.455  30.687  1.00 24.90           C  
ANISOU 1538  C   ASP A6977     2993   3049   3417    335   -404   -687       C  
ATOM   1539  O   ASP A6977     102.860  20.809  29.741  1.00 24.75           O  
ANISOU 1539  O   ASP A6977     2883   3043   3478    307   -335   -746       O  
ATOM   1540  CB  ASP A6977     102.962  18.330  31.817  1.00 29.22           C  
ANISOU 1540  CB  ASP A6977     3564   3552   3986    508   -576   -670       C  
ATOM   1541  CG  ASP A6977     103.959  17.735  32.798  1.00 33.93           C  
ANISOU 1541  CG  ASP A6977     4116   4151   4623    607   -713   -691       C  
ATOM   1542  OD1 ASP A6977     104.875  18.470  33.231  1.00 36.02           O  
ANISOU 1542  OD1 ASP A6977     4276   4466   4944    612   -765   -755       O  
ATOM   1543  OD2 ASP A6977     103.818  16.538  33.119  1.00 39.77           O  
ANISOU 1543  OD2 ASP A6977     4928   4839   5341    679   -771   -644       O  
ATOM   1544  N   LEU A6978     100.804  20.577  30.692  1.00 23.25           N  
ANISOU 1544  N   LEU A6978     2892   2824   3117    291   -369   -618       N  
ATOM   1545  CA  LEU A6978     100.092  21.174  29.533  1.00 22.37           C  
ANISOU 1545  CA  LEU A6978     2800   2706   2993    210   -257   -604       C  
ATOM   1546  C   LEU A6978     100.480  22.655  29.410  1.00 21.69           C  
ANISOU 1546  C   LEU A6978     2643   2653   2944    148   -223   -649       C  
ATOM   1547  O   LEU A6978     100.726  23.107  28.281  1.00 21.58           O  
ANISOU 1547  O   LEU A6978     2589   2638   2971     96   -136   -673       O  
ATOM   1548  CB  LEU A6978      98.582  20.994  29.710  1.00 21.82           C  
ANISOU 1548  CB  LEU A6978     2847   2615   2827    184   -244   -523       C  
ATOM   1549  CG  LEU A6978      97.730  21.561  28.578  1.00 21.98           C  
ANISOU 1549  CG  LEU A6978     2895   2627   2829    109   -149   -499       C  
ATOM   1550  CD1 LEU A6978      98.102  20.936  27.247  1.00 22.80           C  
ANISOU 1550  CD1 LEU A6978     2981   2710   2969    102    -85   -519       C  
ATOM   1551  CD2 LEU A6978      96.253  21.374  28.864  1.00 21.72           C  
ANISOU 1551  CD2 LEU A6978     2959   2579   2714     88   -146   -426       C  
ATOM   1552  N   TYR A6979     100.512  23.394  30.523  1.00 21.63           N  
ANISOU 1552  N   TYR A6979     2629   2669   2918    147   -285   -660       N  
ATOM   1553  CA  TYR A6979     100.982  24.803  30.446  1.00 22.19           C  
ANISOU 1553  CA  TYR A6979     2630   2762   3036     87   -258   -712       C  
ATOM   1554  C   TYR A6979     102.428  24.848  29.937  1.00 23.34           C  
ANISOU 1554  C   TYR A6979     2649   2927   3291     89   -245   -790       C  
ATOM   1555  O   TYR A6979     102.746  25.720  29.111  1.00 24.00           O  
ANISOU 1555  O   TYR A6979     2682   3013   3424     19   -165   -819       O  
ATOM   1556  CB  TYR A6979     100.916  25.492  31.804  1.00 22.02           C  
ANISOU 1556  CB  TYR A6979     2621   2763   2980     92   -337   -728       C  
ATOM   1557  CG  TYR A6979      99.581  26.066  32.193  1.00 21.30           C  
ANISOU 1557  CG  TYR A6979     2626   2661   2806     60   -317   -678       C  
ATOM   1558  CD1 TYR A6979      99.155  27.273  31.665  1.00 21.15           C  
ANISOU 1558  CD1 TYR A6979     2605   2627   2802     -8   -248   -682       C  
ATOM   1559  CD2 TYR A6979      98.786  25.459  33.152  1.00 21.08           C  
ANISOU 1559  CD2 TYR A6979     2686   2635   2688     99   -367   -631       C  
ATOM   1560  CE1 TYR A6979      97.959  27.852  32.055  1.00 20.70           C  
ANISOU 1560  CE1 TYR A6979     2622   2558   2683    -28   -231   -646       C  
ATOM   1561  CE2 TYR A6979      97.582  26.019  33.546  1.00 20.89           C  
ANISOU 1561  CE2 TYR A6979     2735   2606   2595     71   -340   -596       C  
ATOM   1562  CZ  TYR A6979      97.173  27.227  33.005  1.00 20.17           C  
ANISOU 1562  CZ  TYR A6979     2630   2500   2530     11   -274   -607       C  
ATOM   1563  OH  TYR A6979      96.003  27.809  33.391  1.00 20.46           O  
ANISOU 1563  OH  TYR A6979     2728   2531   2514     -8   -247   -580       O  
ATOM   1564  N   LYS A6980     103.284  23.956  30.445  1.00 24.93           N  
ANISOU 1564  N   LYS A6980     2799   3141   3532    167   -324   -821       N  
ATOM   1565  CA  LYS A6980     104.701  23.901  30.000  1.00 26.59           C  
ANISOU 1565  CA  LYS A6980     2868   3373   3860    179   -314   -904       C  
ATOM   1566  C   LYS A6980     104.748  23.684  28.479  1.00 25.94           C  
ANISOU 1566  C   LYS A6980     2770   3274   3810    140   -185   -908       C  
ATOM   1567  O   LYS A6980     105.563  24.348  27.800  1.00 25.83           O  
ANISOU 1567  O   LYS A6980     2658   3280   3875     86   -114   -968       O  
ATOM   1568  CB  LYS A6980     105.431  22.800  30.775  1.00 29.76           C  
ANISOU 1568  CB  LYS A6980     3231   3781   4293    287   -429   -923       C  
ATOM   1569  CG  LYS A6980     106.914  22.650  30.472  1.00 33.83           C  
ANISOU 1569  CG  LYS A6980     3586   4323   4942    318   -437  -1015       C  
ATOM   1570  CD  LYS A6980     107.585  21.595  31.332  1.00 37.77           C  
ANISOU 1570  CD  LYS A6980     4052   4824   5475    436   -572  -1028       C  
ATOM   1571  CE  LYS A6980     109.055  21.432  31.022  1.00 42.30           C  
ANISOU 1571  CE  LYS A6980     4447   5426   6197    475   -581  -1126       C  
ATOM   1572  NZ  LYS A6980     109.677  20.377  31.859  1.00 47.06           N  
ANISOU 1572  NZ  LYS A6980     5021   6023   6837    602   -726  -1133       N  
ATOM   1573  N  ALEU A6981     103.893  22.793  27.959  0.50 25.01           N  
ANISOU 1573  N  ALEU A6981     2751   3121   3630    160   -152   -849       N  
ATOM   1574  N  BLEU A6981     103.870  22.815  27.972  0.50 25.17           N  
ANISOU 1574  N  BLEU A6981     2773   3141   3648    159   -152   -848       N  
ATOM   1575  CA ALEU A6981     103.861  22.494  26.497  0.50 24.90           C  
ANISOU 1575  CA ALEU A6981     2741   3091   3628    123    -33   -854       C  
ATOM   1576  CA BLEU A6981     103.821  22.473  26.524  0.50 25.17           C  
ANISOU 1576  CA BLEU A6981     2779   3124   3658    125    -36   -851       C  
ATOM   1577  C  ALEU A6981     103.407  23.723  25.701  0.50 24.44           C  
ANISOU 1577  C  ALEU A6981     2705   3036   3545     16     62   -837       C  
ATOM   1578  C  BLEU A6981     103.374  23.692  25.703  0.50 24.60           C  
ANISOU 1578  C  BLEU A6981     2728   3054   3561     17     61   -835       C  
ATOM   1579  O  ALEU A6981     103.749  23.796  24.507  0.50 24.87           O  
ANISOU 1579  O  ALEU A6981     2734   3091   3623    -30    165   -861       O  
ATOM   1580  O  BLEU A6981     103.686  23.728  24.499  0.50 25.04           O  
ANISOU 1580  O  BLEU A6981     2762   3110   3639    -27    164   -857       O  
ATOM   1581  CB ALEU A6981     102.949  21.294  26.226  0.50 24.43           C  
ANISOU 1581  CB ALEU A6981     2792   2989   3499    163    -34   -794       C  
ATOM   1582  CB BLEU A6981     102.875  21.282  26.346  0.50 24.90           C  
ANISOU 1582  CB BLEU A6981     2860   3049   3553    166    -44   -788       C  
ATOM   1583  CG ALEU A6981     103.552  19.932  26.562  0.50 25.32           C  
ANISOU 1583  CG ALEU A6981     2883   3082   3655    266    -97   -817       C  
ATOM   1584  CG BLEU A6981     102.918  20.596  24.983  0.50 25.37           C  
ANISOU 1584  CG BLEU A6981     2932   3087   3620    154     52   -803       C  
ATOM   1585  CD1ALEU A6981     102.552  18.816  26.314  0.50 24.77           C  
ANISOU 1585  CD1ALEU A6981     2936   2960   3514    291    -96   -755       C  
ATOM   1586  CD1BLEU A6981     104.346  20.262  24.582  0.50 26.68           C  
ANISOU 1586  CD1BLEU A6981     2969   3271   3896    192     82   -896       C  
ATOM   1587  CD2ALEU A6981     104.824  19.693  25.762  0.50 26.60           C  
ANISOU 1587  CD2ALEU A6981     2922   3258   3924    285    -38   -907       C  
ATOM   1588  CD2BLEU A6981     102.061  19.342  24.993  0.50 25.40           C  
ANISOU 1588  CD2BLEU A6981     3043   3042   3563    201     23   -750       C  
ATOM   1589  N   MET A6982     102.672  24.650  26.322  1.00 23.81           N  
ANISOU 1589  N   MET A6982     2675   2954   3416    -21     31   -798       N  
ATOM   1590  CA  MET A6982     102.252  25.879  25.593  1.00 23.89           C  
ANISOU 1590  CA  MET A6982     2710   2955   3411   -117    113   -778       C  
ATOM   1591  C   MET A6982     103.514  26.628  25.130  1.00 24.64           C  
ANISOU 1591  C   MET A6982     2689   3073   3600   -170    171   -852       C  
ATOM   1592  O   MET A6982     103.443  27.351  24.120  1.00 24.63           O  
ANISOU 1592  O   MET A6982     2700   3059   3596   -252    267   -841       O  
ATOM   1593  CB  MET A6982     101.397  26.810  26.460  1.00 24.03           C  
ANISOU 1593  CB  MET A6982     2783   2963   3382   -137     65   -740       C  
ATOM   1594  CG  MET A6982      99.988  26.307  26.771  1.00 23.91           C  
ANISOU 1594  CG  MET A6982     2882   2928   3274   -110     35   -663       C  
ATOM   1595  SD  MET A6982      98.960  25.980  25.303  1.00 24.85           S  
ANISOU 1595  SD  MET A6982     3088   3017   3334   -152    121   -597       S  
ATOM   1596  CE  MET A6982      99.209  24.217  25.127  1.00 25.69           C  
ANISOU 1596  CE  MET A6982     3204   3122   3435    -81    103   -603       C  
ATOM   1597  N   GLY A6983     104.638  26.430  25.828  1.00 25.26           N  
ANISOU 1597  N   GLY A6983     2655   3182   3760   -126    113   -923       N  
ATOM   1598  CA  GLY A6983     105.912  27.079  25.458  1.00 26.72           C  
ANISOU 1598  CA  GLY A6983     2708   3393   4049   -178    166  -1004       C  
ATOM   1599  C   GLY A6983     106.559  26.436  24.238  1.00 27.37           C  
ANISOU 1599  C   GLY A6983     2738   3485   4173   -185    271  -1039       C  
ATOM   1600  O   GLY A6983     107.611  26.941  23.801  1.00 28.98           O  
ANISOU 1600  O   GLY A6983     2829   3714   4466   -237    337  -1107       O  
ATOM   1601  N   HIS A6984     105.953  25.367  23.705  1.00 26.97           N  
ANISOU 1601  N   HIS A6984     2769   3415   4062   -140    291  -1000       N  
ATOM   1602  CA  HIS A6984     106.459  24.632  22.511  1.00 27.60           C  
ANISOU 1602  CA  HIS A6984     2820   3500   4167   -140    395  -1038       C  
ATOM   1603  C   HIS A6984     105.709  25.105  21.262  1.00 26.86           C  
ANISOU 1603  C   HIS A6984     2827   3387   3989   -234    509   -985       C  
ATOM   1604  O   HIS A6984     105.881  24.487  20.195  1.00 27.33           O  
ANISOU 1604  O   HIS A6984     2899   3447   4035   -242    600  -1004       O  
ATOM   1605  CB  HIS A6984     106.322  23.118  22.715  1.00 28.05           C  
ANISOU 1605  CB  HIS A6984     2904   3539   4212    -31    339  -1037       C  
ATOM   1606  CG  HIS A6984     107.187  22.559  23.794  1.00 29.43           C  
ANISOU 1606  CG  HIS A6984     2976   3729   4473     66    229  -1089       C  
ATOM   1607  ND1 HIS A6984     107.959  21.427  23.602  1.00 31.44           N  
ANISOU 1607  ND1 HIS A6984     3162   3983   4800    151    227  -1148       N  
ATOM   1608  CD2 HIS A6984     107.428  22.972  25.057  1.00 30.13           C  
ANISOU 1608  CD2 HIS A6984     3022   3835   4589     96    112  -1095       C  
ATOM   1609  CE1 HIS A6984     108.620  21.155  24.709  1.00 32.18           C  
ANISOU 1609  CE1 HIS A6984     3173   4089   4962    233    105  -1180       C  
ATOM   1610  NE2 HIS A6984     108.318  22.093  25.616  1.00 31.46           N  
ANISOU 1610  NE2 HIS A6984     3098   4013   4839    197     32  -1149       N  
ATOM   1611  N   PHE A6985     104.895  26.152  21.412  1.00 25.78           N  
ANISOU 1611  N   PHE A6985     2766   3232   3798   -296    498   -921       N  
ATOM   1612  CA  PHE A6985     104.127  26.760  20.295  1.00 25.38           C  
ANISOU 1612  CA  PHE A6985     2819   3158   3666   -384    586   -859       C  
ATOM   1613  C   PHE A6985     104.691  28.154  20.021  1.00 26.12           C  
ANISOU 1613  C   PHE A6985     2864   3253   3804   -485    651   -874       C  
ATOM   1614  O   PHE A6985     105.331  28.721  20.927  1.00 27.08           O  
ANISOU 1614  O   PHE A6985     2895   3386   4004   -482    601   -919       O  
ATOM   1615  CB  PHE A6985     102.637  26.836  20.640  1.00 23.70           C  
ANISOU 1615  CB  PHE A6985     2733   2912   3360   -371    518   -767       C  
ATOM   1616  CG  PHE A6985     101.945  25.501  20.735  1.00 22.58           C  
ANISOU 1616  CG  PHE A6985     2655   2759   3163   -295    471   -741       C  
ATOM   1617  CD1 PHE A6985     102.034  24.732  21.884  1.00 22.35           C  
ANISOU 1617  CD1 PHE A6985     2598   2734   3159   -205    372   -756       C  
ATOM   1618  CD2 PHE A6985     101.204  25.011  19.672  1.00 22.46           C  
ANISOU 1618  CD2 PHE A6985     2735   2728   3069   -319    521   -699       C  
ATOM   1619  CE1 PHE A6985     101.398  23.504  21.967  1.00 21.91           C  
ANISOU 1619  CE1 PHE A6985     2608   2659   3057   -144    332   -727       C  
ATOM   1620  CE2 PHE A6985     100.563  23.785  19.761  1.00 21.61           C  
ANISOU 1620  CE2 PHE A6985     2687   2605   2918   -258    477   -679       C  
ATOM   1621  CZ  PHE A6985     100.664  23.032  20.905  1.00 21.21           C  
ANISOU 1621  CZ  PHE A6985     2608   2552   2900   -172    387   -691       C  
ATOM   1622  N   ALA A6986     104.444  28.689  18.823  1.00 26.44           N  
ANISOU 1622  N   ALA A6986     2973   3278   3793   -573    754   -837       N  
ATOM   1623  CA  ALA A6986     104.931  30.043  18.471  1.00 27.36           C  
ANISOU 1623  CA  ALA A6986     3064   3384   3946   -681    825   -839       C  
ATOM   1624  C   ALA A6986     104.223  31.076  19.353  1.00 26.77           C  
ANISOU 1624  C   ALA A6986     3032   3269   3867   -690    740   -791       C  
ATOM   1625  O   ALA A6986     104.816  32.133  19.635  1.00 26.75           O  
ANISOU 1625  O   ALA A6986     2973   3256   3933   -752    756   -819       O  
ATOM   1626  CB  ALA A6986     104.689  30.313  17.009  1.00 28.25           C  
ANISOU 1626  CB  ALA A6986     3267   3484   3982   -768    944   -793       C  
ATOM   1627  N   TRP A6987     103.000  30.758  19.783  1.00 25.53           N  
ANISOU 1627  N   TRP A6987     2969   3091   3638   -632    658   -727       N  
ATOM   1628  CA  TRP A6987     102.198  31.689  20.617  1.00 25.70           C  
ANISOU 1628  CA  TRP A6987     3038   3075   3652   -631    583   -684       C  
ATOM   1629  C   TRP A6987     101.163  30.881  21.400  1.00 23.97           C  
ANISOU 1629  C   TRP A6987     2873   2858   3376   -539    486   -649       C  
ATOM   1630  O   TRP A6987     100.798  29.782  20.937  1.00 22.70           O  
ANISOU 1630  O   TRP A6987     2750   2710   3164   -499    491   -630       O  
ATOM   1631  CB  TRP A6987     101.535  32.745  19.729  1.00 27.01           C  
ANISOU 1631  CB  TRP A6987     3301   3188   3771   -714    638   -609       C  
ATOM   1632  CG  TRP A6987     100.829  33.840  20.470  1.00 28.08           C  
ANISOU 1632  CG  TRP A6987     3477   3276   3916   -719    577   -576       C  
ATOM   1633  CD1 TRP A6987     101.378  34.995  20.949  1.00 30.16           C  
ANISOU 1633  CD1 TRP A6987     3696   3509   4252   -770    579   -610       C  
ATOM   1634  CD2 TRP A6987      99.428  33.907  20.780  1.00 28.21           C  
ANISOU 1634  CD2 TRP A6987     3585   3262   3872   -674    512   -507       C  
ATOM   1635  NE1 TRP A6987     100.418  35.767  21.547  1.00 30.11           N  
ANISOU 1635  NE1 TRP A6987     3753   3454   4233   -754    519   -570       N  
ATOM   1636  CE2 TRP A6987      99.213  35.127  21.458  1.00 29.22           C  
ANISOU 1636  CE2 TRP A6987     3717   3342   4040   -693    479   -507       C  
ATOM   1637  CE3 TRP A6987      98.339  33.057  20.557  1.00 28.86           C  
ANISOU 1637  CE3 TRP A6987     3737   3353   3875   -622    479   -452       C  
ATOM   1638  CZ2 TRP A6987      97.955  35.510  21.916  1.00 29.74           C  
ANISOU 1638  CZ2 TRP A6987     3852   3371   4073   -655    421   -456       C  
ATOM   1639  CZ3 TRP A6987      97.094  33.441  21.007  1.00 28.75           C  
ANISOU 1639  CZ3 TRP A6987     3785   3306   3831   -590    420   -399       C  
ATOM   1640  CH2 TRP A6987      96.909  34.655  21.666  1.00 28.62           C  
ANISOU 1640  CH2 TRP A6987     3769   3245   3858   -603    394   -402       C  
ATOM   1641  N   TRP A6988     100.727  31.404  22.545  1.00 22.62           N  
ANISOU 1641  N   TRP A6988     2705   2673   3215   -510    405   -646       N  
ATOM   1642  CA  TRP A6988      99.713  30.680  23.348  1.00 21.83           C  
ANISOU 1642  CA  TRP A6988     2659   2578   3058   -431    323   -611       C  
ATOM   1643  C   TRP A6988      98.907  31.687  24.163  1.00 21.44           C  
ANISOU 1643  C   TRP A6988     2649   2497   3000   -433    275   -587       C  
ATOM   1644  O   TRP A6988      99.375  32.841  24.359  1.00 21.57           O  
ANISOU 1644  O   TRP A6988     2634   2491   3070   -482    287   -617       O  
ATOM   1645  CB  TRP A6988     100.371  29.661  24.287  1.00 22.36           C  
ANISOU 1645  CB  TRP A6988     2659   2685   3151   -354    258   -666       C  
ATOM   1646  CG  TRP A6988     100.950  30.306  25.507  1.00 22.90           C  
ANISOU 1646  CG  TRP A6988     2663   2765   3272   -343    193   -722       C  
ATOM   1647  CD1 TRP A6988     102.168  30.910  25.620  1.00 24.22           C  
ANISOU 1647  CD1 TRP A6988     2730   2946   3525   -381    206   -794       C  
ATOM   1648  CD2 TRP A6988     100.305  30.460  26.786  1.00 22.53           C  
ANISOU 1648  CD2 TRP A6988     2651   2718   3192   -299    108   -714       C  
ATOM   1649  NE1 TRP A6988     102.327  31.424  26.880  1.00 24.35           N  
ANISOU 1649  NE1 TRP A6988     2718   2970   3561   -363    124   -833       N  
ATOM   1650  CE2 TRP A6988     101.203  31.161  27.618  1.00 23.39           C  
ANISOU 1650  CE2 TRP A6988     2684   2841   3362   -311     66   -785       C  
ATOM   1651  CE3 TRP A6988      99.063  30.075  27.307  1.00 21.76           C  
ANISOU 1651  CE3 TRP A6988     2639   2612   3016   -256     68   -657       C  
ATOM   1652  CZ2 TRP A6988     100.895  31.479  28.940  1.00 23.79           C  
ANISOU 1652  CZ2 TRP A6988     2752   2897   3388   -279    -16   -803       C  
ATOM   1653  CZ3 TRP A6988      98.759  30.391  28.614  1.00 22.18           C  
ANISOU 1653  CZ3 TRP A6988     2705   2672   3048   -225     -1   -673       C  
ATOM   1654  CH2 TRP A6988      99.665  31.083  29.418  1.00 22.68           C  
ANISOU 1654  CH2 TRP A6988     2703   2750   3163   -235    -44   -745       C  
ATOM   1655  N   THR A6989      97.742  31.254  24.624  1.00 20.48           N  
ANISOU 1655  N   THR A6989     2592   2372   2818   -383    227   -540       N  
ATOM   1656  CA  THR A6989      96.940  32.091  25.540  1.00 20.24           C  
ANISOU 1656  CA  THR A6989     2592   2317   2779   -371    183   -528       C  
ATOM   1657  C   THR A6989      95.924  31.212  26.258  1.00 19.39           C  
ANISOU 1657  C   THR A6989     2529   2228   2608   -305    131   -496       C  
ATOM   1658  O   THR A6989      95.818  30.013  25.930  1.00 19.55           O  
ANISOU 1658  O   THR A6989     2563   2269   2594   -277    130   -476       O  
ATOM   1659  CB  THR A6989      96.202  33.218  24.807  1.00 20.96           C  
ANISOU 1659  CB  THR A6989     2739   2354   2869   -422    222   -477       C  
ATOM   1660  OG1 THR A6989      95.763  34.143  25.802  1.00 20.58           O  
ANISOU 1660  OG1 THR A6989     2698   2281   2839   -410    184   -494       O  
ATOM   1661  CG2 THR A6989      95.028  32.732  23.984  1.00 21.02           C  
ANISOU 1661  CG2 THR A6989     2820   2352   2814   -414    233   -398       C  
ATOM   1662  N   ALA A6990      95.265  31.804  27.244  1.00 18.72           N  
ANISOU 1662  N   ALA A6990     2464   2134   2512   -286     94   -499       N  
ATOM   1663  CA  ALA A6990      94.106  31.198  27.925  1.00 18.13           C  
ANISOU 1663  CA  ALA A6990     2439   2073   2376   -237     60   -463       C  
ATOM   1664  C   ALA A6990      92.929  32.067  27.489  1.00 17.88           C  
ANISOU 1664  C   ALA A6990     2451   2001   2342   -257     85   -416       C  
ATOM   1665  O   ALA A6990      92.967  33.287  27.761  1.00 18.21           O  
ANISOU 1665  O   ALA A6990     2486   2009   2422   -276     90   -440       O  
ATOM   1666  CB  ALA A6990      94.298  31.166  29.419  1.00 18.49           C  
ANISOU 1666  CB  ALA A6990     2472   2145   2406   -198      4   -510       C  
ATOM   1667  N   PHE A6991      91.969  31.476  26.778  1.00 17.74           N  
ANISOU 1667  N   PHE A6991     2473   1980   2286   -253     98   -353       N  
ATOM   1668  CA  PHE A6991      90.832  32.240  26.212  1.00 17.58           C  
ANISOU 1668  CA  PHE A6991     2488   1922   2269   -267    112   -302       C  
ATOM   1669  C   PHE A6991      89.539  31.915  26.959  1.00 17.20           C  
ANISOU 1669  C   PHE A6991     2457   1888   2187   -226     90   -280       C  
ATOM   1670  O   PHE A6991      89.186  30.731  27.110  1.00 16.77           O  
ANISOU 1670  O   PHE A6991     2415   1867   2089   -207     79   -260       O  
ATOM   1671  CB  PHE A6991      90.681  31.944  24.718  1.00 17.97           C  
ANISOU 1671  CB  PHE A6991     2567   1959   2302   -302    139   -248       C  
ATOM   1672  CG  PHE A6991      89.486  32.607  24.084  1.00 18.32           C  
ANISOU 1672  CG  PHE A6991     2648   1966   2345   -310    135   -188       C  
ATOM   1673  CD1 PHE A6991      89.500  33.961  23.794  1.00 19.44           C  
ANISOU 1673  CD1 PHE A6991     2800   2054   2532   -333    145   -179       C  
ATOM   1674  CD2 PHE A6991      88.349  31.876  23.777  1.00 18.80           C  
ANISOU 1674  CD2 PHE A6991     2733   2043   2367   -294    117   -140       C  
ATOM   1675  CE1 PHE A6991      88.395  34.574  23.221  1.00 19.69           C  
ANISOU 1675  CE1 PHE A6991     2865   2045   2568   -330    130   -121       C  
ATOM   1676  CE2 PHE A6991      87.248  32.489  23.198  1.00 19.35           C  
ANISOU 1676  CE2 PHE A6991     2825   2081   2444   -295    101    -86       C  
ATOM   1677  CZ  PHE A6991      87.271  33.835  22.929  1.00 19.66           C  
ANISOU 1677  CZ  PHE A6991     2875   2065   2528   -308    105    -75       C  
ATOM   1678  N   VAL A6992      88.840  32.971  27.369  1.00 17.53           N  
ANISOU 1678  N   VAL A6992     2501   1901   2256   -216     90   -284       N  
ATOM   1679  CA  VAL A6992      87.545  32.852  28.091  1.00 17.39           C  
ANISOU 1679  CA  VAL A6992     2490   1897   2219   -179     83   -271       C  
ATOM   1680  C   VAL A6992      86.422  33.285  27.150  1.00 17.44           C  
ANISOU 1680  C   VAL A6992     2507   1870   2248   -183     86   -212       C  
ATOM   1681  O   VAL A6992      86.473  34.433  26.676  1.00 17.92           O  
ANISOU 1681  O   VAL A6992     2573   1877   2357   -195     89   -207       O  
ATOM   1682  CB  VAL A6992      87.556  33.717  29.363  1.00 18.26           C  
ANISOU 1682  CB  VAL A6992     2588   2001   2346   -156     81   -333       C  
ATOM   1683  CG1 VAL A6992      86.208  33.709  30.061  1.00 18.87           C  
ANISOU 1683  CG1 VAL A6992     2666   2093   2408   -121     90   -327       C  
ATOM   1684  CG2 VAL A6992      88.667  33.288  30.308  1.00 18.81           C  
ANISOU 1684  CG2 VAL A6992     2650   2109   2389   -151     62   -390       C  
ATOM   1685  N   THR A6993      85.456  32.402  26.879  1.00 17.12           N  
ANISOU 1685  N   THR A6993     2472   1857   2176   -175     79   -168       N  
ATOM   1686  CA  THR A6993      84.315  32.826  26.026  1.00 17.17           C  
ANISOU 1686  CA  THR A6993     2480   1836   2208   -174     67   -114       C  
ATOM   1687  C   THR A6993      83.475  33.847  26.798  1.00 17.81           C  
ANISOU 1687  C   THR A6993     2534   1893   2337   -135     71   -137       C  
ATOM   1688  O   THR A6993      83.329  33.717  28.039  1.00 18.24           O  
ANISOU 1688  O   THR A6993     2572   1978   2380   -110     89   -184       O  
ATOM   1689  CB  THR A6993      83.459  31.643  25.556  1.00 17.43           C  
ANISOU 1689  CB  THR A6993     2515   1904   2202   -181     54    -69       C  
ATOM   1690  OG1 THR A6993      82.799  31.072  26.687  1.00 18.06           O  
ANISOU 1690  OG1 THR A6993     2571   2022   2265   -157     66    -89       O  
ATOM   1691  CG2 THR A6993      84.268  30.595  24.824  1.00 17.28           C  
ANISOU 1691  CG2 THR A6993     2526   1902   2136   -215     54    -57       C  
ATOM   1692  N   ASN A6994      82.940  34.836  26.091  1.00 18.42           N  
ANISOU 1692  N   ASN A6994     2613   1917   2466   -128     56   -106       N  
ATOM   1693  CA  ASN A6994      82.091  35.856  26.757  1.00 18.99           C  
ANISOU 1693  CA  ASN A6994     2656   1958   2600    -81     60   -132       C  
ATOM   1694  C   ASN A6994      80.780  35.240  27.265  1.00 19.03           C  
ANISOU 1694  C   ASN A6994     2617   2010   2601    -50     66   -128       C  
ATOM   1695  O   ASN A6994      80.241  35.758  28.259  1.00 19.65           O  
ANISOU 1695  O   ASN A6994     2665   2089   2711    -11     91   -177       O  
ATOM   1696  CB  ASN A6994      81.829  37.058  25.850  1.00 20.02           C  
ANISOU 1696  CB  ASN A6994     2803   2008   2795    -74     34    -93       C  
ATOM   1697  CG  ASN A6994      82.889  38.128  25.979  1.00 21.19           C  
ANISOU 1697  CG  ASN A6994     2980   2094   2977    -91     48   -128       C  
ATOM   1698  OD1 ASN A6994      83.593  38.194  26.990  1.00 21.07           O  
ANISOU 1698  OD1 ASN A6994     2956   2093   2953    -93     74   -199       O  
ATOM   1699  ND2 ASN A6994      82.965  39.005  24.990  1.00 21.42           N  
ANISOU 1699  ND2 ASN A6994     3045   2048   3044   -106     28    -80       N  
ATOM   1700  N  AVAL A6995      80.274  34.173  26.629  0.60 18.23           N  
ANISOU 1700  N  AVAL A6995     2513   1949   2465    -70     48    -78       N  
ATOM   1701  N  BVAL A6995      80.327  34.158  26.628  0.40 18.89           N  
ANISOU 1701  N  BVAL A6995     2598   2033   2547    -72     49    -79       N  
ATOM   1702  CA AVAL A6995      78.985  33.574  27.105  0.60 18.51           C  
ANISOU 1702  CA AVAL A6995     2497   2030   2505    -51     58    -75       C  
ATOM   1703  CA BVAL A6995      79.038  33.512  27.004  0.40 19.42           C  
ANISOU 1703  CA BVAL A6995     2616   2145   2616    -55     55    -71       C  
ATOM   1704  C  AVAL A6995      79.216  32.805  28.409  0.60 18.67           C  
ANISOU 1704  C  AVAL A6995     2517   2104   2470    -55    104   -122       C  
ATOM   1705  C  BVAL A6995      79.209  32.719  28.307  0.40 19.22           C  
ANISOU 1705  C  BVAL A6995     2589   2175   2538    -58    101   -116       C  
ATOM   1706  O  AVAL A6995      78.242  32.660  29.172  0.60 18.70           O  
ANISOU 1706  O  AVAL A6995     2479   2141   2485    -36    135   -141       O  
ATOM   1707  O  BVAL A6995      78.183  32.465  28.970  0.40 19.42           O  
ANISOU 1707  O  BVAL A6995     2570   2235   2572    -43    129   -128       O  
ATOM   1708  CB AVAL A6995      78.300  32.665  26.063  0.60 18.17           C  
ANISOU 1708  CB AVAL A6995     2447   2011   2445    -79     21    -13       C  
ATOM   1709  CB BVAL A6995      78.527  32.619  25.859  0.40 19.71           C  
ANISOU 1709  CB BVAL A6995     2655   2201   2631    -87     16     -6       C  
ATOM   1710  CG1AVAL A6995      77.723  33.458  24.905  0.60 18.30           C  
ANISOU 1710  CG1AVAL A6995     2458   1981   2515    -66    -32     36       C  
ATOM   1711  CG1BVAL A6995      79.308  31.316  25.768  0.40 19.15           C  
ANISOU 1711  CG1BVAL A6995     2627   2167   2483   -132     24     -1       C  
ATOM   1712  CG2AVAL A6995      79.208  31.547  25.571  0.60 17.60           C  
ANISOU 1712  CG2AVAL A6995     2428   1960   2299   -128     17      4       C  
ATOM   1713  CG2BVAL A6995      77.045  32.340  25.991  0.40 20.59           C  
ANISOU 1713  CG2BVAL A6995     2701   2343   2779    -71     10      5       C  
ATOM   1714  N   ASN A6996      80.443  32.341  28.664  1.00 18.51           N  
ANISOU 1714  N   ASN A6996     2541   2094   2395    -78    108   -139       N  
ATOM   1715  CA  ASN A6996      80.690  31.555  29.902  1.00 19.51           C  
ANISOU 1715  CA  ASN A6996     2681   2269   2461    -79    138   -174       C  
ATOM   1716  C   ASN A6996      81.681  32.285  30.818  1.00 20.33           C  
ANISOU 1716  C   ASN A6996     2804   2362   2556    -63    148   -239       C  
ATOM   1717  O   ASN A6996      82.346  31.614  31.620  1.00 22.14           O  
ANISOU 1717  O   ASN A6996     3062   2625   2724    -69    151   -261       O  
ATOM   1718  CB  ASN A6996      81.178  30.149  29.553  1.00 19.51           C  
ANISOU 1718  CB  ASN A6996     2714   2295   2400   -113    124   -140       C  
ATOM   1719  CG  ASN A6996      80.873  29.147  30.642  1.00 20.47           C  
ANISOU 1719  CG  ASN A6996     2849   2464   2463   -117    150   -147       C  
ATOM   1720  OD1 ASN A6996      79.922  29.335  31.404  1.00 21.20           O  
ANISOU 1720  OD1 ASN A6996     2915   2580   2560   -105    187   -162       O  
ATOM   1721  ND2 ASN A6996      81.648  28.075  30.704  1.00 18.95           N  
ANISOU 1721  ND2 ASN A6996     2699   2283   2217   -133    135   -134       N  
ATOM   1722  N   ALA A6997      81.706  33.616  30.754  1.00 20.89           N  
ANISOU 1722  N   ALA A6997     2862   2385   2688    -43    148   -268       N  
ATOM   1723  CA  ALA A6997      82.659  34.443  31.532  1.00 21.71           C  
ANISOU 1723  CA  ALA A6997     2983   2469   2795    -35    152   -337       C  
ATOM   1724  C   ALA A6997      82.450  34.298  33.051  1.00 21.79           C  
ANISOU 1724  C   ALA A6997     2999   2525   2753    -16    183   -396       C  
ATOM   1725  O   ALA A6997      83.372  34.682  33.794  1.00 22.25           O  
ANISOU 1725  O   ALA A6997     3080   2582   2790    -17    175   -455       O  
ATOM   1726  CB  ALA A6997      82.518  35.877  31.094  1.00 23.54           C  
ANISOU 1726  CB  ALA A6997     3203   2628   3111    -19    148   -351       C  
ATOM   1727  N   SER A6998      81.313  33.748  33.498  1.00 21.48           N  
ANISOU 1727  N   SER A6998     2943   2526   2691     -5    218   -384       N  
ATOM   1728  CA  SER A6998      81.056  33.590  34.957  1.00 22.52           C  
ANISOU 1728  CA  SER A6998     3091   2706   2758      6    260   -437       C  
ATOM   1729  C   SER A6998      81.656  32.274  35.470  1.00 21.35           C  
ANISOU 1729  C   SER A6998     2990   2609   2511    -18    246   -415       C  
ATOM   1730  O   SER A6998      81.494  31.975  36.666  1.00 22.30           O  
ANISOU 1730  O   SER A6998     3141   2774   2558    -16    276   -446       O  
ATOM   1731  CB  SER A6998      79.580  33.689  35.273  1.00 24.57           C  
ANISOU 1731  CB  SER A6998     3305   2986   3041     26    317   -441       C  
ATOM   1732  OG  SER A6998      78.889  32.526  34.849  1.00 26.44           O  
ANISOU 1732  OG  SER A6998     3516   3245   3283      4    316   -369       O  
ATOM   1733  N   SER A6999      82.333  31.531  34.592  1.00 19.88           N  
ANISOU 1733  N   SER A6999     2816   2415   2323    -40    203   -364       N  
ATOM   1734  CA  SER A6999      82.984  30.243  34.943  1.00 19.56           C  
ANISOU 1734  CA  SER A6999     2820   2408   2203    -56    179   -338       C  
ATOM   1735  C   SER A6999      84.508  30.402  34.918  1.00 18.67           C  
ANISOU 1735  C   SER A6999     2725   2281   2087    -54    127   -367       C  
ATOM   1736  O   SER A6999      85.000  31.220  34.119  1.00 18.26           O  
ANISOU 1736  O   SER A6999     2646   2189   2103    -58    112   -380       O  
ATOM   1737  CB  SER A6999      82.554  29.157  33.980  1.00 19.50           C  
ANISOU 1737  CB  SER A6999     2808   2399   2200    -79    173   -265       C  
ATOM   1738  OG  SER A6999      83.317  27.975  34.178  1.00 19.43           O  
ANISOU 1738  OG  SER A6999     2845   2405   2131    -89    143   -242       O  
ATOM   1739  N   SER A7000      85.219  29.622  35.742  1.00 18.48           N  
ANISOU 1739  N   SER A7000     2742   2288   1989    -50     98   -375       N  
ATOM   1740  CA  SER A7000      86.707  29.605  35.746  1.00 18.54           C  
ANISOU 1740  CA  SER A7000     2754   2291   2000    -45     40   -404       C  
ATOM   1741  C   SER A7000      87.218  28.883  34.492  1.00 17.97           C  
ANISOU 1741  C   SER A7000     2665   2197   1966    -57     20   -357       C  
ATOM   1742  O   SER A7000      88.450  28.778  34.302  1.00 17.69           O  
ANISOU 1742  O   SER A7000     2617   2156   1948    -54    -20   -379       O  
ATOM   1743  CB  SER A7000      87.236  28.962  36.996  1.00 19.23           C  
ANISOU 1743  CB  SER A7000     2891   2418   1998    -30      4   -420       C  
ATOM   1744  OG  SER A7000      86.875  27.590  37.044  1.00 19.11           O  
ANISOU 1744  OG  SER A7000     2915   2417   1929    -32      4   -356       O  
ATOM   1745  N   GLU A7001      86.298  28.361  33.681  1.00 18.22           N  
ANISOU 1745  N   GLU A7001     2693   2219   2009    -72     48   -300       N  
ATOM   1746  CA  GLU A7001      86.679  27.696  32.416  1.00 17.64           C  
ANISOU 1746  CA  GLU A7001     2612   2124   1966    -88     36   -261       C  
ATOM   1747  C   GLU A7001      87.502  28.630  31.528  1.00 17.50           C  
ANISOU 1747  C   GLU A7001     2559   2076   2013    -99     30   -287       C  
ATOM   1748  O   GLU A7001      87.251  29.853  31.516  1.00 16.79           O  
ANISOU 1748  O   GLU A7001     2448   1966   1962   -102     46   -311       O  
ATOM   1749  CB  GLU A7001      85.421  27.291  31.648  1.00 18.17           C  
ANISOU 1749  CB  GLU A7001     2677   2184   2041   -108     64   -206       C  
ATOM   1750  CG  GLU A7001      85.674  26.836  30.221  1.00 18.12           C  
ANISOU 1750  CG  GLU A7001     2666   2154   2062   -130     56   -174       C  
ATOM   1751  CD  GLU A7001      84.381  26.513  29.501  1.00 19.33           C  
ANISOU 1751  CD  GLU A7001     2816   2304   2223   -153     72   -125       C  
ATOM   1752  OE1 GLU A7001      83.881  25.377  29.664  1.00 19.30           O  
ANISOU 1752  OE1 GLU A7001     2836   2311   2184   -164     74    -95       O  
ATOM   1753  OE2 GLU A7001      83.824  27.437  28.861  1.00 20.03           O  
ANISOU 1753  OE2 GLU A7001     2878   2377   2355   -159     79   -117       O  
ATOM   1754  N   ALA A7002      88.469  28.046  30.829  1.00 16.91           N  
ANISOU 1754  N   ALA A7002     2478   1994   1950   -105     13   -284       N  
ATOM   1755  CA  ALA A7002      89.194  28.742  29.748  1.00 17.40           C  
ANISOU 1755  CA  ALA A7002     2510   2028   2069   -130     24   -297       C  
ATOM   1756  C   ALA A7002      89.654  27.685  28.751  1.00 16.84           C  
ANISOU 1756  C   ALA A7002     2446   1955   1995   -140     25   -272       C  
ATOM   1757  O   ALA A7002      89.659  26.490  29.104  1.00 16.71           O  
ANISOU 1757  O   ALA A7002     2453   1954   1942   -120      7   -258       O  
ATOM   1758  CB  ALA A7002      90.365  29.537  30.272  1.00 17.81           C  
ANISOU 1758  CB  ALA A7002     2531   2080   2153   -128      6   -361       C  
ATOM   1759  N   PHE A7003      89.941  28.119  27.531  1.00 16.98           N  
ANISOU 1759  N   PHE A7003     2453   1951   2046   -172     50   -264       N  
ATOM   1760  CA  PHE A7003      90.581  27.222  26.553  1.00 17.32           C  
ANISOU 1760  CA  PHE A7003     2499   1992   2086   -184     62   -258       C  
ATOM   1761  C   PHE A7003      92.055  27.602  26.469  1.00 17.21           C  
ANISOU 1761  C   PHE A7003     2439   1980   2117   -189     69   -314       C  
ATOM   1762  O   PHE A7003      92.370  28.774  26.167  1.00 17.40           O  
ANISOU 1762  O   PHE A7003     2442   1988   2178   -221     91   -329       O  
ATOM   1763  CB  PHE A7003      89.884  27.292  25.196  1.00 17.98           C  
ANISOU 1763  CB  PHE A7003     2611   2057   2162   -222     89   -212       C  
ATOM   1764  CG  PHE A7003      88.528  26.644  25.215  1.00 18.63           C  
ANISOU 1764  CG  PHE A7003     2726   2144   2208   -218     75   -164       C  
ATOM   1765  CD1 PHE A7003      88.394  25.292  24.941  1.00 19.29           C  
ANISOU 1765  CD1 PHE A7003     2837   2232   2259   -216     69   -149       C  
ATOM   1766  CD2 PHE A7003      87.401  27.369  25.560  1.00 18.91           C  
ANISOU 1766  CD2 PHE A7003     2759   2176   2249   -216     70   -140       C  
ATOM   1767  CE1 PHE A7003      87.149  24.688  24.976  1.00 19.40           C  
ANISOU 1767  CE1 PHE A7003     2876   2248   2246   -223     58   -108       C  
ATOM   1768  CE2 PHE A7003      86.159  26.758  25.611  1.00 19.90           C  
ANISOU 1768  CE2 PHE A7003     2899   2310   2350   -217     61   -101       C  
ATOM   1769  CZ  PHE A7003      86.035  25.420  25.316  1.00 19.86           C  
ANISOU 1769  CZ  PHE A7003     2921   2310   2311   -225     55    -84       C  
ATOM   1770  N  ALEU A7004      92.933  26.660  26.834  0.50 16.92           N  
ANISOU 1770  N  ALEU A7004     2384   1962   2083   -158     47   -344       N  
ATOM   1771  N  BLEU A7004      92.928  26.649  26.783  0.50 17.77           N  
ANISOU 1771  N  BLEU A7004     2492   2068   2190   -159     49   -343       N  
ATOM   1772  CA ALEU A7004      94.386  26.880  26.631  0.50 17.38           C  
ANISOU 1772  CA ALEU A7004     2381   2028   2195   -162     56   -402       C  
ATOM   1773  CA BLEU A7004      94.390  26.858  26.670  0.50 18.77           C  
ANISOU 1773  CA BLEU A7004     2557   2204   2370   -161     54   -403       C  
ATOM   1774  C  ALEU A7004      94.641  26.657  25.148  0.50 17.97           C  
ANISOU 1774  C  ALEU A7004     2459   2090   2278   -200    114   -393       C  
ATOM   1775  C  BLEU A7004      94.739  26.635  25.193  0.50 18.91           C  
ANISOU 1775  C  BLEU A7004     2574   2211   2401   -198    113   -398       C  
ATOM   1776  O  ALEU A7004      94.385  25.532  24.658  0.50 17.53           O  
ANISOU 1776  O  ALEU A7004     2436   2032   2193   -186    119   -373       O  
ATOM   1777  O  BLEU A7004      94.645  25.470  24.736  0.50 18.77           O  
ANISOU 1777  O  BLEU A7004     2581   2192   2358   -180    117   -385       O  
ATOM   1778  CB ALEU A7004      95.233  25.928  27.474  0.50 17.79           C  
ANISOU 1778  CB ALEU A7004     2404   2099   2253   -106      5   -438       C  
ATOM   1779  CB BLEU A7004      95.067  25.867  27.617  0.50 20.18           C  
ANISOU 1779  CB BLEU A7004     2716   2402   2547   -102      0   -432       C  
ATOM   1780  CG ALEU A7004      95.215  26.193  28.973  0.50 17.51           C  
ANISOU 1780  CG ALEU A7004     2368   2083   2201    -73    -57   -456       C  
ATOM   1781  CG BLEU A7004      96.506  26.175  28.011  0.50 21.42           C  
ANISOU 1781  CG BLEU A7004     2794   2579   2765    -89    -24   -503       C  
ATOM   1782  CD1ALEU A7004      96.211  25.291  29.678  0.50 18.14           C  
ANISOU 1782  CD1ALEU A7004     2419   2180   2292    -16   -118   -490       C  
ATOM   1783  CD1BLEU A7004      96.649  27.605  28.511  0.50 21.56           C  
ANISOU 1783  CD1BLEU A7004     2782   2598   2809   -122    -27   -534       C  
ATOM   1784  CD2ALEU A7004      95.512  27.655  29.261  0.50 17.86           C  
ANISOU 1784  CD2ALEU A7004     2375   2128   2282   -106    -50   -496       C  
ATOM   1785  CD2BLEU A7004      96.977  25.192  29.069  0.50 21.96           C  
ANISOU 1785  CD2BLEU A7004     2856   2663   2821    -21    -99   -518       C  
ATOM   1786  N   ILE A7005      95.078  27.714  24.475  1.00 18.72           N  
ANISOU 1786  N   ILE A7005     2531   2175   2407   -251    159   -407       N  
ATOM   1787  CA  ILE A7005      95.321  27.659  23.012  1.00 19.54           C  
ANISOU 1787  CA  ILE A7005     2650   2270   2505   -299    225   -396       C  
ATOM   1788  C   ILE A7005      96.817  27.728  22.726  1.00 20.67           C  
ANISOU 1788  C   ILE A7005     2718   2428   2707   -315    266   -462       C  
ATOM   1789  O   ILE A7005      97.470  28.678  23.176  1.00 20.65           O  
ANISOU 1789  O   ILE A7005     2663   2426   2757   -336    266   -498       O  
ATOM   1790  CB  ILE A7005      94.529  28.779  22.314  1.00 19.96           C  
ANISOU 1790  CB  ILE A7005     2749   2292   2540   -353    251   -344       C  
ATOM   1791  CG1 ILE A7005      93.024  28.598  22.537  1.00 20.34           C  
ANISOU 1791  CG1 ILE A7005     2855   2331   2541   -331    210   -284       C  
ATOM   1792  CG2 ILE A7005      94.874  28.860  20.833  1.00 20.36           C  
ANISOU 1792  CG2 ILE A7005     2825   2335   2573   -411    320   -331       C  
ATOM   1793  CD1 ILE A7005      92.189  29.776  22.102  1.00 20.92           C  
ANISOU 1793  CD1 ILE A7005     2964   2372   2613   -365    215   -235       C  
ATOM   1794  N   GLY A7006      97.312  26.697  22.046  1.00 21.11           N  
ANISOU 1794  N   GLY A7006     2766   2495   2757   -303    298   -484       N  
ATOM   1795  CA  GLY A7006      98.685  26.644  21.524  1.00 21.78           C  
ANISOU 1795  CA  GLY A7006     2777   2599   2900   -321    356   -550       C  
ATOM   1796  C   GLY A7006      98.608  26.898  20.033  1.00 22.29           C  
ANISOU 1796  C   GLY A7006     2887   2655   2928   -392    447   -529       C  
ATOM   1797  O   GLY A7006      97.916  26.117  19.347  1.00 21.44           O  
ANISOU 1797  O   GLY A7006     2850   2540   2755   -388    456   -496       O  
ATOM   1798  N   CYS A7007      99.237  27.972  19.555  1.00 23.33           N  
ANISOU 1798  N   CYS A7007     2988   2784   3091   -461    509   -543       N  
ATOM   1799  CA  CYS A7007      99.133  28.333  18.115  1.00 25.06           C  
ANISOU 1799  CA  CYS A7007     3269   2993   3259   -539    597   -511       C  
ATOM   1800  C   CYS A7007     100.473  28.105  17.399  1.00 25.30           C  
ANISOU 1800  C   CYS A7007     3230   3052   3330   -573    696   -583       C  
ATOM   1801  O   CYS A7007     101.459  28.788  17.752  1.00 24.93           O  
ANISOU 1801  O   CYS A7007     3092   3014   3363   -601    722   -633       O  
ATOM   1802  CB  CYS A7007      98.674  29.778  17.956  1.00 26.89           C  
ANISOU 1802  CB  CYS A7007     3544   3189   3482   -604    603   -456       C  
ATOM   1803  SG  CYS A7007      98.278  30.221  16.245  1.00 32.81           S  
ANISOU 1803  SG  CYS A7007     4404   3919   4144   -694    687   -390       S  
ATOM   1804  N   ASN A7008     100.490  27.163  16.445  1.00 25.21           N  
ANISOU 1804  N   ASN A7008     3257   3053   3267   -573    749   -595       N  
ATOM   1805  CA  ASN A7008     101.664  26.839  15.585  1.00 25.83           C  
ANISOU 1805  CA  ASN A7008     3280   3161   3372   -606    862   -667       C  
ATOM   1806  C   ASN A7008     102.720  26.076  16.394  1.00 25.67           C  
ANISOU 1806  C   ASN A7008     3129   3167   3455   -529    841   -759       C  
ATOM   1807  O   ASN A7008     103.662  26.705  16.905  1.00 25.34           O  
ANISOU 1807  O   ASN A7008     2979   3142   3504   -543    851   -808       O  
ATOM   1808  CB  ASN A7008     102.221  28.094  14.912  1.00 27.32           C  
ANISOU 1808  CB  ASN A7008     3462   3349   3569   -713    957   -660       C  
ATOM   1809  CG  ASN A7008     101.176  28.844  14.110  1.00 27.81           C  
ANISOU 1809  CG  ASN A7008     3661   3377   3528   -781    964   -561       C  
ATOM   1810  OD1 ASN A7008     101.063  30.061  14.231  1.00 29.50           O  
ANISOU 1810  OD1 ASN A7008     3891   3562   3757   -835    962   -518       O  
ATOM   1811  ND2 ASN A7008     100.387  28.130  13.320  1.00 27.02           N  
ANISOU 1811  ND2 ASN A7008     3663   3276   3326   -775    964   -525       N  
ATOM   1812  N   TYR A7009     102.585  24.749  16.431  1.00 24.73           N  
ANISOU 1812  N   TYR A7009     3022   3049   3324   -453    813   -784       N  
ATOM   1813  CA  TYR A7009     103.472  23.852  17.214  1.00 25.55           C  
ANISOU 1813  CA  TYR A7009     3017   3167   3523   -360    772   -862       C  
ATOM   1814  C   TYR A7009     104.876  23.819  16.594  1.00 26.96           C  
ANISOU 1814  C   TYR A7009     3081   3380   3780   -382    883   -958       C  
ATOM   1815  O   TYR A7009     104.988  23.597  15.369  1.00 27.25           O  
ANISOU 1815  O   TYR A7009     3160   3425   3768   -431    995   -977       O  
ATOM   1816  CB  TYR A7009     102.817  22.471  17.295  1.00 25.30           C  
ANISOU 1816  CB  TYR A7009     3052   3109   3448   -282    718   -849       C  
ATOM   1817  CG  TYR A7009     103.558  21.460  18.125  1.00 26.36           C  
ANISOU 1817  CG  TYR A7009     3100   3243   3672   -175    658   -912       C  
ATOM   1818  CD1 TYR A7009     103.886  21.724  19.445  1.00 26.71           C  
ANISOU 1818  CD1 TYR A7009     3071   3294   3782   -124    559   -916       C  
ATOM   1819  CD2 TYR A7009     103.864  20.210  17.615  1.00 27.39           C  
ANISOU 1819  CD2 TYR A7009     3233   3358   3813   -121    690   -964       C  
ATOM   1820  CE1 TYR A7009     104.557  20.792  20.218  1.00 27.77           C  
ANISOU 1820  CE1 TYR A7009     3133   3424   3991    -22    489   -965       C  
ATOM   1821  CE2 TYR A7009     104.521  19.262  18.379  1.00 28.39           C  
ANISOU 1821  CE2 TYR A7009     3287   3474   4026    -14    624  -1015       C  
ATOM   1822  CZ  TYR A7009     104.866  19.554  19.685  1.00 28.45           C  
ANISOU 1822  CZ  TYR A7009     3221   3491   4098     36    520  -1011       C  
ATOM   1823  OH  TYR A7009     105.518  18.621  20.433  1.00 30.76           O  
ANISOU 1823  OH  TYR A7009     3447   3768   4470    145    444  -1054       O  
ATOM   1824  N   LEU A7010     105.909  23.995  17.428  1.00 28.11           N  
ANISOU 1824  N   LEU A7010     3087   3550   4044   -346    852  -1023       N  
ATOM   1825  CA  LEU A7010     107.322  24.036  16.953  1.00 30.49           C  
ANISOU 1825  CA  LEU A7010     3248   3891   4443   -367    955  -1125       C  
ATOM   1826  C   LEU A7010     108.057  22.737  17.310  1.00 32.17           C  
ANISOU 1826  C   LEU A7010     3367   4111   4742   -249    921  -1207       C  
ATOM   1827  O   LEU A7010     109.193  22.565  16.827  1.00 33.10           O  
ANISOU 1827  O   LEU A7010     3366   4263   4947   -252   1014  -1301       O  
ATOM   1828  CB  LEU A7010     108.023  25.257  17.561  1.00 31.01           C  
ANISOU 1828  CB  LEU A7010     3207   3978   4594   -421    946  -1146       C  
ATOM   1829  CG  LEU A7010     107.357  26.601  17.271  1.00 30.92           C  
ANISOU 1829  CG  LEU A7010     3286   3946   4514   -533    975  -1067       C  
ATOM   1830  CD1 LEU A7010     108.119  27.736  17.929  1.00 32.12           C  
ANISOU 1830  CD1 LEU A7010     3328   4112   4763   -585    962  -1101       C  
ATOM   1831  CD2 LEU A7010     107.224  26.842  15.776  1.00 31.54           C  
ANISOU 1831  CD2 LEU A7010     3446   4024   4511   -631   1121  -1045       C  
ATOM   1832  N   GLY A7011     107.445  21.868  18.125  1.00 32.71           N  
ANISOU 1832  N   GLY A7011     3488   4147   4793   -150    796  -1172       N  
ATOM   1833  CA  GLY A7011     108.045  20.564  18.480  1.00 35.21           C  
ANISOU 1833  CA  GLY A7011     3738   4454   5186    -29    749  -1237       C  
ATOM   1834  C   GLY A7011     109.241  20.687  19.408  1.00 37.69           C  
ANISOU 1834  C   GLY A7011     3879   4800   5642     30    686  -1310       C  
ATOM   1835  O   GLY A7011     109.962  19.685  19.574  1.00 39.74           O  
ANISOU 1835  O   GLY A7011     4055   5053   5988    131    661  -1378       O  
ATOM   1836  N   LYS A7012     109.460  21.876  19.968  1.00 38.13           N  
ANISOU 1836  N   LYS A7012     3878   4883   5724    -30    658  -1299       N  
ATOM   1837  CA  LYS A7012     110.569  22.114  20.927  1.00 40.87           C  
ANISOU 1837  CA  LYS A7012     4059   5266   6204     15    580  -1369       C  
ATOM   1838  C   LYS A7012     110.214  23.353  21.738  1.00 39.84           C  
ANISOU 1838  C   LYS A7012     3947   5143   6048    -48    511  -1320       C  
ATOM   1839  O   LYS A7012     109.409  24.170  21.295  1.00 37.31           O  
ANISOU 1839  O   LYS A7012     3731   4807   5638   -142    565  -1255       O  
ATOM   1840  CB  LYS A7012     111.907  22.273  20.196  1.00 44.29           C  
ANISOU 1840  CB  LYS A7012     4325   5745   6757    -17    702  -1480       C  
ATOM   1841  CG  LYS A7012     112.040  23.516  19.327  1.00 46.97           C  
ANISOU 1841  CG  LYS A7012     4659   6110   7076   -169    845  -1480       C  
ATOM   1842  CD  LYS A7012     113.394  23.619  18.651  1.00 51.14           C  
ANISOU 1842  CD  LYS A7012     5014   6689   7728   -205    975  -1595       C  
ATOM   1843  CE  LYS A7012     113.601  24.929  17.923  1.00 53.32           C  
ANISOU 1843  CE  LYS A7012     5281   6986   7990   -366   1111  -1591       C  
ATOM   1844  NZ  LYS A7012     114.948  25.000  17.308  1.00 57.20           N  
ANISOU 1844  NZ  LYS A7012     5592   7531   8607   -406   1246  -1707       N  
ATOM   1845  N   PRO A7013     110.795  23.535  22.945  1.00 40.79           N  
ANISOU 1845  N   PRO A7013     3970   5284   6245      2    386  -1352       N  
ATOM   1846  CA  PRO A7013     110.464  24.689  23.774  1.00 40.74           C  
ANISOU 1846  CA  PRO A7013     3985   5281   6212    -54    317  -1317       C  
ATOM   1847  C   PRO A7013     111.046  26.013  23.264  1.00 41.70           C  
ANISOU 1847  C   PRO A7013     4028   5427   6387   -183    418  -1357       C  
ATOM   1848  O   PRO A7013     112.254  26.122  23.150  1.00 45.12           O  
ANISOU 1848  O   PRO A7013     4299   5900   6942   -194    453  -1449       O  
ATOM   1849  CB  PRO A7013     111.075  24.335  25.139  1.00 41.28           C  
ANISOU 1849  CB  PRO A7013     3964   5370   6350     43    153  -1356       C  
ATOM   1850  CG  PRO A7013     112.222  23.408  24.808  1.00 43.01           C  
ANISOU 1850  CG  PRO A7013     4039   5612   6689    120    171  -1445       C  
ATOM   1851  CD  PRO A7013     111.769  22.637  23.584  1.00 42.43           C  
ANISOU 1851  CD  PRO A7013     4048   5508   6563    121    296  -1425       C  
ATOM   1852  N  AARG A7014     110.178  26.979  22.940  0.60 40.73           N  
ANISOU 1852  N  AARG A7014     4021   5276   6178   -279    467  -1286       N  
ATOM   1853  N  BARG A7014     110.156  26.955  22.942  0.40 40.18           N  
ANISOU 1853  N  BARG A7014     3955   5206   6106   -277    466  -1285       N  
ATOM   1854  CA AARG A7014     110.661  28.323  22.518  0.60 42.02           C  
ANISOU 1854  CA AARG A7014     4131   5447   6388   -409    557  -1312       C  
ATOM   1855  CA BARG A7014     110.528  28.325  22.502  0.40 40.70           C  
ANISOU 1855  CA BARG A7014     3981   5275   6207   -409    556  -1302       C  
ATOM   1856  C  AARG A7014     110.790  29.177  23.785  0.60 41.86           C  
ANISOU 1856  C  AARG A7014     4071   5429   6405   -417    437  -1327       C  
ATOM   1857  C  BARG A7014     110.754  29.169  23.760  0.40 41.07           C  
ANISOU 1857  C  BARG A7014     3976   5328   6301   -417    440  -1324       C  
ATOM   1858  O  AARG A7014     111.575  30.144  23.772  0.60 42.09           O  
ANISOU 1858  O  AARG A7014     4000   5472   6519   -504    476  -1382       O  
ATOM   1859  O  BARG A7014     111.575  30.107  23.717  0.40 41.66           O  
ANISOU 1859  O  BARG A7014     3946   5419   6464   -503    481  -1382       O  
ATOM   1860  CB AARG A7014     109.747  28.986  21.482  0.60 42.21           C  
ANISOU 1860  CB AARG A7014     4297   5430   6308   -508    667  -1230       C  
ATOM   1861  CB BARG A7014     109.410  28.916  21.639  0.40 39.59           C  
ANISOU 1861  CB BARG A7014     4004   5090   5949   -492    640  -1207       C  
ATOM   1862  CG AARG A7014     108.457  29.573  22.038  0.60 42.15           C  
ANISOU 1862  CG AARG A7014     4434   5377   6202   -514    591  -1137       C  
ATOM   1863  CG BARG A7014     109.659  30.346  21.185  0.40 40.22           C  
ANISOU 1863  CG BARG A7014     4073   5155   6052   -629    728  -1205       C  
ATOM   1864  CD AARG A7014     107.722  30.387  20.989  0.60 42.66           C  
ANISOU 1864  CD AARG A7014     4618   5402   6188   -617    694  -1063       C  
ATOM   1865  CD BARG A7014     108.421  30.958  20.558  0.40 39.66           C  
ANISOU 1865  CD BARG A7014     4176   5030   5862   -690    770  -1099       C  
ATOM   1866  NE AARG A7014     108.530  31.485  20.474  0.60 44.94           N  
ANISOU 1866  NE AARG A7014     4839   5690   6544   -735    793  -1098       N  
ATOM   1867  NE BARG A7014     107.302  30.958  21.490  0.40 38.44           N  
ANISOU 1867  NE BARG A7014     4120   4846   5639   -627    646  -1036       N  
ATOM   1868  CZ AARG A7014     108.651  32.681  21.046  0.60 45.37           C  
ANISOU 1868  CZ AARG A7014     4875   5720   6642   -798    763  -1104       C  
ATOM   1869  CZ BARG A7014     107.111  31.874  22.431  0.40 39.08           C  
ANISOU 1869  CZ BARG A7014     4203   4905   5739   -643    569  -1034       C  
ATOM   1870  NH1AARG A7014     109.416  33.605  20.488  0.60 46.69           N  
ANISOU 1870  NH1AARG A7014     4984   5883   6874   -914    864  -1135       N  
ATOM   1871  NH1BARG A7014     106.064  31.791  23.234  0.40 38.43           N  
ANISOU 1871  NH1BARG A7014     4211   4800   5588   -584    471   -981       N  
ATOM   1872  NH2AARG A7014     108.016  32.951  22.174  0.60 45.03           N  
ANISOU 1872  NH2AARG A7014     4873   5655   6578   -749    638  -1082       N  
ATOM   1873  NH2BARG A7014     107.974  32.864  22.571  0.40 40.62           N  
ANISOU 1873  NH2BARG A7014     4307   5101   6023   -722    597  -1089       N  
ATOM   1874  N   GLU A7015     110.021  28.836  24.827  1.00 40.05           N  
ANISOU 1874  N   GLU A7015     3923   5184   6108   -336    303  -1281       N  
ATOM   1875  CA  GLU A7015     110.124  29.528  26.140  1.00 40.57           C  
ANISOU 1875  CA  GLU A7015     3961   5257   6195   -331    177  -1303       C  
ATOM   1876  C   GLU A7015     109.865  28.485  27.231  1.00 38.25           C  
ANISOU 1876  C   GLU A7015     3695   4973   5863   -201     30  -1289       C  
ATOM   1877  O   GLU A7015     109.075  27.540  26.995  1.00 36.69           O  
ANISOU 1877  O   GLU A7015     3600   4753   5584   -139     31  -1225       O  
ATOM   1878  CB  GLU A7015     109.180  30.729  26.268  1.00 42.34           C  
ANISOU 1878  CB  GLU A7015     4302   5436   6349   -412    190  -1244       C  
ATOM   1879  CG  GLU A7015     107.700  30.391  26.265  1.00 42.82           C  
ANISOU 1879  CG  GLU A7015     4534   5457   6276   -374    175  -1142       C  
ATOM   1880  CD  GLU A7015     106.796  31.511  26.766  1.00 44.22           C  
ANISOU 1880  CD  GLU A7015     4809   5595   6398   -422    149  -1099       C  
ATOM   1881  OE1 GLU A7015     105.650  31.608  26.285  1.00 46.16           O  
ANISOU 1881  OE1 GLU A7015     5179   5801   6557   -435    190  -1017       O  
ATOM   1882  OE2 GLU A7015     107.221  32.257  27.666  1.00 46.15           O  
ANISOU 1882  OE2 GLU A7015     5002   5846   6687   -441     83  -1151       O  
ATOM   1883  N  AGLN A7016     110.525  28.657  28.379  0.50 37.87           N  
ANISOU 1883  N  AGLN A7016     3563   4957   5870   -166    -95  -1346       N  
ATOM   1884  N  BGLN A7016     110.540  28.629  28.374  0.50 37.82           N  
ANISOU 1884  N  BGLN A7016     3554   4950   5864   -164    -95  -1347       N  
ATOM   1885  CA AGLN A7016     110.382  27.737  29.535  0.50 37.50           C  
ANISOU 1885  CA AGLN A7016     3545   4921   5782    -45   -250  -1332       C  
ATOM   1886  CA BGLN A7016     110.360  27.679  29.501  0.50 37.35           C  
ANISOU 1886  CA BGLN A7016     3529   4901   5761    -42   -247  -1329       C  
ATOM   1887  C  AGLN A7016     109.213  28.223  30.395  0.50 35.80           C  
ANISOU 1887  C  AGLN A7016     3478   4680   5444    -53   -313  -1265       C  
ATOM   1888  C  BGLN A7016     109.228  28.201  30.391  0.50 35.77           C  
ANISOU 1888  C  BGLN A7016     3471   4676   5440    -51   -313  -1266       C  
ATOM   1889  O  AGLN A7016     109.302  29.351  30.920  0.50 35.55           O  
ANISOU 1889  O  AGLN A7016     3432   4652   5423   -118   -338  -1297       O  
ATOM   1890  O  BGLN A7016     109.361  29.318  30.927  0.50 35.68           O  
ANISOU 1890  O  BGLN A7016     3441   4670   5444   -115   -341  -1301       O  
ATOM   1891  CB AGLN A7016     111.677  27.712  30.351  0.50 40.12           C  
ANISOU 1891  CB AGLN A7016     3714   5303   6225     -5   -363  -1427       C  
ATOM   1892  CB BGLN A7016     111.674  27.498  30.265  0.50 39.83           C  
ANISOU 1892  CB BGLN A7016     3679   5265   6189      8   -360  -1423       C  
ATOM   1893  CG AGLN A7016     111.720  26.608  31.397  0.50 41.02           C  
ANISOU 1893  CG AGLN A7016     3848   5428   6309    128   -523  -1412       C  
ATOM   1894  CG BGLN A7016     112.796  26.923  29.409  0.50 41.40           C  
ANISOU 1894  CG BGLN A7016     3722   5490   6518     28   -291  -1494       C  
ATOM   1895  CD AGLN A7016     111.897  25.246  30.773  0.50 42.00           C  
ANISOU 1895  CD AGLN A7016     3957   5538   6460    219   -496  -1399       C  
ATOM   1896  CD BGLN A7016     112.466  25.556  28.859  0.50 42.25           C  
ANISOU 1896  CD BGLN A7016     3885   5572   6593    121   -262  -1452       C  
ATOM   1897  OE1AGLN A7016     112.470  25.106  29.694  0.50 43.39           O  
ANISOU 1897  OE1AGLN A7016     4043   5721   6722    195   -379  -1443       O  
ATOM   1898  OE1BGLN A7016     111.474  24.932  29.234  0.50 43.63           O  
ANISOU 1898  OE1BGLN A7016     4207   5713   6655    178   -314  -1369       O  
ATOM   1899  NE2AGLN A7016     111.428  24.221  31.467  0.50 42.60           N  
ANISOU 1899  NE2AGLN A7016     4127   5595   6464    324   -602  -1342       N  
ATOM   1900  NE2BGLN A7016     113.307  25.073  27.959  0.50 43.51           N  
ANISOU 1900  NE2BGLN A7016     3926   5749   6856    133   -173  -1513       N  
ATOM   1901  N   ILE A7017     108.147  27.425  30.502  1.00 33.29           N  
ANISOU 1901  N   ILE A7017     3295   4334   5017      4   -329  -1182       N  
ATOM   1902  CA  ILE A7017     106.973  27.811  31.336  1.00 31.97           C  
ANISOU 1902  CA  ILE A7017     3266   4147   4732      1   -379  -1120       C  
ATOM   1903  C   ILE A7017     106.857  26.851  32.521  1.00 31.30           C  
ANISOU 1903  C   ILE A7017     3227   4076   4588    105   -517  -1098       C  
ATOM   1904  O   ILE A7017     106.920  25.623  32.304  1.00 31.08           O  
ANISOU 1904  O   ILE A7017     3209   4040   4559    180   -533  -1072       O  
ATOM   1905  CB  ILE A7017     105.676  27.840  30.502  1.00 29.77           C  
ANISOU 1905  CB  ILE A7017     3114   3824   4370    -35   -275  -1034       C  
ATOM   1906  CG1 ILE A7017     105.702  28.967  29.468  1.00 30.08           C  
ANISOU 1906  CG1 ILE A7017     3133   3845   4450   -144   -154  -1045       C  
ATOM   1907  CG2 ILE A7017     104.448  27.933  31.400  1.00 29.00           C  
ANISOU 1907  CG2 ILE A7017     3149   3712   4157    -17   -329   -972       C  
ATOM   1908  CD1 ILE A7017     104.512  28.980  28.536  1.00 29.21           C  
ANISOU 1908  CD1 ILE A7017     3139   3694   4265   -177    -61   -962       C  
ATOM   1909  N   ASP A7018     106.732  27.419  33.719  1.00 30.55           N  
ANISOU 1909  N   ASP A7018     3162   3998   4445    104   -613  -1113       N  
ATOM   1910  CA  ASP A7018     106.445  26.656  34.959  1.00 30.64           C  
ANISOU 1910  CA  ASP A7018     3251   4022   4367    189   -744  -1079       C  
ATOM   1911  C   ASP A7018     104.917  26.586  35.050  1.00 28.45           C  
ANISOU 1911  C   ASP A7018     3135   3712   3962    177   -695   -989       C  
ATOM   1912  O   ASP A7018     104.296  27.649  35.260  1.00 26.72           O  
ANISOU 1912  O   ASP A7018     2962   3487   3704    113   -659   -992       O  
ATOM   1913  CB  ASP A7018     107.096  27.325  36.170  1.00 32.85           C  
ANISOU 1913  CB  ASP A7018     3485   4343   4652    188   -867  -1147       C  
ATOM   1914  CG  ASP A7018     106.773  26.667  37.500  1.00 34.43           C  
ANISOU 1914  CG  ASP A7018     3783   4558   4739    264  -1001  -1110       C  
ATOM   1915  OD1 ASP A7018     105.646  26.155  37.653  1.00 33.38           O  
ANISOU 1915  OD1 ASP A7018     3786   4399   4495    283   -975  -1025       O  
ATOM   1916  OD2 ASP A7018     107.658  26.667  38.373  1.00 37.86           O  
ANISOU 1916  OD2 ASP A7018     4155   5032   5195    300  -1133  -1165       O  
ATOM   1917  N   GLY A7019     104.349  25.392  34.868  1.00 27.34           N  
ANISOU 1917  N   GLY A7019     3070   3547   3769    234   -691   -918       N  
ATOM   1918  CA  GLY A7019     102.888  25.178  34.835  1.00 26.46           C  
ANISOU 1918  CA  GLY A7019     3098   3405   3548    220   -637   -832       C  
ATOM   1919  C   GLY A7019     102.169  25.556  36.118  1.00 26.17           C  
ANISOU 1919  C   GLY A7019     3157   3384   3402    220   -697   -811       C  
ATOM   1920  O   GLY A7019     101.039  26.066  36.032  1.00 25.29           O  
ANISOU 1920  O   GLY A7019     3122   3256   3230    175   -627   -774       O  
ATOM   1921  N  ATYR A7020     102.759  25.255  37.280  0.50 27.29           N  
ANISOU 1921  N  ATYR A7020     3298   3556   3513    274   -823   -833       N  
ATOM   1922  N  BTYR A7020     102.786  25.285  37.270  0.50 27.33           N  
ANISOU 1922  N  BTYR A7020     3300   3562   3522    272   -823   -836       N  
ATOM   1923  CA ATYR A7020     102.113  25.637  38.565  0.50 27.76           C  
ANISOU 1923  CA ATYR A7020     3457   3636   3453    270   -878   -821       C  
ATOM   1924  CA BTYR A7020     102.172  25.624  38.580  0.50 27.86           C  
ANISOU 1924  CA BTYR A7020     3466   3650   3468    272   -883   -824       C  
ATOM   1925  C  ATYR A7020     102.028  27.164  38.649  0.50 27.53           C  
ANISOU 1925  C  ATYR A7020     3398   3618   3443    194   -837   -886       C  
ATOM   1926  C  BTYR A7020     102.053  27.149  38.686  0.50 27.63           C  
ANISOU 1926  C  BTYR A7020     3410   3631   3454    196   -842   -887       C  
ATOM   1927  O  ATYR A7020     100.960  27.686  39.022  0.50 27.53           O  
ANISOU 1927  O  ATYR A7020     3487   3611   3361    162   -791   -863       O  
ATOM   1928  O  BTYR A7020     101.000  27.652  39.121  0.50 27.80           O  
ANISOU 1928  O  BTYR A7020     3523   3648   3390    166   -801   -865       O  
ATOM   1929  CB ATYR A7020     102.841  25.021  39.764  0.50 29.65           C  
ANISOU 1929  CB ATYR A7020     3709   3907   3649    340  -1032   -832       C  
ATOM   1930  CB BTYR A7020     103.000  25.007  39.711  0.50 29.78           C  
ANISOU 1930  CB BTYR A7020     3709   3925   3680    344  -1038   -839       C  
ATOM   1931  CG ATYR A7020     102.273  23.702  40.226  0.50 29.96           C  
ANISOU 1931  CG ATYR A7020     3865   3926   3592    403  -1072   -740       C  
ATOM   1932  CG BTYR A7020     103.156  23.512  39.593  0.50 30.30           C  
ANISOU 1932  CG BTYR A7020     3804   3965   3743    424  -1084   -776       C  
ATOM   1933  CD1ATYR A7020     102.649  22.503  39.646  0.50 30.46           C  
ANISOU 1933  CD1ATYR A7020     3908   3956   3709    464  -1087   -702       C  
ATOM   1934  CD1BTYR A7020     104.181  22.959  38.845  0.50 31.08           C  
ANISOU 1934  CD1BTYR A7020     3787   4053   3966    468  -1100   -807       C  
ATOM   1935  CD2ATYR A7020     101.348  23.659  41.256  0.50 30.40           C  
ANISOU 1935  CD2ATYR A7020     4056   3992   3501    397  -1090   -692       C  
ATOM   1936  CD2BTYR A7020     102.261  22.648  40.203  0.50 30.56           C  
ANISOU 1936  CD2BTYR A7020     3978   3978   3653    455  -1102   -687       C  
ATOM   1937  CE1ATYR A7020     102.121  21.295  40.077  0.50 30.81           C  
ANISOU 1937  CE1ATYR A7020     4067   3969   3668    516  -1124   -614       C  
ATOM   1938  CE1BTYR A7020     104.323  21.587  38.716  0.50 31.67           C  
ANISOU 1938  CE1BTYR A7020     3891   4093   4047    548  -1140   -754       C  
ATOM   1939  CE2ATYR A7020     100.808  22.462  41.697  0.50 30.81           C  
ANISOU 1939  CE2ATYR A7020     4223   4021   3462    442  -1119   -602       C  
ATOM   1940  CE2BTYR A7020     102.391  21.273  40.089  0.50 31.11           C  
ANISOU 1940  CE2BTYR A7020     4084   4011   3725    527  -1144   -626       C  
ATOM   1941  CZ ATYR A7020     101.194  21.275  41.105  0.50 30.78           C  
ANISOU 1941  CZ ATYR A7020     4201   3975   3517    501  -1140   -560       C  
ATOM   1942  CZ BTYR A7020     103.424  20.741  39.340  0.50 31.61           C  
ANISOU 1942  CZ BTYR A7020     4034   4057   3917    577  -1166   -661       C  
ATOM   1943  OH ATYR A7020     100.658  20.094  41.539  0.50 31.66           O  
ANISOU 1943  OH ATYR A7020     4433   4052   3542    541  -1169   -467       O  
ATOM   1944  OH BTYR A7020     103.559  19.388  39.218  0.50 33.34           O  
ANISOU 1944  OH BTYR A7020     4290   4228   4147    654  -1207   -607       O  
ATOM   1945  N   VAL A7021     103.104  27.854  38.267  1.00 27.30           N  
ANISOU 1945  N   VAL A7021     3245   3600   3527    164   -846   -966       N  
ATOM   1946  CA  VAL A7021     103.121  29.343  38.304  1.00 26.98           C  
ANISOU 1946  CA  VAL A7021     3174   3558   3519     85   -808  -1032       C  
ATOM   1947  C   VAL A7021     102.129  29.883  37.264  1.00 24.88           C  
ANISOU 1947  C   VAL A7021     2945   3245   3263     28   -667   -989       C  
ATOM   1948  O   VAL A7021     101.367  30.805  37.595  1.00 23.80           O  
ANISOU 1948  O   VAL A7021     2865   3091   3084    -11   -632   -996       O  
ATOM   1949  CB  VAL A7021     104.539  29.894  38.062  1.00 28.16           C  
ANISOU 1949  CB  VAL A7021     3175   3727   3798     57   -844  -1125       C  
ATOM   1950  CG1 VAL A7021     104.521  31.400  37.851  1.00 28.75           C  
ANISOU 1950  CG1 VAL A7021     3221   3779   3922    -35   -783  -1184       C  
ATOM   1951  CG2 VAL A7021     105.494  29.521  39.188  1.00 29.55           C  
ANISOU 1951  CG2 VAL A7021     3309   3953   3965    111  -1002  -1177       C  
ATOM   1952  N   MET A7022     102.106  29.312  36.059  1.00 23.76           N  
ANISOU 1952  N   MET A7022     2776   3079   3171     28   -592   -946       N  
ATOM   1953  CA  MET A7022     101.221  29.896  35.019  1.00 22.76           C  
ANISOU 1953  CA  MET A7022     2682   2909   3054    -28   -469   -905       C  
ATOM   1954  C   MET A7022      99.744  29.695  35.391  1.00 21.79           C  
ANISOU 1954  C   MET A7022     2682   2772   2824    -13   -445   -835       C  
ATOM   1955  O   MET A7022      98.950  30.605  35.102  1.00 20.83           O  
ANISOU 1955  O   MET A7022     2593   2621   2698    -59   -378   -826       O  
ATOM   1956  CB  MET A7022     101.512  29.317  33.633  1.00 22.58           C  
ANISOU 1956  CB  MET A7022     2613   2869   3095    -36   -395   -878       C  
ATOM   1957  CG  MET A7022     100.916  30.162  32.527  1.00 22.43           C  
ANISOU 1957  CG  MET A7022     2612   2810   3100   -107   -284   -852       C  
ATOM   1958  SD  MET A7022     101.577  31.855  32.504  1.00 23.79           S  
ANISOU 1958  SD  MET A7022     2718   2965   3356   -192   -261   -929       S  
ATOM   1959  CE  MET A7022     103.238  31.534  31.917  1.00 25.10           C  
ANISOU 1959  CE  MET A7022     2739   3160   3636   -205   -260   -995       C  
ATOM   1960  N   HIS A7023      99.372  28.562  36.000  1.00 21.70           N  
ANISOU 1960  N   HIS A7023     2734   2778   2733     45   -494   -788       N  
ATOM   1961  CA  HIS A7023      97.951  28.414  36.413  1.00 20.87           C  
ANISOU 1961  CA  HIS A7023     2737   2664   2527     49   -461   -727       C  
ATOM   1962  C   HIS A7023      97.639  29.454  37.498  1.00 21.34           C  
ANISOU 1962  C   HIS A7023     2830   2738   2538     30   -483   -775       C  
ATOM   1963  O   HIS A7023      96.521  30.011  37.482  1.00 20.77           O  
ANISOU 1963  O   HIS A7023     2809   2647   2433      6   -418   -754       O  
ATOM   1964  CB  HIS A7023      97.642  26.984  36.869  1.00 21.01           C  
ANISOU 1964  CB  HIS A7023     2822   2691   2470    106   -504   -664       C  
ATOM   1965  CG  HIS A7023      96.178  26.735  37.005  1.00 20.09           C  
ANISOU 1965  CG  HIS A7023     2799   2562   2270     97   -448   -597       C  
ATOM   1966  ND1 HIS A7023      95.312  26.868  35.933  1.00 19.73           N  
ANISOU 1966  ND1 HIS A7023     2758   2487   2252     63   -356   -556       N  
ATOM   1967  CD2 HIS A7023      95.432  26.332  38.055  1.00 20.38           C  
ANISOU 1967  CD2 HIS A7023     2925   2616   2200    115   -468   -563       C  
ATOM   1968  CE1 HIS A7023      94.087  26.574  36.329  1.00 19.66           C  
ANISOU 1968  CE1 HIS A7023     2824   2477   2166     61   -325   -505       C  
ATOM   1969  NE2 HIS A7023      94.135  26.245  37.632  1.00 19.28           N  
ANISOU 1969  NE2 HIS A7023     2830   2458   2034     89   -385   -509       N  
ATOM   1970  N   ALA A7024      98.592  29.710  38.402  1.00 21.94           N  
ANISOU 1970  N   ALA A7024     2875   2845   2613     43   -574   -842       N  
ATOM   1971  CA  ALA A7024      98.383  30.739  39.450  1.00 22.55           C  
ANISOU 1971  CA  ALA A7024     2988   2937   2642     21   -598   -903       C  
ATOM   1972  C   ALA A7024      98.190  32.100  38.774  1.00 22.26           C  
ANISOU 1972  C   ALA A7024     2913   2857   2685    -40   -520   -942       C  
ATOM   1973  O   ALA A7024      97.316  32.877  39.226  1.00 22.39           O  
ANISOU 1973  O   ALA A7024     2987   2860   2661    -58   -481   -957       O  
ATOM   1974  CB  ALA A7024      99.547  30.758  40.412  1.00 23.69           C  
ANISOU 1974  CB  ALA A7024     3097   3123   2778     41   -721   -973       C  
ATOM   1975  N   ASN A7025      98.978  32.366  37.727  1.00 21.94           N  
ANISOU 1975  N   ASN A7025     2783   2794   2756    -73   -493   -958       N  
ATOM   1976  CA  ASN A7025      98.884  33.639  36.963  1.00 21.92           C  
ANISOU 1976  CA  ASN A7025     2750   2740   2837   -139   -418   -985       C  
ATOM   1977  C   ASN A7025      97.498  33.723  36.313  1.00 21.02           C  
ANISOU 1977  C   ASN A7025     2701   2586   2696   -142   -327   -910       C  
ATOM   1978  O   ASN A7025      96.903  34.817  36.319  1.00 21.16           O  
ANISOU 1978  O   ASN A7025     2745   2564   2731   -173   -284   -929       O  
ATOM   1979  CB  ASN A7025      99.986  33.752  35.907  1.00 22.20           C  
ANISOU 1979  CB  ASN A7025     2684   2763   2986   -177   -396  -1005       C  
ATOM   1980  CG  ASN A7025     101.375  33.894  36.491  1.00 23.50           C  
ANISOU 1980  CG  ASN A7025     2760   2964   3203   -184   -482  -1092       C  
ATOM   1981  OD1 ASN A7025     101.539  34.266  37.656  1.00 24.43           O  
ANISOU 1981  OD1 ASN A7025     2896   3106   3281   -176   -559  -1150       O  
ATOM   1982  ND2 ASN A7025     102.384  33.630  35.676  1.00 24.20           N  
ANISOU 1982  ND2 ASN A7025     2750   3060   3383   -202   -469  -1107       N  
ATOM   1983  N   TYR A7026      97.021  32.597  35.774  1.00 20.15           N  
ANISOU 1983  N   TYR A7026     2616   2486   2553   -111   -305   -832       N  
ATOM   1984  CA  TYR A7026      95.690  32.531  35.121  1.00 19.90           C  
ANISOU 1984  CA  TYR A7026     2638   2424   2497   -113   -230   -759       C  
ATOM   1985  C   TYR A7026      94.587  32.884  36.134  1.00 20.01           C  
ANISOU 1985  C   TYR A7026     2722   2444   2437    -96   -225   -763       C  
ATOM   1986  O   TYR A7026      93.732  33.749  35.847  1.00 20.23           O  
ANISOU 1986  O   TYR A7026     2767   2432   2486   -114   -169   -757       O  
ATOM   1987  CB  TYR A7026      95.469  31.158  34.473  1.00 19.47           C  
ANISOU 1987  CB  TYR A7026     2597   2383   2418    -85   -219   -686       C  
ATOM   1988  CG  TYR A7026      94.026  30.953  34.104  1.00 18.80           C  
ANISOU 1988  CG  TYR A7026     2570   2279   2291    -83   -163   -616       C  
ATOM   1989  CD1 TYR A7026      93.461  31.644  33.048  1.00 18.23           C  
ANISOU 1989  CD1 TYR A7026     2494   2165   2266   -118   -101   -589       C  
ATOM   1990  CD2 TYR A7026      93.208  30.131  34.858  1.00 19.19           C  
ANISOU 1990  CD2 TYR A7026     2679   2354   2255    -50   -176   -579       C  
ATOM   1991  CE1 TYR A7026      92.117  31.519  32.744  1.00 17.94           C  
ANISOU 1991  CE1 TYR A7026     2499   2115   2200   -114    -61   -531       C  
ATOM   1992  CE2 TYR A7026      91.864  29.989  34.563  1.00 18.79           C  
ANISOU 1992  CE2 TYR A7026     2668   2292   2178    -53   -123   -524       C  
ATOM   1993  CZ  TYR A7026      91.317  30.685  33.501  1.00 18.13           C  
ANISOU 1993  CZ  TYR A7026     2568   2169   2149    -83    -70   -502       C  
ATOM   1994  OH  TYR A7026      89.988  30.560  33.224  1.00 18.15           O  
ANISOU 1994  OH  TYR A7026     2598   2164   2133    -83    -30   -451       O  
ATOM   1995  N  AILE A7027      94.616  32.238  37.302  0.60 20.60           N  
ANISOU 1995  N  AILE A7027     2836   2565   2426    -59   -281   -773       N  
ATOM   1996  N  BILE A7027      94.610  32.247  37.306  0.40 20.77           N  
ANISOU 1996  N  BILE A7027     2857   2586   2446    -59   -281   -774       N  
ATOM   1997  CA AILE A7027      93.591  32.497  38.358  0.60 21.01           C  
ANISOU 1997  CA AILE A7027     2958   2632   2392    -45   -267   -783       C  
ATOM   1998  CA BILE A7027      93.565  32.512  38.341  0.40 21.24           C  
ANISOU 1998  CA BILE A7027     2987   2660   2422    -46   -264   -782       C  
ATOM   1999  C  AILE A7027      93.683  33.959  38.812  0.60 21.41           C  
ANISOU 1999  C  AILE A7027     3000   2658   2476    -72   -260   -868       C  
ATOM   2000  C  BILE A7027      93.678  33.959  38.839  0.40 21.64           C  
ANISOU 2000  C  BILE A7027     3030   2688   2503    -71   -261   -869       C  
ATOM   2001  O  AILE A7027      92.623  34.584  39.000  0.60 21.07           O  
ANISOU 2001  O  AILE A7027     2990   2593   2419    -72   -203   -872       O  
ATOM   2002  O  BILE A7027      92.625  34.571  39.096  0.40 21.44           O  
ANISOU 2002  O  BILE A7027     3041   2644   2459    -71   -206   -875       O  
ATOM   2003  CB AILE A7027      93.753  31.510  39.531  0.60 21.76           C  
ANISOU 2003  CB AILE A7027     3107   2782   2377     -8   -332   -776       C  
ATOM   2004  CB BILE A7027      93.653  31.480  39.479  0.40 22.05           C  
ANISOU 2004  CB BILE A7027     3146   2817   2413     -8   -326   -769       C  
ATOM   2005  CG1AILE A7027      93.554  30.061  39.075  0.60 21.57           C  
ANISOU 2005  CG1AILE A7027     3102   2765   2325     16   -334   -687       C  
ATOM   2006  CG1BILE A7027      93.347  30.076  38.954  0.40 21.91           C  
ANISOU 2006  CG1BILE A7027     3148   2804   2371     13   -318   -679       C  
ATOM   2007  CG2AILE A7027      92.821  31.870  40.675  0.60 22.35           C  
ANISOU 2007  CG2AILE A7027     3255   2878   2356     -3   -309   -798       C  
ATOM   2008  CG2BILE A7027      92.742  31.861  40.634  0.40 22.61           C  
ANISOU 2008  CG2BILE A7027     3289   2910   2389     -3   -304   -794       C  
ATOM   2009  CD1AILE A7027      92.187  29.774  38.479  0.60 20.91           C  
ANISOU 2009  CD1AILE A7027     3049   2663   2232      7   -248   -618       C  
ATOM   2010  CD1BILE A7027      93.260  29.028  40.027  0.40 22.68           C  
ANISOU 2010  CD1BILE A7027     3320   2942   2356     47   -369   -648       C  
ATOM   2011  N   PHE A7028      94.900  34.486  38.961  1.00 22.36           N  
ANISOU 2011  N   PHE A7028     3070   2777   2645    -93   -316   -938       N  
ATOM   2012  CA  PHE A7028      95.078  35.896  39.399  1.00 23.15           C  
ANISOU 2012  CA  PHE A7028     3164   2845   2784   -126   -315  -1028       C  
ATOM   2013  C   PHE A7028      94.396  36.820  38.384  1.00 21.72           C  
ANISOU 2013  C   PHE A7028     2974   2590   2688   -154   -230  -1006       C  
ATOM   2014  O   PHE A7028      93.678  37.751  38.784  1.00 21.90           O  
ANISOU 2014  O   PHE A7028     3030   2578   2712   -156   -195  -1044       O  
ATOM   2015  CB  PHE A7028      96.558  36.238  39.573  1.00 25.02           C  
ANISOU 2015  CB  PHE A7028     3336   3093   3077   -155   -389  -1103       C  
ATOM   2016  CG  PHE A7028      96.803  37.686  39.902  1.00 26.84           C  
ANISOU 2016  CG  PHE A7028     3557   3278   3360   -200   -387  -1197       C  
ATOM   2017  CD1 PHE A7028      96.434  38.201  41.133  1.00 28.78           C  
ANISOU 2017  CD1 PHE A7028     3864   3538   3532   -190   -411  -1267       C  
ATOM   2018  CD2 PHE A7028      97.418  38.530  38.990  1.00 28.52           C  
ANISOU 2018  CD2 PHE A7028     3707   3433   3696   -257   -359  -1218       C  
ATOM   2019  CE1 PHE A7028      96.662  39.533  41.443  1.00 30.23           C  
ANISOU 2019  CE1 PHE A7028     4044   3672   3768   -232   -410  -1362       C  
ATOM   2020  CE2 PHE A7028      97.643  39.863  39.302  1.00 29.42           C  
ANISOU 2020  CE2 PHE A7028     3819   3493   3863   -303   -358  -1305       C  
ATOM   2021  CZ  PHE A7028      97.258  40.362  40.522  1.00 30.35           C  
ANISOU 2021  CZ  PHE A7028     3997   3621   3913   -289   -385  -1379       C  
ATOM   2022  N   TRP A7029      94.652  36.586  37.101  1.00 20.98           N  
ANISOU 2022  N   TRP A7029     2836   2470   2664   -174   -200   -948       N  
ATOM   2023  CA  TRP A7029      93.977  37.362  36.030  1.00 21.12           C  
ANISOU 2023  CA  TRP A7029     2855   2416   2752   -199   -128   -909       C  
ATOM   2024  C   TRP A7029      92.450  37.258  36.187  1.00 20.40           C  
ANISOU 2024  C   TRP A7029     2818   2320   2613   -160    -83   -864       C  
ATOM   2025  O   TRP A7029      91.780  38.309  36.245  1.00 20.76           O  
ANISOU 2025  O   TRP A7029     2881   2312   2694   -162    -48   -888       O  
ATOM   2026  CB  TRP A7029      94.445  36.880  34.651  1.00 20.81           C  
ANISOU 2026  CB  TRP A7029     2776   2365   2764   -224   -104   -845       C  
ATOM   2027  CG  TRP A7029      93.591  37.408  33.548  1.00 20.92           C  
ANISOU 2027  CG  TRP A7029     2810   2317   2822   -240    -41   -783       C  
ATOM   2028  CD1 TRP A7029      93.284  38.716  33.304  1.00 22.15           C  
ANISOU 2028  CD1 TRP A7029     2978   2397   3039   -266    -11   -800       C  
ATOM   2029  CD2 TRP A7029      92.934  36.640  32.528  1.00 20.49           C  
ANISOU 2029  CD2 TRP A7029     2768   2265   2750   -230     -8   -692       C  
ATOM   2030  NE1 TRP A7029      92.462  38.810  32.215  1.00 21.60           N  
ANISOU 2030  NE1 TRP A7029     2930   2285   2989   -267     31   -720       N  
ATOM   2031  CE2 TRP A7029      92.234  37.555  31.716  1.00 20.73           C  
ANISOU 2031  CE2 TRP A7029     2819   2226   2829   -248     33   -656       C  
ATOM   2032  CE3 TRP A7029      92.880  35.274  32.220  1.00 20.27           C  
ANISOU 2032  CE3 TRP A7029     2741   2287   2673   -207    -15   -641       C  
ATOM   2033  CZ2 TRP A7029      91.488  37.142  30.612  1.00 20.77           C  
ANISOU 2033  CZ2 TRP A7029     2843   2219   2828   -246     61   -570       C  
ATOM   2034  CZ3 TRP A7029      92.141  34.869  31.131  1.00 20.01           C  
ANISOU 2034  CZ3 TRP A7029     2727   2239   2636   -210     20   -563       C  
ATOM   2035  CH2 TRP A7029      91.456  35.794  30.341  1.00 20.06           C  
ANISOU 2035  CH2 TRP A7029     2752   2185   2685   -230     55   -528       C  
ATOM   2036  N   ARG A7030      91.912  36.038  36.259  1.00 20.27           N  
ANISOU 2036  N   ARG A7030     2822   2354   2525   -127    -82   -803       N  
ATOM   2037  CA  ARG A7030      90.435  35.865  36.387  1.00 20.01           C  
ANISOU 2037  CA  ARG A7030     2826   2323   2452    -98    -34   -760       C  
ATOM   2038  C   ARG A7030      89.902  36.551  37.654  1.00 20.86           C  
ANISOU 2038  C   ARG A7030     2968   2438   2518    -79    -24   -832       C  
ATOM   2039  O   ARG A7030      88.806  37.146  37.583  1.00 21.03           O  
ANISOU 2039  O   ARG A7030     2998   2427   2563    -64     27   -829       O  
ATOM   2040  CB  ARG A7030      90.059  34.381  36.417  1.00 19.59           C  
ANISOU 2040  CB  ARG A7030     2792   2324   2324    -75    -39   -693       C  
ATOM   2041  CG  ARG A7030      90.405  33.599  35.154  1.00 19.14           C  
ANISOU 2041  CG  ARG A7030     2711   2260   2301    -89    -40   -624       C  
ATOM   2042  CD  ARG A7030      89.853  34.204  33.879  1.00 18.93           C  
ANISOU 2042  CD  ARG A7030     2667   2178   2345   -109      3   -582       C  
ATOM   2043  NE  ARG A7030      88.443  34.553  33.993  1.00 18.94           N  
ANISOU 2043  NE  ARG A7030     2686   2166   2344    -90     43   -561       N  
ATOM   2044  CZ  ARG A7030      87.431  33.704  33.852  1.00 19.42           C  
ANISOU 2044  CZ  ARG A7030     2758   2251   2366    -76     63   -503       C  
ATOM   2045  NH1 ARG A7030      87.648  32.427  33.583  1.00 19.11           N  
ANISOU 2045  NH1 ARG A7030     2729   2246   2286    -78     47   -458       N  
ATOM   2046  NH2 ARG A7030      86.193  34.141  33.990  1.00 20.75           N  
ANISOU 2046  NH2 ARG A7030     2926   2409   2547    -58     99   -496       N  
ATOM   2047  N   ASN A7031      90.624  36.446  38.774  1.00 21.40           N  
ANISOU 2047  N   ASN A7031     3056   2549   2524    -77    -74   -897       N  
ATOM   2048  CA  ASN A7031      90.168  37.033  40.065  1.00 23.05           C  
ANISOU 2048  CA  ASN A7031     3311   2774   2672    -62    -64   -974       C  
ATOM   2049  C   ASN A7031      90.144  38.561  40.036  1.00 23.73           C  
ANISOU 2049  C   ASN A7031     3386   2789   2841    -77    -41  -1051       C  
ATOM   2050  O   ASN A7031      89.327  39.140  40.793  1.00 24.20           O  
ANISOU 2050  O   ASN A7031     3480   2842   2873    -57      0  -1103       O  
ATOM   2051  CB  ASN A7031      91.057  36.610  41.238  1.00 24.13           C  
ANISOU 2051  CB  ASN A7031     3479   2973   2716    -60   -138  -1027       C  
ATOM   2052  CG  ASN A7031      90.746  35.219  41.739  1.00 24.87           C  
ANISOU 2052  CG  ASN A7031     3618   3134   2696    -35   -151   -964       C  
ATOM   2053  OD1 ASN A7031      89.708  34.655  41.401  1.00 26.80           O  
ANISOU 2053  OD1 ASN A7031     3874   3382   2924    -23    -92   -895       O  
ATOM   2054  ND2 ASN A7031      91.629  34.667  42.552  1.00 25.54           N  
ANISOU 2054  ND2 ASN A7031     3729   3269   2706    -29   -233   -987       N  
ATOM   2055  N   THR A7032      90.987  39.186  39.211  1.00 23.64           N  
ANISOU 2055  N   THR A7032     3332   2721   2928   -113    -61  -1059       N  
ATOM   2056  CA  THR A7032      91.118  40.665  39.243  1.00 24.44           C  
ANISOU 2056  CA  THR A7032     3432   2743   3112   -136    -48  -1136       C  
ATOM   2057  C   THR A7032      90.531  41.311  37.986  1.00 25.03           C  
ANISOU 2057  C   THR A7032     3488   2730   3291   -142      2  -1077       C  
ATOM   2058  O   THR A7032      90.531  42.553  37.930  1.00 25.86           O  
ANISOU 2058  O   THR A7032     3599   2753   3473   -157     17  -1129       O  
ATOM   2059  CB  THR A7032      92.585  41.056  39.454  1.00 25.03           C  
ANISOU 2059  CB  THR A7032     3477   2813   3218   -185   -113  -1206       C  
ATOM   2060  OG1 THR A7032      93.364  40.548  38.371  1.00 23.85           O  
ANISOU 2060  OG1 THR A7032     3275   2664   3121   -214   -127  -1142       O  
ATOM   2061  CG2 THR A7032      93.133  40.537  40.766  1.00 26.04           C  
ANISOU 2061  CG2 THR A7032     3629   3022   3240   -174   -179  -1270       C  
ATOM   2062  N   ASN A7033      90.040  40.512  37.038  1.00 24.20           N  
ANISOU 2062  N   ASN A7033     3369   2639   3186   -130     23   -974       N  
ATOM   2063  CA  ASN A7033      89.466  41.074  35.788  1.00 25.46           C  
ANISOU 2063  CA  ASN A7033     3519   2720   3433   -135     59   -908       C  
ATOM   2064  C   ASN A7033      88.094  40.478  35.525  1.00 25.55           C  
ANISOU 2064  C   ASN A7033     3535   2754   3418    -88     95   -838       C  
ATOM   2065  O   ASN A7033      87.974  39.512  34.770  1.00 24.31           O  
ANISOU 2065  O   ASN A7033     3366   2631   3238    -92     93   -756       O  
ATOM   2066  CB  ASN A7033      90.357  40.821  34.576  1.00 26.12           C  
ANISOU 2066  CB  ASN A7033     3575   2788   3559   -183     47   -849       C  
ATOM   2067  CG  ASN A7033      91.664  41.566  34.680  1.00 28.62           C  
ANISOU 2067  CG  ASN A7033     3873   3071   3929   -239     22   -917       C  
ATOM   2068  OD1 ASN A7033      92.496  41.262  35.538  1.00 29.86           O  
ANISOU 2068  OD1 ASN A7033     4015   3282   4047   -248    -19   -982       O  
ATOM   2069  ND2 ASN A7033      91.847  42.536  33.802  1.00 29.85           N  
ANISOU 2069  ND2 ASN A7033     4030   3136   4173   -279     44   -900       N  
ATOM   2070  N   PRO A7034      87.031  41.026  36.141  1.00 27.26           N  
ANISOU 2070  N   PRO A7034     3763   2952   3639    -46    130   -874       N  
ATOM   2071  CA  PRO A7034      85.681  40.547  35.882  1.00 27.90           C  
ANISOU 2071  CA  PRO A7034     3834   3055   3712     -4    165   -815       C  
ATOM   2072  C   PRO A7034      85.404  40.692  34.384  1.00 27.10           C  
ANISOU 2072  C   PRO A7034     3715   2896   3684    -13    160   -723       C  
ATOM   2073  O   PRO A7034      85.720  41.719  33.818  1.00 28.26           O  
ANISOU 2073  O   PRO A7034     3868   2957   3910    -28    153   -727       O  
ATOM   2074  CB  PRO A7034      84.769  41.465  36.707  1.00 29.28           C  
ANISOU 2074  CB  PRO A7034     4013   3197   3913     39    207   -889       C  
ATOM   2075  CG  PRO A7034      85.679  42.044  37.765  1.00 30.57           C  
ANISOU 2075  CG  PRO A7034     4207   3358   4048     20    191   -997       C  
ATOM   2076  CD  PRO A7034      87.060  42.104  37.141  1.00 29.72           C  
ANISOU 2076  CD  PRO A7034     4095   3227   3967    -35    139   -983       C  
ATOM   2077  N   ILE A7035      84.846  39.652  33.784  1.00 26.61           N  
ANISOU 2077  N   ILE A7035     3639   2881   3590     -8    162   -642       N  
ATOM   2078  CA  ILE A7035      84.512  39.710  32.335  1.00 26.45           C  
ANISOU 2078  CA  ILE A7035     3610   2815   3623    -17    150   -552       C  
ATOM   2079  C   ILE A7035      82.993  39.795  32.238  1.00 27.08           C  
ANISOU 2079  C   ILE A7035     3664   2890   3734     32    170   -524       C  
ATOM   2080  O   ILE A7035      82.313  38.962  32.874  1.00 27.87           O  
ANISOU 2080  O   ILE A7035     3746   3061   3779     51    193   -528       O  
ATOM   2081  CB  ILE A7035      85.121  38.508  31.591  1.00 25.68           C  
ANISOU 2081  CB  ILE A7035     3516   2769   3473    -55    130   -488       C  
ATOM   2082  CG1 ILE A7035      86.649  38.524  31.693  1.00 25.79           C  
ANISOU 2082  CG1 ILE A7035     3538   2785   3475    -99    112   -526       C  
ATOM   2083  CG2 ILE A7035      84.647  38.475  30.148  1.00 25.34           C  
ANISOU 2083  CG2 ILE A7035     3473   2691   3464    -65    119   -399       C  
ATOM   2084  CD1 ILE A7035      87.317  37.242  31.233  1.00 26.11           C  
ANISOU 2084  CD1 ILE A7035     3575   2884   3461   -125     97   -485       C  
ATOM   2085  N   GLN A7036      82.498  40.801  31.513  1.00 27.52           N  
ANISOU 2085  N   GLN A7036     3716   2861   3878     53    161   -499       N  
ATOM   2086  CA  GLN A7036      81.039  41.012  31.344  1.00 28.90           C  
ANISOU 2086  CA  GLN A7036     3853   3023   4105    110    169   -475       C  
ATOM   2087  C   GLN A7036      80.478  39.862  30.504  1.00 26.37           C  
ANISOU 2087  C   GLN A7036     3512   2759   3748     97    150   -387       C  
ATOM   2088  O   GLN A7036      81.008  39.621  29.406  1.00 26.04           O  
ANISOU 2088  O   GLN A7036     3496   2701   3695     58    116   -320       O  
ATOM   2089  CB  GLN A7036      80.780  42.372  30.686  1.00 32.46           C  
ANISOU 2089  CB  GLN A7036     4313   3356   4662    137    148   -461       C  
ATOM   2090  CG  GLN A7036      79.319  42.647  30.351  1.00 36.70           C  
ANISOU 2090  CG  GLN A7036     4801   3870   5270    203    140   -430       C  
ATOM   2091  CD  GLN A7036      79.116  43.983  29.670  1.00 40.94           C  
ANISOU 2091  CD  GLN A7036     5359   4281   5915    236    106   -407       C  
ATOM   2092  OE1 GLN A7036      79.957  44.876  29.739  1.00 46.12           O  
ANISOU 2092  OE1 GLN A7036     6064   4858   6601    215    106   -439       O  
ATOM   2093  NE2 GLN A7036      77.981  44.135  29.006  1.00 43.91           N  
ANISOU 2093  NE2 GLN A7036     5696   4632   6353    288     73   -350       N  
ATOM   2094  N   LEU A7037      79.476  39.156  31.028  1.00 24.64           N  
ANISOU 2094  N   LEU A7037     3249   2606   3506    122    176   -392       N  
ATOM   2095  CA  LEU A7037      78.809  38.094  30.235  1.00 24.16           C  
ANISOU 2095  CA  LEU A7037     3164   2594   3421    108    155   -313       C  
ATOM   2096  C   LEU A7037      78.267  38.729  28.955  1.00 23.65           C  
ANISOU 2096  C   LEU A7037     3089   2463   3432    126    104   -246       C  
ATOM   2097  O   LEU A7037      77.643  39.819  29.048  1.00 23.51           O  
ANISOU 2097  O   LEU A7037     3046   2383   3502    180    102   -268       O  
ATOM   2098  CB  LEU A7037      77.675  37.490  31.062  1.00 25.55           C  
ANISOU 2098  CB  LEU A7037     3284   2838   3584    132    200   -338       C  
ATOM   2099  CG  LEU A7037      78.103  36.493  32.134  1.00 26.60           C  
ANISOU 2099  CG  LEU A7037     3441   3049   3617    103    242   -373       C  
ATOM   2100  CD1 LEU A7037      77.006  36.318  33.170  1.00 29.17           C  
ANISOU 2100  CD1 LEU A7037     3719   3426   3938    129    307   -418       C  
ATOM   2101  CD2 LEU A7037      78.468  35.163  31.504  1.00 25.95           C  
ANISOU 2101  CD2 LEU A7037     3382   3010   3468     52    214   -306       C  
ATOM   2102  N   SER A7038      78.493  38.091  27.809  1.00 22.10           N  
ANISOU 2102  N   SER A7038     2917   2275   3202     85     62   -170       N  
ATOM   2103  CA  SER A7038      77.997  38.688  26.546  1.00 22.49           C  
ANISOU 2103  CA  SER A7038     2972   2263   3308     99      4    -98       C  
ATOM   2104  C   SER A7038      77.789  37.635  25.459  1.00 21.39           C  
ANISOU 2104  C   SER A7038     2843   2168   3115     58    -37    -22       C  
ATOM   2105  O   SER A7038      78.643  36.741  25.302  1.00 20.74           O  
ANISOU 2105  O   SER A7038     2797   2126   2954      5    -24    -15       O  
ATOM   2106  CB  SER A7038      78.932  39.748  26.051  1.00 22.94           C  
ANISOU 2106  CB  SER A7038     3091   2231   3391     83    -10    -88       C  
ATOM   2107  OG  SER A7038      78.504  40.220  24.784  1.00 24.31           O  
ANISOU 2107  OG  SER A7038     3288   2347   3599     89    -71     -6       O  
ATOM   2108  N  ASER A7039      76.663  37.736  24.752  0.60 21.83           N  
ANISOU 2108  N  ASER A7039     2862   2214   3217     87    -88     27       N  
ATOM   2109  N  BSER A7039      76.691  37.803  24.715  0.40 21.91           N  
ANISOU 2109  N  BSER A7039     2875   2219   3229     88    -90     29       N  
ATOM   2110  CA ASER A7039      76.285  36.841  23.628  0.60 21.67           C  
ANISOU 2110  CA ASER A7039     2850   2230   3151     51   -141     98       C  
ATOM   2111  CA BSER A7039      76.331  36.968  23.543  0.40 21.70           C  
ANISOU 2111  CA BSER A7039     2861   2225   3160     52   -145    102       C  
ATOM   2112  C  ASER A7039      76.363  37.620  22.310  0.60 21.79           C  
ANISOU 2112  C  ASER A7039     2921   2173   3183     49   -211    172       C  
ATOM   2113  C  BSER A7039      76.352  37.846  22.284  0.40 22.13           C  
ANISOU 2113  C  BSER A7039     2967   2202   3238     56   -215    174       C  
ATOM   2114  O  ASER A7039      76.054  37.032  21.254  0.60 21.71           O  
ANISOU 2114  O  ASER A7039     2932   2186   3131     19   -266    234       O  
ATOM   2115  O  BSER A7039      75.864  37.374  21.243  0.40 22.14           O  
ANISOU 2115  O  BSER A7039     2979   2221   3211     37   -277    238       O  
ATOM   2116  CB ASER A7039      74.893  36.322  23.840  0.60 22.67           C  
ANISOU 2116  CB ASER A7039     2887   2408   3316     79   -156     98       C  
ATOM   2117  CB BSER A7039      74.972  36.326  23.720  0.40 22.31           C  
ANISOU 2117  CB BSER A7039     2850   2359   3266     75   -160    104       C  
ATOM   2118  OG ASER A7039      73.983  37.410  23.938  0.60 24.54           O  
ANISOU 2118  OG ASER A7039     3068   2596   3660    152   -182     93       O  
ATOM   2119  OG BSER A7039      74.946  35.453  24.841  0.40 22.22           O  
ANISOU 2119  OG BSER A7039     2804   2417   3220     61    -92     48       O  
ATOM   2120  N  ATYR A7040      76.790  38.895  22.382  0.50 21.97           N  
ANISOU 2120  N  ATYR A7040     2978   2110   3259     75   -208    166       N  
ATOM   2121  N  BTYR A7040      76.899  39.070  22.367  0.50 22.42           N  
ANISOU 2121  N  BTYR A7040     3043   2154   3321     75   -208    166       N  
ATOM   2122  CA ATYR A7040      76.777  39.835  21.222  0.50 22.53           C  
ANISOU 2122  CA ATYR A7040     3109   2094   3355     80   -275    242       C  
ATOM   2123  CA BTYR A7040      76.871  39.968  21.182  0.50 23.20           C  
ANISOU 2123  CA BTYR A7040     3204   2169   3443     79   -275    245       C  
ATOM   2124  C  ATYR A7040      77.397  39.231  19.948  0.50 22.33           C  
ANISOU 2124  C  ATYR A7040     3166   2086   3231      5   -303    312       C  
ATOM   2125  C  BTYR A7040      77.440  39.303  19.924  0.50 22.71           C  
ANISOU 2125  C  BTYR A7040     3219   2128   3280      5   -303    314       C  
ATOM   2126  O  ATYR A7040      76.753  39.345  18.884  0.50 22.67           O  
ANISOU 2126  O  ATYR A7040     3234   2110   3268     11   -382    388       O  
ATOM   2127  O  BTYR A7040      76.808  39.432  18.855  0.50 22.94           O  
ANISOU 2127  O  BTYR A7040     3274   2138   3304     10   -382    390       O  
ATOM   2128  CB ATYR A7040      77.493  41.159  21.524  0.50 22.88           C  
ANISOU 2128  CB ATYR A7040     3199   2038   3453     93   -250    221       C  
ATOM   2129  CB BTYR A7040      77.686  41.239  21.403  0.50 23.94           C  
ANISOU 2129  CB BTYR A7040     3351   2164   3582     83   -249    227       C  
ATOM   2130  CG ATYR A7040      76.963  41.989  22.672  0.50 23.09           C  
ANISOU 2130  CG ATYR A7040     3164   2026   3580    168   -223    148       C  
ATOM   2131  CG BTYR A7040      77.932  41.990  20.120  0.50 24.77           C  
ANISOU 2131  CG BTYR A7040     3546   2183   3680     60   -305    318       C  
ATOM   2132  CD1ATYR A7040      75.693  41.799  23.193  0.50 23.34           C  
ANISOU 2132  CD1ATYR A7040     3100   2095   3671    234   -233    121       C  
ATOM   2133  CD1BTYR A7040      76.975  42.843  19.595  0.50 26.14           C  
ANISOU 2133  CD1BTYR A7040     3720   2282   3928    123   -384    376       C  
ATOM   2134  CD2ATYR A7040      77.688  43.074  23.142  0.50 23.53           C  
ANISOU 2134  CD2ATYR A7040     3260   1997   3683    172   -190    106       C  
ATOM   2135  CD2BTYR A7040      79.103  41.810  19.402  0.50 24.68           C  
ANISOU 2135  CD2BTYR A7040     3621   2169   3587    -23   -280    351       C  
ATOM   2136  CE1ATYR A7040      75.212  42.583  24.231  0.50 23.96           C  
ANISOU 2136  CE1ATYR A7040     3123   2137   3840    305   -198     45       C  
ATOM   2137  CE1BTYR A7040      77.191  43.525  18.409  0.50 26.87           C  
ANISOU 2137  CE1BTYR A7040     3911   2294   4005    100   -441    471       C  
ATOM   2138  CE2ATYR A7040      77.213  43.885  24.160  0.50 23.90           C  
ANISOU 2138  CE2ATYR A7040     3259   2000   3822    242   -164     32       C  
ATOM   2139  CE2BTYR A7040      79.334  42.481  18.212  0.50 25.70           C  
ANISOU 2139  CE2BTYR A7040     3844   2223   3697    -54   -323    439       C  
ATOM   2140  CZ ATYR A7040      75.971  43.635  24.713  0.50 24.45           C  
ANISOU 2140  CZ ATYR A7040     3233   2114   3940    311   -164      0       C  
ATOM   2141  CZ BTYR A7040      78.372  43.342  17.713  0.50 26.87           C  
ANISOU 2141  CZ BTYR A7040     4006   2292   3910      6   -406    504       C  
ATOM   2142  OH ATYR A7040      75.495  44.432  25.716  0.50 25.37           O  
ANISOU 2142  OH ATYR A7040     3302   2190   4145    381   -129    -82       O  
ATOM   2143  OH BTYR A7040      78.588  44.020  16.548  0.50 28.54           O  
ANISOU 2143  OH BTYR A7040     4325   2424   4094    -24   -453    601       O  
ATOM   2144  N   SER A7041      78.594  38.638  20.038  1.00 21.64           N  
ANISOU 2144  N   SER A7041     3121   2032   3069    -58   -243    285       N  
ATOM   2145  CA  SER A7041      79.293  38.094  18.837  1.00 21.89           C  
ANISOU 2145  CA  SER A7041     3232   2079   3005   -130   -252    339       C  
ATOM   2146  C   SER A7041      78.495  36.984  18.136  1.00 22.50           C  
ANISOU 2146  C   SER A7041     3298   2222   3026   -144   -304    376       C  
ATOM   2147  O   SER A7041      78.771  36.726  16.946  1.00 22.82           O  
ANISOU 2147  O   SER A7041     3413   2264   2992   -194   -332    431       O  
ATOM   2148  CB  SER A7041      80.682  37.622  19.192  1.00 21.13           C  
ANISOU 2148  CB  SER A7041     3159   2011   2858   -185   -175    288       C  
ATOM   2149  OG  SER A7041      80.641  36.361  19.844  1.00 19.84           O  
ANISOU 2149  OG  SER A7041     2947   1931   2659   -188   -147    240       O  
ATOM   2150  N   LEU A7042      77.530  36.377  18.825  1.00 22.58           N  
ANISOU 2150  N   LEU A7042     3222   2285   3070   -107   -313    344       N  
ATOM   2151  CA  LEU A7042      76.761  35.241  18.246  1.00 23.33           C  
ANISOU 2151  CA  LEU A7042     3298   2445   3120   -129   -360    370       C  
ATOM   2152  C   LEU A7042      75.805  35.731  17.154  1.00 24.80           C  
ANISOU 2152  C   LEU A7042     3497   2602   3323   -109   -464    445       C  
ATOM   2153  O   LEU A7042      75.399  34.902  16.323  1.00 25.83           O  
ANISOU 2153  O   LEU A7042     3644   2775   3393   -145   -516    477       O  
ATOM   2154  CB  LEU A7042      75.953  34.557  19.352  1.00 22.96           C  
ANISOU 2154  CB  LEU A7042     3150   2457   3115   -100   -334    316       C  
ATOM   2155  CG  LEU A7042      76.715  34.041  20.570  1.00 22.99           C  
ANISOU 2155  CG  LEU A7042     3139   2493   3102   -110   -244    244       C  
ATOM   2156  CD1 LEU A7042      75.745  33.349  21.513  1.00 23.43           C  
ANISOU 2156  CD1 LEU A7042     3106   2605   3188    -90   -223    207       C  
ATOM   2157  CD2 LEU A7042      77.841  33.095  20.175  1.00 22.93           C  
ANISOU 2157  CD2 LEU A7042     3198   2511   3000   -174   -213    240       C  
ATOM   2158  N   PHE A7043      75.453  37.021  17.155  1.00 24.99           N  
ANISOU 2158  N   PHE A7043     3516   2551   3425    -53   -501    472       N  
ATOM   2159  CA  PHE A7043      74.447  37.594  16.223  1.00 26.38           C  
ANISOU 2159  CA  PHE A7043     3696   2691   3634    -16   -616    547       C  
ATOM   2160  C   PHE A7043      75.043  37.929  14.850  1.00 28.35           C  
ANISOU 2160  C   PHE A7043     4078   2897   3795    -66   -662    630       C  
ATOM   2161  O   PHE A7043      74.239  38.216  13.952  1.00 33.02           O  
ANISOU 2161  O   PHE A7043     4689   3470   4388    -45   -771    701       O  
ATOM   2162  CB  PHE A7043      73.756  38.784  16.891  1.00 26.55           C  
ANISOU 2162  CB  PHE A7043     3651   2647   3789     76   -634    535       C  
ATOM   2163  CG  PHE A7043      72.818  38.382  18.000  1.00 26.11           C  
ANISOU 2163  CG  PHE A7043     3458   2647   3815    126   -607    464       C  
ATOM   2164  CD1 PHE A7043      73.288  38.154  19.283  1.00 25.24           C  
ANISOU 2164  CD1 PHE A7043     3309   2564   3716    124   -499    379       C  
ATOM   2165  CD2 PHE A7043      71.467  38.198  17.750  1.00 26.77           C  
ANISOU 2165  CD2 PHE A7043     3450   2760   3958    169   -688    483       C  
ATOM   2166  CE1 PHE A7043      72.423  37.764  20.295  1.00 25.46           C  
ANISOU 2166  CE1 PHE A7043     3220   2647   3804    161   -463    317       C  
ATOM   2167  CE2 PHE A7043      70.604  37.813  18.765  1.00 26.76           C  
ANISOU 2167  CE2 PHE A7043     3318   2816   4034    205   -649    416       C  
ATOM   2168  CZ  PHE A7043      71.083  37.596  20.034  1.00 25.97           C  
ANISOU 2168  CZ  PHE A7043     3191   2741   3934    199   -531    335       C  
ATOM   2169  N   ASP A7044      76.370  37.927  14.689  1.00 28.17           N  
ANISOU 2169  N   ASP A7044     4141   2859   3700   -129   -586    623       N  
ATOM   2170  CA  ASP A7044      76.954  38.200  13.345  1.00 29.47           C  
ANISOU 2170  CA  ASP A7044     4438   2990   3768   -189   -614    701       C  
ATOM   2171  C   ASP A7044      77.824  37.010  12.948  1.00 27.55           C  
ANISOU 2171  C   ASP A7044     4241   2819   3407   -273   -552    673       C  
ATOM   2172  O   ASP A7044      78.977  36.931  13.428  1.00 27.22           O  
ANISOU 2172  O   ASP A7044     4210   2777   3352   -307   -451    623       O  
ATOM   2173  CB  ASP A7044      77.762  39.500  13.292  1.00 31.71           C  
ANISOU 2173  CB  ASP A7044     4795   3173   4079   -194   -580    730       C  
ATOM   2174  CG  ASP A7044      78.271  39.824  11.896  1.00 34.37           C  
ANISOU 2174  CG  ASP A7044     5274   3472   4312   -259   -606    819       C  
ATOM   2175  OD1 ASP A7044      78.005  39.028  10.960  1.00 34.00           O  
ANISOU 2175  OD1 ASP A7044     5272   3482   4164   -299   -653    855       O  
ATOM   2176  OD2 ASP A7044      78.907  40.880  11.744  1.00 40.65           O  
ANISOU 2176  OD2 ASP A7044     6140   4179   5125   -275   -579    854       O  
ATOM   2177  N   MET A7045      77.276  36.130  12.107  1.00 26.80           N  
ANISOU 2177  N   MET A7045     4168   2779   3235   -301   -614    700       N  
ATOM   2178  CA  MET A7045      77.970  34.901  11.650  1.00 26.29           C  
ANISOU 2178  CA  MET A7045     4148   2780   3059   -376   -562    668       C  
ATOM   2179  C   MET A7045      78.429  35.062  10.198  1.00 27.14           C  
ANISOU 2179  C   MET A7045     4394   2872   3045   -441   -584    735       C  
ATOM   2180  O   MET A7045      78.884  34.061   9.625  1.00 26.79           O  
ANISOU 2180  O   MET A7045     4396   2880   2900   -502   -552    712       O  
ATOM   2181  CB  MET A7045      77.019  33.705  11.763  1.00 25.97           C  
ANISOU 2181  CB  MET A7045     4038   2813   3015   -371   -610    639       C  
ATOM   2182  CG  MET A7045      76.627  33.405  13.191  1.00 25.40           C  
ANISOU 2182  CG  MET A7045     3841   2765   3045   -322   -570    571       C  
ATOM   2183  SD  MET A7045      78.030  32.799  14.154  1.00 23.87           S  
ANISOU 2183  SD  MET A7045     3641   2592   2836   -349   -432    488       S  
ATOM   2184  CE  MET A7045      78.199  31.154  13.464  1.00 23.23           C  
ANISOU 2184  CE  MET A7045     3600   2577   2648   -416   -426    465       C  
ATOM   2185  N   SER A7046      78.362  36.285   9.652  1.00 29.11           N  
ANISOU 2185  N   SER A7046     4712   3046   3301   -430   -630    814       N  
ATOM   2186  CA  SER A7046      78.721  36.520   8.228  1.00 30.57           C  
ANISOU 2186  CA  SER A7046     5045   3213   3358   -496   -656    892       C  
ATOM   2187  C   SER A7046      80.180  36.134   7.938  1.00 31.41           C  
ANISOU 2187  C   SER A7046     5220   3339   3375   -581   -524    853       C  
ATOM   2188  O   SER A7046      80.442  35.703   6.800  1.00 34.06           O  
ANISOU 2188  O   SER A7046     5660   3702   3576   -648   -526    882       O  
ATOM   2189  CB  SER A7046      78.443  37.949   7.811  1.00 31.93           C  
ANISOU 2189  CB  SER A7046     5282   3287   3560   -467   -723    988       C  
ATOM   2190  OG  SER A7046      79.259  38.858   8.529  1.00 31.52           O  
ANISOU 2190  OG  SER A7046     5221   3166   3586   -461   -635    969       O  
ATOM   2191  N   LYS A7047      81.096  36.309   8.894  1.00 30.16           N  
ANISOU 2191  N   LYS A7047     5006   3168   3286   -579   -416    788       N  
ATOM   2192  CA  LYS A7047      82.530  35.979   8.653  1.00 31.75           C  
ANISOU 2192  CA  LYS A7047     5253   3388   3420   -655   -289    745       C  
ATOM   2193  C   LYS A7047      82.953  34.786   9.518  1.00 28.87           C  
ANISOU 2193  C   LYS A7047     4793   3093   3081   -646   -222    639       C  
ATOM   2194  O   LYS A7047      84.149  34.675   9.837  1.00 29.34           O  
ANISOU 2194  O   LYS A7047     4840   3160   3146   -679   -116    583       O  
ATOM   2195  CB  LYS A7047      83.387  37.214   8.944  1.00 34.88           C  
ANISOU 2195  CB  LYS A7047     5671   3707   3873   -671   -223    760       C  
ATOM   2196  CG  LYS A7047      83.071  38.425   8.075  1.00 39.29           C  
ANISOU 2196  CG  LYS A7047     6341   4182   4406   -685   -283    872       C  
ATOM   2197  CD  LYS A7047      83.946  39.620   8.371  1.00 43.42           C  
ANISOU 2197  CD  LYS A7047     6888   4618   4990   -711   -212    884       C  
ATOM   2198  CE  LYS A7047      83.647  40.804   7.475  1.00 47.58           C  
ANISOU 2198  CE  LYS A7047     7541   5050   5488   -729   -272   1005       C  
ATOM   2199  NZ  LYS A7047      84.555  41.942   7.753  1.00 51.56           N  
ANISOU 2199  NZ  LYS A7047     8073   5462   6053   -768   -193   1013       N  
ATOM   2200  N   PHE A7048      82.021  33.882   9.817  1.00 26.98           N  
ANISOU 2200  N   PHE A7048     4494   2902   2853   -608   -283    615       N  
ATOM   2201  CA  PHE A7048      82.329  32.774  10.753  1.00 24.81           C  
ANISOU 2201  CA  PHE A7048     4132   2681   2611   -593   -228    524       C  
ATOM   2202  C   PHE A7048      83.232  31.707  10.140  1.00 25.33           C  
ANISOU 2202  C   PHE A7048     4246   2794   2583   -653   -156    477       C  
ATOM   2203  O   PHE A7048      84.188  31.288  10.786  1.00 23.53           O  
ANISOU 2203  O   PHE A7048     3974   2582   2383   -655    -71    408       O  
ATOM   2204  CB  PHE A7048      81.046  32.127  11.270  1.00 23.57           C  
ANISOU 2204  CB  PHE A7048     3899   2558   2498   -544   -307    514       C  
ATOM   2205  CG  PHE A7048      81.301  31.001  12.237  1.00 21.70           C  
ANISOU 2205  CG  PHE A7048     3588   2367   2290   -531   -255    433       C  
ATOM   2206  CD1 PHE A7048      81.790  31.267  13.505  1.00 21.05           C  
ANISOU 2206  CD1 PHE A7048     3433   2273   2288   -494   -199    385       C  
ATOM   2207  CD2 PHE A7048      81.042  29.686  11.888  1.00 21.28           C  
ANISOU 2207  CD2 PHE A7048     3543   2361   2179   -558   -267    406       C  
ATOM   2208  CE1 PHE A7048      82.033  30.237  14.400  1.00 19.89           C  
ANISOU 2208  CE1 PHE A7048     3230   2165   2160   -481   -158    320       C  
ATOM   2209  CE2 PHE A7048      81.281  28.657  12.784  1.00 20.70           C  
ANISOU 2209  CE2 PHE A7048     3413   2318   2134   -545   -222    339       C  
ATOM   2210  CZ  PHE A7048      81.770  28.934  14.041  1.00 19.72           C  
ANISOU 2210  CZ  PHE A7048     3222   2184   2085   -505   -170    301       C  
ATOM   2211  N   PRO A7049      82.957  31.197   8.919  1.00 24.85           N  
ANISOU 2211  N   PRO A7049     3266   3026   3149     64     43     95       N  
ATOM   2212  CA  PRO A7049      83.741  30.087   8.374  1.00 25.16           C  
ANISOU 2212  CA  PRO A7049     3359   3112   3086    -14     48    113       C  
ATOM   2213  C   PRO A7049      85.256  30.327   8.340  1.00 25.47           C  
ANISOU 2213  C   PRO A7049     3458   3077   3142    -47     74    104       C  
ATOM   2214  O   PRO A7049      85.688  31.404   7.945  1.00 26.85           O  
ANISOU 2214  O   PRO A7049     3626   3148   3427    -24     83    158       O  
ATOM   2215  CB  PRO A7049      83.188  29.894   6.947  1.00 26.83           C  
ANISOU 2215  CB  PRO A7049     3554   3403   3237     -7     -8    189       C  
ATOM   2216  CG  PRO A7049      81.806  30.516   6.989  1.00 27.69           C  
ANISOU 2216  CG  PRO A7049     3585   3530   3403     63    -42    211       C  
ATOM   2217  CD  PRO A7049      81.890  31.636   8.007  1.00 26.98           C  
ANISOU 2217  CD  PRO A7049     3489   3320   3440    109     -1    187       C  
ATOM   2218  N   LEU A7050      86.018  29.322   8.781  1.00 24.28           N  
ANISOU 2218  N   LEU A7050     3339   2962   2922    -94     97     52       N  
ATOM   2219  CA  LEU A7050      87.499  29.363   8.737  1.00 25.00           C  
ANISOU 2219  CA  LEU A7050     3472   3000   3027   -130    117     29       C  
ATOM   2220  C   LEU A7050      87.926  29.384   7.266  1.00 27.89           C  
ANISOU 2220  C   LEU A7050     3866   3365   3363   -160    121    139       C  
ATOM   2221  O   LEU A7050      87.508  28.485   6.521  1.00 27.82           O  
ANISOU 2221  O   LEU A7050     3861   3460   3246   -175     97    150       O  
ATOM   2222  CB  LEU A7050      88.053  28.129   9.446  1.00 23.59           C  
ANISOU 2222  CB  LEU A7050     3309   2885   2766   -154    141    -19       C  
ATOM   2223  CG  LEU A7050      89.571  28.004   9.481  1.00 23.49           C  
ANISOU 2223  CG  LEU A7050     3326   2838   2759   -185    153    -59       C  
ATOM   2224  CD1 LEU A7050      90.205  29.174  10.221  1.00 25.40           C  
ANISOU 2224  CD1 LEU A7050     3525   3015   3109   -140    133   -172       C  
ATOM   2225  CD2 LEU A7050      89.980  26.679  10.105  1.00 23.37           C  
ANISOU 2225  CD2 LEU A7050     3315   2894   2668   -186    181    -65       C  
ATOM   2226  N   LYS A7051      88.729  30.367   6.871  1.00 31.19           N  
ANISOU 2226  N   LYS A7051     4276   3682   3893   -153    157    208       N  
ATOM   2227  CA  LYS A7051      89.138  30.447   5.444  1.00 35.35           C  
ANISOU 2227  CA  LYS A7051     4814   4261   4355   -138    195    372       C  
ATOM   2228  C   LYS A7051      90.135  29.333   5.115  1.00 33.45           C  
ANISOU 2228  C   LYS A7051     4615   4099   3993   -191    210    321       C  
ATOM   2229  O   LYS A7051      91.092  29.131   5.880  1.00 31.14           O  
ANISOU 2229  O   LYS A7051     4331   3726   3775   -242    228    229       O  
ATOM   2230  CB  LYS A7051      89.677  31.842   5.127  1.00 40.85           C  
ANISOU 2230  CB  LYS A7051     5454   4795   5272   -105    272    526       C  
ATOM   2231  CG  LYS A7051      88.609  32.925   5.179  1.00 46.53           C  
ANISOU 2231  CG  LYS A7051     6114   5432   6130    -31    263    609       C  
ATOM   2232  CD  LYS A7051      89.058  34.283   4.689  1.00 51.94           C  
ANISOU 2232  CD  LYS A7051     6709   5919   7105     14    366    822       C  
ATOM   2233  CE  LYS A7051      87.919  35.282   4.648  1.00 55.72           C  
ANISOU 2233  CE  LYS A7051     7121   6315   7733    104    359    927       C  
ATOM   2234  NZ  LYS A7051      87.266  35.423   5.972  1.00 57.48           N  
ANISOU 2234  NZ  LYS A7051     7324   6461   8053     84    274    651       N  
ATOM   2235  N   LEU A7052      89.872  28.616   4.021  1.00 36.13           N  
ANISOU 2235  N   LEU A7052     4963   4613   4151   -161    188    346       N  
ATOM   2236  CA  LEU A7052      90.779  27.550   3.526  1.00 37.35           C  
ANISOU 2236  CA  LEU A7052     5137   4854   4197   -193    201    274       C  
ATOM   2237  C   LEU A7052      91.993  28.261   2.924  1.00 39.58           C  
ANISOU 2237  C   LEU A7052     5416   5112   4510   -172    303    429       C  
ATOM   2238  O   LEU A7052      91.838  28.907   1.874  1.00 42.99           O  
ANISOU 2238  O   LEU A7052     5819   5654   4858    -74    350    617       O  
ATOM   2239  CB  LEU A7052      90.020  26.703   2.497  1.00 39.29           C  
ANISOU 2239  CB  LEU A7052     5352   5316   4261   -137    127    193       C  
ATOM   2240  CG  LEU A7052      90.803  25.569   1.838  1.00 41.02           C  
ANISOU 2240  CG  LEU A7052     5561   5647   4376   -144    124     63       C  
ATOM   2241  CD1 LEU A7052      91.407  24.635   2.873  1.00 39.35           C  
ANISOU 2241  CD1 LEU A7052     5368   5270   4313   -253    138    -59       C  
ATOM   2242  CD2 LEU A7052      89.908  24.795   0.880  1.00 43.84           C  
ANISOU 2242  CD2 LEU A7052     5841   6224   4592    -72     16   -104       C  
ATOM   2243  N  AARG A7053      93.156  28.148   3.574  0.50 38.56           N  
ANISOU 2243  N  AARG A7053     5293   4854   4502   -244    346    373       N  
ATOM   2244  N  BARG A7053      93.149  28.148   3.584  0.50 38.07           N  
ANISOU 2244  N  BARG A7053     5232   4792   4441   -244    345    372       N  
ATOM   2245  CA AARG A7053      94.380  28.853   3.102  0.50 40.00           C  
ANISOU 2245  CA AARG A7053     5436   4966   4793   -240    461    518       C  
ATOM   2246  CA BARG A7053      94.393  28.832   3.141  0.50 39.16           C  
ANISOU 2246  CA BARG A7053     5331   4857   4690   -243    459    511       C  
ATOM   2247  C  AARG A7053      95.216  27.937   2.198  0.50 39.46           C  
ANISOU 2247  C  AARG A7053     5379   5064   4548   -224    504    511       C  
ATOM   2248  C  BARG A7053      95.194  27.940   2.185  0.50 38.99           C  
ANISOU 2248  C  BARG A7053     5320   5008   4486   -222    503    512       C  
ATOM   2249  O  AARG A7053      96.122  28.463   1.521  0.50 40.28           O  
ANISOU 2249  O  AARG A7053     5436   5172   4695   -192    626    683       O  
ATOM   2250  O  BARG A7053      96.046  28.487   1.458  0.50 39.84           O  
ANISOU 2250  O  BARG A7053     5380   5128   4627   -184    626    693       O  
ATOM   2251  CB AARG A7053      95.199  29.355   4.296  0.50 40.12           C  
ANISOU 2251  CB AARG A7053     5411   4757   5075   -315    467    418       C  
ATOM   2252  CB BARG A7053      95.251  29.189   4.359  0.50 38.59           C  
ANISOU 2252  CB BARG A7053     5224   4573   4864   -321    460    394       C  
ATOM   2253  CG AARG A7053      94.381  30.159   5.298  0.50 40.95           C  
ANISOU 2253  CG AARG A7053     5489   4734   5337   -309    407    343       C  
ATOM   2254  CG BARG A7053      94.557  30.101   5.360  0.50 39.20           C  
ANISOU 2254  CG BARG A7053     5264   4505   5123   -317    409    327       C  
ATOM   2255  CD AARG A7053      95.184  31.122   6.154  0.50 42.88           C  
ANISOU 2255  CD AARG A7053     5630   4760   5902   -340    418    243       C  
ATOM   2256  CD BARG A7053      94.125  31.412   4.729  0.50 41.94           C  
ANISOU 2256  CD BARG A7053     5545   4748   5642   -265    480    535       C  
ATOM   2257  NE AARG A7053      96.260  30.523   6.926  0.50 43.74           N  
ANISOU 2257  NE AARG A7053     5724   4871   6024   -381    381     53       N  
ATOM   2258  NE BARG A7053      93.422  32.273   5.670  0.50 42.43           N  
ANISOU 2258  NE BARG A7053     5556   4663   5902   -253    424    432       N  
ATOM   2259  CZ AARG A7053      96.969  31.177   7.841  0.50 45.04           C  
ANISOU 2259  CZ AARG A7053     5775   4899   6437   -391    345   -132       C  
ATOM   2260  CZ BARG A7053      92.969  33.485   5.383  0.50 45.08           C  
ANISOU 2260  CZ BARG A7053     5809   4847   6472   -207    477    579       C  
ATOM   2261  NH1AARG A7053      97.935  30.562   8.500  0.50 44.36           N  
ANISOU 2261  NH1AARG A7053     5668   4866   6319   -401    297   -301       N  
ATOM   2262  NH1BARG A7053      92.342  34.190   6.307  0.50 46.17           N  
ANISOU 2262  NH1BARG A7053     5889   4856   6796   -190    414    425       N  
ATOM   2263  NH2AARG A7053      96.698  32.443   8.107  0.50 47.30           N  
ANISOU 2263  NH2AARG A7053     5948   4998   7025   -376    345   -175       N  
ATOM   2264  NH2BARG A7053      93.148  33.989   4.174  0.50 47.49           N  
ANISOU 2264  NH2BARG A7053     6075   5143   6825   -155    602    892       N  
ATOM   2265  N   GLY A7054      94.926  26.631   2.185  1.00 37.02           N  
ANISOU 2265  N   GLY A7054     5105   4873   4087   -238    420    322       N  
ATOM   2266  CA  GLY A7054      95.692  25.683   1.353  1.00 37.62           C  
ANISOU 2266  CA  GLY A7054     5172   5104   4015   -213    446    250       C  
ATOM   2267  C   GLY A7054      97.142  25.641   1.805  1.00 37.05           C  
ANISOU 2267  C   GLY A7054     5090   4901   4086   -279    521    248       C  
ATOM   2268  O   GLY A7054      98.038  25.501   0.948  1.00 36.17           O  
ANISOU 2268  O   GLY A7054     4948   4901   3893   -236    608    305       O  
ATOM   2269  N   THR A7055      97.357  25.806   3.115  1.00 32.30           N  
ANISOU 2269  N   THR A7055     4494   4102   3674   -357    488    180       N  
ATOM   2270  CA  THR A7055      98.702  25.814   3.744  1.00 31.95           C  
ANISOU 2270  CA  THR A7055     4415   3937   3786   -410    526    134       C  
ATOM   2271  C   THR A7055      99.510  24.599   3.279  1.00 33.47           C  
ANISOU 2271  C   THR A7055     4610   4223   3883   -410    544     44       C  
ATOM   2272  O   THR A7055      98.966  23.472   3.316  1.00 32.26           O  
ANISOU 2272  O   THR A7055     4485   4129   3642   -405    477    -79       O  
ATOM   2273  CB  THR A7055      98.587  25.819   5.275  1.00 29.86           C  
ANISOU 2273  CB  THR A7055     4150   3556   3637   -442    441      6       C  
ATOM   2274  OG1 THR A7055      97.736  26.908   5.637  1.00 28.55           O  
ANISOU 2274  OG1 THR A7055     3971   3320   3554   -428    418     49       O  
ATOM   2275  CG2 THR A7055      99.930  25.944   5.957  1.00 29.87           C  
ANISOU 2275  CG2 THR A7055     4086   3470   3791   -469    449    -74       C  
ATOM   2276  N   ALA A7056     100.772  24.830   2.910  1.00 34.08           N  
ANISOU 2276  N   ALA A7056     4633   4283   4030   -416    637     98       N  
ATOM   2277  CA  ALA A7056     101.655  23.750   2.415  1.00 34.79           C  
ANISOU 2277  CA  ALA A7056     4709   4464   4043   -404    668      7       C  
ATOM   2278  C   ALA A7056     101.885  22.694   3.501  1.00 34.06           C  
ANISOU 2278  C   ALA A7056     4631   4285   4022   -443    581   -160       C  
ATOM   2279  O   ALA A7056     102.084  23.065   4.682  1.00 31.12           O  
ANISOU 2279  O   ALA A7056     4245   3797   3779   -470    535   -181       O  
ATOM   2280  CB  ALA A7056     102.965  24.331   1.945  1.00 37.13           C  
ANISOU 2280  CB  ALA A7056     4923   4742   4441   -405    801    121       C  
ATOM   2281  N   VAL A7057     101.830  21.423   3.093  1.00 33.33           N  
ANISOU 2281  N   VAL A7057     4543   4264   3857   -421    559   -281       N  
ATOM   2282  CA  VAL A7057     102.127  20.254   3.967  1.00 34.54           C  
ANISOU 2282  CA  VAL A7057     4683   4324   4116   -434    512   -388       C  
ATOM   2283  C   VAL A7057     103.397  19.597   3.419  1.00 37.40           C  
ANISOU 2283  C   VAL A7057     4992   4716   4500   -418    570   -460       C  
ATOM   2284  O   VAL A7057     103.390  19.235   2.233  1.00 37.66           O  
ANISOU 2284  O   VAL A7057     5005   4880   4423   -378    603   -533       O  
ATOM   2285  CB  VAL A7057     100.955  19.255   4.006  1.00 34.82           C  
ANISOU 2285  CB  VAL A7057     4721   4340   4169   -428    453   -473       C  
ATOM   2286  CG1 VAL A7057     101.304  18.017   4.817  1.00 35.11           C  
ANISOU 2286  CG1 VAL A7057     4713   4255   4373   -423    448   -515       C  
ATOM   2287  CG2 VAL A7057      99.679  19.900   4.529  1.00 34.68           C  
ANISOU 2287  CG2 VAL A7057     4742   4304   4129   -438    408   -397       C  
ATOM   2288  N   MET A7058     104.441  19.477   4.242  1.00 38.70           N  
ANISOU 2288  N   MET A7058     5121   4798   4782   -427    574   -457       N  
ATOM   2289  CA  MET A7058     105.716  18.846   3.809  1.00 43.56           C  
ANISOU 2289  CA  MET A7058     5673   5431   5444   -409    630   -526       C  
ATOM   2290  C   MET A7058     106.125  17.770   4.814  1.00 43.98           C  
ANISOU 2290  C   MET A7058     5694   5385   5630   -383    584   -572       C  
ATOM   2291  O   MET A7058     105.811  17.926   6.007  1.00 40.13           O  
ANISOU 2291  O   MET A7058     5220   4851   5175   -368    526   -507       O  
ATOM   2292  CB  MET A7058     106.843  19.878   3.726  1.00 45.08           C  
ANISOU 2292  CB  MET A7058     5807   5625   5694   -430    700   -453       C  
ATOM   2293  CG  MET A7058     106.564  21.000   2.759  1.00 49.09           C  
ANISOU 2293  CG  MET A7058     6316   6210   6125   -433    790   -323       C  
ATOM   2294  SD  MET A7058     107.918  22.198   2.717  1.00 54.21           S  
ANISOU 2294  SD  MET A7058     6836   6779   6981   -470    908   -208       S  
ATOM   2295  CE  MET A7058     107.270  23.366   1.522  1.00 55.71           C  
ANISOU 2295  CE  MET A7058     7024   7057   7085   -437   1045     37       C  
ATOM   2296  N   SER A7059     106.808  16.730   4.334  1.00 45.87           N  
ANISOU 2296  N   SER A7059     5878   5615   5935   -355    618   -671       N  
ATOM   2297  CA  SER A7059     107.318  15.638   5.202  1.00 51.36           C  
ANISOU 2297  CA  SER A7059     6518   6202   6794   -308    598   -676       C  
ATOM   2298  C   SER A7059     108.833  15.805   5.365  1.00 55.04           C  
ANISOU 2298  C   SER A7059     6915   6691   7303   -286    624   -687       C  
ATOM   2299  O   SER A7059     109.586  15.152   4.616  1.00 61.47           O  
ANISOU 2299  O   SER A7059     7670   7512   8171   -268    678   -787       O  
ATOM   2300  CB  SER A7059     106.960  14.290   4.638  1.00 54.23           C  
ANISOU 2300  CB  SER A7059     6831   6482   7289   -288    612   -800       C  
ATOM   2301  OG  SER A7059     107.445  13.254   5.477  1.00 59.65           O  
ANISOU 2301  OG  SER A7059     7446   7032   8183   -230    618   -748       O  
ATOM   2302  N   LEU A7060     109.252  16.662   6.300  1.00 56.01           N  
ANISOU 2302  N   LEU A7060     7023   6837   7418   -280    577   -622       N  
ATOM   2303  CA  LEU A7060     110.689  16.955   6.556  1.00 59.73           C  
ANISOU 2303  CA  LEU A7060     7393   7330   7970   -262    580   -662       C  
ATOM   2304  C   LEU A7060     111.172  16.160   7.773  1.00 65.27           C  
ANISOU 2304  C   LEU A7060     8036   8032   8731   -150    508   -637       C  
ATOM   2305  O   LEU A7060     110.346  15.899   8.672  1.00 66.31           O  
ANISOU 2305  O   LEU A7060     8207   8176   8810    -86    456   -543       O  
ATOM   2306  CB  LEU A7060     110.848  18.460   6.795  1.00 58.49           C  
ANISOU 2306  CB  LEU A7060     7205   7192   7823   -313    558   -661       C  
ATOM   2307  CG  LEU A7060     110.368  19.368   5.663  1.00 58.18           C  
ANISOU 2307  CG  LEU A7060     7207   7156   7744   -395    653   -606       C  
ATOM   2308  CD1 LEU A7060     110.455  20.831   6.069  1.00 58.82           C  
ANISOU 2308  CD1 LEU A7060     7224   7185   7937   -442    634   -593       C  
ATOM   2309  CD2 LEU A7060     111.160  19.123   4.386  1.00 59.53           C  
ANISOU 2309  CD2 LEU A7060     7326   7372   7919   -403    788   -605       C  
ATOM   2310  N   LYS A7061     112.460  15.792   7.789  1.00 71.85           N  
ANISOU 2310  N   LYS A7061     8763   8872   9662   -109    517   -694       N  
ATOM   2311  CA  LYS A7061     113.056  15.060   8.941  1.00 77.70           C  
ANISOU 2311  CA  LYS A7061     9425   9653  10444     35    446   -647       C  
ATOM   2312  C   LYS A7061     113.462  16.097   9.995  1.00 80.97           C  
ANISOU 2312  C   LYS A7061     9765  10203  10795     90    325   -705       C  
ATOM   2313  O   LYS A7061     113.525  17.293   9.645  1.00 81.29           O  
ANISOU 2313  O   LYS A7061     9790  10234  10861    -13    320   -803       O  
ATOM   2314  CB  LYS A7061     114.270  14.217   8.531  1.00 81.79           C  
ANISOU 2314  CB  LYS A7061     9841  10130  11105     74    494   -702       C  
ATOM   2315  CG  LYS A7061     114.064  13.262   7.362  1.00 83.79           C  
ANISOU 2315  CG  LYS A7061    10121  10265  11451     29    603   -745       C  
ATOM   2316  CD  LYS A7061     115.109  12.162   7.308  1.00 86.57           C  
ANISOU 2316  CD  LYS A7061    10359  10557  11975    116    635   -779       C  
ATOM   2317  CE  LYS A7061     115.178  11.446   5.975  1.00 88.25           C  
ANISOU 2317  CE  LYS A7061    10556  10692  12281     74    735   -928       C  
ATOM   2318  NZ  LYS A7061     115.821  12.287   4.937  1.00 89.10           N  
ANISOU 2318  NZ  LYS A7061    10645  10916  12291      0    806  -1041       N  
ATOM   2319  N   GLU A7062     113.747  15.649  11.222  1.00 84.66           N  
ANISOU 2319  N   GLU A7062    10164  10802  11201    269    232   -651       N  
ATOM   2320  CA  GLU A7062     114.122  16.563  12.339  1.00 87.91           C  
ANISOU 2320  CA  GLU A7062    10470  11410  11519    373     78   -775       C  
ATOM   2321  C   GLU A7062     115.384  17.361  11.979  1.00 86.50           C  
ANISOU 2321  C   GLU A7062    10141  11207  11517    294     41  -1002       C  
ATOM   2322  O   GLU A7062     115.497  18.516  12.437  1.00 87.47           O  
ANISOU 2322  O   GLU A7062    10171  11391  11671    282    -63  -1188       O  
ATOM   2323  CB  GLU A7062     114.333  15.764  13.627  1.00 93.32           C  
ANISOU 2323  CB  GLU A7062    11083  12310  12062    635     -3   -655       C  
ATOM   2324  CG  GLU A7062     113.108  14.976  14.058  1.00 96.49           C  
ANISOU 2324  CG  GLU A7062    11592  12721  12348    728     68   -375       C  
ATOM   2325  CD  GLU A7062     113.257  14.229  15.374  1.00101.79           C  
ANISOU 2325  CD  GLU A7062    12175  13641  12859   1030     25   -168       C  
ATOM   2326  OE1 GLU A7062     114.374  14.228  15.932  1.00105.37           O  
ANISOU 2326  OE1 GLU A7062    12486  14282  13267   1183    -82   -264       O  
ATOM   2327  OE2 GLU A7062     112.253  13.654  15.841  1.00104.00           O  
ANISOU 2327  OE2 GLU A7062    12510  13942  13063   1128    107    104       O  
ATOM   2328  N   GLY A7063     116.283  16.772  11.184  1.00 83.41           N  
ANISOU 2328  N   GLY A7063     9702  10714  11274    245    131  -1001       N  
ATOM   2329  CA  GLY A7063     117.542  17.439  10.796  1.00 82.06           C  
ANISOU 2329  CA  GLY A7063     9359  10506  11315    171    131  -1182       C  
ATOM   2330  C   GLY A7063     117.344  18.514   9.738  1.00 79.07           C  
ANISOU 2330  C   GLY A7063     8995   9973  11073    -28    249  -1209       C  
ATOM   2331  O   GLY A7063     118.316  19.246   9.464  1.00 81.55           O  
ANISOU 2331  O   GLY A7063     9133  10227  11623    -98    272  -1331       O  
ATOM   2332  N   GLN A7064     116.135  18.624   9.173  1.00 73.91           N  
ANISOU 2332  N   GLN A7064     8519   9260  10302   -105    330  -1080       N  
ATOM   2333  CA  GLN A7064     115.842  19.622   8.105  1.00 71.31           C  
ANISOU 2333  CA  GLN A7064     8209   8815  10069   -260    462  -1037       C  
ATOM   2334  C   GLN A7064     115.033  20.798   8.674  1.00 67.99           C  
ANISOU 2334  C   GLN A7064     7796   8371   9664   -292    381  -1082       C  
ATOM   2335  O   GLN A7064     114.723  21.734   7.910  1.00 67.80           O  
ANISOU 2335  O   GLN A7064     7770   8237   9751   -403    489  -1015       O  
ATOM   2336  CB  GLN A7064     115.081  18.961   6.953  1.00 72.33           C  
ANISOU 2336  CB  GLN A7064     8504   8929  10047   -298    601   -891       C  
ATOM   2337  CG  GLN A7064     115.793  17.752   6.361  1.00 74.62           C  
ANISOU 2337  CG  GLN A7064     8774   9238  10339   -253    676   -898       C  
ATOM   2338  CD  GLN A7064     115.016  17.120   5.231  1.00 76.24           C  
ANISOU 2338  CD  GLN A7064     9104   9457  10405   -269    781   -844       C  
ATOM   2339  OE1 GLN A7064     114.296  17.788   4.492  1.00 78.67           O  
ANISOU 2339  OE1 GLN A7064     9480   9788  10624   -326    851   -777       O  
ATOM   2340  NE2 GLN A7064     115.174  15.816   5.077  1.00 79.83           N  
ANISOU 2340  NE2 GLN A7064     9564   9904  10861   -201    787   -891       N  
ATOM   2341  N  AILE A7065     114.704  20.747   9.970  0.50 66.19           N  
ANISOU 2341  N  AILE A7065     7561   8262   9324   -175    206  -1180       N  
ATOM   2342  N  BILE A7065     114.709  20.746   9.972  0.50 65.69           N  
ANISOU 2342  N  BILE A7065     7497   8200   9261   -175    206  -1180       N  
ATOM   2343  CA AILE A7065     113.919  21.836  10.627  0.50 64.96           C  
ANISOU 2343  CA AILE A7065     7394   8113   9172   -177    109  -1276       C  
ATOM   2344  CA BILE A7065     113.929  21.831  10.641  0.50 64.17           C  
ANISOU 2344  CA BILE A7065     7293   8015   9072   -175    107  -1278       C  
ATOM   2345  C  AILE A7065     114.878  22.959  11.037  0.50 64.88           C  
ANISOU 2345  C  AILE A7065     7129   8044   9477   -202     23  -1537       C  
ATOM   2346  C  BILE A7065     114.891  22.956  11.039  0.50 64.46           C  
ANISOU 2346  C  BILE A7065     7073   7990   9425   -201     22  -1539       C  
ATOM   2347  O  AILE A7065     115.289  22.983  12.215  0.50 68.34           O  
ANISOU 2347  O  AILE A7065     7435   8652   9879    -58   -167  -1763       O  
ATOM   2348  O  BILE A7065     115.317  22.978  12.211  0.50 68.00           O  
ANISOU 2348  O  BILE A7065     7388   8608   9839    -58   -166  -1765       O  
ATOM   2349  CB AILE A7065     113.130  21.283  11.830  0.50 65.36           C  
ANISOU 2349  CB AILE A7065     7527   8369   8936     -6    -24  -1268       C  
ATOM   2350  CB BILE A7065     113.163  21.279  11.860  0.50 63.97           C  
ANISOU 2350  CB BILE A7065     7345   8198   8761     -2    -28  -1274       C  
ATOM   2351  CG1AILE A7065     112.278  20.073  11.437  0.50 64.00           C  
ANISOU 2351  CG1AILE A7065     7551   8198   8566      9     75  -1015       C  
ATOM   2352  CG1BILE A7065     112.323  20.053  11.494  0.50 62.06           C  
ANISOU 2352  CG1BILE A7065     7299   7962   8319     18     68  -1020       C  
ATOM   2353  CG2AILE A7065     112.294  22.376  12.478  0.50 65.91           C  
ANISOU 2353  CG2AILE A7065     7581   8471   8989      8   -120  -1393       C  
ATOM   2354  CG2BILE A7065     112.321  22.367  12.507  0.50 64.56           C  
ANISOU 2354  CG2BILE A7065     7405   8305   8817     13   -124  -1398       C  
ATOM   2355  CD1AILE A7065     111.526  19.454  12.590  0.50 64.38           C  
ANISOU 2355  CD1AILE A7065     7652   8430   8378    187     -3   -925       C  
ATOM   2356  CD1BILE A7065     111.279  20.320  10.439  0.50 59.92           C  
ANISOU 2356  CD1BILE A7065     7175   7551   8041   -124    190   -894       C  
ATOM   2357  N   ASN A7066     115.207  23.851  10.096  1.00 74.92           N  
ANISOU 2357  N   ASN A7066     7621   9074  11771   -868   1885   -472       N  
ATOM   2358  CA  ASN A7066     116.137  24.989  10.349  1.00 72.42           C  
ANISOU 2358  CA  ASN A7066     7119   8724  11672  -1005   1791   -358       C  
ATOM   2359  C   ASN A7066     115.334  26.207  10.830  1.00 67.11           C  
ANISOU 2359  C   ASN A7066     6729   8126  10643  -1120   1558   -375       C  
ATOM   2360  O   ASN A7066     114.100  26.088  10.966  1.00 62.11           O  
ANISOU 2360  O   ASN A7066     6388   7560   9648  -1077   1494   -464       O  
ATOM   2361  CB  ASN A7066     116.994  25.291   9.114  1.00 73.33           C  
ANISOU 2361  CB  ASN A7066     7084   8780  11998  -1020   2201   -352       C  
ATOM   2362  CG  ASN A7066     116.183  25.649   7.886  1.00 72.09           C  
ANISOU 2362  CG  ASN A7066     7267   8673  11449  -1022   2503   -481       C  
ATOM   2363  OD1 ASN A7066     115.100  26.217   7.992  1.00 67.52           O  
ANISOU 2363  OD1 ASN A7066     6994   8180  10480  -1062   2351   -538       O  
ATOM   2364  ND2 ASN A7066     116.711  25.339   6.713  1.00 73.70           N  
ANISOU 2364  ND2 ASN A7066     7432   8804  11767   -990   2934   -519       N  
ATOM   2365  N   ASP A7067     116.018  27.331  11.072  1.00 65.16           N  
ANISOU 2365  N   ASP A7067     6388   7850  10520  -1261   1446   -284       N  
ATOM   2366  CA  ASP A7067     115.373  28.578  11.571  1.00 62.14           C  
ANISOU 2366  CA  ASP A7067     6272   7506   9833  -1378   1236   -293       C  
ATOM   2367  C   ASP A7067     114.383  29.114  10.529  1.00 58.89           C  
ANISOU 2367  C   ASP A7067     6147   7161   9066  -1357   1477   -405       C  
ATOM   2368  O   ASP A7067     113.360  29.702  10.940  1.00 55.12           O  
ANISOU 2368  O   ASP A7067     5944   6719   8278  -1379   1335   -449       O  
ATOM   2369  CB  ASP A7067     116.417  29.641  11.931  1.00 64.57           C  
ANISOU 2369  CB  ASP A7067     6413   7748  10372  -1546   1082   -166       C  
ATOM   2370  CG  ASP A7067     117.277  29.286  13.134  1.00 67.03           C  
ANISOU 2370  CG  ASP A7067     6496   7971  10999  -1614    726    -25       C  
ATOM   2371  OD1 ASP A7067     116.875  28.383  13.900  1.00 66.56           O  
ANISOU 2371  OD1 ASP A7067     6491   7908  10887  -1546    545    -39       O  
ATOM   2372  OD2 ASP A7067     118.347  29.911  13.290  1.00 70.02           O  
ANISOU 2372  OD2 ASP A7067     6646   8272  11683  -1746    615    109       O  
ATOM   2373  N   MET A7068     114.679  28.923   9.239  1.00 57.88           N  
ANISOU 2373  N   MET A7068     5971   7028   8990  -1324   1831   -441       N  
ATOM   2374  CA  MET A7068     113.777  29.405   8.157  1.00 56.97           C  
ANISOU 2374  CA  MET A7068     6155   6955   8536  -1330   2034   -528       C  
ATOM   2375  C   MET A7068     112.460  28.616   8.218  1.00 52.60           C  
ANISOU 2375  C   MET A7068     5833   6449   7702  -1222   1978   -614       C  
ATOM   2376  O   MET A7068     111.389  29.236   8.058  1.00 49.90           O  
ANISOU 2376  O   MET A7068     5751   6140   7068  -1244   1917   -647       O  
ATOM   2377  CB  MET A7068     114.445  29.244   6.786  1.00 62.22           C  
ANISOU 2377  CB  MET A7068     6765   7574   9302  -1336   2436   -547       C  
ATOM   2378  CG  MET A7068     113.639  29.803   5.625  1.00 64.17           C  
ANISOU 2378  CG  MET A7068     7348   7837   9197  -1384   2614   -614       C  
ATOM   2379  SD  MET A7068     112.328  28.698   5.046  1.00 69.46           S  
ANISOU 2379  SD  MET A7068     8318   8527   9545  -1277   2672   -721       S  
ATOM   2380  CE  MET A7068     113.294  27.340   4.385  1.00 70.76           C  
ANISOU 2380  CE  MET A7068     8319   8606   9959  -1189   3037   -760       C  
ATOM   2381  N   ILE A7069     112.542  27.305   8.465  1.00 50.37           N  
ANISOU 2381  N   ILE A7069     5441   6157   7538  -1111   1990   -635       N  
ATOM   2382  CA  ILE A7069     111.325  26.442   8.568  1.00 47.96           C  
ANISOU 2382  CA  ILE A7069     5333   5890   6999  -1011   1927   -706       C  
ATOM   2383  C   ILE A7069     110.544  26.851   9.824  1.00 45.02           C  
ANISOU 2383  C   ILE A7069     5061   5550   6493  -1024   1610   -685       C  
ATOM   2384  O   ILE A7069     109.308  26.978   9.731  1.00 41.07           O  
ANISOU 2384  O   ILE A7069     4789   5079   5735  -1000   1571   -724       O  
ATOM   2385  CB  ILE A7069     111.698  24.944   8.578  1.00 49.02           C  
ANISOU 2385  CB  ILE A7069     5318   5990   7314   -894   2015   -728       C  
ATOM   2386  CG1 ILE A7069     112.335  24.495   7.258  1.00 51.61           C  
ANISOU 2386  CG1 ILE A7069     5616   6255   7736   -873   2400   -770       C  
ATOM   2387  CG2 ILE A7069     110.490  24.088   8.922  1.00 47.14           C  
ANISOU 2387  CG2 ILE A7069     5257   5789   6863   -807   1890   -781       C  
ATOM   2388  CD1 ILE A7069     111.435  24.635   6.049  1.00 51.40           C  
ANISOU 2388  CD1 ILE A7069     5933   6234   7362   -902   2577   -847       C  
ATOM   2389  N   LEU A7070     111.246  27.059  10.945  1.00 45.03           N  
ANISOU 2389  N   LEU A7070     4910   5524   6675  -1072   1396   -617       N  
ATOM   2390  CA  LEU A7070     110.589  27.464  12.218  1.00 43.71           C  
ANISOU 2390  CA  LEU A7070     4893   5353   6361  -1106   1118   -602       C  
ATOM   2391  C   LEU A7070     109.848  28.791  12.020  1.00 41.33           C  
ANISOU 2391  C   LEU A7070     4816   5058   5829  -1174   1128   -619       C  
ATOM   2392  O   LEU A7070     108.784  28.973  12.636  1.00 39.05           O  
ANISOU 2392  O   LEU A7070     4727   4763   5344  -1150   1032   -644       O  
ATOM   2393  CB  LEU A7070     111.644  27.564  13.325  1.00 46.38           C  
ANISOU 2393  CB  LEU A7070     5066   5630   6926  -1192    874   -510       C  
ATOM   2394  CG  LEU A7070     112.210  26.230  13.809  1.00 48.20           C  
ANISOU 2394  CG  LEU A7070     5091   5831   7390  -1124    785   -472       C  
ATOM   2395  CD1 LEU A7070     113.403  26.445  14.727  1.00 51.11           C  
ANISOU 2395  CD1 LEU A7070     5263   6114   8040  -1241    517   -343       C  
ATOM   2396  CD2 LEU A7070     111.138  25.407  14.510  1.00 47.02           C  
ANISOU 2396  CD2 LEU A7070     5127   5701   7035  -1042    677   -523       C  
ATOM   2397  N  ASER A7071     110.399  29.675  11.181  0.60 41.82           N  
ANISOU 2397  N  ASER A7071     4839   5114   5934  -1252   1260   -600       N  
ATOM   2398  N  BSER A7071     110.393  29.678  11.180  0.40 41.59           N  
ANISOU 2398  N  BSER A7071     4811   5085   5904  -1252   1260   -600       N  
ATOM   2399  CA ASER A7071     109.770  30.991  10.888  0.60 41.13           C  
ANISOU 2399  CA ASER A7071     4953   5018   5654  -1321   1273   -605       C  
ATOM   2400  CA BSER A7071     109.758  30.994  10.903  0.40 40.66           C  
ANISOU 2400  CA BSER A7071     4897   4959   5593  -1321   1270   -605       C  
ATOM   2401  C  ASER A7071     108.450  30.773  10.138  0.60 39.03           C  
ANISOU 2401  C  ASER A7071     4877   4780   5169  -1242   1378   -655       C  
ATOM   2402  C  BSER A7071     108.450  30.787  10.127  0.40 38.79           C  
ANISOU 2402  C  BSER A7071     4849   4750   5139  -1243   1380   -655       C  
ATOM   2403  O  ASER A7071     107.447  31.423  10.498  0.60 38.29           O  
ANISOU 2403  O  ASER A7071     4961   4663   4923  -1239   1301   -656       O  
ATOM   2404  O  BSER A7071     107.455  31.462  10.458  0.40 38.01           O  
ANISOU 2404  O  BSER A7071     4927   4627   4886  -1242   1305   -656       O  
ATOM   2405  CB ASER A7071     110.706  31.878  10.106  0.60 43.22           C  
ANISOU 2405  CB ASER A7071     5129   5268   6025  -1429   1393   -565       C  
ATOM   2406  CB BSER A7071     110.705  31.908  10.168  0.40 42.34           C  
ANISOU 2406  CB BSER A7071     5020   5154   5913  -1431   1381   -563       C  
ATOM   2407  OG ASER A7071     110.103  33.133   9.827  0.60 43.11           O  
ANISOU 2407  OG ASER A7071     5313   5234   5831  -1495   1392   -563       O  
ATOM   2408  OG BSER A7071     111.854  32.182  10.958  0.40 43.65           O  
ANISOU 2408  OG BSER A7071     5002   5276   6305  -1522   1230   -490       O  
ATOM   2409  N   LEU A7072     108.457  29.886   9.138  1.00 38.45           N  
ANISOU 2409  N   LEU A7072     4775   4733   5099  -1187   1549   -686       N  
ATOM   2410  CA  LEU A7072     107.234  29.588   8.342  1.00 37.04           C  
ANISOU 2410  CA  LEU A7072     4789   4563   4721  -1138   1608   -714       C  
ATOM   2411  C   LEU A7072     106.180  28.953   9.259  1.00 34.45           C  
ANISOU 2411  C   LEU A7072     4515   4242   4331  -1044   1458   -724       C  
ATOM   2412  O   LEU A7072     105.002  29.333   9.152  1.00 33.79           O  
ANISOU 2412  O   LEU A7072     4580   4138   4118  -1029   1412   -707       O  
ATOM   2413  CB  LEU A7072     107.581  28.648   7.183  1.00 38.27           C  
ANISOU 2413  CB  LEU A7072     4941   4718   4879  -1117   1816   -752       C  
ATOM   2414  CG  LEU A7072     108.388  29.267   6.042  1.00 41.30           C  
ANISOU 2414  CG  LEU A7072     5347   5073   5271  -1217   2031   -746       C  
ATOM   2415  CD1 LEU A7072     108.795  28.203   5.034  1.00 42.99           C  
ANISOU 2415  CD1 LEU A7072     5587   5254   5489  -1190   2280   -797       C  
ATOM   2416  CD2 LEU A7072     107.600  30.377   5.360  1.00 41.49           C  
ANISOU 2416  CD2 LEU A7072     5599   5075   5088  -1305   2003   -715       C  
ATOM   2417  N   LEU A7073     106.599  28.025  10.122  1.00 34.05           N  
ANISOU 2417  N   LEU A7073     4337   4204   4395   -987   1387   -738       N  
ATOM   2418  CA  LEU A7073     105.687  27.339  11.079  1.00 33.31           C  
ANISOU 2418  CA  LEU A7073     4298   4109   4246   -906   1259   -746       C  
ATOM   2419  C   LEU A7073     105.055  28.383  12.007  1.00 33.42           C  
ANISOU 2419  C   LEU A7073     4440   4079   4179   -939   1153   -724       C  
ATOM   2420  O   LEU A7073     103.834  28.304  12.242  1.00 32.40           O  
ANISOU 2420  O   LEU A7073     4425   3927   3959   -882   1138   -720       O  
ATOM   2421  CB  LEU A7073     106.476  26.315  11.901  1.00 34.01           C  
ANISOU 2421  CB  LEU A7073     4233   4203   4486   -869   1178   -749       C  
ATOM   2422  CG  LEU A7073     106.994  25.092  11.147  1.00 34.82           C  
ANISOU 2422  CG  LEU A7073     4212   4322   4696   -805   1304   -777       C  
ATOM   2423  CD1 LEU A7073     107.897  24.257  12.042  1.00 35.88           C  
ANISOU 2423  CD1 LEU A7073     4158   4437   5037   -778   1196   -754       C  
ATOM   2424  CD2 LEU A7073     105.845  24.250  10.613  1.00 33.94           C  
ANISOU 2424  CD2 LEU A7073     4232   4223   4439   -729   1350   -811       C  
ATOM   2425  N   SER A7074     105.871  29.328  12.484  1.00 34.27           N  
ANISOU 2425  N   SER A7074     4529   4155   4335  -1033   1095   -704       N  
ATOM   2426  CA  SER A7074     105.442  30.374  13.451  1.00 35.69           C  
ANISOU 2426  CA  SER A7074     4870   4260   4429  -1082   1008   -693       C  
ATOM   2427  C   SER A7074     104.446  31.355  12.825  1.00 36.24           C  
ANISOU 2427  C   SER A7074     5072   4294   4402  -1076   1097   -681       C  
ATOM   2428  O   SER A7074     103.765  32.055  13.599  1.00 35.86           O  
ANISOU 2428  O   SER A7074     5174   4161   4287  -1076   1078   -679       O  
ATOM   2429  CB  SER A7074     106.642  31.106  13.994  1.00 37.27           C  
ANISOU 2429  CB  SER A7074     5031   4423   4706  -1207    902   -665       C  
ATOM   2430  OG  SER A7074     107.485  30.219  14.711  1.00 38.20           O  
ANISOU 2430  OG  SER A7074     5024   4544   4944  -1220    770   -648       O  
ATOM   2431  N   LYS A7075     104.372  31.408  11.491  1.00 37.46           N  
ANISOU 2431  N   LYS A7075     5190   4488   4552  -1078   1195   -669       N  
ATOM   2432  CA  LYS A7075     103.469  32.361  10.785  1.00 38.89           C  
ANISOU 2432  CA  LYS A7075     5489   4621   4665  -1090   1240   -631       C  
ATOM   2433  C   LYS A7075     102.228  31.636  10.253  1.00 36.07           C  
ANISOU 2433  C   LYS A7075     5166   4263   4276  -1004   1251   -607       C  
ATOM   2434  O   LYS A7075     101.413  32.296   9.584  1.00 36.23           O  
ANISOU 2434  O   LYS A7075     5263   4228   4273  -1016   1254   -549       O  
ATOM   2435  CB  LYS A7075     104.216  33.050   9.636  1.00 42.83           C  
ANISOU 2435  CB  LYS A7075     5975   5137   5159  -1189   1311   -613       C  
ATOM   2436  CG  LYS A7075     105.305  34.026  10.058  1.00 46.73           C  
ANISOU 2436  CG  LYS A7075     6438   5610   5706  -1294   1288   -609       C  
ATOM   2437  CD  LYS A7075     106.066  34.617   8.885  1.00 50.11           C  
ANISOU 2437  CD  LYS A7075     6841   6053   6142  -1394   1389   -586       C  
ATOM   2438  CE  LYS A7075     107.014  35.727   9.285  1.00 54.35           C  
ANISOU 2438  CE  LYS A7075     7353   6555   6743  -1510   1349   -563       C  
ATOM   2439  NZ  LYS A7075     108.044  35.264  10.246  1.00 57.18           N  
ANISOU 2439  NZ  LYS A7075     7559   6926   7239  -1533   1261   -569       N  
ATOM   2440  N   GLY A7076     102.076  30.344  10.560  1.00 34.01           N  
ANISOU 2440  N   GLY A7076     4846   4044   4030   -930   1234   -634       N  
ATOM   2441  CA  GLY A7076     100.925  29.565  10.062  1.00 33.63           C  
ANISOU 2441  CA  GLY A7076     4824   3988   3963   -864   1219   -600       C  
ATOM   2442  C   GLY A7076     101.000  29.332   8.558  1.00 34.00           C  
ANISOU 2442  C   GLY A7076     4917   4054   3946   -918   1251   -582       C  
ATOM   2443  O   GLY A7076      99.938  29.130   7.930  1.00 34.52           O  
ANISOU 2443  O   GLY A7076     5052   4077   3985   -911   1195   -519       O  
ATOM   2444  N  AARG A7077     102.216  29.343   8.000  0.50 33.97           N  
ANISOU 2444  N  AARG A7077     4886   4093   3928   -982   1340   -627       N  
ATOM   2445  N  BARG A7077     102.215  29.344   7.996  0.50 34.40           N  
ANISOU 2445  N  BARG A7077     4940   4146   3981   -982   1341   -627       N  
ATOM   2446  CA AARG A7077     102.432  29.164   6.537  0.50 35.07           C  
ANISOU 2446  CA AARG A7077     5129   4226   3970  -1056   1424   -625       C  
ATOM   2447  CA BARG A7077     102.417  29.159   6.531  0.50 35.76           C  
ANISOU 2447  CA BARG A7077     5217   4312   4056  -1056   1423   -624       C  
ATOM   2448  C  AARG A7077     102.953  27.754   6.215  0.50 34.88           C  
ANISOU 2448  C  AARG A7077     5074   4234   3943  -1018   1514   -689       C  
ATOM   2449  C  BARG A7077     102.949  27.753   6.214  0.50 35.26           C  
ANISOU 2449  C  BARG A7077     5123   4283   3992  -1018   1514   -689       C  
ATOM   2450  O  AARG A7077     103.268  27.514   5.031  0.50 35.03           O  
ANISOU 2450  O  AARG A7077     5216   4228   3865  -1085   1632   -706       O  
ATOM   2451  O  BARG A7077     103.269  27.513   5.031  0.50 35.38           O  
ANISOU 2451  O  BARG A7077     5261   4272   3910  -1085   1632   -707       O  
ATOM   2452  CB AARG A7077     103.418  30.224   6.037  0.50 36.76           C  
ANISOU 2452  CB AARG A7077     5353   4435   4178  -1161   1524   -627       C  
ATOM   2453  CB BARG A7077     103.380  30.229   6.006  0.50 38.02           C  
ANISOU 2453  CB BARG A7077     5519   4593   4334  -1162   1522   -625       C  
ATOM   2454  CG AARG A7077     102.906  31.652   6.159  0.50 37.43           C  
ANISOU 2454  CG AARG A7077     5501   4467   4251  -1210   1445   -561       C  
ATOM   2455  CG BARG A7077     102.873  31.652   6.190  0.50 39.21           C  
ANISOU 2455  CG BARG A7077     5726   4692   4478  -1207   1441   -560       C  
ATOM   2456  CD AARG A7077     103.965  32.678   5.804  0.50 39.42           C  
ANISOU 2456  CD AARG A7077     5748   4716   4511  -1317   1535   -563       C  
ATOM   2457  CD BARG A7077     103.875  32.709   5.763  0.50 41.83           C  
ANISOU 2457  CD BARG A7077     6066   5018   4810  -1318   1529   -559       C  
ATOM   2458  NE AARG A7077     104.520  32.469   4.476  0.50 41.39           N  
ANISOU 2458  NE AARG A7077     6094   4961   4669  -1405   1682   -574       N  
ATOM   2459  NE BARG A7077     103.387  34.052   6.048  0.50 43.11           N  
ANISOU 2459  NE BARG A7077     6285   5118   4975  -1352   1446   -501       N  
ATOM   2460  CZ AARG A7077     105.502  33.192   3.949  0.50 42.66           C  
ANISOU 2460  CZ AARG A7077     6258   5114   4837  -1508   1811   -574       C  
ATOM   2461  CZ BARG A7077     104.099  35.163   5.897  0.50 44.82           C  
ANISOU 2461  CZ BARG A7077     6514   5314   5200  -1448   1484   -487       C  
ATOM   2462  NH1AARG A7077     106.044  34.179   4.641  0.50 43.19           N  
ANISOU 2462  NH1AARG A7077     6222   5183   5004  -1541   1775   -558       N  
ATOM   2463  NH1BARG A7077     105.347  35.098   5.467  0.50 46.60           N  
ANISOU 2463  NH1BARG A7077     6675   5579   5450  -1522   1613   -519       N  
ATOM   2464  NH2AARG A7077     105.942  32.923   2.735  0.50 43.94           N  
ANISOU 2464  NH2AARG A7077     6546   5250   4897  -1590   1987   -589       N  
ATOM   2465  NH2BARG A7077     103.565  36.335   6.189  0.50 45.00           N  
ANISOU 2465  NH2BARG A7077     6604   5262   5229  -1468   1409   -437       N  
ATOM   2466  N   LEU A7078     103.022  26.852   7.202  1.00 34.03           N  
ANISOU 2466  N   LEU A7078     4839   4161   3927   -921   1471   -723       N  
ATOM   2467  CA  LEU A7078     103.553  25.487   6.930  1.00 34.19           C  
ANISOU 2467  CA  LEU A7078     4818   4195   3974   -874   1562   -783       C  
ATOM   2468  C   LEU A7078     103.059  24.456   7.952  1.00 32.58           C  
ANISOU 2468  C   LEU A7078     4536   4013   3830   -769   1449   -791       C  
ATOM   2469  O   LEU A7078     102.939  24.784   9.145  1.00 30.45           O  
ANISOU 2469  O   LEU A7078     4185   3756   3625   -736   1347   -774       O  
ATOM   2470  CB  LEU A7078     105.084  25.559   6.947  1.00 35.93           C  
ANISOU 2470  CB  LEU A7078     4885   4429   4335   -892   1709   -821       C  
ATOM   2471  CG  LEU A7078     105.820  24.258   6.623  1.00 37.29           C  
ANISOU 2471  CG  LEU A7078     4985   4586   4596   -836   1856   -879       C  
ATOM   2472  CD1 LEU A7078     105.508  23.793   5.210  1.00 38.83           C  
ANISOU 2472  CD1 LEU A7078     5413   4725   4616   -879   2010   -912       C  
ATOM   2473  CD2 LEU A7078     107.321  24.427   6.802  1.00 38.62           C  
ANISOU 2473  CD2 LEU A7078     4932   4747   4992   -846   1987   -884       C  
ATOM   2474  N   ILE A7079     102.795  23.247   7.454  1.00 32.53           N  
ANISOU 2474  N   ILE A7079     4587   3991   3779   -731   1478   -819       N  
ATOM   2475  CA  ILE A7079     102.414  22.051   8.257  1.00 31.36           C  
ANISOU 2475  CA  ILE A7079     4375   3856   3684   -636   1391   -832       C  
ATOM   2476  C   ILE A7079     103.444  20.963   7.931  1.00 32.61           C  
ANISOU 2476  C   ILE A7079     4466   4002   3921   -596   1528   -899       C  
ATOM   2477  O   ILE A7079     103.698  20.734   6.725  1.00 32.67           O  
ANISOU 2477  O   ILE A7079     4601   3963   3846   -640   1683   -934       O  
ATOM   2478  CB  ILE A7079     100.969  21.595   7.956  1.00 31.25           C  
ANISOU 2478  CB  ILE A7079     4495   3810   3566   -630   1279   -783       C  
ATOM   2479  CG1 ILE A7079      99.925  22.489   8.628  1.00 30.56           C  
ANISOU 2479  CG1 ILE A7079     4400   3713   3497   -627   1159   -703       C  
ATOM   2480  CG2 ILE A7079     100.772  20.140   8.356  1.00 31.23           C  
ANISOU 2480  CG2 ILE A7079     4461   3807   3595   -550   1240   -810       C  
ATOM   2481  CD1 ILE A7079      99.835  22.315  10.131  1.00 30.53           C  
ANISOU 2481  CD1 ILE A7079     4286   3730   3585   -552   1105   -707       C  
ATOM   2482  N   ILE A7080     104.045  20.358   8.957  1.00 32.40           N  
ANISOU 2482  N   ILE A7080     4264   3994   4053   -525   1482   -911       N  
ATOM   2483  CA  ILE A7080     105.043  19.273   8.736  1.00 34.29           C  
ANISOU 2483  CA  ILE A7080     4394   4198   4434   -468   1612   -960       C  
ATOM   2484  C   ILE A7080     104.477  17.970   9.299  1.00 33.54           C  
ANISOU 2484  C   ILE A7080     4302   4094   4344   -384   1505   -968       C  
ATOM   2485  O   ILE A7080     104.311  17.864  10.534  1.00 31.48           O  
ANISOU 2485  O   ILE A7080     3951   3862   4147   -352   1334   -933       O  
ATOM   2486  CB  ILE A7080     106.417  19.618   9.336  1.00 36.28           C  
ANISOU 2486  CB  ILE A7080     4403   4449   4930   -468   1637   -942       C  
ATOM   2487  CG1 ILE A7080     106.998  20.872   8.678  1.00 37.78           C  
ANISOU 2487  CG1 ILE A7080     4594   4640   5122   -559   1763   -931       C  
ATOM   2488  CG2 ILE A7080     107.363  18.428   9.226  1.00 37.84           C  
ANISOU 2488  CG2 ILE A7080     4446   4587   5345   -388   1761   -970       C  
ATOM   2489  CD1 ILE A7080     108.312  21.324   9.261  1.00 40.42           C  
ANISOU 2489  CD1 ILE A7080     4675   4963   5720   -582   1757   -888       C  
ATOM   2490  N   ARG A7081     104.191  17.032   8.396  1.00 33.68           N  
ANISOU 2490  N   ARG A7081     4456   4061   4278   -365   1607  -1013       N  
ATOM   2491  CA  ARG A7081     103.669  15.689   8.743  1.00 33.59           C  
ANISOU 2491  CA  ARG A7081     4470   4026   4265   -292   1523  -1024       C  
ATOM   2492  C   ARG A7081     103.528  14.872   7.458  1.00 36.03           C  
ANISOU 2492  C   ARG A7081     4988   4249   4451   -306   1680  -1084       C  
ATOM   2493  O   ARG A7081     103.559  15.476   6.360  1.00 34.98           O  
ANISOU 2493  O   ARG A7081     5025   4081   4182   -392   1811  -1102       O  
ATOM   2494  CB  ARG A7081     102.296  15.761   9.423  1.00 30.67           C  
ANISOU 2494  CB  ARG A7081     4168   3696   3787   -298   1307   -964       C  
ATOM   2495  CG  ARG A7081     101.225  16.494   8.624  1.00 29.38           C  
ANISOU 2495  CG  ARG A7081     4187   3526   3446   -382   1270   -923       C  
ATOM   2496  CD  ARG A7081      99.825  16.104   9.061  1.00 28.24           C  
ANISOU 2496  CD  ARG A7081     4096   3379   3254   -371   1095   -855       C  
ATOM   2497  NE  ARG A7081      98.766  16.920   8.475  1.00 27.83           N  
ANISOU 2497  NE  ARG A7081     4159   3305   3110   -449   1018   -777       N  
ATOM   2498  CZ  ARG A7081      98.224  16.742   7.271  1.00 29.38           C  
ANISOU 2498  CZ  ARG A7081     4547   3436   3177   -531    990   -751       C  
ATOM   2499  NH1 ARG A7081      97.258  17.547   6.860  1.00 28.64           N  
ANISOU 2499  NH1 ARG A7081     4523   3310   3047   -606    875   -650       N  
ATOM   2500  NH2 ARG A7081      98.647  15.770   6.477  1.00 31.15           N  
ANISOU 2500  NH2 ARG A7081     4913   3607   3315   -548   1070   -819       N  
ATOM   2501  N   GLU A7082     103.406  13.552   7.598  1.00 39.07           N  
ANISOU 2501  N   GLU A7082     5390   4585   4867   -236   1666  -1113       N  
ATOM   2502  CA  GLU A7082     103.110  12.699   6.424  1.00 43.34           C  
ANISOU 2502  CA  GLU A7082     6198   5021   5248   -266   1788  -1171       C  
ATOM   2503  C   GLU A7082     101.696  13.065   5.968  1.00 41.42           C  
ANISOU 2503  C   GLU A7082     6184   4786   4765   -371   1603  -1111       C  
ATOM   2504  O   GLU A7082     100.929  13.591   6.803  1.00 37.25           O  
ANISOU 2504  O   GLU A7082     5549   4340   4262   -369   1397  -1030       O  
ATOM   2505  CB  GLU A7082     103.239  11.217   6.781  1.00 48.18           C  
ANISOU 2505  CB  GLU A7082     6775   5571   5959   -167   1789  -1208       C  
ATOM   2506  CG  GLU A7082     104.673  10.773   7.024  1.00 53.71           C  
ANISOU 2506  CG  GLU A7082     7249   6217   6941    -64   1989  -1252       C  
ATOM   2507  CD  GLU A7082     105.571  10.771   5.796  1.00 60.92           C  
ANISOU 2507  CD  GLU A7082     8275   7009   7862    -80   2352  -1335       C  
ATOM   2508  OE1 GLU A7082     106.805  10.687   5.969  1.00 65.93           O  
ANISOU 2508  OE1 GLU A7082     8667   7594   8788     -2   2541  -1346       O  
ATOM   2509  OE2 GLU A7082     105.038  10.836   4.664  1.00 65.84           O  
ANISOU 2509  OE2 GLU A7082     9237   7568   8210   -178   2447  -1377       O  
ATOM   2510  N   ASN A7083     101.380  12.836   4.695  1.00 42.79           N  
ANISOU 2510  N   ASN A7083     6671   4859   4727   -468   1678  -1139       N  
ATOM   2511  CA  ASN A7083     100.029  13.160   4.168  1.00 44.69           C  
ANISOU 2511  CA  ASN A7083     7132   5078   4768   -592   1455  -1051       C  
ATOM   2512  C   ASN A7083      99.385  11.842   3.719  1.00 46.22           C  
ANISOU 2512  C   ASN A7083     7554   5165   4839   -620   1375  -1062       C  
ATOM   2513  O   ASN A7083      98.655  11.838   2.711  1.00 48.03           O  
ANISOU 2513  O   ASN A7083     8099   5299   4851   -765   1275  -1022       O  
ATOM   2514  CB  ASN A7083     100.103  14.224   3.069  1.00 47.93           C  
ANISOU 2514  CB  ASN A7083     7753   5447   5009   -731   1529  -1038       C  
ATOM   2515  CG  ASN A7083      98.783  14.926   2.826  1.00 49.60           C  
ANISOU 2515  CG  ASN A7083     8070   5656   5119   -845   1248   -903       C  
ATOM   2516  OD1 ASN A7083      97.953  15.037   3.728  1.00 46.78           O  
ANISOU 2516  OD1 ASN A7083     7519   5364   4888   -793   1044   -813       O  
ATOM   2517  ND2 ASN A7083      98.595  15.432   1.617  1.00 52.58           N  
ANISOU 2517  ND2 ASN A7083     8752   5941   5283  -1005   1246   -878       N  
ATOM   2518  N   ASN A7084      99.667  10.770   4.464  1.00 45.95           N  
ANISOU 2518  N   ASN A7084     7377   5137   4943   -498   1395  -1106       N  
ATOM   2519  CA  ASN A7084      99.126   9.414   4.190  1.00 48.92           C  
ANISOU 2519  CA  ASN A7084     7946   5409   5230   -509   1319  -1122       C  
ATOM   2520  C   ASN A7084      97.663   9.334   4.651  1.00 46.43           C  
ANISOU 2520  C   ASN A7084     7608   5130   4904   -556    987   -988       C  
ATOM   2521  O   ASN A7084      97.125  10.342   5.155  1.00 45.03           O  
ANISOU 2521  O   ASN A7084     7266   5043   4797   -568    857   -891       O  
ATOM   2522  CB  ASN A7084      99.969   8.334   4.878  1.00 50.77           C  
ANISOU 2522  CB  ASN A7084     8010   5629   5650   -355   1453  -1204       C  
ATOM   2523  CG  ASN A7084     101.403   8.293   4.390  1.00 54.15           C  
ANISOU 2523  CG  ASN A7084     8426   5986   6160   -298   1806  -1319       C  
ATOM   2524  OD1 ASN A7084     101.694   8.673   3.257  1.00 55.11           O  
ANISOU 2524  OD1 ASN A7084     8801   6019   6118   -392   1996  -1370       O  
ATOM   2525  ND2 ASN A7084     102.304   7.815   5.234  1.00 55.94           N  
ANISOU 2525  ND2 ASN A7084     8365   6230   6656   -152   1896  -1348       N  
ATOM   2526  N   ARG A7085      97.059   8.162   4.470  1.00 44.80           N  
ANISOU 2526  N   ARG A7085     7559   4833   4628   -582    872   -979       N  
ATOM   2527  CA  ARG A7085      95.651   7.888   4.864  1.00 44.42           C  
ANISOU 2527  CA  ARG A7085     7480   4790   4606   -631    563   -837       C  
ATOM   2528  C   ARG A7085      95.477   8.082   6.377  1.00 39.56           C  
ANISOU 2528  C   ARG A7085     6498   4309   4222   -501    507   -784       C  
ATOM   2529  O   ARG A7085      96.411   7.761   7.140  1.00 39.58           O  
ANISOU 2529  O   ARG A7085     6332   4363   4340   -375    648   -869       O  
ATOM   2530  CB  ARG A7085      95.283   6.471   4.405  1.00 49.85           C  
ANISOU 2530  CB  ARG A7085     8412   5343   5183   -678    486   -858       C  
ATOM   2531  CG  ARG A7085      96.356   5.434   4.714  1.00 54.81           C  
ANISOU 2531  CG  ARG A7085     9010   5940   5873   -543    711  -1003       C  
ATOM   2532  CD  ARG A7085      96.294   4.191   3.844  1.00 59.70           C  
ANISOU 2532  CD  ARG A7085     9988   6376   6316   -610    735  -1070       C  
ATOM   2533  NE  ARG A7085      95.359   3.171   4.296  1.00 63.42           N  
ANISOU 2533  NE  ARG A7085    10462   6815   6819   -621    493   -994       N  
ATOM   2534  CZ  ARG A7085      95.630   2.256   5.227  1.00 65.90           C  
ANISOU 2534  CZ  ARG A7085    10589   7154   7295   -483    517  -1026       C  
ATOM   2535  NH1 ARG A7085      94.717   1.357   5.557  1.00 67.19           N  
ANISOU 2535  NH1 ARG A7085    10781   7276   7470   -516    293   -948       N  
ATOM   2536  NH2 ARG A7085      96.806   2.246   5.836  1.00 66.17           N  
ANISOU 2536  NH2 ARG A7085    10402   7242   7495   -324    743  -1120       N  
ATOM   2537  N   VAL A7086      94.320   8.610   6.779  1.00 34.52           N  
ANISOU 2537  N   VAL A7086     5753   3702   3658   -542    311   -640       N  
ATOM   2538  CA  VAL A7086      94.004   8.817   8.222  1.00 31.87           C  
ANISOU 2538  CA  VAL A7086     5129   3462   3515   -438    282   -585       C  
ATOM   2539  C   VAL A7086      93.388   7.523   8.764  1.00 29.84           C  
ANISOU 2539  C   VAL A7086     4856   3168   3312   -411    167   -547       C  
ATOM   2540  O   VAL A7086      92.331   7.104   8.253  1.00 29.48           O  
ANISOU 2540  O   VAL A7086     4915   3039   3243   -507    -15   -442       O  
ATOM   2541  CB  VAL A7086      93.087  10.036   8.413  1.00 31.55           C  
ANISOU 2541  CB  VAL A7086     4977   3447   3564   -481    193   -450       C  
ATOM   2542  CG1 VAL A7086      92.559  10.142   9.839  1.00 31.17           C  
ANISOU 2542  CG1 VAL A7086     4700   3451   3691   -393    190   -387       C  
ATOM   2543  CG2 VAL A7086      93.806  11.310   7.995  1.00 31.70           C  
ANISOU 2543  CG2 VAL A7086     5003   3506   3532   -499    315   -496       C  
ATOM   2544  N   VAL A7087      94.062   6.916   9.741  1.00 28.39           N  
ANISOU 2544  N   VAL A7087     4552   3031   3203   -297    250   -620       N  
ATOM   2545  CA  VAL A7087      93.626   5.631  10.357  1.00 28.19           C  
ANISOU 2545  CA  VAL A7087     4512   2970   3227   -263    157   -595       C  
ATOM   2546  C   VAL A7087      93.560   5.835  11.868  1.00 26.53           C  
ANISOU 2546  C   VAL A7087     4094   2837   3148   -182    171   -560       C  
ATOM   2547  O   VAL A7087      94.561   6.310  12.456  1.00 25.88           O  
ANISOU 2547  O   VAL A7087     3919   2815   3096   -117    280   -631       O  
ATOM   2548  CB  VAL A7087      94.577   4.479   9.983  1.00 29.51           C  
ANISOU 2548  CB  VAL A7087     4797   3074   3339   -216    239   -720       C  
ATOM   2549  CG1 VAL A7087      94.141   3.166  10.617  1.00 29.95           C  
ANISOU 2549  CG1 VAL A7087     4845   3086   3446   -184    131   -691       C  
ATOM   2550  CG2 VAL A7087      94.704   4.334   8.476  1.00 31.30           C  
ANISOU 2550  CG2 VAL A7087     5298   3196   3395   -310    276   -772       C  
ATOM   2551  N   ILE A7088      92.422   5.480  12.458  1.00 25.03           N  
ANISOU 2551  N   ILE A7088     3852   2624   3031   -200     65   -446       N  
ATOM   2552  CA  ILE A7088      92.201   5.670  13.918  1.00 23.89           C  
ANISOU 2552  CA  ILE A7088     3570   2524   2982   -145    104   -406       C  
ATOM   2553  C   ILE A7088      91.689   4.362  14.510  1.00 23.25           C  
ANISOU 2553  C   ILE A7088     3499   2395   2937   -135     18   -363       C  
ATOM   2554  O   ILE A7088      91.160   3.523  13.759  1.00 23.08           O  
ANISOU 2554  O   ILE A7088     3565   2306   2898   -186    -94   -327       O  
ATOM   2555  CB  ILE A7088      91.200   6.817  14.174  1.00 24.09           C  
ANISOU 2555  CB  ILE A7088     3503   2550   3099   -176    131   -290       C  
ATOM   2556  CG1 ILE A7088      89.775   6.438  13.756  1.00 25.10           C  
ANISOU 2556  CG1 ILE A7088     3611   2596   3327   -245      3   -137       C  
ATOM   2557  CG2 ILE A7088      91.671   8.092  13.499  1.00 24.81           C  
ANISOU 2557  CG2 ILE A7088     3599   2677   3149   -196    196   -326       C  
ATOM   2558  CD1 ILE A7088      88.733   7.508  14.018  1.00 26.02           C  
ANISOU 2558  CD1 ILE A7088     3594   2682   3610   -261     45      0       C  
ATOM   2559  N   SER A7089      91.830   4.216  15.820  1.00 22.82           N  
ANISOU 2559  N   SER A7089     3388   2363   2919    -88     61   -362       N  
ATOM   2560  CA  SER A7089      91.279   3.011  16.476  1.00 23.53           C  
ANISOU 2560  CA  SER A7089     3494   2402   3042    -88    -13   -308       C  
ATOM   2561  C   SER A7089      91.114   3.268  17.968  1.00 23.54           C  
ANISOU 2561  C   SER A7089     3463   2412   3067    -71     63   -273       C  
ATOM   2562  O   SER A7089      91.770   4.177  18.510  1.00 23.30           O  
ANISOU 2562  O   SER A7089     3428   2423   2999    -53    149   -322       O  
ATOM   2563  CB  SER A7089      92.159   1.809  16.246  1.00 23.87           C  
ANISOU 2563  CB  SER A7089     3611   2418   3039    -50    -78   -398       C  
ATOM   2564  OG  SER A7089      93.428   2.006  16.844  1.00 24.61           O  
ANISOU 2564  OG  SER A7089     3674   2550   3126     10    -26   -485       O  
ATOM   2565  N  ASER A7090      90.239   2.480  18.586  0.60 24.29           N  
ANISOU 2565  N  ASER A7090     3563   2452   3211    -92     34   -186       N  
ATOM   2566  N  BSER A7090      90.254   2.478  18.608  0.40 24.84           N  
ANISOU 2566  N  BSER A7090     3634   2522   3280    -91     35   -187       N  
ATOM   2567  CA ASER A7090      90.032   2.517  20.053  0.60 25.18           C  
ANISOU 2567  CA ASER A7090     3711   2542   3314    -94    124   -152       C  
ATOM   2568  CA BSER A7090      90.032   2.569  20.073  0.40 25.99           C  
ANISOU 2568  CA BSER A7090     3812   2646   3416    -94    130   -152       C  
ATOM   2569  C  ASER A7090      90.349   1.125  20.597  0.60 25.61           C  
ANISOU 2569  C  ASER A7090     3840   2561   3329    -89     12   -164       C  
ATOM   2570  C  BSER A7090      90.270   1.183  20.679  0.40 26.24           C  
ANISOU 2570  C  BSER A7090     3920   2638   3410    -92     24   -157       C  
ATOM   2571  O  ASER A7090      89.778   0.136  20.086  0.60 26.16           O  
ANISOU 2571  O  ASER A7090     3901   2589   3448   -105    -85   -116       O  
ATOM   2572  O  BSER A7090      89.528   0.248  20.320  0.40 27.32           O  
ANISOU 2572  O  BSER A7090     4044   2729   3608   -114    -54    -91       O  
ATOM   2573  CB ASER A7090      88.644   2.964  20.428  0.60 26.05           C  
ANISOU 2573  CB ASER A7090     3758   2595   3543   -126    250    -22       C  
ATOM   2574  CB BSER A7090      88.661   3.117  20.388  0.40 27.19           C  
ANISOU 2574  CB BSER A7090     3896   2743   3689   -124    261    -25       C  
ATOM   2575  OG ASER A7090      88.487   2.957  21.843  0.60 26.41           O  
ANISOU 2575  OG ASER A7090     3894   2594   3544   -138    379     -3       O  
ATOM   2576  OG BSER A7090      87.645   2.344  19.768  0.40 28.93           O  
ANISOU 2576  OG BSER A7090     4045   2911   4034   -158    166     83       O  
ATOM   2577  N   ASP A7091      91.298   1.059  21.527  1.00 26.08           N  
ANISOU 2577  N   ASP A7091     3979   2625   3305    -77     -4   -222       N  
ATOM   2578  CA  ASP A7091      91.668  -0.221  22.175  1.00 26.76           C  
ANISOU 2578  CA  ASP A7091     4142   2661   3362    -77   -130   -220       C  
ATOM   2579  C   ASP A7091      90.492  -0.725  23.004  1.00 27.66           C  
ANISOU 2579  C   ASP A7091     4317   2708   3482   -131    -77   -114       C  
ATOM   2580  O   ASP A7091      89.893   0.081  23.751  1.00 27.86           O  
ANISOU 2580  O   ASP A7091     4387   2712   3486   -168     89    -68       O  
ATOM   2581  CB  ASP A7091      92.899  -0.067  23.065  1.00 27.96           C  
ANISOU 2581  CB  ASP A7091     4368   2811   3445    -78   -196   -271       C  
ATOM   2582  CG  ASP A7091      94.208  -0.041  22.304  1.00 29.40           C  
ANISOU 2582  CG  ASP A7091     4459   3026   3683    -16   -277   -359       C  
ATOM   2583  OD1 ASP A7091      94.200  -0.374  21.105  1.00 29.65           O  
ANISOU 2583  OD1 ASP A7091     4417   3071   3775     29   -272   -397       O  
ATOM   2584  OD2 ASP A7091      95.227   0.290  22.929  1.00 33.39           O  
ANISOU 2584  OD2 ASP A7091     4981   3526   4178    -25   -344   -380       O  
ATOM   2585  N   VAL A7092      90.187  -2.012  22.868  1.00 27.08           N  
ANISOU 2585  N   VAL A7092     4255   2588   3444   -136   -192    -77       N  
ATOM   2586  CA  VAL A7092      89.087  -2.645  23.644  1.00 28.56           C  
ANISOU 2586  CA  VAL A7092     4493   2701   3654   -194   -145     33       C  
ATOM   2587  C   VAL A7092      89.700  -3.646  24.622  1.00 29.89           C  
ANISOU 2587  C   VAL A7092     4807   2816   3732   -212   -264     25       C  
ATOM   2588  O   VAL A7092      90.425  -4.565  24.170  1.00 27.85           O  
ANISOU 2588  O   VAL A7092     4541   2549   3490   -171   -440    -22       O  
ATOM   2589  CB  VAL A7092      88.068  -3.333  22.719  1.00 29.38           C  
ANISOU 2589  CB  VAL A7092     4498   2775   3888   -211   -207    114       C  
ATOM   2590  CG1 VAL A7092      87.035  -4.128  23.508  1.00 30.99           C  
ANISOU 2590  CG1 VAL A7092     4735   2894   4145   -273   -173    237       C  
ATOM   2591  CG2 VAL A7092      87.393  -2.338  21.793  1.00 29.56           C  
ANISOU 2591  CG2 VAL A7092     4385   2826   4019   -215   -132    156       C  
ATOM   2592  N  ALEU A7093      89.452  -3.448  25.919  0.70 30.82           N  
ANISOU 2592  N  ALEU A7093     5075   2880   3754   -277   -164     70       N  
ATOM   2593  N  BLEU A7093      89.413  -3.466  25.916  0.30 31.18           N  
ANISOU 2593  N  BLEU A7093     5119   2924   3802   -278   -162     73       N  
ATOM   2594  CA ALEU A7093      89.940  -4.407  26.942  0.70 33.03           C  
ANISOU 2594  CA ALEU A7093     5532   3086   3930   -324   -301     87       C  
ATOM   2595  CA BLEU A7093      89.892  -4.398  26.971  0.30 33.20           C  
ANISOU 2595  CA BLEU A7093     5558   3106   3951   -327   -293     91       C  
ATOM   2596  C  ALEU A7093      88.968  -5.587  26.970  0.70 34.46           C  
ANISOU 2596  C  ALEU A7093     5712   3204   4177   -355   -322    179       C  
ATOM   2597  C  BLEU A7093      88.950  -5.601  27.011  0.30 34.50           C  
ANISOU 2597  C  BLEU A7093     5722   3205   4179   -357   -320    182       C  
ATOM   2598  O  ALEU A7093      87.757  -5.344  27.116  0.70 35.56           O  
ANISOU 2598  O  ALEU A7093     5819   3313   4379   -394   -130    265       O  
ATOM   2599  O  BLEU A7093      87.742  -5.390  27.237  0.30 35.31           O  
ANISOU 2599  O  BLEU A7093     5806   3272   4336   -402   -127    270       O  
ATOM   2600  CB ALEU A7093      90.014  -3.714  28.307  0.70 34.59           C  
ANISOU 2600  CB ALEU A7093     5961   3224   3955   -413   -183    103       C  
ATOM   2601  CB BLEU A7093      89.910  -3.680  28.324  0.30 34.61           C  
ANISOU 2601  CB BLEU A7093     5964   3225   3959   -415   -162    108       C  
ATOM   2602  CG ALEU A7093      90.392  -4.611  29.486  0.70 36.38           C  
ANISOU 2602  CG ALEU A7093     6429   3349   4042   -499   -329    145       C  
ATOM   2603  CG BLEU A7093      90.829  -2.466  28.406  0.30 34.58           C  
ANISOU 2603  CG BLEU A7093     5995   3266   3878   -411   -154     30       C  
ATOM   2604  CD1ALEU A7093      91.766  -5.234  29.284  0.70 36.34           C  
ANISOU 2604  CD1ALEU A7093     6387   3352   4069   -458   -642    102       C  
ATOM   2605  CD1BLEU A7093      90.885  -1.923  29.826  0.30 36.32           C  
ANISOU 2605  CD1BLEU A7093     6525   3389   3884   -529    -62     49       C  
ATOM   2606  CD2ALEU A7093      90.350  -3.828  30.792  0.70 37.95           C  
ANISOU 2606  CD2ALEU A7093     6927   3464   4027   -617   -187    160       C  
ATOM   2607  CD2BLEU A7093      92.219  -2.823  27.917  0.30 34.39           C  
ANISOU 2607  CD2BLEU A7093     5880   3284   3903   -354   -421    -32       C  
ATOM   2608  N   VAL A7094      89.480  -6.805  26.789  1.00 34.94           N  
ANISOU 2608  N   VAL A7094     5785   3232   4256   -333   -540    169       N  
ATOM   2609  CA  VAL A7094      88.627  -8.027  26.809  1.00 37.84           C  
ANISOU 2609  CA  VAL A7094     6166   3528   4680   -371   -593    256       C  
ATOM   2610  C   VAL A7094      88.795  -8.695  28.176  1.00 42.15           C  
ANISOU 2610  C   VAL A7094     6933   3980   5099   -451   -651    308       C  
ATOM   2611  O   VAL A7094      89.944  -9.004  28.539  1.00 41.43           O  
ANISOU 2611  O   VAL A7094     6926   3866   4946   -436   -839    264       O  
ATOM   2612  CB  VAL A7094      88.990  -8.981  25.660  1.00 36.86           C  
ANISOU 2612  CB  VAL A7094     5949   3402   4652   -303   -784    211       C  
ATOM   2613  CG1 VAL A7094      88.026 -10.154  25.591  1.00 37.91           C  
ANISOU 2613  CG1 VAL A7094     6098   3457   4848   -356   -846    307       C  
ATOM   2614  CG2 VAL A7094      89.040  -8.253  24.326  1.00 35.66           C  
ANISOU 2614  CG2 VAL A7094     5648   3328   4573   -244   -741    145       C  
ATOM   2615  N   ASN A7095      87.687  -8.895  28.893  1.00 49.53           N  
ANISOU 2615  N   ASN A7095     7955   4848   6014   -538   -495    413       N  
ATOM   2616  CA  ASN A7095      87.724  -9.538  30.235  1.00 57.95           C  
ANISOU 2616  CA  ASN A7095     9286   5805   6926   -642   -526    473       C  
ATOM   2617  C   ASN A7095      86.416 -10.307  30.466  1.00 63.02           C  
ANISOU 2617  C   ASN A7095     9929   6371   7642   -710   -408    597       C  
ATOM   2618  O   ASN A7095      85.580 -10.352  29.536  1.00 63.52           O  
ANISOU 2618  O   ASN A7095     9767   6467   7898   -675   -352    639       O  
ATOM   2619  CB  ASN A7095      88.023  -8.505  31.328  1.00 61.81           C  
ANISOU 2619  CB  ASN A7095    10005   6261   7217   -717   -377    455       C  
ATOM   2620  CG  ASN A7095      87.134  -7.281  31.255  1.00 64.87           C  
ANISOU 2620  CG  ASN A7095    10327   6672   7647   -715    -30    463       C  
ATOM   2621  OD1 ASN A7095      86.044  -7.327  30.687  1.00 70.38           O  
ANISOU 2621  OD1 ASN A7095    10831   7378   8531   -690    123    529       O  
ATOM   2622  ND2 ASN A7095      87.589  -6.178  31.828  1.00 67.11           N  
ANISOU 2622  ND2 ASN A7095    10769   6948   7779   -748     82    409       N  
ATOM   2623  N   ASN A7096      86.265 -10.906  31.651  1.00 70.77           N  
ANISOU 2623  N   ASN A7096    11164   7241   8482   -819   -394    665       N  
ATOM   2624  CA  ASN A7096      85.045 -11.685  32.003  1.00 75.79           C  
ANISOU 2624  CA  ASN A7096    11819   7787   9189   -900   -264    795       C  
ATOM   2625  C   ASN A7096      84.925 -11.760  33.531  1.00 80.56           C  
ANISOU 2625  C   ASN A7096    12784   8262   9562  -1041   -121    850       C  
ATOM   2626  O   ASN A7096      85.521 -10.956  34.251  1.00 83.29           O  
ANISOU 2626  O   ASN A7096    13354   8587   9705  -1083    -57    793       O  
ATOM   2627  CB  ASN A7096      85.054 -13.073  31.354  1.00 76.50           C  
ANISOU 2627  CB  ASN A7096    11809   7862   9394   -875   -541    826       C  
ATOM   2628  CG  ASN A7096      86.235 -13.930  31.766  1.00 77.55           C  
ANISOU 2628  CG  ASN A7096    12119   7950   9396   -876   -851    783       C  
ATOM   2629  OD1 ASN A7096      87.084 -13.503  32.546  1.00 79.22           O  
ANISOU 2629  OD1 ASN A7096    12524   8141   9434   -908   -901    743       O  
ATOM   2630  ND2 ASN A7096      86.299 -15.142  31.242  1.00 77.31           N  
ANISOU 2630  ND2 ASN A7096    12027   7884   9461   -848  -1076    801       N  
ATOM   2631  OXT ASN A7096      84.233 -12.620  34.082  1.00 84.77           O  
ANISOU 2631  OXT ASN A7096    13423   8694  10091  -1130    -68    953       O  
TER    2632      ASN A7096                                                      
ATOM   2633  N   ALA B4271      60.598 -11.480   8.293  1.00 62.99           N  
ANISOU 2633  N   ALA B4271     9964   5727   8241   -191   -141    242       N  
ATOM   2634  CA  ALA B4271      59.606 -10.468   7.810  1.00 63.62           C  
ANISOU 2634  CA  ALA B4271    10100   5750   8320   -203   -470    146       C  
ATOM   2635  C   ALA B4271      59.403  -9.373   8.866  1.00 60.53           C  
ANISOU 2635  C   ALA B4271     9201   5612   8184   -302   -448    156       C  
ATOM   2636  O   ALA B4271      59.002  -8.254   8.479  1.00 62.01           O  
ANISOU 2636  O   ALA B4271     9426   5779   8355   -274   -595    119       O  
ATOM   2637  CB  ALA B4271      58.302 -11.146   7.463  1.00 66.33           C  
ANISOU 2637  CB  ALA B4271    10537   5924   8740   -270   -921     -3       C  
ATOM   2638  N   PHE B4272      59.658  -9.682  10.144  1.00 56.47           N  
ANISOU 2638  N   PHE B4272     8301   5290   7862   -398   -285    200       N  
ATOM   2639  CA  PHE B4272      59.498  -8.672  11.225  1.00 53.37           C  
ANISOU 2639  CA  PHE B4272     7517   5096   7664   -475   -252    213       C  
ATOM   2640  C   PHE B4272      60.552  -7.572  11.073  1.00 54.04           C  
ANISOU 2640  C   PHE B4272     7595   5244   7694   -382    -64    300       C  
ATOM   2641  O   PHE B4272      61.719  -7.883  10.758  1.00 56.06           O  
ANISOU 2641  O   PHE B4272     7971   5439   7887   -286    176    381       O  
ATOM   2642  CB  PHE B4272      59.619  -9.295  12.618  1.00 49.81           C  
ANISOU 2642  CB  PHE B4272     6821   4757   7348   -558   -122    244       C  
ATOM   2643  CG  PHE B4272      59.627  -8.287  13.742  1.00 46.74           C  
ANISOU 2643  CG  PHE B4272     6163   4514   7079   -600    -68    269       C  
ATOM   2644  CD1 PHE B4272      58.466  -7.621  14.109  1.00 46.10           C  
ANISOU 2644  CD1 PHE B4272     5904   4450   7161   -693   -167    199       C  
ATOM   2645  CD2 PHE B4272      60.792  -8.002  14.437  1.00 44.46           C  
ANISOU 2645  CD2 PHE B4272     5806   4305   6781   -536     59    352       C  
ATOM   2646  CE1 PHE B4272      58.473  -6.691  15.139  1.00 44.79           C  
ANISOU 2646  CE1 PHE B4272     5565   4388   7065   -717    -90    226       C  
ATOM   2647  CE2 PHE B4272      60.797  -7.075  15.468  1.00 43.99           C  
ANISOU 2647  CE2 PHE B4272     5579   4336   6798   -560     54    365       C  
ATOM   2648  CZ  PHE B4272      59.638  -6.420  15.817  1.00 43.75           C  
ANISOU 2648  CZ  PHE B4272     5440   4332   6848   -648      3    309       C  
ATOM   2649  N   ALA B4273      60.132  -6.328  11.313  1.00 53.52           N  
ANISOU 2649  N   ALA B4273     7360   5266   7707   -414   -149    278       N  
ATOM   2650  CA  ALA B4273      61.022  -5.148  11.252  1.00 54.80           C  
ANISOU 2650  CA  ALA B4273     7471   5475   7875   -348     19    348       C  
ATOM   2651  C   ALA B4273      60.430  -4.045  12.132  1.00 53.54           C  
ANISOU 2651  C   ALA B4273     7015   5468   7857   -429    -91    320       C  
ATOM   2652  O   ALA B4273      59.255  -3.688  11.918  1.00 53.66           O  
ANISOU 2652  O   ALA B4273     7023   5464   7899   -473   -308    235       O  
ATOM   2653  CB  ALA B4273      61.184  -4.688   9.823  1.00 56.75           C  
ANISOU 2653  CB  ALA B4273     8116   5532   7915   -231     64    353       C  
ATOM   2654  N   VAL B4274      61.205  -3.562  13.106  1.00 53.15           N  
ANISOU 2654  N   VAL B4274     6738   5527   7928   -438     22    378       N  
ATOM   2655  CA  VAL B4274      60.742  -2.464  14.004  1.00 53.39           C  
ANISOU 2655  CA  VAL B4274     6554   5676   8055   -498    -56    360       C  
ATOM   2656  C   VAL B4274      60.440  -1.241  13.128  1.00 53.02           C  
ANISOU 2656  C   VAL B4274     6579   5607   7957   -464   -105    340       C  
ATOM   2657  O   VAL B4274      61.296  -0.899  12.285  1.00 55.59           O  
ANISOU 2657  O   VAL B4274     7055   5842   8222   -379     43    389       O  
ATOM   2658  CB  VAL B4274      61.795  -2.151  15.085  1.00 55.38           C  
ANISOU 2658  CB  VAL B4274     6642   5979   8418   -480      4    417       C  
ATOM   2659  CG1 VAL B4274      61.369  -0.998  15.981  1.00 56.66           C  
ANISOU 2659  CG1 VAL B4274     6675   6225   8628   -523    -76    401       C  
ATOM   2660  CG2 VAL B4274      62.126  -3.380  15.919  1.00 56.32           C  
ANISOU 2660  CG2 VAL B4274     6784   6071   8543   -478      4    430       C  
ATOM   2661  N   ASP B4275      59.261  -0.635  13.300  1.00 49.55           N  
ANISOU 2661  N   ASP B4275     6056   5204   7567   -517   -273    271       N  
ATOM   2662  CA  ASP B4275      58.866   0.557  12.500  1.00 49.16           C  
ANISOU 2662  CA  ASP B4275     6103   5114   7461   -470   -378    240       C  
ATOM   2663  C   ASP B4275      58.912   1.787  13.418  1.00 45.57           C  
ANISOU 2663  C   ASP B4275     5420   4785   7106   -506   -340    262       C  
ATOM   2664  O   ASP B4275      57.845   2.221  13.898  1.00 45.30           O  
ANISOU 2664  O   ASP B4275     5238   4784   7187   -559   -457    202       O  
ATOM   2665  CB  ASP B4275      57.501   0.348  11.838  1.00 50.39           C  
ANISOU 2665  CB  ASP B4275     6341   5153   7649   -474   -673    124       C  
ATOM   2666  CG  ASP B4275      57.110   1.450  10.866  1.00 53.55           C  
ANISOU 2666  CG  ASP B4275     6952   5448   7944   -383   -859     79       C  
ATOM   2667  OD1 ASP B4275      57.870   2.440  10.754  1.00 52.69           O  
ANISOU 2667  OD1 ASP B4275     6916   5376   7727   -334   -688    149       O  
ATOM   2668  OD2 ASP B4275      56.049   1.308  10.223  1.00 56.29           O  
ANISOU 2668  OD2 ASP B4275     7399   5641   8346   -356  -1198    -34       O  
ATOM   2669  N   ALA B4276      60.116   2.317  13.645  1.00 43.77           N  
ANISOU 2669  N   ALA B4276     5155   4587   6888   -476   -176    338       N  
ATOM   2670  CA  ALA B4276      60.319   3.485  14.535  1.00 41.46           C  
ANISOU 2670  CA  ALA B4276     4683   4383   6686   -503   -172    357       C  
ATOM   2671  C   ALA B4276      59.580   4.712  13.985  1.00 39.58           C  
ANISOU 2671  C   ALA B4276     4495   4142   6401   -485   -259    320       C  
ATOM   2672  O   ALA B4276      59.012   5.465  14.799  1.00 38.78           O  
ANISOU 2672  O   ALA B4276     4250   4117   6366   -527   -321    298       O  
ATOM   2673  CB  ALA B4276      61.796   3.752  14.686  1.00 41.74           C  
ANISOU 2673  CB  ALA B4276     4644   4379   6835   -469    -32    424       C  
ATOM   2674  N   ALA B4277      59.597   4.897  12.661  1.00 40.19           N  
ANISOU 2674  N   ALA B4277     4830   4096   6341   -407   -255    313       N  
ATOM   2675  CA  ALA B4277      58.925   6.050  12.014  1.00 40.74           C  
ANISOU 2675  CA  ALA B4277     5038   4113   6326   -357   -381    270       C  
ATOM   2676  C   ALA B4277      57.446   6.087  12.415  1.00 41.57           C  
ANISOU 2676  C   ALA B4277     4980   4258   6552   -400   -651    172       C  
ATOM   2677  O   ALA B4277      56.989   7.137  12.910  1.00 40.19           O  
ANISOU 2677  O   ALA B4277     4660   4147   6461   -418   -696    155       O  
ATOM   2678  CB  ALA B4277      59.087   5.965  10.517  1.00 43.23           C  
ANISOU 2678  CB  ALA B4277     5807   4211   6406   -235   -365    268       C  
ATOM   2679  N   LYS B4278      56.732   4.975  12.208  1.00 42.45           N  
ANISOU 2679  N   LYS B4278     5097   4303   6728   -418   -803    106       N  
ATOM   2680  CA  LYS B4278      55.290   4.892  12.563  1.00 43.63           C  
ANISOU 2680  CA  LYS B4278     5013   4418   7147   -470  -1025     -2       C  
ATOM   2681  C   LYS B4278      55.118   5.083  14.074  1.00 41.14           C  
ANISOU 2681  C   LYS B4278     4378   4233   7019   -571   -815     29       C  
ATOM   2682  O   LYS B4278      54.180   5.794  14.470  1.00 41.16           O  
ANISOU 2682  O   LYS B4278     4190   4216   7234   -590   -869    -25       O  
ATOM   2683  CB  LYS B4278      54.702   3.545  12.124  1.00 46.78           C  
ANISOU 2683  CB  LYS B4278     5444   4681   7648   -487  -1196    -79       C  
ATOM   2684  CG  LYS B4278      53.275   3.285  12.589  1.00 50.40           C  
ANISOU 2684  CG  LYS B4278     5560   5047   8540   -565  -1356   -197       C  
ATOM   2685  CD  LYS B4278      52.695   1.979  12.089  1.00 53.87           C  
ANISOU 2685  CD  LYS B4278     6012   5308   9147   -590  -1565   -290       C  
ATOM   2686  CE  LYS B4278      51.362   1.645  12.728  1.00 57.35           C  
ANISOU 2686  CE  LYS B4278     6013   5616  10159   -696  -1609   -402       C  
ATOM   2687  NZ  LYS B4278      50.371   2.732  12.536  1.00 60.39           N  
ANISOU 2687  NZ  LYS B4278     6190   5889  10867   -655  -1866   -506       N  
ATOM   2688  N   ALA B4279      56.006   4.484  14.873  1.00 40.23           N  
ANISOU 2688  N   ALA B4279     4258   4204   6823   -612   -592    112       N  
ATOM   2689  CA  ALA B4279      55.917   4.564  16.351  1.00 39.73           C  
ANISOU 2689  CA  ALA B4279     4057   4193   6843   -676   -404    144       C  
ATOM   2690  C   ALA B4279      56.028   6.022  16.819  1.00 39.31           C  
ANISOU 2690  C   ALA B4279     3973   4202   6761   -655   -379    170       C  
ATOM   2691  O   ALA B4279      55.276   6.410  17.737  1.00 40.27           O  
ANISOU 2691  O   ALA B4279     4000   4294   7007   -688   -275    153       O  
ATOM   2692  CB  ALA B4279      56.988   3.703  16.974  1.00 39.55           C  
ANISOU 2692  CB  ALA B4279     4131   4200   6692   -681   -279    217       C  
ATOM   2693  N   TYR B4280      56.923   6.804  16.208  1.00 39.31           N  
ANISOU 2693  N   TYR B4280     4068   4248   6620   -601   -425    210       N  
ATOM   2694  CA  TYR B4280      57.096   8.218  16.641  1.00 39.05           C  
ANISOU 2694  CA  TYR B4280     4011   4262   6565   -586   -411    233       C  
ATOM   2695  C   TYR B4280      55.879   9.045  16.204  1.00 40.09           C  
ANISOU 2695  C   TYR B4280     4077   4357   6797   -565   -524    161       C  
ATOM   2696  O   TYR B4280      55.375   9.838  17.023  1.00 39.93           O  
ANISOU 2696  O   TYR B4280     3969   4348   6853   -580   -465    156       O  
ATOM   2697  CB  TYR B4280      58.419   8.788  16.127  1.00 38.13           C  
ANISOU 2697  CB  TYR B4280     3978   4153   6357   -547   -378    292       C  
ATOM   2698  CG  TYR B4280      58.707  10.189  16.603  1.00 36.69           C  
ANISOU 2698  CG  TYR B4280     3764   3996   6180   -543   -374    313       C  
ATOM   2699  CD1 TYR B4280      58.796  10.476  17.957  1.00 36.77           C  
ANISOU 2699  CD1 TYR B4280     3737   4022   6209   -571   -375    325       C  
ATOM   2700  CD2 TYR B4280      58.928  11.222  15.708  1.00 37.24           C  
ANISOU 2700  CD2 TYR B4280     3911   4031   6205   -500   -364    320       C  
ATOM   2701  CE1 TYR B4280      59.073  11.758  18.408  1.00 36.08           C  
ANISOU 2701  CE1 TYR B4280     3654   3934   6120   -565   -405    338       C  
ATOM   2702  CE2 TYR B4280      59.208  12.508  16.142  1.00 36.32           C  
ANISOU 2702  CE2 TYR B4280     3764   3927   6110   -505   -357    336       C  
ATOM   2703  CZ  TYR B4280      59.278  12.779  17.497  1.00 36.04           C  
ANISOU 2703  CZ  TYR B4280     3653   3925   6117   -541   -395    342       C  
ATOM   2704  OH  TYR B4280      59.557  14.046  17.931  1.00 34.60           O  
ANISOU 2704  OH  TYR B4280     3469   3729   5947   -542   -421    352       O  
ATOM   2705  N   LYS B4281      55.413   8.849  14.965  1.00 43.21           N  
ANISOU 2705  N   LYS B4281     4551   4670   7193   -514   -708    101       N  
ATOM   2706  CA  LYS B4281      54.218   9.578  14.448  1.00 46.17           C  
ANISOU 2706  CA  LYS B4281     4869   4955   7717   -466   -928      6       C  
ATOM   2707  C   LYS B4281      53.009   9.291  15.349  1.00 46.99           C  
ANISOU 2707  C   LYS B4281     4662   5006   8183   -533   -878    -57       C  
ATOM   2708  O   LYS B4281      52.282  10.249  15.680  1.00 46.95           O  
ANISOU 2708  O   LYS B4281     4516   4970   8351   -518   -885    -93       O  
ATOM   2709  CB  LYS B4281      53.939   9.185  12.994  1.00 49.20           C  
ANISOU 2709  CB  LYS B4281     5484   5183   8024   -376  -1221    -64       C  
ATOM   2710  CG  LYS B4281      55.014   9.613  12.004  1.00 51.04           C  
ANISOU 2710  CG  LYS B4281     6115   5378   7900   -283  -1174      0       C  
ATOM   2711  CD  LYS B4281      54.777   9.129  10.591  1.00 54.74           C  
ANISOU 2711  CD  LYS B4281     6977   5623   8196   -164  -1438    -63       C  
ATOM   2712  CE  LYS B4281      55.917   9.478   9.659  1.00 56.19           C  
ANISOU 2712  CE  LYS B4281     7633   5701   8013    -66  -1237     22       C  
ATOM   2713  NZ  LYS B4281      55.671   8.992   8.281  1.00 60.10           N  
ANISOU 2713  NZ  LYS B4281     8669   5910   8255     81  -1482    -38       N  
ATOM   2714  N   ASP B4282      52.803   8.022  15.725  1.00 48.47           N  
ANISOU 2714  N   ASP B4282     4757   5150   8507   -602   -782    -69       N  
ATOM   2715  CA  ASP B4282      51.672   7.626  16.611  1.00 50.55           C  
ANISOU 2715  CA  ASP B4282     4738   5293   9176   -676   -610   -123       C  
ATOM   2716  C   ASP B4282      51.860   8.270  17.992  1.00 49.00           C  
ANISOU 2716  C   ASP B4282     4566   5144   8905   -700   -262    -43       C  
ATOM   2717  O   ASP B4282      50.854   8.707  18.581  1.00 49.19           O  
ANISOU 2717  O   ASP B4282     4400   5041   9249   -715    -96    -84       O  
ATOM   2718  CB  ASP B4282      51.547   6.101  16.702  1.00 52.98           C  
ANISOU 2718  CB  ASP B4282     5004   5519   9604   -745   -536   -142       C  
ATOM   2719  CG  ASP B4282      51.156   5.430  15.393  1.00 55.46           C  
ANISOU 2719  CG  ASP B4282     5314   5717  10039   -716   -918   -245       C  
ATOM   2720  OD1 ASP B4282      50.709   6.146  14.473  1.00 57.78           O  
ANISOU 2720  OD1 ASP B4282     5620   5934  10399   -633  -1266   -326       O  
ATOM   2721  OD2 ASP B4282      51.311   4.194  15.299  1.00 55.80           O  
ANISOU 2721  OD2 ASP B4282     5399   5717  10082   -762   -894   -248       O  
ATOM   2722  N   TYR B4283      53.105   8.321  18.477  1.00 47.38           N  
ANISOU 2722  N   TYR B4283     4605   5068   8327   -692   -172     59       N  
ATOM   2723  CA  TYR B4283      53.451   8.942  19.785  1.00 46.65           C  
ANISOU 2723  CA  TYR B4283     4661   4978   8083   -687     57    129       C  
ATOM   2724  C   TYR B4283      53.071  10.430  19.774  1.00 46.39           C  
ANISOU 2724  C   TYR B4283     4576   4960   8089   -645     19    115       C  
ATOM   2725  O   TYR B4283      52.448  10.895  20.751  1.00 47.46           O  
ANISOU 2725  O   TYR B4283     4728   4987   8318   -644    264    122       O  
ATOM   2726  CB  TYR B4283      54.937   8.710  20.080  1.00 45.64           C  
ANISOU 2726  CB  TYR B4283     4767   4944   7630   -669      0    209       C  
ATOM   2727  CG  TYR B4283      55.540   9.597  21.139  1.00 45.41           C  
ANISOU 2727  CG  TYR B4283     4941   4901   7411   -634     43    262       C  
ATOM   2728  CD1 TYR B4283      55.488   9.260  22.482  1.00 46.09           C  
ANISOU 2728  CD1 TYR B4283     5288   4841   7381   -619    232    292       C  
ATOM   2729  CD2 TYR B4283      56.199  10.765  20.789  1.00 44.96           C  
ANISOU 2729  CD2 TYR B4283     4879   4928   7273   -603   -116    277       C  
ATOM   2730  CE1 TYR B4283      56.059  10.070  23.452  1.00 46.99           C  
ANISOU 2730  CE1 TYR B4283     5682   4887   7282   -564    191    327       C  
ATOM   2731  CE2 TYR B4283      56.773  11.586  21.744  1.00 44.36           C  
ANISOU 2731  CE2 TYR B4283     4993   4807   7053   -572   -143    311       C  
ATOM   2732  CZ  TYR B4283      56.706  11.238  23.081  1.00 46.17           C  
ANISOU 2732  CZ  TYR B4283     5510   4883   7146   -545    -26    331       C  
ATOM   2733  OH  TYR B4283      57.272  12.047  24.022  1.00 46.36           O  
ANISOU 2733  OH  TYR B4283     5808   4811   6996   -492   -126    351       O  
ATOM   2734  N   LEU B4284      53.446  11.151  18.710  1.00 44.86           N  
ANISOU 2734  N   LEU B4284     4376   4862   7806   -601   -236    103       N  
ATOM   2735  CA  LEU B4284      53.110  12.598  18.587  1.00 44.72           C  
ANISOU 2735  CA  LEU B4284     4331   4853   7805   -551   -299     87       C  
ATOM   2736  C   LEU B4284      51.584  12.766  18.542  1.00 47.11           C  
ANISOU 2736  C   LEU B4284     4376   5011   8513   -541   -284     -6       C  
ATOM   2737  O   LEU B4284      51.074  13.676  19.222  1.00 47.73           O  
ANISOU 2737  O   LEU B4284     4413   5034   8686   -521   -129     -4       O  
ATOM   2738  CB  LEU B4284      53.765  13.169  17.325  1.00 42.91           C  
ANISOU 2738  CB  LEU B4284     4211   4692   7399   -495   -540     88       C  
ATOM   2739  CG  LEU B4284      55.294  13.228  17.338  1.00 41.10           C  
ANISOU 2739  CG  LEU B4284     4154   4548   6913   -505   -499    175       C  
ATOM   2740  CD1 LEU B4284      55.827  13.647  15.977  1.00 40.96           C  
ANISOU 2740  CD1 LEU B4284     4281   4513   6767   -445   -614    178       C  
ATOM   2741  CD2 LEU B4284      55.797  14.168  18.423  1.00 40.38           C  
ANISOU 2741  CD2 LEU B4284     4119   4481   6741   -517   -406    225       C  
ATOM   2742  N   ALA B4285      50.895  11.912  17.779  1.00 49.67           N  
ANISOU 2742  N   ALA B4285     4523   5239   9110   -549   -452    -94       N  
ATOM   2743  CA  ALA B4285      49.416  11.949  17.637  1.00 53.65           C  
ANISOU 2743  CA  ALA B4285     4683   5537  10165   -540   -510   -215       C  
ATOM   2744  C   ALA B4285      48.729  11.754  18.998  1.00 56.47           C  
ANISOU 2744  C   ALA B4285     4884   5747  10826   -602    -24   -196       C  
ATOM   2745  O   ALA B4285      47.625  12.297  19.191  1.00 59.33           O  
ANISOU 2745  O   ALA B4285     4961   5926  11655   -582     66   -268       O  
ATOM   2746  CB  ALA B4285      48.977  10.898  16.647  1.00 54.25           C  
ANISOU 2746  CB  ALA B4285     4636   5498  10478   -545   -824   -318       C  
ATOM   2747  N  ASER B4286      49.370  11.006  19.905  0.50 56.39           N  
ANISOU 2747  N  ASER B4286     5093   5768  10563   -660    291   -104       N  
ATOM   2748  N  BSER B4286      49.368  11.006  19.906  0.50 56.40           N  
ANISOU 2748  N  BSER B4286     5094   5769  10566   -660    292   -104       N  
ATOM   2749  CA ASER B4286      48.812  10.737  21.259  0.50 58.54           C  
ANISOU 2749  CA ASER B4286     5394   5833  11015   -698    833    -68       C  
ATOM   2750  CA BSER B4286      48.805  10.739  21.258  0.50 58.57           C  
ANISOU 2750  CA BSER B4286     5396   5836  11021   -698    834    -68       C  
ATOM   2751  C  ASER B4286      49.152  11.881  22.224  0.50 58.52           C  
ANISOU 2751  C  ASER B4286     5689   5842  10701   -640   1055     15       C  
ATOM   2752  C  BSER B4286      49.138  11.888  22.221  0.50 58.54           C  
ANISOU 2752  C  BSER B4286     5688   5844  10710   -640   1056     14       C  
ATOM   2753  O  ASER B4286      48.858  11.735  23.428  0.50 60.79           O  
ANISOU 2753  O  ASER B4286     6185   5923  10988   -641   1535     64       O  
ATOM   2754  O  BSER B4286      48.823  11.752  23.421  0.50 60.84           O  
ANISOU 2754  O  BSER B4286     6180   5925  11009   -641   1538     62       O  
ATOM   2755  CB ASER B4286      49.308   9.416  21.786  0.50 59.00           C  
ANISOU 2755  CB ASER B4286     5661   5860  10895   -755   1035    -14       C  
ATOM   2756  CB BSER B4286      49.306   9.426  21.797  0.50 59.04           C  
ANISOU 2756  CB BSER B4286     5668   5865  10900   -754   1038    -14       C  
ATOM   2757  OG ASER B4286      48.916   8.351  20.932  0.50 60.17           O  
ANISOU 2757  OG ASER B4286     5539   5965  11355   -811    846    -97       O  
ATOM   2758  OG BSER B4286      50.716   9.450  21.957  0.50 56.93           O  
ANISOU 2758  OG BSER B4286     5778   5802  10049   -724    879     76       O  
ATOM   2759  N   GLY B4287      49.754  12.965  21.716  1.00 55.91           N  
ANISOU 2759  N   GLY B4287     5436   5704  10102   -586    738     29       N  
ATOM   2760  CA  GLY B4287      50.115  14.136  22.544  1.00 54.88           C  
ANISOU 2760  CA  GLY B4287     5588   5579   9681   -531    871     96       C  
ATOM   2761  C   GLY B4287      51.511  14.035  23.149  1.00 52.92           C  
ANISOU 2761  C   GLY B4287     5766   5433   8907   -524    800    187       C  
ATOM   2762  O   GLY B4287      51.807  14.829  24.068  1.00 53.72           O  
ANISOU 2762  O   GLY B4287     6184   5465   8761   -475    913    237       O  
ATOM   2763  N   GLY B4288      52.346  13.120  22.646  1.00 49.59           N  
ANISOU 2763  N   GLY B4288     5358   5135   8349   -559    588    198       N  
ATOM   2764  CA  GLY B4288      53.718  12.942  23.165  1.00 48.56           C  
ANISOU 2764  CA  GLY B4288     5553   5059   7837   -544    456    263       C  
ATOM   2765  C   GLY B4288      54.599  14.151  22.881  1.00 46.22           C  
ANISOU 2765  C   GLY B4288     5305   4884   7372   -515    194    281       C  
ATOM   2766  O   GLY B4288      54.433  14.768  21.808  1.00 45.37           O  
ANISOU 2766  O   GLY B4288     4971   4888   7378   -516     49    250       O  
ATOM   2767  N   GLN B4289      55.503  14.476  23.810  1.00 53.10           N  
ANISOU 2767  N   GLN B4289     5292   5715   9167   -479    780    884       N  
ATOM   2768  CA  GLN B4289      56.425  15.635  23.658  1.00 50.75           C  
ANISOU 2768  CA  GLN B4289     5183   5496   8601   -369    710    787       C  
ATOM   2769  C   GLN B4289      57.506  15.294  22.634  1.00 45.24           C  
ANISOU 2769  C   GLN B4289     4626   4816   7748   -415    431    689       C  
ATOM   2770  O   GLN B4289      58.142  14.246  22.725  1.00 43.67           O  
ANISOU 2770  O   GLN B4289     4537   4582   7472   -481    397    688       O  
ATOM   2771  CB  GLN B4289      57.046  16.003  25.009  1.00 53.80           C  
ANISOU 2771  CB  GLN B4289     5793   5912   8733   -283    951    802       C  
ATOM   2772  CG  GLN B4289      56.028  16.451  26.052  1.00 59.45           C  
ANISOU 2772  CG  GLN B4289     6411   6616   9561   -217   1266    884       C  
ATOM   2773  CD  GLN B4289      55.319  17.733  25.684  1.00 62.17           C  
ANISOU 2773  CD  GLN B4289     6602   6974  10042   -121   1279    853       C  
ATOM   2774  OE1 GLN B4289      55.783  18.514  24.855  1.00 64.88           O  
ANISOU 2774  OE1 GLN B4289     6984   7348  10316    -83   1073    767       O  
ATOM   2775  NE2 GLN B4289      54.182  17.969  26.319  1.00 67.79           N  
ANISOU 2775  NE2 GLN B4289     7138   7657  10961    -75   1537    932       N  
ATOM   2776  N   PRO B4290      57.740  16.161  21.622  1.00 41.28           N  
ANISOU 2776  N   PRO B4290     4124   4361   7199   -377    236    611       N  
ATOM   2777  CA  PRO B4290      58.767  15.912  20.610  1.00 38.20           C  
ANISOU 2777  CA  PRO B4290     3871   3992   6648   -412      1    519       C  
ATOM   2778  C   PRO B4290      60.176  15.635  21.162  1.00 35.09           C  
ANISOU 2778  C   PRO B4290     3728   3618   5986   -389     44    484       C  
ATOM   2779  O   PRO B4290      60.489  16.086  22.254  1.00 34.16           O  
ANISOU 2779  O   PRO B4290     3713   3522   5744   -323    219    512       O  
ATOM   2780  CB  PRO B4290      58.814  17.225  19.813  1.00 38.37           C  
ANISOU 2780  CB  PRO B4290     3884   4070   6622   -340   -124    472       C  
ATOM   2781  CG  PRO B4290      57.429  17.816  19.981  1.00 40.89           C  
ANISOU 2781  CG  PRO B4290     3967   4372   7198   -304    -45    544       C  
ATOM   2782  CD  PRO B4290      57.001  17.409  21.375  1.00 42.22           C  
ANISOU 2782  CD  PRO B4290     4106   4505   7429   -294    242    619       C  
ATOM   2783  N   ILE B4291      60.975  14.896  20.388  1.00 32.34           N  
ANISOU 2783  N   ILE B4291     3469   3256   5559   -442   -117    422       N  
ATOM   2784  CA  ILE B4291      62.392  14.595  20.748  1.00 31.01           C  
ANISOU 2784  CA  ILE B4291     3511   3103   5167   -417   -108    391       C  
ATOM   2785  C   ILE B4291      63.123  15.928  20.955  1.00 29.61           C  
ANISOU 2785  C   ILE B4291     3442   3004   4803   -325    -92    358       C  
ATOM   2786  O   ILE B4291      63.011  16.819  20.083  1.00 28.64           O  
ANISOU 2786  O   ILE B4291     3282   2918   4682   -302   -199    314       O  
ATOM   2787  CB  ILE B4291      63.040  13.705  19.670  1.00 30.66           C  
ANISOU 2787  CB  ILE B4291     3520   3027   5101   -475   -283    316       C  
ATOM   2788  CG1 ILE B4291      62.459  12.289  19.730  1.00 31.98           C  
ANISOU 2788  CG1 ILE B4291     3616   3088   5446   -569   -276    349       C  
ATOM   2789  CG2 ILE B4291      64.559  13.700  19.796  1.00 29.71           C  
ANISOU 2789  CG2 ILE B4291     3582   2937   4769   -426   -295    277       C  
ATOM   2790  CD1 ILE B4291      62.879  11.392  18.596  1.00 32.48           C  
ANISOU 2790  CD1 ILE B4291     3727   3096   5518   -631   -447    254       C  
ATOM   2791  N   THR B4292      63.814  16.055  22.087  1.00 28.91           N  
ANISOU 2791  N   THR B4292     3489   2931   4564   -281     29    384       N  
ATOM   2792  CA  THR B4292      64.532  17.305  22.444  1.00 28.55           C  
ANISOU 2792  CA  THR B4292     3558   2943   4346   -207     45    347       C  
ATOM   2793  C   THR B4292      66.015  17.205  22.078  1.00 26.62           C  
ANISOU 2793  C   THR B4292     3442   2726   3943   -206    -74    296       C  
ATOM   2794  O   THR B4292      66.443  16.164  21.540  1.00 25.46           O  
ANISOU 2794  O   THR B4292     3298   2553   3821   -249   -152    287       O  
ATOM   2795  CB  THR B4292      64.388  17.588  23.945  1.00 30.29           C  
ANISOU 2795  CB  THR B4292     3862   3164   4479   -162    237    395       C  
ATOM   2796  OG1 THR B4292      64.933  16.469  24.646  1.00 30.90           O  
ANISOU 2796  OG1 THR B4292     4032   3221   4485   -191    272    448       O  
ATOM   2797  CG2 THR B4292      62.954  17.815  24.368  1.00 32.69           C  
ANISOU 2797  CG2 THR B4292     4033   3442   4945   -146    401    446       C  
ATOM   2798  N   ASN B4293      66.746  18.291  22.333  1.00 26.21           N  
ANISOU 2798  N   ASN B4293     3486   2716   3757   -158    -82    261       N  
ATOM   2799  CA  ASN B4293      68.221  18.372  22.162  1.00 25.44           C  
ANISOU 2799  CA  ASN B4293     3495   2648   3523   -154   -177    226       C  
ATOM   2800  C   ASN B4293      68.633  18.291  20.691  1.00 23.63           C  
ANISOU 2800  C   ASN B4293     3223   2430   3325   -176   -308    178       C  
ATOM   2801  O   ASN B4293      69.794  17.936  20.432  1.00 23.49           O  
ANISOU 2801  O   ASN B4293     3260   2423   3238   -180   -367    159       O  
ATOM   2802  CB  ASN B4293      68.919  17.372  23.081  1.00 26.95           C  
ANISOU 2802  CB  ASN B4293     3771   2825   3642   -161   -149    271       C  
ATOM   2803  CG  ASN B4293      68.757  17.780  24.527  1.00 29.38           C  
ANISOU 2803  CG  ASN B4293     4177   3141   3844   -131    -33    308       C  
ATOM   2804  OD1 ASN B4293      68.826  18.965  24.838  1.00 33.22           O  
ANISOU 2804  OD1 ASN B4293     4717   3650   4253   -100    -15    267       O  
ATOM   2805  ND2 ASN B4293      68.525  16.823  25.406  1.00 32.17           N  
ANISOU 2805  ND2 ASN B4293     4569   3467   4186   -141     50    384       N  
ATOM   2806  N   CYS B4294      67.725  18.602  19.763  1.00 23.56           N  
ANISOU 2806  N   CYS B4294     3120   2419   3412   -188   -353    164       N  
ATOM   2807  CA  CYS B4294      68.182  18.797  18.365  1.00 22.90           C  
ANISOU 2807  CA  CYS B4294     3038   2359   3302   -201   -476    119       C  
ATOM   2808  C   CYS B4294      69.103  20.026  18.422  1.00 21.94           C  
ANISOU 2808  C   CYS B4294     2990   2273   3072   -166   -482    106       C  
ATOM   2809  O   CYS B4294      68.733  21.004  19.104  1.00 22.93           O  
ANISOU 2809  O   CYS B4294     3120   2392   3198   -133   -424    120       O  
ATOM   2810  CB  CYS B4294      67.013  18.981  17.408  1.00 24.12           C  
ANISOU 2810  CB  CYS B4294     3092   2509   3563   -220   -549    118       C  
ATOM   2811  SG  CYS B4294      65.937  17.523  17.343  1.00 26.26           S  
ANISOU 2811  SG  CYS B4294     3260   2722   3995   -286   -562    128       S  
ATOM   2812  N   VAL B4295      70.269  19.957  17.781  1.00 20.93           N  
ANISOU 2812  N   VAL B4295     2915   2169   2868   -173   -535     80       N  
ATOM   2813  CA  VAL B4295      71.309  21.020  17.916  1.00 20.30           C  
ANISOU 2813  CA  VAL B4295     2892   2112   2707   -156   -539     77       C  
ATOM   2814  C   VAL B4295      71.050  22.166  16.932  1.00 20.32           C  
ANISOU 2814  C   VAL B4295     2885   2125   2708   -150   -584     80       C  
ATOM   2815  O   VAL B4295      71.385  22.027  15.741  1.00 20.72           O  
ANISOU 2815  O   VAL B4295     2944   2199   2727   -164   -636     72       O  
ATOM   2816  CB  VAL B4295      72.711  20.413  17.742  1.00 19.84           C  
ANISOU 2816  CB  VAL B4295     2868   2070   2599   -165   -556     65       C  
ATOM   2817  CG1 VAL B4295      73.805  21.465  17.852  1.00 20.03           C  
ANISOU 2817  CG1 VAL B4295     2924   2113   2574   -164   -569     69       C  
ATOM   2818  CG2 VAL B4295      72.946  19.288  18.741  1.00 19.71           C  
ANISOU 2818  CG2 VAL B4295     2864   2032   2593   -162   -526     82       C  
ATOM   2819  N   LYS B4296      70.500  23.269  17.435  1.00 20.44           N  
ANISOU 2819  N   LYS B4296     2897   2117   2751   -123   -555     95       N  
ATOM   2820  CA  LYS B4296      70.234  24.443  16.569  1.00 20.95           C  
ANISOU 2820  CA  LYS B4296     2955   2174   2830   -107   -600    117       C  
ATOM   2821  C   LYS B4296      71.532  25.240  16.396  1.00 20.03           C  
ANISOU 2821  C   LYS B4296     2905   2060   2645   -123   -609    117       C  
ATOM   2822  O   LYS B4296      72.216  25.505  17.397  1.00 20.06           O  
ANISOU 2822  O   LYS B4296     2951   2047   2624   -129   -576     96       O  
ATOM   2823  CB  LYS B4296      69.116  25.312  17.141  1.00 22.18           C  
ANISOU 2823  CB  LYS B4296     3071   2281   3072    -61   -556    133       C  
ATOM   2824  CG  LYS B4296      68.590  26.332  16.147  1.00 23.42           C  
ANISOU 2824  CG  LYS B4296     3200   2420   3279    -35   -620    177       C  
ATOM   2825  CD  LYS B4296      67.257  26.925  16.529  1.00 25.99           C  
ANISOU 2825  CD  LYS B4296     3443   2694   3738     24   -581    202       C  
ATOM   2826  CE  LYS B4296      67.321  27.851  17.715  1.00 26.30           C  
ANISOU 2826  CE  LYS B4296     3536   2668   3788     69   -469    172       C  
ATOM   2827  NZ  LYS B4296      66.021  28.525  17.935  1.00 27.77           N  
ANISOU 2827  NZ  LYS B4296     3633   2793   4123    146   -414    199       N  
ATOM   2828  N   MET B4297      71.834  25.620  15.157  1.00 20.48           N  
ANISOU 2828  N   MET B4297     2973   2135   2673   -135   -658    145       N  
ATOM   2829  CA  MET B4297      73.094  26.335  14.858  1.00 20.21           C  
ANISOU 2829  CA  MET B4297     2982   2099   2594   -160   -651    162       C  
ATOM   2830  C   MET B4297      72.859  27.845  14.797  1.00 21.19           C  
ANISOU 2830  C   MET B4297     3127   2164   2758   -147   -658    201       C  
ATOM   2831  O   MET B4297      71.720  28.290  14.464  1.00 21.28           O  
ANISOU 2831  O   MET B4297     3117   2150   2818   -108   -685    232       O  
ATOM   2832  CB  MET B4297      73.652  25.900  13.497  1.00 21.16           C  
ANISOU 2832  CB  MET B4297     3121   2270   2647   -180   -667    182       C  
ATOM   2833  CG  MET B4297      73.684  24.394  13.286  1.00 21.17           C  
ANISOU 2833  CG  MET B4297     3112   2310   2619   -183   -665    135       C  
ATOM   2834  SD  MET B4297      74.517  23.495  14.611  1.00 20.98           S  
ANISOU 2834  SD  MET B4297     3064   2280   2627   -187   -619     97       S  
ATOM   2835  CE  MET B4297      76.149  24.232  14.559  1.00 20.81           C  
ANISOU 2835  CE  MET B4297     3042   2265   2598   -211   -589    124       C  
ATOM   2836  N   LEU B4298      73.913  28.597  15.109  1.00 21.28           N  
ANISOU 2836  N   LEU B4298     3172   2144   2770   -180   -641    204       N  
ATOM   2837  CA  LEU B4298      73.903  30.056  14.865  1.00 21.98           C  
ANISOU 2837  CA  LEU B4298     3291   2156   2904   -180   -648    248       C  
ATOM   2838  C   LEU B4298      74.218  30.245  13.379  1.00 22.60           C  
ANISOU 2838  C   LEU B4298     3381   2266   2939   -197   -663    329       C  
ATOM   2839  O   LEU B4298      75.126  29.556  12.873  1.00 22.97           O  
ANISOU 2839  O   LEU B4298     3423   2376   2927   -230   -640    331       O  
ATOM   2840  CB  LEU B4298      74.945  30.727  15.756  1.00 21.91           C  
ANISOU 2840  CB  LEU B4298     3313   2092   2920   -227   -637    215       C  
ATOM   2841  CG  LEU B4298      74.556  30.782  17.229  1.00 22.31           C  
ANISOU 2841  CG  LEU B4298     3398   2099   2978   -207   -624    134       C  
ATOM   2842  CD1 LEU B4298      75.767  31.002  18.106  1.00 23.13           C  
ANISOU 2842  CD1 LEU B4298     3535   2181   3071   -271   -652     89       C  
ATOM   2843  CD2 LEU B4298      73.504  31.853  17.463  1.00 22.43           C  
ANISOU 2843  CD2 LEU B4298     3446   2018   3059   -152   -599    129       C  
ATOM   2844  N   CYS B4299      73.469  31.105  12.701  1.00 23.27           N  
ANISOU 2844  N   CYS B4299     3484   2308   3050   -166   -695    398       N  
ATOM   2845  CA  CYS B4299      73.730  31.340  11.260  1.00 24.78           C  
ANISOU 2845  CA  CYS B4299     3715   2530   3167   -180   -713    491       C  
ATOM   2846  C   CYS B4299      73.168  32.712  10.875  1.00 25.46           C  
ANISOU 2846  C   CYS B4299     3831   2524   3318   -151   -746    585       C  
ATOM   2847  O   CYS B4299      72.546  33.364  11.742  1.00 25.16           O  
ANISOU 2847  O   CYS B4299     3772   2396   3391   -112   -748    558       O  
ATOM   2848  CB  CYS B4299      73.176  30.197  10.414  1.00 25.52           C  
ANISOU 2848  CB  CYS B4299     3812   2719   3164   -164   -759    482       C  
ATOM   2849  SG  CYS B4299      71.405  29.899  10.641  1.00 28.37           S  
ANISOU 2849  SG  CYS B4299     4109   3072   3597   -103   -851    466       S  
ATOM   2850  N   THR B4300      73.428  33.139   9.641  1.00 26.33           N  
ANISOU 2850  N   THR B4300     3998   2647   3356   -165   -759    693       N  
ATOM   2851  CA  THR B4300      72.994  34.469   9.137  1.00 27.80           C  
ANISOU 2851  CA  THR B4300     4225   2736   3602   -137   -795    814       C  
ATOM   2852  C   THR B4300      71.491  34.507   8.839  1.00 28.06           C  
ANISOU 2852  C   THR B4300     4228   2763   3669    -55   -904    851       C  
ATOM   2853  O   THR B4300      70.929  35.613   8.842  1.00 28.37           O  
ANISOU 2853  O   THR B4300     4268   2691   3818     -6   -935    929       O  
ATOM   2854  CB  THR B4300      73.754  34.814   7.852  1.00 29.19           C  
ANISOU 2854  CB  THR B4300     4485   2940   3665   -179   -767    938       C  
ATOM   2855  OG1 THR B4300      73.433  33.801   6.898  1.00 29.07           O  
ANISOU 2855  OG1 THR B4300     4509   3050   3484   -167   -814    940       O  
ATOM   2856  CG2 THR B4300      75.252  34.880   8.051  1.00 29.34           C  
ANISOU 2856  CG2 THR B4300     4502   2956   3689   -262   -650    926       C  
ATOM   2857  N   HIS B4301      70.873  33.350   8.584  1.00 27.42           N  
ANISOU 2857  N   HIS B4301     4114   2785   3519    -41   -965    802       N  
ATOM   2858  CA  HIS B4301      69.444  33.295   8.162  1.00 28.43           C  
ANISOU 2858  CA  HIS B4301     4191   2919   3692     22  -1097    849       C  
ATOM   2859  C   HIS B4301      69.275  34.023   6.818  1.00 30.36           C  
ANISOU 2859  C   HIS B4301     4520   3159   3855     37  -1193   1006       C  
ATOM   2860  O   HIS B4301      68.185  34.570   6.574  1.00 31.94           O  
ANISOU 2860  O   HIS B4301     4672   3311   4153    105  -1306   1089       O  
ATOM   2861  CB  HIS B4301      68.509  33.790   9.273  1.00 28.16           C  
ANISOU 2861  CB  HIS B4301     4049   2787   3863     92  -1081    817       C  
ATOM   2862  CG  HIS B4301      68.521  32.882  10.453  1.00 27.38           C  
ANISOU 2862  CG  HIS B4301     3888   2716   3797     78  -1000    678       C  
ATOM   2863  ND1 HIS B4301      67.611  31.850  10.601  1.00 27.47           N  
ANISOU 2863  ND1 HIS B4301     3808   2787   3840     92  -1046    631       N  
ATOM   2864  CD2 HIS B4301      69.366  32.804  11.503  1.00 26.22           C  
ANISOU 2864  CD2 HIS B4301     3764   2548   3650     44   -887    586       C  
ATOM   2865  CE1 HIS B4301      67.883  31.190  11.712  1.00 26.58           C  
ANISOU 2865  CE1 HIS B4301     3671   2685   3741     72   -946    526       C  
ATOM   2866  NE2 HIS B4301      68.962  31.750  12.279  1.00 26.25           N  
ANISOU 2866  NE2 HIS B4301     3704   2600   3669     46   -858    496       N  
ATOM   2867  N   THR B4302      70.328  34.026   5.993  1.00 31.04           N  
ANISOU 2867  N   THR B4302     4724   3293   3774    -19  -1143   1053       N  
ATOM   2868  CA  THR B4302      70.308  34.592   4.615  1.00 33.61           C  
ANISOU 2868  CA  THR B4302     5171   3635   3963    -16  -1217   1213       C  
ATOM   2869  C   THR B4302      70.783  33.505   3.639  1.00 34.34           C  
ANISOU 2869  C   THR B4302     5371   3867   3807    -64  -1218   1177       C  
ATOM   2870  O   THR B4302      71.328  33.861   2.571  1.00 35.80           O  
ANISOU 2870  O   THR B4302     5697   4083   3823    -86  -1194   1287       O  
ATOM   2871  CB  THR B4302      71.153  35.872   4.516  1.00 34.82           C  
ANISOU 2871  CB  THR B4302     5387   3684   4157    -36  -1117   1330       C  
ATOM   2872  OG1 THR B4302      72.513  35.546   4.801  1.00 34.33           O  
ANISOU 2872  OG1 THR B4302     5343   3651   4050   -113   -955   1262       O  
ATOM   2873  CG2 THR B4302      70.687  36.960   5.457  1.00 35.13           C  
ANISOU 2873  CG2 THR B4302     5344   3563   4438     13  -1113   1347       C  
ATOM   2874  N   GLY B4303      70.549  32.233   3.992  1.00 33.07           N  
ANISOU 2874  N   GLY B4303     5157   3780   3628    -77  -1237   1030       N  
ATOM   2875  CA  GLY B4303      70.984  31.073   3.189  1.00 33.48           C  
ANISOU 2875  CA  GLY B4303     5313   3945   3463   -117  -1227    958       C  
ATOM   2876  C   GLY B4303      70.033  30.740   2.048  1.00 35.41           C  
ANISOU 2876  C   GLY B4303     5647   4253   3554   -106  -1425    997       C  
ATOM   2877  O   GLY B4303      69.007  31.436   1.893  1.00 36.12           O  
ANISOU 2877  O   GLY B4303     5693   4302   3728    -63  -1583   1100       O  
ATOM   2878  N   THR B4304      70.365  29.690   1.291  1.00 35.94           N  
ANISOU 2878  N   THR B4304     5835   4411   3409   -142  -1422    913       N  
ATOM   2879  CA  THR B4304      69.585  29.247   0.102  1.00 38.47           C  
ANISOU 2879  CA  THR B4304     6284   4801   3529   -148  -1625    926       C  
ATOM   2880  C   THR B4304      68.199  28.732   0.510  1.00 38.03           C  
ANISOU 2880  C   THR B4304     6083   4732   3635   -140  -1837    868       C  
ATOM   2881  O   THR B4304      67.284  28.787  -0.331  1.00 39.16           O  
ANISOU 2881  O   THR B4304     6279   4906   3694   -137  -2066    929       O  
ATOM   2882  CB  THR B4304      70.335  28.152  -0.666  1.00 39.74           C  
ANISOU 2882  CB  THR B4304     6619   5045   3435   -189  -1542    809       C  
ATOM   2883  OG1 THR B4304      70.401  26.994   0.166  1.00 38.39           O  
ANISOU 2883  OG1 THR B4304     6338   4864   3382   -207  -1489    634       O  
ATOM   2884  CG2 THR B4304      71.729  28.568  -1.083  1.00 40.50           C  
ANISOU 2884  CG2 THR B4304     6836   5158   3391   -195  -1302    866       C  
ATOM   2885  N   GLY B4305      68.055  28.242   1.742  1.00 36.10           N  
ANISOU 2885  N   GLY B4305     5661   4444   3611   -140  -1766    765       N  
ATOM   2886  CA  GLY B4305      66.765  27.694   2.202  1.00 36.28           C  
ANISOU 2886  CA  GLY B4305     5522   4448   3813   -139  -1930    715       C  
ATOM   2887  C   GLY B4305      66.572  26.241   1.785  1.00 36.55           C  
ANISOU 2887  C   GLY B4305     5611   4533   3741   -201  -2014    569       C  
ATOM   2888  O   GLY B4305      65.481  25.703   2.046  1.00 37.41           O  
ANISOU 2888  O   GLY B4305     5586   4626   4001   -218  -2166    530       O  
ATOM   2889  N   GLN B4306      67.579  25.625   1.151  1.00 36.72           N  
ANISOU 2889  N   GLN B4306     5817   4604   3529   -233  -1913    490       N  
ATOM   2890  CA  GLN B4306      67.484  24.190   0.761  1.00 37.60           C  
ANISOU 2890  CA  GLN B4306     6004   4741   3539   -289  -1973    327       C  
ATOM   2891  C   GLN B4306      67.350  23.334   2.031  1.00 34.86           C  
ANISOU 2891  C   GLN B4306     5476   4337   3430   -303  -1890    221       C  
ATOM   2892  O   GLN B4306      67.787  23.793   3.110  1.00 32.00           O  
ANISOU 2892  O   GLN B4306     4996   3937   3224   -269  -1726    255       O  
ATOM   2893  CB  GLN B4306      68.668  23.793  -0.122  1.00 39.97           C  
ANISOU 2893  CB  GLN B4306     6541   5092   3552   -299  -1834    265       C  
ATOM   2894  CG  GLN B4306      68.602  24.408  -1.515  1.00 44.35           C  
ANISOU 2894  CG  GLN B4306     7311   5711   3826   -298  -1947    360       C  
ATOM   2895  CD  GLN B4306      69.753  23.987  -2.394  1.00 47.33           C  
ANISOU 2895  CD  GLN B4306     7932   6139   3910   -302  -1773    295       C  
ATOM   2896  OE1 GLN B4306      70.834  23.654  -1.917  1.00 51.90           O  
ANISOU 2896  OE1 GLN B4306     8489   6702   4527   -288  -1524    233       O  
ATOM   2897  NE2 GLN B4306      69.535  24.023  -3.696  1.00 51.68           N  
ANISOU 2897  NE2 GLN B4306     8719   6752   4162   -317  -1903    315       N  
ATOM   2898  N   ALA B4307      66.787  22.128   1.887  1.00 34.44           N  
ANISOU 2898  N   ALA B4307     5420   4272   3392   -358  -2003     98       N  
ATOM   2899  CA  ALA B4307      66.439  21.222   3.010  1.00 33.24           C  
ANISOU 2899  CA  ALA B4307     5098   4057   3473   -383  -1956     14       C  
ATOM   2900  C   ALA B4307      67.664  20.671   3.753  1.00 31.45           C  
ANISOU 2900  C   ALA B4307     4890   3806   3252   -366  -1707    -59       C  
ATOM   2901  O   ALA B4307      67.696  20.796   4.990  1.00 30.17           O  
ANISOU 2901  O   ALA B4307     4576   3605   3281   -344  -1597    -32       O  
ATOM   2902  CB  ALA B4307      65.593  20.091   2.483  1.00 34.84           C  
ANISOU 2902  CB  ALA B4307     5318   4241   3678   -460  -2153    -92       C  
ATOM   2903  N   ILE B4308      68.594  20.034   3.037  1.00 32.05           N  
ANISOU 2903  N   ILE B4308     5145   3901   3130   -373  -1626   -151       N  
ATOM   2904  CA  ILE B4308      69.779  19.365   3.659  1.00 31.43           C  
ANISOU 2904  CA  ILE B4308     5072   3793   3075   -351  -1403   -223       C  
ATOM   2905  C   ILE B4308      71.019  19.881   2.934  1.00 31.89           C  
ANISOU 2905  C   ILE B4308     5280   3904   2932   -313  -1253   -197       C  
ATOM   2906  O   ILE B4308      71.113  19.662   1.710  1.00 33.15           O  
ANISOU 2906  O   ILE B4308     5627   4100   2865   -325  -1295   -244       O  
ATOM   2907  CB  ILE B4308      69.630  17.832   3.583  1.00 32.54           C  
ANISOU 2907  CB  ILE B4308     5253   3874   3235   -393  -1431   -377       C  
ATOM   2908  CG1 ILE B4308      68.315  17.374   4.220  1.00 33.27           C  
ANISOU 2908  CG1 ILE B4308     5186   3910   3542   -446  -1584   -383       C  
ATOM   2909  CG2 ILE B4308      70.833  17.133   4.204  1.00 31.83           C  
ANISOU 2909  CG2 ILE B4308     5160   3743   3187   -356  -1214   -436       C  
ATOM   2910  CD1 ILE B4308      68.011  15.902   4.031  1.00 34.76           C  
ANISOU 2910  CD1 ILE B4308     5420   4022   3765   -507  -1647   -528       C  
ATOM   2911  N   THR B4309      71.936  20.511   3.674  1.00 30.10           N  
ANISOU 2911  N   THR B4309     4973   3677   2784   -275  -1082   -126       N  
ATOM   2912  CA  THR B4309      73.091  21.211   3.055  1.00 30.66           C  
ANISOU 2912  CA  THR B4309     5143   3794   2709   -247   -930    -66       C  
ATOM   2913  C   THR B4309      74.398  20.898   3.793  1.00 29.78           C  
ANISOU 2913  C   THR B4309     4960   3661   2694   -218   -719    -89       C  
ATOM   2914  O   THR B4309      74.345  20.419   4.940  1.00 28.08           O  
ANISOU 2914  O   THR B4309     4611   3397   2660   -215   -711   -119       O  
ATOM   2915  CB  THR B4309      72.779  22.711   3.026  1.00 30.88           C  
ANISOU 2915  CB  THR B4309     5139   3841   2750   -241   -983     88       C  
ATOM   2916  OG1 THR B4309      72.426  23.081   4.359  1.00 29.08           O  
ANISOU 2916  OG1 THR B4309     4728   3565   2754   -234   -994    123       O  
ATOM   2917  CG2 THR B4309      71.635  23.051   2.096  1.00 32.96           C  
ANISOU 2917  CG2 THR B4309     5489   4134   2899   -257  -1195    132       C  
ATOM   2918  N  AVAL B4310      75.532  21.237   3.169  0.50 30.49           N  
ANISOU 2918  N  AVAL B4310     5127   3785   2672   -197   -555    -55       N  
ATOM   2919  N  BVAL B4310      75.531  21.148   3.128  0.50 30.67           N  
ANISOU 2919  N  BVAL B4310     5156   3807   2687   -197   -555    -65       N  
ATOM   2920  CA AVAL B4310      76.875  20.982   3.774  0.50 30.51           C  
ANISOU 2920  CA AVAL B4310     5038   3768   2783   -168   -358    -63       C  
ATOM   2921  CA BVAL B4310      76.890  20.852   3.675  0.50 30.77           C  
ANISOU 2921  CA BVAL B4310     5087   3803   2801   -166   -353    -76       C  
ATOM   2922  C  AVAL B4310      77.127  21.991   4.903  0.50 28.94           C  
ANISOU 2922  C  AVAL B4310     4677   3552   2766   -177   -354     42       C  
ATOM   2923  C  BVAL B4310      77.190  21.787   4.854  0.50 29.07           C  
ANISOU 2923  C  BVAL B4310     4702   3568   2776   -174   -343     24       C  
ATOM   2924  O  AVAL B4310      77.854  21.630   5.845  0.50 27.39           O  
ANISOU 2924  O  AVAL B4310     4362   3325   2718   -164   -280     24       O  
ATOM   2925  O  BVAL B4310      78.076  21.456   5.663  0.50 27.58           O  
ANISOU 2925  O  BVAL B4310     4402   3353   2723   -157   -246     12       O  
ATOM   2926  CB AVAL B4310      77.992  21.017   2.715  0.50 32.41           C  
ANISOU 2926  CB AVAL B4310     5393   4050   2870   -142   -164    -56       C  
ATOM   2927  CB BVAL B4310      77.954  20.990   2.570  0.50 32.85           C  
ANISOU 2927  CB BVAL B4310     5471   4110   2899   -142   -166    -60       C  
ATOM   2928  CG1AVAL B4310      77.835  19.890   1.706  0.50 34.45           C  
ANISOU 2928  CG1AVAL B4310     5832   4312   2943   -125   -148   -193       C  
ATOM   2929  CG1BVAL B4310      79.360  20.779   3.108  0.50 32.77           C  
ANISOU 2929  CG1BVAL B4310     5337   4081   3031   -109     36    -52       C  
ATOM   2930  CG2AVAL B4310      78.075  22.363   2.015  0.50 33.31           C  
ANISOU 2930  CG2AVAL B4310     5575   4211   2868   -162   -146     84       C  
ATOM   2931  CG2BVAL B4310      77.675  20.049   1.407  0.50 35.12           C  
ANISOU 2931  CG2BVAL B4310     5964   4412   2967   -131   -169   -183       C  
ATOM   2932  N  ATHR B4311      76.572  23.206   4.797  0.60 29.21           N  
ANISOU 2932  N  ATHR B4311     4717   3595   2786   -198   -437    145       N  
ATOM   2933  N  BTHR B4311      76.487  22.930   4.913  0.40 29.03           N  
ANISOU 2933  N  BTHR B4311     4686   3567   2777   -196   -447    119       N  
ATOM   2934  CA ATHR B4311      76.706  24.226   5.867  0.60 28.71           C  
ANISOU 2934  CA ATHR B4311     4525   3494   2888   -210   -445    227       C  
ATOM   2935  CA BTHR B4311      76.649  23.964   5.978  0.40 28.36           C  
ANISOU 2935  CA BTHR B4311     4472   3448   2854   -207   -451    203       C  
ATOM   2936  C  ATHR B4311      75.309  24.759   6.137  0.60 27.89           C  
ANISOU 2936  C  ATHR B4311     4404   3368   2823   -213   -612    257       C  
ATOM   2937  C  BTHR B4311      75.286  24.627   6.194  0.40 27.79           C  
ANISOU 2937  C  BTHR B4311     4387   3355   2815   -213   -614    245       C  
ATOM   2938  O  ATHR B4311      74.425  24.607   5.296  0.60 29.12           O  
ANISOU 2938  O  ATHR B4311     4645   3548   2869   -213   -720    253       O  
ATOM   2939  O  BTHR B4311      74.406  24.479   5.349  0.40 28.84           O  
ANISOU 2939  O  BTHR B4311     4605   3512   2840   -213   -721    241       O  
ATOM   2940  CB ATHR B4311      77.680  25.344   5.471  0.60 30.10           C  
ANISOU 2940  CB ATHR B4311     4710   3676   3050   -226   -331    338       C  
ATOM   2941  CB BTHR B4311      77.764  24.951   5.600  0.40 29.56           C  
ANISOU 2941  CB BTHR B4311     4629   3609   2993   -220   -320    303       C  
ATOM   2942  OG1ATHR B4311      77.157  25.984   4.307  0.60 32.59           O  
ANISOU 2942  OG1ATHR B4311     5159   4020   3203   -230   -375    414       O  
ATOM   2943  OG1BTHR B4311      78.155  25.703   6.749  0.40 29.05           O  
ANISOU 2943  OG1BTHR B4311     4437   3496   3102   -240   -317    348       O  
ATOM   2944  CG2ATHR B4311      79.083  24.840   5.208  0.60 31.00           C  
ANISOU 2944  CG2ATHR B4311     4805   3811   3161   -219   -145    320       C  
ATOM   2945  CG2BTHR B4311      77.360  25.893   4.488  0.40 31.18           C  
ANISOU 2945  CG2BTHR B4311     4956   3837   3052   -230   -352    403       C  
ATOM   2946  N   PRO B4312      75.042  25.345   7.321  1.00 26.86           N  
ANISOU 2946  N   PRO B4312     4164   3189   2850   -214   -642    281       N  
ATOM   2947  CA  PRO B4312      73.732  25.940   7.581  1.00 26.49           C  
ANISOU 2947  CA  PRO B4312     4086   3111   2864   -202   -769    317       C  
ATOM   2948  C   PRO B4312      73.292  26.861   6.433  1.00 27.70           C  
ANISOU 2948  C   PRO B4312     4328   3277   2917   -197   -839    418       C  
ATOM   2949  O   PRO B4312      74.079  27.689   6.003  1.00 28.04           O  
ANISOU 2949  O   PRO B4312     4419   3317   2915   -207   -763    498       O  
ATOM   2950  CB  PRO B4312      73.949  26.700   8.895  1.00 25.34           C  
ANISOU 2950  CB  PRO B4312     3850   2906   2870   -199   -731    336       C  
ATOM   2951  CG  PRO B4312      75.042  25.910   9.577  1.00 24.83           C  
ANISOU 2951  CG  PRO B4312     3747   2851   2836   -213   -637    272       C  
ATOM   2952  CD  PRO B4312      75.974  25.513   8.450  1.00 26.08           C  
ANISOU 2952  CD  PRO B4312     3972   3058   2876   -222   -558    276       C  
ATOM   2953  N   GLU B4313      72.063  26.661   5.953  1.00 28.19           N  
ANISOU 2953  N   GLU B4313     4404   3353   2954   -186   -988    420       N  
ATOM   2954  CA  GLU B4313      71.508  27.455   4.823  1.00 29.75           C  
ANISOU 2954  CA  GLU B4313     4691   3565   3045   -176  -1097    527       C  
ATOM   2955  C   GLU B4313      70.119  27.994   5.174  1.00 29.37           C  
ANISOU 2955  C   GLU B4313     4543   3472   3142   -143  -1246    579       C  
ATOM   2956  O   GLU B4313      69.367  28.326   4.243  1.00 30.66           O  
ANISOU 2956  O   GLU B4313     4759   3654   3235   -131  -1395    655       O  
ATOM   2957  CB  GLU B4313      71.479  26.599   3.558  1.00 31.59           C  
ANISOU 2957  CB  GLU B4313     5069   3872   3060   -196  -1156    484       C  
ATOM   2958  CG  GLU B4313      72.851  26.365   2.960  1.00 32.56           C  
ANISOU 2958  CG  GLU B4313     5311   4036   3025   -210   -981    468       C  
ATOM   2959  CD  GLU B4313      73.527  27.585   2.361  1.00 34.42           C  
ANISOU 2959  CD  GLU B4313     5623   4270   3182   -209   -896    613       C  
ATOM   2960  OE1 GLU B4313      72.894  28.662   2.311  1.00 35.65           O  
ANISOU 2960  OE1 GLU B4313     5765   4389   3391   -194   -993    733       O  
ATOM   2961  OE2 GLU B4313      74.686  27.449   1.926  1.00 36.56           O  
ANISOU 2961  OE2 GLU B4313     5965   4571   3353   -221   -724    613       O  
ATOM   2962  N   ALA B4314      69.813  28.121   6.466  1.00 27.92           N  
ANISOU 2962  N   ALA B4314     4224   3230   3153   -123  -1203    546       N  
ATOM   2963  CA  ALA B4314      68.497  28.657   6.880  1.00 27.86           C  
ANISOU 2963  CA  ALA B4314     4101   3170   3314    -77  -1306    594       C  
ATOM   2964  C   ALA B4314      68.256  30.028   6.240  1.00 29.75           C  
ANISOU 2964  C   ALA B4314     4381   3367   3555    -38  -1369    738       C  
ATOM   2965  O   ALA B4314      69.213  30.843   6.167  1.00 28.80           O  
ANISOU 2965  O   ALA B4314     4334   3215   3390    -45  -1268    793       O  
ATOM   2966  CB  ALA B4314      68.424  28.767   8.383  1.00 26.94           C  
ANISOU 2966  CB  ALA B4314     3872   2991   3371    -56  -1197    542       C  
ATOM   2967  N   ASN B4315      67.029  30.244   5.763  1.00 30.79           N  
ANISOU 2967  N   ASN B4315     4457   3492   3747     -2  -1537    807       N  
ATOM   2968  CA  ASN B4315      66.613  31.573   5.257  1.00 32.88           C  
ANISOU 2968  CA  ASN B4315     4737   3697   4058     54  -1616    963       C  
ATOM   2969  C   ASN B4315      65.938  32.272   6.444  1.00 33.29           C  
ANISOU 2969  C   ASN B4315     4633   3639   4374    123  -1559    966       C  
ATOM   2970  O   ASN B4315      66.018  31.730   7.568  1.00 31.34           O  
ANISOU 2970  O   ASN B4315     4308   3382   4215    114  -1443    851       O  
ATOM   2971  CB  ASN B4315      65.755  31.475   3.990  1.00 35.28           C  
ANISOU 2971  CB  ASN B4315     5081   4054   4268     61  -1848   1052       C  
ATOM   2972  CG  ASN B4315      64.453  30.728   4.190  1.00 35.72           C  
ANISOU 2972  CG  ASN B4315     4976   4126   4468     68  -2000   1007       C  
ATOM   2973  OD1 ASN B4315      63.953  30.624   5.307  1.00 34.80           O  
ANISOU 2973  OD1 ASN B4315     4694   3956   4570     97  -1923    953       O  
ATOM   2974  ND2 ASN B4315      63.887  30.227   3.104  1.00 37.25           N  
ANISOU 2974  ND2 ASN B4315     5222   4390   4541     39  -2216   1032       N  
ATOM   2975  N   MET B4316      65.286  33.408   6.210  1.00 34.84           N  
ANISOU 2975  N   MET B4316     4794   3754   4689    197  -1633   1096       N  
ATOM   2976  CA  MET B4316      64.662  34.174   7.322  1.00 36.69           C  
ANISOU 2976  CA  MET B4316     4895   3865   5179    279  -1551   1093       C  
ATOM   2977  C   MET B4316      63.483  33.409   7.937  1.00 36.06           C  
ANISOU 2977  C   MET B4316     4629   3802   5268    309  -1584   1030       C  
ATOM   2978  O   MET B4316      63.081  33.772   9.060  1.00 36.08           O  
ANISOU 2978  O   MET B4316     4530   3720   5457    370  -1457    987       O  
ATOM   2979  CB  MET B4316      64.170  35.529   6.809  1.00 40.27           C  
ANISOU 2979  CB  MET B4316     5348   4212   5739    363  -1632   1258       C  
ATOM   2980  CG  MET B4316      63.190  35.412   5.662  1.00 44.69           C  
ANISOU 2980  CG  MET B4316     5868   4823   6286    392  -1875   1382       C  
ATOM   2981  SD  MET B4316      62.866  37.021   4.913  1.00 50.90           S  
ANISOU 2981  SD  MET B4316     6698   5484   7156    488  -1978   1609       S  
ATOM   2982  CE  MET B4316      61.631  36.596   3.686  1.00 51.89           C  
ANISOU 2982  CE  MET B4316     6755   5699   7259    511  -2305   1735       C  
ATOM   2983  N   ASP B4317      62.980  32.378   7.248  1.00 36.31           N  
ANISOU 2983  N   ASP B4317     4626   3935   5234    263  -1737   1019       N  
ATOM   2984  CA  ASP B4317      61.784  31.615   7.697  1.00 37.12           C  
ANISOU 2984  CA  ASP B4317     4530   4050   5523    275  -1792    979       C  
ATOM   2985  C   ASP B4317      62.184  30.246   8.251  1.00 34.58           C  
ANISOU 2985  C   ASP B4317     4215   3796   5127    189  -1703    832       C  
ATOM   2986  O   ASP B4317      61.272  29.418   8.466  1.00 34.55           O  
ANISOU 2986  O   ASP B4317     4061   3811   5254    171  -1760    801       O  
ATOM   2987  CB  ASP B4317      60.826  31.378   6.527  1.00 40.77           C  
ANISOU 2987  CB  ASP B4317     4931   4562   5996    269  -2066   1071       C  
ATOM   2988  CG  ASP B4317      60.387  32.645   5.818  1.00 44.31           C  
ANISOU 2988  CG  ASP B4317     5378   4949   6505    356  -2198   1244       C  
ATOM   2989  OD1 ASP B4317      60.230  33.675   6.505  1.00 46.04           O  
ANISOU 2989  OD1 ASP B4317     5532   5055   6904    450  -2076   1291       O  
ATOM   2990  OD2 ASP B4317      60.225  32.594   4.579  1.00 46.72           O  
ANISOU 2990  OD2 ASP B4317     5765   5316   6668    330  -2423   1330       O  
ATOM   2991  N   GLN B4318      63.479  30.026   8.494  1.00 31.14           N  
ANISOU 2991  N   GLN B4318     3931   3385   4516    140  -1569    756       N  
ATOM   2992  CA  GLN B4318      63.937  28.683   8.931  1.00 29.67           C  
ANISOU 2992  CA  GLN B4318     3761   3255   4254     65  -1498    630       C  
ATOM   2993  C   GLN B4318      64.982  28.762  10.042  1.00 27.82           C  
ANISOU 2993  C   GLN B4318     3587   2994   3986     60  -1290    556       C  
ATOM   2994  O   GLN B4318      65.550  29.846  10.277  1.00 26.67           O  
ANISOU 2994  O   GLN B4318     3504   2795   3835     94  -1215    591       O  
ATOM   2995  CB  GLN B4318      64.621  27.965   7.768  1.00 29.59           C  
ANISOU 2995  CB  GLN B4318     3902   3330   4011     -7  -1594    603       C  
ATOM   2996  CG  GLN B4318      63.734  27.701   6.560  1.00 31.12           C  
ANISOU 2996  CG  GLN B4318     4086   3566   4171    -25  -1833    653       C  
ATOM   2997  CD  GLN B4318      64.555  27.263   5.370  1.00 31.79           C  
ANISOU 2997  CD  GLN B4318     4374   3725   3977    -82  -1895    628       C  
ATOM   2998  OE1 GLN B4318      65.717  27.633   5.225  1.00 30.52           O  
ANISOU 2998  OE1 GLN B4318     4350   3576   3670    -84  -1769    632       O  
ATOM   2999  NE2 GLN B4318      63.948  26.483   4.490  1.00 33.16           N  
ANISOU 2999  NE2 GLN B4318     4572   3947   4078   -131  -2088    600       N  
ATOM   3000  N   GLU B4319      65.199  27.616  10.685  1.00 26.65           N  
ANISOU 3000  N   GLU B4319     3423   2876   3825     14  -1218    462       N  
ATOM   3001  CA  GLU B4319      66.282  27.376  11.666  1.00 25.77           C  
ANISOU 3001  CA  GLU B4319     3379   2760   3651     -5  -1059    388       C  
ATOM   3002  C   GLU B4319      67.147  26.263  11.066  1.00 25.81           C  
ANISOU 3002  C   GLU B4319     3472   2833   3500    -73  -1081    330       C  
ATOM   3003  O   GLU B4319      66.575  25.403  10.353  1.00 27.30           O  
ANISOU 3003  O   GLU B4319     3639   3055   3676   -105  -1190    313       O  
ATOM   3004  CB  GLU B4319      65.706  26.956  13.017  1.00 25.94           C  
ANISOU 3004  CB  GLU B4319     3305   2749   3802     13   -947    344       C  
ATOM   3005  CG  GLU B4319      64.864  28.017  13.703  1.00 27.28           C  
ANISOU 3005  CG  GLU B4319     3393   2842   4128     94   -883    384       C  
ATOM   3006  CD  GLU B4319      65.638  29.069  14.479  1.00 28.27           C  
ANISOU 3006  CD  GLU B4319     3615   2907   4220    126   -769    362       C  
ATOM   3007  OE1 GLU B4319      65.081  29.582  15.465  1.00 29.13           O  
ANISOU 3007  OE1 GLU B4319     3683   2950   4433    186   -659    347       O  
ATOM   3008  OE2 GLU B4319      66.802  29.353  14.117  1.00 28.96           O  
ANISOU 3008  OE2 GLU B4319     3816   3008   4178     87   -784    356       O  
ATOM   3009  N   SER B4320      68.462  26.315  11.284  1.00 24.55           N  
ANISOU 3009  N   SER B4320     3405   2684   3239    -92   -990    300       N  
ATOM   3010  CA  SER B4320      69.394  25.260  10.814  1.00 24.13           C  
ANISOU 3010  CA  SER B4320     3425   2683   3060   -139   -975    242       C  
ATOM   3011  C   SER B4320      69.787  24.405  12.017  1.00 23.57           C  
ANISOU 3011  C   SER B4320     3322   2599   3033   -149   -879    178       C  
ATOM   3012  O   SER B4320      70.070  24.984  13.080  1.00 22.77           O  
ANISOU 3012  O   SER B4320     3208   2465   2978   -130   -802    182       O  
ATOM   3013  CB  SER B4320      70.623  25.827  10.143  1.00 24.58           C  
ANISOU 3013  CB  SER B4320     3582   2761   2994   -150   -934    270       C  
ATOM   3014  OG  SER B4320      70.312  26.398   8.884  1.00 25.59           O  
ANISOU 3014  OG  SER B4320     3771   2911   3040   -146  -1023    338       O  
ATOM   3015  N   PHE B4321      69.803  23.085  11.837  1.00 23.27           N  
ANISOU 3015  N   PHE B4321     3287   2579   2975   -179   -893    120       N  
ATOM   3016  CA  PHE B4321      70.171  22.148  12.924  1.00 22.07           C  
ANISOU 3016  CA  PHE B4321     3112   2408   2864   -187   -812     77       C  
ATOM   3017  C   PHE B4321      71.241  21.166  12.450  1.00 22.10           C  
ANISOU 3017  C   PHE B4321     3180   2429   2786   -205   -787     26       C  
ATOM   3018  O   PHE B4321      71.270  20.840  11.239  1.00 22.42           O  
ANISOU 3018  O   PHE B4321     3278   2492   2746   -220   -840     -1       O  
ATOM   3019  CB  PHE B4321      68.962  21.310  13.360  1.00 22.31           C  
ANISOU 3019  CB  PHE B4321     3058   2409   3008   -201   -835     65       C  
ATOM   3020  CG  PHE B4321      67.861  22.072  14.049  1.00 22.12           C  
ANISOU 3020  CG  PHE B4321     2943   2358   3102   -172   -818    113       C  
ATOM   3021  CD1 PHE B4321      66.881  22.727  13.316  1.00 23.51           C  
ANISOU 3021  CD1 PHE B4321     3061   2534   3337   -159   -912    154       C  
ATOM   3022  CD2 PHE B4321      67.785  22.104  15.433  1.00 21.86           C  
ANISOU 3022  CD2 PHE B4321     2886   2297   3120   -150   -704    121       C  
ATOM   3023  CE1 PHE B4321      65.862  23.414  13.957  1.00 23.79           C  
ANISOU 3023  CE1 PHE B4321     2993   2534   3510   -116   -877    200       C  
ATOM   3024  CE2 PHE B4321      66.765  22.793  16.070  1.00 22.54           C  
ANISOU 3024  CE2 PHE B4321     2895   2352   3314   -111   -654    156       C  
ATOM   3025  CZ  PHE B4321      65.804  23.441  15.330  1.00 23.23           C  
ANISOU 3025  CZ  PHE B4321     2902   2433   3491    -90   -734    195       C  
ATOM   3026  N   GLY B4322      72.106  20.738  13.375  1.00 21.01           N  
ANISOU 3026  N   GLY B4322     3040   2278   2662   -197   -709     15       N  
ATOM   3027  CA  GLY B4322      73.047  19.643  13.072  1.00 21.28           C  
ANISOU 3027  CA  GLY B4322     3109   2310   2663   -199   -674    -30       C  
ATOM   3028  C   GLY B4322      72.231  18.429  12.650  1.00 22.27           C  
ANISOU 3028  C   GLY B4322     3236   2403   2821   -222   -721    -83       C  
ATOM   3029  O   GLY B4322      71.281  18.081  13.380  1.00 23.11           O  
ANISOU 3029  O   GLY B4322     3284   2475   3021   -237   -736    -70       O  
ATOM   3030  N   GLY B4323      72.561  17.832  11.505  1.00 23.44           N  
ANISOU 3030  N   GLY B4323     3456   2555   2895   -229   -736   -144       N  
ATOM   3031  CA  GLY B4323      71.776  16.730  10.913  1.00 24.27           C  
ANISOU 3031  CA  GLY B4323     3586   2616   3018   -265   -806   -216       C  
ATOM   3032  C   GLY B4323      71.612  15.514  11.813  1.00 24.69           C  
ANISOU 3032  C   GLY B4323     3595   2592   3194   -276   -775   -234       C  
ATOM   3033  O   GLY B4323      70.460  15.056  11.987  1.00 25.88           O  
ANISOU 3033  O   GLY B4323     3694   2700   3439   -322   -841   -238       O  
ATOM   3034  N   ALA B4324      72.710  14.981  12.347  1.00 24.34           N  
ANISOU 3034  N   ALA B4324     3560   2521   3164   -238   -684   -234       N  
ATOM   3035  CA  ALA B4324      72.624  13.746  13.165  1.00 24.98           C  
ANISOU 3035  CA  ALA B4324     3615   2514   3360   -242   -655   -235       C  
ATOM   3036  C   ALA B4324      71.617  13.914  14.311  1.00 24.68           C  
ANISOU 3036  C   ALA B4324     3496   2463   3416   -270   -663   -159       C  
ATOM   3037  O   ALA B4324      70.866  12.948  14.589  1.00 24.26           O  
ANISOU 3037  O   ALA B4324     3416   2333   3468   -309   -675   -164       O  
ATOM   3038  CB  ALA B4324      73.995  13.382  13.678  1.00 25.14           C  
ANISOU 3038  CB  ALA B4324     3641   2520   3390   -183   -570   -215       C  
ATOM   3039  N   SER B4325      71.569  15.100  14.931  1.00 23.29           N  
ANISOU 3039  N   SER B4325     3288   2352   3210   -251   -645    -95       N  
ATOM   3040  CA  SER B4325      70.675  15.324  16.102  1.00 23.09           C  
ANISOU 3040  CA  SER B4325     3200   2315   3257   -262   -614    -27       C  
ATOM   3041  C   SER B4325      69.195  15.365  15.686  1.00 24.06           C  
ANISOU 3041  C   SER B4325     3251   2422   3466   -309   -670    -30       C  
ATOM   3042  O   SER B4325      68.341  15.288  16.590  1.00 23.82           O  
ANISOU 3042  O   SER B4325     3153   2367   3530   -321   -619     24       O  
ATOM   3043  CB  SER B4325      71.056  16.580  16.855  1.00 23.03           C  
ANISOU 3043  CB  SER B4325     3198   2364   3187   -226   -575     20       C  
ATOM   3044  OG  SER B4325      70.779  17.740  16.082  1.00 23.21           O  
ANISOU 3044  OG  SER B4325     3214   2432   3169   -223   -620      9       O  
ATOM   3045  N   CYS B4326      68.907  15.471  14.384  1.00 24.58           N  
ANISOU 3045  N   CYS B4326     3331   2504   3503   -333   -770    -87       N  
ATOM   3046  CA  CYS B4326      67.504  15.552  13.887  1.00 26.28           C  
ANISOU 3046  CA  CYS B4326     3461   2708   3813   -381   -866    -86       C  
ATOM   3047  C   CYS B4326      67.088  14.240  13.219  1.00 27.14           C  
ANISOU 3047  C   CYS B4326     3578   2744   3988   -450   -948   -157       C  
ATOM   3048  O   CYS B4326      65.988  14.189  12.650  1.00 28.18           O  
ANISOU 3048  O   CYS B4326     3639   2863   4202   -506  -1065   -168       O  
ATOM   3049  CB  CYS B4326      67.351  16.676  12.873  1.00 27.83           C  
ANISOU 3049  CB  CYS B4326     3676   2972   3925   -366   -960    -88       C  
ATOM   3050  SG  CYS B4326      67.700  18.300  13.586  1.00 29.08           S  
ANISOU 3050  SG  CYS B4326     3823   3185   4039   -295   -877    -11       S  
ATOM   3051  N   CYS B4327      67.951  13.232  13.280  1.00 27.06           N  
ANISOU 3051  N   CYS B4327     3648   2679   3952   -446   -898   -205       N  
ATOM   3052  CA  CYS B4327      67.650  11.938  12.621  1.00 28.27           C  
ANISOU 3052  CA  CYS B4327     3836   2737   4167   -511   -970   -293       C  
ATOM   3053  C   CYS B4327      67.068  10.952  13.637  1.00 27.96           C  
ANISOU 3053  C   CYS B4327     3715   2595   4313   -556   -914   -243       C  
ATOM   3054  O   CYS B4327      67.768  10.623  14.607  1.00 26.13           O  
ANISOU 3054  O   CYS B4327     3503   2337   4087   -511   -794   -188       O  
ATOM   3055  CB  CYS B4327      68.911  11.375  11.992  1.00 28.76           C  
ANISOU 3055  CB  CYS B4327     4038   2777   4110   -471   -935   -382       C  
ATOM   3056  SG  CYS B4327      68.664   9.731  11.283  1.00 30.70           S  
ANISOU 3056  SG  CYS B4327     4358   2874   4431   -540  -1001   -513       S  
ATOM   3057  N   LEU B4328      65.842  10.480  13.395  1.00 29.64           N  
ANISOU 3057  N   LEU B4328     3838   2747   4675   -646  -1006   -253       N  
ATOM   3058  CA  LEU B4328      65.194   9.517  14.327  1.00 30.22           C  
ANISOU 3058  CA  LEU B4328     3821   2709   4950   -704   -940   -190       C  
ATOM   3059  C   LEU B4328      66.096   8.297  14.545  1.00 29.68           C  
ANISOU 3059  C   LEU B4328     3859   2529   4886   -692   -875   -225       C  
ATOM   3060  O   LEU B4328      66.222   7.855  15.699  1.00 28.91           O  
ANISOU 3060  O   LEU B4328     3739   2382   4864   -677   -751   -125       O  
ATOM   3061  CB  LEU B4328      63.848   9.070  13.750  1.00 32.39           C  
ANISOU 3061  CB  LEU B4328     3984   2919   5402   -821  -1080   -220       C  
ATOM   3062  CG  LEU B4328      63.064   8.094  14.628  1.00 34.41           C  
ANISOU 3062  CG  LEU B4328     4124   3050   5898   -900  -1009   -143       C  
ATOM   3063  CD1 LEU B4328      62.529   8.793  15.864  1.00 34.34           C  
ANISOU 3063  CD1 LEU B4328     3986   3099   5962   -863   -853      8       C  
ATOM   3064  CD2 LEU B4328      61.929   7.441  13.857  1.00 36.54           C  
ANISOU 3064  CD2 LEU B4328     4297   3229   6356  -1036  -1182   -203       C  
ATOM   3065  N   TYR B4329      66.679   7.775  13.465  1.00 30.86           N  
ANISOU 3065  N   TYR B4329     4131   2637   4956   -695   -951   -359       N  
ATOM   3066  CA  TYR B4329      67.491   6.531  13.517  1.00 31.92           C  
ANISOU 3066  CA  TYR B4329     4365   2637   5124   -677   -894   -411       C  
ATOM   3067  C   TYR B4329      68.780   6.785  14.302  1.00 30.90           C  
ANISOU 3067  C   TYR B4329     4279   2555   4904   -559   -758   -337       C  
ATOM   3068  O   TYR B4329      69.113   5.958  15.169  1.00 31.90           O  
ANISOU 3068  O   TYR B4329     4408   2585   5127   -540   -676   -267       O  
ATOM   3069  CB  TYR B4329      67.668   6.009  12.091  1.00 33.84           C  
ANISOU 3069  CB  TYR B4329     4735   2825   5297   -706  -1004   -591       C  
ATOM   3070  CG  TYR B4329      66.342   5.925  11.381  1.00 35.50           C  
ANISOU 3070  CG  TYR B4329     4891   3008   5587   -832  -1179   -651       C  
ATOM   3071  CD1 TYR B4329      65.449   4.903  11.661  1.00 37.87           C  
ANISOU 3071  CD1 TYR B4329     5118   3155   6114   -943  -1226   -649       C  
ATOM   3072  CD2 TYR B4329      65.939   6.914  10.498  1.00 35.89           C  
ANISOU 3072  CD2 TYR B4329     4944   3184   5507   -844  -1307   -688       C  
ATOM   3073  CE1 TYR B4329      64.210   4.838  11.044  1.00 39.92           C  
ANISOU 3073  CE1 TYR B4329     5298   3389   6480  -1069  -1408   -695       C  
ATOM   3074  CE2 TYR B4329      64.705   6.862   9.870  1.00 38.11           C  
ANISOU 3074  CE2 TYR B4329     5157   3445   5876   -958  -1498   -729       C  
ATOM   3075  CZ  TYR B4329      63.835   5.824  10.149  1.00 39.81           C  
ANISOU 3075  CZ  TYR B4329     5284   3510   6330  -1074  -1554   -736       C  
ATOM   3076  OH  TYR B4329      62.616   5.765   9.542  1.00 42.19           O  
ANISOU 3076  OH  TYR B4329     5495   3789   6747  -1198  -1763   -772       O  
ATOM   3077  N   CYS B4330      69.473   7.887  14.012  1.00 30.05           N  
ANISOU 3077  N   CYS B4330     4201   2587   4629   -489   -747   -342       N  
ATOM   3078  CA  CYS B4330      70.686   8.235  14.796  1.00 29.52           C  
ANISOU 3078  CA  CYS B4330     4151   2572   4492   -389   -643   -266       C  
ATOM   3079  C   CYS B4330      70.315   8.394  16.278  1.00 28.65           C  
ANISOU 3079  C   CYS B4330     3967   2471   4446   -390   -577   -117       C  
ATOM   3080  O   CYS B4330      70.969   7.757  17.124  1.00 29.44           O  
ANISOU 3080  O   CYS B4330     4089   2512   4584   -347   -512    -47       O  
ATOM   3081  CB  CYS B4330      71.319   9.533  14.306  1.00 29.22           C  
ANISOU 3081  CB  CYS B4330     4132   2678   4289   -337   -647   -280       C  
ATOM   3082  SG  CYS B4330      72.247   9.393  12.755  1.00 30.23           S  
ANISOU 3082  SG  CYS B4330     4379   2813   4293   -299   -655   -424       S  
ATOM   3083  N   ARG B4331      69.268   9.175  16.564  1.00 28.22           N  
ANISOU 3083  N   ARG B4331     3834   2479   4406   -433   -591    -70       N  
ATOM   3084  CA  ARG B4331      68.870   9.524  17.957  1.00 27.73           C  
ANISOU 3084  CA  ARG B4331     3721   2444   4370   -425   -501     61       C  
ATOM   3085  C   ARG B4331      68.377   8.302  18.740  1.00 29.91           C  
ANISOU 3085  C   ARG B4331     3977   2592   4794   -470   -440    138       C  
ATOM   3086  O   ARG B4331      68.672   8.238  19.949  1.00 29.37           O  
ANISOU 3086  O   ARG B4331     3934   2526   4698   -434   -349    251       O  
ATOM   3087  CB  ARG B4331      67.797  10.620  17.948  1.00 27.13           C  
ANISOU 3087  CB  ARG B4331     3557   2450   4301   -451   -512     80       C  
ATOM   3088  CG  ARG B4331      68.302  11.987  17.507  1.00 25.58           C  
ANISOU 3088  CG  ARG B4331     3387   2373   3958   -397   -546     46       C  
ATOM   3089  CD  ARG B4331      69.375  12.552  18.416  1.00 24.48           C  
ANISOU 3089  CD  ARG B4331     3311   2290   3699   -326   -478     97       C  
ATOM   3090  NE  ARG B4331      68.934  12.704  19.796  1.00 24.65           N  
ANISOU 3090  NE  ARG B4331     3320   2312   3731   -317   -379    195       N  
ATOM   3091  CZ  ARG B4331      68.253  13.743  20.270  1.00 24.65           C  
ANISOU 3091  CZ  ARG B4331     3284   2366   3713   -306   -330    224       C  
ATOM   3092  NH1 ARG B4331      67.914  14.746  19.474  1.00 24.72           N  
ANISOU 3092  NH1 ARG B4331     3252   2427   3712   -301   -387    176       N  
ATOM   3093  NH2 ARG B4331      67.912  13.776  21.545  1.00 24.75           N  
ANISOU 3093  NH2 ARG B4331     3313   2374   3714   -293   -216    305       N  
ATOM   3094  N   CYS B4332      67.663   7.378  18.090  1.00 31.88           N  
ANISOU 3094  N   CYS B4332     4192   2728   5190   -552   -494     83       N  
ATOM   3095  CA  CYS B4332      67.101   6.201  18.810  1.00 34.71           C  
ANISOU 3095  CA  CYS B4332     4520   2943   5722   -612   -431    168       C  
ATOM   3096  C   CYS B4332      68.077   5.016  18.778  1.00 35.42           C  
ANISOU 3096  C   CYS B4332     4710   2904   5843   -578   -424    151       C  
ATOM   3097  O   CYS B4332      67.746   3.976  19.372  1.00 35.69           O  
ANISOU 3097  O   CYS B4332     4737   2798   6023   -622   -371    231       O  
ATOM   3098  CB  CYS B4332      65.750   5.807  18.225  1.00 37.17           C  
ANISOU 3098  CB  CYS B4332     4724   3181   6218   -734   -498    129       C  
ATOM   3099  SG  CYS B4332      64.485   7.080  18.467  1.00 40.03           S  
ANISOU 3099  SG  CYS B4332     4927   3669   6611   -760   -480    189       S  
ATOM   3100  N   HIS B4333      69.237   5.185  18.136  1.00 35.55           N  
ANISOU 3100  N   HIS B4333     4808   2958   5741   -499   -462     61       N  
ATOM   3101  CA  HIS B4333      70.264   4.112  18.028  1.00 38.10           C  
ANISOU 3101  CA  HIS B4333     5214   3153   6107   -442   -446     36       C  
ATOM   3102  C   HIS B4333      69.635   2.879  17.368  1.00 39.91           C  
ANISOU 3102  C   HIS B4333     5458   3194   6510   -528   -488    -50       C  
ATOM   3103  O   HIS B4333      69.655   1.783  17.975  1.00 41.60           O  
ANISOU 3103  O   HIS B4333     5689   3248   6868   -538   -440     26       O  
ATOM   3104  CB  HIS B4333      70.888   3.794  19.396  1.00 40.73           C  
ANISOU 3104  CB  HIS B4333     5566   3464   6445   -376   -365    205       C  
ATOM   3105  CG  HIS B4333      71.289   5.005  20.166  1.00 41.66           C  
ANISOU 3105  CG  HIS B4333     5676   3755   6398   -319   -341    286       C  
ATOM   3106  ND1 HIS B4333      70.854   5.233  21.458  1.00 44.97           N  
ANISOU 3106  ND1 HIS B4333     6089   4209   6788   -329   -274    437       N  
ATOM   3107  CD2 HIS B4333      72.016   6.088  19.813  1.00 42.54           C  
ANISOU 3107  CD2 HIS B4333     5792   4007   6362   -262   -373    233       C  
ATOM   3108  CE1 HIS B4333      71.334   6.389  21.881  1.00 44.76           C  
ANISOU 3108  CE1 HIS B4333     6076   4333   6597   -277   -278    457       C  
ATOM   3109  NE2 HIS B4333      72.044   6.935  20.888  1.00 41.83           N  
ANISOU 3109  NE2 HIS B4333     5701   4024   6166   -240   -343    338       N  
ATOM   3110  N   ILE B4334      69.083   3.066  16.170  1.00 39.06           N  
ANISOU 3110  N   ILE B4334     5353   3099   6387   -593   -588   -201       N  
ATOM   3111  CA  ILE B4334      68.444   1.965  15.395  1.00 41.38           C  
ANISOU 3111  CA  ILE B4334     5676   3213   6832   -694   -665   -319       C  
ATOM   3112  C   ILE B4334      68.960   2.046  13.957  1.00 40.86           C  
ANISOU 3112  C   ILE B4334     5725   3163   6635   -668   -743   -522       C  
ATOM   3113  O   ILE B4334      69.482   3.114  13.570  1.00 40.03           O  
ANISOU 3113  O   ILE B4334     5639   3229   6341   -601   -744   -545       O  
ATOM   3114  CB  ILE B4334      66.905   2.022  15.486  1.00 43.11           C  
ANISOU 3114  CB  ILE B4334     5769   3415   7193   -837   -731   -282       C  
ATOM   3115  CG1 ILE B4334      66.337   3.313  14.900  1.00 42.47           C  
ANISOU 3115  CG1 ILE B4334     5625   3519   6992   -856   -821   -321       C  
ATOM   3116  CG2 ILE B4334      66.443   1.813  16.921  1.00 44.13           C  
ANISOU 3116  CG2 ILE B4334     5804   3511   7450   -857   -610    -78       C  
ATOM   3117  CD1 ILE B4334      64.833   3.361  14.889  1.00 44.31           C  
ANISOU 3117  CD1 ILE B4334     5706   3733   7397   -989   -900   -289       C  
ATOM   3118  N   ASP B4335      68.834   0.949  13.209  1.00 41.03           N  
ANISOU 3118  N   ASP B4335     5835   3004   6749   -722   -798   -663       N  
ATOM   3119  CA  ASP B4335      69.349   0.888  11.816  1.00 42.16           C  
ANISOU 3119  CA  ASP B4335     6128   3143   6746   -694   -853   -874       C  
ATOM   3120  C   ASP B4335      68.592   1.888  10.937  1.00 41.39           C  
ANISOU 3120  C   ASP B4335     6018   3201   6504   -764   -994   -944       C  
ATOM   3121  O   ASP B4335      67.397   2.128  11.193  1.00 40.67           O  
ANISOU 3121  O   ASP B4335     5803   3130   6517   -874  -1090   -880       O  
ATOM   3122  CB  ASP B4335      69.235  -0.529  11.242  1.00 44.90           C  
ANISOU 3122  CB  ASP B4335     6589   3242   7229   -750   -890  -1026       C  
ATOM   3123  CG  ASP B4335      70.086  -1.568  11.957  1.00 46.37           C  
ANISOU 3123  CG  ASP B4335     6806   3250   7562   -661   -752   -967       C  
ATOM   3124  OD1 ASP B4335      70.968  -1.169  12.741  1.00 46.50           O  
ANISOU 3124  OD1 ASP B4335     6774   3354   7537   -539   -637   -828       O  
ATOM   3125  OD2 ASP B4335      69.859  -2.769  11.723  1.00 50.19           O  
ANISOU 3125  OD2 ASP B4335     7362   3498   8209   -717   -774  -1059       O  
ATOM   3126  N   HIS B4336      69.286   2.461   9.953  1.00 41.18           N  
ANISOU 3126  N   HIS B4336     6111   3280   6254   -695   -998  -1055       N  
ATOM   3127  CA  HIS B4336      68.654   3.391   8.982  1.00 41.98           C  
ANISOU 3127  CA  HIS B4336     6235   3524   6190   -751  -1145  -1120       C  
ATOM   3128  C   HIS B4336      67.855   2.539   8.000  1.00 46.94           C  
ANISOU 3128  C   HIS B4336     6964   4017   6855   -876  -1317  -1298       C  
ATOM   3129  O   HIS B4336      68.343   1.506   7.549  1.00 48.04           O  
ANISOU 3129  O   HIS B4336     7250   3996   7006   -863  -1282  -1442       O  
ATOM   3130  CB  HIS B4336      69.716   4.294   8.344  1.00 39.77           C  
ANISOU 3130  CB  HIS B4336     6055   3397   5658   -636  -1067  -1151       C  
ATOM   3131  CG  HIS B4336      70.235   5.330   9.285  1.00 36.41           C  
ANISOU 3131  CG  HIS B4336     5507   3116   5210   -553   -958   -975       C  
ATOM   3132  ND1 HIS B4336      71.099   5.026  10.322  1.00 35.33           N  
ANISOU 3132  ND1 HIS B4336     5317   2939   5165   -467   -810   -876       N  
ATOM   3133  CD2 HIS B4336      70.011   6.659   9.355  1.00 34.92           C  
ANISOU 3133  CD2 HIS B4336     5247   3098   4921   -544   -988   -884       C  
ATOM   3134  CE1 HIS B4336      71.381   6.131  10.992  1.00 33.32           C  
ANISOU 3134  CE1 HIS B4336     4971   2831   4856   -418   -763   -742       C  
ATOM   3135  NE2 HIS B4336      70.728   7.146  10.414  1.00 32.28           N  
ANISOU 3135  NE2 HIS B4336     4827   2823   4612   -463   -860   -748       N  
ATOM   3136  N   PRO B4337      66.612   2.940   7.646  1.00 51.81           N  
ANISOU 3136  N   PRO B4337     7501   4682   7501   -998  -1513  -1297       N  
ATOM   3137  CA  PRO B4337      65.744   2.124   6.795  1.00 58.88           C  
ANISOU 3137  CA  PRO B4337     8469   5443   8460  -1142  -1718  -1458       C  
ATOM   3138  C   PRO B4337      66.115   2.140   5.305  1.00 65.45           C  
ANISOU 3138  C   PRO B4337     9554   6300   9013  -1133  -1819  -1669       C  
ATOM   3139  O   PRO B4337      65.444   2.809   4.538  1.00 70.35           O  
ANISOU 3139  O   PRO B4337    10190   7031   9507  -1195  -2012  -1698       O  
ATOM   3140  CB  PRO B4337      64.372   2.773   7.031  1.00 58.22           C  
ANISOU 3140  CB  PRO B4337     8173   5440   8507  -1253  -1886  -1343       C  
ATOM   3141  CG  PRO B4337      64.704   4.234   7.210  1.00 54.78           C  
ANISOU 3141  CG  PRO B4337     7678   5231   7902  -1145  -1818  -1214       C  
ATOM   3142  CD  PRO B4337      65.993   4.225   8.006  1.00 52.18           C  
ANISOU 3142  CD  PRO B4337     7383   4911   7529  -1002  -1560  -1145       C  
ATOM   3143  N   ASN B4338      67.157   1.388   4.939  1.00 70.40           N  
ANISOU 3143  N   ASN B4338    10376   6819   9554  -1052  -1682  -1807       N  
ATOM   3144  CA  ASN B4338      67.638   1.271   3.536  1.00 75.24           C  
ANISOU 3144  CA  ASN B4338    11269   7436   9881  -1027  -1723  -2027       C  
ATOM   3145  C   ASN B4338      68.848   0.342   3.512  1.00 77.99           C  
ANISOU 3145  C   ASN B4338    11769   7634  10228   -910  -1499  -2139       C  
ATOM   3146  O   ASN B4338      69.531   0.195   4.524  1.00 76.96           O  
ANISOU 3146  O   ASN B4338    11518   7472  10250   -813  -1306  -2007       O  
ATOM   3147  CB  ASN B4338      67.982   2.637   2.928  1.00 74.88           C  
ANISOU 3147  CB  ASN B4338    11274   7636   9540   -954  -1719  -1975       C  
ATOM   3148  CG  ASN B4338      69.192   3.287   3.564  1.00 72.74           C  
ANISOU 3148  CG  ASN B4338    10938   7473   9224   -790  -1455  -1837       C  
ATOM   3149  OD1 ASN B4338      70.253   2.675   3.661  1.00 73.83           O  
ANISOU 3149  OD1 ASN B4338    11156   7523   9370   -686  -1255  -1894       O  
ATOM   3150  ND2 ASN B4338      69.055   4.542   3.961  1.00 71.72           N  
ANISOU 3150  ND2 ASN B4338    10664   7530   9056   -764  -1459  -1661       N  
ATOM   3151  N   PRO B4339      69.140  -0.331   2.373  1.00 81.82           N  
ANISOU 3151  N   PRO B4339    12526   8013  10548   -912  -1519  -2385       N  
ATOM   3152  CA  PRO B4339      70.318  -1.192   2.274  1.00 82.79           C  
ANISOU 3152  CA  PRO B4339    12796   7984  10676   -780  -1284  -2502       C  
ATOM   3153  C   PRO B4339      71.597  -0.363   2.485  1.00 81.29           C  
ANISOU 3153  C   PRO B4339    12566   7963  10357   -595  -1031  -2382       C  
ATOM   3154  O   PRO B4339      71.661   0.747   1.982  1.00 81.04           O  
ANISOU 3154  O   PRO B4339    12558   8143  10090   -578  -1053  -2337       O  
ATOM   3155  CB  PRO B4339      70.240  -1.786   0.857  1.00 86.68           C  
ANISOU 3155  CB  PRO B4339    13612   8377  10943   -825  -1374  -2799       C  
ATOM   3156  CG  PRO B4339      68.789  -1.597   0.443  1.00 87.76           C  
ANISOU 3156  CG  PRO B4339    13733   8544  11066  -1027  -1720  -2834       C  
ATOM   3157  CD  PRO B4339      68.342  -0.327   1.138  1.00 84.75           C  
ANISOU 3157  CD  PRO B4339    13084   8395  10721  -1036  -1773  -2567       C  
ATOM   3158  N   LYS B4340      72.555  -0.916   3.239  1.00 80.02           N  
ANISOU 3158  N   LYS B4340    12333   7695  10373   -469   -812  -2321       N  
ATOM   3159  CA  LYS B4340      73.851  -0.265   3.597  1.00 77.40           C  
ANISOU 3159  CA  LYS B4340    11922   7494   9993   -296   -573  -2194       C  
ATOM   3160  C   LYS B4340      73.648   0.639   4.822  1.00 71.02           C  
ANISOU 3160  C   LYS B4340    10845   6837   9303   -306   -600  -1924       C  
ATOM   3161  O   LYS B4340      74.663   1.032   5.428  1.00 69.27           O  
ANISOU 3161  O   LYS B4340    10513   6686   9119   -180   -431  -1793       O  
ATOM   3162  CB  LYS B4340      74.469   0.518   2.432  1.00 79.85           C  
ANISOU 3162  CB  LYS B4340    12400   7966   9973   -227   -485  -2284       C  
ATOM   3163  CG  LYS B4340      74.850  -0.319   1.216  1.00 85.70           C  
ANISOU 3163  CG  LYS B4340    13437   8570  10553   -188   -404  -2557       C  
ATOM   3164  CD  LYS B4340      75.779   0.385   0.243  1.00 87.71           C  
ANISOU 3164  CD  LYS B4340    13842   8976  10507    -77   -219  -2611       C  
ATOM   3165  CE  LYS B4340      77.151   0.662   0.827  1.00 88.17           C  
ANISOU 3165  CE  LYS B4340    13740   9083  10677     96     63  -2470       C  
ATOM   3166  NZ  LYS B4340      78.060   1.283  -0.166  1.00 90.38           N  
ANISOU 3166  NZ  LYS B4340    14161   9493  10685    198    271  -2522       N  
ATOM   3167  N   GLY B4341      72.391   0.950   5.163  1.00 67.07           N  
ANISOU 3167  N   GLY B4341    10243   6377   8863   -449   -804  -1851       N  
ATOM   3168  CA  GLY B4341      72.072   1.775   6.346  1.00 63.98           C  
ANISOU 3168  CA  GLY B4341     9615   6113   8580   -462   -822  -1612       C  
ATOM   3169  C   GLY B4341      72.723   3.147   6.292  1.00 60.14           C  
ANISOU 3169  C   GLY B4341     9081   5856   7911   -380   -745  -1507       C  
ATOM   3170  O   GLY B4341      73.263   3.583   7.330  1.00 59.97           O  
ANISOU 3170  O   GLY B4341     8908   5897   7980   -311   -646  -1337       O  
ATOM   3171  N   PHE B4342      72.665   3.808   5.132  1.00 58.54           N  
ANISOU 3171  N   PHE B4342     9013   5769   7459   -392   -797  -1600       N  
ATOM   3172  CA  PHE B4342      73.261   5.160   4.961  1.00 56.73           C  
ANISOU 3172  CA  PHE B4342     8754   5747   7054   -325   -724  -1498       C  
ATOM   3173  C   PHE B4342      72.339   6.210   5.594  1.00 50.63           C  
ANISOU 3173  C   PHE B4342     7813   5102   6320   -397   -860  -1335       C  
ATOM   3174  O   PHE B4342      71.105   6.013   5.617  1.00 50.61           O  
ANISOU 3174  O   PHE B4342     7773   5061   6395   -511  -1043  -1347       O  
ATOM   3175  CB  PHE B4342      73.518   5.443   3.478  1.00 61.18           C  
ANISOU 3175  CB  PHE B4342     9542   6376   7325   -312   -718  -1642       C  
ATOM   3176  CG  PHE B4342      73.978   6.846   3.165  1.00 63.27           C  
ANISOU 3176  CG  PHE B4342     9792   6841   7404   -265   -661  -1533       C  
ATOM   3177  CD1 PHE B4342      75.310   7.208   3.308  1.00 64.80           C  
ANISOU 3177  CD1 PHE B4342     9951   7088   7580   -144   -431  -1471       C  
ATOM   3178  CD2 PHE B4342      73.081   7.803   2.712  1.00 65.21           C  
ANISOU 3178  CD2 PHE B4342    10051   7213   7513   -344   -841  -1483       C  
ATOM   3179  CE1 PHE B4342      75.730   8.499   3.020  1.00 64.37           C  
ANISOU 3179  CE1 PHE B4342     9879   7202   7376   -116   -377  -1364       C  
ATOM   3180  CE2 PHE B4342      73.504   9.091   2.421  1.00 64.77           C  
ANISOU 3180  CE2 PHE B4342     9989   7320   7299   -303   -785  -1373       C  
ATOM   3181  CZ  PHE B4342      74.826   9.437   2.575  1.00 64.39           C  
ANISOU 3181  CZ  PHE B4342     9912   7316   7235   -195   -550  -1315       C  
ATOM   3182  N   CYS B4343      72.929   7.294   6.102  1.00 45.68           N  
ANISOU 3182  N   CYS B4343     7082   4613   5660   -331   -770  -1188       N  
ATOM   3183  CA  CYS B4343      72.144   8.398   6.719  1.00 41.09           C  
ANISOU 3183  CA  CYS B4343     6352   4147   5111   -379   -870  -1038       C  
ATOM   3184  C   CYS B4343      72.275   9.649   5.847  1.00 40.04           C  
ANISOU 3184  C   CYS B4343     6286   4170   4756   -364   -894  -1016       C  
ATOM   3185  O   CYS B4343      73.416  10.025   5.532  1.00 40.35           O  
ANISOU 3185  O   CYS B4343     6380   4265   4685   -282   -743  -1010       O  
ATOM   3186  CB  CYS B4343      72.620   8.691   8.134  1.00 38.47           C  
ANISOU 3186  CB  CYS B4343     5855   3833   4927   -326   -766   -883       C  
ATOM   3187  SG  CYS B4343      71.650   9.984   8.952  1.00 35.19           S  
ANISOU 3187  SG  CYS B4343     5279   3534   4556   -372   -856   -723       S  
ATOM   3188  N   ASP B4344      71.146  10.267   5.489  1.00 39.91           N  
ANISOU 3188  N   ASP B4344     6253   4214   4696   -441  -1075   -990       N  
ATOM   3189  CA  ASP B4344      71.139  11.477   4.623  1.00 41.47           C  
ANISOU 3189  CA  ASP B4344     6523   4549   4684   -432  -1124   -949       C  
ATOM   3190  C   ASP B4344      71.334  12.747   5.460  1.00 36.86           C  
ANISOU 3190  C   ASP B4344     5788   4060   4155   -391  -1064   -777       C  
ATOM   3191  O   ASP B4344      71.542  13.804   4.851  1.00 37.23           O  
ANISOU 3191  O   ASP B4344     5889   4208   4050   -370  -1067   -721       O  
ATOM   3192  CB  ASP B4344      69.821  11.613   3.853  1.00 45.04           C  
ANISOU 3192  CB  ASP B4344     7016   5018   5077   -526  -1373   -984       C  
ATOM   3193  CG  ASP B4344      69.555  10.513   2.841  1.00 50.99           C  
ANISOU 3193  CG  ASP B4344     7957   5686   5730   -584  -1477  -1172       C  
ATOM   3194  OD1 ASP B4344      70.449   9.666   2.637  1.00 55.31           O  
ANISOU 3194  OD1 ASP B4344     8625   6157   6233   -538  -1329  -1287       O  
ATOM   3195  OD2 ASP B4344      68.451  10.513   2.264  1.00 55.67           O  
ANISOU 3195  OD2 ASP B4344     8572   6281   6297   -675  -1713  -1206       O  
ATOM   3196  N   LEU B4345      71.278  12.644   6.794  1.00 35.12           N  
ANISOU 3196  N   LEU B4345     5547   3469   4327   -104   -898   -513       N  
ATOM   3197  CA  LEU B4345      71.353  13.856   7.663  1.00 33.03           C  
ANISOU 3197  CA  LEU B4345     5137   3354   4056   -132   -899   -369       C  
ATOM   3198  C   LEU B4345      72.710  13.987   8.371  1.00 31.38           C  
ANISOU 3198  C   LEU B4345     4862   3244   3814    -42   -760   -233       C  
ATOM   3199  O   LEU B4345      73.210  15.122   8.475  1.00 29.61           O  
ANISOU 3199  O   LEU B4345     4582   3166   3501    -50   -759   -160       O  
ATOM   3200  CB  LEU B4345      70.215  13.775   8.684  1.00 33.09           C  
ANISOU 3200  CB  LEU B4345     5036   3300   4236   -226   -952   -326       C  
ATOM   3201  CG  LEU B4345      68.812  13.974   8.112  1.00 34.49           C  
ANISOU 3201  CG  LEU B4345     5212   3434   4459   -330  -1108   -413       C  
ATOM   3202  CD1 LEU B4345      67.747  13.550   9.107  1.00 35.27           C  
ANISOU 3202  CD1 LEU B4345     5193   3447   4760   -410  -1124   -360       C  
ATOM   3203  CD2 LEU B4345      68.606  15.422   7.697  1.00 34.98           C  
ANISOU 3203  CD2 LEU B4345     5244   3636   4408   -342  -1180   -385       C  
ATOM   3204  N   LYS B4346      73.257  12.878   8.863  1.00 31.39           N  
ANISOU 3204  N   LYS B4346     4862   3165   3900     32   -654   -190       N  
ATOM   3205  CA  LYS B4346      74.536  12.890   9.624  1.00 31.81           C  
ANISOU 3205  CA  LYS B4346     4819   3332   3935    121   -535    -32       C  
ATOM   3206  C   LYS B4346      75.636  13.625   8.842  1.00 30.46           C  
ANISOU 3206  C   LYS B4346     4657   3309   3607    183   -490     -7       C  
ATOM   3207  O   LYS B4346      75.842  13.309   7.658  1.00 30.49           O  
ANISOU 3207  O   LYS B4346     4784   3270   3530    250   -459   -104       O  
ATOM   3208  CB  LYS B4346      74.932  11.444   9.929  1.00 35.01           C  
ANISOU 3208  CB  LYS B4346     5246   3598   4457    226   -419      6       C  
ATOM   3209  CG  LYS B4346      76.234  11.257  10.683  1.00 37.51           C  
ANISOU 3209  CG  LYS B4346     5446   4033   4770    339   -299    194       C  
ATOM   3210  CD  LYS B4346      76.616   9.802  10.812  1.00 40.48           C  
ANISOU 3210  CD  LYS B4346     5859   4246   5274    474   -167    240       C  
ATOM   3211  CE  LYS B4346      77.962   9.596  11.471  1.00 43.24           C  
ANISOU 3211  CE  LYS B4346     6071   4736   5619    610    -50    455       C  
ATOM   3212  NZ  LYS B4346      77.928   9.966  12.904  1.00 44.49           N  
ANISOU 3212  NZ  LYS B4346     6066   5043   5793    545    -99    624       N  
ATOM   3213  N   GLY B4347      76.312  14.579   9.489  1.00 28.46           N  
ANISOU 3213  N   GLY B4347     4279   3226   3307    152   -487    118       N  
ATOM   3214  CA  GLY B4347      77.429  15.322   8.869  1.00 28.66           C  
ANISOU 3214  CA  GLY B4347     4274   3400   3213    190   -438    181       C  
ATOM   3215  C   GLY B4347      76.953  16.480   8.012  1.00 28.34           C  
ANISOU 3215  C   GLY B4347     4294   3394   3079    112   -521    114       C  
ATOM   3216  O   GLY B4347      77.810  17.172   7.424  1.00 29.26           O  
ANISOU 3216  O   GLY B4347     4387   3626   3103    132   -476    179       O  
ATOM   3217  N   LYS B4348      75.636  16.686   7.957  1.00 27.95           N  
ANISOU 3217  N   LYS B4348     4301   3252   3064     30   -633     13       N  
ATOM   3218  CA  LYS B4348      75.018  17.782   7.174  1.00 29.31           C  
ANISOU 3218  CA  LYS B4348     4523   3449   3163    -32   -723    -28       C  
ATOM   3219  C   LYS B4348      74.204  18.668   8.120  1.00 27.15           C  
ANISOU 3219  C   LYS B4348     4176   3167   2971   -140   -803     -7       C  
ATOM   3220  O   LYS B4348      74.222  18.409   9.346  1.00 26.27           O  
ANISOU 3220  O   LYS B4348     3986   3054   2941   -164   -781     32       O  
ATOM   3221  CB  LYS B4348      74.089  17.217   6.093  1.00 32.14           C  
ANISOU 3221  CB  LYS B4348     5014   3715   3481    -17   -795   -167       C  
ATOM   3222  CG  LYS B4348      74.715  16.247   5.099  1.00 36.91           C  
ANISOU 3222  CG  LYS B4348     5739   4296   3988     95   -713   -239       C  
ATOM   3223  CD  LYS B4348      75.746  16.871   4.193  1.00 40.05           C  
ANISOU 3223  CD  LYS B4348     6163   4831   4224    169   -630   -173       C  
ATOM   3224  CE  LYS B4348      75.971  16.077   2.921  1.00 43.98           C  
ANISOU 3224  CE  LYS B4348     6829   5307   4573    279   -573   -290       C  
ATOM   3225  NZ  LYS B4348      76.388  14.682   3.198  1.00 47.48           N  
ANISOU 3225  NZ  LYS B4348     7317   5630   5091    376   -463   -349       N  
ATOM   3226  N   TYR B4349      73.529  19.672   7.555  1.00 26.08           N  
ANISOU 3226  N   TYR B4349     4069   3032   2805   -186   -880    -25       N  
ATOM   3227  CA  TYR B4349      72.646  20.596   8.307  1.00 25.28           C  
ANISOU 3227  CA  TYR B4349     3917   2902   2786   -264   -938    -15       C  
ATOM   3228  C   TYR B4349      71.257  20.523   7.687  1.00 26.17           C  
ANISOU 3228  C   TYR B4349     4065   2944   2932   -273  -1041    -81       C  
ATOM   3229  O   TYR B4349      71.142  20.474   6.442  1.00 28.56           O  
ANISOU 3229  O   TYR B4349     4444   3265   3142   -243  -1091   -112       O  
ATOM   3230  CB  TYR B4349      73.242  22.007   8.342  1.00 24.99           C  
ANISOU 3230  CB  TYR B4349     3858   2923   2714   -307   -919     57       C  
ATOM   3231  CG  TYR B4349      74.558  21.983   9.059  1.00 23.76           C  
ANISOU 3231  CG  TYR B4349     3637   2851   2540   -325   -844    122       C  
ATOM   3232  CD1 TYR B4349      75.726  21.694   8.379  1.00 23.89           C  
ANISOU 3232  CD1 TYR B4349     3647   2950   2479   -274   -779    182       C  
ATOM   3233  CD2 TYR B4349      74.614  22.107  10.438  1.00 22.70           C  
ANISOU 3233  CD2 TYR B4349     3437   2730   2455   -383   -838    129       C  
ATOM   3234  CE1 TYR B4349      76.932  21.583   9.044  1.00 23.62           C  
ANISOU 3234  CE1 TYR B4349     3518   3014   2442   -287   -719    264       C  
ATOM   3235  CE2 TYR B4349      75.811  21.999  11.118  1.00 22.02           C  
ANISOU 3235  CE2 TYR B4349     3273   2750   2341   -406   -796    197       C  
ATOM   3236  CZ  TYR B4349      76.972  21.735  10.418  1.00 22.53           C  
ANISOU 3236  CZ  TYR B4349     3306   2899   2352   -360   -742    273       C  
ATOM   3237  OH  TYR B4349      78.152  21.614  11.081  1.00 22.67           O  
ANISOU 3237  OH  TYR B4349     3214   3042   2355   -381   -711    364       O  
ATOM   3238  N   VAL B4350      70.246  20.432   8.543  1.00 26.41           N  
ANISOU 3238  N   VAL B4350     4034   2913   3084   -311  -1071    -94       N  
ATOM   3239  CA  VAL B4350      68.845  20.376   8.050  1.00 27.00           C  
ANISOU 3239  CA  VAL B4350     4099   2937   3222   -331  -1180   -133       C  
ATOM   3240  C   VAL B4350      68.171  21.712   8.374  1.00 26.84           C  
ANISOU 3240  C   VAL B4350     4024   2915   3255   -342  -1194    -75       C  
ATOM   3241  O   VAL B4350      68.302  22.203   9.518  1.00 26.34           O  
ANISOU 3241  O   VAL B4350     3919   2843   3244   -356  -1118    -47       O  
ATOM   3242  CB  VAL B4350      68.068  19.176   8.621  1.00 28.39           C  
ANISOU 3242  CB  VAL B4350     4228   3032   3525   -359  -1196   -174       C  
ATOM   3243  CG1 VAL B4350      67.967  19.209  10.138  1.00 28.72           C  
ANISOU 3243  CG1 VAL B4350     4184   3064   3664   -371  -1109   -118       C  
ATOM   3244  CG2 VAL B4350      66.685  19.073   8.000  1.00 29.80           C  
ANISOU 3244  CG2 VAL B4350     4373   3176   3775   -400  -1329   -207       C  
ATOM   3245  N   GLN B4351      67.530  22.291   7.363  1.00 27.19           N  
ANISOU 3245  N   GLN B4351     4082   2974   3274   -329  -1285    -56       N  
ATOM   3246  CA  GLN B4351      66.764  23.548   7.510  1.00 27.31           C  
ANISOU 3246  CA  GLN B4351     4045   2967   3361   -314  -1296     15       C  
ATOM   3247  C   GLN B4351      65.328  23.173   7.878  1.00 28.67           C  
ANISOU 3247  C   GLN B4351     4110   3103   3678   -323  -1356     15       C  
ATOM   3248  O   GLN B4351      64.722  22.342   7.170  1.00 30.17           O  
ANISOU 3248  O   GLN B4351     4283   3309   3868   -349  -1472    -21       O  
ATOM   3249  CB  GLN B4351      66.873  24.379   6.231  1.00 28.21           C  
ANISOU 3249  CB  GLN B4351     4212   3128   3375   -279  -1355     79       C  
ATOM   3250  CG  GLN B4351      68.155  25.198   6.146  1.00 28.19           C  
ANISOU 3250  CG  GLN B4351     4275   3141   3292   -276  -1261    129       C  
ATOM   3251  CD  GLN B4351      69.423  24.379   6.175  1.00 28.04           C  
ANISOU 3251  CD  GLN B4351     4303   3173   3175   -290  -1199     82       C  
ATOM   3252  OE1 GLN B4351      70.291  24.578   7.028  1.00 27.24           O  
ANISOU 3252  OE1 GLN B4351     4188   3068   3094   -323  -1110     89       O  
ATOM   3253  NE2 GLN B4351      69.535  23.437   5.252  1.00 28.33           N  
ANISOU 3253  NE2 GLN B4351     4395   3262   3105   -263  -1247     32       N  
ATOM   3254  N   ILE B4352      64.820  23.744   8.965  1.00 28.39           N  
ANISOU 3254  N   ILE B4352     4005   3022   3758   -308  -1275     49       N  
ATOM   3255  CA  ILE B4352      63.439  23.443   9.439  1.00 29.49           C  
ANISOU 3255  CA  ILE B4352     4012   3136   4054   -305  -1298     79       C  
ATOM   3256  C   ILE B4352      62.666  24.752   9.478  1.00 29.89           C  
ANISOU 3256  C   ILE B4352     4007   3160   4187   -233  -1273    165       C  
ATOM   3257  O   ILE B4352      63.163  25.742  10.014  1.00 28.66           O  
ANISOU 3257  O   ILE B4352     3913   2959   4016   -199  -1164    169       O  
ATOM   3258  CB  ILE B4352      63.459  22.776  10.830  1.00 28.99           C  
ANISOU 3258  CB  ILE B4352     3908   3047   4057   -325  -1185     56       C  
ATOM   3259  CG1 ILE B4352      64.375  21.547  10.889  1.00 28.63           C  
ANISOU 3259  CG1 ILE B4352     3923   3009   3943   -372  -1181     -2       C  
ATOM   3260  CG2 ILE B4352      62.042  22.450  11.281  1.00 30.29           C  
ANISOU 3260  CG2 ILE B4352     3918   3194   4394   -321  -1191    111       C  
ATOM   3261  CD1 ILE B4352      63.921  20.378  10.041  1.00 29.51           C  
ANISOU 3261  CD1 ILE B4352     4020   3100   4090   -422  -1301    -43       C  
ATOM   3262  N   PRO B4353      61.444  24.813   8.902  1.00 31.50           N  
ANISOU 3262  N   PRO B4353     4092   3388   4489   -208  -1376    238       N  
ATOM   3263  CA  PRO B4353      60.627  26.019   8.991  1.00 32.61           C  
ANISOU 3263  CA  PRO B4353     4157   3495   4737   -111  -1333    346       C  
ATOM   3264  C   PRO B4353      60.509  26.410  10.470  1.00 32.38           C  
ANISOU 3264  C   PRO B4353     4116   3391   4795    -66  -1141    328       C  
ATOM   3265  O   PRO B4353      60.297  25.533  11.290  1.00 31.96           O  
ANISOU 3265  O   PRO B4353     4007   3350   4784   -104  -1095    293       O  
ATOM   3266  CB  PRO B4353      59.278  25.606   8.381  1.00 34.49           C  
ANISOU 3266  CB  PRO B4353     4218   3800   5086   -111  -1480    430       C  
ATOM   3267  CG  PRO B4353      59.627  24.454   7.457  1.00 34.26           C  
ANISOU 3267  CG  PRO B4353     4239   3840   4939   -221  -1648    345       C  
ATOM   3268  CD  PRO B4353      60.803  23.754   8.106  1.00 32.94           C  
ANISOU 3268  CD  PRO B4353     4203   3627   4685   -275  -1544    223       C  
ATOM   3269  N   THR B4354      60.653  27.703  10.774  1.00 32.55           N  
ANISOU 3269  N   THR B4354     4201   3330   4836     13  -1029    351       N  
ATOM   3270  CA  THR B4354      60.615  28.170  12.186  1.00 33.50           C  
ANISOU 3270  CA  THR B4354     4352   3375   5000     57   -839    301       C  
ATOM   3271  C   THR B4354      59.329  27.686  12.870  1.00 35.07           C  
ANISOU 3271  C   THR B4354     4378   3601   5344    112   -781    360       C  
ATOM   3272  O   THR B4354      59.408  27.299  14.053  1.00 34.52           O  
ANISOU 3272  O   THR B4354     4321   3537   5257    104   -657    303       O  
ATOM   3273  CB  THR B4354      60.788  29.692  12.253  1.00 35.07           C  
ANISOU 3273  CB  THR B4354     4651   3446   5227    138   -736    311       C  
ATOM   3274  OG1 THR B4354      62.007  29.995  11.573  1.00 34.65           O  
ANISOU 3274  OG1 THR B4354     4730   3382   5051     62   -796    279       O  
ATOM   3275  CG2 THR B4354      60.833  30.228  13.668  1.00 36.21           C  
ANISOU 3275  CG2 THR B4354     4872   3505   5381    176   -543    218       C  
ATOM   3276  N   THR B4355      58.205  27.681  12.148  1.00 36.66           N  
ANISOU 3276  N   THR B4355     4413   3837   5677    163   -872    486       N  
ATOM   3277  CA  THR B4355      56.892  27.257  12.708  1.00 39.24           C  
ANISOU 3277  CA  THR B4355     4529   4201   6176    213   -821    579       C  
ATOM   3278  C   THR B4355      56.903  25.768  13.092  1.00 39.14           C  
ANISOU 3278  C   THR B4355     4455   4257   6160     89   -866    540       C  
ATOM   3279  O   THR B4355      56.024  25.375  13.879  1.00 40.88           O  
ANISOU 3279  O   THR B4355     4522   4498   6510    117   -770    609       O  
ATOM   3280  CB  THR B4355      55.760  27.541  11.711  1.00 41.25           C  
ANISOU 3280  CB  THR B4355     4595   4507   6572    273   -952    740       C  
ATOM   3281  OG1 THR B4355      56.066  26.861  10.494  1.00 41.08           O  
ANISOU 3281  OG1 THR B4355     4583   4566   6459    153  -1189    723       O  
ATOM   3282  CG2 THR B4355      55.573  29.015  11.431  1.00 43.06           C  
ANISOU 3282  CG2 THR B4355     4857   4652   6850    429   -876    824       C  
ATOM   3283  N   CYS B4356      57.852  24.983  12.566  1.00 37.79           N  
ANISOU 3283  N   CYS B4356     4393   4108   5857    -32   -987    448       N  
ATOM   3284  CA  CYS B4356      57.925  23.520  12.852  1.00 37.72           C  
ANISOU 3284  CA  CYS B4356     4343   4127   5861   -147  -1028    413       C  
ATOM   3285  C   CYS B4356      59.210  23.165  13.613  1.00 36.32           C  
ANISOU 3285  C   CYS B4356     4333   3933   5532   -182   -931    310       C  
ATOM   3286  O   CYS B4356      59.437  21.961  13.835  1.00 35.64           O  
ANISOU 3286  O   CYS B4356     4236   3853   5450   -262   -951    291       O  
ATOM   3287  CB  CYS B4356      57.913  22.715  11.558  1.00 38.55           C  
ANISOU 3287  CB  CYS B4356     4435   4264   5949   -254  -1253    388       C  
ATOM   3288  SG  CYS B4356      56.434  22.981  10.549  1.00 42.61           S  
ANISOU 3288  SG  CYS B4356     4731   4843   6616   -246  -1430    517       S  
ATOM   3289  N   ALA B4357      59.994  24.172  14.014  1.00 35.17           N  
ANISOU 3289  N   ALA B4357     4326   3763   5271   -127   -832    257       N  
ATOM   3290  CA  ALA B4357      61.309  23.959  14.671  1.00 33.52           C  
ANISOU 3290  CA  ALA B4357     4264   3567   4904   -170   -769    168       C  
ATOM   3291  C   ALA B4357      61.165  23.335  16.066  1.00 33.52           C  
ANISOU 3291  C   ALA B4357     4225   3601   4909   -163   -632    183       C  
ATOM   3292  O   ALA B4357      62.203  22.948  16.634  1.00 31.19           O  
ANISOU 3292  O   ALA B4357     4022   3345   4484   -202   -600    136       O  
ATOM   3293  CB  ALA B4357      62.060  25.266  14.736  1.00 33.92           C  
ANISOU 3293  CB  ALA B4357     4452   3580   4855   -137   -716    110       C  
ATOM   3294  N   ASN B4358      59.943  23.224  16.596  1.00 34.81           N  
ANISOU 3294  N   ASN B4358     4246   3768   5212   -111   -551    267       N  
ATOM   3295  CA  ASN B4358      59.758  22.579  17.926  1.00 35.67           C  
ANISOU 3295  CA  ASN B4358     4311   3924   5316    -96   -404    310       C  
ATOM   3296  C   ASN B4358      59.922  21.056  17.800  1.00 34.33           C  
ANISOU 3296  C   ASN B4358     4083   3763   5194   -192   -475    356       C  
ATOM   3297  O   ASN B4358      60.060  20.398  18.846  1.00 33.70           O  
ANISOU 3297  O   ASN B4358     3991   3727   5084   -189   -364    405       O  
ATOM   3298  CB  ASN B4358      58.389  22.880  18.537  1.00 39.22           C  
ANISOU 3298  CB  ASN B4358     4609   4381   5910     -2   -269    410       C  
ATOM   3299  CG  ASN B4358      57.249  22.401  17.665  1.00 42.31           C  
ANISOU 3299  CG  ASN B4358     4797   4757   6522    -32   -381    519       C  
ATOM   3300  OD1 ASN B4358      57.235  22.653  16.461  1.00 44.52           O  
ANISOU 3300  OD1 ASN B4358     5075   5009   6831    -65   -547    499       O  
ATOM   3301  ND2 ASN B4358      56.283  21.724  18.266  1.00 45.22           N  
ANISOU 3301  ND2 ASN B4358     4984   5154   7040    -28   -295    645       N  
ATOM   3302  N   ASP B4359      59.892  20.520  16.574  1.00 32.65           N  
ANISOU 3302  N   ASP B4359     3846   3506   5050   -267   -647    340       N  
ATOM   3303  CA  ASP B4359      60.004  19.049  16.368  1.00 31.70           C  
ANISOU 3303  CA  ASP B4359     3692   3350   5002   -361   -713    362       C  
ATOM   3304  C   ASP B4359      60.746  18.774  15.063  1.00 30.17           C  
ANISOU 3304  C   ASP B4359     3604   3118   4740   -421   -879    262       C  
ATOM   3305  O   ASP B4359      60.143  18.349  14.079  1.00 30.35           O  
ANISOU 3305  O   ASP B4359     3570   3101   4858   -487  -1020    249       O  
ATOM   3306  CB  ASP B4359      58.616  18.401  16.373  1.00 33.10           C  
ANISOU 3306  CB  ASP B4359     3666   3497   5411   -406   -728    470       C  
ATOM   3307  CG  ASP B4359      58.616  16.884  16.256  1.00 34.25           C  
ANISOU 3307  CG  ASP B4359     3776   3565   5670   -517   -780    493       C  
ATOM   3308  OD1 ASP B4359      59.698  16.271  16.422  1.00 33.32           O  
ANISOU 3308  OD1 ASP B4359     3787   3421   5450   -526   -758    450       O  
ATOM   3309  OD2 ASP B4359      57.525  16.321  16.004  1.00 35.87           O  
ANISOU 3309  OD2 ASP B4359     3816   3730   6083   -595   -840    564       O  
ATOM   3310  N   PRO B4360      62.071  19.034  14.998  1.00 28.12           N  
ANISOU 3310  N   PRO B4360     3498   2884   4302   -402   -867    190       N  
ATOM   3311  CA  PRO B4360      62.843  18.769  13.783  1.00 27.82           C  
ANISOU 3311  CA  PRO B4360     3564   2823   4181   -437   -990    106       C  
ATOM   3312  C   PRO B4360      62.820  17.290  13.357  1.00 28.21           C  
ANISOU 3312  C   PRO B4360     3611   2791   4313   -506  -1052     85       C  
ATOM   3313  O   PRO B4360      62.755  17.023  12.170  1.00 29.03           O  
ANISOU 3313  O   PRO B4360     3760   2861   4406   -549  -1184     10       O  
ATOM   3314  CB  PRO B4360      64.265  19.216  14.162  1.00 26.55           C  
ANISOU 3314  CB  PRO B4360     3523   2718   3844   -401   -921     75       C  
ATOM   3315  CG  PRO B4360      64.046  20.220  15.272  1.00 26.90           C  
ANISOU 3315  CG  PRO B4360     3547   2809   3861   -355   -808    105       C  
ATOM   3316  CD  PRO B4360      62.882  19.657  16.056  1.00 27.90           C  
ANISOU 3316  CD  PRO B4360     3545   2921   4134   -349   -740    186       C  
ATOM   3317  N   VAL B4361      62.863  16.364  14.319  1.00 28.47           N  
ANISOU 3317  N   VAL B4361     3605   2790   4422   -515   -953    150       N  
ATOM   3318  CA  VAL B4361      62.855  14.911  13.968  1.00 29.29           C  
ANISOU 3318  CA  VAL B4361     3720   2771   4636   -581   -993    132       C  
ATOM   3319  C   VAL B4361      61.549  14.585  13.237  1.00 31.03           C  
ANISOU 3319  C   VAL B4361     3841   2922   5025   -682  -1127    112       C  
ATOM   3320  O   VAL B4361      61.614  13.953  12.162  1.00 32.24           O  
ANISOU 3320  O   VAL B4361     4070   2994   5184   -749  -1253      2       O  
ATOM   3321  CB  VAL B4361      63.040  14.021  15.209  1.00 29.63           C  
ANISOU 3321  CB  VAL B4361     3719   2782   4754   -564   -848    250       C  
ATOM   3322  CG1 VAL B4361      62.920  12.544  14.858  1.00 30.49           C  
ANISOU 3322  CG1 VAL B4361     3841   2720   5023   -636   -876    240       C  
ATOM   3323  CG2 VAL B4361      64.364  14.302  15.905  1.00 28.54           C  
ANISOU 3323  CG2 VAL B4361     3664   2743   4435   -475   -747    278       C  
ATOM   3324  N   GLY B4362      60.415  15.010  13.800  1.00 32.09           N  
ANISOU 3324  N   GLY B4362     3811   3096   5285   -690  -1099    213       N  
ATOM   3325  CA  GLY B4362      59.097  14.751  13.190  1.00 34.15           C  
ANISOU 3325  CA  GLY B4362     3926   3320   5729   -794  -1235    227       C  
ATOM   3326  C   GLY B4362      58.987  15.406  11.825  1.00 34.87           C  
ANISOU 3326  C   GLY B4362     4065   3461   5720   -810  -1422    125       C  
ATOM   3327  O   GLY B4362      58.426  14.778  10.906  1.00 36.62           O  
ANISOU 3327  O   GLY B4362     4262   3632   6018   -928  -1596     59       O  
ATOM   3328  N   PHE B4363      59.525  16.619  11.688  1.00 33.77           N  
ANISOU 3328  N   PHE B4363     4001   3417   5411   -704  -1392    114       N  
ATOM   3329  CA  PHE B4363      59.452  17.323  10.384  1.00 34.68           C  
ANISOU 3329  CA  PHE B4363     4163   3593   5417   -701  -1555     52       C  
ATOM   3330  C   PHE B4363      60.221  16.539   9.311  1.00 35.72           C  
ANISOU 3330  C   PHE B4363     4466   3680   5425   -757  -1667    -95       C  
ATOM   3331  O   PHE B4363      59.667  16.362   8.214  1.00 37.85           O  
ANISOU 3331  O   PHE B4363     4730   3968   5683   -832  -1854   -157       O  
ATOM   3332  CB  PHE B4363      59.989  18.753  10.486  1.00 32.86           C  
ANISOU 3332  CB  PHE B4363     3995   3442   5048   -578  -1477     82       C  
ATOM   3333  CG  PHE B4363      59.814  19.532   9.210  1.00 33.37           C  
ANISOU 3333  CG  PHE B4363     4086   3574   5018   -560  -1627     68       C  
ATOM   3334  CD1 PHE B4363      58.648  20.243   8.974  1.00 34.66           C  
ANISOU 3334  CD1 PHE B4363     4090   3791   5285   -536  -1699    170       C  
ATOM   3335  CD2 PHE B4363      60.786  19.507   8.221  1.00 33.07           C  
ANISOU 3335  CD2 PHE B4363     4219   3557   4788   -559  -1693    -25       C  
ATOM   3336  CE1 PHE B4363      58.472  20.940   7.789  1.00 35.33           C  
ANISOU 3336  CE1 PHE B4363     4192   3953   5277   -511  -1844    188       C  
ATOM   3337  CE2 PHE B4363      60.604  20.204   7.035  1.00 34.15           C  
ANISOU 3337  CE2 PHE B4363     4381   3774   4819   -537  -1828    -14       C  
ATOM   3338  CZ  PHE B4363      59.450  20.918   6.822  1.00 34.70           C  
ANISOU 3338  CZ  PHE B4363     4296   3900   4987   -515  -1910     95       C  
ATOM   3339  N   THR B4364      61.444  16.087   9.615  1.00 35.89           N  
ANISOU 3339  N   THR B4364     4631   3655   5348   -717  -1554   -147       N  
ATOM   3340  CA  THR B4364      62.271  15.357   8.611  1.00 38.19           C  
ANISOU 3340  CA  THR B4364     5100   3898   5512   -736  -1618   -288       C  
ATOM   3341  C   THR B4364      61.606  14.029   8.226  1.00 40.90           C  
ANISOU 3341  C   THR B4364     5436   4108   5996   -866  -1725   -374       C  
ATOM   3342  O   THR B4364      61.710  13.632   7.048  1.00 43.24           O  
ANISOU 3342  O   THR B4364     5855   4383   6188   -913  -1858   -518       O  
ATOM   3343  CB  THR B4364      63.707  15.140   9.110  1.00 37.92           C  
ANISOU 3343  CB  THR B4364     5185   3849   5374   -647  -1455   -292       C  
ATOM   3344  OG1 THR B4364      63.687  14.318  10.278  1.00 40.28           O  
ANISOU 3344  OG1 THR B4364     5421   4062   5821   -658  -1336   -221       O  
ATOM   3345  CG2 THR B4364      64.413  16.441   9.417  1.00 36.18           C  
ANISOU 3345  CG2 THR B4364     4977   3749   5019   -554  -1374   -227       C  
ATOM   3346  N  ALEU B4365      60.947  13.360   9.181  0.60 41.24           N  
ANISOU 3346  N  ALEU B4365     5347   4060   6261   -929  -1666   -291       N  
ATOM   3347  N  BLEU B4365      60.919  13.409   9.187  0.40 41.88           N  
ANISOU 3347  N  BLEU B4365     5423   4146   6342   -928  -1667   -287       N  
ATOM   3348  CA ALEU B4365      60.255  12.066   8.913  0.60 43.84           C  
ANISOU 3348  CA ALEU B4365     5654   4228   6776  -1082  -1763   -360       C  
ATOM   3349  CA BLEU B4365      60.256  12.091   9.007  0.40 44.62           C  
ANISOU 3349  CA BLEU B4365     5744   4329   6880  -1077  -1750   -348       C  
ATOM   3350  C  ALEU B4365      59.004  12.281   8.055  0.60 46.18           C  
ANISOU 3350  C  ALEU B4365     5833   4580   7131  -1210  -1995   -393       C  
ATOM   3351  C  BLEU B4365      58.973  12.229   8.172  0.40 46.60           C  
ANISOU 3351  C  BLEU B4365     5874   4624   7206  -1213  -1981   -381       C  
ATOM   3352  O  ALEU B4365      58.777  11.468   7.136  0.60 48.90           O  
ANISOU 3352  O  ALEU B4365     6261   4834   7482  -1338  -2156   -549       O  
ATOM   3353  O  BLEU B4365      58.694  11.311   7.374  0.40 48.93           O  
ANISOU 3353  O  BLEU B4365     6238   4810   7542  -1350  -2131   -526       O  
ATOM   3354  CB ALEU B4365      59.850  11.416  10.240  0.60 43.49           C  
ANISOU 3354  CB ALEU B4365     5469   4087   6966  -1110  -1618   -213       C  
ATOM   3355  CB BLEU B4365      59.950  11.544  10.403  0.40 44.82           C  
ANISOU 3355  CB BLEU B4365     5634   4273   7120  -1086  -1588   -192       C  
ATOM   3356  CG ALEU B4365      60.983  10.852  11.091  0.60 41.67           C  
ANISOU 3356  CG ALEU B4365     5339   3781   6711  -1011  -1416   -166       C  
ATOM   3357  CG BLEU B4365      59.576  10.068  10.472  0.40 46.99           C  
ANISOU 3357  CG BLEU B4365     5905   4329   7618  -1223  -1605   -223       C  
ATOM   3358  CD1ALEU B4365      60.465  10.463  12.465  0.60 41.50           C  
ANISOU 3358  CD1ALEU B4365     5156   3724   6888  -1020  -1270     23       C  
ATOM   3359  CD1BLEU B4365      60.734   9.201  10.001  0.40 47.13           C  
ANISOU 3359  CD1BLEU B4365     6159   4201   7545  -1184  -1561   -366       C  
ATOM   3360  CD2ALEU B4365      61.641   9.663  10.407  0.60 42.85           C  
ANISOU 3360  CD2ALEU B4365     5673   3744   6862  -1044  -1436   -316       C  
ATOM   3361  CD2BLEU B4365      59.163   9.690  11.884  0.40 47.22           C  
ANISOU 3361  CD2BLEU B4365     5770   4314   7855  -1221  -1434    -17       C  
ATOM   3362  N   LYS B4366      58.223  13.323   8.359  1.00 46.20           N  
ANISOU 3362  N   LYS B4366     5652   4726   7176  -1175  -2009   -252       N  
ATOM   3363  CA  LYS B4366      56.932  13.574   7.658  1.00 48.28           C  
ANISOU 3363  CA  LYS B4366     5745   5071   7527  -1285  -2229   -229       C  
ATOM   3364  C   LYS B4366      57.092  14.338   6.336  1.00 48.35           C  
ANISOU 3364  C   LYS B4366     5853   5220   7295  -1251  -2405   -313       C  
ATOM   3365  O   LYS B4366      56.072  14.471   5.631  1.00 50.72           O  
ANISOU 3365  O   LYS B4366     6020   5608   7640  -1348  -2620   -298       O  
ATOM   3366  CB  LYS B4366      56.014  14.405   8.560  1.00 49.08           C  
ANISOU 3366  CB  LYS B4366     5592   5268   7787  -1225  -2142    -15       C  
ATOM   3367  CG  LYS B4366      55.604  13.753   9.873  1.00 50.57           C  
ANISOU 3367  CG  LYS B4366     5637   5362   8215  -1256  -1971    111       C  
ATOM   3368  CD  LYS B4366      54.862  14.707  10.786  1.00 51.64           C  
ANISOU 3368  CD  LYS B4366     5561   5609   8451  -1148  -1837    311       C  
ATOM   3369  CE  LYS B4366      54.463  14.094  12.112  1.00 53.15           C  
ANISOU 3369  CE  LYS B4366     5613   5733   8847  -1161  -1644    455       C  
ATOM   3370  NZ  LYS B4366      53.858  15.105  13.013  1.00 53.36           N  
ANISOU 3370  NZ  LYS B4366     5473   5877   8923  -1020  -1477    628       N  
ATOM   3371  N   ASN B4367      58.293  14.809   5.990  1.00 45.72           N  
ANISOU 3371  N   ASN B4367     5727   4923   6719  -1125  -2324   -380       N  
ATOM   3372  CA  ASN B4367      58.421  15.645   4.763  1.00 45.50           C  
ANISOU 3372  CA  ASN B4367     5781   5048   6457  -1077  -2468   -416       C  
ATOM   3373  C   ASN B4367      59.403  15.020   3.769  1.00 45.70           C  
ANISOU 3373  C   ASN B4367     6071   5039   6252  -1084  -2511   -617       C  
ATOM   3374  O   ASN B4367      60.196  14.145   4.164  1.00 44.63           O  
ANISOU 3374  O   ASN B4367     6062   4758   6135  -1079  -2379   -706       O  
ATOM   3375  CB  ASN B4367      58.754  17.089   5.140  1.00 43.00           C  
ANISOU 3375  CB  ASN B4367     5430   4837   6069   -911  -2338   -267       C  
ATOM   3376  CG  ASN B4367      57.556  17.784   5.751  1.00 43.31           C  
ANISOU 3376  CG  ASN B4367     5214   4931   6308   -895  -2340    -88       C  
ATOM   3377  OD1 ASN B4367      56.630  18.168   5.040  1.00 45.26           O  
ANISOU 3377  OD1 ASN B4367     5336   5286   6574   -926  -2521    -27       O  
ATOM   3378  ND2 ASN B4367      57.558  17.947   7.062  1.00 41.30           N  
ANISOU 3378  ND2 ASN B4367     4878   4617   6194   -837  -2138      4       N  
ATOM   3379  N  ATHR B4368      59.342  15.491   2.517  0.60 47.05           N  
ANISOU 3379  N  ATHR B4368     6319   5352   6205  -1077  -2680   -667       N  
ATOM   3380  N  BTHR B4368      59.336  15.462   2.508  0.40 46.86           N  
ANISOU 3380  N  BTHR B4368     6296   5325   6182  -1080  -2682   -671       N  
ATOM   3381  CA ATHR B4368      60.162  14.973   1.388  0.60 48.27           C  
ANISOU 3381  CA ATHR B4368     6734   5511   6095  -1072  -2733   -864       C  
ATOM   3382  CA BTHR B4368      60.217  14.932   1.433  0.40 47.76           C  
ANISOU 3382  CA BTHR B4368     6675   5436   6033  -1070  -2721   -868       C  
ATOM   3383  C  ATHR B4368      60.938  16.123   0.739  0.60 46.96           C  
ANISOU 3383  C  ATHR B4368     6666   5510   5666   -917  -2682   -792       C  
ATOM   3384  C  BTHR B4368      60.934  16.096   0.742  0.40 46.78           C  
ANISOU 3384  C  BTHR B4368     6643   5484   5645   -919  -2683   -796       C  
ATOM   3385  O  ATHR B4368      60.374  17.231   0.637  0.60 46.64           O  
ANISOU 3385  O  ATHR B4368     6487   5605   5626   -872  -2744   -627       O  
ATOM   3386  O  BTHR B4368      60.330  17.180   0.621  0.40 46.63           O  
ANISOU 3386  O  BTHR B4368     6485   5603   5629   -880  -2754   -633       O  
ATOM   3387  CB ATHR B4368      59.270  14.288   0.345  0.60 52.17           C  
ANISOU 3387  CB ATHR B4368     7248   6035   6538  -1243  -3018  -1017       C  
ATOM   3388  CB BTHR B4368      59.422  14.065   0.446  0.40 51.19           C  
ANISOU 3388  CB BTHR B4368     7154   5867   6429  -1246  -2986  -1045       C  
ATOM   3389  OG1ATHR B4368      58.443  13.342   1.024  0.60 53.64           O  
ANISOU 3389  OG1ATHR B4368     7299   6061   7019  -1407  -3066  -1043       O  
ATOM   3390  OG1BTHR B4368      58.362  14.844  -0.109  0.40 52.27           O  
ANISOU 3390  OG1BTHR B4368     7121   6197   6541  -1289  -3207   -935       O  
ATOM   3391  CG2ATHR B4368      60.053  13.605  -0.755  0.60 53.93           C  
ANISOU 3391  CG2ATHR B4368     7766   6238   6484  -1243  -3059  -1257       C  
ATOM   3392  CG2BTHR B4368      58.848  12.824   1.094  0.40 52.48           C  
ANISOU 3392  CG2BTHR B4368     7249   5818   6871  -1412  -3005  -1125       C  
ATOM   3393  N   VAL B4369      62.177  15.856   0.316  1.00 46.33           N  
ANISOU 3393  N   VAL B4369     6806   5410   5386   -832  -2561   -897       N  
ATOM   3394  CA  VAL B4369      63.022  16.878  -0.365  1.00 45.67           C  
ANISOU 3394  CA  VAL B4369     6822   5480   5050   -690  -2493   -820       C  
ATOM   3395  C   VAL B4369      62.827  16.747  -1.878  1.00 49.03           C  
ANISOU 3395  C   VAL B4369     7390   6045   5192   -715  -2687   -936       C  
ATOM   3396  O   VAL B4369      62.814  15.604  -2.382  1.00 50.25           O  
ANISOU 3396  O   VAL B4369     7692   6124   5275   -796  -2764  -1157       O  
ATOM   3397  CB  VAL B4369      64.506  16.711   0.013  1.00 44.53           C  
ANISOU 3397  CB  VAL B4369     6806   5268   4845   -577  -2243   -837       C  
ATOM   3398  CG1 VAL B4369      65.390  17.724  -0.700  1.00 44.23           C  
ANISOU 3398  CG1 VAL B4369     6853   5383   4569   -449  -2165   -743       C  
ATOM   3399  CG2 VAL B4369      64.707  16.784   1.518  1.00 42.04           C  
ANISOU 3399  CG2 VAL B4369     6357   4840   4775   -563  -2075   -731       C  
ATOM   3400  N   CYS B4370      62.666  17.879  -2.563  1.00 49.59           N  
ANISOU 3400  N   CYS B4370     7428   6307   5104   -646  -2760   -791       N  
ATOM   3401  CA  CYS B4370      62.532  17.879  -4.040  1.00 52.87           C  
ANISOU 3401  CA  CYS B4370     7985   6904   5196   -649  -2941   -871       C  
ATOM   3402  C   CYS B4370      63.897  17.540  -4.645  1.00 54.18           C  
ANISOU 3402  C   CYS B4370     8407   7076   5099   -540  -2771   -987       C  
ATOM   3403  O   CYS B4370      64.877  18.236  -4.314  1.00 52.00           O  
ANISOU 3403  O   CYS B4370     8135   6806   4814   -412  -2552   -848       O  
ATOM   3404  CB  CYS B4370      62.034  19.229  -4.531  1.00 52.87           C  
ANISOU 3404  CB  CYS B4370     7866   7106   5115   -580  -3038   -633       C  
ATOM   3405  SG  CYS B4370      61.932  19.366  -6.332  1.00 55.68           S  
ANISOU 3405  SG  CYS B4370     8392   7735   5029   -558  -3253   -679       S  
ATOM   3406  N   THR B4371      63.948  16.500  -5.482  1.00 58.10           N  
ANISOU 3406  N   THR B4371     9108   7566   5400   -594  -2864  -1238       N  
ATOM   3407  CA  THR B4371      65.216  16.039  -6.109  1.00 60.06           C  
ANISOU 3407  CA  THR B4371     9614   7813   5390   -473  -2683  -1371       C  
ATOM   3408  C   THR B4371      65.700  17.043  -7.164  1.00 61.41           C  
ANISOU 3408  C   THR B4371     9865   8238   5227   -340  -2663  -1235       C  
ATOM   3409  O   THR B4371      66.858  16.905  -7.604  1.00 63.67           O  
ANISOU 3409  O   THR B4371    10326   8552   5312   -207  -2462  -1275       O  
ATOM   3410  CB  THR B4371      65.038  14.644  -6.720  1.00 63.72           C  
ANISOU 3410  CB  THR B4371    10294   8175   5738   -567  -2788  -1702       C  
ATOM   3411  OG1 THR B4371      63.992  14.714  -7.690  1.00 67.33           O  
ANISOU 3411  OG1 THR B4371    10770   8804   6007   -684  -3101  -1775       O  
ATOM   3412  CG2 THR B4371      64.700  13.589  -5.690  1.00 63.51           C  
ANISOU 3412  CG2 THR B4371    10206   7867   6057   -689  -2768  -1819       C  
ATOM   3413  N   VAL B4372      64.869  18.027  -7.527  1.00 60.99           N  
ANISOU 3413  N   VAL B4372     9677   8364   5131   -360  -2843  -1052       N  
ATOM   3414  CA  VAL B4372      65.242  19.010  -8.589  1.00 61.81           C  
ANISOU 3414  CA  VAL B4372     9851   8718   4913   -233  -2835   -887       C  
ATOM   3415  C   VAL B4372      65.841  20.277  -7.962  1.00 58.91           C  
ANISOU 3415  C   VAL B4372     9338   8344   4699   -122  -2629   -585       C  
ATOM   3416  O   VAL B4372      66.976  20.630  -8.344  1.00 59.42           O  
ANISOU 3416  O   VAL B4372     9510   8472   4595      5  -2424   -509       O  
ATOM   3417  CB  VAL B4372      64.036  19.353  -9.488  1.00 65.05           C  
ANISOU 3417  CB  VAL B4372    10213   9348   5153   -304  -3159   -842       C  
ATOM   3418  CG1 VAL B4372      64.362  20.458 -10.484  1.00 66.33           C  
ANISOU 3418  CG1 VAL B4372    10420   9769   5012   -162  -3143   -612       C  
ATOM   3419  CG2 VAL B4372      63.504  18.126 -10.215  1.00 68.46           C  
ANISOU 3419  CG2 VAL B4372    10814   9803   5394   -438  -3385  -1165       C  
ATOM   3420  N   CYS B4373      65.121  20.925  -7.035  1.00 55.32           N  
ANISOU 3420  N   CYS B4373     8652   7809   4557   -170  -2672   -426       N  
ATOM   3421  CA  CYS B4373      65.586  22.222  -6.467  1.00 52.22           C  
ANISOU 3421  CA  CYS B4373     8135   7393   4313    -80  -2497   -154       C  
ATOM   3422  C   CYS B4373      66.217  22.053  -5.075  1.00 48.70           C  
ANISOU 3422  C   CYS B4373     7617   6728   4157    -95  -2289   -175       C  
ATOM   3423  O   CYS B4373      66.841  23.023  -4.608  1.00 48.08           O  
ANISOU 3423  O   CYS B4373     7475   6616   4175    -33  -2125      3       O  
ATOM   3424  CB  CYS B4373      64.441  23.229  -6.407  1.00 52.31           C  
ANISOU 3424  CB  CYS B4373     7954   7465   4454    -88  -2652     58       C  
ATOM   3425  SG  CYS B4373      63.081  22.738  -5.311  1.00 50.77           S  
ANISOU 3425  SG  CYS B4373     7544   7127   4616   -224  -2801    -10       S  
ATOM   3426  N   GLY B4374      66.051  20.888  -4.436  1.00 47.55           N  
ANISOU 3426  N   GLY B4374     7480   6440   4145   -180  -2301   -378       N  
ATOM   3427  CA  GLY B4374      66.645  20.633  -3.106  1.00 44.26           C  
ANISOU 3427  CA  GLY B4374     6997   5841   3978   -189  -2114   -390       C  
ATOM   3428  C   GLY B4374      65.865  21.289  -1.976  1.00 42.41           C  
ANISOU 3428  C   GLY B4374     6555   5518   4038   -235  -2130   -263       C  
ATOM   3429  O   GLY B4374      66.354  21.261  -0.823  1.00 39.81           O  
ANISOU 3429  O   GLY B4374     6167   5066   3893   -237  -1977   -248       O  
ATOM   3430  N   MET B4375      64.694  21.850  -2.282  1.00 43.43           N  
ANISOU 3430  N   MET B4375     6575   5721   4204   -260  -2306   -170       N  
ATOM   3431  CA  MET B4375      63.842  22.514  -1.259  1.00 42.43           C  
ANISOU 3431  CA  MET B4375     6248   5516   4357   -279  -2307    -43       C  
ATOM   3432  C   MET B4375      62.832  21.492  -0.733  1.00 42.24           C  
ANISOU 3432  C   MET B4375     6125   5416   4508   -395  -2428   -163       C  
ATOM   3433  O   MET B4375      62.564  20.504  -1.452  1.00 43.81           O  
ANISOU 3433  O   MET B4375     6404   5650   4590   -471  -2576   -321       O  
ATOM   3434  CB  MET B4375      63.060  23.689  -1.859  1.00 45.08           C  
ANISOU 3434  CB  MET B4375     6487   5967   4672   -222  -2418    157       C  
ATOM   3435  CG  MET B4375      63.919  24.719  -2.577  1.00 46.49           C  
ANISOU 3435  CG  MET B4375     6760   6229   4673   -115  -2323    307       C  
ATOM   3436  SD  MET B4375      65.000  25.659  -1.476  1.00 45.69           S  
ANISOU 3436  SD  MET B4375     6650   5971   4738    -68  -2046    407       S  
ATOM   3437  CE  MET B4375      63.797  26.607  -0.545  1.00 46.32           C  
ANISOU 3437  CE  MET B4375     6534   5946   5118    -50  -2058    548       C  
ATOM   3438  N   TRP B4376      62.298  21.723   0.469  1.00 40.50           N  
ANISOU 3438  N   TRP B4376     5743   5091   4553   -411  -2361    -92       N  
ATOM   3439  CA  TRP B4376      61.241  20.840   1.025  1.00 41.17           C  
ANISOU 3439  CA  TRP B4376     5695   5109   4837   -522  -2461   -159       C  
ATOM   3440  C   TRP B4376      59.973  20.995   0.184  1.00 44.47           C  
ANISOU 3440  C   TRP B4376     5993   5658   5243   -570  -2712   -101       C  
ATOM   3441  O   TRP B4376      59.610  22.151  -0.116  1.00 44.06           O  
ANISOU 3441  O   TRP B4376     5858   5701   5179   -480  -2738     79       O  
ATOM   3442  CB  TRP B4376      60.930  21.181   2.485  1.00 39.49           C  
ANISOU 3442  CB  TRP B4376     5331   4786   4886   -503  -2310    -67       C  
ATOM   3443  CG  TRP B4376      61.990  20.813   3.473  1.00 36.56           C  
ANISOU 3443  CG  TRP B4376     5042   4300   4549   -487  -2102   -128       C  
ATOM   3444  CD1 TRP B4376      62.833  21.662   4.129  1.00 35.27           C  
ANISOU 3444  CD1 TRP B4376     4911   4109   4380   -407  -1924    -58       C  
ATOM   3445  CD2 TRP B4376      62.307  19.490   3.938  1.00 36.29           C  
ANISOU 3445  CD2 TRP B4376     5057   4165   4567   -558  -2061   -259       C  
ATOM   3446  NE1 TRP B4376      63.647  20.959   4.976  1.00 33.60           N  
ANISOU 3446  NE1 TRP B4376     4751   3818   4197   -424  -1789   -130       N  
ATOM   3447  CE2 TRP B4376      63.351  19.625   4.880  1.00 34.37           C  
ANISOU 3447  CE2 TRP B4376     4860   3864   4335   -502  -1858   -242       C  
ATOM   3448  CE3 TRP B4376      61.810  18.211   3.662  1.00 37.97           C  
ANISOU 3448  CE3 TRP B4376     5278   4319   4829   -669  -2177   -385       C  
ATOM   3449  CZ2 TRP B4376      63.913  18.528   5.529  1.00 34.18           C  
ANISOU 3449  CZ2 TRP B4376     4881   3744   4361   -529  -1765   -320       C  
ATOM   3450  CZ3 TRP B4376      62.365  17.127   4.306  1.00 37.66           C  
ANISOU 3450  CZ3 TRP B4376     5300   4148   4860   -699  -2068   -473       C  
ATOM   3451  CH2 TRP B4376      63.401  17.286   5.228  1.00 35.50           C  
ANISOU 3451  CH2 TRP B4376     5061   3835   4589   -618  -1861   -428       C  
ATOM   3452  N   LYS B4377      59.326  19.884  -0.174  1.00 47.20           N  
ANISOU 3452  N   LYS B4377     6324   6004   5604   -710  -2893   -240       N  
ATOM   3453  CA  LYS B4377      58.043  19.989  -0.917  1.00 51.67           C  
ANISOU 3453  CA  LYS B4377     6738   6718   6175   -782  -3165   -178       C  
ATOM   3454  C   LYS B4377      57.025  20.558   0.077  1.00 51.14           C  
ANISOU 3454  C   LYS B4377     6390   6621   6417   -761  -3124     14       C  
ATOM   3455  O   LYS B4377      56.968  20.044   1.214  1.00 50.02           O  
ANISOU 3455  O   LYS B4377     6182   6329   6494   -801  -2986    -14       O  
ATOM   3456  CB  LYS B4377      57.632  18.642  -1.526  1.00 55.20           C  
ANISOU 3456  CB  LYS B4377     7245   7158   6569   -967  -3380   -397       C  
ATOM   3457  CG  LYS B4377      58.645  18.041  -2.496  1.00 57.57           C  
ANISOU 3457  CG  LYS B4377     7848   7473   6551   -967  -3391   -611       C  
ATOM   3458  CD  LYS B4377      58.109  16.913  -3.356  1.00 62.35           C  
ANISOU 3458  CD  LYS B4377     8538   8101   7052  -1148  -3650   -838       C  
ATOM   3459  CE  LYS B4377      57.198  17.371  -4.480  1.00 66.72           C  
ANISOU 3459  CE  LYS B4377     9011   8909   7430  -1197  -3958   -775       C  
ATOM   3460  NZ  LYS B4377      57.936  18.112  -5.534  1.00 67.83           N  
ANISOU 3460  NZ  LYS B4377     9335   9238   7199  -1049  -3946   -734       N  
ATOM   3461  N   GLY B4378      56.332  21.635  -0.305  1.00 51.94           N  
ANISOU 3461  N   GLY B4378     6344   6860   6529   -673  -3207    221       N  
ATOM   3462  CA  GLY B4378      55.337  22.288   0.571  1.00 51.98           C  
ANISOU 3462  CA  GLY B4378     6080   6844   6824   -613  -3145    422       C  
ATOM   3463  C   GLY B4378      55.961  23.349   1.467  1.00 49.74           C  
ANISOU 3463  C   GLY B4378     5835   6448   6615   -446  -2857    528       C  
ATOM   3464  O   GLY B4378      55.199  24.057   2.155  1.00 50.12           O  
ANISOU 3464  O   GLY B4378     5691   6473   6879   -358  -2773    696       O  
ATOM   3465  N   TYR B4379      57.295  23.462   1.469  1.00 47.40           N  
ANISOU 3465  N   TYR B4379     5774   6083   6151   -404  -2708    433       N  
ATOM   3466  CA  TYR B4379      57.990  24.468   2.318  1.00 45.27           C  
ANISOU 3466  CA  TYR B4379     5558   5700   5942   -277  -2451    508       C  
ATOM   3467  C   TYR B4379      59.181  25.076   1.565  1.00 44.83           C  
ANISOU 3467  C   TYR B4379     5708   5672   5650   -211  -2398    510       C  
ATOM   3468  O   TYR B4379      60.275  25.171   2.164  1.00 43.42           O  
ANISOU 3468  O   TYR B4379     5658   5393   5446   -196  -2213    444       O  
ATOM   3469  CB  TYR B4379      58.450  23.833   3.632  1.00 43.15           C  
ANISOU 3469  CB  TYR B4379     5317   5282   5793   -321  -2268    393       C  
ATOM   3470  CG  TYR B4379      57.349  23.294   4.510  1.00 43.64           C  
ANISOU 3470  CG  TYR B4379     5175   5308   6099   -373  -2268    420       C  
ATOM   3471  CD1 TYR B4379      56.706  24.108   5.429  1.00 43.65           C  
ANISOU 3471  CD1 TYR B4379     5030   5263   6292   -272  -2128    556       C  
ATOM   3472  CD2 TYR B4379      56.958  21.966   4.437  1.00 44.68           C  
ANISOU 3472  CD2 TYR B4379     5261   5436   6278   -521  -2391    312       C  
ATOM   3473  CE1 TYR B4379      55.703  23.620   6.251  1.00 44.05           C  
ANISOU 3473  CE1 TYR B4379     4879   5293   6564   -307  -2100    603       C  
ATOM   3474  CE2 TYR B4379      55.957  21.462   5.252  1.00 45.11           C  
ANISOU 3474  CE2 TYR B4379     5110   5454   6574   -578  -2378    363       C  
ATOM   3475  CZ  TYR B4379      55.328  22.292   6.163  1.00 45.18           C  
ANISOU 3475  CZ  TYR B4379     4959   5445   6761   -466  -2228    518       C  
ATOM   3476  OH  TYR B4379      54.341  21.805   6.970  1.00 47.14           O  
ANISOU 3476  OH  TYR B4379     4992   5673   7245   -510  -2191    590       O  
ATOM   3477  N   GLY B4380      58.982  25.469   0.300  1.00 45.72           N  
ANISOU 3477  N   GLY B4380     5840   5936   5594   -177  -2558    599       N  
ATOM   3478  CA  GLY B4380      60.065  26.101  -0.481  1.00 45.89           C  
ANISOU 3478  CA  GLY B4380     6042   6002   5391   -106  -2495    641       C  
ATOM   3479  C   GLY B4380      60.084  25.667  -1.935  1.00 47.52           C  
ANISOU 3479  C   GLY B4380     6342   6402   5311   -134  -2698    608       C  
ATOM   3480  O   GLY B4380      60.429  26.505  -2.790  1.00 49.44           O  
ANISOU 3480  O   GLY B4380     6651   6743   5390    -42  -2700    753       O  
ATOM   3481  N   CYS B4381      59.755  24.402  -2.212  1.00 48.31           N  
ANISOU 3481  N   CYS B4381     6461   6549   5345   -259  -2856    420       N  
ATOM   3482  CA  CYS B4381      59.753  23.902  -3.613  1.00 50.60           C  
ANISOU 3482  CA  CYS B4381     6870   7027   5325   -299  -3064    342       C  
ATOM   3483  C   CYS B4381      58.608  24.555  -4.398  1.00 54.39           C  
ANISOU 3483  C   CYS B4381     7193   7700   5770   -267  -3293    538       C  
ATOM   3484  O   CYS B4381      57.443  24.393  -3.986  1.00 55.26           O  
ANISOU 3484  O   CYS B4381     7085   7813   6096   -328  -3420    584       O  
ATOM   3485  CB  CYS B4381      59.636  22.384  -3.664  1.00 50.41           C  
ANISOU 3485  CB  CYS B4381     6918   6968   5266   -456  -3178     70       C  
ATOM   3486  SG  CYS B4381      59.361  21.743  -5.337  1.00 53.35           S  
ANISOU 3486  SG  CYS B4381     7433   7573   5262   -530  -3476    -64       S  
ATOM   3487  N   SER B4382      58.944  25.250  -5.489  1.00 57.36           N  
ANISOU 3487  N   SER B4382     7665   8244   5885   -171  -3337    669       N  
ATOM   3488  CA  SER B4382      57.946  25.945  -6.348  1.00 62.14           C  
ANISOU 3488  CA  SER B4382     8126   9066   6416   -114  -3559    898       C  
ATOM   3489  C   SER B4382      57.932  25.330  -7.755  1.00 66.49           C  
ANISOU 3489  C   SER B4382     8819   9869   6571   -175  -3806    790       C  
ATOM   3490  O   SER B4382      57.416  25.988  -8.689  1.00 68.98           O  
ANISOU 3490  O   SER B4382     9073  10413   6720   -103  -3976   1000       O  
ATOM   3491  CB  SER B4382      58.236  27.425  -6.394  1.00 62.31           C  
ANISOU 3491  CB  SER B4382     8120   9070   6481     68  -3397   1196       C  
ATOM   3492  OG  SER B4382      59.557  27.665  -6.860  1.00 62.15           O  
ANISOU 3492  OG  SER B4382     8331   9048   6233    128  -3230   1179       O  
ATOM   3493  N   CYS B4383      58.445  24.101  -7.891  1.00 67.57           N  
ANISOU 3493  N   CYS B4383     9143   9968   6563   -298  -3826    477       N  
ATOM   3494  CA  CYS B4383      58.522  23.407  -9.210  1.00 72.77           C  
ANISOU 3494  CA  CYS B4383     9992  10844   6812   -362  -4041    310       C  
ATOM   3495  C   CYS B4383      57.126  23.158  -9.802  1.00 78.09           C  
ANISOU 3495  C   CYS B4383    10494  11727   7448   -480  -4420    334       C  
ATOM   3496  O   CYS B4383      57.023  23.121 -11.042  1.00 82.19           O  
ANISOU 3496  O   CYS B4383    11123  12510   7592   -482  -4628    324       O  
ATOM   3497  CB  CYS B4383      59.262  22.078  -9.085  1.00 71.22           C  
ANISOU 3497  CB  CYS B4383    10021  10505   6532   -468  -3967    -49       C  
ATOM   3498  SG  CYS B4383      61.023  22.253  -8.673  1.00 66.83           S  
ANISOU 3498  SG  CYS B4383     9678   9780   5934   -328  -3559    -78       S  
ATOM   3499  N   ASP B4384      56.100  23.003  -8.955  1.00 80.79           N  
ANISOU 3499  N   ASP B4384    10568  11976   8151   -574  -4504    377       N  
ATOM   3500  CA  ASP B4384      54.717  22.703  -9.426  1.00 86.40           C  
ANISOU 3500  CA  ASP B4384    11063  12886   8878   -713  -4877    410       C  
ATOM   3501  C   ASP B4384      53.998  23.978  -9.891  1.00 89.40           C  
ANISOU 3501  C   ASP B4384    11223  13492   9250   -562  -4989    797       C  
ATOM   3502  O   ASP B4384      52.908  23.840 -10.486  1.00 93.95           O  
ANISOU 3502  O   ASP B4384    11617  14303   9776   -657  -5327    867       O  
ATOM   3503  CB  ASP B4384      53.908  21.988  -8.338  1.00 87.04           C  
ANISOU 3503  CB  ASP B4384    10922  12782   9365   -874  -4907    324       C  
ATOM   3504  CG  ASP B4384      54.425  20.599  -8.001  1.00 87.64           C  
ANISOU 3504  CG  ASP B4384    11196  12648   9453  -1046  -4856    -46       C  
ATOM   3505  OD1 ASP B4384      54.960  19.934  -8.914  1.00 90.16           O  
ANISOU 3505  OD1 ASP B4384    11787  13038   9429  -1110  -4953   -287       O  
ATOM   3506  OD2 ASP B4384      54.308  20.200  -6.824  1.00 85.84           O  
ANISOU 3506  OD2 ASP B4384    10859  12184   9571  -1100  -4703    -85       O  
ATOM   3507  N   GLN B4385      54.573  25.162  -9.646  1.00 88.80           N  
ANISOU 3507  N   GLN B4385    11158  13348   9230   -343  -4726   1047       N  
ATOM   3508  CA  GLN B4385      53.927  26.436 -10.072  1.00 92.36           C  
ANISOU 3508  CA  GLN B4385    11410  13979   9703   -171  -4798   1445       C  
ATOM   3509  C   GLN B4385      54.017  26.579 -11.597  1.00 96.47           C  
ANISOU 3509  C   GLN B4385    12065  14839   9750   -139  -5028   1513       C  
ATOM   3510  O   GLN B4385      54.888  25.924 -12.205  1.00 96.26           O  
ANISOU 3510  O   GLN B4385    12336  14854   9382   -196  -5016   1263       O  
ATOM   3511  CB  GLN B4385      54.576  27.638  -9.383  1.00 89.84           C  
ANISOU 3511  CB  GLN B4385    11098  13448   9586     38  -4439   1668       C  
ATOM   3512  CG  GLN B4385      54.388  27.651  -7.874  1.00 87.88           C  
ANISOU 3512  CG  GLN B4385    10707  12899   9781     30  -4220   1633       C  
ATOM   3513  CD  GLN B4385      54.957  28.894  -7.233  1.00 86.49           C  
ANISOU 3513  CD  GLN B4385    10549  12519   9794    223  -3895   1838       C  
ATOM   3514  OE1 GLN B4385      55.392  29.824  -7.909  1.00 87.73           O  
ANISOU 3514  OE1 GLN B4385    10789  12746   9799    367  -3835   2050       O  
ATOM   3515  NE2 GLN B4385      54.951  28.920  -5.910  1.00 83.95           N  
ANISOU 3515  NE2 GLN B4385    10154  11937   9804    222  -3680   1777       N  
ATOM   3516  N   LEU B4386      53.145  27.414 -12.176  1.00101.48           N  
ANISOU 3516  N   LEU B4386    12483  15712  10360    -35  -5216   1853       N  
ATOM   3517  CA  LEU B4386      53.108  27.655 -13.646  1.00105.56           C  
ANISOU 3517  CA  LEU B4386    13096  16602  10410     13  -5458   1979       C  
ATOM   3518  C   LEU B4386      54.475  28.168 -14.114  1.00105.03           C  
ANISOU 3518  C   LEU B4386    13337  16503  10065    166  -5187   2015       C  
ATOM   3519  O   LEU B4386      54.705  28.344 -15.310  1.00108.29           O  
ANISOU 3519  O   LEU B4386    13893  17204  10047    225  -5314   2100       O  
ATOM   3520  CB  LEU B4386      52.006  28.673 -13.962  1.00109.55           C  
ANISOU 3520  CB  LEU B4386    13277  17320  11024    153  -5633   2421       C  
ATOM   3521  CG  LEU B4386      50.590  28.277 -13.544  1.00111.96           C  
ANISOU 3521  CG  LEU B4386    13219  17695  11623     21  -5902   2454       C  
ATOM   3522  CD1 LEU B4386      49.620  29.430 -13.763  1.00114.51           C  
ANISOU 3522  CD1 LEU B4386    13210  18197  12099    218  -6002   2943       C  
ATOM   3523  CD2 LEU B4386      50.121  27.038 -14.293  1.00115.28           C  
ANISOU 3523  CD2 LEU B4386    13683  18365  11751   -248  -6308   2157       C  
TER    3524      LEU B4386                                                      
HETATM 3525  S   SO3 A7101      82.292  47.945  18.254  0.50 69.41           S  
HETATM 3526  O1  SO3 A7101      80.916  48.145  18.806  0.50 67.83           O  
HETATM 3527  O2  SO3 A7101      83.139  47.685  19.460  0.50 66.52           O  
HETATM 3528  O3  SO3 A7101      82.222  46.619  17.562  0.50 67.92           O  
HETATM 3529  N   SAM A7102      81.976  19.248  24.241  1.00 22.37           N  
HETATM 3530  CA  SAM A7102      80.645  18.721  24.638  1.00 21.65           C  
HETATM 3531  C   SAM A7102      79.549  19.545  23.944  1.00 23.13           C  
HETATM 3532  O   SAM A7102      79.816  19.973  22.801  1.00 22.10           O  
HETATM 3533  OXT SAM A7102      78.464  19.699  24.538  1.00 23.14           O  
HETATM 3534  CB  SAM A7102      80.504  18.746  26.166  1.00 23.79           C  
HETATM 3535  CG  SAM A7102      81.590  17.912  26.848  1.00 24.12           C  
HETATM 3536  SD  SAM A7102      81.319  17.667  28.619  1.00 27.21           S  
HETATM 3537  CE  SAM A7102      81.617  19.312  29.244  1.00 28.09           C  
HETATM 3538  C5' SAM A7102      82.878  16.831  29.024  1.00 24.97           C  
HETATM 3539  C4' SAM A7102      83.014  15.458  28.389  1.00 24.22           C  
HETATM 3540  O4' SAM A7102      84.322  14.915  28.684  1.00 25.28           O  
HETATM 3541  C3' SAM A7102      82.007  14.407  28.874  1.00 24.27           C  
HETATM 3542  O3' SAM A7102      81.163  13.996  27.802  1.00 22.55           O  
HETATM 3543  C2' SAM A7102      82.884  13.261  29.404  1.00 24.60           C  
HETATM 3544  O2' SAM A7102      82.361  11.982  29.117  1.00 25.16           O  
HETATM 3545  C1' SAM A7102      84.200  13.514  28.678  1.00 24.37           C  
HETATM 3546  N9  SAM A7102      85.364  12.902  29.315  1.00 23.32           N  
HETATM 3547  C8  SAM A7102      85.790  13.079  30.610  1.00 24.25           C  
HETATM 3548  N7  SAM A7102      86.853  12.373  30.912  1.00 23.26           N  
HETATM 3549  C5  SAM A7102      87.147  11.674  29.749  1.00 22.72           C  
HETATM 3550  C6  SAM A7102      88.161  10.747  29.429  1.00 23.65           C  
HETATM 3551  N6  SAM A7102      89.094  10.341  30.288  1.00 24.41           N  
HETATM 3552  N1  SAM A7102      88.165  10.230  28.177  1.00 22.53           N  
HETATM 3553  C2  SAM A7102      87.221  10.637  27.318  1.00 22.92           C  
HETATM 3554  N3  SAM A7102      86.222  11.497  27.507  1.00 22.69           N  
HETATM 3555  C4  SAM A7102      86.236  11.990  28.758  1.00 22.82           C  
HETATM 3556  C   ACT A7103      81.982  24.910  32.710  1.00 34.71           C  
HETATM 3557  O   ACT A7103      81.123  24.208  32.143  1.00 35.46           O  
HETATM 3558  OXT ACT A7103      81.853  26.134  32.919  1.00 28.86           O  
HETATM 3559  CH3 ACT A7103      83.267  24.227  33.180  1.00 33.83           C  
HETATM 3560  C   ACT A7104      90.633  14.108  34.606  1.00 41.49           C  
HETATM 3561  O   ACT A7104      90.898  12.981  34.132  1.00 39.39           O  
HETATM 3562  OXT ACT A7104      89.487  14.467  34.963  1.00 39.02           O  
HETATM 3563  CH3 ACT A7104      91.778  15.112  34.744  1.00 36.45           C  
HETATM 3564  C1  BDF A7105      99.835  38.691  16.378  1.00 76.73           C  
HETATM 3565  C2  BDF A7105     100.223  37.463  17.192  1.00 74.22           C  
HETATM 3566  C3  BDF A7105     100.680  36.298  16.299  1.00 72.18           C  
HETATM 3567  C4  BDF A7105     100.432  34.967  16.998  1.00 68.97           C  
HETATM 3568  C5  BDF A7105      98.941  34.747  17.189  1.00 66.01           C  
HETATM 3569  C6  BDF A7105      98.234  36.085  17.324  1.00 67.78           C  
HETATM 3570  O1  BDF A7105      98.724  38.431  15.531  1.00 79.07           O  
HETATM 3571  O2  BDF A7105     101.279  37.794  18.057  1.00 75.75           O  
HETATM 3572  O3  BDF A7105     102.063  36.445  16.000  1.00 73.12           O  
HETATM 3573  O4  BDF A7105     101.003  33.906  16.233  1.00 68.57           O  
HETATM 3574  O5  BDF A7105      98.396  34.029  16.076  1.00 55.17           O  
HETATM 3575  O6  BDF A7105      99.066  37.082  17.946  1.00 72.02           O  
HETATM 3576 ZN    ZN B4401      70.844   9.080  10.932  1.00 32.30          ZN  
ANISOU 3576 ZN    ZN B4401     4987   2772   4512   -752   -745   -748      ZN  
HETATM 3577 ZN    ZN B4402      61.397  21.623  -6.466  1.00 55.54          ZN  
ANISOU 3577 ZN    ZN B4402     8670   7314   5116    107  -2909   -206      ZN  
HETATM 3578  C1  BDF B4403      64.071  20.367  19.693  1.00 41.13           C  
HETATM 3579  C2  BDF B4403      64.420  21.323  20.825  1.00 41.53           C  
HETATM 3580  C3  BDF B4403      65.931  21.594  20.912  1.00 39.42           C  
HETATM 3581  C4  BDF B4403      66.244  22.457  22.129  1.00 40.78           C  
HETATM 3582  C5  BDF B4403      65.700  21.808  23.391  1.00 41.96           C  
HETATM 3583  C6  BDF B4403      64.229  21.476  23.215  1.00 42.82           C  
HETATM 3584  O1  BDF B4403      64.854  19.184  19.763  1.00 36.18           O  
HETATM 3585  O2  BDF B4403      63.752  22.545  20.635  1.00 43.11           O  
HETATM 3586  O3  BDF B4403      66.366  22.237  19.721  1.00 35.21           O  
HETATM 3587  O4  BDF B4403      67.655  22.648  22.237  1.00 39.48           O  
HETATM 3588  O5  BDF B4403      66.418  20.607  23.683  1.00 41.68           O  
HETATM 3589  O6  BDF B4403      63.993  20.691  22.032  1.00 42.69           O  
HETATM 3590  O   HOH A7201      76.668  39.615  35.466  1.00 50.31           O  
HETATM 3591  O   HOH A7202     101.426  31.500  16.428  1.00 41.77           O  
HETATM 3592  O   HOH A7203      79.107  31.567  32.600  1.00 43.94           O  
HETATM 3593  O   HOH A7204      71.325  37.010  23.473  1.00 44.31           O  
HETATM 3594  O  AHOH A7205      82.503  40.053  17.577  0.50 29.40           O  
HETATM 3595  O  BHOH A7205      84.042  40.141  17.249  0.50 38.69           O  
HETATM 3596  O   HOH A7206     100.369  16.774  36.979  1.00 34.58           O  
HETATM 3597  O   HOH A7207      90.005  10.923  33.020  1.00 37.15           O  
HETATM 3598  O   HOH A7208     105.483  20.338  34.785  1.00 45.49           O  
HETATM 3599  O  BHOH A7209     102.029  18.119  40.779  0.40 34.86           O  
HETATM 3600  O   HOH A7210      83.272   3.882  27.412  1.00 50.92           O  
HETATM 3601  O   HOH A7211      82.719  11.507   5.857  1.00 43.73           O  
HETATM 3602  O   HOH A7212      79.488   5.102  29.058  1.00 50.18           O  
HETATM 3603  O   HOH A7213      85.376  27.092   6.415  1.00 33.18           O  
HETATM 3604  O   HOH A7214      86.544   1.633  22.876  1.00 38.61           O  
HETATM 3605  O   HOH A7215     106.731  16.677  19.182  1.00 41.43           O  
HETATM 3606  O   HOH A7216      93.785  44.088  33.110  1.00 38.63           O  
HETATM 3607  O   HOH A7217      94.335  37.723  21.318  1.00 35.63           O  
HETATM 3608  O   HOH A7218      73.728  17.008  15.150  1.00 24.94           O  
HETATM 3609  O   HOH A7219      79.389  25.230  30.524  1.00 25.82           O  
HETATM 3610  O   HOH A7220      87.362  40.746  40.251  0.50 31.17           O  
HETATM 3611  O   HOH A7221      91.752  42.238  28.527  1.00 38.62           O  
HETATM 3612  O   HOH A7222     104.289  29.725  23.091  1.00 34.38           O  
HETATM 3613  O   HOH A7223      78.097  31.978   8.275  1.00 29.41           O  
HETATM 3614  O   HOH A7224     107.416  19.162  22.137  1.00 38.66           O  
HETATM 3615  O   HOH A7225      92.785  31.745  48.119  1.00 37.20           O  
HETATM 3616  O   HOH A7226      86.338  36.758  15.061  1.00 47.39           O  
HETATM 3617  O   HOH A7227      98.833  29.275   5.529  1.00 37.29           O  
HETATM 3618  O   HOH A7228      86.400  22.371  37.692  1.00 28.61           O  
HETATM 3619  O   HOH A7229     105.139  16.722  14.696  1.00 44.78           O  
HETATM 3620  O   HOH A7230      97.052  36.510  25.194  1.00 28.43           O  
HETATM 3621  O   HOH A7231      81.545  22.501  27.727  1.00 23.20           O  
HETATM 3622  O   HOH A7232     106.872  33.108  18.341  1.00 39.66           O  
HETATM 3623  O   HOH A7233     106.718  26.179  40.768  1.00 50.12           O  
HETATM 3624  O   HOH A7234      76.389  32.092  30.934  1.00 35.01           O  
HETATM 3625  O  AHOH A7235     105.847  31.695  23.674  0.40 39.18           O  
HETATM 3626  O   HOH A7236      80.546  18.191  20.793  1.00 18.61           O  
HETATM 3627  O   HOH A7237     102.282  26.998  10.398  1.00 32.21           O  
HETATM 3628  O   HOH A7238      86.455  28.621  43.555  1.00 39.82           O  
HETATM 3629  O   HOH A7239      91.043  23.448  46.336  1.00 43.31           O  
HETATM 3630  O  AHOH A7240      73.668  31.276  29.582  0.60 31.91           O  
HETATM 3631  O  BHOH A7240      72.422  29.781  30.237  0.40 40.25           O  
HETATM 3632  O   HOH A7241     103.941  15.879  17.450  1.00 42.92           O  
HETATM 3633  O   HOH A7242      86.365  11.138  35.059  1.00 55.55           O  
HETATM 3634  O   HOH A7243      81.690  21.981  37.214  1.00 44.98           O  
HETATM 3635  O  AHOH A7244     102.070  34.083  13.660  0.50 36.22           O  
HETATM 3636  O  BHOH A7244     102.530  35.885  12.470  0.50 40.66           O  
HETATM 3637  O   HOH A7245      82.747  18.392  42.356  0.50 39.48           O  
HETATM 3638  O  AHOH A7246      76.535  39.747  39.802  0.70 59.49           O  
HETATM 3639  O  BHOH A7246      75.978  40.115  41.631  0.30 41.46           O  
HETATM 3640  O   HOH A7247     100.252  11.883   9.389  1.00 37.92           O  
HETATM 3641  O   HOH A7248      84.676  33.416   6.534  1.00 53.46           O  
HETATM 3642  O   HOH A7249      98.468  23.794  44.255  1.00 45.25           O  
HETATM 3643  O   HOH A7250      89.983  20.437  54.150  1.00 39.71           O  
HETATM 3644  O  AHOH A7251      88.941  40.285  23.803  0.50 35.16           O  
HETATM 3645  O  AHOH A7252      78.561  41.227  38.878  0.70 51.05           O  
HETATM 3646  O  BHOH A7252      77.397  41.813  37.234  0.30 34.35           O  
HETATM 3647  O   HOH A7253      82.105  24.695   6.546  1.00 37.14           O  
HETATM 3648  O   HOH A7254      87.751   9.533  24.142  1.00 26.78           O  
HETATM 3649  O   HOH A7255      83.460  21.108   7.676  1.00 26.49           O  
HETATM 3650  O   HOH A7256      90.581  34.217  46.164  1.00 38.37           O  
HETATM 3651  O  AHOH A7257      68.763  14.194  24.888  0.60 39.00           O  
HETATM 3652  O  BHOH A7257      66.836  14.120  24.252  0.40 29.28           O  
HETATM 3653  O   HOH A7258      76.992  42.304  27.332  0.50 31.52           O  
HETATM 3654  O   HOH A7259      68.935  29.070  24.973  1.00 48.75           O  
HETATM 3655  O  AHOH A7260      88.464  12.337  36.209  0.60 50.03           O  
HETATM 3656  O  BHOH A7260      88.075  13.512  37.890  0.40 45.21           O  
HETATM 3657  O  AHOH A7261      94.889   1.425  25.324  0.60 43.56           O  
HETATM 3658  O  BHOH A7261      94.418  -0.137  26.608  0.40 36.69           O  
HETATM 3659  O   HOH A7262     113.549  30.203  21.919  0.50 47.21           O  
HETATM 3660  O   HOH A7263      84.765  30.662  30.959  1.00 20.44           O  
HETATM 3661  O   HOH A7264      97.229   5.934  25.604  1.00 46.80           O  
HETATM 3662  O   HOH A7265      92.785  40.583  26.538  1.00 36.90           O  
HETATM 3663  O   HOH A7266     111.568  32.974  19.027  0.50 42.17           O  
HETATM 3664  O   HOH A7267      97.802  25.815  13.169  1.00 22.11           O  
HETATM 3665  O   HOH A7268     103.625  36.246  18.166  0.50 46.67           O  
HETATM 3666  O   HOH A7269      92.334  -9.230  29.729  1.00 41.95           O  
HETATM 3667  O   HOH A7270     103.136  11.754   2.982  1.00 57.62           O  
HETATM 3668  O   HOH A7271      92.195  30.986   7.678  1.00 39.73           O  
HETATM 3669  O   HOH A7272      81.893  21.979  30.861  1.00 31.18           O  
HETATM 3670  O   HOH A7273      96.830  36.766  14.232  1.00 51.91           O  
HETATM 3671  O   HOH A7274      88.421  37.767  43.149  1.00 39.53           O  
HETATM 3672  O   HOH A7275     108.494  37.314  33.698  1.00 40.27           O  
HETATM 3673  O   HOH A7276      93.938  38.922  14.061  1.00 51.37           O  
HETATM 3674  O   HOH A7277      84.566  15.996  44.111  0.50 40.16           O  
HETATM 3675  O   HOH A7278      91.738   3.599  29.393  1.00 45.63           O  
HETATM 3676  O   HOH A7279      89.117  20.289  31.657  1.00 16.60           O  
HETATM 3677  O   HOH A7280      99.008  24.103  -1.146  1.00 64.75           O  
HETATM 3678  O   HOH A7281      74.847  36.656  11.055  1.00 35.94           O  
HETATM 3679  O   HOH A7282      88.508  -1.145  18.078  1.00 25.62           O  
HETATM 3680  O   HOH A7283      97.402  21.962   1.705  1.00 35.89           O  
HETATM 3681  O   HOH A7284      88.533  26.625  44.968  1.00 33.07           O  
HETATM 3682  O   HOH A7285      81.884  14.979  32.405  1.00 46.62           O  
HETATM 3683  O   HOH A7286      80.622  38.095  15.237  1.00 35.21           O  
HETATM 3684  O  AHOH A7287     101.592  15.501  34.266  0.60 43.89           O  
HETATM 3685  O  BHOH A7287     100.961  15.202  32.562  0.40 42.34           O  
HETATM 3686  O   HOH A7288      79.624  26.401  34.440  1.00 56.57           O  
HETATM 3687  O  AHOH A7289      88.794  38.686  19.498  0.60 42.46           O  
HETATM 3688  O  BHOH A7289      88.940  38.424  21.689  0.40 26.93           O  
HETATM 3689  O   HOH A7290     108.014  25.359  28.388  1.00 28.99           O  
HETATM 3690  O   HOH A7291      84.009  37.971  37.570  1.00 36.00           O  
HETATM 3691  O   HOH A7292      67.612  31.869  25.404  0.50 45.65           O  
HETATM 3692  O   HOH A7293      84.079   5.835  10.443  1.00 48.74           O  
HETATM 3693  O   HOH A7294      82.980  40.761  27.919  1.00 21.14           O  
HETATM 3694  O   HOH A7295      67.229  35.448  24.101  1.00 39.06           O  
HETATM 3695  O   HOH A7296      96.637  17.391   4.090  1.00 43.02           O  
HETATM 3696  O   HOH A7297      93.598  35.090  11.186  1.00 46.67           O  
HETATM 3697  O   HOH A7298      85.042   5.212  14.352  1.00 43.34           O  
HETATM 3698  O   HOH A7299      94.619  14.630   5.486  1.00 48.51           O  
HETATM 3699  O   HOH A7300     105.165  11.722  24.457  1.00 53.09           O  
HETATM 3700  O   HOH A7301     105.771  16.268  12.188  1.00 41.60           O  
HETATM 3701  O   HOH A7302      84.710  29.960  28.340  1.00 18.75           O  
HETATM 3702  O   HOH A7303     104.480  33.074  28.266  1.00 44.51           O  
HETATM 3703  O   HOH A7304      85.987  27.007  39.881  1.00 37.25           O  
HETATM 3704  O   HOH A7305      77.346  16.797  15.955  1.00 21.64           O  
HETATM 3705  O   HOH A7306     106.896  33.938  35.357  1.00 55.88           O  
HETATM 3706  O   HOH A7307      87.254  36.921  35.241  1.00 22.29           O  
HETATM 3707  O   HOH A7308      92.749  31.462  11.897  1.00 31.63           O  
HETATM 3708  O   HOH A7309     100.983  35.598  44.755  1.00 50.64           O  
HETATM 3709  O   HOH A7310      76.308  41.083  31.073  1.00 47.51           O  
HETATM 3710  O   HOH A7311     108.355  31.201  17.111  0.50 34.48           O  
HETATM 3711  O   HOH A7312     104.925  10.081  16.956  1.00 55.87           O  
HETATM 3712  O   HOH A7313      92.588   8.768  30.633  1.00 40.99           O  
HETATM 3713  O   HOH A7314      96.385  15.323  41.023  1.00 56.36           O  
HETATM 3714  O   HOH A7315     111.271  20.935  16.105  1.00 49.49           O  
HETATM 3715  O   HOH A7316      85.196  45.091  20.398  1.00 56.18           O  
HETATM 3716  O   HOH A7317      80.866   7.163  32.143  0.50 33.18           O  
HETATM 3717  O   HOH A7318     109.746  28.610  37.992  1.00 62.00           O  
HETATM 3718  O   HOH A7319      72.416   9.601  21.722  1.00 35.35           O  
HETATM 3719  O   HOH A7320      84.101  37.141  35.027  1.00 28.49           O  
HETATM 3720  O   HOH A7321      92.508  27.448  43.189  1.00 25.04           O  
HETATM 3721  O   HOH A7322     101.723  27.533   2.762  1.00 43.48           O  
HETATM 3722  O   HOH A7323      67.406  32.290  18.062  1.00 28.05           O  
HETATM 3723  O   HOH A7324      81.045  37.055  11.538  1.00 32.70           O  
HETATM 3724  O   HOH A7325      95.836  24.261  12.480  1.00 25.05           O  
HETATM 3725  O   HOH A7326      77.314  40.408  16.335  1.00 33.07           O  
HETATM 3726  O   HOH A7327      91.201  19.570  45.354  0.50 37.89           O  
HETATM 3727  O   HOH A7328     101.196  28.377  43.908  1.00 53.51           O  
HETATM 3728  O   HOH A7329      87.794  12.648  33.489  1.00 50.50           O  
HETATM 3729  O  AHOH A7330     109.792  17.349  18.117  0.60 55.84           O  
HETATM 3730  O  BHOH A7330     109.889  17.941  16.471  0.40 46.67           O  
HETATM 3731  O   HOH A7331     105.257  15.809  35.358  0.50 51.05           O  
HETATM 3732  O   HOH A7332      88.373  17.191  34.708  1.00 22.18           O  
HETATM 3733  O   HOH A7333      96.429  32.673  41.833  1.00 24.93           O  
HETATM 3734  O   HOH A7334      75.222  15.666  17.364  1.00 23.13           O  
HETATM 3735  O   HOH A7335      80.135  38.520  22.545  1.00 21.08           O  
HETATM 3736  O   HOH A7336     103.683  15.234   3.604  1.00 44.11           O  
HETATM 3737  O   HOH A7337     112.148  30.891  28.598  1.00 40.87           O  
HETATM 3738  O   HOH A7338      81.504  20.652  39.603  0.50 46.26           O  
HETATM 3739  O   HOH A7339      96.658  23.042  32.077  1.00 24.66           O  
HETATM 3740  O   HOH A7340      84.785  15.771   5.664  1.00 42.60           O  
HETATM 3741  O   HOH A7341      93.988  30.784   9.634  1.00 33.65           O  
HETATM 3742  O   HOH A7342     105.668  22.949  35.048  1.00 31.79           O  
HETATM 3743  O   HOH A7343     113.318  30.916  13.444  0.50 39.64           O  
HETATM 3744  O   HOH A7344      99.015  36.891  36.423  0.50 25.37           O  
HETATM 3745  O   HOH A7345     114.411  24.917  21.859  0.50 39.48           O  
HETATM 3746  O   HOH A7346      78.117  27.253  31.855  1.00 35.24           O  
HETATM 3747  O   HOH A7347     109.624  23.084  28.252  1.00 49.59           O  
HETATM 3748  O   HOH A7348      89.983  19.368  28.205  1.00 17.50           O  
HETATM 3749  O  AHOH A7349     102.173  12.715  28.978  0.70 41.34           O  
HETATM 3750  O  BHOH A7349     103.754  13.564  27.856  0.30 27.09           O  
HETATM 3751  O   HOH A7350      81.455   4.975  17.107  0.50 39.01           O  
HETATM 3752  O   HOH A7351      94.842  24.802  46.662  1.00 36.45           O  
HETATM 3753  O   HOH A7352      99.203  10.134  24.910  1.00 35.79           O  
HETATM 3754  O   HOH A7353      99.900  10.667   7.258  1.00 46.81           O  
HETATM 3755  O   HOH A7354      76.740  27.739  15.411  1.00 19.72           O  
HETATM 3756  O   HOH A7355      83.792  43.690  33.280  1.00 63.70           O  
HETATM 3757  O   HOH A7356      83.616  17.933   4.521  1.00 40.91           O  
HETATM 3758  O   HOH A7357      95.625   9.683  36.335  1.00 40.13           O  
HETATM 3759  O   HOH A7358      78.969  12.260  28.089  1.00 24.99           O  
HETATM 3760  O   HOH A7359     101.642  38.738  21.923  1.00 49.68           O  
HETATM 3761  O   HOH A7360      66.187  29.683  24.725  1.00 50.31           O  
HETATM 3762  O   HOH A7361      86.551  38.453  38.651  1.00 26.84           O  
HETATM 3763  O   HOH A7362      75.900  20.158  25.612  1.00 32.47           O  
HETATM 3764  O   HOH A7363      95.240   9.251  30.467  1.00 40.26           O  
HETATM 3765  O  AHOH A7364      99.604  42.713  28.684  0.60 24.51           O  
HETATM 3766  O  BHOH A7364      98.873  43.051  29.807  0.40 21.04           O  
HETATM 3767  O  AHOH A7365      83.911  28.106  37.728  0.60 22.58           O  
HETATM 3768  O  BHOH A7365      82.697  26.817  37.278  0.40 49.50           O  
HETATM 3769  O   HOH A7366      87.429   2.845  27.288  1.00 31.29           O  
HETATM 3770  O   HOH A7367      91.117  20.001  42.824  1.00 37.92           O  
HETATM 3771  O   HOH A7368     104.602  38.335  40.204  1.00 30.30           O  
HETATM 3772  O   HOH A7369      69.557  32.387  27.977  1.00 46.20           O  
HETATM 3773  O   HOH A7370      95.175  42.720  38.279  1.00 28.74           O  
HETATM 3774  O   HOH A7371      94.862  13.560  38.864  1.00 39.09           O  
HETATM 3775  O   HOH A7372     104.061  12.574  10.178  1.00 54.80           O  
HETATM 3776  O   HOH A7373      93.662  37.665  18.490  1.00 44.21           O  
HETATM 3777  O   HOH A7374      87.580   0.862  25.197  1.00 42.29           O  
HETATM 3778  O   HOH A7375      73.462  38.051  31.506  0.50 49.31           O  
HETATM 3779  O  BHOH A7376     100.272  20.235  42.043  0.50 43.42           O  
HETATM 3780  O   HOH A7377      85.370   0.725  20.300  1.00 56.00           O  
HETATM 3781  O   HOH A7378      84.983  35.329  12.993  1.00 41.12           O  
HETATM 3782  O  AHOH A7379      75.154  10.629  26.733  0.60 43.55           O  
HETATM 3783  O  BHOH A7379      73.276  10.307  26.853  0.40 41.78           O  
HETATM 3784  O   HOH A7380      74.424  39.274  26.047  1.00 34.03           O  
HETATM 3785  O   HOH A7381      73.683  38.369  28.381  1.00 62.73           O  
HETATM 3786  O   HOH A7382      71.776  18.966  29.151  1.00 57.78           O  
HETATM 3787  O   HOH A7383      87.439  12.153  24.413  1.00 20.36           O  
HETATM 3788  O   HOH A7384     102.749  29.435  41.937  1.00 45.85           O  
HETATM 3789  O   HOH A7385      69.159  11.958  23.431  1.00 56.93           O  
HETATM 3790  O   HOH A7386      69.409  23.799  20.214  1.00 24.09           O  
HETATM 3791  O  AHOH A7387      99.988  16.571  40.886  0.60 37.27           O  
HETATM 3792  O  BHOH A7387     100.505  15.416  39.285  0.40 39.73           O  
HETATM 3793  O  AHOH A7388      83.225  43.955  17.108  0.50 39.50           O  
HETATM 3794  O  BHOH A7388      81.399  44.817  16.401  0.50 45.85           O  
HETATM 3795  O   HOH A7389      87.803  -1.259  26.837  1.00 40.90           O  
HETATM 3796  O  AHOH A7390      77.108  17.132  29.291  0.70 31.20           O  
HETATM 3797  O  BHOH A7390      78.167  16.222  30.541  0.30 27.60           O  
HETATM 3798  O   HOH A7391      72.035  25.492  27.170  1.00 31.75           O  
HETATM 3799  O   HOH A7392      87.478  29.045   2.465  0.50 40.30           O  
HETATM 3800  O   HOH A7393      78.650  39.850  33.709  1.00 34.55           O  
HETATM 3801  O   HOH A7394      91.384  39.507  24.375  1.00 27.29           O  
HETATM 3802  O   HOH A7395      77.844  23.614  29.145  1.00 40.50           O  
HETATM 3803  O   HOH A7396      90.594  21.241   4.825  1.00 31.47           O  
HETATM 3804  O  AHOH A7397      94.182  18.327  43.432  0.70 27.37           O  
HETATM 3805  O   HOH A7398      91.397  41.223  30.997  1.00 33.55           O  
HETATM 3806  O   HOH A7399      75.030  23.017  25.871  1.00 22.78           O  
HETATM 3807  O   HOH A7400      84.486  25.469   2.804  1.00 37.00           O  
HETATM 3808  O   HOH A7401      84.153  42.313  29.650  1.00 31.24           O  
HETATM 3809  O   HOH A7402      78.301   4.890  26.778  1.00 41.76           O  
HETATM 3810  O   HOH A7403      70.125  23.203  26.510  0.50 41.63           O  
HETATM 3811  O   HOH A7404      84.079  31.862  41.571  1.00 42.52           O  
HETATM 3812  O   HOH A7405     111.744  32.928  24.637  1.00 60.58           O  
HETATM 3813  O   HOH A7406      99.049   9.797  34.637  0.50 40.60           O  
HETATM 3814  O  BHOH A7407      97.844  31.347   9.052  0.50 30.95           O  
HETATM 3815  O   HOH A7408      81.822   6.803  13.327  1.00 39.53           O  
HETATM 3816  O   HOH A7409      86.857  33.983   8.945  1.00 58.27           O  
HETATM 3817  O   HOH A7410      79.502  12.447   8.988  0.50 36.92           O  
HETATM 3818  O   HOH A7411      87.235  39.081  16.896  0.50 36.98           O  
HETATM 3819  O   HOH A7412      81.123  13.080  37.099  0.50 43.28           O  
HETATM 3820  O   HOH A7413      98.160  40.777  25.575  1.00 31.52           O  
HETATM 3821  O   HOH A7414      95.108   3.165  14.708  1.00 44.20           O  
HETATM 3822  O   HOH A7415     109.822  29.652  33.826  0.50 50.28           O  
HETATM 3823  O   HOH A7416      81.641   6.998  10.608  0.50 43.19           O  
HETATM 3824  O   HOH A7417      79.007  30.577  37.443  1.00 49.27           O  
HETATM 3825  O   HOH A7418      76.639  30.703  36.213  0.50 44.42           O  
HETATM 3826  O   HOH A7419     102.646   9.681  13.893  0.50 40.54           O  
HETATM 3827  O   HOH A7420      97.609   7.668  21.244  1.00 54.07           O  
HETATM 3828  O   HOH A7421     102.218  16.588   1.520  1.00 55.82           O  
HETATM 3829  O  AHOH A7422      84.959   3.336  19.108  0.50 28.94           O  
HETATM 3830  O  BHOH A7422      83.457   3.552  19.193  0.50 25.13           O  
HETATM 3831  O   HOH A7423      88.022  41.961  31.938  1.00 53.37           O  
HETATM 3832  O  AHOH A7424     105.387  19.253  29.429  0.70 36.36           O  
HETATM 3833  O  BHOH A7424     107.416  19.625  28.449  0.30 34.00           O  
HETATM 3834  O   HOH A7425     106.495  30.404  33.823  1.00 39.86           O  
HETATM 3835  O   HOH A7426      98.347   6.922  18.803  1.00 42.44           O  
HETATM 3836  O   HOH A7427      78.888  21.180  29.233  1.00 46.83           O  
HETATM 3837  O   HOH A7428      78.085  29.240   8.708  1.00 31.11           O  
HETATM 3838  O  AHOH A7429     100.823  21.014   0.284  0.60 31.47           O  
HETATM 3839  O  BHOH A7429      99.055  21.552  -0.337  0.40 35.21           O  
HETATM 3840  O   HOH A7430      80.175  12.715   6.646  0.50 53.91           O  
HETATM 3841  O  BHOH A7431      78.059   6.353  20.296  0.40 32.77           O  
HETATM 3842  O   HOH A7432      86.394  45.785  30.978  1.00 57.91           O  
HETATM 3843  O  AHOH A7433      94.821  35.069  42.492  0.60 28.68           O  
HETATM 3844  O  BHOH A7433      93.672  36.155  43.912  0.40 29.51           O  
HETATM 3845  O   HOH A7434      89.101  32.669   8.813  1.00 44.67           O  
HETATM 3846  O  AHOH A7435      72.969  43.557  27.198  0.60 43.99           O  
HETATM 3847  O  BHOH A7435      73.438  41.806  26.989  0.40 44.42           O  
HETATM 3848  O   HOH A7436     102.806  14.847  30.777  1.00 52.81           O  
HETATM 3849  O   HOH A7437      77.905  43.370  13.229  1.00 54.55           O  
HETATM 3850  O   HOH A7438      97.370  -1.704  21.968  1.00 64.39           O  
HETATM 3851  O   HOH A7439      78.331  11.340  25.551  1.00 25.56           O  
HETATM 3852  O   HOH A7440      81.714  10.799  32.059  1.00 55.35           O  
HETATM 3853  O   HOH A7441     113.355  27.536  26.064  0.50 37.39           O  
HETATM 3854  O   HOH A7442      72.738  23.146  27.208  1.00 64.05           O  
HETATM 3855  O   HOH A7443     107.326  31.691  31.461  1.00 54.99           O  
HETATM 3856  O   HOH A7444      86.938  24.348  38.890  1.00 24.86           O  
HETATM 3857  O   HOH A7445      91.310  38.697  18.589  1.00 57.50           O  
HETATM 3858  O   HOH A7446     102.022  17.815  35.413  0.50 33.73           O  
HETATM 3859  O   HOH A7447      99.714  39.512  20.242  0.50 49.65           O  
HETATM 3860  O   HOH A7448      82.158  35.214  13.127  1.00 33.06           O  
HETATM 3861  O  AHOH A7449      88.901  43.787  33.930  0.60 43.69           O  
HETATM 3862  O  BHOH A7449      87.267  43.954  34.454  0.40 32.24           O  
HETATM 3863  O   HOH A7450      81.774  42.908  34.786  1.00 51.27           O  
HETATM 3864  O   HOH A7451      96.235  37.846  19.253  0.50 47.66           O  
HETATM 3865  O   HOH A7452     107.332  14.558   8.428  1.00 53.88           O  
HETATM 3866  O   HOH A7453      90.313  16.156  42.472  1.00 51.51           O  
HETATM 3867  O   HOH A7454      74.553  41.360  13.246  0.50 34.19           O  
HETATM 3868  O   HOH A7455     106.323  16.551   1.109  0.50 42.84           O  
HETATM 3869  O  AHOH A7456      89.642  35.377   9.419  0.60 54.89           O  
HETATM 3870  O  BHOH A7456      89.536  37.135   6.724  0.40 47.60           O  
HETATM 3871  O   HOH A7457      86.715  36.382  10.939  0.50 49.57           O  
HETATM 3872  O  AHOH A7458      98.373  28.202  -0.891  0.50 47.16           O  
HETATM 3873  O  BHOH A7458      99.807  29.087   0.044  0.50 59.22           O  
HETATM 3874  O  AHOH A7459      75.738  19.345  28.202  0.70 35.89           O  
HETATM 3875  O  BHOH A7459      77.592  18.894  28.742  0.30 26.90           O  
HETATM 3876  O  AHOH A7460      96.025  18.796  50.346  0.50 38.46           O  
HETATM 3877  O  BHOH A7460      97.761  19.133  50.027  0.50 46.28           O  
HETATM 3878  O   HOH A7461      81.885  19.582   5.795  1.00 35.49           O  
HETATM 3879  O   HOH A7462      97.453  19.043   1.794  1.00 54.86           O  
HETATM 3880  O   HOH A7463     101.146  40.718  40.073  1.00 44.82           O  
HETATM 3881  O   HOH A7464     100.030  18.260   0.426  1.00 63.69           O  
HETATM 3882  O   HOH A7465      73.212  38.216  34.172  1.00 60.53           O  
HETATM 3883  O  AHOH A7466      83.514  28.638  42.811  0.60 48.00           O  
HETATM 3884  O  BHOH A7466      82.154  29.072  43.999  0.40 53.88           O  
HETATM 3885  O  AHOH A7467      78.968   6.164  17.898  0.60 40.23           O  
HETATM 3886  O  BHOH A7467      78.357   7.734  17.314  0.40 27.39           O  
HETATM 3887  O   HOH A7468     104.786   8.229  18.853  1.00 69.21           O  
HETATM 3888  O   HOH A7469      98.393   4.745   7.647  1.00 63.45           O  
HETATM 3889  O   HOH A7470      99.443   9.578  22.271  0.50 41.66           O  
HETATM 3890  O   HOH A7471     113.949  22.214  15.429  0.50 46.30           O  
HETATM 3891  O   HOH A7472     102.913  35.190  25.010  1.00 52.48           O  
HETATM 3892  O  AHOH A7473      94.372  28.405  47.442  0.50 38.90           O  
HETATM 3893  O  BHOH A7473      96.310  28.861  48.334  0.50 52.34           O  
HETATM 3894  O  AHOH A7474      79.329  44.618  16.886  0.50 48.36           O  
HETATM 3895  O  AHOH A7475      85.870  41.242  42.411  0.60 41.22           O  
HETATM 3896  O   HOH A7476     110.885  30.667  17.878  1.00 58.25           O  
HETATM 3897  O   HOH A7477     105.170  35.252  29.389  0.50 36.15           O  
HETATM 3898  O  AHOH A7478      94.330   2.365  27.818  0.60 39.73           O  
HETATM 3899  O  BHOH A7478      96.026   2.542  27.032  0.40 34.10           O  
HETATM 3900  O   HOH A7479     100.815   9.620  27.029  1.00 60.81           O  
HETATM 3901  O   HOH A7480      77.230  12.272  30.071  0.50 40.29           O  
HETATM 3902  O  BHOH A7481      94.862  33.568   9.036  0.50 38.64           O  
HETATM 3903  O  BHOH A7482      73.399  39.813  23.127  0.50 24.32           O  
HETATM 3904  O   HOH A7483      83.376  12.498  33.265  1.00 54.92           O  
HETATM 3905  O   HOH A7484      93.501  29.319  49.769  1.00 72.77           O  
HETATM 3906  O  AHOH A7485      90.528  37.378  44.829  0.50 44.71           O  
HETATM 3907  O  BHOH A7485      89.524  36.627  45.527  0.50 52.70           O  
HETATM 3908  O   HOH A7486      79.188  42.680  34.312  0.50 42.14           O  
HETATM 3909  O  AHOH A7487      80.533  28.382  37.107  0.50 47.77           O  
HETATM 3910  O  BHOH A7487      79.245  28.337  36.180  0.50 48.41           O  
HETATM 3911  O   HOH A7488      83.354  37.670  16.398  1.00 50.89           O  
HETATM 3912  O   HOH A7489      91.736   8.902  33.071  1.00 50.49           O  
HETATM 3913  O   HOH A7490      98.083   2.548   9.367  0.50 44.81           O  
HETATM 3914  O   HOH A7491      93.032  26.685  -6.246  1.00 35.05           O  
HETATM 3915  O   HOH A7492      81.004  17.383  31.787  1.00 46.86           O  
HETATM 3916  O   HOH A7493      98.122  39.728  23.065  1.00 50.29           O  
HETATM 3917  O   HOH A7494      74.709  40.977  10.904  0.50 44.19           O  
HETATM 3918  O   HOH A7495     106.354  13.947  10.857  1.00 59.16           O  
HETATM 3919  O   HOH A7496      81.563  13.562   3.964  0.50 52.96           O  
HETATM 3920  O   HOH A7497      80.172  40.584  15.734  1.00 44.40           O  
HETATM 3921  O   HOH A7498     103.112  37.311  44.410  1.00 74.95           O  
HETATM 3922  O   HOH A7499      69.154  25.595  26.000  1.00 64.78           O  
HETATM 3923  O   HOH A7500      82.456  39.301  12.213  0.50 38.94           O  
HETATM 3924  O   HOH A7501      97.478   8.075  29.013  1.00 57.90           O  
HETATM 3925  O  AHOH A7502      92.849  38.447  44.018  0.60 44.10           O  
HETATM 3926  O  BHOH A7502      94.574  38.574  44.670  0.40 40.18           O  
HETATM 3927  O   HOH A7503      78.590  32.346   5.704  1.00 48.53           O  
HETATM 3928  O   HOH A7504      84.896  29.869  40.100  1.00 52.30           O  
HETATM 3929  O   HOH A7505      97.926   3.231  15.760  1.00 50.63           O  
HETATM 3930  O  AHOH A7506      82.768  31.508  43.842  0.50 53.41           O  
HETATM 3931  O  BHOH A7506      82.565  33.487  43.692  0.50 45.01           O  
HETATM 3932  O   HOH A7507      80.855   2.141  20.352  1.00 55.62           O  
HETATM 3933  O   HOH A7508     109.306  33.827  13.894  0.50 47.80           O  
HETATM 3934  O   HOH A7509      86.242   8.762  36.170  0.50 54.20           O  
HETATM 3935  O   HOH A7510     107.571  16.843  16.673  0.50 39.57           O  
HETATM 3936  O   HOH A7511      80.319  20.168  32.466  1.00 53.99           O  
HETATM 3937  O   HOH A7512      92.380  13.578  37.961  0.50 54.67           O  
HETATM 3938  O   HOH A7513      94.751   7.943  33.937  0.50 45.70           O  
HETATM 3939  O   HOH A7514      97.343   1.118  17.934  0.50 35.62           O  
HETATM 3940  O   HOH A7515     100.285  29.746   3.170  1.00 54.46           O  
HETATM 3941  O   HOH A7516      74.629  38.485   8.572  0.50 39.15           O  
HETATM 3942  O   HOH A7517      96.050  38.334  23.295  1.00 32.82           O  
HETATM 3943  O   HOH A7518      85.848   1.633  15.995  1.00 47.57           O  
HETATM 3944  O   HOH A7519     107.030  38.333  41.620  0.50 42.28           O  
HETATM 3945  O   HOH A7520      88.373   9.520  34.620  0.50 52.52           O  
HETATM 3946  O   HOH A7521      93.241  12.010   4.031  0.50 43.22           O  
HETATM 3947  O   HOH A7522      84.193   2.749  14.202  0.50 36.71           O  
HETATM 3948  O  AHOH A7523      68.483  10.768  25.720  0.50 47.52           O  
HETATM 3949  O  BHOH A7523      68.609  12.059  26.583  0.50 61.87           O  
HETATM 3950  O   HOH A7524      73.029  41.128  29.210  0.50 40.06           O  
HETATM 3951  O   HOH A7525      89.360   2.290  29.234  1.00 41.00           O  
HETATM 3952  O   HOH A7526      79.870  21.195  35.136  1.00 53.10           O  
HETATM 3953  O   HOH A7527     100.938  37.420  11.734  0.50 48.52           O  
HETATM 3954  O   HOH A7528     108.065  35.816  31.278  1.00 45.98           O  
HETATM 3955  O   HOH A7529      95.407  41.840  25.901  1.00 48.00           O  
HETATM 3956  O   HOH A7530      98.718   7.498  23.742  0.50 39.56           O  
HETATM 3957  O   HOH A7531      75.173  23.467  29.034  1.00 60.53           O  
HETATM 3958  O   HOH A7532      74.976  39.737  33.001  1.00 58.07           O  
HETATM 3959  O   HOH A7533      87.021  -1.132  29.413  0.50 35.90           O  
HETATM 3960  O   HOH A7534      83.690   2.606  11.564  0.50 48.68           O  
HETATM 3961  O   HOH A7535      81.908   8.871  34.138  0.50 46.63           O  
HETATM 3962  O   HOH A7536     108.158  15.092  35.042  0.50 48.32           O  
HETATM 3963  O   HOH A7537      99.585   1.858  14.151  0.50 54.39           O  
HETATM 3964  O   HOH B4501      74.885  12.196   5.602  1.00 42.59           O  
HETATM 3965  O   HOH B4502      79.807  27.508   7.509  1.00 38.59           O  
HETATM 3966  O   HOH B4503      78.985  19.067   5.938  1.00 32.81           O  
HETATM 3967  O   HOH B4504      52.550  15.650  20.110  0.50 38.12           O  
HETATM 3968  O   HOH B4505      66.150  24.847  19.866  1.00 38.22           O  
HETATM 3969  O   HOH B4506      52.837   2.565  16.681  1.00 60.78           O  
HETATM 3970  O   HOH B4507      67.410  29.807  -2.757  0.50 39.36           O  
HETATM 3971  O   HOH B4508      72.434  25.345  -0.673  1.00 52.27           O  
HETATM 3972  O  AHOH B4509      56.761  25.083  -1.525  0.60 39.48           O  
HETATM 3973  O  BHOH B4509      55.788  25.885  -0.605  0.40 44.37           O  
HETATM 3974  O   HOH B4510      72.000  14.323   2.297  0.50 36.22           O  
HETATM 3975  O   HOH B4511      57.351  17.676   2.339  1.00 42.48           O  
HETATM 3976  O   HOH B4512      68.386  19.799   0.072  1.00 34.81           O  
HETATM 3977  O   HOH B4513      74.078  30.753   1.157  1.00 50.00           O  
HETATM 3978  O   HOH B4514      69.814  10.298  21.199  1.00 33.54           O  
HETATM 3979  O   HOH B4515      67.233  25.473  -5.601  0.50 37.40           O  
HETATM 3980  O   HOH B4516      61.726  32.611  11.051  1.00 48.38           O  
HETATM 3981  O   HOH B4517      71.331   0.205  19.337  1.00 41.54           O  
HETATM 3982  O   HOH B4518      54.264   4.944  19.735  0.50 41.48           O  
HETATM 3983  O   HOH B4519      62.348   1.490  11.663  1.00 52.40           O  
HETATM 3984  O   HOH B4520      72.932   6.108  16.330  1.00 40.80           O  
HETATM 3985  O   HOH B4521      56.024  21.046  14.682  0.50 39.64           O  
HETATM 3986  O   HOH B4522      76.580  28.560   6.452  1.00 35.71           O  
HETATM 3987  O   HOH B4523      76.950   9.285  15.314  1.00 43.96           O  
HETATM 3988  O   HOH B4524      71.810  25.020  20.014  1.00 21.54           O  
HETATM 3989  O   HOH B4525      61.226  25.998   4.548  1.00 45.02           O  
HETATM 3990  O   HOH B4526      67.358  -3.708  12.093  0.50 47.23           O  
HETATM 3991  O   HOH B4527      53.175  23.366   8.835  0.50 45.10           O  
HETATM 3992  O   HOH B4528      70.273   2.527   0.505  1.00 85.98           O  
HETATM 3993  O   HOH B4529      56.185  22.227  -2.981  0.50 37.80           O  
HETATM 3994  O   HOH B4530      55.257  17.572  16.773  1.00 47.25           O  
HETATM 3995  O   HOH B4531      76.545  29.393   2.221  1.00 56.74           O  
HETATM 3996  O   HOH B4532      71.972  38.115   8.964  1.00 46.47           O  
HETATM 3997  O  AHOH B4533      72.917  35.996  12.320  0.60 33.04           O  
HETATM 3998  O  BHOH B4533      73.684  35.095  13.737  0.40 24.90           O  
HETATM 3999  O   HOH B4534      80.620   9.946  13.343  1.00 28.34           O  
HETATM 4000  O   HOH B4535      58.343  25.270 -12.090  0.50 51.65           O  
HETATM 4001  O   HOH B4536      64.751  31.740  17.108  1.00 36.83           O  
HETATM 4002  O   HOH B4537      59.582  18.271  23.621  0.50 34.40           O  
HETATM 4003  O  AHOH B4538      64.123  26.671  18.677  0.60 34.22           O  
HETATM 4004  O  BHOH B4538      63.420  28.260  19.919  0.40 39.97           O  
HETATM 4005  O   HOH B4539      71.800  32.661   0.135  0.50 33.30           O  
HETATM 4006  O   HOH B4540      58.975   8.562   7.329  0.50 46.31           O  
HETATM 4007  O   HOH B4541      67.633   1.398  20.396  1.00 45.56           O  
HETATM 4008  O   HOH B4542      68.394  30.702  15.963  1.00 31.54           O  
HETATM 4009  O  BHOH B4543      79.844  23.106   7.059  0.40 24.65           O  
HETATM 4010  O   HOH B4544      76.795  18.549  10.425  1.00 36.96           O  
HETATM 4011  O   HOH B4545      69.282  28.307  13.092  1.00 24.86           O  
HETATM 4012  O   HOH B4546      56.230  16.500  13.518  1.00 49.30           O  
HETATM 4013  O   HOH B4547      63.088  24.096   1.729  1.00 39.42           O  
HETATM 4014  O   HOH B4548      62.326  16.625  17.347  1.00 29.93           O  
HETATM 4015  O   HOH B4549      64.471  11.776  11.181  1.00 39.71           O  
HETATM 4016  O   HOH B4550      70.548  30.931  14.453  1.00 25.54           O  
HETATM 4017  O   HOH B4551      52.218  12.516  14.014  1.00 56.30           O  
HETATM 4018  O   HOH B4552      71.748  30.807   7.406  1.00 28.38           O  
HETATM 4019  O   HOH B4553      71.924   4.312  14.326  1.00 45.92           O  
HETATM 4020  O  AHOH B4554      65.177  30.545   0.345  0.50 32.32           O  
HETATM 4021  O  BHOH B4554      65.824  32.908   0.184  0.50 37.66           O  
HETATM 4022  O   HOH B4555      75.828  24.862   1.899  1.00 46.34           O  
HETATM 4023  O   HOH B4556      56.419  21.078  21.024  1.00 53.33           O  
HETATM 4024  O   HOH B4557      73.909  30.521   5.746  1.00 33.06           O  
HETATM 4025  O   HOH B4558      60.963   3.475  10.599  1.00 47.97           O  
HETATM 4026  O   HOH B4559      67.792  34.008   2.321  1.00 45.79           O  
HETATM 4027  O   HOH B4560      55.226  18.997   8.394  1.00 50.16           O  
HETATM 4028  O   HOH B4561      70.636  20.900  -1.062  1.00 47.32           O  
HETATM 4029  O   HOH B4562      63.330  13.344   1.163  1.00 55.75           O  
HETATM 4030  O   HOH B4563      67.823  25.053  23.840  1.00 66.43           O  
HETATM 4031  O   HOH B4564      72.178   2.191   9.977  1.00 50.82           O  
HETATM 4032  O   HOH B4565      58.479  29.384   9.369  1.00 42.90           O  
HETATM 4033  O   HOH B4566      75.261  31.378   8.169  1.00 30.81           O  
HETATM 4034  O   HOH B4567      65.952  35.050   3.865  1.00 44.74           O  
HETATM 4035  O   HOH B4568      61.830  25.438  -6.098  0.50 39.02           O  
HETATM 4036  O   HOH B4569      52.574  23.191   3.246  1.00 72.81           O  
HETATM 4037  O   HOH B4570      64.110  13.509  23.606  1.00 49.65           O  
HETATM 4038  O   HOH B4571      57.592  19.545  13.086  1.00 43.26           O  
HETATM 4039  O  AHOH B4572      60.904  29.795   3.299  0.60 45.93           O  
HETATM 4040  O  BHOH B4572      61.826  28.443   2.695  0.40 33.69           O  
HETATM 4041  O   HOH B4573      64.462  36.181  10.300  1.00 60.91           O  
HETATM 4042  O   HOH B4574      75.042  22.178   0.300  1.00 41.75           O  
HETATM 4043  O   HOH B4575      63.715  13.481   4.735  1.00 65.21           O  
HETATM 4044  O   HOH B4576      53.656  11.269   7.822  1.00 64.23           O  
HETATM 4045  O   HOH B4577      60.573  12.425  23.256  1.00 42.69           O  
HETATM 4046  O   HOH B4578      73.803  18.181   0.855  0.50 41.90           O  
HETATM 4047  O   HOH B4579      64.051  25.573  21.632  1.00 50.47           O  
HETATM 4048  O   HOH B4580      78.961  14.608   5.180  1.00 66.99           O  
HETATM 4049  O  AHOH B4581      74.489  37.861   5.958  0.60 45.61           O  
HETATM 4050  O  BHOH B4581      76.311  36.649   4.926  0.40 35.80           O  
HETATM 4051  O   HOH B4582      60.959  14.988  -5.572  0.50 53.09           O  
HETATM 4052  O   HOH B4583      73.040   3.106  12.275  1.00 74.04           O  
HETATM 4053  O   HOH B4584      61.689  25.130  -8.767  0.50 42.46           O  
HETATM 4054  O   HOH B4585      68.800  36.442   1.728  1.00 55.57           O  
HETATM 4055  O   HOH B4586      79.063  17.227   3.803  1.00 52.26           O  
HETATM 4056  O  AHOH B4587      65.684   9.769  21.637  0.60 56.09           O  
HETATM 4057  O  BHOH B4587      64.927  10.939  22.831  0.40 39.78           O  
HETATM 4058  O   HOH B4588      69.329  32.732  -1.670  1.00 71.69           O  
HETATM 4059  O   HOH B4589      65.222  12.104   6.552  0.50 42.71           O  
HETATM 4060  O   HOH B4590      74.896  31.738   3.553  1.00 59.95           O  
HETATM 4061  O   HOH B4591      65.572  13.189   2.613  1.00 65.57           O  
HETATM 4062  O   HOH B4592      80.574  28.153   4.732  1.00 44.38           O  
HETATM 4063  O   HOH B4593      68.925  17.163  -0.531  1.00 55.47           O  
HETATM 4064  O   HOH B4594      77.593  30.027   4.502  1.00 57.19           O  
HETATM 4065  O   HOH B4595      74.659   7.691  14.000  0.50 39.34           O  
HETATM 4066  O   HOH B4596      54.084  19.612  21.054  0.50 46.64           O  
HETATM 4067  O   HOH B4597      67.869   9.755   7.993  1.00 54.17           O  
HETATM 4068  O   HOH B4598      55.832  18.793  11.143  0.50 49.62           O  
HETATM 4069  O   HOH B4599      65.214  10.574   8.755  1.00 62.18           O  
HETATM 4070  O   HOH B4600      52.687  20.568   2.885  1.00 69.69           O  
HETATM 4071  O   HOH B4601      67.930  14.476   0.504  0.50 42.53           O  
HETATM 4072  O   HOH B4602      64.824  25.457  24.211  0.50 45.15           O  
HETATM 4073  O   HOH B4603      52.231  11.907  10.054  1.00 60.51           O  
HETATM 4074  O   HOH B4604      63.772   9.434   6.772  0.50 53.65           O  
HETATM 4075  O   HOH B4605      77.236  22.356  -1.544  0.50 37.68           O  
CONECT 3056 3576                                                                
CONECT 3082 3576                                                                
CONECT 3135 3576                                                                
CONECT 3187 3576                                                                
CONECT 3405 3577                                                                
CONECT 3425 3577                                                                
CONECT 3486 3577                                                                
CONECT 3498 3577                                                                
CONECT 3525 3526 3527 3528                                                      
CONECT 3526 3525                                                                
CONECT 3527 3525                                                                
CONECT 3528 3525                                                                
CONECT 3529 3530                                                                
CONECT 3530 3529 3531 3534                                                      
CONECT 3531 3530 3532 3533                                                      
CONECT 3532 3531                                                                
CONECT 3533 3531                                                                
CONECT 3534 3530 3535                                                           
CONECT 3535 3534 3536                                                           
CONECT 3536 3535 3537 3538                                                      
CONECT 3537 3536                                                                
CONECT 3538 3536 3539                                                           
CONECT 3539 3538 3540 3541                                                      
CONECT 3540 3539 3545                                                           
CONECT 3541 3539 3542 3543                                                      
CONECT 3542 3541                                                                
CONECT 3543 3541 3544 3545                                                      
CONECT 3544 3543                                                                
CONECT 3545 3540 3543 3546                                                      
CONECT 3546 3545 3547 3555                                                      
CONECT 3547 3546 3548                                                           
CONECT 3548 3547 3549                                                           
CONECT 3549 3548 3550 3555                                                      
CONECT 3550 3549 3551 3552                                                      
CONECT 3551 3550                                                                
CONECT 3552 3550 3553                                                           
CONECT 3553 3552 3554                                                           
CONECT 3554 3553 3555                                                           
CONECT 3555 3546 3549 3554                                                      
CONECT 3556 3557 3558 3559                                                      
CONECT 3557 3556                                                                
CONECT 3558 3556                                                                
CONECT 3559 3556                                                                
CONECT 3560 3561 3562 3563                                                      
CONECT 3561 3560                                                                
CONECT 3562 3560                                                                
CONECT 3563 3560                                                                
CONECT 3564 3565 3570                                                           
CONECT 3565 3564 3566 3571 3575                                                 
CONECT 3566 3565 3567 3572                                                      
CONECT 3567 3566 3568 3573                                                      
CONECT 3568 3567 3569 3574                                                      
CONECT 3569 3568 3575                                                           
CONECT 3570 3564                                                                
CONECT 3571 3565                                                                
CONECT 3572 3566                                                                
CONECT 3573 3567                                                                
CONECT 3574 3568                                                                
CONECT 3575 3565 3569                                                           
CONECT 3576 3056 3082 3135 3187                                                 
CONECT 3577 3405 3425 3486 3498                                                 
CONECT 3578 3579 3584                                                           
CONECT 3579 3578 3580 3585 3589                                                 
CONECT 3580 3579 3581 3586                                                      
CONECT 3581 3580 3582 3587                                                      
CONECT 3582 3581 3583 3588                                                      
CONECT 3583 3582 3589                                                           
CONECT 3584 3578                                                                
CONECT 3585 3579                                                                
CONECT 3586 3580                                                                
CONECT 3587 3581                                                                
CONECT 3588 3582                                                                
CONECT 3589 3579 3583                                                           
MASTER      499    0    8   18   17    0    0    6 3708    2   73   35          
END                                                                             
HEADER    HYDROLASE                               22-MAR-20   6W9C              
TITLE     THE CRYSTAL STRUCTURE OF PAPAIN-LIKE PROTEASE OF SARS COV-2           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PAPAIN-LIKE PROTEINASE;                                    
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 EC: 3.4.19.12,3.4.22.-,3.4.22.69;                                    
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: TWO C-TERMINAL ALANINE RESIDUES ARE CLONING ARTIFACTS 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PCPD                                      
KEYWDS    COVID-19, CORONAVIRUS, SARS, COV-2 IN PAPAIN-LIKE PROTEASE, IDP51000, 
KEYWDS   2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID,        
KEYWDS   3 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.OSIPIUK,R.JEDRZEJCZAK,C.TESAR,M.ENDRES,L.STOLS,G.BABNIGG,Y.KIM,     
AUTHOR   2 K.MICHALSKA,A.JOACHIMIAK,CENTER FOR STRUCTURAL GENOMICS OF           
AUTHOR   3 INFECTIOUS DISEASES (CSGID)                                          
REVDAT   3   21-OCT-20 6W9C    1       COMPND REMARK HET    HETNAM              
REVDAT   3 2                   1       FORMUL HELIX  SHEET  SSBOND              
REVDAT   3 3                   1       LINK   SITE   ATOM                       
REVDAT   2   06-MAY-20 6W9C    1       COMPND SOURCE REMARK DBREF               
REVDAT   2 2                   1       SEQADV LINK   SITE   ATOM                
REVDAT   1   01-APR-20 6W9C    0                                                
JRNL        AUTH   J.OSIPIUK,R.JEDRZEJCZAK,C.TESAR,M.ENDRES,L.STOLS,G.BABNIGG,  
JRNL        AUTH 2 Y.KIM,K.MICHALSKA,A.JOACHIMIAK,                              
JRNL        AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES        
JRNL        AUTH 4 (CSGID)                                                      
JRNL        TITL   THE CRYSTAL STRUCTURE OF PAPAIN-LIKE PROTEASE OF SARS COV-2  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0267                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 57.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 19766                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.237                           
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1031                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 977                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 37.54                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 38                           
REMARK   3   BIN FREE R VALUE                    : 0.3600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7364                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.41000                                              
REMARK   3    B22 (A**2) : -4.62000                                             
REMARK   3    B33 (A**2) : 4.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.51000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.564         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.376         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 44.817        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.915                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.872                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7542 ; 0.005 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  6949 ; 0.003 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10230 ; 1.355 ; 1.657       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16046 ; 1.102 ; 1.577       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   920 ; 6.404 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   361 ;38.653 ;23.961       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1277 ;18.705 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;16.343 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1000 ; 0.047 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8540 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1728 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 3                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     3    314       B     3    314    9507 0.080 0.050     
REMARK   3    2     A     4    313       C     4    313    9552 0.070 0.050     
REMARK   3    3     B     4    314       C     4    314    9489 0.070 0.050     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A   315                          
REMARK   3    RESIDUE RANGE :   A   501        A   502                          
REMARK   3    RESIDUE RANGE :   C   401        C   401                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -32.691   34.022   25.550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0204 T22:   0.1819                                     
REMARK   3      T33:   0.4567 T12:   0.0283                                     
REMARK   3      T13:  -0.0255 T23:   0.0369                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3745 L22:   0.9975                                     
REMARK   3      L33:   1.7492 L12:   0.0556                                     
REMARK   3      L13:   0.7977 L23:  -0.0994                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0569 S12:   0.0329 S13:  -0.0006                       
REMARK   3      S21:  -0.0824 S22:  -0.0930 S23:  -0.0715                       
REMARK   3      S31:   0.1381 S32:   0.1077 S33:   0.0361                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     3        B   314                          
REMARK   3    RESIDUE RANGE :   B   501        B   502                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -18.183    0.776   25.442              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0180 T22:   0.2265                                     
REMARK   3      T33:   0.5016 T12:  -0.0028                                     
REMARK   3      T13:  -0.0274 T23:   0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4564 L22:   0.6883                                     
REMARK   3      L33:   1.2651 L12:  -0.1537                                     
REMARK   3      L13:  -0.3195 L23:  -0.0357                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0537 S12:   0.0792 S13:  -0.0929                       
REMARK   3      S21:   0.0150 S22:  -0.0828 S23:   0.0533                       
REMARK   3      S31:  -0.0623 S32:  -0.0460 S33:   0.1365                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     4        C   314                          
REMARK   3    RESIDUE RANGE :   C   402        C   403                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -54.631    4.716   25.466              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0411 T22:   0.1424                                     
REMARK   3      T33:   0.5248 T12:  -0.0068                                     
REMARK   3      T13:  -0.0826 T23:  -0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6072 L22:   0.3872                                     
REMARK   3      L33:   1.0308 L12:  -0.0922                                     
REMARK   3      L13:  -0.1709 L23:   0.6203                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0112 S12:  -0.0237 S13:   0.1203                       
REMARK   3      S21:  -0.0282 S22:  -0.0129 S23:   0.0820                       
REMARK   3      S31:  -0.0124 S32:   0.0017 S33:   0.0240                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 6W9C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000247849.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-MAR-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 X 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20799                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.680                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 57.3                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 38.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5Y3Q                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THIN PLATES                                                  
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM ACETATE, 10% PEG 8000,   
REMARK 280  PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       95.39300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.14000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       95.39300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       55.14000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -204.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     THR A   225                                                      
REMARK 465     CYS A   226                                                      
REMARK 465     GLY A   227                                                      
REMARK 465     ALA A   316                                                      
REMARK 465     ALA A   317                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     CYS B   224                                                      
REMARK 465     THR B   225                                                      
REMARK 465     CYS B   226                                                      
REMARK 465     GLY B   227                                                      
REMARK 465     LYS B   228                                                      
REMARK 465     LYS B   315                                                      
REMARK 465     ALA B   316                                                      
REMARK 465     ALA B   317                                                      
REMARK 465     GLU C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     THR C   225                                                      
REMARK 465     CYS C   226                                                      
REMARK 465     LYS C   315                                                      
REMARK 465     ALA C   316                                                      
REMARK 465     ALA C   317                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU B   263     OH   TYR B   296              2.11            
REMARK 500   OE2  GLU C   263     OH   TYR C   296              2.13            
REMARK 500   OE2  GLU A   263     OH   TYR A   296              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A  14      -52.21   -126.76                                   
REMARK 500    GLU A  51      117.59    -39.80                                   
REMARK 500    PRO A  59      100.64    -47.41                                   
REMARK 500    ASP A  76      108.31    -56.06                                   
REMARK 500    TYR A  95       75.70   -117.98                                   
REMARK 500    SER A 103     -162.94   -100.67                                   
REMARK 500    LYS A 218      -72.76    -75.04                                   
REMARK 500    VAL A 235      -61.50    -92.99                                   
REMARK 500    THR A 259      -75.11    -82.24                                   
REMARK 500    TYR A 268      -97.75   -117.68                                   
REMARK 500    LYS A 279     -135.00   -129.30                                   
REMARK 500    ASP A 286       71.97   -113.92                                   
REMARK 500    THR A 313       55.40   -101.20                                   
REMARK 500    ILE B  14      -50.95   -126.30                                   
REMARK 500    PRO B  59      101.45    -48.03                                   
REMARK 500    ASP B  76      107.66    -53.91                                   
REMARK 500    TYR B  95       76.85   -117.49                                   
REMARK 500    SER B 103     -163.10   -100.86                                   
REMARK 500    ALA B 107      129.65   -170.20                                   
REMARK 500    LYS B 218      -72.91    -75.47                                   
REMARK 500    VAL B 235      -61.78    -92.15                                   
REMARK 500    THR B 259      -74.65    -81.73                                   
REMARK 500    TYR B 268      -95.45   -116.01                                   
REMARK 500    LYS B 279     -134.88   -130.21                                   
REMARK 500    ASP B 286       72.12   -112.79                                   
REMARK 500    THR B 313       51.02   -100.28                                   
REMARK 500    ILE C  14      -51.15   -126.16                                   
REMARK 500    GLU C  51      117.25    -39.86                                   
REMARK 500    PRO C  59      100.45    -47.14                                   
REMARK 500    ASP C  76      108.28    -54.52                                   
REMARK 500    TYR C  95       76.19   -117.90                                   
REMARK 500    SER C 103     -163.32   -100.48                                   
REMARK 500    ALA C 107      129.78   -170.88                                   
REMARK 500    LYS C 218      -72.62    -74.58                                   
REMARK 500    VAL C 235      -60.72    -93.26                                   
REMARK 500    THR C 259      -74.38    -82.63                                   
REMARK 500    ASN C 267      -50.77   -124.08                                   
REMARK 500    TYR C 268      -93.43   -116.84                                   
REMARK 500    LYS C 279     -134.76   -130.23                                   
REMARK 500    ASP C 286       72.50   -115.06                                   
REMARK 500    THR C 313       56.32   -101.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 189   SG                                                     
REMARK 620 2 CYS A 192   SG  112.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 270   SG                                                     
REMARK 620 2 CYS B 270   SG   73.9                                              
REMARK 620 3 CYS C 270   SG   78.1  84.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 189   SG                                                     
REMARK 620 2 CYS B 192   SG  103.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 189   SG                                                     
REMARK 620 2 CYS C 192   SG  127.2                                              
REMARK 620 3 CYS C 224   SG  139.4  66.9                                        
REMARK 620 N                    1     2                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: IDP51000   RELATED DB: TARGETTRACK                       
DBREF  6W9C A    1   315  UNP    P0DTC1   R1A_SARS2     1564   1878             
DBREF  6W9C B    1   315  UNP    P0DTC1   R1A_SARS2     1564   1878             
DBREF  6W9C C    1   315  UNP    P0DTC1   R1A_SARS2     1564   1878             
SEQADV 6W9C ALA A  316  UNP  P0DTC1              EXPRESSION TAG                 
SEQADV 6W9C ALA A  317  UNP  P0DTC1              EXPRESSION TAG                 
SEQADV 6W9C ALA B  316  UNP  P0DTC1              EXPRESSION TAG                 
SEQADV 6W9C ALA B  317  UNP  P0DTC1              EXPRESSION TAG                 
SEQADV 6W9C ALA C  316  UNP  P0DTC1              EXPRESSION TAG                 
SEQADV 6W9C ALA C  317  UNP  P0DTC1              EXPRESSION TAG                 
SEQRES   1 A  317  GLU VAL ARG THR ILE LYS VAL PHE THR THR VAL ASP ASN          
SEQRES   2 A  317  ILE ASN LEU HIS THR GLN VAL VAL ASP MET SER MET THR          
SEQRES   3 A  317  TYR GLY GLN GLN PHE GLY PRO THR TYR LEU ASP GLY ALA          
SEQRES   4 A  317  ASP VAL THR LYS ILE LYS PRO HIS ASN SER HIS GLU GLY          
SEQRES   5 A  317  LYS THR PHE TYR VAL LEU PRO ASN ASP ASP THR LEU ARG          
SEQRES   6 A  317  VAL GLU ALA PHE GLU TYR TYR HIS THR THR ASP PRO SER          
SEQRES   7 A  317  PHE LEU GLY ARG TYR MET SER ALA LEU ASN HIS THR LYS          
SEQRES   8 A  317  LYS TRP LYS TYR PRO GLN VAL ASN GLY LEU THR SER ILE          
SEQRES   9 A  317  LYS TRP ALA ASP ASN ASN CYS TYR LEU ALA THR ALA LEU          
SEQRES  10 A  317  LEU THR LEU GLN GLN ILE GLU LEU LYS PHE ASN PRO PRO          
SEQRES  11 A  317  ALA LEU GLN ASP ALA TYR TYR ARG ALA ARG ALA GLY GLU          
SEQRES  12 A  317  ALA ALA ASN PHE CYS ALA LEU ILE LEU ALA TYR CYS ASN          
SEQRES  13 A  317  LYS THR VAL GLY GLU LEU GLY ASP VAL ARG GLU THR MET          
SEQRES  14 A  317  SER TYR LEU PHE GLN HIS ALA ASN LEU ASP SER CYS LYS          
SEQRES  15 A  317  ARG VAL LEU ASN VAL VAL CYS LYS THR CYS GLY GLN GLN          
SEQRES  16 A  317  GLN THR THR LEU LYS GLY VAL GLU ALA VAL MET TYR MET          
SEQRES  17 A  317  GLY THR LEU SER TYR GLU GLN PHE LYS LYS GLY VAL GLN          
SEQRES  18 A  317  ILE PRO CYS THR CYS GLY LYS GLN ALA THR LYS TYR LEU          
SEQRES  19 A  317  VAL GLN GLN GLU SER PRO PHE VAL MET MET SER ALA PRO          
SEQRES  20 A  317  PRO ALA GLN TYR GLU LEU LYS HIS GLY THR PHE THR CYS          
SEQRES  21 A  317  ALA SER GLU TYR THR GLY ASN TYR GLN CYS GLY HIS TYR          
SEQRES  22 A  317  LYS HIS ILE THR SER LYS GLU THR LEU TYR CYS ILE ASP          
SEQRES  23 A  317  GLY ALA LEU LEU THR LYS SER SER GLU TYR LYS GLY PRO          
SEQRES  24 A  317  ILE THR ASP VAL PHE TYR LYS GLU ASN SER TYR THR THR          
SEQRES  25 A  317  THR ILE LYS ALA ALA                                          
SEQRES   1 B  317  GLU VAL ARG THR ILE LYS VAL PHE THR THR VAL ASP ASN          
SEQRES   2 B  317  ILE ASN LEU HIS THR GLN VAL VAL ASP MET SER MET THR          
SEQRES   3 B  317  TYR GLY GLN GLN PHE GLY PRO THR TYR LEU ASP GLY ALA          
SEQRES   4 B  317  ASP VAL THR LYS ILE LYS PRO HIS ASN SER HIS GLU GLY          
SEQRES   5 B  317  LYS THR PHE TYR VAL LEU PRO ASN ASP ASP THR LEU ARG          
SEQRES   6 B  317  VAL GLU ALA PHE GLU TYR TYR HIS THR THR ASP PRO SER          
SEQRES   7 B  317  PHE LEU GLY ARG TYR MET SER ALA LEU ASN HIS THR LYS          
SEQRES   8 B  317  LYS TRP LYS TYR PRO GLN VAL ASN GLY LEU THR SER ILE          
SEQRES   9 B  317  LYS TRP ALA ASP ASN ASN CYS TYR LEU ALA THR ALA LEU          
SEQRES  10 B  317  LEU THR LEU GLN GLN ILE GLU LEU LYS PHE ASN PRO PRO          
SEQRES  11 B  317  ALA LEU GLN ASP ALA TYR TYR ARG ALA ARG ALA GLY GLU          
SEQRES  12 B  317  ALA ALA ASN PHE CYS ALA LEU ILE LEU ALA TYR CYS ASN          
SEQRES  13 B  317  LYS THR VAL GLY GLU LEU GLY ASP VAL ARG GLU THR MET          
SEQRES  14 B  317  SER TYR LEU PHE GLN HIS ALA ASN LEU ASP SER CYS LYS          
SEQRES  15 B  317  ARG VAL LEU ASN VAL VAL CYS LYS THR CYS GLY GLN GLN          
SEQRES  16 B  317  GLN THR THR LEU LYS GLY VAL GLU ALA VAL MET TYR MET          
SEQRES  17 B  317  GLY THR LEU SER TYR GLU GLN PHE LYS LYS GLY VAL GLN          
SEQRES  18 B  317  ILE PRO CYS THR CYS GLY LYS GLN ALA THR LYS TYR LEU          
SEQRES  19 B  317  VAL GLN GLN GLU SER PRO PHE VAL MET MET SER ALA PRO          
SEQRES  20 B  317  PRO ALA GLN TYR GLU LEU LYS HIS GLY THR PHE THR CYS          
SEQRES  21 B  317  ALA SER GLU TYR THR GLY ASN TYR GLN CYS GLY HIS TYR          
SEQRES  22 B  317  LYS HIS ILE THR SER LYS GLU THR LEU TYR CYS ILE ASP          
SEQRES  23 B  317  GLY ALA LEU LEU THR LYS SER SER GLU TYR LYS GLY PRO          
SEQRES  24 B  317  ILE THR ASP VAL PHE TYR LYS GLU ASN SER TYR THR THR          
SEQRES  25 B  317  THR ILE LYS ALA ALA                                          
SEQRES   1 C  317  GLU VAL ARG THR ILE LYS VAL PHE THR THR VAL ASP ASN          
SEQRES   2 C  317  ILE ASN LEU HIS THR GLN VAL VAL ASP MET SER MET THR          
SEQRES   3 C  317  TYR GLY GLN GLN PHE GLY PRO THR TYR LEU ASP GLY ALA          
SEQRES   4 C  317  ASP VAL THR LYS ILE LYS PRO HIS ASN SER HIS GLU GLY          
SEQRES   5 C  317  LYS THR PHE TYR VAL LEU PRO ASN ASP ASP THR LEU ARG          
SEQRES   6 C  317  VAL GLU ALA PHE GLU TYR TYR HIS THR THR ASP PRO SER          
SEQRES   7 C  317  PHE LEU GLY ARG TYR MET SER ALA LEU ASN HIS THR LYS          
SEQRES   8 C  317  LYS TRP LYS TYR PRO GLN VAL ASN GLY LEU THR SER ILE          
SEQRES   9 C  317  LYS TRP ALA ASP ASN ASN CYS TYR LEU ALA THR ALA LEU          
SEQRES  10 C  317  LEU THR LEU GLN GLN ILE GLU LEU LYS PHE ASN PRO PRO          
SEQRES  11 C  317  ALA LEU GLN ASP ALA TYR TYR ARG ALA ARG ALA GLY GLU          
SEQRES  12 C  317  ALA ALA ASN PHE CYS ALA LEU ILE LEU ALA TYR CYS ASN          
SEQRES  13 C  317  LYS THR VAL GLY GLU LEU GLY ASP VAL ARG GLU THR MET          
SEQRES  14 C  317  SER TYR LEU PHE GLN HIS ALA ASN LEU ASP SER CYS LYS          
SEQRES  15 C  317  ARG VAL LEU ASN VAL VAL CYS LYS THR CYS GLY GLN GLN          
SEQRES  16 C  317  GLN THR THR LEU LYS GLY VAL GLU ALA VAL MET TYR MET          
SEQRES  17 C  317  GLY THR LEU SER TYR GLU GLN PHE LYS LYS GLY VAL GLN          
SEQRES  18 C  317  ILE PRO CYS THR CYS GLY LYS GLN ALA THR LYS TYR LEU          
SEQRES  19 C  317  VAL GLN GLN GLU SER PRO PHE VAL MET MET SER ALA PRO          
SEQRES  20 C  317  PRO ALA GLN TYR GLU LEU LYS HIS GLY THR PHE THR CYS          
SEQRES  21 C  317  ALA SER GLU TYR THR GLY ASN TYR GLN CYS GLY HIS TYR          
SEQRES  22 C  317  LYS HIS ILE THR SER LYS GLU THR LEU TYR CYS ILE ASP          
SEQRES  23 C  317  GLY ALA LEU LEU THR LYS SER SER GLU TYR LYS GLY PRO          
SEQRES  24 C  317  ILE THR ASP VAL PHE TYR LYS GLU ASN SER TYR THR THR          
SEQRES  25 C  317  THR ILE LYS ALA ALA                                          
HET     ZN  A 501       1                                                       
HET     CL  A 502       1                                                       
HET     ZN  B 501       1                                                       
HET     CL  B 502       1                                                       
HET     ZN  C 401       1                                                       
HET     ZN  C 402       1                                                       
HET     CL  C 403       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
FORMUL   4   ZN    4(ZN 2+)                                                     
FORMUL   5   CL    3(CL 1-)                                                     
HELIX    1 AA1 THR A   26  GLY A   32  1                                   7    
HELIX    2 AA2 ASP A   61  HIS A   73  1                                  13    
HELIX    3 AA3 SER A   78  LYS A   91  1                                  14    
HELIX    4 AA4 ASN A  110  GLN A  121  1                                  12    
HELIX    5 AA5 PRO A  129  GLY A  142  1                                  14    
HELIX    6 AA6 ALA A  144  CYS A  155  1                                  12    
HELIX    7 AA7 ASP A  164  HIS A  175  1                                  12    
HELIX    8 AA8 VAL A  202  ALA A  204  5                                   3    
HELIX    9 AA9 SER A  212  GLY A  219  1                                   8    
HELIX   10 AB1 THR B   26  GLY B   32  1                                   7    
HELIX   11 AB2 ASP B   61  HIS B   73  1                                  13    
HELIX   12 AB3 SER B   78  LYS B   91  1                                  14    
HELIX   13 AB4 ASN B  110  GLN B  121  1                                  12    
HELIX   14 AB5 PRO B  129  GLY B  142  1                                  14    
HELIX   15 AB6 ALA B  144  CYS B  155  1                                  12    
HELIX   16 AB7 ASP B  164  HIS B  175  1                                  12    
HELIX   17 AB8 VAL B  202  ALA B  204  5                                   3    
HELIX   18 AB9 SER B  212  GLY B  219  1                                   8    
HELIX   19 AC1 THR C   26  GLY C   32  1                                   7    
HELIX   20 AC2 ASP C   61  HIS C   73  1                                  13    
HELIX   21 AC3 SER C   78  LYS C   91  1                                  14    
HELIX   22 AC4 ASN C  110  GLN C  121  1                                  12    
HELIX   23 AC5 PRO C  129  GLY C  142  1                                  14    
HELIX   24 AC6 ALA C  144  CYS C  155  1                                  12    
HELIX   25 AC7 ASP C  164  HIS C  175  1                                  12    
HELIX   26 AC8 VAL C  202  ALA C  204  5                                   3    
HELIX   27 AC9 SER C  212  GLY C  219  1                                   8    
SHEET    1 AA1 5 HIS A  17  ASP A  22  0                                        
SHEET    2 AA1 5 THR A   4  THR A  10 -1  N  THR A   9   O  HIS A  17           
SHEET    3 AA1 5 THR A  54  VAL A  57  1  O  PHE A  55   N  PHE A   8           
SHEET    4 AA1 5 THR A  34  LEU A  36 -1  N  TYR A  35   O  TYR A  56           
SHEET    5 AA1 5 ALA A  39  ASP A  40 -1  O  ALA A  39   N  LEU A  36           
SHEET    1 AA2 2 GLN A  97  VAL A  98  0                                        
SHEET    2 AA2 2 LEU A 101  THR A 102 -1  O  LEU A 101   N  VAL A  98           
SHEET    1 AA3 4 GLN A 196  LYS A 200  0                                        
SHEET    2 AA3 4 LYS A 182  VAL A 188 -1  N  LEU A 185   O  THR A 197           
SHEET    3 AA3 4 ALA A 230  GLU A 238 -1  O  VAL A 235   N  VAL A 184           
SHEET    4 AA3 4 VAL A 220  ILE A 222 -1  N  VAL A 220   O  LYS A 232           
SHEET    1 AA4 4 GLN A 196  LYS A 200  0                                        
SHEET    2 AA4 4 LYS A 182  VAL A 188 -1  N  LEU A 185   O  THR A 197           
SHEET    3 AA4 4 ALA A 230  GLU A 238 -1  O  VAL A 235   N  VAL A 184           
SHEET    4 AA4 4 SER A 309  THR A 311 -1  O  TYR A 310   N  GLN A 237           
SHEET    1 AA5 7 MET A 206  MET A 208  0                                        
SHEET    2 AA5 7 PHE A 241  LEU A 253  1  O  SER A 245   N  TYR A 207           
SHEET    3 AA5 7 TYR A 296  LYS A 306 -1  O  TYR A 296   N  LEU A 253           
SHEET    4 AA5 7 CYS A 260  THR A 265 -1  N  CYS A 260   O  PHE A 304           
SHEET    5 AA5 7 HIS A 272  SER A 278 -1  O  ILE A 276   N  ALA A 261           
SHEET    6 AA5 7 LEU A 282  ASP A 286 -1  O  ILE A 285   N  HIS A 275           
SHEET    7 AA5 7 LEU A 289  SER A 293 -1  O  LEU A 289   N  ASP A 286           
SHEET    1 AA6 5 HIS B  17  ASP B  22  0                                        
SHEET    2 AA6 5 THR B   4  THR B  10 -1  N  THR B   9   O  HIS B  17           
SHEET    3 AA6 5 THR B  54  VAL B  57  1  O  PHE B  55   N  PHE B   8           
SHEET    4 AA6 5 THR B  34  LEU B  36 -1  N  TYR B  35   O  TYR B  56           
SHEET    5 AA6 5 ALA B  39  ASP B  40 -1  O  ALA B  39   N  LEU B  36           
SHEET    1 AA7 2 GLN B  97  VAL B  98  0                                        
SHEET    2 AA7 2 LEU B 101  THR B 102 -1  O  LEU B 101   N  VAL B  98           
SHEET    1 AA8 4 GLN B 196  LYS B 200  0                                        
SHEET    2 AA8 4 LYS B 182  VAL B 188 -1  N  LEU B 185   O  THR B 197           
SHEET    3 AA8 4 ALA B 230  GLU B 238 -1  O  VAL B 235   N  VAL B 184           
SHEET    4 AA8 4 VAL B 220  ILE B 222 -1  N  VAL B 220   O  LYS B 232           
SHEET    1 AA9 4 GLN B 196  LYS B 200  0                                        
SHEET    2 AA9 4 LYS B 182  VAL B 188 -1  N  LEU B 185   O  THR B 197           
SHEET    3 AA9 4 ALA B 230  GLU B 238 -1  O  VAL B 235   N  VAL B 184           
SHEET    4 AA9 4 TYR B 310  THR B 311 -1  O  TYR B 310   N  GLN B 237           
SHEET    1 AB1 7 MET B 206  MET B 208  0                                        
SHEET    2 AB1 7 PHE B 241  LEU B 253  1  O  SER B 245   N  TYR B 207           
SHEET    3 AB1 7 TYR B 296  LYS B 306 -1  O  TYR B 296   N  LEU B 253           
SHEET    4 AB1 7 CYS B 260  THR B 265 -1  N  CYS B 260   O  PHE B 304           
SHEET    5 AB1 7 HIS B 272  SER B 278 -1  O  ILE B 276   N  ALA B 261           
SHEET    6 AB1 7 LEU B 282  ASP B 286 -1  O  ILE B 285   N  HIS B 275           
SHEET    7 AB1 7 LEU B 289  SER B 293 -1  O  LEU B 289   N  ASP B 286           
SHEET    1 AB2 5 HIS C  17  VAL C  21  0                                        
SHEET    2 AB2 5 ILE C   5  THR C  10 -1  N  THR C   9   O  HIS C  17           
SHEET    3 AB2 5 THR C  54  VAL C  57  1  O  PHE C  55   N  PHE C   8           
SHEET    4 AB2 5 THR C  34  LEU C  36 -1  N  TYR C  35   O  TYR C  56           
SHEET    5 AB2 5 ALA C  39  ASP C  40 -1  O  ALA C  39   N  LEU C  36           
SHEET    1 AB3 2 GLN C  97  VAL C  98  0                                        
SHEET    2 AB3 2 LEU C 101  THR C 102 -1  O  LEU C 101   N  VAL C  98           
SHEET    1 AB4 4 GLN C 196  LYS C 200  0                                        
SHEET    2 AB4 4 LYS C 182  VAL C 188 -1  N  LEU C 185   O  THR C 197           
SHEET    3 AB4 4 GLN C 229  GLU C 238 -1  O  VAL C 235   N  VAL C 184           
SHEET    4 AB4 4 VAL C 220  PRO C 223 -1  N  ILE C 222   O  ALA C 230           
SHEET    1 AB5 4 GLN C 196  LYS C 200  0                                        
SHEET    2 AB5 4 LYS C 182  VAL C 188 -1  N  LEU C 185   O  THR C 197           
SHEET    3 AB5 4 GLN C 229  GLU C 238 -1  O  VAL C 235   N  VAL C 184           
SHEET    4 AB5 4 SER C 309  THR C 311 -1  O  TYR C 310   N  GLN C 237           
SHEET    1 AB6 7 MET C 206  MET C 208  0                                        
SHEET    2 AB6 7 PHE C 241  LEU C 253  1  O  SER C 245   N  TYR C 207           
SHEET    3 AB6 7 TYR C 296  LYS C 306 -1  O  TYR C 296   N  LEU C 253           
SHEET    4 AB6 7 CYS C 260  THR C 265 -1  N  CYS C 260   O  PHE C 304           
SHEET    5 AB6 7 HIS C 272  SER C 278 -1  O  ILE C 276   N  ALA C 261           
SHEET    6 AB6 7 LEU C 282  ASP C 286 -1  O  ILE C 285   N  HIS C 275           
SHEET    7 AB6 7 LEU C 289  SER C 293 -1  O  LEU C 289   N  ASP C 286           
LINK         SG  CYS A 189                ZN    ZN A 501     1555   1555  2.19  
LINK         SG  CYS A 192                ZN    ZN A 501     1555   1555  2.53  
LINK         SG  CYS A 270                ZN    ZN C 401     1555   1555  2.39  
LINK         SG  CYS B 189                ZN    ZN B 501     1555   1555  2.64  
LINK         SG  CYS B 192                ZN    ZN B 501     1555   1555  2.50  
LINK         SG  CYS B 270                ZN    ZN C 401     1555   1555  2.34  
LINK         SG  CYS C 189                ZN    ZN C 402     1555   1555  2.48  
LINK         SG  CYS C 192                ZN    ZN C 402     1555   1555  2.85  
LINK         SG  CYS C 224                ZN    ZN C 402     1555   1555  2.57  
LINK         SG  CYS C 270                ZN    ZN C 401     1555   1555  2.36  
CRYST1  190.786  110.280   64.069  90.00  96.22  90.00 C 1 2 1      12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005241  0.000000  0.000571        0.00000                         
SCALE2      0.000000  0.009068  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015700        0.00000                         
ATOM      1  N   ARG A   3     -57.952  22.516 -10.608  1.00 98.36           N  
ANISOU    1  N   ARG A   3    14387   9395  13590   -199  -3322    310       N  
ATOM      2  CA  ARG A   3     -58.636  23.469  -9.686  1.00 97.80           C  
ANISOU    2  CA  ARG A   3    13994   9484  13679   -264  -3294    320       C  
ATOM      3  C   ARG A   3     -57.628  23.966  -8.639  1.00 97.17           C  
ANISOU    3  C   ARG A   3    13739   9545  13635   -191  -3076    296       C  
ATOM      4  O   ARG A   3     -57.186  23.140  -7.820  1.00 95.84           O  
ANISOU    4  O   ARG A   3    13553   9406  13457   -203  -3020    305       O  
ATOM      5  CB  ARG A   3     -59.849  22.793  -9.039  1.00 97.75           C  
ANISOU    5  CB  ARG A   3    13869   9511  13761   -423  -3441    369       C  
ATOM      6  CG  ARG A   3     -61.007  23.752  -8.802  1.00 97.17           C  
ANISOU    6  CG  ARG A   3    13552   9543  13825   -494  -3510    380       C  
ATOM      7  CD  ARG A   3     -62.183  23.100  -8.115  1.00 97.42           C  
ANISOU    7  CD  ARG A   3    13438   9636  13941   -657  -3640    433       C  
ATOM      8  NE  ARG A   3     -62.138  23.248  -6.663  1.00 96.14           N  
ANISOU    8  NE  ARG A   3    13006   9650  13870   -691  -3516    439       N  
ATOM      9  CZ  ARG A   3     -61.689  22.333  -5.802  1.00 95.37           C  
ANISOU    9  CZ  ARG A   3    12910   9576  13747   -733  -3457    459       C  
ATOM     10  NH1 ARG A   3     -61.208  21.176  -6.232  1.00 96.50           N  
ANISOU   10  NH1 ARG A   3    13315   9574  13776   -736  -3511    474       N  
ATOM     11  NH2 ARG A   3     -61.712  22.584  -4.501  1.00 94.09           N  
ANISOU   11  NH2 ARG A   3    12498   9580  13670   -765  -3348    464       N  
ATOM     12  N   THR A   4     -57.299  25.268  -8.661  1.00 97.77           N  
ANISOU   12  N   THR A   4    13698   9698  13751   -123  -2972    269       N  
ATOM     13  CA  THR A   4     -56.223  25.918  -7.856  1.00 97.45           C  
ANISOU   13  CA  THR A   4    13517   9777  13732    -43  -2765    244       C  
ATOM     14  C   THR A   4     -56.821  26.941  -6.870  1.00 97.08           C  
ANISOU   14  C   THR A   4    13174   9879  13831    -84  -2734    243       C  
ATOM     15  O   THR A   4     -57.899  27.490  -7.174  1.00 97.64           O  
ANISOU   15  O   THR A   4    13177   9951  13970   -134  -2856    249       O  
ATOM     16  CB  THR A   4     -55.192  26.579  -8.784  1.00 97.13           C  
ANISOU   16  CB  THR A   4    13621   9693  13591     73  -2666    215       C  
ATOM     17  OG1 THR A   4     -55.760  27.761  -9.350  1.00 97.52           O  
ANISOU   17  OG1 THR A   4    13628   9741  13683     68  -2721    209       O  
ATOM     18  CG2 THR A   4     -54.728  25.668  -9.901  1.00 97.50           C  
ANISOU   18  CG2 THR A   4    13967   9592  13483    125  -2708    210       C  
ATOM     19  N   ILE A   5     -56.143  27.192  -5.741  1.00 96.36           N  
ANISOU   19  N   ILE A   5    12917   9908  13785    -57  -2581    234       N  
ATOM     20  CA  ILE A   5     -56.532  28.223  -4.726  1.00 96.17           C  
ANISOU   20  CA  ILE A   5    12620  10031  13887    -74  -2527    225       C  
ATOM     21  C   ILE A   5     -55.385  29.223  -4.541  1.00 94.81           C  
ANISOU   21  C   ILE A   5    12407   9914  13702     23  -2362    199       C  
ATOM     22  O   ILE A   5     -54.269  28.936  -4.994  1.00 91.99           O  
ANISOU   22  O   ILE A   5    12201   9507  13244     92  -2274    193       O  
ATOM     23  CB  ILE A   5     -56.937  27.588  -3.378  1.00 96.32           C  
ANISOU   23  CB  ILE A   5    12460  10155  13982   -156  -2513    246       C  
ATOM     24  CG1 ILE A   5     -55.740  26.998  -2.626  1.00 96.59           C  
ANISOU   24  CG1 ILE A   5    12509  10217  13971   -116  -2368    245       C  
ATOM     25  CG2 ILE A   5     -58.036  26.559  -3.583  1.00 97.39           C  
ANISOU   25  CG2 ILE A   5    12644  10237  14123   -272  -2682    283       C  
ATOM     26  CD1 ILE A   5     -55.994  26.768  -1.155  1.00 96.01           C  
ANISOU   26  CD1 ILE A   5    12226  10271  13980   -182  -2320    259       C  
ATOM     27  N   LYS A   6     -55.675  30.344  -3.873  1.00 93.90           N  
ANISOU   27  N   LYS A   6    12091   9904  13682     29  -2326    183       N  
ATOM     28  CA  LYS A   6     -54.736  31.475  -3.631  1.00 91.92           C  
ANISOU   28  CA  LYS A   6    11782   9708  13432    105  -2191    162       C  
ATOM     29  C   LYS A   6     -54.239  31.418  -2.180  1.00 88.96           C  
ANISOU   29  C   LYS A   6    11227   9458  13114    103  -2064    162       C  
ATOM     30  O   LYS A   6     -55.082  31.305  -1.271  1.00 85.74           O  
ANISOU   30  O   LYS A   6    10649   9132  12795     45  -2100    164       O  
ATOM     31  CB  LYS A   6     -55.406  32.817  -3.954  1.00 92.12           C  
ANISOU   31  CB  LYS A   6    11741   9744  13517    120  -2259    143       C  
ATOM     32  CG  LYS A   6     -55.132  33.352  -5.358  1.00 92.07           C  
ANISOU   32  CG  LYS A   6    11934   9623  13424    161  -2303    139       C  
ATOM     33  CD  LYS A   6     -55.768  34.705  -5.625  1.00 91.54           C  
ANISOU   33  CD  LYS A   6    11808   9556  13413    179  -2381    119       C  
ATOM     34  CE  LYS A   6     -54.975  35.564  -6.594  1.00 91.49           C  
ANISOU   34  CE  LYS A   6    11961   9478  13320    228  -2348    117       C  
ATOM     35  NZ  LYS A   6     -55.344  36.998  -6.495  1.00 90.69           N  
ANISOU   35  NZ  LYS A   6    11778   9399  13280    253  -2392     96       N  
ATOM     36  N   VAL A   7     -52.915  31.467  -1.986  1.00 87.55           N  
ANISOU   36  N   VAL A   7    11085   9297  12881    162  -1922    159       N  
ATOM     37  CA  VAL A   7     -52.245  31.465  -0.650  1.00 86.06           C  
ANISOU   37  CA  VAL A   7    10744   9217  12735    170  -1794    159       C  
ATOM     38  C   VAL A   7     -50.999  32.363  -0.710  1.00 83.57           C  
ANISOU   38  C   VAL A   7    10437   8929  12384    241  -1665    151       C  
ATOM     39  O   VAL A   7     -50.690  32.887  -1.809  1.00 84.06           O  
ANISOU   39  O   VAL A   7    10630   8927  12382    276  -1676    150       O  
ATOM     40  CB  VAL A   7     -51.892  30.034  -0.189  1.00 87.40           C  
ANISOU   40  CB  VAL A   7    10962   9376  12867    148  -1770    175       C  
ATOM     41  CG1 VAL A   7     -53.123  29.140  -0.124  1.00 88.33           C  
ANISOU   41  CG1 VAL A   7    11078   9466  13015     56  -1906    193       C  
ATOM     42  CG2 VAL A   7     -50.804  29.395  -1.044  1.00 87.37           C  
ANISOU   42  CG2 VAL A   7    11162   9289  12742    215  -1720    176       C  
ATOM     43  N   PHE A   8     -50.315  32.524   0.431  1.00 80.73           N  
ANISOU   43  N   PHE A   8     9946   8663  12061    253  -1552    151       N  
ATOM     44  CA  PHE A   8     -49.049  33.291   0.585  1.00 77.77           C  
ANISOU   44  CA  PHE A   8     9556   8333  11660    306  -1423    152       C  
ATOM     45  C   PHE A   8     -47.919  32.387   1.101  1.00 76.25           C  
ANISOU   45  C   PHE A   8     9376   8170  11423    336  -1313    162       C  
ATOM     46  O   PHE A   8     -48.156  31.570   2.013  1.00 75.06           O  
ANISOU   46  O   PHE A   8     9156   8051  11309    306  -1314    164       O  
ATOM     47  CB  PHE A   8     -49.256  34.462   1.546  1.00 76.15           C  
ANISOU   47  CB  PHE A   8     9174   8214  11546    298  -1400    141       C  
ATOM     48  CG  PHE A   8     -50.228  35.511   1.070  1.00 75.15           C  
ANISOU   48  CG  PHE A   8     9031   8060  11459    291  -1504    124       C  
ATOM     49  CD1 PHE A   8     -50.059  36.138  -0.155  1.00 74.53           C  
ANISOU   49  CD1 PHE A   8     9092   7904  11320    313  -1541    127       C  
ATOM     50  CD2 PHE A   8     -51.293  35.893   1.868  1.00 74.23           C  
ANISOU   50  CD2 PHE A   8     8760   8003  11440    268  -1563    104       C  
ATOM     51  CE1 PHE A   8     -50.948  37.113  -0.578  1.00 74.70           C  
ANISOU   51  CE1 PHE A   8     9107   7893  11379    312  -1649    109       C  
ATOM     52  CE2 PHE A   8     -52.177  36.873   1.447  1.00 73.97           C  
ANISOU   52  CE2 PHE A   8     8710   7949  11445    278  -1665     82       C  
ATOM     53  CZ  PHE A   8     -52.005  37.478   0.223  1.00 74.36           C  
ANISOU   53  CZ  PHE A   8     8908   7908  11437    301  -1713     85       C  
ATOM     54  N   THR A   9     -46.721  32.543   0.529  1.00 74.95           N  
ANISOU   54  N   THR A   9     9298   8002  11178    394  -1221    169       N  
ATOM     55  CA  THR A   9     -45.441  31.984   1.038  1.00 74.18           C  
ANISOU   55  CA  THR A   9     9188   7956  11042    441  -1098    176       C  
ATOM     56  C   THR A   9     -44.574  33.136   1.558  1.00 72.92           C  
ANISOU   56  C   THR A   9     8914   7882  10909    452   -997    186       C  
ATOM     57  O   THR A   9     -44.726  34.247   1.041  1.00 74.83           O  
ANISOU   57  O   THR A   9     9164   8115  11153    439  -1017    190       O  
ATOM     58  CB  THR A   9     -44.723  31.169  -0.044  1.00 75.44           C  
ANISOU   58  CB  THR A   9     9529   8055  11079    506  -1072    175       C  
ATOM     59  OG1 THR A   9     -44.420  32.031  -1.140  1.00 76.00           O  
ANISOU   59  OG1 THR A   9     9682   8105  11087    525  -1056    181       O  
ATOM     60  CG2 THR A   9     -45.546  29.994  -0.527  1.00 76.21           C  
ANISOU   60  CG2 THR A   9     9756   8054  11143    493  -1184    166       C  
ATOM     61  N   THR A  10     -43.707  32.875   2.540  1.00 71.65           N  
ANISOU   61  N   THR A  10     8660   7794  10766    471   -903    192       N  
ATOM     62  CA  THR A  10     -42.793  33.873   3.164  1.00 70.46           C  
ANISOU   62  CA  THR A  10     8398   7730  10643    474   -808    207       C  
ATOM     63  C   THR A  10     -41.692  33.149   3.952  1.00 69.98           C  
ANISOU   63  C   THR A  10     8284   7731  10571    513   -709    214       C  
ATOM     64  O   THR A  10     -41.888  31.965   4.257  1.00 71.80           O  
ANISOU   64  O   THR A  10     8545   7937  10797    526   -732    203       O  
ATOM     65  CB  THR A  10     -43.572  34.843   4.064  1.00 69.55           C  
ANISOU   65  CB  THR A  10     8148   7647  10629    423   -852    200       C  
ATOM     66  OG1 THR A  10     -42.702  35.886   4.509  1.00 69.75           O  
ANISOU   66  OG1 THR A  10     8096   7736  10669    422   -778    217       O  
ATOM     67  CG2 THR A  10     -44.183  34.155   5.262  1.00 69.43           C  
ANISOU   67  CG2 THR A  10     8032   7661  10684    395   -874    188       C  
ATOM     68  N   VAL A  11     -40.584  33.838   4.248  1.00 68.04           N  
ANISOU   68  N   VAL A  11     7969   7561  10322    527   -613    234       N  
ATOM     69  CA  VAL A  11     -39.481  33.357   5.137  1.00 66.37           C  
ANISOU   69  CA  VAL A  11     7678   7424  10116    562   -521    243       C  
ATOM     70  C   VAL A  11     -39.469  34.169   6.439  1.00 64.86           C  
ANISOU   70  C   VAL A  11     7333   7293  10016    514   -507    252       C  
ATOM     71  O   VAL A  11     -38.934  33.654   7.439  1.00 62.51           O  
ANISOU   71  O   VAL A  11     6962   7042   9747    527   -463    253       O  
ATOM     72  CB  VAL A  11     -38.110  33.433   4.438  1.00 66.71           C  
ANISOU   72  CB  VAL A  11     7755   7518  10073    618   -418    263       C  
ATOM     73  CG1 VAL A  11     -37.968  32.355   3.380  1.00 68.35           C  
ANISOU   73  CG1 VAL A  11     8112   7675  10180    691   -418    246       C  
ATOM     74  CG2 VAL A  11     -37.827  34.807   3.847  1.00 66.28           C  
ANISOU   74  CG2 VAL A  11     7693   7489  10000    578   -396    292       C  
ATOM     75  N   ASP A  12     -40.015  35.394   6.416  1.00 64.94           N  
ANISOU   75  N   ASP A  12     7308   7299  10067    466   -548    255       N  
ATOM     76  CA  ASP A  12     -39.944  36.382   7.531  1.00 63.99           C  
ANISOU   76  CA  ASP A  12     7061   7230  10020    428   -538    262       C  
ATOM     77  C   ASP A  12     -41.337  36.713   8.068  1.00 62.03           C  
ANISOU   77  C   ASP A  12     6766   6956   9844    393   -629    233       C  
ATOM     78  O   ASP A  12     -41.398  37.273   9.177  1.00 59.48           O  
ANISOU   78  O   ASP A  12     6338   6677   9583    373   -623    229       O  
ATOM     79  CB  ASP A  12     -39.238  37.671   7.108  1.00 64.43           C  
ANISOU   79  CB  ASP A  12     7118   7310  10053    408   -508    293       C  
ATOM     80  CG  ASP A  12     -39.679  38.240   5.769  1.00 65.65           C  
ANISOU   80  CG  ASP A  12     7387   7402  10155    398   -561    296       C  
ATOM     81  OD1 ASP A  12     -40.707  37.783   5.233  1.00 64.54           O  
ANISOU   81  OD1 ASP A  12     7313   7195  10011    406   -635    269       O  
ATOM     82  OD2 ASP A  12     -38.966  39.128   5.264  1.00 68.50           O  
ANISOU   82  OD2 ASP A  12     7771   7780  10474    377   -531    329       O  
ATOM     83  N   ASN A  13     -42.402  36.403   7.310  1.00 63.35           N  
ANISOU   83  N   ASN A  13     7005   7061  10002    389   -710    214       N  
ATOM     84  CA  ASN A  13     -43.811  36.692   7.693  1.00 63.31           C  
ANISOU   84  CA  ASN A  13     6947   7044  10064    360   -801    185       C  
ATOM     85  C   ASN A  13     -44.032  38.211   7.696  1.00 62.93           C  
ANISOU   85  C   ASN A  13     6867   6997  10045    354   -836    179       C  
ATOM     86  O   ASN A  13     -44.873  38.685   8.479  1.00 62.16           O  
ANISOU   86  O   ASN A  13     6679   6925  10013    345   -881    153       O  
ATOM     87  CB  ASN A  13     -44.135  36.072   9.055  1.00 63.05           C  
ANISOU   87  CB  ASN A  13     6804   7064  10088    339   -788    174       C  
ATOM     88  CG  ASN A  13     -45.606  36.045   9.373  1.00 63.40           C  
ANISOU   88  CG  ASN A  13     6790   7112  10186    309   -873    148       C  
ATOM     89  OD1 ASN A  13     -46.424  35.728   8.512  1.00 63.54           O  
ANISOU   89  OD1 ASN A  13     6873   7078  10190    299   -949    141       O  
ATOM     90  ND2 ASN A  13     -45.933  36.367  10.613  1.00 63.88           N  
ANISOU   90  ND2 ASN A  13     6726   7239  10306    293   -861    134       N  
ATOM     91  N   ILE A  14     -43.275  38.933   6.866  1.00 63.33           N  
ANISOU   91  N   ILE A  14     6993   7024  10043    359   -815    203       N  
ATOM     92  CA  ILE A  14     -43.381  40.404   6.657  1.00 64.20           C  
ANISOU   92  CA  ILE A  14     7115   7114  10163    348   -862    203       C  
ATOM     93  C   ILE A  14     -43.534  40.642   5.150  1.00 65.84           C  
ANISOU   93  C   ILE A  14     7464   7247  10303    347   -911    213       C  
ATOM     94  O   ILE A  14     -44.494  41.334   4.764  1.00 66.94           O  
ANISOU   94  O   ILE A  14     7633   7335  10463    347  -1013    190       O  
ATOM     95  CB  ILE A  14     -42.162  41.124   7.282  1.00 64.14           C  
ANISOU   95  CB  ILE A  14     7060   7159  10152    333   -787    236       C  
ATOM     96  CG1 ILE A  14     -42.371  41.403   8.774  1.00 63.44           C  
ANISOU   96  CG1 ILE A  14     6844   7121  10139    332   -783    215       C  
ATOM     97  CG2 ILE A  14     -41.819  42.402   6.529  1.00 63.89           C  
ANISOU   97  CG2 ILE A  14     7106   7088  10079    309   -820    260       C  
ATOM     98  CD1 ILE A  14     -41.459  40.623   9.699  1.00 63.31           C  
ANISOU   98  CD1 ILE A  14     6753   7171  10129    331   -687    233       C  
ATOM     99  N   ASN A  15     -42.632  40.076   4.340  1.00 67.44           N  
ANISOU   99  N   ASN A  15     7750   7447  10424    353   -844    244       N  
ATOM    100  CA  ASN A  15     -42.722  40.044   2.854  1.00 68.47           C  
ANISOU  100  CA  ASN A  15     8032   7510  10474    355   -878    253       C  
ATOM    101  C   ASN A  15     -43.519  38.801   2.434  1.00 69.24           C  
ANISOU  101  C   ASN A  15     8183   7561  10562    377   -923    228       C  
ATOM    102  O   ASN A  15     -42.905  37.723   2.353  1.00 69.82           O  
ANISOU  102  O   ASN A  15     8283   7653  10591    404   -855    236       O  
ATOM    103  CB  ASN A  15     -41.336  40.067   2.200  1.00 68.11           C  
ANISOU  103  CB  ASN A  15     8046   7497  10334    353   -776    297       C  
ATOM    104  CG  ASN A  15     -40.582  41.346   2.486  1.00 68.38           C  
ANISOU  104  CG  ASN A  15     8043   7569  10368    310   -748    333       C  
ATOM    105  OD1 ASN A  15     -40.174  41.598   3.619  1.00 66.38           O  
ANISOU  105  OD1 ASN A  15     7673   7376  10171    301   -710    338       O  
ATOM    106  ND2 ASN A  15     -40.379  42.156   1.456  1.00 70.29           N  
ANISOU  106  ND2 ASN A  15     8392   7773  10540    277   -773    361       N  
ATOM    107  N   LEU A  16     -44.828  38.964   2.198  1.00 70.06           N  
ANISOU  107  N   LEU A  16     8303   7608  10708    369  -1041    200       N  
ATOM    108  CA  LEU A  16     -45.756  37.899   1.722  1.00 70.88           C  
ANISOU  108  CA  LEU A  16     8464   7658  10806    373  -1114    181       C  
ATOM    109  C   LEU A  16     -45.682  37.802   0.193  1.00 72.07           C  
ANISOU  109  C   LEU A  16     8795   7725  10860    382  -1148    192       C  
ATOM    110  O   LEU A  16     -45.828  38.842  -0.458  1.00 73.41           O  
ANISOU  110  O   LEU A  16     9024   7855  11012    370  -1198    197       O  
ATOM    111  CB  LEU A  16     -47.188  38.230   2.161  1.00 70.60           C  
ANISOU  111  CB  LEU A  16     8347   7615  10861    356  -1227    149       C  
ATOM    112  CG  LEU A  16     -47.424  38.412   3.662  1.00 69.67           C  
ANISOU  112  CG  LEU A  16     8053   7583  10834    350  -1200    133       C  
ATOM    113  CD1 LEU A  16     -48.915  38.503   3.962  1.00 69.12           C  
ANISOU  113  CD1 LEU A  16     7903   7518  10839    339  -1309    100       C  
ATOM    114  CD2 LEU A  16     -46.801  37.283   4.473  1.00 69.35           C  
ANISOU  114  CD2 LEU A  16     7962   7596  10792    345  -1110    145       C  
ATOM    115  N   HIS A  17     -45.471  36.598  -0.352  1.00 73.55           N  
ANISOU  115  N   HIS A  17     9078   7882  10983    403  -1129    195       N  
ATOM    116  CA  HIS A  17     -45.350  36.321  -1.814  1.00 75.07           C  
ANISOU  116  CA  HIS A  17     9459   7995  11068    420  -1154    202       C  
ATOM    117  C   HIS A  17     -46.583  35.540  -2.284  1.00 76.94           C  
ANISOU  117  C   HIS A  17     9770   8147  11315    409  -1283    183       C  
ATOM    118  O   HIS A  17     -46.820  34.443  -1.745  1.00 76.12           O  
ANISOU  118  O   HIS A  17     9637   8051  11234    409  -1288    175       O  
ATOM    119  CB  HIS A  17     -44.015  35.618  -2.111  1.00 73.99           C  
ANISOU  119  CB  HIS A  17     9384   7894  10833    468  -1026    219       C  
ATOM    120  CG  HIS A  17     -42.840  36.405  -1.635  1.00 73.51           C  
ANISOU  120  CG  HIS A  17     9234   7926  10768    467   -908    244       C  
ATOM    121  ND1 HIS A  17     -42.088  37.194  -2.481  1.00 74.26           N  
ANISOU  121  ND1 HIS A  17     9403   8032  10780    460   -859    273       N  
ATOM    122  CD2 HIS A  17     -42.325  36.581  -0.397  1.00 73.18           C  
ANISOU  122  CD2 HIS A  17     9037   7971  10794    461   -839    250       C  
ATOM    123  CE1 HIS A  17     -41.144  37.799  -1.788  1.00 74.16           C  
ANISOU  123  CE1 HIS A  17     9279   8111  10787    446   -766    298       C  
ATOM    124  NE2 HIS A  17     -41.271  37.443  -0.504  1.00 73.54           N  
ANISOU  124  NE2 HIS A  17     9061   8077  10802    450   -754    283       N  
ATOM    125  N   THR A  18     -47.358  36.108  -3.219  1.00 80.16           N  
ANISOU  125  N   THR A  18    10272   8476  11709    392  -1392    178       N  
ATOM    126  CA  THR A  18     -48.677  35.568  -3.660  1.00 82.67           C  
ANISOU  126  CA  THR A  18    10643   8714  12051    368  -1539    163       C  
ATOM    127  C   THR A  18     -48.444  34.361  -4.573  1.00 84.00           C  
ANISOU  127  C   THR A  18    10990   8808  12115    391  -1546    167       C  
ATOM    128  O   THR A  18     -47.539  34.431  -5.434  1.00 85.00           O  
ANISOU  128  O   THR A  18    11248   8913  12132    427  -1478    178       O  
ATOM    129  CB  THR A  18     -49.547  36.628  -4.351  1.00 83.91           C  
ANISOU  129  CB  THR A  18    10841   8810  12230    350  -1662    155       C  
ATOM    130  OG1 THR A  18     -49.355  37.886  -3.703  1.00 85.27           O  
ANISOU  130  OG1 THR A  18    10897   9041  12460    349  -1632    152       O  
ATOM    131  CG2 THR A  18     -51.018  36.268  -4.330  1.00 84.09           C  
ANISOU  131  CG2 THR A  18    10829   8794  12325    319  -1812    137       C  
ATOM    132  N   GLN A  19     -49.235  33.302  -4.382  1.00 83.75           N  
ANISOU  132  N   GLN A  19    10965   8742  12111    368  -1627    160       N  
ATOM    133  CA  GLN A  19     -49.034  31.986  -5.043  1.00 84.55           C  
ANISOU  133  CA  GLN A  19    11238   8769  12118    391  -1644    161       C  
ATOM    134  C   GLN A  19     -50.393  31.366  -5.398  1.00 86.07           C  
ANISOU  134  C   GLN A  19    11488   8876  12339    336  -1814    160       C  
ATOM    135  O   GLN A  19     -51.381  31.646  -4.690  1.00 84.17           O  
ANISOU  135  O   GLN A  19    11094   8675  12209    280  -1887    159       O  
ATOM    136  CB  GLN A  19     -48.216  31.074  -4.123  1.00 83.23           C  
ANISOU  136  CB  GLN A  19    11012   8663  11945    420  -1538    162       C  
ATOM    137  CG  GLN A  19     -46.811  31.585  -3.808  1.00 80.57           C  
ANISOU  137  CG  GLN A  19    10620   8416  11577    475  -1372    167       C  
ATOM    138  CD  GLN A  19     -45.833  31.411  -4.943  1.00 79.30           C  
ANISOU  138  CD  GLN A  19    10631   8223  11276    544  -1303    168       C  
ATOM    139  OE1 GLN A  19     -46.166  30.883  -6.000  1.00 79.29           O  
ANISOU  139  OE1 GLN A  19    10811   8122  11192    560  -1377    161       O  
ATOM    140  NE2 GLN A  19     -44.603  31.850  -4.727  1.00 78.96           N  
ANISOU  140  NE2 GLN A  19    10532   8269  11200    586  -1160    177       N  
ATOM    141  N   VAL A  20     -50.427  30.567  -6.471  1.00 88.99           N  
ANISOU  141  N   VAL A  20    12068   9136  12605    354  -1877    160       N  
ATOM    142  CA  VAL A  20     -51.622  29.809  -6.953  1.00 91.75           C  
ANISOU  142  CA  VAL A  20    12512   9387  12961    298  -2050    165       C  
ATOM    143  C   VAL A  20     -51.255  28.317  -6.976  1.00 93.47           C  
ANISOU  143  C   VAL A  20    12863   9550  13102    318  -2050    167       C  
ATOM    144  O   VAL A  20     -50.568  27.882  -7.921  1.00 93.29           O  
ANISOU  144  O   VAL A  20    13042   9453  12949    386  -2024    158       O  
ATOM    145  CB  VAL A  20     -52.126  30.336  -8.316  1.00 93.17           C  
ANISOU  145  CB  VAL A  20    12851   9461  13085    297  -2158    164       C  
ATOM    146  CG1 VAL A  20     -51.097  30.209  -9.434  1.00 93.95           C  
ANISOU  146  CG1 VAL A  20    13169   9498  13029    374  -2087    159       C  
ATOM    147  CG2 VAL A  20     -53.446  29.695  -8.713  1.00 92.99           C  
ANISOU  147  CG2 VAL A  20    12893   9349  13089    227  -2349    173       C  
ATOM    148  N   VAL A  21     -51.688  27.571  -5.951  1.00 95.83           N  
ANISOU  148  N   VAL A  21    13054   9885  13470    262  -2080    177       N  
ATOM    149  CA  VAL A  21     -51.279  26.154  -5.696  1.00 97.55           C  
ANISOU  149  CA  VAL A  21    13377  10060  13626    277  -2078    180       C  
ATOM    150  C   VAL A  21     -52.242  25.198  -6.418  1.00100.39           C  
ANISOU  150  C   VAL A  21    13911  10287  13945    217  -2261    194       C  
ATOM    151  O   VAL A  21     -53.467  25.395  -6.303  1.00101.66           O  
ANISOU  151  O   VAL A  21    13986  10449  14191    118  -2386    213       O  
ATOM    152  CB  VAL A  21     -51.185  25.830  -4.188  1.00 96.15           C  
ANISOU  152  CB  VAL A  21    13009   9986  13535    237  -2018    189       C  
ATOM    153  CG1 VAL A  21     -49.948  26.457  -3.566  1.00 94.74           C  
ANISOU  153  CG1 VAL A  21    12719   9914  13363    314  -1834    175       C  
ATOM    154  CG2 VAL A  21     -52.431  26.219  -3.405  1.00 95.82           C  
ANISOU  154  CG2 VAL A  21    12770  10012  13626    124  -2098    208       C  
ATOM    155  N   ASP A  22     -51.693  24.209  -7.137  1.00100.95           N  
ANISOU  155  N   ASP A  22    14217  10250  13886    281  -2279    183       N  
ATOM    156  CA  ASP A  22     -52.427  23.064  -7.749  1.00101.51           C  
ANISOU  156  CA  ASP A  22    14493  10178  13897    231  -2455    197       C  
ATOM    157  C   ASP A  22     -52.937  22.161  -6.618  1.00101.89           C  
ANISOU  157  C   ASP A  22    14450  10250  14014    134  -2516    224       C  
ATOM    158  O   ASP A  22     -52.110  21.725  -5.790  1.00101.28           O  
ANISOU  158  O   ASP A  22    14327  10226  13928    179  -2411    216       O  
ATOM    159  CB  ASP A  22     -51.532  22.316  -8.747  1.00101.04           C  
ANISOU  159  CB  ASP A  22    14713  10007  13671    351  -2435    169       C  
ATOM    160  CG  ASP A  22     -52.218  21.219  -9.547  1.00101.51           C  
ANISOU  160  CG  ASP A  22    15023   9897  13647    314  -2624    178       C  
ATOM    161  OD1 ASP A  22     -53.374  20.885  -9.227  1.00101.89           O  
ANISOU  161  OD1 ASP A  22    15022   9917  13773    180  -2775    215       O  
ATOM    162  OD2 ASP A  22     -51.585  20.710 -10.490  1.00101.40           O  
ANISOU  162  OD2 ASP A  22    15252   9785  13489    420  -2619    151       O  
ATOM    163  N   MET A  23     -54.249  21.904  -6.584  1.00103.22           N  
ANISOU  163  N   MET A  23    14588  10385  14243      1  -2682    259       N  
ATOM    164  CA  MET A  23     -54.939  21.180  -5.481  1.00103.82           C  
ANISOU  164  CA  MET A  23    14546  10504  14395   -126  -2751    297       C  
ATOM    165  C   MET A  23     -54.490  19.712  -5.436  1.00104.67           C  
ANISOU  165  C   MET A  23    14865  10502  14401   -114  -2802    303       C  
ATOM    166  O   MET A  23     -54.339  19.182  -4.321  1.00103.83           O  
ANISOU  166  O   MET A  23    14665  10454  14331   -159  -2769    319       O  
ATOM    167  CB  MET A  23     -56.457  21.239  -5.660  1.00106.04           C  
ANISOU  167  CB  MET A  23    14764  10773  14751   -271  -2928    337       C  
ATOM    168  CG  MET A  23     -57.049  22.565  -5.229  1.00106.47           C  
ANISOU  168  CG  MET A  23    14548  10970  14935   -301  -2884    334       C  
ATOM    169  SD  MET A  23     -57.087  22.718  -3.428  1.00109.14           S  
ANISOU  169  SD  MET A  23    14581  11496  15390   -364  -2771    348       S  
ATOM    170  CE  MET A  23     -58.846  22.882  -3.107  1.00108.61           C  
ANISOU  170  CE  MET A  23    14318  11506  15442   -531  -2926    391       C  
ATOM    171  N   SER A  24     -54.303  19.076  -6.598  1.00105.79           N  
ANISOU  171  N   SER A  24    15291  10487  14416    -54  -2888    289       N  
ATOM    172  CA  SER A  24     -53.896  17.648  -6.717  1.00105.48           C  
ANISOU  172  CA  SER A  24    15499  10315  14262    -25  -2962    287       C  
ATOM    173  C   SER A  24     -52.521  17.465  -6.066  1.00102.69           C  
ANISOU  173  C   SER A  24    15124  10023  13871    106  -2787    250       C  
ATOM    174  O   SER A  24     -52.431  16.704  -5.086  1.00103.85           O  
ANISOU  174  O   SER A  24    15238  10183  14036     59  -2798    268       O  
ATOM    175  CB  SER A  24     -53.896  17.180  -8.155  1.00107.16           C  
ANISOU  175  CB  SER A  24    16021  10355  14340     37  -3072    269       C  
ATOM    176  OG  SER A  24     -52.632  17.397  -8.770  1.00107.25           O  
ANISOU  176  OG  SER A  24    16148  10357  14243    226  -2928    212       O  
ATOM    177  N   MET A  25     -51.510  18.168  -6.585  1.00 99.53           N  
ANISOU  177  N   MET A  25    14734   9662  13419    258  -2634    204       N  
ATOM    178  CA  MET A  25     -50.102  18.132  -6.101  1.00 97.18           C  
ANISOU  178  CA  MET A  25    14404   9437  13081    401  -2454    166       C  
ATOM    179  C   MET A  25     -50.077  18.578  -4.633  1.00 94.93           C  
ANISOU  179  C   MET A  25    13832   9305  12931    332  -2360    187       C  
ATOM    180  O   MET A  25     -50.907  19.436  -4.267  1.00 96.05           O  
ANISOU  180  O   MET A  25    13775   9530  13189    224  -2371    214       O  
ATOM    181  CB  MET A  25     -49.197  19.065  -6.922  1.00 96.75           C  
ANISOU  181  CB  MET A  25    14359   9431  12968    539  -2305    127       C  
ATOM    182  CG  MET A  25     -49.187  18.817  -8.428  1.00 97.67           C  
ANISOU  182  CG  MET A  25    14749   9413  12947    613  -2376    104       C  
ATOM    183  SD  MET A  25     -48.747  20.308  -9.380  1.00 96.42           S  
ANISOU  183  SD  MET A  25    14541   9327  12764    681  -2246     87       S  
ATOM    184  CE  MET A  25     -46.985  20.360  -9.044  1.00 95.77           C  
ANISOU  184  CE  MET A  25    14408   9363  12615    855  -2013     46       C  
ATOM    185  N   THR A  26     -49.185  18.000  -3.822  1.00 92.71           N  
ANISOU  185  N   THR A  26    13536   9056  12630    397  -2279    172       N  
ATOM    186  CA  THR A  26     -48.930  18.417  -2.416  1.00 90.66           C  
ANISOU  186  CA  THR A  26    13021   8942  12482    356  -2170    185       C  
ATOM    187  C   THR A  26     -48.215  19.769  -2.431  1.00 88.38           C  
ANISOU  187  C   THR A  26    12561   8785  12235    434  -1993    164       C  
ATOM    188  O   THR A  26     -47.821  20.221  -3.525  1.00 89.03           O  
ANISOU  188  O   THR A  26    12742   8840  12245    524  -1954    139       O  
ATOM    189  CB  THR A  26     -48.077  17.403  -1.643  1.00 91.07           C  
ANISOU  189  CB  THR A  26    13133   8978  12489    419  -2140    173       C  
ATOM    190  OG1 THR A  26     -46.814  17.304  -2.304  1.00 92.60           O  
ANISOU  190  OG1 THR A  26    13452   9156  12576    608  -2037    122       O  
ATOM    191  CG2 THR A  26     -48.721  16.037  -1.538  1.00 92.56           C  
ANISOU  191  CG2 THR A  26    13506   9031  12631    335  -2322    198       C  
ATOM    192  N   TYR A  27     -48.047  20.382  -1.261  1.00 86.00           N  
ANISOU  192  N   TYR A  27    12021   8616  12036    396  -1894    175       N  
ATOM    193  CA  TYR A  27     -47.268  21.634  -1.089  1.00 84.62           C  
ANISOU  193  CA  TYR A  27    11679   8569  11904    463  -1728    159       C  
ATOM    194  C   TYR A  27     -45.807  21.372  -1.485  1.00 83.58           C  
ANISOU  194  C   TYR A  27    11649   8440  11669    627  -1610    123       C  
ATOM    195  O   TYR A  27     -45.289  22.068  -2.380  1.00 83.41           O  
ANISOU  195  O   TYR A  27    11662   8435  11594    705  -1536    106       O  
ATOM    196  CB  TYR A  27     -47.427  22.162   0.339  1.00 83.43           C  
ANISOU  196  CB  TYR A  27    11277   8545  11877    385  -1667    179       C  
ATOM    197  CG  TYR A  27     -48.728  22.882   0.592  1.00 83.46           C  
ANISOU  197  CG  TYR A  27    11134   8591  11985    255  -1739    204       C  
ATOM    198  CD1 TYR A  27     -49.627  22.427   1.543  1.00 84.41           C  
ANISOU  198  CD1 TYR A  27    11159   8736  12175    130  -1815    234       C  
ATOM    199  CD2 TYR A  27     -49.077  24.010  -0.137  1.00 83.02           C  
ANISOU  199  CD2 TYR A  27    11038   8553  11953    259  -1734    198       C  
ATOM    200  CE1 TYR A  27     -50.820  23.093   1.786  1.00 84.44           C  
ANISOU  200  CE1 TYR A  27    11011   8798  12272     22  -1873    253       C  
ATOM    201  CE2 TYR A  27     -50.271  24.676   0.084  1.00 82.79           C  
ANISOU  201  CE2 TYR A  27    10872   8565  12018    158  -1805    214       C  
ATOM    202  CZ  TYR A  27     -51.146  24.219   1.051  1.00 82.84           C  
ANISOU  202  CZ  TYR A  27    10766   8611  12096     44  -1871    240       C  
ATOM    203  OH  TYR A  27     -52.324  24.870   1.268  1.00 82.25           O  
ANISOU  203  OH  TYR A  27    10542   8595  12112    -44  -1936    252       O  
ATOM    204  N   GLY A  28     -45.185  20.370  -0.857  1.00 82.97           N  
ANISOU  204  N   GLY A  28    11621   8345  11557    678  -1600    113       N  
ATOM    205  CA  GLY A  28     -43.781  19.970  -1.073  1.00 82.95           C  
ANISOU  205  CA  GLY A  28    11699   8356  11459    845  -1493     75       C  
ATOM    206  C   GLY A  28     -43.412  19.989  -2.542  1.00 83.68           C  
ANISOU  206  C   GLY A  28    11976   8389  11428    954  -1481     46       C  
ATOM    207  O   GLY A  28     -42.460  20.708  -2.899  1.00 83.91           O  
ANISOU  207  O   GLY A  28    11947   8509  11425   1048  -1338     30       O  
ATOM    208  N   GLN A  29     -44.151  19.246  -3.369  1.00 84.23           N  
ANISOU  208  N   GLN A  29    12263   8314  11427    935  -1628     43       N  
ATOM    209  CA  GLN A  29     -43.921  19.166  -4.835  1.00 86.37           C  
ANISOU  209  CA  GLN A  29    12744   8507  11564   1034  -1638     14       C  
ATOM    210  C   GLN A  29     -43.707  20.578  -5.391  1.00 87.18           C  
ANISOU  210  C   GLN A  29    12731   8707  11685   1035  -1525     20       C  
ATOM    211  O   GLN A  29     -42.731  20.786  -6.130  1.00 88.43           O  
ANISOU  211  O   GLN A  29    12952   8903  11743   1163  -1413     -6       O  
ATOM    212  CB  GLN A  29     -45.099  18.486  -5.530  1.00 86.79           C  
ANISOU  212  CB  GLN A  29    13000   8397  11579    954  -1836     27       C  
ATOM    213  CG  GLN A  29     -45.172  16.991  -5.264  1.00 87.69           C  
ANISOU  213  CG  GLN A  29    13299   8386  11631    973  -1960     17       C  
ATOM    214  CD  GLN A  29     -46.351  16.364  -5.967  1.00 88.31           C  
ANISOU  214  CD  GLN A  29    13579   8302  11672    878  -2166     37       C  
ATOM    215  OE1 GLN A  29     -47.284  15.875  -5.334  1.00 87.99           O  
ANISOU  215  OE1 GLN A  29    13517   8215  11698    733  -2299     78       O  
ATOM    216  NE2 GLN A  29     -46.326  16.392  -7.292  1.00 89.05           N  
ANISOU  216  NE2 GLN A  29    13868   8313  11654    952  -2195     13       N  
ATOM    217  N   GLN A  30     -44.570  21.516  -5.006  1.00 87.08           N  
ANISOU  217  N   GLN A  30    12551   8739  11794    900  -1552     56       N  
ATOM    218  CA  GLN A  30     -44.640  22.874  -5.600  1.00 88.26           C  
ANISOU  218  CA  GLN A  30    12620   8948  11964    876  -1492     67       C  
ATOM    219  C   GLN A  30     -43.586  23.798  -4.975  1.00 89.04           C  
ANISOU  219  C   GLN A  30    12519   9205  12107    917  -1312     69       C  
ATOM    220  O   GLN A  30     -42.982  24.575  -5.741  1.00 91.32           O  
ANISOU  220  O   GLN A  30    12822   9540  12336    968  -1221     65       O  
ATOM    221  CB  GLN A  30     -46.050  23.429  -5.420  1.00 88.97           C  
ANISOU  221  CB  GLN A  30    12624   9014  12166    725  -1615     98       C  
ATOM    222  CG  GLN A  30     -47.130  22.529  -6.009  1.00 90.33           C  
ANISOU  222  CG  GLN A  30    12980   9036  12303    667  -1804    104       C  
ATOM    223  CD  GLN A  30     -48.511  23.085  -5.773  1.00 90.65           C  
ANISOU  223  CD  GLN A  30    12905   9075  12461    520  -1921    136       C  
ATOM    224  OE1 GLN A  30     -48.791  24.238  -6.088  1.00 90.18           O  
ANISOU  224  OE1 GLN A  30    12759   9058  12446    495  -1902    141       O  
ATOM    225  NE2 GLN A  30     -49.388  22.269  -5.206  1.00 92.08           N  
ANISOU  225  NE2 GLN A  30    13083   9211  12690    423  -2047    158       N  
ATOM    226  N   PHE A  31     -43.367  23.724  -3.654  1.00 89.08           N  
ANISOU  226  N   PHE A  31    12350   9289  12205    889  -1268     78       N  
ATOM    227  CA  PHE A  31     -42.590  24.727  -2.870  1.00 87.49           C  
ANISOU  227  CA  PHE A  31    11930   9235  12074    892  -1124     89       C  
ATOM    228  C   PHE A  31     -41.374  24.134  -2.141  1.00 87.16           C  
ANISOU  228  C   PHE A  31    11840   9264  12011    989  -1017     74       C  
ATOM    229  O   PHE A  31     -40.539  24.940  -1.696  1.00 89.53           O  
ANISOU  229  O   PHE A  31    11985   9686  12345   1008   -890     83       O  
ATOM    230  CB  PHE A  31     -43.484  25.396  -1.822  1.00 87.17           C  
ANISOU  230  CB  PHE A  31    11697   9241  12181    762  -1166    116       C  
ATOM    231  CG  PHE A  31     -44.647  26.187  -2.366  1.00 87.83           C  
ANISOU  231  CG  PHE A  31    11777   9283  12309    671  -1261    130       C  
ATOM    232  CD1 PHE A  31     -44.603  26.762  -3.631  1.00 89.07           C  
ANISOU  232  CD1 PHE A  31    12048   9402  12392    700  -1262    126       C  
ATOM    233  CD2 PHE A  31     -45.777  26.392  -1.589  1.00 88.01           C  
ANISOU  233  CD2 PHE A  31    11677   9316  12447    559  -1347    146       C  
ATOM    234  CE1 PHE A  31     -45.672  27.501  -4.114  1.00 89.34           C  
ANISOU  234  CE1 PHE A  31    12081   9393  12468    622  -1361    137       C  
ATOM    235  CE2 PHE A  31     -46.846  27.130  -2.074  1.00 89.04           C  
ANISOU  235  CE2 PHE A  31    11792   9416  12620    489  -1439    155       C  
ATOM    236  CZ  PHE A  31     -46.793  27.682  -3.335  1.00 89.51           C  
ANISOU  236  CZ  PHE A  31    11974   9425  12610    521  -1451    150       C  
ATOM    237  N   GLY A  32     -41.266  22.808  -2.011  1.00 86.57           N  
ANISOU  237  N   GLY A  32    11894   9114  11882   1046  -1075     52       N  
ATOM    238  CA  GLY A  32     -40.305  22.160  -1.095  1.00 85.33           C  
ANISOU  238  CA  GLY A  32    11681   9011  11726   1124  -1006     38       C  
ATOM    239  C   GLY A  32     -40.799  22.261   0.347  1.00 83.33           C  
ANISOU  239  C   GLY A  32    11256   8798  11606   1010  -1035     64       C  
ATOM    240  O   GLY A  32     -42.003  22.367   0.572  1.00 81.45           O  
ANISOU  240  O   GLY A  32    10996   8514  11435    884  -1139     87       O  
ATOM    241  N   PRO A  33     -39.902  22.252   1.364  1.00 82.39           N  
ANISOU  241  N   PRO A  33    11005   8772  11527   1050   -943     63       N  
ATOM    242  CA  PRO A  33     -40.324  22.408   2.760  1.00 80.98           C  
ANISOU  242  CA  PRO A  33    10663   8638  11467    943   -960     89       C  
ATOM    243  C   PRO A  33     -41.305  23.582   2.937  1.00 78.49           C  
ANISOU  243  C   PRO A  33    10210   8361  11249    812   -978    117       C  
ATOM    244  O   PRO A  33     -40.941  24.688   2.587  1.00 77.95           O  
ANISOU  244  O   PRO A  33    10059   8364  11192    824   -895    123       O  
ATOM    245  CB  PRO A  33     -39.002  22.663   3.513  1.00 80.49           C  
ANISOU  245  CB  PRO A  33    10466   8691  11423   1022   -827     84       C  
ATOM    246  CG  PRO A  33     -37.937  22.003   2.651  1.00 81.13           C  
ANISOU  246  CG  PRO A  33    10685   8759  11379   1189   -776     47       C  
ATOM    247  CD  PRO A  33     -38.443  22.107   1.225  1.00 81.93           C  
ANISOU  247  CD  PRO A  33    10942   8787  11400   1201   -818     38       C  
ATOM    248  N   THR A  34     -42.513  23.306   3.450  1.00 76.24           N  
ANISOU  248  N   THR A  34     9908   8032  11025    692  -1089    136       N  
ATOM    249  CA  THR A  34     -43.650  24.263   3.587  1.00 73.66           C  
ANISOU  249  CA  THR A  34     9464   7735  10789    573  -1132    156       C  
ATOM    250  C   THR A  34     -44.313  24.074   4.960  1.00 71.99           C  
ANISOU  250  C   THR A  34     9120   7563  10668    466  -1168    177       C  
ATOM    251  O   THR A  34     -44.597  22.917   5.303  1.00 73.02           O  
ANISOU  251  O   THR A  34     9336   7630  10775    433  -1247    184       O  
ATOM    252  CB  THR A  34     -44.672  24.061   2.458  1.00 73.04           C  
ANISOU  252  CB  THR A  34     9527   7553  10670    534  -1253    158       C  
ATOM    253  OG1 THR A  34     -43.982  23.914   1.216  1.00 73.19           O  
ANISOU  253  OG1 THR A  34     9710   7519  10579    643  -1226    136       O  
ATOM    254  CG2 THR A  34     -45.654  25.203   2.344  1.00 72.50           C  
ANISOU  254  CG2 THR A  34     9345   7519  10680    449  -1286    170       C  
ATOM    255  N   TYR A  35     -44.565  25.155   5.708  1.00 69.91           N  
ANISOU  255  N   TYR A  35     8666   7397  10498    411  -1119    186       N  
ATOM    256  CA  TYR A  35     -45.082  25.113   7.106  1.00 68.60           C  
ANISOU  256  CA  TYR A  35     8354   7294  10414    318  -1127    203       C  
ATOM    257  C   TYR A  35     -46.281  26.057   7.283  1.00 67.84           C  
ANISOU  257  C   TYR A  35     8126   7248  10399    228  -1167    210       C  
ATOM    258  O   TYR A  35     -46.318  27.133   6.670  1.00 66.38           O  
ANISOU  258  O   TYR A  35     7908   7083  10229    255  -1143    200       O  
ATOM    259  CB  TYR A  35     -43.976  25.457   8.110  1.00 67.62           C  
ANISOU  259  CB  TYR A  35     8116   7256  10318    365  -1010    200       C  
ATOM    260  CG  TYR A  35     -42.704  24.666   7.945  1.00 67.32           C  
ANISOU  260  CG  TYR A  35     8183   7189  10206    473   -961    188       C  
ATOM    261  CD1 TYR A  35     -42.427  23.579   8.760  1.00 66.97           C  
ANISOU  261  CD1 TYR A  35     8177   7120  10147    471   -985    191       C  
ATOM    262  CD2 TYR A  35     -41.776  24.998   6.970  1.00 66.52           C  
ANISOU  262  CD2 TYR A  35     8143   7088  10043    580   -893    172       C  
ATOM    263  CE1 TYR A  35     -41.259  22.848   8.614  1.00 67.63           C  
ANISOU  263  CE1 TYR A  35     8355   7178  10163    586   -948    174       C  
ATOM    264  CE2 TYR A  35     -40.609  24.271   6.802  1.00 66.97           C  
ANISOU  264  CE2 TYR A  35     8282   7133  10028    694   -844    156       C  
ATOM    265  CZ  TYR A  35     -40.351  23.191   7.627  1.00 67.70           C  
ANISOU  265  CZ  TYR A  35     8411   7199  10113    704   -874    154       C  
ATOM    266  OH  TYR A  35     -39.202  22.473   7.466  1.00 69.47           O  
ANISOU  266  OH  TYR A  35     8716   7412  10267    832   -833    131       O  
ATOM    267  N   LEU A  36     -47.226  25.646   8.135  1.00 68.67           N  
ANISOU  267  N   LEU A  36     8158   7379  10553    123  -1228    228       N  
ATOM    268  CA  LEU A  36     -48.478  26.371   8.472  1.00 68.99           C  
ANISOU  268  CA  LEU A  36     8055   7485  10672     36  -1272    233       C  
ATOM    269  C   LEU A  36     -48.552  26.519   9.994  1.00 68.88           C  
ANISOU  269  C   LEU A  36     7876   7575  10718    -17  -1218    241       C  
ATOM    270  O   LEU A  36     -49.040  25.589  10.658  1.00 68.88           O  
ANISOU  270  O   LEU A  36     7877   7578  10717   -103  -1267    265       O  
ATOM    271  CB  LEU A  36     -49.664  25.570   7.926  1.00 70.33           C  
ANISOU  271  CB  LEU A  36     8305   7591  10826    -51  -1410    253       C  
ATOM    272  CG  LEU A  36     -51.059  26.046   8.340  1.00 70.73           C  
ANISOU  272  CG  LEU A  36     8200   7719  10953   -152  -1469    263       C  
ATOM    273  CD1 LEU A  36     -51.231  27.542   8.110  1.00 70.48           C  
ANISOU  273  CD1 LEU A  36     8054   7748  10977   -100  -1428    234       C  
ATOM    274  CD2 LEU A  36     -52.130  25.269   7.591  1.00 71.51           C  
ANISOU  274  CD2 LEU A  36     8394   7746  11030   -236  -1613    287       C  
ATOM    275  N   ASP A  37     -48.061  27.644  10.512  1.00 69.36           N  
ANISOU  275  N   ASP A  37     7813   7714  10823     28  -1125    224       N  
ATOM    276  CA  ASP A  37     -47.886  27.899  11.966  1.00 70.07           C  
ANISOU  276  CA  ASP A  37     7760   7900  10961      0  -1058    226       C  
ATOM    277  C   ASP A  37     -47.188  26.680  12.594  1.00 71.22           C  
ANISOU  277  C   ASP A  37     7980   8015  11066    -10  -1045    244       C  
ATOM    278  O   ASP A  37     -47.755  26.074  13.538  1.00 72.41           O  
ANISOU  278  O   ASP A  37     8081   8200  11229   -101  -1073    264       O  
ATOM    279  CB  ASP A  37     -49.223  28.249  12.630  1.00 70.13           C  
ANISOU  279  CB  ASP A  37     7622   7992  11030    -89  -1098    228       C  
ATOM    280  CG  ASP A  37     -49.102  29.242  13.785  1.00 69.32           C  
ANISOU  280  CG  ASP A  37     7356   7998  10984    -78  -1017    211       C  
ATOM    281  OD1 ASP A  37     -48.246  30.155  13.686  1.00 66.84           O  
ANISOU  281  OD1 ASP A  37     7031   7687  10676      2   -951    193       O  
ATOM    282  OD2 ASP A  37     -49.851  29.088  14.788  1.00 68.94           O  
ANISOU  282  OD2 ASP A  37     7196   8031  10965   -153  -1021    219       O  
ATOM    283  N   GLY A  38     -46.011  26.324  12.068  1.00 71.11           N  
ANISOU  283  N   GLY A  38     8081   7939  10996     80  -1009    238       N  
ATOM    284  CA  GLY A  38     -45.120  25.296  12.641  1.00 72.23           C  
ANISOU  284  CA  GLY A  38     8295   8051  11097    104   -990    247       C  
ATOM    285  C   GLY A  38     -45.340  23.930  12.013  1.00 73.93           C  
ANISOU  285  C   GLY A  38     8690   8156  11241     90  -1087    257       C  
ATOM    286  O   GLY A  38     -44.333  23.266  11.685  1.00 78.59           O  
ANISOU  286  O   GLY A  38     9402   8686  11770    181  -1072    246       O  
ATOM    287  N   ALA A  39     -46.605  23.520  11.866  1.00 73.30           N  
ANISOU  287  N   ALA A  39     8629   8054  11168    -15  -1188    276       N  
ATOM    288  CA  ALA A  39     -47.042  22.233  11.268  1.00 72.57           C  
ANISOU  288  CA  ALA A  39     8716   7848  11009    -56  -1308    293       C  
ATOM    289  C   ALA A  39     -46.369  22.020   9.902  1.00 70.36           C  
ANISOU  289  C   ALA A  39     8608   7470  10656     63  -1317    268       C  
ATOM    290  O   ALA A  39     -46.589  22.844   8.997  1.00 69.40           O  
ANISOU  290  O   ALA A  39     8472   7353  10543     97  -1306    254       O  
ATOM    291  CB  ALA A  39     -48.549  22.217  11.143  1.00 72.48           C  
ANISOU  291  CB  ALA A  39     8659   7849  11029   -188  -1406    318       C  
ATOM    292  N   ASP A  40     -45.584  20.952   9.761  1.00 68.22           N  
ANISOU  292  N   ASP A  40     8498   7113  10309    130  -1340    261       N  
ATOM    293  CA  ASP A  40     -44.916  20.568   8.489  1.00 68.18           C  
ANISOU  293  CA  ASP A  40     8675   7014  10214    256  -1350    233       C  
ATOM    294  C   ASP A  40     -45.969  20.019   7.517  1.00 68.53           C  
ANISOU  294  C   ASP A  40     8865   6955  10217    193  -1488    245       C  
ATOM    295  O   ASP A  40     -46.426  18.879   7.725  1.00 66.44           O  
ANISOU  295  O   ASP A  40     8720   6608   9915    122  -1602    267       O  
ATOM    296  CB  ASP A  40     -43.796  19.552   8.737  1.00 67.94           C  
ANISOU  296  CB  ASP A  40     8769   6928  10115    357  -1340    216       C  
ATOM    297  CG  ASP A  40     -42.955  19.267   7.508  1.00 67.61           C  
ANISOU  297  CG  ASP A  40     8891   6819   9978    513  -1323    179       C  
ATOM    298  OD1 ASP A  40     -43.475  19.440   6.386  1.00 66.18           O  
ANISOU  298  OD1 ASP A  40     8795   6586   9763    515  -1368    174       O  
ATOM    299  OD2 ASP A  40     -41.777  18.881   7.686  1.00 68.43           O  
ANISOU  299  OD2 ASP A  40     9032   6927  10039    637  -1263    154       O  
ATOM    300  N   VAL A  41     -46.318  20.796   6.486  1.00 68.92           N  
ANISOU  300  N   VAL A  41     8915   7002  10268    214  -1487    235       N  
ATOM    301  CA  VAL A  41     -47.376  20.444   5.490  1.00 70.20           C  
ANISOU  301  CA  VAL A  41     9202   7070  10399    151  -1622    247       C  
ATOM    302  C   VAL A  41     -46.732  20.163   4.122  1.00 72.56           C  
ANISOU  302  C   VAL A  41     9707   7269  10593    281  -1629    216       C  
ATOM    303  O   VAL A  41     -47.434  20.325   3.103  1.00 73.03           O  
ANISOU  303  O   VAL A  41     9849   7268  10630    258  -1706    218       O  
ATOM    304  CB  VAL A  41     -48.465  21.535   5.416  1.00 68.79           C  
ANISOU  304  CB  VAL A  41     8863   6965  10307     60  -1636    261       C  
ATOM    305  CG1 VAL A  41     -49.110  21.771   6.774  1.00 67.98           C  
ANISOU  305  CG1 VAL A  41     8559   6971  10297    -57  -1624    287       C  
ATOM    306  CG2 VAL A  41     -47.950  22.850   4.844  1.00 68.19           C  
ANISOU  306  CG2 VAL A  41     8714   6944  10249    152  -1531    233       C  
ATOM    307  N   THR A  42     -45.468  19.716   4.103  1.00 75.23           N  
ANISOU  307  N   THR A  42    10128   7591  10863    415  -1555    187       N  
ATOM    308  CA  THR A  42     -44.700  19.366   2.874  1.00 77.98           C  
ANISOU  308  CA  THR A  42    10672   7860  11096    562  -1544    150       C  
ATOM    309  C   THR A  42     -45.393  18.217   2.127  1.00 81.78           C  
ANISOU  309  C   THR A  42    11395   8183  11494    533  -1711    155       C  
ATOM    310  O   THR A  42     -45.386  18.232   0.882  1.00 85.22           O  
ANISOU  310  O   THR A  42    11980   8547  11852    599  -1738    134       O  
ATOM    311  CB  THR A  42     -43.248  18.986   3.196  1.00 77.54           C  
ANISOU  311  CB  THR A  42    10637   7834  10988    710  -1439    119       C  
ATOM    312  OG1 THR A  42     -42.687  20.016   4.008  1.00 76.47           O  
ANISOU  312  OG1 THR A  42    10274   7842  10938    712  -1302    124       O  
ATOM    313  CG2 THR A  42     -42.381  18.818   1.966  1.00 78.38           C  
ANISOU  313  CG2 THR A  42    10904   7899  10978    875  -1394     77       C  
ATOM    314  N   LYS A  43     -45.960  17.242   2.843  1.00 84.31           N  
ANISOU  314  N   LYS A  43    11765   8444  11822    433  -1825    182       N  
ATOM    315  CA  LYS A  43     -46.410  15.956   2.231  1.00 86.60           C  
ANISOU  315  CA  LYS A  43    12319   8566  12017    416  -1995    187       C  
ATOM    316  C   LYS A  43     -47.942  15.890   2.137  1.00 87.93           C  
ANISOU  316  C   LYS A  43    12479   8696  12231    225  -2143    238       C  
ATOM    317  O   LYS A  43     -48.428  14.934   1.499  1.00 88.46           O  
ANISOU  317  O   LYS A  43    12770   8619  12222    194  -2298    248       O  
ATOM    318  CB  LYS A  43     -45.773  14.773   2.973  1.00 87.87           C  
ANISOU  318  CB  LYS A  43    12592   8668  12127    458  -2031    180       C  
ATOM    319  CG  LYS A  43     -44.383  14.395   2.463  1.00 89.21           C  
ANISOU  319  CG  LYS A  43    12897   8805  12193    680  -1954    118       C  
ATOM    320  CD  LYS A  43     -43.361  14.043   3.540  1.00 89.53           C  
ANISOU  320  CD  LYS A  43    12875   8898  12244    756  -1879    102       C  
ATOM    321  CE  LYS A  43     -41.953  14.467   3.151  1.00 90.14           C  
ANISOU  321  CE  LYS A  43    12920   9050  12277    964  -1719     47       C  
ATOM    322  NZ  LYS A  43     -40.923  13.836   4.018  1.00 90.53           N  
ANISOU  322  NZ  LYS A  43    12969   9115  12310   1066  -1682     24       N  
ATOM    323  N   ILE A  44     -48.685  16.868   2.676  1.00 87.30           N  
ANISOU  323  N   ILE A  44    12162   8739  12269    110  -2104    266       N  
ATOM    324  CA  ILE A  44     -50.173  16.949   2.504  1.00 86.73           C  
ANISOU  324  CA  ILE A  44    12048   8655  12248    -60  -2236    312       C  
ATOM    325  C   ILE A  44     -50.473  17.883   1.324  1.00 87.80           C  
ANISOU  325  C   ILE A  44    12185   8787  12386    -17  -2229    293       C  
ATOM    326  O   ILE A  44     -49.564  18.633   0.900  1.00 89.17           O  
ANISOU  326  O   ILE A  44    12337   9000  12541    119  -2099    253       O  
ATOM    327  CB  ILE A  44     -50.907  17.362   3.802  1.00 84.57           C  
ANISOU  327  CB  ILE A  44    11521   8519  12092   -210  -2214    352       C  
ATOM    328  CG1 ILE A  44     -50.960  18.881   4.009  1.00 82.50           C  
ANISOU  328  CG1 ILE A  44    11013   8404  11927   -188  -2084    336       C  
ATOM    329  CG2 ILE A  44     -50.319  16.636   5.003  1.00 84.27           C  
ANISOU  329  CG2 ILE A  44    11472   8498  12046   -223  -2182    363       C  
ATOM    330  CD1 ILE A  44     -51.655  19.300   5.289  1.00 81.56           C  
ANISOU  330  CD1 ILE A  44    10650   8426  11913   -315  -2056    367       C  
ATOM    331  N   LYS A  45     -51.703  17.822   0.806  1.00 89.35           N  
ANISOU  331  N   LYS A  45    12409   8937  12601   -136  -2370    325       N  
ATOM    332  CA  LYS A  45     -52.131  18.528  -0.429  1.00 90.65           C  
ANISOU  332  CA  LYS A  45    12621   9064  12755   -108  -2407    312       C  
ATOM    333  C   LYS A  45     -52.976  19.735  -0.036  1.00 91.69           C  
ANISOU  333  C   LYS A  45    12492   9332  13014   -191  -2377    327       C  
ATOM    334  O   LYS A  45     -53.680  19.702   0.974  1.00 90.22           O  
ANISOU  334  O   LYS A  45    12134   9233  12909   -315  -2398    361       O  
ATOM    335  CB  LYS A  45     -52.904  17.584  -1.359  1.00 91.96           C  
ANISOU  335  CB  LYS A  45    13021   9070  12847   -174  -2604    335       C  
ATOM    336  CG  LYS A  45     -52.210  16.271  -1.714  1.00 92.34           C  
ANISOU  336  CG  LYS A  45    13354   8968  12763    -97  -2665    320       C  
ATOM    337  CD  LYS A  45     -53.149  15.238  -2.331  1.00 93.51           C  
ANISOU  337  CD  LYS A  45    13717   8961  12851   -206  -2887    357       C  
ATOM    338  CE  LYS A  45     -52.830  13.808  -1.940  1.00 93.92           C  
ANISOU  338  CE  LYS A  45    13967   8898  12818   -217  -2978    368       C  
ATOM    339  NZ  LYS A  45     -54.003  12.914  -2.110  1.00 94.22           N  
ANISOU  339  NZ  LYS A  45    14133   8826  12839   -396  -3203    429       N  
ATOM    340  N   PRO A  46     -52.930  20.839  -0.818  1.00 94.28           N  
ANISOU  340  N   PRO A  46    12785   9680  13356   -123  -2330    301       N  
ATOM    341  CA  PRO A  46     -53.697  22.040  -0.495  1.00 95.56           C  
ANISOU  341  CA  PRO A  46    12713   9961  13632   -180  -2309    306       C  
ATOM    342  C   PRO A  46     -55.171  21.706  -0.197  1.00 98.84           C  
ANISOU  342  C   PRO A  46    13043  10396  14115   -345  -2458    351       C  
ATOM    343  O   PRO A  46     -55.846  21.191  -1.062  1.00101.96           O  
ANISOU  343  O   PRO A  46    13584  10684  14469   -397  -2606    370       O  
ATOM    344  CB  PRO A  46     -53.546  22.922  -1.747  1.00 94.77           C  
ANISOU  344  CB  PRO A  46    12694   9814  13499    -92  -2302    278       C  
ATOM    345  CG  PRO A  46     -52.238  22.475  -2.362  1.00 93.83           C  
ANISOU  345  CG  PRO A  46    12775   9616  13258     42  -2224    248       C  
ATOM    346  CD  PRO A  46     -52.148  20.993  -2.055  1.00 94.34           C  
ANISOU  346  CD  PRO A  46    12983   9599  13262     12  -2297    264       C  
ATOM    347  N   HIS A  47     -55.614  21.979   1.035  1.00100.25           N  
ANISOU  347  N   HIS A  47    12988  10713  14388   -427  -2415    369       N  
ATOM    348  CA  HIS A  47     -57.024  21.883   1.506  1.00101.59           C  
ANISOU  348  CA  HIS A  47    13005  10957  14636   -585  -2524    412       C  
ATOM    349  C   HIS A  47     -57.779  23.166   1.110  1.00100.50           C  
ANISOU  349  C   HIS A  47    12714  10891  14578   -571  -2536    392       C  
ATOM    350  O   HIS A  47     -57.207  23.986   0.358  1.00 99.90           O  
ANISOU  350  O   HIS A  47    12696  10777  14481   -451  -2482    353       O  
ATOM    351  CB  HIS A  47     -57.030  21.605   3.019  1.00102.90           C  
ANISOU  351  CB  HIS A  47    12999  11247  14851   -663  -2453    435       C  
ATOM    352  CG  HIS A  47     -58.273  20.990   3.571  1.00105.34           C  
ANISOU  352  CG  HIS A  47    13210  11614  15201   -846  -2569    492       C  
ATOM    353  ND1 HIS A  47     -59.028  21.616   4.546  1.00105.07           N  
ANISOU  353  ND1 HIS A  47    12901  11757  15262   -919  -2525    503       N  
ATOM    354  CD2 HIS A  47     -58.881  19.806   3.325  1.00107.43           C  
ANISOU  354  CD2 HIS A  47    13609  11790  15417   -975  -2724    546       C  
ATOM    355  CE1 HIS A  47     -60.053  20.853   4.870  1.00105.21           C  
ANISOU  355  CE1 HIS A  47    12876  11808  15292  -1089  -2641    562       C  
ATOM    356  NE2 HIS A  47     -59.987  19.736   4.133  1.00107.20           N  
ANISOU  356  NE2 HIS A  47    13379  11894  15458  -1135  -2770    593       N  
ATOM    357  N   ASN A  48     -59.025  23.335   1.577  1.00 99.65           N  
ANISOU  357  N   ASN A  48    12418  10886  14555   -689  -2610    420       N  
ATOM    358  CA  ASN A  48     -59.901  24.484   1.195  1.00 98.36           C  
ANISOU  358  CA  ASN A  48    12108  10792  14472   -675  -2650    401       C  
ATOM    359  C   ASN A  48     -59.724  25.634   2.191  1.00 96.59           C  
ANISOU  359  C   ASN A  48    11642  10728  14329   -615  -2507    365       C  
ATOM    360  O   ASN A  48     -59.577  26.775   1.724  1.00 94.90           O  
ANISOU  360  O   ASN A  48    11399  10518  14139   -514  -2474    323       O  
ATOM    361  CB  ASN A  48     -61.365  24.067   1.030  1.00 99.52           C  
ANISOU  361  CB  ASN A  48    12185  10964  14661   -822  -2819    446       C  
ATOM    362  CG  ASN A  48     -61.644  23.602  -0.387  1.00100.50           C  
ANISOU  362  CG  ASN A  48    12545  10918  14722   -832  -2976    460       C  
ATOM    363  OD1 ASN A  48     -61.148  24.198  -1.340  1.00 99.27           O  
ANISOU  363  OD1 ASN A  48    12516  10672  14529   -716  -2963    421       O  
ATOM    364  ND2 ASN A  48     -62.443  22.555  -0.546  1.00101.95           N  
ANISOU  364  ND2 ASN A  48    12794  11055  14887   -977  -3129    517       N  
ATOM    365  N   SER A  49     -59.738  25.317   3.489  1.00 97.02           N  
ANISOU  365  N   SER A  49    11548  10899  14415   -679  -2435    383       N  
ATOM    366  CA  SER A  49     -59.566  26.237   4.649  1.00 96.30           C  
ANISOU  366  CA  SER A  49    11230  10965  14392   -635  -2298    353       C  
ATOM    367  C   SER A  49     -58.305  27.101   4.504  1.00 94.47           C  
ANISOU  367  C   SER A  49    11054  10700  14139   -482  -2168    305       C  
ATOM    368  O   SER A  49     -58.261  28.186   5.117  1.00 92.53           O  
ANISOU  368  O   SER A  49    10643  10560  13953   -423  -2083    270       O  
ATOM    369  CB  SER A  49     -59.515  25.448   5.937  1.00 96.18           C  
ANISOU  369  CB  SER A  49    11129  11036  14377   -730  -2244    387       C  
ATOM    370  OG  SER A  49     -60.012  24.130   5.745  1.00 96.07           O  
ANISOU  370  OG  SER A  49    11225  10956  14318   -865  -2366    445       O  
ATOM    371  N   HIS A  50     -57.319  26.623   3.739  1.00 94.33           N  
ANISOU  371  N   HIS A  50    11260  10544  14036   -422  -2156    303       N  
ATOM    372  CA  HIS A  50     -55.988  27.255   3.524  1.00 92.80           C  
ANISOU  372  CA  HIS A  50    11139  10314  13803   -290  -2032    267       C  
ATOM    373  C   HIS A  50     -56.110  28.562   2.722  1.00 91.84           C  
ANISOU  373  C   HIS A  50    11006  10183  13706   -210  -2040    233       C  
ATOM    374  O   HIS A  50     -55.216  29.421   2.870  1.00 90.57           O  
ANISOU  374  O   HIS A  50    10823  10046  13543   -120  -1929    206       O  
ATOM    375  CB  HIS A  50     -55.029  26.258   2.849  1.00 92.82           C  
ANISOU  375  CB  HIS A  50    11385  10181  13698   -252  -2030    276       C  
ATOM    376  CG  HIS A  50     -54.688  25.061   3.683  1.00 91.12           C  
ANISOU  376  CG  HIS A  50    11201   9965  13452   -307  -2013    303       C  
ATOM    377  ND1 HIS A  50     -54.336  23.848   3.126  1.00 89.83           N  
ANISOU  377  ND1 HIS A  50    11258   9674  13197   -311  -2077    320       N  
ATOM    378  CD2 HIS A  50     -54.633  24.882   5.021  1.00 90.07           C  
ANISOU  378  CD2 HIS A  50    10924   9936  13362   -357  -1947    315       C  
ATOM    379  CE1 HIS A  50     -54.082  22.977   4.080  1.00 89.36           C  
ANISOU  379  CE1 HIS A  50    11189   9634  13127   -363  -2057    341       C  
ATOM    380  NE2 HIS A  50     -54.254  23.586   5.250  1.00 89.58           N  
ANISOU  380  NE2 HIS A  50    10995   9804  13235   -395  -1976    341       N  
ATOM    381  N   GLU A  51     -57.159  28.710   1.903  1.00 93.07           N  
ANISOU  381  N   GLU A  51    11180  10300  13880   -245  -2175    237       N  
ATOM    382  CA  GLU A  51     -57.359  29.881   1.003  1.00 93.30           C  
ANISOU  382  CA  GLU A  51    11229  10296  13923   -174  -2213    206       C  
ATOM    383  C   GLU A  51     -56.939  31.163   1.735  1.00 89.63           C  
ANISOU  383  C   GLU A  51    10612   9931  13512    -99  -2100    170       C  
ATOM    384  O   GLU A  51     -57.538  31.476   2.785  1.00 87.69           O  
ANISOU  384  O   GLU A  51    10161   9812  13345   -127  -2081    163       O  
ATOM    385  CB  GLU A  51     -58.814  29.980   0.530  1.00 98.69           C  
ANISOU  385  CB  GLU A  51    11854  10983  14658   -236  -2373    213       C  
ATOM    386  CG  GLU A  51     -59.040  31.035  -0.550  1.00102.14           C  
ANISOU  386  CG  GLU A  51    12356  11354  15097   -166  -2440    184       C  
ATOM    387  CD  GLU A  51     -58.924  30.544  -1.986  1.00105.83           C  
ANISOU  387  CD  GLU A  51    13078  11657  15476   -164  -2536    198       C  
ATOM    388  OE1 GLU A  51     -59.528  29.495  -2.300  1.00108.43           O  
ANISOU  388  OE1 GLU A  51    13480  11933  15784   -248  -2645    232       O  
ATOM    389  OE2 GLU A  51     -58.221  31.202  -2.790  1.00107.20           O  
ANISOU  389  OE2 GLU A  51    13383  11754  15593    -82  -2504    178       O  
ATOM    390  N   GLY A  52     -55.920  31.851   1.209  1.00 87.12           N  
ANISOU  390  N   GLY A  52    10396   9557  13146    -11  -2028    152       N  
ATOM    391  CA  GLY A  52     -55.469  33.177   1.674  1.00 84.11           C  
ANISOU  391  CA  GLY A  52     9912   9240  12803     59  -1944    121       C  
ATOM    392  C   GLY A  52     -54.776  33.122   3.022  1.00 80.86           C  
ANISOU  392  C   GLY A  52     9376   8929  12415     63  -1810    121       C  
ATOM    393  O   GLY A  52     -54.781  34.156   3.710  1.00 78.35           O  
ANISOU  393  O   GLY A  52     8926   8691  12153    101  -1764     95       O  
ATOM    394  N   LYS A  53     -54.198  31.971   3.387  1.00 80.48           N  
ANISOU  394  N   LYS A  53     9381   8871  12325     30  -1759    147       N  
ATOM    395  CA  LYS A  53     -53.358  31.810   4.606  1.00 79.60           C  
ANISOU  395  CA  LYS A  53     9182   8837  12222     37  -1631    149       C  
ATOM    396  C   LYS A  53     -51.878  31.941   4.222  1.00 77.77           C  
ANISOU  396  C   LYS A  53     9072   8556  11921    111  -1530    150       C  
ATOM    397  O   LYS A  53     -51.546  31.789   3.027  1.00 77.23           O  
ANISOU  397  O   LYS A  53     9171   8390  11782    143  -1559    154       O  
ATOM    398  CB  LYS A  53     -53.613  30.468   5.304  1.00 79.82           C  
ANISOU  398  CB  LYS A  53     9194   8886  12246    -43  -1643    178       C  
ATOM    399  CG  LYS A  53     -54.793  30.432   6.270  1.00 80.13           C  
ANISOU  399  CG  LYS A  53     9045   9038  12362   -124  -1683    182       C  
ATOM    400  CD  LYS A  53     -54.652  29.357   7.348  1.00 79.85           C  
ANISOU  400  CD  LYS A  53     8969   9050  12319   -199  -1644    211       C  
ATOM    401  CE  LYS A  53     -55.968  28.966   7.983  1.00 80.58           C  
ANISOU  401  CE  LYS A  53     8919   9235  12462   -310  -1713    232       C  
ATOM    402  NZ  LYS A  53     -56.491  30.047   8.854  1.00 80.08           N  
ANISOU  402  NZ  LYS A  53     8639   9312  12473   -289  -1666    201       N  
ATOM    403  N   THR A  54     -51.030  32.210   5.217  1.00 75.87           N  
ANISOU  403  N   THR A  54     8743   8385  11696    136  -1416    147       N  
ATOM    404  CA  THR A  54     -49.569  32.446   5.077  1.00 74.98           C  
ANISOU  404  CA  THR A  54     8698   8259  11529    202  -1306    150       C  
ATOM    405  C   THR A  54     -48.815  31.155   5.428  1.00 74.70           C  
ANISOU  405  C   THR A  54     8725   8209  11445    201  -1255    167       C  
ATOM    406  O   THR A  54     -49.077  30.593   6.510  1.00 73.73           O  
ANISOU  406  O   THR A  54     8512   8140  11361    154  -1247    174       O  
ATOM    407  CB  THR A  54     -49.142  33.636   5.949  1.00 73.59           C  
ANISOU  407  CB  THR A  54     8387   8166  11406    228  -1228    138       C  
ATOM    408  OG1 THR A  54     -49.836  34.786   5.458  1.00 71.40           O  
ANISOU  408  OG1 THR A  54     8088   7879  11160    240  -1294    118       O  
ATOM    409  CG2 THR A  54     -47.646  33.876   5.952  1.00 73.06           C  
ANISOU  409  CG2 THR A  54     8362   8105  11292    279  -1116    149       C  
ATOM    410  N   PHE A  55     -47.921  30.720   4.535  1.00 75.78           N  
ANISOU  410  N   PHE A  55     9016   8278  11495    256  -1225    172       N  
ATOM    411  CA  PHE A  55     -47.118  29.473   4.641  1.00 77.08           C  
ANISOU  411  CA  PHE A  55     9276   8413  11598    283  -1188    181       C  
ATOM    412  C   PHE A  55     -45.623  29.823   4.619  1.00 75.49           C  
ANISOU  412  C   PHE A  55     9084   8245  11352    365  -1061    180       C  
ATOM    413  O   PHE A  55     -45.173  30.405   3.628  1.00 74.15           O  
ANISOU  413  O   PHE A  55     8989   8052  11133    411  -1037    178       O  
ATOM    414  CB  PHE A  55     -47.462  28.511   3.497  1.00 79.09           C  
ANISOU  414  CB  PHE A  55     9721   8555  11774    288  -1279    183       C  
ATOM    415  CG  PHE A  55     -48.824  27.857   3.572  1.00 80.50           C  
ANISOU  415  CG  PHE A  55     9903   8696  11984    195  -1411    194       C  
ATOM    416  CD1 PHE A  55     -49.053  26.757   4.395  1.00 81.03           C  
ANISOU  416  CD1 PHE A  55     9962   8766  12059    138  -1442    210       C  
ATOM    417  CD2 PHE A  55     -49.882  28.333   2.813  1.00 81.29           C  
ANISOU  417  CD2 PHE A  55    10018   8762  12105    157  -1512    193       C  
ATOM    418  CE1 PHE A  55     -50.303  26.159   4.461  1.00 80.03           C  
ANISOU  418  CE1 PHE A  55     9833   8616  11958     35  -1566    229       C  
ATOM    419  CE2 PHE A  55     -51.131  27.733   2.882  1.00 81.46           C  
ANISOU  419  CE2 PHE A  55    10028   8763  12158     64  -1637    208       C  
ATOM    420  CZ  PHE A  55     -51.337  26.646   3.699  1.00 80.37           C  
ANISOU  420  CZ  PHE A  55     9876   8635  12025     -1  -1661    229       C  
ATOM    421  N   TYR A  56     -44.875  29.473   5.673  1.00 73.94           N  
ANISOU  421  N   TYR A  56     8814   8107  11173    379   -986    184       N  
ATOM    422  CA  TYR A  56     -43.389  29.548   5.705  1.00 72.91           C  
ANISOU  422  CA  TYR A  56     8690   8014  10998    458   -870    186       C  
ATOM    423  C   TYR A  56     -42.821  28.528   4.714  1.00 74.56           C  
ANISOU  423  C   TYR A  56     9075   8151  11101    531   -872    179       C  
ATOM    424  O   TYR A  56     -43.268  27.373   4.744  1.00 75.59           O  
ANISOU  424  O   TYR A  56     9294   8217  11208    518   -945    175       O  
ATOM    425  CB  TYR A  56     -42.839  29.266   7.104  1.00 71.57           C  
ANISOU  425  CB  TYR A  56     8407   7912  10873    452   -811    191       C  
ATOM    426  CG  TYR A  56     -42.748  30.450   8.032  1.00 70.06           C  
ANISOU  426  CG  TYR A  56     8052   7808  10760    421   -760    197       C  
ATOM    427  CD1 TYR A  56     -41.584  31.201   8.106  1.00 68.70           C  
ANISOU  427  CD1 TYR A  56     7831   7692  10580    465   -665    206       C  
ATOM    428  CD2 TYR A  56     -43.802  30.793   8.869  1.00 68.32           C  
ANISOU  428  CD2 TYR A  56     7724   7618  10617    348   -808    193       C  
ATOM    429  CE1 TYR A  56     -41.474  32.260   8.994  1.00 67.82           C  
ANISOU  429  CE1 TYR A  56     7585   7648  10534    435   -630    212       C  
ATOM    430  CE2 TYR A  56     -43.712  31.862   9.746  1.00 67.00           C  
ANISOU  430  CE2 TYR A  56     7419   7524  10512    332   -765    192       C  
ATOM    431  CZ  TYR A  56     -42.535  32.588   9.820  1.00 67.17           C  
ANISOU  431  CZ  TYR A  56     7411   7585  10524    375   -681    202       C  
ATOM    432  OH  TYR A  56     -42.428  33.645  10.676  1.00 65.49           O  
ANISOU  432  OH  TYR A  56     7082   7433  10367    357   -651    202       O  
ATOM    433  N   VAL A  57     -41.889  28.951   3.857  1.00 77.19           N  
ANISOU  433  N   VAL A  57     9463   8497  11367    602   -798    178       N  
ATOM    434  CA  VAL A  57     -41.141  28.067   2.911  1.00 79.83           C  
ANISOU  434  CA  VAL A  57     9959   8785  11587    698   -775    165       C  
ATOM    435  C   VAL A  57     -39.639  28.243   3.162  1.00 82.90           C  
ANISOU  435  C   VAL A  57    10285   9266  11946    778   -640    168       C  
ATOM    436  O   VAL A  57     -39.262  29.185   3.883  1.00 81.87           O  
ANISOU  436  O   VAL A  57    10004   9223  11880    745   -577    186       O  
ATOM    437  CB  VAL A  57     -41.494  28.342   1.435  1.00 79.02           C  
ANISOU  437  CB  VAL A  57     9998   8614  11409    712   -816    160       C  
ATOM    438  CG1 VAL A  57     -42.980  28.155   1.170  1.00 78.62           C  
ANISOU  438  CG1 VAL A  57    10004   8474  11392    632   -959    159       C  
ATOM    439  CG2 VAL A  57     -41.032  29.712   0.977  1.00 78.34           C  
ANISOU  439  CG2 VAL A  57     9855   8589  11320    707   -744    176       C  
ATOM    440  N   LEU A  58     -38.818  27.366   2.580  1.00 87.14           N  
ANISOU  440  N   LEU A  58    10936   9788  12385    883   -602    150       N  
ATOM    441  CA  LEU A  58     -37.335  27.418   2.689  1.00 90.05           C  
ANISOU  441  CA  LEU A  58    11246  10255  12712    976   -472    151       C  
ATOM    442  C   LEU A  58     -36.819  28.389   1.633  1.00 91.77           C  
ANISOU  442  C   LEU A  58    11475  10524  12869    991   -397    166       C  
ATOM    443  O   LEU A  58     -37.388  28.472   0.549  1.00 93.59           O  
ANISOU  443  O   LEU A  58    11833  10684  13040    984   -446    160       O  
ATOM    444  CB  LEU A  58     -36.766  26.009   2.477  1.00 92.04           C  
ANISOU  444  CB  LEU A  58    11624  10468  12879   1095   -474    118       C  
ATOM    445  CG  LEU A  58     -35.446  25.702   3.187  1.00 91.90           C  
ANISOU  445  CG  LEU A  58    11513  10547  12858   1184   -376    113       C  
ATOM    446  CD1 LEU A  58     -35.690  25.345   4.646  1.00 91.14           C  
ANISOU  446  CD1 LEU A  58    11321  10447  12858   1129   -419    119       C  
ATOM    447  CD2 LEU A  58     -34.690  24.592   2.470  1.00 93.84           C  
ANISOU  447  CD2 LEU A  58    11902  10769  12982   1340   -354     74       C  
ATOM    448  N   PRO A  59     -35.756  29.170   1.917  1.00 93.25           N  
ANISOU  448  N   PRO A  59    11532  10832  13064   1001   -283    190       N  
ATOM    449  CA  PRO A  59     -35.033  29.874   0.858  1.00 96.15           C  
ANISOU  449  CA  PRO A  59    11924  11261  13346   1026   -198    208       C  
ATOM    450  C   PRO A  59     -34.718  28.939  -0.324  1.00 99.90           C  
ANISOU  450  C   PRO A  59    12573  11698  13684   1142   -182    177       C  
ATOM    451  O   PRO A  59     -33.807  28.138  -0.203  1.00 99.73           O  
ANISOU  451  O   PRO A  59    12551  11727  13613   1252   -118    156       O  
ATOM    452  CB  PRO A  59     -33.762  30.363   1.570  1.00 96.26           C  
ANISOU  452  CB  PRO A  59    11769  11418  13386   1040    -81    236       C  
ATOM    453  CG  PRO A  59     -34.186  30.526   3.021  1.00 94.77           C  
ANISOU  453  CG  PRO A  59    11453  11226  13327    969   -128    242       C  
ATOM    454  CD  PRO A  59     -35.225  29.449   3.259  1.00 93.07           C  
ANISOU  454  CD  PRO A  59    11335  10893  13131    975   -238    207       C  
ATOM    455  N   ASN A  60     -35.512  29.024  -1.402  1.00103.38           N  
ANISOU  455  N   ASN A  60    13164  12045  14068   1120   -250    170       N  
ATOM    456  CA  ASN A  60     -35.316  28.265  -2.671  1.00106.09           C  
ANISOU  456  CA  ASN A  60    13700  12341  14269   1223   -243    140       C  
ATOM    457  C   ASN A  60     -35.258  29.239  -3.860  1.00107.14           C  
ANISOU  457  C   ASN A  60    13892  12491  14323   1187   -206    165       C  
ATOM    458  O   ASN A  60     -35.466  28.782  -5.002  1.00109.53           O  
ANISOU  458  O   ASN A  60    14379  12723  14513   1241   -234    143       O  
ATOM    459  CB  ASN A  60     -36.379  27.172  -2.855  1.00108.43           C  
ANISOU  459  CB  ASN A  60    14162  12481  14554   1235   -385    105       C  
ATOM    460  CG  ASN A  60     -37.784  27.694  -3.093  1.00108.02           C  
ANISOU  460  CG  ASN A  60    14155  12327  14561   1114   -513    119       C  
ATOM    461  OD1 ASN A  60     -38.116  28.144  -4.188  1.00110.25           O  
ANISOU  461  OD1 ASN A  60    14547  12564  14778   1096   -537    124       O  
ATOM    462  ND2 ASN A  60     -38.633  27.599  -2.084  1.00106.37           N  
ANISOU  462  ND2 ASN A  60    13864  12081  14470   1032   -599    124       N  
ATOM    463  N   ASP A  61     -34.978  30.527  -3.614  1.00106.24           N  
ANISOU  463  N   ASP A  61    13643  12462  14259   1097   -153    211       N  
ATOM    464  CA  ASP A  61     -34.604  31.531  -4.654  1.00104.92           C  
ANISOU  464  CA  ASP A  61    13513  12342  14007   1059    -93    245       C  
ATOM    465  C   ASP A  61     -33.919  32.721  -3.962  1.00103.57           C  
ANISOU  465  C   ASP A  61    13153  12295  13902    976    -17    298       C  
ATOM    466  O   ASP A  61     -33.856  32.721  -2.714  1.00101.55           O  
ANISOU  466  O   ASP A  61    12753  12073  13759    954    -21    300       O  
ATOM    467  CB  ASP A  61     -35.802  31.922  -5.531  1.00104.78           C  
ANISOU  467  CB  ASP A  61    13647  12191  13972    991   -214    244       C  
ATOM    468  CG  ASP A  61     -36.787  32.896  -4.903  1.00105.72           C  
ANISOU  468  CG  ASP A  61    13685  12260  14221    866   -315    266       C  
ATOM    469  OD1 ASP A  61     -36.941  32.869  -3.669  1.00105.94           O  
ANISOU  469  OD1 ASP A  61    13572  12312  14367    840   -331    264       O  
ATOM    470  OD2 ASP A  61     -37.397  33.675  -5.660  1.00106.14           O  
ANISOU  470  OD2 ASP A  61    13822  12252  14254    800   -379    281       O  
ATOM    471  N   ASP A  62     -33.430  33.692  -4.742  1.00104.20           N  
ANISOU  471  N   ASP A  62    13244  12438  13909    924     44    341       N  
ATOM    472  CA  ASP A  62     -32.536  34.791  -4.278  1.00104.49           C  
ANISOU  472  CA  ASP A  62    13119  12606  13974    846    131    400       C  
ATOM    473  C   ASP A  62     -33.323  35.810  -3.446  1.00102.21           C  
ANISOU  473  C   ASP A  62    12754  12262  13818    724     32    422       C  
ATOM    474  O   ASP A  62     -32.742  36.352  -2.473  1.00101.01           O  
ANISOU  474  O   ASP A  62    12442  12196  13741    679     73    453       O  
ATOM    475  CB  ASP A  62     -31.859  35.502  -5.454  1.00106.43           C  
ANISOU  475  CB  ASP A  62    13424  12927  14087    813    214    444       C  
ATOM    476  CG  ASP A  62     -31.089  34.584  -6.382  1.00108.93           C  
ANISOU  476  CG  ASP A  62    13822  13309  14253    940    320    420       C  
ATOM    477  OD1 ASP A  62     -30.822  33.424  -5.990  1.00109.73           O  
ANISOU  477  OD1 ASP A  62    13908  13423  14358   1065    345    371       O  
ATOM    478  OD2 ASP A  62     -30.757  35.036  -7.498  1.00110.34           O  
ANISOU  478  OD2 ASP A  62    14089  13527  14307    917    374    448       O  
ATOM    479  N   THR A  63     -34.590  36.069  -3.796  1.00 99.62           N  
ANISOU  479  N   THR A  63    12534  11797  13519    678    -97    405       N  
ATOM    480  CA  THR A  63     -35.478  36.988  -3.035  1.00 96.87           C  
ANISOU  480  CA  THR A  63    12121  11388  13294    583   -202    413       C  
ATOM    481  C   THR A  63     -35.548  36.496  -1.582  1.00 92.77           C  
ANISOU  481  C   THR A  63    11458  10894  12894    603   -208    391       C  
ATOM    482  O   THR A  63     -35.294  37.309  -0.670  1.00 89.81           O  
ANISOU  482  O   THR A  63    10954  10571  12598    543   -198    418       O  
ATOM    483  CB  THR A  63     -36.862  37.114  -3.692  1.00 97.49           C  
ANISOU  483  CB  THR A  63    12339  11321  13379    556   -343    388       C  
ATOM    484  OG1 THR A  63     -36.680  37.495  -5.056  1.00 98.48           O  
ANISOU  484  OG1 THR A  63    12609  11426  13380    542   -331    409       O  
ATOM    485  CG2 THR A  63     -37.751  38.117  -2.985  1.00 95.78           C  
ANISOU  485  CG2 THR A  63    12056  11055  13280    475   -449    391       C  
ATOM    486  N   LEU A  64     -35.820  35.199  -1.391  1.00 90.13           N  
ANISOU  486  N   LEU A  64    11157  10522  12564    684   -223    347       N  
ATOM    487  CA  LEU A  64     -36.069  34.559  -0.072  1.00 89.22           C  
ANISOU  487  CA  LEU A  64    10937  10409  12553    700   -247    323       C  
ATOM    488  C   LEU A  64     -34.747  34.304   0.663  1.00 88.68           C  
ANISOU  488  C   LEU A  64    10742  10465  12487    744   -129    338       C  
ATOM    489  O   LEU A  64     -34.784  34.193   1.909  1.00 89.61           O  
ANISOU  489  O   LEU A  64    10743  10603  12700    730   -140    334       O  
ATOM    490  CB  LEU A  64     -36.839  33.253  -0.292  1.00 89.57           C  
ANISOU  490  CB  LEU A  64    11094  10357  12581    759   -319    277       C  
ATOM    491  CG  LEU A  64     -38.226  33.415  -0.914  1.00 90.83           C  
ANISOU  491  CG  LEU A  64    11363  10394  12751    711   -450    262       C  
ATOM    492  CD1 LEU A  64     -38.797  32.067  -1.325  1.00 91.18           C  
ANISOU  492  CD1 LEU A  64    11542  10346  12753    767   -517    226       C  
ATOM    493  CD2 LEU A  64     -39.173  34.151   0.032  1.00 90.39           C  
ANISOU  493  CD2 LEU A  64    11198  10321  12824    627   -532    264       C  
ATOM    494  N   ARG A  65     -33.634  34.199  -0.069  1.00 87.75           N  
ANISOU  494  N   ARG A  65    10642  10432  12265    798    -22    355       N  
ATOM    495  CA  ARG A  65     -32.284  33.995   0.521  1.00 87.22           C  
ANISOU  495  CA  ARG A  65    10444  10502  12194    846     94    373       C  
ATOM    496  C   ARG A  65     -31.834  35.312   1.170  1.00 85.83           C  
ANISOU  496  C   ARG A  65    10128  10403  12081    740    120    429       C  
ATOM    497  O   ARG A  65     -31.147  35.253   2.215  1.00 85.70           O  
ANISOU  497  O   ARG A  65     9972  10465  12125    746    163    441       O  
ATOM    498  CB  ARG A  65     -31.291  33.495  -0.535  1.00 89.17           C  
ANISOU  498  CB  ARG A  65    10749  10827  12301    942    201    372       C  
ATOM    499  CG  ARG A  65     -30.340  32.418  -0.018  1.00 89.82           C  
ANISOU  499  CG  ARG A  65    10765  10992  12371   1065    276    346       C  
ATOM    500  CD  ARG A  65     -29.580  31.659  -1.088  1.00 91.99           C  
ANISOU  500  CD  ARG A  65    11125  11323  12501   1196    364    322       C  
ATOM    501  NE  ARG A  65     -30.251  30.418  -1.479  1.00 92.96           N  
ANISOU  501  NE  ARG A  65    11418  11321  12580   1296    292    259       N  
ATOM    502  CZ  ARG A  65     -30.961  30.229  -2.597  1.00 92.88           C  
ANISOU  502  CZ  ARG A  65    11592  11210  12486   1307    240    238       C  
ATOM    503  NH1 ARG A  65     -31.123  31.206  -3.477  1.00 92.81           N  
ANISOU  503  NH1 ARG A  65    11628  11208  12426   1226    253    274       N  
ATOM    504  NH2 ARG A  65     -31.519  29.052  -2.827  1.00 92.00           N  
ANISOU  504  NH2 ARG A  65    11632  10984  12340   1394    164    184       N  
ATOM    505  N   VAL A  66     -32.233  36.452   0.593  1.00 84.08           N  
ANISOU  505  N   VAL A  66     9951  10149  11845    645     81    461       N  
ATOM    506  CA  VAL A  66     -31.919  37.816   1.118  1.00 83.96           C  
ANISOU  506  CA  VAL A  66     9837  10183  11882    533     80    516       C  
ATOM    507  C   VAL A  66     -32.815  38.104   2.333  1.00 82.17           C  
ANISOU  507  C   VAL A  66     9547   9885  11786    490    -17    495       C  
ATOM    508  O   VAL A  66     -32.262  38.356   3.429  1.00 79.96           O  
ANISOU  508  O   VAL A  66     9136   9670  11574    467      9    514       O  
ATOM    509  CB  VAL A  66     -32.075  38.902   0.032  1.00 84.21           C  
ANISOU  509  CB  VAL A  66     9964  10188  11841    449     57    555       C  
ATOM    510  CG1 VAL A  66     -31.842  40.298   0.601  1.00 83.59           C  
ANISOU  510  CG1 VAL A  66     9807  10136  11815    330     31    610       C  
ATOM    511  CG2 VAL A  66     -31.168  38.655  -1.168  1.00 84.32           C  
ANISOU  511  CG2 VAL A  66    10037  10287  11713    484    165    579       C  
ATOM    512  N   GLU A  67     -34.141  38.075   2.137  1.00 82.25           N  
ANISOU  512  N   GLU A  67     9648   9775  11828    481   -126    458       N  
ATOM    513  CA  GLU A  67     -35.178  38.361   3.175  1.00 81.19           C  
ANISOU  513  CA  GLU A  67     9461   9576  11809    446   -223    431       C  
ATOM    514  C   GLU A  67     -34.866  37.574   4.455  1.00 77.81           C  
ANISOU  514  C   GLU A  67     8919   9195  11450    485   -190    414       C  
ATOM    515  O   GLU A  67     -34.982  38.166   5.548  1.00 75.85           O  
ANISOU  515  O   GLU A  67     8573   8960  11284    440   -215    420       O  
ATOM    516  CB  GLU A  67     -36.584  38.010   2.668  1.00 83.01           C  
ANISOU  516  CB  GLU A  67     9800   9690  12049    458   -330    388       C  
ATOM    517  CG  GLU A  67     -37.142  38.989   1.644  1.00 85.45           C  
ANISOU  517  CG  GLU A  67    10215   9933  12319    408   -399    401       C  
ATOM    518  CD  GLU A  67     -38.472  38.595   1.012  1.00 87.09           C  
ANISOU  518  CD  GLU A  67    10533  10029  12528    422   -508    360       C  
ATOM    519  OE1 GLU A  67     -39.162  37.703   1.568  1.00 88.20           O  
ANISOU  519  OE1 GLU A  67    10647  10141  12721    453   -547    324       O  
ATOM    520  OE2 GLU A  67     -38.811  39.169  -0.046  1.00 87.34           O  
ANISOU  520  OE2 GLU A  67    10678  10002  12503    397   -557    370       O  
ATOM    521  N   ALA A  68     -34.491  36.295   4.322  1.00 75.88           N  
ANISOU  521  N   ALA A  68     8698   8966  11164    568   -143    392       N  
ATOM    522  CA  ALA A  68     -34.147  35.386   5.441  1.00 75.80           C  
ANISOU  522  CA  ALA A  68     8604   8991  11206    614   -117    374       C  
ATOM    523  C   ALA A  68     -32.966  35.962   6.235  1.00 76.99           C  
ANISOU  523  C   ALA A  68     8617   9250  11385    592    -42    414       C  
ATOM    524  O   ALA A  68     -33.120  36.186   7.457  1.00 76.60           O  
ANISOU  524  O   ALA A  68     8476   9207  11422    557    -68    414       O  
ATOM    525  CB  ALA A  68     -33.838  34.006   4.915  1.00 75.73           C  
ANISOU  525  CB  ALA A  68     8675   8973  11126    716    -85    345       C  
ATOM    526  N   PHE A  69     -31.834  36.205   5.564  1.00 78.72           N  
ANISOU  526  N   PHE A  69     8821   9558  11530    607     47    451       N  
ATOM    527  CA  PHE A  69     -30.592  36.720   6.199  1.00 78.69           C  
ANISOU  527  CA  PHE A  69     8680   9673  11544    580    121    498       C  
ATOM    528  C   PHE A  69     -30.845  38.118   6.783  1.00 76.63           C  
ANISOU  528  C   PHE A  69     8368   9400  11348    465     69    533       C  
ATOM    529  O   PHE A  69     -30.351  38.406   7.891  1.00 74.12           O  
ANISOU  529  O   PHE A  69     7937   9129  11094    435     77    553       O  
ATOM    530  CB  PHE A  69     -29.411  36.727   5.224  1.00 81.27           C  
ANISOU  530  CB  PHE A  69     9000  10109  11768    612    228    533       C  
ATOM    531  CG  PHE A  69     -28.176  37.341   5.835  1.00 83.09           C  
ANISOU  531  CG  PHE A  69     9080  10469  12018    567    296    590       C  
ATOM    532  CD1 PHE A  69     -27.625  36.802   6.990  1.00 83.21           C  
ANISOU  532  CD1 PHE A  69     8983  10532  12098    608    313    582       C  
ATOM    533  CD2 PHE A  69     -27.605  38.491   5.306  1.00 83.71           C  
ANISOU  533  CD2 PHE A  69     9135  10615  12054    472    329    656       C  
ATOM    534  CE1 PHE A  69     -26.515  37.383   7.585  1.00 83.98           C  
ANISOU  534  CE1 PHE A  69     8941  10746  12221    560    363    638       C  
ATOM    535  CE2 PHE A  69     -26.499  39.073   5.906  1.00 84.12           C  
ANISOU  535  CE2 PHE A  69     9046  10785  12129    414    378    716       C  
ATOM    536  CZ  PHE A  69     -25.956  38.520   7.045  1.00 83.91           C  
ANISOU  536  CZ  PHE A  69     8902  10807  12170    461    395    706       C  
ATOM    537  N   GLU A  70     -31.592  38.957   6.059  1.00 75.62           N  
ANISOU  537  N   GLU A  70     8328   9203  11199    406     10    540       N  
ATOM    538  CA  GLU A  70     -31.947  40.337   6.488  1.00 74.50           C  
ANISOU  538  CA  GLU A  70     8168   9029  11107    306    -59    567       C  
ATOM    539  C   GLU A  70     -32.675  40.295   7.835  1.00 69.94           C  
ANISOU  539  C   GLU A  70     7531   8406  10636    305   -124    531       C  
ATOM    540  O   GLU A  70     -32.354  41.135   8.692  1.00 70.16           O  
ANISOU  540  O   GLU A  70     7486   8457  10711    247   -140    557       O  
ATOM    541  CB  GLU A  70     -32.788  41.040   5.418  1.00 77.41           C  
ANISOU  541  CB  GLU A  70     8666   9312  11433    266   -128    565       C  
ATOM    542  CG  GLU A  70     -31.954  41.528   4.242  1.00 80.73           C  
ANISOU  542  CG  GLU A  70     9138   9788  11748    226    -69    620       C  
ATOM    543  CD  GLU A  70     -32.208  42.949   3.774  1.00 83.19           C  
ANISOU  543  CD  GLU A  70     9518  10051  12038    124   -139    659       C  
ATOM    544  OE1 GLU A  70     -31.241  43.737   3.767  1.00 84.84           O  
ANISOU  544  OE1 GLU A  70     9684  10335  12216     45   -100    726       O  
ATOM    545  OE2 GLU A  70     -33.366  43.264   3.436  1.00 85.73           O  
ANISOU  545  OE2 GLU A  70     9937  10261  12376    120   -240    625       O  
ATOM    546  N   TYR A  71     -33.590  39.336   8.014  1.00 66.40           N  
ANISOU  546  N   TYR A  71     7114   7898  10214    362   -160    475       N  
ATOM    547  CA  TYR A  71     -34.515  39.220   9.175  1.00 62.93           C  
ANISOU  547  CA  TYR A  71     6630   7415   9864    359   -225    436       C  
ATOM    548  C   TYR A  71     -33.877  38.422  10.324  1.00 61.37           C  
ANISOU  548  C   TYR A  71     6337   7273   9706    390   -177    433       C  
ATOM    549  O   TYR A  71     -34.048  38.839  11.485  1.00 59.56           O  
ANISOU  549  O   TYR A  71     6037   7049   9544    358   -205    430       O  
ATOM    550  CB  TYR A  71     -35.830  38.569   8.732  1.00 62.59           C  
ANISOU  550  CB  TYR A  71     6669   7289   9824    388   -292    387       C  
ATOM    551  CG  TYR A  71     -36.969  38.703   9.716  1.00 61.86           C  
ANISOU  551  CG  TYR A  71     6532   7158   9811    369   -367    351       C  
ATOM    552  CD1 TYR A  71     -37.387  39.951  10.148  1.00 61.15           C  
ANISOU  552  CD1 TYR A  71     6413   7055   9765    325   -420    351       C  
ATOM    553  CD2 TYR A  71     -37.633  37.591  10.214  1.00 60.83           C  
ANISOU  553  CD2 TYR A  71     6393   7010   9709    396   -386    316       C  
ATOM    554  CE1 TYR A  71     -38.421  40.094  11.057  1.00 60.31           C  
ANISOU  554  CE1 TYR A  71     6258   6929   9726    320   -480    313       C  
ATOM    555  CE2 TYR A  71     -38.671  37.715  11.124  1.00 59.61           C  
ANISOU  555  CE2 TYR A  71     6186   6841   9622    373   -445    287       C  
ATOM    556  CZ  TYR A  71     -39.073  38.974  11.539  1.00 59.47           C  
ANISOU  556  CZ  TYR A  71     6129   6821   9645    342   -487    282       C  
ATOM    557  OH  TYR A  71     -40.089  39.151  12.431  1.00 58.23           O  
ANISOU  557  OH  TYR A  71     5912   6663   9547    331   -537    248       O  
ATOM    558  N   TYR A  72     -33.184  37.317  10.015  1.00 61.81           N  
ANISOU  558  N   TYR A  72     6401   7366   9717    456   -113    431       N  
ATOM    559  CA  TYR A  72     -32.685  36.316  10.999  1.00 61.33           C  
ANISOU  559  CA  TYR A  72     6276   7340   9686    503    -83    419       C  
ATOM    560  C   TYR A  72     -31.204  36.540  11.338  1.00 61.63           C  
ANISOU  560  C   TYR A  72     6217   7482   9716    508     -5    463       C  
ATOM    561  O   TYR A  72     -30.805  36.138  12.444  1.00 62.60           O  
ANISOU  561  O   TYR A  72     6265   7632   9885    521      1    461       O  
ATOM    562  CB  TYR A  72     -32.930  34.897  10.478  1.00 61.54           C  
ANISOU  562  CB  TYR A  72     6385   7328   9666    584    -81    382       C  
ATOM    563  CG  TYR A  72     -34.387  34.544  10.358  1.00 61.14           C  
ANISOU  563  CG  TYR A  72     6413   7182   9634    568   -167    344       C  
ATOM    564  CD1 TYR A  72     -34.971  34.326   9.123  1.00 62.41           C  
ANISOU  564  CD1 TYR A  72     6689   7285   9737    586   -196    330       C  
ATOM    565  CD2 TYR A  72     -35.188  34.454  11.483  1.00 60.01           C  
ANISOU  565  CD2 TYR A  72     6224   7012   9563    529   -221    326       C  
ATOM    566  CE1 TYR A  72     -36.319  34.023   9.009  1.00 62.88           C  
ANISOU  566  CE1 TYR A  72     6810   7262   9816    563   -282    300       C  
ATOM    567  CE2 TYR A  72     -36.535  34.151  11.385  1.00 60.39           C  
ANISOU  567  CE2 TYR A  72     6325   6991   9628    506   -298    296       C  
ATOM    568  CZ  TYR A  72     -37.104  33.934  10.144  1.00 61.97           C  
ANISOU  568  CZ  TYR A  72     6633   7133   9776    521   -332    284       C  
ATOM    569  OH  TYR A  72     -38.432  33.642  10.046  1.00 63.70           O  
ANISOU  569  OH  TYR A  72     6895   7290  10016    492   -415    260       O  
ATOM    570  N   HIS A  73     -30.416  37.146  10.442  1.00 61.23           N  
ANISOU  570  N   HIS A  73     6164   7492   9607    493     48    504       N  
ATOM    571  CA  HIS A  73     -28.959  37.405  10.630  1.00 60.76           C  
ANISOU  571  CA  HIS A  73     5999   7551   9533    488    126    554       C  
ATOM    572  C   HIS A  73     -28.209  36.074  10.744  1.00 60.80           C  
ANISOU  572  C   HIS A  73     5975   7611   9515    600    185    532       C  
ATOM    573  O   HIS A  73     -27.304  35.971  11.600  1.00 60.65           O  
ANISOU  573  O   HIS A  73     5847   7664   9532    609    215    553       O  
ATOM    574  CB  HIS A  73     -28.702  38.298  11.851  1.00 59.96           C  
ANISOU  574  CB  HIS A  73     5803   7470   9509    408     95    586       C  
ATOM    575  CG  HIS A  73     -29.010  39.738  11.615  1.00 60.22           C  
ANISOU  575  CG  HIS A  73     5860   7475   9544    305     49    621       C  
ATOM    576  ND1 HIS A  73     -28.551  40.736  12.451  1.00 59.74           N  
ANISOU  576  ND1 HIS A  73     5729   7439   9527    224     24    663       N  
ATOM    577  CD2 HIS A  73     -29.726  40.353  10.649  1.00 59.56           C  
ANISOU  577  CD2 HIS A  73     5874   7331   9422    271     11    619       C  
ATOM    578  CE1 HIS A  73     -28.967  41.900  12.001  1.00 60.16           C  
ANISOU  578  CE1 HIS A  73     5842   7448   9567    147    -28    685       C  
ATOM    579  NE2 HIS A  73     -29.690  41.691  10.897  1.00 59.90           N  
ANISOU  579  NE2 HIS A  73     5910   7363   9484    175    -36    659       N  
ATOM    580  N   THR A  74     -28.594  35.089   9.928  1.00 60.88           N  
ANISOU  580  N   THR A  74     6085   7577   9466    684    190    490       N  
ATOM    581  CA  THR A  74     -27.970  33.740   9.881  1.00 60.88           C  
ANISOU  581  CA  THR A  74     6092   7609   9428    810    233    458       C  
ATOM    582  C   THR A  74     -28.123  33.135   8.481  1.00 61.76           C  
ANISOU  582  C   THR A  74     6327   7700   9438    889    259    431       C  
ATOM    583  O   THR A  74     -29.158  33.362   7.838  1.00 61.23           O  
ANISOU  583  O   THR A  74     6367   7543   9355    850    206    417       O  
ATOM    584  CB  THR A  74     -28.553  32.820  10.958  1.00 59.58           C  
ANISOU  584  CB  THR A  74     5945   7367   9324    838    166    417       C  
ATOM    585  OG1 THR A  74     -27.741  31.650  11.044  1.00 58.86           O  
ANISOU  585  OG1 THR A  74     5848   7314   9199    958    202    393       O  
ATOM    586  CG2 THR A  74     -29.971  32.392  10.662  1.00 59.75           C  
ANISOU  586  CG2 THR A  74     6094   7262   9344    826     86    376       C  
ATOM    587  N   THR A  75     -27.119  32.363   8.072  1.00 64.30           N  
ANISOU  587  N   THR A  75     6634   8103   9694   1003    334    421       N  
ATOM    588  CA  THR A  75     -26.980  31.680   6.761  1.00 65.59           C  
ANISOU  588  CA  THR A  75     6908   8269   9742   1107    377    391       C  
ATOM    589  C   THR A  75     -27.435  30.212   6.872  1.00 66.05           C  
ANISOU  589  C   THR A  75     7082   8230   9783   1220    321    326       C  
ATOM    590  O   THR A  75     -27.706  29.590   5.820  1.00 66.56           O  
ANISOU  590  O   THR A  75     7285   8246   9757   1296    319    291       O  
ATOM    591  CB  THR A  75     -25.506  31.741   6.348  1.00 66.15           C  
ANISOU  591  CB  THR A  75     6874   8509   9749   1174    498    418       C  
ATOM    592  OG1 THR A  75     -24.761  31.335   7.499  1.00 64.64           O  
ANISOU  592  OG1 THR A  75     6561   8377   9622   1216    506    418       O  
ATOM    593  CG2 THR A  75     -25.057  33.125   5.931  1.00 66.90           C  
ANISOU  593  CG2 THR A  75     6887   8700   9830   1056    554    489       C  
ATOM    594  N   ASP A  76     -27.497  29.694   8.106  1.00 64.80           N  
ANISOU  594  N   ASP A  76     6878   8039   9702   1225    271    312       N  
ATOM    595  CA  ASP A  76     -27.687  28.253   8.420  1.00 65.36           C  
ANISOU  595  CA  ASP A  76     7045   8030   9759   1330    215    257       C  
ATOM    596  C   ASP A  76     -28.958  27.741   7.754  1.00 65.95           C  
ANISOU  596  C   ASP A  76     7299   7962   9797   1319    130    224       C  
ATOM    597  O   ASP A  76     -30.055  28.059   8.204  1.00 68.11           O  
ANISOU  597  O   ASP A  76     7590   8152  10134   1210     52    231       O  
ATOM    598  CB  ASP A  76     -27.751  28.029   9.932  1.00 63.89           C  
ANISOU  598  CB  ASP A  76     6785   7820   9671   1290    161    260       C  
ATOM    599  CG  ASP A  76     -28.086  26.602  10.320  1.00 62.95           C  
ANISOU  599  CG  ASP A  76     6780   7599   9537   1370     83    211       C  
ATOM    600  OD1 ASP A  76     -28.246  25.756   9.415  1.00 61.30           O  
ANISOU  600  OD1 ASP A  76     6714   7334   9242   1465     66    173       O  
ATOM    601  OD2 ASP A  76     -28.199  26.355  11.524  1.00 62.50           O  
ANISOU  601  OD2 ASP A  76     6681   7515   9549   1333     34    214       O  
ATOM    602  N   PRO A  77     -28.863  26.908   6.698  1.00 66.86           N  
ANISOU  602  N   PRO A  77     7551   8044   9807   1434    136    186       N  
ATOM    603  CA  PRO A  77     -30.041  26.480   5.943  1.00 67.79           C  
ANISOU  603  CA  PRO A  77     7846   8026   9882   1418     51    160       C  
ATOM    604  C   PRO A  77     -30.931  25.469   6.683  1.00 68.12           C  
ANISOU  604  C   PRO A  77     7981   7938   9963   1401    -70    132       C  
ATOM    605  O   PRO A  77     -31.934  25.066   6.116  1.00 67.68           O  
ANISOU  605  O   PRO A  77     8068   7769   9877   1377   -152    115       O  
ATOM    606  CB  PRO A  77     -29.439  25.821   4.695  1.00 69.31           C  
ANISOU  606  CB  PRO A  77     8156   8235   9941   1565    102    125       C  
ATOM    607  CG  PRO A  77     -28.126  25.274   5.198  1.00 70.10           C  
ANISOU  607  CG  PRO A  77     8165   8439  10027   1693    171    110       C  
ATOM    608  CD  PRO A  77     -27.626  26.313   6.181  1.00 68.87           C  
ANISOU  608  CD  PRO A  77     7799   8392   9974   1593    222    163       C  
ATOM    609  N   SER A  78     -30.546  25.078   7.903  1.00 68.46           N  
ANISOU  609  N   SER A  78     7944   7999  10068   1409    -83    133       N  
ATOM    610  CA  SER A  78     -31.355  24.226   8.819  1.00 68.43           C  
ANISOU  610  CA  SER A  78     8005   7885  10109   1364   -195    119       C  
ATOM    611  C   SER A  78     -32.232  25.096   9.735  1.00 67.07           C  
ANISOU  611  C   SER A  78     7729   7709  10044   1200   -229    154       C  
ATOM    612  O   SER A  78     -33.188  24.545  10.325  1.00 66.98           O  
ANISOU  612  O   SER A  78     7774   7609  10064   1131   -324    150       O  
ATOM    613  CB  SER A  78     -30.472  23.300   9.621  1.00 69.13           C  
ANISOU  613  CB  SER A  78     8082   7989  10195   1464   -198     99       C  
ATOM    614  OG  SER A  78     -29.877  23.975  10.721  1.00 68.49           O  
ANISOU  614  OG  SER A  78     7821   8001  10198   1415   -150    130       O  
ATOM    615  N   PHE A  79     -31.929  26.396   9.848  1.00 65.66           N  
ANISOU  615  N   PHE A  79     7409   7624   9912   1139   -158    188       N  
ATOM    616  CA  PHE A  79     -32.490  27.307  10.885  1.00 64.18           C  
ANISOU  616  CA  PHE A  79     7103   7455   9826   1008   -176    217       C  
ATOM    617  C   PHE A  79     -34.016  27.200  10.913  1.00 64.76           C  
ANISOU  617  C   PHE A  79     7248   7431   9926    914   -273    210       C  
ATOM    618  O   PHE A  79     -34.561  26.837  11.972  1.00 66.20           O  
ANISOU  618  O   PHE A  79     7409   7583  10161    854   -328    211       O  
ATOM    619  CB  PHE A  79     -32.088  28.771  10.676  1.00 62.32           C  
ANISOU  619  CB  PHE A  79     6751   7309   9617    957   -105    253       C  
ATOM    620  CG  PHE A  79     -32.548  29.668  11.800  1.00 59.64           C  
ANISOU  620  CG  PHE A  79     6300   6986   9372    845   -126    276       C  
ATOM    621  CD1 PHE A  79     -31.831  29.744  12.983  1.00 59.55           C  
ANISOU  621  CD1 PHE A  79     6180   7031   9413    839   -102    291       C  
ATOM    622  CD2 PHE A  79     -33.722  30.391  11.707  1.00 57.47           C  
ANISOU  622  CD2 PHE A  79     6034   6667   9133    754   -178    278       C  
ATOM    623  CE1 PHE A  79     -32.251  30.557  14.029  1.00 57.51           C  
ANISOU  623  CE1 PHE A  79     5832   6783   9233    744   -123    308       C  
ATOM    624  CE2 PHE A  79     -34.148  31.192  12.757  1.00 56.24           C  
ANISOU  624  CE2 PHE A  79     5782   6530   9057    668   -197    291       C  
ATOM    625  CZ  PHE A  79     -33.408  31.284  13.912  1.00 55.87           C  
ANISOU  625  CZ  PHE A  79     5637   6537   9055    663   -168    306       C  
ATOM    626  N   LEU A  80     -34.673  27.520   9.795  1.00 65.63           N  
ANISOU  626  N   LEU A  80     7436   7501   9999    898   -294    206       N  
ATOM    627  CA  LEU A  80     -36.158  27.591   9.697  1.00 65.67           C  
ANISOU  627  CA  LEU A  80     7490   7428  10033    804   -387    203       C  
ATOM    628  C   LEU A  80     -36.766  26.266  10.152  1.00 64.23           C  
ANISOU  628  C   LEU A  80     7399   7161   9841    796   -475    187       C  
ATOM    629  O   LEU A  80     -37.624  26.295  11.045  1.00 63.44           O  
ANISOU  629  O   LEU A  80     7248   7051   9804    700   -527    196       O  
ATOM    630  CB  LEU A  80     -36.578  27.925   8.265  1.00 68.25           C  
ANISOU  630  CB  LEU A  80     7914   7715  10301    815   -400    198       C  
ATOM    631  CG  LEU A  80     -36.848  29.408   8.015  1.00 69.64           C  
ANISOU  631  CG  LEU A  80     8008   7933  10516    748   -377    219       C  
ATOM    632  CD1 LEU A  80     -35.546  30.183   7.823  1.00 69.92           C  
ANISOU  632  CD1 LEU A  80     7969   8067  10531    788   -269    241       C  
ATOM    633  CD2 LEU A  80     -37.760  29.584   6.816  1.00 71.68           C  
ANISOU  633  CD2 LEU A  80     8379   8119  10735    728   -439    211       C  
ATOM    634  N   GLY A  81     -36.330  25.160   9.553  1.00 64.41           N  
ANISOU  634  N   GLY A  81     7558   7130   9782    892   -493    165       N  
ATOM    635  CA  GLY A  81     -36.688  23.791   9.967  1.00 63.88           C  
ANISOU  635  CA  GLY A  81     7605   6974   9691    896   -583    152       C  
ATOM    636  C   GLY A  81     -36.829  23.679  11.475  1.00 62.23           C  
ANISOU  636  C   GLY A  81     7298   6789   9556    820   -601    168       C  
ATOM    637  O   GLY A  81     -37.897  23.263  11.931  1.00 62.21           O  
ANISOU  637  O   GLY A  81     7326   6733   9577    720   -687    178       O  
ATOM    638  N   ARG A  82     -35.800  24.065  12.227  1.00 62.06           N  
ANISOU  638  N   ARG A  82     7160   6852   9568    858   -522    174       N  
ATOM    639  CA  ARG A  82     -35.715  23.827  13.697  1.00 62.46           C  
ANISOU  639  CA  ARG A  82     7135   6921   9675    806   -537    187       C  
ATOM    640  C   ARG A  82     -36.587  24.847  14.435  1.00 60.43           C  
ANISOU  640  C   ARG A  82     6749   6709   9500    675   -535    210       C  
ATOM    641  O   ARG A  82     -37.222  24.460  15.433  1.00 59.52           O  
ANISOU  641  O   ARG A  82     6621   6577   9417    591   -586    220       O  
ATOM    642  CB  ARG A  82     -34.259  23.888  14.173  1.00 63.33           C  
ANISOU  642  CB  ARG A  82     7169   7103   9788    901   -461    185       C  
ATOM    643  CG  ARG A  82     -33.331  22.900  13.482  1.00 64.34           C  
ANISOU  643  CG  ARG A  82     7410   7203   9833   1053   -457    155       C  
ATOM    644  CD  ARG A  82     -31.938  22.925  14.077  1.00 65.05           C  
ANISOU  644  CD  ARG A  82     7404   7376   9935   1144   -389    154       C  
ATOM    645  NE  ARG A  82     -31.626  24.192  14.740  1.00 64.00           N  
ANISOU  645  NE  ARG A  82     7090   7345   9880   1074   -318    187       N  
ATOM    646  CZ  ARG A  82     -30.989  25.217  14.183  1.00 63.75           C  
ANISOU  646  CZ  ARG A  82     6960   7408   9852   1094   -228    203       C  
ATOM    647  NH1 ARG A  82     -30.547  25.148  12.942  1.00 64.95           N  
ANISOU  647  NH1 ARG A  82     7164   7580   9932   1185   -183    188       N  
ATOM    648  NH2 ARG A  82     -30.748  26.302  14.889  1.00 63.12           N  
ANISOU  648  NH2 ARG A  82     6735   7404   9841   1021   -185    235       N  
ATOM    649  N   TYR A  83     -36.606  26.093  13.954  1.00 59.56           N  
ANISOU  649  N   TYR A  83     6556   6656   9416    662   -479    217       N  
ATOM    650  CA  TYR A  83     -37.486  27.192  14.436  1.00 58.26           C  
ANISOU  650  CA  TYR A  83     6283   6531   9321    559   -482    230       C  
ATOM    651  C   TYR A  83     -38.953  26.743  14.313  1.00 58.82           C  
ANISOU  651  C   TYR A  83     6411   6541   9394    476   -573    226       C  
ATOM    652  O   TYR A  83     -39.680  26.768  15.326  1.00 58.32           O  
ANISOU  652  O   TYR A  83     6283   6497   9378    389   -601    234       O  
ATOM    653  CB  TYR A  83     -37.159  28.486  13.676  1.00 57.21           C  
ANISOU  653  CB  TYR A  83     6094   6447   9195    578   -422    236       C  
ATOM    654  CG  TYR A  83     -38.161  29.602  13.829  1.00 55.48           C  
ANISOU  654  CG  TYR A  83     5801   6246   9031    495   -444    239       C  
ATOM    655  CD1 TYR A  83     -38.752  29.860  15.052  1.00 54.62           C  
ANISOU  655  CD1 TYR A  83     5603   6166   8983    423   -461    241       C  
ATOM    656  CD2 TYR A  83     -38.509  30.407  12.756  1.00 54.68           C  
ANISOU  656  CD2 TYR A  83     5724   6135   8916    495   -448    237       C  
ATOM    657  CE1 TYR A  83     -39.675  30.878  15.206  1.00 54.37           C  
ANISOU  657  CE1 TYR A  83     5502   6157   8998    366   -482    236       C  
ATOM    658  CE2 TYR A  83     -39.432  31.429  12.890  1.00 54.36           C  
ANISOU  658  CE2 TYR A  83     5622   6107   8926    434   -478    234       C  
ATOM    659  CZ  TYR A  83     -40.016  31.664  14.122  1.00 54.49           C  
ANISOU  659  CZ  TYR A  83     5544   6157   9003    375   -494    231       C  
ATOM    660  OH  TYR A  83     -40.932  32.659  14.284  1.00 54.75           O  
ANISOU  660  OH  TYR A  83     5513   6208   9081    332   -525    220       O  
ATOM    661  N   MET A  84     -39.366  26.318  13.116  1.00 59.67           N  
ANISOU  661  N   MET A  84     6639   6583   9450    499   -619    216       N  
ATOM    662  CA  MET A  84     -40.737  25.811  12.837  1.00 61.27           C  
ANISOU  662  CA  MET A  84     6908   6723   9648    419   -718    218       C  
ATOM    663  C   MET A  84     -41.032  24.587  13.714  1.00 61.93           C  
ANISOU  663  C   MET A  84     7042   6766   9722    367   -782    227       C  
ATOM    664  O   MET A  84     -42.147  24.526  14.272  1.00 63.41           O  
ANISOU  664  O   MET A  84     7184   6962   9944    256   -836    242       O  
ATOM    665  CB  MET A  84     -40.911  25.448  11.357  1.00 62.43           C  
ANISOU  665  CB  MET A  84     7200   6792   9726    468   -760    206       C  
ATOM    666  CG  MET A  84     -40.932  26.661  10.430  1.00 63.14           C  
ANISOU  666  CG  MET A  84     7256   6911   9823    489   -721    202       C  
ATOM    667  SD  MET A  84     -42.406  27.716  10.633  1.00 64.03           S  
ANISOU  667  SD  MET A  84     7259   7054  10015    378   -770    207       S  
ATOM    668  CE  MET A  84     -41.806  28.971  11.768  1.00 62.63           C  
ANISOU  668  CE  MET A  84     6901   6985   9909    372   -678    212       C  
ATOM    669  N   SER A  85     -40.076  23.659  13.844  1.00 60.97           N  
ANISOU  669  N   SER A  85     7006   6606   9552    443   -778    221       N  
ATOM    670  CA  SER A  85     -40.186  22.456  14.712  1.00 60.71           C  
ANISOU  670  CA  SER A  85     7043   6524   9500    401   -846    231       C  
ATOM    671  C   SER A  85     -40.424  22.896  16.152  1.00 58.90           C  
ANISOU  671  C   SER A  85     6669   6369   9338    310   -818    250       C  
ATOM    672  O   SER A  85     -41.438  22.481  16.740  1.00 59.89           O  
ANISOU  672  O   SER A  85     6793   6485   9474    192   -883    270       O  
ATOM    673  CB  SER A  85     -38.973  21.588  14.624  1.00 62.30           C  
ANISOU  673  CB  SER A  85     7347   6681   9643    524   -838    213       C  
ATOM    674  OG  SER A  85     -38.929  20.954  13.356  1.00 64.73           O  
ANISOU  674  OG  SER A  85     7815   6904   9872    602   -883    193       O  
ATOM    675  N   ALA A  86     -39.506  23.699  16.689  1.00 56.79           N  
ANISOU  675  N   ALA A  86     6289   6178   9109    360   -727    246       N  
ATOM    676  CA  ALA A  86     -39.612  24.309  18.032  1.00 54.59           C  
ANISOU  676  CA  ALA A  86     5872   5977   8892    289   -690    260       C  
ATOM    677  C   ALA A  86     -41.002  24.939  18.165  1.00 52.70           C  
ANISOU  677  C   ALA A  86     5554   5776   8694    179   -713    267       C  
ATOM    678  O   ALA A  86     -41.715  24.575  19.119  1.00 51.19           O  
ANISOU  678  O   ALA A  86     5333   5602   8515     80   -747    283       O  
ATOM    679  CB  ALA A  86     -38.513  25.326  18.230  1.00 54.20           C  
ANISOU  679  CB  ALA A  86     5718   5999   8876    360   -596    255       C  
ATOM    680  N   LEU A  87     -41.371  25.798  17.206  1.00 51.28           N  
ANISOU  680  N   LEU A  87     5346   5609   8526    199   -699    256       N  
ATOM    681  CA  LEU A  87     -42.614  26.619  17.225  1.00 50.96           C  
ANISOU  681  CA  LEU A  87     5214   5617   8531    122   -716    254       C  
ATOM    682  C   LEU A  87     -43.835  25.714  17.393  1.00 51.22           C  
ANISOU  682  C   LEU A  87     5285   5624   8550     16   -803    270       C  
ATOM    683  O   LEU A  87     -44.696  26.038  18.235  1.00 50.21           O  
ANISOU  683  O   LEU A  87     5050   5567   8461    -69   -805    277       O  
ATOM    684  CB  LEU A  87     -42.712  27.429  15.928  1.00 51.26           C  
ANISOU  684  CB  LEU A  87     5266   5640   8567    174   -710    239       C  
ATOM    685  CG  LEU A  87     -43.997  28.244  15.755  1.00 51.03           C  
ANISOU  685  CG  LEU A  87     5158   5648   8581    115   -743    232       C  
ATOM    686  CD1 LEU A  87     -44.231  29.165  16.947  1.00 50.86           C  
ANISOU  686  CD1 LEU A  87     4986   5719   8617     81   -699    226       C  
ATOM    687  CD2 LEU A  87     -43.965  29.035  14.456  1.00 50.76           C  
ANISOU  687  CD2 LEU A  87     5160   5588   8539    171   -744    218       C  
ATOM    688  N   ASN A  88     -43.878  24.620  16.626  1.00 52.46           N  
ANISOU  688  N   ASN A  88     5593   5688   8651     23   -874    277       N  
ATOM    689  CA  ASN A  88     -44.994  23.636  16.576  1.00 53.59           C  
ANISOU  689  CA  ASN A  88     5804   5786   8768    -84   -977    300       C  
ATOM    690  C   ASN A  88     -45.363  23.162  17.992  1.00 54.06           C  
ANISOU  690  C   ASN A  88     5807   5894   8839   -192   -987    326       C  
ATOM    691  O   ASN A  88     -46.536  22.805  18.194  1.00 54.89           O  
ANISOU  691  O   ASN A  88     5890   6019   8946   -314  -1050    350       O  
ATOM    692  CB  ASN A  88     -44.634  22.455  15.673  1.00 54.71           C  
ANISOU  692  CB  ASN A  88     6148   5804   8834    -39  -1051    301       C  
ATOM    693  CG  ASN A  88     -45.838  21.790  15.043  1.00 55.57           C  
ANISOU  693  CG  ASN A  88     6340   5854   8917   -134  -1167    321       C  
ATOM    694  OD1 ASN A  88     -45.744  21.232  13.955  1.00 56.57           O  
ANISOU  694  OD1 ASN A  88     6621   5883   8989    -85  -1226    314       O  
ATOM    695  ND2 ASN A  88     -46.958  21.793  15.745  1.00 55.94           N  
ANISOU  695  ND2 ASN A  88     6292   5964   8998   -271  -1202    349       N  
ATOM    696  N   HIS A  89     -44.402  23.142  18.921  1.00 54.93           N  
ANISOU  696  N   HIS A  89     5894   6024   8952   -155   -929    324       N  
ATOM    697  CA  HIS A  89     -44.579  22.742  20.347  1.00 56.20           C  
ANISOU  697  CA  HIS A  89     6008   6229   9117   -250   -929    348       C  
ATOM    698  C   HIS A  89     -44.904  23.978  21.210  1.00 55.48           C  
ANISOU  698  C   HIS A  89     5729   6262   9086   -275   -848    338       C  
ATOM    699  O   HIS A  89     -45.882  23.902  21.997  1.00 55.26           O  
ANISOU  699  O   HIS A  89     5626   6303   9067   -391   -862    357       O  
ATOM    700  CB  HIS A  89     -43.320  22.008  20.858  1.00 57.63           C  
ANISOU  700  CB  HIS A  89     6281   6351   9262   -186   -923    349       C  
ATOM    701  CG  HIS A  89     -42.996  20.724  20.160  1.00 59.63           C  
ANISOU  701  CG  HIS A  89     6730   6478   9447   -151  -1011    353       C  
ATOM    702  ND1 HIS A  89     -42.008  20.622  19.179  1.00 59.81           N  
ANISOU  702  ND1 HIS A  89     6843   6440   9442     -5   -997    324       N  
ATOM    703  CD2 HIS A  89     -43.495  19.479  20.320  1.00 61.45           C  
ANISOU  703  CD2 HIS A  89     7091   6630   9623   -241  -1117    382       C  
ATOM    704  CE1 HIS A  89     -41.931  19.373  18.763  1.00 61.48           C  
ANISOU  704  CE1 HIS A  89     7235   6538   9584      7  -1092    328       C  
ATOM    705  NE2 HIS A  89     -42.829  18.649  19.450  1.00 62.40           N  
ANISOU  705  NE2 HIS A  89     7387   6635   9684   -140  -1173    365       N  
ATOM    706  N   THR A  90     -44.130  25.071  21.066  1.00 54.30           N  
ANISOU  706  N   THR A  90     5512   6146   8973   -173   -770    311       N  
ATOM    707  CA  THR A  90     -44.135  26.257  21.976  1.00 53.29           C  
ANISOU  707  CA  THR A  90     5233   6118   8895   -173   -695    297       C  
ATOM    708  C   THR A  90     -45.473  26.996  21.875  1.00 53.77           C  
ANISOU  708  C   THR A  90     5185   6254   8989   -228   -703    287       C  
ATOM    709  O   THR A  90     -45.835  27.663  22.866  1.00 53.09           O  
ANISOU  709  O   THR A  90     4981   6258   8929   -259   -661    278       O  
ATOM    710  CB  THR A  90     -42.988  27.248  21.707  1.00 51.99           C  
ANISOU  710  CB  THR A  90     5039   5957   8755    -60   -627    276       C  
ATOM    711  OG1 THR A  90     -43.102  27.793  20.390  1.00 51.23           O  
ANISOU  711  OG1 THR A  90     4964   5837   8664     -3   -634    261       O  
ATOM    712  CG2 THR A  90     -41.620  26.633  21.896  1.00 51.79           C  
ANISOU  712  CG2 THR A  90     5090   5883   8705      4   -611    284       C  
ATOM    713  N   LYS A  91     -46.167  26.875  20.735  1.00 53.84           N  
ANISOU  713  N   LYS A  91     5233   6229   8993   -234   -758    285       N  
ATOM    714  CA  LYS A  91     -47.519  27.453  20.499  1.00 53.60           C  
ANISOU  714  CA  LYS A  91     5105   6267   8994   -283   -784    275       C  
ATOM    715  C   LYS A  91     -48.580  26.692  21.319  1.00 53.71           C  
ANISOU  715  C   LYS A  91     5071   6341   8994   -419   -821    304       C  
ATOM    716  O   LYS A  91     -49.722  27.184  21.370  1.00 54.21           O  
ANISOU  716  O   LYS A  91     5020   6492   9085   -465   -832    296       O  
ATOM    717  CB  LYS A  91     -47.842  27.443  19.000  1.00 54.00           C  
ANISOU  717  CB  LYS A  91     5230   6247   9037   -250   -844    269       C  
ATOM    718  CG  LYS A  91     -48.173  26.070  18.431  1.00 55.50           C  
ANISOU  718  CG  LYS A  91     5554   6355   9179   -314   -933    300       C  
ATOM    719  CD  LYS A  91     -48.613  26.071  16.967  1.00 56.39           C  
ANISOU  719  CD  LYS A  91     5745   6398   9280   -289  -1000    293       C  
ATOM    720  CE  LYS A  91     -49.179  24.728  16.540  1.00 57.63           C  
ANISOU  720  CE  LYS A  91     6027   6479   9388   -375  -1106    328       C  
ATOM    721  NZ  LYS A  91     -50.177  24.859  15.448  1.00 58.56           N  
ANISOU  721  NZ  LYS A  91     6160   6574   9514   -401  -1186    328       N  
ATOM    722  N   LYS A  92     -48.247  25.544  21.928  1.00 52.93           N  
ANISOU  722  N   LYS A  92     5056   6203   8851   -484   -844    338       N  
ATOM    723  CA  LYS A  92     -49.181  24.764  22.789  1.00 53.34           C  
ANISOU  723  CA  LYS A  92     5073   6314   8878   -634   -879    376       C  
ATOM    724  C   LYS A  92     -48.831  24.959  24.265  1.00 52.07           C  
ANISOU  724  C   LYS A  92     4840   6228   8714   -659   -808    378       C  
ATOM    725  O   LYS A  92     -49.628  24.520  25.114  1.00 51.80           O  
ANISOU  725  O   LYS A  92     4750   6271   8658   -784   -817    407       O  
ATOM    726  CB  LYS A  92     -49.145  23.273  22.438  1.00 54.74           C  
ANISOU  726  CB  LYS A  92     5419   6383   8996   -708   -975    419       C  
ATOM    727  CG  LYS A  92     -49.685  22.909  21.061  1.00 55.35           C  
ANISOU  727  CG  LYS A  92     5581   6384   9062   -711  -1063    424       C  
ATOM    728  CD  LYS A  92     -49.244  21.536  20.598  1.00 56.15           C  
ANISOU  728  CD  LYS A  92     5892   6344   9098   -731  -1156    452       C  
ATOM    729  CE  LYS A  92     -49.771  21.162  19.230  1.00 56.82           C  
ANISOU  729  CE  LYS A  92     6078   6344   9164   -733  -1250    457       C  
ATOM    730  NZ  LYS A  92     -48.864  20.201  18.564  1.00 57.13           N  
ANISOU  730  NZ  LYS A  92     6334   6229   9142   -662  -1308    456       N  
ATOM    731  N   TRP A  93     -47.678  25.564  24.558  1.00 51.16           N  
ANISOU  731  N   TRP A  93     4729   6092   8616   -552   -744    352       N  
ATOM    732  CA  TRP A  93     -47.278  25.965  25.935  1.00 51.07           C  
ANISOU  732  CA  TRP A  93     4647   6148   8607   -559   -675    347       C  
ATOM    733  C   TRP A  93     -48.192  27.092  26.424  1.00 49.68           C  
ANISOU  733  C   TRP A  93     4302   6107   8465   -566   -622    318       C  
ATOM    734  O   TRP A  93     -48.678  27.871  25.587  1.00 48.41           O  
ANISOU  734  O   TRP A  93     4085   5966   8340   -511   -627    290       O  
ATOM    735  CB  TRP A  93     -45.814  26.417  26.003  1.00 51.10           C  
ANISOU  735  CB  TRP A  93     4693   6095   8625   -440   -629    327       C  
ATOM    736  CG  TRP A  93     -44.788  25.346  25.794  1.00 52.15           C  
ANISOU  736  CG  TRP A  93     4975   6115   8722   -415   -669    348       C  
ATOM    737  CD1 TRP A  93     -44.982  23.997  25.677  1.00 52.86           C  
ANISOU  737  CD1 TRP A  93     5185   6134   8762   -487   -746    381       C  
ATOM    738  CD2 TRP A  93     -43.367  25.553  25.707  1.00 51.68           C  
ANISOU  738  CD2 TRP A  93     4961   6002   8672   -303   -637    335       C  
ATOM    739  NE1 TRP A  93     -43.781  23.355  25.505  1.00 52.34           N  
ANISOU  739  NE1 TRP A  93     5242   5971   8672   -411   -765    382       N  
ATOM    740  CE2 TRP A  93     -42.775  24.286  25.522  1.00 51.70           C  
ANISOU  740  CE2 TRP A  93     5106   5907   8628   -298   -695    355       C  
ATOM    741  CE3 TRP A  93     -42.545  26.685  25.756  1.00 51.09           C  
ANISOU  741  CE3 TRP A  93     4820   5955   8637   -209   -572    311       C  
ATOM    742  CZ2 TRP A  93     -41.397  24.132  25.393  1.00 51.89           C  
ANISOU  742  CZ2 TRP A  93     5191   5874   8648   -191   -681    347       C  
ATOM    743  CZ3 TRP A  93     -41.183  26.530  25.634  1.00 50.58           C  
ANISOU  743  CZ3 TRP A  93     4812   5836   8569   -123   -558    312       C  
ATOM    744  CH2 TRP A  93     -40.620  25.268  25.452  1.00 51.27           C  
ANISOU  744  CH2 TRP A  93     5025   5840   8613   -108   -608    327       C  
ATOM    745  N   LYS A  94     -48.376  27.186  27.739  1.00 49.31           N  
ANISOU  745  N   LYS A  94     4186   6147   8402   -621   -576    323       N  
ATOM    746  CA  LYS A  94     -49.114  28.294  28.393  1.00 49.46           C  
ANISOU  746  CA  LYS A  94     4047   6301   8443   -607   -516    287       C  
ATOM    747  C   LYS A  94     -48.095  29.354  28.819  1.00 47.24           C  
ANISOU  747  C   LYS A  94     3756   6005   8187   -492   -458    251       C  
ATOM    748  O   LYS A  94     -47.058  28.974  29.398  1.00 46.10           O  
ANISOU  748  O   LYS A  94     3688   5802   8024   -488   -446    268       O  
ATOM    749  CB  LYS A  94     -49.931  27.769  29.578  1.00 51.71           C  
ANISOU  749  CB  LYS A  94     4265   6697   8682   -737   -496    314       C  
ATOM    750  CG  LYS A  94     -50.973  26.713  29.229  1.00 53.68           C  
ANISOU  750  CG  LYS A  94     4519   6971   8903   -875   -560    361       C  
ATOM    751  CD  LYS A  94     -52.192  27.284  28.511  1.00 55.30           C  
ANISOU  751  CD  LYS A  94     4599   7267   9144   -870   -574    339       C  
ATOM    752  CE  LYS A  94     -52.646  26.443  27.327  1.00 56.73           C  
ANISOU  752  CE  LYS A  94     4855   7374   9324   -930   -671    373       C  
ATOM    753  NZ  LYS A  94     -53.173  27.303  26.233  1.00 57.83           N  
ANISOU  753  NZ  LYS A  94     4928   7525   9517   -842   -691    333       N  
ATOM    754  N   TYR A  95     -48.384  30.629  28.530  1.00 45.76           N  
ANISOU  754  N   TYR A  95     3483   5863   8039   -404   -433    204       N  
ATOM    755  CA  TYR A  95     -47.584  31.805  28.962  1.00 43.85           C  
ANISOU  755  CA  TYR A  95     3225   5616   7820   -304   -388    168       C  
ATOM    756  C   TYR A  95     -48.436  32.696  29.851  1.00 43.05           C  
ANISOU  756  C   TYR A  95     2999   5641   7715   -291   -345    128       C  
ATOM    757  O   TYR A  95     -48.891  33.749  29.422  1.00 42.22           O  
ANISOU  757  O   TYR A  95     2833   5567   7641   -213   -348     84       O  
ATOM    758  CB  TYR A  95     -47.072  32.574  27.749  1.00 43.52           C  
ANISOU  758  CB  TYR A  95     3219   5499   7817   -203   -410    148       C  
ATOM    759  CG  TYR A  95     -46.308  31.707  26.789  1.00 43.62           C  
ANISOU  759  CG  TYR A  95     3348   5400   7823   -203   -446    182       C  
ATOM    760  CD1 TYR A  95     -44.931  31.578  26.869  1.00 42.80           C  
ANISOU  760  CD1 TYR A  95     3320   5223   7716   -162   -431    198       C  
ATOM    761  CD2 TYR A  95     -46.981  30.990  25.815  1.00 44.01           C  
ANISOU  761  CD2 TYR A  95     3430   5423   7866   -242   -498    197       C  
ATOM    762  CE1 TYR A  95     -44.239  30.771  25.982  1.00 42.73           C  
ANISOU  762  CE1 TYR A  95     3414   5125   7695   -147   -460    223       C  
ATOM    763  CE2 TYR A  95     -46.298  30.189  24.917  1.00 43.98           C  
ANISOU  763  CE2 TYR A  95     3545   5316   7847   -230   -533    222       C  
ATOM    764  CZ  TYR A  95     -44.926  30.075  25.004  1.00 43.13           C  
ANISOU  764  CZ  TYR A  95     3509   5144   7733   -177   -510    232       C  
ATOM    765  OH  TYR A  95     -44.278  29.261  24.127  1.00 43.50           O  
ANISOU  765  OH  TYR A  95     3669   5101   7758   -152   -541    250       O  
ATOM    766  N   PRO A  96     -48.667  32.308  31.123  1.00 43.01           N  
ANISOU  766  N   PRO A  96     2961   5712   7669   -362   -306    139       N  
ATOM    767  CA  PRO A  96     -49.417  33.146  32.048  1.00 43.56           C  
ANISOU  767  CA  PRO A  96     2916   5910   7724   -339   -256     96       C  
ATOM    768  C   PRO A  96     -48.598  34.372  32.468  1.00 43.34           C  
ANISOU  768  C   PRO A  96     2905   5848   7711   -226   -232     55       C  
ATOM    769  O   PRO A  96     -47.383  34.325  32.471  1.00 42.88           O  
ANISOU  769  O   PRO A  96     2941   5689   7662   -206   -240     75       O  
ATOM    770  CB  PRO A  96     -49.684  32.214  33.236  1.00 44.04           C  
ANISOU  770  CB  PRO A  96     2968   6041   7723   -461   -224    132       C  
ATOM    771  CG  PRO A  96     -48.493  31.286  33.227  1.00 43.44           C  
ANISOU  771  CG  PRO A  96     3032   5834   7637   -501   -253    182       C  
ATOM    772  CD  PRO A  96     -48.182  31.073  31.761  1.00 43.00           C  
ANISOU  772  CD  PRO A  96     3039   5674   7624   -462   -311    192       C  
ATOM    773  N   GLN A  97     -49.304  35.449  32.784  1.00 44.49           N  
ANISOU  773  N   GLN A  97     2961   6083   7859   -154   -209     -2       N  
ATOM    774  CA  GLN A  97     -48.755  36.643  33.466  1.00 45.26           C  
ANISOU  774  CA  GLN A  97     3071   6170   7954    -57   -189    -46       C  
ATOM    775  C   GLN A  97     -48.537  36.236  34.921  1.00 45.18           C  
ANISOU  775  C   GLN A  97     3068   6209   7886   -117   -138    -31       C  
ATOM    776  O   GLN A  97     -49.459  35.643  35.512  1.00 45.99           O  
ANISOU  776  O   GLN A  97     3097   6429   7948   -194   -102    -25       O  
ATOM    777  CB  GLN A  97     -49.726  37.821  33.368  1.00 47.01           C  
ANISOU  777  CB  GLN A  97     3200   6475   8185     43   -189   -117       C  
ATOM    778  CG  GLN A  97     -50.061  38.218  31.935  1.00 47.93           C  
ANISOU  778  CG  GLN A  97     3312   6545   8354     98   -248   -132       C  
ATOM    779  CD  GLN A  97     -48.876  38.841  31.248  1.00 48.73           C  
ANISOU  779  CD  GLN A  97     3523   6502   8487    158   -289   -124       C  
ATOM    780  OE1 GLN A  97     -48.303  39.804  31.758  1.00 50.75           O  
ANISOU  780  OE1 GLN A  97     3816   6726   8738    226   -289   -151       O  
ATOM    781  NE2 GLN A  97     -48.484  38.283  30.108  1.00 48.87           N  
ANISOU  781  NE2 GLN A  97     3599   6435   8534    127   -325    -83       N  
ATOM    782  N   VAL A  98     -47.362  36.519  35.469  1.00 44.05           N  
ANISOU  782  N   VAL A  98     3011   5984   7739    -93   -138    -22       N  
ATOM    783  CA  VAL A  98     -47.039  36.240  36.895  1.00 44.49           C  
ANISOU  783  CA  VAL A  98     3092   6072   7739   -142    -98    -11       C  
ATOM    784  C   VAL A  98     -46.325  37.477  37.454  1.00 44.11           C  
ANISOU  784  C   VAL A  98     3085   5981   7692    -45   -101    -49       C  
ATOM    785  O   VAL A  98     -45.146  37.713  37.083  1.00 43.31           O  
ANISOU  785  O   VAL A  98     3065   5763   7627    -18   -139    -26       O  
ATOM    786  CB  VAL A  98     -46.203  34.946  37.025  1.00 44.43           C  
ANISOU  786  CB  VAL A  98     3172   5986   7721   -243   -114     58       C  
ATOM    787  CG1 VAL A  98     -45.950  34.559  38.475  1.00 44.63           C  
ANISOU  787  CG1 VAL A  98     3230   6042   7684   -306    -81     74       C  
ATOM    788  CG2 VAL A  98     -46.840  33.783  36.272  1.00 44.31           C  
ANISOU  788  CG2 VAL A  98     3141   5984   7707   -331   -133     96       C  
ATOM    789  N   ASN A  99     -47.030  38.262  38.274  1.00 44.26           N  
ANISOU  789  N   ASN A  99     3050   6096   7670      7    -66   -105       N  
ATOM    790  CA  ASN A  99     -46.469  39.457  38.959  1.00 43.83           C  
ANISOU  790  CA  ASN A  99     3047   6003   7601     99    -75   -147       C  
ATOM    791  C   ASN A  99     -45.866  40.404  37.909  1.00 42.91           C  
ANISOU  791  C   ASN A  99     2977   5779   7547    185   -140   -158       C  
ATOM    792  O   ASN A  99     -44.784  40.983  38.168  1.00 42.97           O  
ANISOU  792  O   ASN A  99     3070   5691   7562    212   -174   -148       O  
ATOM    793  CB  ASN A  99     -45.453  39.036  40.023  1.00 43.59           C  
ANISOU  793  CB  ASN A  99     3104   5920   7537     40    -68   -108       C  
ATOM    794  CG  ASN A  99     -45.326  40.048  41.139  1.00 44.13           C  
ANISOU  794  CG  ASN A  99     3207   6003   7556    110    -59   -156       C  
ATOM    795  OD1 ASN A  99     -46.326  40.484  41.712  1.00 45.43           O  
ANISOU  795  OD1 ASN A  99     3308   6281   7669    156    -16   -213       O  
ATOM    796  ND2 ASN A  99     -44.102  40.409  41.476  1.00 43.48           N  
ANISOU  796  ND2 ASN A  99     3225   5810   7485    119   -102   -133       N  
ATOM    797  N   GLY A 100     -46.545  40.542  36.768  1.00 42.55           N  
ANISOU  797  N   GLY A 100     2877   5747   7540    218   -161   -175       N  
ATOM    798  CA  GLY A 100     -46.266  41.538  35.720  1.00 41.97           C  
ANISOU  798  CA  GLY A 100     2839   5591   7514    302   -223   -194       C  
ATOM    799  C   GLY A 100     -45.522  40.946  34.542  1.00 41.16           C  
ANISOU  799  C   GLY A 100     2781   5394   7462    254   -254   -135       C  
ATOM    800  O   GLY A 100     -45.375  41.667  33.530  1.00 41.74           O  
ANISOU  800  O   GLY A 100     2881   5405   7571    309   -303   -145       O  
ATOM    801  N   LEU A 101     -45.081  39.690  34.662  1.00 40.54           N  
ANISOU  801  N   LEU A 101     2718   5304   7379    159   -231    -78       N  
ATOM    802  CA  LEU A 101     -44.058  39.076  33.778  1.00 39.51           C  
ANISOU  802  CA  LEU A 101     2651   5077   7284    123   -256    -20       C  
ATOM    803  C   LEU A 101     -44.640  37.861  33.064  1.00 39.70           C  
ANISOU  803  C   LEU A 101     2648   5122   7313     58   -250      6       C  
ATOM    804  O   LEU A 101     -45.383  37.094  33.704  1.00 40.28           O  
ANISOU  804  O   LEU A 101     2678   5274   7353     -5   -220      9       O  
ATOM    805  CB  LEU A 101     -42.854  38.662  34.624  1.00 38.91           C  
ANISOU  805  CB  LEU A 101     2637   4952   7194     81   -248     21       C  
ATOM    806  CG  LEU A 101     -42.127  39.811  35.299  1.00 38.72           C  
ANISOU  806  CG  LEU A 101     2654   4890   7166    131   -266      5       C  
ATOM    807  CD1 LEU A 101     -41.266  39.270  36.425  1.00 38.97           C  
ANISOU  807  CD1 LEU A 101     2729   4902   7173     80   -255     39       C  
ATOM    808  CD2 LEU A 101     -41.294  40.594  34.297  1.00 38.39           C  
ANISOU  808  CD2 LEU A 101     2655   4764   7167    174   -313     20       C  
ATOM    809  N   THR A 102     -44.268  37.682  31.797  1.00 39.53           N  
ANISOU  809  N   THR A 102     2662   5032   7324     68   -282     29       N  
ATOM    810  CA  THR A 102     -44.617  36.486  31.003  1.00 39.84           C  
ANISOU  810  CA  THR A 102     2707   5063   7366     10   -291     60       C  
ATOM    811  C   THR A 102     -43.674  35.351  31.408  1.00 39.90           C  
ANISOU  811  C   THR A 102     2780   5023   7357    -49   -284    111       C  
ATOM    812  O   THR A 102     -42.472  35.423  31.112  1.00 38.91           O  
ANISOU  812  O   THR A 102     2712   4823   7247    -21   -293    135       O  
ATOM    813  CB  THR A 102     -44.578  36.763  29.499  1.00 39.81           C  
ANISOU  813  CB  THR A 102     2729   5002   7396     53   -328     61       C  
ATOM    814  OG1 THR A 102     -45.389  37.900  29.192  1.00 40.28           O  
ANISOU  814  OG1 THR A 102     2738   5095   7470    117   -347     11       O  
ATOM    815  CG2 THR A 102     -45.092  35.583  28.708  1.00 40.11           C  
ANISOU  815  CG2 THR A 102     2779   5032   7429     -2   -347     86       C  
ATOM    816  N   SER A 103     -44.226  34.344  32.078  1.00 40.90           N  
ANISOU  816  N   SER A 103     2895   5197   7448   -131   -270    128       N  
ATOM    817  CA  SER A 103     -43.549  33.083  32.457  1.00 40.85           C  
ANISOU  817  CA  SER A 103     2960   5142   7416   -196   -278    175       C  
ATOM    818  C   SER A 103     -43.963  31.986  31.471  1.00 41.73           C  
ANISOU  818  C   SER A 103     3108   5223   7524   -242   -314    201       C  
ATOM    819  O   SER A 103     -44.467  32.317  30.375  1.00 42.71           O  
ANISOU  819  O   SER A 103     3210   5343   7673   -208   -332    185       O  
ATOM    820  CB  SER A 103     -43.893  32.727  33.870  1.00 41.05           C  
ANISOU  820  CB  SER A 103     2969   5231   7395   -266   -251    180       C  
ATOM    821  OG  SER A 103     -43.075  31.675  34.330  1.00 41.06           O  
ANISOU  821  OG  SER A 103     3055   5172   7374   -317   -269    222       O  
ATOM    822  N   ILE A 104     -43.749  30.722  31.829  1.00 42.31           N  
ANISOU  822  N   ILE A 104     3247   5264   7563   -315   -334    239       N  
ATOM    823  CA  ILE A 104     -44.254  29.549  31.057  1.00 43.35           C  
ANISOU  823  CA  ILE A 104     3431   5363   7677   -376   -380    267       C  
ATOM    824  C   ILE A 104     -44.652  28.462  32.058  1.00 44.23           C  
ANISOU  824  C   ILE A 104     3572   5499   7733   -496   -392    301       C  
ATOM    825  O   ILE A 104     -43.842  28.182  32.957  1.00 45.57           O  
ANISOU  825  O   ILE A 104     3792   5638   7882   -505   -387    316       O  
ATOM    826  CB  ILE A 104     -43.196  29.032  30.064  1.00 43.16           C  
ANISOU  826  CB  ILE A 104     3508   5225   7664   -317   -416    283       C  
ATOM    827  CG1 ILE A 104     -42.340  30.161  29.484  1.00 43.11           C  
ANISOU  827  CG1 ILE A 104     3482   5196   7702   -206   -391    259       C  
ATOM    828  CG2 ILE A 104     -43.856  28.200  28.977  1.00 43.36           C  
ANISOU  828  CG2 ILE A 104     3582   5215   7677   -351   -468    296       C  
ATOM    829  CD1 ILE A 104     -41.258  29.694  28.528  1.00 42.97           C  
ANISOU  829  CD1 ILE A 104     3548   5089   7688   -142   -412    274       C  
ATOM    830  N   LYS A 105     -45.842  27.877  31.914  1.00 44.31           N  
ANISOU  830  N   LYS A 105     3554   5561   7718   -591   -413    317       N  
ATOM    831  CA  LYS A 105     -46.239  26.670  32.683  1.00 44.92           C  
ANISOU  831  CA  LYS A 105     3682   5651   7734   -729   -441    363       C  
ATOM    832  C   LYS A 105     -45.194  25.590  32.368  1.00 44.45           C  
ANISOU  832  C   LYS A 105     3780   5451   7658   -721   -505    394       C  
ATOM    833  O   LYS A 105     -44.754  25.519  31.186  1.00 43.67           O  
ANISOU  833  O   LYS A 105     3733   5271   7586   -642   -537    385       O  
ATOM    834  CB  LYS A 105     -47.672  26.247  32.326  1.00 45.55           C  
ANISOU  834  CB  LYS A 105     3702   5807   7795   -834   -465    381       C  
ATOM    835  CG  LYS A 105     -48.239  25.048  33.078  1.00 46.59           C  
ANISOU  835  CG  LYS A 105     3878   5966   7857  -1001   -498    437       C  
ATOM    836  CD  LYS A 105     -49.682  24.762  32.675  1.00 47.85           C  
ANISOU  836  CD  LYS A 105     3955   6220   8005  -1109   -520    458       C  
ATOM    837  CE  LYS A 105     -50.372  23.703  33.512  1.00 48.93           C  
ANISOU  837  CE  LYS A 105     4110   6412   8065  -1297   -545    520       C  
ATOM    838  NZ  LYS A 105     -50.270  22.366  32.879  1.00 49.39           N  
ANISOU  838  NZ  LYS A 105     4328   6345   8093  -1382   -656    574       N  
ATOM    839  N   TRP A 106     -44.771  24.809  33.367  1.00 44.02           N  
ANISOU  839  N   TRP A 106     3803   5366   7555   -788   -524    426       N  
ATOM    840  CA  TRP A 106     -43.676  23.830  33.157  1.00 43.97           C  
ANISOU  840  CA  TRP A 106     3949   5223   7533   -758   -590    447       C  
ATOM    841  C   TRP A 106     -44.106  22.787  32.118  1.00 44.76           C  
ANISOU  841  C   TRP A 106     4144   5250   7609   -799   -671    471       C  
ATOM    842  O   TRP A 106     -45.216  22.253  32.240  1.00 46.33           O  
ANISOU  842  O   TRP A 106     4335   5494   7771   -931   -700    501       O  
ATOM    843  CB  TRP A 106     -43.216  23.177  34.459  1.00 43.99           C  
ANISOU  843  CB  TRP A 106     4026   5203   7485   -827   -608    476       C  
ATOM    844  CG  TRP A 106     -41.983  22.372  34.213  1.00 43.90           C  
ANISOU  844  CG  TRP A 106     4156   5055   7467   -758   -673    484       C  
ATOM    845  CD1 TRP A 106     -40.691  22.785  34.352  1.00 43.76           C  
ANISOU  845  CD1 TRP A 106     4147   4994   7484   -639   -657    464       C  
ATOM    846  CD2 TRP A 106     -41.924  21.043  33.670  1.00 44.69           C  
ANISOU  846  CD2 TRP A 106     4406   5047   7525   -790   -771    512       C  
ATOM    847  NE1 TRP A 106     -39.832  21.793  33.971  1.00 43.96           N  
ANISOU  847  NE1 TRP A 106     4306   4903   7492   -588   -731    474       N  
ATOM    848  CE2 TRP A 106     -40.558  20.707  33.557  1.00 44.48           C  
ANISOU  848  CE2 TRP A 106     4471   4920   7509   -674   -805    500       C  
ATOM    849  CE3 TRP A 106     -42.886  20.101  33.286  1.00 45.06           C  
ANISOU  849  CE3 TRP A 106     4522   5072   7525   -907   -840    546       C  
ATOM    850  CZ2 TRP A 106     -40.136  19.465  33.080  1.00 44.79           C  
ANISOU  850  CZ2 TRP A 106     4674   4835   7508   -655   -904    514       C  
ATOM    851  CZ3 TRP A 106     -42.468  18.877  32.819  1.00 45.44           C  
ANISOU  851  CZ3 TRP A 106     4745   4986   7532   -901   -945    565       C  
ATOM    852  CH2 TRP A 106     -41.111  18.565  32.718  1.00 45.45           C  
ANISOU  852  CH2 TRP A 106     4841   4885   7540   -769   -976    545       C  
ATOM    853  N   ALA A 107     -43.232  22.504  31.150  1.00 44.57           N  
ANISOU  853  N   ALA A 107     4209   5120   7602   -691   -708    458       N  
ATOM    854  CA  ALA A 107     -43.449  21.561  30.031  1.00 45.04           C  
ANISOU  854  CA  ALA A 107     4384   5090   7638   -697   -791    472       C  
ATOM    855  C   ALA A 107     -42.121  21.342  29.298  1.00 45.38           C  
ANISOU  855  C   ALA A 107     4523   5027   7692   -547   -810    450       C  
ATOM    856  O   ALA A 107     -41.464  22.336  28.959  1.00 44.63           O  
ANISOU  856  O   ALA A 107     4349   4959   7647   -433   -744    417       O  
ATOM    857  CB  ALA A 107     -44.506  22.098  29.102  1.00 44.45           C  
ANISOU  857  CB  ALA A 107     4225   5073   7591   -713   -779    461       C  
ATOM    858  N   ASP A 108     -41.730  20.086  29.084  1.00 46.96           N  
ANISOU  858  N   ASP A 108     4888   5113   7842   -548   -900    467       N  
ATOM    859  CA  ASP A 108     -40.602  19.700  28.194  1.00 47.93           C  
ANISOU  859  CA  ASP A 108     5112   5136   7960   -397   -928    443       C  
ATOM    860  C   ASP A 108     -39.293  20.305  28.716  1.00 47.29           C  
ANISOU  860  C   ASP A 108     4976   5074   7916   -284   -867    421       C  
ATOM    861  O   ASP A 108     -38.522  20.861  27.888  1.00 47.24           O  
ANISOU  861  O   ASP A 108     4936   5070   7943   -151   -823    392       O  
ATOM    862  CB  ASP A 108     -40.895  20.120  26.751  1.00 48.54           C  
ANISOU  862  CB  ASP A 108     5172   5212   8059   -330   -915    419       C  
ATOM    863  CG  ASP A 108     -42.230  19.597  26.256  1.00 50.02           C  
ANISOU  863  CG  ASP A 108     5400   5387   8216   -449   -981    444       C  
ATOM    864  OD1 ASP A 108     -42.798  18.749  26.961  1.00 51.99           O  
ANISOU  864  OD1 ASP A 108     5715   5617   8422   -581  -1046    482       O  
ATOM    865  OD2 ASP A 108     -42.692  20.033  25.180  1.00 51.18           O  
ANISOU  865  OD2 ASP A 108     5518   5544   8383   -419   -972    428       O  
ATOM    866  N   ASN A 109     -39.058  20.190  30.029  1.00 46.60           N  
ANISOU  866  N   ASN A 109     4882   5003   7820   -341   -867    439       N  
ATOM    867  CA  ASN A 109     -37.832  20.680  30.714  1.00 45.48           C  
ANISOU  867  CA  ASN A 109     4695   4875   7710   -254   -825    426       C  
ATOM    868  C   ASN A 109     -37.562  22.142  30.355  1.00 44.96           C  
ANISOU  868  C   ASN A 109     4476   4896   7711   -180   -726    401       C  
ATOM    869  O   ASN A 109     -36.381  22.446  30.103  1.00 45.10           O  
ANISOU  869  O   ASN A 109     4475   4904   7756    -61   -702    385       O  
ATOM    870  CB  ASN A 109     -36.606  19.864  30.308  1.00 45.19           C  
ANISOU  870  CB  ASN A 109     4772   4741   7655   -126   -880    413       C  
ATOM    871  CG  ASN A 109     -36.755  18.410  30.666  1.00 45.87           C  
ANISOU  871  CG  ASN A 109     5035   4721   7671   -185   -995    435       C  
ATOM    872  OD1 ASN A 109     -36.984  18.099  31.826  1.00 45.75           O  
ANISOU  872  OD1 ASN A 109     5047   4705   7631   -290  -1024    463       O  
ATOM    873  ND2 ASN A 109     -36.612  17.534  29.686  1.00 46.63           N  
ANISOU  873  ND2 ASN A 109     5261   4726   7729   -117  -1064    423       N  
ATOM    874  N   ASN A 110     -38.595  22.999  30.339  1.00 44.26           N  
ANISOU  874  N   ASN A 110     4282   4890   7644   -247   -677    397       N  
ATOM    875  CA  ASN A 110     -38.519  24.379  29.772  1.00 42.79           C  
ANISOU  875  CA  ASN A 110     3972   4772   7514   -180   -601    372       C  
ATOM    876  C   ASN A 110     -38.270  25.421  30.872  1.00 41.40           C  
ANISOU  876  C   ASN A 110     3695   4667   7369   -191   -544    368       C  
ATOM    877  O   ASN A 110     -38.264  26.611  30.537  1.00 39.85           O  
ANISOU  877  O   ASN A 110     3405   4522   7214   -147   -491    349       O  
ATOM    878  CB  ASN A 110     -39.773  24.751  28.972  1.00 43.17           C  
ANISOU  878  CB  ASN A 110     3974   4858   7568   -224   -593    363       C  
ATOM    879  CG  ASN A 110     -41.032  24.831  29.814  1.00 43.30           C  
ANISOU  879  CG  ASN A 110     3933   4948   7570   -352   -588    375       C  
ATOM    880  OD1 ASN A 110     -41.030  24.524  31.006  1.00 42.73           O  
ANISOU  880  OD1 ASN A 110     3869   4892   7473   -421   -590    392       O  
ATOM    881  ND2 ASN A 110     -42.127  25.219  29.186  1.00 43.96           N  
ANISOU  881  ND2 ASN A 110     3958   5079   7665   -385   -582    366       N  
ATOM    882  N   CYS A 111     -38.061  24.992  32.121  1.00 41.29           N  
ANISOU  882  N   CYS A 111     3711   4646   7330   -247   -562    385       N  
ATOM    883  CA  CYS A 111     -37.787  25.874  33.286  1.00 41.03           C  
ANISOU  883  CA  CYS A 111     3604   4669   7315   -261   -518    382       C  
ATOM    884  C   CYS A 111     -36.643  26.858  32.968  1.00 40.80           C  
ANISOU  884  C   CYS A 111     3517   4645   7338   -151   -483    369       C  
ATOM    885  O   CYS A 111     -36.695  28.008  33.473  1.00 41.08           O  
ANISOU  885  O   CYS A 111     3470   4738   7400   -152   -439    357       O  
ATOM    886  CB  CYS A 111     -37.474  25.040  34.523  1.00 41.61           C  
ANISOU  886  CB  CYS A 111     3755   4708   7346   -323   -560    407       C  
ATOM    887  SG  CYS A 111     -35.977  24.029  34.364  1.00 41.72           S  
ANISOU  887  SG  CYS A 111     3880   4614   7356   -231   -627    417       S  
ATOM    888  N   TYR A 112     -35.667  26.461  32.140  1.00 40.18           N  
ANISOU  888  N   TYR A 112     3478   4516   7272    -61   -501    370       N  
ATOM    889  CA  TYR A 112     -34.493  27.303  31.784  1.00 39.29           C  
ANISOU  889  CA  TYR A 112     3305   4419   7204     33   -469    367       C  
ATOM    890  C   TYR A 112     -34.914  28.387  30.790  1.00 38.92           C  
ANISOU  890  C   TYR A 112     3186   4415   7186     59   -423    351       C  
ATOM    891  O   TYR A 112     -34.415  29.506  30.917  1.00 39.30           O  
ANISOU  891  O   TYR A 112     3162   4499   7268     83   -390    351       O  
ATOM    892  CB  TYR A 112     -33.320  26.456  31.282  1.00 39.10           C  
ANISOU  892  CB  TYR A 112     3339   4343   7174    125   -499    373       C  
ATOM    893  CG  TYR A 112     -33.364  26.051  29.831  1.00 38.65           C  
ANISOU  893  CG  TYR A 112     3319   4262   7104    191   -499    360       C  
ATOM    894  CD1 TYR A 112     -32.542  26.644  28.885  1.00 37.98           C  
ANISOU  894  CD1 TYR A 112     3181   4205   7043    282   -458    356       C  
ATOM    895  CD2 TYR A 112     -34.217  25.051  29.406  1.00 38.76           C  
ANISOU  895  CD2 TYR A 112     3427   4223   7074    156   -544    356       C  
ATOM    896  CE1 TYR A 112     -32.574  26.253  27.557  1.00 37.89           C  
ANISOU  896  CE1 TYR A 112     3214   4172   7009    345   -456    343       C  
ATOM    897  CE2 TYR A 112     -34.266  24.647  28.083  1.00 38.62           C  
ANISOU  897  CE2 TYR A 112     3460   4174   7036    219   -552    343       C  
ATOM    898  CZ  TYR A 112     -33.438  25.242  27.155  1.00 38.40           C  
ANISOU  898  CZ  TYR A 112     3383   4175   7029    319   -505    334       C  
ATOM    899  OH  TYR A 112     -33.531  24.800  25.866  1.00 38.34           O  
ANISOU  899  OH  TYR A 112     3439   4136   6992    379   -512    320       O  
ATOM    900  N   LEU A 113     -35.805  28.070  29.854  1.00 39.47           N  
ANISOU  900  N   LEU A 113     3281   4475   7239     47   -430    340       N  
ATOM    901  CA  LEU A 113     -36.396  29.062  28.905  1.00 39.95           C  
ANISOU  901  CA  LEU A 113     3285   4570   7323     62   -398    323       C  
ATOM    902  C   LEU A 113     -37.277  30.063  29.664  1.00 39.34           C  
ANISOU  902  C   LEU A 113     3132   4552   7260      6   -375    309       C  
ATOM    903  O   LEU A 113     -37.193  31.266  29.389  1.00 38.58           O  
ANISOU  903  O   LEU A 113     2977   4486   7193     37   -348    298       O  
ATOM    904  CB  LEU A 113     -37.240  28.345  27.847  1.00 40.85           C  
ANISOU  904  CB  LEU A 113     3456   4653   7410     53   -425    316       C  
ATOM    905  CG  LEU A 113     -36.466  27.726  26.688  1.00 41.78           C  
ANISOU  905  CG  LEU A 113     3643   4719   7512    137   -437    317       C  
ATOM    906  CD1 LEU A 113     -37.424  27.221  25.632  1.00 42.47           C  
ANISOU  906  CD1 LEU A 113     3788   4774   7573    122   -469    309       C  
ATOM    907  CD2 LEU A 113     -35.477  28.709  26.083  1.00 41.90           C  
ANISOU  907  CD2 LEU A 113     3600   4763   7556    216   -389    317       C  
ATOM    908  N   ALA A 114     -38.115  29.578  30.575  1.00 39.62           N  
ANISOU  908  N   ALA A 114     3175   4608   7270    -74   -387    310       N  
ATOM    909  CA  ALA A 114     -38.922  30.424  31.481  1.00 39.44           C  
ANISOU  909  CA  ALA A 114     3081   4654   7248   -120   -360    293       C  
ATOM    910  C   ALA A 114     -37.986  31.416  32.182  1.00 38.14           C  
ANISOU  910  C   ALA A 114     2882   4498   7108    -81   -339    291       C  
ATOM    911  O   ALA A 114     -38.257  32.617  32.124  1.00 37.96           O  
ANISOU  911  O   ALA A 114     2804   4511   7108    -56   -319    269       O  
ATOM    912  CB  ALA A 114     -39.684  29.569  32.475  1.00 40.26           C  
ANISOU  912  CB  ALA A 114     3206   4781   7308   -216   -373    304       C  
ATOM    913  N   THR A 115     -36.914  30.923  32.803  1.00 37.47           N  
ANISOU  913  N   THR A 115     2839   4377   7020    -73   -355    314       N  
ATOM    914  CA  THR A 115     -35.982  31.733  33.637  1.00 36.45           C  
ANISOU  914  CA  THR A 115     2685   4252   6910    -52   -348    321       C  
ATOM    915  C   THR A 115     -35.308  32.794  32.758  1.00 35.28           C  
ANISOU  915  C   THR A 115     2496   4105   6803     13   -335    320       C  
ATOM    916  O   THR A 115     -35.283  33.974  33.173  1.00 34.66           O  
ANISOU  916  O   THR A 115     2380   4048   6739     16   -327    310       O  
ATOM    917  CB  THR A 115     -35.012  30.827  34.395  1.00 35.99           C  
ANISOU  917  CB  THR A 115     2682   4151   6839    -59   -379    348       C  
ATOM    918  OG1 THR A 115     -35.819  30.010  35.238  1.00 36.55           O  
ANISOU  918  OG1 THR A 115     2796   4226   6863   -138   -392    349       O  
ATOM    919  CG2 THR A 115     -34.031  31.600  35.240  1.00 35.91           C  
ANISOU  919  CG2 THR A 115     2649   4142   6850    -43   -383    359       C  
ATOM    920  N   ALA A 116     -34.835  32.400  31.576  1.00 34.64           N  
ANISOU  920  N   ALA A 116     2429   4000   6732     59   -336    331       N  
ATOM    921  CA  ALA A 116     -34.325  33.328  30.542  1.00 34.72           C  
ANISOU  921  CA  ALA A 116     2405   4017   6769    110   -320    335       C  
ATOM    922  C   ALA A 116     -35.360  34.423  30.271  1.00 34.66           C  
ANISOU  922  C   ALA A 116     2364   4034   6768     98   -312    307       C  
ATOM    923  O   ALA A 116     -35.006  35.614  30.347  1.00 35.00           O  
ANISOU  923  O   ALA A 116     2379   4087   6832    109   -312    309       O  
ATOM    924  CB  ALA A 116     -33.999  32.579  29.279  1.00 35.04           C  
ANISOU  924  CB  ALA A 116     2476   4035   6801    157   -317    342       C  
ATOM    925  N   LEU A 117     -36.591  34.018  29.957  1.00 34.64           N  
ANISOU  925  N   LEU A 117     2370   4041   6750     75   -313    283       N  
ATOM    926  CA  LEU A 117     -37.682  34.900  29.477  1.00 34.43           C  
ANISOU  926  CA  LEU A 117     2311   4040   6729     78   -312    252       C  
ATOM    927  C   LEU A 117     -38.023  35.926  30.563  1.00 34.26           C  
ANISOU  927  C   LEU A 117     2252   4053   6710     68   -309    229       C  
ATOM    928  O   LEU A 117     -38.221  37.102  30.230  1.00 33.67           O  
ANISOU  928  O   LEU A 117     2158   3982   6650     99   -318    210       O  
ATOM    929  CB  LEU A 117     -38.875  34.011  29.129  1.00 35.14           C  
ANISOU  929  CB  LEU A 117     2410   4140   6799     44   -321    238       C  
ATOM    930  CG  LEU A 117     -40.089  34.715  28.532  1.00 35.65           C  
ANISOU  930  CG  LEU A 117     2436   4235   6871     51   -328    205       C  
ATOM    931  CD1 LEU A 117     -39.696  35.461  27.271  1.00 35.77           C  
ANISOU  931  CD1 LEU A 117     2466   4218   6907    105   -336    205       C  
ATOM    932  CD2 LEU A 117     -41.202  33.713  28.240  1.00 35.95           C  
ANISOU  932  CD2 LEU A 117     2479   4289   6890      3   -343    201       C  
ATOM    933  N   LEU A 118     -38.080  35.489  31.819  1.00 34.59           N  
ANISOU  933  N   LEU A 118     2296   4114   6732     29   -303    230       N  
ATOM    934  CA  LEU A 118     -38.419  36.348  32.983  1.00 35.06           C  
ANISOU  934  CA  LEU A 118     2332   4209   6781     23   -298    205       C  
ATOM    935  C   LEU A 118     -37.304  37.382  33.176  1.00 34.98           C  
ANISOU  935  C   LEU A 118     2333   4166   6792     55   -315    219       C  
ATOM    936  O   LEU A 118     -37.627  38.568  33.367  1.00 34.73           O  
ANISOU  936  O   LEU A 118     2291   4144   6762     81   -326    190       O  
ATOM    937  CB  LEU A 118     -38.618  35.459  34.216  1.00 35.53           C  
ANISOU  937  CB  LEU A 118     2404   4291   6803    -34   -287    212       C  
ATOM    938  CG  LEU A 118     -39.924  34.657  34.213  1.00 36.24           C  
ANISOU  938  CG  LEU A 118     2473   4432   6863    -85   -272    198       C  
ATOM    939  CD1 LEU A 118     -39.838  33.447  35.136  1.00 36.60           C  
ANISOU  939  CD1 LEU A 118     2560   4476   6869   -158   -274    226       C  
ATOM    940  CD2 LEU A 118     -41.118  35.544  34.592  1.00 36.54           C  
ANISOU  940  CD2 LEU A 118     2448   4548   6887    -73   -251    150       C  
ATOM    941  N   THR A 119     -36.044  36.941  33.082  1.00 35.29           N  
ANISOU  941  N   THR A 119     2393   4168   6845     54   -323    261       N  
ATOM    942  CA  THR A 119     -34.816  37.782  33.169  1.00 35.27           C  
ANISOU  942  CA  THR A 119     2392   4140   6866     69   -344    290       C  
ATOM    943  C   THR A 119     -34.809  38.833  32.053  1.00 35.71           C  
ANISOU  943  C   THR A 119     2440   4187   6941     99   -354    288       C  
ATOM    944  O   THR A 119     -34.602  40.018  32.369  1.00 36.40           O  
ANISOU  944  O   THR A 119     2535   4263   7033    102   -383    285       O  
ATOM    945  CB  THR A 119     -33.551  36.925  33.097  1.00 34.72           C  
ANISOU  945  CB  THR A 119     2329   4051   6809     69   -347    335       C  
ATOM    946  OG1 THR A 119     -33.627  35.938  34.121  1.00 34.71           O  
ANISOU  946  OG1 THR A 119     2353   4048   6787     39   -349    336       O  
ATOM    947  CG2 THR A 119     -32.296  37.740  33.276  1.00 34.98           C  
ANISOU  947  CG2 THR A 119     2349   4073   6867     71   -370    371       C  
ATOM    948  N   LEU A 120     -35.027  38.417  30.802  1.00 36.03           N  
ANISOU  948  N   LEU A 120     2477   4226   6986    116   -340    290       N  
ATOM    949  CA  LEU A 120     -34.932  39.292  29.597  1.00 36.59           C  
ANISOU  949  CA  LEU A 120     2550   4283   7067    139   -351    296       C  
ATOM    950  C   LEU A 120     -35.910  40.470  29.711  1.00 37.13           C  
ANISOU  950  C   LEU A 120     2624   4350   7132    152   -379    254       C  
ATOM    951  O   LEU A 120     -35.619  41.533  29.129  1.00 37.42           O  
ANISOU  951  O   LEU A 120     2679   4363   7175    161   -408    263       O  
ATOM    952  CB  LEU A 120     -35.195  38.460  28.337  1.00 36.44           C  
ANISOU  952  CB  LEU A 120     2539   4262   7043    156   -330    298       C  
ATOM    953  CG  LEU A 120     -34.049  37.528  27.932  1.00 36.10           C  
ANISOU  953  CG  LEU A 120     2500   4218   6999    167   -308    338       C  
ATOM    954  CD1 LEU A 120     -34.547  36.377  27.070  1.00 35.99           C  
ANISOU  954  CD1 LEU A 120     2513   4194   6966    186   -294    327       C  
ATOM    955  CD2 LEU A 120     -32.937  38.289  27.229  1.00 36.05           C  
ANISOU  955  CD2 LEU A 120     2479   4215   7001    175   -305    377       C  
ATOM    956  N   GLN A 121     -37.005  40.297  30.448  1.00 37.62           N  
ANISOU  956  N   GLN A 121     2673   4440   7180    154   -373    209       N  
ATOM    957  CA  GLN A 121     -38.039  41.335  30.678  1.00 38.37           C  
ANISOU  957  CA  GLN A 121     2764   4547   7266    186   -397    157       C  
ATOM    958  C   GLN A 121     -37.574  42.355  31.732  1.00 39.13           C  
ANISOU  958  C   GLN A 121     2886   4626   7353    191   -427    152       C  
ATOM    959  O   GLN A 121     -38.322  43.334  31.961  1.00 40.17           O  
ANISOU  959  O   GLN A 121     3029   4760   7473    233   -457    104       O  
ATOM    960  CB  GLN A 121     -39.346  40.673  31.127  1.00 38.65           C  
ANISOU  960  CB  GLN A 121     2759   4640   7284    183   -370    115       C  
ATOM    961  CG  GLN A 121     -40.016  39.852  30.043  1.00 38.80           C  
ANISOU  961  CG  GLN A 121     2761   4670   7309    177   -360    115       C  
ATOM    962  CD  GLN A 121     -41.149  39.023  30.591  1.00 39.37           C  
ANISOU  962  CD  GLN A 121     2790   4806   7362    148   -335     91       C  
ATOM    963  OE1 GLN A 121     -42.145  39.534  31.089  1.00 39.63           O  
ANISOU  963  OE1 GLN A 121     2780   4893   7382    169   -333     45       O  
ATOM    964  NE2 GLN A 121     -41.003  37.716  30.487  1.00 40.09           N  
ANISOU  964  NE2 GLN A 121     2891   4894   7444    100   -318    122       N  
ATOM    965  N   GLN A 122     -36.423  42.145  32.379  1.00 38.92           N  
ANISOU  965  N   GLN A 122     2873   4582   7331    158   -428    195       N  
ATOM    966  CA  GLN A 122     -36.001  42.949  33.555  1.00 39.71           C  
ANISOU  966  CA  GLN A 122     3006   4663   7417    154   -462    192       C  
ATOM    967  C   GLN A 122     -34.604  43.550  33.379  1.00 40.01           C  
ANISOU  967  C   GLN A 122     3070   4655   7474    125   -502    250       C  
ATOM    968  O   GLN A 122     -34.126  44.160  34.340  1.00 39.77           O  
ANISOU  968  O   GLN A 122     3075   4601   7434    112   -540    257       O  
ATOM    969  CB  GLN A 122     -35.985  42.066  34.796  1.00 40.29           C  
ANISOU  969  CB  GLN A 122     3072   4764   7472    127   -432    191       C  
ATOM    970  CG  GLN A 122     -37.351  41.537  35.192  1.00 40.92           C  
ANISOU  970  CG  GLN A 122     3121   4902   7521    137   -392    139       C  
ATOM    971  CD  GLN A 122     -37.209  40.634  36.388  1.00 41.68           C  
ANISOU  971  CD  GLN A 122     3223   5021   7592     94   -367    150       C  
ATOM    972  OE1 GLN A 122     -36.777  41.060  37.464  1.00 42.00           O  
ANISOU  972  OE1 GLN A 122     3299   5047   7612     88   -386    150       O  
ATOM    973  NE2 GLN A 122     -37.561  39.372  36.200  1.00 42.37           N  
ANISOU  973  NE2 GLN A 122     3287   5136   7674     60   -332    161       N  
ATOM    974  N   ILE A 123     -33.981  43.387  32.209  1.00 40.88           N  
ANISOU  974  N   ILE A 123     3165   4760   7607    112   -495    293       N  
ATOM    975  CA  ILE A 123     -32.628  43.929  31.880  1.00 42.19           C  
ANISOU  975  CA  ILE A 123     3337   4902   7788     75   -526    358       C  
ATOM    976  C   ILE A 123     -32.737  44.705  30.563  1.00 44.07           C  
ANISOU  976  C   ILE A 123     3594   5122   8027     78   -546    367       C  
ATOM    977  O   ILE A 123     -33.434  44.217  29.654  1.00 44.25           O  
ANISOU  977  O   ILE A 123     3604   5160   8049    106   -513    345       O  
ATOM    978  CB  ILE A 123     -31.551  42.818  31.830  1.00 41.52           C  
ANISOU  978  CB  ILE A 123     3205   4847   7723     53   -488    409       C  
ATOM    979  CG1 ILE A 123     -31.913  41.701  30.849  1.00 41.25           C  
ANISOU  979  CG1 ILE A 123     3143   4840   7690     80   -432    400       C  
ATOM    980  CG2 ILE A 123     -31.260  42.279  33.228  1.00 41.33           C  
ANISOU  980  CG2 ILE A 123     3180   4824   7696     39   -492    408       C  
ATOM    981  CD1 ILE A 123     -30.864  40.630  30.695  1.00 41.27           C  
ANISOU  981  CD1 ILE A 123     3108   4868   7704     79   -401    442       C  
ATOM    982  N   GLU A 124     -32.080  45.874  30.489  1.00 46.62           N  
ANISOU  982  N   GLU A 124     3957   5408   8347     44   -607    403       N  
ATOM    983  CA  GLU A 124     -32.017  46.759  29.290  1.00 47.77           C  
ANISOU  983  CA  GLU A 124     4138   5527   8485     29   -642    425       C  
ATOM    984  C   GLU A 124     -31.180  46.032  28.229  1.00 47.91           C  
ANISOU  984  C   GLU A 124     4101   5589   8512      2   -585    481       C  
ATOM    985  O   GLU A 124     -30.020  45.720  28.522  1.00 48.32           O  
ANISOU  985  O   GLU A 124     4109   5672   8576    -35   -571    536       O  
ATOM    986  CB  GLU A 124     -31.423  48.127  29.663  1.00 49.27           C  
ANISOU  986  CB  GLU A 124     4393   5662   8663    -17   -731    458       C  
ATOM    987  CG  GLU A 124     -32.225  49.340  29.185  1.00 51.12           C  
ANISOU  987  CG  GLU A 124     4715   5833   8872      5   -806    422       C  
ATOM    988  CD  GLU A 124     -33.092  50.063  30.227  1.00 52.95           C  
ANISOU  988  CD  GLU A 124     5013   6019   9084     63   -865    351       C  
ATOM    989  OE1 GLU A 124     -32.986  49.753  31.444  1.00 53.85           O  
ANISOU  989  OE1 GLU A 124     5114   6146   9199     70   -854    336       O  
ATOM    990  OE2 GLU A 124     -33.880  50.961  29.834  1.00 53.42           O  
ANISOU  990  OE2 GLU A 124     5144   6029   9124    106   -927    308       O  
ATOM    991  N   LEU A 125     -31.753  45.750  27.055  1.00 47.37           N  
ANISOU  991  N   LEU A 125     4036   5528   8435     29   -556    465       N  
ATOM    992  CA  LEU A 125     -31.112  44.930  25.992  1.00 47.77           C  
ANISOU  992  CA  LEU A 125     4044   5624   8483     24   -493    504       C  
ATOM    993  C   LEU A 125     -31.828  45.156  24.658  1.00 48.94           C  
ANISOU  993  C   LEU A 125     4232   5753   8610     42   -494    487       C  
ATOM    994  O   LEU A 125     -33.064  45.296  24.676  1.00 52.41           O  
ANISOU  994  O   LEU A 125     4705   6160   9048     83   -518    426       O  
ATOM    995  CB  LEU A 125     -31.202  43.460  26.399  1.00 47.24           C  
ANISOU  995  CB  LEU A 125     3928   5593   8428     63   -432    483       C  
ATOM    996  CG  LEU A 125     -30.269  42.523  25.644  1.00 47.45           C  
ANISOU  996  CG  LEU A 125     3908   5670   8450     71   -372    523       C  
ATOM    997  CD1 LEU A 125     -28.889  42.555  26.278  1.00 47.99           C  
ANISOU  997  CD1 LEU A 125     3923   5776   8535     36   -372    580       C  
ATOM    998  CD2 LEU A 125     -30.825  41.107  25.615  1.00 47.03           C  
ANISOU  998  CD2 LEU A 125     3847   5625   8395    123   -329    484       C  
ATOM    999  N   LYS A 126     -31.093  45.150  23.545  1.00 49.69           N  
ANISOU  999  N   LYS A 126     4321   5873   8685     16   -466    538       N  
ATOM   1000  CA  LYS A 126     -31.641  45.358  22.174  1.00 50.39           C  
ANISOU 1000  CA  LYS A 126     4459   5941   8746     26   -468    530       C  
ATOM   1001  C   LYS A 126     -31.018  44.328  21.228  1.00 50.40           C  
ANISOU 1001  C   LYS A 126     4423   5999   8727     41   -388    558       C  
ATOM   1002  O   LYS A 126     -29.787  44.326  21.097  1.00 51.63           O  
ANISOU 1002  O   LYS A 126     4533   6209   8874      5   -355    618       O  
ATOM   1003  CB  LYS A 126     -31.356  46.780  21.674  1.00 52.25           C  
ANISOU 1003  CB  LYS A 126     4756   6138   8956    -34   -534    569       C  
ATOM   1004  CG  LYS A 126     -32.122  47.890  22.388  1.00 53.95           C  
ANISOU 1004  CG  LYS A 126     5037   6280   9178    -30   -628    530       C  
ATOM   1005  CD  LYS A 126     -33.600  48.007  21.988  1.00 55.31           C  
ANISOU 1005  CD  LYS A 126     5259   6405   9348     35   -662    455       C  
ATOM   1006  CE  LYS A 126     -34.488  48.577  23.082  1.00 54.68           C  
ANISOU 1006  CE  LYS A 126     5204   6287   9285     80   -723    391       C  
ATOM   1007  NZ  LYS A 126     -35.846  48.854  22.560  1.00 54.81           N  
ANISOU 1007  NZ  LYS A 126     5261   6266   9297    143   -765    324       N  
ATOM   1008  N   PHE A 127     -31.834  43.481  20.601  1.00 49.71           N  
ANISOU 1008  N   PHE A 127     4354   5901   8630     95   -361    515       N  
ATOM   1009  CA  PHE A 127     -31.380  42.418  19.670  1.00 50.20           C  
ANISOU 1009  CA  PHE A 127     4403   6005   8664    128   -291    528       C  
ATOM   1010  C   PHE A 127     -31.066  43.034  18.306  1.00 50.21           C  
ANISOU 1010  C   PHE A 127     4447   6010   8618    100   -285    565       C  
ATOM   1011  O   PHE A 127     -31.784  43.932  17.856  1.00 50.82           O  
ANISOU 1011  O   PHE A 127     4590   6032   8685     78   -342    553       O  
ATOM   1012  CB  PHE A 127     -32.412  41.290  19.600  1.00 50.52           C  
ANISOU 1012  CB  PHE A 127     4464   6022   8709    187   -281    470       C  
ATOM   1013  CG  PHE A 127     -32.449  40.474  20.865  1.00 50.97           C  
ANISOU 1013  CG  PHE A 127     4476   6091   8798    205   -272    449       C  
ATOM   1014  CD1 PHE A 127     -31.362  39.699  21.233  1.00 51.73           C  
ANISOU 1014  CD1 PHE A 127     4525   6234   8896    220   -228    477       C  
ATOM   1015  CD2 PHE A 127     -33.540  40.531  21.718  1.00 50.93           C  
ANISOU 1015  CD2 PHE A 127     4476   6056   8818    205   -311    403       C  
ATOM   1016  CE1 PHE A 127     -31.376  38.971  22.411  1.00 51.76           C  
ANISOU 1016  CE1 PHE A 127     4501   6239   8925    231   -230    460       C  
ATOM   1017  CE2 PHE A 127     -33.559  39.797  22.892  1.00 50.49           C  
ANISOU 1017  CE2 PHE A 127     4387   6012   8782    210   -302    388       C  
ATOM   1018  CZ  PHE A 127     -32.475  39.022  23.237  1.00 51.27           C  
ANISOU 1018  CZ  PHE A 127     4454   6144   8882    220   -266    418       C  
ATOM   1019  N   ASN A 128     -29.996  42.559  17.681  1.00 51.42           N  
ANISOU 1019  N   ASN A 128     4564   6232   8740    103   -217    609       N  
ATOM   1020  CA  ASN A 128     -29.527  43.015  16.350  1.00 53.50           C  
ANISOU 1020  CA  ASN A 128     4861   6522   8945     72   -192    653       C  
ATOM   1021  C   ASN A 128     -30.401  42.383  15.270  1.00 54.45           C  
ANISOU 1021  C   ASN A 128     5056   6603   9030    128   -182    610       C  
ATOM   1022  O   ASN A 128     -30.771  43.066  14.321  1.00 56.68           O  
ANISOU 1022  O   ASN A 128     5410   6850   9274     99   -210    619       O  
ATOM   1023  CB  ASN A 128     -28.029  42.755  16.165  1.00 54.60           C  
ANISOU 1023  CB  ASN A 128     4916   6769   9060     59   -117    715       C  
ATOM   1024  CG  ASN A 128     -27.161  43.802  16.831  1.00 56.30           C  
ANISOU 1024  CG  ASN A 128     5078   7017   9293    -32   -147    779       C  
ATOM   1025  OD1 ASN A 128     -26.758  43.687  17.989  1.00 56.14           O  
ANISOU 1025  OD1 ASN A 128     4996   7013   9321    -36   -160    783       O  
ATOM   1026  ND2 ASN A 128     -26.779  44.803  16.058  1.00 58.73           N  
ANISOU 1026  ND2 ASN A 128     5416   7339   9558   -115   -160    836       N  
ATOM   1027  N   PRO A 129     -30.781  41.084  15.355  1.00 54.30           N  
ANISOU 1027  N   PRO A 129     5034   6579   9016    204   -152    564       N  
ATOM   1028  CA  PRO A 129     -31.738  40.514  14.408  1.00 53.54           C  
ANISOU 1028  CA  PRO A 129     5020   6431   8889    248   -162    523       C  
ATOM   1029  C   PRO A 129     -33.126  41.124  14.597  1.00 52.23           C  
ANISOU 1029  C   PRO A 129     4904   6184   8755    231   -247    481       C  
ATOM   1030  O   PRO A 129     -33.629  41.176  15.718  1.00 51.68           O  
ANISOU 1030  O   PRO A 129     4798   6099   8739    228   -281    454       O  
ATOM   1031  CB  PRO A 129     -31.735  39.004  14.709  1.00 53.61           C  
ANISOU 1031  CB  PRO A 129     5015   6451   8902    322   -127    490       C  
ATOM   1032  CG  PRO A 129     -30.512  38.776  15.564  1.00 54.19           C  
ANISOU 1032  CG  PRO A 129     4995   6598   8996    326    -81    521       C  
ATOM   1033  CD  PRO A 129     -30.278  40.076  16.296  1.00 54.41           C  
ANISOU 1033  CD  PRO A 129     4979   6632   9060    247   -117    555       C  
ATOM   1034  N   PRO A 130     -33.782  41.626  13.524  1.00 51.36           N  
ANISOU 1034  N   PRO A 130     4876   6024   8612    221   -286    474       N  
ATOM   1035  CA  PRO A 130     -35.187  42.014  13.601  1.00 51.00           C  
ANISOU 1035  CA  PRO A 130     4873   5907   8596    226   -368    425       C  
ATOM   1036  C   PRO A 130     -36.046  40.897  14.215  1.00 49.98           C  
ANISOU 1036  C   PRO A 130     4717   5768   8502    269   -373    374       C  
ATOM   1037  O   PRO A 130     -36.716  41.156  15.203  1.00 49.39           O  
ANISOU 1037  O   PRO A 130     4603   5685   8476    265   -411    345       O  
ATOM   1038  CB  PRO A 130     -35.579  42.261  12.136  1.00 51.55           C  
ANISOU 1038  CB  PRO A 130     5042   5933   8612    225   -393    427       C  
ATOM   1039  CG  PRO A 130     -34.281  42.628  11.454  1.00 51.78           C  
ANISOU 1039  CG  PRO A 130     5079   6011   8582    189   -335    491       C  
ATOM   1040  CD  PRO A 130     -33.215  41.848  12.188  1.00 51.91           C  
ANISOU 1040  CD  PRO A 130     5002   6109   8610    208   -253    511       C  
ATOM   1041  N   ALA A 131     -35.967  39.689  13.649  1.00 49.79           N  
ANISOU 1041  N   ALA A 131     4721   5749   8447    308   -335    368       N  
ATOM   1042  CA  ALA A 131     -36.720  38.489  14.089  1.00 50.04           C  
ANISOU 1042  CA  ALA A 131     4747   5765   8499    337   -345    330       C  
ATOM   1043  C   ALA A 131     -36.747  38.421  15.619  1.00 49.56           C  
ANISOU 1043  C   ALA A 131     4602   5733   8492    322   -344    320       C  
ATOM   1044  O   ALA A 131     -37.831  38.198  16.174  1.00 50.49           O  
ANISOU 1044  O   ALA A 131     4705   5836   8642    315   -385    285       O  
ATOM   1045  CB  ALA A 131     -36.111  37.236  13.506  1.00 50.55           C  
ANISOU 1045  CB  ALA A 131     4851   5840   8516    382   -295    337       C  
ATOM   1046  N   LEU A 132     -35.597  38.620  16.264  1.00 49.80           N  
ANISOU 1046  N   LEU A 132     4580   5810   8530    314   -300    352       N  
ATOM   1047  CA  LEU A 132     -35.436  38.515  17.740  1.00 50.05           C  
ANISOU 1047  CA  LEU A 132     4542   5869   8606    300   -296    348       C  
ATOM   1048  C   LEU A 132     -36.028  39.742  18.437  1.00 49.57           C  
ANISOU 1048  C   LEU A 132     4456   5796   8581    268   -346    333       C  
ATOM   1049  O   LEU A 132     -36.644  39.546  19.484  1.00 49.05           O  
ANISOU 1049  O   LEU A 132     4354   5736   8545    264   -362    305       O  
ATOM   1050  CB  LEU A 132     -33.957  38.365  18.110  1.00 50.52           C  
ANISOU 1050  CB  LEU A 132     4555   5979   8660    304   -242    390       C  
ATOM   1051  CG  LEU A 132     -33.430  36.934  18.195  1.00 51.23           C  
ANISOU 1051  CG  LEU A 132     4644   6086   8733    351   -203    389       C  
ATOM   1052  CD1 LEU A 132     -32.062  36.928  18.864  1.00 52.12           C  
ANISOU 1052  CD1 LEU A 132     4689   6257   8857    355   -163    425       C  
ATOM   1053  CD2 LEU A 132     -34.398  36.016  18.937  1.00 50.66           C  
ANISOU 1053  CD2 LEU A 132     4585   5982   8680    352   -234    351       C  
ATOM   1054  N   GLN A 133     -35.809  40.950  17.915  1.00 50.66           N  
ANISOU 1054  N   GLN A 133     4619   5921   8709    246   -370    353       N  
ATOM   1055  CA  GLN A 133     -36.328  42.200  18.539  1.00 51.85           C  
ANISOU 1055  CA  GLN A 133     4765   6048   8885    228   -430    335       C  
ATOM   1056  C   GLN A 133     -37.858  42.181  18.423  1.00 51.17           C  
ANISOU 1056  C   GLN A 133     4695   5933   8813    255   -481    277       C  
ATOM   1057  O   GLN A 133     -38.533  42.308  19.475  1.00 51.35           O  
ANISOU 1057  O   GLN A 133     4674   5968   8866    264   -501    240       O  
ATOM   1058  CB  GLN A 133     -35.673  43.445  17.923  1.00 53.75           C  
ANISOU 1058  CB  GLN A 133     5048   6270   9102    191   -456    375       C  
ATOM   1059  CG  GLN A 133     -35.991  44.751  18.653  1.00 54.68           C  
ANISOU 1059  CG  GLN A 133     5178   6356   9239    176   -528    361       C  
ATOM   1060  CD  GLN A 133     -35.522  44.789  20.091  1.00 55.24           C  
ANISOU 1060  CD  GLN A 133     5193   6454   9340    165   -517    364       C  
ATOM   1061  OE1 GLN A 133     -34.451  44.301  20.430  1.00 56.03           O  
ANISOU 1061  OE1 GLN A 133     5249   6596   9440    142   -466    406       O  
ATOM   1062  NE2 GLN A 133     -36.315  45.393  20.959  1.00 55.84           N  
ANISOU 1062  NE2 GLN A 133     5270   6509   9437    186   -569    318       N  
ATOM   1063  N   ASP A 134     -38.384  41.965  17.209  1.00 50.54           N  
ANISOU 1063  N   ASP A 134     4669   5822   8710    268   -498    269       N  
ATOM   1064  CA  ASP A 134     -39.843  41.828  16.944  1.00 49.66           C  
ANISOU 1064  CA  ASP A 134     4566   5688   8613    292   -551    219       C  
ATOM   1065  C   ASP A 134     -40.436  40.884  17.996  1.00 48.54           C  
ANISOU 1065  C   ASP A 134     4356   5587   8499    294   -531    191       C  
ATOM   1066  O   ASP A 134     -41.301  41.331  18.756  1.00 49.45           O  
ANISOU 1066  O   ASP A 134     4426   5720   8642    305   -564    152       O  
ATOM   1067  CB  ASP A 134     -40.118  41.369  15.503  1.00 50.27           C  
ANISOU 1067  CB  ASP A 134     4715   5728   8655    300   -563    224       C  
ATOM   1068  CG  ASP A 134     -40.094  42.468  14.444  1.00 50.83           C  
ANISOU 1068  CG  ASP A 134     4863   5749   8698    295   -612    235       C  
ATOM   1069  OD1 ASP A 134     -40.066  43.638  14.824  1.00 51.87           O  
ANISOU 1069  OD1 ASP A 134     4996   5869   8844    288   -653    232       O  
ATOM   1070  OD2 ASP A 134     -40.117  42.146  13.237  1.00 51.17           O  
ANISOU 1070  OD2 ASP A 134     4977   5762   8703    298   -615    247       O  
ATOM   1071  N   ALA A 135     -39.947  39.647  18.079  1.00 48.20           N  
ANISOU 1071  N   ALA A 135     4308   5560   8443    287   -481    211       N  
ATOM   1072  CA  ALA A 135     -40.506  38.583  18.950  1.00 48.68           C  
ANISOU 1072  CA  ALA A 135     4324   5650   8518    275   -469    193       C  
ATOM   1073  C   ALA A 135     -40.369  38.962  20.432  1.00 48.45           C  
ANISOU 1073  C   ALA A 135     4229   5663   8516    263   -454    185       C  
ATOM   1074  O   ALA A 135     -41.259  38.584  21.217  1.00 47.67           O  
ANISOU 1074  O   ALA A 135     4083   5597   8431    250   -462    158       O  
ATOM   1075  CB  ALA A 135     -39.836  37.264  18.652  1.00 48.91           C  
ANISOU 1075  CB  ALA A 135     4390   5673   8521    276   -431    219       C  
ATOM   1076  N   TYR A 136     -39.310  39.690  20.795  1.00 48.60           N  
ANISOU 1076  N   TYR A 136     4245   5684   8537    262   -437    210       N  
ATOM   1077  CA  TYR A 136     -39.011  40.153  22.179  1.00 49.21           C  
ANISOU 1077  CA  TYR A 136     4275   5789   8633    251   -429    207       C  
ATOM   1078  C   TYR A 136     -40.059  41.170  22.636  1.00 50.92           C  
ANISOU 1078  C   TYR A 136     4471   6012   8865    269   -475    160       C  
ATOM   1079  O   TYR A 136     -40.413  41.166  23.840  1.00 52.39           O  
ANISOU 1079  O   TYR A 136     4611   6233   9060    267   -468    136       O  
ATOM   1080  CB  TYR A 136     -37.606  40.753  22.223  1.00 49.40           C  
ANISOU 1080  CB  TYR A 136     4309   5807   8652    240   -413    252       C  
ATOM   1081  CG  TYR A 136     -37.080  41.235  23.552  1.00 49.25           C  
ANISOU 1081  CG  TYR A 136     4258   5805   8649    224   -412    258       C  
ATOM   1082  CD1 TYR A 136     -37.424  40.651  24.764  1.00 49.28           C  
ANISOU 1082  CD1 TYR A 136     4225   5836   8662    218   -398    237       C  
ATOM   1083  CD2 TYR A 136     -36.134  42.244  23.571  1.00 49.80           C  
ANISOU 1083  CD2 TYR A 136     4342   5862   8718    205   -428    293       C  
ATOM   1084  CE1 TYR A 136     -36.874  41.094  25.958  1.00 49.40           C  
ANISOU 1084  CE1 TYR A 136     4222   5861   8684    203   -401    245       C  
ATOM   1085  CE2 TYR A 136     -35.569  42.695  24.751  1.00 50.20           C  
ANISOU 1085  CE2 TYR A 136     4373   5919   8779    187   -438    304       C  
ATOM   1086  CZ  TYR A 136     -35.942  42.124  25.950  1.00 50.04           C  
ANISOU 1086  CZ  TYR A 136     4321   5922   8768    190   -424    278       C  
ATOM   1087  OH  TYR A 136     -35.356  42.612  27.084  1.00 49.82           O  
ANISOU 1087  OH  TYR A 136     4287   5894   8745    172   -438    289       O  
ATOM   1088  N   TYR A 137     -40.543  42.018  21.721  1.00 51.42           N  
ANISOU 1088  N   TYR A 137     4570   6041   8926    292   -523    144       N  
ATOM   1089  CA  TYR A 137     -41.653  42.961  22.012  1.00 51.43           C  
ANISOU 1089  CA  TYR A 137     4555   6046   8940    329   -578     89       C  
ATOM   1090  C   TYR A 137     -42.928  42.152  22.250  1.00 52.01           C  
ANISOU 1090  C   TYR A 137     4568   6170   9024    336   -573     50       C  
ATOM   1091  O   TYR A 137     -43.541  42.311  23.326  1.00 52.89           O  
ANISOU 1091  O   TYR A 137     4619   6333   9142    350   -569     14       O  
ATOM   1092  CB  TYR A 137     -41.829  44.001  20.903  1.00 50.96           C  
ANISOU 1092  CB  TYR A 137     4561   5928   8872    353   -643     84       C  
ATOM   1093  CG  TYR A 137     -40.852  45.143  20.994  1.00 50.79           C  
ANISOU 1093  CG  TYR A 137     4593   5864   8838    342   -669    112       C  
ATOM   1094  CD1 TYR A 137     -39.998  45.432  19.945  1.00 50.87           C  
ANISOU 1094  CD1 TYR A 137     4669   5833   8826    310   -674    163       C  
ATOM   1095  CD2 TYR A 137     -40.752  45.913  22.145  1.00 50.95           C  
ANISOU 1095  CD2 TYR A 137     4602   5890   8865    356   -689     93       C  
ATOM   1096  CE1 TYR A 137     -39.091  46.476  20.022  1.00 50.56           C  
ANISOU 1096  CE1 TYR A 137     4678   5761   8772    280   -704    199       C  
ATOM   1097  CE2 TYR A 137     -39.846  46.954  22.243  1.00 50.62           C  
ANISOU 1097  CE2 TYR A 137     4619   5803   8809    334   -727    125       C  
ATOM   1098  CZ  TYR A 137     -39.014  47.235  21.176  1.00 50.80           C  
ANISOU 1098  CZ  TYR A 137     4702   5787   8811    289   -736    182       C  
ATOM   1099  OH  TYR A 137     -38.127  48.262  21.259  1.00 52.48           O  
ANISOU 1099  OH  TYR A 137     4972   5960   9008    250   -778    222       O  
ATOM   1100  N   ARG A 138     -43.290  41.294  21.294  1.00 53.03           N  
ANISOU 1100  N   ARG A 138     4712   6287   9148    321   -575     61       N  
ATOM   1101  CA  ARG A 138     -44.551  40.506  21.322  1.00 55.63           C  
ANISOU 1101  CA  ARG A 138     4988   6661   9485    310   -584     34       C  
ATOM   1102  C   ARG A 138     -44.506  39.488  22.475  1.00 56.14           C  
ANISOU 1102  C   ARG A 138     5001   6782   9546    266   -532     44       C  
ATOM   1103  O   ARG A 138     -45.585  39.077  22.917  1.00 56.15           O  
ANISOU 1103  O   ARG A 138     4936   6843   9552    249   -536     20       O  
ATOM   1104  CB  ARG A 138     -44.816  39.902  19.941  1.00 57.41           C  
ANISOU 1104  CB  ARG A 138     5268   6842   9700    300   -612     49       C  
ATOM   1105  CG  ARG A 138     -45.247  40.952  18.922  1.00 60.07           C  
ANISOU 1105  CG  ARG A 138     5647   7133  10041    342   -678     28       C  
ATOM   1106  CD  ARG A 138     -45.668  40.424  17.557  1.00 61.82           C  
ANISOU 1106  CD  ARG A 138     5928   7310  10250    335   -716     38       C  
ATOM   1107  NE  ARG A 138     -45.270  41.326  16.466  1.00 62.85           N  
ANISOU 1107  NE  ARG A 138     6146   7369  10363    359   -756     46       N  
ATOM   1108  CZ  ARG A 138     -44.225  41.152  15.640  1.00 63.36           C  
ANISOU 1108  CZ  ARG A 138     6294   7386  10391    345   -729     89       C  
ATOM   1109  NH1 ARG A 138     -43.440  40.090  15.741  1.00 63.41           N  
ANISOU 1109  NH1 ARG A 138     6310   7404  10377    321   -665    123       N  
ATOM   1110  NH2 ARG A 138     -43.969  42.049  14.702  1.00 64.04           N  
ANISOU 1110  NH2 ARG A 138     6458   7417  10456    357   -768     98       N  
ATOM   1111  N   ALA A 139     -43.313  39.141  22.976  1.00 56.84           N  
ANISOU 1111  N   ALA A 139     5115   6856   9624    246   -489     80       N  
ATOM   1112  CA  ALA A 139     -43.106  38.330  24.199  1.00 56.64           C  
ANISOU 1112  CA  ALA A 139     5055   6873   9591    206   -447     92       C  
ATOM   1113  C   ALA A 139     -43.607  39.086  25.434  1.00 57.44           C  
ANISOU 1113  C   ALA A 139     5093   7032   9697    220   -441     55       C  
ATOM   1114  O   ALA A 139     -44.474  38.546  26.148  1.00 55.30           O  
ANISOU 1114  O   ALA A 139     4764   6827   9419    191   -426     38       O  
ATOM   1115  CB  ALA A 139     -41.654  37.972  24.342  1.00 55.67           C  
ANISOU 1115  CB  ALA A 139     4976   6716   9460    198   -415    135       C  
ATOM   1116  N   ARG A 140     -43.072  40.287  25.674  1.00 60.26           N  
ANISOU 1116  N   ARG A 140     5468   7367  10061    260   -454     45       N  
ATOM   1117  CA  ARG A 140     -43.409  41.141  26.850  1.00 63.93           C  
ANISOU 1117  CA  ARG A 140     5895   7873  10522    289   -455      5       C  
ATOM   1118  C   ARG A 140     -44.926  41.353  26.906  1.00 63.92           C  
ANISOU 1118  C   ARG A 140     5824   7938  10522    321   -472    -50       C  
ATOM   1119  O   ARG A 140     -45.467  41.409  28.025  1.00 65.01           O  
ANISOU 1119  O   ARG A 140     5905   8148  10645    327   -447    -81       O  
ATOM   1120  CB  ARG A 140     -42.699  42.500  26.779  1.00 67.64           C  
ANISOU 1120  CB  ARG A 140     6418   8287  10995    331   -493      2       C  
ATOM   1121  CG  ARG A 140     -41.905  42.864  28.028  1.00 71.23           C  
ANISOU 1121  CG  ARG A 140     6882   8741  11438    323   -478     11       C  
ATOM   1122  CD  ARG A 140     -40.430  42.508  27.861  1.00 74.41           C  
ANISOU 1122  CD  ARG A 140     7326   9099  11845    278   -461     77       C  
ATOM   1123  NE  ARG A 140     -39.670  43.485  27.085  1.00 77.99           N  
ANISOU 1123  NE  ARG A 140     7836   9492  12303    286   -502    102       N  
ATOM   1124  CZ  ARG A 140     -38.937  44.481  27.596  1.00 81.17           C  
ANISOU 1124  CZ  ARG A 140     8276   9862  12702    285   -535    115       C  
ATOM   1125  NH1 ARG A 140     -38.862  44.676  28.906  1.00 82.36           N  
ANISOU 1125  NH1 ARG A 140     8419  10029  12843    287   -533     99       N  
ATOM   1126  NH2 ARG A 140     -38.287  45.299  26.783  1.00 81.87           N  
ANISOU 1126  NH2 ARG A 140     8417   9898  12789    275   -576    147       N  
ATOM   1127  N   ALA A 141     -45.567  41.478  25.740  1.00 62.61           N  
ANISOU 1127  N   ALA A 141     5663   7754  10371    343   -513    -62       N  
ATOM   1128  CA  ALA A 141     -47.031  41.617  25.566  1.00 64.56           C  
ANISOU 1128  CA  ALA A 141     5836   8067  10626    374   -540   -112       C  
ATOM   1129  C   ALA A 141     -47.758  40.376  26.108  1.00 64.77           C  
ANISOU 1129  C   ALA A 141     5784   8181  10643    307   -498   -102       C  
ATOM   1130  O   ALA A 141     -48.729  40.541  26.871  1.00 69.68           O  
ANISOU 1130  O   ALA A 141     6315   8902  11257    323   -483   -143       O  
ATOM   1131  CB  ALA A 141     -47.347  41.842  24.109  1.00 65.19           C  
ANISOU 1131  CB  ALA A 141     5955   8089  10722    397   -599   -113       C  
ATOM   1132  N   GLY A 142     -47.303  39.176  25.737  1.00 63.02           N  
ANISOU 1132  N   GLY A 142     5601   7927  10415    233   -481    -50       N  
ATOM   1133  CA  GLY A 142     -47.932  37.903  26.141  1.00 62.22           C  
ANISOU 1133  CA  GLY A 142     5452   7890  10299    150   -458    -29       C  
ATOM   1134  C   GLY A 142     -47.827  36.824  25.078  1.00 61.22           C  
ANISOU 1134  C   GLY A 142     5386   7703  10171     98   -484     13       C  
ATOM   1135  O   GLY A 142     -48.007  35.640  25.450  1.00 60.72           O  
ANISOU 1135  O   GLY A 142     5319   7663  10086     17   -471     44       O  
ATOM   1136  N   GLU A 143     -47.583  37.198  23.813  1.00 60.53           N  
ANISOU 1136  N   GLU A 143     5361   7538  10097    140   -525     14       N  
ATOM   1137  CA  GLU A 143     -47.330  36.259  22.676  1.00 60.64           C  
ANISOU 1137  CA  GLU A 143     5459   7480  10102    108   -552     51       C  
ATOM   1138  C   GLU A 143     -45.831  35.912  22.655  1.00 57.40           C  
ANISOU 1138  C   GLU A 143     5134   6999   9673    112   -518     88       C  
ATOM   1139  O   GLU A 143     -45.087  36.483  21.810  1.00 55.88           O  
ANISOU 1139  O   GLU A 143     5002   6745   9482    159   -525     94       O  
ATOM   1140  CB  GLU A 143     -47.844  36.888  21.370  1.00 63.80           C  
ANISOU 1140  CB  GLU A 143     5883   7839  10518    153   -611     32       C  
ATOM   1141  CG  GLU A 143     -47.391  36.201  20.073  1.00 65.97           C  
ANISOU 1141  CG  GLU A 143     6267   8024  10774    143   -638     65       C  
ATOM   1142  CD  GLU A 143     -47.115  37.104  18.863  1.00 66.43           C  
ANISOU 1142  CD  GLU A 143     6392   8014  10835    202   -673     56       C  
ATOM   1143  OE1 GLU A 143     -47.925  38.027  18.606  1.00 69.11           O  
ANISOU 1143  OE1 GLU A 143     6692   8369  11197    239   -719     20       O  
ATOM   1144  OE2 GLU A 143     -46.100  36.874  18.150  1.00 63.83           O  
ANISOU 1144  OE2 GLU A 143     6155   7617  10480    213   -658     85       O  
ATOM   1145  N   ALA A 144     -45.405  34.997  23.538  1.00 55.09           N  
ANISOU 1145  N   ALA A 144     4847   6721   9362     63   -485    113       N  
ATOM   1146  CA  ALA A 144     -43.986  34.620  23.771  1.00 52.15           C  
ANISOU 1146  CA  ALA A 144     4537   6300   8975     73   -452    145       C  
ATOM   1147  C   ALA A 144     -43.674  33.263  23.137  1.00 50.58           C  
ANISOU 1147  C   ALA A 144     4423   6045   8749     46   -469    176       C  
ATOM   1148  O   ALA A 144     -42.587  32.753  23.374  1.00 49.59           O  
ANISOU 1148  O   ALA A 144     4345   5886   8608     57   -447    199       O  
ATOM   1149  CB  ALA A 144     -43.695  34.592  25.251  1.00 51.87           C  
ANISOU 1149  CB  ALA A 144     4460   6310   8936     47   -416    146       C  
ATOM   1150  N   ALA A 145     -44.604  32.693  22.374  1.00 50.84           N  
ANISOU 1150  N   ALA A 145     4476   6065   8773     16   -514    176       N  
ATOM   1151  CA  ALA A 145     -44.422  31.407  21.669  1.00 50.96           C  
ANISOU 1151  CA  ALA A 145     4593   6014   8754     -3   -546    202       C  
ATOM   1152  C   ALA A 145     -43.299  31.579  20.654  1.00 50.42           C  
ANISOU 1152  C   ALA A 145     4603   5879   8672     72   -533    208       C  
ATOM   1153  O   ALA A 145     -42.310  30.841  20.755  1.00 51.01           O  
ANISOU 1153  O   ALA A 145     4740   5919   8722     92   -516    226       O  
ATOM   1154  CB  ALA A 145     -45.702  30.962  21.012  1.00 51.59           C  
ANISOU 1154  CB  ALA A 145     4677   6094   8829    -53   -608    200       C  
ATOM   1155  N   ASN A 146     -43.440  32.542  19.742  1.00 50.42           N  
ANISOU 1155  N   ASN A 146     4600   5870   8686    115   -540    192       N  
ATOM   1156  CA  ASN A 146     -42.432  32.805  18.680  1.00 50.39           C  
ANISOU 1156  CA  ASN A 146     4667   5816   8661    179   -522    201       C  
ATOM   1157  C   ASN A 146     -41.055  33.007  19.311  1.00 49.67           C  
ANISOU 1157  C   ASN A 146     4561   5740   8571    211   -463    218       C  
ATOM   1158  O   ASN A 146     -40.116  32.284  18.937  1.00 50.65           O  
ANISOU 1158  O   ASN A 146     4747   5833   8662    246   -443    234       O  
ATOM   1159  CB  ASN A 146     -42.754  34.033  17.834  1.00 50.62           C  
ANISOU 1159  CB  ASN A 146     4688   5840   8705    209   -539    185       C  
ATOM   1160  CG  ASN A 146     -43.446  33.642  16.553  1.00 51.29           C  
ANISOU 1160  CG  ASN A 146     4847   5873   8767    209   -593    181       C  
ATOM   1161  OD1 ASN A 146     -42.797  33.463  15.526  1.00 51.04           O  
ANISOU 1161  OD1 ASN A 146     4902   5792   8696    248   -586    193       O  
ATOM   1162  ND2 ASN A 146     -44.751  33.452  16.633  1.00 51.67           N  
ANISOU 1162  ND2 ASN A 146     4861   5937   8833    166   -647    166       N  
ATOM   1163  N   PHE A 147     -40.947  33.976  20.216  1.00 48.17           N  
ANISOU 1163  N   PHE A 147     4291   5596   8414    204   -440    211       N  
ATOM   1164  CA  PHE A 147     -39.674  34.387  20.856  1.00 46.38           C  
ANISOU 1164  CA  PHE A 147     4040   5388   8194    226   -394    229       C  
ATOM   1165  C   PHE A 147     -38.946  33.153  21.381  1.00 46.05           C  
ANISOU 1165  C   PHE A 147     4027   5335   8132    226   -377    248       C  
ATOM   1166  O   PHE A 147     -37.731  33.054  21.145  1.00 47.16           O  
ANISOU 1166  O   PHE A 147     4185   5471   8260    269   -346    268       O  
ATOM   1167  CB  PHE A 147     -39.937  35.390  21.978  1.00 45.50           C  
ANISOU 1167  CB  PHE A 147     3851   5320   8115    207   -390    215       C  
ATOM   1168  CG  PHE A 147     -38.683  35.969  22.569  1.00 44.43           C  
ANISOU 1168  CG  PHE A 147     3694   5197   7989    221   -357    237       C  
ATOM   1169  CD1 PHE A 147     -37.708  36.517  21.756  1.00 44.00           C  
ANISOU 1169  CD1 PHE A 147     3661   5128   7926    250   -341    261       C  
ATOM   1170  CD2 PHE A 147     -38.487  35.970  23.937  1.00 44.05           C  
ANISOU 1170  CD2 PHE A 147     3604   5177   7954    198   -345    237       C  
ATOM   1171  CE1 PHE A 147     -36.561  37.062  22.304  1.00 44.53           C  
ANISOU 1171  CE1 PHE A 147     3699   5215   8004    250   -317    288       C  
ATOM   1172  CE2 PHE A 147     -37.342  36.521  24.486  1.00 44.50           C  
ANISOU 1172  CE2 PHE A 147     3643   5242   8022    205   -326    261       C  
ATOM   1173  CZ  PHE A 147     -36.377  37.057  23.667  1.00 44.85           C  
ANISOU 1173  CZ  PHE A 147     3701   5277   8063    229   -314    288       C  
ATOM   1174  N   CYS A 148     -39.668  32.252  22.055  1.00 45.49           N  
ANISOU 1174  N   CYS A 148     3962   5266   8056    179   -402    243       N  
ATOM   1175  CA  CYS A 148     -39.127  30.993  22.635  1.00 45.68           C  
ANISOU 1175  CA  CYS A 148     4033   5268   8056    171   -405    259       C  
ATOM   1176  C   CYS A 148     -38.573  30.123  21.500  1.00 45.85           C  
ANISOU 1176  C   CYS A 148     4150   5232   8037    226   -416    266       C  
ATOM   1177  O   CYS A 148     -37.384  29.777  21.547  1.00 45.46           O  
ANISOU 1177  O   CYS A 148     4121   5175   7974    281   -391    277       O  
ATOM   1178  CB  CYS A 148     -40.189  30.256  23.443  1.00 46.43           C  
ANISOU 1178  CB  CYS A 148     4124   5373   8143     91   -439    258       C  
ATOM   1179  SG  CYS A 148     -40.533  31.028  25.047  1.00 47.71           S  
ANISOU 1179  SG  CYS A 148     4184   5610   8333     40   -412    250       S  
ATOM   1180  N   ALA A 149     -39.388  29.837  20.484  1.00 46.04           N  
ANISOU 1180  N   ALA A 149     4228   5221   8041    220   -453    257       N  
ATOM   1181  CA  ALA A 149     -38.999  29.066  19.278  1.00 45.68           C  
ANISOU 1181  CA  ALA A 149     4291   5116   7947    278   -469    257       C  
ATOM   1182  C   ALA A 149     -37.673  29.602  18.740  1.00 45.26           C  
ANISOU 1182  C   ALA A 149     4228   5082   7886    362   -409    263       C  
ATOM   1183  O   ALA A 149     -36.740  28.800  18.511  1.00 46.05           O  
ANISOU 1183  O   ALA A 149     4385   5161   7950    427   -397    266       O  
ATOM   1184  CB  ALA A 149     -40.080  29.157  18.234  1.00 45.81           C  
ANISOU 1184  CB  ALA A 149     4347   5102   7953    257   -513    246       C  
ATOM   1185  N   LEU A 150     -37.596  30.917  18.545  1.00 44.65           N  
ANISOU 1185  N   LEU A 150     4082   5045   7838    359   -377    265       N  
ATOM   1186  CA  LEU A 150     -36.385  31.584  18.013  1.00 44.75           C  
ANISOU 1186  CA  LEU A 150     4073   5088   7840    415   -321    281       C  
ATOM   1187  C   LEU A 150     -35.227  31.316  18.975  1.00 44.75           C  
ANISOU 1187  C   LEU A 150     4027   5123   7852    439   -286    297       C  
ATOM   1188  O   LEU A 150     -34.152  30.968  18.495  1.00 44.72           O  
ANISOU 1188  O   LEU A 150     4039   5133   7818    506   -250    307       O  
ATOM   1189  CB  LEU A 150     -36.646  33.080  17.830  1.00 44.17           C  
ANISOU 1189  CB  LEU A 150     3942   5042   7797    385   -313    284       C  
ATOM   1190  CG  LEU A 150     -37.553  33.439  16.657  1.00 44.45           C  
ANISOU 1190  CG  LEU A 150     4031   5042   7815    380   -348    271       C  
ATOM   1191  CD1 LEU A 150     -37.809  34.946  16.635  1.00 44.79           C  
ANISOU 1191  CD1 LEU A 150     4023   5103   7888    353   -354    272       C  
ATOM   1192  CD2 LEU A 150     -36.953  32.987  15.343  1.00 44.42           C  
ANISOU 1192  CD2 LEU A 150     4110   5014   7750    438   -326    278       C  
ATOM   1193  N   ILE A 151     -35.442  31.435  20.284  1.00 44.89           N  
ANISOU 1193  N   ILE A 151     3989   5157   7908    389   -298    298       N  
ATOM   1194  CA  ILE A 151     -34.361  31.197  21.285  1.00 45.69           C  
ANISOU 1194  CA  ILE A 151     4049   5287   8023    406   -276    315       C  
ATOM   1195  C   ILE A 151     -33.854  29.761  21.102  1.00 46.01           C  
ANISOU 1195  C   ILE A 151     4167   5292   8023    466   -289    310       C  
ATOM   1196  O   ILE A 151     -32.651  29.604  20.860  1.00 46.10           O  
ANISOU 1196  O   ILE A 151     4164   5329   8020    537   -254    320       O  
ATOM   1197  CB  ILE A 151     -34.824  31.503  22.724  1.00 45.52           C  
ANISOU 1197  CB  ILE A 151     3975   5281   8040    338   -293    314       C  
ATOM   1198  CG1 ILE A 151     -35.072  33.000  22.915  1.00 45.51           C  
ANISOU 1198  CG1 ILE A 151     3905   5314   8073    304   -281    315       C  
ATOM   1199  CG2 ILE A 151     -33.829  30.977  23.746  1.00 45.57           C  
ANISOU 1199  CG2 ILE A 151     3964   5296   8052    353   -288    329       C  
ATOM   1200  CD1 ILE A 151     -35.825  33.335  24.182  1.00 45.82           C  
ANISOU 1200  CD1 ILE A 151     3903   5368   8137    245   -299    302       C  
ATOM   1201  N   LEU A 152     -34.747  28.769  21.175  1.00 46.21           N  
ANISOU 1201  N   LEU A 152     4270   5260   8026    439   -342    295       N  
ATOM   1202  CA  LEU A 152     -34.428  27.332  20.949  1.00 47.18           C  
ANISOU 1202  CA  LEU A 152     4499   5326   8100    494   -377    286       C  
ATOM   1203  C   LEU A 152     -33.662  27.184  19.633  1.00 47.97           C  
ANISOU 1203  C   LEU A 152     4642   5426   8157    598   -345    279       C  
ATOM   1204  O   LEU A 152     -32.627  26.500  19.621  1.00 48.00           O  
ANISOU 1204  O   LEU A 152     4672   5430   8134    686   -335    275       O  
ATOM   1205  CB  LEU A 152     -35.725  26.519  20.917  1.00 47.68           C  
ANISOU 1205  CB  LEU A 152     4648   5326   8141    427   -448    278       C  
ATOM   1206  CG  LEU A 152     -36.395  26.303  22.272  1.00 47.51           C  
ANISOU 1206  CG  LEU A 152     4601   5308   8142    328   -481    288       C  
ATOM   1207  CD1 LEU A 152     -37.811  25.781  22.090  1.00 47.99           C  
ANISOU 1207  CD1 LEU A 152     4716   5333   8184    242   -541    287       C  
ATOM   1208  CD2 LEU A 152     -35.572  25.360  23.145  1.00 47.54           C  
ANISOU 1208  CD2 LEU A 152     4650   5284   8128    354   -504    295       C  
ATOM   1209  N   ALA A 153     -34.151  27.828  18.572  1.00 48.69           N  
ANISOU 1209  N   ALA A 153     4740   5519   8237    592   -330    275       N  
ATOM   1210  CA  ALA A 153     -33.523  27.819  17.232  1.00 49.79           C  
ANISOU 1210  CA  ALA A 153     4924   5667   8327    681   -292    269       C  
ATOM   1211  C   ALA A 153     -32.095  28.367  17.326  1.00 50.54           C  
ANISOU 1211  C   ALA A 153     4925   5846   8430    740   -218    287       C  
ATOM   1212  O   ALA A 153     -31.168  27.625  16.991  1.00 52.11           O  
ANISOU 1212  O   ALA A 153     5155   6056   8586    840   -196    278       O  
ATOM   1213  CB  ALA A 153     -34.353  28.610  16.259  1.00 49.85           C  
ANISOU 1213  CB  ALA A 153     4945   5665   8330    642   -294    268       C  
ATOM   1214  N   TYR A 154     -31.930  29.605  17.797  1.00 50.44           N  
ANISOU 1214  N   TYR A 154     4803   5892   8468    680   -185    312       N  
ATOM   1215  CA  TYR A 154     -30.645  30.352  17.821  1.00 50.67           C  
ANISOU 1215  CA  TYR A 154     4732   6010   8508    707   -119    341       C  
ATOM   1216  C   TYR A 154     -29.610  29.634  18.700  1.00 51.82           C  
ANISOU 1216  C   TYR A 154     4840   6184   8664    762   -114    345       C  
ATOM   1217  O   TYR A 154     -28.414  29.880  18.478  1.00 53.37           O  
ANISOU 1217  O   TYR A 154     4965   6459   8853    815    -59    365       O  
ATOM   1218  CB  TYR A 154     -30.853  31.799  18.284  1.00 49.81           C  
ANISOU 1218  CB  TYR A 154     4537   5935   8452    615   -113    367       C  
ATOM   1219  CG  TYR A 154     -31.200  32.761  17.176  1.00 49.74           C  
ANISOU 1219  CG  TYR A 154     4542   5932   8423    589    -97    376       C  
ATOM   1220  CD1 TYR A 154     -30.297  33.033  16.159  1.00 50.38           C  
ANISOU 1220  CD1 TYR A 154     4612   6069   8458    632    -38    398       C  
ATOM   1221  CD2 TYR A 154     -32.426  33.409  17.140  1.00 49.38           C  
ANISOU 1221  CD2 TYR A 154     4520   5842   8400    523   -141    364       C  
ATOM   1222  CE1 TYR A 154     -30.610  33.901  15.124  1.00 50.37           C  
ANISOU 1222  CE1 TYR A 154     4640   6068   8431    600    -29    410       C  
ATOM   1223  CE2 TYR A 154     -32.755  34.275  16.108  1.00 49.36           C  
ANISOU 1223  CE2 TYR A 154     4543   5834   8376    502   -139    371       C  
ATOM   1224  CZ  TYR A 154     -31.838  34.534  15.107  1.00 49.81           C  
ANISOU 1224  CZ  TYR A 154     4603   5936   8384    536    -85    396       C  
ATOM   1225  OH  TYR A 154     -32.161  35.391  14.098  1.00 50.15           O  
ANISOU 1225  OH  TYR A 154     4684   5968   8401    507    -88    406       O  
ATOM   1226  N   CYS A 155     -30.033  28.793  19.651  1.00 52.05           N  
ANISOU 1226  N   CYS A 155     4911   6155   8707    747   -171    329       N  
ATOM   1227  CA  CYS A 155     -29.137  28.056  20.589  1.00 52.92           C  
ANISOU 1227  CA  CYS A 155     5002   6276   8829    796   -184    330       C  
ATOM   1228  C   CYS A 155     -28.958  26.592  20.155  1.00 54.49           C  
ANISOU 1228  C   CYS A 155     5316   6418   8969    900   -218    298       C  
ATOM   1229  O   CYS A 155     -28.323  25.822  20.900  1.00 54.58           O  
ANISOU 1229  O   CYS A 155     5337   6418   8981    950   -248    292       O  
ATOM   1230  CB  CYS A 155     -29.689  28.110  22.005  1.00 52.61           C  
ANISOU 1230  CB  CYS A 155     4947   6205   8836    706   -232    336       C  
ATOM   1231  SG  CYS A 155     -30.082  29.788  22.562  1.00 52.91           S  
ANISOU 1231  SG  CYS A 155     4879   6290   8933    594   -209    363       S  
ATOM   1232  N   ASN A 156     -29.514  26.222  19.000  1.00 55.59           N  
ANISOU 1232  N   ASN A 156     5552   6515   9055    933   -224    276       N  
ATOM   1233  CA  ASN A 156     -29.453  24.864  18.396  1.00 56.80           C  
ANISOU 1233  CA  ASN A 156     5843   6599   9138   1036   -265    241       C  
ATOM   1234  C   ASN A 156     -29.971  23.807  19.375  1.00 56.71           C  
ANISOU 1234  C   ASN A 156     5923   6495   9127   1002   -359    231       C  
ATOM   1235  O   ASN A 156     -29.577  22.655  19.247  1.00 58.14           O  
ANISOU 1235  O   ASN A 156     6208   6623   9258   1098   -404    205       O  
ATOM   1236  CB  ASN A 156     -28.049  24.535  17.899  1.00 58.29           C  
ANISOU 1236  CB  ASN A 156     6002   6855   9288   1185   -212    229       C  
ATOM   1237  CG  ASN A 156     -28.087  23.778  16.588  1.00 60.64           C  
ANISOU 1237  CG  ASN A 156     6428   7113   9498   1294   -213    193       C  
ATOM   1238  OD1 ASN A 156     -28.824  22.799  16.447  1.00 60.27           O  
ANISOU 1238  OD1 ASN A 156     6533   6955   9411   1301   -294    167       O  
ATOM   1239  ND2 ASN A 156     -27.319  24.244  15.611  1.00 62.30           N  
ANISOU 1239  ND2 ASN A 156     6583   7414   9671   1372   -126    194       N  
ATOM   1240  N   LYS A 157     -30.853  24.188  20.295  1.00 56.71           N  
ANISOU 1240  N   LYS A 157     5893   6478   9175    870   -389    250       N  
ATOM   1241  CA  LYS A 157     -31.547  23.264  21.227  1.00 57.53           C  
ANISOU 1241  CA  LYS A 157     6084   6499   9273    803   -477    249       C  
ATOM   1242  C   LYS A 157     -32.856  22.790  20.586  1.00 57.45           C  
ANISOU 1242  C   LYS A 157     6187   6412   9227    741   -536    241       C  
ATOM   1243  O   LYS A 157     -33.314  23.442  19.618  1.00 57.64           O  
ANISOU 1243  O   LYS A 157     6195   6456   9249    732   -502    239       O  
ATOM   1244  CB  LYS A 157     -31.794  23.975  22.557  1.00 58.01           C  
ANISOU 1244  CB  LYS A 157     6042   6599   9397    692   -470    275       C  
ATOM   1245  CG  LYS A 157     -30.530  24.512  23.209  1.00 58.44           C  
ANISOU 1245  CG  LYS A 157     5986   6726   9491    739   -423    288       C  
ATOM   1246  CD  LYS A 157     -30.569  24.523  24.689  1.00 59.53           C  
ANISOU 1246  CD  LYS A 157     6093   6860   9664    663   -454    305       C  
ATOM   1247  CE  LYS A 157     -30.135  23.205  25.286  1.00 60.85           C  
ANISOU 1247  CE  LYS A 157     6361   6959   9799    709   -527    296       C  
ATOM   1248  NZ  LYS A 157     -28.687  23.222  25.606  1.00 62.90           N  
ANISOU 1248  NZ  LYS A 157     6555   7264  10077    810   -508    298       N  
ATOM   1249  N   THR A 158     -33.415  21.677  21.078  1.00 57.18           N  
ANISOU 1249  N   THR A 158     6271   6290   9162    697   -627    241       N  
ATOM   1250  CA  THR A 158     -34.740  21.140  20.658  1.00 57.31           C  
ANISOU 1250  CA  THR A 158     6396   6233   9146    609   -700    244       C  
ATOM   1251  C   THR A 158     -35.627  20.999  21.900  1.00 56.57           C  
ANISOU 1251  C   THR A 158     6283   6132   9077    459   -746    271       C  
ATOM   1252  O   THR A 158     -35.088  21.038  23.032  1.00 57.23           O  
ANISOU 1252  O   THR A 158     6315   6241   9185    446   -736    281       O  
ATOM   1253  CB  THR A 158     -34.620  19.813  19.892  1.00 58.04           C  
ANISOU 1253  CB  THR A 158     6676   6217   9157    692   -781    221       C  
ATOM   1254  OG1 THR A 158     -34.187  18.817  20.822  1.00 58.83           O  
ANISOU 1254  OG1 THR A 158     6856   6259   9236    704   -850    223       O  
ATOM   1255  CG2 THR A 158     -33.684  19.887  18.702  1.00 58.20           C  
ANISOU 1255  CG2 THR A 158     6717   6254   9140    854   -728    190       C  
ATOM   1256  N   VAL A 159     -36.937  20.880  21.704  1.00 55.04           N  
ANISOU 1256  N   VAL A 159     6122   5914   8875    346   -793    284       N  
ATOM   1257  CA  VAL A 159     -37.901  20.814  22.837  1.00 55.31           C  
ANISOU 1257  CA  VAL A 159     6120   5966   8926    191   -825    313       C  
ATOM   1258  C   VAL A 159     -37.600  19.537  23.628  1.00 55.37           C  
ANISOU 1258  C   VAL A 159     6255   5894   8888    172   -909    325       C  
ATOM   1259  O   VAL A 159     -37.192  18.558  23.007  1.00 56.91           O  
ANISOU 1259  O   VAL A 159     6598   5996   9026    252   -974    311       O  
ATOM   1260  CB  VAL A 159     -39.356  20.881  22.340  1.00 55.73           C  
ANISOU 1260  CB  VAL A 159     6178   6020   8977     81   -862    325       C  
ATOM   1261  CG1 VAL A 159     -40.345  20.768  23.491  1.00 55.37           C  
ANISOU 1261  CG1 VAL A 159     6085   6012   8940    -77   -887    356       C  
ATOM   1262  CG2 VAL A 159     -39.602  22.154  21.530  1.00 55.44           C  
ANISOU 1262  CG2 VAL A 159     6029   6051   8983    112   -790    309       C  
ATOM   1263  N   GLY A 160     -37.738  19.576  24.954  1.00 54.78           N  
ANISOU 1263  N   GLY A 160     6131   5852   8830     80   -909    348       N  
ATOM   1264  CA  GLY A 160     -37.473  18.430  25.846  1.00 55.00           C  
ANISOU 1264  CA  GLY A 160     6280   5804   8812     45   -993    365       C  
ATOM   1265  C   GLY A 160     -36.014  18.355  26.263  1.00 54.28           C  
ANISOU 1265  C   GLY A 160     6188   5703   8730    175   -975    347       C  
ATOM   1266  O   GLY A 160     -35.759  17.940  27.410  1.00 55.46           O  
ANISOU 1266  O   GLY A 160     6366   5833   8870    128  -1011    364       O  
ATOM   1267  N   GLU A 161     -35.091  18.718  25.368  1.00 52.73           N  
ANISOU 1267  N   GLU A 161     5962   5524   8548    328   -923    315       N  
ATOM   1268  CA  GLU A 161     -33.639  18.862  25.665  1.00 51.69           C  
ANISOU 1268  CA  GLU A 161     5786   5417   8437    461   -887    298       C  
ATOM   1269  C   GLU A 161     -33.488  19.663  26.966  1.00 50.26           C  
ANISOU 1269  C   GLU A 161     5475   5311   8311    386   -840    320       C  
ATOM   1270  O   GLU A 161     -34.166  20.708  27.088  1.00 50.35           O  
ANISOU 1270  O   GLU A 161     5368   5398   8362    303   -776    331       O  
ATOM   1271  CB  GLU A 161     -32.943  19.541  24.479  1.00 51.79           C  
ANISOU 1271  CB  GLU A 161     5726   5485   8465    595   -806    271       C  
ATOM   1272  CG  GLU A 161     -31.426  19.395  24.463  1.00 52.57           C  
ANISOU 1272  CG  GLU A 161     5802   5604   8566    754   -783    251       C  
ATOM   1273  CD  GLU A 161     -30.733  19.942  23.216  1.00 52.86           C  
ANISOU 1273  CD  GLU A 161     5778   5703   8602    883   -702    228       C  
ATOM   1274  OE1 GLU A 161     -29.531  20.279  23.302  1.00 52.43           O  
ANISOU 1274  OE1 GLU A 161     5632   5717   8570    984   -650    222       O  
ATOM   1275  OE2 GLU A 161     -31.401  20.046  22.149  1.00 54.25           O  
ANISOU 1275  OE2 GLU A 161     5995   5864   8751    877   -692    219       O  
ATOM   1276  N   LEU A 162     -32.677  19.170  27.911  1.00 49.52           N  
ANISOU 1276  N   LEU A 162     5414   5189   8213    416   -879    324       N  
ATOM   1277  CA  LEU A 162     -32.238  19.911  29.126  1.00 48.13           C  
ANISOU 1277  CA  LEU A 162     5124   5076   8085    374   -839    341       C  
ATOM   1278  C   LEU A 162     -31.493  21.173  28.710  1.00 46.55           C  
ANISOU 1278  C   LEU A 162     4766   4976   7945    451   -738    333       C  
ATOM   1279  O   LEU A 162     -30.932  21.182  27.605  1.00 46.51           O  
ANISOU 1279  O   LEU A 162     4755   4981   7935    567   -710    312       O  
ATOM   1280  CB  LEU A 162     -31.297  19.035  29.946  1.00 49.11           C  
ANISOU 1280  CB  LEU A 162     5331   5138   8189    429   -913    341       C  
ATOM   1281  CG  LEU A 162     -31.980  17.943  30.742  1.00 50.40           C  
ANISOU 1281  CG  LEU A 162     5646   5208   8295    319  -1017    362       C  
ATOM   1282  CD1 LEU A 162     -31.051  16.736  30.856  1.00 51.86           C  
ANISOU 1282  CD1 LEU A 162     5974   5291   8437    429  -1119    345       C  
ATOM   1283  CD2 LEU A 162     -32.386  18.486  32.105  1.00 49.79           C  
ANISOU 1283  CD2 LEU A 162     5502   5177   8238    181   -996    392       C  
ATOM   1284  N   GLY A 163     -31.433  22.163  29.594  1.00 45.40           N  
ANISOU 1284  N   GLY A 163     4505   4897   7847    389   -690    350       N  
ATOM   1285  CA  GLY A 163     -30.927  23.500  29.240  1.00 44.31           C  
ANISOU 1285  CA  GLY A 163     4220   4851   7763    427   -603    350       C  
ATOM   1286  C   GLY A 163     -30.237  24.195  30.385  1.00 43.29           C  
ANISOU 1286  C   GLY A 163     4004   4765   7676    406   -586    368       C  
ATOM   1287  O   GLY A 163     -30.470  23.811  31.539  1.00 42.95           O  
ANISOU 1287  O   GLY A 163     4006   4691   7621    334   -631    379       O  
ATOM   1288  N   ASP A 164     -29.417  25.188  30.042  1.00 42.68           N  
ANISOU 1288  N   ASP A 164     3814   4759   7642    460   -528    373       N  
ATOM   1289  CA  ASP A 164     -28.665  26.055  30.984  1.00 41.96           C  
ANISOU 1289  CA  ASP A 164     3628   4716   7596    442   -511    395       C  
ATOM   1290  C   ASP A 164     -29.047  27.515  30.705  1.00 41.39           C  
ANISOU 1290  C   ASP A 164     3457   4708   7558    393   -448    402       C  
ATOM   1291  O   ASP A 164     -28.911  27.967  29.547  1.00 40.50           O  
ANISOU 1291  O   ASP A 164     3305   4631   7451    439   -404    399       O  
ATOM   1292  CB  ASP A 164     -27.162  25.795  30.864  1.00 41.50           C  
ANISOU 1292  CB  ASP A 164     3531   4681   7556    554   -518    400       C  
ATOM   1293  CG  ASP A 164     -26.331  26.550  31.882  1.00 41.01           C  
ANISOU 1293  CG  ASP A 164     3382   4659   7539    530   -521    428       C  
ATOM   1294  OD1 ASP A 164     -26.542  26.364  33.082  1.00 40.47           O  
ANISOU 1294  OD1 ASP A 164     3355   4553   7468    465   -566    435       O  
ATOM   1295  OD2 ASP A 164     -25.547  27.387  31.462  1.00 41.73           O  
ANISOU 1295  OD2 ASP A 164     3367   4823   7665    564   -477    445       O  
ATOM   1296  N   VAL A 165     -29.517  28.226  31.731  1.00 41.80           N  
ANISOU 1296  N   VAL A 165     3483   4773   7626    305   -448    410       N  
ATOM   1297  CA  VAL A 165     -29.856  29.674  31.649  1.00 42.37           C  
ANISOU 1297  CA  VAL A 165     3475   4896   7728    263   -405    414       C  
ATOM   1298  C   VAL A 165     -28.624  30.437  31.150  1.00 43.32           C  
ANISOU 1298  C   VAL A 165     3511   5064   7883    319   -378    437       C  
ATOM   1299  O   VAL A 165     -28.751  31.118  30.111  1.00 43.57           O  
ANISOU 1299  O   VAL A 165     3506   5127   7920    333   -339    437       O  
ATOM   1300  CB  VAL A 165     -30.360  30.201  33.005  1.00 42.53           C  
ANISOU 1300  CB  VAL A 165     3491   4916   7750    179   -418    416       C  
ATOM   1301  CG1 VAL A 165     -30.352  31.721  33.094  1.00 42.43           C  
ANISOU 1301  CG1 VAL A 165     3406   4946   7768    157   -391    421       C  
ATOM   1302  CG2 VAL A 165     -31.742  29.657  33.303  1.00 42.45           C  
ANISOU 1302  CG2 VAL A 165     3540   4887   7702    112   -426    396       C  
ATOM   1303  N   ARG A 166     -27.483  30.300  31.841  1.00 44.38           N  
ANISOU 1303  N   ARG A 166     3617   5207   8037    344   -403    459       N  
ATOM   1304  CA  ARG A 166     -26.228  31.055  31.574  1.00 44.71           C  
ANISOU 1304  CA  ARG A 166     3562   5309   8114    378   -384    491       C  
ATOM   1305  C   ARG A 166     -25.748  30.803  30.145  1.00 44.87           C  
ANISOU 1305  C   ARG A 166     3553   5369   8123    460   -341    490       C  
ATOM   1306  O   ARG A 166     -25.351  31.769  29.488  1.00 44.33           O  
ANISOU 1306  O   ARG A 166     3413   5358   8070    454   -303    513       O  
ATOM   1307  CB  ARG A 166     -25.124  30.646  32.554  1.00 45.95           C  
ANISOU 1307  CB  ARG A 166     3700   5466   8292    400   -430    512       C  
ATOM   1308  CG  ARG A 166     -23.851  31.474  32.453  1.00 46.64           C  
ANISOU 1308  CG  ARG A 166     3675   5624   8419    414   -420    554       C  
ATOM   1309  CD  ARG A 166     -22.858  30.991  33.493  1.00 47.71           C  
ANISOU 1309  CD  ARG A 166     3796   5753   8576    435   -478    571       C  
ATOM   1310  NE  ARG A 166     -22.298  29.710  33.119  1.00 48.95           N  
ANISOU 1310  NE  ARG A 166     3973   5907   8718    542   -491    553       N  
ATOM   1311  CZ  ARG A 166     -21.404  29.535  32.152  1.00 50.66           C  
ANISOU 1311  CZ  ARG A 166     4114   6195   8938    635   -456    560       C  
ATOM   1312  NH1 ARG A 166     -20.974  30.566  31.434  1.00 51.27           N  
ANISOU 1312  NH1 ARG A 166     4088   6358   9035    616   -401    592       N  
ATOM   1313  NH2 ARG A 166     -20.954  28.318  31.896  1.00 51.52           N  
ANISOU 1313  NH2 ARG A 166     4256   6291   9026    746   -477    534       N  
ATOM   1314  N   GLU A 167     -25.758  29.548  29.700  1.00 45.89           N  
ANISOU 1314  N   GLU A 167     3747   5466   8219    534   -352    465       N  
ATOM   1315  CA  GLU A 167     -25.355  29.159  28.322  1.00 47.17           C  
ANISOU 1315  CA  GLU A 167     3902   5661   8356    628   -312    455       C  
ATOM   1316  C   GLU A 167     -26.251  29.908  27.325  1.00 46.77           C  
ANISOU 1316  C   GLU A 167     3857   5620   8294    588   -268    449       C  
ATOM   1317  O   GLU A 167     -25.706  30.539  26.393  1.00 45.85           O  
ANISOU 1317  O   GLU A 167     3676   5567   8176    615   -217    466       O  
ATOM   1318  CB  GLU A 167     -25.445  27.639  28.165  1.00 48.37           C  
ANISOU 1318  CB  GLU A 167     4160   5752   8466    708   -351    422       C  
ATOM   1319  CG  GLU A 167     -24.968  27.127  26.817  1.00 50.00           C  
ANISOU 1319  CG  GLU A 167     4374   5988   8636    825   -315    404       C  
ATOM   1320  CD  GLU A 167     -25.174  25.640  26.571  1.00 51.41           C  
ANISOU 1320  CD  GLU A 167     4683   6087   8762    907   -366    365       C  
ATOM   1321  OE1 GLU A 167     -25.279  24.878  27.559  1.00 51.61           O  
ANISOU 1321  OE1 GLU A 167     4779   6044   8784    892   -437    359       O  
ATOM   1322  OE2 GLU A 167     -25.227  25.246  25.379  1.00 53.20           O  
ANISOU 1322  OE2 GLU A 167     4953   6314   8944    985   -340    343       O  
ATOM   1323  N   THR A 168     -27.575  29.852  27.550  1.00 46.80           N  
ANISOU 1323  N   THR A 168     3930   5565   8285    522   -289    428       N  
ATOM   1324  CA  THR A 168     -28.629  30.474  26.706  1.00 46.08           C  
ANISOU 1324  CA  THR A 168     3854   5468   8182    482   -264    416       C  
ATOM   1325  C   THR A 168     -28.414  31.984  26.640  1.00 46.38           C  
ANISOU 1325  C   THR A 168     3810   5557   8252    435   -236    441       C  
ATOM   1326  O   THR A 168     -28.401  32.507  25.521  1.00 47.12           O  
ANISOU 1326  O   THR A 168     3889   5678   8335    450   -201    447       O  
ATOM   1327  CB  THR A 168     -30.030  30.173  27.240  1.00 45.84           C  
ANISOU 1327  CB  THR A 168     3890   5384   8142    412   -299    392       C  
ATOM   1328  OG1 THR A 168     -30.125  28.767  27.468  1.00 46.10           O  
ANISOU 1328  OG1 THR A 168     4009   5363   8143    439   -340    378       O  
ATOM   1329  CG2 THR A 168     -31.125  30.627  26.296  1.00 45.50           C  
ANISOU 1329  CG2 THR A 168     3866   5335   8087    387   -284    376       C  
ATOM   1330  N   MET A 169     -28.260  32.647  27.788  1.00 47.13           N  
ANISOU 1330  N   MET A 169     3867   5659   8379    378   -257    457       N  
ATOM   1331  CA  MET A 169     -28.000  34.114  27.871  1.00 48.38           C  
ANISOU 1331  CA  MET A 169     3963   5853   8565    327   -249    485       C  
ATOM   1332  C   MET A 169     -26.794  34.460  26.992  1.00 50.67           C  
ANISOU 1332  C   MET A 169     4186   6207   8856    364   -213    522       C  
ATOM   1333  O   MET A 169     -26.907  35.413  26.188  1.00 52.14           O  
ANISOU 1333  O   MET A 169     4357   6416   9039    337   -192    537       O  
ATOM   1334  CB  MET A 169     -27.730  34.593  29.303  1.00 47.47           C  
ANISOU 1334  CB  MET A 169     3827   5731   8477    276   -286    499       C  
ATOM   1335  CG  MET A 169     -28.901  34.409  30.258  1.00 46.72           C  
ANISOU 1335  CG  MET A 169     3787   5590   8373    231   -312    466       C  
ATOM   1336  SD  MET A 169     -30.477  34.982  29.593  1.00 46.18           S  
ANISOU 1336  SD  MET A 169     3749   5508   8289    205   -299    429       S  
ATOM   1337  CE  MET A 169     -30.646  36.559  30.431  1.00 46.75           C  
ANISOU 1337  CE  MET A 169     3799   5584   8379    152   -322    432       C  
ATOM   1338  N   SER A 170     -25.700  33.704  27.112  1.00 53.50           N  
ANISOU 1338  N   SER A 170     4509   6600   9218    423   -207    537       N  
ATOM   1339  CA  SER A 170     -24.464  33.917  26.317  1.00 56.22           C  
ANISOU 1339  CA  SER A 170     4770   7031   9560    465   -165    573       C  
ATOM   1340  C   SER A 170     -24.815  33.983  24.830  1.00 58.06           C  
ANISOU 1340  C   SER A 170     5026   7280   9751    496   -115    563       C  
ATOM   1341  O   SER A 170     -24.655  35.065  24.243  1.00 58.74           O  
ANISOU 1341  O   SER A 170     5075   7406   9836    446    -92    596       O  
ATOM   1342  CB  SER A 170     -23.432  32.869  26.584  1.00 57.21           C  
ANISOU 1342  CB  SER A 170     4862   7189   9686    552   -168    574       C  
ATOM   1343  OG  SER A 170     -22.207  33.230  25.962  1.00 59.53           O  
ANISOU 1343  OG  SER A 170     5049   7588   9981    582   -124    615       O  
ATOM   1344  N   TYR A 171     -25.310  32.887  24.249  1.00 60.53           N  
ANISOU 1344  N   TYR A 171     5415   7556  10027    567   -107    521       N  
ATOM   1345  CA  TYR A 171     -25.689  32.811  22.811  1.00 62.91           C  
ANISOU 1345  CA  TYR A 171     5759   7862  10281    604    -66    507       C  
ATOM   1346  C   TYR A 171     -26.574  34.003  22.421  1.00 59.81           C  
ANISOU 1346  C   TYR A 171     5384   7447   9893    517    -69    514       C  
ATOM   1347  O   TYR A 171     -26.369  34.543  21.320  1.00 58.09           O  
ANISOU 1347  O   TYR A 171     5155   7268   9646    518    -30    532       O  
ATOM   1348  CB  TYR A 171     -26.362  31.479  22.482  1.00 67.47           C  
ANISOU 1348  CB  TYR A 171     6443   8370  10820    672    -85    458       C  
ATOM   1349  CG  TYR A 171     -25.372  30.403  22.094  1.00 72.43           C  
ANISOU 1349  CG  TYR A 171     7069   9033  11415    795    -64    446       C  
ATOM   1350  CD1 TYR A 171     -24.627  30.512  20.922  1.00 75.10           C  
ANISOU 1350  CD1 TYR A 171     7369   9450  11713    862      0    456       C  
ATOM   1351  CD2 TYR A 171     -25.145  29.301  22.914  1.00 75.53           C  
ANISOU 1351  CD2 TYR A 171     7499   9385  11811    847   -111    425       C  
ATOM   1352  CE1 TYR A 171     -23.706  29.540  20.562  1.00 78.69           C  
ANISOU 1352  CE1 TYR A 171     7817   9948  12132    992     23    439       C  
ATOM   1353  CE2 TYR A 171     -24.231  28.316  22.568  1.00 77.96           C  
ANISOU 1353  CE2 TYR A 171     7812   9722  12087    977   -101    407       C  
ATOM   1354  CZ  TYR A 171     -23.505  28.435  21.386  1.00 79.71           C  
ANISOU 1354  CZ  TYR A 171     7988  10029  12269   1057    -31    411       C  
ATOM   1355  OH  TYR A 171     -22.598  27.473  21.030  1.00 79.79           O  
ANISOU 1355  OH  TYR A 171     7997  10077  12240   1202    -17    387       O  
ATOM   1356  N   LEU A 172     -27.525  34.383  23.279  1.00 57.19           N  
ANISOU 1356  N   LEU A 172     5081   7058   9590    451   -116    499       N  
ATOM   1357  CA  LEU A 172     -28.506  35.469  22.994  1.00 55.74           C  
ANISOU 1357  CA  LEU A 172     4922   6844   9411    384   -132    494       C  
ATOM   1358  C   LEU A 172     -27.792  36.821  22.999  1.00 55.22           C  
ANISOU 1358  C   LEU A 172     4795   6823   9361    327   -128    542       C  
ATOM   1359  O   LEU A 172     -28.156  37.671  22.148  1.00 56.17           O  
ANISOU 1359  O   LEU A 172     4937   6939   9465    297   -126    550       O  
ATOM   1360  CB  LEU A 172     -29.646  35.458  24.018  1.00 55.07           C  
ANISOU 1360  CB  LEU A 172     4873   6703   9349    342   -179    461       C  
ATOM   1361  CG  LEU A 172     -30.674  34.332  23.871  1.00 54.26           C  
ANISOU 1361  CG  LEU A 172     4841   6550   9225    365   -193    419       C  
ATOM   1362  CD1 LEU A 172     -31.606  34.317  25.069  1.00 54.26           C  
ANISOU 1362  CD1 LEU A 172     4851   6520   9244    314   -230    396       C  
ATOM   1363  CD2 LEU A 172     -31.473  34.439  22.579  1.00 53.83           C  
ANISOU 1363  CD2 LEU A 172     4837   6474   9142    376   -188    401       C  
ATOM   1364  N   PHE A 173     -26.823  37.014  23.903  1.00 53.44           N  
ANISOU 1364  N   PHE A 173     4503   6634   9165    308   -137    575       N  
ATOM   1365  CA  PHE A 173     -26.053  38.277  24.039  1.00 53.27           C  
ANISOU 1365  CA  PHE A 173     4425   6655   9160    239   -148    630       C  
ATOM   1366  C   PHE A 173     -25.122  38.469  22.833  1.00 56.15           C  
ANISOU 1366  C   PHE A 173     4740   7100   9493    249    -93    674       C  
ATOM   1367  O   PHE A 173     -24.707  39.622  22.603  1.00 57.93           O  
ANISOU 1367  O   PHE A 173     4939   7353   9716    174   -104    723       O  
ATOM   1368  CB  PHE A 173     -25.286  38.310  25.362  1.00 51.60           C  
ANISOU 1368  CB  PHE A 173     4159   6457   8987    215   -180    655       C  
ATOM   1369  CG  PHE A 173     -26.112  38.468  26.612  1.00 49.99           C  
ANISOU 1369  CG  PHE A 173     4003   6184   8807    183   -234    623       C  
ATOM   1370  CD1 PHE A 173     -25.555  38.205  27.854  1.00 49.56           C  
ANISOU 1370  CD1 PHE A 173     3922   6129   8780    174   -265    634       C  
ATOM   1371  CD2 PHE A 173     -27.422  38.918  26.566  1.00 48.67           C  
ANISOU 1371  CD2 PHE A 173     3902   5958   8630    164   -255    582       C  
ATOM   1372  CE1 PHE A 173     -26.292  38.378  29.016  1.00 48.62           C  
ANISOU 1372  CE1 PHE A 173     3849   5952   8671    144   -309    605       C  
ATOM   1373  CE2 PHE A 173     -28.159  39.078  27.727  1.00 47.88           C  
ANISOU 1373  CE2 PHE A 173     3835   5811   8543    141   -295    551       C  
ATOM   1374  CZ  PHE A 173     -27.597  38.804  28.950  1.00 47.93           C  
ANISOU 1374  CZ  PHE A 173     3822   5818   8570    129   -319    563       C  
ATOM   1375  N   GLN A 174     -24.802  37.403  22.086  1.00 58.48           N  
ANISOU 1375  N   GLN A 174     5031   7433   9756    336    -40    658       N  
ATOM   1376  CA  GLN A 174     -24.068  37.486  20.788  1.00 59.89           C  
ANISOU 1376  CA  GLN A 174     5172   7694   9886    359     24    690       C  
ATOM   1377  C   GLN A 174     -24.845  38.384  19.826  1.00 59.18           C  
ANISOU 1377  C   GLN A 174     5150   7569   9766    305     20    693       C  
ATOM   1378  O   GLN A 174     -24.201  39.184  19.116  1.00 58.57           O  
ANISOU 1378  O   GLN A 174     5036   7556   9661    254     48    746       O  
ATOM   1379  CB  GLN A 174     -23.935  36.125  20.102  1.00 62.59           C  
ANISOU 1379  CB  GLN A 174     5536   8055  10187    480     73    651       C  
ATOM   1380  CG  GLN A 174     -23.265  35.053  20.946  1.00 64.42           C  
ANISOU 1380  CG  GLN A 174     5726   8307  10442    557     67    635       C  
ATOM   1381  CD  GLN A 174     -21.901  35.481  21.410  1.00 66.18           C  
ANISOU 1381  CD  GLN A 174     5818   8634  10692    536     82    693       C  
ATOM   1382  OE1 GLN A 174     -21.184  36.177  20.695  1.00 69.88           O  
ANISOU 1382  OE1 GLN A 174     6215   9197  11139    502    128    743       O  
ATOM   1383  NE2 GLN A 174     -21.540  35.073  22.620  1.00 67.12           N  
ANISOU 1383  NE2 GLN A 174     5904   8739  10857    547     38    690       N  
ATOM   1384  N   HIS A 175     -26.177  38.219  19.808  1.00 57.98           N  
ANISOU 1384  N   HIS A 175     5092   7321   9615    313    -15    640       N  
ATOM   1385  CA  HIS A 175     -27.130  38.910  18.901  1.00 56.89           C  
ANISOU 1385  CA  HIS A 175     5034   7132   9450    279    -33    628       C  
ATOM   1386  C   HIS A 175     -27.701  40.168  19.562  1.00 55.12           C  
ANISOU 1386  C   HIS A 175     4828   6854   9260    194   -102    635       C  
ATOM   1387  O   HIS A 175     -28.466  40.866  18.895  1.00 54.59           O  
ANISOU 1387  O   HIS A 175     4826   6740   9173    166   -131    626       O  
ATOM   1388  CB  HIS A 175     -28.231  37.941  18.461  1.00 56.59           C  
ANISOU 1388  CB  HIS A 175     5079   7027   9392    342    -39    566       C  
ATOM   1389  CG  HIS A 175     -27.721  36.719  17.774  1.00 57.57           C  
ANISOU 1389  CG  HIS A 175     5211   7187   9473    434     15    553       C  
ATOM   1390  ND1 HIS A 175     -27.592  36.627  16.395  1.00 57.83           N  
ANISOU 1390  ND1 HIS A 175     5285   7244   9444    467     59    557       N  
ATOM   1391  CD2 HIS A 175     -27.344  35.520  18.270  1.00 58.25           C  
ANISOU 1391  CD2 HIS A 175     5284   7282   9564    508     26    531       C  
ATOM   1392  CE1 HIS A 175     -27.140  35.427  16.081  1.00 59.19           C  
ANISOU 1392  CE1 HIS A 175     5466   7440   9581    565     98    536       C  
ATOM   1393  NE2 HIS A 175     -26.981  34.725  17.214  1.00 58.75           N  
ANISOU 1393  NE2 HIS A 175     5380   7373   9568    592     75    519       N  
ATOM   1394  N   ALA A 176     -27.352  40.443  20.817  1.00 54.19           N  
ANISOU 1394  N   ALA A 176     4664   6739   9186    162   -134    648       N  
ATOM   1395  CA  ALA A 176     -27.660  41.719  21.501  1.00 54.25           C  
ANISOU 1395  CA  ALA A 176     4691   6702   9218     87   -203    660       C  
ATOM   1396  C   ALA A 176     -26.633  42.753  21.051  1.00 55.17           C  
ANISOU 1396  C   ALA A 176     4776   6869   9317     10   -205    735       C  
ATOM   1397  O   ALA A 176     -25.534  42.353  20.694  1.00 55.96           O  
ANISOU 1397  O   ALA A 176     4802   7056   9402     16   -149    778       O  
ATOM   1398  CB  ALA A 176     -27.638  41.546  22.998  1.00 54.07           C  
ANISOU 1398  CB  ALA A 176     4642   6661   9239     83   -236    646       C  
ATOM   1399  N   ASN A 177     -27.003  44.030  21.030  1.00 57.04           N  
ANISOU 1399  N   ASN A 177     5069   7054   9550    -58   -270    749       N  
ATOM   1400  CA  ASN A 177     -26.072  45.154  20.751  1.00 58.37           C  
ANISOU 1400  CA  ASN A 177     5223   7256   9699   -157   -295    829       C  
ATOM   1401  C   ASN A 177     -25.457  45.552  22.093  1.00 58.52           C  
ANISOU 1401  C   ASN A 177     5199   7275   9759   -204   -344    858       C  
ATOM   1402  O   ASN A 177     -26.069  46.353  22.821  1.00 57.25           O  
ANISOU 1402  O   ASN A 177     5105   7033   9614   -230   -425    836       O  
ATOM   1403  CB  ASN A 177     -26.774  46.310  20.035  1.00 59.23           C  
ANISOU 1403  CB  ASN A 177     5434   7293   9775   -208   -357    831       C  
ATOM   1404  CG  ASN A 177     -25.854  47.471  19.737  1.00 60.86           C  
ANISOU 1404  CG  ASN A 177     5644   7525   9954   -326   -395    920       C  
ATOM   1405  OD1 ASN A 177     -24.650  47.394  19.968  1.00 60.78           O  
ANISOU 1405  OD1 ASN A 177     5541   7603   9949   -374   -364    985       O  
ATOM   1406  ND2 ASN A 177     -26.419  48.558  19.239  1.00 62.51           N  
ANISOU 1406  ND2 ASN A 177     5959   7657  10133   -377   -469    924       N  
ATOM   1407  N   LEU A 178     -24.299  44.975  22.410  1.00 60.04           N  
ANISOU 1407  N   LEU A 178     5287   7558   9967   -205   -300    900       N  
ATOM   1408  CA  LEU A 178     -23.560  45.211  23.677  1.00 60.38           C  
ANISOU 1408  CA  LEU A 178     5279   7611  10050   -248   -346    933       C  
ATOM   1409  C   LEU A 178     -22.179  45.795  23.373  1.00 61.87           C  
ANISOU 1409  C   LEU A 178     5385   7893  10227   -343   -342   1033       C  
ATOM   1410  O   LEU A 178     -21.354  45.801  24.283  1.00 63.18           O  
ANISOU 1410  O   LEU A 178     5484   8092  10428   -375   -369   1070       O  
ATOM   1411  CB  LEU A 178     -23.454  43.880  24.428  1.00 59.76           C  
ANISOU 1411  CB  LEU A 178     5145   7555  10005   -159   -306    892       C  
ATOM   1412  CG  LEU A 178     -24.782  43.273  24.881  1.00 58.52           C  
ANISOU 1412  CG  LEU A 178     5062   7315   9857    -85   -314    803       C  
ATOM   1413  CD1 LEU A 178     -24.563  41.903  25.505  1.00 57.97           C  
ANISOU 1413  CD1 LEU A 178     4947   7269   9809     -9   -278    773       C  
ATOM   1414  CD2 LEU A 178     -25.491  44.198  25.863  1.00 57.81           C  
ANISOU 1414  CD2 LEU A 178     5044   7137   9782   -126   -398    780       C  
ATOM   1415  N   ASP A 179     -21.964  46.296  22.154  1.00 64.15           N  
ANISOU 1415  N   ASP A 179     5681   8223  10468   -393   -316   1077       N  
ATOM   1416  CA  ASP A 179     -20.652  46.780  21.638  1.00 66.90           C  
ANISOU 1416  CA  ASP A 179     5938   8688  10792   -492   -294   1179       C  
ATOM   1417  C   ASP A 179     -20.040  47.823  22.583  1.00 66.28           C  
ANISOU 1417  C   ASP A 179     5855   8588  10739   -613   -394   1246       C  
ATOM   1418  O   ASP A 179     -18.827  47.718  22.868  1.00 68.72           O  
ANISOU 1418  O   ASP A 179     6041   9005  11065   -660   -378   1315       O  
ATOM   1419  CB  ASP A 179     -20.798  47.378  20.235  1.00 68.86           C  
ANISOU 1419  CB  ASP A 179     6238   8952  10973   -546   -270   1212       C  
ATOM   1420  CG  ASP A 179     -21.403  46.427  19.221  1.00 70.08           C  
ANISOU 1420  CG  ASP A 179     6414   9120  11094   -434   -181   1150       C  
ATOM   1421  OD1 ASP A 179     -21.571  45.233  19.560  1.00 71.74           O  
ANISOU 1421  OD1 ASP A 179     6585   9340  11331   -316   -131   1089       O  
ATOM   1422  OD2 ASP A 179     -21.699  46.891  18.103  1.00 71.75           O  
ANISOU 1422  OD2 ASP A 179     6690   9322  11247   -470   -169   1165       O  
ATOM   1423  N   SER A 180     -20.839  48.792  23.042  1.00 63.54           N  
ANISOU 1423  N   SER A 180     5640   8110  10393   -657   -498   1226       N  
ATOM   1424  CA  SER A 180     -20.391  49.952  23.856  1.00 62.58           C  
ANISOU 1424  CA  SER A 180     5557   7939  10282   -779   -616   1286       C  
ATOM   1425  C   SER A 180     -20.282  49.578  25.341  1.00 60.82           C  
ANISOU 1425  C   SER A 180     5310   7684  10115   -740   -656   1257       C  
ATOM   1426  O   SER A 180     -19.931  50.466  26.132  1.00 60.85           O  
ANISOU 1426  O   SER A 180     5355   7637  10128   -830   -760   1300       O  
ATOM   1427  CB  SER A 180     -21.304  51.130  23.654  1.00 62.33           C  
ANISOU 1427  CB  SER A 180     5691   7775  10216   -825   -715   1269       C  
ATOM   1428  OG  SER A 180     -22.607  50.841  24.134  1.00 60.97           O  
ANISOU 1428  OG  SER A 180     5604   7499  10061   -710   -730   1160       O  
ATOM   1429  N   CYS A 181     -20.571  48.326  25.712  1.00 58.76           N  
ANISOU 1429  N   CYS A 181     4997   7442   9884   -616   -586   1188       N  
ATOM   1430  CA  CYS A 181     -20.304  47.775  27.070  1.00 59.13           C  
ANISOU 1430  CA  CYS A 181     5006   7478   9980   -579   -610   1167       C  
ATOM   1431  C   CYS A 181     -18.804  47.496  27.216  1.00 60.79           C  
ANISOU 1431  C   CYS A 181     5069   7813  10214   -628   -591   1251       C  
ATOM   1432  O   CYS A 181     -18.170  47.067  26.230  1.00 62.42           O  
ANISOU 1432  O   CYS A 181     5174   8138  10402   -620   -506   1287       O  
ATOM   1433  CB  CYS A 181     -21.078  46.492  27.343  1.00 59.04           C  
ANISOU 1433  CB  CYS A 181     4996   7449   9986   -442   -546   1073       C  
ATOM   1434  SG  CYS A 181     -22.880  46.714  27.411  1.00 60.23           S  
ANISOU 1434  SG  CYS A 181     5297   7469  10119   -379   -571    971       S  
ATOM   1435  N   LYS A 182     -18.257  47.709  28.413  1.00 59.93           N  
ANISOU 1435  N   LYS A 182     4945   7684  10141   -672   -667   1278       N  
ATOM   1436  CA  LYS A 182     -16.796  47.681  28.666  1.00 60.39           C  
ANISOU 1436  CA  LYS A 182     4862   7854  10225   -741   -678   1370       C  
ATOM   1437  C   LYS A 182     -16.556  47.327  30.132  1.00 59.61           C  
ANISOU 1437  C   LYS A 182     4762   7712  10175   -719   -741   1353       C  
ATOM   1438  O   LYS A 182     -17.261  47.882  30.998  1.00 58.99           O  
ANISOU 1438  O   LYS A 182     4813   7505  10094   -734   -824   1316       O  
ATOM   1439  CB  LYS A 182     -16.191  49.046  28.321  1.00 62.32           C  
ANISOU 1439  CB  LYS A 182     5119   8113  10445   -908   -753   1472       C  
ATOM   1440  CG  LYS A 182     -14.703  49.034  28.000  1.00 64.21           C  
ANISOU 1440  CG  LYS A 182     5184   8517  10695   -993   -729   1580       C  
ATOM   1441  CD  LYS A 182     -14.103  50.413  27.813  1.00 66.29           C  
ANISOU 1441  CD  LYS A 182     5469   8786  10932  -1182   -823   1692       C  
ATOM   1442  CE  LYS A 182     -13.645  51.052  29.111  1.00 67.01           C  
ANISOU 1442  CE  LYS A 182     5595   8806  11057  -1274   -962   1736       C  
ATOM   1443  NZ  LYS A 182     -12.911  52.320  28.876  1.00 68.41           N  
ANISOU 1443  NZ  LYS A 182     5781   9003  11206  -1473  -1058   1860       N  
ATOM   1444  N   ARG A 183     -15.586  46.444  30.381  1.00 59.89           N  
ANISOU 1444  N   ARG A 183     4657   7852  10246   -679   -704   1376       N  
ATOM   1445  CA  ARG A 183     -15.154  46.007  31.735  1.00 59.71           C  
ANISOU 1445  CA  ARG A 183     4614   7802  10269   -660   -766   1371       C  
ATOM   1446  C   ARG A 183     -13.626  46.074  31.805  1.00 61.63           C  
ANISOU 1446  C   ARG A 183     4693   8178  10545   -731   -787   1471       C  
ATOM   1447  O   ARG A 183     -12.977  45.830  30.765  1.00 61.69           O  
ANISOU 1447  O   ARG A 183     4571   8326  10541   -726   -704   1512       O  
ATOM   1448  CB  ARG A 183     -15.689  44.597  32.006  1.00 58.30           C  
ANISOU 1448  CB  ARG A 183     4440   7607  10103   -506   -700   1278       C  
ATOM   1449  CG  ARG A 183     -15.291  43.990  33.345  1.00 57.93           C  
ANISOU 1449  CG  ARG A 183     4383   7529  10096   -475   -758   1266       C  
ATOM   1450  CD  ARG A 183     -15.958  42.642  33.561  1.00 57.49           C  
ANISOU 1450  CD  ARG A 183     4361   7440  10040   -337   -702   1175       C  
ATOM   1451  NE  ARG A 183     -17.088  42.713  34.481  1.00 57.39           N  
ANISOU 1451  NE  ARG A 183     4499   7293  10014   -327   -745   1110       N  
ATOM   1452  CZ  ARG A 183     -18.070  41.816  34.591  1.00 56.62           C  
ANISOU 1452  CZ  ARG A 183     4470   7142   9898   -237   -700   1028       C  
ATOM   1453  NH1 ARG A 183     -18.106  40.737  33.821  1.00 57.03           N  
ANISOU 1453  NH1 ARG A 183     4474   7248   9945   -142   -620    996       N  
ATOM   1454  NH2 ARG A 183     -19.028  42.009  35.481  1.00 55.76           N  
ANISOU 1454  NH2 ARG A 183     4483   6929   9772   -243   -740    978       N  
ATOM   1455  N   VAL A 184     -13.084  46.405  32.980  1.00 63.01           N  
ANISOU 1455  N   VAL A 184     4873   8314  10754   -794   -893   1509       N  
ATOM   1456  CA  VAL A 184     -11.618  46.401  33.256  1.00 66.06           C  
ANISOU 1456  CA  VAL A 184     5095   8822  11181   -860   -931   1602       C  
ATOM   1457  C   VAL A 184     -11.370  45.667  34.585  1.00 67.44           C  
ANISOU 1457  C   VAL A 184     5270   8949  11402   -797   -991   1570       C  
ATOM   1458  O   VAL A 184     -11.869  46.140  35.633  1.00 65.87           O  
ANISOU 1458  O   VAL A 184     5214   8610  11203   -834  -1087   1549       O  
ATOM   1459  CB  VAL A 184     -11.055  47.835  33.239  1.00 66.79           C  
ANISOU 1459  CB  VAL A 184     5196   8916  11262  -1050  -1031   1711       C  
ATOM   1460  CG1 VAL A 184      -9.573  47.877  33.571  1.00 68.48           C  
ANISOU 1460  CG1 VAL A 184     5236   9261  11521  -1133  -1080   1815       C  
ATOM   1461  CG2 VAL A 184     -11.309  48.504  31.900  1.00 66.68           C  
ANISOU 1461  CG2 VAL A 184     5193   8946  11196  -1113   -974   1743       C  
ATOM   1462  N   LEU A 185     -10.630  44.550  34.514  1.00 70.80           N  
ANISOU 1462  N   LEU A 185     5549   9488  11861   -698   -935   1565       N  
ATOM   1463  CA  LEU A 185     -10.282  43.637  35.641  1.00 73.38           C  
ANISOU 1463  CA  LEU A 185     5860   9787  12232   -619   -984   1533       C  
ATOM   1464  C   LEU A 185      -8.772  43.676  35.895  1.00 76.60           C  
ANISOU 1464  C   LEU A 185     6085  10329  12690   -672  -1036   1626       C  
ATOM   1465  O   LEU A 185      -8.015  43.757  34.912  1.00 76.79           O  
ANISOU 1465  O   LEU A 185     5947  10516  12713   -693   -971   1685       O  
ATOM   1466  CB  LEU A 185     -10.704  42.210  35.280  1.00 73.11           C  
ANISOU 1466  CB  LEU A 185     5814   9770  12191   -441   -884   1441       C  
ATOM   1467  CG  LEU A 185     -12.186  41.898  35.447  1.00 73.07           C  
ANISOU 1467  CG  LEU A 185     5993   9620  12149   -378   -858   1342       C  
ATOM   1468  CD1 LEU A 185     -12.583  40.676  34.627  1.00 72.69           C  
ANISOU 1468  CD1 LEU A 185     5924   9612  12081   -229   -747   1271       C  
ATOM   1469  CD2 LEU A 185     -12.522  41.709  36.917  1.00 73.67           C  
ANISOU 1469  CD2 LEU A 185     6185   9566  12239   -377   -951   1308       C  
ATOM   1470  N   ASN A 186      -8.364  43.553  37.161  1.00 79.64           N  
ANISOU 1470  N   ASN A 186     6490  10653  13114   -687  -1145   1637       N  
ATOM   1471  CA  ASN A 186      -6.941  43.589  37.593  1.00 83.44           C  
ANISOU 1471  CA  ASN A 186     6803  11248  13652   -741  -1219   1726       C  
ATOM   1472  C   ASN A 186      -6.670  42.414  38.541  1.00 84.39           C  
ANISOU 1472  C   ASN A 186     6913  11339  13812   -616  -1258   1673       C  
ATOM   1473  O   ASN A 186      -7.419  42.284  39.520  1.00 85.91           O  
ANISOU 1473  O   ASN A 186     7279  11367  13993   -600  -1318   1616       O  
ATOM   1474  CB  ASN A 186      -6.605  44.930  38.249  1.00 84.67           C  
ANISOU 1474  CB  ASN A 186     7011  11344  13813   -932  -1357   1816       C  
ATOM   1475  CG  ASN A 186      -5.153  45.324  38.078  1.00 87.76           C  
ANISOU 1475  CG  ASN A 186     7192  11904  14247  -1038  -1403   1938       C  
ATOM   1476  OD1 ASN A 186      -4.373  44.599  37.461  1.00 89.42           O  
ANISOU 1476  OD1 ASN A 186     7202  12289  14482   -960  -1324   1953       O  
ATOM   1477  ND2 ASN A 186      -4.762  46.460  38.636  1.00 89.96           N  
ANISOU 1477  ND2 ASN A 186     7512  12135  14531  -1214  -1535   2027       N  
ATOM   1478  N   VAL A 187      -5.638  41.608  38.260  1.00 86.06           N  
ANISOU 1478  N   VAL A 187     6930  11705  14062   -530  -1227   1692       N  
ATOM   1479  CA  VAL A 187      -5.213  40.425  39.071  1.00 86.69           C  
ANISOU 1479  CA  VAL A 187     6982  11772  14182   -398  -1272   1646       C  
ATOM   1480  C   VAL A 187      -3.821  40.702  39.663  1.00 89.29           C  
ANISOU 1480  C   VAL A 187     7147  12201  14575   -470  -1380   1741       C  
ATOM   1481  O   VAL A 187      -2.846  40.737  38.884  1.00 87.32           O  
ANISOU 1481  O   VAL A 187     6679  12151  14348   -473  -1332   1803       O  
ATOM   1482  CB  VAL A 187      -5.214  39.131  38.231  1.00 87.82           C  
ANISOU 1482  CB  VAL A 187     7046  12005  14314   -205  -1153   1573       C  
ATOM   1483  CG1 VAL A 187      -4.939  37.897  39.089  1.00 88.40           C  
ANISOU 1483  CG1 VAL A 187     7136  12033  14419    -64  -1212   1516       C  
ATOM   1484  CG2 VAL A 187      -6.504  38.972  37.441  1.00 86.81           C  
ANISOU 1484  CG2 VAL A 187     7055  11804  14123   -155  -1043   1497       C  
ATOM   1485  N   VAL A 188      -3.741  40.870  40.989  1.00 90.27           N  
ANISOU 1485  N   VAL A 188     7372  12199  14725   -526  -1520   1752       N  
ATOM   1486  CA  VAL A 188      -2.519  41.302  41.734  1.00 91.40           C  
ANISOU 1486  CA  VAL A 188     7395  12402  14928   -625  -1655   1850       C  
ATOM   1487  C   VAL A 188      -1.955  40.104  42.513  1.00 92.57           C  
ANISOU 1487  C   VAL A 188     7498  12549  15124   -485  -1715   1809       C  
ATOM   1488  O   VAL A 188      -2.601  39.695  43.507  1.00 91.16           O  
ANISOU 1488  O   VAL A 188     7511  12194  14931   -447  -1780   1745       O  
ATOM   1489  CB  VAL A 188      -2.841  42.476  42.686  1.00 90.19           C  
ANISOU 1489  CB  VAL A 188     7413  12090  14763   -801  -1788   1896       C  
ATOM   1490  CG1 VAL A 188      -1.635  42.881  43.531  1.00 91.85           C  
ANISOU 1490  CG1 VAL A 188     7524  12341  15034   -907  -1944   1994       C  
ATOM   1491  CG2 VAL A 188      -3.408  43.677  41.942  1.00 88.85           C  
ANISOU 1491  CG2 VAL A 188     7308  11906  14544   -933  -1747   1933       C  
ATOM   1492  N   CYS A 189      -0.797  39.576  42.091  1.00 94.98           N  
ANISOU 1492  N   CYS A 189     7562  13047  15478   -411  -1698   1844       N  
ATOM   1493  CA  CYS A 189       0.063  38.646  42.882  1.00 96.06           C  
ANISOU 1493  CA  CYS A 189     7614  13208  15673   -302  -1792   1833       C  
ATOM   1494  C   CYS A 189       1.352  39.386  43.267  1.00 96.93           C  
ANISOU 1494  C   CYS A 189     7541  13438  15849   -437  -1908   1957       C  
ATOM   1495  O   CYS A 189       1.894  40.115  42.414  1.00 98.21           O  
ANISOU 1495  O   CYS A 189     7530  13770  16015   -536  -1854   2040       O  
ATOM   1496  CB  CYS A 189       0.377  37.362  42.119  1.00 97.74           C  
ANISOU 1496  CB  CYS A 189     7695  13550  15891    -81  -1690   1764       C  
ATOM   1497  SG  CYS A 189       1.219  36.099  43.116  1.00100.45           S  
ANISOU 1497  SG  CYS A 189     7988  13883  16294     83  -1814   1725       S  
ATOM   1498  N   LYS A 190       1.805  39.220  44.513  1.00 95.85           N  
ANISOU 1498  N   LYS A 190     7447  13213  15756   -453  -2067   1972       N  
ATOM   1499  CA  LYS A 190       3.031  39.867  45.053  1.00 96.69           C  
ANISOU 1499  CA  LYS A 190     7395  13412  15929   -586  -2207   2091       C  
ATOM   1500  C   LYS A 190       4.271  39.285  44.358  1.00 99.06           C  
ANISOU 1500  C   LYS A 190     7372  13978  16286   -482  -2160   2125       C  
ATOM   1501  O   LYS A 190       5.305  39.984  44.336  1.00 98.07           O  
ANISOU 1501  O   LYS A 190     7050  14002  16209   -614  -2226   2242       O  
ATOM   1502  CB  LYS A 190       3.071  39.717  46.576  1.00 95.51           C  
ANISOU 1502  CB  LYS A 190     7405  13079  15804   -608  -2387   2082       C  
ATOM   1503  CG  LYS A 190       2.054  40.580  47.311  1.00 93.12           C  
ANISOU 1503  CG  LYS A 190     7388  12546  15445   -747  -2449   2076       C  
ATOM   1504  CD  LYS A 190       1.783  40.112  48.716  1.00 92.42           C  
ANISOU 1504  CD  LYS A 190     7502  12257  15353   -714  -2582   2027       C  
ATOM   1505  CE  LYS A 190       0.973  41.105  49.521  1.00 91.07           C  
ANISOU 1505  CE  LYS A 190     7591  11884  15127   -864  -2661   2036       C  
ATOM   1506  NZ  LYS A 190       0.991  40.761  50.963  1.00 90.95           N  
ANISOU 1506  NZ  LYS A 190     7742  11701  15114   -857  -2814   2013       N  
ATOM   1507  N   THR A 191       4.160  38.071  43.798  1.00100.23           N  
ANISOU 1507  N   THR A 191     7471  14186  16424   -256  -2053   2027       N  
ATOM   1508  CA  THR A 191       5.198  37.402  42.960  1.00102.25           C  
ANISOU 1508  CA  THR A 191     7430  14705  16716   -112  -1975   2034       C  
ATOM   1509  C   THR A 191       5.162  37.964  41.529  1.00102.42           C  
ANISOU 1509  C   THR A 191     7313  14908  16694   -164  -1805   2073       C  
ATOM   1510  O   THR A 191       6.123  38.684  41.166  1.00103.42           O  
ANISOU 1510  O   THR A 191     7207  15235  16852   -289  -1811   2187       O  
ATOM   1511  CB  THR A 191       5.030  35.873  42.937  1.00101.97           C  
ANISOU 1511  CB  THR A 191     7432  14637  16672    159  -1939   1906       C  
ATOM   1512  OG1 THR A 191       4.610  35.423  44.226  1.00101.27           O  
ANISOU 1512  OG1 THR A 191     7569  14317  16593    183  -2079   1855       O  
ATOM   1513  CG2 THR A 191       6.301  35.147  42.549  1.00103.55           C  
ANISOU 1513  CG2 THR A 191     7337  15079  16926    320  -1929   1913       C  
ATOM   1514  N   CYS A 192       4.092  37.680  40.771  1.00 99.67           N  
ANISOU 1514  N   CYS A 192     7107  14488  16273    -87  -1667   1988       N  
ATOM   1515  CA  CYS A 192       4.000  37.884  39.295  1.00 98.82           C  
ANISOU 1515  CA  CYS A 192     6880  14551  16114    -74  -1487   1996       C  
ATOM   1516  C   CYS A 192       3.490  39.289  38.932  1.00 95.83           C  
ANISOU 1516  C   CYS A 192     6580  14133  15694   -314  -1466   2077       C  
ATOM   1517  O   CYS A 192       3.211  39.499  37.740  1.00 94.86           O  
ANISOU 1517  O   CYS A 192     6412  14110  15517   -315  -1321   2076       O  
ATOM   1518  CB  CYS A 192       3.077  36.855  38.642  1.00 98.96           C  
ANISOU 1518  CB  CYS A 192     7027  14500  16071    129  -1360   1863       C  
ATOM   1519  SG  CYS A 192       2.809  35.348  39.613  1.00101.61           S  
ANISOU 1519  SG  CYS A 192     7515  14665  16426    356  -1447   1737       S  
ATOM   1520  N   GLY A 193       3.352  40.198  39.908  1.00 93.49           N  
ANISOU 1520  N   GLY A 193     6414  13689  15418   -501  -1610   2138       N  
ATOM   1521  CA  GLY A 193       2.892  41.585  39.693  1.00 91.51           C  
ANISOU 1521  CA  GLY A 193     6264  13377  15129   -731  -1623   2216       C  
ATOM   1522  C   GLY A 193       1.431  41.647  39.264  1.00 88.53           C  
ANISOU 1522  C   GLY A 193     6129  12831  14675   -701  -1531   2127       C  
ATOM   1523  O   GLY A 193       0.618  40.850  39.795  1.00 86.52           O  
ANISOU 1523  O   GLY A 193     6054  12410  14409   -568  -1536   2018       O  
ATOM   1524  N   GLN A 194       1.114  42.555  38.331  1.00 86.81           N  
ANISOU 1524  N   GLN A 194     5915  12659  14407   -826  -1456   2176       N  
ATOM   1525  CA  GLN A 194      -0.269  42.944  37.945  1.00 83.22           C  
ANISOU 1525  CA  GLN A 194     5696  12040  13882   -847  -1394   2115       C  
ATOM   1526  C   GLN A 194      -0.643  42.329  36.590  1.00 81.81           C  
ANISOU 1526  C   GLN A 194     5458  11969  13654   -712  -1209   2053       C  
ATOM   1527  O   GLN A 194       0.275  42.005  35.810  1.00 80.50           O  
ANISOU 1527  O   GLN A 194     5057  12031  13498   -663  -1128   2091       O  
ATOM   1528  CB  GLN A 194      -0.395  44.468  37.872  1.00 83.81           C  
ANISOU 1528  CB  GLN A 194     5846  12068  13930  -1087  -1461   2214       C  
ATOM   1529  CG  GLN A 194      -0.420  45.150  39.235  1.00 84.03           C  
ANISOU 1529  CG  GLN A 194     6023  11920  13982  -1214  -1647   2250       C  
ATOM   1530  CD  GLN A 194      -1.078  46.507  39.194  1.00 84.05           C  
ANISOU 1530  CD  GLN A 194     6208  11792  13934  -1397  -1705   2294       C  
ATOM   1531  OE1 GLN A 194      -1.344  47.062  38.126  1.00 84.65           O  
ANISOU 1531  OE1 GLN A 194     6273  11927  13961  -1460  -1620   2322       O  
ATOM   1532  NE2 GLN A 194      -1.353  47.048  40.370  1.00 83.54           N  
ANISOU 1532  NE2 GLN A 194     6325  11541  13873  -1477  -1856   2299       N  
ATOM   1533  N   GLN A 195      -1.956  42.174  36.347  1.00 79.83           N  
ANISOU 1533  N   GLN A 195     5419  11562  13351   -652  -1148   1960       N  
ATOM   1534  CA  GLN A 195      -2.563  41.687  35.072  1.00 77.67           C  
ANISOU 1534  CA  GLN A 195     5147  11342  13018   -538   -984   1894       C  
ATOM   1535  C   GLN A 195      -3.956  42.301  34.889  1.00 74.89           C  
ANISOU 1535  C   GLN A 195     5035  10808  12610   -599   -969   1850       C  
ATOM   1536  O   GLN A 195      -4.912  41.783  35.515  1.00 74.19           O  
ANISOU 1536  O   GLN A 195     5128  10544  12515   -514   -991   1756       O  
ATOM   1537  CB  GLN A 195      -2.680  40.162  35.057  1.00 76.91           C  
ANISOU 1537  CB  GLN A 195     5042  11251  12929   -298   -924   1783       C  
ATOM   1538  CG  GLN A 195      -3.171  39.623  33.717  1.00 76.73           C  
ANISOU 1538  CG  GLN A 195     5010  11296  12844   -177   -763   1721       C  
ATOM   1539  CD  GLN A 195      -3.581  38.173  33.788  1.00 76.76           C  
ANISOU 1539  CD  GLN A 195     5081  11241  12841     46   -725   1601       C  
ATOM   1540  OE1 GLN A 195      -4.726  37.854  34.123  1.00 75.60           O  
ANISOU 1540  OE1 GLN A 195     5144  10908  12671     85   -736   1522       O  
ATOM   1541  NE2 GLN A 195      -2.648  37.282  33.455  1.00 78.18           N  
ANISOU 1541  NE2 GLN A 195     5081  11584  13037    197   -682   1587       N  
ATOM   1542  N   GLN A 196      -4.080  43.340  34.053  1.00 73.38           N  
ANISOU 1542  N   GLN A 196     4842  10661  12377   -738   -933   1914       N  
ATOM   1543  CA  GLN A 196      -5.388  43.983  33.753  1.00 70.77           C  
ANISOU 1543  CA  GLN A 196     4728  10170  11991   -790   -918   1873       C  
ATOM   1544  C   GLN A 196      -5.823  43.577  32.341  1.00 70.63           C  
ANISOU 1544  C   GLN A 196     4685  10234  11917   -699   -761   1829       C  
ATOM   1545  O   GLN A 196      -4.947  43.458  31.452  1.00 71.01           O  
ANISOU 1545  O   GLN A 196     4539  10486  11955   -694   -679   1882       O  
ATOM   1546  CB  GLN A 196      -5.341  45.504  33.955  1.00 69.99           C  
ANISOU 1546  CB  GLN A 196     4698  10014  11878  -1013  -1022   1970       C  
ATOM   1547  CG  GLN A 196      -5.318  46.315  32.658  1.00 69.94           C  
ANISOU 1547  CG  GLN A 196     4651  10104  11816  -1121   -950   2035       C  
ATOM   1548  CD  GLN A 196      -5.895  47.702  32.805  1.00 69.14           C  
ANISOU 1548  CD  GLN A 196     4728   9860  11680  -1297  -1050   2080       C  
ATOM   1549  OE1 GLN A 196      -5.868  48.294  33.883  1.00 68.27           O  
ANISOU 1549  OE1 GLN A 196     4715   9629  11593  -1386  -1191   2106       O  
ATOM   1550  NE2 GLN A 196      -6.445  48.218  31.717  1.00 68.56           N  
ANISOU 1550  NE2 GLN A 196     4713   9791  11545  -1340   -982   2084       N  
ATOM   1551  N   THR A 197      -7.130  43.353  32.172  1.00 69.57           N  
ANISOU 1551  N   THR A 197     4736   9951  11745   -628   -723   1734       N  
ATOM   1552  CA  THR A 197      -7.787  42.941  30.903  1.00 69.64           C  
ANISOU 1552  CA  THR A 197     4769   9993  11696   -536   -588   1677       C  
ATOM   1553  C   THR A 197      -8.902  43.944  30.558  1.00 68.43           C  
ANISOU 1553  C   THR A 197     4797   9706  11496   -637   -603   1671       C  
ATOM   1554  O   THR A 197      -9.583  44.423  31.485  1.00 65.81           O  
ANISOU 1554  O   THR A 197     4622   9207  11175   -688   -700   1648       O  
ATOM   1555  CB  THR A 197      -8.327  41.508  31.009  1.00 68.92           C  
ANISOU 1555  CB  THR A 197     4727   9850  11607   -330   -534   1560       C  
ATOM   1556  OG1 THR A 197      -9.287  41.509  32.067  1.00 69.10           O  
ANISOU 1556  OG1 THR A 197     4936   9673  11642   -332   -616   1502       O  
ATOM   1557  CG2 THR A 197      -7.258  40.467  31.275  1.00 68.63           C  
ANISOU 1557  CG2 THR A 197     4525   9939  11612   -207   -523   1556       C  
ATOM   1558  N   THR A 198      -9.067  44.248  29.267  1.00 69.37           N  
ANISOU 1558  N   THR A 198     4898   9899  11560   -660   -512   1688       N  
ATOM   1559  CA  THR A 198     -10.094  45.174  28.724  1.00 68.88           C  
ANISOU 1559  CA  THR A 198     4999   9725  11446   -744   -519   1681       C  
ATOM   1560  C   THR A 198     -10.984  44.399  27.748  1.00 67.86           C  
ANISOU 1560  C   THR A 198     4929   9580  11272   -606   -403   1590       C  
ATOM   1561  O   THR A 198     -10.605  44.277  26.555  1.00 67.22           O  
ANISOU 1561  O   THR A 198     4756   9636  11148   -592   -302   1615       O  
ATOM   1562  CB  THR A 198      -9.460  46.428  28.111  1.00 71.37           C  
ANISOU 1562  CB  THR A 198     5259  10125  11730   -934   -544   1801       C  
ATOM   1563  OG1 THR A 198      -9.077  47.248  29.215  1.00 73.59           O  
ANISOU 1563  OG1 THR A 198     5571  10338  12050  -1066   -687   1864       O  
ATOM   1564  CG2 THR A 198     -10.381  47.197  27.188  1.00 70.52           C  
ANISOU 1564  CG2 THR A 198     5294   9942  11558   -994   -524   1794       C  
ATOM   1565  N   LEU A 199     -12.130  43.922  28.264  1.00 66.45           N  
ANISOU 1565  N   LEU A 199     4902   9244  11099   -515   -421   1491       N  
ATOM   1566  CA  LEU A 199     -13.180  43.198  27.507  1.00 64.25           C  
ANISOU 1566  CA  LEU A 199     4714   8914  10782   -392   -337   1398       C  
ATOM   1567  C   LEU A 199     -14.204  44.203  26.983  1.00 62.55           C  
ANISOU 1567  C   LEU A 199     4644   8597  10524   -475   -356   1393       C  
ATOM   1568  O   LEU A 199     -14.481  45.186  27.686  1.00 61.25           O  
ANISOU 1568  O   LEU A 199     4567   8332  10370   -581   -457   1417       O  
ATOM   1569  CB  LEU A 199     -13.821  42.155  28.430  1.00 63.44           C  
ANISOU 1569  CB  LEU A 199     4688   8705  10709   -268   -358   1304       C  
ATOM   1570  CG  LEU A 199     -12.854  41.111  28.998  1.00 64.78           C  
ANISOU 1570  CG  LEU A 199     4736   8957  10920   -174   -355   1301       C  
ATOM   1571  CD1 LEU A 199     -13.465  40.331  30.159  1.00 63.22           C  
ANISOU 1571  CD1 LEU A 199     4640   8630  10751    -98   -410   1227       C  
ATOM   1572  CD2 LEU A 199     -12.373  40.160  27.906  1.00 66.00           C  
ANISOU 1572  CD2 LEU A 199     4784   9247  11046    -48   -242   1282       C  
ATOM   1573  N   LYS A 200     -14.704  43.956  25.770  1.00 62.52           N  
ANISOU 1573  N   LYS A 200     4667   8618  10470   -423   -268   1361       N  
ATOM   1574  CA  LYS A 200     -15.877  44.634  25.161  1.00 62.30           C  
ANISOU 1574  CA  LYS A 200     4789   8481  10399   -459   -278   1331       C  
ATOM   1575  C   LYS A 200     -16.902  43.557  24.797  1.00 62.00           C  
ANISOU 1575  C   LYS A 200     4824   8384  10346   -311   -215   1227       C  
ATOM   1576  O   LYS A 200     -16.538  42.357  24.843  1.00 62.10           O  
ANISOU 1576  O   LYS A 200     4767   8457  10371   -193   -159   1192       O  
ATOM   1577  CB  LYS A 200     -15.452  45.424  23.920  1.00 63.84           C  
ANISOU 1577  CB  LYS A 200     4949   8767  10538   -557   -238   1407       C  
ATOM   1578  CG  LYS A 200     -15.421  44.618  22.619  1.00 64.67           C  
ANISOU 1578  CG  LYS A 200     5007   8971  10592   -459   -111   1380       C  
ATOM   1579  CD  LYS A 200     -14.409  45.093  21.580  1.00 66.80           C  
ANISOU 1579  CD  LYS A 200     5162   9407  10811   -546    -48   1475       C  
ATOM   1580  CE  LYS A 200     -13.662  43.949  20.912  1.00 67.18           C  
ANISOU 1580  CE  LYS A 200     5070   9619  10837   -418     76   1460       C  
ATOM   1581  NZ  LYS A 200     -12.705  44.446  19.899  1.00 68.59           N  
ANISOU 1581  NZ  LYS A 200     5130   9974  10957   -507    146   1554       N  
ATOM   1582  N   GLY A 201     -18.128  43.965  24.453  1.00 61.57           N  
ANISOU 1582  N   GLY A 201     4909   8217  10266   -317   -233   1180       N  
ATOM   1583  CA  GLY A 201     -19.194  43.066  23.965  1.00 59.94           C  
ANISOU 1583  CA  GLY A 201     4780   7953  10039   -199   -181   1089       C  
ATOM   1584  C   GLY A 201     -19.720  42.160  25.067  1.00 59.39           C  
ANISOU 1584  C   GLY A 201     4745   7808  10009   -114   -207   1019       C  
ATOM   1585  O   GLY A 201     -19.774  42.608  26.237  1.00 60.48           O  
ANISOU 1585  O   GLY A 201     4910   7885  10184   -164   -285   1024       O  
ATOM   1586  N   VAL A 202     -20.083  40.924  24.708  1.00 58.22           N  
ANISOU 1586  N   VAL A 202     4609   7662   9849      4   -148    957       N  
ATOM   1587  CA  VAL A 202     -20.726  39.910  25.602  1.00 56.77           C  
ANISOU 1587  CA  VAL A 202     4477   7402   9689     84   -169    887       C  
ATOM   1588  C   VAL A 202     -19.855  39.670  26.847  1.00 56.14           C  
ANISOU 1588  C   VAL A 202     4330   7342   9655     78   -214    911       C  
ATOM   1589  O   VAL A 202     -20.416  39.598  27.953  1.00 54.38           O  
ANISOU 1589  O   VAL A 202     4171   7032   9456     69   -271    879       O  
ATOM   1590  CB  VAL A 202     -20.982  38.590  24.845  1.00 56.81           C  
ANISOU 1590  CB  VAL A 202     4498   7422   9665    207   -103    833       C  
ATOM   1591  CG1 VAL A 202     -21.615  37.531  25.739  1.00 55.64           C  
ANISOU 1591  CG1 VAL A 202     4412   7193   9534    273   -133    770       C  
ATOM   1592  CG2 VAL A 202     -21.807  38.820  23.590  1.00 56.73           C  
ANISOU 1592  CG2 VAL A 202     4558   7390   9607    211    -65    811       C  
ATOM   1593  N   GLU A 203     -18.534  39.542  26.670  1.00 56.94           N  
ANISOU 1593  N   GLU A 203     4305   7560   9767     85   -190    966       N  
ATOM   1594  CA  GLU A 203     -17.589  39.080  27.729  1.00 56.52           C  
ANISOU 1594  CA  GLU A 203     4174   7541   9759    104   -229    986       C  
ATOM   1595  C   GLU A 203     -17.472  40.147  28.824  1.00 55.05           C  
ANISOU 1595  C   GLU A 203     4006   7304   9607    -15   -322   1029       C  
ATOM   1596  O   GLU A 203     -16.923  39.820  29.895  1.00 53.62           O  
ANISOU 1596  O   GLU A 203     3792   7116   9463     -9   -374   1038       O  
ATOM   1597  CB  GLU A 203     -16.241  38.737  27.100  1.00 58.38           C  
ANISOU 1597  CB  GLU A 203     4255   7933   9991    147   -174   1033       C  
ATOM   1598  CG  GLU A 203     -16.373  37.980  25.786  1.00 60.03           C  
ANISOU 1598  CG  GLU A 203     4460   8199  10148    253    -78    996       C  
ATOM   1599  CD  GLU A 203     -16.005  38.757  24.520  1.00 62.40           C  
ANISOU 1599  CD  GLU A 203     4701   8602  10404    195    -11   1051       C  
ATOM   1600  OE1 GLU A 203     -14.886  39.353  24.480  1.00 64.80           O  
ANISOU 1600  OE1 GLU A 203     4874   9028  10719    126     -7   1130       O  
ATOM   1601  OE2 GLU A 203     -16.824  38.764  23.569  1.00 61.80           O  
ANISOU 1601  OE2 GLU A 203     4711   8489  10280    213     31   1018       O  
ATOM   1602  N   ALA A 204     -18.007  41.355  28.582  1.00 54.60           N  
ANISOU 1602  N   ALA A 204     4011   7199   9532   -114   -349   1051       N  
ATOM   1603  CA  ALA A 204     -17.945  42.538  29.480  1.00 53.97           C  
ANISOU 1603  CA  ALA A 204     3972   7060   9472   -232   -445   1093       C  
ATOM   1604  C   ALA A 204     -18.959  42.416  30.625  1.00 53.01           C  
ANISOU 1604  C   ALA A 204     3970   6810   9360   -212   -500   1027       C  
ATOM   1605  O   ALA A 204     -18.648  42.910  31.728  1.00 52.32           O  
ANISOU 1605  O   ALA A 204     3900   6681   9295   -271   -581   1052       O  
ATOM   1606  CB  ALA A 204     -18.186  43.797  28.683  1.00 53.68           C  
ANISOU 1606  CB  ALA A 204     3975   7015   9403   -329   -457   1133       C  
ATOM   1607  N   VAL A 205     -20.118  41.792  30.365  1.00 52.63           N  
ANISOU 1607  N   VAL A 205     4000   6705   9290   -137   -459    950       N  
ATOM   1608  CA  VAL A 205     -21.304  41.744  31.279  1.00 51.94           C  
ANISOU 1608  CA  VAL A 205     4028   6509   9199   -123   -496    884       C  
ATOM   1609  C   VAL A 205     -21.350  40.409  32.044  1.00 52.74           C  
ANISOU 1609  C   VAL A 205     4130   6596   9312    -47   -487    842       C  
ATOM   1610  O   VAL A 205     -21.919  40.399  33.152  1.00 53.20           O  
ANISOU 1610  O   VAL A 205     4259   6582   9370    -58   -531    810       O  
ATOM   1611  CB  VAL A 205     -22.619  42.001  30.509  1.00 50.85           C  
ANISOU 1611  CB  VAL A 205     3971   6323   9027   -104   -467    831       C  
ATOM   1612  CG1 VAL A 205     -22.664  43.417  29.947  1.00 50.72           C  
ANISOU 1612  CG1 VAL A 205     3983   6293   8994   -184   -501    869       C  
ATOM   1613  CG2 VAL A 205     -22.872  40.980  29.408  1.00 50.18           C  
ANISOU 1613  CG2 VAL A 205     3864   6277   8923    -24   -385    801       C  
ATOM   1614  N   MET A 206     -20.790  39.324  31.493  1.00 53.65           N  
ANISOU 1614  N   MET A 206     4179   6774   9429     28   -435    840       N  
ATOM   1615  CA  MET A 206     -20.859  37.958  32.087  1.00 53.19           C  
ANISOU 1615  CA  MET A 206     4141   6694   9376    107   -434    798       C  
ATOM   1616  C   MET A 206     -19.564  37.639  32.838  1.00 52.86           C  
ANISOU 1616  C   MET A 206     4019   6695   9369    114   -476    840       C  
ATOM   1617  O   MET A 206     -18.483  37.937  32.303  1.00 52.76           O  
ANISOU 1617  O   MET A 206     3897   6776   9372    106   -461    895       O  
ATOM   1618  CB  MET A 206     -21.078  36.902  31.000  1.00 54.15           C  
ANISOU 1618  CB  MET A 206     4258   6844   9470    202   -365    763       C  
ATOM   1619  CG  MET A 206     -22.467  36.946  30.408  1.00 54.66           C  
ANISOU 1619  CG  MET A 206     4412   6853   9502    203   -336    713       C  
ATOM   1620  SD  MET A 206     -22.680  35.715  29.106  1.00 57.26           S  
ANISOU 1620  SD  MET A 206     4754   7206   9795    311   -268    675       S  
ATOM   1621  CE  MET A 206     -22.794  34.226  30.101  1.00 57.24           C  
ANISOU 1621  CE  MET A 206     4808   7147   9793    373   -305    635       C  
ATOM   1622  N   TYR A 207     -19.683  37.051  34.030  1.00 52.04           N  
ANISOU 1622  N   TYR A 207     3969   6530   9274    125   -527    817       N  
ATOM   1623  CA  TYR A 207     -18.559  36.457  34.797  1.00 51.88           C  
ANISOU 1623  CA  TYR A 207     3890   6535   9286    153   -576    843       C  
ATOM   1624  C   TYR A 207     -19.012  35.130  35.410  1.00 50.67           C  
ANISOU 1624  C   TYR A 207     3819   6316   9117    222   -592    788       C  
ATOM   1625  O   TYR A 207     -20.164  35.043  35.899  1.00 49.82           O  
ANISOU 1625  O   TYR A 207     3821   6126   8980    195   -598    747       O  
ATOM   1626  CB  TYR A 207     -18.062  37.427  35.870  1.00 52.76           C  
ANISOU 1626  CB  TYR A 207     3996   6625   9424     58   -656    890       C  
ATOM   1627  CG  TYR A 207     -16.959  36.888  36.747  1.00 53.86           C  
ANISOU 1627  CG  TYR A 207     4082   6782   9600     79   -721    919       C  
ATOM   1628  CD1 TYR A 207     -15.632  36.898  36.331  1.00 55.00           C  
ANISOU 1628  CD1 TYR A 207     4081   7035   9779     97   -722    974       C  
ATOM   1629  CD2 TYR A 207     -17.240  36.376  38.004  1.00 54.12           C  
ANISOU 1629  CD2 TYR A 207     4207   6727   9628     78   -783    892       C  
ATOM   1630  CE1 TYR A 207     -14.614  36.404  37.134  1.00 55.76           C  
ANISOU 1630  CE1 TYR A 207     4120   7152   9912    122   -789    999       C  
ATOM   1631  CE2 TYR A 207     -16.235  35.882  38.821  1.00 55.24           C  
ANISOU 1631  CE2 TYR A 207     4309   6875   9802     98   -854    917       C  
ATOM   1632  CZ  TYR A 207     -14.916  35.897  38.388  1.00 56.25           C  
ANISOU 1632  CZ  TYR A 207     4288   7112   9972    124   -860    969       C  
ATOM   1633  OH  TYR A 207     -13.943  35.393  39.208  1.00 56.20           O  
ANISOU 1633  OH  TYR A 207     4237   7112  10000    151   -937    991       O  
ATOM   1634  N   MET A 208     -18.130  34.126  35.352  1.00 50.00           N  
ANISOU 1634  N   MET A 208     3680   6270   9045    310   -601    789       N  
ATOM   1635  CA  MET A 208     -18.290  32.798  35.995  1.00 49.49           C  
ANISOU 1635  CA  MET A 208     3696   6140   8966    379   -640    747       C  
ATOM   1636  C   MET A 208     -17.227  32.668  37.093  1.00 49.77           C  
ANISOU 1636  C   MET A 208     3693   6177   9039    376   -724    780       C  
ATOM   1637  O   MET A 208     -16.039  32.644  36.734  1.00 51.86           O  
ANISOU 1637  O   MET A 208     3831   6533   9337    425   -726    815       O  
ATOM   1638  CB  MET A 208     -18.128  31.693  34.945  1.00 49.87           C  
ANISOU 1638  CB  MET A 208     3729   6224   8993    503   -593    715       C  
ATOM   1639  CG  MET A 208     -18.276  30.278  35.480  1.00 50.58           C  
ANISOU 1639  CG  MET A 208     3918   6239   9061    578   -643    672       C  
ATOM   1640  SD  MET A 208     -19.898  29.937  36.193  1.00 50.18           S  
ANISOU 1640  SD  MET A 208     4043   6059   8963    502   -664    630       S  
ATOM   1641  CE  MET A 208     -19.974  28.153  36.052  1.00 50.83           C  
ANISOU 1641  CE  MET A 208     4229   6077   9004    614   -701    583       C  
ATOM   1642  N   GLY A 209     -17.624  32.632  38.375  1.00 48.91           N  
ANISOU 1642  N   GLY A 209     3682   5977   8923    319   -791    773       N  
ATOM   1643  CA  GLY A 209     -16.686  32.527  39.514  1.00 48.95           C  
ANISOU 1643  CA  GLY A 209     3671   5966   8961    308   -885    803       C  
ATOM   1644  C   GLY A 209     -17.324  32.783  40.872  1.00 48.21           C  
ANISOU 1644  C   GLY A 209     3701   5770   8845    220   -946    796       C  
ATOM   1645  O   GLY A 209     -17.051  32.000  41.800  1.00 48.11           O  
ANISOU 1645  O   GLY A 209     3750   5701   8828    240  -1018    789       O  
ATOM   1646  N   THR A 210     -18.105  33.859  41.009  1.00 48.02           N  
ANISOU 1646  N   THR A 210     3716   5725   8803    131   -923    798       N  
ATOM   1647  CA  THR A 210     -18.822  34.248  42.257  1.00 48.29           C  
ANISOU 1647  CA  THR A 210     3870   5673   8803     51   -967    785       C  
ATOM   1648  C   THR A 210     -20.112  34.989  41.893  1.00 47.63           C  
ANISOU 1648  C   THR A 210     3837   5576   8682      7   -902    754       C  
ATOM   1649  O   THR A 210     -20.187  35.475  40.753  1.00 46.69           O  
ANISOU 1649  O   THR A 210     3650   5513   8576     20   -843    759       O  
ATOM   1650  CB  THR A 210     -17.971  35.139  43.169  1.00 48.80           C  
ANISOU 1650  CB  THR A 210     3915   5728   8898    -14  -1051    836       C  
ATOM   1651  OG1 THR A 210     -18.713  35.402  44.357  1.00 48.81           O  
ANISOU 1651  OG1 THR A 210     4046   5644   8853    -76  -1088    815       O  
ATOM   1652  CG2 THR A 210     -17.628  36.472  42.544  1.00 49.17           C  
ANISOU 1652  CG2 THR A 210     3879   5831   8973    -65  -1037    878       C  
ATOM   1653  N   LEU A 211     -21.056  35.080  42.834  1.00 48.08           N  
ANISOU 1653  N   LEU A 211     4006   5568   8692    -40   -913    723       N  
ATOM   1654  CA  LEU A 211     -22.416  35.652  42.609  1.00 49.01           C  
ANISOU 1654  CA  LEU A 211     4176   5678   8767    -69   -853    682       C  
ATOM   1655  C   LEU A 211     -22.484  37.097  43.135  1.00 50.04           C  
ANISOU 1655  C   LEU A 211     4328   5791   8893   -130   -885    695       C  
ATOM   1656  O   LEU A 211     -23.240  37.899  42.542  1.00 49.18           O  
ANISOU 1656  O   LEU A 211     4218   5696   8771   -138   -841    674       O  
ATOM   1657  CB  LEU A 211     -23.471  34.771  43.298  1.00 49.04           C  
ANISOU 1657  CB  LEU A 211     4283   5636   8711    -79   -839    638       C  
ATOM   1658  CG  LEU A 211     -23.461  33.293  42.902  1.00 48.96           C  
ANISOU 1658  CG  LEU A 211     4286   5621   8695    -28   -829    625       C  
ATOM   1659  CD1 LEU A 211     -24.312  32.462  43.842  1.00 48.45           C  
ANISOU 1659  CD1 LEU A 211     4336   5505   8568    -66   -840    599       C  
ATOM   1660  CD2 LEU A 211     -23.930  33.102  41.470  1.00 49.03           C  
ANISOU 1660  CD2 LEU A 211     4244   5674   8711     17   -756    607       C  
ATOM   1661  N   SER A 212     -21.747  37.414  44.212  1.00 51.17           N  
ANISOU 1661  N   SER A 212     4500   5898   9043   -169   -967    726       N  
ATOM   1662  CA  SER A 212     -21.759  38.739  44.886  1.00 51.76           C  
ANISOU 1662  CA  SER A 212     4624   5938   9104   -227  -1018    737       C  
ATOM   1663  C   SER A 212     -20.972  39.749  44.049  1.00 53.41           C  
ANISOU 1663  C   SER A 212     4745   6186   9361   -249  -1037    788       C  
ATOM   1664  O   SER A 212     -19.749  39.530  43.827  1.00 54.62           O  
ANISOU 1664  O   SER A 212     4809   6378   9567   -249  -1073    843       O  
ATOM   1665  CB  SER A 212     -21.197  38.678  46.269  1.00 51.76           C  
ANISOU 1665  CB  SER A 212     4693   5880   9092   -264  -1107    757       C  
ATOM   1666  OG  SER A 212     -21.111  39.984  46.822  1.00 51.75           O  
ANISOU 1666  OG  SER A 212     4743   5841   9077   -316  -1166    772       O  
ATOM   1667  N   TYR A 213     -21.649  40.820  43.622  1.00 53.71           N  
ANISOU 1667  N   TYR A 213     4809   6218   9379   -268  -1017    771       N  
ATOM   1668  CA  TYR A 213     -21.077  41.913  42.794  1.00 53.60           C  
ANISOU 1668  CA  TYR A 213     4736   6233   9396   -304  -1038    820       C  
ATOM   1669  C   TYR A 213     -20.199  42.804  43.671  1.00 55.23           C  
ANISOU 1669  C   TYR A 213     4975   6397   9612   -376  -1150    873       C  
ATOM   1670  O   TYR A 213     -19.145  43.232  43.195  1.00 56.46           O  
ANISOU 1670  O   TYR A 213     5046   6593   9812   -419  -1189    942       O  
ATOM   1671  CB  TYR A 213     -22.207  42.712  42.144  1.00 52.35           C  
ANISOU 1671  CB  TYR A 213     4622   6064   9204   -295   -994    776       C  
ATOM   1672  CG  TYR A 213     -21.781  43.681  41.074  1.00 51.73           C  
ANISOU 1672  CG  TYR A 213     4491   6016   9149   -330  -1004    821       C  
ATOM   1673  CD1 TYR A 213     -20.764  43.384  40.179  1.00 52.10           C  
ANISOU 1673  CD1 TYR A 213     4416   6138   9241   -338   -985    881       C  
ATOM   1674  CD2 TYR A 213     -22.441  44.889  40.926  1.00 50.90           C  
ANISOU 1674  CD2 TYR A 213     4461   5865   9011   -351  -1031    802       C  
ATOM   1675  CE1 TYR A 213     -20.396  44.281  39.187  1.00 52.08           C  
ANISOU 1675  CE1 TYR A 213     4369   6169   9250   -384   -990    927       C  
ATOM   1676  CE2 TYR A 213     -22.093  45.792  39.937  1.00 50.88           C  
ANISOU 1676  CE2 TYR A 213     4428   5881   9022   -393  -1048    846       C  
ATOM   1677  CZ  TYR A 213     -21.068  45.485  39.063  1.00 51.25           C  
ANISOU 1677  CZ  TYR A 213     4353   6007   9112   -417  -1025    912       C  
ATOM   1678  OH  TYR A 213     -20.731  46.378  38.093  1.00 51.19           O  
ANISOU 1678  OH  TYR A 213     4318   6022   9107   -471  -1039    962       O  
ATOM   1679  N   GLU A 214     -20.633  43.061  44.907  1.00 56.72           N  
ANISOU 1679  N   GLU A 214     5284   6510   9757   -391  -1201    843       N  
ATOM   1680  CA  GLU A 214     -19.869  43.865  45.897  1.00 58.85           C  
ANISOU 1680  CA  GLU A 214     5612   6720  10025   -459  -1321    888       C  
ATOM   1681  C   GLU A 214     -18.512  43.191  46.113  1.00 61.13           C  
ANISOU 1681  C   GLU A 214     5809   7044  10373   -479  -1371    954       C  
ATOM   1682  O   GLU A 214     -17.489  43.893  46.043  1.00 63.01           O  
ANISOU 1682  O   GLU A 214     5998   7293  10649   -545  -1450   1027       O  
ATOM   1683  CB  GLU A 214     -20.613  44.035  47.222  1.00 59.12           C  
ANISOU 1683  CB  GLU A 214     5799   6673   9991   -456  -1354    835       C  
ATOM   1684  CG  GLU A 214     -20.583  45.482  47.709  1.00 60.56           C  
ANISOU 1684  CG  GLU A 214     6085   6783  10141   -506  -1449    847       C  
ATOM   1685  CD  GLU A 214     -20.758  45.738  49.199  1.00 61.60           C  
ANISOU 1685  CD  GLU A 214     6364   6828  10211   -519  -1522    822       C  
ATOM   1686  OE1 GLU A 214     -21.219  46.854  49.543  1.00 63.01           O  
ANISOU 1686  OE1 GLU A 214     6658   6945  10338   -525  -1571    796       O  
ATOM   1687  OE2 GLU A 214     -20.424  44.853  50.018  1.00 60.35           O  
ANISOU 1687  OE2 GLU A 214     6217   6660  10052   -520  -1536    827       O  
ATOM   1688  N   GLN A 215     -18.512  41.876  46.336  1.00 61.45           N  
ANISOU 1688  N   GLN A 215     5825   7102  10420   -425  -1333    931       N  
ATOM   1689  CA  GLN A 215     -17.297  41.039  46.536  1.00 61.72           C  
ANISOU 1689  CA  GLN A 215     5770   7170  10508   -416  -1378    979       C  
ATOM   1690  C   GLN A 215     -16.354  41.208  45.350  1.00 61.93           C  
ANISOU 1690  C   GLN A 215     5635   7297  10598   -419  -1360   1039       C  
ATOM   1691  O   GLN A 215     -15.129  41.316  45.559  1.00 63.59           O  
ANISOU 1691  O   GLN A 215     5763   7540  10856   -455  -1436   1106       O  
ATOM   1692  CB  GLN A 215     -17.637  39.548  46.540  1.00 61.42           C  
ANISOU 1692  CB  GLN A 215     5730   7143  10461   -338  -1320    934       C  
ATOM   1693  CG  GLN A 215     -16.530  38.700  47.146  1.00 61.87           C  
ANISOU 1693  CG  GLN A 215     5747   7201  10557   -321  -1394    969       C  
ATOM   1694  CD  GLN A 215     -16.757  38.660  48.635  1.00 62.35           C  
ANISOU 1694  CD  GLN A 215     5953   7164  10573   -358  -1471    953       C  
ATOM   1695  OE1 GLN A 215     -17.561  37.866  49.126  1.00 62.21           O  
ANISOU 1695  OE1 GLN A 215     6030   7104  10503   -332  -1439    902       O  
ATOM   1696  NE2 GLN A 215     -16.085  39.541  49.366  1.00 62.89           N  
ANISOU 1696  NE2 GLN A 215     6048   7194  10652   -427  -1574   1000       N  
ATOM   1697  N   PHE A 216     -16.926  41.183  44.146  1.00 61.09           N  
ANISOU 1697  N   PHE A 216     5481   7244  10487   -382  -1261   1014       N  
ATOM   1698  CA  PHE A 216     -16.190  41.240  42.861  1.00 61.62           C  
ANISOU 1698  CA  PHE A 216     5395   7418  10597   -375  -1216   1061       C  
ATOM   1699  C   PHE A 216     -15.423  42.562  42.755  1.00 62.21           C  
ANISOU 1699  C   PHE A 216     5432   7511  10693   -479  -1289   1140       C  
ATOM   1700  O   PHE A 216     -14.438  42.608  42.005  1.00 63.27           O  
ANISOU 1700  O   PHE A 216     5423   7746  10870   -496  -1281   1202       O  
ATOM   1701  CB  PHE A 216     -17.173  41.090  41.704  1.00 61.51           C  
ANISOU 1701  CB  PHE A 216     5379   7432  10557   -325  -1104   1012       C  
ATOM   1702  CG  PHE A 216     -16.547  40.922  40.345  1.00 62.34           C  
ANISOU 1702  CG  PHE A 216     5342   7650  10693   -298  -1040   1047       C  
ATOM   1703  CD1 PHE A 216     -16.888  41.766  39.297  1.00 62.82           C  
ANISOU 1703  CD1 PHE A 216     5387   7739  10739   -331   -995   1059       C  
ATOM   1704  CD2 PHE A 216     -15.652  39.894  40.099  1.00 63.53           C  
ANISOU 1704  CD2 PHE A 216     5381   7876  10879   -233  -1022   1063       C  
ATOM   1705  CE1 PHE A 216     -16.331  41.600  38.038  1.00 63.39           C  
ANISOU 1705  CE1 PHE A 216     5335   7920  10829   -310   -929   1091       C  
ATOM   1706  CE2 PHE A 216     -15.091  39.731  38.841  1.00 64.30           C  
ANISOU 1706  CE2 PHE A 216     5347   8088  10994   -199   -954   1091       C  
ATOM   1707  CZ  PHE A 216     -15.439  40.577  37.810  1.00 64.28           C  
ANISOU 1707  CZ  PHE A 216     5332   8118  10974   -241   -903   1105       C  
ATOM   1708  N   LYS A 217     -15.882  43.605  43.453  1.00 62.26           N  
ANISOU 1708  N   LYS A 217     5566   7425  10665   -546  -1359   1137       N  
ATOM   1709  CA  LYS A 217     -15.252  44.951  43.455  1.00 64.58           C  
ANISOU 1709  CA  LYS A 217     5861   7708  10966   -658  -1451   1211       C  
ATOM   1710  C   LYS A 217     -14.107  44.982  44.475  1.00 66.71           C  
ANISOU 1710  C   LYS A 217     6109   7964  11270   -718  -1571   1275       C  
ATOM   1711  O   LYS A 217     -13.071  45.620  44.186  1.00 67.38           O  
ANISOU 1711  O   LYS A 217     6104   8105  11393   -805  -1633   1364       O  
ATOM   1712  CB  LYS A 217     -16.283  46.037  43.784  1.00 63.57           C  
ANISOU 1712  CB  LYS A 217     5900   7474  10778   -688  -1485   1171       C  
ATOM   1713  CG  LYS A 217     -17.345  46.266  42.723  1.00 62.06           C  
ANISOU 1713  CG  LYS A 217     5728   7295  10557   -645  -1390   1119       C  
ATOM   1714  CD  LYS A 217     -18.578  46.961  43.246  1.00 61.57           C  
ANISOU 1714  CD  LYS A 217     5833   7130  10431   -627  -1408   1048       C  
ATOM   1715  CE  LYS A 217     -19.578  47.286  42.157  1.00 60.61           C  
ANISOU 1715  CE  LYS A 217     5723   7021  10284   -588  -1329   1002       C  
ATOM   1716  NZ  LYS A 217     -20.678  48.121  42.681  1.00 60.59           N  
ANISOU 1716  NZ  LYS A 217     5876   6925  10219   -567  -1363    937       N  
ATOM   1717  N   LYS A 218     -14.302  44.341  45.632  1.00 67.84           N  
ANISOU 1717  N   LYS A 218     6338   8038  11400   -680  -1606   1234       N  
ATOM   1718  CA  LYS A 218     -13.324  44.337  46.754  1.00 70.94           C  
ANISOU 1718  CA  LYS A 218     6738   8395  11818   -731  -1733   1286       C  
ATOM   1719  C   LYS A 218     -12.162  43.406  46.394  1.00 72.17           C  
ANISOU 1719  C   LYS A 218     6712   8665  12045   -697  -1725   1332       C  
ATOM   1720  O   LYS A 218     -11.087  43.932  46.067  1.00 74.24           O  
ANISOU 1720  O   LYS A 218     6853   9000  12353   -770  -1780   1419       O  
ATOM   1721  CB  LYS A 218     -14.025  43.989  48.068  1.00 71.34           C  
ANISOU 1721  CB  LYS A 218     6958   8331  11816   -701  -1768   1222       C  
ATOM   1722  CG  LYS A 218     -15.164  44.939  48.408  1.00 71.76           C  
ANISOU 1722  CG  LYS A 218     7182   8289  11794   -720  -1771   1170       C  
ATOM   1723  CD  LYS A 218     -15.678  44.826  49.822  1.00 73.19           C  
ANISOU 1723  CD  LYS A 218     7531   8363  11915   -711  -1823   1122       C  
ATOM   1724  CE  LYS A 218     -16.910  45.682  50.040  1.00 73.93           C  
ANISOU 1724  CE  LYS A 218     7778   8384  11928   -701  -1803   1056       C  
ATOM   1725  NZ  LYS A 218     -17.524  45.437  51.368  1.00 74.59           N  
ANISOU 1725  NZ  LYS A 218     8016   8383  11939   -678  -1826    999       N  
ATOM   1726  N   GLY A 219     -12.374  42.087  46.410  1.00 72.77           N  
ANISOU 1726  N   GLY A 219     6765   8758  12124   -590  -1660   1278       N  
ATOM   1727  CA  GLY A 219     -11.322  41.106  46.074  1.00 73.88           C  
ANISOU 1727  CA  GLY A 219     6742   9003  12326   -528  -1653   1307       C  
ATOM   1728  C   GLY A 219     -11.856  39.692  45.973  1.00 73.42           C  
ANISOU 1728  C   GLY A 219     6703   8940  12253   -402  -1576   1231       C  
ATOM   1729  O   GLY A 219     -12.815  39.366  46.690  1.00 72.63           O  
ANISOU 1729  O   GLY A 219     6758   8737  12100   -385  -1572   1169       O  
ATOM   1730  N   VAL A 220     -11.243  38.885  45.107  1.00 76.20           N  
ANISOU 1730  N   VAL A 220     6905   9402  12643   -318  -1520   1237       N  
ATOM   1731  CA  VAL A 220     -11.574  37.447  44.876  1.00 77.90           C  
ANISOU 1731  CA  VAL A 220     7130   9619  12846   -188  -1459   1171       C  
ATOM   1732  C   VAL A 220     -10.249  36.701  44.664  1.00 80.69           C  
ANISOU 1732  C   VAL A 220     7321  10076  13262   -113  -1491   1205       C  
ATOM   1733  O   VAL A 220      -9.401  37.216  43.918  1.00 80.69           O  
ANISOU 1733  O   VAL A 220     7156  10199  13301   -136  -1474   1264       O  
ATOM   1734  CB  VAL A 220     -12.544  37.276  43.689  1.00 76.77           C  
ANISOU 1734  CB  VAL A 220     6993   9506  12668   -138  -1325   1120       C  
ATOM   1735  CG1 VAL A 220     -12.741  35.807  43.321  1.00 76.26           C  
ANISOU 1735  CG1 VAL A 220     6931   9451  12593     -7  -1273   1061       C  
ATOM   1736  CG2 VAL A 220     -13.883  37.951  43.962  1.00 76.03           C  
ANISOU 1736  CG2 VAL A 220     7054   9316  12516   -198  -1299   1080       C  
ATOM   1737  N   GLN A 221     -10.076  35.546  45.314  1.00 83.73           N  
ANISOU 1737  N   GLN A 221     7752  10413  13648    -28  -1539   1169       N  
ATOM   1738  CA  GLN A 221      -8.795  34.787  45.358  1.00 86.05           C  
ANISOU 1738  CA  GLN A 221     7908  10786  13999     56  -1598   1194       C  
ATOM   1739  C   GLN A 221      -8.837  33.678  44.295  1.00 86.53           C  
ANISOU 1739  C   GLN A 221     7904  10918  14052    207  -1504   1142       C  
ATOM   1740  O   GLN A 221      -9.862  33.000  44.196  1.00 86.17           O  
ANISOU 1740  O   GLN A 221     7993  10793  13955    255  -1455   1074       O  
ATOM   1741  CB  GLN A 221      -8.558  34.272  46.781  1.00 86.79           C  
ANISOU 1741  CB  GLN A 221     8112  10768  14095     54  -1729   1188       C  
ATOM   1742  CG  GLN A 221      -8.267  35.375  47.796  1.00 87.83           C  
ANISOU 1742  CG  GLN A 221     8289  10843  14238    -86  -1836   1248       C  
ATOM   1743  CD  GLN A 221      -9.457  36.273  48.065  1.00 87.92           C  
ANISOU 1743  CD  GLN A 221     8458  10759  14187   -187  -1802   1229       C  
ATOM   1744  OE1 GLN A 221     -10.583  35.817  48.262  1.00 88.11           O  
ANISOU 1744  OE1 GLN A 221     8629  10697  14149   -163  -1752   1162       O  
ATOM   1745  NE2 GLN A 221      -9.223  37.577  48.066  1.00 88.62           N  
ANISOU 1745  NE2 GLN A 221     8517  10864  14288   -302  -1833   1288       N  
ATOM   1746  N   ILE A 222      -7.761  33.532  43.518  1.00 89.01           N  
ANISOU 1746  N   ILE A 222     8020  11385  14414    277  -1481   1174       N  
ATOM   1747  CA  ILE A 222      -7.631  32.600  42.353  1.00 90.92           C  
ANISOU 1747  CA  ILE A 222     8175  11721  14646    431  -1386   1129       C  
ATOM   1748  C   ILE A 222      -6.189  32.087  42.301  1.00 96.03           C  
ANISOU 1748  C   ILE A 222     8636  12496  15352    533  -1437   1157       C  
ATOM   1749  O   ILE A 222      -5.280  32.738  42.826  1.00 97.90           O  
ANISOU 1749  O   ILE A 222     8766  12788  15643    456  -1516   1228       O  
ATOM   1750  CB  ILE A 222      -8.046  33.306  41.042  1.00 89.52           C  
ANISOU 1750  CB  ILE A 222     7931  11635  14447    396  -1254   1140       C  
ATOM   1751  CG1 ILE A 222      -8.209  32.329  39.872  1.00 88.96           C  
ANISOU 1751  CG1 ILE A 222     7826  11627  14346    551  -1151   1080       C  
ATOM   1752  CG2 ILE A 222      -7.082  34.445  40.692  1.00 89.93           C  
ANISOU 1752  CG2 ILE A 222     7797  11827  14543    298  -1254   1233       C  
ATOM   1753  CD1 ILE A 222      -8.737  32.961  38.594  1.00 88.40           C  
ANISOU 1753  CD1 ILE A 222     7718  11626  14242    518  -1023   1084       C  
ATOM   1754  N   PRO A 223      -5.930  30.894  41.705  1.00 97.57           N  
ANISOU 1754  N   PRO A 223     8792  12739  15538    713  -1403   1100       N  
ATOM   1755  CA  PRO A 223      -4.559  30.471  41.403  1.00 99.67           C  
ANISOU 1755  CA  PRO A 223     8849  13164  15856    831  -1426   1120       C  
ATOM   1756  C   PRO A 223      -3.896  31.318  40.299  1.00101.18           C  
ANISOU 1756  C   PRO A 223     8813  13562  16068    795  -1326   1183       C  
ATOM   1757  O   PRO A 223      -4.601  31.813  39.422  1.00100.75           O  
ANISOU 1757  O   PRO A 223     8783  13525  15971    745  -1214   1179       O  
ATOM   1758  CB  PRO A 223      -4.685  29.001  40.953  1.00 99.66           C  
ANISOU 1758  CB  PRO A 223     8904  13141  15819   1040  -1405   1030       C  
ATOM   1759  CG  PRO A 223      -6.097  28.579  41.332  1.00 97.49           C  
ANISOU 1759  CG  PRO A 223     8892  12668  15481   1007  -1407    970       C  
ATOM   1760  CD  PRO A 223      -6.917  29.853  41.376  1.00 96.58           C  
ANISOU 1760  CD  PRO A 223     8829  12515  15351    815  -1357   1012       C  
ATOM   1761  N   CYS A 224      -2.562  31.463  40.359  1.00101.85           N  
ANISOU 1761  N   CYS A 224     8681  13802  16212    817  -1370   1241       N  
ATOM   1762  CA  CYS A 224      -1.720  32.165  39.347  1.00102.00           C  
ANISOU 1762  CA  CYS A 224     8451  14050  16251    786  -1282   1310       C  
ATOM   1763  C   CYS A 224      -1.386  31.197  38.199  1.00103.50           C  
ANISOU 1763  C   CYS A 224     8532  14379  16414    997  -1174   1249       C  
ATOM   1764  O   CYS A 224      -0.672  30.200  38.465  1.00103.84           O  
ANISOU 1764  O   CYS A 224     8513  14459  16482   1168  -1232   1209       O  
ATOM   1765  CB  CYS A 224      -0.442  32.723  39.977  1.00103.24           C  
ANISOU 1765  CB  CYS A 224     8419  14321  16485    709  -1384   1403       C  
ATOM   1766  SG  CYS A 224       0.715  33.455  38.780  1.00101.39           S  
ANISOU 1766  SG  CYS A 224     7854  14395  16272    672  -1280   1495       S  
ATOM   1767  N   LYS A 228      -0.326  28.715  44.094  1.00101.82           N  
ANISOU 1767  N   LYS A 228     8760  13578  16347   1114  -1896   1183       N  
ATOM   1768  CA  LYS A 228      -0.562  29.804  45.083  1.00101.37           C  
ANISOU 1768  CA  LYS A 228     8785  13423  16307    893  -1974   1254       C  
ATOM   1769  C   LYS A 228      -1.518  30.847  44.479  1.00100.27           C  
ANISOU 1769  C   LYS A 228     8699  13273  16124    741  -1851   1277       C  
ATOM   1770  O   LYS A 228      -1.811  30.769  43.261  1.00 98.56           O  
ANISOU 1770  O   LYS A 228     8420  13151  15876    802  -1710   1251       O  
ATOM   1771  CB  LYS A 228       0.773  30.423  45.514  1.00102.16           C  
ANISOU 1771  CB  LYS A 228     8671  13654  16492    833  -2072   1346       C  
ATOM   1772  CG  LYS A 228       0.822  30.946  46.943  1.00101.97           C  
ANISOU 1772  CG  LYS A 228     8767  13485  16491    684  -2232   1394       C  
ATOM   1773  CD  LYS A 228       0.441  29.914  47.982  1.00101.74           C  
ANISOU 1773  CD  LYS A 228     8961  13259  16436    763  -2346   1327       C  
ATOM   1774  CE  LYS A 228       1.286  30.019  49.248  1.00103.09           C  
ANISOU 1774  CE  LYS A 228     9125  13379  16663    713  -2536   1377       C  
ATOM   1775  NZ  LYS A 228       0.911  28.954  50.223  1.00102.49           N  
ANISOU 1775  NZ  LYS A 228     9278  13109  16552    793  -2649   1310       N  
ATOM   1776  N   GLN A 229      -1.956  31.817  45.290  1.00100.79           N  
ANISOU 1776  N   GLN A 229     8878  13229  16185    555  -1909   1324       N  
ATOM   1777  CA  GLN A 229      -3.215  32.581  45.070  1.00 99.99           C  
ANISOU 1777  CA  GLN A 229     8929  13036  16025    429  -1825   1316       C  
ATOM   1778  C   GLN A 229      -2.914  34.032  44.667  1.00100.98           C  
ANISOU 1778  C   GLN A 229     8932  13262  16172    265  -1794   1407       C  
ATOM   1779  O   GLN A 229      -1.889  34.578  45.132  1.00102.87           O  
ANISOU 1779  O   GLN A 229     9044  13571  16470    191  -1891   1487       O  
ATOM   1780  CB  GLN A 229      -4.034  32.546  46.362  1.00 98.25           C  
ANISOU 1780  CB  GLN A 229     8960  12603  15768    354  -1917   1290       C  
ATOM   1781  CG  GLN A 229      -5.534  32.473  46.147  1.00 95.98           C  
ANISOU 1781  CG  GLN A 229     8868  12198  15402    334  -1825   1226       C  
ATOM   1782  CD  GLN A 229      -5.991  31.072  45.824  1.00 95.67           C  
ANISOU 1782  CD  GLN A 229     8910  12115  15325    493  -1786   1140       C  
ATOM   1783  OE1 GLN A 229      -5.204  30.206  45.449  1.00 96.15           O  
ANISOU 1783  OE1 GLN A 229     8862  12255  15413    639  -1800   1121       O  
ATOM   1784  NE2 GLN A 229      -7.282  30.833  45.977  1.00 94.66           N  
ANISOU 1784  NE2 GLN A 229     8978  11859  15128    467  -1744   1086       N  
ATOM   1785  N   ALA A 230      -3.807  34.627  43.863  1.00100.14           N  
ANISOU 1785  N   ALA A 230     8877  13153  16018    206  -1677   1397       N  
ATOM   1786  CA  ALA A 230      -3.818  36.054  43.458  1.00 98.96           C  
ANISOU 1786  CA  ALA A 230     8673  13057  15868     37  -1648   1474       C  
ATOM   1787  C   ALA A 230      -5.119  36.724  43.932  1.00 96.27           C  
ANISOU 1787  C   ALA A 230     8564  12541  15471    -70  -1649   1448       C  
ATOM   1788  O   ALA A 230      -5.976  36.030  44.522  1.00 95.43           O  
ANISOU 1788  O   ALA A 230     8638  12294  15326    -14  -1659   1373       O  
ATOM   1789  CB  ALA A 230      -3.659  36.164  41.957  1.00100.00           C  
ANISOU 1789  CB  ALA A 230     8645  13358  15989     78  -1505   1484       C  
ATOM   1790  N   THR A 231      -5.254  38.032  43.689  1.00 93.18           N  
ANISOU 1790  N   THR A 231     8170  12162  15071   -220  -1644   1508       N  
ATOM   1791  CA  THR A 231      -6.454  38.848  44.019  1.00 88.29           C  
ANISOU 1791  CA  THR A 231     7755  11395  14396   -320  -1642   1486       C  
ATOM   1792  C   THR A 231      -7.008  39.466  42.730  1.00 84.12           C  
ANISOU 1792  C   THR A 231     7195  10930  13834   -350  -1519   1488       C  
ATOM   1793  O   THR A 231      -6.266  40.232  42.079  1.00 83.36           O  
ANISOU 1793  O   THR A 231     6953  10958  13761   -432  -1511   1569       O  
ATOM   1794  CB  THR A 231      -6.132  39.915  45.073  1.00 89.91           C  
ANISOU 1794  CB  THR A 231     8026  11521  14613   -473  -1782   1553       C  
ATOM   1795  OG1 THR A 231      -5.568  39.240  46.198  1.00 91.45           O  
ANISOU 1795  OG1 THR A 231     8242  11664  14839   -434  -1896   1550       O  
ATOM   1796  CG2 THR A 231      -7.346  40.716  45.497  1.00 88.71           C  
ANISOU 1796  CG2 THR A 231     8090  11216  14398   -553  -1788   1520       C  
ATOM   1797  N   LYS A 232      -8.259  39.132  42.389  1.00 78.43           N  
ANISOU 1797  N   LYS A 232     6608  10131  13059   -292  -1431   1406       N  
ATOM   1798  CA  LYS A 232      -9.028  39.674  41.238  1.00 74.75           C  
ANISOU 1798  CA  LYS A 232     6155   9692  12553   -313  -1320   1392       C  
ATOM   1799  C   LYS A 232     -10.042  40.694  41.769  1.00 71.33           C  
ANISOU 1799  C   LYS A 232     5904   9119  12076   -418  -1359   1380       C  
ATOM   1800  O   LYS A 232     -10.724  40.387  42.768  1.00 69.77           O  
ANISOU 1800  O   LYS A 232     5860   8793  11854   -400  -1402   1327       O  
ATOM   1801  CB  LYS A 232      -9.723  38.521  40.509  1.00 75.04           C  
ANISOU 1801  CB  LYS A 232     6214   9736  12559   -167  -1207   1306       C  
ATOM   1802  CG  LYS A 232     -10.072  38.761  39.043  1.00 75.23           C  
ANISOU 1802  CG  LYS A 232     6181   9847  12556   -152  -1084   1301       C  
ATOM   1803  CD  LYS A 232     -10.938  37.653  38.463  1.00 74.59           C  
ANISOU 1803  CD  LYS A 232     6165   9737  12438    -18   -991   1210       C  
ATOM   1804  CE  LYS A 232     -10.675  37.304  37.010  1.00 75.18           C  
ANISOU 1804  CE  LYS A 232     6119   9945  12500     60   -877   1207       C  
ATOM   1805  NZ  LYS A 232     -11.098  35.912  36.706  1.00 74.59           N  
ANISOU 1805  NZ  LYS A 232     6091   9848  12402    216   -826   1124       N  
ATOM   1806  N   TYR A 233     -10.127  41.871  41.142  1.00 68.98           N  
ANISOU 1806  N   TYR A 233     5597   8847  11764   -521  -1348   1428       N  
ATOM   1807  CA  TYR A 233     -11.129  42.920  41.475  1.00 66.50           C  
ANISOU 1807  CA  TYR A 233     5456   8406  11402   -605  -1381   1411       C  
ATOM   1808  C   TYR A 233     -11.527  43.687  40.213  1.00 64.89           C  
ANISOU 1808  C   TYR A 233     5233   8250  11172   -647  -1306   1426       C  
ATOM   1809  O   TYR A 233     -10.753  43.706  39.227  1.00 64.48           O  
ANISOU 1809  O   TYR A 233     5021   8336  11140   -660  -1256   1482       O  
ATOM   1810  CB  TYR A 233     -10.613  43.879  42.553  1.00 66.87           C  
ANISOU 1810  CB  TYR A 233     5564   8383  11461   -729  -1528   1473       C  
ATOM   1811  CG  TYR A 233      -9.337  44.605  42.202  1.00 68.34           C  
ANISOU 1811  CG  TYR A 233     5600   8677  11688   -841  -1587   1588       C  
ATOM   1812  CD1 TYR A 233      -8.119  44.200  42.730  1.00 70.15           C  
ANISOU 1812  CD1 TYR A 233     5702   8976  11974   -850  -1659   1645       C  
ATOM   1813  CD2 TYR A 233      -9.337  45.702  41.351  1.00 68.74           C  
ANISOU 1813  CD2 TYR A 233     5634   8763  11718   -945  -1577   1644       C  
ATOM   1814  CE1 TYR A 233      -6.938  44.853  42.419  1.00 70.94           C  
ANISOU 1814  CE1 TYR A 233     5648   9192  12114   -962  -1714   1757       C  
ATOM   1815  CE2 TYR A 233      -8.161  46.367  41.033  1.00 70.08           C  
ANISOU 1815  CE2 TYR A 233     5664   9041  11920  -1067  -1634   1758       C  
ATOM   1816  CZ  TYR A 233      -6.961  45.948  41.575  1.00 70.78           C  
ANISOU 1816  CZ  TYR A 233     5613   9211  12068  -1078  -1700   1816       C  
ATOM   1817  OH  TYR A 233      -5.803  46.595  41.271  1.00 71.83           O  
ANISOU 1817  OH  TYR A 233     5594   9464  12233  -1206  -1756   1935       O  
ATOM   1818  N   LEU A 234     -12.712  44.304  40.271  1.00 63.03           N  
ANISOU 1818  N   LEU A 234     5156   7904  10886   -665  -1301   1377       N  
ATOM   1819  CA  LEU A 234     -13.297  45.143  39.194  1.00 61.66           C  
ANISOU 1819  CA  LEU A 234     5009   7739  10677   -707  -1250   1381       C  
ATOM   1820  C   LEU A 234     -12.702  46.552  39.293  1.00 61.62           C  
ANISOU 1820  C   LEU A 234     5019   7722  10671   -861  -1356   1472       C  
ATOM   1821  O   LEU A 234     -12.778  47.150  40.389  1.00 60.91           O  
ANISOU 1821  O   LEU A 234     5047   7522  10572   -917  -1468   1477       O  
ATOM   1822  CB  LEU A 234     -14.824  45.171  39.340  1.00 59.75           C  
ANISOU 1822  CB  LEU A 234     4933   7383  10386   -650  -1214   1284       C  
ATOM   1823  CG  LEU A 234     -15.573  45.993  38.290  1.00 59.10           C  
ANISOU 1823  CG  LEU A 234     4898   7291  10265   -677  -1171   1274       C  
ATOM   1824  CD1 LEU A 234     -15.422  45.384  36.903  1.00 58.70           C  
ANISOU 1824  CD1 LEU A 234     4725   7358  10220   -624  -1054   1277       C  
ATOM   1825  CD2 LEU A 234     -17.043  46.139  38.650  1.00 57.85           C  
ANISOU 1825  CD2 LEU A 234     4901   7019  10060   -625  -1159   1181       C  
ATOM   1826  N   VAL A 235     -12.151  47.047  38.179  1.00 61.47           N  
ANISOU 1826  N   VAL A 235     4892   7807  10654   -928  -1323   1542       N  
ATOM   1827  CA  VAL A 235     -11.549  48.407  38.051  1.00 62.72           C  
ANISOU 1827  CA  VAL A 235     5058   7967  10804  -1094  -1422   1643       C  
ATOM   1828  C   VAL A 235     -12.619  49.372  37.537  1.00 61.22           C  
ANISOU 1828  C   VAL A 235     5025   7679  10556  -1126  -1425   1612       C  
ATOM   1829  O   VAL A 235     -12.930  50.355  38.246  1.00 60.32           O  
ANISOU 1829  O   VAL A 235     5064   7437  10415  -1198  -1543   1617       O  
ATOM   1830  CB  VAL A 235     -10.336  48.401  37.102  1.00 64.31           C  
ANISOU 1830  CB  VAL A 235     5050   8351  11032  -1160  -1381   1743       C  
ATOM   1831  CG1 VAL A 235      -9.652  49.762  37.078  1.00 65.70           C  
ANISOU 1831  CG1 VAL A 235     5234   8529  11198  -1352  -1498   1859       C  
ATOM   1832  CG2 VAL A 235      -9.355  47.286  37.443  1.00 64.85           C  
ANISOU 1832  CG2 VAL A 235     4946   8535  11159  -1088  -1357   1756       C  
ATOM   1833  N   GLN A 236     -13.129  49.097  36.334  1.00 60.15           N  
ANISOU 1833  N   GLN A 236     4853   7601  10398  -1070  -1308   1580       N  
ATOM   1834  CA  GLN A 236     -14.160  49.918  35.652  1.00 59.65           C  
ANISOU 1834  CA  GLN A 236     4923   7459  10281  -1086  -1301   1547       C  
ATOM   1835  C   GLN A 236     -15.209  48.987  35.022  1.00 57.14           C  
ANISOU 1835  C   GLN A 236     4614   7146   9948   -939  -1170   1444       C  
ATOM   1836  O   GLN A 236     -14.807  48.000  34.357  1.00 56.54           O  
ANISOU 1836  O   GLN A 236     4400   7189   9892   -872  -1065   1443       O  
ATOM   1837  CB  GLN A 236     -13.497  50.828  34.615  1.00 61.51           C  
ANISOU 1837  CB  GLN A 236     5102   7769  10497  -1222  -1317   1650       C  
ATOM   1838  CG  GLN A 236     -14.498  51.683  33.854  1.00 62.15           C  
ANISOU 1838  CG  GLN A 236     5325   7767  10522  -1240  -1322   1620       C  
ATOM   1839  CD  GLN A 236     -13.871  52.510  32.758  1.00 64.16           C  
ANISOU 1839  CD  GLN A 236     5531   8097  10748  -1379  -1332   1723       C  
ATOM   1840  OE1 GLN A 236     -12.818  52.179  32.219  1.00 64.92           O  
ANISOU 1840  OE1 GLN A 236     5452   8350  10863  -1429  -1279   1802       O  
ATOM   1841  NE2 GLN A 236     -14.542  53.592  32.396  1.00 64.96           N  
ANISOU 1841  NE2 GLN A 236     5791   8091  10797  -1438  -1401   1722       N  
ATOM   1842  N   GLN A 237     -16.495  49.298  35.239  1.00 54.57           N  
ANISOU 1842  N   GLN A 237     4446   6698   9587   -888  -1181   1361       N  
ATOM   1843  CA  GLN A 237     -17.662  48.661  34.570  1.00 51.99           C  
ANISOU 1843  CA  GLN A 237     4151   6361   9239   -771  -1075   1268       C  
ATOM   1844  C   GLN A 237     -18.525  49.738  33.901  1.00 50.57           C  
ANISOU 1844  C   GLN A 237     4092   6108   9012   -804  -1103   1251       C  
ATOM   1845  O   GLN A 237     -18.961  50.667  34.613  1.00 48.83           O  
ANISOU 1845  O   GLN A 237     4008   5775   8768   -838  -1205   1236       O  
ATOM   1846  CB  GLN A 237     -18.498  47.889  35.591  1.00 50.62           C  
ANISOU 1846  CB  GLN A 237     4047   6118   9068   -668  -1062   1174       C  
ATOM   1847  CG  GLN A 237     -19.529  46.974  34.953  1.00 49.44           C  
ANISOU 1847  CG  GLN A 237     3897   5980   8905   -553   -950   1089       C  
ATOM   1848  CD  GLN A 237     -18.860  45.838  34.229  1.00 48.96           C  
ANISOU 1848  CD  GLN A 237     3695   6036   8871   -503   -857   1108       C  
ATOM   1849  OE1 GLN A 237     -18.092  45.087  34.817  1.00 48.49           O  
ANISOU 1849  OE1 GLN A 237     3561   6019   8843   -482   -860   1125       O  
ATOM   1850  NE2 GLN A 237     -19.142  45.719  32.942  1.00 48.98           N  
ANISOU 1850  NE2 GLN A 237     3666   6089   8855   -477   -780   1101       N  
ATOM   1851  N   GLU A 238     -18.758  49.609  32.589  1.00 50.30           N  
ANISOU 1851  N   GLU A 238     4017   6132   8961   -786  -1021   1251       N  
ATOM   1852  CA  GLU A 238     -19.738  50.428  31.821  1.00 50.18           C  
ANISOU 1852  CA  GLU A 238     4117   6046   8900   -790  -1035   1219       C  
ATOM   1853  C   GLU A 238     -20.687  49.487  31.069  1.00 48.24           C  
ANISOU 1853  C   GLU A 238     3855   5824   8649   -669   -919   1137       C  
ATOM   1854  O   GLU A 238     -20.281  48.972  30.014  1.00 48.11           O  
ANISOU 1854  O   GLU A 238     3743   5905   8630   -661   -834   1165       O  
ATOM   1855  CB  GLU A 238     -19.033  51.390  30.861  1.00 52.28           C  
ANISOU 1855  CB  GLU A 238     4369   6352   9142   -919  -1071   1317       C  
ATOM   1856  CG  GLU A 238     -18.323  52.525  31.588  1.00 54.27           C  
ANISOU 1856  CG  GLU A 238     4680   6549   9389  -1053  -1213   1395       C  
ATOM   1857  CD  GLU A 238     -17.756  53.658  30.744  1.00 56.60           C  
ANISOU 1857  CD  GLU A 238     4999   6857   9648  -1204  -1277   1495       C  
ATOM   1858  OE1 GLU A 238     -16.587  53.530  30.288  1.00 58.38           O  
ANISOU 1858  OE1 GLU A 238     5084   7211   9885  -1295  -1247   1594       O  
ATOM   1859  OE2 GLU A 238     -18.468  54.689  30.561  1.00 56.89           O  
ANISOU 1859  OE2 GLU A 238     5198   6776   9640  -1233  -1363   1478       O  
ATOM   1860  N   SER A 239     -21.894  49.274  31.609  1.00 46.30           N  
ANISOU 1860  N   SER A 239     3698   5497   8394   -580   -918   1041       N  
ATOM   1861  CA  SER A 239     -22.985  48.446  31.023  1.00 44.43           C  
ANISOU 1861  CA  SER A 239     3464   5265   8149   -472   -827    959       C  
ATOM   1862  C   SER A 239     -24.258  48.666  31.831  1.00 42.89           C  
ANISOU 1862  C   SER A 239     3380   4975   7939   -410   -862    869       C  
ATOM   1863  O   SER A 239     -24.173  49.074  32.987  1.00 42.66           O  
ANISOU 1863  O   SER A 239     3404   4893   7909   -428   -933    864       O  
ATOM   1864  CB  SER A 239     -22.599  46.983  30.996  1.00 44.70           C  
ANISOU 1864  CB  SER A 239     3389   5383   8212   -406   -733    949       C  
ATOM   1865  OG  SER A 239     -22.323  46.487  32.304  1.00 44.84           O  
ANISOU 1865  OG  SER A 239     3397   5386   8254   -390   -760    937       O  
ATOM   1866  N   PRO A 240     -25.461  48.407  31.256  1.00 41.23           N  
ANISOU 1866  N   PRO A 240     3205   4748   7712   -334   -815    797       N  
ATOM   1867  CA  PRO A 240     -26.729  48.586  31.976  1.00 39.88           C  
ANISOU 1867  CA  PRO A 240     3119   4509   7523   -268   -838    709       C  
ATOM   1868  C   PRO A 240     -27.022  47.515  33.049  1.00 38.64           C  
ANISOU 1868  C   PRO A 240     2933   4368   7379   -213   -795    662       C  
ATOM   1869  O   PRO A 240     -27.700  47.810  34.024  1.00 38.62           O  
ANISOU 1869  O   PRO A 240     2996   4317   7357   -185   -830    610       O  
ATOM   1870  CB  PRO A 240     -27.777  48.580  30.854  1.00 39.41           C  
ANISOU 1870  CB  PRO A 240     3080   4445   7447   -216   -800    661       C  
ATOM   1871  CG  PRO A 240     -27.157  47.788  29.719  1.00 39.44           C  
ANISOU 1871  CG  PRO A 240     2994   4527   7463   -227   -721    706       C  
ATOM   1872  CD  PRO A 240     -25.661  47.953  29.871  1.00 40.62           C  
ANISOU 1872  CD  PRO A 240     3085   4720   7628   -310   -740    797       C  
ATOM   1873  N   PHE A 241     -26.516  46.299  32.853  1.00 37.35           N  
ANISOU 1873  N   PHE A 241     2680   4271   7240   -198   -723    680       N  
ATOM   1874  CA  PHE A 241     -26.571  45.190  33.845  1.00 36.57           C  
ANISOU 1874  CA  PHE A 241     2557   4185   7151   -162   -692    652       C  
ATOM   1875  C   PHE A 241     -25.213  44.469  33.893  1.00 36.89           C  
ANISOU 1875  C   PHE A 241     2510   4282   7223   -186   -677    716       C  
ATOM   1876  O   PHE A 241     -24.376  44.687  33.004  1.00 36.73           O  
ANISOU 1876  O   PHE A 241     2431   4309   7215   -219   -667    774       O  
ATOM   1877  CB  PHE A 241     -27.673  44.192  33.489  1.00 35.06           C  
ANISOU 1877  CB  PHE A 241     2359   4011   6950    -93   -619    587       C  
ATOM   1878  CG  PHE A 241     -27.448  43.535  32.158  1.00 34.52           C  
ANISOU 1878  CG  PHE A 241     2232   3992   6890    -72   -557    606       C  
ATOM   1879  CD1 PHE A 241     -26.785  42.322  32.078  1.00 34.38           C  
ANISOU 1879  CD1 PHE A 241     2153   4021   6889    -49   -511    625       C  
ATOM   1880  CD2 PHE A 241     -27.830  44.155  30.984  1.00 34.22           C  
ANISOU 1880  CD2 PHE A 241     2211   3952   6840    -73   -551    606       C  
ATOM   1881  CE1 PHE A 241     -26.533  41.724  30.855  1.00 34.33           C  
ANISOU 1881  CE1 PHE A 241     2101   4060   6881    -19   -455    638       C  
ATOM   1882  CE2 PHE A 241     -27.593  43.547  29.759  1.00 34.34           C  
ANISOU 1882  CE2 PHE A 241     2180   4011   6853    -53   -493    623       C  
ATOM   1883  CZ  PHE A 241     -26.945  42.334  29.697  1.00 34.30           C  
ANISOU 1883  CZ  PHE A 241     2114   4055   6861    -23   -442    637       C  
ATOM   1884  N   VAL A 242     -25.029  43.635  34.912  1.00 37.14           N  
ANISOU 1884  N   VAL A 242     2533   4312   7264   -167   -676    704       N  
ATOM   1885  CA  VAL A 242     -23.979  42.578  34.949  1.00 38.20           C  
ANISOU 1885  CA  VAL A 242     2584   4502   7428   -154   -651    742       C  
ATOM   1886  C   VAL A 242     -24.636  41.269  35.402  1.00 38.21           C  
ANISOU 1886  C   VAL A 242     2604   4494   7419    -94   -609    686       C  
ATOM   1887  O   VAL A 242     -25.532  41.320  36.275  1.00 37.44           O  
ANISOU 1887  O   VAL A 242     2578   4350   7297    -92   -624    639       O  
ATOM   1888  CB  VAL A 242     -22.785  42.958  35.856  1.00 39.21           C  
ANISOU 1888  CB  VAL A 242     2688   4628   7580   -212   -724    801       C  
ATOM   1889  CG1 VAL A 242     -21.943  44.086  35.254  1.00 40.01           C  
ANISOU 1889  CG1 VAL A 242     2753   4756   7692   -287   -764    874       C  
ATOM   1890  CG2 VAL A 242     -23.217  43.312  37.275  1.00 39.12           C  
ANISOU 1890  CG2 VAL A 242     2770   4543   7550   -230   -786    772       C  
ATOM   1891  N   MET A 243     -24.208  40.152  34.804  1.00 38.67           N  
ANISOU 1891  N   MET A 243     2604   4598   7489    -46   -562    693       N  
ATOM   1892  CA  MET A 243     -24.583  38.767  35.177  1.00 38.41           C  
ANISOU 1892  CA  MET A 243     2592   4554   7445      4   -536    654       C  
ATOM   1893  C   MET A 243     -23.423  38.125  35.943  1.00 39.32           C  
ANISOU 1893  C   MET A 243     2671   4681   7585     11   -574    688       C  
ATOM   1894  O   MET A 243     -22.301  38.069  35.391  1.00 40.33           O  
ANISOU 1894  O   MET A 243     2714   4868   7740     25   -570    734       O  
ATOM   1895  CB  MET A 243     -24.853  37.947  33.922  1.00 38.37           C  
ANISOU 1895  CB  MET A 243     2565   4582   7432     63   -472    636       C  
ATOM   1896  CG  MET A 243     -25.498  36.611  34.201  1.00 38.18           C  
ANISOU 1896  CG  MET A 243     2589   4530   7387    105   -457    593       C  
ATOM   1897  SD  MET A 243     -25.955  35.799  32.652  1.00 38.13           S  
ANISOU 1897  SD  MET A 243     2579   4545   7360    170   -394    568       S  
ATOM   1898  CE  MET A 243     -26.657  34.283  33.299  1.00 38.21           C  
ANISOU 1898  CE  MET A 243     2667   4506   7342    193   -406    528       C  
ATOM   1899  N   MET A 244     -23.688  37.682  37.169  1.00 39.55           N  
ANISOU 1899  N   MET A 244     2762   4662   7603      0   -610    668       N  
ATOM   1900  CA  MET A 244     -22.721  36.981  38.045  1.00 40.20           C  
ANISOU 1900  CA  MET A 244     2832   4739   7704      9   -659    692       C  
ATOM   1901  C   MET A 244     -23.175  35.522  38.194  1.00 40.43           C  
ANISOU 1901  C   MET A 244     2908   4742   7708     60   -642    654       C  
ATOM   1902  O   MET A 244     -24.158  35.259  38.907  1.00 39.27           O  
ANISOU 1902  O   MET A 244     2845   4549   7524     35   -644    618       O  
ATOM   1903  CB  MET A 244     -22.636  37.653  39.418  1.00 40.50           C  
ANISOU 1903  CB  MET A 244     2923   4726   7736    -52   -728    703       C  
ATOM   1904  CG  MET A 244     -22.241  39.118  39.357  1.00 41.16           C  
ANISOU 1904  CG  MET A 244     2986   4816   7835   -110   -764    742       C  
ATOM   1905  SD  MET A 244     -20.734  39.479  38.399  1.00 43.14           S  
ANISOU 1905  SD  MET A 244     3101   5151   8137   -118   -770    819       S  
ATOM   1906  CE  MET A 244     -19.495  38.697  39.431  1.00 43.73           C  
ANISOU 1906  CE  MET A 244     3138   5230   8246   -108   -838    854       C  
ATOM   1907  N   SER A 245     -22.470  34.608  37.526  1.00 41.75           N  
ANISOU 1907  N   SER A 245     3026   4944   7891    129   -628    663       N  
ATOM   1908  CA  SER A 245     -22.711  33.144  37.579  1.00 42.31           C  
ANISOU 1908  CA  SER A 245     3152   4983   7937    186   -630    631       C  
ATOM   1909  C   SER A 245     -21.634  32.478  38.443  1.00 43.13           C  
ANISOU 1909  C   SER A 245     3251   5072   8061    213   -699    653       C  
ATOM   1910  O   SER A 245     -20.506  33.016  38.508  1.00 43.20           O  
ANISOU 1910  O   SER A 245     3172   5128   8113    214   -725    696       O  
ATOM   1911  CB  SER A 245     -22.741  32.551  36.203  1.00 42.36           C  
ANISOU 1911  CB  SER A 245     3130   5027   7938    260   -575    616       C  
ATOM   1912  OG  SER A 245     -23.411  33.409  35.298  1.00 42.34           O  
ANISOU 1912  OG  SER A 245     3107   5050   7930    235   -520    610       O  
ATOM   1913  N   ALA A 246     -21.992  31.354  39.071  1.00 43.54           N  
ANISOU 1913  N   ALA A 246     3397   5063   8082    227   -733    627       N  
ATOM   1914  CA  ALA A 246     -21.109  30.485  39.877  1.00 44.98           C  
ANISOU 1914  CA  ALA A 246     3603   5213   8273    264   -810    638       C  
ATOM   1915  C   ALA A 246     -21.783  29.125  40.039  1.00 46.09           C  
ANISOU 1915  C   ALA A 246     3863   5285   8364    288   -830    602       C  
ATOM   1916  O   ALA A 246     -23.009  29.047  40.115  1.00 45.51           O  
ANISOU 1916  O   ALA A 246     3865   5179   8246    231   -801    578       O  
ATOM   1917  CB  ALA A 246     -20.835  31.133  41.215  1.00 44.92           C  
ANISOU 1917  CB  ALA A 246     3618   5174   8275    188   -872    663       C  
ATOM   1918  N   PRO A 247     -21.030  28.002  40.077  1.00 47.71           N  
ANISOU 1918  N   PRO A 247     4091   5465   8570    372   -886    598       N  
ATOM   1919  CA  PRO A 247     -21.626  26.694  40.353  1.00 48.41           C  
ANISOU 1919  CA  PRO A 247     4317   5470   8605    382   -928    569       C  
ATOM   1920  C   PRO A 247     -22.664  26.762  41.471  1.00 48.77           C  
ANISOU 1920  C   PRO A 247     4471   5456   8603    260   -946    567       C  
ATOM   1921  O   PRO A 247     -22.410  27.349  42.526  1.00 49.57           O  
ANISOU 1921  O   PRO A 247     4574   5547   8713    201   -979    588       O  
ATOM   1922  CB  PRO A 247     -20.415  25.850  40.745  1.00 49.13           C  
ANISOU 1922  CB  PRO A 247     4415   5537   8715    472  -1017    575       C  
ATOM   1923  CG  PRO A 247     -19.304  26.433  39.899  1.00 49.94           C  
ANISOU 1923  CG  PRO A 247     4353   5743   8877    557   -980    593       C  
ATOM   1924  CD  PRO A 247     -19.588  27.921  39.831  1.00 48.66           C  
ANISOU 1924  CD  PRO A 247     4107   5640   8741    463   -916    619       C  
ATOM   1925  N   PRO A 248     -23.868  26.176  41.271  1.00 48.93           N  
ANISOU 1925  N   PRO A 248     4582   5440   8567    217   -923    544       N  
ATOM   1926  CA  PRO A 248     -24.959  26.285  42.235  1.00 48.53           C  
ANISOU 1926  CA  PRO A 248     4615   5359   8463     97   -921    542       C  
ATOM   1927  C   PRO A 248     -24.461  26.031  43.659  1.00 49.20           C  
ANISOU 1927  C   PRO A 248     4774   5388   8532     56  -1003    561       C  
ATOM   1928  O   PRO A 248     -23.753  25.078  43.860  1.00 48.82           O  
ANISOU 1928  O   PRO A 248     4782   5285   8480    109  -1082    565       O  
ATOM   1929  CB  PRO A 248     -25.946  25.192  41.819  1.00 48.16           C  
ANISOU 1929  CB  PRO A 248     4668   5270   8358     76   -921    523       C  
ATOM   1930  CG  PRO A 248     -25.715  25.045  40.330  1.00 48.46           C  
ANISOU 1930  CG  PRO A 248     4646   5341   8426    176   -884    507       C  
ATOM   1931  CD  PRO A 248     -24.239  25.339  40.117  1.00 49.43           C  
ANISOU 1931  CD  PRO A 248     4675   5495   8609    279   -902    519       C  
ATOM   1932  N   ALA A 249     -24.824  26.913  44.584  1.00 50.27           N  
ANISOU 1932  N   ALA A 249     4911   5535   8653    -28   -988    570       N  
ATOM   1933  CA  ALA A 249     -24.387  26.855  45.994  1.00 52.44           C  
ANISOU 1933  CA  ALA A 249     5258   5757   8906    -77  -1063    589       C  
ATOM   1934  C   ALA A 249     -25.412  27.583  46.866  1.00 53.37           C  
ANISOU 1934  C   ALA A 249     5415   5890   8970   -185  -1020    583       C  
ATOM   1935  O   ALA A 249     -25.985  28.568  46.381  1.00 52.08           O  
ANISOU 1935  O   ALA A 249     5178   5789   8820   -194   -942    569       O  
ATOM   1936  CB  ALA A 249     -23.007  27.446  46.124  1.00 52.26           C  
ANISOU 1936  CB  ALA A 249     5152   5749   8954    -18  -1110    613       C  
ATOM   1937  N   GLN A 250     -25.638  27.074  48.081  1.00 56.55           N  
ANISOU 1937  N   GLN A 250     5937   6238   9308   -258  -1071    592       N  
ATOM   1938  CA  GLN A 250     -26.533  27.693  49.094  1.00 58.95           C  
ANISOU 1938  CA  GLN A 250     6289   6560   9546   -357  -1034    585       C  
ATOM   1939  C   GLN A 250     -26.098  29.152  49.289  1.00 60.00           C  
ANISOU 1939  C   GLN A 250     6345   6729   9723   -339  -1016    585       C  
ATOM   1940  O   GLN A 250     -24.916  29.376  49.539  1.00 62.31           O  
ANISOU 1940  O   GLN A 250     6618   6991  10066   -301  -1086    609       O  
ATOM   1941  CB  GLN A 250     -26.511  26.899  50.400  1.00 60.36           C  
ANISOU 1941  CB  GLN A 250     6613   6668   9653   -430  -1108    602       C  
ATOM   1942  CG  GLN A 250     -27.901  26.661  50.972  1.00 61.95           C  
ANISOU 1942  CG  GLN A 250     6889   6896   9753   -540  -1052    593       C  
ATOM   1943  CD  GLN A 250     -28.753  25.743  50.121  1.00 63.03           C  
ANISOU 1943  CD  GLN A 250     7034   7047   9865   -560  -1019    587       C  
ATOM   1944  OE1 GLN A 250     -28.308  25.147  49.141  1.00 64.08           O  
ANISOU 1944  OE1 GLN A 250     7144   7154  10046   -488  -1047    587       O  
ATOM   1945  NE2 GLN A 250     -30.007  25.590  50.513  1.00 63.46           N  
ANISOU 1945  NE2 GLN A 250     7128   7147   9837   -662   -963    582       N  
ATOM   1946  N   TYR A 251     -27.019  30.107  49.158  1.00 60.59           N  
ANISOU 1946  N   TYR A 251     6378   6863   9778   -364   -934    561       N  
ATOM   1947  CA  TYR A 251     -26.729  31.564  49.178  1.00 61.05           C  
ANISOU 1947  CA  TYR A 251     6372   6949   9872   -344   -920    557       C  
ATOM   1948  C   TYR A 251     -27.993  32.332  49.566  1.00 61.89           C  
ANISOU 1948  C   TYR A 251     6495   7104   9915   -387   -847    520       C  
ATOM   1949  O   TYR A 251     -29.071  31.957  49.075  1.00 61.44           O  
ANISOU 1949  O   TYR A 251     6423   7093   9826   -403   -778    497       O  
ATOM   1950  CB  TYR A 251     -26.209  32.009  47.810  1.00 60.93           C  
ANISOU 1950  CB  TYR A 251     6236   6970   9941   -271   -898    562       C  
ATOM   1951  CG  TYR A 251     -25.684  33.418  47.744  1.00 62.03           C  
ANISOU 1951  CG  TYR A 251     6316   7126  10124   -257   -907    572       C  
ATOM   1952  CD1 TYR A 251     -25.084  34.030  48.838  1.00 63.03           C  
ANISOU 1952  CD1 TYR A 251     6492   7213  10243   -287   -974    590       C  
ATOM   1953  CD2 TYR A 251     -25.745  34.127  46.555  1.00 62.45           C  
ANISOU 1953  CD2 TYR A 251     6275   7228  10224   -217   -859    567       C  
ATOM   1954  CE1 TYR A 251     -24.608  35.328  48.767  1.00 63.32           C  
ANISOU 1954  CE1 TYR A 251     6487   7255  10314   -284   -995    603       C  
ATOM   1955  CE2 TYR A 251     -25.265  35.424  46.466  1.00 63.09           C  
ANISOU 1955  CE2 TYR A 251     6313   7317  10339   -216   -878    581       C  
ATOM   1956  CZ  TYR A 251     -24.689  36.023  47.572  1.00 63.63           C  
ANISOU 1956  CZ  TYR A 251     6434   7343  10398   -250   -949    601       C  
ATOM   1957  OH  TYR A 251     -24.207  37.295  47.455  1.00 64.78           O  
ANISOU 1957  OH  TYR A 251     6549   7488  10574   -257   -981    620       O  
ATOM   1958  N   GLU A 252     -27.853  33.350  50.426  1.00 63.94           N  
ANISOU 1958  N   GLU A 252     6787   7354  10154   -402   -866    515       N  
ATOM   1959  CA  GLU A 252     -28.964  34.197  50.940  1.00 64.41           C  
ANISOU 1959  CA  GLU A 252     6869   7459  10144   -424   -804    473       C  
ATOM   1960  C   GLU A 252     -29.080  35.433  50.041  1.00 62.47           C  
ANISOU 1960  C   GLU A 252     6538   7249   9949   -368   -772    453       C  
ATOM   1961  O   GLU A 252     -28.086  36.162  49.925  1.00 63.19           O  
ANISOU 1961  O   GLU A 252     6608   7304  10095   -343   -831    477       O  
ATOM   1962  CB  GLU A 252     -28.735  34.553  52.418  1.00 67.25           C  
ANISOU 1962  CB  GLU A 252     7336   7776  10439   -464   -853    475       C  
ATOM   1963  CG  GLU A 252     -29.725  35.558  52.998  1.00 70.76           C  
ANISOU 1963  CG  GLU A 252     7808   8266  10809   -465   -796    427       C  
ATOM   1964  CD  GLU A 252     -30.308  35.254  54.371  1.00 74.71           C  
ANISOU 1964  CD  GLU A 252     8419   8772  11194   -526   -782    413       C  
ATOM   1965  OE1 GLU A 252     -30.542  34.056  54.673  1.00 78.03           O  
ANISOU 1965  OE1 GLU A 252     8881   9191  11573   -587   -777    432       O  
ATOM   1966  OE2 GLU A 252     -30.556  36.220  55.113  1.00 75.61           O  
ANISOU 1966  OE2 GLU A 252     8583   8889  11253   -513   -778    382       O  
ATOM   1967  N   LEU A 253     -30.240  35.621  49.404  1.00 60.76           N  
ANISOU 1967  N   LEU A 253     6272   7099   9713   -353   -689    413       N  
ATOM   1968  CA  LEU A 253     -30.579  36.834  48.614  1.00 59.17           C  
ANISOU 1968  CA  LEU A 253     6007   6931   9544   -300   -660    385       C  
ATOM   1969  C   LEU A 253     -31.283  37.843  49.526  1.00 58.94           C  
ANISOU 1969  C   LEU A 253     6031   6920   9444   -295   -643    340       C  
ATOM   1970  O   LEU A 253     -32.341  37.497  50.117  1.00 59.75           O  
ANISOU 1970  O   LEU A 253     6158   7075   9467   -319   -585    306       O  
ATOM   1971  CB  LEU A 253     -31.473  36.446  47.434  1.00 58.40           C  
ANISOU 1971  CB  LEU A 253     5832   6894   9463   -281   -588    364       C  
ATOM   1972  CG  LEU A 253     -30.789  35.666  46.318  1.00 57.60           C  
ANISOU 1972  CG  LEU A 253     5678   6776   9432   -263   -602    400       C  
ATOM   1973  CD1 LEU A 253     -31.793  35.268  45.256  1.00 57.72           C  
ANISOU 1973  CD1 LEU A 253     5636   6843   9449   -251   -536    376       C  
ATOM   1974  CD2 LEU A 253     -29.664  36.474  45.710  1.00 57.83           C  
ANISOU 1974  CD2 LEU A 253     5662   6776   9533   -223   -647    428       C  
ATOM   1975  N   LYS A 254     -30.696  39.033  49.644  1.00 57.85           N  
ANISOU 1975  N   LYS A 254     5913   6740   9327   -265   -698    341       N  
ATOM   1976  CA  LYS A 254     -31.255  40.161  50.424  1.00 57.47           C  
ANISOU 1976  CA  LYS A 254     5929   6694   9212   -239   -699    293       C  
ATOM   1977  C   LYS A 254     -32.025  41.070  49.461  1.00 54.84           C  
ANISOU 1977  C   LYS A 254     5537   6403   8896   -175   -659    249       C  
ATOM   1978  O   LYS A 254     -31.493  41.380  48.367  1.00 51.59           O  
ANISOU 1978  O   LYS A 254     5067   5972   8560   -158   -684    275       O  
ATOM   1979  CB  LYS A 254     -30.144  40.911  51.161  1.00 60.06           C  
ANISOU 1979  CB  LYS A 254     6337   6935   9546   -250   -801    323       C  
ATOM   1980  CG  LYS A 254     -30.495  41.325  52.584  1.00 63.05           C  
ANISOU 1980  CG  LYS A 254     6834   7297   9825   -255   -815    288       C  
ATOM   1981  CD  LYS A 254     -29.465  42.259  53.189  1.00 64.53           C  
ANISOU 1981  CD  LYS A 254     7106   7390  10020   -261   -928    315       C  
ATOM   1982  CE  LYS A 254     -29.843  42.758  54.568  1.00 65.33           C  
ANISOU 1982  CE  LYS A 254     7340   7468  10013   -255   -945    274       C  
ATOM   1983  NZ  LYS A 254     -29.038  43.945  54.929  1.00 65.61           N  
ANISOU 1983  NZ  LYS A 254     7462   7411  10055   -246  -1059    289       N  
ATOM   1984  N   HIS A 255     -33.243  41.444  49.862  1.00 53.23           N  
ANISOU 1984  N   HIS A 255     5346   6260   8618   -141   -600    184       N  
ATOM   1985  CA  HIS A 255     -34.191  42.292  49.094  1.00 51.88           C  
ANISOU 1985  CA  HIS A 255     5124   6138   8447    -67   -562    127       C  
ATOM   1986  C   HIS A 255     -33.478  43.564  48.610  1.00 51.19           C  
ANISOU 1986  C   HIS A 255     5067   5975   8406    -27   -645    136       C  
ATOM   1987  O   HIS A 255     -32.795  44.227  49.429  1.00 50.85           O  
ANISOU 1987  O   HIS A 255     5118   5861   8340    -33   -721    147       O  
ATOM   1988  CB  HIS A 255     -35.431  42.587  49.947  1.00 52.35           C  
ANISOU 1988  CB  HIS A 255     5209   6273   8406    -29   -500     54       C  
ATOM   1989  CG  HIS A 255     -36.304  43.656  49.391  1.00 52.57           C  
ANISOU 1989  CG  HIS A 255     5207   6338   8425     64   -483    -11       C  
ATOM   1990  ND1 HIS A 255     -36.683  44.760  50.125  1.00 53.39           N  
ANISOU 1990  ND1 HIS A 255     5388   6436   8459    139   -504    -73       N  
ATOM   1991  CD2 HIS A 255     -36.848  43.808  48.168  1.00 52.43           C  
ANISOU 1991  CD2 HIS A 255     5103   6358   8460    104   -458    -27       C  
ATOM   1992  CE1 HIS A 255     -37.425  45.548  49.376  1.00 53.70           C  
ANISOU 1992  CE1 HIS A 255     5387   6507   8510    225   -495   -126       C  
ATOM   1993  NE2 HIS A 255     -37.543  44.988  48.172  1.00 53.33           N  
ANISOU 1993  NE2 HIS A 255     5237   6486   8538    201   -467    -98       N  
ATOM   1994  N   GLY A 256     -33.600  43.858  47.311  1.00 49.73           N  
ANISOU 1994  N   GLY A 256     4812   5800   8283      0   -639    138       N  
ATOM   1995  CA  GLY A 256     -33.233  45.149  46.698  1.00 48.33           C  
ANISOU 1995  CA  GLY A 256     4661   5564   8137     39   -710    138       C  
ATOM   1996  C   GLY A 256     -31.737  45.354  46.588  1.00 46.85           C  
ANISOU 1996  C   GLY A 256     4497   5296   8005    -16   -798    216       C  
ATOM   1997  O   GLY A 256     -31.354  46.501  46.371  1.00 46.89           O  
ANISOU 1997  O   GLY A 256     4553   5243   8020     -2   -874    222       O  
ATOM   1998  N   THR A 257     -30.931  44.289  46.711  1.00 45.87           N  
ANISOU 1998  N   THR A 257     4339   5173   7917    -76   -794    273       N  
ATOM   1999  CA  THR A 257     -29.450  44.282  46.501  1.00 44.23           C  
ANISOU 1999  CA  THR A 257     4118   4913   7773   -129   -868    353       C  
ATOM   2000  C   THR A 257     -29.116  43.670  45.134  1.00 42.19           C  
ANISOU 2000  C   THR A 257     3750   4692   7586   -134   -830    391       C  
ATOM   2001  O   THR A 257     -27.921  43.472  44.849  1.00 42.43           O  
ANISOU 2001  O   THR A 257     3742   4706   7671   -172   -872    457       O  
ATOM   2002  CB  THR A 257     -28.734  43.479  47.594  1.00 44.34           C  
ANISOU 2002  CB  THR A 257     4168   4903   7776   -177   -897    387       C  
ATOM   2003  OG1 THR A 257     -29.161  42.119  47.479  1.00 44.63           O  
ANISOU 2003  OG1 THR A 257     4155   4992   7810   -183   -821    381       O  
ATOM   2004  CG2 THR A 257     -29.017  43.995  48.986  1.00 45.02           C  
ANISOU 2004  CG2 THR A 257     4373   4951   7782   -174   -933    352       C  
ATOM   2005  N   PHE A 258     -30.137  43.349  44.340  1.00 40.26           N  
ANISOU 2005  N   PHE A 258     3455   4501   7338    -97   -753    350       N  
ATOM   2006  CA  PHE A 258     -30.014  42.697  43.014  1.00 39.02           C  
ANISOU 2006  CA  PHE A 258     3207   4382   7236    -93   -709    374       C  
ATOM   2007  C   PHE A 258     -31.327  42.912  42.262  1.00 38.29           C  
ANISOU 2007  C   PHE A 258     3089   4331   7126    -45   -651    317       C  
ATOM   2008  O   PHE A 258     -32.312  43.314  42.913  1.00 39.11           O  
ANISOU 2008  O   PHE A 258     3234   4450   7176    -16   -635    258       O  
ATOM   2009  CB  PHE A 258     -29.683  41.208  43.168  1.00 38.77           C  
ANISOU 2009  CB  PHE A 258     3142   4371   7216   -116   -676    400       C  
ATOM   2010  CG  PHE A 258     -30.812  40.365  43.710  1.00 38.23           C  
ANISOU 2010  CG  PHE A 258     3091   4339   7094   -115   -616    354       C  
ATOM   2011  CD1 PHE A 258     -31.570  39.571  42.865  1.00 37.76           C  
ANISOU 2011  CD1 PHE A 258     2980   4325   7040   -103   -554    337       C  
ATOM   2012  CD2 PHE A 258     -31.117  40.380  45.061  1.00 38.35           C  
ANISOU 2012  CD2 PHE A 258     3176   4344   7048   -134   -626    332       C  
ATOM   2013  CE1 PHE A 258     -32.619  38.818  43.362  1.00 38.21           C  
ANISOU 2013  CE1 PHE A 258     3049   4422   7044   -119   -504    303       C  
ATOM   2014  CE2 PHE A 258     -32.168  39.626  45.559  1.00 38.67           C  
ANISOU 2014  CE2 PHE A 258     3227   4433   7032   -146   -566    296       C  
ATOM   2015  CZ  PHE A 258     -32.921  38.851  44.709  1.00 38.54           C  
ANISOU 2015  CZ  PHE A 258     3151   4466   7023   -144   -506    284       C  
ATOM   2016  N   THR A 259     -31.319  42.682  40.949  1.00 36.97           N  
ANISOU 2016  N   THR A 259     2858   4185   7001    -34   -623    332       N  
ATOM   2017  CA  THR A 259     -32.505  42.744  40.068  1.00 36.52           C  
ANISOU 2017  CA  THR A 259     2769   4168   6937      6   -573    285       C  
ATOM   2018  C   THR A 259     -33.262  41.414  40.175  1.00 36.74           C  
ANISOU 2018  C   THR A 259     2764   4246   6947      0   -506    265       C  
ATOM   2019  O   THR A 259     -34.312  41.368  40.842  1.00 36.79           O  
ANISOU 2019  O   THR A 259     2783   4290   6905     10   -475    216       O  
ATOM   2020  CB  THR A 259     -32.091  43.033  38.623  1.00 36.11           C  
ANISOU 2020  CB  THR A 259     2676   4109   6932     12   -579    316       C  
ATOM   2021  OG1 THR A 259     -31.356  44.257  38.578  1.00 36.31           O  
ANISOU 2021  OG1 THR A 259     2739   4086   6967      0   -650    344       O  
ATOM   2022  CG2 THR A 259     -33.282  43.088  37.690  1.00 36.10           C  
ANISOU 2022  CG2 THR A 259     2648   4140   6925     54   -539    269       C  
ATOM   2023  N   CYS A 260     -32.729  40.364  39.548  1.00 36.81           N  
ANISOU 2023  N   CYS A 260     2737   4260   6989    -18   -488    304       N  
ATOM   2024  CA  CYS A 260     -33.288  38.989  39.548  1.00 36.60           C  
ANISOU 2024  CA  CYS A 260     2695   4266   6946    -36   -441    298       C  
ATOM   2025  C   CYS A 260     -32.140  37.979  39.627  1.00 37.03           C  
ANISOU 2025  C   CYS A 260     2752   4292   7023    -58   -461    349       C  
ATOM   2026  O   CYS A 260     -30.978  38.372  39.423  1.00 36.75           O  
ANISOU 2026  O   CYS A 260     2705   4231   7024    -52   -497    388       O  
ATOM   2027  CB  CYS A 260     -34.141  38.741  38.311  1.00 36.14           C  
ANISOU 2027  CB  CYS A 260     2593   4238   6898    -13   -403    277       C  
ATOM   2028  SG  CYS A 260     -33.234  38.878  36.748  1.00 35.90           S  
ANISOU 2028  SG  CYS A 260     2530   4186   6924     12   -413    316       S  
ATOM   2029  N   ALA A 261     -32.471  36.732  39.947  1.00 37.74           N  
ANISOU 2029  N   ALA A 261     2859   4390   7088    -83   -442    348       N  
ATOM   2030  CA  ALA A 261     -31.538  35.600  40.124  1.00 38.17           C  
ANISOU 2030  CA  ALA A 261     2933   4414   7154    -94   -468    387       C  
ATOM   2031  C   ALA A 261     -32.094  34.367  39.406  1.00 39.19           C  
ANISOU 2031  C   ALA A 261     3065   4552   7272    -95   -442    382       C  
ATOM   2032  O   ALA A 261     -33.254  34.409  38.901  1.00 40.60           O  
ANISOU 2032  O   ALA A 261     3226   4765   7434   -100   -404    352       O  
ATOM   2033  CB  ALA A 261     -31.338  35.324  41.593  1.00 38.25           C  
ANISOU 2033  CB  ALA A 261     3002   4402   7126   -136   -497    393       C  
ATOM   2034  N   SER A 262     -31.286  33.308  39.357  1.00 39.21           N  
ANISOU 2034  N   SER A 262     3092   4521   7284    -87   -470    411       N  
ATOM   2035  CA  SER A 262     -31.665  31.973  38.840  1.00 39.36           C  
ANISOU 2035  CA  SER A 262     3145   4527   7284    -89   -468    410       C  
ATOM   2036  C   SER A 262     -31.271  30.932  39.893  1.00 40.21           C  
ANISOU 2036  C   SER A 262     3327   4591   7359   -124   -515    429       C  
ATOM   2037  O   SER A 262     -30.082  30.871  40.268  1.00 40.89           O  
ANISOU 2037  O   SER A 262     3418   4647   7470    -96   -558    453       O  
ATOM   2038  CB  SER A 262     -31.039  31.729  37.493  1.00 39.13           C  
ANISOU 2038  CB  SER A 262     3082   4492   7291    -22   -464    420       C  
ATOM   2039  OG  SER A 262     -31.082  32.918  36.704  1.00 38.89           O  
ANISOU 2039  OG  SER A 262     2989   4495   7293      4   -433    414       O  
ATOM   2040  N   GLU A 263     -32.263  30.206  40.411  1.00 40.58           N  
ANISOU 2040  N   GLU A 263     3428   4639   7350   -191   -511    420       N  
ATOM   2041  CA  GLU A 263     -32.081  29.082  41.364  1.00 40.67           C  
ANISOU 2041  CA  GLU A 263     3533   4603   7316   -241   -562    439       C  
ATOM   2042  C   GLU A 263     -31.979  27.776  40.575  1.00 39.96           C  
ANISOU 2042  C   GLU A 263     3496   4467   7220   -220   -596    449       C  
ATOM   2043  O   GLU A 263     -32.627  27.680  39.525  1.00 39.93           O  
ANISOU 2043  O   GLU A 263     3467   4484   7221   -207   -566    436       O  
ATOM   2044  CB  GLU A 263     -33.260  29.017  42.331  1.00 41.54           C  
ANISOU 2044  CB  GLU A 263     3676   4749   7358   -339   -537    430       C  
ATOM   2045  CG  GLU A 263     -33.028  28.073  43.485  1.00 42.72           C  
ANISOU 2045  CG  GLU A 263     3929   4850   7453   -404   -591    455       C  
ATOM   2046  CD  GLU A 263     -34.303  27.491  44.062  1.00 44.06           C  
ANISOU 2046  CD  GLU A 263     4142   5056   7542   -515   -569    456       C  
ATOM   2047  OE1 GLU A 263     -35.008  26.775  43.320  1.00 44.61           O  
ANISOU 2047  OE1 GLU A 263     4219   5131   7596   -544   -565    459       O  
ATOM   2048  OE2 GLU A 263     -34.593  27.759  45.248  1.00 45.65           O  
ANISOU 2048  OE2 GLU A 263     4371   5283   7691   -577   -556    457       O  
ATOM   2049  N   TYR A 264     -31.197  26.813  41.069  1.00 39.30           N  
ANISOU 2049  N   TYR A 264     3492   4316   7121   -213   -665    469       N  
ATOM   2050  CA  TYR A 264     -31.019  25.475  40.450  1.00 38.60           C  
ANISOU 2050  CA  TYR A 264     3483   4166   7016   -183   -718    475       C  
ATOM   2051  C   TYR A 264     -30.908  24.406  41.536  1.00 38.93           C  
ANISOU 2051  C   TYR A 264     3651   4139   7001   -244   -795    495       C  
ATOM   2052  O   TYR A 264     -29.863  24.329  42.190  1.00 38.77           O  
ANISOU 2052  O   TYR A 264     3654   4080   6997   -208   -847    507       O  
ATOM   2053  CB  TYR A 264     -29.780  25.452  39.561  1.00 38.17           C  
ANISOU 2053  CB  TYR A 264     3387   4096   7017    -56   -733    473       C  
ATOM   2054  CG  TYR A 264     -29.745  24.314  38.577  1.00 38.44           C  
ANISOU 2054  CG  TYR A 264     3488   4082   7035      0   -768    465       C  
ATOM   2055  CD1 TYR A 264     -29.099  23.126  38.881  1.00 39.20           C  
ANISOU 2055  CD1 TYR A 264     3689   4098   7105     37   -855    471       C  
ATOM   2056  CD2 TYR A 264     -30.349  24.425  37.341  1.00 38.04           C  
ANISOU 2056  CD2 TYR A 264     3405   4058   6990     24   -723    449       C  
ATOM   2057  CE1 TYR A 264     -29.043  22.076  37.978  1.00 39.68           C  
ANISOU 2057  CE1 TYR A 264     3828   4105   7144    102   -897    459       C  
ATOM   2058  CE2 TYR A 264     -30.310  23.390  36.426  1.00 38.74           C  
ANISOU 2058  CE2 TYR A 264     3568   4095   7056     82   -760    439       C  
ATOM   2059  CZ  TYR A 264     -29.649  22.212  36.741  1.00 39.69           C  
ANISOU 2059  CZ  TYR A 264     3797   4133   7147    124   -847    443       C  
ATOM   2060  OH  TYR A 264     -29.631  21.191  35.833  1.00 40.64           O  
ANISOU 2060  OH  TYR A 264     4007   4195   7237    190   -891    429       O  
ATOM   2061  N   THR A 265     -31.981  23.635  41.721  1.00 39.09           N  
ANISOU 2061  N   THR A 265     3749   4146   6955   -343   -807    503       N  
ATOM   2062  CA  THR A 265     -32.060  22.409  42.550  1.00 39.74           C  
ANISOU 2062  CA  THR A 265     3977   4152   6967   -420   -891    528       C  
ATOM   2063  C   THR A 265     -31.801  21.225  41.623  1.00 40.59           C  
ANISOU 2063  C   THR A 265     4174   4179   7067   -362   -961    527       C  
ATOM   2064  O   THR A 265     -31.965  21.411  40.407  1.00 40.04           O  
ANISOU 2064  O   THR A 265     4046   4134   7031   -297   -923    508       O  
ATOM   2065  CB  THR A 265     -33.434  22.302  43.217  1.00 39.86           C  
ANISOU 2065  CB  THR A 265     4019   4214   6909   -574   -859    542       C  
ATOM   2066  OG1 THR A 265     -33.645  23.568  43.833  1.00 38.98           O  
ANISOU 2066  OG1 THR A 265     3809   4188   6814   -590   -782    529       O  
ATOM   2067  CG2 THR A 265     -33.544  21.202  44.252  1.00 40.94           C  
ANISOU 2067  CG2 THR A 265     4308   4282   6964   -680   -941    576       C  
ATOM   2068  N   GLY A 266     -31.388  20.083  42.180  1.00 42.29           N  
ANISOU 2068  N   GLY A 266     4534   4297   7236   -377  -1065    545       N  
ATOM   2069  CA  GLY A 266     -31.074  18.858  41.413  1.00 43.73           C  
ANISOU 2069  CA  GLY A 266     4833   4383   7399   -311  -1154    540       C  
ATOM   2070  C   GLY A 266     -29.656  18.890  40.881  1.00 44.68           C  
ANISOU 2070  C   GLY A 266     4917   4478   7581   -132  -1180    516       C  
ATOM   2071  O   GLY A 266     -29.023  19.943  40.976  1.00 44.10           O  
ANISOU 2071  O   GLY A 266     4712   4473   7571    -76  -1120    508       O  
ATOM   2072  N   ASN A 267     -29.173  17.777  40.335  1.00 46.92           N  
ANISOU 2072  N   ASN A 267     5313   4670   7842    -44  -1270    504       N  
ATOM   2073  CA  ASN A 267     -27.725  17.566  40.090  1.00 48.78           C  
ANISOU 2073  CA  ASN A 267     5535   4876   8121    128  -1317    482       C  
ATOM   2074  C   ASN A 267     -27.453  17.198  38.633  1.00 50.10           C  
ANISOU 2074  C   ASN A 267     5696   5036   8300    268  -1310    449       C  
ATOM   2075  O   ASN A 267     -26.508  17.794  38.061  1.00 51.21           O  
ANISOU 2075  O   ASN A 267     5711   5242   8504    401  -1259    429       O  
ATOM   2076  CB  ASN A 267     -27.156  16.499  41.021  1.00 50.48           C  
ANISOU 2076  CB  ASN A 267     5910   4976   8292    133  -1454    492       C  
ATOM   2077  CG  ASN A 267     -26.714  17.073  42.343  1.00 50.93           C  
ANISOU 2077  CG  ASN A 267     5931   5052   8368     77  -1460    514       C  
ATOM   2078  OD1 ASN A 267     -27.170  18.144  42.727  1.00 51.14           O  
ANISOU 2078  OD1 ASN A 267     5849   5166   8416     -8  -1367    527       O  
ATOM   2079  ND2 ASN A 267     -25.824  16.375  43.034  1.00 51.89           N  
ANISOU 2079  ND2 ASN A 267     6149   5088   8477    131  -1575    516       N  
ATOM   2080  N   TYR A 268     -28.179  16.235  38.060  1.00 50.92           N  
ANISOU 2080  N   TYR A 268     5937   5066   8342    242  -1364    444       N  
ATOM   2081  CA  TYR A 268     -27.827  15.651  36.741  1.00 51.81           C  
ANISOU 2081  CA  TYR A 268     6091   5146   8448    392  -1384    408       C  
ATOM   2082  C   TYR A 268     -28.974  15.952  35.779  1.00 51.33           C  
ANISOU 2082  C   TYR A 268     6002   5124   8375    324  -1314    408       C  
ATOM   2083  O   TYR A 268     -28.976  17.085  35.272  1.00 51.98           O  
ANISOU 2083  O   TYR A 268     5919   5315   8516    345  -1199    402       O  
ATOM   2084  CB  TYR A 268     -27.425  14.183  36.886  1.00 52.93           C  
ANISOU 2084  CB  TYR A 268     6440   5145   8525    457  -1536    396       C  
ATOM   2085  CG  TYR A 268     -26.397  13.941  37.959  1.00 53.46           C  
ANISOU 2085  CG  TYR A 268     6534   5173   8605    506  -1612    399       C  
ATOM   2086  CD1 TYR A 268     -25.084  14.373  37.830  1.00 53.74           C  
ANISOU 2086  CD1 TYR A 268     6445   5268   8705    671  -1587    374       C  
ATOM   2087  CD2 TYR A 268     -26.753  13.298  39.131  1.00 54.09           C  
ANISOU 2087  CD2 TYR A 268     6761   5162   8628    377  -1712    432       C  
ATOM   2088  CE1 TYR A 268     -24.151  14.154  38.833  1.00 54.22           C  
ANISOU 2088  CE1 TYR A 268     6526   5293   8780    714  -1666    379       C  
ATOM   2089  CE2 TYR A 268     -25.831  13.058  40.138  1.00 54.60           C  
ANISOU 2089  CE2 TYR A 268     6863   5180   8700    418  -1794    435       C  
ATOM   2090  CZ  TYR A 268     -24.526  13.492  39.993  1.00 54.54           C  
ANISOU 2090  CZ  TYR A 268     6728   5229   8764    590  -1773    408       C  
ATOM   2091  OH  TYR A 268     -23.645  13.254  41.006  1.00 54.78           O  
ANISOU 2091  OH  TYR A 268     6794   5214   8805    626  -1863    413       O  
ATOM   2092  N   GLN A 269     -29.902  15.016  35.553  1.00 51.09           N  
ANISOU 2092  N   GLN A 269     6126   5009   8274    241  -1386    419       N  
ATOM   2093  CA  GLN A 269     -31.077  15.231  34.662  1.00 50.34           C  
ANISOU 2093  CA  GLN A 269     6013   4947   8167    164  -1335    423       C  
ATOM   2094  C   GLN A 269     -32.325  15.504  35.513  1.00 49.83           C  
ANISOU 2094  C   GLN A 269     5933   4920   8079    -50  -1314    467       C  
ATOM   2095  O   GLN A 269     -33.411  15.644  34.929  1.00 49.56           O  
ANISOU 2095  O   GLN A 269     5881   4917   8033   -135  -1281    476       O  
ATOM   2096  CB  GLN A 269     -31.262  14.042  33.711  1.00 51.07           C  
ANISOU 2096  CB  GLN A 269     6281   4926   8195    221  -1432    407       C  
ATOM   2097  CG  GLN A 269     -31.736  12.732  34.351  1.00 51.86           C  
ANISOU 2097  CG  GLN A 269     6602   4893   8209    113  -1580    435       C  
ATOM   2098  CD  GLN A 269     -30.634  11.923  34.990  1.00 52.11           C  
ANISOU 2098  CD  GLN A 269     6754   4826   8217    215  -1690    422       C  
ATOM   2099  OE1 GLN A 269     -29.538  12.419  35.217  1.00 51.79           O  
ANISOU 2099  OE1 GLN A 269     6608   4834   8232    343  -1649    398       O  
ATOM   2100  NE2 GLN A 269     -30.928  10.672  35.311  1.00 52.66           N  
ANISOU 2100  NE2 GLN A 269     7048   4757   8204    153  -1838    440       N  
ATOM   2101  N   CYS A 270     -32.158  15.605  36.837  1.00 49.90           N  
ANISOU 2101  N   CYS A 270     5943   4933   8082   -128  -1329    491       N  
ATOM   2102  CA  CYS A 270     -33.220  15.940  37.827  1.00 49.32           C  
ANISOU 2102  CA  CYS A 270     5841   4916   7981   -324  -1296    530       C  
ATOM   2103  C   CYS A 270     -33.114  17.420  38.221  1.00 47.96           C  
ANISOU 2103  C   CYS A 270     5474   4872   7877   -320  -1170    522       C  
ATOM   2104  O   CYS A 270     -33.707  17.800  39.242  1.00 47.97           O  
ANISOU 2104  O   CYS A 270     5444   4924   7857   -449  -1138    546       O  
ATOM   2105  CB  CYS A 270     -33.118  15.054  39.067  1.00 50.19           C  
ANISOU 2105  CB  CYS A 270     6103   4942   8025   -419  -1400    563       C  
ATOM   2106  SG  CYS A 270     -33.671  13.390  38.804  1.00 51.53           S  
ANISOU 2106  SG  CYS A 270     6520   4964   8094   -496  -1556    589       S  
ATOM   2107  N   GLY A 271     -32.386  18.222  37.434  1.00 46.95           N  
ANISOU 2107  N   GLY A 271     5225   4793   7820   -178  -1103    490       N  
ATOM   2108  CA  GLY A 271     -32.125  19.648  37.709  1.00 45.60           C  
ANISOU 2108  CA  GLY A 271     4882   4728   7714   -159  -1000    481       C  
ATOM   2109  C   GLY A 271     -33.317  20.529  37.353  1.00 44.41           C  
ANISOU 2109  C   GLY A 271     4627   4671   7575   -240   -909    480       C  
ATOM   2110  O   GLY A 271     -33.889  20.324  36.280  1.00 43.49           O  
ANISOU 2110  O   GLY A 271     4517   4552   7453   -228   -902    470       O  
ATOM   2111  N   HIS A 272     -33.660  21.493  38.212  1.00 43.79           N  
ANISOU 2111  N   HIS A 272     4457   4670   7509   -309   -846    485       N  
ATOM   2112  CA  HIS A 272     -34.789  22.440  38.021  1.00 42.74           C  
ANISOU 2112  CA  HIS A 272     4215   4636   7387   -374   -760    477       C  
ATOM   2113  C   HIS A 272     -34.340  23.877  38.335  1.00 41.41           C  
ANISOU 2113  C   HIS A 272     3918   4539   7274   -325   -687    461       C  
ATOM   2114  O   HIS A 272     -33.808  24.117  39.439  1.00 41.30           O  
ANISOU 2114  O   HIS A 272     3912   4523   7257   -341   -697    470       O  
ATOM   2115  CB  HIS A 272     -35.984  22.003  38.877  1.00 43.37           C  
ANISOU 2115  CB  HIS A 272     4339   4742   7398   -535   -768    502       C  
ATOM   2116  CG  HIS A 272     -37.201  22.833  38.661  1.00 43.41           C  
ANISOU 2116  CG  HIS A 272     4231   4854   7408   -594   -688    491       C  
ATOM   2117  ND1 HIS A 272     -37.711  23.037  37.398  1.00 43.50           N  
ANISOU 2117  ND1 HIS A 272     4192   4886   7448   -556   -665    474       N  
ATOM   2118  CD2 HIS A 272     -37.985  23.526  39.522  1.00 43.58           C  
ANISOU 2118  CD2 HIS A 272     4178   4969   7408   -675   -627    489       C  
ATOM   2119  CE1 HIS A 272     -38.780  23.808  37.486  1.00 43.74           C  
ANISOU 2119  CE1 HIS A 272     4120   5018   7480   -613   -600    464       C  
ATOM   2120  NE2 HIS A 272     -38.970  24.123  38.784  1.00 43.78           N  
ANISOU 2120  NE2 HIS A 272     4106   5074   7453   -681   -572    470       N  
ATOM   2121  N   TYR A 273     -34.586  24.803  37.404  1.00 40.22           N  
ANISOU 2121  N   TYR A 273     3666   4445   7169   -274   -625    439       N  
ATOM   2122  CA  TYR A 273     -34.449  26.272  37.581  1.00 39.23           C  
ANISOU 2122  CA  TYR A 273     3426   4389   7089   -245   -559    423       C  
ATOM   2123  C   TYR A 273     -35.754  26.884  38.076  1.00 39.01           C  
ANISOU 2123  C   TYR A 273     3345   4439   7035   -332   -509    412       C  
ATOM   2124  O   TYR A 273     -36.797  26.633  37.458  1.00 39.68           O  
ANISOU 2124  O   TYR A 273     3420   4551   7103   -372   -497    406       O  
ATOM   2125  CB  TYR A 273     -34.194  26.987  36.258  1.00 38.70           C  
ANISOU 2125  CB  TYR A 273     3285   4343   7074   -154   -522    405       C  
ATOM   2126  CG  TYR A 273     -32.775  26.962  35.764  1.00 38.49           C  
ANISOU 2126  CG  TYR A 273     3252   4284   7086    -48   -539    411       C  
ATOM   2127  CD1 TYR A 273     -32.411  26.124  34.726  1.00 38.71           C  
ANISOU 2127  CD1 TYR A 273     3327   4270   7110     19   -564    409       C  
ATOM   2128  CD2 TYR A 273     -31.810  27.799  36.301  1.00 37.99           C  
ANISOU 2128  CD2 TYR A 273     3134   4240   7060    -15   -531    419       C  
ATOM   2129  CE1 TYR A 273     -31.111  26.098  34.249  1.00 38.77           C  
ANISOU 2129  CE1 TYR A 273     3315   4267   7148    125   -571    411       C  
ATOM   2130  CE2 TYR A 273     -30.507  27.780  35.834  1.00 38.08           C  
ANISOU 2130  CE2 TYR A 273     3120   4241   7108     76   -543    429       C  
ATOM   2131  CZ  TYR A 273     -30.158  26.925  34.805  1.00 38.11           C  
ANISOU 2131  CZ  TYR A 273     3158   4215   7104    150   -558    423       C  
ATOM   2132  OH  TYR A 273     -28.899  26.900  34.306  1.00 38.12           O  
ANISOU 2132  OH  TYR A 273     3122   4225   7135    249   -561    430       O  
ATOM   2133  N   LYS A 274     -35.678  27.696  39.126  1.00 38.56           N  
ANISOU 2133  N   LYS A 274     3254   4420   6975   -353   -484    406       N  
ATOM   2134  CA  LYS A 274     -36.715  28.698  39.489  1.00 38.02           C  
ANISOU 2134  CA  LYS A 274     3109   4441   6895   -388   -423    381       C  
ATOM   2135  C   LYS A 274     -36.110  30.087  39.283  1.00 37.45           C  
ANISOU 2135  C   LYS A 274     2967   4384   6877   -304   -397    361       C  
ATOM   2136  O   LYS A 274     -34.872  30.189  39.221  1.00 37.87           O  
ANISOU 2136  O   LYS A 274     3034   4387   6966   -249   -427    376       O  
ATOM   2137  CB  LYS A 274     -37.162  28.551  40.944  1.00 38.03           C  
ANISOU 2137  CB  LYS A 274     3142   4474   6832   -478   -416    388       C  
ATOM   2138  CG  LYS A 274     -37.791  27.214  41.302  1.00 38.51           C  
ANISOU 2138  CG  LYS A 274     3281   4524   6827   -586   -446    418       C  
ATOM   2139  CD  LYS A 274     -38.329  27.192  42.710  1.00 38.99           C  
ANISOU 2139  CD  LYS A 274     3363   4636   6815   -683   -425    425       C  
ATOM   2140  CE  LYS A 274     -38.536  25.795  43.246  1.00 39.46           C  
ANISOU 2140  CE  LYS A 274     3533   4655   6805   -797   -478    468       C  
ATOM   2141  NZ  LYS A 274     -39.244  25.866  44.537  1.00 40.08           N  
ANISOU 2141  NZ  LYS A 274     3616   4808   6803   -902   -441    475       N  
ATOM   2142  N   HIS A 275     -36.953  31.112  39.196  1.00 37.24           N  
ANISOU 2142  N   HIS A 275     2870   4425   6854   -298   -351    329       N  
ATOM   2143  CA  HIS A 275     -36.543  32.526  39.016  1.00 36.71           C  
ANISOU 2143  CA  HIS A 275     2751   4369   6829   -228   -336    308       C  
ATOM   2144  C   HIS A 275     -36.940  33.330  40.257  1.00 36.51           C  
ANISOU 2144  C   HIS A 275     2719   4387   6766   -248   -315    284       C  
ATOM   2145  O   HIS A 275     -38.098  33.214  40.685  1.00 36.76           O  
ANISOU 2145  O   HIS A 275     2729   4486   6750   -294   -280    264       O  
ATOM   2146  CB  HIS A 275     -37.161  33.085  37.736  1.00 36.85           C  
ANISOU 2146  CB  HIS A 275     2709   4413   6878   -184   -314    284       C  
ATOM   2147  CG  HIS A 275     -36.740  34.489  37.450  1.00 37.05           C  
ANISOU 2147  CG  HIS A 275     2698   4437   6941   -120   -312    267       C  
ATOM   2148  ND1 HIS A 275     -35.500  34.789  36.904  1.00 36.97           N  
ANISOU 2148  ND1 HIS A 275     2693   4379   6974    -75   -336    293       N  
ATOM   2149  CD2 HIS A 275     -37.373  35.668  37.646  1.00 36.89           C  
ANISOU 2149  CD2 HIS A 275     2642   4457   6917    -95   -295    230       C  
ATOM   2150  CE1 HIS A 275     -35.406  36.093  36.756  1.00 36.84           C  
ANISOU 2150  CE1 HIS A 275     2651   4369   6979    -39   -338    278       C  
ATOM   2151  NE2 HIS A 275     -36.540  36.654  37.207  1.00 36.63           N  
ANISOU 2151  NE2 HIS A 275     2606   4388   6923    -44   -318    236       N  
ATOM   2152  N   ILE A 276     -35.996  34.070  40.837  1.00 36.16           N  
ANISOU 2152  N   ILE A 276     2692   4309   6737   -218   -339    290       N  
ATOM   2153  CA  ILE A 276     -36.269  34.993  41.972  1.00 36.49           C  
ANISOU 2153  CA  ILE A 276     2742   4380   6742   -221   -327    263       C  
ATOM   2154  C   ILE A 276     -36.039  36.418  41.475  1.00 36.28           C  
ANISOU 2154  C   ILE A 276     2683   4346   6755   -150   -335    240       C  
ATOM   2155  O   ILE A 276     -35.055  36.657  40.778  1.00 35.27           O  
ANISOU 2155  O   ILE A 276     2550   4169   6680   -119   -368    267       O  
ATOM   2156  CB  ILE A 276     -35.425  34.664  43.219  1.00 36.81           C  
ANISOU 2156  CB  ILE A 276     2854   4375   6754   -258   -363    290       C  
ATOM   2157  CG1 ILE A 276     -35.865  33.349  43.870  1.00 37.29           C  
ANISOU 2157  CG1 ILE A 276     2963   4447   6757   -340   -358    308       C  
ATOM   2158  CG2 ILE A 276     -35.479  35.812  44.212  1.00 37.09           C  
ANISOU 2158  CG2 ILE A 276     2909   4424   6759   -241   -363    262       C  
ATOM   2159  CD1 ILE A 276     -35.316  32.120  43.182  1.00 37.17           C  
ANISOU 2159  CD1 ILE A 276     2976   4377   6769   -352   -394    345       C  
ATOM   2160  N   THR A 277     -36.960  37.313  41.820  1.00 37.32           N  
ANISOU 2160  N   THR A 277     2794   4530   6854   -125   -309    192       N  
ATOM   2161  CA  THR A 277     -36.971  38.730  41.392  1.00 37.78           C  
ANISOU 2161  CA  THR A 277     2837   4579   6937    -56   -326    161       C  
ATOM   2162  C   THR A 277     -37.173  39.595  42.638  1.00 39.18           C  
ANISOU 2162  C   THR A 277     3056   4769   7061    -38   -331    125       C  
ATOM   2163  O   THR A 277     -37.989  39.208  43.489  1.00 40.36           O  
ANISOU 2163  O   THR A 277     3204   4980   7148    -64   -288    101       O  
ATOM   2164  CB  THR A 277     -38.020  38.947  40.296  1.00 37.54           C  
ANISOU 2164  CB  THR A 277     2743   4597   6923    -20   -297    127       C  
ATOM   2165  OG1 THR A 277     -37.736  40.219  39.726  1.00 37.35           O  
ANISOU 2165  OG1 THR A 277     2724   4537   6930     42   -333    112       O  
ATOM   2166  CG2 THR A 277     -39.447  38.877  40.791  1.00 38.08           C  
ANISOU 2166  CG2 THR A 277     2770   4760   6936    -23   -246     78       C  
ATOM   2167  N   SER A 278     -36.414  40.683  42.758  1.00 40.24           N  
ANISOU 2167  N   SER A 278     3232   4842   7212     -1   -385    127       N  
ATOM   2168  CA  SER A 278     -36.521  41.677  43.851  1.00 41.25           C  
ANISOU 2168  CA  SER A 278     3420   4962   7288     29   -407     90       C  
ATOM   2169  C   SER A 278     -37.435  42.801  43.376  1.00 41.67           C  
ANISOU 2169  C   SER A 278     3454   5044   7333    111   -404     27       C  
ATOM   2170  O   SER A 278     -37.078  43.463  42.387  1.00 40.50           O  
ANISOU 2170  O   SER A 278     3302   4850   7235    140   -446     37       O  
ATOM   2171  CB  SER A 278     -35.163  42.196  44.270  1.00 41.58           C  
ANISOU 2171  CB  SER A 278     3531   4914   7351     14   -483    132       C  
ATOM   2172  OG  SER A 278     -35.260  42.979  45.454  1.00 42.63           O  
ANISOU 2172  OG  SER A 278     3741   5032   7423     36   -510     99       O  
ATOM   2173  N   LYS A 279     -38.578  42.966  44.047  1.00 43.53           N  
ANISOU 2173  N   LYS A 279     3677   5359   7503    147   -357    -34       N  
ATOM   2174  CA  LYS A 279     -39.589  44.021  43.774  1.00 44.62           C  
ANISOU 2174  CA  LYS A 279     3795   5538   7620    244   -354   -109       C  
ATOM   2175  C   LYS A 279     -39.890  44.703  45.111  1.00 45.85           C  
ANISOU 2175  C   LYS A 279     4016   5713   7692    292   -354   -162       C  
ATOM   2176  O   LYS A 279     -38.909  45.009  45.818  1.00 46.91           O  
ANISOU 2176  O   LYS A 279     4244   5766   7814    270   -409   -135       O  
ATOM   2177  CB  LYS A 279     -40.747  43.393  42.998  1.00 44.59           C  
ANISOU 2177  CB  LYS A 279     3682   5631   7627    247   -290   -130       C  
ATOM   2178  CG  LYS A 279     -40.379  43.219  41.525  1.00 44.32           C  
ANISOU 2178  CG  LYS A 279     3616   5549   7674    234   -317    -91       C  
ATOM   2179  CD  LYS A 279     -40.890  41.976  40.824  1.00 45.23           C  
ANISOU 2179  CD  LYS A 279     3653   5720   7812    177   -267    -66       C  
ATOM   2180  CE  LYS A 279     -42.043  42.222  39.862  1.00 46.80           C  
ANISOU 2180  CE  LYS A 279     3774   5978   8026    228   -251   -109       C  
ATOM   2181  NZ  LYS A 279     -42.014  41.290  38.707  1.00 46.59           N  
ANISOU 2181  NZ  LYS A 279     3710   5943   8050    178   -245    -65       N  
ATOM   2182  N   GLU A 280     -41.154  44.953  45.450  1.00 46.96           N  
ANISOU 2182  N   GLU A 280     4111   5958   7774    358   -298   -236       N  
ATOM   2183  CA  GLU A 280     -41.496  45.578  46.757  1.00 48.77           C  
ANISOU 2183  CA  GLU A 280     4403   6217   7907    417   -288   -295       C  
ATOM   2184  C   GLU A 280     -41.030  44.632  47.873  1.00 49.13           C  
ANISOU 2184  C   GLU A 280     4488   6272   7906    317   -255   -250       C  
ATOM   2185  O   GLU A 280     -40.585  45.136  48.920  1.00 49.79           O  
ANISOU 2185  O   GLU A 280     4675   6309   7932    334   -288   -264       O  
ATOM   2186  CB  GLU A 280     -42.984  45.923  46.842  1.00 50.25           C  
ANISOU 2186  CB  GLU A 280     4510   6541   8040    512   -223   -383       C  
ATOM   2187  CG  GLU A 280     -43.899  44.740  47.097  1.00 51.04           C  
ANISOU 2187  CG  GLU A 280     4496   6789   8105    443   -115   -377       C  
ATOM   2188  CD  GLU A 280     -44.287  43.918  45.878  1.00 51.01           C  
ANISOU 2188  CD  GLU A 280     4382   6823   8175    387    -92   -340       C  
ATOM   2189  OE1 GLU A 280     -43.629  44.046  44.805  1.00 49.40           O  
ANISOU 2189  OE1 GLU A 280     4194   6518   8056    381   -154   -303       O  
ATOM   2190  OE2 GLU A 280     -45.270  43.157  46.007  1.00 52.53           O  
ANISOU 2190  OE2 GLU A 280     4472   7150   8334    346    -12   -347       O  
ATOM   2191  N   THR A 281     -41.142  43.317  47.626  1.00 48.75           N  
ANISOU 2191  N   THR A 281     4369   6273   7879    218   -202   -200       N  
ATOM   2192  CA  THR A 281     -40.581  42.189  48.418  1.00 47.63           C  
ANISOU 2192  CA  THR A 281     4265   6120   7711    104   -186   -140       C  
ATOM   2193  C   THR A 281     -39.975  41.180  47.431  1.00 45.67           C  
ANISOU 2193  C   THR A 281     3979   5824   7548     26   -204    -67       C  
ATOM   2194  O   THR A 281     -39.917  41.508  46.230  1.00 44.68           O  
ANISOU 2194  O   THR A 281     3809   5670   7495     64   -229    -65       O  
ATOM   2195  CB  THR A 281     -41.666  41.568  49.306  1.00 48.51           C  
ANISOU 2195  CB  THR A 281     4335   6369   7726     69    -92   -167       C  
ATOM   2196  OG1 THR A 281     -41.064  40.632  50.193  1.00 48.75           O  
ANISOU 2196  OG1 THR A 281     4434   6370   7719    -36    -93   -112       O  
ATOM   2197  CG2 THR A 281     -42.740  40.849  48.525  1.00 48.53           C  
ANISOU 2197  CG2 THR A 281     4208   6486   7745     39    -25   -169       C  
ATOM   2198  N   LEU A 282     -39.550  40.005  47.902  1.00 45.04           N  
ANISOU 2198  N   LEU A 282     3924   5732   7454    -73   -196    -12       N  
ATOM   2199  CA  LEU A 282     -38.986  38.930  47.038  1.00 44.24           C  
ANISOU 2199  CA  LEU A 282     3800   5586   7423   -139   -215     51       C  
ATOM   2200  C   LEU A 282     -40.105  38.018  46.524  1.00 43.68           C  
ANISOU 2200  C   LEU A 282     3643   5612   7339   -184   -151     50       C  
ATOM   2201  O   LEU A 282     -40.911  37.528  47.348  1.00 44.45           O  
ANISOU 2201  O   LEU A 282     3731   5799   7358   -237    -95     39       O  
ATOM   2202  CB  LEU A 282     -37.969  38.103  47.828  1.00 44.91           C  
ANISOU 2202  CB  LEU A 282     3968   5600   7495   -215   -255    108       C  
ATOM   2203  CG  LEU A 282     -36.671  38.818  48.196  1.00 45.13           C  
ANISOU 2203  CG  LEU A 282     4073   5522   7553   -188   -335    128       C  
ATOM   2204  CD1 LEU A 282     -35.784  37.913  49.025  1.00 45.27           C  
ANISOU 2204  CD1 LEU A 282     4166   5480   7554   -263   -375    181       C  
ATOM   2205  CD2 LEU A 282     -35.907  39.267  46.961  1.00 44.50           C  
ANISOU 2205  CD2 LEU A 282     3958   5380   7570   -146   -382    151       C  
ATOM   2206  N   TYR A 283     -40.126  37.783  45.212  1.00 42.25           N  
ANISOU 2206  N   TYR A 283     3407   5414   7229   -173   -162     65       N  
ATOM   2207  CA  TYR A 283     -41.041  36.837  44.523  1.00 41.82           C  
ANISOU 2207  CA  TYR A 283     3281   5429   7177   -225   -123     75       C  
ATOM   2208  C   TYR A 283     -40.211  35.705  43.914  1.00 40.53           C  
ANISOU 2208  C   TYR A 283     3154   5183   7060   -282   -164    139       C  
ATOM   2209  O   TYR A 283     -39.218  36.017  43.218  1.00 39.55           O  
ANISOU 2209  O   TYR A 283     3050   4973   7002   -236   -211    157       O  
ATOM   2210  CB  TYR A 283     -41.829  37.543  43.414  1.00 41.69           C  
ANISOU 2210  CB  TYR A 283     3179   5457   7202   -150   -110     33       C  
ATOM   2211  CG  TYR A 283     -42.877  38.522  43.882  1.00 42.23           C  
ANISOU 2211  CG  TYR A 283     3196   5626   7223    -82    -67    -38       C  
ATOM   2212  CD1 TYR A 283     -42.535  39.799  44.300  1.00 42.17           C  
ANISOU 2212  CD1 TYR A 283     3232   5582   7206      9    -94    -80       C  
ATOM   2213  CD2 TYR A 283     -44.217  38.180  43.880  1.00 42.92           C  
ANISOU 2213  CD2 TYR A 283     3189   5846   7272   -104     -6    -63       C  
ATOM   2214  CE1 TYR A 283     -43.495  40.702  44.720  1.00 43.16           C  
ANISOU 2214  CE1 TYR A 283     3319   5796   7282     92    -60   -154       C  
ATOM   2215  CE2 TYR A 283     -45.185  39.071  44.301  1.00 43.86           C  
ANISOU 2215  CE2 TYR A 283     3248   6071   7345    -25     35   -134       C  
ATOM   2216  CZ  TYR A 283     -44.826  40.336  44.723  1.00 43.96           C  
ANISOU 2216  CZ  TYR A 283     3314   6040   7346     81      8   -184       C  
ATOM   2217  OH  TYR A 283     -45.793  41.202  45.131  1.00 45.29           O  
ANISOU 2217  OH  TYR A 283     3432   6312   7464    175     45   -263       O  
ATOM   2218  N   CYS A 284     -40.612  34.455  44.164  1.00 40.18           N  
ANISOU 2218  N   CYS A 284     3121   5168   6976   -378   -149    171       N  
ATOM   2219  CA  CYS A 284     -40.057  33.246  43.507  1.00 40.00           C  
ANISOU 2219  CA  CYS A 284     3138   5074   6985   -428   -191    224       C  
ATOM   2220  C   CYS A 284     -41.032  32.776  42.431  1.00 39.89           C  
ANISOU 2220  C   CYS A 284     3058   5110   6987   -447   -172    222       C  
ATOM   2221  O   CYS A 284     -42.132  32.318  42.782  1.00 41.16           O  
ANISOU 2221  O   CYS A 284     3182   5362   7092   -521   -134    220       O  
ATOM   2222  CB  CYS A 284     -39.793  32.126  44.511  1.00 40.79           C  
ANISOU 2222  CB  CYS A 284     3322   5149   7025   -527   -210    266       C  
ATOM   2223  SG  CYS A 284     -39.071  30.641  43.752  1.00 40.54           S  
ANISOU 2223  SG  CYS A 284     3361   5016   7025   -568   -277    323       S  
ATOM   2224  N   ILE A 285     -40.661  32.925  41.166  1.00 39.39           N  
ANISOU 2224  N   ILE A 285     2978   4995   6993   -388   -198    224       N  
ATOM   2225  CA  ILE A 285     -41.479  32.479  40.004  1.00 39.84           C  
ANISOU 2225  CA  ILE A 285     2986   5079   7071   -400   -194    224       C  
ATOM   2226  C   ILE A 285     -40.984  31.088  39.595  1.00 40.87           C  
ANISOU 2226  C   ILE A 285     3192   5134   7202   -456   -241    274       C  
ATOM   2227  O   ILE A 285     -39.832  30.975  39.108  1.00 40.34           O  
ANISOU 2227  O   ILE A 285     3173   4975   7176   -404   -279    291       O  
ATOM   2228  CB  ILE A 285     -41.410  33.498  38.849  1.00 38.94           C  
ANISOU 2228  CB  ILE A 285     2823   4950   7021   -300   -198    193       C  
ATOM   2229  CG1 ILE A 285     -41.869  34.886  39.302  1.00 38.86           C  
ANISOU 2229  CG1 ILE A 285     2759   5000   7004   -236   -169    140       C  
ATOM   2230  CG2 ILE A 285     -42.193  33.007  37.643  1.00 39.04           C  
ANISOU 2230  CG2 ILE A 285     2799   4980   7054   -314   -204    196       C  
ATOM   2231  CD1 ILE A 285     -41.807  35.940  38.210  1.00 38.37           C  
ANISOU 2231  CD1 ILE A 285     2665   4913   6998   -143   -185    111       C  
ATOM   2232  N   ASP A 286     -41.843  30.083  39.789  1.00 42.78           N  
ANISOU 2232  N   ASP A 286     3443   5416   7393   -558   -240    296       N  
ATOM   2233  CA  ASP A 286     -41.614  28.659  39.430  1.00 43.59           C  
ANISOU 2233  CA  ASP A 286     3634   5447   7481   -624   -296    343       C  
ATOM   2234  C   ASP A 286     -42.601  28.281  38.322  1.00 43.16           C  
ANISOU 2234  C   ASP A 286     3539   5422   7436   -652   -302    344       C  
ATOM   2235  O   ASP A 286     -43.567  27.544  38.612  1.00 42.83           O  
ANISOU 2235  O   ASP A 286     3494   5437   7343   -765   -303    368       O  
ATOM   2236  CB  ASP A 286     -41.765  27.768  40.664  1.00 45.45           C  
ANISOU 2236  CB  ASP A 286     3937   5691   7638   -742   -307    378       C  
ATOM   2237  CG  ASP A 286     -41.438  26.308  40.399  1.00 46.88           C  
ANISOU 2237  CG  ASP A 286     4236   5779   7797   -806   -383    425       C  
ATOM   2238  OD1 ASP A 286     -41.166  25.974  39.233  1.00 47.57           O  
ANISOU 2238  OD1 ASP A 286     4345   5802   7926   -755   -420    427       O  
ATOM   2239  OD2 ASP A 286     -41.438  25.516  41.363  1.00 48.77           O  
ANISOU 2239  OD2 ASP A 286     4554   6004   7971   -904   -409    459       O  
ATOM   2240  N   GLY A 287     -42.371  28.794  37.108  1.00 42.63           N  
ANISOU 2240  N   GLY A 287     3444   5323   7431   -559   -309    323       N  
ATOM   2241  CA  GLY A 287     -43.251  28.590  35.944  1.00 43.37           C  
ANISOU 2241  CA  GLY A 287     3501   5436   7541   -568   -321    320       C  
ATOM   2242  C   GLY A 287     -44.554  29.340  36.135  1.00 44.52           C  
ANISOU 2242  C   GLY A 287     3524   5711   7678   -588   -271    289       C  
ATOM   2243  O   GLY A 287     -44.525  30.589  36.054  1.00 45.24           O  
ANISOU 2243  O   GLY A 287     3550   5835   7804   -497   -237    245       O  
ATOM   2244  N   ALA A 288     -45.649  28.627  36.418  1.00 45.31           N  
ANISOU 2244  N   ALA A 288     3597   5887   7731   -704   -270    311       N  
ATOM   2245  CA  ALA A 288     -46.994  29.215  36.626  1.00 45.89           C  
ANISOU 2245  CA  ALA A 288     3536   6109   7791   -729   -220    283       C  
ATOM   2246  C   ALA A 288     -47.214  29.511  38.112  1.00 46.35           C  
ANISOU 2246  C   ALA A 288     3556   6261   7790   -768   -161    274       C  
ATOM   2247  O   ALA A 288     -48.196  30.190  38.405  1.00 48.10           O  
ANISOU 2247  O   ALA A 288     3660   6616   7998   -758   -108    239       O  
ATOM   2248  CB  ALA A 288     -48.070  28.294  36.093  1.00 46.38           C  
ANISOU 2248  CB  ALA A 288     3574   6215   7832   -841   -252    318       C  
ATOM   2249  N   LEU A 289     -46.347  29.013  39.000  1.00 45.63           N  
ANISOU 2249  N   LEU A 289     3566   6108   7664   -806   -172    302       N  
ATOM   2250  CA  LEU A 289     -46.517  29.139  40.468  1.00 46.12           C  
ANISOU 2250  CA  LEU A 289     3616   6249   7655   -860   -121    301       C  
ATOM   2251  C   LEU A 289     -45.709  30.335  40.951  1.00 45.50           C  
ANISOU 2251  C   LEU A 289     3542   6144   7601   -737    -95    255       C  
ATOM   2252  O   LEU A 289     -44.757  30.701  40.251  1.00 45.69           O  
ANISOU 2252  O   LEU A 289     3608   6062   7689   -644   -131    247       O  
ATOM   2253  CB  LEU A 289     -46.065  27.844  41.145  1.00 46.47           C  
ANISOU 2253  CB  LEU A 289     3785   6229   7642   -983   -164    363       C  
ATOM   2254  CG  LEU A 289     -46.598  26.556  40.512  1.00 46.72           C  
ANISOU 2254  CG  LEU A 289     3860   6237   7654  -1102   -221    417       C  
ATOM   2255  CD1 LEU A 289     -46.251  25.343  41.360  1.00 47.11           C  
ANISOU 2255  CD1 LEU A 289     4041   6229   7630  -1231   -268    477       C  
ATOM   2256  CD2 LEU A 289     -48.101  26.630  40.295  1.00 47.53           C  
ANISOU 2256  CD2 LEU A 289     3828   6493   7735  -1174   -182    415       C  
ATOM   2257  N   LEU A 290     -46.084  30.896  42.104  1.00 45.72           N  
ANISOU 2257  N   LEU A 290     3529   6267   7572   -741    -36    228       N  
ATOM   2258  CA  LEU A 290     -45.592  32.195  42.621  1.00 45.47           C  
ANISOU 2258  CA  LEU A 290     3491   6233   7553   -623    -11    175       C  
ATOM   2259  C   LEU A 290     -45.564  32.152  44.144  1.00 46.43           C  
ANISOU 2259  C   LEU A 290     3649   6403   7587   -676     27    178       C  
ATOM   2260  O   LEU A 290     -46.606  31.876  44.733  1.00 47.07           O  
ANISOU 2260  O   LEU A 290     3668   6618   7598   -754     81    178       O  
ATOM   2261  CB  LEU A 290     -46.539  33.304  42.159  1.00 46.12           C  
ANISOU 2261  CB  LEU A 290     3449   6416   7656   -530     28    111       C  
ATOM   2262  CG  LEU A 290     -46.150  34.725  42.575  1.00 46.17           C  
ANISOU 2262  CG  LEU A 290     3457   6412   7671   -399     41     51       C  
ATOM   2263  CD1 LEU A 290     -44.869  35.157  41.864  1.00 45.11           C  
ANISOU 2263  CD1 LEU A 290     3399   6125   7612   -324    -21     59       C  
ATOM   2264  CD2 LEU A 290     -47.290  35.696  42.290  1.00 46.57           C  
ANISOU 2264  CD2 LEU A 290     3387   6583   7724   -313     80    -16       C  
ATOM   2265  N   THR A 291     -44.424  32.482  44.746  1.00 46.69           N  
ANISOU 2265  N   THR A 291     3775   6340   7624   -634      0    179       N  
ATOM   2266  CA  THR A 291     -44.247  32.569  46.217  1.00 47.81           C  
ANISOU 2266  CA  THR A 291     3972   6507   7683   -670     26    177       C  
ATOM   2267  C   THR A 291     -43.762  33.979  46.565  1.00 47.39           C  
ANISOU 2267  C   THR A 291     3926   6432   7646   -541     30    121       C  
ATOM   2268  O   THR A 291     -43.338  34.687  45.637  1.00 47.09           O  
ANISOU 2268  O   THR A 291     3870   6331   7688   -444     -2    101       O  
ATOM   2269  CB  THR A 291     -43.348  31.409  46.658  1.00 48.41           C  
ANISOU 2269  CB  THR A 291     4175   6477   7740   -766    -31    243       C  
ATOM   2270  OG1 THR A 291     -44.242  30.293  46.624  1.00 49.35           O  
ANISOU 2270  OG1 THR A 291     4276   6666   7809   -898    -17    283       O  
ATOM   2271  CG2 THR A 291     -42.704  31.562  48.023  1.00 49.18           C  
ANISOU 2271  CG2 THR A 291     4365   6544   7777   -782    -35    247       C  
ATOM   2272  N   LYS A 292     -43.859  34.363  47.842  1.00 48.00           N  
ANISOU 2272  N   LYS A 292     4036   6558   7643   -545     66     99       N  
ATOM   2273  CA  LYS A 292     -43.318  35.627  48.402  1.00 48.44           C  
ANISOU 2273  CA  LYS A 292     4133   6575   7695   -435     56     51       C  
ATOM   2274  C   LYS A 292     -42.664  35.365  49.761  1.00 50.02           C  
ANISOU 2274  C   LYS A 292     4448   6733   7822   -491     43     74       C  
ATOM   2275  O   LYS A 292     -43.256  34.592  50.553  1.00 50.25           O  
ANISOU 2275  O   LYS A 292     4485   6844   7763   -595     89     95       O  
ATOM   2276  CB  LYS A 292     -44.433  36.644  48.641  1.00 48.96           C  
ANISOU 2276  CB  LYS A 292     4111   6776   7715   -349    124    -25       C  
ATOM   2277  CG  LYS A 292     -45.194  37.088  47.405  1.00 48.94           C  
ANISOU 2277  CG  LYS A 292     3992   6825   7775   -278    134    -60       C  
ATOM   2278  CD  LYS A 292     -46.063  38.314  47.653  1.00 49.91           C  
ANISOU 2278  CD  LYS A 292     4047   7054   7862   -154    179   -148       C  
ATOM   2279  CE  LYS A 292     -46.817  38.273  48.969  1.00 51.43           C  
ANISOU 2279  CE  LYS A 292     4220   7387   7933   -180    261   -177       C  
ATOM   2280  NZ  LYS A 292     -48.058  39.090  48.937  1.00 52.34           N  
ANISOU 2280  NZ  LYS A 292     4214   7657   8012    -74    324   -259       N  
ATOM   2281  N   SER A 293     -41.527  36.022  50.031  1.00 50.80           N  
ANISOU 2281  N   SER A 293     4634   6714   7952   -430    -18     72       N  
ATOM   2282  CA  SER A 293     -40.869  36.092  51.365  1.00 52.39           C  
ANISOU 2282  CA  SER A 293     4951   6866   8085   -456    -41     82       C  
ATOM   2283  C   SER A 293     -40.164  37.444  51.527  1.00 52.84           C  
ANISOU 2283  C   SER A 293     5057   6849   8170   -343    -89     43       C  
ATOM   2284  O   SER A 293     -39.906  38.089  50.504  1.00 51.74           O  
ANISOU 2284  O   SER A 293     4874   6666   8116   -267   -122     30       O  
ATOM   2285  CB  SER A 293     -39.902  34.944  51.567  1.00 53.01           C  
ANISOU 2285  CB  SER A 293     5119   6842   8180   -552   -105    155       C  
ATOM   2286  OG  SER A 293     -38.912  34.898  50.535  1.00 52.98           O  
ANISOU 2286  OG  SER A 293     5113   6727   8287   -512   -176    184       O  
ATOM   2287  N   SER A 294     -39.878  37.860  52.764  1.00 54.85           N  
ANISOU 2287  N   SER A 294     5406   7085   8348   -339    -99     28       N  
ATOM   2288  CA  SER A 294     -39.104  39.094  53.064  1.00 56.18           C  
ANISOU 2288  CA  SER A 294     5651   7162   8532   -248   -164      1       C  
ATOM   2289  C   SER A 294     -37.616  38.866  52.753  1.00 57.28           C  
ANISOU 2289  C   SER A 294     5849   7153   8759   -275   -267     65       C  
ATOM   2290  O   SER A 294     -36.926  39.859  52.447  1.00 57.17           O  
ANISOU 2290  O   SER A 294     5861   7062   8799   -206   -332     57       O  
ATOM   2291  CB  SER A 294     -39.329  39.576  54.472  1.00 57.00           C  
ANISOU 2291  CB  SER A 294     5843   7294   8517   -234   -144    -37       C  
ATOM   2292  OG  SER A 294     -38.752  38.693  55.417  1.00 57.82           O  
ANISOU 2292  OG  SER A 294     6042   7352   8572   -338   -168     15       O  
ATOM   2293  N   GLU A 295     -37.142  37.613  52.835  1.00 59.31           N  
ANISOU 2293  N   GLU A 295     6129   7376   9029   -371   -287    127       N  
ATOM   2294  CA  GLU A 295     -35.772  37.187  52.415  1.00 60.09           C  
ANISOU 2294  CA  GLU A 295     6260   7354   9216   -391   -378    189       C  
ATOM   2295  C   GLU A 295     -35.817  35.759  51.857  1.00 58.83           C  
ANISOU 2295  C   GLU A 295     6069   7199   9083   -465   -369    235       C  
ATOM   2296  O   GLU A 295     -36.821  35.081  52.082  1.00 57.22           O  
ANISOU 2296  O   GLU A 295     5847   7080   8814   -524   -305    229       O  
ATOM   2297  CB  GLU A 295     -34.758  37.292  53.552  1.00 62.60           C  
ANISOU 2297  CB  GLU A 295     6699   7581   9505   -417   -454    215       C  
ATOM   2298  CG  GLU A 295     -35.260  36.729  54.866  1.00 65.68           C  
ANISOU 2298  CG  GLU A 295     7170   8008   9774   -488   -421    211       C  
ATOM   2299  CD  GLU A 295     -34.553  37.279  56.100  1.00 68.31           C  
ANISOU 2299  CD  GLU A 295     7631   8267  10054   -488   -485    212       C  
ATOM   2300  OE1 GLU A 295     -33.288  37.332  56.097  1.00 69.60           O  
ANISOU 2300  OE1 GLU A 295     7839   8319  10284   -488   -585    254       O  
ATOM   2301  OE2 GLU A 295     -35.261  37.645  57.079  1.00 70.12           O  
ANISOU 2301  OE2 GLU A 295     7914   8555  10172   -487   -435    170       O  
ATOM   2302  N   TYR A 296     -34.775  35.345  51.125  1.00 58.89           N  
ANISOU 2302  N   TYR A 296     6070   7123   9179   -458   -434    279       N  
ATOM   2303  CA  TYR A 296     -34.708  34.070  50.357  1.00 59.06           C  
ANISOU 2303  CA  TYR A 296     6068   7134   9238   -500   -440    317       C  
ATOM   2304  C   TYR A 296     -33.324  33.422  50.491  1.00 59.59           C  
ANISOU 2304  C   TYR A 296     6196   7095   9351   -511   -532    369       C  
ATOM   2305  O   TYR A 296     -32.312  34.132  50.358  1.00 59.28           O  
ANISOU 2305  O   TYR A 296     6151   6999   9371   -458   -586    379       O  
ATOM   2306  CB  TYR A 296     -34.982  34.289  48.868  1.00 58.61           C  
ANISOU 2306  CB  TYR A 296     5907   7103   9256   -444   -414    305       C  
ATOM   2307  CG  TYR A 296     -35.148  33.014  48.087  1.00 58.88           C  
ANISOU 2307  CG  TYR A 296     5926   7135   9311   -483   -413    334       C  
ATOM   2308  CD1 TYR A 296     -36.397  32.433  47.943  1.00 60.28           C  
ANISOU 2308  CD1 TYR A 296     6072   7391   9438   -539   -354    324       C  
ATOM   2309  CD2 TYR A 296     -34.054  32.361  47.534  1.00 58.72           C  
ANISOU 2309  CD2 TYR A 296     5924   7033   9352   -466   -477    374       C  
ATOM   2310  CE1 TYR A 296     -36.564  31.253  47.240  1.00 61.31           C  
ANISOU 2310  CE1 TYR A 296     6207   7508   9581   -582   -367    353       C  
ATOM   2311  CE2 TYR A 296     -34.199  31.175  46.831  1.00 58.88           C  
ANISOU 2311  CE2 TYR A 296     5949   7039   9382   -493   -485    396       C  
ATOM   2312  CZ  TYR A 296     -35.460  30.618  46.694  1.00 60.95           C  
ANISOU 2312  CZ  TYR A 296     6197   7368   9593   -555   -435    387       C  
ATOM   2313  OH  TYR A 296     -35.653  29.453  46.015  1.00 62.41           O  
ANISOU 2313  OH  TYR A 296     6401   7530   9778   -589   -455    410       O  
ATOM   2314  N   LYS A 297     -33.309  32.097  50.685  1.00 59.48           N  
ANISOU 2314  N   LYS A 297     6234   7055   9307   -578   -554    402       N  
ATOM   2315  CA  LYS A 297     -32.103  31.239  50.810  1.00 59.24           C  
ANISOU 2315  CA  LYS A 297     6268   6927   9311   -585   -646    448       C  
ATOM   2316  C   LYS A 297     -32.283  29.983  49.951  1.00 56.91           C  
ANISOU 2316  C   LYS A 297     5969   6621   9033   -603   -654    468       C  
ATOM   2317  O   LYS A 297     -33.329  29.329  50.074  1.00 58.95           O  
ANISOU 2317  O   LYS A 297     6248   6925   9225   -677   -613    466       O  
ATOM   2318  CB  LYS A 297     -31.905  30.850  52.276  1.00 62.20           C  
ANISOU 2318  CB  LYS A 297     6765   7262   9606   -656   -690    466       C  
ATOM   2319  CG  LYS A 297     -30.678  29.993  52.558  1.00 64.55           C  
ANISOU 2319  CG  LYS A 297     7139   7454   9932   -659   -797    509       C  
ATOM   2320  CD  LYS A 297     -30.157  30.159  53.970  1.00 67.19           C  
ANISOU 2320  CD  LYS A 297     7582   7735  10213   -699   -857    522       C  
ATOM   2321  CE  LYS A 297     -28.666  29.918  54.084  1.00 68.31           C  
ANISOU 2321  CE  LYS A 297     7753   7778  10421   -657   -972    557       C  
ATOM   2322  NZ  LYS A 297     -27.892  30.916  53.311  1.00 69.29           N  
ANISOU 2322  NZ  LYS A 297     7770   7909  10647   -569   -981    554       N  
ATOM   2323  N   GLY A 298     -31.304  29.651  49.115  1.00 53.97           N  
ANISOU 2323  N   GLY A 298     5572   6193   8740   -539   -705    486       N  
ATOM   2324  CA  GLY A 298     -31.343  28.435  48.280  1.00 52.08           C  
ANISOU 2324  CA  GLY A 298     5347   5926   8513   -538   -727    502       C  
ATOM   2325  C   GLY A 298     -30.174  28.367  47.299  1.00 50.47           C  
ANISOU 2325  C   GLY A 298     5094   5681   8401   -438   -770    512       C  
ATOM   2326  O   GLY A 298     -29.324  29.260  47.242  1.00 48.71           O  
ANISOU 2326  O   GLY A 298     4815   5455   8235   -380   -783    514       O  
ATOM   2327  N   PRO A 299     -30.092  27.286  46.500  1.00 48.91           N  
ANISOU 2327  N   PRO A 299     4918   5450   8214   -415   -797    521       N  
ATOM   2328  CA  PRO A 299     -29.011  27.130  45.529  1.00 48.12           C  
ANISOU 2328  CA  PRO A 299     4769   5323   8189   -310   -830    526       C  
ATOM   2329  C   PRO A 299     -29.156  28.070  44.320  1.00 46.36           C  
ANISOU 2329  C   PRO A 299     4425   5165   8024   -249   -759    508       C  
ATOM   2330  O   PRO A 299     -29.897  27.744  43.407  1.00 45.20           O  
ANISOU 2330  O   PRO A 299     4262   5040   7871   -246   -721    494       O  
ATOM   2331  CB  PRO A 299     -29.128  25.649  45.141  1.00 48.64           C  
ANISOU 2331  CB  PRO A 299     4923   5333   8225   -311   -879    533       C  
ATOM   2332  CG  PRO A 299     -30.593  25.336  45.324  1.00 48.94           C  
ANISOU 2332  CG  PRO A 299     5003   5401   8189   -418   -835    528       C  
ATOM   2333  CD  PRO A 299     -31.013  26.145  46.525  1.00 49.13           C  
ANISOU 2333  CD  PRO A 299     5026   5465   8173   -492   -802    527       C  
ATOM   2334  N   ILE A 300     -28.432  29.194  44.347  1.00 45.43           N  
ANISOU 2334  N   ILE A 300     4234   5069   7958   -209   -754    512       N  
ATOM   2335  CA  ILE A 300     -28.425  30.224  43.262  1.00 44.41           C  
ANISOU 2335  CA  ILE A 300     3997   4993   7881   -158   -699    501       C  
ATOM   2336  C   ILE A 300     -27.200  29.980  42.383  1.00 43.33           C  
ANISOU 2336  C   ILE A 300     3805   4850   7806    -71   -725    520       C  
ATOM   2337  O   ILE A 300     -26.145  29.645  42.954  1.00 44.03           O  
ANISOU 2337  O   ILE A 300     3910   4905   7913    -49   -790    543       O  
ATOM   2338  CB  ILE A 300     -28.414  31.661  43.825  1.00 44.71           C  
ANISOU 2338  CB  ILE A 300     4000   5058   7929   -178   -685    497       C  
ATOM   2339  CG1 ILE A 300     -29.341  31.816  45.037  1.00 45.14           C  
ANISOU 2339  CG1 ILE A 300     4122   5115   7912   -253   -672    479       C  
ATOM   2340  CG2 ILE A 300     -28.739  32.666  42.721  1.00 44.49           C  
ANISOU 2340  CG2 ILE A 300     3886   5079   7937   -143   -630    482       C  
ATOM   2341  CD1 ILE A 300     -30.776  31.412  44.763  1.00 45.16           C  
ANISOU 2341  CD1 ILE A 300     4133   5160   7864   -292   -611    451       C  
ATOM   2342  N   THR A 301     -27.344  30.162  41.067  1.00 41.56           N  
ANISOU 2342  N   THR A 301     3516   4663   7609    -22   -677    510       N  
ATOM   2343  CA  THR A 301     -26.265  29.974  40.060  1.00 40.67           C  
ANISOU 2343  CA  THR A 301     3339   4567   7547     66   -683    524       C  
ATOM   2344  C   THR A 301     -26.090  31.221  39.178  1.00 39.59           C  
ANISOU 2344  C   THR A 301     3101   4488   7451     85   -633    530       C  
ATOM   2345  O   THR A 301     -25.014  31.348  38.576  1.00 39.95           O  
ANISOU 2345  O   THR A 301     3075   4564   7538    143   -637    553       O  
ATOM   2346  CB  THR A 301     -26.520  28.730  39.201  1.00 40.52           C  
ANISOU 2346  CB  THR A 301     3363   4525   7506    116   -681    508       C  
ATOM   2347  OG1 THR A 301     -25.336  28.490  38.446  1.00 40.77           O  
ANISOU 2347  OG1 THR A 301     3337   4576   7577    213   -692    519       O  
ATOM   2348  CG2 THR A 301     -27.692  28.879  38.258  1.00 40.19           C  
ANISOU 2348  CG2 THR A 301     3316   4506   7445     99   -620    484       C  
ATOM   2349  N   ASP A 302     -27.103  32.083  39.051  1.00 37.96           N  
ANISOU 2349  N   ASP A 302     2889   4303   7231     41   -589    511       N  
ATOM   2350  CA  ASP A 302     -26.989  33.383  38.335  1.00 37.12           C  
ANISOU 2350  CA  ASP A 302     2708   4238   7157     48   -557    518       C  
ATOM   2351  C   ASP A 302     -27.596  34.485  39.201  1.00 36.46           C  
ANISOU 2351  C   ASP A 302     2645   4151   7057     -9   -561    506       C  
ATOM   2352  O   ASP A 302     -28.540  34.200  39.920  1.00 36.87           O  
ANISOU 2352  O   ASP A 302     2753   4189   7064    -46   -554    479       O  
ATOM   2353  CB  ASP A 302     -27.656  33.353  36.961  1.00 36.75           C  
ANISOU 2353  CB  ASP A 302     2637   4217   7107     78   -503    498       C  
ATOM   2354  CG  ASP A 302     -27.099  32.281  36.039  1.00 37.34           C  
ANISOU 2354  CG  ASP A 302     2705   4295   7188    147   -497    503       C  
ATOM   2355  OD1 ASP A 302     -25.870  32.274  35.811  1.00 38.18           O  
ANISOU 2355  OD1 ASP A 302     2757   4423   7325    193   -510    531       O  
ATOM   2356  OD2 ASP A 302     -27.892  31.456  35.553  1.00 37.77           O  
ANISOU 2356  OD2 ASP A 302     2807   4331   7212    157   -482    478       O  
ATOM   2357  N   VAL A 303     -27.031  35.685  39.155  1.00 36.26           N  
ANISOU 2357  N   VAL A 303     2579   4138   7061    -17   -576    527       N  
ATOM   2358  CA  VAL A 303     -27.601  36.909  39.777  1.00 36.00           C  
ANISOU 2358  CA  VAL A 303     2573   4096   7010    -55   -586    511       C  
ATOM   2359  C   VAL A 303     -27.314  38.071  38.823  1.00 36.14           C  
ANISOU 2359  C   VAL A 303     2539   4134   7057    -47   -582    527       C  
ATOM   2360  O   VAL A 303     -26.162  38.206  38.386  1.00 35.88           O  
ANISOU 2360  O   VAL A 303     2452   4118   7062    -41   -602    574       O  
ATOM   2361  CB  VAL A 303     -27.049  37.169  41.192  1.00 36.31           C  
ANISOU 2361  CB  VAL A 303     2656   4099   7037    -92   -646    527       C  
ATOM   2362  CG1 VAL A 303     -27.758  38.333  41.862  1.00 36.34           C  
ANISOU 2362  CG1 VAL A 303     2708   4090   7008   -117   -655    499       C  
ATOM   2363  CG2 VAL A 303     -27.139  35.930  42.070  1.00 36.27           C  
ANISOU 2363  CG2 VAL A 303     2707   4070   7002   -104   -659    521       C  
ATOM   2364  N   PHE A 304     -28.357  38.830  38.474  1.00 36.25           N  
ANISOU 2364  N   PHE A 304     2569   4152   7051    -45   -558    490       N  
ATOM   2365  CA  PHE A 304     -28.294  40.030  37.605  1.00 36.69           C  
ANISOU 2365  CA  PHE A 304     2602   4214   7124    -44   -564    500       C  
ATOM   2366  C   PHE A 304     -28.345  41.268  38.505  1.00 37.57           C  
ANISOU 2366  C   PHE A 304     2766   4289   7218    -72   -620    494       C  
ATOM   2367  O   PHE A 304     -29.104  41.268  39.488  1.00 37.47           O  
ANISOU 2367  O   PHE A 304     2806   4262   7166    -72   -621    453       O  
ATOM   2368  CB  PHE A 304     -29.402  39.977  36.553  1.00 36.29           C  
ANISOU 2368  CB  PHE A 304     2543   4182   7061    -13   -514    461       C  
ATOM   2369  CG  PHE A 304     -29.308  38.786  35.632  1.00 36.14           C  
ANISOU 2369  CG  PHE A 304     2490   4188   7053     14   -470    467       C  
ATOM   2370  CD1 PHE A 304     -28.835  38.918  34.338  1.00 36.05           C  
ANISOU 2370  CD1 PHE A 304     2436   4198   7061     34   -450    492       C  
ATOM   2371  CD2 PHE A 304     -29.668  37.520  36.067  1.00 36.14           C  
ANISOU 2371  CD2 PHE A 304     2511   4186   7034     20   -453    450       C  
ATOM   2372  CE1 PHE A 304     -28.743  37.818  33.497  1.00 36.01           C  
ANISOU 2372  CE1 PHE A 304     2412   4211   7057     72   -413    493       C  
ATOM   2373  CE2 PHE A 304     -29.560  36.417  35.232  1.00 36.13           C  
ANISOU 2373  CE2 PHE A 304     2496   4194   7036     51   -426    454       C  
ATOM   2374  CZ  PHE A 304     -29.105  36.569  33.944  1.00 36.05           C  
ANISOU 2374  CZ  PHE A 304     2447   4205   7045     84   -405    472       C  
ATOM   2375  N   TYR A 305     -27.496  42.257  38.216  1.00 38.98           N  
ANISOU 2375  N   TYR A 305     2934   4455   7419    -99   -668    539       N  
ATOM   2376  CA  TYR A 305     -27.375  43.534  38.965  1.00 39.93           C  
ANISOU 2376  CA  TYR A 305     3119   4527   7523   -129   -741    543       C  
ATOM   2377  C   TYR A 305     -27.484  44.698  37.982  1.00 41.65           C  
ANISOU 2377  C   TYR A 305     3344   4733   7744   -136   -764    552       C  
ATOM   2378  O   TYR A 305     -26.914  44.577  36.880  1.00 41.26           O  
ANISOU 2378  O   TYR A 305     3232   4718   7724   -148   -742    594       O  
ATOM   2379  CB  TYR A 305     -26.036  43.615  39.698  1.00 39.30           C  
ANISOU 2379  CB  TYR A 305     3033   4431   7467   -179   -806    605       C  
ATOM   2380  CG  TYR A 305     -25.812  42.543  40.728  1.00 38.43           C  
ANISOU 2380  CG  TYR A 305     2930   4319   7352   -176   -803    601       C  
ATOM   2381  CD1 TYR A 305     -26.092  42.778  42.064  1.00 38.30           C  
ANISOU 2381  CD1 TYR A 305     2997   4257   7296   -189   -844    577       C  
ATOM   2382  CD2 TYR A 305     -25.304  41.304  40.374  1.00 37.81           C  
ANISOU 2382  CD2 TYR A 305     2785   4278   7301   -157   -766    621       C  
ATOM   2383  CE1 TYR A 305     -25.876  41.803  43.024  1.00 38.51           C  
ANISOU 2383  CE1 TYR A 305     3044   4276   7313   -195   -848    577       C  
ATOM   2384  CE2 TYR A 305     -25.080  40.320  41.322  1.00 37.89           C  
ANISOU 2384  CE2 TYR A 305     2817   4275   7303   -156   -778    619       C  
ATOM   2385  CZ  TYR A 305     -25.367  40.570  42.653  1.00 38.24           C  
ANISOU 2385  CZ  TYR A 305     2946   4273   7309   -181   -819    599       C  
ATOM   2386  OH  TYR A 305     -25.158  39.614  43.603  1.00 38.47           O  
ANISOU 2386  OH  TYR A 305     3009   4284   7324   -187   -836    600       O  
ATOM   2387  N   LYS A 306     -28.195  45.760  38.372  1.00 44.33           N  
ANISOU 2387  N   LYS A 306     3765   5027   8049   -125   -808    511       N  
ATOM   2388  CA  LYS A 306     -28.284  47.028  37.596  1.00 46.34           C  
ANISOU 2388  CA  LYS A 306     4059   5248   8298   -135   -857    519       C  
ATOM   2389  C   LYS A 306     -26.958  47.792  37.731  1.00 48.58           C  
ANISOU 2389  C   LYS A 306     4355   5502   8599   -215   -942    601       C  
ATOM   2390  O   LYS A 306     -26.380  47.791  38.836  1.00 49.34           O  
ANISOU 2390  O   LYS A 306     4479   5573   8694   -244   -990    620       O  
ATOM   2391  CB  LYS A 306     -29.486  47.860  38.057  1.00 46.47           C  
ANISOU 2391  CB  LYS A 306     4166   5222   8267    -81   -885    442       C  
ATOM   2392  CG  LYS A 306     -30.746  47.678  37.215  1.00 46.59           C  
ANISOU 2392  CG  LYS A 306     4158   5268   8273    -16   -826    380       C  
ATOM   2393  CD  LYS A 306     -31.647  48.904  37.145  1.00 47.23           C  
ANISOU 2393  CD  LYS A 306     4323   5303   8318     35   -880    322       C  
ATOM   2394  CE  LYS A 306     -31.070  50.033  36.312  1.00 47.64           C  
ANISOU 2394  CE  LYS A 306     4425   5298   8377     -4   -962    369       C  
ATOM   2395  NZ  LYS A 306     -30.757  49.604  34.927  1.00 47.23           N  
ANISOU 2395  NZ  LYS A 306     4300   5284   8358    -34   -917    414       N  
ATOM   2396  N   GLU A 307     -26.470  48.387  36.640  1.00 50.26           N  
ANISOU 2396  N   GLU A 307     4547   5721   8827   -257   -962    651       N  
ATOM   2397  CA  GLU A 307     -25.231  49.214  36.638  1.00 52.81           C  
ANISOU 2397  CA  GLU A 307     4876   6025   9163   -352  -1048    739       C  
ATOM   2398  C   GLU A 307     -25.326  50.285  35.545  1.00 54.19           C  
ANISOU 2398  C   GLU A 307     5092   6175   9322   -388  -1089    764       C  
ATOM   2399  O   GLU A 307     -26.003  50.033  34.529  1.00 54.14           O  
ANISOU 2399  O   GLU A 307     5062   6196   9313   -344  -1026    732       O  
ATOM   2400  CB  GLU A 307     -23.987  48.342  36.426  1.00 53.49           C  
ANISOU 2400  CB  GLU A 307     4838   6191   9295   -394  -1010    812       C  
ATOM   2401  CG  GLU A 307     -22.658  49.049  36.703  1.00 53.95           C  
ANISOU 2401  CG  GLU A 307     4883   6244   9369   -500  -1101    907       C  
ATOM   2402  CD  GLU A 307     -22.425  49.469  38.150  1.00 54.42           C  
ANISOU 2402  CD  GLU A 307     5026   6232   9417   -527  -1196    907       C  
ATOM   2403  OE1 GLU A 307     -22.917  50.552  38.542  1.00 54.22           O  
ANISOU 2403  OE1 GLU A 307     5130   6119   9353   -537  -1278    883       O  
ATOM   2404  OE2 GLU A 307     -21.738  48.726  38.881  1.00 54.70           O  
ANISOU 2404  OE2 GLU A 307     5008   6295   9479   -533  -1195    930       O  
ATOM   2405  N   ASN A 308     -24.669  51.430  35.766  1.00 54.55           N  
ANISOU 2405  N   ASN A 308     5208   6164   9355   -472  -1201    820       N  
ATOM   2406  CA  ASN A 308     -24.555  52.535  34.782  1.00 54.96           C  
ANISOU 2406  CA  ASN A 308     5312   6181   9386   -534  -1263    863       C  
ATOM   2407  C   ASN A 308     -23.082  52.706  34.426  1.00 55.24           C  
ANISOU 2407  C   ASN A 308     5272   6270   9445   -661  -1293    983       C  
ATOM   2408  O   ASN A 308     -22.709  52.445  33.263  1.00 54.74           O  
ANISOU 2408  O   ASN A 308     5121   6282   9393   -692  -1231   1028       O  
ATOM   2409  CB  ASN A 308     -25.139  53.850  35.304  1.00 55.81           C  
ANISOU 2409  CB  ASN A 308     5591   6167   9445   -528  -1387    827       C  
ATOM   2410  CG  ASN A 308     -25.587  54.736  34.162  1.00 56.35           C  
ANISOU 2410  CG  ASN A 308     5728   6194   9485   -541  -1427    828       C  
ATOM   2411  OD1 ASN A 308     -24.836  54.991  33.219  1.00 55.77           O  
ANISOU 2411  OD1 ASN A 308     5617   6155   9418   -637  -1435    913       O  
ATOM   2412  ND2 ASN A 308     -26.843  55.153  34.211  1.00 57.55           N  
ANISOU 2412  ND2 ASN A 308     5977   6284   9603   -441  -1447    733       N  
ATOM   2413  N   SER A 309     -22.304  53.135  35.423  1.00 55.94           N  
ANISOU 2413  N   SER A 309     5393   6321   9538   -730  -1386   1031       N  
ATOM   2414  CA  SER A 309     -20.851  53.420  35.360  1.00 56.05           C  
ANISOU 2414  CA  SER A 309     5337   6382   9575   -865  -1441   1151       C  
ATOM   2415  C   SER A 309     -20.256  53.221  36.757  1.00 56.04           C  
ANISOU 2415  C   SER A 309     5341   6357   9592   -883  -1501   1165       C  
ATOM   2416  O   SER A 309     -20.731  53.894  37.695  1.00 55.12           O  
ANISOU 2416  O   SER A 309     5371   6129   9442   -868  -1594   1124       O  
ATOM   2417  CB  SER A 309     -20.615  54.809  34.843  1.00 57.14           C  
ANISOU 2417  CB  SER A 309     5576   6456   9676   -976  -1556   1214       C  
ATOM   2418  OG  SER A 309     -19.250  54.993  34.472  1.00 58.57           O  
ANISOU 2418  OG  SER A 309     5659   6717   9878  -1117  -1583   1339       O  
ATOM   2419  N   TYR A 310     -19.300  52.295  36.890  1.00 56.68           N  
ANISOU 2419  N   TYR A 310     5273   6537   9722   -902  -1449   1215       N  
ATOM   2420  CA  TYR A 310     -18.521  52.062  38.131  1.00 57.91           C  
ANISOU 2420  CA  TYR A 310     5416   6682   9903   -934  -1514   1246       C  
ATOM   2421  C   TYR A 310     -17.048  52.370  37.873  1.00 61.23           C  
ANISOU 2421  C   TYR A 310     5729   7177  10356  -1070  -1569   1374       C  
ATOM   2422  O   TYR A 310     -16.542  52.081  36.763  1.00 62.07           O  
ANISOU 2422  O   TYR A 310     5702   7400  10482  -1098  -1493   1425       O  
ATOM   2423  CB  TYR A 310     -18.630  50.616  38.611  1.00 56.84           C  
ANISOU 2423  CB  TYR A 310     5194   6602   9800   -832  -1416   1193       C  
ATOM   2424  CG  TYR A 310     -17.848  50.322  39.864  1.00 57.13           C  
ANISOU 2424  CG  TYR A 310     5221   6623   9860   -860  -1485   1223       C  
ATOM   2425  CD1 TYR A 310     -18.302  50.739  41.107  1.00 56.72           C  
ANISOU 2425  CD1 TYR A 310     5318   6458   9775   -849  -1569   1179       C  
ATOM   2426  CD2 TYR A 310     -16.652  49.621  39.809  1.00 57.37           C  
ANISOU 2426  CD2 TYR A 310     5096   6755   9944   -892  -1469   1292       C  
ATOM   2427  CE1 TYR A 310     -17.591  50.464  42.263  1.00 57.20           C  
ANISOU 2427  CE1 TYR A 310     5382   6498   9854   -877  -1639   1207       C  
ATOM   2428  CE2 TYR A 310     -15.930  49.334  40.956  1.00 57.69           C  
ANISOU 2428  CE2 TYR A 310     5129   6778  10010   -916  -1542   1319       C  
ATOM   2429  CZ  TYR A 310     -16.400  49.760  42.187  1.00 57.63           C  
ANISOU 2429  CZ  TYR A 310     5280   6647   9967   -913  -1629   1278       C  
ATOM   2430  OH  TYR A 310     -15.685  49.480  43.317  1.00 58.36           O  
ANISOU 2430  OH  TYR A 310     5375   6716  10080   -940  -1707   1307       O  
ATOM   2431  N   THR A 311     -16.385  52.940  38.884  1.00 63.68           N  
ANISOU 2431  N   THR A 311     6096   7430  10670  -1154  -1699   1425       N  
ATOM   2432  CA  THR A 311     -14.908  53.075  38.983  1.00 64.51           C  
ANISOU 2432  CA  THR A 311     6084   7611  10815  -1283  -1764   1548       C  
ATOM   2433  C   THR A 311     -14.508  52.791  40.437  1.00 65.81           C  
ANISOU 2433  C   THR A 311     6282   7722  10999  -1279  -1845   1544       C  
ATOM   2434  O   THR A 311     -15.196  53.314  41.353  1.00 65.90           O  
ANISOU 2434  O   THR A 311     6474   7596  10969  -1254  -1925   1487       O  
ATOM   2435  CB  THR A 311     -14.455  54.445  38.466  1.00 65.16           C  
ANISOU 2435  CB  THR A 311     6226   7663  10867  -1441  -1877   1643       C  
ATOM   2436  OG1 THR A 311     -15.125  54.707  37.233  1.00 64.14           O  
ANISOU 2436  OG1 THR A 311     6113   7549  10706  -1421  -1805   1620       O  
ATOM   2437  CG2 THR A 311     -12.957  54.511  38.268  1.00 66.74           C  
ANISOU 2437  CG2 THR A 311     6264   7982  11109  -1583  -1916   1778       C  
ATOM   2438  N   THR A 312     -13.481  51.954  40.636  1.00 67.12           N  
ANISOU 2438  N   THR A 312     6283   7995  11224  -1289  -1822   1595       N  
ATOM   2439  CA  THR A 312     -13.001  51.495  41.968  1.00 67.82           C  
ANISOU 2439  CA  THR A 312     6382   8047  11338  -1279  -1893   1595       C  
ATOM   2440  C   THR A 312     -12.092  52.552  42.596  1.00 69.55           C  
ANISOU 2440  C   THR A 312     6653   8212  11558  -1436  -2067   1696       C  
ATOM   2441  O   THR A 312     -11.397  53.259  41.842  1.00 70.19           O  
ANISOU 2441  O   THR A 312     6666   8356  11646  -1562  -2106   1795       O  
ATOM   2442  CB  THR A 312     -12.233  50.169  41.891  1.00 68.71           C  
ANISOU 2442  CB  THR A 312     6298   8293  11514  -1219  -1810   1609       C  
ATOM   2443  OG1 THR A 312     -11.893  49.811  43.232  1.00 69.55           O  
ANISOU 2443  OG1 THR A 312     6448   8339  11637  -1210  -1894   1602       O  
ATOM   2444  CG2 THR A 312     -10.966  50.240  41.065  1.00 69.67           C  
ANISOU 2444  CG2 THR A 312     6220   8568  11680  -1312  -1804   1722       C  
ATOM   2445  N   THR A 313     -12.086  52.615  43.930  1.00 70.69           N  
ANISOU 2445  N   THR A 313     6915   8251  11693  -1433  -2169   1675       N  
ATOM   2446  CA  THR A 313     -11.205  53.496  44.747  1.00 72.50           C  
ANISOU 2446  CA  THR A 313     7209   8412  11923  -1575  -2353   1766       C  
ATOM   2447  C   THR A 313     -10.041  52.651  45.297  1.00 73.70           C  
ANISOU 2447  C   THR A 313     7200   8654  12146  -1593  -2375   1825       C  
ATOM   2448  O   THR A 313      -9.847  52.635  46.534  1.00 73.48           O  
ANISOU 2448  O   THR A 313     7268   8535  12115  -1600  -2481   1819       O  
ATOM   2449  CB  THR A 313     -12.024  54.220  45.827  1.00 71.60           C  
ANISOU 2449  CB  THR A 313     7356   8109  11738  -1553  -2459   1700       C  
ATOM   2450  OG1 THR A 313     -12.545  53.257  46.739  1.00 70.55           O  
ANISOU 2450  OG1 THR A 313     7260   7944  11601  -1426  -2404   1607       O  
ATOM   2451  CG2 THR A 313     -13.182  55.011  45.261  1.00 70.44           C  
ANISOU 2451  CG2 THR A 313     7357   7882  11524  -1515  -2437   1634       C  
ATOM   2452  N   ILE A 314      -9.303  51.981  44.398  1.00 75.03           N  
ANISOU 2452  N   ILE A 314     7137   8997  12373  -1592  -2281   1875       N  
ATOM   2453  CA  ILE A 314      -8.126  51.106  44.712  1.00 76.68           C  
ANISOU 2453  CA  ILE A 314     7153   9324  12656  -1592  -2289   1931       C  
ATOM   2454  C   ILE A 314      -6.958  51.488  43.787  1.00 78.65           C  
ANISOU 2454  C   ILE A 314     7198   9736  12946  -1720  -2298   2059       C  
ATOM   2455  O   ILE A 314      -7.166  51.485  42.547  1.00 78.07           O  
ANISOU 2455  O   ILE A 314     7039   9760  12861  -1708  -2180   2061       O  
ATOM   2456  CB  ILE A 314      -8.507  49.612  44.585  1.00 75.11           C  
ANISOU 2456  CB  ILE A 314     6867   9189  12481  -1413  -2141   1838       C  
ATOM   2457  CG1 ILE A 314      -9.414  49.166  45.737  1.00 74.14           C  
ANISOU 2457  CG1 ILE A 314     6927   8919  12322  -1314  -2157   1734       C  
ATOM   2458  CG2 ILE A 314      -7.277  48.712  44.457  1.00 74.78           C  
ANISOU 2458  CG2 ILE A 314     6591   9306  12515  -1394  -2122   1895       C  
ATOM   2459  CD1 ILE A 314     -10.189  47.887  45.452  1.00 73.07           C  
ANISOU 2459  CD1 ILE A 314     6764   8816  12184  -1149  -2005   1630       C  
ATOM   2460  N   LYS A 315      -5.792  51.806  44.378  1.00 79.44           N  
ANISOU 2460  N   LYS A 315     7225   9868  13087  -1843  -2434   2164       N  
ATOM   2461  CA  LYS A 315      -4.530  52.168  43.676  1.00 80.30           C  
ANISOU 2461  CA  LYS A 315     7121  10150  13239  -1986  -2460   2302       C  
ATOM   2462  C   LYS A 315      -4.835  53.177  42.558  1.00 81.33           C  
ANISOU 2462  C   LYS A 315     7285  10296  13317  -2093  -2434   2348       C  
ATOM   2463  O   LYS A 315      -4.741  54.396  42.737  1.00 82.30           O  
ANISOU 2463  O   LYS A 315     7538  10327  13405  -2254  -2575   2419       O  
ATOM   2464  CB  LYS A 315      -3.854  50.899  43.143  1.00 80.19           C  
ANISOU 2464  CB  LYS A 315     6840  10337  13288  -1876  -2329   2299       C  
ATOM   2465  CG  LYS A 315      -2.779  50.308  44.050  1.00 80.52           C  
ANISOU 2465  CG  LYS A 315     6757  10435  13401  -1874  -2418   2343       C  
ATOM   2466  CD  LYS A 315      -1.396  50.911  43.800  1.00 81.36           C  
ANISOU 2466  CD  LYS A 315     6668  10694  13552  -2053  -2507   2498       C  
ATOM   2467  CE  LYS A 315      -0.400  50.561  44.882  1.00 82.13           C  
ANISOU 2467  CE  LYS A 315     6683  10805  13715  -2075  -2640   2547       C  
ATOM   2468  NZ  LYS A 315      -0.437  49.111  45.196  1.00 81.83           N  
ANISOU 2468  NZ  LYS A 315     6570  10803  13718  -1866  -2557   2451       N  
TER    2469      LYS A 315                                                      
ATOM   2470  N   ARG B   3     -15.785  28.185 -10.321  1.00 87.70           N  
ANISOU 2470  N   ARG B   3    11726  10623  10973   1656   -160   1246       N  
ATOM   2471  CA  ARG B   3     -14.635  28.452  -9.412  1.00 87.43           C  
ANISOU 2471  CA  ARG B   3    11697  10477  11044   1475    -80   1273       C  
ATOM   2472  C   ARG B   3     -14.585  27.365  -8.325  1.00 87.71           C  
ANISOU 2472  C   ARG B   3    11534  10573  11218   1370   -127   1186       C  
ATOM   2473  O   ARG B   3     -15.475  27.371  -7.468  1.00 86.04           O  
ANISOU 2473  O   ARG B   3    11271  10371  11048   1414   -193   1142       O  
ATOM   2474  CB  ARG B   3     -14.789  29.854  -8.816  1.00 86.90           C  
ANISOU 2474  CB  ARG B   3    11793  10265  10958   1493    -44   1336       C  
ATOM   2475  CG  ARG B   3     -13.470  30.549  -8.506  1.00 86.50           C  
ANISOU 2475  CG  ARG B   3    11838  10080  10948   1332     65   1403       C  
ATOM   2476  CD  ARG B   3     -13.646  31.636  -7.462  1.00 86.51           C  
ANISOU 2476  CD  ARG B   3    11947   9945  10977   1309     83   1430       C  
ATOM   2477  NE  ARG B   3     -13.344  31.170  -6.112  1.00 85.10           N  
ANISOU 2477  NE  ARG B   3    11638   9761  10934   1173     62   1373       N  
ATOM   2478  CZ  ARG B   3     -13.579  31.855  -4.992  1.00 84.76           C  
ANISOU 2478  CZ  ARG B   3    11647   9621  10935   1144     59   1371       C  
ATOM   2479  NH1 ARG B   3     -14.144  33.052  -5.033  1.00 86.10           N  
ANISOU 2479  NH1 ARG B   3    12000   9687  11028   1245     78   1422       N  
ATOM   2480  NH2 ARG B   3     -13.245  31.340  -3.823  1.00 83.10           N  
ANISOU 2480  NH2 ARG B   3    11312   9418  10842   1018     40   1319       N  
ATOM   2481  N   THR B   4     -13.583  26.474  -8.365  1.00 90.54           N  
ANISOU 2481  N   THR B   4    11788  10968  11643   1242    -91   1166       N  
ATOM   2482  CA  THR B   4     -13.531  25.188  -7.600  1.00 91.37           C  
ANISOU 2482  CA  THR B   4    11696  11154  11865   1160   -136   1080       C  
ATOM   2483  C   THR B   4     -12.338  25.178  -6.627  1.00 91.45           C  
ANISOU 2483  C   THR B   4    11664  11095  11988    981    -74   1097       C  
ATOM   2484  O   THR B   4     -11.333  25.848  -6.923  1.00 93.21           O  
ANISOU 2484  O   THR B   4    11982  11240  12192    905     12   1169       O  
ATOM   2485  CB  THR B   4     -13.479  23.983  -8.556  1.00 91.58           C  
ANISOU 2485  CB  THR B   4    11626  11303  11865   1185   -156   1033       C  
ATOM   2486  OG1 THR B   4     -12.175  23.905  -9.133  1.00 91.89           O  
ANISOU 2486  OG1 THR B   4    11693  11319  11900   1093    -63   1082       O  
ATOM   2487  CG2 THR B   4     -14.511  24.051  -9.663  1.00 92.45           C  
ANISOU 2487  CG2 THR B   4    11791  11486  11848   1354   -212   1023       C  
ATOM   2488  N   ILE B   5     -12.449  24.439  -5.512  1.00 90.62           N  
ANISOU 2488  N   ILE B   5    11418  11020  11993    914   -117   1033       N  
ATOM   2489  CA  ILE B   5     -11.354  24.231  -4.511  1.00 89.50           C  
ANISOU 2489  CA  ILE B   5    11204  10835  11963    747    -73   1037       C  
ATOM   2490  C   ILE B   5     -11.074  22.730  -4.376  1.00 88.19           C  
ANISOU 2490  C   ILE B   5    10861  10774  11873    697    -95    970       C  
ATOM   2491  O   ILE B   5     -11.883  21.922  -4.867  1.00 87.54           O  
ANISOU 2491  O   ILE B   5    10713  10782  11764    788   -153    912       O  
ATOM   2492  CB  ILE B   5     -11.689  24.868  -3.146  1.00 89.12           C  
ANISOU 2492  CB  ILE B   5    11175  10709  11975    710    -97   1030       C  
ATOM   2493  CG1 ILE B   5     -12.787  24.108  -2.392  1.00 87.95           C  
ANISOU 2493  CG1 ILE B   5    10907  10629  11878    768   -186    947       C  
ATOM   2494  CG2 ILE B   5     -12.034  26.342  -3.323  1.00 90.45           C  
ANISOU 2494  CG2 ILE B   5    11534  10769  12062    773    -72   1094       C  
ATOM   2495  CD1 ILE B   5     -12.927  24.506  -0.928  1.00 86.63           C  
ANISOU 2495  CD1 ILE B   5    10731  10395  11787    708   -202    933       C  
ATOM   2496  N   LYS B   6      -9.967  22.386  -3.709  1.00 88.26           N  
ANISOU 2496  N   LYS B   6    10795  10768  11971    557    -51    978       N  
ATOM   2497  CA  LYS B   6      -9.497  20.991  -3.484  1.00 87.79           C  
ANISOU 2497  CA  LYS B   6    10572  10793  11991    498    -57    926       C  
ATOM   2498  C   LYS B   6      -9.831  20.568  -2.045  1.00 84.24           C  
ANISOU 2498  C   LYS B   6    10021  10343  11643    451   -109    873       C  
ATOM   2499  O   LYS B   6      -9.505  21.333  -1.123  1.00 82.19           O  
ANISOU 2499  O   LYS B   6     9800  10005  11422    377    -95    903       O  
ATOM   2500  CB  LYS B   6      -7.995  20.887  -3.780  1.00 89.74           C  
ANISOU 2500  CB  LYS B   6    10801  11033  12261    385     30    978       C  
ATOM   2501  CG  LYS B   6      -7.636  20.355  -5.168  1.00 90.79           C  
ANISOU 2501  CG  LYS B   6    10940  11228  12326    431     71    989       C  
ATOM   2502  CD  LYS B   6      -6.162  20.008  -5.331  1.00 91.65           C  
ANISOU 2502  CD  LYS B   6    10994  11351  12476    320    157   1029       C  
ATOM   2503  CE  LYS B   6      -5.902  18.669  -6.023  1.00 91.48           C  
ANISOU 2503  CE  LYS B   6    10874  11426  12456    348    168    989       C  
ATOM   2504  NZ  LYS B   6      -4.482  18.263  -5.875  1.00 90.55           N  
ANISOU 2504  NZ  LYS B   6    10676  11326  12400    238    245   1023       N  
ATOM   2505  N   VAL B   7     -10.459  19.401  -1.874  1.00 82.35           N  
ANISOU 2505  N   VAL B   7     9663  10184  11440    489   -164    798       N  
ATOM   2506  CA  VAL B   7     -10.758  18.789  -0.542  1.00 82.31           C  
ANISOU 2506  CA  VAL B   7     9549  10189  11534    445   -208    744       C  
ATOM   2507  C   VAL B   7     -10.610  17.259  -0.636  1.00 81.02           C  
ANISOU 2507  C   VAL B   7     9248  10114  11422    431   -217    685       C  
ATOM   2508  O   VAL B   7     -10.331  16.753  -1.746  1.00 81.27           O  
ANISOU 2508  O   VAL B   7     9278  10194  11406    461   -192    684       O  
ATOM   2509  CB  VAL B   7     -12.156  19.195  -0.022  1.00 82.61           C  
ANISOU 2509  CB  VAL B   7     9612  10215  11558    532   -278    707       C  
ATOM   2510  CG1 VAL B   7     -12.315  20.708   0.075  1.00 83.09           C  
ANISOU 2510  CG1 VAL B   7     9822  10182  11565    556   -264    767       C  
ATOM   2511  CG2 VAL B   7     -13.279  18.592  -0.854  1.00 82.93           C  
ANISOU 2511  CG2 VAL B   7     9624  10340  11543    652   -333    652       C  
ATOM   2512  N   PHE B   8     -10.787  16.561   0.496  1.00 79.29           N  
ANISOU 2512  N   PHE B   8     8927   9908  11291    389   -248    638       N  
ATOM   2513  CA  PHE B   8     -10.744  15.078   0.624  1.00 77.03           C  
ANISOU 2513  CA  PHE B   8     8513   9692  11062    376   -258    578       C  
ATOM   2514  C   PHE B   8     -12.078  14.541   1.169  1.00 73.78           C  
ANISOU 2514  C   PHE B   8     8045   9312  10675    432   -330    502       C  
ATOM   2515  O   PHE B   8     -12.651  15.137   2.110  1.00 72.77           O  
ANISOU 2515  O   PHE B   8     7932   9144  10571    434   -362    499       O  
ATOM   2516  CB  PHE B   8      -9.603  14.649   1.550  1.00 77.76           C  
ANISOU 2516  CB  PHE B   8     8528   9771  11244    265   -219    597       C  
ATOM   2517  CG  PHE B   8      -8.225  15.003   1.059  1.00 80.57           C  
ANISOU 2517  CG  PHE B   8     8911  10114  11588    198   -146    667       C  
ATOM   2518  CD1 PHE B   8      -7.785  14.562  -0.180  1.00 81.24           C  
ANISOU 2518  CD1 PHE B   8     9002  10241  11623    227   -103    676       C  
ATOM   2519  CD2 PHE B   8      -7.365  15.767   1.837  1.00 81.46           C  
ANISOU 2519  CD2 PHE B   8     9040  10173  11737    102   -117    720       C  
ATOM   2520  CE1 PHE B   8      -6.517  14.890  -0.633  1.00 81.78           C  
ANISOU 2520  CE1 PHE B   8     9088  10301  11681    166    -29    743       C  
ATOM   2521  CE2 PHE B   8      -6.098  16.093   1.381  1.00 81.95           C  
ANISOU 2521  CE2 PHE B   8     9116  10229  11790     33    -47    784       C  
ATOM   2522  CZ  PHE B   8      -5.680  15.657   0.145  1.00 82.79           C  
ANISOU 2522  CZ  PHE B   8     9225  10381  11850     67     -1    797       C  
ATOM   2523  N   THR B   9     -12.558  13.442   0.578  1.00 70.41           N  
ANISOU 2523  N   THR B   9     7555   8956  10240    475   -351    440       N  
ATOM   2524  CA  THR B   9     -13.681  12.613   1.084  1.00 68.26           C  
ANISOU 2524  CA  THR B   9     7202   8727  10006    506   -409    359       C  
ATOM   2525  C   THR B   9     -13.117  11.271   1.555  1.00 65.90           C  
ANISOU 2525  C   THR B   9     6799   8451   9787    442   -385    323       C  
ATOM   2526  O   THR B   9     -12.087  10.846   1.009  1.00 64.55           O  
ANISOU 2526  O   THR B   9     6623   8289   9614    409   -331    348       O  
ATOM   2527  CB  THR B   9     -14.766  12.435   0.015  1.00 69.18           C  
ANISOU 2527  CB  THR B   9     7334   8907  10043    604   -457    310       C  
ATOM   2528  OG1 THR B   9     -14.191  11.770  -1.110  1.00 69.57           O  
ANISOU 2528  OG1 THR B   9     7385   8995  10051    608   -424    304       O  
ATOM   2529  CG2 THR B   9     -15.370  13.748  -0.437  1.00 70.26           C  
ANISOU 2529  CG2 THR B   9     7574   9023  10095    684   -483    349       C  
ATOM   2530  N   THR B  10     -13.769  10.637   2.532  1.00 64.60           N  
ANISOU 2530  N   THR B  10     6559   8295   9689    428   -418    270       N  
ATOM   2531  CA  THR B  10     -13.378   9.321   3.107  1.00 64.03           C  
ANISOU 2531  CA  THR B  10     6394   8238   9696    374   -396    233       C  
ATOM   2532  C   THR B  10     -14.549   8.747   3.917  1.00 63.73           C  
ANISOU 2532  C   THR B  10     6292   8218   9705    386   -445    164       C  
ATOM   2533  O   THR B  10     -15.448   9.522   4.271  1.00 62.68           O  
ANISOU 2533  O   THR B  10     6184   8076   9555    424   -488    159       O  
ATOM   2534  CB  THR B  10     -12.120   9.464   3.974  1.00 63.46           C  
ANISOU 2534  CB  THR B  10     6305   8122   9683    293   -349    292       C  
ATOM   2535  OG1 THR B  10     -11.659   8.167   4.357  1.00 61.91           O  
ANISOU 2535  OG1 THR B  10     6026   7944   9551    256   -323    264       O  
ATOM   2536  CG2 THR B  10     -12.359  10.315   5.204  1.00 63.70           C  
ANISOU 2536  CG2 THR B  10     6351   8104   9749    266   -374    315       C  
ATOM   2537  N   VAL B  11     -14.525   7.437   4.186  1.00 64.63           N  
ANISOU 2537  N   VAL B  11     6330   8351   9872    357   -432    114       N  
ATOM   2538  CA  VAL B  11     -15.470   6.726   5.101  1.00 64.61           C  
ANISOU 2538  CA  VAL B  11     6259   8359   9930    349   -462     51       C  
ATOM   2539  C   VAL B  11     -14.726   6.271   6.368  1.00 64.57           C  
ANISOU 2539  C   VAL B  11     6209   8314  10011    281   -428     74       C  
ATOM   2540  O   VAL B  11     -15.406   6.068   7.391  1.00 62.45           O  
ANISOU 2540  O   VAL B  11     5901   8035   9791    270   -449     45       O  
ATOM   2541  CB  VAL B  11     -16.145   5.531   4.398  1.00 65.47           C  
ANISOU 2541  CB  VAL B  11     6324   8520  10029    367   -475    -31       C  
ATOM   2542  CG1 VAL B  11     -17.170   5.980   3.367  1.00 66.10           C  
ANISOU 2542  CG1 VAL B  11     6433   8652  10027    437   -528    -66       C  
ATOM   2543  CG2 VAL B  11     -15.132   4.591   3.757  1.00 66.16           C  
ANISOU 2543  CG2 VAL B  11     6407   8610  10119    342   -419    -30       C  
ATOM   2544  N   ASP B  12     -13.393   6.124   6.305  1.00 65.80           N  
ANISOU 2544  N   ASP B  12     6368   8452  10180    242   -376    125       N  
ATOM   2545  CA  ASP B  12     -12.548   5.537   7.387  1.00 65.76           C  
ANISOU 2545  CA  ASP B  12     6313   8423  10250    184   -341    148       C  
ATOM   2546  C   ASP B  12     -11.502   6.542   7.888  1.00 67.60           C  
ANISOU 2546  C   ASP B  12     6574   8623  10487    142   -324    229       C  
ATOM   2547  O   ASP B  12     -10.932   6.279   8.974  1.00 68.19           O  
ANISOU 2547  O   ASP B  12     6608   8680  10620     95   -310    250       O  
ATOM   2548  CB  ASP B  12     -11.840   4.251   6.927  1.00 64.45           C  
ANISOU 2548  CB  ASP B  12     6108   8276  10104    176   -292    133       C  
ATOM   2549  CG  ASP B  12     -11.182   4.343   5.552  1.00 63.28           C  
ANISOU 2549  CG  ASP B  12     5997   8151   9894    198   -260    155       C  
ATOM   2550  OD1 ASP B  12     -11.047   5.464   5.021  1.00 63.21           O  
ANISOU 2550  OD1 ASP B  12     6045   8139   9831    211   -269    196       O  
ATOM   2551  OD2 ASP B  12     -10.824   3.294   5.014  1.00 62.78           O  
ANISOU 2551  OD2 ASP B  12     5913   8105   9833    206   -223    130       O  
ATOM   2552  N   ASN B  13     -11.226   7.611   7.131  1.00 70.28           N  
ANISOU 2552  N   ASN B  13     6979   8955  10766    153   -323    272       N  
ATOM   2553  CA  ASN B  13     -10.207   8.646   7.471  1.00 71.87           C  
ANISOU 2553  CA  ASN B  13     7218   9125  10965    102   -302    347       C  
ATOM   2554  C   ASN B  13      -8.806   8.022   7.401  1.00 73.18           C  
ANISOU 2554  C   ASN B  13     7334   9310  11161     56   -247    386       C  
ATOM   2555  O   ASN B  13      -7.908   8.483   8.133  1.00 73.51           O  
ANISOU 2555  O   ASN B  13     7364   9335  11231     -5   -233    437       O  
ATOM   2556  CB  ASN B  13     -10.466   9.267   8.848  1.00 71.55           C  
ANISOU 2556  CB  ASN B  13     7181   9042  10961     68   -332    357       C  
ATOM   2557  CG  ASN B  13      -9.665  10.530   9.097  1.00 71.47           C  
ANISOU 2557  CG  ASN B  13     7229   8991  10933     16   -321    425       C  
ATOM   2558  OD1 ASN B  13      -9.539  11.381   8.220  1.00 71.53           O  
ANISOU 2558  OD1 ASN B  13     7309   8986  10882     30   -311    456       O  
ATOM   2559  ND2 ASN B  13      -9.123  10.668  10.296  1.00 71.35           N  
ANISOU 2559  ND2 ASN B  13     7189   8955  10966    -47   -323    447       N  
ATOM   2560  N   ILE B  14      -8.637   7.001   6.559  1.00 74.58           N  
ANISOU 2560  N   ILE B  14     7482   9524  11330     86   -216    360       N  
ATOM   2561  CA  ILE B  14      -7.337   6.310   6.300  1.00 75.62           C  
ANISOU 2561  CA  ILE B  14     7566   9681  11482     61   -155    395       C  
ATOM   2562  C   ILE B  14      -7.098   6.325   4.784  1.00 79.64           C  
ANISOU 2562  C   ILE B  14     8118  10216  11924    100   -122    401       C  
ATOM   2563  O   ILE B  14      -6.003   6.759   4.352  1.00 79.41           O  
ANISOU 2563  O   ILE B  14     8097  10197  11878     73    -75    463       O  
ATOM   2564  CB  ILE B  14      -7.341   4.894   6.916  1.00 72.67           C  
ANISOU 2564  CB  ILE B  14     7120   9321  11170     66   -142    356       C  
ATOM   2565  CG1 ILE B  14      -6.922   4.936   8.389  1.00 71.55           C  
ANISOU 2565  CG1 ILE B  14     6929   9162  11092     15   -152    384       C  
ATOM   2566  CG2 ILE B  14      -6.475   3.933   6.121  1.00 72.28           C  
ANISOU 2566  CG2 ILE B  14     7041   9304  11116     84    -80    363       C  
ATOM   2567  CD1 ILE B  14      -6.994   3.601   9.091  1.00 70.94           C  
ANISOU 2567  CD1 ILE B  14     6791   9090  11072     24   -139    350       C  
ATOM   2568  N   ASN B  15      -8.098   5.889   4.010  1.00 84.23           N  
ANISOU 2568  N   ASN B  15     8726  10812  12466    158   -144    339       N  
ATOM   2569  CA  ASN B  15      -8.142   6.028   2.530  1.00 86.59           C  
ANISOU 2569  CA  ASN B  15     9081  11134  12683    206   -127    335       C  
ATOM   2570  C   ASN B  15      -8.791   7.376   2.188  1.00 86.61           C  
ANISOU 2570  C   ASN B  15     9164  11118  12624    228   -168    354       C  
ATOM   2571  O   ASN B  15     -10.037   7.429   2.159  1.00 90.54           O  
ANISOU 2571  O   ASN B  15     9678  11620  13101    271   -225    300       O  
ATOM   2572  CB  ASN B  15      -8.878   4.851   1.886  1.00 87.72           C  
ANISOU 2572  CB  ASN B  15     9212  11305  12809    254   -136    254       C  
ATOM   2573  CG  ASN B  15      -8.189   3.520   2.120  1.00 88.22           C  
ANISOU 2573  CG  ASN B  15     9214  11378  12926    240    -85    240       C  
ATOM   2574  OD1 ASN B  15      -8.173   3.003   3.240  1.00 87.95           O  
ANISOU 2574  OD1 ASN B  15     9124  11327  12964    211    -88    231       O  
ATOM   2575  ND2 ASN B  15      -7.639   2.941   1.060  1.00 88.94           N  
ANISOU 2575  ND2 ASN B  15     9321  11493  12978    268    -34    237       N  
ATOM   2576  N   LEU B  16      -7.974   8.418   1.972  1.00 85.06           N  
ANISOU 2576  N   LEU B  16     9015  10901  12400    199   -137    428       N  
ATOM   2577  CA  LEU B  16      -8.416   9.785   1.577  1.00 85.11           C  
ANISOU 2577  CA  LEU B  16     9117  10879  12342    221   -161    459       C  
ATOM   2578  C   LEU B  16      -8.566   9.840   0.052  1.00 87.22           C  
ANISOU 2578  C   LEU B  16     9447  11175  12517    285   -145    456       C  
ATOM   2579  O   LEU B  16      -7.603   9.468  -0.635  1.00 89.54           O  
ANISOU 2579  O   LEU B  16     9734  11490  12796    273    -84    484       O  
ATOM   2580  CB  LEU B  16      -7.389  10.822   2.047  1.00 83.99           C  
ANISOU 2580  CB  LEU B  16     9000  10696  12213    148   -127    540       C  
ATOM   2581  CG  LEU B  16      -7.067  10.840   3.543  1.00 82.96           C  
ANISOU 2581  CG  LEU B  16     8812  10541  12166     77   -140    550       C  
ATOM   2582  CD1 LEU B  16      -6.185  12.032   3.887  1.00 82.95           C  
ANISOU 2582  CD1 LEU B  16     8854  10498  12164      2   -115    623       C  
ATOM   2583  CD2 LEU B  16      -8.329  10.869   4.386  1.00 82.07           C  
ANISOU 2583  CD2 LEU B  16     8698  10408  12075    106   -207    497       C  
ATOM   2584  N   HIS B  17      -9.718  10.300  -0.450  1.00 89.57           N  
ANISOU 2584  N   HIS B  17     9803  11477  12751    355   -198    426       N  
ATOM   2585  CA  HIS B  17     -10.044  10.391  -1.902  1.00 90.62           C  
ANISOU 2585  CA  HIS B  17    10003  11642  12783    428   -197    417       C  
ATOM   2586  C   HIS B  17     -10.079  11.872  -2.312  1.00 89.52           C  
ANISOU 2586  C   HIS B  17     9974  11464  12573    452   -195    482       C  
ATOM   2587  O   HIS B  17     -10.895  12.621  -1.742  1.00 88.43           O  
ANISOU 2587  O   HIS B  17     9866  11297  12434    474   -245    479       O  
ATOM   2588  CB  HIS B  17     -11.342   9.621  -2.196  1.00 90.99           C  
ANISOU 2588  CB  HIS B  17    10023  11739  12810    492   -262    326       C  
ATOM   2589  CG  HIS B  17     -11.283   8.195  -1.759  1.00 91.94           C  
ANISOU 2589  CG  HIS B  17    10048  11883  13000    460   -255    265       C  
ATOM   2590  ND1 HIS B  17     -11.026   7.160  -2.636  1.00 94.07           N  
ANISOU 2590  ND1 HIS B  17    10306  12192  13245    477   -225    226       N  
ATOM   2591  CD2 HIS B  17     -11.411   7.629  -0.538  1.00 92.51           C  
ANISOU 2591  CD2 HIS B  17    10044  11941  13165    415   -267    238       C  
ATOM   2592  CE1 HIS B  17     -11.012   6.017  -1.976  1.00 94.44           C  
ANISOU 2592  CE1 HIS B  17    10274  12241  13365    443   -219    178       C  
ATOM   2593  NE2 HIS B  17     -11.243   6.277  -0.685  1.00 93.50           N  
ANISOU 2593  NE2 HIS B  17    10113  12091  13319    405   -244    186       N  
ATOM   2594  N   THR B  18      -9.215  12.279  -3.251  1.00 88.93           N  
ANISOU 2594  N   THR B  18     9962  11386  12442    449   -134    540       N  
ATOM   2595  CA  THR B  18      -9.032  13.697  -3.670  1.00 89.41           C  
ANISOU 2595  CA  THR B  18    10139  11397  12436    460   -113    614       C  
ATOM   2596  C   THR B  18     -10.210  14.112  -4.557  1.00 88.20           C  
ANISOU 2596  C   THR B  18    10065  11264  12181    571   -166    590       C  
ATOM   2597  O   THR B  18     -10.630  13.302  -5.419  1.00 88.20           O  
ANISOU 2597  O   THR B  18    10048  11327  12134    630   -184    538       O  
ATOM   2598  CB  THR B  18      -7.692  13.936  -4.381  1.00 89.46           C  
ANISOU 2598  CB  THR B  18    10179  11395  12416    415    -22    685       C  
ATOM   2599  OG1 THR B  18      -6.689  13.140  -3.750  1.00 89.83           O  
ANISOU 2599  OG1 THR B  18    10122  11457  12551    333     19    688       O  
ATOM   2600  CG2 THR B  18      -7.271  15.390  -4.358  1.00 88.90           C  
ANISOU 2600  CG2 THR B  18    10211  11253  12313    382     11    767       C  
ATOM   2601  N   GLN B  19     -10.717  15.328  -4.341  1.00 85.54           N  
ANISOU 2601  N   GLN B  19     9814  10876  11809    601   -190    626       N  
ATOM   2602  CA  GLN B  19     -11.952  15.839  -4.989  1.00 85.17           C  
ANISOU 2602  CA  GLN B  19     9840  10850  11671    718   -250    607       C  
ATOM   2603  C   GLN B  19     -11.778  17.326  -5.335  1.00 84.70           C  
ANISOU 2603  C   GLN B  19     9923  10718  11539    743   -219    692       C  
ATOM   2604  O   GLN B  19     -11.029  18.028  -4.616  1.00 83.72           O  
ANISOU 2604  O   GLN B  19     9829  10518  11461    660   -175    747       O  
ATOM   2605  CB  GLN B  19     -13.146  15.600  -4.061  1.00 83.74           C  
ANISOU 2605  CB  GLN B  19     9592  10686  11537    747   -331    542       C  
ATOM   2606  CG  GLN B  19     -13.413  14.130  -3.739  1.00 83.00           C  
ANISOU 2606  CG  GLN B  19     9367  10657  11510    723   -360    457       C  
ATOM   2607  CD  GLN B  19     -14.094  13.394  -4.869  1.00 83.60           C  
ANISOU 2607  CD  GLN B  19     9431  10817  11513    799   -397    396       C  
ATOM   2608  OE1 GLN B  19     -14.396  13.958  -5.917  1.00 84.62           O  
ANISOU 2608  OE1 GLN B  19     9647  10966  11539    879   -407    417       O  
ATOM   2609  NE2 GLN B  19     -14.369  12.119  -4.653  1.00 83.53           N  
ANISOU 2609  NE2 GLN B  19     9321  10859  11557    776   -419    318       N  
ATOM   2610  N   VAL B  20     -12.453  17.774  -6.399  1.00 84.25           N  
ANISOU 2610  N   VAL B  20     9955  10686  11370    853   -242    700       N  
ATOM   2611  CA  VAL B  20     -12.515  19.197  -6.849  1.00 85.59           C  
ANISOU 2611  CA  VAL B  20    10279  10787  11452    906   -219    778       C  
ATOM   2612  C   VAL B  20     -13.989  19.635  -6.833  1.00 86.83           C  
ANISOU 2612  C   VAL B  20    10468  10967  11556   1031   -305    748       C  
ATOM   2613  O   VAL B  20     -14.738  19.269  -7.765  1.00 88.15           O  
ANISOU 2613  O   VAL B  20    10635  11214  11641   1132   -352    711       O  
ATOM   2614  CB  VAL B  20     -11.838  19.388  -8.223  1.00 85.98           C  
ANISOU 2614  CB  VAL B  20    10418  10843  11404    932   -156    830       C  
ATOM   2615  CG1 VAL B  20     -12.493  18.574  -9.337  1.00 85.89           C  
ANISOU 2615  CG1 VAL B  20    10386  10935  11314   1029   -201    773       C  
ATOM   2616  CG2 VAL B  20     -11.738  20.860  -8.602  1.00 86.57           C  
ANISOU 2616  CG2 VAL B  20    10660  10833  11399    969   -115    919       C  
ATOM   2617  N   VAL B  21     -14.391  20.374  -5.791  1.00 85.79           N  
ANISOU 2617  N   VAL B  21    10358  10772  11465   1025   -324    761       N  
ATOM   2618  CA  VAL B  21     -15.812  20.742  -5.513  1.00 85.84           C  
ANISOU 2618  CA  VAL B  21    10370  10801  11441   1139   -405    728       C  
ATOM   2619  C   VAL B  21     -16.152  22.067  -6.212  1.00 86.75           C  
ANISOU 2619  C   VAL B  21    10653  10866  11441   1247   -393    799       C  
ATOM   2620  O   VAL B  21     -15.358  23.023  -6.090  1.00 86.12           O  
ANISOU 2620  O   VAL B  21    10687  10680  11354   1195   -323    876       O  
ATOM   2621  CB  VAL B  21     -16.111  20.808  -3.999  1.00 85.49           C  
ANISOU 2621  CB  VAL B  21    10265  10717  11501   1086   -428    703       C  
ATOM   2622  CG1 VAL B  21     -16.205  19.424  -3.384  1.00 85.00           C  
ANISOU 2622  CG1 VAL B  21    10036  10725  11535   1023   -460    620       C  
ATOM   2623  CG2 VAL B  21     -15.116  21.659  -3.223  1.00 85.56           C  
ANISOU 2623  CG2 VAL B  21    10346  10605  11556    982   -359    769       C  
ATOM   2624  N   ASP B  22     -17.298  22.108  -6.909  1.00 86.98           N  
ANISOU 2624  N   ASP B  22    10695  10971  11382   1390   -461    774       N  
ATOM   2625  CA  ASP B  22     -17.915  23.338  -7.484  1.00 86.75           C  
ANISOU 2625  CA  ASP B  22    10816  10907  11237   1525   -469    835       C  
ATOM   2626  C   ASP B  22     -18.431  24.206  -6.324  1.00 86.24           C  
ANISOU 2626  C   ASP B  22    10789  10763  11215   1542   -479    851       C  
ATOM   2627  O   ASP B  22     -19.216  23.693  -5.501  1.00 85.58           O  
ANISOU 2627  O   ASP B  22    10589  10730  11197   1550   -541    785       O  
ATOM   2628  CB  ASP B  22     -19.021  22.984  -8.488  1.00 85.95           C  
ANISOU 2628  CB  ASP B  22    10691  10930  11035   1672   -549    792       C  
ATOM   2629  CG  ASP B  22     -19.568  24.163  -9.280  1.00 85.91           C  
ANISOU 2629  CG  ASP B  22    10843  10902  10894   1825   -554    861       C  
ATOM   2630  OD1 ASP B  22     -19.296  25.313  -8.897  1.00 85.05           O  
ANISOU 2630  OD1 ASP B  22    10864  10672  10775   1828   -502    935       O  
ATOM   2631  OD2 ASP B  22     -20.274  23.924 -10.278  1.00 85.79           O  
ANISOU 2631  OD2 ASP B  22    10825  10991  10781   1942   -612    838       O  
ATOM   2632  N   MET B  23     -17.992  25.466  -6.255  1.00 85.96           N  
ANISOU 2632  N   MET B  23    10915  10603  11142   1543   -417    936       N  
ATOM   2633  CA  MET B  23     -18.258  26.395  -5.123  1.00 85.25           C  
ANISOU 2633  CA  MET B  23    10889  10409  11091   1540   -407    960       C  
ATOM   2634  C   MET B  23     -19.746  26.756  -5.059  1.00 85.02           C  
ANISOU 2634  C   MET B  23    10865  10430  11008   1710   -483    939       C  
ATOM   2635  O   MET B  23     -20.261  26.871  -3.934  1.00 84.09           O  
ANISOU 2635  O   MET B  23    10703  10289  10956   1705   -508    911       O  
ATOM   2636  CB  MET B  23     -17.434  27.677  -5.266  1.00 86.29           C  
ANISOU 2636  CB  MET B  23    11213  10393  11178   1506   -317   1058       C  
ATOM   2637  CG  MET B  23     -15.989  27.510  -4.877  1.00 86.03           C  
ANISOU 2637  CG  MET B  23    11167  10294  11225   1317   -241   1079       C  
ATOM   2638  SD  MET B  23     -15.841  27.409  -3.094  1.00 86.78           S  
ANISOU 2638  SD  MET B  23    11179  10334  11458   1193   -250   1038       S  
ATOM   2639  CE  MET B  23     -14.587  28.648  -2.783  1.00 86.78           C  
ANISOU 2639  CE  MET B  23    11346  10163  11461   1063   -145   1126       C  
ATOM   2640  N   SER B  24     -20.402  26.939  -6.208  1.00 86.29           N  
ANISOU 2640  N   SER B  24    11076  10659  11051   1858   -518    954       N  
ATOM   2641  CA  SER B  24     -21.844  27.295  -6.308  1.00 88.38           C  
ANISOU 2641  CA  SER B  24    11340  10990  11247   2039   -594    939       C  
ATOM   2642  C   SER B  24     -22.690  26.200  -5.650  1.00 86.70           C  
ANISOU 2642  C   SER B  24    10924  10901  11117   2031   -677    837       C  
ATOM   2643  O   SER B  24     -23.374  26.498  -4.657  1.00 85.07           O  
ANISOU 2643  O   SER B  24    10689  10675  10956   2063   -701    820       O  
ATOM   2644  CB  SER B  24     -22.268  27.516  -7.742  1.00 91.72           C  
ANISOU 2644  CB  SER B  24    11836  11484  11528   2185   -620    969       C  
ATOM   2645  OG  SER B  24     -22.699  26.309  -8.366  1.00 92.78           O  
ANISOU 2645  OG  SER B  24    11820  11778  11653   2200   -693    890       O  
ATOM   2646  N   MET B  25     -22.610  24.976  -6.185  1.00 85.92           N  
ANISOU 2646  N   MET B  25    10694  10916  11034   1986   -713    772       N  
ATOM   2647  CA  MET B  25     -23.341  23.779  -5.696  1.00 83.90           C  
ANISOU 2647  CA  MET B  25    10242  10781  10854   1961   -787    670       C  
ATOM   2648  C   MET B  25     -22.927  23.512  -4.247  1.00 81.98           C  
ANISOU 2648  C   MET B  25     9931  10467  10750   1827   -757    646       C  
ATOM   2649  O   MET B  25     -21.759  23.780  -3.911  1.00 80.95           O  
ANISOU 2649  O   MET B  25     9866  10227  10662   1711   -681    692       O  
ATOM   2650  CB  MET B  25     -23.033  22.554  -6.565  1.00 83.54           C  
ANISOU 2650  CB  MET B  25    10101  10837  10801   1910   -808    613       C  
ATOM   2651  CG  MET B  25     -23.569  22.683  -7.988  1.00 84.76           C  
ANISOU 2651  CG  MET B  25    10306  11084  10814   2047   -853    622       C  
ATOM   2652  SD  MET B  25     -22.863  21.493  -9.162  1.00 85.18           S  
ANISOU 2652  SD  MET B  25    10312  11215  10836   1979   -847    579       S  
ATOM   2653  CE  MET B  25     -23.437  19.935  -8.479  1.00 84.64           C  
ANISOU 2653  CE  MET B  25    10020  11256  10881   1895   -913    450       C  
ATOM   2654  N   THR B  26     -23.862  23.022  -3.425  1.00 80.79           N  
ANISOU 2654  N   THR B  26     9651  10381  10661   1843   -813    580       N  
ATOM   2655  CA  THR B  26     -23.606  22.563  -2.033  1.00 76.88           C  
ANISOU 2655  CA  THR B  26     9069   9842  10298   1720   -796    544       C  
ATOM   2656  C   THR B  26     -22.801  21.268  -2.092  1.00 73.48           C  
ANISOU 2656  C   THR B  26     8530   9448   9940   1581   -781    495       C  
ATOM   2657  O   THR B  26     -22.634  20.717  -3.201  1.00 71.51           O  
ANISOU 2657  O   THR B  26     8265   9267   9636   1594   -794    479       O  
ATOM   2658  CB  THR B  26     -24.901  22.343  -1.240  1.00 77.01           C  
ANISOU 2658  CB  THR B  26     8976   9931  10354   1786   -858    486       C  
ATOM   2659  OG1 THR B  26     -25.646  21.327  -1.914  1.00 77.57           O  
ANISOU 2659  OG1 THR B  26     8915  10151  10405   1823   -928    411       O  
ATOM   2660  CG2 THR B  26     -25.738  23.597  -1.089  1.00 77.53           C  
ANISOU 2660  CG2 THR B  26     9143   9963  10352   1933   -869    533       C  
ATOM   2661  N   TYR B  27     -22.348  20.793  -0.934  1.00 71.55           N  
ANISOU 2661  N   TYR B  27     8216   9160   9810   1461   -757    470       N  
ATOM   2662  CA  TYR B  27     -21.674  19.478  -0.792  1.00 70.69           C  
ANISOU 2662  CA  TYR B  27     7991   9086   9781   1334   -744    419       C  
ATOM   2663  C   TYR B  27     -22.658  18.372  -1.194  1.00 71.14           C  
ANISOU 2663  C   TYR B  27     7912   9279   9837   1376   -814    330       C  
ATOM   2664  O   TYR B  27     -22.331  17.597  -2.126  1.00 70.60           O  
ANISOU 2664  O   TYR B  27     7814   9269   9741   1355   -817    303       O  
ATOM   2665  CB  TYR B  27     -21.117  19.312   0.624  1.00 68.88           C  
ANISOU 2665  CB  TYR B  27     7721   8782   9666   1216   -709    416       C  
ATOM   2666  CG  TYR B  27     -19.836  20.065   0.880  1.00 68.63           C  
ANISOU 2666  CG  TYR B  27     7798   8631   9645   1131   -636    491       C  
ATOM   2667  CD1 TYR B  27     -19.760  21.044   1.857  1.00 68.55           C  
ANISOU 2667  CD1 TYR B  27     7866   8521   9657   1116   -613    531       C  
ATOM   2668  CD2 TYR B  27     -18.691  19.801   0.139  1.00 68.68           C  
ANISOU 2668  CD2 TYR B  27     7830   8625   9638   1063   -587    521       C  
ATOM   2669  CE1 TYR B  27     -18.584  21.738   2.093  1.00 68.74           C  
ANISOU 2669  CE1 TYR B  27     7988   8439   9691   1026   -547    595       C  
ATOM   2670  CE2 TYR B  27     -17.505  20.484   0.362  1.00 68.44           C  
ANISOU 2670  CE2 TYR B  27     7888   8494   9620    976   -519    589       C  
ATOM   2671  CZ  TYR B  27     -17.451  21.456   1.347  1.00 68.49           C  
ANISOU 2671  CZ  TYR B  27     7969   8403   9649    952   -501    625       C  
ATOM   2672  OH  TYR B  27     -16.293  22.140   1.576  1.00 67.54           O  
ANISOU 2672  OH  TYR B  27     7935   8186   9541    856   -437    687       O  
ATOM   2673  N   GLY B  28     -23.832  18.339  -0.549  1.00 72.14           N  
ANISOU 2673  N   GLY B  28     7965   9456   9987   1433   -867    286       N  
ATOM   2674  CA  GLY B  28     -24.895  17.339  -0.779  1.00 72.39           C  
ANISOU 2674  CA  GLY B  28     7858   9621  10025   1465   -936    197       C  
ATOM   2675  C   GLY B  28     -25.075  17.030  -2.253  1.00 73.89           C  
ANISOU 2675  C   GLY B  28     8055   9901  10116   1526   -973    178       C  
ATOM   2676  O   GLY B  28     -24.942  15.850  -2.630  1.00 73.42           O  
ANISOU 2676  O   GLY B  28     7909   9904  10081   1461   -985    113       O  
ATOM   2677  N   GLN B  29     -25.343  18.057  -3.062  1.00 75.79           N  
ANISOU 2677  N   GLN B  29     8405  10144  10246   1647   -987    233       N  
ATOM   2678  CA  GLN B  29     -25.552  17.928  -4.529  1.00 77.72           C  
ANISOU 2678  CA  GLN B  29     8677  10476  10376   1726  -1025    224       C  
ATOM   2679  C   GLN B  29     -24.458  17.030  -5.113  1.00 77.59           C  
ANISOU 2679  C   GLN B  29     8656  10449  10374   1618   -982    209       C  
ATOM   2680  O   GLN B  29     -24.786  16.087  -5.855  1.00 77.32           O  
ANISOU 2680  O   GLN B  29     8550  10517  10312   1617  -1026    139       O  
ATOM   2681  CB  GLN B  29     -25.554  19.306  -5.192  1.00 78.69           C  
ANISOU 2681  CB  GLN B  29     8959  10553  10384   1850  -1013    315       C  
ATOM   2682  CG  GLN B  29     -26.801  20.121  -4.869  1.00 79.12           C  
ANISOU 2682  CG  GLN B  29     9015  10646  10400   1989  -1066    325       C  
ATOM   2683  CD  GLN B  29     -26.780  21.474  -5.535  1.00 80.06           C  
ANISOU 2683  CD  GLN B  29     9305  10711  10402   2119  -1048    418       C  
ATOM   2684  OE1 GLN B  29     -26.708  22.510  -4.876  1.00 79.12           O  
ANISOU 2684  OE1 GLN B  29     9284  10487  10290   2150  -1008    481       O  
ATOM   2685  NE2 GLN B  29     -26.822  21.471  -6.859  1.00 81.01           N  
ANISOU 2685  NE2 GLN B  29     9473  10898  10409   2193  -1074    428       N  
ATOM   2686  N   GLN B  30     -23.206  17.294  -4.743  1.00 78.31           N  
ANISOU 2686  N   GLN B  30     8818  10423  10511   1527   -899    268       N  
ATOM   2687  CA  GLN B  30     -22.011  16.672  -5.366  1.00 79.42           C  
ANISOU 2687  CA  GLN B  30     8979  10542  10653   1440   -843    275       C  
ATOM   2688  C   GLN B  30     -21.735  15.290  -4.756  1.00 80.35           C  
ANISOU 2688  C   GLN B  30     8966  10682  10881   1321   -836    201       C  
ATOM   2689  O   GLN B  30     -21.381  14.385  -5.535  1.00 81.90           O  
ANISOU 2689  O   GLN B  30     9134  10925  11058   1289   -830    162       O  
ATOM   2690  CB  GLN B  30     -20.818  17.609  -5.202  1.00 79.94           C  
ANISOU 2690  CB  GLN B  30     9171  10481  10722   1395   -758    373       C  
ATOM   2691  CG  GLN B  30     -21.057  19.005  -5.762  1.00 81.54           C  
ANISOU 2691  CG  GLN B  30     9521  10644  10817   1509   -754    452       C  
ATOM   2692  CD  GLN B  30     -19.869  19.908  -5.535  1.00 81.76           C  
ANISOU 2692  CD  GLN B  30     9671  10539  10854   1446   -665    544       C  
ATOM   2693  OE1 GLN B  30     -18.736  19.572  -5.872  1.00 81.56           O  
ANISOU 2693  OE1 GLN B  30     9660  10484  10844   1358   -603    566       O  
ATOM   2694  NE2 GLN B  30     -20.118  21.071  -4.955  1.00 82.01           N  
ANISOU 2694  NE2 GLN B  30     9793  10491  10877   1488   -654    598       N  
ATOM   2695  N   PHE B  31     -21.891  15.122  -3.433  1.00 80.69           N  
ANISOU 2695  N   PHE B  31     8937  10689  11030   1261   -833    182       N  
ATOM   2696  CA  PHE B  31     -21.406  13.937  -2.666  1.00 79.89           C  
ANISOU 2696  CA  PHE B  31     8732  10579  11041   1139   -807    132       C  
ATOM   2697  C   PHE B  31     -22.517  13.181  -1.922  1.00 80.31           C  
ANISOU 2697  C   PHE B  31     8658  10698  11159   1133   -863     48       C  
ATOM   2698  O   PHE B  31     -22.231  12.051  -1.481  1.00 82.11           O  
ANISOU 2698  O   PHE B  31     8800  10930  11466   1042   -845     -2       O  
ATOM   2699  CB  PHE B  31     -20.365  14.359  -1.626  1.00 79.20           C  
ANISOU 2699  CB  PHE B  31     8679  10378  11032   1050   -739    193       C  
ATOM   2700  CG  PHE B  31     -19.104  14.980  -2.175  1.00 79.74           C  
ANISOU 2700  CG  PHE B  31     8857  10378  11063   1022   -671    275       C  
ATOM   2701  CD1 PHE B  31     -18.646  14.681  -3.452  1.00 80.15           C  
ANISOU 2701  CD1 PHE B  31     8945  10464  11041   1040   -654    280       C  
ATOM   2702  CD2 PHE B  31     -18.350  15.842  -1.389  1.00 79.48           C  
ANISOU 2702  CD2 PHE B  31     8887  10243  11067    970   -622    344       C  
ATOM   2703  CE1 PHE B  31     -17.483  15.255  -3.938  1.00 80.11           C  
ANISOU 2703  CE1 PHE B  31     9035  10397  11003   1011   -584    357       C  
ATOM   2704  CE2 PHE B  31     -17.179  16.404  -1.873  1.00 79.10           C  
ANISOU 2704  CE2 PHE B  31     8931  10133  10987    932   -556    418       C  
ATOM   2705  CZ  PHE B  31     -16.750  16.108  -3.146  1.00 79.62           C  
ANISOU 2705  CZ  PHE B  31     9029  10238  10984    953   -535    426       C  
ATOM   2706  N   GLY B  32     -23.719  13.749  -1.779  1.00 81.27           N  
ANISOU 2706  N   GLY B  32     8764  10867  11247   1225   -922     35       N  
ATOM   2707  CA  GLY B  32     -24.761  13.229  -0.870  1.00 80.83           C  
ANISOU 2707  CA  GLY B  32     8588  10862  11261   1217   -964    -31       C  
ATOM   2708  C   GLY B  32     -24.427  13.586   0.575  1.00 80.20           C  
ANISOU 2708  C   GLY B  32     8510  10687  11273   1160   -922      2       C  
ATOM   2709  O   GLY B  32     -23.723  14.565   0.813  1.00 81.11           O  
ANISOU 2709  O   GLY B  32     8730  10711  11377   1162   -880     80       O  
ATOM   2710  N   PRO B  33     -24.889  12.811   1.584  1.00 79.58           N  
ANISOU 2710  N   PRO B  33     8323  10626  11287   1102   -929    -53       N  
ATOM   2711  CA  PRO B  33     -24.530  13.073   2.979  1.00 79.01           C  
ANISOU 2711  CA  PRO B  33     8254  10466  11299   1044   -888    -23       C  
ATOM   2712  C   PRO B  33     -23.016  13.295   3.149  1.00 77.55           C  
ANISOU 2712  C   PRO B  33     8149  10178  11138    964   -820     41       C  
ATOM   2713  O   PRO B  33     -22.258  12.420   2.786  1.00 75.75           O  
ANISOU 2713  O   PRO B  33     7895   9953  10931    894   -793     24       O  
ATOM   2714  CB  PRO B  33     -24.999  11.813   3.720  1.00 79.09           C  
ANISOU 2714  CB  PRO B  33     8132  10518  11400    973   -895   -102       C  
ATOM   2715  CG  PRO B  33     -26.125  11.275   2.869  1.00 80.46           C  
ANISOU 2715  CG  PRO B  33     8229  10815  11527   1028   -960   -175       C  
ATOM   2716  CD  PRO B  33     -25.762  11.636   1.440  1.00 80.60           C  
ANISOU 2716  CD  PRO B  33     8325  10856  11441   1084   -973   -149       C  
ATOM   2717  N   THR B  34     -22.629  14.466   3.670  1.00 76.64           N  
ANISOU 2717  N   THR B  34     8129   9976  11013    977   -793    112       N  
ATOM   2718  CA  THR B  34     -21.223  14.947   3.801  1.00 76.05           C  
ANISOU 2718  CA  THR B  34     8142   9805  10948    905   -731    182       C  
ATOM   2719  C   THR B  34     -21.043  15.588   5.183  1.00 75.11           C  
ANISOU 2719  C   THR B  34     8051   9601  10885    866   -709    214       C  
ATOM   2720  O   THR B  34     -21.895  16.416   5.543  1.00 75.66           O  
ANISOU 2720  O   THR B  34     8158   9660  10929    943   -733    223       O  
ATOM   2721  CB  THR B  34     -20.880  15.945   2.686  1.00 76.18           C  
ANISOU 2721  CB  THR B  34     8281   9799  10864    968   -720    244       C  
ATOM   2722  OG1 THR B  34     -21.373  15.444   1.443  1.00 76.30           O  
ANISOU 2722  OG1 THR B  34     8271   9906  10813   1030   -757    207       O  
ATOM   2723  CG2 THR B  34     -19.395  16.209   2.571  1.00 75.93           C  
ANISOU 2723  CG2 THR B  34     8320   9690  10840    882   -654    307       C  
ATOM   2724  N   TYR B  35     -19.982  15.235   5.919  1.00 73.84           N  
ANISOU 2724  N   TYR B  35     7876   9385  10794    756   -665    231       N  
ATOM   2725  CA  TYR B  35     -19.751  15.678   7.321  1.00 73.01           C  
ANISOU 2725  CA  TYR B  35     7787   9205  10745    704   -647    252       C  
ATOM   2726  C   TYR B  35     -18.326  16.230   7.491  1.00 75.54           C  
ANISOU 2726  C   TYR B  35     8184   9443  11073    618   -596    319       C  
ATOM   2727  O   TYR B  35     -17.371  15.724   6.855  1.00 75.48           O  
ANISOU 2727  O   TYR B  35     8162   9448  11067    564   -567    333       O  
ATOM   2728  CB  TYR B  35     -20.015  14.529   8.297  1.00 70.81           C  
ANISOU 2728  CB  TYR B  35     7389   8958  10556    650   -653    195       C  
ATOM   2729  CG  TYR B  35     -21.350  13.847   8.118  1.00 70.18           C  
ANISOU 2729  CG  TYR B  35     7220   8965  10478    714   -698    124       C  
ATOM   2730  CD1 TYR B  35     -22.427  14.148   8.939  1.00 69.86           C  
ANISOU 2730  CD1 TYR B  35     7156   8933  10453    762   -723    101       C  
ATOM   2731  CD2 TYR B  35     -21.537  12.889   7.133  1.00 69.45           C  
ANISOU 2731  CD2 TYR B  35     7064   8951  10371    721   -715     78       C  
ATOM   2732  CE1 TYR B  35     -23.659  13.535   8.773  1.00 69.60           C  
ANISOU 2732  CE1 TYR B  35     7031   8990  10424    815   -763     36       C  
ATOM   2733  CE2 TYR B  35     -22.752  12.246   6.972  1.00 69.44           C  
ANISOU 2733  CE2 TYR B  35     6976   9035  10373    766   -758      8       C  
ATOM   2734  CZ  TYR B  35     -23.819  12.570   7.793  1.00 69.88           C  
ANISOU 2734  CZ  TYR B  35     6999   9104  10446    811   -783    -12       C  
ATOM   2735  OH  TYR B  35     -25.030  11.955   7.642  1.00 69.07           O  
ANISOU 2735  OH  TYR B  35     6800   9093  10348    850   -825    -81       O  
ATOM   2736  N   LEU B  36     -18.200  17.246   8.350  1.00 77.24           N  
ANISOU 2736  N   LEU B  36     8478   9577  11291    603   -584    357       N  
ATOM   2737  CA  LEU B  36     -16.932  17.934   8.702  1.00 78.92           C  
ANISOU 2737  CA  LEU B  36     8768   9705  11511    511   -539    417       C  
ATOM   2738  C   LEU B  36     -16.771  17.896  10.224  1.00 78.89           C  
ANISOU 2738  C   LEU B  36     8739   9659  11576    442   -537    408       C  
ATOM   2739  O   LEU B  36     -17.328  18.780  10.901  1.00 76.34           O  
ANISOU 2739  O   LEU B  36     8487   9282  11238    477   -546    416       O  
ATOM   2740  CB  LEU B  36     -16.995  19.372   8.178  1.00 81.77           C  
ANISOU 2740  CB  LEU B  36     9277   9999  11790    565   -527    472       C  
ATOM   2741  CG  LEU B  36     -15.839  20.288   8.592  1.00 83.19           C  
ANISOU 2741  CG  LEU B  36     9555  10081  11971    469   -482    533       C  
ATOM   2742  CD1 LEU B  36     -14.487  19.632   8.335  1.00 83.12           C  
ANISOU 2742  CD1 LEU B  36     9490  10091  11999    359   -446    552       C  
ATOM   2743  CD2 LEU B  36     -15.924  21.627   7.872  1.00 84.16           C  
ANISOU 2743  CD2 LEU B  36     9834  10136  12006    528   -462    588       C  
ATOM   2744  N   ASP B  37     -16.048  16.892  10.730  1.00 80.11           N  
ANISOU 2744  N   ASP B  37     8800   9839  11799    356   -525    392       N  
ATOM   2745  CA  ASP B  37     -15.930  16.592  12.182  1.00 80.67           C  
ANISOU 2745  CA  ASP B  37     8826   9886  11937    294   -527    376       C  
ATOM   2746  C   ASP B  37     -17.343  16.564  12.781  1.00 80.86           C  
ANISOU 2746  C   ASP B  37     8829   9926  11967    373   -560    330       C  
ATOM   2747  O   ASP B  37     -17.599  17.325  13.730  1.00 80.30           O  
ANISOU 2747  O   ASP B  37     8818   9796  11896    374   -563    340       O  
ATOM   2748  CB  ASP B  37     -15.006  17.595  12.888  1.00 81.67           C  
ANISOU 2748  CB  ASP B  37     9040   9927  12061    214   -505    427       C  
ATOM   2749  CG  ASP B  37     -13.608  17.669  12.301  1.00 83.07           C  
ANISOU 2749  CG  ASP B  37     9231  10097  12234    130   -469    475       C  
ATOM   2750  OD1 ASP B  37     -13.084  16.607  11.912  1.00 84.09           O  
ANISOU 2750  OD1 ASP B  37     9266  10287  12395    103   -458    464       O  
ATOM   2751  OD2 ASP B  37     -13.053  18.790  12.232  1.00 84.93           O  
ANISOU 2751  OD2 ASP B  37     9572  10265  12433     92   -448    522       O  
ATOM   2752  N   GLY B  38     -18.233  15.733  12.217  1.00 80.87           N  
ANISOU 2752  N   GLY B  38     8750  10004  11970    437   -584    281       N  
ATOM   2753  CA  GLY B  38     -19.583  15.451  12.752  1.00 79.69           C  
ANISOU 2753  CA  GLY B  38     8548   9892  11838    503   -613    229       C  
ATOM   2754  C   GLY B  38     -20.643  16.356  12.148  1.00 79.72           C  
ANISOU 2754  C   GLY B  38     8611   9906  11771    620   -639    231       C  
ATOM   2755  O   GLY B  38     -21.706  15.824  11.755  1.00 79.49           O  
ANISOU 2755  O   GLY B  38     8509   9955  11737    688   -670    183       O  
ATOM   2756  N   ALA B  39     -20.357  17.666  12.077  1.00 79.17           N  
ANISOU 2756  N   ALA B  39     8670   9760  11648    641   -626    285       N  
ATOM   2757  CA  ALA B  39     -21.223  18.734  11.524  1.00 78.61           C  
ANISOU 2757  CA  ALA B  39     8686   9680  11500    759   -643    303       C  
ATOM   2758  C   ALA B  39     -21.747  18.328  10.145  1.00 77.99           C  
ANISOU 2758  C   ALA B  39     8566   9691  11374    835   -671    283       C  
ATOM   2759  O   ALA B  39     -20.927  18.127   9.230  1.00 79.68           O  
ANISOU 2759  O   ALA B  39     8795   9911  11566    799   -656    305       O  
ATOM   2760  CB  ALA B  39     -20.467  20.038  11.468  1.00 79.39           C  
ANISOU 2760  CB  ALA B  39     8938   9674  11551    742   -612    370       C  
ATOM   2761  N   ASP B  40     -23.070  18.207  10.016  1.00 76.27           N  
ANISOU 2761  N   ASP B  40     8295   9545  11139    936   -710    243       N  
ATOM   2762  CA  ASP B  40     -23.752  17.844   8.749  1.00 75.50           C  
ANISOU 2762  CA  ASP B  40     8151   9546  10989   1018   -748    216       C  
ATOM   2763  C   ASP B  40     -23.681  19.044   7.798  1.00 75.49           C  
ANISOU 2763  C   ASP B  40     8284   9510  10889   1104   -746    275       C  
ATOM   2764  O   ASP B  40     -24.418  20.023   8.023  1.00 75.60           O  
ANISOU 2764  O   ASP B  40     8366   9498  10859   1202   -755    296       O  
ATOM   2765  CB  ASP B  40     -25.194  17.403   9.013  1.00 75.37           C  
ANISOU 2765  CB  ASP B  40     8028   9622  10985   1094   -792    155       C  
ATOM   2766  CG  ASP B  40     -25.894  16.856   7.783  1.00 75.51           C  
ANISOU 2766  CG  ASP B  40     7976   9755  10956   1160   -839    114       C  
ATOM   2767  OD1 ASP B  40     -25.484  17.229   6.661  1.00 76.35           O  
ANISOU 2767  OD1 ASP B  40     8154   9863  10992   1192   -841    147       O  
ATOM   2768  OD2 ASP B  40     -26.832  16.047   7.957  1.00 74.28           O  
ANISOU 2768  OD2 ASP B  40     7698   9691  10834   1173   -871     49       O  
ATOM   2769  N   VAL B  41     -22.840  18.958   6.766  1.00 75.35           N  
ANISOU 2769  N   VAL B  41     8304   9489  10833   1074   -731    302       N  
ATOM   2770  CA  VAL B  41     -22.598  20.059   5.788  1.00 77.96           C  
ANISOU 2770  CA  VAL B  41     8774   9778  11068   1143   -718    365       C  
ATOM   2771  C   VAL B  41     -23.163  19.654   4.418  1.00 80.20           C  
ANISOU 2771  C   VAL B  41     9022  10168  11283   1228   -759    342       C  
ATOM   2772  O   VAL B  41     -22.676  20.188   3.405  1.00 80.93           O  
ANISOU 2772  O   VAL B  41     9210  10239  11300   1257   -742    390       O  
ATOM   2773  CB  VAL B  41     -21.102  20.438   5.721  1.00 77.92           C  
ANISOU 2773  CB  VAL B  41     8859   9677  11067   1036   -659    424       C  
ATOM   2774  CG1 VAL B  41     -20.572  20.874   7.078  1.00 77.09           C  
ANISOU 2774  CG1 VAL B  41     8791   9474  11023    950   -626    444       C  
ATOM   2775  CG2 VAL B  41     -20.235  19.331   5.141  1.00 77.35           C  
ANISOU 2775  CG2 VAL B  41     8709   9653  11027    948   -645    406       C  
ATOM   2776  N   THR B  42     -24.195  18.799   4.393  1.00 82.81           N  
ANISOU 2776  N   THR B  42     9222  10608  11631   1269   -812    270       N  
ATOM   2777  CA  THR B  42     -24.924  18.358   3.167  1.00 84.18           C  
ANISOU 2777  CA  THR B  42     9346  10900  11738   1353   -864    234       C  
ATOM   2778  C   THR B  42     -25.575  19.563   2.474  1.00 85.73           C  
ANISOU 2778  C   THR B  42     9647  11100  11826   1503   -887    281       C  
ATOM   2779  O   THR B  42     -25.572  19.585   1.226  1.00 84.22           O  
ANISOU 2779  O   THR B  42     9487  10959  11550   1560   -906    290       O  
ATOM   2780  CB  THR B  42     -25.987  17.294   3.480  1.00 83.54           C  
ANISOU 2780  CB  THR B  42     9103  10931  11706   1358   -916    145       C  
ATOM   2781  OG1 THR B  42     -25.384  16.273   4.275  1.00 82.48           O  
ANISOU 2781  OG1 THR B  42     8889  10775  11674   1224   -886    109       O  
ATOM   2782  CG2 THR B  42     -26.589  16.668   2.240  1.00 83.83           C  
ANISOU 2782  CG2 THR B  42     9077  11093  11682   1413   -971     96       C  
ATOM   2783  N   LYS B  43     -26.084  20.519   3.261  1.00 88.06           N  
ANISOU 2783  N   LYS B  43    10000  11340  12117   1567   -881    311       N  
ATOM   2784  CA  LYS B  43     -26.965  21.632   2.825  1.00 89.90           C  
ANISOU 2784  CA  LYS B  43    10318  11583  12254   1732   -906    350       C  
ATOM   2785  C   LYS B  43     -26.178  22.937   2.600  1.00 91.03           C  
ANISOU 2785  C   LYS B  43    10658  11592  12336   1752   -849    443       C  
ATOM   2786  O   LYS B  43     -26.758  23.850   1.981  1.00 94.45           O  
ANISOU 2786  O   LYS B  43    11183  12028  12672   1895   -864    485       O  
ATOM   2787  CB  LYS B  43     -28.038  21.854   3.891  1.00 90.11           C  
ANISOU 2787  CB  LYS B  43    10289  11629  12318   1795   -926    325       C  
ATOM   2788  CG  LYS B  43     -29.352  21.115   3.675  1.00 90.84           C  
ANISOU 2788  CG  LYS B  43    10221  11881  12409   1869   -997    252       C  
ATOM   2789  CD  LYS B  43     -30.428  21.602   4.622  1.00 91.24           C  
ANISOU 2789  CD  LYS B  43    10241  11946  12478   1958  -1008    245       C  
ATOM   2790  CE  LYS B  43     -31.789  21.784   3.978  1.00 91.71           C  
ANISOU 2790  CE  LYS B  43    10236  12142  12464   2122  -1076    225       C  
ATOM   2791  NZ  LYS B  43     -32.725  22.454   4.939  1.00 92.13           N  
ANISOU 2791  NZ  LYS B  43    10284  12190  12529   2220  -1071    234       N  
ATOM   2792  N   ILE B  44     -24.944  23.052   3.109  1.00 89.87           N  
ANISOU 2792  N   ILE B  44    10573  11331  12239   1619   -787    475       N  
ATOM   2793  CA  ILE B  44     -24.105  24.278   2.946  1.00 89.22           C  
ANISOU 2793  CA  ILE B  44    10679  11112  12106   1612   -727    561       C  
ATOM   2794  C   ILE B  44     -23.193  24.079   1.727  1.00 89.86           C  
ANISOU 2794  C   ILE B  44    10803  11200  12140   1572   -704    590       C  
ATOM   2795  O   ILE B  44     -23.032  22.928   1.274  1.00 85.50           O  
ANISOU 2795  O   ILE B  44    10131  10739  11615   1521   -727    541       O  
ATOM   2796  CB  ILE B  44     -23.330  24.646   4.234  1.00 86.87           C  
ANISOU 2796  CB  ILE B  44    10432  10690  11885   1492   -674    579       C  
ATOM   2797  CG1 ILE B  44     -21.980  23.938   4.351  1.00 85.67           C  
ANISOU 2797  CG1 ILE B  44    10238  10510  11800   1320   -636    577       C  
ATOM   2798  CG2 ILE B  44     -24.181  24.415   5.472  1.00 85.61           C  
ANISOU 2798  CG2 ILE B  44    10186  10549  11789   1508   -699    531       C  
ATOM   2799  CD1 ILE B  44     -21.182  24.352   5.565  1.00 84.89           C  
ANISOU 2799  CD1 ILE B  44    10191  10297  11766   1202   -590    597       C  
ATOM   2800  N   LYS B  45     -22.653  25.183   1.204  1.00 92.75           N  
ANISOU 2800  N   LYS B  45    11339  11468  12431   1599   -656    669       N  
ATOM   2801  CA  LYS B  45     -21.851  25.218  -0.047  1.00 94.45           C  
ANISOU 2801  CA  LYS B  45    11623  11682  12581   1583   -626    711       C  
ATOM   2802  C   LYS B  45     -20.378  25.331   0.317  1.00 94.92           C  
ANISOU 2802  C   LYS B  45    11732  11636  12695   1418   -551    748       C  
ATOM   2803  O   LYS B  45     -20.042  25.949   1.323  1.00 93.52           O  
ANISOU 2803  O   LYS B  45    11615  11355  12562   1355   -517    770       O  
ATOM   2804  CB  LYS B  45     -22.315  26.362  -0.955  1.00 95.75           C  
ANISOU 2804  CB  LYS B  45    11944  11817  12618   1735   -622    775       C  
ATOM   2805  CG  LYS B  45     -22.272  27.767  -0.362  1.00 95.25           C  
ANISOU 2805  CG  LYS B  45    12052  11608  12528   1767   -573    842       C  
ATOM   2806  CD  LYS B  45     -22.892  28.815  -1.283  1.00 94.67           C  
ANISOU 2806  CD  LYS B  45    12128  11517  12324   1943   -574    903       C  
ATOM   2807  CE  LYS B  45     -22.122  30.148  -1.255  1.00 94.75           C  
ANISOU 2807  CE  LYS B  45    12357  11352  12289   1917   -488    993       C  
ATOM   2808  NZ  LYS B  45     -22.988  31.251  -1.781  1.00 95.44           N  
ANISOU 2808  NZ  LYS B  45    12592  11409  12259   2111   -492   1048       N  
ATOM   2809  N   PRO B  46     -19.461  24.739  -0.482  1.00 96.60           N  
ANISOU 2809  N   PRO B  46    11921  11876  12904   1343   -523    755       N  
ATOM   2810  CA  PRO B  46     -18.032  24.770  -0.162  1.00 98.11           C  
ANISOU 2810  CA  PRO B  46    12139  11987  13150   1184   -453    790       C  
ATOM   2811  C   PRO B  46     -17.559  26.194   0.165  1.00101.59           C  
ANISOU 2811  C   PRO B  46    12758  12281  13561   1162   -393    866       C  
ATOM   2812  O   PRO B  46     -17.648  27.057  -0.687  1.00104.49           O  
ANISOU 2812  O   PRO B  46    13262  12606  13831   1245   -369    923       O  
ATOM   2813  CB  PRO B  46     -17.361  24.207  -1.426  1.00 97.60           C  
ANISOU 2813  CB  PRO B  46    12061  11978  13043   1166   -430    802       C  
ATOM   2814  CG  PRO B  46     -18.432  23.334  -2.062  1.00 97.15           C  
ANISOU 2814  CG  PRO B  46    11900  12057  12952   1274   -506    736       C  
ATOM   2815  CD  PRO B  46     -19.742  24.024  -1.737  1.00 97.30           C  
ANISOU 2815  CD  PRO B  46    11957  12080  12932   1409   -557    730       C  
ATOM   2816  N   HIS B  47     -17.126  26.402   1.411  1.00104.51           N  
ANISOU 2816  N   HIS B  47    13124  12575  14010   1056   -373    862       N  
ATOM   2817  CA  HIS B  47     -16.611  27.690   1.951  1.00107.39           C  
ANISOU 2817  CA  HIS B  47    13649  12790  14361   1005   -316    922       C  
ATOM   2818  C   HIS B  47     -15.107  27.782   1.655  1.00107.36           C  
ANISOU 2818  C   HIS B  47    13680  12735  14374    854   -245    968       C  
ATOM   2819  O   HIS B  47     -14.607  26.942   0.853  1.00108.71           O  
ANISOU 2819  O   HIS B  47    13768  12988  14548    826   -239    961       O  
ATOM   2820  CB  HIS B  47     -16.974  27.805   3.443  1.00109.36           C  
ANISOU 2820  CB  HIS B  47    13870  12998  14682    970   -337    886       C  
ATOM   2821  CG  HIS B  47     -17.079  29.213   3.938  1.00111.72           C  
ANISOU 2821  CG  HIS B  47    14351  13156  14941    991   -301    933       C  
ATOM   2822  ND1 HIS B  47     -17.820  30.181   3.276  1.00112.26           N  
ANISOU 2822  ND1 HIS B  47    14564  13181  14908   1141   -295    976       N  
ATOM   2823  CD2 HIS B  47     -16.551  29.816   5.026  1.00111.17           C  
ANISOU 2823  CD2 HIS B  47    14348  12976  14914    884   -269    942       C  
ATOM   2824  CE1 HIS B  47     -17.735  31.320   3.934  1.00112.12           C  
ANISOU 2824  CE1 HIS B  47    14701  13025  14873   1126   -255   1010       C  
ATOM   2825  NE2 HIS B  47     -16.965  31.123   5.012  1.00112.14           N  
ANISOU 2825  NE2 HIS B  47    14659  12985  14964    965   -240    988       N  
ATOM   2826  N   ASN B  48     -14.420  28.748   2.281  1.00105.01           N  
ANISOU 2826  N   ASN B  48    13499  12309  14087    759   -191   1011       N  
ATOM   2827  CA  ASN B  48     -13.019  29.162   1.993  1.00100.98           C  
ANISOU 2827  CA  ASN B  48    13056  11731  13580    616   -114   1067       C  
ATOM   2828  C   ASN B  48     -12.056  28.343   2.846  1.00 97.23           C  
ANISOU 2828  C   ASN B  48    12438  11290  13214    451   -112   1035       C  
ATOM   2829  O   ASN B  48     -11.090  27.782   2.293  1.00 96.35           O  
ANISOU 2829  O   ASN B  48    12259  11226  13121    368    -78   1050       O  
ATOM   2830  CB  ASN B  48     -12.798  30.641   2.336  1.00100.92           C  
ANISOU 2830  CB  ASN B  48    13249  11563  13531    586    -60   1124       C  
ATOM   2831  CG  ASN B  48     -13.492  31.573   1.350  1.00100.01           C  
ANISOU 2831  CG  ASN B  48    13304  11397  13299    740    -41   1176       C  
ATOM   2832  OD1 ASN B  48     -14.298  32.435   1.736  1.00 97.41           O  
ANISOU 2832  OD1 ASN B  48    13093  10990  12928    834    -49   1186       O  
ATOM   2833  ND2 ASN B  48     -13.215  31.350   0.065  1.00 99.47           N  
ANISOU 2833  ND2 ASN B  48    13243  11379  13172    777    -17   1209       N  
ATOM   2834  N   SER B  49     -12.334  28.305   4.153  1.00 96.27           N  
ANISOU 2834  N   SER B  49    12277  11145  13156    413   -145    995       N  
ATOM   2835  CA  SER B  49     -11.576  27.598   5.219  1.00 96.46           C  
ANISOU 2835  CA  SER B  49    12171  11196  13281    269   -154    960       C  
ATOM   2836  C   SER B  49     -11.364  26.119   4.860  1.00 96.98           C  
ANISOU 2836  C   SER B  49    12051  11398  13397    261   -179    921       C  
ATOM   2837  O   SER B  49     -10.398  25.525   5.387  1.00 98.68           O  
ANISOU 2837  O   SER B  49    12167  11641  13685    134   -167    912       O  
ATOM   2838  CB  SER B  49     -12.303  27.723   6.540  1.00 95.42           C  
ANISOU 2838  CB  SER B  49    12031  11034  13189    285   -198    916       C  
ATOM   2839  OG  SER B  49     -13.335  28.708   6.470  1.00 96.30           O  
ANISOU 2839  OG  SER B  49    12284  11074  13230    412   -204    930       O  
ATOM   2840  N   HIS B  50     -12.262  25.550   4.046  1.00 97.48           N  
ANISOU 2840  N   HIS B  50    12072  11543  13422    394   -215    895       N  
ATOM   2841  CA  HIS B  50     -12.397  24.084   3.817  1.00 95.88           C  
ANISOU 2841  CA  HIS B  50    11698  11466  13264    409   -251    840       C  
ATOM   2842  C   HIS B  50     -11.234  23.551   2.970  1.00 96.39           C  
ANISOU 2842  C   HIS B  50    11718  11573  13332    335   -202    868       C  
ATOM   2843  O   HIS B  50     -10.944  22.342   3.073  1.00 94.00           O  
ANISOU 2843  O   HIS B  50    11272  11354  13088    300   -215    828       O  
ATOM   2844  CB  HIS B  50     -13.753  23.762   3.168  1.00 95.85           C  
ANISOU 2844  CB  HIS B  50    11678  11533  13208    570   -306    802       C  
ATOM   2845  CG  HIS B  50     -14.939  24.044   4.030  1.00 94.92           C  
ANISOU 2845  CG  HIS B  50    11565  11400  13098    648   -356    767       C  
ATOM   2846  ND1 HIS B  50     -16.173  24.357   3.492  1.00 94.39           N  
ANISOU 2846  ND1 HIS B  50    11540  11361  12961    802   -395    757       N  
ATOM   2847  CD2 HIS B  50     -15.092  24.067   5.371  1.00 93.64           C  
ANISOU 2847  CD2 HIS B  50    11373  11204  13002    600   -372    740       C  
ATOM   2848  CE1 HIS B  50     -17.041  24.544   4.463  1.00 93.58           C  
ANISOU 2848  CE1 HIS B  50    11426  11244  12884    846   -430    726       C  
ATOM   2849  NE2 HIS B  50     -16.402  24.379   5.626  1.00 93.23           N  
ANISOU 2849  NE2 HIS B  50    11343  11159  12922    723   -415    715       N  
ATOM   2850  N   GLU B  51     -10.612  24.403   2.147  1.00 99.28           N  
ANISOU 2850  N   GLU B  51    12204  11883  13635    317   -143    934       N  
ATOM   2851  CA  GLU B  51      -9.545  23.993   1.189  1.00102.38           C  
ANISOU 2851  CA  GLU B  51    12567  12315  14016    261    -87    967       C  
ATOM   2852  C   GLU B  51      -8.612  22.981   1.872  1.00102.97           C  
ANISOU 2852  C   GLU B  51    12487  12446  14190    141    -80    943       C  
ATOM   2853  O   GLU B  51      -8.003  23.331   2.896  1.00102.79           O  
ANISOU 2853  O   GLU B  51    12458  12374  14223     30    -69    953       O  
ATOM   2854  CB  GLU B  51      -8.789  25.218   0.670  1.00104.27           C  
ANISOU 2854  CB  GLU B  51    12959  12459  14198    209    -12   1048       C  
ATOM   2855  CG  GLU B  51      -7.812  24.903  -0.451  1.00105.51           C  
ANISOU 2855  CG  GLU B  51    13101  12658  14328    171     51   1088       C  
ATOM   2856  CD  GLU B  51      -8.052  25.630  -1.769  1.00107.32           C  
ANISOU 2856  CD  GLU B  51    13476  12856  14443    264     89   1141       C  
ATOM   2857  OE1 GLU B  51      -8.385  26.838  -1.747  1.00108.24           O  
ANISOU 2857  OE1 GLU B  51    13750  12871  14504    293    105   1182       O  
ATOM   2858  OE2 GLU B  51      -7.868  24.991  -2.824  1.00108.18           O  
ANISOU 2858  OE2 GLU B  51    13549  13039  14515    307    107   1143       O  
ATOM   2859  N   GLY B  52      -8.541  21.761   1.331  1.00103.05           N  
ANISOU 2859  N   GLY B  52    12380  12555  14216    168    -89    909       N  
ATOM   2860  CA  GLY B  52      -7.609  20.699   1.760  1.00101.01           C  
ANISOU 2860  CA  GLY B  52    11978  12359  14041     74    -74    892       C  
ATOM   2861  C   GLY B  52      -7.975  20.108   3.111  1.00 98.79           C  
ANISOU 2861  C   GLY B  52    11598  12092  13844     47   -127    837       C  
ATOM   2862  O   GLY B  52      -7.060  19.600   3.783  1.00 99.31           O  
ANISOU 2862  O   GLY B  52    11571  12180  13981    -51   -111    839       O  
ATOM   2863  N   LYS B  53      -9.255  20.164   3.498  1.00 97.30           N  
ANISOU 2863  N   LYS B  53    11425  11897  13645    136   -188    793       N  
ATOM   2864  CA  LYS B  53      -9.791  19.478   4.710  1.00 95.02           C  
ANISOU 2864  CA  LYS B  53    11040  11631  13431    129   -239    734       C  
ATOM   2865  C   LYS B  53     -10.399  18.124   4.315  1.00 92.13           C  
ANISOU 2865  C   LYS B  53    10564  11360  13081    197   -272    672       C  
ATOM   2866  O   LYS B  53     -10.710  17.932   3.123  1.00 89.46           O  
ANISOU 2866  O   LYS B  53    10247  11061  12681    271   -269    668       O  
ATOM   2867  CB  LYS B  53     -10.832  20.339   5.439  1.00 95.43           C  
ANISOU 2867  CB  LYS B  53    11172  11621  13466    180   -280    722       C  
ATOM   2868  CG  LYS B  53     -10.274  21.354   6.429  1.00 96.47           C  
ANISOU 2868  CG  LYS B  53    11377  11659  13617     87   -261    757       C  
ATOM   2869  CD  LYS B  53     -11.280  21.778   7.490  1.00 97.05           C  
ANISOU 2869  CD  LYS B  53    11484  11689  13702    129   -306    725       C  
ATOM   2870  CE  LYS B  53     -10.912  23.078   8.176  1.00 98.38           C  
ANISOU 2870  CE  LYS B  53    11778  11745  13856     63   -284    764       C  
ATOM   2871  NZ  LYS B  53      -9.579  23.007   8.836  1.00 99.10           N  
ANISOU 2871  NZ  LYS B  53    11826  11824  14003    -91   -256    785       N  
ATOM   2872  N   THR B  54     -10.567  17.232   5.297  1.00 89.10           N  
ANISOU 2872  N   THR B  54    10073  11007  12773    170   -300    625       N  
ATOM   2873  CA  THR B  54     -11.103  15.855   5.134  1.00 86.38           C  
ANISOU 2873  CA  THR B  54     9618  10742  12458    214   -327    560       C  
ATOM   2874  C   THR B  54     -12.580  15.833   5.542  1.00 83.55           C  
ANISOU 2874  C   THR B  54     9255  10392  12095    297   -388    505       C  
ATOM   2875  O   THR B  54     -12.886  16.286   6.655  1.00 81.53           O  
ANISOU 2875  O   THR B  54     9011  10093  11872    277   -407    503       O  
ATOM   2876  CB  THR B  54     -10.268  14.842   5.926  1.00 86.09           C  
ANISOU 2876  CB  THR B  54     9470  10733  12507    131   -310    549       C  
ATOM   2877  OG1 THR B  54      -8.930  14.907   5.431  1.00 85.47           O  
ANISOU 2877  OG1 THR B  54     9391  10656  12425     65   -252    602       O  
ATOM   2878  CG2 THR B  54     -10.794  13.427   5.818  1.00 86.15           C  
ANISOU 2878  CG2 THR B  54     9377  10807  12547    170   -329    483       C  
ATOM   2879  N   PHE B  55     -13.445  15.320   4.661  1.00 82.53           N  
ANISOU 2879  N   PHE B  55     9107  10324  11926    384   -416    462       N  
ATOM   2880  CA  PHE B  55     -14.922  15.266   4.816  1.00 82.74           C  
ANISOU 2880  CA  PHE B  55     9119  10380  11938    473   -475    408       C  
ATOM   2881  C   PHE B  55     -15.390  13.806   4.761  1.00 81.95           C  
ANISOU 2881  C   PHE B  55     8900  10356  11879    480   -497    334       C  
ATOM   2882  O   PHE B  55     -15.124  13.131   3.739  1.00 84.34           O  
ANISOU 2882  O   PHE B  55     9182  10707  12154    491   -484    319       O  
ATOM   2883  CB  PHE B  55     -15.595  16.071   3.698  1.00 84.09           C  
ANISOU 2883  CB  PHE B  55     9380  10559  12008    575   -493    424       C  
ATOM   2884  CG  PHE B  55     -15.464  17.572   3.803  1.00 84.94           C  
ANISOU 2884  CG  PHE B  55     9620  10583  12069    590   -476    490       C  
ATOM   2885  CD1 PHE B  55     -16.311  18.304   4.628  1.00 84.68           C  
ANISOU 2885  CD1 PHE B  55     9625  10511  12037    633   -506    486       C  
ATOM   2886  CD2 PHE B  55     -14.529  18.260   3.044  1.00 85.25           C  
ANISOU 2886  CD2 PHE B  55     9752  10579  12057    565   -426    556       C  
ATOM   2887  CE1 PHE B  55     -16.203  19.685   4.714  1.00 84.42           C  
ANISOU 2887  CE1 PHE B  55     9727  10390  11956    650   -486    544       C  
ATOM   2888  CE2 PHE B  55     -14.419  19.640   3.139  1.00 86.08           C  
ANISOU 2888  CE2 PHE B  55     9989  10597  12117    573   -405    615       C  
ATOM   2889  CZ  PHE B  55     -15.258  20.350   3.970  1.00 84.99           C  
ANISOU 2889  CZ  PHE B  55     9896  10415  11981    617   -436    609       C  
ATOM   2890  N   TYR B  56     -16.073  13.332   5.808  1.00 80.24           N  
ANISOU 2890  N   TYR B  56     8614  10149  11724    472   -526    288       N  
ATOM   2891  CA  TYR B  56     -16.754  12.010   5.822  1.00 79.81           C  
ANISOU 2891  CA  TYR B  56     8454  10160  11706    482   -550    211       C  
ATOM   2892  C   TYR B  56     -17.931  12.061   4.844  1.00 79.42           C  
ANISOU 2892  C   TYR B  56     8411  10174  11588    579   -597    170       C  
ATOM   2893  O   TYR B  56     -18.704  13.027   4.905  1.00 77.38           O  
ANISOU 2893  O   TYR B  56     8205   9908  11289    646   -628    183       O  
ATOM   2894  CB  TYR B  56     -17.246  11.633   7.224  1.00 80.18           C  
ANISOU 2894  CB  TYR B  56     8438  10195  11831    452   -564    179       C  
ATOM   2895  CG  TYR B  56     -16.212  10.981   8.113  1.00 81.14           C  
ANISOU 2895  CG  TYR B  56     8513  10288  12029    359   -525    193       C  
ATOM   2896  CD1 TYR B  56     -16.014   9.608   8.107  1.00 81.15           C  
ANISOU 2896  CD1 TYR B  56     8430  10324  12076    327   -509    152       C  
ATOM   2897  CD2 TYR B  56     -15.440  11.736   8.984  1.00 81.94           C  
ANISOU 2897  CD2 TYR B  56     8655  10326  12151    305   -505    248       C  
ATOM   2898  CE1 TYR B  56     -15.057   9.004   8.909  1.00 80.90           C  
ANISOU 2898  CE1 TYR B  56     8357  10269  12109    255   -473    170       C  
ATOM   2899  CE2 TYR B  56     -14.481  11.151   9.796  1.00 81.36           C  
ANISOU 2899  CE2 TYR B  56     8534  10236  12141    225   -475    263       C  
ATOM   2900  CZ  TYR B  56     -14.274   9.782   9.744  1.00 80.70           C  
ANISOU 2900  CZ  TYR B  56     8367  10193  12103    205   -459    227       C  
ATOM   2901  OH  TYR B  56     -13.345   9.192  10.548  1.00 77.85           O  
ANISOU 2901  OH  TYR B  56     7958   9819  11800    139   -430    246       O  
ATOM   2902  N   VAL B  57     -18.050  11.061   3.966  1.00 80.88           N  
ANISOU 2902  N   VAL B  57     8548  10422  11757    588   -603    121       N  
ATOM   2903  CA  VAL B  57     -19.209  10.891   3.036  1.00 82.86           C  
ANISOU 2903  CA  VAL B  57     8785  10753  11946    671   -656     67       C  
ATOM   2904  C   VAL B  57     -19.827   9.511   3.272  1.00 83.74           C  
ANISOU 2904  C   VAL B  57     8786  10919  12110    642   -675    -19       C  
ATOM   2905  O   VAL B  57     -19.213   8.695   3.974  1.00 83.47           O  
ANISOU 2905  O   VAL B  57     8704  10856  12152    566   -638    -28       O  
ATOM   2906  CB  VAL B  57     -18.817  11.073   1.557  1.00 84.20           C  
ANISOU 2906  CB  VAL B  57     9018  10948  12023    712   -648     87       C  
ATOM   2907  CG1 VAL B  57     -18.217  12.448   1.308  1.00 85.45           C  
ANISOU 2907  CG1 VAL B  57     9293  11045  12127    737   -623    176       C  
ATOM   2908  CG2 VAL B  57     -17.890   9.967   1.058  1.00 83.99           C  
ANISOU 2908  CG2 VAL B  57     8961  10933  12017    653   -604     70       C  
ATOM   2909  N   LEU B  58     -21.011   9.284   2.706  1.00 86.76           N  
ANISOU 2909  N   LEU B  58     9132  11379  12452    702   -731    -80       N  
ATOM   2910  CA  LEU B  58     -21.749   7.999   2.810  1.00 87.15           C  
ANISOU 2910  CA  LEU B  58     9079  11488  12544    673   -753   -172       C  
ATOM   2911  C   LEU B  58     -21.224   7.081   1.715  1.00 85.36           C  
ANISOU 2911  C   LEU B  58     8855  11290  12285    651   -736   -204       C  
ATOM   2912  O   LEU B  58     -20.900   7.550   0.622  1.00 84.62           O  
ANISOU 2912  O   LEU B  58     8830  11212  12109    697   -738   -176       O  
ATOM   2913  CB  LEU B  58     -23.255   8.245   2.651  1.00 89.49           C  
ANISOU 2913  CB  LEU B  58     9331  11864  12805    745   -824   -222       C  
ATOM   2914  CG  LEU B  58     -24.151   7.322   3.479  1.00 91.28           C  
ANISOU 2914  CG  LEU B  58     9447  12126  13106    703   -841   -298       C  
ATOM   2915  CD1 LEU B  58     -24.272   7.836   4.911  1.00 91.01           C  
ANISOU 2915  CD1 LEU B  58     9403  12036  13139    689   -824   -263       C  
ATOM   2916  CD2 LEU B  58     -25.535   7.173   2.850  1.00 92.62           C  
ANISOU 2916  CD2 LEU B  58     9554  12406  13228    760   -912   -368       C  
ATOM   2917  N   PRO B  59     -21.086   5.762   1.978  1.00 83.73           N  
ANISOU 2917  N   PRO B  59     8586  11087  12142    582   -712   -261       N  
ATOM   2918  CA  PRO B  59     -20.865   4.802   0.899  1.00 84.92           C  
ANISOU 2918  CA  PRO B  59     8736  11273  12255    570   -703   -311       C  
ATOM   2919  C   PRO B  59     -21.865   5.023  -0.252  1.00 86.70           C  
ANISOU 2919  C   PRO B  59     8967  11588  12384    641   -772   -359       C  
ATOM   2920  O   PRO B  59     -23.008   4.637  -0.108  1.00 86.41           O  
ANISOU 2920  O   PRO B  59     8861  11612  12358    645   -822   -429       O  
ATOM   2921  CB  PRO B  59     -21.068   3.452   1.604  1.00 84.72           C  
ANISOU 2921  CB  PRO B  59     8632  11240  12316    496   -683   -379       C  
ATOM   2922  CG  PRO B  59     -20.666   3.712   3.044  1.00 83.47           C  
ANISOU 2922  CG  PRO B  59     8456  11013  12243    457   -649   -328       C  
ATOM   2923  CD  PRO B  59     -21.086   5.141   3.312  1.00 82.78           C  
ANISOU 2923  CD  PRO B  59     8402  10925  12123    516   -686   -276       C  
ATOM   2924  N   ASN B  60     -21.422   5.673  -1.339  1.00 88.99           N  
ANISOU 2924  N   ASN B  60     9340  11890  12583    697   -772   -316       N  
ATOM   2925  CA  ASN B  60     -22.215   5.894  -2.583  1.00 91.00           C  
ANISOU 2925  CA  ASN B  60     9614  12233  12729    773   -835   -354       C  
ATOM   2926  C   ASN B  60     -21.464   5.321  -3.801  1.00 94.09           C  
ANISOU 2926  C   ASN B  60    10059  12633  13056    769   -805   -365       C  
ATOM   2927  O   ASN B  60     -21.784   5.731  -4.932  1.00 95.93           O  
ANISOU 2927  O   ASN B  60    10341  12924  13182    840   -844   -369       O  
ATOM   2928  CB  ASN B  60     -22.597   7.369  -2.757  1.00 90.44           C  
ANISOU 2928  CB  ASN B  60     9602  12170  12589    868   -871   -288       C  
ATOM   2929  CG  ASN B  60     -21.426   8.289  -3.046  1.00 88.86           C  
ANISOU 2929  CG  ASN B  60     9510  11897  12353    884   -815   -187       C  
ATOM   2930  OD1 ASN B  60     -20.926   8.335  -4.167  1.00 88.22           O  
ANISOU 2930  OD1 ASN B  60     9496  11831  12194    912   -800   -170       O  
ATOM   2931  ND2 ASN B  60     -21.008   9.059  -2.055  1.00 87.44           N  
ANISOU 2931  ND2 ASN B  60     9353  11641  12226    866   -784   -119       N  
ATOM   2932  N   ASP B  61     -20.512   4.405  -3.575  1.00 95.26           N  
ANISOU 2932  N   ASP B  61    10201  12728  13263    695   -736   -370       N  
ATOM   2933  CA  ASP B  61     -19.881   3.551  -4.618  1.00 97.26           C  
ANISOU 2933  CA  ASP B  61    10491  12992  13471    682   -701   -401       C  
ATOM   2934  C   ASP B  61     -19.200   2.353  -3.931  1.00 96.79           C  
ANISOU 2934  C   ASP B  61    10391  12877  13509    596   -635   -425       C  
ATOM   2935  O   ASP B  61     -19.187   2.314  -2.675  1.00 95.19           O  
ANISOU 2935  O   ASP B  61    10137  12630  13401    553   -620   -408       O  
ATOM   2936  CB  ASP B  61     -18.944   4.360  -5.527  1.00 98.65           C  
ANISOU 2936  CB  ASP B  61    10766  13149  13564    731   -663   -320       C  
ATOM   2937  CG  ASP B  61     -17.580   4.697  -4.942  1.00 99.14           C  
ANISOU 2937  CG  ASP B  61    10857  13126  13683    692   -579   -227       C  
ATOM   2938  OD1 ASP B  61     -17.486   4.854  -3.709  1.00101.62           O  
ANISOU 2938  OD1 ASP B  61    11127  13394  14087    650   -568   -201       O  
ATOM   2939  OD2 ASP B  61     -16.618   4.803  -5.729  1.00 97.74           O  
ANISOU 2939  OD2 ASP B  61    10744  12934  13456    703   -525   -182       O  
ATOM   2940  N   ASP B  62     -18.665   1.413  -4.722  1.00 96.80           N  
ANISOU 2940  N   ASP B  62    10419  12879  13482    579   -595   -462       N  
ATOM   2941  CA  ASP B  62     -18.196   0.083  -4.235  1.00 97.48           C  
ANISOU 2941  CA  ASP B  62    10471  12919  13646    509   -536   -504       C  
ATOM   2942  C   ASP B  62     -16.856   0.235  -3.499  1.00 94.71           C  
ANISOU 2942  C   ASP B  62    10129  12492  13363    484   -455   -413       C  
ATOM   2943  O   ASP B  62     -16.645  -0.531  -2.544  1.00 94.42           O  
ANISOU 2943  O   ASP B  62    10044  12411  13417    430   -419   -425       O  
ATOM   2944  CB  ASP B  62     -18.161  -0.976  -5.344  1.00 99.79           C  
ANISOU 2944  CB  ASP B  62    10796  13237  13880    505   -522   -581       C  
ATOM   2945  CG  ASP B  62     -19.239  -2.054  -5.246  1.00101.14           C  
ANISOU 2945  CG  ASP B  62    10913  13439  14074    457   -563   -700       C  
ATOM   2946  OD1 ASP B  62     -20.010  -2.052  -4.260  1.00100.24           O  
ANISOU 2946  OD1 ASP B  62    10729  13328  14031    425   -597   -721       O  
ATOM   2947  OD2 ASP B  62     -19.292  -2.898  -6.157  1.00101.25           O  
ANISOU 2947  OD2 ASP B  62    10961  13473  14035    449   -558   -771       O  
ATOM   2948  N   THR B  63     -15.996   1.170  -3.902  1.00 93.11           N  
ANISOU 2948  N   THR B  63     9983  12277  13118    518   -425   -325       N  
ATOM   2949  CA  THR B  63     -14.713   1.458  -3.195  1.00 91.88           C  
ANISOU 2949  CA  THR B  63     9827  12059  13021    489   -354   -233       C  
ATOM   2950  C   THR B  63     -15.024   1.789  -1.726  1.00 89.98           C  
ANISOU 2950  C   THR B  63     9528  11786  12871    453   -374   -213       C  
ATOM   2951  O   THR B  63     -14.425   1.149  -0.837  1.00 87.85           O  
ANISOU 2951  O   THR B  63     9218  11475  12685    405   -328   -201       O  
ATOM   2952  CB  THR B  63     -13.880   2.525  -3.925  1.00 91.65           C  
ANISOU 2952  CB  THR B  63     9869  12028  12924    526   -325   -146       C  
ATOM   2953  OG1 THR B  63     -12.546   2.447  -3.422  1.00 90.54           O  
ANISOU 2953  OG1 THR B  63     9718  11842  12841    489   -247    -76       O  
ATOM   2954  CG2 THR B  63     -14.375   3.949  -3.778  1.00 91.88           C  
ANISOU 2954  CG2 THR B  63     9927  12061  12920    560   -375    -97       C  
ATOM   2955  N   LEU B  64     -15.976   2.699  -1.494  1.00 89.38           N  
ANISOU 2955  N   LEU B  64     9451  11732  12777    480   -442   -213       N  
ATOM   2956  CA  LEU B  64     -16.339   3.242  -0.153  1.00 87.23           C  
ANISOU 2956  CA  LEU B  64     9137  11430  12575    457   -464   -188       C  
ATOM   2957  C   LEU B  64     -17.214   2.244   0.616  1.00 84.64           C  
ANISOU 2957  C   LEU B  64     8734  11110  12316    420   -486   -268       C  
ATOM   2958  O   LEU B  64     -17.244   2.330   1.856  1.00 81.08           O  
ANISOU 2958  O   LEU B  64     8244  10622  11940    387   -481   -249       O  
ATOM   2959  CB  LEU B  64     -17.065   4.579  -0.341  1.00 88.96           C  
ANISOU 2959  CB  LEU B  64     9394  11671  12735    514   -522   -161       C  
ATOM   2960  CG  LEU B  64     -16.230   5.683  -0.994  1.00 90.33           C  
ANISOU 2960  CG  LEU B  64     9651  11824  12843    546   -496    -74       C  
ATOM   2961  CD1 LEU B  64     -17.087   6.878  -1.393  1.00 91.22           C  
ANISOU 2961  CD1 LEU B  64     9814  11962  12882    619   -555    -58       C  
ATOM   2962  CD2 LEU B  64     -15.114   6.122  -0.060  1.00 90.61           C  
ANISOU 2962  CD2 LEU B  64     9690  11793  12943    493   -442      4       C  
ATOM   2963  N   ARG B  65     -17.915   1.348  -0.086  1.00 85.21           N  
ANISOU 2963  N   ARG B  65     8789  11226  12358    422   -509   -356       N  
ATOM   2964  CA  ARG B  65     -18.762   0.301   0.544  1.00 85.13           C  
ANISOU 2964  CA  ARG B  65     8711  11223  12411    377   -523   -440       C  
ATOM   2965  C   ARG B  65     -17.846  -0.774   1.141  1.00 82.27           C  
ANISOU 2965  C   ARG B  65     8336  10798  12123    322   -447   -434       C  
ATOM   2966  O   ARG B  65     -18.221  -1.354   2.164  1.00 80.15           O  
ANISOU 2966  O   ARG B  65     8016  10504  11931    278   -440   -462       O  
ATOM   2967  CB  ARG B  65     -19.769  -0.267  -0.462  1.00 87.96           C  
ANISOU 2967  CB  ARG B  65     9061  11651  12709    389   -573   -537       C  
ATOM   2968  CG  ARG B  65     -21.071  -0.728   0.181  1.00 90.37           C  
ANISOU 2968  CG  ARG B  65     9287  11989  13060    356   -620   -615       C  
ATOM   2969  CD  ARG B  65     -22.045  -1.319  -0.824  1.00 94.33           C  
ANISOU 2969  CD  ARG B  65     9772  12567  13500    357   -673   -717       C  
ATOM   2970  NE  ARG B  65     -22.209  -0.453  -1.992  1.00 97.73           N  
ANISOU 2970  NE  ARG B  65    10250  13062  13820    433   -724   -701       N  
ATOM   2971  CZ  ARG B  65     -23.225   0.382  -2.218  1.00 97.89           C  
ANISOU 2971  CZ  ARG B  65    10246  13156  13789    488   -802   -710       C  
ATOM   2972  NH1 ARG B  65     -24.228   0.484  -1.360  1.00 97.39           N  
ANISOU 2972  NH1 ARG B  65    10104  13121  13778    475   -841   -738       N  
ATOM   2973  NH2 ARG B  65     -23.235   1.113  -3.322  1.00 98.96           N  
ANISOU 2973  NH2 ARG B  65    10438  13342  13819    563   -839   -689       N  
ATOM   2974  N   VAL B  66     -16.689  -1.021   0.519  1.00 81.66           N  
ANISOU 2974  N   VAL B  66     8305  10700  12022    329   -389   -398       N  
ATOM   2975  CA  VAL B  66     -15.664  -2.001   0.996  1.00 80.67           C  
ANISOU 2975  CA  VAL B  66     8172  10519  11958    293   -309   -380       C  
ATOM   2976  C   VAL B  66     -14.909  -1.395   2.186  1.00 76.99           C  
ANISOU 2976  C   VAL B  66     7684  10011  11557    276   -285   -292       C  
ATOM   2977  O   VAL B  66     -14.935  -2.014   3.276  1.00 74.31           O  
ANISOU 2977  O   VAL B  66     7302   9635  11295    239   -265   -300       O  
ATOM   2978  CB  VAL B  66     -14.698  -2.416  -0.134  1.00 83.48           C  
ANISOU 2978  CB  VAL B  66     8582  10876  12260    317   -255   -369       C  
ATOM   2979  CG1 VAL B  66     -13.593  -3.331   0.377  1.00 84.43           C  
ANISOU 2979  CG1 VAL B  66     8692  10943  12441    295   -171   -340       C  
ATOM   2980  CG2 VAL B  66     -15.427  -3.064  -1.309  1.00 85.19           C  
ANISOU 2980  CG2 VAL B  66     8827  11133  12406    330   -280   -462       C  
ATOM   2981  N   GLU B  67     -14.269  -0.236   1.979  1.00 75.90           N  
ANISOU 2981  N   GLU B  67     7577   9875  11383    300   -285   -213       N  
ATOM   2982  CA  GLU B  67     -13.472   0.508   2.999  1.00 76.24           C  
ANISOU 2982  CA  GLU B  67     7608   9883  11475    279   -266   -126       C  
ATOM   2983  C   GLU B  67     -14.271   0.618   4.310  1.00 73.34           C  
ANISOU 2983  C   GLU B  67     7195   9498  11171    252   -303   -143       C  
ATOM   2984  O   GLU B  67     -13.683   0.391   5.397  1.00 73.83           O  
ANISOU 2984  O   GLU B  67     7227   9524  11300    218   -273   -107       O  
ATOM   2985  CB  GLU B  67     -13.081   1.896   2.480  1.00 78.16           C  
ANISOU 2985  CB  GLU B  67     7901  10136  11658    304   -279    -58       C  
ATOM   2986  CG  GLU B  67     -11.992   1.888   1.410  1.00 79.92           C  
ANISOU 2986  CG  GLU B  67     8166  10369  11830    321   -225    -17       C  
ATOM   2987  CD  GLU B  67     -11.681   3.239   0.773  1.00 81.66           C  
ANISOU 2987  CD  GLU B  67     8447  10596  11983    346   -233     47       C  
ATOM   2988  OE1 GLU B  67     -12.048   4.279   1.364  1.00 83.37           O  
ANISOU 2988  OE1 GLU B  67     8675  10796  12204    342   -271     78       O  
ATOM   2989  OE2 GLU B  67     -11.061   3.253  -0.313  1.00 82.13           O  
ANISOU 2989  OE2 GLU B  67     8549  10673  11983    369   -195     67       O  
ATOM   2990  N   ALA B  68     -15.561   0.952   4.209  1.00 70.03           N  
ANISOU 2990  N   ALA B  68     6770   9107  10728    271   -365   -194       N  
ATOM   2991  CA  ALA B  68     -16.493   1.103   5.349  1.00 67.39           C  
ANISOU 2991  CA  ALA B  68     6393   8766  10446    255   -401   -216       C  
ATOM   2992  C   ALA B  68     -16.599  -0.222   6.121  1.00 65.53           C  
ANISOU 2992  C   ALA B  68     6108   8504  10284    210   -368   -261       C  
ATOM   2993  O   ALA B  68     -16.325  -0.227   7.333  1.00 63.92           O  
ANISOU 2993  O   ALA B  68     5881   8262  10142    182   -350   -228       O  
ATOM   2994  CB  ALA B  68     -17.840   1.575   4.862  1.00 68.14           C  
ANISOU 2994  CB  ALA B  68     6485   8913  10493    293   -469   -268       C  
ATOM   2995  N   PHE B  69     -16.974  -1.308   5.448  1.00 64.37           N  
ANISOU 2995  N   PHE B  69     5955   8374  10128    202   -358   -335       N  
ATOM   2996  CA  PHE B  69     -17.168  -2.646   6.066  1.00 63.65           C  
ANISOU 2996  CA  PHE B  69     5830   8252  10102    158   -321   -386       C  
ATOM   2997  C   PHE B  69     -15.830  -3.164   6.613  1.00 62.40           C  
ANISOU 2997  C   PHE B  69     5679   8040   9987    144   -249   -326       C  
ATOM   2998  O   PHE B  69     -15.825  -3.761   7.711  1.00 60.90           O  
ANISOU 2998  O   PHE B  69     5462   7812   9866    114   -223   -325       O  
ATOM   2999  CB  PHE B  69     -17.775  -3.642   5.078  1.00 64.34           C  
ANISOU 2999  CB  PHE B  69     5923   8364  10158    150   -323   -479       C  
ATOM   3000  CG  PHE B  69     -17.885  -5.029   5.651  1.00 64.91           C  
ANISOU 3000  CG  PHE B  69     5976   8391  10293    101   -274   -529       C  
ATOM   3001  CD1 PHE B  69     -18.609  -5.253   6.813  1.00 64.19           C  
ANISOU 3001  CD1 PHE B  69     5839   8281  10267     65   -279   -548       C  
ATOM   3002  CD2 PHE B  69     -17.214  -6.096   5.076  1.00 66.05           C  
ANISOU 3002  CD2 PHE B  69     6156   8505  10432     95   -215   -551       C  
ATOM   3003  CE1 PHE B  69     -18.692  -6.520   7.369  1.00 64.39           C  
ANISOU 3003  CE1 PHE B  69     5857   8257  10350     20   -227   -589       C  
ATOM   3004  CE2 PHE B  69     -17.312  -7.369   5.621  1.00 66.41           C  
ANISOU 3004  CE2 PHE B  69     6197   8499  10534     53   -164   -594       C  
ATOM   3005  CZ  PHE B  69     -18.053  -7.579   6.766  1.00 65.59           C  
ANISOU 3005  CZ  PHE B  69     6050   8375  10495     14   -170   -612       C  
ATOM   3006  N   GLU B  70     -14.731  -2.941   5.882  1.00 62.61           N  
ANISOU 3006  N   GLU B  70     5741   8070   9977    169   -218   -276       N  
ATOM   3007  CA  GLU B  70     -13.357  -3.332   6.305  1.00 62.53           C  
ANISOU 3007  CA  GLU B  70     5730   8025  10001    165   -152   -211       C  
ATOM   3008  C   GLU B  70     -13.039  -2.712   7.676  1.00 60.54           C  
ANISOU 3008  C   GLU B  70     5447   7751   9802    144   -160   -146       C  
ATOM   3009  O   GLU B  70     -12.490  -3.432   8.542  1.00 61.15           O  
ANISOU 3009  O   GLU B  70     5502   7796   9936    129   -117   -125       O  
ATOM   3010  CB  GLU B  70     -12.318  -2.879   5.281  1.00 64.03           C  
ANISOU 3010  CB  GLU B  70     5956   8237  10136    195   -126   -159       C  
ATOM   3011  CG  GLU B  70     -12.217  -3.751   4.044  1.00 66.24           C  
ANISOU 3011  CG  GLU B  70     6270   8527  10369    217    -92   -210       C  
ATOM   3012  CD  GLU B  70     -10.834  -3.714   3.404  1.00 68.54           C  
ANISOU 3012  CD  GLU B  70     6584   8824  10634    243    -32   -146       C  
ATOM   3013  OE1 GLU B  70     -10.740  -3.322   2.214  1.00 70.05           O  
ANISOU 3013  OE1 GLU B  70     6816   9045  10751    272    -35   -148       O  
ATOM   3014  OE2 GLU B  70      -9.839  -4.083   4.080  1.00 70.37           O  
ANISOU 3014  OE2 GLU B  70     6789   9034  10914    239     19    -92       O  
ATOM   3015  N   TYR B  71     -13.393  -1.433   7.865  1.00 59.03           N  
ANISOU 3015  N   TYR B  71     5262   7575   9589    148   -212   -118       N  
ATOM   3016  CA  TYR B  71     -13.003  -0.589   9.028  1.00 57.81           C  
ANISOU 3016  CA  TYR B  71     5094   7401   9468    129   -224    -52       C  
ATOM   3017  C   TYR B  71     -14.007  -0.727  10.185  1.00 57.02           C  
ANISOU 3017  C   TYR B  71     4965   7282   9415    109   -250    -86       C  
ATOM   3018  O   TYR B  71     -13.563  -0.799  11.358  1.00 56.43           O  
ANISOU 3018  O   TYR B  71     4870   7180   9390     87   -235    -48       O  
ATOM   3019  CB  TYR B  71     -12.866   0.871   8.585  1.00 57.85           C  
ANISOU 3019  CB  TYR B  71     5137   7423   9420    143   -258     -6       C  
ATOM   3020  CG  TYR B  71     -12.153   1.768   9.568  1.00 56.84           C  
ANISOU 3020  CG  TYR B  71     5008   7272   9314    115   -261     67       C  
ATOM   3021  CD1 TYR B  71     -10.878   1.466  10.010  1.00 55.74           C  
ANISOU 3021  CD1 TYR B  71     4846   7124   9207     91   -218    122       C  
ATOM   3022  CD2 TYR B  71     -12.752   2.921  10.061  1.00 56.56           C  
ANISOU 3022  CD2 TYR B  71     4995   7226   9266    115   -308     80       C  
ATOM   3023  CE1 TYR B  71     -10.220   2.274  10.920  1.00 55.72           C  
ANISOU 3023  CE1 TYR B  71     4839   7107   9222     57   -225    185       C  
ATOM   3024  CE2 TYR B  71     -12.103   3.745  10.965  1.00 55.49           C  
ANISOU 3024  CE2 TYR B  71     4868   7066   9148     83   -311    142       C  
ATOM   3025  CZ  TYR B  71     -10.828   3.421  11.390  1.00 55.79           C  
ANISOU 3025  CZ  TYR B  71     4880   7100   9217     49   -272    192       C  
ATOM   3026  OH  TYR B  71     -10.145   4.200  12.275  1.00 56.62           O  
ANISOU 3026  OH  TYR B  71     4988   7188   9336      9   -279    249       O  
ATOM   3027  N   TYR B  72     -15.314  -0.766   9.875  1.00 56.63           N  
ANISOU 3027  N   TYR B  72     4911   7254   9351    119   -289   -155       N  
ATOM   3028  CA  TYR B  72     -16.433  -0.706  10.859  1.00 54.81           C  
ANISOU 3028  CA  TYR B  72     4649   7017   9156    106   -318   -189       C  
ATOM   3029  C   TYR B  72     -16.966  -2.111  11.186  1.00 54.50           C  
ANISOU 3029  C   TYR B  72     4578   6962   9165     78   -288   -254       C  
ATOM   3030  O   TYR B  72     -17.495  -2.265  12.296  1.00 54.55           O  
ANISOU 3030  O   TYR B  72     4558   6948   9219     58   -287   -262       O  
ATOM   3031  CB  TYR B  72     -17.530   0.242  10.356  1.00 54.52           C  
ANISOU 3031  CB  TYR B  72     4620   7021   9071    138   -380   -217       C  
ATOM   3032  CG  TYR B  72     -17.077   1.681  10.249  1.00 53.92           C  
ANISOU 3032  CG  TYR B  72     4587   6944   8953    163   -405   -149       C  
ATOM   3033  CD1 TYR B  72     -16.930   2.310   9.021  1.00 54.05           C  
ANISOU 3033  CD1 TYR B  72     4645   6989   8900    199   -423   -138       C  
ATOM   3034  CD2 TYR B  72     -16.763   2.411  11.381  1.00 53.10           C  
ANISOU 3034  CD2 TYR B  72     4492   6805   8876    149   -407    -96       C  
ATOM   3035  CE1 TYR B  72     -16.480   3.616   8.915  1.00 53.77           C  
ANISOU 3035  CE1 TYR B  72     4660   6942   8824    218   -437    -73       C  
ATOM   3036  CE2 TYR B  72     -16.329   3.726  11.296  1.00 53.43           C  
ANISOU 3036  CE2 TYR B  72     4584   6836   8879    163   -425    -36       C  
ATOM   3037  CZ  TYR B  72     -16.175   4.330  10.059  1.00 53.54           C  
ANISOU 3037  CZ  TYR B  72     4641   6874   8827    196   -438    -23       C  
ATOM   3038  OH  TYR B  72     -15.727   5.620   9.967  1.00 53.63           O  
ANISOU 3038  OH  TYR B  72     4711   6866   8799    206   -448     36       O  
ATOM   3039  N   HIS B  73     -16.835  -3.091  10.285  1.00 54.73           N  
ANISOU 3039  N   HIS B  73     4615   6996   9181     76   -259   -298       N  
ATOM   3040  CA  HIS B  73     -17.330  -4.487  10.464  1.00 55.52           C  
ANISOU 3040  CA  HIS B  73     4698   7072   9323     43   -223   -366       C  
ATOM   3041  C   HIS B  73     -18.856  -4.496  10.598  1.00 57.50           C  
ANISOU 3041  C   HIS B  73     4913   7353   9581     24   -265   -440       C  
ATOM   3042  O   HIS B  73     -19.380  -5.261  11.449  1.00 58.24           O  
ANISOU 3042  O   HIS B  73     4980   7417   9729    -12   -240   -472       O  
ATOM   3043  CB  HIS B  73     -16.690  -5.154  11.695  1.00 53.92           C  
ANISOU 3043  CB  HIS B  73     4489   6813   9185     23   -168   -327       C  
ATOM   3044  CG  HIS B  73     -15.301  -5.629  11.465  1.00 52.77           C  
ANISOU 3044  CG  HIS B  73     4367   6643   9038     40   -114   -276       C  
ATOM   3045  ND1 HIS B  73     -14.690  -6.515  12.330  1.00 51.64           N  
ANISOU 3045  ND1 HIS B  73     4222   6452   8945     32    -56   -249       N  
ATOM   3046  CD2 HIS B  73     -14.430  -5.368  10.469  1.00 52.40           C  
ANISOU 3046  CD2 HIS B  73     4345   6616   8946     68   -104   -246       C  
ATOM   3047  CE1 HIS B  73     -13.480  -6.764  11.896  1.00 52.00           C  
ANISOU 3047  CE1 HIS B  73     4284   6493   8977     59    -16   -203       C  
ATOM   3048  NE2 HIS B  73     -13.293  -6.070  10.753  1.00 52.66           N  
ANISOU 3048  NE2 HIS B  73     4383   6619   9004     78    -43   -201       N  
ATOM   3049  N   THR B  74     -19.539  -3.655   9.819  1.00 59.23           N  
ANISOU 3049  N   THR B  74     5128   7631   9745     52   -326   -462       N  
ATOM   3050  CA  THR B  74     -21.020  -3.575   9.782  1.00 60.64           C  
ANISOU 3050  CA  THR B  74     5262   7858   9920     43   -375   -533       C  
ATOM   3051  C   THR B  74     -21.476  -3.062   8.415  1.00 62.29           C  
ANISOU 3051  C   THR B  74     5480   8137  10050     80   -431   -567       C  
ATOM   3052  O   THR B  74     -20.788  -2.206   7.823  1.00 60.70           O  
ANISOU 3052  O   THR B  74     5322   7944   9797    125   -444   -512       O  
ATOM   3053  CB  THR B  74     -21.584  -2.708  10.910  1.00 60.65           C  
ANISOU 3053  CB  THR B  74     5233   7860   9948     53   -401   -502       C  
ATOM   3054  OG1 THR B  74     -22.994  -2.952  10.970  1.00 61.78           O  
ANISOU 3054  OG1 THR B  74     5319   8050  10102     36   -431   -577       O  
ATOM   3055  CG2 THR B  74     -21.287  -1.240  10.708  1.00 60.73           C  
ANISOU 3055  CG2 THR B  74     5276   7890   9909    108   -442   -437       C  
ATOM   3056  N   THR B  75     -22.599  -3.616   7.949  1.00 65.16           N  
ANISOU 3056  N   THR B  75     5803   8548  10403     59   -460   -657       N  
ATOM   3057  CA  THR B  75     -23.236  -3.342   6.638  1.00 67.03           C  
ANISOU 3057  CA  THR B  75     6039   8865  10563     89   -519   -709       C  
ATOM   3058  C   THR B  75     -24.422  -2.386   6.827  1.00 66.70           C  
ANISOU 3058  C   THR B  75     5947   8893  10503    125   -589   -719       C  
ATOM   3059  O   THR B  75     -24.923  -1.898   5.801  1.00 67.83           O  
ANISOU 3059  O   THR B  75     6089   9108  10572    169   -647   -745       O  
ATOM   3060  CB  THR B  75     -23.630  -4.672   5.984  1.00 68.52           C  
ANISOU 3060  CB  THR B  75     6218   9064  10751     34   -505   -806       C  
ATOM   3061  OG1 THR B  75     -24.235  -5.458   7.011  1.00 69.71           O  
ANISOU 3061  OG1 THR B  75     6319   9186  10980    -28   -476   -845       O  
ATOM   3062  CG2 THR B  75     -22.455  -5.417   5.391  1.00 67.86           C  
ANISOU 3062  CG2 THR B  75     6201   8927  10655     26   -446   -795       C  
ATOM   3063  N   ASP B  76     -24.830  -2.101   8.074  1.00 66.43           N  
ANISOU 3063  N   ASP B  76     5874   8838  10526    115   -581   -697       N  
ATOM   3064  CA  ASP B  76     -25.959  -1.192   8.424  1.00 66.90           C  
ANISOU 3064  CA  ASP B  76     5883   8959  10576    156   -637   -702       C  
ATOM   3065  C   ASP B  76     -25.756   0.169   7.758  1.00 67.04           C  
ANISOU 3065  C   ASP B  76     5948   9006  10515    243   -684   -645       C  
ATOM   3066  O   ASP B  76     -24.913   0.957   8.186  1.00 68.24           O  
ANISOU 3066  O   ASP B  76     6156   9104  10667    268   -664   -563       O  
ATOM   3067  CB  ASP B  76     -26.097  -1.025   9.938  1.00 66.87           C  
ANISOU 3067  CB  ASP B  76     5856   8909  10643    139   -606   -666       C  
ATOM   3068  CG  ASP B  76     -27.101   0.039  10.350  1.00 68.17           C  
ANISOU 3068  CG  ASP B  76     5981   9125  10793    195   -653   -656       C  
ATOM   3069  OD1 ASP B  76     -27.771   0.602   9.450  1.00 69.90           O  
ANISOU 3069  OD1 ASP B  76     6184   9424  10948    250   -714   -680       O  
ATOM   3070  OD2 ASP B  76     -27.210   0.284  11.567  1.00 69.13           O  
ANISOU 3070  OD2 ASP B  76     6092   9209  10964    189   -628   -625       O  
ATOM   3071  N   PRO B  77     -26.546   0.509   6.713  1.00 67.13           N  
ANISOU 3071  N   PRO B  77     5941   9108  10456    289   -748   -686       N  
ATOM   3072  CA  PRO B  77     -26.300   1.716   5.924  1.00 67.00           C  
ANISOU 3072  CA  PRO B  77     5984   9115  10356    375   -787   -632       C  
ATOM   3073  C   PRO B  77     -26.691   3.015   6.642  1.00 66.11           C  
ANISOU 3073  C   PRO B  77     5878   9000  10238    440   -809   -573       C  
ATOM   3074  O   PRO B  77     -26.507   4.069   6.054  1.00 65.99           O  
ANISOU 3074  O   PRO B  77     5923   8995  10155    513   -836   -524       O  
ATOM   3075  CB  PRO B  77     -27.169   1.525   4.670  1.00 68.56           C  
ANISOU 3075  CB  PRO B  77     6150   9417  10481    404   -851   -705       C  
ATOM   3076  CG  PRO B  77     -27.653   0.082   4.735  1.00 69.41           C  
ANISOU 3076  CG  PRO B  77     6190   9542  10638    314   -836   -800       C  
ATOM   3077  CD  PRO B  77     -27.706  -0.242   6.216  1.00 68.44           C  
ANISOU 3077  CD  PRO B  77     6029   9358  10615    261   -786   -787       C  
ATOM   3078  N   SER B  78     -27.226   2.909   7.865  1.00 65.18           N  
ANISOU 3078  N   SER B  78     5707   8866  10190    415   -793   -580       N  
ATOM   3079  CA  SER B  78     -27.553   4.054   8.757  1.00 63.94           C  
ANISOU 3079  CA  SER B  78     5562   8691  10038    470   -801   -525       C  
ATOM   3080  C   SER B  78     -26.349   4.407   9.650  1.00 62.26           C  
ANISOU 3080  C   SER B  78     5421   8371   9864    443   -747   -447       C  
ATOM   3081  O   SER B  78     -26.346   5.531  10.219  1.00 61.55           O  
ANISOU 3081  O   SER B  78     5373   8250   9760    491   -752   -390       O  
ATOM   3082  CB  SER B  78     -28.783   3.761   9.588  1.00 63.21           C  
ANISOU 3082  CB  SER B  78     5374   8645   9995    459   -810   -575       C  
ATOM   3083  OG  SER B  78     -28.483   2.918  10.692  1.00 62.36           O  
ANISOU 3083  OG  SER B  78     5244   8474   9974    377   -752   -582       O  
ATOM   3084  N   PHE B  79     -25.384   3.488   9.783  1.00 60.77           N  
ANISOU 3084  N   PHE B  79     5245   8129   9716    370   -697   -445       N  
ATOM   3085  CA  PHE B  79     -24.319   3.536  10.818  1.00 60.21           C  
ANISOU 3085  CA  PHE B  79     5213   7966   9695    330   -645   -383       C  
ATOM   3086  C   PHE B  79     -23.645   4.912  10.836  1.00 58.93           C  
ANISOU 3086  C   PHE B  79     5134   7764   9489    375   -652   -301       C  
ATOM   3087  O   PHE B  79     -23.693   5.565  11.897  1.00 57.54           O  
ANISOU 3087  O   PHE B  79     4975   7549   9336    381   -645   -264       O  
ATOM   3088  CB  PHE B  79     -23.257   2.452  10.614  1.00 60.53           C  
ANISOU 3088  CB  PHE B  79     5265   7968   9765    267   -596   -385       C  
ATOM   3089  CG  PHE B  79     -22.261   2.405  11.743  1.00 60.44           C  
ANISOU 3089  CG  PHE B  79     5279   7879   9807    228   -547   -326       C  
ATOM   3090  CD1 PHE B  79     -22.569   1.764  12.934  1.00 60.52           C  
ANISOU 3090  CD1 PHE B  79     5248   7862   9885    187   -519   -343       C  
ATOM   3091  CD2 PHE B  79     -21.039   3.054  11.641  1.00 60.82           C  
ANISOU 3091  CD2 PHE B  79     5389   7885   9832    232   -532   -253       C  
ATOM   3092  CE1 PHE B  79     -21.652   1.721  13.971  1.00 60.16           C  
ANISOU 3092  CE1 PHE B  79     5224   7752   9880    156   -479   -289       C  
ATOM   3093  CE2 PHE B  79     -20.126   3.019  12.687  1.00 60.53           C  
ANISOU 3093  CE2 PHE B  79     5368   7789   9841    194   -494   -201       C  
ATOM   3094  CZ  PHE B  79     -20.442   2.363  13.855  1.00 59.79           C  
ANISOU 3094  CZ  PHE B  79     5234   7672   9809    160   -471   -219       C  
ATOM   3095  N   LEU B  80     -23.024   5.317   9.720  1.00 58.66           N  
ANISOU 3095  N   LEU B  80     5157   7738   9393    402   -661   -274       N  
ATOM   3096  CA  LEU B  80     -22.206   6.557   9.648  1.00 58.18           C  
ANISOU 3096  CA  LEU B  80     5185   7629   9291    430   -657   -192       C  
ATOM   3097  C   LEU B  80     -23.045   7.756  10.093  1.00 57.84           C  
ANISOU 3097  C   LEU B  80     5166   7587   9221    496   -690   -173       C  
ATOM   3098  O   LEU B  80     -22.578   8.489  10.993  1.00 57.52           O  
ANISOU 3098  O   LEU B  80     5174   7483   9197    485   -672   -119       O  
ATOM   3099  CB  LEU B  80     -21.662   6.761   8.234  1.00 59.03           C  
ANISOU 3099  CB  LEU B  80     5342   7757   9327    458   -663   -177       C  
ATOM   3100  CG  LEU B  80     -20.193   6.374   8.072  1.00 59.51           C  
ANISOU 3100  CG  LEU B  80     5434   7772   9404    402   -611   -135       C  
ATOM   3101  CD1 LEU B  80     -20.076   4.948   7.555  1.00 59.87           C  
ANISOU 3101  CD1 LEU B  80     5429   7845   9470    366   -591   -193       C  
ATOM   3102  CD2 LEU B  80     -19.459   7.360   7.161  1.00 60.02           C  
ANISOU 3102  CD2 LEU B  80     5585   7823   9397    435   -608    -73       C  
ATOM   3103  N   GLY B  81     -24.220   7.936   9.479  1.00 57.58           N  
ANISOU 3103  N   GLY B  81     5102   7628   9145    563   -738   -215       N  
ATOM   3104  CA  GLY B  81     -25.221   8.939   9.885  1.00 56.11           C  
ANISOU 3104  CA  GLY B  81     4923   7459   8935    639   -770   -206       C  
ATOM   3105  C   GLY B  81     -25.247   9.124  11.391  1.00 54.54           C  
ANISOU 3105  C   GLY B  81     4720   7202   8797    610   -742   -187       C  
ATOM   3106  O   GLY B  81     -25.050  10.259  11.854  1.00 53.45           O  
ANISOU 3106  O   GLY B  81     4660   7010   8637    644   -737   -132       O  
ATOM   3107  N   ARG B  82     -25.454   8.038  12.135  1.00 54.56           N  
ANISOU 3107  N   ARG B  82     4645   7211   8873    547   -720   -231       N  
ATOM   3108  CA  ARG B  82     -25.715   8.078  13.600  1.00 55.21           C  
ANISOU 3108  CA  ARG B  82     4710   7254   9013    524   -695   -225       C  
ATOM   3109  C   ARG B  82     -24.398   8.298  14.354  1.00 54.17           C  
ANISOU 3109  C   ARG B  82     4647   7029   8906    467   -655   -164       C  
ATOM   3110  O   ARG B  82     -24.416   9.035  15.360  1.00 54.99           O  
ANISOU 3110  O   ARG B  82     4791   7083   9018    477   -646   -131       O  
ATOM   3111  CB  ARG B  82     -26.435   6.805  14.057  1.00 55.83           C  
ANISOU 3111  CB  ARG B  82     4683   7372   9155    477   -682   -294       C  
ATOM   3112  CG  ARG B  82     -27.766   6.564  13.357  1.00 57.23           C  
ANISOU 3112  CG  ARG B  82     4780   7653   9310    521   -724   -360       C  
ATOM   3113  CD  ARG B  82     -28.495   5.347  13.896  1.00 57.78           C  
ANISOU 3113  CD  ARG B  82     4748   7758   9447    462   -705   -428       C  
ATOM   3114  NE  ARG B  82     -27.925   4.100  13.387  1.00 57.67           N  
ANISOU 3114  NE  ARG B  82     4714   7737   9459    385   -683   -464       N  
ATOM   3115  CZ  ARG B  82     -27.019   3.346  14.015  1.00 56.90           C  
ANISOU 3115  CZ  ARG B  82     4635   7569   9415    313   -631   -448       C  
ATOM   3116  NH1 ARG B  82     -26.550   3.696  15.205  1.00 56.53           N  
ANISOU 3116  NH1 ARG B  82     4624   7453   9400    301   -598   -397       N  
ATOM   3117  NH2 ARG B  82     -26.585   2.240  13.434  1.00 56.65           N  
ANISOU 3117  NH2 ARG B  82     4590   7535   9398    257   -611   -483       N  
ATOM   3118  N   TYR B  83     -23.311   7.680  13.889  1.00 52.63           N  
ANISOU 3118  N   TYR B  83     4461   6815   8721    412   -633   -152       N  
ATOM   3119  CA  TYR B  83     -21.925   7.881  14.395  1.00 51.71           C  
ANISOU 3119  CA  TYR B  83     4400   6625   8619    357   -600    -91       C  
ATOM   3120  C   TYR B  83     -21.557   9.372  14.291  1.00 51.40           C  
ANISOU 3120  C   TYR B  83     4460   6544   8525    393   -612    -30       C  
ATOM   3121  O   TYR B  83     -21.180   9.978  15.318  1.00 49.85           O  
ANISOU 3121  O   TYR B  83     4308   6289   8343    371   -600      7       O  
ATOM   3122  CB  TYR B  83     -20.967   6.949  13.643  1.00 51.71           C  
ANISOU 3122  CB  TYR B  83     4384   6632   8629    310   -576    -93       C  
ATOM   3123  CG  TYR B  83     -19.498   7.242  13.814  1.00 51.43           C  
ANISOU 3123  CG  TYR B  83     4400   6544   8596    265   -548    -28       C  
ATOM   3124  CD1 TYR B  83     -18.985   7.616  15.045  1.00 50.90           C  
ANISOU 3124  CD1 TYR B  83     4355   6424   8559    228   -533     11       C  
ATOM   3125  CD2 TYR B  83     -18.618   7.130  12.746  1.00 51.55           C  
ANISOU 3125  CD2 TYR B  83     4437   6568   8580    256   -535     -6       C  
ATOM   3126  CE1 TYR B  83     -17.641   7.897  15.204  1.00 51.04           C  
ANISOU 3126  CE1 TYR B  83     4410   6405   8578    181   -512     69       C  
ATOM   3127  CE2 TYR B  83     -17.266   7.397  12.892  1.00 51.34           C  
ANISOU 3127  CE2 TYR B  83     4445   6503   8558    211   -507     53       C  
ATOM   3128  CZ  TYR B  83     -16.780   7.783  14.128  1.00 50.79           C  
ANISOU 3128  CZ  TYR B  83     4390   6387   8520    171   -498     91       C  
ATOM   3129  OH  TYR B  83     -15.463   8.056  14.306  1.00 50.41           O  
ANISOU 3129  OH  TYR B  83     4366   6311   8476    121   -475    148       O  
ATOM   3130  N   MET B  84     -21.687   9.956  13.094  1.00 52.27           N  
ANISOU 3130  N   MET B  84     4608   6680   8569    447   -636    -21       N  
ATOM   3131  CA  MET B  84     -21.405  11.393  12.843  1.00 53.22           C  
ANISOU 3131  CA  MET B  84     4835   6757   8629    488   -644     36       C  
ATOM   3132  C   MET B  84     -22.332  12.264  13.703  1.00 53.92           C  
ANISOU 3132  C   MET B  84     4951   6824   8710    543   -658     38       C  
ATOM   3133  O   MET B  84     -21.837  13.248  14.274  1.00 53.13           O  
ANISOU 3133  O   MET B  84     4938   6651   8595    533   -646     87       O  
ATOM   3134  CB  MET B  84     -21.598  11.738  11.369  1.00 54.55           C  
ANISOU 3134  CB  MET B  84     5034   6968   8725    550   -667     37       C  
ATOM   3135  CG  MET B  84     -20.533  11.166  10.454  1.00 55.91           C  
ANISOU 3135  CG  MET B  84     5207   7146   8888    504   -645     50       C  
ATOM   3136  SD  MET B  84     -18.872  11.913  10.693  1.00 57.46           S  
ANISOU 3136  SD  MET B  84     5491   7256   9081    434   -601    135       S  
ATOM   3137  CE  MET B  84     -18.108  10.700  11.763  1.00 56.09           C  
ANISOU 3137  CE  MET B  84     5238   7072   9001    337   -569    122       C  
ATOM   3138  N   SER B  85     -23.621  11.913  13.805  1.00 55.58           N  
ANISOU 3138  N   SER B  85     5091   7096   8929    595   -682    -14       N  
ATOM   3139  CA  SER B  85     -24.616  12.608  14.666  1.00 56.33           C  
ANISOU 3139  CA  SER B  85     5197   7183   9022    656   -691    -18       C  
ATOM   3140  C   SER B  85     -24.141  12.572  16.115  1.00 55.78           C  
ANISOU 3140  C   SER B  85     5142   7044   9005    591   -658     -1       C  
ATOM   3141  O   SER B  85     -24.004  13.642  16.710  1.00 57.16           O  
ANISOU 3141  O   SER B  85     5406   7154   9156    611   -651     38       O  
ATOM   3142  CB  SER B  85     -25.983  12.008  14.554  1.00 56.95           C  
ANISOU 3142  CB  SER B  85     5171   7352   9113    705   -716    -82       C  
ATOM   3143  OG  SER B  85     -26.539  12.291  13.286  1.00 58.56           O  
ANISOU 3143  OG  SER B  85     5372   7623   9253    782   -755    -93       O  
ATOM   3144  N   ALA B  86     -23.922  11.372  16.650  1.00 54.78           N  
ANISOU 3144  N   ALA B  86     4937   6931   8945    520   -638    -31       N  
ATOM   3145  CA  ALA B  86     -23.362  11.145  18.001  1.00 54.38           C  
ANISOU 3145  CA  ALA B  86     4894   6823   8945    453   -607    -15       C  
ATOM   3146  C   ALA B  86     -22.124  12.033  18.158  1.00 54.93           C  
ANISOU 3146  C   ALA B  86     5065   6816   8988    414   -598     47       C  
ATOM   3147  O   ALA B  86     -22.089  12.835  19.117  1.00 53.98           O  
ANISOU 3147  O   ALA B  86     5011   6639   8861    415   -592     72       O  
ATOM   3148  CB  ALA B  86     -23.029   9.683  18.196  1.00 53.98           C  
ANISOU 3148  CB  ALA B  86     4758   6796   8956    383   -585    -46       C  
ATOM   3149  N   LEU B  87     -21.183  11.923  17.211  1.00 55.05           N  
ANISOU 3149  N   LEU B  87     5096   6833   8985    383   -596     70       N  
ATOM   3150  CA  LEU B  87     -19.855  12.590  17.253  1.00 55.68           C  
ANISOU 3150  CA  LEU B  87     5255   6853   9048    327   -583    129       C  
ATOM   3151  C   LEU B  87     -20.027  14.103  17.421  1.00 56.65           C  
ANISOU 3151  C   LEU B  87     5492   6916   9116    367   -591    165       C  
ATOM   3152  O   LEU B  87     -19.322  14.691  18.258  1.00 56.37           O  
ANISOU 3152  O   LEU B  87     5519   6816   9083    314   -579    198       O  
ATOM   3153  CB  LEU B  87     -19.091  12.263  15.966  1.00 56.28           C  
ANISOU 3153  CB  LEU B  87     5323   6956   9105    309   -578    143       C  
ATOM   3154  CG  LEU B  87     -17.739  12.953  15.801  1.00 56.42           C  
ANISOU 3154  CG  LEU B  87     5412   6923   9101    251   -561    204       C  
ATOM   3155  CD1 LEU B  87     -16.840  12.691  17.002  1.00 55.64           C  
ANISOU 3155  CD1 LEU B  87     5300   6791   9050    166   -544    224       C  
ATOM   3156  CD2 LEU B  87     -17.072  12.489  14.515  1.00 56.75           C  
ANISOU 3156  CD2 LEU B  87     5433   7001   9125    241   -549    213       C  
ATOM   3157  N   ASN B  88     -20.948  14.689  16.654  1.00 58.36           N  
ANISOU 3157  N   ASN B  88     5735   7154   9282    459   -611    156       N  
ATOM   3158  CA  ASN B  88     -21.249  16.145  16.605  1.00 59.50           C  
ANISOU 3158  CA  ASN B  88     5999   7243   9364    521   -616    190       C  
ATOM   3159  C   ASN B  88     -21.483  16.701  18.017  1.00 59.67           C  
ANISOU 3159  C   ASN B  88     6068   7203   9400    514   -606    194       C  
ATOM   3160  O   ASN B  88     -21.200  17.904  18.228  1.00 60.10           O  
ANISOU 3160  O   ASN B  88     6244   7179   9411    520   -598    232       O  
ATOM   3161  CB  ASN B  88     -22.459  16.422  15.712  1.00 60.72           C  
ANISOU 3161  CB  ASN B  88     6145   7453   9470    639   -642    169       C  
ATOM   3162  CG  ASN B  88     -22.438  17.800  15.092  1.00 62.55           C  
ANISOU 3162  CG  ASN B  88     6508   7633   9625    703   -644    217       C  
ATOM   3163  OD1 ASN B  88     -22.951  17.984  13.995  1.00 65.31           O  
ANISOU 3163  OD1 ASN B  88     6862   8029   9923    783   -664    216       O  
ATOM   3164  ND2 ASN B  88     -21.821  18.762  15.755  1.00 63.00           N  
ANISOU 3164  ND2 ASN B  88     6677   7592   9667    667   -621    258       N  
ATOM   3165  N   HIS B  89     -21.984  15.870  18.941  1.00 58.92           N  
ANISOU 3165  N   HIS B  89     5888   7137   9359    501   -603    155       N  
ATOM   3166  CA  HIS B  89     -22.245  16.218  20.366  1.00 57.54           C  
ANISOU 3166  CA  HIS B  89     5748   6914   9201    494   -590    153       C  
ATOM   3167  C   HIS B  89     -21.013  15.887  21.226  1.00 56.32           C  
ANISOU 3167  C   HIS B  89     5599   6715   9082    379   -575    173       C  
ATOM   3168  O   HIS B  89     -20.594  16.770  22.006  1.00 56.46           O  
ANISOU 3168  O   HIS B  89     5714   6659   9078    351   -568    199       O  
ATOM   3169  CB  HIS B  89     -23.503  15.498  20.870  1.00 56.98           C  
ANISOU 3169  CB  HIS B  89     5581   6903   9165    546   -591    102       C  
ATOM   3170  CG  HIS B  89     -24.779  15.870  20.178  1.00 57.74           C  
ANISOU 3170  CG  HIS B  89     5661   7052   9225    662   -609     82       C  
ATOM   3171  ND1 HIS B  89     -25.806  16.518  20.833  1.00 57.50           N  
ANISOU 3171  ND1 HIS B  89     5658   7013   9177    744   -604     74       N  
ATOM   3172  CD2 HIS B  89     -25.223  15.636  18.921  1.00 57.72           C  
ANISOU 3172  CD2 HIS B  89     5610   7120   9199    713   -633     66       C  
ATOM   3173  CE1 HIS B  89     -26.813  16.688  20.001  1.00 58.53           C  
ANISOU 3173  CE1 HIS B  89     5753   7210   9276    843   -626     57       C  
ATOM   3174  NE2 HIS B  89     -26.478  16.154  18.819  1.00 57.99           N  
ANISOU 3174  NE2 HIS B  89     5638   7192   9202    824   -647     50       N  
ATOM   3175  N   THR B  90     -20.446  14.676  21.080  1.00 54.95           N  
ANISOU 3175  N   THR B  90     5331   6588   8957    318   -570    161       N  
ATOM   3176  CA  THR B  90     -19.418  14.089  21.991  1.00 53.49           C  
ANISOU 3176  CA  THR B  90     5123   6385   8814    223   -557    174       C  
ATOM   3177  C   THR B  90     -18.112  14.883  21.900  1.00 53.71           C  
ANISOU 3177  C   THR B  90     5231   6359   8815    153   -557    224       C  
ATOM   3178  O   THR B  90     -17.361  14.872  22.886  1.00 53.64           O  
ANISOU 3178  O   THR B  90     5236   6321   8823     83   -554    240       O  
ATOM   3179  CB  THR B  90     -19.139  12.601  21.725  1.00 52.39           C  
ANISOU 3179  CB  THR B  90     4870   6307   8729    188   -547    152       C  
ATOM   3180  OG1 THR B  90     -18.614  12.426  20.412  1.00 51.32           O  
ANISOU 3180  OG1 THR B  90     4719   6200   8579    184   -550    163       O  
ATOM   3181  CG2 THR B  90     -20.359  11.725  21.901  1.00 52.28           C  
ANISOU 3181  CG2 THR B  90     4772   6342   8748    236   -543    100       C  
ATOM   3182  N   LYS B  91     -17.862  15.542  20.765  1.00 53.42           N  
ANISOU 3182  N   LYS B  91     5245   6315   8736    170   -561    248       N  
ATOM   3183  CA  LYS B  91     -16.694  16.435  20.544  1.00 52.64           C  
ANISOU 3183  CA  LYS B  91     5231   6162   8605    103   -555    297       C  
ATOM   3184  C   LYS B  91     -16.836  17.739  21.359  1.00 52.32           C  
ANISOU 3184  C   LYS B  91     5317   6036   8526    102   -556    312       C  
ATOM   3185  O   LYS B  91     -15.849  18.490  21.419  1.00 51.95           O  
ANISOU 3185  O   LYS B  91     5345   5937   8457     28   -551    348       O  
ATOM   3186  CB  LYS B  91     -16.545  16.717  19.044  1.00 52.96           C  
ANISOU 3186  CB  LYS B  91     5294   6220   8609    133   -552    316       C  
ATOM   3187  CG  LYS B  91     -17.574  17.685  18.479  1.00 54.30           C  
ANISOU 3187  CG  LYS B  91     5546   6365   8720    234   -560    315       C  
ATOM   3188  CD  LYS B  91     -17.334  18.111  17.057  1.00 55.27           C  
ANISOU 3188  CD  LYS B  91     5710   6493   8794    263   -555    343       C  
ATOM   3189  CE  LYS B  91     -18.215  19.274  16.645  1.00 56.43           C  
ANISOU 3189  CE  LYS B  91     5964   6600   8874    362   -560    354       C  
ATOM   3190  NZ  LYS B  91     -18.134  19.509  15.183  1.00 57.51           N  
ANISOU 3190  NZ  LYS B  91     6130   6759   8961    407   -558    376       N  
ATOM   3191  N   LYS B  92     -18.004  18.021  21.953  1.00 52.06           N  
ANISOU 3191  N   LYS B  92     5309   5988   8483    179   -560    285       N  
ATOM   3192  CA  LYS B  92     -18.233  19.227  22.802  1.00 52.55           C  
ANISOU 3192  CA  LYS B  92     5498   5963   8505    188   -556    294       C  
ATOM   3193  C   LYS B  92     -18.242  18.836  24.284  1.00 50.97           C  
ANISOU 3193  C   LYS B  92     5275   5753   8336    148   -556    274       C  
ATOM   3194  O   LYS B  92     -18.241  19.747  25.131  1.00 50.35           O  
ANISOU 3194  O   LYS B  92     5303   5601   8226    136   -553    279       O  
ATOM   3195  CB  LYS B  92     -19.552  19.916  22.443  1.00 53.81           C  
ANISOU 3195  CB  LYS B  92     5712   6111   8622    316   -555    282       C  
ATOM   3196  CG  LYS B  92     -19.596  20.550  21.061  1.00 55.37           C  
ANISOU 3196  CG  LYS B  92     5964   6304   8770    369   -556    308       C  
ATOM   3197  CD  LYS B  92     -21.006  20.896  20.612  1.00 56.50           C  
ANISOU 3197  CD  LYS B  92     6117   6470   8878    512   -562    292       C  
ATOM   3198  CE  LYS B  92     -21.056  21.540  19.240  1.00 57.74           C  
ANISOU 3198  CE  LYS B  92     6335   6625   8978    573   -564    321       C  
ATOM   3199  NZ  LYS B  92     -22.329  21.225  18.550  1.00 58.24           N  
ANISOU 3199  NZ  LYS B  92     6330   6771   9028    699   -583    294       N  
ATOM   3200  N   TRP B  93     -18.271  17.533  24.580  1.00 49.36           N  
ANISOU 3200  N   TRP B  93     4947   5618   8189    132   -557    251       N  
ATOM   3201  CA  TRP B  93     -18.104  16.992  25.955  1.00 48.88           C  
ANISOU 3201  CA  TRP B  93     4856   5555   8160     86   -555    238       C  
ATOM   3202  C   TRP B  93     -16.667  17.234  26.424  1.00 48.29           C  
ANISOU 3202  C   TRP B  93     4815   5450   8081    -28   -564    269       C  
ATOM   3203  O   TRP B  93     -15.764  17.267  25.578  1.00 47.77           O  
ANISOU 3203  O   TRP B  93     4738   5396   8013    -78   -567    296       O  
ATOM   3204  CB  TRP B  93     -18.437  15.496  26.019  1.00 48.27           C  
ANISOU 3204  CB  TRP B  93     4642   5555   8142     96   -548    210       C  
ATOM   3205  CG  TRP B  93     -19.875  15.137  25.801  1.00 47.84           C  
ANISOU 3205  CG  TRP B  93     4538   5540   8099    193   -540    172       C  
ATOM   3206  CD1 TRP B  93     -20.945  15.975  25.675  1.00 48.09           C  
ANISOU 3206  CD1 TRP B  93     4624   5552   8093    281   -539    160       C  
ATOM   3207  CD2 TRP B  93     -20.403  13.804  25.707  1.00 47.37           C  
ANISOU 3207  CD2 TRP B  93     4357   5549   8091    207   -529    139       C  
ATOM   3208  NE1 TRP B  93     -22.096  15.256  25.499  1.00 48.12           N  
ANISOU 3208  NE1 TRP B  93     4538   5620   8124    348   -533    122       N  
ATOM   3209  CE2 TRP B  93     -21.793  13.921  25.517  1.00 47.63           C  
ANISOU 3209  CE2 TRP B  93     4370   5608   8117    298   -526    106       C  
ATOM   3210  CE3 TRP B  93     -19.834  12.526  25.767  1.00 46.96           C  
ANISOU 3210  CE3 TRP B  93     4215   5537   8090    154   -520    134       C  
ATOM   3211  CZ2 TRP B  93     -22.615  12.806  25.394  1.00 47.60           C  
ANISOU 3211  CZ2 TRP B  93     4256   5671   8157    323   -515     66       C  
ATOM   3212  CZ3 TRP B  93     -20.648  11.424  25.639  1.00 46.72           C  
ANISOU 3212  CZ3 TRP B  93     4089   5560   8100    182   -505     95       C  
ATOM   3213  CH2 TRP B  93     -22.022  11.566  25.461  1.00 47.11           C  
ANISOU 3213  CH2 TRP B  93     4118   5637   8145    260   -503     59       C  
ATOM   3214  N   LYS B  94     -16.471  17.367  27.734  1.00 48.32           N  
ANISOU 3214  N   LYS B  94     4854   5422   8082    -69   -568    265       N  
ATOM   3215  CA  LYS B  94     -15.130  17.450  28.363  1.00 48.82           C  
ANISOU 3215  CA  LYS B  94     4930   5473   8144   -182   -584    289       C  
ATOM   3216  C   LYS B  94     -14.713  16.042  28.797  1.00 47.72           C  
ANISOU 3216  C   LYS B  94     4666   5405   8058   -209   -585    286       C  
ATOM   3217  O   LYS B  94     -15.550  15.331  29.385  1.00 47.74           O  
ANISOU 3217  O   LYS B  94     4625   5428   8085   -156   -573    260       O  
ATOM   3218  CB  LYS B  94     -15.146  18.433  29.537  1.00 50.40           C  
ANISOU 3218  CB  LYS B  94     5249   5597   8300   -210   -592    284       C  
ATOM   3219  CG  LYS B  94     -15.588  19.851  29.198  1.00 51.95           C  
ANISOU 3219  CG  LYS B  94     5587   5709   8440   -176   -584    287       C  
ATOM   3220  CD  LYS B  94     -14.980  20.378  27.928  1.00 52.81           C  
ANISOU 3220  CD  LYS B  94     5723   5808   8534   -205   -582    318       C  
ATOM   3221  CE  LYS B  94     -15.468  21.762  27.572  1.00 54.19           C  
ANISOU 3221  CE  LYS B  94     6047   5892   8649   -160   -568    324       C  
ATOM   3222  NZ  LYS B  94     -15.111  22.086  26.170  1.00 54.76           N  
ANISOU 3222  NZ  LYS B  94     6131   5966   8709   -160   -559    354       N  
ATOM   3223  N   TYR B  95     -13.474  15.652  28.491  1.00 46.79           N  
ANISOU 3223  N   TYR B  95     4494   5324   7957   -286   -595    315       N  
ATOM   3224  CA  TYR B  95     -12.843  14.380  28.925  1.00 45.86           C  
ANISOU 3224  CA  TYR B  95     4268   5271   7885   -316   -595    322       C  
ATOM   3225  C   TYR B  95     -11.635  14.693  29.796  1.00 45.06           C  
ANISOU 3225  C   TYR B  95     4186   5168   7768   -413   -621    347       C  
ATOM   3226  O   TYR B  95     -10.500  14.602  29.341  1.00 44.90           O  
ANISOU 3226  O   TYR B  95     4122   5182   7754   -477   -630    378       O  
ATOM   3227  CB  TYR B  95     -12.449  13.543  27.713  1.00 45.79           C  
ANISOU 3227  CB  TYR B  95     4166   5320   7909   -308   -581    334       C  
ATOM   3228  CG  TYR B  95     -13.590  13.307  26.766  1.00 45.66           C  
ANISOU 3228  CG  TYR B  95     4134   5312   7902   -221   -563    306       C  
ATOM   3229  CD1 TYR B  95     -14.373  12.173  26.860  1.00 45.40           C  
ANISOU 3229  CD1 TYR B  95     4025   5315   7908   -167   -545    276       C  
ATOM   3230  CD2 TYR B  95     -13.901  14.238  25.796  1.00 46.21           C  
ANISOU 3230  CD2 TYR B  95     4267   5353   7936   -194   -563    309       C  
ATOM   3231  CE1 TYR B  95     -15.425  11.954  25.988  1.00 46.29           C  
ANISOU 3231  CE1 TYR B  95     4116   5445   8026    -95   -534    246       C  
ATOM   3232  CE2 TYR B  95     -14.942  14.034  24.913  1.00 46.56           C  
ANISOU 3232  CE2 TYR B  95     4293   5416   7982   -112   -553    284       C  
ATOM   3233  CZ  TYR B  95     -15.713  12.891  25.011  1.00 46.90           C  
ANISOU 3233  CZ  TYR B  95     4250   5503   8065    -65   -542    249       C  
ATOM   3234  OH  TYR B  95     -16.758  12.703  24.152  1.00 47.38           O  
ANISOU 3234  OH  TYR B  95     4286   5590   8125      9   -537    220       O  
ATOM   3235  N   PRO B  96     -11.842  15.076  31.074  1.00 44.64           N  
ANISOU 3235  N   PRO B  96     4194   5078   7689   -427   -635    334       N  
ATOM   3236  CA  PRO B  96     -10.724  15.331  31.976  1.00 44.85           C  
ANISOU 3236  CA  PRO B  96     4234   5110   7694   -521   -667    353       C  
ATOM   3237  C   PRO B  96     -10.034  14.018  32.380  1.00 44.62           C  
ANISOU 3237  C   PRO B  96     4087   5161   7704   -534   -672    371       C  
ATOM   3238  O   PRO B  96     -10.683  12.976  32.392  1.00 43.78           O  
ANISOU 3238  O   PRO B  96     3918   5081   7634   -464   -647    358       O  
ATOM   3239  CB  PRO B  96     -11.395  16.001  33.181  1.00 45.06           C  
ANISOU 3239  CB  PRO B  96     4365   5074   7680   -509   -675    327       C  
ATOM   3240  CG  PRO B  96     -12.788  15.409  33.193  1.00 44.63           C  
ANISOU 3240  CG  PRO B  96     4290   5017   7649   -399   -642    299       C  
ATOM   3241  CD  PRO B  96     -13.151  15.250  31.731  1.00 44.48           C  
ANISOU 3241  CD  PRO B  96     4228   5015   7655   -352   -621    300       C  
ATOM   3242  N   GLN B  97      -8.728  14.089  32.658  1.00 44.61           N  
ANISOU 3242  N   GLN B  97     4055   5198   7694   -621   -702    400       N  
ATOM   3243  CA  GLN B  97      -7.996  13.039  33.397  1.00 44.12           C  
ANISOU 3243  CA  GLN B  97     3902   5207   7652   -635   -716    420       C  
ATOM   3244  C   GLN B  97      -8.455  13.062  34.848  1.00 43.28           C  
ANISOU 3244  C   GLN B  97     3850   5076   7517   -624   -731    400       C  
ATOM   3245  O   GLN B  97      -8.494  14.158  35.425  1.00 43.48           O  
ANISOU 3245  O   GLN B  97     3977   5048   7494   -669   -755    386       O  
ATOM   3246  CB  GLN B  97      -6.486  13.271  33.305  1.00 45.41           C  
ANISOU 3246  CB  GLN B  97     4020   5426   7807   -734   -748    456       C  
ATOM   3247  CG  GLN B  97      -5.919  13.062  31.909  1.00 45.55           C  
ANISOU 3247  CG  GLN B  97     3968   5482   7855   -742   -726    481       C  
ATOM   3248  CD  GLN B  97      -6.078  11.636  31.442  1.00 44.88           C  
ANISOU 3248  CD  GLN B  97     3781   5450   7821   -663   -692    489       C  
ATOM   3249  OE1 GLN B  97      -5.699  10.678  32.133  1.00 44.09           O  
ANISOU 3249  OE1 GLN B  97     3613   5402   7737   -646   -696    504       O  
ATOM   3250  NE2 GLN B  97      -6.649  11.505  30.253  1.00 44.69           N  
ANISOU 3250  NE2 GLN B  97     3752   5410   7818   -613   -657    479       N  
ATOM   3251  N   VAL B  98      -8.797  11.899  35.398  1.00 42.08           N  
ANISOU 3251  N   VAL B  98     3640   4955   7391   -564   -713    400       N  
ATOM   3252  CA  VAL B  98      -9.192  11.767  36.828  1.00 41.90           C  
ANISOU 3252  CA  VAL B  98     3663   4916   7341   -548   -722    387       C  
ATOM   3253  C   VAL B  98      -8.483  10.539  37.396  1.00 41.32           C  
ANISOU 3253  C   VAL B  98     3497   4916   7287   -539   -727    417       C  
ATOM   3254  O   VAL B  98      -8.866   9.416  37.045  1.00 40.74           O  
ANISOU 3254  O   VAL B  98     3356   4863   7259   -475   -686    420       O  
ATOM   3255  CB  VAL B  98     -10.725  11.700  36.981  1.00 41.88           C  
ANISOU 3255  CB  VAL B  98     3709   4858   7346   -463   -680    350       C  
ATOM   3256  CG1 VAL B  98     -11.159  11.709  38.450  1.00 42.15           C  
ANISOU 3256  CG1 VAL B  98     3803   4867   7343   -447   -683    336       C  
ATOM   3257  CG2 VAL B  98     -11.413  12.819  36.203  1.00 41.93           C  
ANISOU 3257  CG2 VAL B  98     3792   4802   7336   -453   -672    327       C  
ATOM   3258  N   ASN B  99      -7.440  10.760  38.199  1.00 41.67           N  
ANISOU 3258  N   ASN B  99     3538   4999   7294   -605   -775    438       N  
ATOM   3259  CA  ASN B  99      -6.708   9.686  38.923  1.00 41.19           C  
ANISOU 3259  CA  ASN B  99     3400   5011   7237   -592   -788    471       C  
ATOM   3260  C   ASN B  99      -6.197   8.663  37.902  1.00 40.32           C  
ANISOU 3260  C   ASN B  99     3174   4959   7183   -561   -759    502       C  
ATOM   3261  O   ASN B  99      -6.248   7.458  38.195  1.00 39.95           O  
ANISOU 3261  O   ASN B  99     3074   4942   7162   -499   -732    519       O  
ATOM   3262  CB  ASN B  99      -7.603   9.054  39.992  1.00 41.15           C  
ANISOU 3262  CB  ASN B  99     3431   4979   7222   -522   -762    458       C  
ATOM   3263  CG  ASN B  99      -6.812   8.506  41.156  1.00 41.76           C  
ANISOU 3263  CG  ASN B  99     3483   5115   7268   -529   -796    488       C  
ATOM   3264  OD1 ASN B  99      -5.985   9.211  41.731  1.00 41.97           O  
ANISOU 3264  OD1 ASN B  99     3531   5170   7244   -602   -856    495       O  
ATOM   3265  ND2 ASN B  99      -7.080   7.264  41.516  1.00 41.80           N  
ANISOU 3265  ND2 ASN B  99     3446   5138   7297   -455   -758    505       N  
ATOM   3266  N   GLY B 100      -5.734   9.150  36.741  1.00 39.93           N  
ANISOU 3266  N   GLY B 100     3099   4920   7151   -602   -761    509       N  
ATOM   3267  CA  GLY B 100      -5.024   8.377  35.705  1.00 39.47           C  
ANISOU 3267  CA  GLY B 100     2936   4923   7137   -588   -739    540       C  
ATOM   3268  C   GLY B 100      -5.913   8.041  34.525  1.00 38.49           C  
ANISOU 3268  C   GLY B 100     2807   4759   7055   -530   -685    518       C  
ATOM   3269  O   GLY B 100      -5.370   7.605  33.477  1.00 38.64           O  
ANISOU 3269  O   GLY B 100     2756   4819   7105   -524   -664    538       O  
ATOM   3270  N   LEU B 101      -7.223   8.282  34.659  1.00 37.55           N  
ANISOU 3270  N   LEU B 101     2761   4570   6934   -488   -663    477       N  
ATOM   3271  CA  LEU B 101      -8.277   7.710  33.781  1.00 36.28           C  
ANISOU 3271  CA  LEU B 101     2589   4382   6814   -419   -612    450       C  
ATOM   3272  C   LEU B 101      -9.019   8.822  33.044  1.00 35.92           C  
ANISOU 3272  C   LEU B 101     2612   4281   6752   -425   -613    420       C  
ATOM   3273  O   LEU B 101      -9.276   9.881  33.661  1.00 35.94           O  
ANISOU 3273  O   LEU B 101     2700   4239   6714   -454   -639    407       O  
ATOM   3274  CB  LEU B 101      -9.239   6.918  34.658  1.00 35.79           C  
ANISOU 3274  CB  LEU B 101     2539   4295   6763   -358   -583    430       C  
ATOM   3275  CG  LEU B 101      -8.633   5.704  35.337  1.00 35.74           C  
ANISOU 3275  CG  LEU B 101     2473   4334   6771   -335   -572    461       C  
ATOM   3276  CD1 LEU B 101      -9.434   5.272  36.550  1.00 35.65           C  
ANISOU 3276  CD1 LEU B 101     2502   4292   6751   -296   -554    447       C  
ATOM   3277  CD2 LEU B 101      -8.545   4.575  34.340  1.00 35.51           C  
ANISOU 3277  CD2 LEU B 101     2368   4329   6792   -293   -527    468       C  
ATOM   3278  N   THR B 102      -9.358   8.571  31.782  1.00 35.56           N  
ANISOU 3278  N   THR B 102     2536   4237   6735   -393   -585    410       N  
ATOM   3279  CA  THR B 102     -10.216   9.476  30.983  1.00 36.05           C  
ANISOU 3279  CA  THR B 102     2660   4252   6783   -377   -580    382       C  
ATOM   3280  C   THR B 102     -11.678   9.257  31.394  1.00 36.23           C  
ANISOU 3280  C   THR B 102     2712   4238   6814   -309   -557    340       C  
ATOM   3281  O   THR B 102     -12.231   8.169  31.106  1.00 35.74           O  
ANISOU 3281  O   THR B 102     2593   4195   6791   -260   -523    324       O  
ATOM   3282  CB  THR B 102     -10.037   9.283  29.476  1.00 35.83           C  
ANISOU 3282  CB  THR B 102     2589   4248   6775   -364   -561    387       C  
ATOM   3283  OG1 THR B 102      -8.650   9.303  29.161  1.00 36.13           O  
ANISOU 3283  OG1 THR B 102     2583   4330   6811   -423   -574    428       O  
ATOM   3284  CG2 THR B 102     -10.759  10.356  28.691  1.00 35.98           C  
ANISOU 3284  CG2 THR B 102     2680   4222   6768   -350   -564    367       C  
ATOM   3285  N   SER B 103     -12.260  10.255  32.056  1.00 36.94           N  
ANISOU 3285  N   SER B 103     2890   4277   6867   -310   -572    324       N  
ATOM   3286  CA  SER B 103     -13.693  10.300  32.438  1.00 37.48           C  
ANISOU 3286  CA  SER B 103     2994   4310   6935   -245   -549    285       C  
ATOM   3287  C   SER B 103     -14.456  11.194  31.457  1.00 38.37           C  
ANISOU 3287  C   SER B 103     3153   4393   7032   -211   -548    265       C  
ATOM   3288  O   SER B 103     -13.932  11.443  30.361  1.00 38.88           O  
ANISOU 3288  O   SER B 103     3205   4471   7095   -229   -555    280       O  
ATOM   3289  CB  SER B 103     -13.829  10.777  33.846  1.00 37.63           C  
ANISOU 3289  CB  SER B 103     3083   4295   6919   -257   -562    282       C  
ATOM   3290  OG  SER B 103     -15.141  10.560  34.306  1.00 37.12           O  
ANISOU 3290  OG  SER B 103     3032   4209   6862   -192   -531    249       O  
ATOM   3291  N   ILE B 104     -15.659  11.630  31.824  1.00 39.44           N  
ANISOU 3291  N   ILE B 104     3337   4494   7153   -156   -535    235       N  
ATOM   3292  CA  ILE B 104     -16.456  12.629  31.051  1.00 40.62           C  
ANISOU 3292  CA  ILE B 104     3545   4612   7276   -109   -536    219       C  
ATOM   3293  C   ILE B 104     -17.211  13.514  32.043  1.00 42.05           C  
ANISOU 3293  C   ILE B 104     3821   4738   7418    -79   -533    204       C  
ATOM   3294  O   ILE B 104     -17.839  12.961  32.960  1.00 41.82           O  
ANISOU 3294  O   ILE B 104     3773   4714   7402    -50   -513    186       O  
ATOM   3295  CB  ILE B 104     -17.432  11.951  30.073  1.00 40.25           C  
ANISOU 3295  CB  ILE B 104     3425   4604   7262    -42   -514    192       C  
ATOM   3296  CG1 ILE B 104     -16.871  10.645  29.507  1.00 40.23           C  
ANISOU 3296  CG1 ILE B 104     3320   4657   7307    -65   -503    197       C  
ATOM   3297  CG2 ILE B 104     -17.833  12.924  28.980  1.00 40.31           C  
ANISOU 3297  CG2 ILE B 104     3481   4596   7238     -4   -524    189       C  
ATOM   3298  CD1 ILE B 104     -17.810   9.930  28.561  1.00 40.45           C  
ANISOU 3298  CD1 ILE B 104     3280   4724   7366    -10   -484    163       C  
ATOM   3299  N   LYS B 105     -17.121  14.837  31.888  1.00 44.08           N  
ANISOU 3299  N   LYS B 105     4183   4940   7625    -86   -549    211       N  
ATOM   3300  CA  LYS B 105     -17.967  15.789  32.649  1.00 45.93           C  
ANISOU 3300  CA  LYS B 105     4520   5113   7816    -39   -540    193       C  
ATOM   3301  C   LYS B 105     -19.425  15.431  32.323  1.00 46.40           C  
ANISOU 3301  C   LYS B 105     4533   5199   7897     63   -511    163       C  
ATOM   3302  O   LYS B 105     -19.704  15.081  31.148  1.00 46.96           O  
ANISOU 3302  O   LYS B 105     4538   5311   7991     95   -509    159       O  
ATOM   3303  CB  LYS B 105     -17.584  17.235  32.304  1.00 47.20           C  
ANISOU 3303  CB  LYS B 105     4806   5205   7921    -63   -556    208       C  
ATOM   3304  CG  LYS B 105     -18.339  18.324  33.059  1.00 48.45           C  
ANISOU 3304  CG  LYS B 105     5092   5288   8028    -15   -544    193       C  
ATOM   3305  CD  LYS B 105     -18.196  19.707  32.434  1.00 49.24           C  
ANISOU 3305  CD  LYS B 105     5316   5315   8075    -15   -549    206       C  
ATOM   3306  CE  LYS B 105     -19.092  20.733  33.096  1.00 50.01           C  
ANISOU 3306  CE  LYS B 105     5543   5337   8121     53   -529    189       C  
ATOM   3307  NZ  LYS B 105     -19.822  21.549  32.095  1.00 50.56           N  
ANISOU 3307  NZ  LYS B 105     5670   5376   8164    141   -515    194       N  
ATOM   3308  N   TRP B 106     -20.315  15.452  33.318  1.00 46.18           N  
ANISOU 3308  N   TRP B 106     4528   5155   7861    112   -487    142       N  
ATOM   3309  CA  TRP B 106     -21.708  14.984  33.119  1.00 46.23           C  
ANISOU 3309  CA  TRP B 106     4468   5200   7894    203   -457    112       C  
ATOM   3310  C   TRP B 106     -22.407  15.871  32.077  1.00 46.77           C  
ANISOU 3310  C   TRP B 106     4572   5262   7936    277   -461    108       C  
ATOM   3311  O   TRP B 106     -22.319  17.111  32.186  1.00 46.55           O  
ANISOU 3311  O   TRP B 106     4666   5168   7854    291   -468    119       O  
ATOM   3312  CB  TRP B 106     -22.500  14.918  34.428  1.00 46.51           C  
ANISOU 3312  CB  TRP B 106     4528   5220   7923    240   -425     94       C  
ATOM   3313  CG  TRP B 106     -23.813  14.242  34.197  1.00 46.16           C  
ANISOU 3313  CG  TRP B 106     4389   5232   7917    315   -391     64       C  
ATOM   3314  CD1 TRP B 106     -24.093  12.917  34.349  1.00 45.95           C  
ANISOU 3314  CD1 TRP B 106     4253   5260   7947    303   -367     49       C  
ATOM   3315  CD2 TRP B 106     -24.994  14.840  33.648  1.00 47.01           C  
ANISOU 3315  CD2 TRP B 106     4499   5353   8010    412   -380     46       C  
ATOM   3316  NE1 TRP B 106     -25.382  12.655  33.974  1.00 46.56           N  
ANISOU 3316  NE1 TRP B 106     4258   5383   8046    374   -341     19       N  
ATOM   3317  CE2 TRP B 106     -25.962  13.815  33.538  1.00 47.31           C  
ANISOU 3317  CE2 TRP B 106     4414   5461   8098    446   -351     17       C  
ATOM   3318  CE3 TRP B 106     -25.341  16.141  33.262  1.00 47.51           C  
ANISOU 3318  CE3 TRP B 106     4656   5375   8020    475   -389     52       C  
ATOM   3319  CZ2 TRP B 106     -27.256  14.058  33.076  1.00 47.44           C  
ANISOU 3319  CZ2 TRP B 106     4389   5519   8115    539   -337     -6       C  
ATOM   3320  CZ3 TRP B 106     -26.615  16.374  32.793  1.00 47.91           C  
ANISOU 3320  CZ3 TRP B 106     4670   5463   8068    579   -373     32       C  
ATOM   3321  CH2 TRP B 106     -27.558  15.347  32.704  1.00 47.82           C  
ANISOU 3321  CH2 TRP B 106     4526   5534   8108    609   -350      3       C  
ATOM   3322  N   ALA B 107     -23.092  15.237  31.120  1.00 46.66           N  
ANISOU 3322  N   ALA B 107     4459   5314   7956    324   -456     90       N  
ATOM   3323  CA  ALA B 107     -23.817  15.875  29.999  1.00 47.01           C  
ANISOU 3323  CA  ALA B 107     4511   5372   7976    405   -465     85       C  
ATOM   3324  C   ALA B 107     -24.664  14.820  29.277  1.00 47.37           C  
ANISOU 3324  C   ALA B 107     4420   5509   8070    444   -458     53       C  
ATOM   3325  O   ALA B 107     -24.132  13.756  28.949  1.00 47.47           O  
ANISOU 3325  O   ALA B 107     4349   5560   8125    384   -461     49       O  
ATOM   3326  CB  ALA B 107     -22.834  16.533  29.069  1.00 46.61           C  
ANISOU 3326  CB  ALA B 107     4522   5292   7896    365   -492    116       C  
ATOM   3327  N   ASP B 108     -25.950  15.097  29.057  1.00 48.22           N  
ANISOU 3327  N   ASP B 108     4503   5649   8166    540   -448     30       N  
ATOM   3328  CA  ASP B 108     -26.842  14.304  28.168  1.00 48.43           C  
ANISOU 3328  CA  ASP B 108     4404   5769   8226    582   -451     -2       C  
ATOM   3329  C   ASP B 108     -26.967  12.876  28.705  1.00 48.14           C  
ANISOU 3329  C   ASP B 108     4258   5775   8255    527   -426    -30       C  
ATOM   3330  O   ASP B 108     -26.868  11.920  27.895  1.00 47.58           O  
ANISOU 3330  O   ASP B 108     4096   5759   8220    495   -434    -48       O  
ATOM   3331  CB  ASP B 108     -26.335  14.334  26.725  1.00 48.44           C  
ANISOU 3331  CB  ASP B 108     4393   5795   8215    574   -485      7       C  
ATOM   3332  CG  ASP B 108     -26.110  15.747  26.217  1.00 49.09           C  
ANISOU 3332  CG  ASP B 108     4598   5823   8230    621   -504     40       C  
ATOM   3333  OD1 ASP B 108     -26.522  16.676  26.919  1.00 51.02           O  
ANISOU 3333  OD1 ASP B 108     4929   6017   8439    673   -490     49       O  
ATOM   3334  OD2 ASP B 108     -25.526  15.914  25.134  1.00 48.64           O  
ANISOU 3334  OD2 ASP B 108     4556   5770   8155    607   -527     58       O  
ATOM   3335  N   ASN B 109     -27.195  12.751  30.017  1.00 48.38           N  
ANISOU 3335  N   ASN B 109     4306   5779   8297    520   -392    -32       N  
ATOM   3336  CA  ASN B 109     -27.387  11.457  30.725  1.00 47.90           C  
ANISOU 3336  CA  ASN B 109     4159   5746   8293    473   -357    -54       C  
ATOM   3337  C   ASN B 109     -26.245  10.493  30.388  1.00 47.54           C  
ANISOU 3337  C   ASN B 109     4080   5702   8281    383   -367    -43       C  
ATOM   3338  O   ASN B 109     -26.577   9.314  30.171  1.00 47.77           O  
ANISOU 3338  O   ASN B 109     4010   5778   8360    359   -347    -71       O  
ATOM   3339  CB  ASN B 109     -28.707  10.800  30.326  1.00 48.34           C  
ANISOU 3339  CB  ASN B 109     4097   5884   8385    518   -339    -98       C  
ATOM   3340  CG  ASN B 109     -29.900  11.683  30.636  1.00 49.24           C  
ANISOU 3340  CG  ASN B 109     4226   6012   8468    617   -325   -108       C  
ATOM   3341  OD1 ASN B 109     -30.063  12.135  31.769  1.00 49.88           O  
ANISOU 3341  OD1 ASN B 109     4371   6049   8531    637   -296    -97       O  
ATOM   3342  ND2 ASN B 109     -30.728  11.948  29.639  1.00 48.67           N  
ANISOU 3342  ND2 ASN B 109     4099   6005   8385    685   -347   -129       N  
ATOM   3343  N   ASN B 110     -24.979  10.964  30.356  1.00 46.15           N  
ANISOU 3343  N   ASN B 110     3980   5476   8079    336   -393     -5       N  
ATOM   3344  CA  ASN B 110     -23.815  10.209  29.804  1.00 45.15           C  
ANISOU 3344  CA  ASN B 110     3820   5356   7975    263   -406     10       C  
ATOM   3345  C   ASN B 110     -23.034   9.493  30.917  1.00 43.86           C  
ANISOU 3345  C   ASN B 110     3660   5168   7834    200   -387     28       C  
ATOM   3346  O   ASN B 110     -21.989   8.906  30.606  1.00 43.33           O  
ANISOU 3346  O   ASN B 110     3572   5106   7784    145   -396     48       O  
ATOM   3347  CB  ASN B 110     -22.864  11.097  28.992  1.00 45.35           C  
ANISOU 3347  CB  ASN B 110     3912   5356   7961    246   -444     42       C  
ATOM   3348  CG  ASN B 110     -22.160  12.159  29.815  1.00 45.88           C  
ANISOU 3348  CG  ASN B 110     4094   5355   7984    221   -456     76       C  
ATOM   3349  OD1 ASN B 110     -22.421  12.322  31.002  1.00 47.24           O  
ANISOU 3349  OD1 ASN B 110     4304   5497   8148    226   -439     74       O  
ATOM   3350  ND2 ASN B 110     -21.283  12.919  29.187  1.00 45.76           N  
ANISOU 3350  ND2 ASN B 110     4138   5312   7936    193   -483    105       N  
ATOM   3351  N   CYS B 111     -23.526   9.517  32.157  1.00 43.10           N  
ANISOU 3351  N   CYS B 111     3589   5050   7736    214   -360     24       N  
ATOM   3352  CA  CYS B 111     -22.903   8.860  33.339  1.00 42.38           C  
ANISOU 3352  CA  CYS B 111     3508   4937   7657    166   -340     42       C  
ATOM   3353  C   CYS B 111     -22.585   7.386  33.036  1.00 41.65           C  
ANISOU 3353  C   CYS B 111     3326   4878   7620    128   -318     37       C  
ATOM   3354  O   CYS B 111     -21.552   6.882  33.543  1.00 42.18           O  
ANISOU 3354  O   CYS B 111     3402   4932   7691     81   -319     67       O  
ATOM   3355  CB  CYS B 111     -23.796   8.991  34.568  1.00 42.70           C  
ANISOU 3355  CB  CYS B 111     3575   4958   7688    202   -303     30       C  
ATOM   3356  SG  CYS B 111     -25.407   8.174  34.415  1.00 43.12           S  
ANISOU 3356  SG  CYS B 111     3527   5065   7790    250   -252    -17       S  
ATOM   3357  N   TYR B 112     -23.410   6.720  32.220  1.00 40.61           N  
ANISOU 3357  N   TYR B 112     3114   4790   7525    148   -300      1       N  
ATOM   3358  CA  TYR B 112     -23.270   5.281  31.882  1.00 39.69           C  
ANISOU 3358  CA  TYR B 112     2920   4699   7462    114   -272    -12       C  
ATOM   3359  C   TYR B 112     -22.122   5.102  30.885  1.00 39.43           C  
ANISOU 3359  C   TYR B 112     2879   4674   7428     81   -302      8       C  
ATOM   3360  O   TYR B 112     -21.406   4.101  31.014  1.00 39.12           O  
ANISOU 3360  O   TYR B 112     2814   4632   7415     45   -282     22       O  
ATOM   3361  CB  TYR B 112     -24.600   4.690  31.391  1.00 39.09           C  
ANISOU 3361  CB  TYR B 112     2764   4667   7421    138   -244    -65       C  
ATOM   3362  CG  TYR B 112     -24.918   4.912  29.936  1.00 38.49           C  
ANISOU 3362  CG  TYR B 112     2647   4635   7341    157   -277    -91       C  
ATOM   3363  CD1 TYR B 112     -24.797   3.897  29.003  1.00 38.13           C  
ANISOU 3363  CD1 TYR B 112     2538   4618   7328    128   -270   -116       C  
ATOM   3364  CD2 TYR B 112     -25.354   6.144  29.493  1.00 38.43           C  
ANISOU 3364  CD2 TYR B 112     2672   4637   7290    210   -312    -92       C  
ATOM   3365  CE1 TYR B 112     -25.092   4.108  27.666  1.00 38.16           C  
ANISOU 3365  CE1 TYR B 112     2510   4666   7321    148   -303   -142       C  
ATOM   3366  CE2 TYR B 112     -25.646   6.373  28.160  1.00 38.61           C  
ANISOU 3366  CE2 TYR B 112     2663   4703   7302    236   -344   -113       C  
ATOM   3367  CZ  TYR B 112     -25.520   5.351  27.243  1.00 38.31           C  
ANISOU 3367  CZ  TYR B 112     2560   4701   7296    203   -341   -139       C  
ATOM   3368  OH  TYR B 112     -25.802   5.601  25.933  1.00 38.84           O  
ANISOU 3368  OH  TYR B 112     2600   4813   7343    231   -375   -160       O  
ATOM   3369  N   LEU B 113     -21.952   6.031  29.941  1.00 39.84           N  
ANISOU 3369  N   LEU B 113     2955   4734   7448     97   -342     12       N  
ATOM   3370  CA  LEU B 113     -20.810   6.056  28.981  1.00 40.04           C  
ANISOU 3370  CA  LEU B 113     2982   4766   7464     67   -369     38       C  
ATOM   3371  C   LEU B 113     -19.505   6.318  29.736  1.00 39.56           C  
ANISOU 3371  C   LEU B 113     2971   4674   7385     23   -382     88       C  
ATOM   3372  O   LEU B 113     -18.510   5.632  29.451  1.00 39.19           O  
ANISOU 3372  O   LEU B 113     2894   4639   7354    -10   -379    110       O  
ATOM   3373  CB  LEU B 113     -21.028   7.143  27.923  1.00 40.89           C  
ANISOU 3373  CB  LEU B 113     3119   4883   7533     99   -405     34       C  
ATOM   3374  CG  LEU B 113     -21.844   6.703  26.713  1.00 41.45           C  
ANISOU 3374  CG  LEU B 113     3126   5004   7618    130   -406     -7       C  
ATOM   3375  CD1 LEU B 113     -22.001   7.839  25.710  1.00 41.73           C  
ANISOU 3375  CD1 LEU B 113     3202   5048   7606    171   -442     -2       C  
ATOM   3376  CD2 LEU B 113     -21.184   5.491  26.072  1.00 41.56           C  
ANISOU 3376  CD2 LEU B 113     3085   5039   7667     91   -390    -12       C  
ATOM   3377  N   ALA B 114     -19.502   7.293  30.645  1.00 39.36           N  
ANISOU 3377  N   ALA B 114     3017   4613   7323     26   -397    104       N  
ATOM   3378  CA  ALA B 114     -18.354   7.577  31.538  1.00 39.33           C  
ANISOU 3378  CA  ALA B 114     3060   4584   7297    -20   -414    145       C  
ATOM   3379  C   ALA B 114     -17.959   6.278  32.245  1.00 38.56           C  
ANISOU 3379  C   ALA B 114     2915   4499   7234    -40   -384    156       C  
ATOM   3380  O   ALA B 114     -16.788   5.915  32.181  1.00 38.53           O  
ANISOU 3380  O   ALA B 114     2895   4509   7234    -76   -396    189       O  
ATOM   3381  CB  ALA B 114     -18.691   8.667  32.530  1.00 39.71           C  
ANISOU 3381  CB  ALA B 114     3195   4590   7301     -9   -425    147       C  
ATOM   3382  N   THR B 115     -18.921   5.593  32.866  1.00 38.24           N  
ANISOU 3382  N   THR B 115     2853   4456   7219    -13   -344    130       N  
ATOM   3383  CA  THR B 115     -18.680   4.393  33.707  1.00 37.77           C  
ANISOU 3383  CA  THR B 115     2766   4396   7188    -24   -307    142       C  
ATOM   3384  C   THR B 115     -18.099   3.275  32.833  1.00 37.70           C  
ANISOU 3384  C   THR B 115     2692   4413   7218    -39   -291    146       C  
ATOM   3385  O   THR B 115     -17.078   2.671  33.243  1.00 37.49           O  
ANISOU 3385  O   THR B 115     2659   4390   7195    -59   -288    184       O  
ATOM   3386  CB  THR B 115     -19.950   4.011  34.470  1.00 37.53           C  
ANISOU 3386  CB  THR B 115     2730   4353   7174      5   -261    111       C  
ATOM   3387  OG1 THR B 115     -20.252   5.132  35.301  1.00 37.00           O  
ANISOU 3387  OG1 THR B 115     2736   4261   7062     20   -278    115       O  
ATOM   3388  CG2 THR B 115     -19.778   2.763  35.309  1.00 37.65           C  
ANISOU 3388  CG2 THR B 115     2727   4361   7217     -4   -215    125       C  
ATOM   3389  N   ALA B 116     -18.685   3.048  31.655  1.00 37.38           N  
ANISOU 3389  N   ALA B 116     2608   4392   7200    -26   -284    111       N  
ATOM   3390  CA  ALA B 116     -18.139   2.130  30.626  1.00 37.31           C  
ANISOU 3390  CA  ALA B 116     2549   4406   7220    -38   -272    110       C  
ATOM   3391  C   ALA B 116     -16.675   2.489  30.341  1.00 36.69           C  
ANISOU 3391  C   ALA B 116     2482   4338   7118    -62   -305    158       C  
ATOM   3392  O   ALA B 116     -15.815   1.597  30.409  1.00 36.36           O  
ANISOU 3392  O   ALA B 116     2414   4304   7094    -73   -286    185       O  
ATOM   3393  CB  ALA B 116     -18.969   2.202  29.366  1.00 37.44           C  
ANISOU 3393  CB  ALA B 116     2531   4446   7245    -21   -276     63       C  
ATOM   3394  N   LEU B 117     -16.425   3.756  30.015  1.00 36.47           N  
ANISOU 3394  N   LEU B 117     2493   4310   7053    -70   -349    170       N  
ATOM   3395  CA  LEU B 117     -15.120   4.269  29.523  1.00 36.38           C  
ANISOU 3395  CA  LEU B 117     2490   4314   7019   -102   -381    212       C  
ATOM   3396  C   LEU B 117     -14.049   4.055  30.596  1.00 36.33           C  
ANISOU 3396  C   LEU B 117     2489   4310   7005   -131   -388    257       C  
ATOM   3397  O   LEU B 117     -12.937   3.626  30.244  1.00 36.42           O  
ANISOU 3397  O   LEU B 117     2465   4350   7023   -149   -390    291       O  
ATOM   3398  CB  LEU B 117     -15.287   5.752  29.183  1.00 36.41           C  
ANISOU 3398  CB  LEU B 117     2551   4302   6980   -106   -420    211       C  
ATOM   3399  CG  LEU B 117     -14.081   6.422  28.547  1.00 36.79           C  
ANISOU 3399  CG  LEU B 117     2612   4362   7003   -145   -449    249       C  
ATOM   3400  CD1 LEU B 117     -13.709   5.702  27.262  1.00 36.99           C  
ANISOU 3400  CD1 LEU B 117     2581   4423   7051   -139   -431    248       C  
ATOM   3401  CD2 LEU B 117     -14.368   7.888  28.282  1.00 37.09           C  
ANISOU 3401  CD2 LEU B 117     2723   4371   6997   -148   -479    248       C  
ATOM   3402  N   LEU B 118     -14.383   4.331  31.856  1.00 36.33           N  
ANISOU 3402  N   LEU B 118     2529   4286   6988   -130   -392    259       N  
ATOM   3403  CA  LEU B 118     -13.453   4.203  33.005  1.00 36.71           C  
ANISOU 3403  CA  LEU B 118     2590   4340   7019   -154   -406    300       C  
ATOM   3404  C   LEU B 118     -13.109   2.722  33.197  1.00 37.22           C  
ANISOU 3404  C   LEU B 118     2599   4421   7119   -135   -366    316       C  
ATOM   3405  O   LEU B 118     -11.925   2.413  33.377  1.00 37.01           O  
ANISOU 3405  O   LEU B 118     2548   4426   7087   -150   -379    359       O  
ATOM   3406  CB  LEU B 118     -14.104   4.827  34.244  1.00 36.59           C  
ANISOU 3406  CB  LEU B 118     2640   4290   6973   -150   -414    289       C  
ATOM   3407  CG  LEU B 118     -14.153   6.352  34.227  1.00 36.81           C  
ANISOU 3407  CG  LEU B 118     2737   4294   6955   -173   -456    284       C  
ATOM   3408  CD1 LEU B 118     -15.233   6.878  35.151  1.00 37.19           C  
ANISOU 3408  CD1 LEU B 118     2848   4300   6980   -146   -446    257       C  
ATOM   3409  CD2 LEU B 118     -12.799   6.957  34.581  1.00 37.39           C  
ANISOU 3409  CD2 LEU B 118     2830   4382   6992   -232   -503    324       C  
ATOM   3410  N   THR B 119     -14.117   1.847  33.127  1.00 37.94           N  
ANISOU 3410  N   THR B 119     2674   4494   7245   -102   -316    282       N  
ATOM   3411  CA  THR B 119     -13.993   0.368  33.222  1.00 38.13           C  
ANISOU 3411  CA  THR B 119     2659   4518   7306    -81   -265    289       C  
ATOM   3412  C   THR B 119     -13.113  -0.174  32.084  1.00 38.43           C  
ANISOU 3412  C   THR B 119     2650   4587   7363    -82   -259    304       C  
ATOM   3413  O   THR B 119     -12.197  -0.936  32.386  1.00 38.77           O  
ANISOU 3413  O   THR B 119     2672   4646   7412    -72   -245    344       O  
ATOM   3414  CB  THR B 119     -15.370  -0.292  33.175  1.00 38.48           C  
ANISOU 3414  CB  THR B 119     2698   4535   7386    -60   -213    238       C  
ATOM   3415  OG1 THR B 119     -16.189   0.283  34.194  1.00 39.39           O  
ANISOU 3415  OG1 THR B 119     2856   4627   7482    -55   -215    226       O  
ATOM   3416  CG2 THR B 119     -15.296  -1.790  33.352  1.00 38.93           C  
ANISOU 3416  CG2 THR B 119     2733   4578   7479    -44   -153    244       C  
ATOM   3417  N   LEU B 120     -13.378   0.203  30.831  1.00 38.67           N  
ANISOU 3417  N   LEU B 120     2666   4627   7399    -87   -269    276       N  
ATOM   3418  CA  LEU B 120     -12.679  -0.324  29.621  1.00 39.03           C  
ANISOU 3418  CA  LEU B 120     2670   4699   7460    -84   -256    283       C  
ATOM   3419  C   LEU B 120     -11.169  -0.045  29.707  1.00 39.39           C  
ANISOU 3419  C   LEU B 120     2699   4782   7484   -101   -284    343       C  
ATOM   3420  O   LEU B 120     -10.392  -0.800  29.108  1.00 39.47           O  
ANISOU 3420  O   LEU B 120     2670   4815   7509    -87   -260    364       O  
ATOM   3421  CB  LEU B 120     -13.275   0.328  28.368  1.00 39.35           C  
ANISOU 3421  CB  LEU B 120     2710   4744   7493    -87   -273    244       C  
ATOM   3422  CG  LEU B 120     -14.658  -0.180  27.961  1.00 39.55           C  
ANISOU 3422  CG  LEU B 120     2729   4753   7545    -69   -243    181       C  
ATOM   3423  CD1 LEU B 120     -15.382   0.852  27.127  1.00 39.53           C  
ANISOU 3423  CD1 LEU B 120     2739   4759   7520    -66   -277    149       C  
ATOM   3424  CD2 LEU B 120     -14.560  -1.493  27.204  1.00 39.76           C  
ANISOU 3424  CD2 LEU B 120     2721   4781   7604    -58   -196    163       C  
ATOM   3425  N   GLN B 121     -10.769   0.993  30.445  1.00 39.63           N  
ANISOU 3425  N   GLN B 121     2757   4819   7480   -131   -331    369       N  
ATOM   3426  CA  GLN B 121      -9.349   1.367  30.670  1.00 39.91           C  
ANISOU 3426  CA  GLN B 121     2771   4899   7492   -160   -366    424       C  
ATOM   3427  C   GLN B 121      -8.693   0.463  31.730  1.00 40.56           C  
ANISOU 3427  C   GLN B 121     2831   4999   7577   -140   -353    463       C  
ATOM   3428  O   GLN B 121      -7.472   0.607  31.934  1.00 41.35           O  
ANISOU 3428  O   GLN B 121     2900   5151   7661   -158   -380    511       O  
ATOM   3429  CB  GLN B 121      -9.268   2.832  31.102  1.00 39.64           C  
ANISOU 3429  CB  GLN B 121     2785   4859   7417   -209   -421    428       C  
ATOM   3430  CG  GLN B 121      -9.628   3.817  30.000  1.00 39.21           C  
ANISOU 3430  CG  GLN B 121     2756   4792   7351   -227   -436    404       C  
ATOM   3431  CD  GLN B 121      -9.791   5.204  30.567  1.00 39.37           C  
ANISOU 3431  CD  GLN B 121     2843   4785   7330   -267   -480    400       C  
ATOM   3432  OE1 GLN B 121      -8.859   5.790  31.117  1.00 39.28           O  
ANISOU 3432  OE1 GLN B 121     2840   4792   7291   -316   -516    433       O  
ATOM   3433  NE2 GLN B 121     -11.004   5.728  30.482  1.00 39.69           N  
ANISOU 3433  NE2 GLN B 121     2934   4781   7363   -244   -477    359       N  
ATOM   3434  N   GLN B 122      -9.447  -0.423  32.387  1.00 40.52           N  
ANISOU 3434  N   GLN B 122     2843   4960   7592   -103   -312    447       N  
ATOM   3435  CA  GLN B 122      -8.965  -1.183  33.569  1.00 41.10           C  
ANISOU 3435  CA  GLN B 122     2915   5042   7658    -77   -300    486       C  
ATOM   3436  C   GLN B 122      -9.138  -2.696  33.384  1.00 42.05           C  
ANISOU 3436  C   GLN B 122     3018   5142   7817    -24   -230    486       C  
ATOM   3437  O   GLN B 122      -8.811  -3.418  34.351  1.00 42.23           O  
ANISOU 3437  O   GLN B 122     3047   5164   7834      7   -212    521       O  
ATOM   3438  CB  GLN B 122      -9.741  -0.751  34.808  1.00 41.01           C  
ANISOU 3438  CB  GLN B 122     2961   4996   7624    -83   -313    472       C  
ATOM   3439  CG  GLN B 122      -9.505   0.691  35.201  1.00 41.13           C  
ANISOU 3439  CG  GLN B 122     3009   5023   7594   -133   -379    475       C  
ATOM   3440  CD  GLN B 122     -10.345   1.068  36.397  1.00 41.19           C  
ANISOU 3440  CD  GLN B 122     3081   4991   7575   -131   -383    457       C  
ATOM   3441  OE1 GLN B 122     -10.198   0.511  37.474  1.00 41.93           O  
ANISOU 3441  OE1 GLN B 122     3188   5086   7655   -109   -373    481       O  
ATOM   3442  NE2 GLN B 122     -11.251   2.014  36.218  1.00 41.06           N  
ANISOU 3442  NE2 GLN B 122     3108   4941   7550   -147   -394    416       N  
ATOM   3443  N   ILE B 123      -9.639  -3.154  32.225  1.00 42.23           N  
ANISOU 3443  N   ILE B 123     3026   5144   7873    -16   -192    448       N  
ATOM   3444  CA  ILE B 123      -9.857  -4.599  31.918  1.00 42.51           C  
ANISOU 3444  CA  ILE B 123     3056   5150   7946     25   -120    439       C  
ATOM   3445  C   ILE B 123      -9.226  -4.892  30.553  1.00 42.98           C  
ANISOU 3445  C   ILE B 123     3076   5235   8018     34   -106    439       C  
ATOM   3446  O   ILE B 123      -9.375  -4.052  29.645  1.00 42.16           O  
ANISOU 3446  O   ILE B 123     2963   5147   7907      4   -137    414       O  
ATOM   3447  CB  ILE B 123     -11.355  -4.984  31.960  1.00 42.61           C  
ANISOU 3447  CB  ILE B 123     3100   5103   7984     21    -78    377       C  
ATOM   3448  CG1 ILE B 123     -12.214  -4.140  31.016  1.00 42.32           C  
ANISOU 3448  CG1 ILE B 123     3061   5067   7951     -9   -104    321       C  
ATOM   3449  CG2 ILE B 123     -11.905  -4.938  33.377  1.00 42.87           C  
ANISOU 3449  CG2 ILE B 123     3173   5109   8006     24    -73    384       C  
ATOM   3450  CD1 ILE B 123     -13.459  -4.837  30.577  1.00 42.26           C  
ANISOU 3450  CD1 ILE B 123     3058   5020   7978    -10    -55    258       C  
ATOM   3451  N   GLU B 124      -8.546  -6.038  30.437  1.00 44.21           N  
ANISOU 3451  N   GLU B 124     3215   5392   8188     79    -58    470       N  
ATOM   3452  CA  GLU B 124      -7.767  -6.454  29.236  1.00 45.26           C  
ANISOU 3452  CA  GLU B 124     3313   5553   8330    100    -36    480       C  
ATOM   3453  C   GLU B 124      -8.784  -6.844  28.157  1.00 44.39           C  
ANISOU 3453  C   GLU B 124     3222   5398   8245     91      0    410       C  
ATOM   3454  O   GLU B 124      -9.604  -7.735  28.435  1.00 43.96           O  
ANISOU 3454  O   GLU B 124     3200   5287   8215    102     51    377       O  
ATOM   3455  CB  GLU B 124      -6.810  -7.611  29.578  1.00 46.86           C  
ANISOU 3455  CB  GLU B 124     3501   5764   8538    164     10    535       C  
ATOM   3456  CG  GLU B 124      -5.358  -7.373  29.169  1.00 48.23           C  
ANISOU 3456  CG  GLU B 124     3614   6016   8694    181    -11    593       C  
ATOM   3457  CD  GLU B 124      -4.364  -7.037  30.291  1.00 49.36           C  
ANISOU 3457  CD  GLU B 124     3725   6221   8808    191    -56    662       C  
ATOM   3458  OE1 GLU B 124      -4.761  -7.109  31.508  1.00 51.76           O  
ANISOU 3458  OE1 GLU B 124     4062   6500   9101    194    -66    669       O  
ATOM   3459  OE2 GLU B 124      -3.164  -6.722  29.959  1.00 46.96           O  
ANISOU 3459  OE2 GLU B 124     3358   5994   8490    194    -81    709       O  
ATOM   3460  N   LEU B 125      -8.752  -6.191  26.992  1.00 44.23           N  
ANISOU 3460  N   LEU B 125     3184   5403   8215     69    -23    387       N  
ATOM   3461  CA  LEU B 125      -9.759  -6.382  25.912  1.00 44.64           C  
ANISOU 3461  CA  LEU B 125     3251   5426   8281     56     -3    315       C  
ATOM   3462  C   LEU B 125      -9.214  -5.894  24.563  1.00 44.68           C  
ANISOU 3462  C   LEU B 125     3235   5471   8269     51    -20    314       C  
ATOM   3463  O   LEU B 125      -8.478  -4.903  24.559  1.00 43.84           O  
ANISOU 3463  O   LEU B 125     3108   5410   8139     34    -65    355       O  
ATOM   3464  CB  LEU B 125     -10.998  -5.581  26.313  1.00 44.67           C  
ANISOU 3464  CB  LEU B 125     3276   5412   8283     19    -39    271       C  
ATOM   3465  CG  LEU B 125     -12.282  -5.949  25.589  1.00 44.96           C  
ANISOU 3465  CG  LEU B 125     3325   5418   8338      7    -17    194       C  
ATOM   3466  CD1 LEU B 125     -12.900  -7.182  26.222  1.00 45.40           C  
ANISOU 3466  CD1 LEU B 125     3400   5420   8427     14     44    171       C  
ATOM   3467  CD2 LEU B 125     -13.270  -4.790  25.611  1.00 45.07           C  
ANISOU 3467  CD2 LEU B 125     3345   5442   8338    -20    -68    159       C  
ATOM   3468  N   LYS B 126      -9.596  -6.542  23.460  1.00 45.88           N  
ANISOU 3468  N   LYS B 126     3395   5605   8430     61     16    267       N  
ATOM   3469  CA  LYS B 126      -9.143  -6.189  22.080  1.00 47.27           C  
ANISOU 3469  CA  LYS B 126     3559   5817   8585     63      9    262       C  
ATOM   3470  C   LYS B 126     -10.340  -6.215  21.126  1.00 46.69           C  
ANISOU 3470  C   LYS B 126     3507   5723   8509     46      8    183       C  
ATOM   3471  O   LYS B 126     -10.951  -7.290  20.974  1.00 46.54           O  
ANISOU 3471  O   LYS B 126     3506   5663   8512     54     54    135       O  
ATOM   3472  CB  LYS B 126      -8.066  -7.164  21.581  1.00 49.09           C  
ANISOU 3472  CB  LYS B 126     3776   6056   8819    108     65    295       C  
ATOM   3473  CG  LYS B 126      -6.704  -7.032  22.256  1.00 50.93           C  
ANISOU 3473  CG  LYS B 126     3970   6334   9046    130     60    379       C  
ATOM   3474  CD  LYS B 126      -5.877  -5.828  21.789  1.00 51.94           C  
ANISOU 3474  CD  LYS B 126     4061   6526   9145    104     13    419       C  
ATOM   3475  CE  LYS B 126      -4.940  -5.282  22.855  1.00 52.45           C  
ANISOU 3475  CE  LYS B 126     4088   6636   9203     93    -22    488       C  
ATOM   3476  NZ  LYS B 126      -4.202  -4.091  22.382  1.00 52.76           N  
ANISOU 3476  NZ  LYS B 126     4097   6732   9216     53    -63    520       N  
ATOM   3477  N   PHE B 127     -10.652  -5.080  20.504  1.00 46.31           N  
ANISOU 3477  N   PHE B 127     3459   5703   8433     25    -42    169       N  
ATOM   3478  CA  PHE B 127     -11.799  -4.922  19.577  1.00 46.94           C  
ANISOU 3478  CA  PHE B 127     3553   5780   8501     14    -57     96       C  
ATOM   3479  C   PHE B 127     -11.432  -5.495  18.209  1.00 47.44           C  
ANISOU 3479  C   PHE B 127     3622   5855   8548     33    -26     75       C  
ATOM   3480  O   PHE B 127     -10.316  -5.310  17.755  1.00 48.84           O  
ANISOU 3480  O   PHE B 127     3789   6059   8707     49    -17    124       O  
ATOM   3481  CB  PHE B 127     -12.260  -3.462  19.516  1.00 46.60           C  
ANISOU 3481  CB  PHE B 127     3517   5761   8429     -3   -121     97       C  
ATOM   3482  CG  PHE B 127     -12.936  -3.034  20.792  1.00 46.48           C  
ANISOU 3482  CG  PHE B 127     3506   5726   8428    -19   -144     97       C  
ATOM   3483  CD1 PHE B 127     -14.151  -3.592  21.163  1.00 46.59           C  
ANISOU 3483  CD1 PHE B 127     3520   5714   8467    -24   -131     41       C  
ATOM   3484  CD2 PHE B 127     -12.329  -2.143  21.657  1.00 46.09           C  
ANISOU 3484  CD2 PHE B 127     3461   5683   8367    -31   -175    153       C  
ATOM   3485  CE1 PHE B 127     -14.761  -3.234  22.353  1.00 46.34           C  
ANISOU 3485  CE1 PHE B 127     3493   5665   8447    -35   -144     43       C  
ATOM   3486  CE2 PHE B 127     -12.936  -1.793  22.851  1.00 46.23           C  
ANISOU 3486  CE2 PHE B 127     3490   5680   8394    -42   -192    152       C  
ATOM   3487  CZ  PHE B 127     -14.157  -2.329  23.192  1.00 46.36           C  
ANISOU 3487  CZ  PHE B 127     3508   5672   8434    -40   -175     98       C  
ATOM   3488  N   ASN B 128     -12.381  -6.190  17.590  1.00 48.69           N  
ANISOU 3488  N   ASN B 128     3793   5993   8711     29     -9      2       N  
ATOM   3489  CA  ASN B 128     -12.223  -6.821  16.258  1.00 49.45           C  
ANISOU 3489  CA  ASN B 128     3905   6095   8787     44     20    -33       C  
ATOM   3490  C   ASN B 128     -12.356  -5.753  15.177  1.00 49.11           C  
ANISOU 3490  C   ASN B 128     3865   6098   8695     45    -27    -42       C  
ATOM   3491  O   ASN B 128     -11.590  -5.769  14.223  1.00 50.15           O  
ANISOU 3491  O   ASN B 128     4007   6251   8798     66    -10    -25       O  
ATOM   3492  CB  ASN B 128     -13.155  -8.025  16.113  1.00 50.61           C  
ANISOU 3492  CB  ASN B 128     4070   6200   8957     30     58   -111       C  
ATOM   3493  CG  ASN B 128     -12.584  -9.229  16.843  1.00 51.79           C  
ANISOU 3493  CG  ASN B 128     4233   6299   9144     46    128    -87       C  
ATOM   3494  OD1 ASN B 128     -13.038  -9.602  17.924  1.00 52.26           O  
ANISOU 3494  OD1 ASN B 128     4293   6323   9239     31    142    -88       O  
ATOM   3495  ND2 ASN B 128     -11.504  -9.779  16.316  1.00 53.07           N  
ANISOU 3495  ND2 ASN B 128     4408   6459   9296     84    173    -54       N  
ATOM   3496  N   PRO B 129     -13.296  -4.784  15.267  1.00 48.71           N  
ANISOU 3496  N   PRO B 129     3811   6064   8629     29    -85    -65       N  
ATOM   3497  CA  PRO B 129     -13.316  -3.667  14.318  1.00 48.70           C  
ANISOU 3497  CA  PRO B 129     3822   6103   8576     39   -130    -59       C  
ATOM   3498  C   PRO B 129     -12.100  -2.760  14.495  1.00 48.43           C  
ANISOU 3498  C   PRO B 129     3789   6085   8527     41   -138     24       C  
ATOM   3499  O   PRO B 129     -11.794  -2.353  15.613  1.00 48.18           O  
ANISOU 3499  O   PRO B 129     3745   6041   8516     26   -148     68       O  
ATOM   3500  CB  PRO B 129     -14.621  -2.916  14.633  1.00 48.62           C  
ANISOU 3500  CB  PRO B 129     3808   6102   8560     29   -184    -97       C  
ATOM   3501  CG  PRO B 129     -15.432  -3.876  15.493  1.00 48.35           C  
ANISOU 3501  CG  PRO B 129     3756   6038   8577      9   -160   -143       C  
ATOM   3502  CD  PRO B 129     -14.410  -4.723  16.226  1.00 48.20           C  
ANISOU 3502  CD  PRO B 129     3736   5983   8594      7   -105    -97       C  
ATOM   3503  N   PRO B 130     -11.341  -2.452  13.418  1.00 48.35           N  
ANISOU 3503  N   PRO B 130     3792   6102   8477     56   -129     48       N  
ATOM   3504  CA  PRO B 130     -10.276  -1.455  13.495  1.00 48.07           C  
ANISOU 3504  CA  PRO B 130     3755   6085   8423     48   -139    124       C  
ATOM   3505  C   PRO B 130     -10.789  -0.138  14.102  1.00 48.09           C  
ANISOU 3505  C   PRO B 130     3773   6083   8414     27   -195    139       C  
ATOM   3506  O   PRO B 130     -10.214   0.321  15.091  1.00 49.04           O  
ANISOU 3506  O   PRO B 130     3882   6196   8551      2   -204    188       O  
ATOM   3507  CB  PRO B 130      -9.849  -1.254  12.036  1.00 48.04           C  
ANISOU 3507  CB  PRO B 130     3772   6110   8369     68   -125    127       C  
ATOM   3508  CG  PRO B 130     -10.232  -2.543  11.338  1.00 48.58           C  
ANISOU 3508  CG  PRO B 130     3846   6172   8440     92    -88     65       C  
ATOM   3509  CD  PRO B 130     -11.445  -3.063  12.083  1.00 48.62           C  
ANISOU 3509  CD  PRO B 130     3843   6149   8480     79   -106      4       C  
ATOM   3510  N   ALA B 131     -11.862   0.418  13.524  1.00 46.90           N  
ANISOU 3510  N   ALA B 131     3649   5938   8231     40   -232     95       N  
ATOM   3511  CA  ALA B 131     -12.483   1.690  13.961  1.00 46.29           C  
ANISOU 3511  CA  ALA B 131     3599   5853   8135     34   -283    103       C  
ATOM   3512  C   ALA B 131     -12.553   1.729  15.498  1.00 45.25           C  
ANISOU 3512  C   ALA B 131     3452   5695   8046     10   -290    120       C  
ATOM   3513  O   ALA B 131     -12.211   2.773  16.064  1.00 45.05           O  
ANISOU 3513  O   ALA B 131     3449   5658   8010     -9   -314    164       O  
ATOM   3514  CB  ALA B 131     -13.854   1.824  13.355  1.00 46.70           C  
ANISOU 3514  CB  ALA B 131     3663   5919   8161     63   -316     39       C  
ATOM   3515  N   LEU B 132     -12.983   0.639  16.143  1.00 45.04           N  
ANISOU 3515  N   LEU B 132     3394   5653   8063      9   -268     86       N  
ATOM   3516  CA  LEU B 132     -13.158   0.549  17.619  1.00 44.92           C  
ANISOU 3516  CA  LEU B 132     3368   5611   8086     -8   -270     97       C  
ATOM   3517  C   LEU B 132     -11.805   0.437  18.318  1.00 45.68           C  
ANISOU 3517  C   LEU B 132     3451   5707   8199    -29   -250    163       C  
ATOM   3518  O   LEU B 132     -11.672   1.058  19.384  1.00 47.43           O  
ANISOU 3518  O   LEU B 132     3681   5915   8425    -49   -272    194       O  
ATOM   3519  CB  LEU B 132     -14.015  -0.661  18.005  1.00 44.56           C  
ANISOU 3519  CB  LEU B 132     3299   5550   8081     -4   -243     42       C  
ATOM   3520  CG  LEU B 132     -15.516  -0.421  18.105  1.00 44.47           C  
ANISOU 3520  CG  LEU B 132     3287   5540   8069      1   -270    -17       C  
ATOM   3521  CD1 LEU B 132     -16.177  -1.602  18.791  1.00 44.83           C  
ANISOU 3521  CD1 LEU B 132     3307   5563   8162     -9   -235    -59       C  
ATOM   3522  CD2 LEU B 132     -15.836   0.863  18.858  1.00 44.08           C  
ANISOU 3522  CD2 LEU B 132     3260   5483   8003      2   -311      8       C  
ATOM   3523  N   GLN B 133     -10.869  -0.363  17.797  1.00 45.78           N  
ANISOU 3523  N   GLN B 133     3441   5734   8219    -20   -210    183       N  
ATOM   3524  CA  GLN B 133      -9.533  -0.537  18.433  1.00 46.28           C  
ANISOU 3524  CA  GLN B 133     3477   5809   8296    -32   -192    249       C  
ATOM   3525  C   GLN B 133      -8.784   0.803  18.332  1.00 46.32           C  
ANISOU 3525  C   GLN B 133     3494   5836   8269    -63   -225    301       C  
ATOM   3526  O   GLN B 133      -8.347   1.315  19.385  1.00 45.33           O  
ANISOU 3526  O   GLN B 133     3364   5709   8149    -93   -247    339       O  
ATOM   3527  CB  GLN B 133      -8.779  -1.725  17.815  1.00 46.86           C  
ANISOU 3527  CB  GLN B 133     3525   5896   8382     -4   -136    256       C  
ATOM   3528  CG  GLN B 133      -7.492  -2.106  18.548  1.00 47.10           C  
ANISOU 3528  CG  GLN B 133     3517   5947   8432     -2   -113    322       C  
ATOM   3529  CD  GLN B 133      -7.687  -2.524  19.989  1.00 47.29           C  
ANISOU 3529  CD  GLN B 133     3534   5947   8486     -4   -116    330       C  
ATOM   3530  OE1 GLN B 133      -8.638  -3.214  20.339  1.00 46.88           O  
ANISOU 3530  OE1 GLN B 133     3498   5857   8456      6   -101    284       O  
ATOM   3531  NE2 GLN B 133      -6.764  -2.124  20.849  1.00 47.88           N  
ANISOU 3531  NE2 GLN B 133     3582   6048   8560    -21   -134    390       N  
ATOM   3532  N   ASP B 134      -8.694   1.371  17.122  1.00 46.64           N  
ANISOU 3532  N   ASP B 134     3554   5891   8273    -59   -228    300       N  
ATOM   3533  CA  ASP B 134      -8.080   2.704  16.870  1.00 46.73           C  
ANISOU 3533  CA  ASP B 134     3590   5915   8250    -93   -253    345       C  
ATOM   3534  C   ASP B 134      -8.608   3.693  17.921  1.00 45.97           C  
ANISOU 3534  C   ASP B 134     3528   5788   8150   -122   -298    347       C  
ATOM   3535  O   ASP B 134      -7.798   4.225  18.681  1.00 46.14           O  
ANISOU 3535  O   ASP B 134     3543   5815   8173   -164   -312    393       O  
ATOM   3536  CB  ASP B 134      -8.308   3.173  15.426  1.00 47.50           C  
ANISOU 3536  CB  ASP B 134     3722   6021   8303    -75   -250    331       C  
ATOM   3537  CG  ASP B 134      -7.349   2.580  14.392  1.00 48.31           C  
ANISOU 3537  CG  ASP B 134     3798   6158   8397    -60   -203    353       C  
ATOM   3538  OD1 ASP B 134      -7.522   2.883  13.180  1.00 48.89           O  
ANISOU 3538  OD1 ASP B 134     3904   6241   8429    -41   -197    341       O  
ATOM   3539  OD2 ASP B 134      -6.436   1.821  14.787  1.00 48.39           O  
ANISOU 3539  OD2 ASP B 134     3758   6188   8436    -62   -170    384       O  
ATOM   3540  N   ALA B 135      -9.924   3.885  18.002  1.00 45.49           N  
ANISOU 3540  N   ALA B 135     3500   5701   8084    -98   -321    297       N  
ATOM   3541  CA  ALA B 135     -10.569   4.884  18.891  1.00 45.43           C  
ANISOU 3541  CA  ALA B 135     3534   5660   8065   -113   -360    294       C  
ATOM   3542  C   ALA B 135     -10.308   4.562  20.373  1.00 44.50           C  
ANISOU 3542  C   ALA B 135     3396   5531   7979   -137   -363    310       C  
ATOM   3543  O   ALA B 135     -10.187   5.510  21.171  1.00 44.05           O  
ANISOU 3543  O   ALA B 135     3375   5454   7907   -168   -392    332       O  
ATOM   3544  CB  ALA B 135     -12.047   4.954  18.595  1.00 45.89           C  
ANISOU 3544  CB  ALA B 135     3615   5705   8113    -70   -376    235       C  
ATOM   3545  N   TYR B 136     -10.213   3.277  20.724  1.00 44.11           N  
ANISOU 3545  N   TYR B 136     3299   5491   7967   -121   -333    300       N  
ATOM   3546  CA  TYR B 136      -9.952   2.774  22.104  1.00 43.94           C  
ANISOU 3546  CA  TYR B 136     3257   5462   7974   -132   -329    317       C  
ATOM   3547  C   TYR B 136      -8.540   3.170  22.554  1.00 44.26           C  
ANISOU 3547  C   TYR B 136     3279   5529   8006   -174   -340    381       C  
ATOM   3548  O   TYR B 136      -8.354   3.458  23.752  1.00 43.44           O  
ANISOU 3548  O   TYR B 136     3183   5418   7903   -198   -362    400       O  
ATOM   3549  CB  TYR B 136     -10.144   1.258  22.149  1.00 43.38           C  
ANISOU 3549  CB  TYR B 136     3148   5391   7941   -100   -285    294       C  
ATOM   3550  CG  TYR B 136      -9.982   0.567  23.484  1.00 43.01           C  
ANISOU 3550  CG  TYR B 136     3085   5333   7921    -98   -272    310       C  
ATOM   3551  CD1 TYR B 136     -10.335   1.154  24.689  1.00 42.76           C  
ANISOU 3551  CD1 TYR B 136     3081   5281   7884   -116   -301    315       C  
ATOM   3552  CD2 TYR B 136      -9.546  -0.745  23.521  1.00 43.10           C  
ANISOU 3552  CD2 TYR B 136     3064   5350   7961    -72   -226    318       C  
ATOM   3553  CE1 TYR B 136     -10.231   0.466  25.893  1.00 42.64           C  
ANISOU 3553  CE1 TYR B 136     3057   5256   7888   -109   -286    330       C  
ATOM   3554  CE2 TYR B 136      -9.425  -1.439  24.710  1.00 43.04           C  
ANISOU 3554  CE2 TYR B 136     3048   5328   7973    -62   -210    336       C  
ATOM   3555  CZ  TYR B 136      -9.780  -0.843  25.902  1.00 42.58           C  
ANISOU 3555  CZ  TYR B 136     3015   5255   7908    -81   -241    342       C  
ATOM   3556  OH  TYR B 136      -9.645  -1.589  27.040  1.00 41.82           O  
ANISOU 3556  OH  TYR B 136     2914   5146   7826    -66   -221    362       O  
ATOM   3557  N   TYR B 137      -7.571   3.169  21.635  1.00 44.82           N  
ANISOU 3557  N   TYR B 137     3323   5636   8068   -182   -324    412       N  
ATOM   3558  CA  TYR B 137      -6.197   3.656  21.920  1.00 46.17           C  
ANISOU 3558  CA  TYR B 137     3467   5845   8230   -229   -335    473       C  
ATOM   3559  C   TYR B 137      -6.252   5.165  22.173  1.00 47.89           C  
ANISOU 3559  C   TYR B 137     3741   6040   8414   -284   -379    482       C  
ATOM   3560  O   TYR B 137      -5.804   5.587  23.250  1.00 46.95           O  
ANISOU 3560  O   TYR B 137     3623   5924   8291   -326   -408    506       O  
ATOM   3561  CB  TYR B 137      -5.216   3.304  20.798  1.00 45.41           C  
ANISOU 3561  CB  TYR B 137     3326   5794   8132   -223   -300    502       C  
ATOM   3562  CG  TYR B 137      -4.720   1.883  20.829  1.00 44.47           C  
ANISOU 3562  CG  TYR B 137     3148   5703   8044   -177   -256    512       C  
ATOM   3563  CD1 TYR B 137      -4.215   1.322  21.989  1.00 44.33           C  
ANISOU 3563  CD1 TYR B 137     3092   5703   8047   -174   -258    540       C  
ATOM   3564  CD2 TYR B 137      -4.752   1.100  19.687  1.00 44.24           C  
ANISOU 3564  CD2 TYR B 137     3108   5681   8019   -133   -210    495       C  
ATOM   3565  CE1 TYR B 137      -3.752   0.017  22.013  1.00 44.73           C  
ANISOU 3565  CE1 TYR B 137     3098   5775   8123   -122   -213    554       C  
ATOM   3566  CE2 TYR B 137      -4.297  -0.207  19.690  1.00 44.21           C  
ANISOU 3566  CE2 TYR B 137     3063   5694   8041    -86   -163    504       C  
ATOM   3567  CZ  TYR B 137      -3.795  -0.750  20.860  1.00 44.72           C  
ANISOU 3567  CZ  TYR B 137     3091   5773   8127    -78   -163    535       C  
ATOM   3568  OH  TYR B 137      -3.350  -2.039  20.892  1.00 44.88           O  
ANISOU 3568  OH  TYR B 137     3078   5804   8170    -23   -113    549       O  
ATOM   3569  N   ARG B 138      -6.823   5.927  21.234  1.00 51.19           N  
ANISOU 3569  N   ARG B 138     4211   6434   8805   -279   -383    463       N  
ATOM   3570  CA  ARG B 138      -6.885   7.413  21.293  1.00 54.34           C  
ANISOU 3570  CA  ARG B 138     4680   6800   9166   -325   -416    473       C  
ATOM   3571  C   ARG B 138      -7.778   7.859  22.465  1.00 54.02           C  
ANISOU 3571  C   ARG B 138     4689   6713   9121   -324   -448    447       C  
ATOM   3572  O   ARG B 138      -7.590   8.989  22.936  1.00 53.34           O  
ANISOU 3572  O   ARG B 138     4660   6599   9008   -373   -475    462       O  
ATOM   3573  CB  ARG B 138      -7.314   7.977  19.932  1.00 57.49           C  
ANISOU 3573  CB  ARG B 138     5124   7185   9534   -302   -406    461       C  
ATOM   3574  CG  ARG B 138      -6.238   7.864  18.860  1.00 60.70           C  
ANISOU 3574  CG  ARG B 138     5496   7634   9933   -319   -375    498       C  
ATOM   3575  CD  ARG B 138      -6.515   8.708  17.625  1.00 63.19           C  
ANISOU 3575  CD  ARG B 138     5873   7930  10205   -308   -368    498       C  
ATOM   3576  NE  ARG B 138      -6.473  10.160  17.836  1.00 65.67           N  
ANISOU 3576  NE  ARG B 138     6267   8200  10483   -358   -392    519       N  
ATOM   3577  CZ  ARG B 138      -7.539  10.965  17.984  1.00 66.36           C  
ANISOU 3577  CZ  ARG B 138     6436   8233  10543   -333   -417    492       C  
ATOM   3578  NH1 ARG B 138      -8.775  10.479  17.981  1.00 66.58           N  
ANISOU 3578  NH1 ARG B 138     6466   8253  10578   -261   -427    443       N  
ATOM   3579  NH2 ARG B 138      -7.356  12.269  18.142  1.00 66.35           N  
ANISOU 3579  NH2 ARG B 138     6515   8185  10507   -380   -431    515       N  
ATOM   3580  N   ALA B 139      -8.677   6.993  22.948  1.00 54.40           N  
ANISOU 3580  N   ALA B 139     4720   6752   9195   -275   -439    409       N  
ATOM   3581  CA  ALA B 139      -9.469   7.194  24.186  1.00 54.46           C  
ANISOU 3581  CA  ALA B 139     4764   6724   9204   -270   -460    387       C  
ATOM   3582  C   ALA B 139      -8.551   7.202  25.416  1.00 55.60           C  
ANISOU 3582  C   ALA B 139     4892   6881   9350   -319   -478    422       C  
ATOM   3583  O   ALA B 139      -8.578   8.195  26.156  1.00 56.36           O  
ANISOU 3583  O   ALA B 139     5046   6947   9419   -356   -509    427       O  
ATOM   3584  CB  ALA B 139     -10.509   6.115  24.311  1.00 54.20           C  
ANISOU 3584  CB  ALA B 139     4703   6687   9203   -213   -437    343       C  
ATOM   3585  N   ARG B 140      -7.775   6.130  25.620  1.00 57.01           N  
ANISOU 3585  N   ARG B 140     4999   7105   9557   -314   -459    446       N  
ATOM   3586  CA  ARG B 140      -6.849   5.957  26.780  1.00 58.06           C  
ANISOU 3586  CA  ARG B 140     5102   7266   9691   -350   -478    482       C  
ATOM   3587  C   ARG B 140      -5.904   7.161  26.867  1.00 57.06           C  
ANISOU 3587  C   ARG B 140     4995   7151   9531   -429   -514    516       C  
ATOM   3588  O   ARG B 140      -5.588   7.578  28.000  1.00 57.17           O  
ANISOU 3588  O   ARG B 140     5028   7166   9528   -470   -548    527       O  
ATOM   3589  CB  ARG B 140      -6.034   4.661  26.682  1.00 59.76           C  
ANISOU 3589  CB  ARG B 140     5233   7535   9937   -322   -447    510       C  
ATOM   3590  CG  ARG B 140      -6.116   3.772  27.922  1.00 61.78           C  
ANISOU 3590  CG  ARG B 140     5470   7794  10208   -294   -442    515       C  
ATOM   3591  CD  ARG B 140      -4.766   3.317  28.453  1.00 64.33           C  
ANISOU 3591  CD  ARG B 140     5727   8182  10532   -307   -450    569       C  
ATOM   3592  NE  ARG B 140      -4.004   2.606  27.427  1.00 66.41           N  
ANISOU 3592  NE  ARG B 140     5926   8491  10816   -282   -413    594       N  
ATOM   3593  CZ  ARG B 140      -2.692   2.733  27.193  1.00 66.77           C  
ANISOU 3593  CZ  ARG B 140     5909   8605  10855   -311   -420    643       C  
ATOM   3594  NH1 ARG B 140      -1.935   3.548  27.919  1.00 65.97           N  
ANISOU 3594  NH1 ARG B 140     5797   8539  10729   -376   -470    672       N  
ATOM   3595  NH2 ARG B 140      -2.147   2.036  26.208  1.00 66.51           N  
ANISOU 3595  NH2 ARG B 140     5823   8606  10840   -275   -377    660       N  
ATOM   3596  N   ALA B 141      -5.480   7.679  25.708  1.00 56.63           N  
ANISOU 3596  N   ALA B 141     4941   7107   9467   -451   -504    529       N  
ATOM   3597  CA  ALA B 141      -4.617   8.875  25.548  1.00 56.67           C  
ANISOU 3597  CA  ALA B 141     4971   7118   9441   -535   -528    559       C  
ATOM   3598  C   ALA B 141      -5.304  10.118  26.125  1.00 56.73           C  
ANISOU 3598  C   ALA B 141     5085   7055   9413   -566   -560    536       C  
ATOM   3599  O   ALA B 141      -4.646  10.857  26.889  1.00 56.60           O  
ANISOU 3599  O   ALA B 141     5091   7039   9374   -642   -594    554       O  
ATOM   3600  CB  ALA B 141      -4.286   9.076  24.090  1.00 56.67           C  
ANISOU 3600  CB  ALA B 141     4962   7131   9437   -535   -498    573       C  
ATOM   3601  N   GLY B 142      -6.578  10.335  25.780  1.00 56.40           N  
ANISOU 3601  N   GLY B 142     5105   6959   9365   -509   -551    497       N  
ATOM   3602  CA  GLY B 142      -7.365  11.497  26.246  1.00 56.04           C  
ANISOU 3602  CA  GLY B 142     5167   6841   9283   -519   -573    474       C  
ATOM   3603  C   GLY B 142      -8.407  11.940  25.232  1.00 54.55           C  
ANISOU 3603  C   GLY B 142     5035   6611   9080   -461   -556    449       C  
ATOM   3604  O   GLY B 142      -9.361  12.617  25.654  1.00 55.44           O  
ANISOU 3604  O   GLY B 142     5226   6668   9170   -434   -567    422       O  
ATOM   3605  N   GLU B 143      -8.213  11.605  23.949  1.00 52.94           N  
ANISOU 3605  N   GLU B 143     4793   6436   8884   -439   -531    457       N  
ATOM   3606  CA  GLU B 143      -9.158  11.923  22.847  1.00 53.20           C  
ANISOU 3606  CA  GLU B 143     4870   6444   8898   -376   -518    435       C  
ATOM   3607  C   GLU B 143     -10.206  10.801  22.729  1.00 52.06           C  
ANISOU 3607  C   GLU B 143     4676   6320   8784   -296   -505    392       C  
ATOM   3608  O   GLU B 143     -10.075   9.901  21.849  1.00 52.60           O  
ANISOU 3608  O   GLU B 143     4682   6430   8873   -268   -481    388       O  
ATOM   3609  CB  GLU B 143      -8.399  12.204  21.555  1.00 54.07           C  
ANISOU 3609  CB  GLU B 143     4976   6574   8992   -399   -499    466       C  
ATOM   3610  CG  GLU B 143      -9.263  12.794  20.446  1.00 55.53           C  
ANISOU 3610  CG  GLU B 143     5225   6729   9142   -340   -492    450       C  
ATOM   3611  CD  GLU B 143     -10.717  13.182  20.720  1.00 55.71           C  
ANISOU 3611  CD  GLU B 143     5309   6710   9148   -270   -507    410       C  
ATOM   3612  OE1 GLU B 143     -11.022  13.755  21.800  1.00 55.07           O  
ANISOU 3612  OE1 GLU B 143     5278   6584   9058   -285   -526    403       O  
ATOM   3613  OE2 GLU B 143     -11.552  12.860  19.850  1.00 55.06           O  
ANISOU 3613  OE2 GLU B 143     5217   6644   9060   -198   -501    383       O  
ATOM   3614  N   ALA B 144     -11.227  10.870  23.592  1.00 49.63           N  
ANISOU 3614  N   ALA B 144     4397   5982   8478   -262   -516    360       N  
ATOM   3615  CA  ALA B 144     -12.247   9.818  23.800  1.00 48.30           C  
ANISOU 3615  CA  ALA B 144     4179   5829   8343   -201   -503    317       C  
ATOM   3616  C   ALA B 144     -13.583  10.204  23.152  1.00 46.99           C  
ANISOU 3616  C   ALA B 144     4047   5648   8158   -132   -505    279       C  
ATOM   3617  O   ALA B 144     -14.566   9.501  23.387  1.00 46.58           O  
ANISOU 3617  O   ALA B 144     3960   5608   8130    -87   -497    240       O  
ATOM   3618  CB  ALA B 144     -12.400   9.575  25.280  1.00 48.04           C  
ANISOU 3618  CB  ALA B 144     4146   5781   8325   -213   -509    312       C  
ATOM   3619  N   ALA B 145     -13.620  11.294  22.388  1.00 46.23           N  
ANISOU 3619  N   ALA B 145     4018   5529   8018   -125   -516    292       N  
ATOM   3620  CA  ALA B 145     -14.822  11.773  21.682  1.00 45.42           C  
ANISOU 3620  CA  ALA B 145     3950   5418   7887    -51   -522    263       C  
ATOM   3621  C   ALA B 145     -15.223  10.712  20.663  1.00 45.29           C  
ANISOU 3621  C   ALA B 145     3858   5457   7890    -10   -510    233       C  
ATOM   3622  O   ALA B 145     -16.365  10.218  20.756  1.00 46.17           O  
ANISOU 3622  O   ALA B 145     3937   5588   8018     40   -512    188       O  
ATOM   3623  CB  ALA B 145     -14.574  13.100  21.024  1.00 45.63           C  
ANISOU 3623  CB  ALA B 145     4071   5407   7860    -53   -531    293       C  
ATOM   3624  N   ASN B 146     -14.317  10.355  19.754  1.00 44.72           N  
ANISOU 3624  N   ASN B 146     3760   5411   7818    -36   -497    255       N  
ATOM   3625  CA  ASN B 146     -14.603   9.358  18.689  1.00 45.46           C  
ANISOU 3625  CA  ASN B 146     3793   5555   7923     -1   -484    225       C  
ATOM   3626  C   ASN B 146     -15.117   8.059  19.310  1.00 44.68           C  
ANISOU 3626  C   ASN B 146     3620   5477   7876      5   -470    184       C  
ATOM   3627  O   ASN B 146     -16.207   7.599  18.931  1.00 44.76           O  
ANISOU 3627  O   ASN B 146     3602   5512   7892     51   -474    135       O  
ATOM   3628  CB  ASN B 146     -13.383   9.018  17.841  1.00 46.64           C  
ANISOU 3628  CB  ASN B 146     3921   5728   8070    -35   -462    258       C  
ATOM   3629  CG  ASN B 146     -13.392   9.798  16.555  1.00 48.57           C  
ANISOU 3629  CG  ASN B 146     4218   5975   8261     -9   -467    271       C  
ATOM   3630  OD1 ASN B 146     -13.861   9.297  15.540  1.00 49.57           O  
ANISOU 3630  OD1 ASN B 146     4322   6136   8374     34   -464    241       O  
ATOM   3631  ND2 ASN B 146     -12.922  11.036  16.608  1.00 50.44           N  
ANISOU 3631  ND2 ASN B 146     4530   6173   8463    -35   -473    313       N  
ATOM   3632  N   PHE B 147     -14.330   7.486  20.217  1.00 43.45           N  
ANISOU 3632  N   PHE B 147     3434   5316   7756    -39   -455    205       N  
ATOM   3633  CA  PHE B 147     -14.609   6.174  20.844  1.00 41.98           C  
ANISOU 3633  CA  PHE B 147     3185   5142   7620    -38   -432    177       C  
ATOM   3634  C   PHE B 147     -16.044   6.156  21.376  1.00 41.85           C  
ANISOU 3634  C   PHE B 147     3168   5118   7613     -1   -440    129       C  
ATOM   3635  O   PHE B 147     -16.739   5.147  21.148  1.00 42.51           O  
ANISOU 3635  O   PHE B 147     3202   5224   7725     16   -422     84       O  
ATOM   3636  CB  PHE B 147     -13.604   5.905  21.959  1.00 41.14           C  
ANISOU 3636  CB  PHE B 147     3067   5025   7537    -84   -423    216       C  
ATOM   3637  CG  PHE B 147     -13.729   4.533  22.555  1.00 40.12           C  
ANISOU 3637  CG  PHE B 147     2883   4903   7454    -79   -392    198       C  
ATOM   3638  CD1 PHE B 147     -13.738   3.422  21.734  1.00 39.89           C  
ANISOU 3638  CD1 PHE B 147     2810   4898   7447    -63   -362    174       C  
ATOM   3639  CD2 PHE B 147     -13.848   4.360  23.924  1.00 39.66           C  
ANISOU 3639  CD2 PHE B 147     2828   4825   7415    -91   -390    204       C  
ATOM   3640  CE1 PHE B 147     -13.853   2.155  22.276  1.00 39.79           C  
ANISOU 3640  CE1 PHE B 147     2759   4881   7476    -60   -328    157       C  
ATOM   3641  CE2 PHE B 147     -13.966   3.094  24.465  1.00 39.41           C  
ANISOU 3641  CE2 PHE B 147     2755   4794   7423    -84   -356    190       C  
ATOM   3642  CZ  PHE B 147     -13.979   1.995  23.640  1.00 39.64           C  
ANISOU 3642  CZ  PHE B 147     2744   4841   7477    -69   -324    167       C  
ATOM   3643  N   CYS B 148     -16.465   7.234  22.051  1.00 41.26           N  
ANISOU 3643  N   CYS B 148     3149   5013   7515      7   -462    138       N  
ATOM   3644  CA  CYS B 148     -17.825   7.391  22.630  1.00 40.92           C  
ANISOU 3644  CA  CYS B 148     3108   4964   7475     48   -467     99       C  
ATOM   3645  C   CYS B 148     -18.853   7.330  21.491  1.00 40.59           C  
ANISOU 3645  C   CYS B 148     3042   4961   7419    101   -477     55       C  
ATOM   3646  O   CYS B 148     -19.739   6.466  21.535  1.00 40.13           O  
ANISOU 3646  O   CYS B 148     2924   4930   7390    116   -464      8       O  
ATOM   3647  CB  CYS B 148     -17.934   8.682  23.439  1.00 41.14           C  
ANISOU 3647  CB  CYS B 148     3213   4947   7469     52   -486    122       C  
ATOM   3648  SG  CYS B 148     -17.113   8.607  25.057  1.00 41.00           S  
ANISOU 3648  SG  CYS B 148     3216   4894   7468     -3   -478    154       S  
ATOM   3649  N   ALA B 149     -18.695   8.179  20.478  1.00 40.69           N  
ANISOU 3649  N   ALA B 149     3097   4978   7385    124   -498     71       N  
ATOM   3650  CA  ALA B 149     -19.553   8.222  19.272  1.00 41.02           C  
ANISOU 3650  CA  ALA B 149     3121   5062   7399    179   -515     36       C  
ATOM   3651  C   ALA B 149     -19.750   6.803  18.733  1.00 40.99           C  
ANISOU 3651  C   ALA B 149     3038   5105   7432    167   -498     -9       C  
ATOM   3652  O   ALA B 149     -20.908   6.396  18.500  1.00 41.20           O  
ANISOU 3652  O   ALA B 149     3017   5170   7466    199   -506    -62       O  
ATOM   3653  CB  ALA B 149     -18.930   9.116  18.233  1.00 41.19           C  
ANISOU 3653  CB  ALA B 149     3204   5078   7367    190   -530     72       C  
ATOM   3654  N   LEU B 150     -18.651   6.080  18.539  1.00 41.03           N  
ANISOU 3654  N   LEU B 150     3027   5104   7456    122   -474     10       N  
ATOM   3655  CA  LEU B 150     -18.675   4.701  18.002  1.00 41.28           C  
ANISOU 3655  CA  LEU B 150     2997   5165   7519    108   -450    -28       C  
ATOM   3656  C   LEU B 150     -19.475   3.825  18.962  1.00 41.60           C  
ANISOU 3656  C   LEU B 150     2990   5204   7611     96   -430    -69       C  
ATOM   3657  O   LEU B 150     -20.319   3.069  18.468  1.00 43.02           O  
ANISOU 3657  O   LEU B 150     3123   5418   7804    104   -427   -127       O  
ATOM   3658  CB  LEU B 150     -17.247   4.188  17.824  1.00 41.24           C  
ANISOU 3658  CB  LEU B 150     2993   5149   7526     69   -422     11       C  
ATOM   3659  CG  LEU B 150     -16.491   4.783  16.643  1.00 41.81           C  
ANISOU 3659  CG  LEU B 150     3100   5233   7551     76   -430     42       C  
ATOM   3660  CD1 LEU B 150     -15.064   4.271  16.610  1.00 41.59           C  
ANISOU 3660  CD1 LEU B 150     3062   5200   7540     38   -397     86       C  
ATOM   3661  CD2 LEU B 150     -17.193   4.467  15.329  1.00 42.32           C  
ANISOU 3661  CD2 LEU B 150     3151   5340   7586    113   -441     -6       C  
ATOM   3662  N   ILE B 151     -19.262   3.947  20.274  1.00 41.21           N  
ANISOU 3662  N   ILE B 151     2954   5118   7586     76   -418    -42       N  
ATOM   3663  CA  ILE B 151     -20.010   3.127  21.273  1.00 41.20           C  
ANISOU 3663  CA  ILE B 151     2912   5109   7631     65   -391    -74       C  
ATOM   3664  C   ILE B 151     -21.508   3.398  21.076  1.00 41.21           C  
ANISOU 3664  C   ILE B 151     2886   5145   7625    103   -410   -127       C  
ATOM   3665  O   ILE B 151     -22.236   2.428  20.812  1.00 41.26           O  
ANISOU 3665  O   ILE B 151     2836   5179   7660     94   -393   -181       O  
ATOM   3666  CB  ILE B 151     -19.540   3.387  22.718  1.00 41.13           C  
ANISOU 3666  CB  ILE B 151     2932   5056   7635     45   -379    -32       C  
ATOM   3667  CG1 ILE B 151     -18.110   2.891  22.939  1.00 41.28           C  
ANISOU 3667  CG1 ILE B 151     2958   5058   7668      8   -360     14       C  
ATOM   3668  CG2 ILE B 151     -20.502   2.769  23.726  1.00 40.96           C  
ANISOU 3668  CG2 ILE B 151     2881   5028   7652     44   -352    -65       C  
ATOM   3669  CD1 ILE B 151     -17.478   3.392  24.219  1.00 41.25           C  
ANISOU 3669  CD1 ILE B 151     2990   5021   7661    -11   -363     61       C  
ATOM   3670  N   LEU B 152     -21.929   4.667  21.150  1.00 41.41           N  
ANISOU 3670  N   LEU B 152     2951   5170   7611    145   -442   -112       N  
ATOM   3671  CA  LEU B 152     -23.333   5.114  20.926  1.00 41.78           C  
ANISOU 3671  CA  LEU B 152     2973   5259   7642    198   -465   -153       C  
ATOM   3672  C   LEU B 152     -23.837   4.514  19.610  1.00 43.06           C  
ANISOU 3672  C   LEU B 152     3082   5482   7796    208   -480   -204       C  
ATOM   3673  O   LEU B 152     -24.935   3.925  19.596  1.00 43.09           O  
ANISOU 3673  O   LEU B 152     3018   5530   7823    212   -477   -261       O  
ATOM   3674  CB  LEU B 152     -23.400   6.646  20.887  1.00 41.14           C  
ANISOU 3674  CB  LEU B 152     2961   5162   7505    250   -497   -118       C  
ATOM   3675  CG  LEU B 152     -23.222   7.347  22.234  1.00 40.54           C  
ANISOU 3675  CG  LEU B 152     2942   5030   7430    247   -486    -81       C  
ATOM   3676  CD1 LEU B 152     -22.990   8.830  22.043  1.00 40.46           C  
ANISOU 3676  CD1 LEU B 152     3021   4988   7361    285   -514    -41       C  
ATOM   3677  CD2 LEU B 152     -24.409   7.111  23.151  1.00 40.49           C  
ANISOU 3677  CD2 LEU B 152     2894   5039   7452    269   -468   -116       C  
ATOM   3678  N   ALA B 153     -23.046   4.635  18.545  1.00 44.36           N  
ANISOU 3678  N   ALA B 153     3274   5651   7928    207   -494   -186       N  
ATOM   3679  CA  ALA B 153     -23.379   4.109  17.202  1.00 45.88           C  
ANISOU 3679  CA  ALA B 153     3430   5899   8101    217   -511   -232       C  
ATOM   3680  C   ALA B 153     -23.614   2.595  17.280  1.00 47.30           C  
ANISOU 3680  C   ALA B 153     3546   6091   8335    166   -477   -286       C  
ATOM   3681  O   ALA B 153     -24.731   2.157  16.947  1.00 47.35           O  
ANISOU 3681  O   ALA B 153     3492   6150   8347    171   -489   -349       O  
ATOM   3682  CB  ALA B 153     -22.279   4.462  16.238  1.00 46.23           C  
ANISOU 3682  CB  ALA B 153     3527   5934   8105    219   -519   -193       C  
ATOM   3683  N   TYR B 154     -22.608   1.837  17.736  1.00 48.82           N  
ANISOU 3683  N   TYR B 154     3751   6235   8563    118   -435   -261       N  
ATOM   3684  CA  TYR B 154     -22.595   0.350  17.732  1.00 50.48           C  
ANISOU 3684  CA  TYR B 154     3922   6438   8819     69   -392   -304       C  
ATOM   3685  C   TYR B 154     -23.726  -0.215  18.602  1.00 51.04           C  
ANISOU 3685  C   TYR B 154     3941   6515   8936     49   -372   -350       C  
ATOM   3686  O   TYR B 154     -24.101  -1.370  18.366  1.00 50.98           O  
ANISOU 3686  O   TYR B 154     3895   6514   8959     10   -344   -404       O  
ATOM   3687  CB  TYR B 154     -21.232  -0.197  18.175  1.00 51.05           C  
ANISOU 3687  CB  TYR B 154     4025   6455   8915     38   -350   -254       C  
ATOM   3688  CG  TYR B 154     -20.225  -0.344  17.058  1.00 51.93           C  
ANISOU 3688  CG  TYR B 154     4161   6572   8997     41   -348   -236       C  
ATOM   3689  CD1 TYR B 154     -20.443  -1.222  16.006  1.00 52.65           C  
ANISOU 3689  CD1 TYR B 154     4234   6688   9083     32   -339   -291       C  
ATOM   3690  CD2 TYR B 154     -19.056   0.402  17.037  1.00 51.68           C  
ANISOU 3690  CD2 TYR B 154     4173   6522   8941     49   -353   -167       C  
ATOM   3691  CE1 TYR B 154     -19.529  -1.363  14.974  1.00 52.67           C  
ANISOU 3691  CE1 TYR B 154     4262   6694   9054     39   -332   -275       C  
ATOM   3692  CE2 TYR B 154     -18.142   0.289  16.003  1.00 51.51           C  
ANISOU 3692  CE2 TYR B 154     4169   6509   8891     53   -346   -148       C  
ATOM   3693  CZ  TYR B 154     -18.373  -0.604  14.974  1.00 52.01           C  
ANISOU 3693  CZ  TYR B 154     4217   6595   8948     52   -333   -201       C  
ATOM   3694  OH  TYR B 154     -17.476  -0.712  13.953  1.00 52.58           O  
ANISOU 3694  OH  TYR B 154     4312   6677   8989     60   -321   -183       O  
ATOM   3695  N   CYS B 155     -24.234   0.550  19.573  1.00 52.22           N  
ANISOU 3695  N   CYS B 155     4092   6658   9088     71   -380   -330       N  
ATOM   3696  CA  CYS B 155     -25.297   0.115  20.526  1.00 54.43           C  
ANISOU 3696  CA  CYS B 155     4324   6943   9412     55   -353   -365       C  
ATOM   3697  C   CYS B 155     -26.672   0.681  20.130  1.00 55.37           C  
ANISOU 3697  C   CYS B 155     4391   7135   9510     95   -392   -411       C  
ATOM   3698  O   CYS B 155     -27.633   0.481  20.902  1.00 54.26           O  
ANISOU 3698  O   CYS B 155     4205   7010   9402     88   -372   -438       O  
ATOM   3699  CB  CYS B 155     -24.949   0.553  21.944  1.00 54.23           C  
ANISOU 3699  CB  CYS B 155     4338   6865   9401     58   -331   -311       C  
ATOM   3700  SG  CYS B 155     -23.293   0.035  22.452  1.00 53.91           S  
ANISOU 3700  SG  CYS B 155     4352   6755   9376     22   -296   -249       S  
ATOM   3701  N   ASN B 156     -26.749   1.375  18.987  1.00 57.01           N  
ANISOU 3701  N   ASN B 156     4606   7389   9664    139   -444   -416       N  
ATOM   3702  CA  ASN B 156     -27.983   2.006  18.442  1.00 58.90           C  
ANISOU 3702  CA  ASN B 156     4797   7708   9870    194   -490   -454       C  
ATOM   3703  C   ASN B 156     -28.602   2.953  19.476  1.00 58.16           C  
ANISOU 3703  C   ASN B 156     4710   7610   9776    243   -491   -427       C  
ATOM   3704  O   ASN B 156     -29.822   3.174  19.414  1.00 57.48           O  
ANISOU 3704  O   ASN B 156     4560   7592   9685    279   -510   -465       O  
ATOM   3705  CB  ASN B 156     -29.007   0.965  17.983  1.00 61.22           C  
ANISOU 3705  CB  ASN B 156     4999   8069  10192    155   -489   -538       C  
ATOM   3706  CG  ASN B 156     -28.417   0.018  16.962  1.00 63.44           C  
ANISOU 3706  CG  ASN B 156     5285   8348  10470    108   -485   -569       C  
ATOM   3707  OD1 ASN B 156     -28.656   0.165  15.764  1.00 66.19           O  
ANISOU 3707  OD1 ASN B 156     5620   8756  10771    132   -531   -600       O  
ATOM   3708  ND2 ASN B 156     -27.611  -0.929  17.422  1.00 63.18           N  
ANISOU 3708  ND2 ASN B 156     5278   8246  10480     48   -430   -559       N  
ATOM   3709  N   LYS B 157     -27.783   3.519  20.365  1.00 56.72           N  
ANISOU 3709  N   LYS B 157     4602   7354   9593    246   -472   -364       N  
ATOM   3710  CA  LYS B 157     -28.188   4.607  21.292  1.00 56.53           C  
ANISOU 3710  CA  LYS B 157     4612   7312   9553    299   -474   -330       C  
ATOM   3711  C   LYS B 157     -27.975   5.959  20.596  1.00 56.06           C  
ANISOU 3711  C   LYS B 157     4619   7256   9425    370   -521   -293       C  
ATOM   3712  O   LYS B 157     -27.255   6.007  19.586  1.00 55.63           O  
ANISOU 3712  O   LYS B 157     4594   7201   9341    365   -543   -281       O  
ATOM   3713  CB  LYS B 157     -27.405   4.501  22.602  1.00 55.33           C  
ANISOU 3713  CB  LYS B 157     4512   7079   9429    260   -432   -286       C  
ATOM   3714  CG  LYS B 157     -27.520   3.148  23.290  1.00 55.25           C  
ANISOU 3714  CG  LYS B 157     4451   7056   9482    194   -379   -315       C  
ATOM   3715  CD  LYS B 157     -27.662   3.248  24.806  1.00 55.29           C  
ANISOU 3715  CD  LYS B 157     4478   7017   9510    189   -340   -291       C  
ATOM   3716  CE  LYS B 157     -28.404   2.079  25.427  1.00 55.52           C  
ANISOU 3716  CE  LYS B 157     4439   7057   9597    145   -287   -333       C  
ATOM   3717  NZ  LYS B 157     -29.849   2.089  25.084  1.00 55.85           N  
ANISOU 3717  NZ  LYS B 157     4396   7177   9645    170   -295   -390       N  
ATOM   3718  N   THR B 158     -28.632   7.006  21.093  1.00 56.01           N  
ANISOU 3718  N   THR B 158     4637   7250   9391    439   -531   -277       N  
ATOM   3719  CA  THR B 158     -28.422   8.421  20.681  1.00 55.16           C  
ANISOU 3719  CA  THR B 158     4617   7123   9217    511   -564   -232       C  
ATOM   3720  C   THR B 158     -28.081   9.233  21.935  1.00 54.13           C  
ANISOU 3720  C   THR B 158     4570   6913   9081    519   -541   -186       C  
ATOM   3721  O   THR B 158     -28.307   8.745  23.070  1.00 53.16           O  
ANISOU 3721  O   THR B 158     4423   6772   9002    487   -504   -195       O  
ATOM   3722  CB  THR B 158     -29.636   8.998  19.934  1.00 55.08           C  
ANISOU 3722  CB  THR B 158     4567   7195   9165    605   -602   -259       C  
ATOM   3723  OG1 THR B 158     -30.712   9.056  20.864  1.00 54.52           O  
ANISOU 3723  OG1 THR B 158     4447   7149   9118    638   -582   -279       O  
ATOM   3724  CG2 THR B 158     -30.050   8.189  18.724  1.00 55.00           C  
ANISOU 3724  CG2 THR B 158     4471   7271   9154    594   -632   -312       C  
ATOM   3725  N   VAL B 159     -27.545  10.433  21.738  1.00 53.43           N  
ANISOU 3725  N   VAL B 159     4585   6776   8939    556   -559   -138       N  
ATOM   3726  CA  VAL B 159     -27.159  11.337  22.856  1.00 52.76           C  
ANISOU 3726  CA  VAL B 159     4598   6609   8839    560   -541    -95       C  
ATOM   3727  C   VAL B 159     -28.430  11.680  23.637  1.00 52.72           C  
ANISOU 3727  C   VAL B 159     4570   6626   8835    629   -527   -116       C  
ATOM   3728  O   VAL B 159     -29.490  11.793  23.004  1.00 52.91           O  
ANISOU 3728  O   VAL B 159     4536   6724   8844    702   -546   -144       O  
ATOM   3729  CB  VAL B 159     -26.439  12.591  22.333  1.00 52.37           C  
ANISOU 3729  CB  VAL B 159     4665   6504   8726    586   -563    -46       C  
ATOM   3730  CG1 VAL B 159     -26.069  13.527  23.471  1.00 52.05           C  
ANISOU 3730  CG1 VAL B 159     4731   6377   8666    582   -546     -9       C  
ATOM   3731  CG2 VAL B 159     -25.216  12.211  21.511  1.00 51.93           C  
ANISOU 3731  CG2 VAL B 159     4621   6439   8671    518   -572    -26       C  
ATOM   3732  N   GLY B 160     -28.329  11.788  24.962  1.00 52.37           N  
ANISOU 3732  N   GLY B 160     4564   6528   8807    608   -494   -103       N  
ATOM   3733  CA  GLY B 160     -29.467  12.137  25.835  1.00 53.31           C  
ANISOU 3733  CA  GLY B 160     4669   6659   8924    674   -470   -118       C  
ATOM   3734  C   GLY B 160     -30.261  10.912  26.256  1.00 53.07           C  
ANISOU 3734  C   GLY B 160     4515   6692   8957    646   -440   -165       C  
ATOM   3735  O   GLY B 160     -30.766  10.904  27.400  1.00 52.91           O  
ANISOU 3735  O   GLY B 160     4494   6657   8952    656   -402   -169       O  
ATOM   3736  N   GLU B 161     -30.380   9.922  25.365  1.00 52.74           N  
ANISOU 3736  N   GLU B 161     4377   6715   8946    609   -454   -200       N  
ATOM   3737  CA  GLU B 161     -30.966   8.589  25.657  1.00 53.02           C  
ANISOU 3737  CA  GLU B 161     4298   6801   9046    556   -422   -248       C  
ATOM   3738  C   GLU B 161     -30.371   8.077  26.974  1.00 51.76           C  
ANISOU 3738  C   GLU B 161     4173   6572   8921    490   -374   -229       C  
ATOM   3739  O   GLU B 161     -29.133   8.156  27.127  1.00 53.36           O  
ANISOU 3739  O   GLU B 161     4451   6708   9115    444   -379   -191       O  
ATOM   3740  CB  GLU B 161     -30.686   7.634  24.491  1.00 54.01           C  
ANISOU 3740  CB  GLU B 161     4358   6972   9191    504   -444   -279       C  
ATOM   3741  CG  GLU B 161     -31.551   6.384  24.466  1.00 55.58           C  
ANISOU 3741  CG  GLU B 161     4433   7237   9445    460   -419   -340       C  
ATOM   3742  CD  GLU B 161     -31.555   5.594  23.165  1.00 56.95           C  
ANISOU 3742  CD  GLU B 161     4541   7469   9625    425   -448   -383       C  
ATOM   3743  OE1 GLU B 161     -32.141   4.492  23.153  1.00 58.98           O  
ANISOU 3743  OE1 GLU B 161     4708   7770   9931    372   -425   -435       O  
ATOM   3744  OE2 GLU B 161     -31.028   6.093  22.163  1.00 57.25           O  
ANISOU 3744  OE2 GLU B 161     4621   7510   9618    451   -492   -366       O  
ATOM   3745  N   LEU B 162     -31.221   7.615  27.897  1.00 50.91           N  
ANISOU 3745  N   LEU B 162     4012   6482   8848    490   -329   -252       N  
ATOM   3746  CA  LEU B 162     -30.813   6.897  29.132  1.00 49.61           C  
ANISOU 3746  CA  LEU B 162     3864   6263   8720    427   -277   -240       C  
ATOM   3747  C   LEU B 162     -30.097   5.612  28.737  1.00 48.03           C  
ANISOU 3747  C   LEU B 162     3625   6058   8563    339   -268   -252       C  
ATOM   3748  O   LEU B 162     -30.368   5.095  27.642  1.00 47.64           O  
ANISOU 3748  O   LEU B 162     3508   6065   8528    327   -288   -288       O  
ATOM   3749  CB  LEU B 162     -32.041   6.565  29.974  1.00 50.44           C  
ANISOU 3749  CB  LEU B 162     3903   6405   8855    446   -226   -269       C  
ATOM   3750  CG  LEU B 162     -32.698   7.774  30.621  1.00 51.75           C  
ANISOU 3750  CG  LEU B 162     4118   6564   8979    536   -220   -252       C  
ATOM   3751  CD1 LEU B 162     -34.182   7.504  30.841  1.00 52.80           C  
ANISOU 3751  CD1 LEU B 162     4143   6777   9139    575   -184   -293       C  
ATOM   3752  CD2 LEU B 162     -31.973   8.165  31.917  1.00 51.29           C  
ANISOU 3752  CD2 LEU B 162     4172   6414   8901    524   -193   -210       C  
ATOM   3753  N   GLY B 163     -29.241   5.113  29.622  1.00 46.25           N  
ANISOU 3753  N   GLY B 163     3447   5770   8356    286   -237   -223       N  
ATOM   3754  CA  GLY B 163     -28.318   4.024  29.277  1.00 45.38           C  
ANISOU 3754  CA  GLY B 163     3323   5641   8276    214   -229   -221       C  
ATOM   3755  C   GLY B 163     -28.068   3.101  30.442  1.00 44.51           C  
ANISOU 3755  C   GLY B 163     3219   5488   8202    167   -172   -209       C  
ATOM   3756  O   GLY B 163     -28.303   3.510  31.596  1.00 44.22           O  
ANISOU 3756  O   GLY B 163     3223   5423   8153    187   -147   -190       O  
ATOM   3757  N   ASP B 164     -27.610   1.896  30.117  1.00 43.83           N  
ANISOU 3757  N   ASP B 164     3102   5395   8154    110   -150   -220       N  
ATOM   3758  CA  ASP B 164     -27.258   0.824  31.078  1.00 44.15           C  
ANISOU 3758  CA  ASP B 164     3153   5392   8230     64    -91   -206       C  
ATOM   3759  C   ASP B 164     -25.798   0.421  30.819  1.00 44.48           C  
ANISOU 3759  C   ASP B 164     3235   5396   8266     34   -105   -168       C  
ATOM   3760  O   ASP B 164     -25.454   0.084  29.658  1.00 44.01           O  
ANISOU 3760  O   ASP B 164     3149   5358   8213     19   -126   -184       O  
ATOM   3761  CB  ASP B 164     -28.234  -0.343  30.926  1.00 44.10           C  
ANISOU 3761  CB  ASP B 164     3065   5413   8277     27    -40   -261       C  
ATOM   3762  CG  ASP B 164     -28.066  -1.426  31.966  1.00 44.00           C  
ANISOU 3762  CG  ASP B 164     3068   5350   8299    -14     30   -247       C  
ATOM   3763  OD1 ASP B 164     -26.985  -1.989  32.074  1.00 44.93           O  
ANISOU 3763  OD1 ASP B 164     3226   5423   8419    -36     38   -214       O  
ATOM   3764  OD2 ASP B 164     -29.044  -1.685  32.677  1.00 44.29           O  
ANISOU 3764  OD2 ASP B 164     3074   5394   8358    -18     79   -268       O  
ATOM   3765  N   VAL B 165     -24.963   0.457  31.856  1.00 44.90           N  
ANISOU 3765  N   VAL B 165     3350   5403   8307     28    -93   -118       N  
ATOM   3766  CA  VAL B 165     -23.533   0.045  31.762  1.00 46.01           C  
ANISOU 3766  CA  VAL B 165     3522   5516   8443      4   -103    -75       C  
ATOM   3767  C   VAL B 165     -23.477  -1.407  31.260  1.00 47.35           C  
ANISOU 3767  C   VAL B 165     3648   5683   8659    -30    -59    -99       C  
ATOM   3768  O   VAL B 165     -22.814  -1.634  30.218  1.00 48.18           O  
ANISOU 3768  O   VAL B 165     3741   5799   8764    -39    -80    -99       O  
ATOM   3769  CB  VAL B 165     -22.817   0.237  33.110  1.00 45.68           C  
ANISOU 3769  CB  VAL B 165     3543   5434   8378      5    -95    -22       C  
ATOM   3770  CG1 VAL B 165     -21.502  -0.529  33.178  1.00 44.92           C  
ANISOU 3770  CG1 VAL B 165     3461   5319   8288    -17    -89     18       C  
ATOM   3771  CG2 VAL B 165     -22.609   1.714  33.409  1.00 45.69           C  
ANISOU 3771  CG2 VAL B 165     3601   5432   8326     29   -147      0       C  
ATOM   3772  N   ARG B 166     -24.185  -2.324  31.938  1.00 47.67           N  
ANISOU 3772  N   ARG B 166     3670   5706   8736    -48      4   -119       N  
ATOM   3773  CA  ARG B 166     -24.149  -3.786  31.662  1.00 48.65           C  
ANISOU 3773  CA  ARG B 166     3770   5809   8905    -86     59   -140       C  
ATOM   3774  C   ARG B 166     -24.595  -4.063  30.223  1.00 49.06           C  
ANISOU 3774  C   ARG B 166     3766   5899   8972   -104     42   -198       C  
ATOM   3775  O   ARG B 166     -23.960  -4.885  29.555  1.00 48.21           O  
ANISOU 3775  O   ARG B 166     3660   5777   8879   -124     56   -201       O  
ATOM   3776  CB  ARG B 166     -25.028  -4.555  32.650  1.00 49.91           C  
ANISOU 3776  CB  ARG B 166     3922   5943   9098   -106    133   -157       C  
ATOM   3777  CG  ARG B 166     -24.867  -6.063  32.535  1.00 51.07           C  
ANISOU 3777  CG  ARG B 166     4067   6050   9287   -146    199   -169       C  
ATOM   3778  CD  ARG B 166     -25.833  -6.925  33.331  1.00 52.32           C  
ANISOU 3778  CD  ARG B 166     4214   6179   9483   -178    281   -194       C  
ATOM   3779  NE  ARG B 166     -27.223  -6.506  33.245  1.00 53.55           N  
ANISOU 3779  NE  ARG B 166     4309   6383   9653   -189    283   -247       N  
ATOM   3780  CZ  ARG B 166     -27.961  -6.502  32.137  1.00 54.09           C  
ANISOU 3780  CZ  ARG B 166     4308   6504   9738   -212    259   -311       C  
ATOM   3781  NH1 ARG B 166     -27.461  -6.898  30.977  1.00 53.78           N  
ANISOU 3781  NH1 ARG B 166     4259   6471   9701   -229    234   -332       N  
ATOM   3782  NH2 ARG B 166     -29.213  -6.085  32.196  1.00 55.03           N  
ANISOU 3782  NH2 ARG B 166     4366   6676   9867   -214    261   -353       N  
ATOM   3783  N   GLU B 167     -25.676  -3.430  29.783  1.00 51.33           N  
ANISOU 3783  N   GLU B 167     4007   6237   9255    -93     16   -243       N  
ATOM   3784  CA  GLU B 167     -26.208  -3.567  28.399  1.00 53.24           C  
ANISOU 3784  CA  GLU B 167     4193   6531   9504   -105    -10   -301       C  
ATOM   3785  C   GLU B 167     -25.114  -3.149  27.408  1.00 52.37           C  
ANISOU 3785  C   GLU B 167     4111   6426   9359    -87    -62   -276       C  
ATOM   3786  O   GLU B 167     -24.842  -3.919  26.466  1.00 52.21           O  
ANISOU 3786  O   GLU B 167     4076   6409   9351   -112    -56   -303       O  
ATOM   3787  CB  GLU B 167     -27.485  -2.734  28.242  1.00 55.30           C  
ANISOU 3787  CB  GLU B 167     4403   6854   9754    -78    -38   -340       C  
ATOM   3788  CG  GLU B 167     -28.171  -2.892  26.894  1.00 57.27           C  
ANISOU 3788  CG  GLU B 167     4586   7168  10006    -89    -70   -404       C  
ATOM   3789  CD  GLU B 167     -29.499  -2.152  26.741  1.00 58.92           C  
ANISOU 3789  CD  GLU B 167     4731   7450  10204    -56    -97   -443       C  
ATOM   3790  OE1 GLU B 167     -30.126  -1.813  27.785  1.00 59.84           O  
ANISOU 3790  OE1 GLU B 167     4842   7565  10329    -38    -69   -432       O  
ATOM   3791  OE2 GLU B 167     -29.908  -1.907  25.573  1.00 59.03           O  
ANISOU 3791  OE2 GLU B 167     4701   7527  10199    -43   -145   -482       O  
ATOM   3792  N   THR B 168     -24.505  -1.981  27.641  1.00 52.05           N  
ANISOU 3792  N   THR B 168     4113   6383   9277    -49   -107   -226       N  
ATOM   3793  CA  THR B 168     -23.434  -1.375  26.803  1.00 51.59           C  
ANISOU 3793  CA  THR B 168     4086   6331   9182    -33   -156   -193       C  
ATOM   3794  C   THR B 168     -22.241  -2.327  26.719  1.00 52.02           C  
ANISOU 3794  C   THR B 168     4159   6351   9252    -58   -127   -164       C  
ATOM   3795  O   THR B 168     -21.793  -2.589  25.590  1.00 51.72           O  
ANISOU 3795  O   THR B 168     4113   6330   9207    -62   -139   -176       O  
ATOM   3796  CB  THR B 168     -22.962  -0.028  27.365  1.00 51.24           C  
ANISOU 3796  CB  THR B 168     4095   6276   9095     -2   -196   -142       C  
ATOM   3797  OG1 THR B 168     -24.122   0.769  27.601  1.00 51.44           O  
ANISOU 3797  OG1 THR B 168     4109   6326   9108     29   -210   -167       O  
ATOM   3798  CG2 THR B 168     -22.004   0.699  26.446  1.00 50.80           C  
ANISOU 3798  CG2 THR B 168     4067   6231   9001      7   -243   -112       C  
ATOM   3799  N   MET B 169     -21.739  -2.804  27.866  1.00 52.97           N  
ANISOU 3799  N   MET B 169     4309   6429   9388    -67    -89   -125       N  
ATOM   3800  CA  MET B 169     -20.598  -3.758  27.928  1.00 53.63           C  
ANISOU 3800  CA  MET B 169     4410   6481   9484    -78    -56    -90       C  
ATOM   3801  C   MET B 169     -20.919  -4.967  27.038  1.00 55.42           C  
ANISOU 3801  C   MET B 169     4608   6703   9743   -102    -17   -142       C  
ATOM   3802  O   MET B 169     -20.062  -5.343  26.218  1.00 55.61           O  
ANISOU 3802  O   MET B 169     4639   6729   9762    -99    -17   -131       O  
ATOM   3803  CB  MET B 169     -20.299  -4.219  29.362  1.00 53.09           C  
ANISOU 3803  CB  MET B 169     4373   6370   9427    -78    -16    -49       C  
ATOM   3804  CG  MET B 169     -19.862  -3.096  30.309  1.00 52.47           C  
ANISOU 3804  CG  MET B 169     4332   6292   9312    -60    -55      0       C  
ATOM   3805  SD  MET B 169     -18.566  -1.996  29.625  1.00 52.56           S  
ANISOU 3805  SD  MET B 169     4360   6332   9278    -51   -125     46       S  
ATOM   3806  CE  MET B 169     -17.127  -2.606  30.498  1.00 52.62           C  
ANISOU 3806  CE  MET B 169     4389   6320   9282    -50   -108    116       C  
ATOM   3807  N   SER B 170     -22.123  -5.533  27.159  1.00 57.82           N  
ANISOU 3807  N   SER B 170     4884   7006  10079   -127     17   -198       N  
ATOM   3808  CA  SER B 170     -22.570  -6.699  26.353  1.00 59.47           C  
ANISOU 3808  CA  SER B 170     5068   7208  10318   -163     56   -259       C  
ATOM   3809  C   SER B 170     -22.343  -6.415  24.864  1.00 62.05           C  
ANISOU 3809  C   SER B 170     5379   7577  10619   -156     10   -286       C  
ATOM   3810  O   SER B 170     -21.480  -7.100  24.273  1.00 64.50           O  
ANISOU 3810  O   SER B 170     5710   7865  10929   -158     30   -277       O  
ATOM   3811  CB  SER B 170     -23.990  -7.063  26.613  1.00 59.55           C  
ANISOU 3811  CB  SER B 170     5037   7228  10359   -198     86   -320       C  
ATOM   3812  OG  SER B 170     -24.268  -8.318  26.016  1.00 60.48           O  
ANISOU 3812  OG  SER B 170     5145   7324  10509   -245    133   -374       O  
ATOM   3813  N   TYR B 171     -23.049  -5.431  24.289  1.00 62.72           N  
ANISOU 3813  N   TYR B 171     5432   7720  10679   -142    -46   -314       N  
ATOM   3814  CA  TYR B 171     -22.919  -5.040  22.855  1.00 62.46           C  
ANISOU 3814  CA  TYR B 171     5387   7732  10612   -128    -94   -339       C  
ATOM   3815  C   TYR B 171     -21.435  -4.886  22.464  1.00 58.91           C  
ANISOU 3815  C   TYR B 171     4980   7265  10136   -107   -103   -280       C  
ATOM   3816  O   TYR B 171     -21.068  -5.327  21.356  1.00 57.91           O  
ANISOU 3816  O   TYR B 171     4855   7148   9998   -110   -103   -301       O  
ATOM   3817  CB  TYR B 171     -23.643  -3.724  22.553  1.00 64.80           C  
ANISOU 3817  CB  TYR B 171     5661   8086  10872    -95   -158   -348       C  
ATOM   3818  CG  TYR B 171     -25.143  -3.759  22.387  1.00 68.75           C  
ANISOU 3818  CG  TYR B 171     6101   8636  11385   -106   -167   -417       C  
ATOM   3819  CD1 TYR B 171     -25.732  -3.931  21.139  1.00 70.05           C  
ANISOU 3819  CD1 TYR B 171     6226   8856  11534   -113   -197   -480       C  
ATOM   3820  CD2 TYR B 171     -25.982  -3.488  23.461  1.00 70.06           C  
ANISOU 3820  CD2 TYR B 171     6245   8803  11571   -103   -152   -418       C  
ATOM   3821  CE1 TYR B 171     -27.110  -3.913  20.980  1.00 71.16           C  
ANISOU 3821  CE1 TYR B 171     6298   9056  11682   -122   -212   -543       C  
ATOM   3822  CE2 TYR B 171     -27.361  -3.449  23.316  1.00 71.34           C  
ANISOU 3822  CE2 TYR B 171     6340   9023  11743   -109   -161   -478       C  
ATOM   3823  CZ  TYR B 171     -27.931  -3.668  22.073  1.00 72.87           C  
ANISOU 3823  CZ  TYR B 171     6485   9277  11924   -120   -193   -541       C  
ATOM   3824  OH  TYR B 171     -29.295  -3.626  21.946  1.00 73.31           O  
ANISOU 3824  OH  TYR B 171     6463   9402  11990   -126   -206   -601       O  
ATOM   3825  N   LEU B 172     -20.612  -4.266  23.328  1.00 55.07           N  
ANISOU 3825  N   LEU B 172     4526   6758   9640    -87   -111   -209       N  
ATOM   3826  CA  LEU B 172     -19.174  -3.980  23.053  1.00 52.77           C  
ANISOU 3826  CA  LEU B 172     4264   6462   9324    -69   -124   -148       C  
ATOM   3827  C   LEU B 172     -18.387  -5.289  23.028  1.00 52.46           C  
ANISOU 3827  C   LEU B 172     4235   6387   9310    -78    -66   -137       C  
ATOM   3828  O   LEU B 172     -17.483  -5.401  22.167  1.00 53.40           O  
ANISOU 3828  O   LEU B 172     4362   6516   9412    -66    -67   -118       O  
ATOM   3829  CB  LEU B 172     -18.581  -3.039  24.111  1.00 50.60           C  
ANISOU 3829  CB  LEU B 172     4015   6177   9033    -57   -147    -82       C  
ATOM   3830  CG  LEU B 172     -18.982  -1.575  24.003  1.00 49.76           C  
ANISOU 3830  CG  LEU B 172     3920   6097   8889    -40   -205    -77       C  
ATOM   3831  CD1 LEU B 172     -18.579  -0.808  25.253  1.00 48.65           C  
ANISOU 3831  CD1 LEU B 172     3811   5935   8735    -37   -219    -25       C  
ATOM   3832  CD2 LEU B 172     -18.375  -0.957  22.759  1.00 49.51           C  
ANISOU 3832  CD2 LEU B 172     3897   6094   8821    -28   -240    -66       C  
ATOM   3833  N   PHE B 173     -18.707  -6.225  23.929  1.00 51.76           N  
ANISOU 3833  N   PHE B 173     4150   6255   9258    -94    -13   -144       N  
ATOM   3834  CA  PHE B 173     -17.995  -7.526  24.058  1.00 51.82           C  
ANISOU 3834  CA  PHE B 173     4180   6218   9291    -93     51   -128       C  
ATOM   3835  C   PHE B 173     -18.312  -8.432  22.853  1.00 52.47           C  
ANISOU 3835  C   PHE B 173     4259   6295   9382   -111     78   -193       C  
ATOM   3836  O   PHE B 173     -17.528  -9.376  22.613  1.00 51.13           O  
ANISOU 3836  O   PHE B 173     4115   6092   9220   -100    126   -178       O  
ATOM   3837  CB  PHE B 173     -18.327  -8.201  25.392  1.00 51.44           C  
ANISOU 3837  CB  PHE B 173     4147   6121   9274   -103    102   -116       C  
ATOM   3838  CG  PHE B 173     -17.796  -7.533  26.638  1.00 50.92           C  
ANISOU 3838  CG  PHE B 173     4096   6053   9195    -82     83    -48       C  
ATOM   3839  CD1 PHE B 173     -16.828  -6.542  26.586  1.00 50.68           C  
ANISOU 3839  CD1 PHE B 173     4067   6056   9129    -60     30      5       C  
ATOM   3840  CD2 PHE B 173     -18.269  -7.912  27.886  1.00 51.10           C  
ANISOU 3840  CD2 PHE B 173     4136   6040   9237    -88    121    -39       C  
ATOM   3841  CE1 PHE B 173     -16.357  -5.944  27.747  1.00 50.48           C  
ANISOU 3841  CE1 PHE B 173     4059   6032   9089    -48      9     61       C  
ATOM   3842  CE2 PHE B 173     -17.794  -7.321  29.047  1.00 50.49           C  
ANISOU 3842  CE2 PHE B 173     4079   5963   9142    -68    102     19       C  
ATOM   3843  CZ  PHE B 173     -16.846  -6.333  28.973  1.00 50.15           C  
ANISOU 3843  CZ  PHE B 173     4036   5956   9063    -50     43     67       C  
ATOM   3844  N   GLN B 174     -19.403  -8.161  22.116  1.00 53.77           N  
ANISOU 3844  N   GLN B 174     4394   6494   9541   -135     49   -262       N  
ATOM   3845  CA  GLN B 174     -19.718  -8.822  20.817  1.00 55.07           C  
ANISOU 3845  CA  GLN B 174     4555   6668   9700   -155     58   -330       C  
ATOM   3846  C   GLN B 174     -18.555  -8.597  19.845  1.00 54.82           C  
ANISOU 3846  C   GLN B 174     4542   6653   9631   -120     42   -296       C  
ATOM   3847  O   GLN B 174     -18.197  -9.554  19.125  1.00 55.37           O  
ANISOU 3847  O   GLN B 174     4635   6699   9702   -123     83   -321       O  
ATOM   3848  CB  GLN B 174     -20.960  -8.240  20.136  1.00 56.49           C  
ANISOU 3848  CB  GLN B 174     4691   6906   9864   -174      6   -398       C  
ATOM   3849  CG  GLN B 174     -22.227  -8.267  20.973  1.00 57.93           C  
ANISOU 3849  CG  GLN B 174     4838   7092  10078   -206     14   -435       C  
ATOM   3850  CD  GLN B 174     -22.568  -9.661  21.435  1.00 59.35           C  
ANISOU 3850  CD  GLN B 174     5031   7213  10306   -255     91   -470       C  
ATOM   3851  OE1 GLN B 174     -22.306 -10.646  20.749  1.00 61.02           O  
ANISOU 3851  OE1 GLN B 174     5267   7395  10523   -276    128   -503       O  
ATOM   3852  NE2 GLN B 174     -23.181  -9.747  22.605  1.00 59.32           N  
ANISOU 3852  NE2 GLN B 174     5016   7188  10334   -273    120   -463       N  
ATOM   3853  N   HIS B 175     -18.017  -7.369  19.829  1.00 53.68           N  
ANISOU 3853  N   HIS B 175     4392   6547   9455    -90    -10   -243       N  
ATOM   3854  CA  HIS B 175     -16.961  -6.883  18.898  1.00 53.35           C  
ANISOU 3854  CA  HIS B 175     4362   6532   9373    -61    -31   -206       C  
ATOM   3855  C   HIS B 175     -15.572  -7.026  19.536  1.00 52.81           C  
ANISOU 3855  C   HIS B 175     4309   6443   9311    -37     -4   -124       C  
ATOM   3856  O   HIS B 175     -14.577  -6.705  18.854  1.00 51.31           O  
ANISOU 3856  O   HIS B 175     4123   6277   9094    -14    -11    -86       O  
ATOM   3857  CB  HIS B 175     -17.221  -5.429  18.476  1.00 53.46           C  
ANISOU 3857  CB  HIS B 175     4366   6598   9346    -48   -102   -197       C  
ATOM   3858  CG  HIS B 175     -18.598  -5.180  17.956  1.00 55.32           C  
ANISOU 3858  CG  HIS B 175     4579   6868   9572    -60   -137   -269       C  
ATOM   3859  ND1 HIS B 175     -19.602  -4.651  18.756  1.00 55.89           N  
ANISOU 3859  ND1 HIS B 175     4629   6948   9657    -67   -160   -284       N  
ATOM   3860  CD2 HIS B 175     -19.144  -5.380  16.733  1.00 55.90           C  
ANISOU 3860  CD2 HIS B 175     4644   6973   9620    -62   -154   -331       C  
ATOM   3861  CE1 HIS B 175     -20.707  -4.549  18.049  1.00 56.58           C  
ANISOU 3861  CE1 HIS B 175     4689   7078   9731    -72   -190   -350       C  
ATOM   3862  NE2 HIS B 175     -20.450  -4.989  16.802  1.00 56.41           N  
ANISOU 3862  NE2 HIS B 175     4676   7073   9684    -71   -190   -381       N  
ATOM   3863  N   ALA B 176     -15.501  -7.466  20.796  1.00 52.47           N  
ANISOU 3863  N   ALA B 176     4271   6363   9300    -40     26    -96       N  
ATOM   3864  CA  ALA B 176     -14.239  -7.839  21.464  1.00 52.78           C  
ANISOU 3864  CA  ALA B 176     4321   6385   9347    -13     57    -22       C  
ATOM   3865  C   ALA B 176     -13.867  -9.244  21.001  1.00 53.89           C  
ANISOU 3865  C   ALA B 176     4483   6487   9504      1    128    -38       C  
ATOM   3866  O   ALA B 176     -14.777  -9.996  20.645  1.00 54.14           O  
ANISOU 3866  O   ALA B 176     4527   6488   9552    -23    157   -108       O  
ATOM   3867  CB  ALA B 176     -14.389  -7.782  22.959  1.00 52.79           C  
ANISOU 3867  CB  ALA B 176     4325   6363   9368    -16     62     10       C  
ATOM   3868  N   ASN B 177     -12.573  -9.566  20.975  1.00 54.93           N  
ANISOU 3868  N   ASN B 177     4618   6621   9629     41    154     22       N  
ATOM   3869  CA  ASN B 177     -12.103 -10.943  20.698  1.00 55.68           C  
ANISOU 3869  CA  ASN B 177     4744   6672   9739     70    231     18       C  
ATOM   3870  C   ASN B 177     -12.083 -11.696  22.033  1.00 56.19           C  
ANISOU 3870  C   ASN B 177     4829   6685   9834     82    276     50       C  
ATOM   3871  O   ASN B 177     -11.067 -11.602  22.735  1.00 55.90           O  
ANISOU 3871  O   ASN B 177     4781   6664   9792    121    277    126       O  
ATOM   3872  CB  ASN B 177     -10.761 -10.956  19.971  1.00 56.18           C  
ANISOU 3872  CB  ASN B 177     4799   6767   9778    116    244     69       C  
ATOM   3873  CG  ASN B 177     -10.345 -12.360  19.584  1.00 58.16           C  
ANISOU 3873  CG  ASN B 177     5090   6968  10040    154    326     60       C  
ATOM   3874  OD1 ASN B 177     -11.069 -13.324  19.838  1.00 59.74           O  
ANISOU 3874  OD1 ASN B 177     5330   7103  10265    138    374     13       O  
ATOM   3875  ND2 ASN B 177      -9.189 -12.497  18.952  1.00 58.68           N  
ANISOU 3875  ND2 ASN B 177     5148   7061  10085    202    349    103       N  
ATOM   3876  N   LEU B 178     -13.184 -12.377  22.370  1.00 56.03           N  
ANISOU 3876  N   LEU B 178     4835   6611   9842     47    310     -7       N  
ATOM   3877  CA  LEU B 178     -13.348 -13.132  23.638  1.00 56.51           C  
ANISOU 3877  CA  LEU B 178     4925   6614   9930     54    360     16       C  
ATOM   3878  C   LEU B 178     -13.606 -14.614  23.349  1.00 57.77           C  
ANISOU 3878  C   LEU B 178     5140   6695  10113     52    449    -25       C  
ATOM   3879  O   LEU B 178     -14.018 -15.328  24.273  1.00 57.34           O  
ANISOU 3879  O   LEU B 178     5120   6580  10084     44    500    -23       O  
ATOM   3880  CB  LEU B 178     -14.518 -12.521  24.405  1.00 56.42           C  
ANISOU 3880  CB  LEU B 178     4897   6606   9932      6    327    -13       C  
ATOM   3881  CG  LEU B 178     -14.325 -11.085  24.872  1.00 56.02           C  
ANISOU 3881  CG  LEU B 178     4809   6618   9857      7    248     27       C  
ATOM   3882  CD1 LEU B 178     -15.602 -10.599  25.537  1.00 56.32           C  
ANISOU 3882  CD1 LEU B 178     4837   6653   9908    -33    227    -10       C  
ATOM   3883  CD2 LEU B 178     -13.147 -10.964  25.824  1.00 55.64           C  
ANISOU 3883  CD2 LEU B 178     4763   6581   9797     53    245    117       C  
ATOM   3884  N   ASP B 179     -13.313 -15.062  22.128  1.00 59.40           N  
ANISOU 3884  N   ASP B 179     5363   6897  10308     61    470    -58       N  
ATOM   3885  CA  ASP B 179     -13.587 -16.438  21.625  1.00 60.88           C  
ANISOU 3885  CA  ASP B 179     5614   7006  10512     52    553   -112       C  
ATOM   3886  C   ASP B 179     -12.967 -17.492  22.555  1.00 61.49           C  
ANISOU 3886  C   ASP B 179     5746   7012  10606    104    634    -54       C  
ATOM   3887  O   ASP B 179     -13.667 -18.482  22.861  1.00 62.83           O  
ANISOU 3887  O   ASP B 179     5972   7099  10802     72    701    -96       O  
ATOM   3888  CB  ASP B 179     -13.070 -16.608  20.195  1.00 61.62           C  
ANISOU 3888  CB  ASP B 179     5718   7116  10577     73    558   -139       C  
ATOM   3889  CG  ASP B 179     -13.626 -15.583  19.213  1.00 61.54           C  
ANISOU 3889  CG  ASP B 179     5662   7178  10542     32    480   -190       C  
ATOM   3890  OD1 ASP B 179     -14.560 -14.845  19.599  1.00 60.96           O  
ANISOU 3890  OD1 ASP B 179     5550   7134  10476    -15    426   -217       O  
ATOM   3891  OD2 ASP B 179     -13.121 -15.528  18.069  1.00 61.29           O  
ANISOU 3891  OD2 ASP B 179     5635   7173  10479     54    475   -202       O  
ATOM   3892  N   SER B 180     -11.717 -17.297  22.993  1.00 61.27           N  
ANISOU 3892  N   SER B 180     5702   7015  10561    180    629     37       N  
ATOM   3893  CA  SER B 180     -10.938 -18.280  23.799  1.00 61.94           C  
ANISOU 3893  CA  SER B 180     5837   7045  10652    252    703    104       C  
ATOM   3894  C   SER B 180     -11.289 -18.181  25.293  1.00 62.78           C  
ANISOU 3894  C   SER B 180     5946   7133  10772    246    701    143       C  
ATOM   3895  O   SER B 180     -10.696 -18.955  26.079  1.00 62.36           O  
ANISOU 3895  O   SER B 180     5936   7036  10719    310    758    204       O  
ATOM   3896  CB  SER B 180      -9.457 -18.122  23.579  1.00 61.10           C  
ANISOU 3896  CB  SER B 180     5702   6994  10519    339    696    185       C  
ATOM   3897  OG  SER B 180      -9.011 -16.868  24.068  1.00 59.72           O  
ANISOU 3897  OG  SER B 180     5451   6911  10327    340    611    239       O  
ATOM   3898  N   CYS B 181     -12.203 -17.276  25.677  1.00 62.90           N  
ANISOU 3898  N   CYS B 181     5923   7182  10795    180    640    112       N  
ATOM   3899  CA  CYS B 181     -12.786 -17.208  27.046  1.00 63.53           C  
ANISOU 3899  CA  CYS B 181     6013   7237  10888    163    645    133       C  
ATOM   3900  C   CYS B 181     -13.789 -18.353  27.238  1.00 65.13           C  
ANISOU 3900  C   CYS B 181     6282   7338  11123    119    731     76       C  
ATOM   3901  O   CYS B 181     -14.490 -18.693  26.271  1.00 66.09           O  
ANISOU 3901  O   CYS B 181     6414   7437  11260     64    748     -6       O  
ATOM   3902  CB  CYS B 181     -13.491 -15.884  27.315  1.00 63.35           C  
ANISOU 3902  CB  CYS B 181     5930   7277  10860    110    559    112       C  
ATOM   3903  SG  CYS B 181     -12.373 -14.461  27.381  1.00 62.27           S  
ANISOU 3903  SG  CYS B 181     5727   7248  10684    147    461    184       S  
ATOM   3904  N   LYS B 182     -13.856 -18.914  28.447  1.00 65.82           N  
ANISOU 3904  N   LYS B 182     6416   7371  11220    140    783    118       N  
ATOM   3905  CA  LYS B 182     -14.590 -20.172  28.734  1.00 66.50           C  
ANISOU 3905  CA  LYS B 182     6583   7346  11337    109    885     81       C  
ATOM   3906  C   LYS B 182     -14.972 -20.203  30.213  1.00 65.82           C  
ANISOU 3906  C   LYS B 182     6520   7232  11256    110    909    124       C  
ATOM   3907  O   LYS B 182     -14.133 -19.836  31.046  1.00 63.99           O  
ANISOU 3907  O   LYS B 182     6280   7037  10996    180    881    209       O  
ATOM   3908  CB  LYS B 182     -13.713 -21.376  28.369  1.00 68.43           C  
ANISOU 3908  CB  LYS B 182     6902   7520  11575    178    968    110       C  
ATOM   3909  CG  LYS B 182     -14.455 -22.679  28.100  1.00 70.23           C  
ANISOU 3909  CG  LYS B 182     7220   7629  11833    129   1073     45       C  
ATOM   3910  CD  LYS B 182     -13.609 -23.934  28.314  1.00 71.63           C  
ANISOU 3910  CD  LYS B 182     7497   7715  12003    216   1173    100       C  
ATOM   3911  CE  LYS B 182     -13.972 -25.062  27.369  1.00 72.98           C  
ANISOU 3911  CE  LYS B 182     7750   7786  12190    177   1259     23       C  
ATOM   3912  NZ  LYS B 182     -13.421 -26.364  27.822  1.00 74.44           N  
ANISOU 3912  NZ  LYS B 182     8054   7856  12373    252   1374     73       N  
ATOM   3913  N   ARG B 183     -16.195 -20.634  30.505  1.00 68.12           N  
ANISOU 3913  N   ARG B 183     6839   7465  11579     33    959     65       N  
ATOM   3914  CA  ARG B 183     -16.757 -20.768  31.876  1.00 70.70           C  
ANISOU 3914  CA  ARG B 183     7196   7753  11913     22    998     95       C  
ATOM   3915  C   ARG B 183     -17.452 -22.134  31.980  1.00 71.46           C  
ANISOU 3915  C   ARG B 183     7379   7727  12043    -23   1118     55       C  
ATOM   3916  O   ARG B 183     -18.018 -22.592  30.960  1.00 70.97           O  
ANISOU 3916  O   ARG B 183     7321   7635  12006    -90   1143    -29       O  
ATOM   3917  CB  ARG B 183     -17.710 -19.595  32.151  1.00 71.35           C  
ANISOU 3917  CB  ARG B 183     7201   7906  12000    -39    926     58       C  
ATOM   3918  CG  ARG B 183     -18.397 -19.630  33.508  1.00 72.68           C  
ANISOU 3918  CG  ARG B 183     7394   8043  12175    -56    965     81       C  
ATOM   3919  CD  ARG B 183     -19.236 -18.378  33.723  1.00 74.54           C  
ANISOU 3919  CD  ARG B 183     7552   8358  12409   -102    889     49       C  
ATOM   3920  NE  ARG B 183     -18.598 -17.419  34.620  1.00 76.40           N  
ANISOU 3920  NE  ARG B 183     7771   8651  12603    -42    824    123       N  
ATOM   3921  CZ  ARG B 183     -18.895 -16.118  34.718  1.00 77.18           C  
ANISOU 3921  CZ  ARG B 183     7808   8830  12686    -55    739    114       C  
ATOM   3922  NH1 ARG B 183     -19.825 -15.559  33.959  1.00 76.43           N  
ANISOU 3922  NH1 ARG B 183     7653   8774  12611   -116    703     39       N  
ATOM   3923  NH2 ARG B 183     -18.237 -15.368  35.585  1.00 78.41           N  
ANISOU 3923  NH2 ARG B 183     7964   9025  12800     -4    688    181       N  
ATOM   3924  N   VAL B 184     -17.401 -22.762  33.160  1.00 70.92           N  
ANISOU 3924  N   VAL B 184     7382   7589  11972     10   1191    112       N  
ATOM   3925  CA  VAL B 184     -18.109 -24.040  33.464  1.00 72.38           C  
ANISOU 3925  CA  VAL B 184     7663   7649  12189    -37   1316     83       C  
ATOM   3926  C   VAL B 184     -18.831 -23.889  34.811  1.00 73.67           C  
ANISOU 3926  C   VAL B 184     7839   7796  12357    -61   1345    110       C  
ATOM   3927  O   VAL B 184     -18.140 -23.670  35.833  1.00 72.19           O  
ANISOU 3927  O   VAL B 184     7673   7624  12133     24   1334    201       O  
ATOM   3928  CB  VAL B 184     -17.145 -25.240  33.421  1.00 72.21           C  
ANISOU 3928  CB  VAL B 184     7748   7532  12153     46   1403    136       C  
ATOM   3929  CG1 VAL B 184     -17.819 -26.551  33.807  1.00 73.34           C  
ANISOU 3929  CG1 VAL B 184     8005   7533  12325      0   1539    113       C  
ATOM   3930  CG2 VAL B 184     -16.532 -25.370  32.035  1.00 71.55           C  
ANISOU 3930  CG2 VAL B 184     7652   7467  12066     63   1379    100       C  
ATOM   3931  N   LEU B 185     -20.171 -23.982  34.782  1.00 75.08           N  
ANISOU 3931  N   LEU B 185     7999   7953  12575   -174   1379     31       N  
ATOM   3932  CA  LEU B 185     -21.101 -23.805  35.935  1.00 75.44           C  
ANISOU 3932  CA  LEU B 185     8044   7988  12632   -217   1413     38       C  
ATOM   3933  C   LEU B 185     -21.813 -25.128  36.234  1.00 76.09           C  
ANISOU 3933  C   LEU B 185     8221   7940  12750   -282   1552     10       C  
ATOM   3934  O   LEU B 185     -22.138 -25.852  35.272  1.00 75.20           O  
ANISOU 3934  O   LEU B 185     8129   7775  12669   -350   1595    -63       O  
ATOM   3935  CB  LEU B 185     -22.135 -22.734  35.576  1.00 75.29           C  
ANISOU 3935  CB  LEU B 185     7908   8066  12632   -298   1335    -35       C  
ATOM   3936  CG  LEU B 185     -21.667 -21.290  35.728  1.00 74.33           C  
ANISOU 3936  CG  LEU B 185     7705   8063  12473   -241   1210      2       C  
ATOM   3937  CD1 LEU B 185     -22.562 -20.348  34.935  1.00 74.16           C  
ANISOU 3937  CD1 LEU B 185     7575   8131  12469   -312   1132    -79       C  
ATOM   3938  CD2 LEU B 185     -21.633 -20.891  37.195  1.00 74.46           C  
ANISOU 3938  CD2 LEU B 185     7745   8086  12461   -195   1217     75       C  
ATOM   3939  N   ASN B 186     -22.084 -25.396  37.512  1.00 76.73           N  
ANISOU 3939  N   ASN B 186     8358   7971  12824   -269   1620     63       N  
ATOM   3940  CA  ASN B 186     -22.703 -26.662  37.979  1.00 81.13           C  
ANISOU 3940  CA  ASN B 186     9021   8394  13410   -326   1765     52       C  
ATOM   3941  C   ASN B 186     -23.832 -26.342  38.963  1.00 83.61           C  
ANISOU 3941  C   ASN B 186     9307   8719  13741   -392   1798     43       C  
ATOM   3942  O   ASN B 186     -23.564 -25.588  39.924  1.00 86.16           O  
ANISOU 3942  O   ASN B 186     9612   9097  14025   -323   1753    112       O  
ATOM   3943  CB  ASN B 186     -21.661 -27.565  38.632  1.00 82.03           C  
ANISOU 3943  CB  ASN B 186     9267   8411  13489   -214   1841    150       C  
ATOM   3944  CG  ASN B 186     -21.955 -29.036  38.462  1.00 84.39           C  
ANISOU 3944  CG  ASN B 186     9690   8555  13818   -263   1984    124       C  
ATOM   3945  OD1 ASN B 186     -22.992 -29.414  37.929  1.00 85.46           O  
ANISOU 3945  OD1 ASN B 186     9813   8653  14003   -394   2031     29       O  
ATOM   3946  ND2 ASN B 186     -21.029 -29.871  38.904  1.00 86.49           N  
ANISOU 3946  ND2 ASN B 186    10078   8732  14051   -157   2054    208       N  
ATOM   3947  N   VAL B 187     -25.037 -26.883  38.724  1.00 84.85           N  
ANISOU 3947  N   VAL B 187     9458   8829  13951   -523   1873    -39       N  
ATOM   3948  CA  VAL B 187     -26.263 -26.661  39.557  1.00 84.44           C  
ANISOU 3948  CA  VAL B 187     9369   8788  13924   -603   1918    -61       C  
ATOM   3949  C   VAL B 187     -26.679 -27.998  40.192  1.00 85.07           C  
ANISOU 3949  C   VAL B 187     9575   8720  14027   -655   2081    -49       C  
ATOM   3950  O   VAL B 187     -27.133 -28.892  39.446  1.00 83.99           O  
ANISOU 3950  O   VAL B 187     9470   8509  13934   -753   2150   -123       O  
ATOM   3951  CB  VAL B 187     -27.405 -26.049  38.722  1.00 84.07           C  
ANISOU 3951  CB  VAL B 187     9186   8835  13922   -721   1861   -172       C  
ATOM   3952  CG1 VAL B 187     -28.592 -25.668  39.591  1.00 84.87           C  
ANISOU 3952  CG1 VAL B 187     9232   8970  14044   -785   1897   -186       C  
ATOM   3953  CG2 VAL B 187     -26.933 -24.850  37.909  1.00 82.49           C  
ANISOU 3953  CG2 VAL B 187     8880   8765  13698   -670   1709   -186       C  
ATOM   3954  N   VAL B 188     -26.539 -28.119  41.518  1.00 86.07           N  
ANISOU 3954  N   VAL B 188     9775   8803  14122   -593   2142     38       N  
ATOM   3955  CA  VAL B 188     -26.735 -29.382  42.295  1.00 89.14           C  
ANISOU 3955  CA  VAL B 188    10309   9039  14518   -613   2304     75       C  
ATOM   3956  C   VAL B 188     -28.042 -29.292  43.100  1.00 92.68           C  
ANISOU 3956  C   VAL B 188    10726   9489  14997   -712   2376     50       C  
ATOM   3957  O   VAL B 188     -28.075 -28.507  44.067  1.00 94.01           O  
ANISOU 3957  O   VAL B 188    10866   9722  15130   -653   2342    107       O  
ATOM   3958  CB  VAL B 188     -25.531 -29.654  43.222  1.00 88.24           C  
ANISOU 3958  CB  VAL B 188    10314   8874  14338   -455   2325    203       C  
ATOM   3959  CG1 VAL B 188     -25.737 -30.894  44.081  1.00 89.14           C  
ANISOU 3959  CG1 VAL B 188    10585   8831  14452   -464   2492    250       C  
ATOM   3960  CG2 VAL B 188     -24.231 -29.769  42.448  1.00 87.77           C  
ANISOU 3960  CG2 VAL B 188    10277   8819  14249   -353   2261    231       C  
ATOM   3961  N   CYS B 189     -29.067 -30.068  42.717  1.00 95.59           N  
ANISOU 3961  N   CYS B 189    11099   9791  15427   -860   2472    -32       N  
ATOM   3962  CA  CYS B 189     -30.283 -30.365  43.533  1.00 97.20           C  
ANISOU 3962  CA  CYS B 189    11305   9960  15665   -965   2585    -49       C  
ATOM   3963  C   CYS B 189     -30.236 -31.836  43.972  1.00 97.89           C  
ANISOU 3963  C   CYS B 189    11568   9863  15762   -994   2756    -18       C  
ATOM   3964  O   CYS B 189     -29.863 -32.692  43.147  1.00 95.80           O  
ANISOU 3964  O   CYS B 189    11376   9509  15514  -1020   2791    -52       O  
ATOM   3965  CB  CYS B 189     -31.569 -30.073  42.763  1.00 98.05           C  
ANISOU 3965  CB  CYS B 189    11268  10146  15839  -1123   2564   -173       C  
ATOM   3966  SG  CYS B 189     -33.089 -30.189  43.755  1.00 99.06           S  
ANISOU 3966  SG  CYS B 189    11357  10270  16008  -1247   2684   -195       S  
ATOM   3967  N   LYS B 190     -30.578 -32.107  45.234  1.00100.26           N  
ANISOU 3967  N   LYS B 190    11943  10104  16047   -985   2861     46       N  
ATOM   3968  CA  LYS B 190     -30.569 -33.473  45.828  1.00102.58           C  
ANISOU 3968  CA  LYS B 190    12418  10214  16343  -1005   3037     91       C  
ATOM   3969  C   LYS B 190     -31.685 -34.318  45.195  1.00104.05           C  
ANISOU 3969  C   LYS B 190    12598  10327  16608  -1203   3141    -19       C  
ATOM   3970  O   LYS B 190     -31.563 -35.559  45.224  1.00103.62           O  
ANISOU 3970  O   LYS B 190    12699  10106  16563  -1236   3275     -8       O  
ATOM   3971  CB  LYS B 190     -30.689 -33.389  47.353  1.00102.66           C  
ANISOU 3971  CB  LYS B 190    12497  10200  16310   -941   3111    189       C  
ATOM   3972  CG  LYS B 190     -29.449 -32.837  48.050  1.00102.00           C  
ANISOU 3972  CG  LYS B 190    12459  10156  16138   -742   3030    307       C  
ATOM   3973  CD  LYS B 190     -29.739 -32.173  49.378  1.00101.10           C  
ANISOU 3973  CD  LYS B 190    12336  10096  15979   -689   3037    375       C  
ATOM   3974  CE  LYS B 190     -30.301 -33.134  50.404  1.00101.73           C  
ANISOU 3974  CE  LYS B 190    12554  10040  16059   -730   3221    422       C  
ATOM   3975  NZ  LYS B 190     -30.908 -32.416  51.547  1.00101.13           N  
ANISOU 3975  NZ  LYS B 190    12439  10031  15953   -718   3233    459       N  
ATOM   3976  N   THR B 191     -32.715 -33.671  44.629  1.00104.74           N  
ANISOU 3976  N   THR B 191    12515  10534  16747  -1327   3081   -120       N  
ATOM   3977  CA  THR B 191     -33.807 -34.311  43.838  1.00106.32           C  
ANISOU 3977  CA  THR B 191    12669  10702  17023  -1528   3146   -244       C  
ATOM   3978  C   THR B 191     -33.324 -34.588  42.404  1.00106.59           C  
ANISOU 3978  C   THR B 191    12698  10729  17071  -1550   3076   -320       C  
ATOM   3979  O   THR B 191     -33.133 -35.773  42.070  1.00109.27           O  
ANISOU 3979  O   THR B 191    13176  10916  17424  -1601   3180   -338       O  
ATOM   3980  CB  THR B 191     -35.085 -33.456  43.826  1.00106.52           C  
ANISOU 3980  CB  THR B 191    12502  10877  17092  -1637   3101   -318       C  
ATOM   3981  OG1 THR B 191     -35.250 -32.799  45.082  1.00106.76           O  
ANISOU 3981  OG1 THR B 191    12516  10956  17090  -1561   3114   -235       O  
ATOM   3982  CG2 THR B 191     -36.323 -34.267  43.508  1.00107.63           C  
ANISOU 3982  CG2 THR B 191    12618  10968  17308  -1849   3214   -419       C  
ATOM   3983  N   CYS B 192     -33.106 -33.536  41.603  1.00104.95           N  
ANISOU 3983  N   CYS B 192    12347  10675  16854  -1508   2910   -358       N  
ATOM   3984  CA  CYS B 192     -32.919 -33.580  40.123  1.00104.59           C  
ANISOU 3984  CA  CYS B 192    12251  10662  16825  -1553   2825   -452       C  
ATOM   3985  C   CYS B 192     -31.438 -33.735  39.728  1.00102.35           C  
ANISOU 3985  C   CYS B 192    12069  10330  16488  -1400   2777   -389       C  
ATOM   3986  O   CYS B 192     -31.138 -33.541  38.527  1.00100.59           O  
ANISOU 3986  O   CYS B 192    11794  10159  16267  -1406   2684   -453       O  
ATOM   3987  CB  CYS B 192     -33.469 -32.319  39.458  1.00104.56           C  
ANISOU 3987  CB  CYS B 192    12039  10853  16833  -1581   2673   -521       C  
ATOM   3988  SG  CYS B 192     -34.816 -31.510  40.365  1.00106.05           S  
ANISOU 3988  SG  CYS B 192    12083  11160  17051  -1651   2682   -532       S  
ATOM   3989  N   GLY B 193     -30.550 -34.053  40.681  1.00100.51           N  
ANISOU 3989  N   GLY B 193    11971  10010  16208  -1264   2834   -268       N  
ATOM   3990  CA  GLY B 193     -29.121 -34.331  40.434  1.00 99.20           C  
ANISOU 3990  CA  GLY B 193    11911   9790  15991  -1111   2808   -197       C  
ATOM   3991  C   GLY B 193     -28.355 -33.095  39.978  1.00 96.34           C  
ANISOU 3991  C   GLY B 193    11429   9584  15590   -996   2632   -176       C  
ATOM   3992  O   GLY B 193     -28.645 -31.986  40.486  1.00 95.36           O  
ANISOU 3992  O   GLY B 193    11189   9587  15455   -971   2549   -156       O  
ATOM   3993  N   GLN B 194     -27.395 -33.279  39.067  1.00 94.67           N  
ANISOU 3993  N   GLN B 194    11251   9360  15358   -927   2583   -179       N  
ATOM   3994  CA  GLN B 194     -26.393 -32.246  38.664  1.00 92.87           C  
ANISOU 3994  CA  GLN B 194    10941   9259  15086   -797   2431   -139       C  
ATOM   3995  C   GLN B 194     -26.719 -31.707  37.267  1.00 90.90           C  
ANISOU 3995  C   GLN B 194    10566   9109  14862   -874   2325   -249       C  
ATOM   3996  O   GLN B 194     -27.360 -32.443  36.493  1.00 91.87           O  
ANISOU 3996  O   GLN B 194    10710   9169  15025  -1000   2381   -345       O  
ATOM   3997  CB  GLN B 194     -24.971 -32.814  38.680  1.00 92.87           C  
ANISOU 3997  CB  GLN B 194    11066   9182  15038   -645   2452    -50       C  
ATOM   3998  CG  GLN B 194     -24.382 -32.955  40.079  1.00 92.75           C  
ANISOU 3998  CG  GLN B 194    11142   9122  14976   -520   2504     78       C  
ATOM   3999  CD  GLN B 194     -22.872 -32.905  40.070  1.00 93.09           C  
ANISOU 3999  CD  GLN B 194    11231   9179  14960   -343   2454    173       C  
ATOM   4000  OE1 GLN B 194     -22.235 -33.118  39.038  1.00 90.92           O  
ANISOU 4000  OE1 GLN B 194    10961   8900  14683   -313   2423    146       O  
ATOM   4001  NE2 GLN B 194     -22.293 -32.646  41.234  1.00 93.63           N  
ANISOU 4001  NE2 GLN B 194    11333   9265  14977   -223   2449    284       N  
ATOM   4002  N   GLN B 195     -26.268 -30.479  36.965  1.00 87.95           N  
ANISOU 4002  N   GLN B 195    10074   8880  14460   -800   2179   -233       N  
ATOM   4003  CA  GLN B 195     -26.461 -29.776  35.661  1.00 85.97           C  
ANISOU 4003  CA  GLN B 195     9699   8742  14220   -847   2062   -323       C  
ATOM   4004  C   GLN B 195     -25.303 -28.796  35.415  1.00 82.80           C  
ANISOU 4004  C   GLN B 195     9247   8443  13770   -708   1934   -260       C  
ATOM   4005  O   GLN B 195     -25.316 -27.694  36.011  1.00 78.91           O  
ANISOU 4005  O   GLN B 195     8670   8054  13257   -661   1854   -218       O  
ATOM   4006  CB  GLN B 195     -27.795 -29.017  35.650  1.00 85.14           C  
ANISOU 4006  CB  GLN B 195     9454   8743  14152   -962   2016   -398       C  
ATOM   4007  CG  GLN B 195     -28.095 -28.277  34.351  1.00 84.08           C  
ANISOU 4007  CG  GLN B 195     9192   8729  14025  -1009   1896   -489       C  
ATOM   4008  CD  GLN B 195     -28.909 -27.024  34.568  1.00 83.36           C  
ANISOU 4008  CD  GLN B 195     8949   8782  13940  -1033   1806   -510       C  
ATOM   4009  OE1 GLN B 195     -29.489 -26.811  35.630  1.00 83.94           O  
ANISOU 4009  OE1 GLN B 195     9007   8862  14023  -1045   1846   -478       O  
ATOM   4010  NE2 GLN B 195     -28.934 -26.164  33.564  1.00 82.49           N  
ANISOU 4010  NE2 GLN B 195     8733   8789  13820  -1031   1684   -561       N  
ATOM   4011  N   GLN B 196     -24.352 -29.166  34.549  1.00 81.99           N  
ANISOU 4011  N   GLN B 196     9193   8312  13647   -649   1919   -257       N  
ATOM   4012  CA  GLN B 196     -23.193 -28.302  34.192  1.00 80.70           C  
ANISOU 4012  CA  GLN B 196     8979   8244  13439   -524   1804   -201       C  
ATOM   4013  C   GLN B 196     -23.398 -27.741  32.777  1.00 80.13           C  
ANISOU 4013  C   GLN B 196     8809   8261  13373   -577   1708   -292       C  
ATOM   4014  O   GLN B 196     -23.956 -28.465  31.926  1.00 80.46           O  
ANISOU 4014  O   GLN B 196     8876   8249  13444   -675   1753   -384       O  
ATOM   4015  CB  GLN B 196     -21.867 -29.052  34.363  1.00 80.13           C  
ANISOU 4015  CB  GLN B 196     9026   8087  13330   -396   1856   -113       C  
ATOM   4016  CG  GLN B 196     -21.197 -29.471  33.055  1.00 79.38           C  
ANISOU 4016  CG  GLN B 196     8958   7973  13227   -374   1845   -151       C  
ATOM   4017  CD  GLN B 196     -19.725 -29.755  33.209  1.00 77.83           C  
ANISOU 4017  CD  GLN B 196     8832   7753  12987   -216   1854    -49       C  
ATOM   4018  OE1 GLN B 196     -19.012 -29.937  32.228  1.00 76.86           O  
ANISOU 4018  OE1 GLN B 196     8719   7632  12849   -173   1836    -63       O  
ATOM   4019  NE2 GLN B 196     -19.258 -29.797  34.446  1.00 77.25           N  
ANISOU 4019  NE2 GLN B 196     8802   7660  12887   -127   1883     53       N  
ATOM   4020  N   THR B 197     -22.960 -26.496  32.560  1.00 79.15           N  
ANISOU 4020  N   THR B 197     8583   8266  13221   -516   1582   -267       N  
ATOM   4021  CA  THR B 197     -23.061 -25.746  31.278  1.00 79.99           C  
ANISOU 4021  CA  THR B 197     8591   8475  13324   -546   1476   -338       C  
ATOM   4022  C   THR B 197     -21.667 -25.251  30.864  1.00 79.35           C  
ANISOU 4022  C   THR B 197     8505   8444  13198   -422   1405   -271       C  
ATOM   4023  O   THR B 197     -20.876 -24.884  31.765  1.00 78.29           O  
ANISOU 4023  O   THR B 197     8384   8327  13036   -324   1389   -172       O  
ATOM   4024  CB  THR B 197     -24.047 -24.573  31.398  1.00 80.51           C  
ANISOU 4024  CB  THR B 197     8528   8659  13401   -603   1392   -377       C  
ATOM   4025  OG1 THR B 197     -23.559 -23.716  32.432  1.00 80.77           O  
ANISOU 4025  OG1 THR B 197     8539   8742  13405   -515   1347   -284       O  
ATOM   4026  CG2 THR B 197     -25.468 -24.996  31.706  1.00 81.08           C  
ANISOU 4026  CG2 THR B 197     8582   8703  13520   -730   1456   -449       C  
ATOM   4027  N   THR B 198     -21.380 -25.250  29.556  1.00 79.92           N  
ANISOU 4027  N   THR B 198     8560   8542  13262   -430   1365   -324       N  
ATOM   4028  CA  THR B 198     -20.074 -24.846  28.965  1.00 81.21           C  
ANISOU 4028  CA  THR B 198     8715   8754  13384   -323   1304   -272       C  
ATOM   4029  C   THR B 198     -20.304 -23.679  27.997  1.00 82.02           C  
ANISOU 4029  C   THR B 198     8705   8983  13475   -349   1184   -322       C  
ATOM   4030  O   THR B 198     -20.651 -23.923  26.818  1.00 82.31           O  
ANISOU 4030  O   THR B 198     8733   9022  13516   -407   1175   -407       O  
ATOM   4031  CB  THR B 198     -19.374 -26.053  28.326  1.00 81.23           C  
ANISOU 4031  CB  THR B 198     8826   8655  13381   -288   1387   -276       C  
ATOM   4032  OG1 THR B 198     -18.820 -26.804  29.408  1.00 81.73           O  
ANISOU 4032  OG1 THR B 198     8985   8628  13440   -216   1475   -189       O  
ATOM   4033  CG2 THR B 198     -18.293 -25.681  27.334  1.00 80.33           C  
ANISOU 4033  CG2 THR B 198     8689   8599  13231   -209   1327   -256       C  
ATOM   4034  N   LEU B 199     -20.112 -22.458  28.502  1.00 82.90           N  
ANISOU 4034  N   LEU B 199     8738   9190  13567   -307   1097   -271       N  
ATOM   4035  CA  LEU B 199     -20.312 -21.171  27.776  1.00 82.00           C  
ANISOU 4035  CA  LEU B 199     8520   9198  13438   -320    980   -303       C  
ATOM   4036  C   LEU B 199     -18.956 -20.743  27.197  1.00 80.58           C  
ANISOU 4036  C   LEU B 199     8334   9063  13218   -226    928   -246       C  
ATOM   4037  O   LEU B 199     -17.925 -20.983  27.870  1.00 80.32           O  
ANISOU 4037  O   LEU B 199     8344   9003  13168   -142    955   -157       O  
ATOM   4038  CB  LEU B 199     -20.864 -20.103  28.734  1.00 82.05           C  
ANISOU 4038  CB  LEU B 199     8459   9271  13443   -325    926   -276       C  
ATOM   4039  CG  LEU B 199     -22.047 -20.501  29.628  1.00 82.96           C  
ANISOU 4039  CG  LEU B 199     8581   9342  13595   -398    989   -305       C  
ATOM   4040  CD1 LEU B 199     -22.228 -19.499  30.766  1.00 81.55           C  
ANISOU 4040  CD1 LEU B 199     8361   9217  13404   -369    946   -251       C  
ATOM   4041  CD2 LEU B 199     -23.338 -20.641  28.823  1.00 83.37           C  
ANISOU 4041  CD2 LEU B 199     8584   9415  13678   -508    987   -418       C  
ATOM   4042  N   LYS B 200     -18.956 -20.175  25.988  1.00 78.55           N  
ANISOU 4042  N   LYS B 200     8026   8874  12945   -241    860   -294       N  
ATOM   4043  CA  LYS B 200     -17.782 -19.517  25.353  1.00 76.32           C  
ANISOU 4043  CA  LYS B 200     7718   8654  12624   -165    799   -245       C  
ATOM   4044  C   LYS B 200     -18.200 -18.109  24.932  1.00 74.32           C  
ANISOU 4044  C   LYS B 200     7373   8509  12353   -187    691   -268       C  
ATOM   4045  O   LYS B 200     -19.405 -17.815  24.996  1.00 73.13           O  
ANISOU 4045  O   LYS B 200     7184   8380  12222   -257    671   -329       O  
ATOM   4046  CB  LYS B 200     -17.227 -20.310  24.160  1.00 78.50           C  
ANISOU 4046  CB  LYS B 200     8044   8895  12888   -148    836   -277       C  
ATOM   4047  CG  LYS B 200     -18.074 -21.458  23.621  1.00 81.13           C  
ANISOU 4047  CG  LYS B 200     8435   9145  13246   -226    910   -371       C  
ATOM   4048  CD  LYS B 200     -17.235 -22.606  23.043  1.00 82.39           C  
ANISOU 4048  CD  LYS B 200     8687   9220  13394   -180    990   -365       C  
ATOM   4049  CE  LYS B 200     -16.808 -23.622  24.093  1.00 83.64           C  
ANISOU 4049  CE  LYS B 200     8935   9274  13568   -133   1091   -303       C  
ATOM   4050  NZ  LYS B 200     -15.599 -24.390  23.699  1.00 83.83           N  
ANISOU 4050  NZ  LYS B 200     9033   9246  13570    -39   1151   -256       N  
ATOM   4051  N   GLY B 201     -17.230 -17.265  24.558  1.00 72.46           N  
ANISOU 4051  N   GLY B 201     7105   8340  12084   -127    627   -216       N  
ATOM   4052  CA  GLY B 201     -17.456 -15.892  24.073  1.00 71.34           C  
ANISOU 4052  CA  GLY B 201     6890   8294  11919   -137    528   -228       C  
ATOM   4053  C   GLY B 201     -17.955 -14.970  25.175  1.00 70.36           C  
ANISOU 4053  C   GLY B 201     6729   8205  11799   -145    486   -200       C  
ATOM   4054  O   GLY B 201     -17.532 -15.138  26.333  1.00 70.45           O  
ANISOU 4054  O   GLY B 201     6766   8186  11815   -113    514   -135       O  
ATOM   4055  N   VAL B 202     -18.824 -14.023  24.816  1.00 69.54           N  
ANISOU 4055  N   VAL B 202     6569   8163  11688   -182    420   -246       N  
ATOM   4056  CA  VAL B 202     -19.361 -12.948  25.706  1.00 68.93           C  
ANISOU 4056  CA  VAL B 202     6454   8127  11608   -185    371   -225       C  
ATOM   4057  C   VAL B 202     -20.031 -13.569  26.948  1.00 69.39           C  
ANISOU 4057  C   VAL B 202     6535   8130  11699   -210    434   -223       C  
ATOM   4058  O   VAL B 202     -19.807 -13.040  28.060  1.00 70.59           O  
ANISOU 4058  O   VAL B 202     6692   8287  11842   -182    422   -164       O  
ATOM   4059  CB  VAL B 202     -20.342 -12.040  24.934  1.00 68.31           C  
ANISOU 4059  CB  VAL B 202     6317   8117  11518   -217    304   -288       C  
ATOM   4060  CG1 VAL B 202     -20.904 -10.942  25.821  1.00 68.45           C  
ANISOU 4060  CG1 VAL B 202     6303   8173  11530   -212    260   -268       C  
ATOM   4061  CG2 VAL B 202     -19.729 -11.445  23.669  1.00 67.56           C  
ANISOU 4061  CG2 VAL B 202     6207   8073  11386   -192    247   -290       C  
ATOM   4062  N   GLU B 203     -20.815 -14.642  26.784  1.00 67.84           N  
ANISOU 4062  N   GLU B 203     6356   7882  11536   -264    501   -284       N  
ATOM   4063  CA  GLU B 203     -21.659 -15.241  27.862  1.00 68.50           C  
ANISOU 4063  CA  GLU B 203     6458   7914  11655   -304    569   -294       C  
ATOM   4064  C   GLU B 203     -20.770 -15.839  28.972  1.00 67.07           C  
ANISOU 4064  C   GLU B 203     6346   7666  11472   -252    628   -211       C  
ATOM   4065  O   GLU B 203     -21.312 -16.173  30.053  1.00 66.45           O  
ANISOU 4065  O   GLU B 203     6288   7545  11411   -270    680   -199       O  
ATOM   4066  CB  GLU B 203     -22.615 -16.296  27.284  1.00 70.43           C  
ANISOU 4066  CB  GLU B 203     6708   8116  11935   -384    629   -384       C  
ATOM   4067  CG  GLU B 203     -24.015 -15.783  26.951  1.00 70.70           C  
ANISOU 4067  CG  GLU B 203     6663   8213  11983   -450    592   -463       C  
ATOM   4068  CD  GLU B 203     -24.790 -16.629  25.942  1.00 73.29           C  
ANISOU 4068  CD  GLU B 203     6981   8531  12334   -532    619   -563       C  
ATOM   4069  OE1 GLU B 203     -24.226 -16.923  24.859  1.00 72.77           O  
ANISOU 4069  OE1 GLU B 203     6937   8461  12249   -523    605   -586       O  
ATOM   4070  OE2 GLU B 203     -25.969 -16.998  26.227  1.00 73.96           O  
ANISOU 4070  OE2 GLU B 203     7034   8611  12453   -608    656   -621       O  
ATOM   4071  N   ALA B 204     -19.462 -15.979  28.714  1.00 65.87           N  
ANISOU 4071  N   ALA B 204     6223   7506  11294   -188    621   -154       N  
ATOM   4072  CA  ALA B 204     -18.466 -16.629  29.601  1.00 64.95           C  
ANISOU 4072  CA  ALA B 204     6171   7336  11170   -125    674    -72       C  
ATOM   4073  C   ALA B 204     -18.024 -15.680  30.721  1.00 64.09           C  
ANISOU 4073  C   ALA B 204     6047   7271  11034    -80    624      2       C  
ATOM   4074  O   ALA B 204     -17.721 -16.185  31.823  1.00 64.04           O  
ANISOU 4074  O   ALA B 204     6089   7218  11023    -47    673     58       O  
ATOM   4075  CB  ALA B 204     -17.284 -17.077  28.784  1.00 65.40           C  
ANISOU 4075  CB  ALA B 204     6251   7386  11210    -73    681    -45       C  
ATOM   4076  N   VAL B 205     -17.993 -14.368  30.446  1.00 63.31           N  
ANISOU 4076  N   VAL B 205     5889   7253  10911    -80    532      2       N  
ATOM   4077  CA  VAL B 205     -17.415 -13.312  31.338  1.00 62.54           C  
ANISOU 4077  CA  VAL B 205     5778   7203  10779    -40    470     69       C  
ATOM   4078  C   VAL B 205     -18.524 -12.594  32.131  1.00 62.38           C  
ANISOU 4078  C   VAL B 205     5741   7198  10762    -74    453     47       C  
ATOM   4079  O   VAL B 205     -18.218 -12.085  33.231  1.00 63.55           O  
ANISOU 4079  O   VAL B 205     5905   7355  10884    -46    434    101       O  
ATOM   4080  CB  VAL B 205     -16.561 -12.309  30.537  1.00 61.64           C  
ANISOU 4080  CB  VAL B 205     5624   7162  10635    -18    386     89       C  
ATOM   4081  CG1 VAL B 205     -15.334 -12.964  29.933  1.00 61.34           C  
ANISOU 4081  CG1 VAL B 205     5599   7117  10589     26    407    126       C  
ATOM   4082  CG2 VAL B 205     -17.352 -11.600  29.448  1.00 62.15           C  
ANISOU 4082  CG2 VAL B 205     5641   7269  10702    -61    338     18       C  
ATOM   4083  N   MET B 206     -19.755 -12.538  31.609  1.00 61.57           N  
ANISOU 4083  N   MET B 206     5606   7101  10685   -130    459    -30       N  
ATOM   4084  CA  MET B 206     -20.887 -11.791  32.229  1.00 61.02           C  
ANISOU 4084  CA  MET B 206     5508   7056  10619   -158    442    -56       C  
ATOM   4085  C   MET B 206     -21.790 -12.757  33.002  1.00 62.37           C  
ANISOU 4085  C   MET B 206     5704   7166  10824   -194    533    -78       C  
ATOM   4086  O   MET B 206     -22.079 -13.853  32.482  1.00 63.91           O  
ANISOU 4086  O   MET B 206     5914   7316  11054   -231    595   -119       O  
ATOM   4087  CB  MET B 206     -21.717 -11.080  31.159  1.00 59.90           C  
ANISOU 4087  CB  MET B 206     5303   6973  10482   -191    388   -126       C  
ATOM   4088  CG  MET B 206     -20.995  -9.898  30.543  1.00 59.44           C  
ANISOU 4088  CG  MET B 206     5224   6976  10384   -157    298   -102       C  
ATOM   4089  SD  MET B 206     -21.896  -9.121  29.181  1.00 59.45           S  
ANISOU 4089  SD  MET B 206     5160   7044  10382   -183    237   -179       S  
ATOM   4090  CE  MET B 206     -23.266  -8.389  30.077  1.00 60.41           C  
ANISOU 4090  CE  MET B 206     5252   7190  10509   -195    233   -203       C  
ATOM   4091  N   TYR B 207     -22.217 -12.360  34.202  1.00 62.71           N  
ANISOU 4091  N   TYR B 207     5760   7208  10859   -186    544    -51       N  
ATOM   4092  CA  TYR B 207     -23.283 -13.036  34.982  1.00 63.39           C  
ANISOU 4092  CA  TYR B 207     5860   7248  10977   -227    628    -75       C  
ATOM   4093  C   TYR B 207     -24.210 -11.978  35.591  1.00 63.09           C  
ANISOU 4093  C   TYR B 207     5784   7259  10929   -231    598    -89       C  
ATOM   4094  O   TYR B 207     -23.705 -10.939  36.074  1.00 62.58           O  
ANISOU 4094  O   TYR B 207     5727   7228  10821   -184    536    -44       O  
ATOM   4095  CB  TYR B 207     -22.671 -13.933  36.059  1.00 64.57           C  
ANISOU 4095  CB  TYR B 207     6090   7324  11119   -195    701    -10       C  
ATOM   4096  CG  TYR B 207     -23.676 -14.614  36.957  1.00 66.09           C  
ANISOU 4096  CG  TYR B 207     6308   7463  11339   -234    795    -23       C  
ATOM   4097  CD1 TYR B 207     -24.337 -15.767  36.559  1.00 66.91           C  
ANISOU 4097  CD1 TYR B 207     6420   7509  11490   -298    880    -75       C  
ATOM   4098  CD2 TYR B 207     -23.967 -14.103  38.212  1.00 66.44           C  
ANISOU 4098  CD2 TYR B 207     6373   7512  11360   -211    804     14       C  
ATOM   4099  CE1 TYR B 207     -25.247 -16.400  37.391  1.00 68.04           C  
ANISOU 4099  CE1 TYR B 207     6589   7603  11660   -341    973    -86       C  
ATOM   4100  CE2 TYR B 207     -24.878 -14.721  39.052  1.00 67.42           C  
ANISOU 4100  CE2 TYR B 207     6521   7588  11506   -246    897      5       C  
ATOM   4101  CZ  TYR B 207     -25.519 -15.876  38.643  1.00 69.06           C  
ANISOU 4101  CZ  TYR B 207     6734   7740  11765   -313    983    -43       C  
ATOM   4102  OH  TYR B 207     -26.415 -16.490  39.474  1.00 72.20           O  
ANISOU 4102  OH  TYR B 207     7156   8089  12188   -355   1082    -50       O  
ATOM   4103  N   MET B 208     -25.518 -12.244  35.553  1.00 62.61           N  
ANISOU 4103  N   MET B 208     5682   7201  10905   -287    643   -150       N  
ATOM   4104  CA  MET B 208     -26.583 -11.442  36.208  1.00 62.08           C  
ANISOU 4104  CA  MET B 208     5576   7175  10835   -292    639   -167       C  
ATOM   4105  C   MET B 208     -27.209 -12.294  37.320  1.00 61.67           C  
ANISOU 4105  C   MET B 208     5559   7064  10807   -320    745   -158       C  
ATOM   4106  O   MET B 208     -27.822 -13.317  36.975  1.00 62.62           O  
ANISOU 4106  O   MET B 208     5667   7152  10974   -385    814   -205       O  
ATOM   4107  CB  MET B 208     -27.641 -11.045  35.171  1.00 63.09           C  
ANISOU 4107  CB  MET B 208     5612   7371  10987   -333    604   -248       C  
ATOM   4108  CG  MET B 208     -28.783 -10.200  35.717  1.00 63.73           C  
ANISOU 4108  CG  MET B 208     5642   7505  11066   -330    600   -268       C  
ATOM   4109  SD  MET B 208     -28.250  -8.607  36.390  1.00 63.86           S  
ANISOU 4109  SD  MET B 208     5689   7555  11018   -245    520   -208       S  
ATOM   4110  CE  MET B 208     -29.723  -7.608  36.172  1.00 65.12           C  
ANISOU 4110  CE  MET B 208     5759   7798  11182   -242    494   -264       C  
ATOM   4111  N   GLY B 209     -27.029 -11.921  38.598  1.00 59.95           N  
ANISOU 4111  N   GLY B 209     5391   6829  10555   -277    760    -99       N  
ATOM   4112  CA  GLY B 209     -27.571 -12.683  39.748  1.00 58.98           C  
ANISOU 4112  CA  GLY B 209     5313   6649  10447   -295    865    -80       C  
ATOM   4113  C   GLY B 209     -27.021 -12.241  41.097  1.00 57.87           C  
ANISOU 4113  C   GLY B 209     5245   6490  10252   -231    865     -4       C  
ATOM   4114  O   GLY B 209     -27.814 -12.088  42.029  1.00 57.81           O  
ANISOU 4114  O   GLY B 209     5244   6479  10241   -234    915     -1       O  
ATOM   4115  N   THR B 210     -25.702 -12.091  41.220  1.00 57.68           N  
ANISOU 4115  N   THR B 210     5273   6457  10186   -175    814     55       N  
ATOM   4116  CA  THR B 210     -24.998 -11.646  42.458  1.00 57.38           C  
ANISOU 4116  CA  THR B 210     5305   6410  10087   -112    798    129       C  
ATOM   4117  C   THR B 210     -23.717 -10.905  42.073  1.00 55.38           C  
ANISOU 4117  C   THR B 210     5055   6196   9790    -66    693    165       C  
ATOM   4118  O   THR B 210     -23.266 -11.087  40.925  1.00 54.23           O  
ANISOU 4118  O   THR B 210     4873   6063   9666    -79    659    144       O  
ATOM   4119  CB  THR B 210     -24.628 -12.814  43.381  1.00 59.06           C  
ANISOU 4119  CB  THR B 210     5601   6545  10291    -95    888    184       C  
ATOM   4120  OG1 THR B 210     -24.053 -12.252  44.561  1.00 59.85           O  
ANISOU 4120  OG1 THR B 210     5762   6652  10326    -34    861    248       O  
ATOM   4121  CG2 THR B 210     -23.642 -13.783  42.765  1.00 59.07           C  
ANISOU 4121  CG2 THR B 210     5630   6507  10305    -83    899    206       C  
ATOM   4122  N   LEU B 211     -23.152 -10.126  43.003  1.00 53.89           N  
ANISOU 4122  N   LEU B 211     4909   6025   9540    -19    647    216       N  
ATOM   4123  CA  LEU B 211     -21.972  -9.251  42.755  1.00 53.17           C  
ANISOU 4123  CA  LEU B 211     4818   5979   9404     14    543    249       C  
ATOM   4124  C   LEU B 211     -20.677  -9.912  43.269  1.00 52.54           C  
ANISOU 4124  C   LEU B 211     4793   5878   9292     59    544    321       C  
ATOM   4125  O   LEU B 211     -19.620  -9.667  42.663  1.00 50.70           O  
ANISOU 4125  O   LEU B 211     4540   5678   9045     75    477    342       O  
ATOM   4126  CB  LEU B 211     -22.221  -7.903  43.437  1.00 53.02           C  
ANISOU 4126  CB  LEU B 211     4813   5996   9336     31    487    251       C  
ATOM   4127  CG  LEU B 211     -23.506  -7.166  43.053  1.00 51.66           C  
ANISOU 4127  CG  LEU B 211     4590   5850   9187      5    486    187       C  
ATOM   4128  CD1 LEU B 211     -23.740  -5.997  43.992  1.00 51.18           C  
ANISOU 4128  CD1 LEU B 211     4568   5806   9070     33    454    199       C  
ATOM   4129  CD2 LEU B 211     -23.456  -6.679  41.613  1.00 51.23           C  
ANISOU 4129  CD2 LEU B 211     4469   5838   9158    -14    423    145       C  
ATOM   4130  N   SER B 212     -20.753 -10.707  44.343  1.00 52.85           N  
ANISOU 4130  N   SER B 212     4895   5867   9316     81    618    361       N  
ATOM   4131  CA  SER B 212     -19.583 -11.345  45.007  1.00 52.66           C  
ANISOU 4131  CA  SER B 212     4929   5826   9251    138    624    437       C  
ATOM   4132  C   SER B 212     -19.103 -12.534  44.184  1.00 53.55           C  
ANISOU 4132  C   SER B 212     5037   5903   9407    141    669    443       C  
ATOM   4133  O   SER B 212     -19.888 -13.492  44.014  1.00 53.71           O  
ANISOU 4133  O   SER B 212     5070   5861   9475    110    763    413       O  
ATOM   4134  CB  SER B 212     -19.880 -11.776  46.415  1.00 52.78           C  
ANISOU 4134  CB  SER B 212     5021   5798   9231    167    691    479       C  
ATOM   4135  OG  SER B 212     -18.780 -12.485  46.960  1.00 51.88           O  
ANISOU 4135  OG  SER B 212     4961   5670   9080    228    699    553       O  
ATOM   4136  N   TYR B 213     -17.847 -12.466  43.733  1.00 54.72           N  
ANISOU 4136  N   TYR B 213     5169   6088   9535    178    607    480       N  
ATOM   4137  CA  TYR B 213     -17.172 -13.500  42.912  1.00 55.20           C  
ANISOU 4137  CA  TYR B 213     5225   6122   9625    197    640    492       C  
ATOM   4138  C   TYR B 213     -16.795 -14.676  43.805  1.00 58.24           C  
ANISOU 4138  C   TYR B 213     5691   6446   9992    253    720    556       C  
ATOM   4139  O   TYR B 213     -16.933 -15.823  43.352  1.00 60.04           O  
ANISOU 4139  O   TYR B 213     5944   6607  10259    251    803    547       O  
ATOM   4140  CB  TYR B 213     -15.933 -12.922  42.235  1.00 54.11           C  
ANISOU 4140  CB  TYR B 213     5039   6054   9465    222    546    517       C  
ATOM   4141  CG  TYR B 213     -15.321 -13.776  41.153  1.00 53.40           C  
ANISOU 4141  CG  TYR B 213     4932   5949   9409    238    571    516       C  
ATOM   4142  CD1 TYR B 213     -16.101 -14.518  40.277  1.00 53.14           C  
ANISOU 4142  CD1 TYR B 213     4895   5861   9433    194    639    456       C  
ATOM   4143  CD2 TYR B 213     -13.950 -13.809  40.983  1.00 52.32           C  
ANISOU 4143  CD2 TYR B 213     4778   5857   9242    294    526    574       C  
ATOM   4144  CE1 TYR B 213     -15.528 -15.283  39.273  1.00 52.98           C  
ANISOU 4144  CE1 TYR B 213     4868   5822   9438    210    664    453       C  
ATOM   4145  CE2 TYR B 213     -13.365 -14.565  39.986  1.00 52.24           C  
ANISOU 4145  CE2 TYR B 213     4754   5835   9259    316    553    575       C  
ATOM   4146  CZ  TYR B 213     -14.151 -15.307  39.126  1.00 52.41           C  
ANISOU 4146  CZ  TYR B 213     4784   5793   9335    275    623    514       C  
ATOM   4147  OH  TYR B 213     -13.568 -16.057  38.144  1.00 51.87           O  
ANISOU 4147  OH  TYR B 213     4711   5707   9288    298    652    513       O  
ATOM   4148  N   GLU B 214     -16.339 -14.391  45.029  1.00 60.73           N  
ANISOU 4148  N   GLU B 214     6049   6781  10244    303    697    617       N  
ATOM   4149  CA  GLU B 214     -15.968 -15.428  46.028  1.00 63.75           C  
ANISOU 4149  CA  GLU B 214     6516   7110  10594    369    770    687       C  
ATOM   4150  C   GLU B 214     -17.194 -16.308  46.277  1.00 65.37           C  
ANISOU 4150  C   GLU B 214     6775   7220  10843    330    894    656       C  
ATOM   4151  O   GLU B 214     -17.059 -17.548  46.201  1.00 65.67           O  
ANISOU 4151  O   GLU B 214     6866   7184  10900    356    983    679       O  
ATOM   4152  CB  GLU B 214     -15.469 -14.805  47.331  1.00 65.30           C  
ANISOU 4152  CB  GLU B 214     6748   7353  10710    419    716    747       C  
ATOM   4153  CG  GLU B 214     -14.209 -15.470  47.852  1.00 68.10           C  
ANISOU 4153  CG  GLU B 214     7140   7719  11013    513    711    835       C  
ATOM   4154  CD  GLU B 214     -13.888 -15.151  49.300  1.00 70.67           C  
ANISOU 4154  CD  GLU B 214     7522   8074  11254    565    683    895       C  
ATOM   4155  OE1 GLU B 214     -14.781 -15.341  50.155  1.00 71.64           O  
ANISOU 4155  OE1 GLU B 214     7711   8142  11366    555    751    892       O  
ATOM   4156  OE2 GLU B 214     -12.743 -14.713  49.573  1.00 72.69           O  
ANISOU 4156  OE2 GLU B 214     7754   8410  11454    612    593    944       O  
ATOM   4157  N   GLN B 215     -18.351 -15.680  46.521  1.00 67.68           N  
ANISOU 4157  N   GLN B 215     7050   7514  11149    270    902    604       N  
ATOM   4158  CA  GLN B 215     -19.625 -16.383  46.820  1.00 69.43           C  
ANISOU 4158  CA  GLN B 215     7309   7658  11413    220   1019    570       C  
ATOM   4159  C   GLN B 215     -19.998 -17.248  45.610  1.00 71.30           C  
ANISOU 4159  C   GLN B 215     7521   7845  11724    166   1076    514       C  
ATOM   4160  O   GLN B 215     -20.487 -18.368  45.827  1.00 75.59           O  
ANISOU 4160  O   GLN B 215     8124   8300  12296    149   1190    515       O  
ATOM   4161  CB  GLN B 215     -20.702 -15.374  47.229  1.00 69.33           C  
ANISOU 4161  CB  GLN B 215     7265   7679  11398    173   1001    525       C  
ATOM   4162  CG  GLN B 215     -22.101 -15.946  47.401  1.00 70.01           C  
ANISOU 4162  CG  GLN B 215     7361   7704  11534    108   1113    479       C  
ATOM   4163  CD  GLN B 215     -22.717 -15.667  48.747  1.00 71.19           C  
ANISOU 4163  CD  GLN B 215     7563   7843  11643    122   1157    504       C  
ATOM   4164  OE1 GLN B 215     -23.032 -14.530  49.092  1.00 71.13           O  
ANISOU 4164  OE1 GLN B 215     7526   7892  11605    122   1097    488       O  
ATOM   4165  NE2 GLN B 215     -22.918 -16.723  49.514  1.00 72.50           N  
ANISOU 4165  NE2 GLN B 215     7812   7929  11804    135   1269    543       N  
ATOM   4166  N   PHE B 216     -19.770 -16.747  44.397  1.00 71.14           N  
ANISOU 4166  N   PHE B 216     7421   7876  11730    139   1003    468       N  
ATOM   4167  CA  PHE B 216     -20.119 -17.428  43.126  1.00 71.55           C  
ANISOU 4167  CA  PHE B 216     7444   7894  11848     84   1041    406       C  
ATOM   4168  C   PHE B 216     -19.337 -18.738  42.995  1.00 72.19           C  
ANISOU 4168  C   PHE B 216     7595   7901  11931    131   1111    450       C  
ATOM   4169  O   PHE B 216     -19.776 -19.618  42.248  1.00 72.49           O  
ANISOU 4169  O   PHE B 216     7644   7876  12020     83   1182    402       O  
ATOM   4170  CB  PHE B 216     -19.821 -16.502  41.950  1.00 71.16           C  
ANISOU 4170  CB  PHE B 216     7304   7925  11807     66    935    363       C  
ATOM   4171  CG  PHE B 216     -20.378 -16.968  40.634  1.00 71.44           C  
ANISOU 4171  CG  PHE B 216     7298   7941  11902      0    961    285       C  
ATOM   4172  CD1 PHE B 216     -21.744 -17.089  40.443  1.00 72.08           C  
ANISOU 4172  CD1 PHE B 216     7352   8004  12030    -81   1009    212       C  
ATOM   4173  CD2 PHE B 216     -19.532 -17.274  39.582  1.00 72.09           C  
ANISOU 4173  CD2 PHE B 216     7367   8030  11991     20    934    283       C  
ATOM   4174  CE1 PHE B 216     -22.247 -17.506  39.220  1.00 73.27           C  
ANISOU 4174  CE1 PHE B 216     7463   8146  12230   -146   1024    136       C  
ATOM   4175  CE2 PHE B 216     -20.037 -17.687  38.360  1.00 72.58           C  
ANISOU 4175  CE2 PHE B 216     7397   8076  12101    -40    954    208       C  
ATOM   4176  CZ  PHE B 216     -21.392 -17.807  38.184  1.00 72.93           C  
ANISOU 4176  CZ  PHE B 216     7416   8104  12189   -125    996    133       C  
ATOM   4177  N   LYS B 217     -18.186 -18.841  43.661  1.00 73.36           N  
ANISOU 4177  N   LYS B 217     7788   8061  12025    225   1089    536       N  
ATOM   4178  CA  LYS B 217     -17.320 -20.052  43.643  1.00 76.77           C  
ANISOU 4178  CA  LYS B 217     8292   8427  12448    294   1153    592       C  
ATOM   4179  C   LYS B 217     -17.821 -21.056  44.686  1.00 80.14           C  
ANISOU 4179  C   LYS B 217     8825   8753  12869    307   1276    628       C  
ATOM   4180  O   LYS B 217     -17.775 -22.272  44.399  1.00 83.55           O  
ANISOU 4180  O   LYS B 217     9325   9091  13327    315   1373    632       O  
ATOM   4181  CB  LYS B 217     -15.858 -19.692  43.921  1.00 76.57           C  
ANISOU 4181  CB  LYS B 217     8256   8473  12362    395   1071    673       C  
ATOM   4182  CG  LYS B 217     -15.168 -18.888  42.830  1.00 74.60           C  
ANISOU 4182  CG  LYS B 217     7912   8312  12117    390    966    650       C  
ATOM   4183  CD  LYS B 217     -13.946 -18.152  43.328  1.00 74.57           C  
ANISOU 4183  CD  LYS B 217     7879   8403  12050    463    867    721       C  
ATOM   4184  CE  LYS B 217     -13.201 -17.456  42.211  1.00 74.31           C  
ANISOU 4184  CE  LYS B 217     7756   8451  12024    456    776    703       C  
ATOM   4185  NZ  LYS B 217     -12.315 -16.372  42.699  1.00 73.90           N  
ANISOU 4185  NZ  LYS B 217     7658   8505  11916    487    664    748       N  
ATOM   4186  N   LYS B 218     -18.264 -20.566  45.850  1.00 80.27           N  
ANISOU 4186  N   LYS B 218     8863   8785  12851    310   1275    652       N  
ATOM   4187  CA  LYS B 218     -18.709 -21.410  46.993  1.00 80.54           C  
ANISOU 4187  CA  LYS B 218     9004   8729  12867    329   1390    696       C  
ATOM   4188  C   LYS B 218     -20.095 -21.975  46.667  1.00 80.31           C  
ANISOU 4188  C   LYS B 218     8982   8622  12908    220   1494    620       C  
ATOM   4189  O   LYS B 218     -20.170 -23.171  46.348  1.00 80.43           O  
ANISOU 4189  O   LYS B 218     9063   8538  12956    208   1595    616       O  
ATOM   4190  CB  LYS B 218     -18.650 -20.618  48.303  1.00 81.31           C  
ANISOU 4190  CB  LYS B 218     9119   8879  12895    372   1346    747       C  
ATOM   4191  CG  LYS B 218     -17.280 -20.019  48.586  1.00 82.54           C  
ANISOU 4191  CG  LYS B 218     9257   9123  12982    466   1234    815       C  
ATOM   4192  CD  LYS B 218     -16.989 -19.635  50.013  1.00 84.72           C  
ANISOU 4192  CD  LYS B 218     9587   9428  13174    531   1211    884       C  
ATOM   4193  CE  LYS B 218     -15.538 -19.204  50.148  1.00 86.73           C  
ANISOU 4193  CE  LYS B 218     9815   9772  13364    620   1101    948       C  
ATOM   4194  NZ  LYS B 218     -15.240 -18.596  51.467  1.00 88.11           N  
ANISOU 4194  NZ  LYS B 218    10028   9999  13452    671   1051   1003       N  
ATOM   4195  N   GLY B 219     -21.140 -21.144  46.706  1.00 80.25           N  
ANISOU 4195  N   GLY B 219     8907   8659  12923    142   1470    559       N  
ATOM   4196  CA  GLY B 219     -22.521 -21.584  46.433  1.00 81.46           C  
ANISOU 4196  CA  GLY B 219     9048   8758  13143     32   1562    483       C  
ATOM   4197  C   GLY B 219     -23.491 -20.422  46.363  1.00 81.83           C  
ANISOU 4197  C   GLY B 219     8997   8888  13206    -31   1504    420       C  
ATOM   4198  O   GLY B 219     -23.284 -19.431  47.076  1.00 79.27           O  
ANISOU 4198  O   GLY B 219     8659   8630  12830     14   1434    453       O  
ATOM   4199  N   VAL B 220     -24.524 -20.560  45.530  1.00 85.16           N  
ANISOU 4199  N   VAL B 220     9355   9306  13696   -133   1534    331       N  
ATOM   4200  CA  VAL B 220     -25.621 -19.565  45.334  1.00 88.04           C  
ANISOU 4200  CA  VAL B 220     9616   9748  14085   -199   1492    262       C  
ATOM   4201  C   VAL B 220     -26.925 -20.354  45.152  1.00 90.96           C  
ANISOU 4201  C   VAL B 220     9973  10064  14522   -308   1605    196       C  
ATOM   4202  O   VAL B 220     -26.897 -21.356  44.403  1.00 94.34           O  
ANISOU 4202  O   VAL B 220    10424  10428  14992   -355   1659    164       O  
ATOM   4203  CB  VAL B 220     -25.315 -18.646  44.131  1.00 88.15           C  
ANISOU 4203  CB  VAL B 220     9531   9853  14107   -203   1365    214       C  
ATOM   4204  CG1 VAL B 220     -26.495 -17.760  43.754  1.00 89.02           C  
ANISOU 4204  CG1 VAL B 220     9536  10038  14248   -269   1329    138       C  
ATOM   4205  CG2 VAL B 220     -24.075 -17.802  44.370  1.00 86.96           C  
ANISOU 4205  CG2 VAL B 220     9388   9759  13891   -108   1257    278       C  
ATOM   4206  N   GLN B 221     -28.016 -19.927  45.804  1.00 91.50           N  
ANISOU 4206  N   GLN B 221    10006  10160  14599   -348   1641    175       N  
ATOM   4207  CA  GLN B 221     -29.316 -20.654  45.831  1.00 92.94           C  
ANISOU 4207  CA  GLN B 221    10171  10298  14843   -457   1758    118       C  
ATOM   4208  C   GLN B 221     -30.243 -20.087  44.744  1.00 93.95           C  
ANISOU 4208  C   GLN B 221    10160  10513  15024   -540   1703     18       C  
ATOM   4209  O   GLN B 221     -30.324 -18.851  44.639  1.00 91.65           O  
ANISOU 4209  O   GLN B 221     9793  10320  14710   -504   1602      7       O  
ATOM   4210  CB  GLN B 221     -29.896 -20.593  47.243  1.00 93.37           C  
ANISOU 4210  CB  GLN B 221    10273  10331  14872   -443   1840    163       C  
ATOM   4211  CG  GLN B 221     -30.389 -19.209  47.646  1.00 93.80           C  
ANISOU 4211  CG  GLN B 221    10250  10491  14898   -416   1766    154       C  
ATOM   4212  CD  GLN B 221     -31.824 -18.963  47.238  1.00 94.68           C  
ANISOU 4212  CD  GLN B 221    10246  10657  15070   -512   1795     69       C  
ATOM   4213  OE1 GLN B 221     -32.723 -19.747  47.541  1.00 94.04           O  
ANISOU 4213  OE1 GLN B 221    10170  10528  15032   -591   1915     46       O  
ATOM   4214  NE2 GLN B 221     -32.056 -17.856  46.547  1.00 94.05           N  
ANISOU 4214  NE2 GLN B 221    10058  10682  14992   -506   1685     22       N  
ATOM   4215  N   ILE B 222     -30.894 -20.966  43.964  1.00 97.89           N  
ANISOU 4215  N   ILE B 222    10633  10974  15587   -645   1766    -52       N  
ATOM   4216  CA  ILE B 222     -31.864 -20.622  42.872  1.00100.24           C  
ANISOU 4216  CA  ILE B 222    10796  11352  15937   -736   1723   -155       C  
ATOM   4217  C   ILE B 222     -32.970 -21.682  42.829  1.00102.53           C  
ANISOU 4217  C   ILE B 222    11077  11587  16292   -866   1849   -215       C  
ATOM   4218  O   ILE B 222     -32.804 -22.755  43.397  1.00102.36           O  
ANISOU 4218  O   ILE B 222    11165  11450  16276   -884   1962   -179       O  
ATOM   4219  CB  ILE B 222     -31.130 -20.486  41.516  1.00 99.67           C  
ANISOU 4219  CB  ILE B 222    10692  11310  15865   -724   1622   -190       C  
ATOM   4220  CG1 ILE B 222     -30.297 -21.725  41.170  1.00101.42           C  
ANISOU 4220  CG1 ILE B 222    11021  11419  16093   -726   1679   -172       C  
ATOM   4221  CG2 ILE B 222     -30.290 -19.219  41.485  1.00 97.83           C  
ANISOU 4221  CG2 ILE B 222    10436  11157  15575   -617   1491   -147       C  
ATOM   4222  CD1 ILE B 222     -29.732 -21.711  39.768  1.00101.94           C  
ANISOU 4222  CD1 ILE B 222    11054  11511  16165   -728   1598   -218       C  
ATOM   4223  N   PRO B 223     -34.134 -21.436  42.172  1.00102.07           N  
ANISOU 4223  N   PRO B 223    10891  11608  16283   -961   1836   -306       N  
ATOM   4224  CA  PRO B 223     -35.129 -22.489  41.945  1.00103.14           C  
ANISOU 4224  CA  PRO B 223    11007  11696  16483  -1101   1946   -374       C  
ATOM   4225  C   PRO B 223     -34.659 -23.612  41.005  1.00103.17           C  
ANISOU 4225  C   PRO B 223    11075  11610  16512  -1161   1974   -413       C  
ATOM   4226  O   PRO B 223     -34.975 -24.738  41.321  1.00104.70           O  
ANISOU 4226  O   PRO B 223    11343  11700  16738  -1240   2100   -420       O  
ATOM   4227  CB  PRO B 223     -36.310 -21.784  41.262  1.00103.30           C  
ANISOU 4227  CB  PRO B 223    10857  11851  16540  -1172   1889   -465       C  
ATOM   4228  CG  PRO B 223     -36.065 -20.295  41.465  1.00101.27           C  
ANISOU 4228  CG  PRO B 223    10542  11701  16232  -1056   1771   -428       C  
ATOM   4229  CD  PRO B 223     -34.570 -20.136  41.638  1.00100.21           C  
ANISOU 4229  CD  PRO B 223    10521  11513  16040   -939   1717   -347       C  
ATOM   4230  N   GLN B 229     -35.255 -25.451  45.889  1.00 85.16           N  
ANISOU 4230  N   GLN B 229     9147   9019  14190  -1126   2435   -164       N  
ATOM   4231  CA  GLN B 229     -34.103 -24.652  45.384  1.00 84.25           C  
ANISOU 4231  CA  GLN B 229     9025   8960  14025  -1006   2286   -134       C  
ATOM   4232  C   GLN B 229     -32.968 -25.579  44.915  1.00 84.62           C  
ANISOU 4232  C   GLN B 229     9193   8898  14059   -971   2298   -106       C  
ATOM   4233  O   GLN B 229     -33.130 -26.827  44.977  1.00 86.03           O  
ANISOU 4233  O   GLN B 229     9466   8953  14268  -1041   2425   -112       O  
ATOM   4234  CB  GLN B 229     -33.599 -23.698  46.474  1.00 83.36           C  
ANISOU 4234  CB  GLN B 229     8941   8890  13839   -874   2237    -45       C  
ATOM   4235  CG  GLN B 229     -32.598 -24.325  47.444  1.00 82.50           C  
ANISOU 4235  CG  GLN B 229     8998   8671  13674   -780   2299     60       C  
ATOM   4236  CD  GLN B 229     -33.062 -24.220  48.876  1.00 82.40           C  
ANISOU 4236  CD  GLN B 229     9037   8640  13630   -753   2386    120       C  
ATOM   4237  OE1 GLN B 229     -34.256 -24.142  49.146  1.00 82.43           O  
ANISOU 4237  OE1 GLN B 229     8973   8672  13671   -837   2452     77       O  
ATOM   4238  NE2 GLN B 229     -32.121 -24.239  49.805  1.00 81.55           N  
ANISOU 4238  NE2 GLN B 229     9046   8488  13449   -636   2388    219       N  
ATOM   4239  N   ALA B 230     -31.878 -24.972  44.423  1.00 82.43           N  
ANISOU 4239  N   ALA B 230     8913   8667  13740   -868   2174    -78       N  
ATOM   4240  CA  ALA B 230     -30.627 -25.648  43.989  1.00 80.46           C  
ANISOU 4240  CA  ALA B 230     8767   8338  13467   -803   2166    -39       C  
ATOM   4241  C   ALA B 230     -29.404 -24.843  44.460  1.00 77.76           C  
ANISOU 4241  C   ALA B 230     8453   8041  13049   -649   2066     51       C  
ATOM   4242  O   ALA B 230     -29.577 -23.751  45.042  1.00 78.21           O  
ANISOU 4242  O   ALA B 230     8450   8188  13075   -605   2001     73       O  
ATOM   4243  CB  ALA B 230     -30.619 -25.837  42.488  1.00 79.68           C  
ANISOU 4243  CB  ALA B 230     8608   8259  13407   -867   2111   -127       C  
ATOM   4244  N   THR B 231     -28.205 -25.375  44.208  1.00 74.97           N  
ANISOU 4244  N   THR B 231     8188   7629  12668   -571   2056    100       N  
ATOM   4245  CA  THR B 231     -26.897 -24.732  44.501  1.00 72.68           C  
ANISOU 4245  CA  THR B 231     7920   7384  12308   -430   1958    183       C  
ATOM   4246  C   THR B 231     -26.123 -24.551  43.190  1.00 69.66           C  
ANISOU 4246  C   THR B 231     7491   7043  11931   -409   1861    151       C  
ATOM   4247  O   THR B 231     -25.845 -25.574  42.533  1.00 69.69           O  
ANISOU 4247  O   THR B 231     7556   6963  11960   -431   1919    132       O  
ATOM   4248  CB  THR B 231     -26.103 -25.538  45.537  1.00 73.58           C  
ANISOU 4248  CB  THR B 231     8182   7399  12374   -337   2040    287       C  
ATOM   4249  OG1 THR B 231     -26.939 -25.662  46.688  1.00 75.19           O  
ANISOU 4249  OG1 THR B 231     8424   7570  12575   -366   2133    310       O  
ATOM   4250  CG2 THR B 231     -24.787 -24.893  45.919  1.00 72.56           C  
ANISOU 4250  CG2 THR B 231     8068   7328  12172   -196   1939    373       C  
ATOM   4251  N   LYS B 232     -25.821 -23.292  42.848  1.00 66.28           N  
ANISOU 4251  N   LYS B 232     6966   6736  11480   -370   1726    144       N  
ATOM   4252  CA  LYS B 232     -25.014 -22.873  41.670  1.00 64.61           C  
ANISOU 4252  CA  LYS B 232     6702   6584  11263   -339   1619    123       C  
ATOM   4253  C   LYS B 232     -23.612 -22.493  42.162  1.00 62.87           C  
ANISOU 4253  C   LYS B 232     6522   6388  10977   -208   1554    220       C  
ATOM   4254  O   LYS B 232     -23.521 -21.742  43.154  1.00 61.58           O  
ANISOU 4254  O   LYS B 232     6356   6271  10770   -158   1518    271       O  
ATOM   4255  CB  LYS B 232     -25.682 -21.696  40.949  1.00 63.56           C  
ANISOU 4255  CB  LYS B 232     6433   6567  11147   -390   1516     50       C  
ATOM   4256  CG  LYS B 232     -25.328 -21.587  39.469  1.00 62.93           C  
ANISOU 4256  CG  LYS B 232     6298   6527  11085   -408   1444     -6       C  
ATOM   4257  CD  LYS B 232     -25.911 -20.405  38.712  1.00 62.01           C  
ANISOU 4257  CD  LYS B 232     6055   6527  10977   -445   1338    -72       C  
ATOM   4258  CE  LYS B 232     -26.227 -20.783  37.272  1.00 62.48           C  
ANISOU 4258  CE  LYS B 232     6069   6593  11075   -517   1325   -161       C  
ATOM   4259  NZ  LYS B 232     -25.961 -19.709  36.279  1.00 61.47           N  
ANISOU 4259  NZ  LYS B 232     5853   6570  10931   -496   1199   -190       N  
ATOM   4260  N   TYR B 233     -22.566 -23.008  41.511  1.00 63.01           N  
ANISOU 4260  N   TYR B 233     6576   6378  10983   -154   1542    244       N  
ATOM   4261  CA  TYR B 233     -21.151 -22.648  41.788  1.00 62.77           C  
ANISOU 4261  CA  TYR B 233     6565   6389  10894    -31   1471    331       C  
ATOM   4262  C   TYR B 233     -20.333 -22.693  40.496  1.00 62.57           C  
ANISOU 4262  C   TYR B 233     6506   6390  10875    -10   1415    310       C  
ATOM   4263  O   TYR B 233     -20.724 -23.393  39.532  1.00 62.43           O  
ANISOU 4263  O   TYR B 233     6494   6321  10903    -74   1463    243       O  
ATOM   4264  CB  TYR B 233     -20.539 -23.558  42.854  1.00 63.52           C  
ANISOU 4264  CB  TYR B 233     6782   6399  10952     51   1557    424       C  
ATOM   4265  CG  TYR B 233     -20.542 -25.028  42.521  1.00 65.13           C  
ANISOU 4265  CG  TYR B 233     7085   6474  11185     39   1680    418       C  
ATOM   4266  CD1 TYR B 233     -21.476 -25.886  43.086  1.00 66.28           C  
ANISOU 4266  CD1 TYR B 233     7307   6516  11359    -24   1808    403       C  
ATOM   4267  CD2 TYR B 233     -19.606 -25.569  41.653  1.00 65.48           C  
ANISOU 4267  CD2 TYR B 233     7153   6496  11228     90   1675    427       C  
ATOM   4268  CE1 TYR B 233     -21.487 -27.240  42.791  1.00 67.10           C  
ANISOU 4268  CE1 TYR B 233     7515   6491  11489    -41   1928    396       C  
ATOM   4269  CE2 TYR B 233     -19.594 -26.922  41.357  1.00 66.75           C  
ANISOU 4269  CE2 TYR B 233     7418   6530  11413     83   1793    422       C  
ATOM   4270  CZ  TYR B 233     -20.540 -27.760  41.927  1.00 67.38           C  
ANISOU 4270  CZ  TYR B 233     7580   6499  11520     14   1920    405       C  
ATOM   4271  OH  TYR B 233     -20.554 -29.093  41.638  1.00 68.22           O  
ANISOU 4271  OH  TYR B 233     7800   6469  11649      0   2042    396       O  
ATOM   4272  N   LEU B 234     -19.212 -21.959  40.504  1.00 62.94           N  
ANISOU 4272  N   LEU B 234     6519   6516  10876     75   1317    366       N  
ATOM   4273  CA  LEU B 234     -18.232 -21.884  39.386  1.00 61.44           C  
ANISOU 4273  CA  LEU B 234     6295   6366  10683    114   1257    364       C  
ATOM   4274  C   LEU B 234     -17.296 -23.092  39.471  1.00 61.79           C  
ANISOU 4274  C   LEU B 234     6435   6330  10712    197   1334    427       C  
ATOM   4275  O   LEU B 234     -16.710 -23.305  40.558  1.00 61.53           O  
ANISOU 4275  O   LEU B 234     6459   6282  10635    281   1354    514       O  
ATOM   4276  CB  LEU B 234     -17.459 -20.566  39.484  1.00 60.30           C  
ANISOU 4276  CB  LEU B 234     6074   6342  10495    163   1127    402       C  
ATOM   4277  CG  LEU B 234     -16.402 -20.337  38.402  1.00 60.19           C  
ANISOU 4277  CG  LEU B 234     6013   6382  10472    204   1061    408       C  
ATOM   4278  CD1 LEU B 234     -17.030 -20.187  37.024  1.00 59.73           C  
ANISOU 4278  CD1 LEU B 234     5899   6337  10457    123   1043    312       C  
ATOM   4279  CD2 LEU B 234     -15.549 -19.128  38.739  1.00 59.62           C  
ANISOU 4279  CD2 LEU B 234     5880   6420  10352    254    945    460       C  
ATOM   4280  N   VAL B 235     -17.172 -23.834  38.364  1.00 62.27           N  
ANISOU 4280  N   VAL B 235     6514   6340  10802    179   1374    383       N  
ATOM   4281  CA  VAL B 235     -16.283 -25.026  38.223  1.00 63.76           C  
ANISOU 4281  CA  VAL B 235     6799   6446  10981    262   1453    433       C  
ATOM   4282  C   VAL B 235     -14.931 -24.570  37.672  1.00 64.12           C  
ANISOU 4282  C   VAL B 235     6792   6578  10992    356   1369    481       C  
ATOM   4283  O   VAL B 235     -13.909 -24.768  38.362  1.00 64.45           O  
ANISOU 4283  O   VAL B 235     6867   6631  10989    468   1369    576       O  
ATOM   4284  CB  VAL B 235     -16.894 -26.097  37.303  1.00 63.97           C  
ANISOU 4284  CB  VAL B 235     6884   6366  11056    189   1549    355       C  
ATOM   4285  CG1 VAL B 235     -16.047 -27.359  37.299  1.00 64.19           C  
ANISOU 4285  CG1 VAL B 235     7029   6292  11068    281   1645    411       C  
ATOM   4286  CG2 VAL B 235     -18.333 -26.401  37.690  1.00 64.72           C  
ANISOU 4286  CG2 VAL B 235     7003   6395  11191     71   1621    292       C  
ATOM   4287  N   GLN B 236     -14.949 -24.005  36.461  1.00 63.83           N  
ANISOU 4287  N   GLN B 236     6675   6602  10974    309   1302    417       N  
ATOM   4288  CA  GLN B 236     -13.750 -23.520  35.738  1.00 63.11           C  
ANISOU 4288  CA  GLN B 236     6524   6597  10857    379   1225    449       C  
ATOM   4289  C   GLN B 236     -14.063 -22.167  35.089  1.00 61.53           C  
ANISOU 4289  C   GLN B 236     6209   6506  10663    312   1110    395       C  
ATOM   4290  O   GLN B 236     -15.128 -22.044  34.454  1.00 62.46           O  
ANISOU 4290  O   GLN B 236     6303   6609  10817    213   1113    304       O  
ATOM   4291  CB  GLN B 236     -13.326 -24.581  34.721  1.00 64.22           C  
ANISOU 4291  CB  GLN B 236     6721   6665  11012    407   1296    429       C  
ATOM   4292  CG  GLN B 236     -12.177 -24.181  33.805  1.00 64.34           C  
ANISOU 4292  CG  GLN B 236     6675   6764  11007    471   1232    452       C  
ATOM   4293  CD  GLN B 236     -12.037 -25.181  32.673  1.00 65.51           C  
ANISOU 4293  CD  GLN B 236     6882   6834  11172    477   1307    408       C  
ATOM   4294  OE1 GLN B 236     -12.233 -26.384  32.850  1.00 66.56           O  
ANISOU 4294  OE1 GLN B 236     7125   6846  11317    491   1418    408       O  
ATOM   4295  NE2 GLN B 236     -11.718 -24.696  31.480  1.00 65.32           N  
ANISOU 4295  NE2 GLN B 236     6793   6874  11149    463   1251    369       N  
ATOM   4296  N   GLN B 237     -13.164 -21.191  35.261  1.00 60.07           N  
ANISOU 4296  N   GLN B 237     5955   6426  10441    365   1013    449       N  
ATOM   4297  CA  GLN B 237     -13.173 -19.862  34.582  1.00 58.44           C  
ANISOU 4297  CA  GLN B 237     5647   6326  10232    321    901    414       C  
ATOM   4298  C   GLN B 237     -11.832 -19.653  33.867  1.00 58.88           C  
ANISOU 4298  C   GLN B 237     5659   6448  10263    391    855    457       C  
ATOM   4299  O   GLN B 237     -10.789 -19.747  34.544  1.00 59.60           O  
ANISOU 4299  O   GLN B 237     5756   6570  10320    478    846    544       O  
ATOM   4300  CB  GLN B 237     -13.388 -18.740  35.602  1.00 57.31           C  
ANISOU 4300  CB  GLN B 237     5464   6248  10063    308    828    440       C  
ATOM   4301  CG  GLN B 237     -13.675 -17.385  34.972  1.00 55.68           C  
ANISOU 4301  CG  GLN B 237     5170   6129   9856    250    727    393       C  
ATOM   4302  CD  GLN B 237     -15.017 -17.402  34.285  1.00 55.55           C  
ANISOU 4302  CD  GLN B 237     5143   6081   9881    158    748    296       C  
ATOM   4303  OE1 GLN B 237     -16.040 -17.707  34.901  1.00 55.50           O  
ANISOU 4303  OE1 GLN B 237     5167   6024   9896    114    798    267       O  
ATOM   4304  NE2 GLN B 237     -15.015 -17.108  32.994  1.00 54.87           N  
ANISOU 4304  NE2 GLN B 237     5012   6028   9807    129    712    244       N  
ATOM   4305  N   GLU B 238     -11.863 -19.376  32.562  1.00 58.95           N  
ANISOU 4305  N   GLU B 238     5626   6485  10287    354    827    400       N  
ATOM   4306  CA  GLU B 238     -10.686 -18.897  31.784  1.00 59.58           C  
ANISOU 4306  CA  GLU B 238     5647   6647  10344    403    770    434       C  
ATOM   4307  C   GLU B 238     -11.067 -17.609  31.051  1.00 57.19           C  
ANISOU 4307  C   GLU B 238     5264   6421  10041    333    678    382       C  
ATOM   4308  O   GLU B 238     -11.748 -17.708  30.007  1.00 57.39           O  
ANISOU 4308  O   GLU B 238     5289   6426  10090    277    689    304       O  
ATOM   4309  CB  GLU B 238     -10.211 -19.931  30.763  1.00 61.75           C  
ANISOU 4309  CB  GLU B 238     5960   6871  10628    444    840    421       C  
ATOM   4310  CG  GLU B 238      -9.710 -21.234  31.351  1.00 64.40           C  
ANISOU 4310  CG  GLU B 238     6382   7126  10958    529    937    478       C  
ATOM   4311  CD  GLU B 238      -9.376 -22.253  30.262  1.00 66.80           C  
ANISOU 4311  CD  GLU B 238     6737   7368  11272    562   1014    452       C  
ATOM   4312  OE1 GLU B 238      -9.102 -21.832  29.113  1.00 67.72           O  
ANISOU 4312  OE1 GLU B 238     6805   7536  11388    547    976    418       O  
ATOM   4313  OE2 GLU B 238      -9.420 -23.472  30.545  1.00 69.87           O  
ANISOU 4313  OE2 GLU B 238     7224   7654  11669    602   1115    464       O  
ATOM   4314  N   SER B 239     -10.661 -16.460  31.602  1.00 54.72           N  
ANISOU 4314  N   SER B 239     4896   6192   9702    336    592    423       N  
ATOM   4315  CA  SER B 239     -10.819 -15.109  31.005  1.00 53.07           C  
ANISOU 4315  CA  SER B 239     4618   6061   9485    283    500    391       C  
ATOM   4316  C   SER B 239      -9.984 -14.116  31.805  1.00 51.82           C  
ANISOU 4316  C   SER B 239     4417   5982   9289    307    422    460       C  
ATOM   4317  O   SER B 239      -9.693 -14.374  32.971  1.00 51.54           O  
ANISOU 4317  O   SER B 239     4406   5939   9236    346    434    514       O  
ATOM   4318  CB  SER B 239     -12.272 -14.709  30.964  1.00 53.03           C  
ANISOU 4318  CB  SER B 239     4614   6031   9501    202    491    313       C  
ATOM   4319  OG  SER B 239     -12.838 -14.698  32.272  1.00 53.34           O  
ANISOU 4319  OG  SER B 239     4683   6042   9539    194    504    330       O  
ATOM   4320  N   PRO B 240      -9.592 -12.962  31.212  1.00 50.68           N  
ANISOU 4320  N   PRO B 240     4212   5915   9128    281    343    457       N  
ATOM   4321  CA  PRO B 240      -8.788 -11.951  31.910  1.00 50.37           C  
ANISOU 4321  CA  PRO B 240     4131   5952   9052    288    266    516       C  
ATOM   4322  C   PRO B 240      -9.553 -11.147  32.983  1.00 49.66           C  
ANISOU 4322  C   PRO B 240     4057   5860   8948    247    225    506       C  
ATOM   4323  O   PRO B 240      -8.944 -10.688  33.953  1.00 48.79           O  
ANISOU 4323  O   PRO B 240     3940   5791   8805    264    182    559       O  
ATOM   4324  CB  PRO B 240      -8.282 -11.035  30.784  1.00 50.05           C  
ANISOU 4324  CB  PRO B 240     4033   5977   9003    262    209    505       C  
ATOM   4325  CG  PRO B 240      -9.274 -11.215  29.652  1.00 49.98           C  
ANISOU 4325  CG  PRO B 240     4040   5927   9023    222    237    424       C  
ATOM   4326  CD  PRO B 240      -9.874 -12.597  29.816  1.00 50.17           C  
ANISOU 4326  CD  PRO B 240     4120   5866   9075    242    326    399       C  
ATOM   4327  N   PHE B 241     -10.867 -11.000  32.808  1.00 49.54           N  
ANISOU 4327  N   PHE B 241     4063   5802   8957    196    238    437       N  
ATOM   4328  CA  PHE B 241     -11.788 -10.407  33.815  1.00 49.29           C  
ANISOU 4328  CA  PHE B 241     4055   5756   8917    164    220    420       C  
ATOM   4329  C   PHE B 241     -13.074 -11.235  33.900  1.00 49.77           C  
ANISOU 4329  C   PHE B 241     4154   5740   9014    141    294    365       C  
ATOM   4330  O   PHE B 241     -13.338 -12.077  33.017  1.00 49.28           O  
ANISOU 4330  O   PHE B 241     4098   5641   8984    135    347    327       O  
ATOM   4331  CB  PHE B 241     -12.149  -8.970  33.445  1.00 47.66           C  
ANISOU 4331  CB  PHE B 241     3818   5595   8697    114    142    388       C  
ATOM   4332  CG  PHE B 241     -12.840  -8.866  32.112  1.00 47.09           C  
ANISOU 4332  CG  PHE B 241     3724   5517   8650     80    146    320       C  
ATOM   4333  CD1 PHE B 241     -14.221  -8.866  32.032  1.00 47.08           C  
ANISOU 4333  CD1 PHE B 241     3732   5482   8672     44    167    255       C  
ATOM   4334  CD2 PHE B 241     -12.106  -8.828  30.936  1.00 46.96           C  
ANISOU 4334  CD2 PHE B 241     3675   5533   8632     87    131    322       C  
ATOM   4335  CE1 PHE B 241     -14.855  -8.775  30.802  1.00 46.72           C  
ANISOU 4335  CE1 PHE B 241     3663   5443   8645     15    163    192       C  
ATOM   4336  CE2 PHE B 241     -12.741  -8.740  29.709  1.00 46.75           C  
ANISOU 4336  CE2 PHE B 241     3634   5504   8622     59    131    260       C  
ATOM   4337  CZ  PHE B 241     -14.114  -8.724  29.643  1.00 46.63           C  
ANISOU 4337  CZ  PHE B 241     3627   5461   8627     24    145    194       C  
ATOM   4338  N   VAL B 242     -13.855 -10.983  34.946  1.00 50.05           N  
ANISOU 4338  N   VAL B 242     4216   5754   9044    125    300    360       N  
ATOM   4339  CA  VAL B 242     -15.288 -11.373  35.018  1.00 50.98           C  
ANISOU 4339  CA  VAL B 242     4353   5819   9197     83    355    297       C  
ATOM   4340  C   VAL B 242     -16.090 -10.148  35.466  1.00 50.56           C  
ANISOU 4340  C   VAL B 242     4285   5795   9128     50    302    272       C  
ATOM   4341  O   VAL B 242     -15.583  -9.380  36.318  1.00 51.14           O  
ANISOU 4341  O   VAL B 242     4369   5900   9161     68    253    317       O  
ATOM   4342  CB  VAL B 242     -15.524 -12.586  35.940  1.00 52.25           C  
ANISOU 4342  CB  VAL B 242     4574   5908   9370    104    445    320       C  
ATOM   4343  CG1 VAL B 242     -14.966 -13.871  35.336  1.00 52.88           C  
ANISOU 4343  CG1 VAL B 242     4679   5943   9471    134    511    330       C  
ATOM   4344  CG2 VAL B 242     -14.980 -12.366  37.343  1.00 52.58           C  
ANISOU 4344  CG2 VAL B 242     4649   5959   9368    147    431    391       C  
ATOM   4345  N   MET B 243     -17.286  -9.989  34.891  1.00 49.75           N  
ANISOU 4345  N   MET B 243     4160   5686   9055      5    313    201       N  
ATOM   4346  CA  MET B 243     -18.293  -8.969  35.264  1.00 48.86           C  
ANISOU 4346  CA  MET B 243     4035   5595   8934    -20    281    168       C  
ATOM   4347  C   MET B 243     -19.406  -9.650  36.057  1.00 49.54           C  
ANISOU 4347  C   MET B 243     4144   5632   9046    -39    358    144       C  
ATOM   4348  O   MET B 243     -20.013 -10.605  35.526  1.00 49.51           O  
ANISOU 4348  O   MET B 243     4132   5594   9085    -69    419     99       O  
ATOM   4349  CB  MET B 243     -18.887  -8.342  34.006  1.00 48.47           C  
ANISOU 4349  CB  MET B 243     3934   5582   8897    -50    240    106       C  
ATOM   4350  CG  MET B 243     -19.707  -7.118  34.273  1.00 48.42           C  
ANISOU 4350  CG  MET B 243     3914   5608   8874    -60    194     82       C  
ATOM   4351  SD  MET B 243     -20.190  -6.329  32.720  1.00 48.12           S  
ANISOU 4351  SD  MET B 243     3822   5621   8839    -78    137     23       S  
ATOM   4352  CE  MET B 243     -21.119  -4.945  33.377  1.00 48.51           C  
ANISOU 4352  CE  MET B 243     3873   5696   8862    -70     98     11       C  
ATOM   4353  N   MET B 244     -19.639  -9.183  37.282  1.00 50.37           N  
ANISOU 4353  N   MET B 244     4279   5734   9124    -25    357    172       N  
ATOM   4354  CA  MET B 244     -20.715  -9.673  38.175  1.00 52.54           C  
ANISOU 4354  CA  MET B 244     4577   5967   9417    -41    431    155       C  
ATOM   4355  C   MET B 244     -21.762  -8.564  38.330  1.00 54.18           C  
ANISOU 4355  C   MET B 244     4757   6211   9618    -58    400    116       C  
ATOM   4356  O   MET B 244     -21.488  -7.576  39.041  1.00 56.01           O  
ANISOU 4356  O   MET B 244     5012   6464   9804    -32    351    147       O  
ATOM   4357  CB  MET B 244     -20.158 -10.069  39.547  1.00 52.74           C  
ANISOU 4357  CB  MET B 244     4669   5958   9409     -2    465    223       C  
ATOM   4358  CG  MET B 244     -19.098 -11.142  39.486  1.00 53.14           C  
ANISOU 4358  CG  MET B 244     4752   5977   9461     29    497    271       C  
ATOM   4359  SD  MET B 244     -19.591 -12.603  38.543  1.00 54.88           S  
ANISOU 4359  SD  MET B 244     4969   6135   9745     -6    589    223       S  
ATOM   4360  CE  MET B 244     -20.827 -13.308  39.631  1.00 55.28           C  
ANISOU 4360  CE  MET B 244     5063   6121   9819    -34    694    209       C  
ATOM   4361  N   SER B 245     -22.911  -8.720  37.670  1.00 54.28           N  
ANISOU 4361  N   SER B 245     4719   6230   9672    -98    426     48       N  
ATOM   4362  CA  SER B 245     -24.053  -7.776  37.727  1.00 54.66           C  
ANISOU 4362  CA  SER B 245     4730   6318   9719   -107    406      6       C  
ATOM   4363  C   SER B 245     -25.162  -8.368  38.606  1.00 55.39           C  
ANISOU 4363  C   SER B 245     4826   6380   9837   -129    494    -11       C  
ATOM   4364  O   SER B 245     -25.271  -9.613  38.683  1.00 56.99           O  
ANISOU 4364  O   SER B 245     5043   6534  10075   -159    571    -15       O  
ATOM   4365  CB  SER B 245     -24.560  -7.460  36.347  1.00 54.89           C  
ANISOU 4365  CB  SER B 245     4691   6394   9771   -131    366    -54       C  
ATOM   4366  OG  SER B 245     -23.480  -7.334  35.433  1.00 54.65           O  
ANISOU 4366  OG  SER B 245     4660   6377   9727   -120    310    -38       O  
ATOM   4367  N   ALA B 246     -25.949  -7.498  39.239  1.00 54.05           N  
ANISOU 4367  N   ALA B 246     4650   6237   9650   -115    487    -19       N  
ATOM   4368  CA  ALA B 246     -27.143  -7.836  40.048  1.00 54.15           C  
ANISOU 4368  CA  ALA B 246     4654   6235   9684   -134    568    -39       C  
ATOM   4369  C   ALA B 246     -27.994  -6.577  40.188  1.00 53.38           C  
ANISOU 4369  C   ALA B 246     4523   6192   9567   -109    532    -63       C  
ATOM   4370  O   ALA B 246     -27.453  -5.477  40.271  1.00 53.55           O  
ANISOU 4370  O   ALA B 246     4573   6233   9539    -67    459    -39       O  
ATOM   4371  CB  ALA B 246     -26.720  -8.377  41.394  1.00 54.33           C  
ANISOU 4371  CB  ALA B 246     4759   6201   9683   -114    628     19       C  
ATOM   4372  N   PRO B 247     -29.340  -6.677  40.189  1.00 53.02           N  
ANISOU 4372  N   PRO B 247     4416   6173   9556   -135    581   -113       N  
ATOM   4373  CA  PRO B 247     -30.189  -5.506  40.413  1.00 52.14           C  
ANISOU 4373  CA  PRO B 247     4275   6113   9422    -98    556   -130       C  
ATOM   4374  C   PRO B 247     -29.665  -4.638  41.557  1.00 50.76           C  
ANISOU 4374  C   PRO B 247     4187   5915   9182    -41    536    -75       C  
ATOM   4375  O   PRO B 247     -29.336  -5.152  42.627  1.00 50.53           O  
ANISOU 4375  O   PRO B 247     4224   5837   9137    -37    588    -34       O  
ATOM   4376  CB  PRO B 247     -31.548  -6.139  40.735  1.00 52.67           C  
ANISOU 4376  CB  PRO B 247     4282   6194   9537   -137    647   -171       C  
ATOM   4377  CG  PRO B 247     -31.556  -7.396  39.896  1.00 53.26           C  
ANISOU 4377  CG  PRO B 247     4315   6252   9667   -208    680   -207       C  
ATOM   4378  CD  PRO B 247     -30.125  -7.900  39.948  1.00 53.73           C  
ANISOU 4378  CD  PRO B 247     4458   6248   9706   -200    664   -155       C  
ATOM   4379  N   PRO B 248     -29.556  -3.304  41.354  1.00 49.25           N  
ANISOU 4379  N   PRO B 248     4006   5757   8948      4    460    -74       N  
ATOM   4380  CA  PRO B 248     -28.897  -2.416  42.308  1.00 49.02           C  
ANISOU 4380  CA  PRO B 248     4069   5703   8852     50    427    -26       C  
ATOM   4381  C   PRO B 248     -29.330  -2.713  43.740  1.00 49.40           C  
ANISOU 4381  C   PRO B 248     4168   5719   8883     63    506     -2       C  
ATOM   4382  O   PRO B 248     -30.502  -2.814  43.958  1.00 51.02           O  
ANISOU 4382  O   PRO B 248     4327   5943   9113     62    567    -32       O  
ATOM   4383  CB  PRO B 248     -29.364  -1.014  41.888  1.00 48.89           C  
ANISOU 4383  CB  PRO B 248     4039   5729   8806     94    368    -49       C  
ATOM   4384  CG  PRO B 248     -29.582  -1.149  40.395  1.00 48.90           C  
ANISOU 4384  CG  PRO B 248     3954   5775   8848     71    331    -92       C  
ATOM   4385  CD  PRO B 248     -30.066  -2.571  40.188  1.00 49.18           C  
ANISOU 4385  CD  PRO B 248     3927   5808   8948     15    403   -119       C  
ATOM   4386  N   ALA B 249     -28.374  -2.852  44.651  1.00 49.78           N  
ANISOU 4386  N   ALA B 249     4304   5723   8887     75    504     50       N  
ATOM   4387  CA  ALA B 249     -28.616  -3.192  46.069  1.00 50.72           C  
ANISOU 4387  CA  ALA B 249     4487   5805   8977     91    577     81       C  
ATOM   4388  C   ALA B 249     -27.439  -2.704  46.916  1.00 51.06           C  
ANISOU 4388  C   ALA B 249     4632   5823   8945    121    526    136       C  
ATOM   4389  O   ALA B 249     -26.305  -2.709  46.404  1.00 49.95           O  
ANISOU 4389  O   ALA B 249     4499   5683   8794    112    458    157       O  
ATOM   4390  CB  ALA B 249     -28.823  -4.681  46.202  1.00 50.84           C  
ANISOU 4390  CB  ALA B 249     4483   5787   9043     50    667     86       C  
ATOM   4391  N   GLN B 250     -27.719  -2.278  48.151  1.00 53.05           N  
ANISOU 4391  N   GLN B 250     4955   6057   9143    156    556    155       N  
ATOM   4392  CA  GLN B 250     -26.702  -1.895  49.165  1.00 54.76           C  
ANISOU 4392  CA  GLN B 250     5275   6250   9280    182    516    205       C  
ATOM   4393  C   GLN B 250     -25.654  -3.011  49.258  1.00 55.43           C  
ANISOU 4393  C   GLN B 250     5377   6314   9370    165    519    250       C  
ATOM   4394  O   GLN B 250     -26.042  -4.175  49.450  1.00 56.06           O  
ANISOU 4394  O   GLN B 250     5442   6367   9489    152    605    257       O  
ATOM   4395  CB  GLN B 250     -27.371  -1.629  50.518  1.00 56.23           C  
ANISOU 4395  CB  GLN B 250     5532   6416   9416    218    578    216       C  
ATOM   4396  CG  GLN B 250     -26.835  -0.399  51.232  1.00 56.71           C  
ANISOU 4396  CG  GLN B 250     5686   6473   9386    251    510    231       C  
ATOM   4397  CD  GLN B 250     -27.084   0.876  50.465  1.00 57.65           C  
ANISOU 4397  CD  GLN B 250     5785   6617   9502    261    445    192       C  
ATOM   4398  OE1 GLN B 250     -27.873   0.929  49.513  1.00 58.39           O  
ANISOU 4398  OE1 GLN B 250     5793   6736   9654    255    458    152       O  
ATOM   4399  NE2 GLN B 250     -26.402   1.931  50.889  1.00 58.12           N  
ANISOU 4399  NE2 GLN B 250     5929   6668   9487    275    373    203       N  
ATOM   4400  N   TYR B 251     -24.377  -2.659  49.108  1.00 56.32           N  
ANISOU 4400  N   TYR B 251     5516   6436   9444    167    431    279       N  
ATOM   4401  CA  TYR B 251     -23.236  -3.607  49.101  1.00 57.02           C  
ANISOU 4401  CA  TYR B 251     5614   6517   9533    162    420    326       C  
ATOM   4402  C   TYR B 251     -21.967  -2.865  49.530  1.00 57.87           C  
ANISOU 4402  C   TYR B 251     5775   6644   9565    175    325    363       C  
ATOM   4403  O   TYR B 251     -21.765  -1.724  49.084  1.00 59.06           O  
ANISOU 4403  O   TYR B 251     5922   6820   9697    164    249    341       O  
ATOM   4404  CB  TYR B 251     -23.093  -4.237  47.717  1.00 56.86           C  
ANISOU 4404  CB  TYR B 251     5509   6507   9587    130    416    304       C  
ATOM   4405  CG  TYR B 251     -22.067  -5.337  47.619  1.00 58.16           C  
ANISOU 4405  CG  TYR B 251     5678   6658   9761    132    423    349       C  
ATOM   4406  CD1 TYR B 251     -21.821  -6.196  48.681  1.00 59.33           C  
ANISOU 4406  CD1 TYR B 251     5888   6772   9882    159    481    398       C  
ATOM   4407  CD2 TYR B 251     -21.341  -5.528  46.455  1.00 58.75           C  
ANISOU 4407  CD2 TYR B 251     5699   6754   9869    115    377    345       C  
ATOM   4408  CE1 TYR B 251     -20.881  -7.210  48.587  1.00 60.10           C  
ANISOU 4408  CE1 TYR B 251     5992   6856   9985    174    491    443       C  
ATOM   4409  CE2 TYR B 251     -20.404  -6.542  46.341  1.00 58.69           C  
ANISOU 4409  CE2 TYR B 251     5694   6734   9869    127    389    387       C  
ATOM   4410  CZ  TYR B 251     -20.172  -7.385  47.412  1.00 59.62           C  
ANISOU 4410  CZ  TYR B 251     5874   6818   9960    159    445    437       C  
ATOM   4411  OH  TYR B 251     -19.258  -8.391  47.319  1.00 60.38           O  
ANISOU 4411  OH  TYR B 251     5978   6901  10061    182    461    482       O  
ATOM   4412  N   GLU B 252     -21.161  -3.495  50.387  1.00 58.34           N  
ANISOU 4412  N   GLU B 252     5887   6695   9583    197    330    418       N  
ATOM   4413  CA  GLU B 252     -19.925  -2.913  50.979  1.00 58.19           C  
ANISOU 4413  CA  GLU B 252     5919   6705   9485    208    241    457       C  
ATOM   4414  C   GLU B 252     -18.740  -3.393  50.143  1.00 55.85           C  
ANISOU 4414  C   GLU B 252     5567   6438   9213    197    190    484       C  
ATOM   4415  O   GLU B 252     -18.572  -4.618  50.025  1.00 55.71           O  
ANISOU 4415  O   GLU B 252     5532   6404   9230    213    245    511       O  
ATOM   4416  CB  GLU B 252     -19.822  -3.316  52.448  1.00 61.02           C  
ANISOU 4416  CB  GLU B 252     6364   7045   9776    247    278    502       C  
ATOM   4417  CG  GLU B 252     -18.534  -2.904  53.141  1.00 62.64           C  
ANISOU 4417  CG  GLU B 252     6617   7286   9895    260    188    545       C  
ATOM   4418  CD  GLU B 252     -18.643  -2.938  54.664  1.00 65.22           C  
ANISOU 4418  CD  GLU B 252     7044   7598  10137    299    215    575       C  
ATOM   4419  OE1 GLU B 252     -19.636  -2.365  55.213  1.00 66.87           O  
ANISOU 4419  OE1 GLU B 252     7301   7779  10324    304    255    545       O  
ATOM   4420  OE2 GLU B 252     -17.753  -3.554  55.313  1.00 65.92           O  
ANISOU 4420  OE2 GLU B 252     7163   7704  10178    330    199    632       O  
ATOM   4421  N   LEU B 253     -18.003  -2.454  49.542  1.00 53.67           N  
ANISOU 4421  N   LEU B 253     5267   6202   8921    171     95    475       N  
ATOM   4422  CA  LEU B 253     -16.800  -2.726  48.706  1.00 52.06           C  
ANISOU 4422  CA  LEU B 253     5006   6038   8736    158     38    500       C  
ATOM   4423  C   LEU B 253     -15.566  -2.618  49.606  1.00 51.26           C  
ANISOU 4423  C   LEU B 253     4943   5975   8558    174    -24    554       C  
ATOM   4424  O   LEU B 253     -15.341  -1.528  50.214  1.00 50.98           O  
ANISOU 4424  O   LEU B 253     4955   5957   8457    157    -88    547       O  
ATOM   4425  CB  LEU B 253     -16.714  -1.738  47.536  1.00 50.70           C  
ANISOU 4425  CB  LEU B 253     4786   5890   8588    117    -23    461       C  
ATOM   4426  CG  LEU B 253     -17.791  -1.869  46.462  1.00 50.17           C  
ANISOU 4426  CG  LEU B 253     4665   5800   8594    104     24    409       C  
ATOM   4427  CD1 LEU B 253     -17.613  -0.822  45.380  1.00 49.40           C  
ANISOU 4427  CD1 LEU B 253     4533   5728   8507     71    -42    378       C  
ATOM   4428  CD2 LEU B 253     -17.782  -3.250  45.836  1.00 50.51           C  
ANISOU 4428  CD2 LEU B 253     4657   5831   8701    111     86    417       C  
ATOM   4429  N   LYS B 254     -14.821  -3.718  49.708  1.00 50.24           N  
ANISOU 4429  N   LYS B 254     4796   5859   8434    207     -5    604       N  
ATOM   4430  CA  LYS B 254     -13.561  -3.801  50.484  1.00 50.24           C  
ANISOU 4430  CA  LYS B 254     4815   5910   8364    232    -66    663       C  
ATOM   4431  C   LYS B 254     -12.408  -3.587  49.500  1.00 48.04           C  
ANISOU 4431  C   LYS B 254     4456   5692   8103    207   -140    675       C  
ATOM   4432  O   LYS B 254     -12.422  -4.199  48.409  1.00 46.45           O  
ANISOU 4432  O   LYS B 254     4194   5481   7972    207   -106    668       O  
ATOM   4433  CB  LYS B 254     -13.400  -5.133  51.229  1.00 51.64           C  
ANISOU 4433  CB  LYS B 254     5023   6069   8529    296      0    719       C  
ATOM   4434  CG  LYS B 254     -14.662  -5.929  51.535  1.00 52.81           C  
ANISOU 4434  CG  LYS B 254     5212   6138   8712    317    118    705       C  
ATOM   4435  CD  LYS B 254     -14.384  -7.430  51.641  1.00 53.99           C  
ANISOU 4435  CD  LYS B 254     5368   6261   8883    371    193    756       C  
ATOM   4436  CE  LYS B 254     -15.618  -8.307  51.559  1.00 54.37           C  
ANISOU 4436  CE  LYS B 254     5438   6228   8991    371    317    733       C  
ATOM   4437  NZ  LYS B 254     -16.096  -8.715  52.905  1.00 55.37           N  
ANISOU 4437  NZ  LYS B 254     5655   6315   9066    410    383    764       N  
ATOM   4438  N   HIS B 255     -11.473  -2.718  49.881  1.00 47.26           N  
ANISOU 4438  N   HIS B 255     4361   5653   7941    182   -236    690       N  
ATOM   4439  CA  HIS B 255     -10.260  -2.348  49.108  1.00 47.03           C  
ANISOU 4439  CA  HIS B 255     4257   5694   7916    149   -316    705       C  
ATOM   4440  C   HIS B 255      -9.536  -3.604  48.601  1.00 46.88           C  
ANISOU 4440  C   HIS B 255     4174   5701   7936    199   -284    753       C  
ATOM   4441  O   HIS B 255      -9.293  -4.529  49.404  1.00 47.14           O  
ANISOU 4441  O   HIS B 255     4233   5735   7941    262   -252    802       O  
ATOM   4442  CB  HIS B 255      -9.368  -1.443  49.968  1.00 47.15           C  
ANISOU 4442  CB  HIS B 255     4298   5771   7844    120   -415    721       C  
ATOM   4443  CG  HIS B 255      -8.029  -1.206  49.377  1.00 47.10           C  
ANISOU 4443  CG  HIS B 255     4210   5848   7835     89   -492    747       C  
ATOM   4444  ND1 HIS B 255      -6.875  -1.432  50.089  1.00 47.76           N  
ANISOU 4444  ND1 HIS B 255     4273   6013   7860    109   -551    800       N  
ATOM   4445  CD2 HIS B 255      -7.662  -0.799  48.143  1.00 46.75           C  
ANISOU 4445  CD2 HIS B 255     4096   5826   7840     43   -517    730       C  
ATOM   4446  CE1 HIS B 255      -5.839  -1.166  49.319  1.00 48.14           C  
ANISOU 4446  CE1 HIS B 255     4235   6133   7923     73   -608    814       C  
ATOM   4447  NE2 HIS B 255      -6.297  -0.773  48.118  1.00 47.36           N  
ANISOU 4447  NE2 HIS B 255     4109   5995   7890     31   -586    772       N  
ATOM   4448  N   GLY B 256      -9.250  -3.639  47.296  1.00 46.56           N  
ANISOU 4448  N   GLY B 256     4060   5674   7955    176   -287    740       N  
ATOM   4449  CA  GLY B 256      -8.341  -4.605  46.653  1.00 46.74           C  
ANISOU 4449  CA  GLY B 256     4013   5735   8009    217   -273    784       C  
ATOM   4450  C   GLY B 256      -8.918  -6.008  46.563  1.00 46.55           C  
ANISOU 4450  C   GLY B 256     4008   5647   8031    278   -167    796       C  
ATOM   4451  O   GLY B 256      -8.131  -6.936  46.333  1.00 47.98           O  
ANISOU 4451  O   GLY B 256     4154   5854   8223    331   -147    844       O  
ATOM   4452  N   THR B 257     -10.236  -6.167  46.720  1.00 45.73           N  
ANISOU 4452  N   THR B 257     3957   5464   7954    271    -98    755       N  
ATOM   4453  CA  THR B 257     -10.995  -7.439  46.522  1.00 44.96           C  
ANISOU 4453  CA  THR B 257     3880   5293   7909    308     12    751       C  
ATOM   4454  C   THR B 257     -11.707  -7.423  45.165  1.00 43.43           C  
ANISOU 4454  C   THR B 257     3643   5066   7791    265     44    691       C  
ATOM   4455  O   THR B 257     -12.445  -8.360  44.884  1.00 43.05           O  
ANISOU 4455  O   THR B 257     3609   4955   7791    277    132    673       O  
ATOM   4456  CB  THR B 257     -12.029  -7.647  47.635  1.00 45.27           C  
ANISOU 4456  CB  THR B 257     4001   5271   7926    322     72    744       C  
ATOM   4457  OG1 THR B 257     -12.991  -6.596  47.528  1.00 44.78           O  
ANISOU 4457  OG1 THR B 257     3949   5193   7871    266     56    683       O  
ATOM   4458  CG2 THR B 257     -11.403  -7.653  49.013  1.00 46.15           C  
ANISOU 4458  CG2 THR B 257     4165   5415   7954    367     41    802       C  
ATOM   4459  N   PHE B 258     -11.485  -6.377  44.372  1.00 42.56           N  
ANISOU 4459  N   PHE B 258     3487   4996   7687    216    -24    660       N  
ATOM   4460  CA  PHE B 258     -12.121  -6.147  43.053  1.00 41.80           C  
ANISOU 4460  CA  PHE B 258     3350   4881   7651    175    -11    601       C  
ATOM   4461  C   PHE B 258     -11.273  -5.127  42.297  1.00 41.21           C  
ANISOU 4461  C   PHE B 258     3224   4869   7564    138    -97    600       C  
ATOM   4462  O   PHE B 258     -10.432  -4.475  42.936  1.00 41.29           O  
ANISOU 4462  O   PHE B 258     3238   4930   7520    131   -166    633       O  
ATOM   4463  CB  PHE B 258     -13.573  -5.684  43.226  1.00 41.52           C  
ANISOU 4463  CB  PHE B 258     3348   4797   7630    145     20    543       C  
ATOM   4464  CG  PHE B 258     -13.727  -4.285  43.771  1.00 41.30           C  
ANISOU 4464  CG  PHE B 258     3348   4789   7552    115    -46    528       C  
ATOM   4465  CD1 PHE B 258     -14.035  -3.225  42.931  1.00 40.66           C  
ANISOU 4465  CD1 PHE B 258     3245   4720   7483     73    -90    483       C  
ATOM   4466  CD2 PHE B 258     -13.533  -4.022  45.118  1.00 41.60           C  
ANISOU 4466  CD2 PHE B 258     3445   4832   7527    132    -65    558       C  
ATOM   4467  CE1 PHE B 258     -14.143  -1.933  43.426  1.00 40.39           C  
ANISOU 4467  CE1 PHE B 258     3250   4696   7401     48   -147    470       C  
ATOM   4468  CE2 PHE B 258     -13.639  -2.728  45.609  1.00 41.55           C  
ANISOU 4468  CE2 PHE B 258     3476   4840   7471    102   -126    541       C  
ATOM   4469  CZ  PHE B 258     -13.948  -1.684  44.763  1.00 40.83           C  
ANISOU 4469  CZ  PHE B 258     3366   4753   7395     60   -165    496       C  
ATOM   4470  N   THR B 259     -11.486  -5.026  40.986  1.00 40.86           N  
ANISOU 4470  N   THR B 259     3135   4822   7566    113    -92    563       N  
ATOM   4471  CA  THR B 259     -10.849  -4.027  40.092  1.00 41.02           C  
ANISOU 4471  CA  THR B 259     3111   4892   7581     72   -162    555       C  
ATOM   4472  C   THR B 259     -11.621  -2.706  40.208  1.00 41.21           C  
ANISOU 4472  C   THR B 259     3168   4903   7585     27   -202    511       C  
ATOM   4473  O   THR B 259     -11.118  -1.765  40.864  1.00 41.83           O  
ANISOU 4473  O   THR B 259     3270   5010   7613      3   -265    527       O  
ATOM   4474  CB  THR B 259     -10.822  -4.529  38.645  1.00 40.66           C  
ANISOU 4474  CB  THR B 259     3015   4844   7589     72   -133    533       C  
ATOM   4475  OG1 THR B 259     -10.109  -5.765  38.614  1.00 41.18           O  
ANISOU 4475  OG1 THR B 259     3061   4915   7668    122    -90    576       O  
ATOM   4476  CG2 THR B 259     -10.208  -3.528  37.693  1.00 40.34           C  
ANISOU 4476  CG2 THR B 259     2933   4850   7541     31   -195    527       C  
ATOM   4477  N   CYS B 260     -12.808  -2.653  39.603  1.00 40.77           N  
ANISOU 4477  N   CYS B 260     3115   4806   7567     18   -165    456       N  
ATOM   4478  CA  CYS B 260     -13.712  -1.479  39.605  1.00 40.61           C  
ANISOU 4478  CA  CYS B 260     3126   4769   7533     -9   -190    411       C  
ATOM   4479  C   CYS B 260     -15.159  -1.974  39.711  1.00 41.99           C  
ANISOU 4479  C   CYS B 260     3314   4896   7742      5   -121    368       C  
ATOM   4480  O   CYS B 260     -15.407  -3.190  39.513  1.00 42.80           O  
ANISOU 4480  O   CYS B 260     3396   4978   7885     23    -57    365       O  
ATOM   4481  CB  CYS B 260     -13.510  -0.623  38.363  1.00 39.28           C  
ANISOU 4481  CB  CYS B 260     2928   4623   7373    -41   -234    390       C  
ATOM   4482  SG  CYS B 260     -13.878  -1.505  36.827  1.00 37.83           S  
ANISOU 4482  SG  CYS B 260     2683   4435   7253    -32   -187    358       S  
ATOM   4483  N   ALA B 261     -16.068  -1.054  40.033  1.00 42.80           N  
ANISOU 4483  N   ALA B 261     3452   4983   7828     -2   -130    334       N  
ATOM   4484  CA  ALA B 261     -17.510  -1.298  40.226  1.00 43.19           C  
ANISOU 4484  CA  ALA B 261     3508   4998   7903      9    -70    291       C  
ATOM   4485  C   ALA B 261     -18.297  -0.214  39.494  1.00 44.07           C  
ANISOU 4485  C   ALA B 261     3612   5115   8016      0    -98    245       C  
ATOM   4486  O   ALA B 261     -17.685   0.751  38.973  1.00 44.69           O  
ANISOU 4486  O   ALA B 261     3697   5214   8070    -16   -162    251       O  
ATOM   4487  CB  ALA B 261     -17.835  -1.320  41.699  1.00 43.38           C  
ANISOU 4487  CB  ALA B 261     3592   4998   7892     28    -45    308       C  
ATOM   4488  N   SER B 262     -19.616  -0.394  39.441  1.00 44.86           N  
ANISOU 4488  N   SER B 262     3698   5200   8146     10    -49    202       N  
ATOM   4489  CA  SER B 262     -20.593   0.591  38.928  1.00 44.76           C  
ANISOU 4489  CA  SER B 262     3680   5195   8131     17    -66    158       C  
ATOM   4490  C   SER B 262     -21.685   0.767  39.991  1.00 44.84           C  
ANISOU 4490  C   SER B 262     3723   5184   8130     41    -21    142       C  
ATOM   4491  O   SER B 262     -22.332  -0.237  40.346  1.00 44.48           O  
ANISOU 4491  O   SER B 262     3655   5127   8119     42     46    132       O  
ATOM   4492  CB  SER B 262     -21.117   0.153  37.585  1.00 45.15           C  
ANISOU 4492  CB  SER B 262     3658   5264   8229     10    -53    117       C  
ATOM   4493  OG  SER B 262     -22.227  -0.715  37.735  1.00 46.83           O  
ANISOU 4493  OG  SER B 262     3837   5470   8486     12     15     84       O  
ATOM   4494  N   GLU B 263     -21.814   1.983  40.530  1.00 45.56           N  
ANISOU 4494  N   GLU B 263     3872   5267   8170     56    -55    143       N  
ATOM   4495  CA  GLU B 263     -22.887   2.397  41.472  1.00 46.74           C  
ANISOU 4495  CA  GLU B 263     4059   5399   8299     87    -16    126       C  
ATOM   4496  C   GLU B 263     -24.081   2.936  40.678  1.00 45.96           C  
ANISOU 4496  C   GLU B 263     3918   5320   8222    111     -9     79       C  
ATOM   4497  O   GLU B 263     -23.851   3.529  39.616  1.00 44.77           O  
ANISOU 4497  O   GLU B 263     3749   5187   8071    108    -58     68       O  
ATOM   4498  CB  GLU B 263     -22.375   3.475  42.426  1.00 48.00           C  
ANISOU 4498  CB  GLU B 263     4314   5536   8385     95    -57    150       C  
ATOM   4499  CG  GLU B 263     -23.338   3.767  43.562  1.00 49.63           C  
ANISOU 4499  CG  GLU B 263     4571   5720   8564    130     -9    139       C  
ATOM   4500  CD  GLU B 263     -23.184   5.158  44.152  1.00 51.27           C  
ANISOU 4500  CD  GLU B 263     4874   5904   8700    145    -52    141       C  
ATOM   4501  OE1 GLU B 263     -23.467   6.150  43.430  1.00 52.41           O  
ANISOU 4501  OE1 GLU B 263     5026   6050   8836    158    -85    119       O  
ATOM   4502  OE2 GLU B 263     -22.783   5.252  45.337  1.00 52.17           O  
ANISOU 4502  OE2 GLU B 263     5062   5997   8763    145    -52    165       O  
ATOM   4503  N   TYR B 264     -25.300   2.736  41.184  1.00 46.58           N  
ANISOU 4503  N   TYR B 264     3980   5399   8316    137     52     54       N  
ATOM   4504  CA  TYR B 264     -26.563   3.250  40.584  1.00 46.65           C  
ANISOU 4504  CA  TYR B 264     3941   5439   8342    170     63      9       C  
ATOM   4505  C   TYR B 264     -27.528   3.694  41.684  1.00 46.90           C  
ANISOU 4505  C   TYR B 264     4009   5459   8349    213    112      2       C  
ATOM   4506  O   TYR B 264     -28.105   2.819  42.345  1.00 47.75           O  
ANISOU 4506  O   TYR B 264     4093   5564   8484    207    183     -1       O  
ATOM   4507  CB  TYR B 264     -27.214   2.187  39.697  1.00 46.50           C  
ANISOU 4507  CB  TYR B 264     3817   5456   8393    148     99    -25       C  
ATOM   4508  CG  TYR B 264     -28.227   2.720  38.719  1.00 46.33           C  
ANISOU 4508  CG  TYR B 264     3731   5483   8387    176     85    -70       C  
ATOM   4509  CD1 TYR B 264     -29.570   2.786  39.036  1.00 46.53           C  
ANISOU 4509  CD1 TYR B 264     3713   5537   8427    208    134   -101       C  
ATOM   4510  CD2 TYR B 264     -27.832   3.157  37.463  1.00 46.24           C  
ANISOU 4510  CD2 TYR B 264     3700   5496   8373    176     22    -79       C  
ATOM   4511  CE1 TYR B 264     -30.499   3.273  38.129  1.00 47.10           C  
ANISOU 4511  CE1 TYR B 264     3718   5665   8510    241    116   -140       C  
ATOM   4512  CE2 TYR B 264     -28.748   3.647  36.546  1.00 46.25           C  
ANISOU 4512  CE2 TYR B 264     3644   5547   8382    210      4   -116       C  
ATOM   4513  CZ  TYR B 264     -30.090   3.712  36.881  1.00 46.79           C  
ANISOU 4513  CZ  TYR B 264     3664   5649   8464    245     48   -147       C  
ATOM   4514  OH  TYR B 264     -31.016   4.199  35.996  1.00 46.19           O  
ANISOU 4514  OH  TYR B 264     3524   5633   8391    286     27   -183       O  
ATOM   4515  N   THR B 265     -27.680   5.009  41.860  1.00 47.22           N  
ANISOU 4515  N   THR B 265     4113   5488   8337    256     79      2       N  
ATOM   4516  CA  THR B 265     -28.736   5.646  42.689  1.00 47.91           C  
ANISOU 4516  CA  THR B 265     4234   5570   8396    313    123    -10       C  
ATOM   4517  C   THR B 265     -29.872   6.046  41.756  1.00 47.79           C  
ANISOU 4517  C   THR B 265     4143   5607   8409    357    127    -49       C  
ATOM   4518  O   THR B 265     -29.606   6.118  40.553  1.00 47.51           O  
ANISOU 4518  O   THR B 265     4063   5596   8392    344     78    -60       O  
ATOM   4519  CB  THR B 265     -28.199   6.853  43.463  1.00 48.65           C  
ANISOU 4519  CB  THR B 265     4455   5616   8411    338     88     10       C  
ATOM   4520  OG1 THR B 265     -26.962   6.452  44.042  1.00 49.43           O  
ANISOU 4520  OG1 THR B 265     4607   5686   8488    287     63     46       O  
ATOM   4521  CG2 THR B 265     -29.125   7.331  44.563  1.00 49.84           C  
ANISOU 4521  CG2 THR B 265     4658   5750   8526    395    145      3       C  
ATOM   4522  N   GLY B 266     -31.072   6.289  42.293  1.00 47.94           N  
ANISOU 4522  N   GLY B 266     4146   5644   8426    411    183    -68       N  
ATOM   4523  CA  GLY B 266     -32.260   6.704  41.521  1.00 48.26           C  
ANISOU 4523  CA  GLY B 266     4105   5743   8486    465    189   -104       C  
ATOM   4524  C   GLY B 266     -33.003   5.497  40.982  1.00 48.19           C  
ANISOU 4524  C   GLY B 266     3961   5796   8553    428    230   -136       C  
ATOM   4525  O   GLY B 266     -32.420   4.400  41.025  1.00 47.31           O  
ANISOU 4525  O   GLY B 266     3830   5668   8475    358    245   -129       O  
ATOM   4526  N   ASN B 267     -34.241   5.680  40.497  1.00 48.95           N  
ANISOU 4526  N   ASN B 267     3965   5961   8672    473    250   -172       N  
ATOM   4527  CA  ASN B 267     -35.187   4.550  40.309  1.00 49.60           C  
ANISOU 4527  CA  ASN B 267     3918   6104   8823    435    308   -207       C  
ATOM   4528  C   ASN B 267     -35.695   4.432  38.874  1.00 49.89           C  
ANISOU 4528  C   ASN B 267     3840   6220   8895    432    266   -248       C  
ATOM   4529  O   ASN B 267     -35.698   3.282  38.362  1.00 50.32           O  
ANISOU 4529  O   ASN B 267     3817   6296   9004    357    279   -273       O  
ATOM   4530  CB  ASN B 267     -36.344   4.620  41.296  1.00 50.10           C  
ANISOU 4530  CB  ASN B 267     3956   6191   8888    478    391   -215       C  
ATOM   4531  CG  ASN B 267     -36.016   3.786  42.512  1.00 50.11           C  
ANISOU 4531  CG  ASN B 267     4009   6135   8896    430    460   -190       C  
ATOM   4532  OD1 ASN B 267     -36.037   4.264  43.640  1.00 50.80           O  
ANISOU 4532  OD1 ASN B 267     4182   6181   8937    470    496   -165       O  
ATOM   4533  ND2 ASN B 267     -35.701   2.525  42.277  1.00 50.18           N  
ANISOU 4533  ND2 ASN B 267     3972   6137   8957    345    481   -197       N  
ATOM   4534  N   TYR B 268     -36.158   5.528  38.275  1.00 49.65           N  
ANISOU 4534  N   TYR B 268     3802   6230   8831    512    221   -257       N  
ATOM   4535  CA  TYR B 268     -36.880   5.471  36.980  1.00 49.78           C  
ANISOU 4535  CA  TYR B 268     3700   6340   8874    526    184   -299       C  
ATOM   4536  C   TYR B 268     -36.045   6.215  35.946  1.00 49.19           C  
ANISOU 4536  C   TYR B 268     3681   6249   8760    547     96   -285       C  
ATOM   4537  O   TYR B 268     -35.127   5.583  35.421  1.00 48.48           O  
ANISOU 4537  O   TYR B 268     3599   6131   8687    476     67   -281       O  
ATOM   4538  CB  TYR B 268     -38.320   5.939  37.181  1.00 50.85           C  
ANISOU 4538  CB  TYR B 268     3755   6555   9009    605    221   -321       C  
ATOM   4539  CG  TYR B 268     -39.049   5.127  38.221  1.00 51.31           C  
ANISOU 4539  CG  TYR B 268     3761   6625   9109    570    316   -332       C  
ATOM   4540  CD1 TYR B 268     -39.338   3.789  38.007  1.00 51.53           C  
ANISOU 4540  CD1 TYR B 268     3687   6686   9204    474    354   -366       C  
ATOM   4541  CD2 TYR B 268     -39.414   5.682  39.433  1.00 51.62           C  
ANISOU 4541  CD2 TYR B 268     3862   6635   9117    630    374   -308       C  
ATOM   4542  CE1 TYR B 268     -40.000   3.032  38.961  1.00 52.34           C  
ANISOU 4542  CE1 TYR B 268     3746   6793   9344    436    448   -373       C  
ATOM   4543  CE2 TYR B 268     -40.064   4.937  40.403  1.00 52.39           C  
ANISOU 4543  CE2 TYR B 268     3916   6740   9248    598    468   -314       C  
ATOM   4544  CZ  TYR B 268     -40.369   3.610  40.163  1.00 52.71           C  
ANISOU 4544  CZ  TYR B 268     3851   6815   9359    500    507   -346       C  
ATOM   4545  OH  TYR B 268     -41.032   2.885  41.110  1.00 53.40           O  
ANISOU 4545  OH  TYR B 268     3900   6909   9481    465    606   -350       O  
ATOM   4546  N   GLN B 269     -36.324   7.495  35.699  1.00 49.44           N  
ANISOU 4546  N   GLN B 269     3754   6290   8739    643     61   -273       N  
ATOM   4547  CA  GLN B 269     -35.536   8.343  34.760  1.00 48.58           C  
ANISOU 4547  CA  GLN B 269     3715   6157   8585    670    -16   -254       C  
ATOM   4548  C   GLN B 269     -34.624   9.272  35.569  1.00 47.11           C  
ANISOU 4548  C   GLN B 269     3689   5869   8342    688    -24   -208       C  
ATOM   4549  O   GLN B 269     -33.993  10.157  34.954  1.00 46.07           O  
ANISOU 4549  O   GLN B 269     3634   5704   8165    714    -79   -187       O  
ATOM   4550  CB  GLN B 269     -36.464   9.115  33.820  1.00 50.05           C  
ANISOU 4550  CB  GLN B 269     3844   6423   8748    764    -51   -273       C  
ATOM   4551  CG  GLN B 269     -37.424  10.046  34.540  1.00 51.33           C  
ANISOU 4551  CG  GLN B 269     4027   6598   8876    872    -15   -266       C  
ATOM   4552  CD  GLN B 269     -38.764   9.393  34.778  1.00 53.14           C  
ANISOU 4552  CD  GLN B 269     4111   6925   9152    884     37   -304       C  
ATOM   4553  OE1 GLN B 269     -39.010   8.790  35.823  1.00 54.49           O  
ANISOU 4553  OE1 GLN B 269     4268   7081   9353    846    106   -307       O  
ATOM   4554  NE2 GLN B 269     -39.658   9.505  33.802  1.00 54.28           N  
ANISOU 4554  NE2 GLN B 269     4143   7177   9303    937      7   -335       N  
ATOM   4555  N   CYS B 270     -34.571   9.081  36.894  1.00 46.52           N  
ANISOU 4555  N   CYS B 270     3663   5745   8264    672     31   -193       N  
ATOM   4556  CA  CYS B 270     -33.765   9.883  37.857  1.00 46.00           C  
ANISOU 4556  CA  CYS B 270     3750   5585   8141    681     29   -155       C  
ATOM   4557  C   CYS B 270     -32.495   9.111  38.251  1.00 44.33           C  
ANISOU 4557  C   CYS B 270     3580   5319   7943    582     21   -133       C  
ATOM   4558  O   CYS B 270     -31.890   9.454  39.288  1.00 44.03           O  
ANISOU 4558  O   CYS B 270     3649   5213   7866    572     30   -106       O  
ATOM   4559  CB  CYS B 270     -34.586  10.218  39.100  1.00 47.20           C  
ANISOU 4559  CB  CYS B 270     3934   5726   8272    740     95   -154       C  
ATOM   4560  SG  CYS B 270     -35.787  11.491  38.832  1.00 47.61           S  
ANISOU 4560  SG  CYS B 270     3987   5817   8283    878    100   -164       S  
ATOM   4561  N   GLY B 271     -32.117   8.100  37.465  1.00 42.80           N  
ANISOU 4561  N   GLY B 271     3307   5156   7799    515      4   -145       N  
ATOM   4562  CA  GLY B 271     -31.039   7.158  37.818  1.00 41.83           C  
ANISOU 4562  CA  GLY B 271     3201   4992   7697    428      8   -125       C  
ATOM   4563  C   GLY B 271     -29.672   7.729  37.490  1.00 40.86           C  
ANISOU 4563  C   GLY B 271     3167   4821   7537    401    -55    -92       C  
ATOM   4564  O   GLY B 271     -29.527   8.343  36.423  1.00 40.67           O  
ANISOU 4564  O   GLY B 271     3141   4813   7498    420   -105    -95       O  
ATOM   4565  N   HIS B 272     -28.693   7.536  38.371  1.00 40.25           N  
ANISOU 4565  N   HIS B 272     3160   4690   7440    357    -53    -60       N  
ATOM   4566  CA  HIS B 272     -27.301   8.018  38.178  1.00 39.85           C  
ANISOU 4566  CA  HIS B 272     3186   4598   7355    318   -113    -27       C  
ATOM   4567  C   HIS B 272     -26.287   6.899  38.463  1.00 38.90           C  
ANISOU 4567  C   HIS B 272     3049   4469   7261    247   -108     -4       C  
ATOM   4568  O   HIS B 272     -26.350   6.314  39.558  1.00 38.43           O  
ANISOU 4568  O   HIS B 272     3004   4392   7204    237    -64      4       O  
ATOM   4569  CB  HIS B 272     -27.053   9.259  39.040  1.00 40.38           C  
ANISOU 4569  CB  HIS B 272     3378   4609   7352    345   -128     -8       C  
ATOM   4570  CG  HIS B 272     -25.749   9.908  38.738  1.00 40.50           C  
ANISOU 4570  CG  HIS B 272     3466   4589   7331    302   -190     19       C  
ATOM   4571  ND1 HIS B 272     -25.359  10.228  37.447  1.00 40.41           N  
ANISOU 4571  ND1 HIS B 272     3433   4593   7325    293   -235     20       N  
ATOM   4572  CD2 HIS B 272     -24.734  10.278  39.546  1.00 40.60           C  
ANISOU 4572  CD2 HIS B 272     3569   4557   7301    260   -214     47       C  
ATOM   4573  CE1 HIS B 272     -24.163  10.777  37.486  1.00 40.05           C  
ANISOU 4573  CE1 HIS B 272     3460   4511   7244    245   -279     48       C  
ATOM   4574  NE2 HIS B 272     -23.769  10.828  38.755  1.00 40.35           N  
ANISOU 4574  NE2 HIS B 272     3563   4514   7252    223   -271     63       N  
ATOM   4575  N   TYR B 273     -25.393   6.637  37.502  1.00 38.29           N  
ANISOU 4575  N   TYR B 273     2945   4402   7198    208   -149      5       N  
ATOM   4576  CA  TYR B 273     -24.183   5.784  37.657  1.00 37.96           C  
ANISOU 4576  CA  TYR B 273     2899   4351   7170    149   -157     35       C  
ATOM   4577  C   TYR B 273     -22.999   6.619  38.132  1.00 37.68           C  
ANISOU 4577  C   TYR B 273     2954   4281   7080    125   -207     73       C  
ATOM   4578  O   TYR B 273     -22.715   7.636  37.498  1.00 37.72           O  
ANISOU 4578  O   TYR B 273     2996   4279   7056    128   -252     75       O  
ATOM   4579  CB  TYR B 273     -23.695   5.195  36.336  1.00 37.72           C  
ANISOU 4579  CB  TYR B 273     2801   4351   7176    121   -179     30       C  
ATOM   4580  CG  TYR B 273     -24.430   3.974  35.859  1.00 38.10           C  
ANISOU 4580  CG  TYR B 273     2758   4431   7285    115   -133     -2       C  
ATOM   4581  CD1 TYR B 273     -25.346   4.066  34.825  1.00 38.31           C  
ANISOU 4581  CD1 TYR B 273     2723   4499   7331    138   -137    -43       C  
ATOM   4582  CD2 TYR B 273     -24.186   2.725  36.400  1.00 38.38           C  
ANISOU 4582  CD2 TYR B 273     2771   4457   7354     85    -87      6       C  
ATOM   4583  CE1 TYR B 273     -26.017   2.955  34.346  1.00 38.22           C  
ANISOU 4583  CE1 TYR B 273     2627   4520   7374    121    -98    -80       C  
ATOM   4584  CE2 TYR B 273     -24.852   1.602  35.932  1.00 38.54           C  
ANISOU 4584  CE2 TYR B 273     2716   4498   7430     70    -41    -27       C  
ATOM   4585  CZ  TYR B 273     -25.770   1.721  34.904  1.00 38.37           C  
ANISOU 4585  CZ  TYR B 273     2630   4518   7428     82    -49    -73       C  
ATOM   4586  OH  TYR B 273     -26.418   0.635  34.401  1.00 38.86           O  
ANISOU 4586  OH  TYR B 273     2617   4604   7542     57     -8   -113       O  
ATOM   4587  N   LYS B 274     -22.322   6.165  39.185  1.00 37.76           N  
ANISOU 4587  N   LYS B 274     2996   4273   7076     99   -198    101       N  
ATOM   4588  CA  LYS B 274     -20.942   6.577  39.537  1.00 37.90           C  
ANISOU 4588  CA  LYS B 274     3071   4276   7053     56   -249    139       C  
ATOM   4589  C   LYS B 274     -20.034   5.365  39.336  1.00 38.10           C  
ANISOU 4589  C   LYS B 274     3036   4326   7113     22   -246    165       C  
ATOM   4590  O   LYS B 274     -20.556   4.239  39.291  1.00 38.05           O  
ANISOU 4590  O   LYS B 274     2972   4331   7154     33   -194    154       O  
ATOM   4591  CB  LYS B 274     -20.851   7.046  40.990  1.00 38.24           C  
ANISOU 4591  CB  LYS B 274     3202   4286   7040     59   -248    153       C  
ATOM   4592  CG  LYS B 274     -21.670   8.274  41.333  1.00 38.84           C  
ANISOU 4592  CG  LYS B 274     3354   4328   7072     98   -247    130       C  
ATOM   4593  CD  LYS B 274     -21.387   8.765  42.738  1.00 39.43           C  
ANISOU 4593  CD  LYS B 274     3529   4367   7083     93   -252    143       C  
ATOM   4594  CE  LYS B 274     -22.454   9.679  43.295  1.00 40.06           C  
ANISOU 4594  CE  LYS B 274     3681   4411   7125    148   -225    118       C  
ATOM   4595  NZ  LYS B 274     -21.838  10.713  44.156  1.00 40.70           N  
ANISOU 4595  NZ  LYS B 274     3885   4448   7128    127   -263    126       N  
ATOM   4596  N   HIS B 275     -18.723   5.590  39.255  1.00 38.54           N  
ANISOU 4596  N   HIS B 275     3106   4389   7145    -17   -296    199       N  
ATOM   4597  CA  HIS B 275     -17.701   4.528  39.072  1.00 38.53           C  
ANISOU 4597  CA  HIS B 275     3051   4416   7170    -42   -296    230       C  
ATOM   4598  C   HIS B 275     -16.815   4.483  40.316  1.00 38.84           C  
ANISOU 4598  C   HIS B 275     3135   4454   7165    -60   -317    269       C  
ATOM   4599  O   HIS B 275     -16.337   5.544  40.731  1.00 38.96           O  
ANISOU 4599  O   HIS B 275     3212   4461   7128    -85   -366    277       O  
ATOM   4600  CB  HIS B 275     -16.906   4.782  37.790  1.00 38.33           C  
ANISOU 4600  CB  HIS B 275     2988   4416   7156    -70   -336    239       C  
ATOM   4601  CG  HIS B 275     -15.903   3.722  37.506  1.00 38.58           C  
ANISOU 4601  CG  HIS B 275     2962   4480   7215    -85   -331    270       C  
ATOM   4602  ND1 HIS B 275     -16.259   2.499  36.965  1.00 38.60           N  
ANISOU 4602  ND1 HIS B 275     2904   4490   7271    -65   -281    259       N  
ATOM   4603  CD2 HIS B 275     -14.563   3.688  37.691  1.00 38.62           C  
ANISOU 4603  CD2 HIS B 275     2961   4512   7201   -115   -368    313       C  
ATOM   4604  CE1 HIS B 275     -15.168   1.771  36.808  1.00 38.53           C  
ANISOU 4604  CE1 HIS B 275     2860   4505   7272    -76   -285    295       C  
ATOM   4605  NE2 HIS B 275     -14.117   2.476  37.246  1.00 38.45           N  
ANISOU 4605  NE2 HIS B 275     2875   4513   7218   -104   -338    330       N  
ATOM   4606  N   ILE B 276     -16.643   3.304  40.908  1.00 39.06           N  
ANISOU 4606  N   ILE B 276     3139   4489   7210    -46   -279    291       N  
ATOM   4607  CA  ILE B 276     -15.686   3.098  42.031  1.00 39.60           C  
ANISOU 4607  CA  ILE B 276     3240   4570   7236    -55   -302    334       C  
ATOM   4608  C   ILE B 276     -14.556   2.198  41.524  1.00 39.42           C  
ANISOU 4608  C   ILE B 276     3151   4586   7237    -64   -312    372       C  
ATOM   4609  O   ILE B 276     -14.836   1.224  40.829  1.00 38.92           O  
ANISOU 4609  O   ILE B 276     3034   4524   7229    -45   -265    365       O  
ATOM   4610  CB  ILE B 276     -16.377   2.537  43.288  1.00 40.18           C  
ANISOU 4610  CB  ILE B 276     3354   4616   7294    -21   -250    336       C  
ATOM   4611  CG1 ILE B 276     -17.317   3.554  43.948  1.00 40.44           C  
ANISOU 4611  CG1 ILE B 276     3461   4615   7289     -9   -246    305       C  
ATOM   4612  CG2 ILE B 276     -15.328   2.054  44.276  1.00 40.81           C  
ANISOU 4612  CG2 ILE B 276     3452   4718   7334    -21   -270    386       C  
ATOM   4613  CD1 ILE B 276     -18.645   3.726  43.270  1.00 40.00           C  
ANISOU 4613  CD1 ILE B 276     3382   4540   7273     14   -203    259       C  
ATOM   4614  N   THR B 277     -13.317   2.557  41.845  1.00 39.82           N  
ANISOU 4614  N   THR B 277     3206   4673   7248    -94   -371    408       N  
ATOM   4615  CA  THR B 277     -12.083   1.851  41.419  1.00 40.00           C  
ANISOU 4615  CA  THR B 277     3164   4747   7286    -99   -388    451       C  
ATOM   4616  C   THR B 277     -11.236   1.587  42.665  1.00 40.61           C  
ANISOU 4616  C   THR B 277     3261   4855   7313    -93   -415    496       C  
ATOM   4617  O   THR B 277     -11.161   2.486  43.522  1.00 41.01           O  
ANISOU 4617  O   THR B 277     3374   4902   7306   -119   -459    492       O  
ATOM   4618  CB  THR B 277     -11.366   2.653  40.326  1.00 39.63           C  
ANISOU 4618  CB  THR B 277     3084   4730   7243   -146   -438    450       C  
ATOM   4619  OG1 THR B 277     -10.402   1.781  39.751  1.00 39.77           O  
ANISOU 4619  OG1 THR B 277     3027   4793   7288   -137   -434    486       O  
ATOM   4620  CG2 THR B 277     -10.694   3.912  40.825  1.00 39.79           C  
ANISOU 4620  CG2 THR B 277     3150   4765   7204   -201   -511    457       C  
ATOM   4621  N   SER B 278     -10.686   0.378  42.788  1.00 41.11           N  
ANISOU 4621  N   SER B 278     3282   4943   7394    -55   -387    536       N  
ATOM   4622  CA  SER B 278      -9.743  -0.011  43.869  1.00 42.16           C  
ANISOU 4622  CA  SER B 278     3421   5119   7478    -37   -415    588       C  
ATOM   4623  C   SER B 278      -8.307   0.248  43.384  1.00 42.54           C  
ANISOU 4623  C   SER B 278     3403   5245   7515    -69   -481    623       C  
ATOM   4624  O   SER B 278      -7.913  -0.316  42.349  1.00 41.74           O  
ANISOU 4624  O   SER B 278     3234   5164   7461    -57   -459    634       O  
ATOM   4625  CB  SER B 278      -9.947  -1.442  44.272  1.00 42.55           C  
ANISOU 4625  CB  SER B 278     3466   5151   7548     29   -344    616       C  
ATOM   4626  OG  SER B 278      -9.206  -1.753  45.445  1.00 43.91           O  
ANISOU 4626  OG  SER B 278     3659   5360   7663     57   -370    665       O  
ATOM   4627  N   LYS B 279      -7.594   1.148  44.061  1.00 43.32           N  
ANISOU 4627  N   LYS B 279     3522   5385   7552   -115   -557    634       N  
ATOM   4628  CA  LYS B 279      -6.188   1.533  43.761  1.00 44.49           C  
ANISOU 4628  CA  LYS B 279     3604   5617   7681   -160   -627    666       C  
ATOM   4629  C   LYS B 279      -5.427   1.447  45.088  1.00 46.03           C  
ANISOU 4629  C   LYS B 279     3812   5868   7806   -153   -678    705       C  
ATOM   4630  O   LYS B 279      -5.635   0.430  45.788  1.00 46.25           O  
ANISOU 4630  O   LYS B 279     3855   5889   7828    -80   -636    732       O  
ATOM   4631  CB  LYS B 279      -6.155   2.894  43.053  1.00 44.04           C  
ANISOU 4631  CB  LYS B 279     3560   5551   7622   -243   -671    630       C  
ATOM   4632  CG  LYS B 279      -7.182   3.086  41.939  1.00 43.08           C  
ANISOU 4632  CG  LYS B 279     3449   5363   7554   -239   -621    586       C  
ATOM   4633  CD  LYS B 279      -6.676   3.140  40.521  1.00 42.89           C  
ANISOU 4633  CD  LYS B 279     3355   5366   7574   -262   -619    590       C  
ATOM   4634  CE  LYS B 279      -6.735   4.554  39.976  1.00 43.07           C  
ANISOU 4634  CE  LYS B 279     3414   5368   7580   -334   -658    559       C  
ATOM   4635  NZ  LYS B 279      -6.178   4.669  38.608  1.00 43.23           N  
ANISOU 4635  NZ  LYS B 279     3371   5416   7637   -359   -657    567       N  
ATOM   4636  N   GLU B 280      -4.593   2.427  45.442  1.00 47.55           N  
ANISOU 4636  N   GLU B 280     4003   6117   7947   -224   -762    707       N  
ATOM   4637  CA  GLU B 280      -3.870   2.402  46.745  1.00 49.19           C  
ANISOU 4637  CA  GLU B 280     4223   6387   8078   -222   -822    740       C  
ATOM   4638  C   GLU B 280      -4.919   2.461  47.863  1.00 50.13           C  
ANISOU 4638  C   GLU B 280     4455   6435   8155   -192   -796    715       C  
ATOM   4639  O   GLU B 280      -4.690   1.822  48.903  1.00 50.89           O  
ANISOU 4639  O   GLU B 280     4568   6562   8206   -140   -800    750       O  
ATOM   4640  CB  GLU B 280      -2.823   3.516  46.834  1.00 49.45           C  
ANISOU 4640  CB  GLU B 280     4233   6491   8065   -322   -919    737       C  
ATOM   4641  CG  GLU B 280      -3.392   4.899  47.100  1.00 49.36           C  
ANISOU 4641  CG  GLU B 280     4321   6417   8015   -402   -951    680       C  
ATOM   4642  CD  GLU B 280      -3.912   5.654  45.888  1.00 48.69           C  
ANISOU 4642  CD  GLU B 280     4248   6270   7982   -448   -925    639       C  
ATOM   4643  OE1 GLU B 280      -4.124   5.029  44.821  1.00 47.50           O  
ANISOU 4643  OE1 GLU B 280     4039   6107   7901   -409   -869    647       O  
ATOM   4644  OE2 GLU B 280      -4.084   6.881  46.015  1.00 49.35           O  
ANISOU 4644  OE2 GLU B 280     4404   6314   8029   -523   -961    600       O  
ATOM   4645  N   THR B 281      -6.010   3.208  47.629  1.00 50.62           N  
ANISOU 4645  N   THR B 281     4590   6412   8231   -218   -768    660       N  
ATOM   4646  CA  THR B 281      -7.269   3.247  48.431  1.00 50.75           C  
ANISOU 4646  CA  THR B 281     4708   6346   8226   -182   -719    630       C  
ATOM   4647  C   THR B 281      -8.451   3.236  47.451  1.00 49.45           C  
ANISOU 4647  C   THR B 281     4548   6104   8133   -167   -646    590       C  
ATOM   4648  O   THR B 281      -8.197   3.032  46.252  1.00 48.99           O  
ANISOU 4648  O   THR B 281     4417   6061   8135   -176   -635    592       O  
ATOM   4649  CB  THR B 281      -7.296   4.469  49.360  1.00 51.77           C  
ANISOU 4649  CB  THR B 281     4932   6463   8273   -239   -780    600       C  
ATOM   4650  OG1 THR B 281      -8.417   4.352  50.246  1.00 52.75           O  
ANISOU 4650  OG1 THR B 281     5150   6520   8371   -190   -727    580       O  
ATOM   4651  CG2 THR B 281      -7.366   5.776  48.598  1.00 51.84           C  
ANISOU 4651  CG2 THR B 281     4963   6442   8290   -320   -813    556       C  
ATOM   4652  N   LEU B 282      -9.682   3.455  47.926  1.00 49.16           N  
ANISOU 4652  N   LEU B 282     4592   5996   8088   -143   -599    555       N  
ATOM   4653  CA  LEU B 282     -10.907   3.486  47.075  1.00 48.54           C  
ANISOU 4653  CA  LEU B 282     4517   5853   8074   -126   -533    513       C  
ATOM   4654  C   LEU B 282     -11.147   4.907  46.560  1.00 48.06           C  
ANISOU 4654  C   LEU B 282     4495   5763   8000   -182   -571    470       C  
ATOM   4655  O   LEU B 282     -11.176   5.839  47.381  1.00 48.56           O  
ANISOU 4655  O   LEU B 282     4642   5808   7997   -210   -608    453       O  
ATOM   4656  CB  LEU B 282     -12.121   3.016  47.880  1.00 48.83           C  
ANISOU 4656  CB  LEU B 282     4611   5833   8106    -69   -460    499       C  
ATOM   4657  CG  LEU B 282     -12.114   1.543  48.286  1.00 49.37           C  
ANISOU 4657  CG  LEU B 282     4652   5909   8195     -9   -400    539       C  
ATOM   4658  CD1 LEU B 282     -13.290   1.247  49.207  1.00 49.49           C  
ANISOU 4658  CD1 LEU B 282     4737   5868   8196     34   -329    525       C  
ATOM   4659  CD2 LEU B 282     -12.107   0.639  47.052  1.00 49.29           C  
ANISOU 4659  CD2 LEU B 282     4554   5903   8269      5   -357    544       C  
ATOM   4660  N   TYR B 283     -11.334   5.046  45.248  1.00 47.13           N  
ANISOU 4660  N   TYR B 283     4328   5638   7941   -194   -558    453       N  
ATOM   4661  CA  TYR B 283     -11.689   6.310  44.558  1.00 46.84           C  
ANISOU 4661  CA  TYR B 283     4329   5565   7901   -234   -580    415       C  
ATOM   4662  C   TYR B 283     -13.077   6.151  43.940  1.00 46.01           C  
ANISOU 4662  C   TYR B 283     4223   5410   7845   -186   -512    378       C  
ATOM   4663  O   TYR B 283     -13.295   5.145  43.238  1.00 45.67           O  
ANISOU 4663  O   TYR B 283     4107   5380   7863   -155   -468    384       O  
ATOM   4664  CB  TYR B 283     -10.677   6.637  43.455  1.00 47.20           C  
ANISOU 4664  CB  TYR B 283     4312   5652   7967   -288   -624    429       C  
ATOM   4665  CG  TYR B 283      -9.311   7.077  43.923  1.00 47.99           C  
ANISOU 4665  CG  TYR B 283     4408   5808   8018   -354   -699    457       C  
ATOM   4666  CD1 TYR B 283      -8.365   6.157  44.346  1.00 48.03           C  
ANISOU 4666  CD1 TYR B 283     4347   5882   8018   -342   -716    503       C  
ATOM   4667  CD2 TYR B 283      -8.954   8.418  43.923  1.00 48.59           C  
ANISOU 4667  CD2 TYR B 283     4542   5868   8049   -428   -753    438       C  
ATOM   4668  CE1 TYR B 283      -7.107   6.560  44.763  1.00 48.48           C  
ANISOU 4668  CE1 TYR B 283     4386   6005   8029   -403   -790    528       C  
ATOM   4669  CE2 TYR B 283      -7.700   8.835  44.335  1.00 48.94           C  
ANISOU 4669  CE2 TYR B 283     4576   5970   8049   -501   -825    459       C  
ATOM   4670  CZ  TYR B 283      -6.770   7.903  44.755  1.00 49.15           C  
ANISOU 4670  CZ  TYR B 283     4524   6078   8072   -489   -846    504       C  
ATOM   4671  OH  TYR B 283      -5.540   8.328  45.160  1.00 50.08           O  
ANISOU 4671  OH  TYR B 283     4620   6264   8144   -562   -921    524       O  
ATOM   4672  N   CYS B 284     -13.979   7.108  44.191  1.00 45.80           N  
ANISOU 4672  N   CYS B 284     4276   5332   7792   -179   -504    342       N  
ATOM   4673  CA  CYS B 284     -15.299   7.224  43.517  1.00 44.46           C  
ANISOU 4673  CA  CYS B 284     4103   5124   7663   -136   -452    304       C  
ATOM   4674  C   CYS B 284     -15.204   8.301  42.433  1.00 43.18           C  
ANISOU 4674  C   CYS B 284     3953   4950   7503   -167   -486    286       C  
ATOM   4675  O   CYS B 284     -15.058   9.484  42.779  1.00 43.96           O  
ANISOU 4675  O   CYS B 284     4137   5018   7547   -196   -522    276       O  
ATOM   4676  CB  CYS B 284     -16.405   7.556  44.506  1.00 45.41           C  
ANISOU 4676  CB  CYS B 284     4301   5200   7751    -95   -413    279       C  
ATOM   4677  SG  CYS B 284     -18.031   7.734  43.719  1.00 46.84           S  
ANISOU 4677  SG  CYS B 284     4465   5351   7979    -38   -353    234       S  
ATOM   4678  N   ILE B 285     -15.251   7.895  41.168  1.00 41.37           N  
ANISOU 4678  N   ILE B 285     3647   4742   7330   -160   -473    284       N  
ATOM   4679  CA  ILE B 285     -15.263   8.818  40.000  1.00 40.29           C  
ANISOU 4679  CA  ILE B 285     3517   4593   7197   -178   -496    269       C  
ATOM   4680  C   ILE B 285     -16.727   9.067  39.613  1.00 39.70           C  
ANISOU 4680  C   ILE B 285     3456   4487   7141   -117   -453    231       C  
ATOM   4681  O   ILE B 285     -17.411   8.123  39.155  1.00 38.84           O  
ANISOU 4681  O   ILE B 285     3275   4397   7084    -79   -409    218       O  
ATOM   4682  CB  ILE B 285     -14.437   8.244  38.836  1.00 39.85           C  
ANISOU 4682  CB  ILE B 285     3373   4583   7184   -203   -507    291       C  
ATOM   4683  CG1 ILE B 285     -12.991   7.975  39.270  1.00 40.19           C  
ANISOU 4683  CG1 ILE B 285     3391   4669   7209   -255   -548    332       C  
ATOM   4684  CG2 ILE B 285     -14.517   9.158  37.618  1.00 39.69           C  
ANISOU 4684  CG2 ILE B 285     3365   4550   7165   -215   -524    277       C  
ATOM   4685  CD1 ILE B 285     -12.084   7.482  38.163  1.00 39.84           C  
ANISOU 4685  CD1 ILE B 285     3262   4673   7202   -278   -556    357       C  
ATOM   4686  N   ASP B 286     -17.173  10.308  39.795  1.00 39.00           N  
ANISOU 4686  N   ASP B 286     3457   4353   7008   -110   -466    212       N  
ATOM   4687  CA  ASP B 286     -18.505  10.812  39.391  1.00 38.12           C  
ANISOU 4687  CA  ASP B 286     3366   4215   6901    -46   -433    178       C  
ATOM   4688  C   ASP B 286     -18.305  11.834  38.273  1.00 37.68           C  
ANISOU 4688  C   ASP B 286     3339   4142   6832    -58   -464    176       C  
ATOM   4689  O   ASP B 286     -18.468  13.030  38.547  1.00 38.51           O  
ANISOU 4689  O   ASP B 286     3547   4198   6887    -54   -478    168       O  
ATOM   4690  CB  ASP B 286     -19.211  11.409  40.607  1.00 38.55           C  
ANISOU 4690  CB  ASP B 286     3513   4225   6908    -13   -414    162       C  
ATOM   4691  CG  ASP B 286     -20.630  11.847  40.327  1.00 38.61           C  
ANISOU 4691  CG  ASP B 286     3533   4215   6921     63   -374    131       C  
ATOM   4692  OD1 ASP B 286     -21.036  11.777  39.143  1.00 38.25           O  
ANISOU 4692  OD1 ASP B 286     3428   4193   6912     88   -371    120       O  
ATOM   4693  OD2 ASP B 286     -21.303  12.263  41.291  1.00 39.03           O  
ANISOU 4693  OD2 ASP B 286     3655   4235   6939    101   -348    117       O  
ATOM   4694  N   GLY B 287     -17.944  11.378  37.073  1.00 36.56           N  
ANISOU 4694  N   GLY B 287     3120   4038   6730    -70   -472    184       N  
ATOM   4695  CA  GLY B 287     -17.677  12.260  35.925  1.00 36.35           C  
ANISOU 4695  CA  GLY B 287     3118   4000   6692    -82   -498    188       C  
ATOM   4696  C   GLY B 287     -16.390  13.041  36.127  1.00 36.73           C  
ANISOU 4696  C   GLY B 287     3228   4027   6698   -163   -543    214       C  
ATOM   4697  O   GLY B 287     -15.318  12.427  36.038  1.00 36.43           O  
ANISOU 4697  O   GLY B 287     3132   4030   6679   -218   -562    240       O  
ATOM   4698  N   ALA B 288     -16.479  14.341  36.418  1.00 37.35           N  
ANISOU 4698  N   ALA B 288     3422   4045   6723   -172   -558    208       N  
ATOM   4699  CA  ALA B 288     -15.315  15.234  36.656  1.00 37.74           C  
ANISOU 4699  CA  ALA B 288     3545   4065   6727   -261   -601    227       C  
ATOM   4700  C   ALA B 288     -15.014  15.328  38.154  1.00 38.11           C  
ANISOU 4700  C   ALA B 288     3649   4095   6734   -296   -616    224       C  
ATOM   4701  O   ALA B 288     -13.985  15.913  38.493  1.00 38.48           O  
ANISOU 4701  O   ALA B 288     3744   4132   6745   -381   -656    236       O  
ATOM   4702  CB  ALA B 288     -15.553  16.606  36.069  1.00 38.08           C  
ANISOU 4702  CB  ALA B 288     3694   4042   6730   -257   -605    220       C  
ATOM   4703  N   LEU B 289     -15.867  14.774  39.013  1.00 38.30           N  
ANISOU 4703  N   LEU B 289     3668   4120   6762   -236   -585    208       N  
ATOM   4704  CA  LEU B 289     -15.695  14.833  40.488  1.00 39.07           C  
ANISOU 4704  CA  LEU B 289     3827   4201   6814   -256   -595    204       C  
ATOM   4705  C   LEU B 289     -15.030  13.538  40.937  1.00 39.19           C  
ANISOU 4705  C   LEU B 289     3744   4285   6859   -278   -602    228       C  
ATOM   4706  O   LEU B 289     -15.155  12.534  40.215  1.00 38.43           O  
ANISOU 4706  O   LEU B 289     3543   4235   6824   -250   -578    237       O  
ATOM   4707  CB  LEU B 289     -17.050  15.012  41.176  1.00 39.45           C  
ANISOU 4707  CB  LEU B 289     3934   4209   6845   -171   -549    175       C  
ATOM   4708  CG  LEU B 289     -17.993  16.033  40.541  1.00 39.67           C  
ANISOU 4708  CG  LEU B 289     4031   4182   6858   -112   -527    154       C  
ATOM   4709  CD1 LEU B 289     -19.229  16.209  41.410  1.00 39.95           C  
ANISOU 4709  CD1 LEU B 289     4123   4185   6871    -29   -481    128       C  
ATOM   4710  CD2 LEU B 289     -17.292  17.358  40.307  1.00 40.29           C  
ANISOU 4710  CD2 LEU B 289     4221   4202   6885   -174   -565    156       C  
ATOM   4711  N   LEU B 290     -14.377  13.581  42.096  1.00 40.45           N  
ANISOU 4711  N   LEU B 290     3946   4449   6973   -323   -632    236       N  
ATOM   4712  CA  LEU B 290     -13.474  12.526  42.611  1.00 41.08           C  
ANISOU 4712  CA  LEU B 290     3947   4595   7064   -352   -651    266       C  
ATOM   4713  C   LEU B 290     -13.530  12.538  44.134  1.00 42.38           C  
ANISOU 4713  C   LEU B 290     4182   4747   7172   -349   -658    262       C  
ATOM   4714  O   LEU B 290     -13.264  13.588  44.718  1.00 42.92           O  
ANISOU 4714  O   LEU B 290     4354   4777   7176   -395   -693    247       O  
ATOM   4715  CB  LEU B 290     -12.043  12.804  42.142  1.00 41.35           C  
ANISOU 4715  CB  LEU B 290     3947   4670   7093   -443   -709    292       C  
ATOM   4716  CG  LEU B 290     -11.012  11.755  42.564  1.00 41.50           C  
ANISOU 4716  CG  LEU B 290     3876   4769   7122   -466   -734    329       C  
ATOM   4717  CD1 LEU B 290     -11.267  10.431  41.846  1.00 40.95           C  
ANISOU 4717  CD1 LEU B 290     3693   4739   7126   -406   -688    346       C  
ATOM   4718  CD2 LEU B 290      -9.587  12.233  42.334  1.00 41.65           C  
ANISOU 4718  CD2 LEU B 290     3871   4832   7121   -565   -797    352       C  
ATOM   4719  N   THR B 291     -13.800  11.389  44.744  1.00 43.33           N  
ANISOU 4719  N   THR B 291     4253   4899   7311   -301   -626    275       N  
ATOM   4720  CA  THR B 291     -13.817  11.205  46.215  1.00 44.75           C  
ANISOU 4720  CA  THR B 291     4492   5076   7435   -291   -628    277       C  
ATOM   4721  C   THR B 291     -12.826  10.096  46.561  1.00 45.17           C  
ANISOU 4721  C   THR B 291     4462   5202   7497   -305   -650    319       C  
ATOM   4722  O   THR B 291     -12.425   9.370  45.641  1.00 45.18           O  
ANISOU 4722  O   THR B 291     4361   5246   7558   -305   -644    341       O  
ATOM   4723  CB  THR B 291     -15.268  10.974  46.663  1.00 45.29           C  
ANISOU 4723  CB  THR B 291     4595   5101   7511   -206   -555    254       C  
ATOM   4724  OG1 THR B 291     -15.842  12.280  46.596  1.00 45.98           O  
ANISOU 4724  OG1 THR B 291     4783   5123   7561   -204   -556    220       O  
ATOM   4725  CG2 THR B 291     -15.435  10.371  48.047  1.00 45.68           C  
ANISOU 4725  CG2 THR B 291     4679   5155   7520   -175   -533    264       C  
ATOM   4726  N   LYS B 292     -12.434   9.999  47.832  1.00 46.28           N  
ANISOU 4726  N   LYS B 292     4651   5358   7576   -314   -675    330       N  
ATOM   4727  CA  LYS B 292     -11.596   8.900  48.379  1.00 47.11           C  
ANISOU 4727  CA  LYS B 292     4690   5533   7677   -308   -692    374       C  
ATOM   4728  C   LYS B 292     -12.131   8.487  49.748  1.00 47.83           C  
ANISOU 4728  C   LYS B 292     4846   5607   7718   -256   -662    377       C  
ATOM   4729  O   LYS B 292     -12.471   9.393  50.546  1.00 47.66           O  
ANISOU 4729  O   LYS B 292     4936   5543   7630   -268   -675    348       O  
ATOM   4730  CB  LYS B 292     -10.147   9.340  48.599  1.00 48.55           C  
ANISOU 4730  CB  LYS B 292     4860   5774   7812   -391   -782    394       C  
ATOM   4731  CG  LYS B 292      -9.420   9.958  47.412  1.00 48.84           C  
ANISOU 4731  CG  LYS B 292     4847   5830   7880   -462   -821    393       C  
ATOM   4732  CD  LYS B 292      -7.924  10.071  47.636  1.00 50.34           C  
ANISOU 4732  CD  LYS B 292     4991   6102   8034   -539   -902    421       C  
ATOM   4733  CE  LYS B 292      -7.485  10.323  49.068  1.00 51.37           C  
ANISOU 4733  CE  LYS B 292     5187   6254   8074   -566   -956    421       C  
ATOM   4734  NZ  LYS B 292      -6.012  10.199  49.198  1.00 52.10           N  
ANISOU 4734  NZ  LYS B 292     5201   6449   8143   -632  -1034    454       N  
ATOM   4735  N   SER B 293     -12.164   7.181  50.020  1.00 48.82           N  
ANISOU 4735  N   SER B 293     4914   5763   7871   -201   -621    411       N  
ATOM   4736  CA  SER B 293     -12.434   6.611  51.365  1.00 50.65           C  
ANISOU 4736  CA  SER B 293     5199   5991   8051   -153   -594    427       C  
ATOM   4737  C   SER B 293     -11.619   5.330  51.558  1.00 51.55           C  
ANISOU 4737  C   SER B 293     5237   6171   8178   -125   -596    483       C  
ATOM   4738  O   SER B 293     -11.199   4.733  50.553  1.00 50.94           O  
ANISOU 4738  O   SER B 293     5062   6125   8167   -126   -591    502       O  
ATOM   4739  CB  SER B 293     -13.917   6.378  51.591  1.00 50.80           C  
ANISOU 4739  CB  SER B 293     5260   5946   8093    -88   -501    403       C  
ATOM   4740  OG  SER B 293     -14.471   5.538  50.590  1.00 50.13           O  
ANISOU 4740  OG  SER B 293     5088   5857   8102    -56   -438    405       O  
ATOM   4741  N   SER B 294     -11.399   4.953  52.818  1.00 53.35           N  
ANISOU 4741  N   SER B 294     5514   6416   8337    -96   -604    508       N  
ATOM   4742  CA  SER B 294     -10.749   3.686  53.230  1.00 54.91           C  
ANISOU 4742  CA  SER B 294     5661   6668   8533    -49   -595    566       C  
ATOM   4743  C   SER B 294     -11.697   2.507  52.961  1.00 56.46           C  
ANISOU 4743  C   SER B 294     5830   6821   8800     21   -486    577       C  
ATOM   4744  O   SER B 294     -11.180   1.396  52.742  1.00 56.81           O  
ANISOU 4744  O   SER B 294     5809   6899   8877     57   -467    622       O  
ATOM   4745  CB  SER B 294     -10.326   3.749  54.680  1.00 55.22           C  
ANISOU 4745  CB  SER B 294     5776   6736   8469    -37   -636    587       C  
ATOM   4746  OG  SER B 294     -10.795   2.610  55.386  1.00 54.99           O  
ANISOU 4746  OG  SER B 294     5766   6691   8435     44   -562    622       O  
ATOM   4747  N   GLU B 295     -13.021   2.727  53.006  1.00 59.11           N  
ANISOU 4747  N   GLU B 295     6216   7086   9157     40   -416    538       N  
ATOM   4748  CA  GLU B 295     -14.056   1.728  52.602  1.00 60.47           C  
ANISOU 4748  CA  GLU B 295     6356   7214   9405     89   -309    536       C  
ATOM   4749  C   GLU B 295     -15.244   2.435  51.941  1.00 59.83           C  
ANISOU 4749  C   GLU B 295     6282   7081   9368     77   -271    479       C  
ATOM   4750  O   GLU B 295     -15.362   3.661  52.114  1.00 59.25           O  
ANISOU 4750  O   GLU B 295     6268   6994   9251     47   -314    446       O  
ATOM   4751  CB  GLU B 295     -14.538   0.894  53.787  1.00 62.59           C  
ANISOU 4751  CB  GLU B 295     6683   7459   9638    149   -241    564       C  
ATOM   4752  CG  GLU B 295     -15.143  -0.418  53.326  1.00 64.00           C  
ANISOU 4752  CG  GLU B 295     6811   7609   9898    189   -142    578       C  
ATOM   4753  CD  GLU B 295     -15.696  -1.313  54.413  1.00 66.21           C  
ANISOU 4753  CD  GLU B 295     7150   7855  10151    245    -58    607       C  
ATOM   4754  OE1 GLU B 295     -16.356  -0.797  55.360  1.00 66.27           O  
ANISOU 4754  OE1 GLU B 295     7241   7835  10103    257    -37    591       O  
ATOM   4755  OE2 GLU B 295     -15.477  -2.538  54.294  1.00 68.50           O  
ANISOU 4755  OE2 GLU B 295     7407   8142  10475    278     -9    646       O  
ATOM   4756  N   TYR B 296     -16.071   1.682  51.201  1.00 60.21           N  
ANISOU 4756  N   TYR B 296     6274   7104   9499    100   -193    467       N  
ATOM   4757  CA  TYR B 296     -17.246   2.198  50.449  1.00 60.62           C  
ANISOU 4757  CA  TYR B 296     6311   7119   9600     96   -154    414       C  
ATOM   4758  C   TYR B 296     -18.467   1.290  50.616  1.00 59.02           C  
ANISOU 4758  C   TYR B 296     6097   6882   9445    137    -46    405       C  
ATOM   4759  O   TYR B 296     -18.314   0.060  50.499  1.00 58.49           O  
ANISOU 4759  O   TYR B 296     5986   6817   9418    152      0    433       O  
ATOM   4760  CB  TYR B 296     -16.937   2.297  48.957  1.00 62.53           C  
ANISOU 4760  CB  TYR B 296     6468   7383   9907     65   -184    400       C  
ATOM   4761  CG  TYR B 296     -17.980   3.062  48.187  1.00 64.26           C  
ANISOU 4761  CG  TYR B 296     6679   7576  10160     62   -167    348       C  
ATOM   4762  CD1 TYR B 296     -17.843   4.427  48.003  1.00 66.39           C  
ANISOU 4762  CD1 TYR B 296     6994   7839  10391     35   -227    325       C  
ATOM   4763  CD2 TYR B 296     -19.111   2.445  47.678  1.00 64.67           C  
ANISOU 4763  CD2 TYR B 296     6683   7611  10278     86    -90    323       C  
ATOM   4764  CE1 TYR B 296     -18.791   5.162  47.313  1.00 67.19           C  
ANISOU 4764  CE1 TYR B 296     7095   7917  10516     45   -211    283       C  
ATOM   4765  CE2 TYR B 296     -20.073   3.166  46.987  1.00 65.96           C  
ANISOU 4765  CE2 TYR B 296     6833   7762  10466     91    -80    277       C  
ATOM   4766  CZ  TYR B 296     -19.903   4.527  46.796  1.00 67.24           C  
ANISOU 4766  CZ  TYR B 296     7043   7918  10587     77   -140    260       C  
ATOM   4767  OH  TYR B 296     -20.824   5.271  46.122  1.00 68.36           O  
ANISOU 4767  OH  TYR B 296     7178   8048  10747     93   -131    220       O  
ATOM   4768  N   LYS B 297     -19.640   1.896  50.832  1.00 57.60           N  
ANISOU 4768  N   LYS B 297     5952   6671   9263    152     -4    366       N  
ATOM   4769  CA  LYS B 297     -20.961   1.211  50.961  1.00 56.58           C  
ANISOU 4769  CA  LYS B 297     5804   6513   9181    182    100    348       C  
ATOM   4770  C   LYS B 297     -21.996   1.988  50.144  1.00 53.73           C  
ANISOU 4770  C   LYS B 297     5409   6146   8857    182    111    295       C  
ATOM   4771  O   LYS B 297     -22.073   3.208  50.321  1.00 53.53           O  
ANISOU 4771  O   LYS B 297     5440   6114   8783    185     68    275       O  
ATOM   4772  CB  LYS B 297     -21.414   1.126  52.424  1.00 58.04           C  
ANISOU 4772  CB  LYS B 297     6076   6672   9304    218    153    364       C  
ATOM   4773  CG  LYS B 297     -22.720   0.365  52.634  1.00 59.10           C  
ANISOU 4773  CG  LYS B 297     6189   6780   9485    243    269    350       C  
ATOM   4774  CD  LYS B 297     -23.633   0.908  53.730  1.00 59.96           C  
ANISOU 4774  CD  LYS B 297     6376   6864   9541    279    321    338       C  
ATOM   4775  CE  LYS B 297     -23.663   0.061  54.991  1.00 60.89           C  
ANISOU 4775  CE  LYS B 297     6557   6960   9618    307    389    379       C  
ATOM   4776  NZ  LYS B 297     -23.945   0.879  56.197  1.00 61.68           N  
ANISOU 4776  NZ  LYS B 297     6765   7044   9627    340    394    377       N  
ATOM   4777  N   GLY B 298     -22.763   1.313  49.287  1.00 50.98           N  
ANISOU 4777  N   GLY B 298     4977   5802   8590    180    166    272       N  
ATOM   4778  CA  GLY B 298     -23.694   1.993  48.369  1.00 49.99           C  
ANISOU 4778  CA  GLY B 298     4805   5686   8502    184    167    223       C  
ATOM   4779  C   GLY B 298     -24.365   1.036  47.394  1.00 48.33           C  
ANISOU 4779  C   GLY B 298     4492   5490   8380    171    220    199       C  
ATOM   4780  O   GLY B 298     -24.022  -0.139  47.323  1.00 48.04           O  
ANISOU 4780  O   GLY B 298     4425   5450   8379    154    253    220       O  
ATOM   4781  N   PRO B 299     -25.360   1.515  46.622  1.00 46.87           N  
ANISOU 4781  N   PRO B 299     4254   5322   8230    180    230    154       N  
ATOM   4782  CA  PRO B 299     -26.052   0.666  45.655  1.00 46.47           C  
ANISOU 4782  CA  PRO B 299     4102   5292   8259    161    273    123       C  
ATOM   4783  C   PRO B 299     -25.182   0.351  44.429  1.00 44.46           C  
ANISOU 4783  C   PRO B 299     3797   5056   8037    128    217    125       C  
ATOM   4784  O   PRO B 299     -25.113   1.161  43.528  1.00 44.13           O  
ANISOU 4784  O   PRO B 299     3735   5036   7994    129    160    105       O  
ATOM   4785  CB  PRO B 299     -27.306   1.490  45.303  1.00 46.89           C  
ANISOU 4785  CB  PRO B 299     4123   5371   8323    192    285     78       C  
ATOM   4786  CG  PRO B 299     -26.863   2.919  45.499  1.00 47.04           C  
ANISOU 4786  CG  PRO B 299     4220   5378   8272    219    216     86       C  
ATOM   4787  CD  PRO B 299     -25.913   2.873  46.683  1.00 47.15           C  
ANISOU 4787  CD  PRO B 299     4328   5359   8226    213    204    130       C  
ATOM   4788  N   ILE B 300     -24.565  -0.834  44.432  1.00 43.37           N  
ANISOU 4788  N   ILE B 300     3645   4906   7926    104    243    150       N  
ATOM   4789  CA  ILE B 300     -23.685  -1.344  43.341  1.00 42.40           C  
ANISOU 4789  CA  ILE B 300     3477   4797   7835     76    205    156       C  
ATOM   4790  C   ILE B 300     -24.515  -2.289  42.482  1.00 42.10           C  
ANISOU 4790  C   ILE B 300     3359   4766   7870     53    261    115       C  
ATOM   4791  O   ILE B 300     -25.330  -3.024  43.052  1.00 42.73           O  
ANISOU 4791  O   ILE B 300     3432   4827   7975     49    341    105       O  
ATOM   4792  CB  ILE B 300     -22.430  -2.045  43.896  1.00 42.07           C  
ANISOU 4792  CB  ILE B 300     3473   4738   7770     74    198    212       C  
ATOM   4793  CG1 ILE B 300     -21.804  -1.287  45.067  1.00 42.10           C  
ANISOU 4793  CG1 ILE B 300     3561   4736   7698     94    158    250       C  
ATOM   4794  CG2 ILE B 300     -21.414  -2.273  42.790  1.00 41.67           C  
ANISOU 4794  CG2 ILE B 300     3381   4708   7740     55    147    222       C  
ATOM   4795  CD1 ILE B 300     -21.466   0.157  44.765  1.00 41.90           C  
ANISOU 4795  CD1 ILE B 300     3558   4730   7631     90     74    240       C  
ATOM   4796  N   THR B 301     -24.300  -2.260  41.165  1.00 41.83           N  
ANISOU 4796  N   THR B 301     3268   4758   7865     35    220     91       N  
ATOM   4797  CA  THR B 301     -25.004  -3.114  40.169  1.00 41.72           C  
ANISOU 4797  CA  THR B 301     3177   4757   7916      6    259     45       C  
ATOM   4798  C   THR B 301     -24.015  -3.893  39.290  1.00 41.10           C  
ANISOU 4798  C   THR B 301     3081   4675   7861    -15    243     57       C  
ATOM   4799  O   THR B 301     -24.446  -4.887  38.700  1.00 41.59           O  
ANISOU 4799  O   THR B 301     3098   4729   7972    -44    290     25       O  
ATOM   4800  CB  THR B 301     -25.959  -2.279  39.310  1.00 41.83           C  
ANISOU 4800  CB  THR B 301     3135   4816   7940     13    229     -6       C  
ATOM   4801  OG1 THR B 301     -26.752  -3.197  38.561  1.00 42.69           O  
ANISOU 4801  OG1 THR B 301     3170   4941   8109    -20    274    -54       O  
ATOM   4802  CG2 THR B 301     -25.253  -1.334  38.366  1.00 41.56           C  
ANISOU 4802  CG2 THR B 301     3102   4807   7879     23    142     -3       C  
ATOM   4803  N   ASP B 302     -22.768  -3.445  39.153  1.00 40.50           N  
ANISOU 4803  N   ASP B 302     3035   4604   7749     -4    180     97       N  
ATOM   4804  CA  ASP B 302     -21.703  -4.193  38.432  1.00 40.27           C  
ANISOU 4804  CA  ASP B 302     2991   4572   7735    -15    169    118       C  
ATOM   4805  C   ASP B 302     -20.440  -4.201  39.289  1.00 39.30           C  
ANISOU 4805  C   ASP B 302     2921   4439   7569      3    147    184       C  
ATOM   4806  O   ASP B 302     -20.193  -3.219  39.999  1.00 38.98           O  
ANISOU 4806  O   ASP B 302     2922   4408   7480     16    103    206       O  
ATOM   4807  CB  ASP B 302     -21.402  -3.603  37.052  1.00 40.56           C  
ANISOU 4807  CB  ASP B 302     2987   4647   7775    -24    107     95       C  
ATOM   4808  CG  ASP B 302     -22.617  -3.566  36.133  1.00 41.38           C  
ANISOU 4808  CG  ASP B 302     3034   4773   7914    -39    119     29       C  
ATOM   4809  OD1 ASP B 302     -23.239  -4.639  35.912  1.00 41.88           O  
ANISOU 4809  OD1 ASP B 302     3065   4822   8023    -62    180     -3       O  
ATOM   4810  OD2 ASP B 302     -22.945  -2.466  35.646  1.00 42.02           O  
ANISOU 4810  OD2 ASP B 302     3103   4886   7974    -27     67     10       O  
ATOM   4811  N   VAL B 303     -19.704  -5.306  39.258  1.00 38.72           N  
ANISOU 4811  N   VAL B 303     2851   4347   7512      7    179    215       N  
ATOM   4812  CA  VAL B 303     -18.352  -5.409  39.870  1.00 38.48           C  
ANISOU 4812  CA  VAL B 303     2855   4323   7442     31    150    281       C  
ATOM   4813  C   VAL B 303     -17.493  -6.229  38.913  1.00 38.18           C  
ANISOU 4813  C   VAL B 303     2784   4291   7431     34    155    295       C  
ATOM   4814  O   VAL B 303     -17.949  -7.297  38.474  1.00 37.40           O  
ANISOU 4814  O   VAL B 303     2673   4159   7378     27    221    270       O  
ATOM   4815  CB  VAL B 303     -18.385  -6.001  41.288  1.00 38.68           C  
ANISOU 4815  CB  VAL B 303     2936   4314   7445     56    201    320       C  
ATOM   4816  CG1 VAL B 303     -17.021  -5.938  41.948  1.00 38.76           C  
ANISOU 4816  CG1 VAL B 303     2975   4346   7404     85    156    387       C  
ATOM   4817  CG2 VAL B 303     -19.416  -5.307  42.159  1.00 38.85           C  
ANISOU 4817  CG2 VAL B 303     2990   4325   7445     55    213    299       C  
ATOM   4818  N   PHE B 304     -16.330  -5.681  38.556  1.00 38.29           N  
ANISOU 4818  N   PHE B 304     2784   4345   7417     39     88    328       N  
ATOM   4819  CA  PHE B 304     -15.328  -6.334  37.680  1.00 38.89           C  
ANISOU 4819  CA  PHE B 304     2828   4437   7510     51     87    350       C  
ATOM   4820  C   PHE B 304     -14.216  -6.901  38.562  1.00 40.26           C  
ANISOU 4820  C   PHE B 304     3024   4616   7653     91     91    420       C  
ATOM   4821  O   PHE B 304     -13.821  -6.238  39.539  1.00 40.08           O  
ANISOU 4821  O   PHE B 304     3027   4616   7582     97     47    454       O  
ATOM   4822  CB  PHE B 304     -14.840  -5.350  36.621  1.00 37.96           C  
ANISOU 4822  CB  PHE B 304     2672   4367   7383     29     17    338       C  
ATOM   4823  CG  PHE B 304     -15.937  -4.858  35.714  1.00 37.14           C  
ANISOU 4823  CG  PHE B 304     2546   4260   7303      2     14    272       C  
ATOM   4824  CD1 PHE B 304     -16.065  -5.356  34.427  1.00 36.76           C  
ANISOU 4824  CD1 PHE B 304     2462   4215   7290     -6     32    238       C  
ATOM   4825  CD2 PHE B 304     -16.841  -3.902  36.147  1.00 36.65           C  
ANISOU 4825  CD2 PHE B 304     2502   4196   7225     -9     -6    245       C  
ATOM   4826  CE1 PHE B 304     -17.054  -4.886  33.580  1.00 36.38           C  
ANISOU 4826  CE1 PHE B 304     2389   4174   7256    -27     21    178       C  
ATOM   4827  CE2 PHE B 304     -17.837  -3.445  35.300  1.00 36.45           C  
ANISOU 4827  CE2 PHE B 304     2452   4178   7218    -24    -12    187       C  
ATOM   4828  CZ  PHE B 304     -17.947  -3.942  34.021  1.00 36.30           C  
ANISOU 4828  CZ  PHE B 304     2392   4169   7232    -33     -1    154       C  
ATOM   4829  N   TYR B 305     -13.795  -8.129  38.261  1.00 42.30           N  
ANISOU 4829  N   TYR B 305     3279   4853   7937    120    146    440       N  
ATOM   4830  CA  TYR B 305     -12.728  -8.864  38.985  1.00 44.46           C  
ANISOU 4830  CA  TYR B 305     3572   5133   8186    174    160    511       C  
ATOM   4831  C   TYR B 305     -11.686  -9.335  37.973  1.00 46.47           C  
ANISOU 4831  C   TYR B 305     3784   5416   8454    197    157    534       C  
ATOM   4832  O   TYR B 305     -12.079  -9.764  36.868  1.00 46.85           O  
ANISOU 4832  O   TYR B 305     3815   5441   8545    181    192    490       O  
ATOM   4833  CB  TYR B 305     -13.313 -10.059  39.734  1.00 44.42           C  
ANISOU 4833  CB  TYR B 305     3622   5058   8195    201    253    520       C  
ATOM   4834  CG  TYR B 305     -14.338  -9.720  40.784  1.00 43.84           C  
ANISOU 4834  CG  TYR B 305     3593   4956   8108    184    271    503       C  
ATOM   4835  CD1 TYR B 305     -13.980  -9.582  42.114  1.00 44.03           C  
ANISOU 4835  CD1 TYR B 305     3661   4988   8079    216    257    555       C  
ATOM   4836  CD2 TYR B 305     -15.670  -9.557  40.453  1.00 43.44           C  
ANISOU 4836  CD2 TYR B 305     3537   4874   8094    138    302    436       C  
ATOM   4837  CE1 TYR B 305     -14.916  -9.282  43.089  1.00 43.88           C  
ANISOU 4837  CE1 TYR B 305     3688   4941   8043    205    280    540       C  
ATOM   4838  CE2 TYR B 305     -16.620  -9.259  41.417  1.00 43.41           C  
ANISOU 4838  CE2 TYR B 305     3569   4846   8077    126    326    422       C  
ATOM   4839  CZ  TYR B 305     -16.243  -9.122  42.742  1.00 43.69           C  
ANISOU 4839  CZ  TYR B 305     3656   4884   8059    160    318    474       C  
ATOM   4840  OH  TYR B 305     -17.164  -8.827  43.710  1.00 43.81           O  
ANISOU 4840  OH  TYR B 305     3712   4876   8057    153    346    462       O  
ATOM   4841  N   LYS B 306     -10.409  -9.246  38.347  1.00 49.47           N  
ANISOU 4841  N   LYS B 306     4146   5851   8797    234    115    599       N  
ATOM   4842  CA  LYS B 306      -9.255  -9.781  37.570  1.00 51.56           C  
ANISOU 4842  CA  LYS B 306     4368   6153   9069    273    118    635       C  
ATOM   4843  C   LYS B 306      -9.269 -11.314  37.680  1.00 53.07           C  
ANISOU 4843  C   LYS B 306     4598   6282   9282    333    213    656       C  
ATOM   4844  O   LYS B 306      -9.560 -11.831  38.794  1.00 53.56           O  
ANISOU 4844  O   LYS B 306     4715   6305   9328    363    250    681       O  
ATOM   4845  CB  LYS B 306      -7.964  -9.182  38.139  1.00 52.49           C  
ANISOU 4845  CB  LYS B 306     4450   6356   9137    293     43    700       C  
ATOM   4846  CG  LYS B 306      -6.917  -8.738  37.133  1.00 53.47           C  
ANISOU 4846  CG  LYS B 306     4502   6552   9262    284     -2    715       C  
ATOM   4847  CD  LYS B 306      -5.842  -7.908  37.802  1.00 54.12           C  
ANISOU 4847  CD  LYS B 306     4545   6723   9293    277    -86    766       C  
ATOM   4848  CE  LYS B 306      -4.631  -7.729  36.921  1.00 55.41           C  
ANISOU 4848  CE  LYS B 306     4630   6965   9458    282   -117    797       C  
ATOM   4849  NZ  LYS B 306      -4.968  -6.998  35.675  1.00 55.74           N  
ANISOU 4849  NZ  LYS B 306     4650   7002   9526    221   -130    746       N  
ATOM   4850  N   GLU B 307      -9.009 -12.022  36.579  1.00 54.21           N  
ANISOU 4850  N   GLU B 307     4725   6411   9459    351    255    644       N  
ATOM   4851  CA  GLU B 307      -8.919 -13.511  36.577  1.00 56.67           C  
ANISOU 4851  CA  GLU B 307     5084   6657   9790    411    351    664       C  
ATOM   4852  C   GLU B 307      -7.972 -13.969  35.465  1.00 57.88           C  
ANISOU 4852  C   GLU B 307     5200   6836   9955    451    365    680       C  
ATOM   4853  O   GLU B 307      -7.878 -13.274  34.452  1.00 57.33           O  
ANISOU 4853  O   GLU B 307     5080   6808   9895    410    322    646       O  
ATOM   4854  CB  GLU B 307     -10.297 -14.168  36.409  1.00 57.23           C  
ANISOU 4854  CB  GLU B 307     5210   6630   9904    371    429    597       C  
ATOM   4855  CG  GLU B 307     -10.321 -15.667  36.717  1.00 57.96           C  
ANISOU 4855  CG  GLU B 307     5373   6638  10010    425    534    620       C  
ATOM   4856  CD  GLU B 307     -10.035 -16.047  38.165  1.00 58.93           C  
ANISOU 4856  CD  GLU B 307     5547   6748  10096    484    555    690       C  
ATOM   4857  OE1 GLU B 307      -8.851 -16.072  38.559  1.00 61.13           O  
ANISOU 4857  OE1 GLU B 307     5806   7083  10335    556    523    764       O  
ATOM   4858  OE2 GLU B 307     -10.993 -16.308  38.906  1.00 59.19           O  
ANISOU 4858  OE2 GLU B 307     5635   6718  10136    459    602    672       O  
ATOM   4859  N   ASN B 308      -7.303 -15.105  35.664  1.00 59.82           N  
ANISOU 4859  N   ASN B 308     5475   7056  10196    535    427    732       N  
ATOM   4860  CA  ASN B 308      -6.400 -15.750  34.672  1.00 60.88           C  
ANISOU 4860  CA  ASN B 308     5586   7205  10340    591    460    753       C  
ATOM   4861  C   ASN B 308      -7.003 -17.107  34.295  1.00 60.83           C  
ANISOU 4861  C   ASN B 308     5661   7085  10367    612    572    721       C  
ATOM   4862  O   ASN B 308      -7.435 -17.282  33.133  1.00 59.53           O  
ANISOU 4862  O   ASN B 308     5497   6887  10233    572    599    657       O  
ATOM   4863  CB  ASN B 308      -4.991 -15.937  35.252  1.00 62.56           C  
ANISOU 4863  CB  ASN B 308     5764   7492  10512    684    439    849       C  
ATOM   4864  CG  ASN B 308      -3.914 -15.135  34.558  1.00 63.66           C  
ANISOU 4864  CG  ASN B 308     5806   7743  10638    683    368    873       C  
ATOM   4865  OD1 ASN B 308      -3.276 -14.278  35.172  1.00 65.15           O  
ANISOU 4865  OD1 ASN B 308     5938   8022  10792    675    287    914       O  
ATOM   4866  ND2 ASN B 308      -3.689 -15.425  33.287  1.00 63.96           N  
ANISOU 4866  ND2 ASN B 308     5825   7775  10700    689    401    848       N  
ATOM   4867  N   SER B 309      -7.031 -18.005  35.284  1.00 60.52           N  
ANISOU 4867  N   SER B 309     5690   6986  10316    670    635    765       N  
ATOM   4868  CA  SER B 309      -7.491 -19.410  35.203  1.00 60.29           C  
ANISOU 4868  CA  SER B 309     5756   6837  10312    700    753    751       C  
ATOM   4869  C   SER B 309      -7.895 -19.861  36.611  1.00 60.25           C  
ANISOU 4869  C   SER B 309     5824   6777  10289    726    793    789       C  
ATOM   4870  O   SER B 309      -7.037 -19.820  37.512  1.00 59.97           O  
ANISOU 4870  O   SER B 309     5781   6795  10210    804    765    872       O  
ATOM   4871  CB  SER B 309      -6.428 -20.296  34.617  1.00 60.99           C  
ANISOU 4871  CB  SER B 309     5855   6922  10394    798    804    797       C  
ATOM   4872  OG  SER B 309      -6.994 -21.513  34.168  1.00 61.43           O  
ANISOU 4872  OG  SER B 309     6004   6854  10481    802    915    758       O  
ATOM   4873  N   TYR B 310      -9.169 -20.223  36.795  1.00 60.11           N  
ANISOU 4873  N   TYR B 310     5869   6666  10303    658    852    730       N  
ATOM   4874  CA  TYR B 310      -9.721 -20.764  38.063  1.00 61.50           C  
ANISOU 4874  CA  TYR B 310     6126   6771  10467    672    911    759       C  
ATOM   4875  C   TYR B 310     -10.180 -22.206  37.856  1.00 63.01           C  
ANISOU 4875  C   TYR B 310     6422   6828  10688    685   1043    741       C  
ATOM   4876  O   TYR B 310     -10.699 -22.519  36.767  1.00 63.63           O  
ANISOU 4876  O   TYR B 310     6505   6861  10810    625   1078    666       O  
ATOM   4877  CB  TYR B 310     -10.906 -19.944  38.577  1.00 60.83           C  
ANISOU 4877  CB  TYR B 310     6029   6689  10392    576    878    706       C  
ATOM   4878  CG  TYR B 310     -11.499 -20.468  39.862  1.00 61.36           C  
ANISOU 4878  CG  TYR B 310     6181   6687  10447    587    944    735       C  
ATOM   4879  CD1 TYR B 310     -10.869 -20.267  41.082  1.00 61.63           C  
ANISOU 4879  CD1 TYR B 310     6230   6762  10423    659    913    817       C  
ATOM   4880  CD2 TYR B 310     -12.690 -21.172  39.862  1.00 62.51           C  
ANISOU 4880  CD2 TYR B 310     6390   6726  10634    524   1039    679       C  
ATOM   4881  CE1 TYR B 310     -11.410 -20.742  42.266  1.00 62.23           C  
ANISOU 4881  CE1 TYR B 310     6389   6773  10480    674    976    846       C  
ATOM   4882  CE2 TYR B 310     -13.252 -21.647  41.038  1.00 63.26           C  
ANISOU 4882  CE2 TYR B 310     6564   6754  10715    531   1107    707       C  
ATOM   4883  CZ  TYR B 310     -12.607 -21.436  42.246  1.00 62.75           C  
ANISOU 4883  CZ  TYR B 310     6521   6730  10591    610   1077    793       C  
ATOM   4884  OH  TYR B 310     -13.155 -21.909  43.401  1.00 62.97           O  
ANISOU 4884  OH  TYR B 310     6633   6690  10600    621   1148    823       O  
ATOM   4885  N   THR B 311      -9.965 -23.042  38.876  1.00 64.25           N  
ANISOU 4885  N   THR B 311     6665   6925  10819    761   1112    809       N  
ATOM   4886  CA  THR B 311     -10.561 -24.394  39.015  1.00 65.67           C  
ANISOU 4886  CA  THR B 311     6967   6959  11023    764   1249    798       C  
ATOM   4887  C   THR B 311     -10.967 -24.592  40.483  1.00 67.60           C  
ANISOU 4887  C   THR B 311     7282   7163  11240    784   1287    848       C  
ATOM   4888  O   THR B 311     -10.157 -24.254  41.376  1.00 68.49           O  
ANISOU 4888  O   THR B 311     7380   7346  11296    870   1235    932       O  
ATOM   4889  CB  THR B 311      -9.613 -25.468  38.470  1.00 65.83           C  
ANISOU 4889  CB  THR B 311     7042   6932  11036    868   1317    841       C  
ATOM   4890  OG1 THR B 311      -9.093 -25.023  37.215  1.00 64.90           O  
ANISOU 4890  OG1 THR B 311     6840   6883  10932    858   1259    807       O  
ATOM   4891  CG2 THR B 311     -10.302 -26.801  38.288  1.00 66.71           C  
ANISOU 4891  CG2 THR B 311     7281   6883  11181    848   1458    807       C  
ATOM   4892  N   THR B 312     -12.196 -25.073  40.719  1.00 68.29           N  
ANISOU 4892  N   THR B 312     7437   7148  11362    701   1371    795       N  
ATOM   4893  CA  THR B 312     -12.801 -25.260  42.069  1.00 68.28           C  
ANISOU 4893  CA  THR B 312     7506   7096  11339    701   1421    830       C  
ATOM   4894  C   THR B 312     -12.328 -26.580  42.679  1.00 69.78           C  
ANISOU 4894  C   THR B 312     7826   7183  11502    805   1534    908       C  
ATOM   4895  O   THR B 312     -12.077 -27.529  41.901  1.00 69.82           O  
ANISOU 4895  O   THR B 312     7887   7110  11532    830   1609    897       O  
ATOM   4896  CB  THR B 312     -14.334 -25.263  42.030  1.00 67.91           C  
ANISOU 4896  CB  THR B 312     7472   6984  11344    565   1474    741       C  
ATOM   4897  OG1 THR B 312     -14.767 -25.364  43.390  1.00 67.78           O  
ANISOU 4897  OG1 THR B 312     7520   6934  11298    578   1518    787       O  
ATOM   4898  CG2 THR B 312     -14.926 -26.393  41.208  1.00 68.69           C  
ANISOU 4898  CG2 THR B 312     7641   6960  11498    507   1587    678       C  
ATOM   4899  N   THR B 313     -12.268 -26.642  44.015  1.00 71.18           N  
ANISOU 4899  N   THR B 313     8059   7353  11630    863   1551    982       N  
ATOM   4900  CA  THR B 313     -11.938 -27.866  44.797  1.00 73.57           C  
ANISOU 4900  CA  THR B 313     8501   7552  11899    966   1665   1064       C  
ATOM   4901  C   THR B 313     -13.237 -28.493  45.330  1.00 75.44           C  
ANISOU 4901  C   THR B 313     8838   7658  12166    881   1786   1029       C  
ATOM   4902  O   THR B 313     -13.295 -28.775  46.538  1.00 77.57           O  
ANISOU 4902  O   THR B 313     9188   7893  12389    934   1832   1097       O  
ATOM   4903  CB  THR B 313     -10.905 -27.544  45.890  1.00 73.56           C  
ANISOU 4903  CB  THR B 313     8494   7640  11813   1099   1600   1175       C  
ATOM   4904  OG1 THR B 313     -11.500 -26.660  46.843  1.00 71.58           O  
ANISOU 4904  OG1 THR B 313     8217   7442  11538   1047   1546   1171       O  
ATOM   4905  CG2 THR B 313      -9.636 -26.928  45.335  1.00 73.13           C  
ANISOU 4905  CG2 THR B 313     8330   7721  11734   1171   1483   1207       C  
ATOM   4906  N   ILE B 314     -14.226 -28.711  44.453  1.00 75.54           N  
ANISOU 4906  N   ILE B 314     8845   7605  12251    751   1835    926       N  
ATOM   4907  CA  ILE B 314     -15.591 -29.233  44.766  1.00 75.79           C  
ANISOU 4907  CA  ILE B 314     8948   7524  12325    638   1947    872       C  
ATOM   4908  C   ILE B 314     -15.952 -30.242  43.672  1.00 75.97           C  
ANISOU 4908  C   ILE B 314     9027   7430  12407    574   2043    802       C  
ATOM   4909  O   ILE B 314     -15.910 -29.903  42.480  1.00 73.52           O  
ANISOU 4909  O   ILE B 314     8634   7167  12132    523   1984    731       O  
ATOM   4910  CB  ILE B 314     -16.643 -28.101  44.840  1.00 75.32           C  
ANISOU 4910  CB  ILE B 314     8782   7542  12293    514   1877    798       C  
ATOM   4911  CG1 ILE B 314     -16.427 -27.152  46.022  1.00 75.03           C  
ANISOU 4911  CG1 ILE B 314     8711   7600  12195    566   1798    860       C  
ATOM   4912  CG2 ILE B 314     -18.047 -28.686  44.854  1.00 75.57           C  
ANISOU 4912  CG2 ILE B 314     8862   7466  12382    383   1992    725       C  
ATOM   4913  CD1 ILE B 314     -17.078 -25.803  45.849  1.00 74.02           C  
ANISOU 4913  CD1 ILE B 314     8457   7581  12085    476   1693    793       C  
TER    4914      ILE B 314                                                      
ATOM   4915  N   THR C   4     -34.555 -13.503  -7.769  1.00 85.61           N  
ANISOU 4915  N   THR C   4     8465  11523  12540   -213   -992   -637       N  
ATOM   4916  CA  THR C   4     -35.704 -12.868  -7.052  1.00 84.85           C  
ANISOU 4916  CA  THR C   4     8428  11321  12490   -213   -993   -547       C  
ATOM   4917  C   THR C   4     -36.283 -13.841  -6.015  1.00 84.37           C  
ANISOU 4917  C   THR C   4     8390  11170  12493   -141  -1019   -557       C  
ATOM   4918  O   THR C   4     -36.171 -15.069  -6.234  1.00 83.88           O  
ANISOU 4918  O   THR C   4     8310  11120  12438    -96  -1039   -619       O  
ATOM   4919  CB  THR C   4     -36.783 -12.399  -8.041  1.00 84.20           C  
ANISOU 4919  CB  THR C   4     8368  11236  12389   -246   -993   -482       C  
ATOM   4920  OG1 THR C   4     -37.490 -13.537  -8.534  1.00 83.70           O  
ANISOU 4920  OG1 THR C   4     8293  11168  12339   -207  -1021   -513       O  
ATOM   4921  CG2 THR C   4     -36.221 -11.627  -9.216  1.00 84.85           C  
ANISOU 4921  CG2 THR C   4     8434  11408  12396   -312   -967   -474       C  
ATOM   4922  N   ILE C   5     -36.888 -13.317  -4.938  1.00 84.04           N  
ANISOU 4922  N   ILE C   5     8393  11040  12497   -132  -1016   -500       N  
ATOM   4923  CA  ILE C   5     -37.601 -14.121  -3.895  1.00 83.00           C  
ANISOU 4923  CA  ILE C   5     8297  10813  12425    -74  -1033   -495       C  
ATOM   4924  C   ILE C   5     -39.050 -13.645  -3.788  1.00 80.79           C  
ANISOU 4924  C   ILE C   5     8056  10460  12179    -90  -1033   -421       C  
ATOM   4925  O   ILE C   5     -39.354 -12.553  -4.333  1.00 81.01           O  
ANISOU 4925  O   ILE C   5     8089  10507  12184   -137  -1022   -368       O  
ATOM   4926  CB  ILE C   5     -36.891 -14.046  -2.526  1.00 84.94           C  
ANISOU 4926  CB  ILE C   5     8554  11027  12691    -39  -1031   -510       C  
ATOM   4927  CG1 ILE C   5     -37.018 -12.662  -1.878  1.00 85.75           C  
ANISOU 4927  CG1 ILE C   5     8676  11100  12803    -79  -1010   -447       C  
ATOM   4928  CG2 ILE C   5     -35.439 -14.486  -2.659  1.00 85.84           C  
ANISOU 4928  CG2 ILE C   5     8620  11225  12767    -17  -1035   -594       C  
ATOM   4929  CD1 ILE C   5     -36.669 -12.636  -0.411  1.00 85.71           C  
ANISOU 4929  CD1 ILE C   5     8689  11048  12827    -39  -1011   -452       C  
ATOM   4930  N   LYS C   6     -39.875 -14.424  -3.078  1.00 79.00           N  
ANISOU 4930  N   LYS C   6     7860  10152  12001    -50  -1044   -419       N  
ATOM   4931  CA  LYS C   6     -41.316 -14.153  -2.824  1.00 78.19           C  
ANISOU 4931  CA  LYS C   6     7790   9980  11938    -59  -1044   -364       C  
ATOM   4932  C   LYS C   6     -41.486 -13.585  -1.407  1.00 76.36           C  
ANISOU 4932  C   LYS C   6     7594   9672  11744    -48  -1035   -323       C  
ATOM   4933  O   LYS C   6     -40.984 -14.207  -0.445  1.00 76.39           O  
ANISOU 4933  O   LYS C   6     7615   9643  11767     -8  -1035   -351       O  
ATOM   4934  CB  LYS C   6     -42.133 -15.442  -3.001  1.00 78.94           C  
ANISOU 4934  CB  LYS C   6     7892  10039  12063    -33  -1054   -400       C  
ATOM   4935  CG  LYS C   6     -42.754 -15.657  -4.372  1.00 80.22           C  
ANISOU 4935  CG  LYS C   6     8023  10255  12201    -55  -1063   -414       C  
ATOM   4936  CD  LYS C   6     -42.755 -17.121  -4.814  1.00 81.26           C  
ANISOU 4936  CD  LYS C   6     8142  10392  12341    -30  -1070   -487       C  
ATOM   4937  CE  LYS C   6     -43.086 -17.265  -6.283  1.00 82.16           C  
ANISOU 4937  CE  LYS C   6     8212  10584  12418    -53  -1080   -512       C  
ATOM   4938  NZ  LYS C   6     -42.047 -16.660  -7.153  1.00 82.28           N  
ANISOU 4938  NZ  LYS C   6     8193  10698  12370    -74  -1081   -515       N  
ATOM   4939  N   VAL C   7     -42.164 -12.439  -1.288  1.00 74.78           N  
ANISOU 4939  N   VAL C   7     7409   9449  11553    -78  -1028   -260       N  
ATOM   4940  CA  VAL C   7     -42.481 -11.768   0.011  1.00 75.15           C  
ANISOU 4940  CA  VAL C   7     7488   9426  11638    -74  -1019   -219       C  
ATOM   4941  C   VAL C   7     -43.867 -11.121  -0.090  1.00 74.61           C  
ANISOU 4941  C   VAL C   7     7436   9318  11593    -91  -1022   -166       C  
ATOM   4942  O   VAL C   7     -44.475 -11.183  -1.184  1.00 74.67           O  
ANISOU 4942  O   VAL C   7     7429   9359  11582   -103  -1033   -164       O  
ATOM   4943  CB  VAL C   7     -41.403 -10.736   0.405  1.00 75.90           C  
ANISOU 4943  CB  VAL C   7     7576   9548  11712    -94  -1004   -208       C  
ATOM   4944  CG1 VAL C   7     -40.024 -11.365   0.498  1.00 76.13           C  
ANISOU 4944  CG1 VAL C   7     7579   9631  11715    -73  -1004   -272       C  
ATOM   4945  CG2 VAL C   7     -41.372  -9.533  -0.529  1.00 76.48           C  
ANISOU 4945  CG2 VAL C   7     7643   9663  11750   -146   -994   -168       C  
ATOM   4946  N   PHE C   8     -44.339 -10.530   1.018  1.00 73.31           N  
ANISOU 4946  N   PHE C   8     7298   9090  11466    -87  -1015   -130       N  
ATOM   4947  CA  PHE C   8     -45.644  -9.823   1.131  1.00 70.72           C  
ANISOU 4947  CA  PHE C   8     6985   8721  11165    -96  -1019    -85       C  
ATOM   4948  C   PHE C   8     -45.426  -8.361   1.543  1.00 66.38           C  
ANISOU 4948  C   PHE C   8     6449   8156  10613   -117  -1009    -34       C  
ATOM   4949  O   PHE C   8     -44.617  -8.103   2.444  1.00 64.21           O  
ANISOU 4949  O   PHE C   8     6181   7867  10346   -116   -995    -39       O  
ATOM   4950  CB  PHE C   8     -46.557 -10.526   2.140  1.00 72.07           C  
ANISOU 4950  CB  PHE C   8     7174   8822  11385    -75  -1016    -95       C  
ATOM   4951  CG  PHE C   8     -46.948 -11.931   1.757  1.00 73.78           C  
ANISOU 4951  CG  PHE C   8     7385   9038  11610    -63  -1018   -144       C  
ATOM   4952  CD1 PHE C   8     -47.587 -12.181   0.550  1.00 74.90           C  
ANISOU 4952  CD1 PHE C   8     7499   9222  11735    -73  -1031   -159       C  
ATOM   4953  CD2 PHE C   8     -46.684 -12.997   2.603  1.00 74.90           C  
ANISOU 4953  CD2 PHE C   8     7551   9135  11772    -38  -1007   -175       C  
ATOM   4954  CE1 PHE C   8     -47.941 -13.470   0.192  1.00 75.80           C  
ANISOU 4954  CE1 PHE C   8     7605   9334  11858    -67  -1030   -211       C  
ATOM   4955  CE2 PHE C   8     -47.037 -14.287   2.244  1.00 75.78           C  
ANISOU 4955  CE2 PHE C   8     7664   9235  11891    -30  -1005   -221       C  
ATOM   4956  CZ  PHE C   8     -47.669 -14.517   1.044  1.00 76.21           C  
ANISOU 4956  CZ  PHE C   8     7687   9333  11936    -48  -1015   -242       C  
ATOM   4957  N   THR C   9     -46.153  -7.446   0.895  1.00 63.09           N  
ANISOU 4957  N   THR C   9     6040   7743  10187   -131  -1017      8       N  
ATOM   4958  CA  THR C   9     -46.331  -6.036   1.321  1.00 61.10           C  
ANISOU 4958  CA  THR C   9     5813   7456   9945   -145  -1009     60       C  
ATOM   4959  C   THR C   9     -47.764  -5.855   1.831  1.00 60.93           C  
ANISOU 4959  C   THR C   9     5801   7382   9966   -124  -1023     79       C  
ATOM   4960  O   THR C   9     -48.660  -6.591   1.359  1.00 61.27           O  
ANISOU 4960  O   THR C   9     5827   7436  10014   -109  -1040     59       O  
ATOM   4961  CB  THR C   9     -46.009  -5.067   0.183  1.00 60.61           C  
ANISOU 4961  CB  THR C   9     5762   7433   9832   -172  -1007     97       C  
ATOM   4962  OG1 THR C   9     -46.911  -5.309  -0.894  1.00 59.38           O  
ANISOU 4962  OG1 THR C   9     5599   7306   9654   -158  -1032    104       O  
ATOM   4963  CG2 THR C   9     -44.582  -5.205  -0.291  1.00 61.55           C  
ANISOU 4963  CG2 THR C   9     5867   7611   9908   -202   -988     71       C  
ATOM   4964  N   THR C  10     -47.968  -4.919   2.760  1.00 60.67           N  
ANISOU 4964  N   THR C  10     5789   7299   9964   -126  -1015    110       N  
ATOM   4965  CA  THR C  10     -49.296  -4.582   3.340  1.00 60.07           C  
ANISOU 4965  CA  THR C  10     5719   7175   9929   -107  -1026    125       C  
ATOM   4966  C   THR C  10     -49.220  -3.218   4.031  1.00 59.53           C  
ANISOU 4966  C   THR C  10     5676   7062   9878   -115  -1016    166       C  
ATOM   4967  O   THR C  10     -48.101  -2.772   4.329  1.00 60.34           O  
ANISOU 4967  O   THR C  10     5788   7166   9970   -138   -995    171       O  
ATOM   4968  CB  THR C  10     -49.746  -5.684   4.305  1.00 59.62           C  
ANISOU 4968  CB  THR C  10     5651   7088   9912    -94  -1020     85       C  
ATOM   4969  OG1 THR C  10     -51.099  -5.442   4.693  1.00 58.50           O  
ANISOU 4969  OG1 THR C  10     5506   6914   9805    -81  -1030     89       O  
ATOM   4970  CG2 THR C  10     -48.854  -5.776   5.525  1.00 58.85           C  
ANISOU 4970  CG2 THR C  10     5566   6963   9831    -96   -998     76       C  
ATOM   4971  N   VAL C  11     -50.376  -2.592   4.270  1.00 59.60           N  
ANISOU 4971  N   VAL C  11     5692   7037   9914    -96  -1031    187       N  
ATOM   4972  CA  VAL C  11     -50.527  -1.349   5.090  1.00 58.46           C  
ANISOU 4972  CA  VAL C  11     5572   6840   9798    -96  -1024    218       C  
ATOM   4973  C   VAL C  11     -51.229  -1.681   6.411  1.00 56.64           C  
ANISOU 4973  C   VAL C  11     5329   6570   9621    -83  -1020    194       C  
ATOM   4974  O   VAL C  11     -51.041  -0.915   7.364  1.00 55.65           O  
ANISOU 4974  O   VAL C  11     5215   6405   9521    -89  -1006    205       O  
ATOM   4975  CB  VAL C  11     -51.279  -0.245   4.321  1.00 59.38           C  
ANISOU 4975  CB  VAL C  11     5713   6946   9900    -78  -1046    262       C  
ATOM   4976  CG1 VAL C  11     -50.406   0.361   3.231  1.00 60.34           C  
ANISOU 4976  CG1 VAL C  11     5866   7093   9968   -100  -1038    298       C  
ATOM   4977  CG2 VAL C  11     -52.592  -0.743   3.744  1.00 59.95           C  
ANISOU 4977  CG2 VAL C  11     5762   7043   9972    -42  -1080    246       C  
ATOM   4978  N   ASP C  12     -52.000  -2.774   6.449  1.00 56.23           N  
ANISOU 4978  N   ASP C  12     5253   6529   9582    -71  -1028    158       N  
ATOM   4979  CA  ASP C  12     -52.885  -3.155   7.581  1.00 56.64           C  
ANISOU 4979  CA  ASP C  12     5294   6547   9679    -63  -1021    132       C  
ATOM   4980  C   ASP C  12     -52.482  -4.502   8.189  1.00 55.85           C  
ANISOU 4980  C   ASP C  12     5191   6443   9584    -71  -1000     95       C  
ATOM   4981  O   ASP C  12     -52.942  -4.777   9.300  1.00 55.95           O  
ANISOU 4981  O   ASP C  12     5207   6422   9629    -71   -985     79       O  
ATOM   4982  CB  ASP C  12     -54.355  -3.198   7.150  1.00 58.37           C  
ANISOU 4982  CB  ASP C  12     5490   6776   9911    -44  -1044    116       C  
ATOM   4983  CG  ASP C  12     -54.637  -3.908   5.846  1.00 59.40           C  
ANISOU 4983  CG  ASP C  12     5600   6958  10008    -39  -1062     98       C  
ATOM   4984  OD1 ASP C  12     -53.735  -4.605   5.354  1.00 60.54           O  
ANISOU 4984  OD1 ASP C  12     5748   7128  10126    -53  -1054     91       O  
ATOM   4985  OD2 ASP C  12     -55.760  -3.736   5.327  1.00 60.65           O  
ANISOU 4985  OD2 ASP C  12     5736   7138  10168    -18  -1087     85       O  
ATOM   4986  N   ASN C  13     -51.703  -5.323   7.480  1.00 55.77           N  
ANISOU 4986  N   ASN C  13     5180   6467   9542    -76   -999     81       N  
ATOM   4987  CA  ASN C  13     -51.279  -6.682   7.926  1.00 55.88           C  
ANISOU 4987  CA  ASN C  13     5200   6474   9556    -75   -982     46       C  
ATOM   4988  C   ASN C  13     -52.505  -7.605   7.964  1.00 56.57           C  
ANISOU 4988  C   ASN C  13     5279   6548   9667    -78   -977     12       C  
ATOM   4989  O   ASN C  13     -52.511  -8.552   8.773  1.00 57.39           O  
ANISOU 4989  O   ASN C  13     5401   6618   9784    -79   -955    -10       O  
ATOM   4990  CB  ASN C  13     -50.580  -6.644   9.289  1.00 56.03           C  
ANISOU 4990  CB  ASN C  13     5241   6460   9587    -70   -962     47       C  
ATOM   4991  CG  ASN C  13     -49.861  -7.933   9.639  1.00 55.89           C  
ANISOU 4991  CG  ASN C  13     5240   6439   9556    -57   -949     18       C  
ATOM   4992  OD1 ASN C  13     -49.203  -8.540   8.793  1.00 55.72           O  
ANISOU 4992  OD1 ASN C  13     5213   6452   9506    -53   -956      1       O  
ATOM   4993  ND2 ASN C  13     -49.981  -8.362  10.885  1.00 55.46           N  
ANISOU 4993  ND2 ASN C  13     5210   6342   9518    -46   -931     10       N  
ATOM   4994  N   ILE C  14     -53.510  -7.321   7.129  1.00 55.55           N  
ANISOU 4994  N   ILE C  14     5123   6444   9539    -78   -997      7       N  
ATOM   4995  CA  ILE C  14     -54.750  -8.132   6.973  1.00 53.42           C  
ANISOU 4995  CA  ILE C  14     4831   6176   9288    -86   -993    -36       C  
ATOM   4996  C   ILE C  14     -54.897  -8.464   5.485  1.00 53.25           C  
ANISOU 4996  C   ILE C  14     4782   6212   9235    -83  -1015    -54       C  
ATOM   4997  O   ILE C  14     -55.053  -9.658   5.165  1.00 53.56           O  
ANISOU 4997  O   ILE C  14     4814   6260   9275    -95  -1003    -98       O  
ATOM   4998  CB  ILE C  14     -55.954  -7.386   7.583  1.00 53.34           C  
ANISOU 4998  CB  ILE C  14     4805   6148   9311    -84   -996    -37       C  
ATOM   4999  CG1 ILE C  14     -56.078  -7.712   9.077  1.00 52.29           C  
ANISOU 4999  CG1 ILE C  14     4696   5961   9211    -98   -962    -46       C  
ATOM   5000  CG2 ILE C  14     -57.240  -7.681   6.819  1.00 54.17           C  
ANISOU 5000  CG2 ILE C  14     4868   6292   9421    -85  -1011    -81       C  
ATOM   5001  CD1 ILE C  14     -57.278  -7.119   9.767  1.00 51.77           C  
ANISOU 5001  CD1 ILE C  14     4609   5880   9178   -101   -960    -59       C  
ATOM   5002  N   ASN C  15     -54.819  -7.448   4.621  1.00 52.99           N  
ANISOU 5002  N   ASN C  15     4740   6216   9175    -67  -1045    -20       N  
ATOM   5003  CA  ASN C  15     -54.732  -7.600   3.146  1.00 53.99           C  
ANISOU 5003  CA  ASN C  15     4847   6407   9259    -60  -1069    -27       C  
ATOM   5004  C   ASN C  15     -53.256  -7.708   2.758  1.00 54.58           C  
ANISOU 5004  C   ASN C  15     4940   6497   9298    -68  -1062     -7       C  
ATOM   5005  O   ASN C  15     -52.608  -6.642   2.630  1.00 55.78           O  
ANISOU 5005  O   ASN C  15     5112   6651   9429    -66  -1067     40       O  
ATOM   5006  CB  ASN C  15     -55.434  -6.450   2.422  1.00 54.66           C  
ANISOU 5006  CB  ASN C  15     4920   6521   9324    -34  -1103      1       C  
ATOM   5007  CG  ASN C  15     -56.923  -6.408   2.702  1.00 54.93           C  
ANISOU 5007  CG  ASN C  15     4924   6557   9390    -20  -1115    -33       C  
ATOM   5008  OD1 ASN C  15     -57.333  -5.975   3.776  1.00 53.91           O  
ANISOU 5008  OD1 ASN C  15     4801   6382   9298    -21  -1104    -28       O  
ATOM   5009  ND2 ASN C  15     -57.735  -6.893   1.767  1.00 55.15           N  
ANISOU 5009  ND2 ASN C  15     4910   6642   9401    -10  -1135    -77       N  
ATOM   5010  N   LEU C  16     -52.746  -8.939   2.611  1.00 54.70           N  
ANISOU 5010  N   LEU C  16     4952   6521   9308    -77  -1048    -46       N  
ATOM   5011  CA  LEU C  16     -51.343  -9.241   2.210  1.00 54.84           C  
ANISOU 5011  CA  LEU C  16     4980   6565   9292    -81  -1043    -44       C  
ATOM   5012  C   LEU C  16     -51.256  -9.256   0.681  1.00 55.54           C  
ANISOU 5012  C   LEU C  16     5043   6725   9332    -81  -1064    -50       C  
ATOM   5013  O   LEU C  16     -52.049  -9.979   0.072  1.00 55.97           O  
ANISOU 5013  O   LEU C  16     5070   6805   9387    -79  -1073    -90       O  
ATOM   5014  CB  LEU C  16     -50.924 -10.601   2.780  1.00 55.20           C  
ANISOU 5014  CB  LEU C  16     5036   6583   9354    -81  -1022    -88       C  
ATOM   5015  CG  LEU C  16     -51.038 -10.772   4.296  1.00 55.27           C  
ANISOU 5015  CG  LEU C  16     5075   6521   9403    -78   -999    -85       C  
ATOM   5016  CD1 LEU C  16     -50.438 -12.095   4.735  1.00 55.82           C  
ANISOU 5016  CD1 LEU C  16     5169   6564   9475    -69   -980   -121       C  
ATOM   5017  CD2 LEU C  16     -50.364  -9.626   5.031  1.00 55.29           C  
ANISOU 5017  CD2 LEU C  16     5093   6508   9403    -75   -997    -40       C  
ATOM   5018  N   HIS C  17     -50.319  -8.502   0.093  1.00 57.06           N  
ANISOU 5018  N   HIS C  17     5244   6951   9482    -87  -1068    -16       N  
ATOM   5019  CA  HIS C  17     -50.137  -8.359  -1.379  1.00 58.74           C  
ANISOU 5019  CA  HIS C  17     5441   7237   9639    -89  -1086    -12       C  
ATOM   5020  C   HIS C  17     -48.835  -9.051  -1.795  1.00 60.84           C  
ANISOU 5020  C   HIS C  17     5698   7542   9874   -103  -1074    -41       C  
ATOM   5021  O   HIS C  17     -47.771  -8.655  -1.280  1.00 63.34           O  
ANISOU 5021  O   HIS C  17     6032   7848  10186   -115  -1057    -26       O  
ATOM   5022  CB  HIS C  17     -50.200  -6.877  -1.778  1.00 58.06           C  
ANISOU 5022  CB  HIS C  17     5380   7156   9524    -89  -1096     51       C  
ATOM   5023  CG  HIS C  17     -51.479  -6.231  -1.366  1.00 57.74           C  
ANISOU 5023  CG  HIS C  17     5345   7080   9513    -66  -1113     72       C  
ATOM   5024  ND1 HIS C  17     -52.524  -6.025  -2.240  1.00 57.49           N  
ANISOU 5024  ND1 HIS C  17     5297   7085   9459    -39  -1143     72       N  
ATOM   5025  CD2 HIS C  17     -51.894  -5.772  -0.168  1.00 57.06           C  
ANISOU 5025  CD2 HIS C  17     5272   6929   9475    -61  -1105     86       C  
ATOM   5026  CE1 HIS C  17     -53.518  -5.440  -1.603  1.00 57.37           C  
ANISOU 5026  CE1 HIS C  17     5286   7031   9478    -18  -1155     84       C  
ATOM   5027  NE2 HIS C  17     -53.161  -5.282  -0.328  1.00 56.29           N  
ANISOU 5027  NE2 HIS C  17     5168   6831   9388    -33  -1130     93       N  
ATOM   5028  N   THR C  18     -48.923 -10.059  -2.672  1.00 61.70           N  
ANISOU 5028  N   THR C  18     5778   7700   9965   -100  -1083    -89       N  
ATOM   5029  CA  THR C  18     -47.787 -10.934  -3.063  1.00 62.20           C  
ANISOU 5029  CA  THR C  18     5827   7802  10004   -106  -1074   -132       C  
ATOM   5030  C   THR C  18     -46.870 -10.165  -4.021  1.00 63.70           C  
ANISOU 5030  C   THR C  18     6013   8057  10130   -125  -1074   -106       C  
ATOM   5031  O   THR C  18     -47.387  -9.466  -4.918  1.00 63.68           O  
ANISOU 5031  O   THR C  18     6012   8090  10092   -129  -1089    -74       O  
ATOM   5032  CB  THR C  18     -48.254 -12.261  -3.673  1.00 62.51           C  
ANISOU 5032  CB  THR C  18     5836   7866  10048    -98  -1081   -196       C  
ATOM   5033  OG1 THR C  18     -49.419 -12.711  -2.984  1.00 62.88           O  
ANISOU 5033  OG1 THR C  18     5887   7856  10146    -91  -1078   -212       O  
ATOM   5034  CG2 THR C  18     -47.194 -13.336  -3.588  1.00 62.75           C  
ANISOU 5034  CG2 THR C  18     5861   7903  10075    -93  -1071   -247       C  
ATOM   5035  N   GLN C  19     -45.556 -10.290  -3.817  1.00 64.51           N  
ANISOU 5035  N   GLN C  19     6114   8177  10217   -137  -1058   -123       N  
ATOM   5036  CA  GLN C  19     -44.524  -9.486  -4.515  1.00 66.05           C  
ANISOU 5036  CA  GLN C  19     6310   8430  10356   -168  -1046   -103       C  
ATOM   5037  C   GLN C  19     -43.298 -10.360  -4.825  1.00 66.82           C  
ANISOU 5037  C   GLN C  19     6376   8585  10428   -171  -1039   -167       C  
ATOM   5038  O   GLN C  19     -43.033 -11.315  -4.066  1.00 65.10           O  
ANISOU 5038  O   GLN C  19     6152   8338  10245   -144  -1039   -212       O  
ATOM   5039  CB  GLN C  19     -44.161  -8.277  -3.651  1.00 66.03           C  
ANISOU 5039  CB  GLN C  19     6339   8381  10365   -186  -1027    -54       C  
ATOM   5040  CG  GLN C  19     -45.315  -7.312  -3.415  1.00 64.89           C  
ANISOU 5040  CG  GLN C  19     6228   8184  10242   -179  -1036      7       C  
ATOM   5041  CD  GLN C  19     -45.645  -6.438  -4.598  1.00 65.28           C  
ANISOU 5041  CD  GLN C  19     6294   8270  10237   -191  -1043     54       C  
ATOM   5042  OE1 GLN C  19     -46.632  -5.714  -4.583  1.00 66.14           O  
ANISOU 5042  OE1 GLN C  19     6429   8345  10355   -175  -1058     99       O  
ATOM   5043  NE2 GLN C  19     -44.815  -6.478  -5.625  1.00 65.47           N  
ANISOU 5043  NE2 GLN C  19     6308   8365  10201   -218  -1034     42       N  
ATOM   5044  N   VAL C  20     -42.596 -10.031  -5.914  1.00 68.64           N  
ANISOU 5044  N   VAL C  20     6590   8892  10596   -201  -1032   -170       N  
ATOM   5045  CA  VAL C  20     -41.364 -10.718  -6.407  1.00 71.08           C  
ANISOU 5045  CA  VAL C  20     6861   9275  10869   -209  -1024   -235       C  
ATOM   5046  C   VAL C  20     -40.249  -9.665  -6.471  1.00 72.42           C  
ANISOU 5046  C   VAL C  20     7036   9481  10998   -256   -994   -217       C  
ATOM   5047  O   VAL C  20     -40.211  -8.897  -7.458  1.00 71.95           O  
ANISOU 5047  O   VAL C  20     6986   9466  10884   -295   -983   -182       O  
ATOM   5048  CB  VAL C  20     -41.614 -11.405  -7.770  1.00 71.49           C  
ANISOU 5048  CB  VAL C  20     6882   9400  10880   -209  -1040   -268       C  
ATOM   5049  CG1 VAL C  20     -40.359 -11.496  -8.641  1.00 71.15           C  
ANISOU 5049  CG1 VAL C  20     6804   9453  10774   -238  -1026   -311       C  
ATOM   5050  CG2 VAL C  20     -42.250 -12.781  -7.609  1.00 70.92           C  
ANISOU 5050  CG2 VAL C  20     6793   9303  10851   -167  -1060   -322       C  
ATOM   5051  N   VAL C  21     -39.379  -9.628  -5.456  1.00 74.68           N  
ANISOU 5051  N   VAL C  21     7317   9751  11307   -254   -980   -243       N  
ATOM   5052  CA  VAL C  21     -38.362  -8.547  -5.262  1.00 76.27           C  
ANISOU 5052  CA  VAL C  21     7522   9976  11481   -304   -945   -232       C  
ATOM   5053  C   VAL C  21     -37.055  -8.951  -5.954  1.00 78.45           C  
ANISOU 5053  C   VAL C  21     7748  10353  11704   -328   -931   -304       C  
ATOM   5054  O   VAL C  21     -36.610 -10.105  -5.750  1.00 77.44           O  
ANISOU 5054  O   VAL C  21     7583  10251  11587   -285   -950   -376       O  
ATOM   5055  CB  VAL C  21     -38.134  -8.213  -3.771  1.00 76.34           C  
ANISOU 5055  CB  VAL C  21     7544   9921  11539   -289   -937   -229       C  
ATOM   5056  CG1 VAL C  21     -39.290  -7.411  -3.196  1.00 77.26           C  
ANISOU 5056  CG1 VAL C  21     7710   9948  11696   -286   -940   -152       C  
ATOM   5057  CG2 VAL C  21     -37.879  -9.450  -2.916  1.00 75.79           C  
ANISOU 5057  CG2 VAL C  21     7453   9838  11505   -228   -959   -290       C  
ATOM   5058  N   ASP C  22     -36.481  -8.026  -6.740  1.00 82.02           N  
ANISOU 5058  N   ASP C  22     8203  10859  12099   -394   -897   -287       N  
ATOM   5059  CA  ASP C  22     -35.139  -8.134  -7.377  1.00 83.90           C  
ANISOU 5059  CA  ASP C  22     8393  11203  12281   -436   -872   -356       C  
ATOM   5060  C   ASP C  22     -34.087  -8.036  -6.264  1.00 84.72           C  
ANISOU 5060  C   ASP C  22     8468  11313  12407   -436   -856   -411       C  
ATOM   5061  O   ASP C  22     -34.118  -7.045  -5.497  1.00 84.81           O  
ANISOU 5061  O   ASP C  22     8512  11271  12441   -462   -833   -370       O  
ATOM   5062  CB  ASP C  22     -34.959  -7.062  -8.460  1.00 84.70           C  
ANISOU 5062  CB  ASP C  22     8519  11345  12315   -515   -833   -310       C  
ATOM   5063  CG  ASP C  22     -33.669  -7.147  -9.264  1.00 85.47           C  
ANISOU 5063  CG  ASP C  22     8568  11560  12347   -570   -800   -381       C  
ATOM   5064  OD1 ASP C  22     -32.788  -7.951  -8.898  1.00 85.13           O  
ANISOU 5064  OD1 ASP C  22     8463  11570  12311   -546   -808   -473       O  
ATOM   5065  OD2 ASP C  22     -33.553  -6.394 -10.249  1.00 86.45           O  
ANISOU 5065  OD2 ASP C  22     8717  11721  12409   -635   -767   -345       O  
ATOM   5066  N   MET C  23     -33.201  -9.032  -6.181  1.00 85.11           N  
ANISOU 5066  N   MET C  23     8459  11428  12448   -402   -869   -505       N  
ATOM   5067  CA  MET C  23     -32.218  -9.194  -5.076  1.00 84.94           C  
ANISOU 5067  CA  MET C  23     8402  11422  12446   -377   -867   -573       C  
ATOM   5068  C   MET C  23     -31.178  -8.070  -5.109  1.00 83.47           C  
ANISOU 5068  C   MET C  23     8196  11295  12223   -460   -815   -595       C  
ATOM   5069  O   MET C  23     -30.791  -7.614  -4.015  1.00 84.73           O  
ANISOU 5069  O   MET C  23     8353  11430  12410   -457   -804   -608       O  
ATOM   5070  CB  MET C  23     -31.508 -10.547  -5.169  1.00 86.01           C  
ANISOU 5070  CB  MET C  23     8482  11625  12572   -314   -898   -673       C  
ATOM   5071  CG  MET C  23     -32.373 -11.709  -4.737  1.00 85.86           C  
ANISOU 5071  CG  MET C  23     8488  11532  12601   -227   -944   -665       C  
ATOM   5072  SD  MET C  23     -32.662 -11.692  -2.952  1.00 87.25           S  
ANISOU 5072  SD  MET C  23     8702  11607  12841   -166   -959   -641       S  
ATOM   5073  CE  MET C  23     -32.155 -13.360  -2.542  1.00 87.16           C  
ANISOU 5073  CE  MET C  23     8668  11608  12838    -60  -1002   -731       C  
ATOM   5074  N   SER C  24     -30.742  -7.647  -6.300  1.00 82.68           N  
ANISOU 5074  N   SER C  24     8082  11269  12060   -534   -781   -602       N  
ATOM   5075  CA  SER C  24     -29.725  -6.576  -6.488  1.00 84.43           C  
ANISOU 5075  CA  SER C  24     8288  11551  12240   -631   -719   -628       C  
ATOM   5076  C   SER C  24     -30.247  -5.268  -5.880  1.00 85.24           C  
ANISOU 5076  C   SER C  24     8456  11558  12370   -675   -687   -540       C  
ATOM   5077  O   SER C  24     -29.624  -4.765  -4.925  1.00 85.12           O  
ANISOU 5077  O   SER C  24     8425  11540  12377   -692   -665   -575       O  
ATOM   5078  CB  SER C  24     -29.350  -6.401  -7.941  1.00 84.08           C  
ANISOU 5078  CB  SER C  24     8232  11593  12121   -703   -686   -637       C  
ATOM   5079  OG  SER C  24     -30.190  -5.451  -8.581  1.00 84.55           O  
ANISOU 5079  OG  SER C  24     8369  11593  12161   -754   -662   -528       O  
ATOM   5080  N   MET C  25     -31.369  -4.767  -6.407  1.00 86.54           N  
ANISOU 5080  N   MET C  25     8694  11651  12536   -686   -690   -436       N  
ATOM   5081  CA  MET C  25     -32.033  -3.511  -5.966  1.00 86.36           C  
ANISOU 5081  CA  MET C  25     8745  11527  12538   -720   -665   -343       C  
ATOM   5082  C   MET C  25     -32.426  -3.657  -4.492  1.00 83.74           C  
ANISOU 5082  C   MET C  25     8416  11120  12282   -656   -694   -341       C  
ATOM   5083  O   MET C  25     -32.746  -4.788  -4.079  1.00 80.39           O  
ANISOU 5083  O   MET C  25     7964  10689  11889   -573   -745   -370       O  
ATOM   5084  CB  MET C  25     -33.278  -3.225  -6.812  1.00 88.94           C  
ANISOU 5084  CB  MET C  25     9141  11799  12851   -713   -680   -242       C  
ATOM   5085  CG  MET C  25     -32.959  -2.925  -8.275  1.00 91.99           C  
ANISOU 5085  CG  MET C  25     9540  12255  13154   -779   -647   -229       C  
ATOM   5086  SD  MET C  25     -34.433  -2.893  -9.345  1.00 96.54           S  
ANISOU 5086  SD  MET C  25    10183  12790  13704   -742   -683   -127       S  
ATOM   5087  CE  MET C  25     -33.799  -2.037 -10.790  1.00 96.17           C  
ANISOU 5087  CE  MET C  25    10175  12811  13553   -844   -621   -100       C  
ATOM   5088  N   THR C  26     -32.373  -2.559  -3.730  1.00 82.98           N  
ANISOU 5088  N   THR C  26     8351  10965  12211   -696   -661   -312       N  
ATOM   5089  CA  THR C  26     -32.863  -2.486  -2.328  1.00 81.42           C  
ANISOU 5089  CA  THR C  26     8165  10687  12083   -643   -684   -297       C  
ATOM   5090  C   THR C  26     -34.391  -2.542  -2.346  1.00 78.94           C  
ANISOU 5090  C   THR C  26     7910  10278  11803   -591   -722   -205       C  
ATOM   5091  O   THR C  26     -34.977  -2.465  -3.447  1.00 76.80           O  
ANISOU 5091  O   THR C  26     7672  10008  11500   -604   -727   -154       O  
ATOM   5092  CB  THR C  26     -32.413  -1.203  -1.614  1.00 82.72           C  
ANISOU 5092  CB  THR C  26     8347  10819  12262   -707   -633   -292       C  
ATOM   5093  OG1 THR C  26     -32.957  -0.091  -2.329  1.00 84.43           O  
ANISOU 5093  OG1 THR C  26     8638  10979  12459   -769   -599   -204       O  
ATOM   5094  CG2 THR C  26     -30.909  -1.070  -1.508  1.00 83.39           C  
ANISOU 5094  CG2 THR C  26     8366  11002  12315   -764   -590   -394       C  
ATOM   5095  N   TYR C  27     -35.005  -2.643  -1.168  1.00 77.00           N  
ANISOU 5095  N   TYR C  27     7676   9961  11619   -537   -748   -188       N  
ATOM   5096  CA  TYR C  27     -36.477  -2.580  -0.996  1.00 77.17           C  
ANISOU 5096  CA  TYR C  27     7749   9890  11680   -493   -780   -109       C  
ATOM   5097  C   TYR C  27     -36.970  -1.198  -1.459  1.00 78.75           C  
ANISOU 5097  C   TYR C  27     8015  10037  11869   -546   -751    -28       C  
ATOM   5098  O   TYR C  27     -37.836  -1.139  -2.359  1.00 80.98           O  
ANISOU 5098  O   TYR C  27     8333  10303  12130   -536   -768     28       O  
ATOM   5099  CB  TYR C  27     -36.861  -2.907   0.451  1.00 75.40           C  
ANISOU 5099  CB  TYR C  27     7520   9609  11518   -435   -804   -119       C  
ATOM   5100  CG  TYR C  27     -36.809  -4.376   0.794  1.00 72.15           C  
ANISOU 5100  CG  TYR C  27     7071   9222  11119   -364   -843   -173       C  
ATOM   5101  CD1 TYR C  27     -35.969  -4.865   1.783  1.00 71.28           C  
ANISOU 5101  CD1 TYR C  27     6923   9138  11020   -333   -846   -239       C  
ATOM   5102  CD2 TYR C  27     -37.613  -5.283   0.131  1.00 70.10           C  
ANISOU 5102  CD2 TYR C  27     6817   8958  10858   -326   -875   -159       C  
ATOM   5103  CE1 TYR C  27     -35.927  -6.214   2.103  1.00 69.98           C  
ANISOU 5103  CE1 TYR C  27     6739   8985  10863   -261   -881   -284       C  
ATOM   5104  CE2 TYR C  27     -37.588  -6.632   0.438  1.00 69.77           C  
ANISOU 5104  CE2 TYR C  27     6751   8926  10829   -264   -905   -207       C  
ATOM   5105  CZ  TYR C  27     -36.745  -7.100   1.428  1.00 69.29           C  
ANISOU 5105  CZ  TYR C  27     6665   8883  10778   -230   -908   -266       C  
ATOM   5106  OH  TYR C  27     -36.723  -8.430   1.726  1.00 69.39           O  
ANISOU 5106  OH  TYR C  27     6668   8896  10800   -164   -938   -309       O  
ATOM   5107  N   GLY C  28     -36.409  -0.126  -0.883  1.00 78.32           N  
ANISOU 5107  N   GLY C  28     7975   9958  11823   -600   -707    -28       N  
ATOM   5108  CA  GLY C  28     -36.776   1.276  -1.168  1.00 77.16           C  
ANISOU 5108  CA  GLY C  28     7901   9746  11670   -652   -673     45       C  
ATOM   5109  C   GLY C  28     -36.984   1.516  -2.651  1.00 76.12           C  
ANISOU 5109  C   GLY C  28     7810   9636  11474   -682   -663     94       C  
ATOM   5110  O   GLY C  28     -38.080   1.960  -3.031  1.00 73.70           O  
ANISOU 5110  O   GLY C  28     7565   9269  11170   -655   -683    173       O  
ATOM   5111  N   GLN C  29     -35.976   1.208  -3.465  1.00 76.68           N  
ANISOU 5111  N   GLN C  29     7847   9798  11487   -731   -636     45       N  
ATOM   5112  CA  GLN C  29     -36.026   1.382  -4.940  1.00 77.41           C  
ANISOU 5112  CA  GLN C  29     7976   9929  11507   -765   -621     85       C  
ATOM   5113  C   GLN C  29     -37.352   0.827  -5.468  1.00 76.01           C  
ANISOU 5113  C   GLN C  29     7820   9728  11331   -688   -682    138       C  
ATOM   5114  O   GLN C  29     -38.029   1.536  -6.234  1.00 77.84           O  
ANISOU 5114  O   GLN C  29     8122   9924  11529   -692   -680    217       O  
ATOM   5115  CB  GLN C  29     -34.842   0.677  -5.597  1.00 78.70           C  
ANISOU 5115  CB  GLN C  29     8074  10211  11618   -805   -601      2       C  
ATOM   5116  CG  GLN C  29     -33.512   1.374  -5.346  1.00 80.48           C  
ANISOU 5116  CG  GLN C  29     8279  10474  11823   -898   -531    -53       C  
ATOM   5117  CD  GLN C  29     -32.379   0.632  -6.010  1.00 82.61           C  
ANISOU 5117  CD  GLN C  29     8476  10871  12040   -932   -515   -144       C  
ATOM   5118  OE1 GLN C  29     -31.492   0.098  -5.346  1.00 84.10           O  
ANISOU 5118  OE1 GLN C  29     8587  11120  12245   -926   -514   -240       O  
ATOM   5119  NE2 GLN C  29     -32.411   0.588  -7.336  1.00 83.64           N  
ANISOU 5119  NE2 GLN C  29     8629  11048  12102   -962   -503   -118       N  
ATOM   5120  N   GLN C  30     -37.726  -0.373  -5.026  1.00 73.26           N  
ANISOU 5120  N   GLN C  30     7415   9396  11021   -617   -732     96       N  
ATOM   5121  CA  GLN C  30     -38.864  -1.148  -5.578  1.00 70.91           C  
ANISOU 5121  CA  GLN C  30     7117   9099  10724   -550   -787    120       C  
ATOM   5122  C   GLN C  30     -40.192  -0.668  -4.973  1.00 69.72           C  
ANISOU 5122  C   GLN C  30     7013   8852  10625   -500   -817    184       C  
ATOM   5123  O   GLN C  30     -41.170  -0.585  -5.741  1.00 72.37           O  
ANISOU 5123  O   GLN C  30     7380   9179  10938   -468   -845    234       O  
ATOM   5124  CB  GLN C  30     -38.635  -2.638  -5.323  1.00 70.31           C  
ANISOU 5124  CB  GLN C  30     6968   9075  10670   -504   -819     40       C  
ATOM   5125  CG  GLN C  30     -37.319  -3.153  -5.890  1.00 70.99           C  
ANISOU 5125  CG  GLN C  30     7002   9263  10707   -544   -795    -33       C  
ATOM   5126  CD  GLN C  30     -37.106  -4.618  -5.586  1.00 70.42           C  
ANISOU 5126  CD  GLN C  30     6865   9231  10658   -488   -830   -111       C  
ATOM   5127  OE1 GLN C  30     -37.962  -5.459  -5.845  1.00 70.26           O  
ANISOU 5127  OE1 GLN C  30     6839   9203  10653   -436   -870   -109       O  
ATOM   5128  NE2 GLN C  30     -35.952  -4.939  -5.025  1.00 70.35           N  
ANISOU 5128  NE2 GLN C  30     6808   9267  10652   -498   -814   -185       N  
ATOM   5129  N   PHE C  31     -40.238  -0.367  -3.666  1.00 66.97           N  
ANISOU 5129  N   PHE C  31     6664   8440  10339   -490   -812    179       N  
ATOM   5130  CA  PHE C  31     -41.492  -0.155  -2.889  1.00 63.95           C  
ANISOU 5130  CA  PHE C  31     6307   7975  10015   -435   -845    219       C  
ATOM   5131  C   PHE C  31     -41.586   1.232  -2.232  1.00 62.47           C  
ANISOU 5131  C   PHE C  31     6174   7707   9853   -462   -817    268       C  
ATOM   5132  O   PHE C  31     -42.698   1.560  -1.779  1.00 62.92           O  
ANISOU 5132  O   PHE C  31     6258   7697   9949   -417   -844    308       O  
ATOM   5133  CB  PHE C  31     -41.613  -1.208  -1.783  1.00 63.19           C  
ANISOU 5133  CB  PHE C  31     6160   7872   9978   -390   -870    164       C  
ATOM   5134  CG  PHE C  31     -41.718  -2.640  -2.248  1.00 63.18           C  
ANISOU 5134  CG  PHE C  31     6111   7927   9966   -354   -900    116       C  
ATOM   5135  CD1 PHE C  31     -42.232  -2.963  -3.498  1.00 63.56           C  
ANISOU 5135  CD1 PHE C  31     6161   8016   9971   -344   -920    131       C  
ATOM   5136  CD2 PHE C  31     -41.336  -3.676  -1.409  1.00 62.31           C  
ANISOU 5136  CD2 PHE C  31     5959   7827   9890   -325   -909     55       C  
ATOM   5137  CE1 PHE C  31     -42.341  -4.283  -3.904  1.00 63.25           C  
ANISOU 5137  CE1 PHE C  31     6078   8026   9928   -313   -946     81       C  
ATOM   5138  CE2 PHE C  31     -41.441  -4.997  -1.818  1.00 61.94           C  
ANISOU 5138  CE2 PHE C  31     5877   7820   9836   -292   -935     10       C  
ATOM   5139  CZ  PHE C  31     -41.940  -5.299  -3.066  1.00 62.58           C  
ANISOU 5139  CZ  PHE C  31     5956   7941   9880   -289   -951     20       C  
ATOM   5140  N   GLY C  32     -40.495   2.003  -2.150  1.00 60.32           N  
ANISOU 5140  N   GLY C  32     5915   7439   9561   -531   -764    259       N  
ATOM   5141  CA  GLY C  32     -40.417   3.209  -1.300  1.00 59.24           C  
ANISOU 5141  CA  GLY C  32     5821   7227   9461   -562   -731    284       C  
ATOM   5142  C   GLY C  32     -40.241   2.822   0.166  1.00 57.80           C  
ANISOU 5142  C   GLY C  32     5589   7029   9343   -538   -739    231       C  
ATOM   5143  O   GLY C  32     -39.738   1.738   0.450  1.00 58.03           O  
ANISOU 5143  O   GLY C  32     5555   7118   9375   -519   -753    167       O  
ATOM   5144  N   PRO C  33     -40.652   3.662   1.145  1.00 56.81           N  
ANISOU 5144  N   PRO C  33     5491   6825   9268   -534   -732    255       N  
ATOM   5145  CA  PRO C  33     -40.566   3.295   2.562  1.00 56.29           C  
ANISOU 5145  CA  PRO C  33     5380   6746   9259   -506   -741    207       C  
ATOM   5146  C   PRO C  33     -41.118   1.881   2.824  1.00 54.86           C  
ANISOU 5146  C   PRO C  33     5155   6593   9096   -437   -791    179       C  
ATOM   5147  O   PRO C  33     -42.265   1.637   2.493  1.00 54.18           O  
ANISOU 5147  O   PRO C  33     5087   6479   9019   -393   -827    218       O  
ATOM   5148  CB  PRO C  33     -41.409   4.366   3.281  1.00 56.11           C  
ANISOU 5148  CB  PRO C  33     5406   6628   9284   -495   -741    255       C  
ATOM   5149  CG  PRO C  33     -41.333   5.565   2.361  1.00 56.81           C  
ANISOU 5149  CG  PRO C  33     5567   6681   9337   -546   -707    313       C  
ATOM   5150  CD  PRO C  33     -41.222   5.002   0.953  1.00 57.20           C  
ANISOU 5150  CD  PRO C  33     5619   6792   9320   -550   -715    326       C  
ATOM   5151  N   THR C  34     -40.282   0.997   3.377  1.00 54.43           N  
ANISOU 5151  N   THR C  34     5045   6593   9043   -428   -791    110       N  
ATOM   5152  CA  THR C  34     -40.549  -0.453   3.592  1.00 54.26           C  
ANISOU 5152  CA  THR C  34     4985   6598   9030   -368   -830     75       C  
ATOM   5153  C   THR C  34     -40.055  -0.854   4.988  1.00 54.03           C  
ANISOU 5153  C   THR C  34     4925   6570   9034   -342   -830     24       C  
ATOM   5154  O   THR C  34     -38.901  -0.505   5.315  1.00 53.82           O  
ANISOU 5154  O   THR C  34     4873   6583   8993   -376   -801    -20       O  
ATOM   5155  CB  THR C  34     -39.869  -1.302   2.505  1.00 53.98           C  
ANISOU 5155  CB  THR C  34     4920   6645   8942   -377   -833     39       C  
ATOM   5156  OG1 THR C  34     -40.088  -0.700   1.226  1.00 53.47           O  
ANISOU 5156  OG1 THR C  34     4889   6589   8837   -413   -822     86       O  
ATOM   5157  CG2 THR C  34     -40.373  -2.727   2.474  1.00 53.39           C  
ANISOU 5157  CG2 THR C  34     4824   6584   8877   -316   -872     15       C  
ATOM   5158  N   TYR C  35     -40.878  -1.561   5.774  1.00 54.51           N  
ANISOU 5158  N   TYR C  35     4985   6592   9131   -286   -859     26       N  
ATOM   5159  CA  TYR C  35     -40.575  -1.924   7.186  1.00 55.85           C  
ANISOU 5159  CA  TYR C  35     5137   6753   9330   -253   -862    -11       C  
ATOM   5160  C   TYR C  35     -40.800  -3.421   7.448  1.00 55.55           C  
ANISOU 5160  C   TYR C  35     5088   6723   9293   -193   -891    -39       C  
ATOM   5161  O   TYR C  35     -41.712  -4.014   6.856  1.00 54.93           O  
ANISOU 5161  O   TYR C  35     5024   6625   9220   -175   -910    -16       O  
ATOM   5162  CB  TYR C  35     -41.417  -1.078   8.140  1.00 56.61           C  
ANISOU 5162  CB  TYR C  35     5259   6776   9474   -250   -858     24       C  
ATOM   5163  CG  TYR C  35     -41.343   0.412   7.912  1.00 57.69           C  
ANISOU 5163  CG  TYR C  35     5418   6885   9614   -304   -830     57       C  
ATOM   5164  CD1 TYR C  35     -40.538   1.226   8.699  1.00 57.38           C  
ANISOU 5164  CD1 TYR C  35     5368   6849   9585   -336   -799     29       C  
ATOM   5165  CD2 TYR C  35     -42.089   1.010   6.910  1.00 58.96           C  
ANISOU 5165  CD2 TYR C  35     5617   7016   9767   -321   -832    114       C  
ATOM   5166  CE1 TYR C  35     -40.482   2.596   8.500  1.00 57.33           C  
ANISOU 5166  CE1 TYR C  35     5391   6807   9585   -390   -767     57       C  
ATOM   5167  CE2 TYR C  35     -42.025   2.378   6.682  1.00 59.06           C  
ANISOU 5167  CE2 TYR C  35     5665   6993   9781   -367   -804    149       C  
ATOM   5168  CZ  TYR C  35     -41.230   3.174   7.487  1.00 58.26           C  
ANISOU 5168  CZ  TYR C  35     5556   6884   9695   -405   -769    121       C  
ATOM   5169  OH  TYR C  35     -41.203   4.520   7.253  1.00 59.14           O  
ANISOU 5169  OH  TYR C  35     5710   6949   9809   -454   -737    155       O  
ATOM   5170  N   LEU C  36     -39.982  -3.991   8.339  1.00 55.96           N  
ANISOU 5170  N   LEU C  36     5119   6802   9341   -161   -893    -90       N  
ATOM   5171  CA  LEU C  36     -39.990  -5.424   8.736  1.00 57.32           C  
ANISOU 5171  CA  LEU C  36     5291   6977   9509    -98   -916   -121       C  
ATOM   5172  C   LEU C  36     -40.059  -5.490  10.258  1.00 57.72           C  
ANISOU 5172  C   LEU C  36     5352   6992   9584    -59   -918   -129       C  
ATOM   5173  O   LEU C  36     -38.994  -5.416  10.902  1.00 58.97           O  
ANISOU 5173  O   LEU C  36     5485   7196   9724    -44   -914   -176       O  
ATOM   5174  CB  LEU C  36     -38.713  -6.095   8.216  1.00 58.59           C  
ANISOU 5174  CB  LEU C  36     5416   7219   9625    -86   -921   -184       C  
ATOM   5175  CG  LEU C  36     -38.430  -7.518   8.699  1.00 59.25           C  
ANISOU 5175  CG  LEU C  36     5503   7309   9699    -13   -945   -225       C  
ATOM   5176  CD1 LEU C  36     -39.645  -8.421   8.513  1.00 59.41           C  
ANISOU 5176  CD1 LEU C  36     5562   7266   9742     11   -959   -192       C  
ATOM   5177  CD2 LEU C  36     -37.212  -8.092   7.988  1.00 59.32           C  
ANISOU 5177  CD2 LEU C  36     5471   7404   9661     -2   -951   -289       C  
ATOM   5178  N   ASP C  37     -41.264  -5.614  10.807  1.00 59.39           N  
ANISOU 5178  N   ASP C  37     5597   7135   9832    -44   -923    -90       N  
ATOM   5179  CA  ASP C  37     -41.520  -5.565  12.273  1.00 60.85           C  
ANISOU 5179  CA  ASP C  37     5797   7280  10040    -14   -921    -89       C  
ATOM   5180  C   ASP C  37     -40.835  -4.309  12.834  1.00 59.83           C  
ANISOU 5180  C   ASP C  37     5644   7173   9913    -44   -902   -101       C  
ATOM   5181  O   ASP C  37     -40.017  -4.448  13.762  1.00 60.06           O  
ANISOU 5181  O   ASP C  37     5658   7233   9928    -13   -903   -142       O  
ATOM   5182  CB  ASP C  37     -41.085  -6.869  12.955  1.00 62.20           C  
ANISOU 5182  CB  ASP C  37     5983   7459  10191     50   -934   -124       C  
ATOM   5183  CG  ASP C  37     -41.976  -7.303  14.114  1.00 64.18           C  
ANISOU 5183  CG  ASP C  37     6275   7643  10466     82   -933   -102       C  
ATOM   5184  OD1 ASP C  37     -43.201  -7.001  14.087  1.00 63.25           O  
ANISOU 5184  OD1 ASP C  37     6174   7472  10383     55   -926    -62       O  
ATOM   5185  OD2 ASP C  37     -41.447  -7.963  15.030  1.00 65.24           O  
ANISOU 5185  OD2 ASP C  37     6425   7782  10580    136   -939   -127       O  
ATOM   5186  N   GLY C  38     -41.143  -3.137  12.258  1.00 58.92           N  
ANISOU 5186  N   GLY C  38     5527   7044   9814   -100   -887    -70       N  
ATOM   5187  CA  GLY C  38     -40.694  -1.818  12.739  1.00 59.00           C  
ANISOU 5187  CA  GLY C  38     5523   7056   9836   -139   -863    -76       C  
ATOM   5188  C   GLY C  38     -39.404  -1.352  12.080  1.00 59.28           C  
ANISOU 5188  C   GLY C  38     5526   7159   9836   -182   -843   -115       C  
ATOM   5189  O   GLY C  38     -39.331  -0.165  11.715  1.00 60.37           O  
ANISOU 5189  O   GLY C  38     5669   7285   9983   -240   -817    -97       O  
ATOM   5190  N   ALA C  39     -38.410  -2.239  11.973  1.00 58.08           N  
ANISOU 5190  N   ALA C  39     5345   7076   9647   -154   -852   -170       N  
ATOM   5191  CA  ALA C  39     -37.078  -1.995  11.364  1.00 56.93           C  
ANISOU 5191  CA  ALA C  39     5157   7012   9461   -191   -834   -225       C  
ATOM   5192  C   ALA C  39     -37.233  -1.373   9.966  1.00 55.75           C  
ANISOU 5192  C   ALA C  39     5021   6860   9300   -258   -814   -189       C  
ATOM   5193  O   ALA C  39     -37.848  -2.019   9.090  1.00 55.89           O  
ANISOU 5193  O   ALA C  39     5058   6866   9310   -244   -833   -156       O  
ATOM   5194  CB  ALA C  39     -36.316  -3.298  11.296  1.00 57.19           C  
ANISOU 5194  CB  ALA C  39     5162   7109   9456   -133   -859   -282       C  
ATOM   5195  N   ASP C  40     -36.690  -0.169   9.764  1.00 53.91           N  
ANISOU 5195  N   ASP C  40     4780   6638   9064   -328   -775   -196       N  
ATOM   5196  CA  ASP C  40     -36.671   0.531   8.451  1.00 53.54           C  
ANISOU 5196  CA  ASP C  40     4755   6591   8996   -397   -748   -162       C  
ATOM   5197  C   ASP C  40     -35.688  -0.189   7.519  1.00 53.84           C  
ANISOU 5197  C   ASP C  40     4754   6720   8980   -408   -746   -214       C  
ATOM   5198  O   ASP C  40     -34.461  -0.042   7.721  1.00 55.53           O  
ANISOU 5198  O   ASP C  40     4920   7007   9169   -435   -722   -288       O  
ATOM   5199  CB  ASP C  40     -36.328   2.013   8.625  1.00 53.52           C  
ANISOU 5199  CB  ASP C  40     4765   6565   9005   -473   -699   -158       C  
ATOM   5200  CG  ASP C  40     -36.355   2.825   7.338  1.00 54.05           C  
ANISOU 5200  CG  ASP C  40     4872   6617   9047   -544   -666   -113       C  
ATOM   5201  OD1 ASP C  40     -36.335   2.220   6.256  1.00 54.02           O  
ANISOU 5201  OD1 ASP C  40     4869   6649   9006   -543   -677   -103       O  
ATOM   5202  OD2 ASP C  40     -36.387   4.053   7.425  1.00 55.11           O  
ANISOU 5202  OD2 ASP C  40     5039   6703   9197   -600   -628    -89       O  
ATOM   5203  N   VAL C  41     -36.204  -0.919   6.525  1.00 53.60           N  
ANISOU 5203  N   VAL C  41     4740   6692   8932   -389   -769   -183       N  
ATOM   5204  CA  VAL C  41     -35.389  -1.722   5.563  1.00 54.30           C  
ANISOU 5204  CA  VAL C  41     4792   6867   8970   -392   -773   -232       C  
ATOM   5205  C   VAL C  41     -35.472  -1.098   4.159  1.00 55.60           C  
ANISOU 5205  C   VAL C  41     4982   7039   9101   -460   -747   -191       C  
ATOM   5206  O   VAL C  41     -35.280  -1.838   3.172  1.00 54.81           O  
ANISOU 5206  O   VAL C  41     4867   6992   8964   -455   -759   -207       O  
ATOM   5207  CB  VAL C  41     -35.808  -3.206   5.572  1.00 53.65           C  
ANISOU 5207  CB  VAL C  41     4705   6789   8891   -310   -821   -242       C  
ATOM   5208  CG1 VAL C  41     -35.687  -3.811   6.963  1.00 53.00           C  
ANISOU 5208  CG1 VAL C  41     4610   6695   8832   -242   -843   -278       C  
ATOM   5209  CG2 VAL C  41     -37.204  -3.424   5.016  1.00 54.10           C  
ANISOU 5209  CG2 VAL C  41     4808   6780   8967   -294   -843   -169       C  
ATOM   5210  N   THR C  42     -35.693   0.220   4.072  1.00 58.04           N  
ANISOU 5210  N   THR C  42     5332   7299   9419   -521   -711   -144       N  
ATOM   5211  CA  THR C  42     -35.772   0.992   2.794  1.00 60.04           C  
ANISOU 5211  CA  THR C  42     5627   7548   9635   -588   -679    -95       C  
ATOM   5212  C   THR C  42     -34.429   0.924   2.053  1.00 62.67           C  
ANISOU 5212  C   THR C  42     5918   7982   9912   -649   -642   -161       C  
ATOM   5213  O   THR C  42     -34.447   0.848   0.809  1.00 62.80           O  
ANISOU 5213  O   THR C  42     5951   8027   9882   -677   -635   -138       O  
ATOM   5214  CB  THR C  42     -36.162   2.457   3.036  1.00 59.66           C  
ANISOU 5214  CB  THR C  42     5638   7417   9610   -637   -644    -37       C  
ATOM   5215  OG1 THR C  42     -37.314   2.498   3.877  1.00 59.35           O  
ANISOU 5215  OG1 THR C  42     5625   7297   9627   -578   -678      7       O  
ATOM   5216  CG2 THR C  42     -36.457   3.210   1.756  1.00 60.07           C  
ANISOU 5216  CG2 THR C  42     5753   7446   9622   -689   -619     29       C  
ATOM   5217  N   LYS C  43     -33.315   0.939   2.793  1.00 66.04           N  
ANISOU 5217  N   LYS C  43     6287   8465  10338   -667   -621   -246       N  
ATOM   5218  CA  LYS C  43     -31.945   1.149   2.247  1.00 68.46           C  
ANISOU 5218  CA  LYS C  43     6547   8869  10593   -742   -573   -323       C  
ATOM   5219  C   LYS C  43     -31.173  -0.173   2.132  1.00 69.58           C  
ANISOU 5219  C   LYS C  43     6612   9116  10706   -691   -605   -412       C  
ATOM   5220  O   LYS C  43     -30.108  -0.150   1.497  1.00 71.67           O  
ANISOU 5220  O   LYS C  43     6833   9474  10923   -748   -571   -480       O  
ATOM   5221  CB  LYS C  43     -31.202   2.158   3.124  1.00 69.12           C  
ANISOU 5221  CB  LYS C  43     6613   8954  10695   -802   -523   -370       C  
ATOM   5222  CG  LYS C  43     -31.380   3.605   2.694  1.00 70.88           C  
ANISOU 5222  CG  LYS C  43     6906   9110  10916   -898   -461   -310       C  
ATOM   5223  CD  LYS C  43     -31.122   4.582   3.816  1.00 73.21           C  
ANISOU 5223  CD  LYS C  43     7199   9364  11252   -934   -425   -335       C  
ATOM   5224  CE  LYS C  43     -30.468   5.870   3.350  1.00 75.40           C  
ANISOU 5224  CE  LYS C  43     7508   9633  11507  -1060   -340   -341       C  
ATOM   5225  NZ  LYS C  43     -30.569   6.928   4.388  1.00 76.42           N  
ANISOU 5225  NZ  LYS C  43     7658   9689  11688  -1091   -308   -341       N  
ATOM   5226  N   ILE C  44     -31.671  -1.275   2.708  1.00 69.50           N  
ANISOU 5226  N   ILE C  44     6591   9092  10723   -590   -665   -415       N  
ATOM   5227  CA  ILE C  44     -31.018  -2.615   2.619  1.00 70.20           C  
ANISOU 5227  CA  ILE C  44     6618   9266  10786   -526   -701   -496       C  
ATOM   5228  C   ILE C  44     -31.654  -3.389   1.458  1.00 71.85           C  
ANISOU 5228  C   ILE C  44     6849   9473  10975   -505   -728   -456       C  
ATOM   5229  O   ILE C  44     -32.739  -2.990   1.002  1.00 71.44           O  
ANISOU 5229  O   ILE C  44     6858   9348  10937   -518   -730   -365       O  
ATOM   5230  CB  ILE C  44     -31.065  -3.375   3.965  1.00 69.37           C  
ANISOU 5230  CB  ILE C  44     6495   9145  10716   -429   -745   -529       C  
ATOM   5231  CG1 ILE C  44     -32.335  -4.206   4.151  1.00 67.01           C  
ANISOU 5231  CG1 ILE C  44     6245   8762  10452   -352   -793   -462       C  
ATOM   5232  CG2 ILE C  44     -30.837  -2.430   5.142  1.00 69.66           C  
ANISOU 5232  CG2 ILE C  44     6528   9157  10782   -451   -721   -541       C  
ATOM   5233  CD1 ILE C  44     -32.359  -4.996   5.445  1.00 66.52           C  
ANISOU 5233  CD1 ILE C  44     6176   8681  10416   -259   -831   -491       C  
ATOM   5234  N   LYS C  45     -30.975  -4.439   0.991  1.00 76.25           N  
ANISOU 5234  N   LYS C  45     7355  10117  11499   -471   -749   -528       N  
ATOM   5235  CA  LYS C  45     -31.354  -5.223  -0.218  1.00 77.98           C  
ANISOU 5235  CA  LYS C  45     7579  10358  11690   -458   -770   -513       C  
ATOM   5236  C   LYS C  45     -31.965  -6.547   0.233  1.00 78.34           C  
ANISOU 5236  C   LYS C  45     7630  10368  11767   -354   -828   -516       C  
ATOM   5237  O   LYS C  45     -31.581  -7.100   1.260  1.00 78.77           O  
ANISOU 5237  O   LYS C  45     7663  10424  11840   -290   -850   -565       O  
ATOM   5238  CB  LYS C  45     -30.147  -5.451  -1.140  1.00 78.95           C  
ANISOU 5238  CB  LYS C  45     7640  10605  11752   -501   -748   -598       C  
ATOM   5239  CG  LYS C  45     -29.371  -4.201  -1.544  1.00 80.01           C  
ANISOU 5239  CG  LYS C  45     7765  10784  11850   -614   -680   -612       C  
ATOM   5240  CD  LYS C  45     -28.032  -4.486  -2.196  1.00 80.67           C  
ANISOU 5240  CD  LYS C  45     7771  11002  11875   -654   -656   -719       C  
ATOM   5241  CE  LYS C  45     -26.993  -3.409  -1.905  1.00 81.05           C  
ANISOU 5241  CE  LYS C  45     7788  11102  11904   -747   -592   -775       C  
ATOM   5242  NZ  LYS C  45     -25.685  -3.771  -2.508  1.00 81.34           N  
ANISOU 5242  NZ  LYS C  45     7739  11281  11883   -782   -570   -894       N  
ATOM   5243  N   PRO C  46     -32.950  -7.090  -0.515  1.00 80.50           N  
ANISOU 5243  N   PRO C  46     7936  10605  12045   -334   -851   -466       N  
ATOM   5244  CA  PRO C  46     -33.634  -8.318  -0.106  1.00 80.86           C  
ANISOU 5244  CA  PRO C  46     7995  10602  12123   -247   -897   -466       C  
ATOM   5245  C   PRO C  46     -32.645  -9.439   0.245  1.00 81.38           C  
ANISOU 5245  C   PRO C  46     8014  10730  12175   -181   -921   -562       C  
ATOM   5246  O   PRO C  46     -31.889  -9.841  -0.611  1.00 82.44           O  
ANISOU 5246  O   PRO C  46     8104  10952  12267   -193   -920   -622       O  
ATOM   5247  CB  PRO C  46     -34.489  -8.669  -1.333  1.00 81.50           C  
ANISOU 5247  CB  PRO C  46     8095  10678  12191   -258   -908   -426       C  
ATOM   5248  CG  PRO C  46     -34.725  -7.343  -2.027  1.00 82.13           C  
ANISOU 5248  CG  PRO C  46     8201  10756  12249   -340   -873   -364       C  
ATOM   5249  CD  PRO C  46     -33.460  -6.547  -1.786  1.00 81.44           C  
ANISOU 5249  CD  PRO C  46     8081  10727  12135   -395   -833   -409       C  
ATOM   5250  N   HIS C  47     -32.656  -9.875   1.507  1.00 82.58           N  
ANISOU 5250  N   HIS C  47     8178  10838  12359   -113   -943   -575       N  
ATOM   5251  CA  HIS C  47     -31.859 -11.016   2.041  1.00 84.09           C  
ANISOU 5251  CA  HIS C  47     8342  11067  12540    -26   -975   -657       C  
ATOM   5252  C   HIS C  47     -32.603 -12.336   1.767  1.00 83.87           C  
ANISOU 5252  C   HIS C  47     8348  10988  12529     36  -1008   -648       C  
ATOM   5253  O   HIS C  47     -33.596 -12.304   1.025  1.00 86.40           O  
ANISOU 5253  O   HIS C  47     8696  11268  12863      2  -1004   -592       O  
ATOM   5254  CB  HIS C  47     -31.545 -10.773   3.530  1.00 85.43           C  
ANISOU 5254  CB  HIS C  47     8517  11212  12728     16   -980   -670       C  
ATOM   5255  CG  HIS C  47     -30.326 -11.483   4.030  1.00 87.01           C  
ANISOU 5255  CG  HIS C  47     8671  11488  12898     90  -1004   -769       C  
ATOM   5256  ND1 HIS C  47     -30.385 -12.429   5.045  1.00 86.99           N  
ANISOU 5256  ND1 HIS C  47     8700  11441  12908    194  -1040   -783       N  
ATOM   5257  CD2 HIS C  47     -29.026 -11.400   3.664  1.00 87.10           C  
ANISOU 5257  CD2 HIS C  47     8609  11620  12865     79   -997   -864       C  
ATOM   5258  CE1 HIS C  47     -29.177 -12.895   5.274  1.00 87.08           C  
ANISOU 5258  CE1 HIS C  47     8662  11542  12883    253  -1060   -879       C  
ATOM   5259  NE2 HIS C  47     -28.327 -12.281   4.440  1.00 87.79           N  
ANISOU 5259  NE2 HIS C  47     8680  11738  12938    182  -1035   -935       N  
ATOM   5260  N   ASN C  48     -32.125 -13.446   2.342  1.00 83.13           N  
ANISOU 5260  N   ASN C  48     8254  10898  12433    126  -1039   -705       N  
ATOM   5261  CA  ASN C  48     -32.618 -14.832   2.115  1.00 82.62           C  
ANISOU 5261  CA  ASN C  48     8223  10787  12382    192  -1068   -715       C  
ATOM   5262  C   ASN C  48     -33.751 -15.150   3.094  1.00 79.78           C  
ANISOU 5262  C   ASN C  48     7938  10302  12070    228  -1073   -648       C  
ATOM   5263  O   ASN C  48     -34.811 -15.637   2.647  1.00 77.94           O  
ANISOU 5263  O   ASN C  48     7742  10006  11863    218  -1073   -609       O  
ATOM   5264  CB  ASN C  48     -31.517 -15.868   2.369  1.00 84.12           C  
ANISOU 5264  CB  ASN C  48     8388  11030  12544    282  -1098   -808       C  
ATOM   5265  CG  ASN C  48     -30.594 -16.121   1.185  1.00 84.96           C  
ANISOU 5265  CG  ASN C  48     8424  11252  12606    265  -1101   -888       C  
ATOM   5266  OD1 ASN C  48     -29.451 -16.543   1.384  1.00 83.91           O  
ANISOU 5266  OD1 ASN C  48     8247  11194  12440    321  -1121   -976       O  
ATOM   5267  ND2 ASN C  48     -31.072 -15.905  -0.035  1.00 85.58           N  
ANISOU 5267  ND2 ASN C  48     8489  11348  12677    193  -1084   -863       N  
ATOM   5268  N   SER C  49     -33.483 -14.908   4.381  1.00 78.07           N  
ANISOU 5268  N   SER C  49     7740  10061  11862    267  -1077   -645       N  
ATOM   5269  CA  SER C  49     -34.367 -15.196   5.543  1.00 77.95           C  
ANISOU 5269  CA  SER C  49     7797   9936  11885    308  -1080   -591       C  
ATOM   5270  C   SER C  49     -35.732 -14.522   5.370  1.00 77.43           C  
ANISOU 5270  C   SER C  49     7760   9799  11858    238  -1057   -507       C  
ATOM   5271  O   SER C  49     -36.698 -14.974   6.012  1.00 74.34           O  
ANISOU 5271  O   SER C  49     7429   9315  11501    260  -1056   -465       O  
ATOM   5272  CB  SER C  49     -33.707 -14.744   6.813  1.00 77.58           C  
ANISOU 5272  CB  SER C  49     7746   9902  11828    347  -1084   -606       C  
ATOM   5273  OG  SER C  49     -32.303 -14.718   6.644  1.00 77.80           O  
ANISOU 5273  OG  SER C  49     7709  10039  11811    372  -1096   -691       O  
ATOM   5274  N   HIS C  50     -35.800 -13.478   4.537  1.00 79.48           N  
ANISOU 5274  N   HIS C  50     7984  10103  12111    158  -1038   -485       N  
ATOM   5275  CA  HIS C  50     -37.004 -12.648   4.262  1.00 79.72           C  
ANISOU 5275  CA  HIS C  50     8036  10082  12172     94  -1020   -409       C  
ATOM   5276  C   HIS C  50     -38.069 -13.453   3.499  1.00 82.24           C  
ANISOU 5276  C   HIS C  50     8378  10359  12508     92  -1027   -391       C  
ATOM   5277  O   HIS C  50     -39.257 -13.090   3.620  1.00 82.11           O  
ANISOU 5277  O   HIS C  50     8391  10281  12525     66  -1019   -334       O  
ATOM   5278  CB  HIS C  50     -36.616 -11.367   3.505  1.00 79.15           C  
ANISOU 5278  CB  HIS C  50     7924  10072  12075     17   -998   -397       C  
ATOM   5279  CG  HIS C  50     -35.734 -10.432   4.267  1.00 78.28           C  
ANISOU 5279  CG  HIS C  50     7791   9995  11956      2   -982   -414       C  
ATOM   5280  ND1 HIS C  50     -34.853  -9.569   3.644  1.00 78.62           N  
ANISOU 5280  ND1 HIS C  50     7790  10116  11963    -57   -959   -439       N  
ATOM   5281  CD2 HIS C  50     -35.594 -10.215   5.592  1.00 77.88           C  
ANISOU 5281  CD2 HIS C  50     7754   9913  11924     34   -983   -414       C  
ATOM   5282  CE1 HIS C  50     -34.204  -8.870   4.552  1.00 78.65           C  
ANISOU 5282  CE1 HIS C  50     7778  10136  11969    -63   -945   -459       C  
ATOM   5283  NE2 HIS C  50     -34.638  -9.249   5.754  1.00 78.19           N  
ANISOU 5283  NE2 HIS C  50     7753  10013  11942     -3   -962   -444       N  
ATOM   5284  N   GLU C  51     -37.681 -14.492   2.751  1.00 83.99           N  
ANISOU 5284  N   GLU C  51     8585  10617  12710    120  -1041   -443       N  
ATOM   5285  CA  GLU C  51     -38.605 -15.309   1.911  1.00 83.26           C  
ANISOU 5285  CA  GLU C  51     8506  10497  12632    114  -1046   -440       C  
ATOM   5286  C   GLU C  51     -39.924 -15.530   2.666  1.00 79.41           C  
ANISOU 5286  C   GLU C  51     8073   9905  12193    119  -1039   -392       C  
ATOM   5287  O   GLU C  51     -39.887 -16.141   3.758  1.00 77.97           O  
ANISOU 5287  O   GLU C  51     7933   9662  12027    169  -1040   -397       O  
ATOM   5288  CB  GLU C  51     -37.969 -16.651   1.526  1.00 85.77           C  
ANISOU 5288  CB  GLU C  51     8816  10838  12931    167  -1063   -511       C  
ATOM   5289  CG  GLU C  51     -38.774 -17.438   0.494  1.00 87.21           C  
ANISOU 5289  CG  GLU C  51     9000  11010  13124    153  -1066   -522       C  
ATOM   5290  CD  GLU C  51     -38.402 -17.183  -0.960  1.00 88.71           C  
ANISOU 5290  CD  GLU C  51     9131  11299  13274    111  -1068   -549       C  
ATOM   5291  OE1 GLU C  51     -37.190 -17.189  -1.265  1.00 90.81           O  
ANISOU 5291  OE1 GLU C  51     9357  11645  13501    122  -1075   -600       O  
ATOM   5292  OE2 GLU C  51     -39.317 -16.966  -1.786  1.00 88.57           O  
ANISOU 5292  OE2 GLU C  51     9107  11285  13261     68  -1064   -521       O  
ATOM   5293  N   GLY C  52     -41.031 -15.021   2.115  1.00 75.92           N  
ANISOU 5293  N   GLY C  52     7629   9447  11767     71  -1031   -349       N  
ATOM   5294  CA  GLY C  52     -42.397 -15.243   2.624  1.00 75.04           C  
ANISOU 5294  CA  GLY C  52     7557   9251  11700     65  -1022   -315       C  
ATOM   5295  C   GLY C  52     -42.659 -14.535   3.946  1.00 73.63           C  
ANISOU 5295  C   GLY C  52     7409   9017  11547     69  -1012   -272       C  
ATOM   5296  O   GLY C  52     -43.526 -15.011   4.707  1.00 72.36           O  
ANISOU 5296  O   GLY C  52     7291   8781  11422     79  -1001   -259       O  
ATOM   5297  N   LYS C  53     -41.946 -13.435   4.214  1.00 73.15           N  
ANISOU 5297  N   LYS C  53     7329   8993  11470     55  -1010   -255       N  
ATOM   5298  CA  LYS C  53     -42.207 -12.527   5.365  1.00 72.12           C  
ANISOU 5298  CA  LYS C  53     7218   8820  11363     49   -999   -214       C  
ATOM   5299  C   LYS C  53     -43.073 -11.354   4.890  1.00 69.67           C  
ANISOU 5299  C   LYS C  53     6897   8507  11065     -1   -993   -163       C  
ATOM   5300  O   LYS C  53     -43.123 -11.088   3.662  1.00 66.31           O  
ANISOU 5300  O   LYS C  53     6447   8131  10617    -30   -998   -161       O  
ATOM   5301  CB  LYS C  53     -40.911 -12.001   5.988  1.00 74.00           C  
ANISOU 5301  CB  LYS C  53     7439   9099  11577     65   -998   -233       C  
ATOM   5302  CG  LYS C  53     -40.269 -12.899   7.043  1.00 76.17           C  
ANISOU 5302  CG  LYS C  53     7739   9354  11847    132  -1006   -268       C  
ATOM   5303  CD  LYS C  53     -39.070 -12.247   7.721  1.00 77.97           C  
ANISOU 5303  CD  LYS C  53     7941   9633  12051    147  -1007   -292       C  
ATOM   5304  CE  LYS C  53     -38.917 -12.568   9.197  1.00 78.88           C  
ANISOU 5304  CE  LYS C  53     8092   9705  12172    205  -1010   -295       C  
ATOM   5305  NZ  LYS C  53     -38.540 -13.984   9.408  1.00 80.00           N  
ANISOU 5305  NZ  LYS C  53     8267   9833  12297    279  -1027   -333       N  
ATOM   5306  N   THR C  54     -43.730 -10.688   5.846  1.00 68.89           N  
ANISOU 5306  N   THR C  54     6820   8356  10999     -7   -985   -126       N  
ATOM   5307  CA  THR C  54     -44.678  -9.566   5.619  1.00 67.40           C  
ANISOU 5307  CA  THR C  54     6629   8150  10828    -43   -982    -78       C  
ATOM   5308  C   THR C  54     -43.961  -8.241   5.895  1.00 64.48           C  
ANISOU 5308  C   THR C  54     6251   7800  10448    -66   -972    -56       C  
ATOM   5309  O   THR C  54     -43.392  -8.102   6.990  1.00 61.52           O  
ANISOU 5309  O   THR C  54     5882   7411  10081    -50   -964    -66       O  
ATOM   5310  CB  THR C  54     -45.938  -9.738   6.475  1.00 67.60           C  
ANISOU 5310  CB  THR C  54     6680   8105  10898    -36   -977    -60       C  
ATOM   5311  OG1 THR C  54     -46.548 -10.971   6.092  1.00 67.96           O  
ANISOU 5311  OG1 THR C  54     6732   8136  10951    -25   -979    -88       O  
ATOM   5312  CG2 THR C  54     -46.922  -8.602   6.306  1.00 67.49           C  
ANISOU 5312  CG2 THR C  54     6663   8077  10903    -61   -979    -18       C  
ATOM   5313  N   PHE C  55     -44.013  -7.315   4.931  1.00 63.17           N  
ANISOU 5313  N   PHE C  55     6075   7663  10264   -102   -972    -29       N  
ATOM   5314  CA  PHE C  55     -43.335  -5.995   4.953  1.00 61.65           C  
ANISOU 5314  CA  PHE C  55     5880   7485  10056   -137   -955     -8       C  
ATOM   5315  C   PHE C  55     -44.380  -4.877   4.847  1.00 58.97           C  
ANISOU 5315  C   PHE C  55     5563   7103   9738   -155   -956     48       C  
ATOM   5316  O   PHE C  55     -45.109  -4.844   3.856  1.00 58.11           O  
ANISOU 5316  O   PHE C  55     5458   7003   9617   -158   -969     69       O  
ATOM   5317  CB  PHE C  55     -42.328  -5.898   3.804  1.00 63.41           C  
ANISOU 5317  CB  PHE C  55     6082   7782  10228   -166   -948    -26       C  
ATOM   5318  CG  PHE C  55     -41.090  -6.753   3.936  1.00 65.32           C  
ANISOU 5318  CG  PHE C  55     6295   8078  10446   -149   -947    -90       C  
ATOM   5319  CD1 PHE C  55     -40.019  -6.342   4.714  1.00 66.31           C  
ANISOU 5319  CD1 PHE C  55     6404   8224  10565   -154   -931   -119       C  
ATOM   5320  CD2 PHE C  55     -40.972  -7.950   3.245  1.00 66.64           C  
ANISOU 5320  CD2 PHE C  55     6446   8280  10593   -125   -963   -127       C  
ATOM   5321  CE1 PHE C  55     -38.870  -7.117   4.815  1.00 66.78           C  
ANISOU 5321  CE1 PHE C  55     6432   8342  10597   -129   -935   -185       C  
ATOM   5322  CE2 PHE C  55     -39.820  -8.722   3.347  1.00 67.45           C  
ANISOU 5322  CE2 PHE C  55     6522   8432  10671   -101   -966   -189       C  
ATOM   5323  CZ  PHE C  55     -38.772  -8.308   4.139  1.00 67.18           C  
ANISOU 5323  CZ  PHE C  55     6472   8423  10629    -99   -954   -219       C  
ATOM   5324  N   TYR C  56     -44.452  -3.996   5.846  1.00 57.39           N  
ANISOU 5324  N   TYR C  56     5377   6860   9567   -161   -943     67       N  
ATOM   5325  CA  TYR C  56     -45.270  -2.754   5.813  1.00 56.75           C  
ANISOU 5325  CA  TYR C  56     5319   6736   9505   -176   -942    118       C  
ATOM   5326  C   TYR C  56     -44.674  -1.807   4.770  1.00 57.11           C  
ANISOU 5326  C   TYR C  56     5378   6810   9511   -217   -928    143       C  
ATOM   5327  O   TYR C  56     -43.443  -1.604   4.801  1.00 58.31           O  
ANISOU 5327  O   TYR C  56     5518   6997   9640   -247   -904    119       O  
ATOM   5328  CB  TYR C  56     -45.310  -2.064   7.179  1.00 56.08           C  
ANISOU 5328  CB  TYR C  56     5243   6603   9459   -175   -929    122       C  
ATOM   5329  CG  TYR C  56     -46.367  -2.570   8.128  1.00 55.99           C  
ANISOU 5329  CG  TYR C  56     5234   6547   9491   -141   -941    119       C  
ATOM   5330  CD1 TYR C  56     -47.642  -2.022   8.144  1.00 56.10           C  
ANISOU 5330  CD1 TYR C  56     5261   6520   9533   -133   -953    150       C  
ATOM   5331  CD2 TYR C  56     -46.092  -3.589   9.025  1.00 55.68           C  
ANISOU 5331  CD2 TYR C  56     5188   6507   9460   -117   -939     84       C  
ATOM   5332  CE1 TYR C  56     -48.616  -2.474   9.020  1.00 55.24           C  
ANISOU 5332  CE1 TYR C  56     5150   6376   9462   -110   -959    140       C  
ATOM   5333  CE2 TYR C  56     -47.050  -4.043   9.918  1.00 55.88           C  
ANISOU 5333  CE2 TYR C  56     5221   6488   9519    -94   -942     82       C  
ATOM   5334  CZ  TYR C  56     -48.316  -3.485   9.915  1.00 55.05           C  
ANISOU 5334  CZ  TYR C  56     5122   6348   9444    -96   -950    108       C  
ATOM   5335  OH  TYR C  56     -49.248  -3.953  10.792  1.00 54.36           O  
ANISOU 5335  OH  TYR C  56     5040   6225   9389    -81   -948     98       O  
ATOM   5336  N   VAL C  57     -45.506  -1.266   3.877  1.00 56.84           N  
ANISOU 5336  N   VAL C  57     5367   6764   9464   -216   -941    187       N  
ATOM   5337  CA  VAL C  57     -45.104  -0.240   2.869  1.00 58.24           C  
ANISOU 5337  CA  VAL C  57     5575   6954   9599   -254   -926    226       C  
ATOM   5338  C   VAL C  57     -46.002   0.987   3.033  1.00 59.32           C  
ANISOU 5338  C   VAL C  57     5755   7025   9758   -246   -930    281       C  
ATOM   5339  O   VAL C  57     -47.001   0.896   3.757  1.00 59.05           O  
ANISOU 5339  O   VAL C  57     5716   6950   9768   -209   -951    282       O  
ATOM   5340  CB  VAL C  57     -45.157  -0.773   1.423  1.00 58.78           C  
ANISOU 5340  CB  VAL C  57     5638   7080   9615   -253   -940    229       C  
ATOM   5341  CG1 VAL C  57     -44.266  -1.987   1.236  1.00 58.72           C  
ANISOU 5341  CG1 VAL C  57     5586   7137   9586   -257   -938    170       C  
ATOM   5342  CG2 VAL C  57     -46.576  -1.084   0.971  1.00 59.32           C  
ANISOU 5342  CG2 VAL C  57     5709   7139   9691   -208   -979    248       C  
ATOM   5343  N   LEU C  58     -45.648   2.088   2.371  1.00 62.41           N  
ANISOU 5343  N   LEU C  58     6191   7404  10117   -279   -909    322       N  
ATOM   5344  CA  LEU C  58     -46.433   3.349   2.371  1.00 65.09           C  
ANISOU 5344  CA  LEU C  58     6585   7675  10469   -267   -913    380       C  
ATOM   5345  C   LEU C  58     -47.512   3.231   1.304  1.00 66.17           C  
ANISOU 5345  C   LEU C  58     6739   7825  10576   -222   -953    414       C  
ATOM   5346  O   LEU C  58     -47.278   2.634   0.261  1.00 66.80           O  
ANISOU 5346  O   LEU C  58     6809   7965  10607   -227   -960    409       O  
ATOM   5347  CB  LEU C  58     -45.494   4.528   2.083  1.00 66.85           C  
ANISOU 5347  CB  LEU C  58     6858   7876  10665   -328   -867    409       C  
ATOM   5348  CG  LEU C  58     -45.883   5.869   2.709  1.00 67.37           C  
ANISOU 5348  CG  LEU C  58     6976   7853  10766   -329   -854    447       C  
ATOM   5349  CD1 LEU C  58     -45.537   5.916   4.196  1.00 67.15           C  
ANISOU 5349  CD1 LEU C  58     6913   7801  10797   -341   -836    403       C  
ATOM   5350  CD2 LEU C  58     -45.203   7.016   1.979  1.00 67.98           C  
ANISOU 5350  CD2 LEU C  58     7123   7903  10800   -385   -810    490       C  
ATOM   5351  N   PRO C  59     -48.731   3.759   1.537  1.00 69.33           N  
ANISOU 5351  N   PRO C  59     7160   8176  11004   -173   -983    442       N  
ATOM   5352  CA  PRO C  59     -49.702   3.937   0.457  1.00 72.09           C  
ANISOU 5352  CA  PRO C  59     7534   8538  11316   -126  -1022    478       C  
ATOM   5353  C   PRO C  59     -49.053   4.593  -0.777  1.00 76.42           C  
ANISOU 5353  C   PRO C  59     8142   9102  11792   -155  -1003    527       C  
ATOM   5354  O   PRO C  59     -48.839   5.791  -0.754  1.00 77.47           O  
ANISOU 5354  O   PRO C  59     8341   9174  11918   -172   -980    574       O  
ATOM   5355  CB  PRO C  59     -50.759   4.846   1.104  1.00 70.96           C  
ANISOU 5355  CB  PRO C  59     7418   8326  11215    -80  -1043    503       C  
ATOM   5356  CG  PRO C  59     -50.701   4.505   2.576  1.00 69.40           C  
ANISOU 5356  CG  PRO C  59     7178   8103  11087    -92  -1030    457       C  
ATOM   5357  CD  PRO C  59     -49.252   4.172   2.849  1.00 69.22           C  
ANISOU 5357  CD  PRO C  59     7142   8103  11057   -156   -985    433       C  
ATOM   5358  N   ASN C  60     -48.710   3.789  -1.794  1.00 80.85           N  
ANISOU 5358  N   ASN C  60     8680   9739  12300   -164  -1008    513       N  
ATOM   5359  CA  ASN C  60     -48.154   4.253  -3.097  1.00 84.39           C  
ANISOU 5359  CA  ASN C  60     9179  10215  12667   -191   -991    556       C  
ATOM   5360  C   ASN C  60     -49.022   3.730  -4.254  1.00 85.87           C  
ANISOU 5360  C   ASN C  60     9357  10463  12805   -136  -1039    563       C  
ATOM   5361  O   ASN C  60     -48.518   3.696  -5.392  1.00 87.59           O  
ANISOU 5361  O   ASN C  60     9596  10732  12950   -157  -1029    582       O  
ATOM   5362  CB  ASN C  60     -46.673   3.881  -3.251  1.00 87.65           C  
ANISOU 5362  CB  ASN C  60     9572  10674  13055   -268   -942    524       C  
ATOM   5363  CG  ASN C  60     -46.413   2.393  -3.391  1.00 90.23           C  
ANISOU 5363  CG  ASN C  60     9818  11082  13381   -265   -956    456       C  
ATOM   5364  OD1 ASN C  60     -46.621   1.816  -4.457  1.00 92.07           O  
ANISOU 5364  OD1 ASN C  60    10037  11378  13564   -249   -978    452       O  
ATOM   5365  ND2 ASN C  60     -45.918   1.768  -2.334  1.00 91.56           N  
ANISOU 5365  ND2 ASN C  60     9937  11250  13601   -280   -944    401       N  
ATOM   5366  N   ASP C  61     -50.276   3.350  -3.982  1.00 85.58           N  
ANISOU 5366  N   ASP C  61     9286  10427  12803    -69  -1088    544       N  
ATOM   5367  CA  ASP C  61     -51.328   3.110  -5.011  1.00 87.37           C  
ANISOU 5367  CA  ASP C  61     9507  10704  12984     -4  -1140    551       C  
ATOM   5368  C   ASP C  61     -52.705   3.166  -4.331  1.00 84.63           C  
ANISOU 5368  C   ASP C  61     9134  10329  12691     63  -1183    533       C  
ATOM   5369  O   ASP C  61     -52.739   3.310  -3.091  1.00 82.72           O  
ANISOU 5369  O   ASP C  61     8881  10030  12519     50  -1168    516       O  
ATOM   5370  CB  ASP C  61     -51.076   1.819  -5.803  1.00 89.91           C  
ANISOU 5370  CB  ASP C  61     9766  11122  13271    -16  -1147    500       C  
ATOM   5371  CG  ASP C  61     -51.455   0.528  -5.097  1.00 91.07           C  
ANISOU 5371  CG  ASP C  61     9828  11292  13479    -10  -1159    421       C  
ATOM   5372  OD1 ASP C  61     -51.355   0.488  -3.859  1.00 92.35           O  
ANISOU 5372  OD1 ASP C  61     9978  11402  13709    -26  -1142    402       O  
ATOM   5373  OD2 ASP C  61     -51.840  -0.434  -5.801  1.00 91.86           O  
ANISOU 5373  OD2 ASP C  61     9880  11463  13557      7  -1184    378       O  
ATOM   5374  N   ASP C  62     -53.790   3.077  -5.114  1.00 81.34           N  
ANISOU 5374  N   ASP C  62     8708   9957  12241    131  -1234    531       N  
ATOM   5375  CA  ASP C  62     -55.182   3.351  -4.657  1.00 77.29           C  
ANISOU 5375  CA  ASP C  62     8176   9424  11764    204  -1280    516       C  
ATOM   5376  C   ASP C  62     -55.692   2.213  -3.761  1.00 73.67           C  
ANISOU 5376  C   ASP C  62     7628   8986  11376    195  -1283    433       C  
ATOM   5377  O   ASP C  62     -56.447   2.510  -2.813  1.00 72.58           O  
ANISOU 5377  O   ASP C  62     7475   8804  11295    221  -1294    416       O  
ATOM   5378  CB  ASP C  62     -56.117   3.627  -5.843  1.00 76.68           C  
ANISOU 5378  CB  ASP C  62     8114   9400  11618    284  -1335    534       C  
ATOM   5379  CG  ASP C  62     -56.270   5.108  -6.147  1.00 77.26           C  
ANISOU 5379  CG  ASP C  62     8290   9412  11654    331  -1348    618       C  
ATOM   5380  OD1 ASP C  62     -56.236   5.899  -5.180  1.00 77.74           O  
ANISOU 5380  OD1 ASP C  62     8385   9384  11766    325  -1330    641       O  
ATOM   5381  OD2 ASP C  62     -56.403   5.464  -7.339  1.00 77.08           O  
ANISOU 5381  OD2 ASP C  62     8314   9425  11547    374  -1373    661       O  
ATOM   5382  N   THR C  63     -55.300   0.964  -4.035  1.00 70.34           N  
ANISOU 5382  N   THR C  63     7150   8623  10950    159  -1271    381       N  
ATOM   5383  CA  THR C  63     -55.661  -0.211  -3.197  1.00 67.25           C  
ANISOU 5383  CA  THR C  63     6687   8243  10623    141  -1263    304       C  
ATOM   5384  C   THR C  63     -55.200   0.060  -1.758  1.00 66.20           C  
ANISOU 5384  C   THR C  63     6567   8031  10555    105  -1227    309       C  
ATOM   5385  O   THR C  63     -56.040  -0.047  -0.850  1.00 65.99           O  
ANISOU 5385  O   THR C  63     6510   7977  10583    122  -1235    277       O  
ATOM   5386  CB  THR C  63     -55.093  -1.513  -3.779  1.00 65.61           C  
ANISOU 5386  CB  THR C  63     6435   8099  10394    105  -1250    257       C  
ATOM   5387  OG1 THR C  63     -55.540  -1.633  -5.130  1.00 64.41           O  
ANISOU 5387  OG1 THR C  63     6271   8023  10176    140  -1285    254       O  
ATOM   5388  CG2 THR C  63     -55.508  -2.737  -2.993  1.00 64.73           C  
ANISOU 5388  CG2 THR C  63     6261   7988  10342     88  -1239    182       C  
ATOM   5389  N   LEU C  64     -53.936   0.463  -1.585  1.00 65.94           N  
ANISOU 5389  N   LEU C  64     6575   7966  10513     58  -1190    346       N  
ATOM   5390  CA  LEU C  64     -53.257   0.651  -0.271  1.00 64.23           C  
ANISOU 5390  CA  LEU C  64     6366   7687  10349     19  -1152    345       C  
ATOM   5391  C   LEU C  64     -53.680   1.975   0.374  1.00 63.13           C  
ANISOU 5391  C   LEU C  64     6271   7477  10237     42  -1156    386       C  
ATOM   5392  O   LEU C  64     -53.565   2.079   1.611  1.00 61.57           O  
ANISOU 5392  O   LEU C  64     6065   7232  10095     25  -1135    372       O  
ATOM   5393  CB  LEU C  64     -51.739   0.616  -0.483  1.00 63.96           C  
ANISOU 5393  CB  LEU C  64     6352   7662  10285    -36  -1113    358       C  
ATOM   5394  CG  LEU C  64     -51.189  -0.702  -1.024  1.00 64.08           C  
ANISOU 5394  CG  LEU C  64     6324   7745  10278    -57  -1107    311       C  
ATOM   5395  CD1 LEU C  64     -49.730  -0.556  -1.442  1.00 64.21           C  
ANISOU 5395  CD1 LEU C  64     6360   7783  10253   -107  -1073    324       C  
ATOM   5396  CD2 LEU C  64     -51.346  -1.810   0.005  1.00 63.62           C  
ANISOU 5396  CD2 LEU C  64     6220   7676  10275    -60  -1100    253       C  
ATOM   5397  N   ARG C  65     -54.132   2.947  -0.425  1.00 62.69           N  
ANISOU 5397  N   ARG C  65     6263   7414  10142     81  -1181    436       N  
ATOM   5398  CA  ARG C  65     -54.615   4.265   0.074  1.00 62.99           C  
ANISOU 5398  CA  ARG C  65     6350   7379  10202    113  -1189    477       C  
ATOM   5399  C   ARG C  65     -55.982   4.062   0.734  1.00 61.93           C  
ANISOU 5399  C   ARG C  65     6168   7244  10117    165  -1224    433       C  
ATOM   5400  O   ARG C  65     -56.252   4.750   1.738  1.00 61.39           O  
ANISOU 5400  O   ARG C  65     6111   7115  10098    173  -1219    436       O  
ATOM   5401  CB  ARG C  65     -54.677   5.292  -1.063  1.00 64.29           C  
ANISOU 5401  CB  ARG C  65     6591   7534  10301    147  -1206    545       C  
ATOM   5402  CG  ARG C  65     -54.168   6.680  -0.702  1.00 64.93           C  
ANISOU 5402  CG  ARG C  65     6755   7525  10388    131  -1178    605       C  
ATOM   5403  CD  ARG C  65     -54.070   7.577  -1.933  1.00 66.50           C  
ANISOU 5403  CD  ARG C  65     7043   7713  10511    155  -1185    678       C  
ATOM   5404  NE  ARG C  65     -53.479   6.952  -3.120  1.00 66.83           N  
ANISOU 5404  NE  ARG C  65     7083   7829  10481    129  -1179    685       N  
ATOM   5405  CZ  ARG C  65     -52.203   7.070  -3.516  1.00 67.27           C  
ANISOU 5405  CZ  ARG C  65     7174   7886  10499     54  -1127    709       C  
ATOM   5406  NH1 ARG C  65     -51.328   7.788  -2.826  1.00 66.87           N  
ANISOU 5406  NH1 ARG C  65     7164   7767  10477     -6  -1075    727       N  
ATOM   5407  NH2 ARG C  65     -51.801   6.460  -4.620  1.00 67.20           N  
ANISOU 5407  NH2 ARG C  65     7155   7952  10423     39  -1127    709       N  
ATOM   5408  N   VAL C  66     -56.783   3.121   0.219  1.00 61.66           N  
ANISOU 5408  N   VAL C  66     6076   7279  10071    194  -1256    386       N  
ATOM   5409  CA  VAL C  66     -58.127   2.762   0.769  1.00 61.98           C  
ANISOU 5409  CA  VAL C  66     6058   7336  10154    235  -1285    327       C  
ATOM   5410  C   VAL C  66     -57.933   1.914   2.037  1.00 62.43           C  
ANISOU 5410  C   VAL C  66     6070   7375  10274    183  -1248    277       C  
ATOM   5411  O   VAL C  66     -58.412   2.347   3.108  1.00 63.52           O  
ANISOU 5411  O   VAL C  66     6202   7468  10463    191  -1245    265       O  
ATOM   5412  CB  VAL C  66     -59.002   2.025  -0.266  1.00 60.87           C  
ANISOU 5412  CB  VAL C  66     5867   7283   9975    275  -1325    284       C  
ATOM   5413  CG1 VAL C  66     -60.335   1.610   0.343  1.00 60.36           C  
ANISOU 5413  CG1 VAL C  66     5734   7240   9956    304  -1347    211       C  
ATOM   5414  CG2 VAL C  66     -59.219   2.840  -1.534  1.00 61.03           C  
ANISOU 5414  CG2 VAL C  66     5935   7328   9923    335  -1366    335       C  
ATOM   5415  N   GLU C  67     -57.267   0.757   1.908  1.00 61.83           N  
ANISOU 5415  N   GLU C  67     5968   7331  10191    137  -1223    249       N  
ATOM   5416  CA  GLU C  67     -56.995  -0.217   3.006  1.00 60.95           C  
ANISOU 5416  CA  GLU C  67     5825   7204  10128     92  -1188    203       C  
ATOM   5417  C   GLU C  67     -56.459   0.519   4.242  1.00 60.27           C  
ANISOU 5417  C   GLU C  67     5769   7048  10082     72  -1160    228       C  
ATOM   5418  O   GLU C  67     -56.919   0.204   5.351  1.00 60.69           O  
ANISOU 5418  O   GLU C  67     5797   7078  10183     65  -1147    193       O  
ATOM   5419  CB  GLU C  67     -55.994  -1.292   2.564  1.00 60.97           C  
ANISOU 5419  CB  GLU C  67     5820   7240  10106     52  -1165    189       C  
ATOM   5420  CG  GLU C  67     -56.573  -2.329   1.608  1.00 61.57           C  
ANISOU 5420  CG  GLU C  67     5852   7383  10156     62  -1184    142       C  
ATOM   5421  CD  GLU C  67     -55.569  -3.321   1.035  1.00 61.52           C  
ANISOU 5421  CD  GLU C  67     5841   7411  10122     28  -1165    128       C  
ATOM   5422  OE1 GLU C  67     -54.458  -3.442   1.606  1.00 63.97           O  
ANISOU 5422  OE1 GLU C  67     6172   7692  10439     -3  -1134    141       O  
ATOM   5423  OE2 GLU C  67     -55.886  -3.962   0.013  1.00 59.79           O  
ANISOU 5423  OE2 GLU C  67     5593   7252   9870     37  -1183     99       O  
ATOM   5424  N   ALA C  68     -55.530   1.461   4.057  1.00 59.59           N  
ANISOU 5424  N   ALA C  68     5734   6932   9975     60  -1148    283       N  
ATOM   5425  CA  ALA C  68     -54.898   2.260   5.136  1.00 58.67           C  
ANISOU 5425  CA  ALA C  68     5646   6753   9891     37  -1119    304       C  
ATOM   5426  C   ALA C  68     -55.970   3.066   5.876  1.00 57.37           C  
ANISOU 5426  C   ALA C  68     5480   6548   9770     74  -1137    301       C  
ATOM   5427  O   ALA C  68     -56.089   2.912   7.104  1.00 54.96           O  
ANISOU 5427  O   ALA C  68     5153   6216   9511     60  -1119    272       O  
ATOM   5428  CB  ALA C  68     -53.831   3.162   4.558  1.00 58.67           C  
ANISOU 5428  CB  ALA C  68     5701   6735   9855     14  -1102    358       C  
ATOM   5429  N   PHE C  69     -56.726   3.894   5.150  1.00 58.41           N  
ANISOU 5429  N   PHE C  69     5633   6676   9881    124  -1173    327       N  
ATOM   5430  CA  PHE C  69     -57.775   4.774   5.728  1.00 58.85           C  
ANISOU 5430  CA  PHE C  69     5691   6696   9973    172  -1197    323       C  
ATOM   5431  C   PHE C  69     -58.883   3.920   6.358  1.00 58.30           C  
ANISOU 5431  C   PHE C  69     5551   6659   9940    184  -1209    253       C  
ATOM   5432  O   PHE C  69     -59.372   4.279   7.439  1.00 57.42           O  
ANISOU 5432  O   PHE C  69     5424   6515   9876    189  -1203    231       O  
ATOM   5433  CB  PHE C  69     -58.340   5.738   4.683  1.00 58.97           C  
ANISOU 5433  CB  PHE C  69     5749   6708   9949    235  -1239    365       C  
ATOM   5434  CG  PHE C  69     -59.458   6.576   5.237  1.00 59.86           C  
ANISOU 5434  CG  PHE C  69     5857   6788  10096    294  -1270    352       C  
ATOM   5435  CD1 PHE C  69     -59.243   7.387   6.343  1.00 59.93           C  
ANISOU 5435  CD1 PHE C  69     5888   6728  10153    281  -1248    360       C  
ATOM   5436  CD2 PHE C  69     -60.739   6.501   4.705  1.00 61.28           C  
ANISOU 5436  CD2 PHE C  69     6003   7016  10263    364  -1322    320       C  
ATOM   5437  CE1 PHE C  69     -60.283   8.131   6.882  1.00 60.50           C  
ANISOU 5437  CE1 PHE C  69     5952   6774  10261    337  -1277    340       C  
ATOM   5438  CE2 PHE C  69     -61.777   7.246   5.246  1.00 61.04           C  
ANISOU 5438  CE2 PHE C  69     5961   6964  10265    423  -1353    298       C  
ATOM   5439  CZ  PHE C  69     -61.546   8.059   6.334  1.00 61.20           C  
ANISOU 5439  CZ  PHE C  69     6006   6910  10334    410  -1330    309       C  
ATOM   5440  N   GLU C  70     -59.258   2.820   5.704  1.00 60.00           N  
ANISOU 5440  N   GLU C  70     5724   6938  10133    183  -1220    216       N  
ATOM   5441  CA  GLU C  70     -60.292   1.861   6.191  1.00 62.46           C  
ANISOU 5441  CA  GLU C  70     5968   7286  10476    181  -1221    142       C  
ATOM   5442  C   GLU C  70     -59.892   1.336   7.575  1.00 61.49           C  
ANISOU 5442  C   GLU C  70     5836   7128  10399    130  -1175    119       C  
ATOM   5443  O   GLU C  70     -60.784   1.256   8.435  1.00 61.82           O  
ANISOU 5443  O   GLU C  70     5843   7166  10480    133  -1172     74       O  
ATOM   5444  CB  GLU C  70     -60.463   0.700   5.201  1.00 64.79           C  
ANISOU 5444  CB  GLU C  70     6229   7650  10738    174  -1229    107       C  
ATOM   5445  CG  GLU C  70     -61.879   0.166   5.048  1.00 67.66           C  
ANISOU 5445  CG  GLU C  70     6527   8069  11112    199  -1253     34       C  
ATOM   5446  CD  GLU C  70     -62.321   0.013   3.596  1.00 71.37           C  
ANISOU 5446  CD  GLU C  70     6977   8610  11528    241  -1295     24       C  
ATOM   5447  OE1 GLU C  70     -62.576  -1.137   3.149  1.00 74.41           O  
ANISOU 5447  OE1 GLU C  70     7317   9049  11904    218  -1289    -29       O  
ATOM   5448  OE2 GLU C  70     -62.411   1.054   2.910  1.00 73.99           O  
ANISOU 5448  OE2 GLU C  70     7343   8942  11825    298  -1334     70       O  
ATOM   5449  N   TYR C  71     -58.602   1.014   7.771  1.00 59.46           N  
ANISOU 5449  N   TYR C  71     5608   6851  10132     87  -1142    146       N  
ATOM   5450  CA  TYR C  71     -58.038   0.321   8.962  1.00 56.94           C  
ANISOU 5450  CA  TYR C  71     5285   6507   9842     43  -1100    126       C  
ATOM   5451  C   TYR C  71     -57.656   1.330  10.054  1.00 55.87           C  
ANISOU 5451  C   TYR C  71     5173   6317   9736     39  -1085    149       C  
ATOM   5452  O   TYR C  71     -57.933   1.037  11.232  1.00 56.29           O  
ANISOU 5452  O   TYR C  71     5210   6353   9824     24  -1063    119       O  
ATOM   5453  CB  TYR C  71     -56.830  -0.531   8.560  1.00 56.61           C  
ANISOU 5453  CB  TYR C  71     5258   6480   9769     11  -1079    136       C  
ATOM   5454  CG  TYR C  71     -56.378  -1.528   9.599  1.00 56.39           C  
ANISOU 5454  CG  TYR C  71     5227   6437   9759    -20  -1043    108       C  
ATOM   5455  CD1 TYR C  71     -57.251  -2.492  10.066  1.00 57.03           C  
ANISOU 5455  CD1 TYR C  71     5282   6524   9862    -29  -1031     60       C  
ATOM   5456  CD2 TYR C  71     -55.088  -1.531  10.106  1.00 55.52           C  
ANISOU 5456  CD2 TYR C  71     5142   6310   9642    -40  -1019    127       C  
ATOM   5457  CE1 TYR C  71     -56.863  -3.425  11.014  1.00 56.56           C  
ANISOU 5457  CE1 TYR C  71     5233   6443   9813    -55   -996     40       C  
ATOM   5458  CE2 TYR C  71     -54.685  -2.444  11.070  1.00 55.06           C  
ANISOU 5458  CE2 TYR C  71     5087   6238   9593    -56   -991    104       C  
ATOM   5459  CZ  TYR C  71     -55.574  -3.404  11.520  1.00 55.04           C  
ANISOU 5459  CZ  TYR C  71     5070   6232   9609    -63   -979     65       C  
ATOM   5460  OH  TYR C  71     -55.196  -4.314  12.466  1.00 53.51           O  
ANISOU 5460  OH  TYR C  71     4893   6018   9420    -76   -949     47       O  
ATOM   5461  N   TYR C  72     -57.040   2.462   9.685  1.00 54.28           N  
ANISOU 5461  N   TYR C  72     5011   6089   9521     48  -1092    198       N  
ATOM   5462  CA  TYR C  72     -56.420   3.443  10.618  1.00 53.02           C  
ANISOU 5462  CA  TYR C  72     4879   5879   9387     35  -1071    219       C  
ATOM   5463  C   TYR C  72     -57.352   4.632  10.897  1.00 52.47           C  
ANISOU 5463  C   TYR C  72     4815   5774   9346     75  -1094    224       C  
ATOM   5464  O   TYR C  72     -57.213   5.236  11.985  1.00 51.32           O  
ANISOU 5464  O   TYR C  72     4672   5589   9236     65  -1076    219       O  
ATOM   5465  CB  TYR C  72     -55.060   3.897  10.078  1.00 53.07           C  
ANISOU 5465  CB  TYR C  72     4927   5876   9361      8  -1053    261       C  
ATOM   5466  CG  TYR C  72     -54.031   2.796  10.028  1.00 52.04           C  
ANISOU 5466  CG  TYR C  72     4786   5779   9207    -26  -1030    247       C  
ATOM   5467  CD1 TYR C  72     -53.562   2.303   8.823  1.00 52.05           C  
ANISOU 5467  CD1 TYR C  72     4794   5820   9162    -33  -1036    259       C  
ATOM   5468  CD2 TYR C  72     -53.563   2.207  11.189  1.00 51.51           C  
ANISOU 5468  CD2 TYR C  72     4703   5708   9160    -47  -1003    217       C  
ATOM   5469  CE1 TYR C  72     -52.634   1.277   8.777  1.00 51.46           C  
ANISOU 5469  CE1 TYR C  72     4707   5778   9067    -59  -1017    240       C  
ATOM   5470  CE2 TYR C  72     -52.633   1.180  11.163  1.00 51.15           C  
ANISOU 5470  CE2 TYR C  72     4650   5692   9090    -67   -986    202       C  
ATOM   5471  CZ  TYR C  72     -52.165   0.713   9.951  1.00 50.94           C  
ANISOU 5471  CZ  TYR C  72     4627   5703   9022    -73   -994    211       C  
ATOM   5472  OH  TYR C  72     -51.259  -0.307   9.938  1.00 49.97           O  
ANISOU 5472  OH  TYR C  72     4497   5611   8877    -87   -980    189       O  
ATOM   5473  N   HIS C  73     -58.267   4.959   9.974  1.00 53.30           N  
ANISOU 5473  N   HIS C  73     4920   5896   9435    122  -1134    231       N  
ATOM   5474  CA  HIS C  73     -59.219   6.103  10.079  1.00 53.26           C  
ANISOU 5474  CA  HIS C  73     4924   5861   9452    176  -1165    234       C  
ATOM   5475  C   HIS C  73     -58.429   7.415  10.116  1.00 55.24           C  
ANISOU 5475  C   HIS C  73     5240   6045   9703    173  -1153    288       C  
ATOM   5476  O   HIS C  73     -58.839   8.316  10.866  1.00 55.83           O  
ANISOU 5476  O   HIS C  73     5322   6075   9816    195  -1157    282       O  
ATOM   5477  CB  HIS C  73     -60.127   5.964  11.310  1.00 51.31           C  
ANISOU 5477  CB  HIS C  73     4627   5613   9255    181  -1162    177       C  
ATOM   5478  CG  HIS C  73     -61.229   4.975  11.143  1.00 50.46           C  
ANISOU 5478  CG  HIS C  73     4458   5565   9147    193  -1178    119       C  
ATOM   5479  ND1 HIS C  73     -62.298   4.899  12.016  1.00 49.33           N  
ANISOU 5479  ND1 HIS C  73     4265   5433   9042    203  -1181     61       N  
ATOM   5480  CD2 HIS C  73     -61.455   4.043  10.193  1.00 49.96           C  
ANISOU 5480  CD2 HIS C  73     4373   5557   9050    194  -1191    104       C  
ATOM   5481  CE1 HIS C  73     -63.115   3.951  11.619  1.00 48.86           C  
ANISOU 5481  CE1 HIS C  73     4157   5432   8973    204  -1190     10       C  
ATOM   5482  NE2 HIS C  73     -62.625   3.408  10.509  1.00 49.02           N  
ANISOU 5482  NE2 HIS C  73     4193   5479   8951    199  -1197     35       N  
ATOM   5483  N   THR C  74     -57.350   7.512   9.326  1.00 55.84           N  
ANISOU 5483  N   THR C  74     5361   6116   9739    145  -1137    334       N  
ATOM   5484  CA  THR C  74     -56.505   8.726   9.204  1.00 57.13           C  
ANISOU 5484  CA  THR C  74     5594   6216   9896    128  -1116    385       C  
ATOM   5485  C   THR C  74     -55.820   8.755   7.833  1.00 58.31           C  
ANISOU 5485  C   THR C  74     5791   6380   9982    117  -1114    435       C  
ATOM   5486  O   THR C  74     -55.475   7.676   7.319  1.00 58.37           O  
ANISOU 5486  O   THR C  74     5769   6447   9959     95  -1111    421       O  
ATOM   5487  CB  THR C  74     -55.477   8.801  10.339  1.00 56.91           C  
ANISOU 5487  CB  THR C  74     5560   6163   9900     68  -1067    369       C  
ATOM   5488  OG1 THR C  74     -54.944  10.126  10.324  1.00 57.49           O  
ANISOU 5488  OG1 THR C  74     5695   6168   9977     56  -1048    407       O  
ATOM   5489  CG2 THR C  74     -54.362   7.783  10.211  1.00 57.10           C  
ANISOU 5489  CG2 THR C  74     5565   6234   9896     14  -1037    359       C  
ATOM   5490  N   THR C  75     -55.634   9.958   7.283  1.00 59.44           N  
ANISOU 5490  N   THR C  75     6010   6467  10107    131  -1114    489       N  
ATOM   5491  CA  THR C  75     -55.011  10.213   5.954  1.00 60.67           C  
ANISOU 5491  CA  THR C  75     6229   6627  10197    120  -1108    545       C  
ATOM   5492  C   THR C  75     -53.569  10.723   6.151  1.00 61.37           C  
ANISOU 5492  C   THR C  75     6359   6676  10281     39  -1046    565       C  
ATOM   5493  O   THR C  75     -52.834  10.820   5.137  1.00 62.24           O  
ANISOU 5493  O   THR C  75     6515   6797  10335      9  -1027    604       O  
ATOM   5494  CB  THR C  75     -55.886  11.160   5.110  1.00 61.68           C  
ANISOU 5494  CB  THR C  75     6421   6719  10295    197  -1150    592       C  
ATOM   5495  OG1 THR C  75     -57.234  11.149   5.588  1.00 60.99           O  
ANISOU 5495  OG1 THR C  75     6290   6639  10243    269  -1198    555       O  
ATOM   5496  CG2 THR C  75     -55.892  10.802   3.636  1.00 61.53           C  
ANISOU 5496  CG2 THR C  75     6427   6752  10200    218  -1172    627       C  
ATOM   5497  N   ASP C  76     -53.170  11.026   7.396  1.00 60.29           N  
ANISOU 5497  N   ASP C  76     6203   6504  10198      4  -1015    535       N  
ATOM   5498  CA  ASP C  76     -51.842  11.600   7.760  1.00 59.56           C  
ANISOU 5498  CA  ASP C  76     6141   6378  10111    -73   -954    539       C  
ATOM   5499  C   ASP C  76     -50.726  10.715   7.206  1.00 59.36           C  
ANISOU 5499  C   ASP C  76     6091   6420  10040   -130   -927    528       C  
ATOM   5500  O   ASP C  76     -50.475   9.629   7.722  1.00 59.05           O  
ANISOU 5500  O   ASP C  76     5984   6439  10011   -142   -927    481       O  
ATOM   5501  CB  ASP C  76     -51.699  11.755   9.277  1.00 58.54           C  
ANISOU 5501  CB  ASP C  76     5969   6227  10046    -93   -933    490       C  
ATOM   5502  CG  ASP C  76     -50.304  12.151   9.733  1.00 57.79           C  
ANISOU 5502  CG  ASP C  76     5882   6118   9955   -174   -873    474       C  
ATOM   5503  OD1 ASP C  76     -49.452  12.403   8.853  1.00 57.54           O  
ANISOU 5503  OD1 ASP C  76     5895   6088   9879   -220   -842    502       O  
ATOM   5504  OD2 ASP C  76     -50.078  12.197  10.965  1.00 56.55           O  
ANISOU 5504  OD2 ASP C  76     5685   5957   9844   -192   -855    428       O  
ATOM   5505  N   PRO C  77     -49.990  11.157   6.164  1.00 59.61           N  
ANISOU 5505  N   PRO C  77     6184   6445  10019   -168   -900    570       N  
ATOM   5506  CA  PRO C  77     -49.007  10.296   5.501  1.00 58.98           C  
ANISOU 5506  CA  PRO C  77     6078   6438   9891   -216   -879    557       C  
ATOM   5507  C   PRO C  77     -47.717  10.086   6.311  1.00 57.91           C  
ANISOU 5507  C   PRO C  77     5902   6327   9772   -289   -829    505       C  
ATOM   5508  O   PRO C  77     -46.840   9.387   5.825  1.00 58.00           O  
ANISOU 5508  O   PRO C  77     5887   6403   9745   -327   -811    485       O  
ATOM   5509  CB  PRO C  77     -48.704  11.062   4.208  1.00 59.86           C  
ANISOU 5509  CB  PRO C  77     6276   6525   9940   -235   -861    620       C  
ATOM   5510  CG  PRO C  77     -48.878  12.509   4.619  1.00 60.64           C  
ANISOU 5510  CG  PRO C  77     6449   6520  10069   -237   -840    654       C  
ATOM   5511  CD  PRO C  77     -50.051  12.504   5.578  1.00 60.43           C  
ANISOU 5511  CD  PRO C  77     6387   6469  10105   -166   -886    632       C  
ATOM   5512  N   SER C  78     -47.624  10.698   7.498  1.00 56.18           N  
ANISOU 5512  N   SER C  78     5675   6062   9608   -302   -809    480       N  
ATOM   5513  CA  SER C  78     -46.527  10.485   8.480  1.00 54.86           C  
ANISOU 5513  CA  SER C  78     5457   5923   9462   -357   -769    419       C  
ATOM   5514  C   SER C  78     -46.873   9.334   9.436  1.00 53.87           C  
ANISOU 5514  C   SER C  78     5254   5846   9365   -318   -799    370       C  
ATOM   5515  O   SER C  78     -45.940   8.808  10.067  1.00 51.49           O  
ANISOU 5515  O   SER C  78     4905   5592   9065   -348   -777    318       O  
ATOM   5516  CB  SER C  78     -46.226  11.756   9.241  1.00 55.36           C  
ANISOU 5516  CB  SER C  78     5553   5915   9564   -393   -729    414       C  
ATOM   5517  OG  SER C  78     -47.144  11.968  10.309  1.00 54.74           O  
ANISOU 5517  OG  SER C  78     5455   5797   9544   -345   -756    400       O  
ATOM   5518  N   PHE C  79     -48.153   8.938   9.509  1.00 54.13           N  
ANISOU 5518  N   PHE C  79     5277   5870   9417   -253   -846    382       N  
ATOM   5519  CA  PHE C  79     -48.698   8.011  10.538  1.00 52.96           C  
ANISOU 5519  CA  PHE C  79     5070   5749   9303   -218   -870    340       C  
ATOM   5520  C   PHE C  79     -47.837   6.749  10.614  1.00 52.52           C  
ANISOU 5520  C   PHE C  79     4967   5766   9222   -235   -862    300       C  
ATOM   5521  O   PHE C  79     -47.277   6.477  11.693  1.00 52.97           O  
ANISOU 5521  O   PHE C  79     4989   5839   9297   -246   -845    257       O  
ATOM   5522  CB  PHE C  79     -50.164   7.628  10.290  1.00 52.03           C  
ANISOU 5522  CB  PHE C  79     4945   5626   9195   -155   -917    355       C  
ATOM   5523  CG  PHE C  79     -50.736   6.821  11.429  1.00 50.58           C  
ANISOU 5523  CG  PHE C  79     4710   5459   9049   -131   -930    311       C  
ATOM   5524  CD1 PHE C  79     -51.159   7.442  12.599  1.00 50.14           C  
ANISOU 5524  CD1 PHE C  79     4646   5363   9042   -122   -925    294       C  
ATOM   5525  CD2 PHE C  79     -50.767   5.438  11.373  1.00 49.77           C  
ANISOU 5525  CD2 PHE C  79     4570   5409   8930   -123   -940    285       C  
ATOM   5526  CE1 PHE C  79     -51.598   6.700  13.688  1.00 49.55           C  
ANISOU 5526  CE1 PHE C  79     4528   5304   8994   -107   -929    254       C  
ATOM   5527  CE2 PHE C  79     -51.234   4.701  12.451  1.00 49.43           C  
ANISOU 5527  CE2 PHE C  79     4490   5374   8915   -107   -943    249       C  
ATOM   5528  CZ  PHE C  79     -51.656   5.329  13.602  1.00 49.22           C  
ANISOU 5528  CZ  PHE C  79     4457   5310   8932   -100   -937    234       C  
ATOM   5529  N   LEU C  80     -47.752   6.012   9.508  1.00 52.77           N  
ANISOU 5529  N   LEU C  80     4998   5841   9209   -231   -875    312       N  
ATOM   5530  CA  LEU C  80     -47.035   4.707   9.411  1.00 53.80           C  
ANISOU 5530  CA  LEU C  80     5087   6041   9313   -237   -874    274       C  
ATOM   5531  C   LEU C  80     -45.610   4.854   9.948  1.00 52.07           C  
ANISOU 5531  C   LEU C  80     4849   5848   9084   -282   -836    235       C  
ATOM   5532  O   LEU C  80     -45.248   4.115  10.878  1.00 50.66           O  
ANISOU 5532  O   LEU C  80     4632   5697   8916   -269   -836    191       O  
ATOM   5533  CB  LEU C  80     -47.001   4.244   7.952  1.00 55.98           C  
ANISOU 5533  CB  LEU C  80     5375   6356   9539   -238   -887    296       C  
ATOM   5534  CG  LEU C  80     -48.097   3.272   7.531  1.00 57.34           C  
ANISOU 5534  CG  LEU C  80     5530   6546   9709   -191   -927    297       C  
ATOM   5535  CD1 LEU C  80     -49.486   3.729   7.982  1.00 57.56           C  
ANISOU 5535  CD1 LEU C  80     5565   6525   9777   -150   -952    313       C  
ATOM   5536  CD2 LEU C  80     -48.054   3.104   6.026  1.00 58.83           C  
ANISOU 5536  CD2 LEU C  80     5734   6771   9844   -194   -938    322       C  
ATOM   5537  N   GLY C  81     -44.851   5.783   9.363  1.00 51.34           N  
ANISOU 5537  N   GLY C  81     4785   5749   8970   -333   -804    250       N  
ATOM   5538  CA  GLY C  81     -43.504   6.162   9.813  1.00 51.52           C  
ANISOU 5538  CA  GLY C  81     4789   5798   8986   -387   -761    206       C  
ATOM   5539  C   GLY C  81     -43.396   6.128  11.325  1.00 51.34           C  
ANISOU 5539  C   GLY C  81     4731   5771   9003   -372   -757    161       C  
ATOM   5540  O   GLY C  81     -42.515   5.415  11.823  1.00 53.30           O  
ANISOU 5540  O   GLY C  81     4934   6080   9238   -372   -752    107       O  
ATOM   5541  N   ARG C  82     -44.272   6.841  12.039  1.00 51.27           N  
ANISOU 5541  N   ARG C  82     4740   5698   9041   -353   -764    180       N  
ATOM   5542  CA  ARG C  82     -44.154   7.064  13.510  1.00 51.28           C  
ANISOU 5542  CA  ARG C  82     4711   5690   9080   -347   -755    139       C  
ATOM   5543  C   ARG C  82     -44.608   5.805  14.258  1.00 50.64           C  
ANISOU 5543  C   ARG C  82     4595   5639   9004   -291   -786    117       C  
ATOM   5544  O   ARG C  82     -43.976   5.465  15.289  1.00 49.58           O  
ANISOU 5544  O   ARG C  82     4425   5539   8872   -285   -778     68       O  
ATOM   5545  CB  ARG C  82     -44.951   8.298  13.946  1.00 51.98           C  
ANISOU 5545  CB  ARG C  82     4834   5699   9216   -347   -750    165       C  
ATOM   5546  CG  ARG C  82     -44.522   9.584  13.247  1.00 52.81           C  
ANISOU 5546  CG  ARG C  82     4989   5759   9316   -402   -713    191       C  
ATOM   5547  CD  ARG C  82     -45.248  10.822  13.740  1.00 53.15           C  
ANISOU 5547  CD  ARG C  82     5070   5716   9408   -398   -707    212       C  
ATOM   5548  NE  ARG C  82     -46.506  10.509  14.414  1.00 52.48           N  
ANISOU 5548  NE  ARG C  82     4970   5610   9358   -333   -749    218       N  
ATOM   5549  CZ  ARG C  82     -47.715  10.534  13.857  1.00 52.62           C  
ANISOU 5549  CZ  ARG C  82     5017   5593   9381   -286   -786    263       C  
ATOM   5550  NH1 ARG C  82     -47.881  10.838  12.577  1.00 53.46           N  
ANISOU 5550  NH1 ARG C  82     5175   5679   9456   -287   -792    315       N  
ATOM   5551  NH2 ARG C  82     -48.768  10.223  14.597  1.00 52.37           N  
ANISOU 5551  NH2 ARG C  82     4959   5554   9382   -236   -817    253       N  
ATOM   5552  N   TYR C  83     -45.655   5.147  13.751  1.00 51.08           N  
ANISOU 5552  N   TYR C  83     4664   5683   9060   -253   -819    150       N  
ATOM   5553  CA  TYR C  83     -46.174   3.847  14.255  1.00 51.36           C  
ANISOU 5553  CA  TYR C  83     4677   5740   9097   -208   -844    134       C  
ATOM   5554  C   TYR C  83     -45.053   2.800  14.190  1.00 50.60           C  
ANISOU 5554  C   TYR C  83     4555   5709   8960   -206   -840     96       C  
ATOM   5555  O   TYR C  83     -44.737   2.173  15.227  1.00 49.98           O  
ANISOU 5555  O   TYR C  83     4456   5651   8881   -182   -840     61       O  
ATOM   5556  CB  TYR C  83     -47.443   3.457  13.484  1.00 51.75           C  
ANISOU 5556  CB  TYR C  83     4742   5769   9149   -181   -873    170       C  
ATOM   5557  CG  TYR C  83     -47.916   2.041  13.697  1.00 51.40           C  
ANISOU 5557  CG  TYR C  83     4682   5746   9100   -148   -890    153       C  
ATOM   5558  CD1 TYR C  83     -47.859   1.443  14.949  1.00 50.72           C  
ANISOU 5558  CD1 TYR C  83     4581   5662   9025   -130   -885    122       C  
ATOM   5559  CD2 TYR C  83     -48.426   1.298  12.641  1.00 51.74           C  
ANISOU 5559  CD2 TYR C  83     4729   5805   9123   -137   -910    166       C  
ATOM   5560  CE1 TYR C  83     -48.278   0.139  15.139  1.00 50.83           C  
ANISOU 5560  CE1 TYR C  83     4594   5686   9032   -104   -894    110       C  
ATOM   5561  CE2 TYR C  83     -48.844  -0.010  12.814  1.00 51.75           C  
ANISOU 5561  CE2 TYR C  83     4720   5820   9121   -114   -920    146       C  
ATOM   5562  CZ  TYR C  83     -48.765  -0.587  14.069  1.00 51.70           C  
ANISOU 5562  CZ  TYR C  83     4708   5807   9127    -99   -910    120       C  
ATOM   5563  OH  TYR C  83     -49.183  -1.866  14.276  1.00 52.46           O  
ANISOU 5563  OH  TYR C  83     4807   5905   9220    -80   -913    104       O  
ATOM   5564  N   MET C  84     -44.450   2.639  13.013  1.00 50.73           N  
ANISOU 5564  N   MET C  84     4576   5759   8940   -228   -836    102       N  
ATOM   5565  CA  MET C  84     -43.323   1.698  12.779  1.00 51.03           C  
ANISOU 5565  CA  MET C  84     4587   5865   8936   -226   -834     60       C  
ATOM   5566  C   MET C  84     -42.141   2.073  13.680  1.00 50.28           C  
ANISOU 5566  C   MET C  84     4461   5805   8835   -242   -810      8       C  
ATOM   5567  O   MET C  84     -41.551   1.145  14.266  1.00 50.05           O  
ANISOU 5567  O   MET C  84     4407   5820   8787   -207   -820    -34       O  
ATOM   5568  CB  MET C  84     -42.899   1.694  11.304  1.00 52.48           C  
ANISOU 5568  CB  MET C  84     4777   6080   9081   -257   -830     74       C  
ATOM   5569  CG  MET C  84     -43.936   1.045  10.386  1.00 53.79           C  
ANISOU 5569  CG  MET C  84     4961   6233   9241   -232   -859    111       C  
ATOM   5570  SD  MET C  84     -44.127  -0.752  10.620  1.00 55.42           S  
ANISOU 5570  SD  MET C  84     5149   6467   9439   -179   -885     80       S  
ATOM   5571  CE  MET C  84     -45.512  -0.824  11.758  1.00 54.95           C  
ANISOU 5571  CE  MET C  84     5102   6344   9430   -146   -896     96       C  
ATOM   5572  N   SER C  85     -41.819   3.368  13.794  1.00 49.90           N  
ANISOU 5572  N   SER C  85     4418   5737   8802   -290   -781      8       N  
ATOM   5573  CA  SER C  85     -40.750   3.895  14.687  1.00 50.18           C  
ANISOU 5573  CA  SER C  85     4420   5807   8838   -313   -754    -49       C  
ATOM   5574  C   SER C  85     -41.043   3.471  16.125  1.00 49.65           C  
ANISOU 5574  C   SER C  85     4335   5737   8791   -262   -770    -73       C  
ATOM   5575  O   SER C  85     -40.188   2.803  16.747  1.00 50.37           O  
ANISOU 5575  O   SER C  85     4391   5889   8856   -234   -774   -127       O  
ATOM   5576  CB  SER C  85     -40.617   5.392  14.621  1.00 50.31           C  
ANISOU 5576  CB  SER C  85     4453   5783   8877   -375   -717    -41       C  
ATOM   5577  OG  SER C  85     -40.089   5.799  13.380  1.00 51.12           O  
ANISOU 5577  OG  SER C  85     4574   5897   8951   -430   -692    -27       O  
ATOM   5578  N   ALA C  86     -42.208   3.870  16.630  1.00 48.81           N  
ANISOU 5578  N   ALA C  86     4253   5565   8727   -248   -778    -36       N  
ATOM   5579  CA  ALA C  86     -42.705   3.483  17.965  1.00 47.84           C  
ANISOU 5579  CA  ALA C  86     4121   5432   8622   -203   -791    -50       C  
ATOM   5580  C   ALA C  86     -42.549   1.967  18.126  1.00 46.73           C  
ANISOU 5580  C   ALA C  86     3976   5330   8448   -149   -814    -64       C  
ATOM   5581  O   ALA C  86     -41.894   1.536  19.095  1.00 46.23           O  
ANISOU 5581  O   ALA C  86     3892   5308   8366   -118   -816   -107       O  
ATOM   5582  CB  ALA C  86     -44.137   3.920  18.114  1.00 47.72           C  
ANISOU 5582  CB  ALA C  86     4135   5346   8651   -195   -800     -4       C  
ATOM   5583  N   LEU C  87     -43.089   1.209  17.166  1.00 46.05           N  
ANISOU 5583  N   LEU C  87     3912   5232   8352   -139   -831    -30       N  
ATOM   5584  CA  LEU C  87     -43.187  -0.273  17.204  1.00 45.56           C  
ANISOU 5584  CA  LEU C  87     3858   5186   8264    -90   -852    -36       C  
ATOM   5585  C   LEU C  87     -41.797  -0.882  17.404  1.00 45.12           C  
ANISOU 5585  C   LEU C  87     3778   5201   8164    -67   -854    -89       C  
ATOM   5586  O   LEU C  87     -41.663  -1.788  18.263  1.00 44.13           O  
ANISOU 5586  O   LEU C  87     3658   5086   8020    -13   -865   -109       O  
ATOM   5587  CB  LEU C  87     -43.820  -0.774  15.902  1.00 45.30           C  
ANISOU 5587  CB  LEU C  87     3844   5138   8227    -97   -865     -1       C  
ATOM   5588  CG  LEU C  87     -43.923  -2.297  15.783  1.00 44.70           C  
ANISOU 5588  CG  LEU C  87     3782   5073   8128    -55   -882     -9       C  
ATOM   5589  CD1 LEU C  87     -44.638  -2.902  16.983  1.00 44.03           C  
ANISOU 5589  CD1 LEU C  87     3718   4952   8058    -19   -883     -7       C  
ATOM   5590  CD2 LEU C  87     -44.617  -2.697  14.493  1.00 44.81           C  
ANISOU 5590  CD2 LEU C  87     3808   5076   8142    -67   -893     18       C  
ATOM   5591  N   ASN C  88     -40.818  -0.382  16.641  1.00 45.61           N  
ANISOU 5591  N   ASN C  88     3814   5310   8206   -104   -841   -113       N  
ATOM   5592  CA  ASN C  88     -39.404  -0.854  16.623  1.00 46.09           C  
ANISOU 5592  CA  ASN C  88     3837   5452   8221    -88   -842   -176       C  
ATOM   5593  C   ASN C  88     -38.831  -0.931  18.048  1.00 46.11           C  
ANISOU 5593  C   ASN C  88     3818   5487   8213    -46   -845   -225       C  
ATOM   5594  O   ASN C  88     -37.947  -1.769  18.273  1.00 46.49           O  
ANISOU 5594  O   ASN C  88     3847   5595   8219      2   -861   -273       O  
ATOM   5595  CB  ASN C  88     -38.537   0.036  15.728  1.00 46.37           C  
ANISOU 5595  CB  ASN C  88     3845   5528   8244   -155   -816   -199       C  
ATOM   5596  CG  ASN C  88     -37.360  -0.702  15.123  1.00 47.10           C  
ANISOU 5596  CG  ASN C  88     3904   5705   8287   -143   -822   -253       C  
ATOM   5597  OD1 ASN C  88     -37.366  -1.930  15.018  1.00 47.61           O  
ANISOU 5597  OD1 ASN C  88     3976   5783   8329    -86   -850   -259       O  
ATOM   5598  ND2 ASN C  88     -36.352   0.041  14.700  1.00 47.39           N  
ANISOU 5598  ND2 ASN C  88     3903   5795   8306   -200   -793   -297       N  
ATOM   5599  N   HIS C  89     -39.301  -0.074  18.961  1.00 46.71           N  
ANISOU 5599  N   HIS C  89     3895   5528   8322    -60   -832   -216       N  
ATOM   5600  CA  HIS C  89     -38.897  -0.020  20.394  1.00 47.10           C  
ANISOU 5600  CA  HIS C  89     3924   5607   8364    -21   -833   -259       C  
ATOM   5601  C   HIS C  89     -39.814  -0.909  21.254  1.00 46.78           C  
ANISOU 5601  C   HIS C  89     3926   5522   8325     39   -852   -226       C  
ATOM   5602  O   HIS C  89     -39.269  -1.712  22.049  1.00 46.55           O  
ANISOU 5602  O   HIS C  89     3897   5532   8257    104   -869   -259       O  
ATOM   5603  CB  HIS C  89     -38.883   1.445  20.863  1.00 47.53           C  
ANISOU 5603  CB  HIS C  89     3955   5648   8454    -77   -804   -274       C  
ATOM   5604  CG  HIS C  89     -37.803   2.286  20.255  1.00 48.75           C  
ANISOU 5604  CG  HIS C  89     4068   5852   8599   -138   -777   -321       C  
ATOM   5605  ND1 HIS C  89     -36.718   2.748  20.998  1.00 49.05           N  
ANISOU 5605  ND1 HIS C  89     4052   5962   8621   -144   -762   -400       N  
ATOM   5606  CD2 HIS C  89     -37.597   2.723  18.988  1.00 49.12           C  
ANISOU 5606  CD2 HIS C  89     4119   5894   8647   -199   -758   -305       C  
ATOM   5607  CE1 HIS C  89     -35.909   3.442  20.219  1.00 49.05           C  
ANISOU 5607  CE1 HIS C  89     4024   5995   8616   -213   -731   -435       C  
ATOM   5608  NE2 HIS C  89     -36.416   3.428  18.980  1.00 49.23           N  
ANISOU 5608  NE2 HIS C  89     4086   5971   8647   -247   -727   -374       N  
ATOM   5609  N   THR C  90     -41.144  -0.785  21.093  1.00 46.28           N  
ANISOU 5609  N   THR C  90     3898   5382   8301     19   -850   -167       N  
ATOM   5610  CA  THR C  90     -42.175  -1.375  22.000  1.00 45.73           C  
ANISOU 5610  CA  THR C  90     3867   5265   8242     56   -856   -138       C  
ATOM   5611  C   THR C  90     -42.151  -2.905  21.915  1.00 45.30           C  
ANISOU 5611  C   THR C  90     3850   5210   8150    112   -873   -132       C  
ATOM   5612  O   THR C  90     -42.546  -3.544  22.909  1.00 45.75           O  
ANISOU 5612  O   THR C  90     3941   5247   8196    154   -875   -125       O  
ATOM   5613  CB  THR C  90     -43.597  -0.870  21.718  1.00 46.04           C  
ANISOU 5613  CB  THR C  90     3927   5232   8332     19   -848    -88       C  
ATOM   5614  OG1 THR C  90     -43.999  -1.249  20.400  1.00 46.00           O  
ANISOU 5614  OG1 THR C  90     3937   5209   8331      0   -855    -58       O  
ATOM   5615  CG2 THR C  90     -43.736   0.628  21.883  1.00 46.65           C  
ANISOU 5615  CG2 THR C  90     3979   5295   8449    -27   -832    -91       C  
ATOM   5616  N   LYS C  91     -41.702  -3.458  20.784  1.00 44.79           N  
ANISOU 5616  N   LYS C  91     3784   5167   8067    111   -883   -135       N  
ATOM   5617  CA  LYS C  91     -41.518  -4.918  20.568  1.00 45.06           C  
ANISOU 5617  CA  LYS C  91     3852   5202   8065    165   -900   -137       C  
ATOM   5618  C   LYS C  91     -40.334  -5.450  21.408  1.00 45.82           C  
ANISOU 5618  C   LYS C  91     3941   5357   8109    234   -915   -187       C  
ATOM   5619  O   LYS C  91     -40.176  -6.679  21.464  1.00 45.74           O  
ANISOU 5619  O   LYS C  91     3971   5340   8065    293   -930   -189       O  
ATOM   5620  CB  LYS C  91     -41.324  -5.196  19.072  1.00 44.90           C  
ANISOU 5620  CB  LYS C  91     3822   5196   8041    139   -906   -134       C  
ATOM   5621  CG  LYS C  91     -39.953  -4.801  18.532  1.00 45.76           C  
ANISOU 5621  CG  LYS C  91     3879   5384   8121    130   -909   -184       C  
ATOM   5622  CD  LYS C  91     -39.641  -5.228  17.112  1.00 45.71           C  
ANISOU 5622  CD  LYS C  91     3864   5403   8100    112   -916   -188       C  
ATOM   5623  CE  LYS C  91     -38.170  -5.081  16.779  1.00 45.41           C  
ANISOU 5623  CE  LYS C  91     3774   5454   8023    114   -919   -252       C  
ATOM   5624  NZ  LYS C  91     -37.929  -4.994  15.321  1.00 45.33           N  
ANISOU 5624  NZ  LYS C  91     3746   5471   8006     68   -914   -252       N  
ATOM   5625  N   LYS C  92     -39.508  -4.583  22.014  1.00 46.88           N  
ANISOU 5625  N   LYS C  92     4027   5549   8234    232   -912   -231       N  
ATOM   5626  CA  LYS C  92     -38.359  -4.991  22.878  1.00 47.94           C  
ANISOU 5626  CA  LYS C  92     4146   5755   8315    305   -930   -289       C  
ATOM   5627  C   LYS C  92     -38.712  -4.795  24.356  1.00 46.81           C  
ANISOU 5627  C   LYS C  92     4020   5598   8168    337   -926   -285       C  
ATOM   5628  O   LYS C  92     -37.929  -5.268  25.210  1.00 45.97           O  
ANISOU 5628  O   LYS C  92     3912   5542   8009    412   -945   -325       O  
ATOM   5629  CB  LYS C  92     -37.093  -4.199  22.532  1.00 49.61           C  
ANISOU 5629  CB  LYS C  92     4281   6057   8512    279   -927   -358       C  
ATOM   5630  CG  LYS C  92     -36.507  -4.528  21.169  1.00 51.38           C  
ANISOU 5630  CG  LYS C  92     4484   6314   8723    260   -932   -376       C  
ATOM   5631  CD  LYS C  92     -35.512  -3.534  20.614  1.00 52.90           C  
ANISOU 5631  CD  LYS C  92     4604   6581   8914    200   -915   -433       C  
ATOM   5632  CE  LYS C  92     -35.019  -3.967  19.242  1.00 54.28           C  
ANISOU 5632  CE  LYS C  92     4765   6788   9071    180   -919   -447       C  
ATOM   5633  NZ  LYS C  92     -34.619  -2.816  18.399  1.00 55.46           N  
ANISOU 5633  NZ  LYS C  92     4868   6965   9236     85   -885   -464       N  
ATOM   5634  N   TRP C  93     -39.818  -4.099  24.638  1.00 45.49           N  
ANISOU 5634  N   TRP C  93     3864   5369   8049    285   -904   -243       N  
ATOM   5635  CA  TRP C  93     -40.361  -3.936  26.010  1.00 45.72           C  
ANISOU 5635  CA  TRP C  93     3915   5378   8079    308   -897   -234       C  
ATOM   5636  C   TRP C  93     -40.882  -5.282  26.518  1.00 45.88           C  
ANISOU 5636  C   TRP C  93     4013   5352   8066    369   -903   -198       C  
ATOM   5637  O   TRP C  93     -41.312  -6.108  25.686  1.00 47.32           O  
ANISOU 5637  O   TRP C  93     4234   5489   8253    365   -905   -166       O  
ATOM   5638  CB  TRP C  93     -41.485  -2.893  26.048  1.00 45.77           C  
ANISOU 5638  CB  TRP C  93     3912   5329   8148    236   -872   -200       C  
ATOM   5639  CG  TRP C  93     -41.057  -1.476  25.825  1.00 45.98           C  
ANISOU 5639  CG  TRP C  93     3876   5386   8207    178   -860   -232       C  
ATOM   5640  CD1 TRP C  93     -39.786  -0.987  25.727  1.00 46.14           C  
ANISOU 5640  CD1 TRP C  93     3842   5482   8207    175   -861   -293       C  
ATOM   5641  CD2 TRP C  93     -41.936  -0.343  25.720  1.00 45.86           C  
ANISOU 5641  CD2 TRP C  93     3850   5322   8252    114   -840   -208       C  
ATOM   5642  NE1 TRP C  93     -39.817   0.369  25.547  1.00 46.14           N  
ANISOU 5642  NE1 TRP C  93     3803   5475   8250    105   -838   -305       N  
ATOM   5643  CE2 TRP C  93     -41.119   0.794  25.540  1.00 46.18           C  
ANISOU 5643  CE2 TRP C  93     3837   5402   8305     72   -827   -251       C  
ATOM   5644  CE3 TRP C  93     -43.325  -0.181  25.759  1.00 45.32           C  
ANISOU 5644  CE3 TRP C  93     3811   5181   8225     89   -831   -160       C  
ATOM   5645  CZ2 TRP C  93     -41.659   2.069  25.387  1.00 46.06           C  
ANISOU 5645  CZ2 TRP C  93     3809   5346   8345     10   -807   -240       C  
ATOM   5646  CZ3 TRP C  93     -43.856   1.080  25.621  1.00 44.94           C  
ANISOU 5646  CZ3 TRP C  93     3742   5102   8230     36   -817   -153       C  
ATOM   5647  CH2 TRP C  93     -43.032   2.189  25.436  1.00 45.75           C  
ANISOU 5647  CH2 TRP C  93     3801   5234   8345     -1   -805   -189       C  
ATOM   5648  N   LYS C  94     -40.879  -5.473  27.837  1.00 45.37           N  
ANISOU 5648  N   LYS C  94     3972   5295   7968    420   -904   -204       N  
ATOM   5649  CA  LYS C  94     -41.481  -6.657  28.503  1.00 45.13           C  
ANISOU 5649  CA  LYS C  94     4031   5210   7905    471   -900   -164       C  
ATOM   5650  C   LYS C  94     -42.921  -6.310  28.912  1.00 43.88           C  
ANISOU 5650  C   LYS C  94     3897   4982   7792    413   -868   -120       C  
ATOM   5651  O   LYS C  94     -43.120  -5.210  29.482  1.00 43.25           O  
ANISOU 5651  O   LYS C  94     3771   4922   7739    380   -858   -135       O  
ATOM   5652  CB  LYS C  94     -40.611  -7.061  29.698  1.00 45.99           C  
ANISOU 5652  CB  LYS C  94     4157   5374   7942    565   -919   -196       C  
ATOM   5653  CG  LYS C  94     -39.186  -7.464  29.349  1.00 46.56           C  
ANISOU 5653  CG  LYS C  94     4201   5524   7963    633   -955   -250       C  
ATOM   5654  CD  LYS C  94     -39.090  -8.832  28.707  1.00 46.97           C  
ANISOU 5654  CD  LYS C  94     4322   5537   7987    683   -969   -227       C  
ATOM   5655  CE  LYS C  94     -37.665  -9.207  28.350  1.00 47.93           C  
ANISOU 5655  CE  LYS C  94     4408   5743   8058    755  -1007   -290       C  
ATOM   5656  NZ  LYS C  94     -37.402 -10.664  28.495  1.00 48.21           N  
ANISOU 5656  NZ  LYS C  94     4531   5750   8035    855  -1029   -276       N  
ATOM   5657  N   TYR C  95     -43.880  -7.198  28.620  1.00 42.89           N  
ANISOU 5657  N   TYR C  95     3836   4782   7675    399   -852    -75       N  
ATOM   5658  CA  TYR C  95     -45.306  -7.073  29.030  1.00 41.78           C  
ANISOU 5658  CA  TYR C  95     3723   4579   7572    347   -819    -40       C  
ATOM   5659  C   TYR C  95     -45.681  -8.236  29.936  1.00 42.42           C  
ANISOU 5659  C   TYR C  95     3897   4614   7605    390   -801    -14       C  
ATOM   5660  O   TYR C  95     -46.367  -9.154  29.504  1.00 43.24           O  
ANISOU 5660  O   TYR C  95     4059   4655   7714    373   -782     14       O  
ATOM   5661  CB  TYR C  95     -46.211  -7.019  27.805  1.00 40.54           C  
ANISOU 5661  CB  TYR C  95     3554   4376   7471    279   -809    -19       C  
ATOM   5662  CG  TYR C  95     -45.828  -5.939  26.837  1.00 39.82           C  
ANISOU 5662  CG  TYR C  95     3387   4322   7419    240   -825    -38       C  
ATOM   5663  CD1 TYR C  95     -46.404  -4.683  26.898  1.00 39.58           C  
ANISOU 5663  CD1 TYR C  95     3308   4291   7439    189   -817    -40       C  
ATOM   5664  CD2 TYR C  95     -44.864  -6.165  25.877  1.00 39.80           C  
ANISOU 5664  CD2 TYR C  95     3366   4355   7401    257   -847    -54       C  
ATOM   5665  CE1 TYR C  95     -46.063  -3.685  25.998  1.00 39.36           C  
ANISOU 5665  CE1 TYR C  95     3225   4286   7443    152   -828    -51       C  
ATOM   5666  CE2 TYR C  95     -44.507  -5.183  24.970  1.00 39.77           C  
ANISOU 5666  CE2 TYR C  95     3300   4381   7426    215   -856    -68       C  
ATOM   5667  CZ  TYR C  95     -45.104  -3.938  25.035  1.00 39.49           C  
ANISOU 5667  CZ  TYR C  95     3227   4335   7439    163   -845    -64       C  
ATOM   5668  OH  TYR C  95     -44.728  -2.965  24.157  1.00 39.96           O  
ANISOU 5668  OH  TYR C  95     3241   4417   7525    122   -849    -73       O  
ATOM   5669  N   PRO C  96     -45.261  -8.222  31.219  1.00 43.05           N  
ANISOU 5669  N   PRO C  96     3997   4723   7635    444   -802    -23       N  
ATOM   5670  CA  PRO C  96     -45.627  -9.284  32.152  1.00 43.97           C  
ANISOU 5670  CA  PRO C  96     4214   4793   7698    485   -780      7       C  
ATOM   5671  C   PRO C  96     -47.109  -9.195  32.546  1.00 45.13           C  
ANISOU 5671  C   PRO C  96     4387   4880   7881    412   -734     35       C  
ATOM   5672  O   PRO C  96     -47.681  -8.119  32.521  1.00 45.40           O  
ANISOU 5672  O   PRO C  96     4351   4929   7969    352   -727     22       O  
ATOM   5673  CB  PRO C  96     -44.733  -9.012  33.366  1.00 44.12           C  
ANISOU 5673  CB  PRO C  96     4229   4880   7656    560   -800    -17       C  
ATOM   5674  CG  PRO C  96     -44.538  -7.506  33.333  1.00 43.40           C  
ANISOU 5674  CG  PRO C  96     4025   4852   7612    516   -810    -58       C  
ATOM   5675  CD  PRO C  96     -44.458  -7.169  31.858  1.00 42.94           C  
ANISOU 5675  CD  PRO C  96     3914   4790   7612    464   -821    -66       C  
ATOM   5676  N   GLN C  97     -47.705 -10.340  32.869  1.00 46.48           N  
ANISOU 5676  N   GLN C  97     4657   4982   8021    416   -701     70       N  
ATOM   5677  CA  GLN C  97     -49.022 -10.420  33.548  1.00 47.06           C  
ANISOU 5677  CA  GLN C  97     4767   5003   8107    356   -650     91       C  
ATOM   5678  C   GLN C  97     -48.807 -10.008  35.003  1.00 46.93           C  
ANISOU 5678  C   GLN C  97     4759   5027   8043    393   -645     86       C  
ATOM   5679  O   GLN C  97     -47.853 -10.510  35.614  1.00 47.54           O  
ANISOU 5679  O   GLN C  97     4886   5126   8048    482   -665     90       O  
ATOM   5680  CB  GLN C  97     -49.588 -11.835  33.446  1.00 48.39           C  
ANISOU 5680  CB  GLN C  97     5048   5086   8252    348   -610    125       C  
ATOM   5681  CG  GLN C  97     -49.818 -12.284  32.010  1.00 48.72           C  
ANISOU 5681  CG  GLN C  97     5078   5093   8339    310   -614    123       C  
ATOM   5682  CD  GLN C  97     -50.954 -11.527  31.373  1.00 48.44           C  
ANISOU 5682  CD  GLN C  97     4966   5056   8383    215   -597    107       C  
ATOM   5683  OE1 GLN C  97     -50.760 -10.740  30.443  1.00 47.66           O  
ANISOU 5683  OE1 GLN C  97     4780   4996   8330    197   -630     87       O  
ATOM   5684  NE2 GLN C  97     -52.149 -11.748  31.898  1.00 49.21           N  
ANISOU 5684  NE2 GLN C  97     5096   5111   8491    154   -545    113       N  
ATOM   5685  N   VAL C  98     -49.637  -9.109  35.522  1.00 46.39           N  
ANISOU 5685  N   VAL C  98     4641   4972   8013    334   -623     73       N  
ATOM   5686  CA  VAL C  98     -49.583  -8.657  36.944  1.00 46.70           C  
ANISOU 5686  CA  VAL C  98     4681   5051   8009    359   -614     65       C  
ATOM   5687  C   VAL C  98     -51.019  -8.625  37.489  1.00 47.05           C  
ANISOU 5687  C   VAL C  98     4745   5054   8076    281   -558     74       C  
ATOM   5688  O   VAL C  98     -51.791  -7.725  37.100  1.00 46.84           O  
ANISOU 5688  O   VAL C  98     4637   5035   8123    212   -553     50       O  
ATOM   5689  CB  VAL C  98     -48.873  -7.296  37.063  1.00 46.20           C  
ANISOU 5689  CB  VAL C  98     4509   5072   7972    373   -653     19       C  
ATOM   5690  CG1 VAL C  98     -48.663  -6.884  38.510  1.00 46.50           C  
ANISOU 5690  CG1 VAL C  98     4545   5161   7960    409   -648      3       C  
ATOM   5691  CG2 VAL C  98     -47.551  -7.291  36.312  1.00 46.01           C  
ANISOU 5691  CG2 VAL C  98     4453   5091   7937    429   -701      0       C  
ATOM   5692  N   ASN C  99     -51.377  -9.610  38.314  1.00 47.37           N  
ANISOU 5692  N   ASN C  99     4892   5050   8054    292   -516    107       N  
ATOM   5693  CA  ASN C  99     -52.697  -9.706  38.982  1.00 47.48           C  
ANISOU 5693  CA  ASN C  99     4936   5029   8076    217   -454    112       C  
ATOM   5694  C   ASN C  99     -53.813  -9.626  37.931  1.00 47.40           C  
ANISOU 5694  C   ASN C  99     4882   4979   8148    123   -432     99       C  
ATOM   5695  O   ASN C  99     -54.831  -8.940  38.177  1.00 47.41           O  
ANISOU 5695  O   ASN C  99     4826   4993   8194     54   -407     72       O  
ATOM   5696  CB  ASN C  99     -52.799  -8.627  40.050  1.00 47.61           C  
ANISOU 5696  CB  ASN C  99     4888   5111   8088    215   -456     83       C  
ATOM   5697  CG  ASN C  99     -53.835  -8.925  41.105  1.00 48.22           C  
ANISOU 5697  CG  ASN C  99     5021   5166   8135    166   -392     92       C  
ATOM   5698  OD1 ASN C  99     -54.631  -8.051  41.413  1.00 49.21           O  
ANISOU 5698  OD1 ASN C  99     5072   5319   8305    108   -377     58       O  
ATOM   5699  ND2 ASN C  99     -53.842 -10.126  41.662  1.00 49.14           N  
ANISOU 5699  ND2 ASN C  99     5266   5229   8174    189   -354    136       N  
ATOM   5700  N   GLY C 100     -53.607 -10.318  36.805  1.00 47.59           N  
ANISOU 5700  N   GLY C 100     4930   4963   8189    125   -443    112       N  
ATOM   5701  CA  GLY C 100     -54.618 -10.559  35.755  1.00 47.53           C  
ANISOU 5701  CA  GLY C 100     4902   4912   8245     45   -419    101       C  
ATOM   5702  C   GLY C 100     -54.425  -9.649  34.554  1.00 46.91           C  
ANISOU 5702  C   GLY C 100     4714   4871   8236     37   -470     76       C  
ATOM   5703  O   GLY C 100     -55.126  -9.872  33.531  1.00 47.20           O  
ANISOU 5703  O   GLY C 100     4731   4881   8321    -15   -461     66       O  
ATOM   5704  N   LEU C 101     -53.521  -8.662  34.669  1.00 45.36           N  
ANISOU 5704  N   LEU C 101     4454   4737   8044     84   -519     63       N  
ATOM   5705  CA  LEU C 101     -53.461  -7.477  33.774  1.00 43.84           C  
ANISOU 5705  CA  LEU C 101     4154   4582   7918     65   -559     36       C  
ATOM   5706  C   LEU C 101     -52.115  -7.418  33.070  1.00 43.38           C  
ANISOU 5706  C   LEU C 101     4080   4553   7847    124   -608     39       C  
ATOM   5707  O   LEU C 101     -51.090  -7.697  33.717  1.00 43.73           O  
ANISOU 5707  O   LEU C 101     4160   4623   7833    191   -622     45       O  
ATOM   5708  CB  LEU C 101     -53.691  -6.216  34.606  1.00 43.47           C  
ANISOU 5708  CB  LEU C 101     4040   4582   7894     54   -562      9       C  
ATOM   5709  CG  LEU C 101     -55.077  -6.133  35.243  1.00 43.60           C  
ANISOU 5709  CG  LEU C 101     4054   4581   7929     -8   -516     -4       C  
ATOM   5710  CD1 LEU C 101     -55.090  -5.179  36.418  1.00 43.51           C  
ANISOU 5710  CD1 LEU C 101     4003   4616   7913     -1   -514    -29       C  
ATOM   5711  CD2 LEU C 101     -56.124  -5.764  34.206  1.00 42.92           C  
ANISOU 5711  CD2 LEU C 101     3911   4481   7915    -68   -516    -25       C  
ATOM   5712  N   THR C 102     -52.125  -7.038  31.794  1.00 42.99           N  
ANISOU 5712  N   THR C 102     3978   4507   7848    100   -632     32       N  
ATOM   5713  CA  THR C 102     -50.895  -6.792  31.004  1.00 42.98           C  
ANISOU 5713  CA  THR C 102     3946   4541   7842    141   -676     27       C  
ATOM   5714  C   THR C 102     -50.352  -5.413  31.379  1.00 42.50           C  
ANISOU 5714  C   THR C 102     3811   4536   7799    148   -699      0       C  
ATOM   5715  O   THR C 102     -51.002  -4.404  31.061  1.00 42.58           O  
ANISOU 5715  O   THR C 102     3762   4548   7867    102   -700    -11       O  
ATOM   5716  CB  THR C 102     -51.133  -6.908  29.497  1.00 43.08           C  
ANISOU 5716  CB  THR C 102     3935   4536   7895    109   -689     30       C  
ATOM   5717  OG1 THR C 102     -51.832  -8.120  29.201  1.00 43.87           O  
ANISOU 5717  OG1 THR C 102     4098   4582   7987     89   -660     46       O  
ATOM   5718  CG2 THR C 102     -49.829  -6.867  28.733  1.00 42.87           C  
ANISOU 5718  CG2 THR C 102     3889   4546   7851    150   -727     24       C  
ATOM   5719  N   SER C 103     -49.211  -5.394  32.065  1.00 42.41           N  
ANISOU 5719  N   SER C 103     3804   4569   7738    207   -716    -11       N  
ATOM   5720  CA  SER C 103     -48.452  -4.174  32.433  1.00 42.05           C  
ANISOU 5720  CA  SER C 103     3688   4585   7703    218   -737    -47       C  
ATOM   5721  C   SER C 103     -47.283  -4.002  31.460  1.00 41.77           C  
ANISOU 5721  C   SER C 103     3618   4586   7666    238   -769    -63       C  
ATOM   5722  O   SER C 103     -47.314  -4.610  30.375  1.00 41.92           O  
ANISOU 5722  O   SER C 103     3656   4578   7692    230   -775    -44       O  
ATOM   5723  CB  SER C 103     -47.983  -4.263  33.850  1.00 42.29           C  
ANISOU 5723  CB  SER C 103     3737   4652   7676    269   -733    -61       C  
ATOM   5724  OG  SER C 103     -47.508  -3.007  34.297  1.00 42.23           O  
ANISOU 5724  OG  SER C 103     3657   4700   7688    265   -745   -102       O  
ATOM   5725  N   ILE C 104     -46.302  -3.176  31.821  1.00 41.44           N  
ANISOU 5725  N   ILE C 104     3524   4606   7615    258   -785   -102       N  
ATOM   5726  CA  ILE C 104     -45.023  -3.030  31.069  1.00 41.32           C  
ANISOU 5726  CA  ILE C 104     3472   4641   7586    278   -811   -130       C  
ATOM   5727  C   ILE C 104     -43.905  -2.816  32.083  1.00 41.73           C  
ANISOU 5727  C   ILE C 104     3498   4768   7587    334   -825   -178       C  
ATOM   5728  O   ILE C 104     -44.087  -1.963  32.970  1.00 41.63           O  
ANISOU 5728  O   ILE C 104     3451   4776   7587    321   -814   -201       O  
ATOM   5729  CB  ILE C 104     -45.091  -1.864  30.065  1.00 40.86           C  
ANISOU 5729  CB  ILE C 104     3353   4579   7591    213   -812   -139       C  
ATOM   5730  CG1 ILE C 104     -46.495  -1.696  29.468  1.00 40.30           C  
ANISOU 5730  CG1 ILE C 104     3294   4439   7576    158   -797   -101       C  
ATOM   5731  CG2 ILE C 104     -44.022  -2.031  28.995  1.00 40.69           C  
ANISOU 5731  CG2 ILE C 104     3312   4593   7555    221   -830   -156       C  
ATOM   5732  CD1 ILE C 104     -46.628  -0.555  28.484  1.00 39.97           C  
ANISOU 5732  CD1 ILE C 104     3207   4388   7591    104   -800   -102       C  
ATOM   5733  N   LYS C 105     -42.808  -3.565  31.973  1.00 42.90           N  
ANISOU 5733  N   LYS C 105     3659   4962   7678    399   -848   -197       N  
ATOM   5734  CA  LYS C 105     -41.572  -3.294  32.759  1.00 44.02           C  
ANISOU 5734  CA  LYS C 105     3760   5195   7769    457   -868   -258       C  
ATOM   5735  C   LYS C 105     -41.130  -1.865  32.413  1.00 43.72           C  
ANISOU 5735  C   LYS C 105     3630   5199   7780    396   -862   -307       C  
ATOM   5736  O   LYS C 105     -41.263  -1.475  31.230  1.00 42.61           O  
ANISOU 5736  O   LYS C 105     3470   5031   7689    336   -856   -295       O  
ATOM   5737  CB  LYS C 105     -40.493  -4.346  32.480  1.00 45.05           C  
ANISOU 5737  CB  LYS C 105     3914   5368   7834    538   -898   -276       C  
ATOM   5738  CG  LYS C 105     -39.242  -4.218  33.357  1.00 46.02           C  
ANISOU 5738  CG  LYS C 105     3996   5595   7893    614   -924   -345       C  
ATOM   5739  CD  LYS C 105     -38.271  -5.386  33.276  1.00 46.75           C  
ANISOU 5739  CD  LYS C 105     4124   5728   7910    715   -959   -362       C  
ATOM   5740  CE  LYS C 105     -36.826  -4.983  33.483  1.00 47.63           C  
ANISOU 5740  CE  LYS C 105     4153   5962   7980    764   -987   -455       C  
ATOM   5741  NZ  LYS C 105     -36.251  -4.369  32.258  1.00 47.91           N  
ANISOU 5741  NZ  LYS C 105     4113   6029   8059    697   -984   -495       N  
ATOM   5742  N   TRP C 106     -40.701  -1.080  33.403  1.00 44.44           N  
ANISOU 5742  N   TRP C 106     3672   5349   7862    405   -860   -359       N  
ATOM   5743  CA  TRP C 106     -40.374   0.348  33.171  1.00 45.66           C  
ANISOU 5743  CA  TRP C 106     3747   5532   8070    337   -846   -408       C  
ATOM   5744  C   TRP C 106     -39.223   0.470  32.155  1.00 46.46           C  
ANISOU 5744  C   TRP C 106     3803   5684   8165    325   -856   -450       C  
ATOM   5745  O   TRP C 106     -38.200  -0.241  32.304  1.00 45.34           O  
ANISOU 5745  O   TRP C 106     3654   5613   7959    394   -880   -490       O  
ATOM   5746  CB  TRP C 106     -40.063   1.087  34.472  1.00 46.81           C  
ANISOU 5746  CB  TRP C 106     3845   5738   8201    352   -841   -466       C  
ATOM   5747  CG  TRP C 106     -39.953   2.554  34.212  1.00 47.33           C  
ANISOU 5747  CG  TRP C 106     3843   5808   8333    271   -818   -508       C  
ATOM   5748  CD1 TRP C 106     -40.942   3.480  34.332  1.00 47.42           C  
ANISOU 5748  CD1 TRP C 106     3849   5758   8410    210   -795   -488       C  
ATOM   5749  CD2 TRP C 106     -38.815   3.251  33.674  1.00 48.30           C  
ANISOU 5749  CD2 TRP C 106     3898   5989   8462    238   -814   -575       C  
ATOM   5750  NE1 TRP C 106     -40.493   4.715  33.949  1.00 47.88           N  
ANISOU 5750  NE1 TRP C 106     3849   5825   8515    145   -776   -534       N  
ATOM   5751  CE2 TRP C 106     -39.192   4.605  33.538  1.00 48.22           C  
ANISOU 5751  CE2 TRP C 106     3854   5942   8524    155   -783   -588       C  
ATOM   5752  CE3 TRP C 106     -37.516   2.869  33.316  1.00 47.64           C  
ANISOU 5752  CE3 TRP C 106     3780   5989   8330    271   -830   -631       C  
ATOM   5753  CZ2 TRP C 106     -38.313   5.574  33.059  1.00 48.11           C  
ANISOU 5753  CZ2 TRP C 106     3781   5964   8535     97   -763   -651       C  
ATOM   5754  CZ3 TRP C 106     -36.656   3.826  32.828  1.00 48.20           C  
ANISOU 5754  CZ3 TRP C 106     3783   6105   8426    209   -810   -698       C  
ATOM   5755  CH2 TRP C 106     -37.052   5.156  32.699  1.00 48.45           C  
ANISOU 5755  CH2 TRP C 106     3789   6090   8529    120   -774   -706       C  
ATOM   5756  N   ALA C 107     -39.395   1.359  31.170  1.00 46.93           N  
ANISOU 5756  N   ALA C 107     3836   5709   8286    242   -836   -445       N  
ATOM   5757  CA  ALA C 107     -38.454   1.614  30.052  1.00 47.03           C  
ANISOU 5757  CA  ALA C 107     3809   5757   8300    207   -835   -478       C  
ATOM   5758  C   ALA C 107     -38.915   2.860  29.277  1.00 47.85           C  
ANISOU 5758  C   ALA C 107     3896   5805   8477    109   -804   -462       C  
ATOM   5759  O   ALA C 107     -40.107   2.941  28.946  1.00 47.26           O  
ANISOU 5759  O   ALA C 107     3864   5646   8445     82   -798   -396       O  
ATOM   5760  CB  ALA C 107     -38.385   0.401  29.153  1.00 46.16           C  
ANISOU 5760  CB  ALA C 107     3743   5633   8161    242   -855   -440       C  
ATOM   5761  N   ASP C 108     -38.012   3.815  29.035  1.00 49.08           N  
ANISOU 5761  N   ASP C 108     3993   6008   8645     59   -784   -525       N  
ATOM   5762  CA  ASP C 108     -38.245   4.976  28.129  1.00 49.88           C  
ANISOU 5762  CA  ASP C 108     4090   6055   8807    -33   -752   -510       C  
ATOM   5763  C   ASP C 108     -39.410   5.827  28.649  1.00 49.79           C  
ANISOU 5763  C   ASP C 108     4097   5966   8854    -62   -737   -476       C  
ATOM   5764  O   ASP C 108     -40.283   6.210  27.821  1.00 50.26           O  
ANISOU 5764  O   ASP C 108     4194   5943   8958   -104   -730   -415       O  
ATOM   5765  CB  ASP C 108     -38.498   4.509  26.690  1.00 49.91           C  
ANISOU 5765  CB  ASP C 108     4133   6016   8814    -54   -757   -452       C  
ATOM   5766  CG  ASP C 108     -37.410   3.588  26.182  1.00 50.33           C  
ANISOU 5766  CG  ASP C 108     4167   6145   8809    -20   -774   -488       C  
ATOM   5767  OD1 ASP C 108     -36.386   3.468  26.871  1.00 52.43           O  
ANISOU 5767  OD1 ASP C 108     4384   6500   9034     13   -780   -564       O  
ATOM   5768  OD2 ASP C 108     -37.602   2.992  25.115  1.00 50.10           O  
ANISOU 5768  OD2 ASP C 108     4169   6090   8774    -23   -783   -444       O  
ATOM   5769  N   ASN C 109     -39.417   6.103  29.959  1.00 49.35           N  
ANISOU 5769  N   ASN C 109     4014   5940   8794    -37   -736   -517       N  
ATOM   5770  CA  ASN C 109     -40.445   6.939  30.637  1.00 49.14           C  
ANISOU 5770  CA  ASN C 109     3994   5854   8820    -59   -723   -501       C  
ATOM   5771  C   ASN C 109     -41.854   6.460  30.273  1.00 48.12           C  
ANISOU 5771  C   ASN C 109     3927   5641   8716    -49   -736   -415       C  
ATOM   5772  O   ASN C 109     -42.694   7.344  30.001  1.00 48.29           O  
ANISOU 5772  O   ASN C 109     3960   5592   8796    -92   -722   -388       O  
ATOM   5773  CB  ASN C 109     -40.323   8.411  30.242  1.00 48.90           C  
ANISOU 5773  CB  ASN C 109     3942   5788   8849   -141   -688   -525       C  
ATOM   5774  CG  ASN C 109     -38.958   8.984  30.541  1.00 48.45           C  
ANISOU 5774  CG  ASN C 109     3821   5813   8775   -168   -666   -621       C  
ATOM   5775  OD1 ASN C 109     -38.492   8.914  31.669  1.00 47.53           O  
ANISOU 5775  OD1 ASN C 109     3661   5768   8630   -132   -671   -683       O  
ATOM   5776  ND2 ASN C 109     -38.313   9.553  29.539  1.00 48.53           N  
ANISOU 5776  ND2 ASN C 109     3824   5817   8799   -233   -639   -636       N  
ATOM   5777  N   ASN C 110     -42.096   5.136  30.270  1.00 47.59           N  
ANISOU 5777  N   ASN C 110     3895   5579   8604      5   -759   -378       N  
ATOM   5778  CA  ASN C 110     -43.332   4.509  29.708  1.00 46.24           C  
ANISOU 5778  CA  ASN C 110     3779   5336   8451      9   -769   -303       C  
ATOM   5779  C   ASN C 110     -44.359   4.230  30.811  1.00 45.07           C  
ANISOU 5779  C   ASN C 110     3651   5166   8306     37   -769   -287       C  
ATOM   5780  O   ASN C 110     -45.392   3.627  30.482  1.00 45.66           O  
ANISOU 5780  O   ASN C 110     3767   5190   8391     39   -773   -236       O  
ATOM   5781  CB  ASN C 110     -43.040   3.223  28.931  1.00 46.23           C  
ANISOU 5781  CB  ASN C 110     3812   5346   8407     42   -787   -274       C  
ATOM   5782  CG  ASN C 110     -42.493   2.100  29.788  1.00 47.21           C  
ANISOU 5782  CG  ASN C 110     3949   5524   8464    115   -803   -293       C  
ATOM   5783  OD1 ASN C 110     -42.234   2.279  30.975  1.00 48.55           O  
ANISOU 5783  OD1 ASN C 110     4098   5734   8613    143   -801   -331       O  
ATOM   5784  ND2 ASN C 110     -42.282   0.939  29.188  1.00 47.28           N  
ANISOU 5784  ND2 ASN C 110     3992   5534   8435    149   -819   -270       N  
ATOM   5785  N   CYS C 111     -44.105   4.666  32.050  1.00 44.11           N  
ANISOU 5785  N   CYS C 111     3498   5085   8174     52   -762   -334       N  
ATOM   5786  CA  CYS C 111     -45.016   4.480  33.214  1.00 43.31           C  
ANISOU 5786  CA  CYS C 111     3411   4972   8070     74   -757   -327       C  
ATOM   5787  C   CYS C 111     -46.448   4.950  32.871  1.00 42.35           C  
ANISOU 5787  C   CYS C 111     3305   4772   8011     34   -749   -287       C  
ATOM   5788  O   CYS C 111     -47.418   4.328  33.370  1.00 42.52           O  
ANISOU 5788  O   CYS C 111     3357   4772   8025     49   -746   -261       O  
ATOM   5789  CB  CYS C 111     -44.471   5.183  34.454  1.00 43.44           C  
ANISOU 5789  CB  CYS C 111     3379   5048   8076     85   -750   -392       C  
ATOM   5790  SG  CYS C 111     -44.355   6.983  34.290  1.00 43.61           S  
ANISOU 5790  SG  CYS C 111     3344   5051   8174     16   -728   -438       S  
ATOM   5791  N   TYR C 112     -46.591   5.984  32.035  1.00 41.14           N  
ANISOU 5791  N   TYR C 112     3135   4579   7914    -12   -744   -285       N  
ATOM   5792  CA  TYR C 112     -47.901   6.573  31.657  1.00 40.12           C  
ANISOU 5792  CA  TYR C 112     3016   4381   7845    -40   -742   -255       C  
ATOM   5793  C   TYR C 112     -48.609   5.651  30.662  1.00 40.16           C  
ANISOU 5793  C   TYR C 112     3062   4349   7845    -36   -754   -199       C  
ATOM   5794  O   TYR C 112     -49.842   5.533  30.788  1.00 41.09           O  
ANISOU 5794  O   TYR C 112     3192   4432   7986    -38   -754   -181       O  
ATOM   5795  CB  TYR C 112     -47.752   8.005  31.137  1.00 39.69           C  
ANISOU 5795  CB  TYR C 112     2940   4293   7846    -83   -734   -271       C  
ATOM   5796  CG  TYR C 112     -47.362   8.145  29.689  1.00 39.42           C  
ANISOU 5796  CG  TYR C 112     2925   4232   7820   -108   -737   -240       C  
ATOM   5797  CD1 TYR C 112     -48.279   8.542  28.731  1.00 39.18           C  
ANISOU 5797  CD1 TYR C 112     2920   4136   7828   -124   -746   -197       C  
ATOM   5798  CD2 TYR C 112     -46.058   7.914  29.283  1.00 39.50           C  
ANISOU 5798  CD2 TYR C 112     2926   4288   7793   -115   -733   -259       C  
ATOM   5799  CE1 TYR C 112     -47.920   8.678  27.400  1.00 39.28           C  
ANISOU 5799  CE1 TYR C 112     2955   4127   7840   -146   -748   -166       C  
ATOM   5800  CE2 TYR C 112     -45.683   8.043  27.958  1.00 39.58           C  
ANISOU 5800  CE2 TYR C 112     2954   4278   7805   -143   -733   -233       C  
ATOM   5801  CZ  TYR C 112     -46.616   8.422  27.012  1.00 39.59           C  
ANISOU 5801  CZ  TYR C 112     2987   4212   7843   -159   -740   -183       C  
ATOM   5802  OH  TYR C 112     -46.223   8.541  25.711  1.00 39.82           O  
ANISOU 5802  OH  TYR C 112     3038   4225   7866   -185   -739   -155       O  
ATOM   5803  N   LEU C 113     -47.873   5.024  29.733  1.00 39.69           N  
ANISOU 5803  N   LEU C 113     3020   4303   7755    -31   -764   -181       N  
ATOM   5804  CA  LEU C 113     -48.416   4.002  28.796  1.00 39.48           C  
ANISOU 5804  CA  LEU C 113     3031   4251   7717    -24   -775   -135       C  
ATOM   5805  C   LEU C 113     -48.875   2.763  29.572  1.00 39.55           C  
ANISOU 5805  C   LEU C 113     3071   4268   7687      7   -771   -125       C  
ATOM   5806  O   LEU C 113     -49.973   2.242  29.274  1.00 39.01           O  
ANISOU 5806  O   LEU C 113     3026   4163   7632      0   -770    -98       O  
ATOM   5807  CB  LEU C 113     -47.355   3.613  27.764  1.00 39.22           C  
ANISOU 5807  CB  LEU C 113     3004   4242   7654    -24   -784   -129       C  
ATOM   5808  CG  LEU C 113     -47.376   4.453  26.493  1.00 39.53           C  
ANISOU 5808  CG  LEU C 113     3041   4250   7729    -63   -786   -110       C  
ATOM   5809  CD1 LEU C 113     -46.341   3.965  25.502  1.00 39.40           C  
ANISOU 5809  CD1 LEU C 113     3029   4265   7677    -65   -791   -107       C  
ATOM   5810  CD2 LEU C 113     -48.763   4.422  25.863  1.00 39.72           C  
ANISOU 5810  CD2 LEU C 113     3085   4220   7786    -70   -795    -70       C  
ATOM   5811  N   ALA C 114     -48.038   2.284  30.493  1.00 39.68           N  
ANISOU 5811  N   ALA C 114     3090   4331   7654     43   -769   -149       N  
ATOM   5812  CA  ALA C 114     -48.390   1.175  31.405  1.00 39.93           C  
ANISOU 5812  CA  ALA C 114     3161   4367   7641     77   -761   -139       C  
ATOM   5813  C   ALA C 114     -49.734   1.493  32.072  1.00 39.87           C  
ANISOU 5813  C   ALA C 114     3152   4327   7667     54   -744   -136       C  
ATOM   5814  O   ALA C 114     -50.644   0.653  32.001  1.00 39.58           O  
ANISOU 5814  O   ALA C 114     3154   4259   7625     48   -733   -110       O  
ATOM   5815  CB  ALA C 114     -47.295   0.953  32.421  1.00 40.10           C  
ANISOU 5815  CB  ALA C 114     3179   4450   7606    125   -764   -172       C  
ATOM   5816  N   THR C 115     -49.848   2.677  32.680  1.00 40.03           N  
ANISOU 5816  N   THR C 115     3129   4358   7722     38   -739   -169       N  
ATOM   5817  CA  THR C 115     -51.021   3.079  33.501  1.00 40.14           C  
ANISOU 5817  CA  THR C 115     3130   4355   7764     20   -723   -180       C  
ATOM   5818  C   THR C 115     -52.270   3.127  32.609  1.00 39.45           C  
ANISOU 5818  C   THR C 115     3047   4216   7725    -10   -724   -156       C  
ATOM   5819  O   THR C 115     -53.309   2.574  33.008  1.00 39.21           O  
ANISOU 5819  O   THR C 115     3033   4171   7692    -20   -708   -152       O  
ATOM   5820  CB  THR C 115     -50.719   4.379  34.255  1.00 40.55           C  
ANISOU 5820  CB  THR C 115     3131   4431   7845     13   -721   -226       C  
ATOM   5821  OG1 THR C 115     -49.598   4.083  35.093  1.00 40.53           O  
ANISOU 5821  OG1 THR C 115     3126   4488   7785     49   -720   -251       O  
ATOM   5822  CG2 THR C 115     -51.896   4.873  35.071  1.00 40.85           C  
ANISOU 5822  CG2 THR C 115     3149   4455   7914     -3   -706   -245       C  
ATOM   5823  N   ALA C 116     -52.159   3.729  31.426  1.00 39.01           N  
ANISOU 5823  N   ALA C 116     2977   4137   7705    -26   -742   -144       N  
ATOM   5824  CA  ALA C 116     -53.211   3.716  30.384  1.00 38.60           C  
ANISOU 5824  CA  ALA C 116     2929   4045   7690    -45   -751   -122       C  
ATOM   5825  C   ALA C 116     -53.637   2.269  30.097  1.00 38.70           C  
ANISOU 5825  C   ALA C 116     2982   4051   7668    -42   -743    -97       C  
ATOM   5826  O   ALA C 116     -54.847   1.981  30.154  1.00 38.65           O  
ANISOU 5826  O   ALA C 116     2977   4028   7679    -59   -733   -101       O  
ATOM   5827  CB  ALA C 116     -52.707   4.390  29.135  1.00 38.36           C  
ANISOU 5827  CB  ALA C 116     2893   3999   7682    -53   -771   -106       C  
ATOM   5828  N   LEU C 117     -52.663   1.401  29.809  1.00 38.57           N  
ANISOU 5828  N   LEU C 117     2998   4050   7606    -23   -746    -80       N  
ATOM   5829  CA  LEU C 117     -52.881   0.009  29.342  1.00 38.64           C  
ANISOU 5829  CA  LEU C 117     3052   4045   7583    -19   -739    -56       C  
ATOM   5830  C   LEU C 117     -53.626  -0.782  30.424  1.00 38.99           C  
ANISOU 5830  C   LEU C 117     3127   4081   7604    -22   -709    -61       C  
ATOM   5831  O   LEU C 117     -54.554  -1.534  30.080  1.00 39.13           O  
ANISOU 5831  O   LEU C 117     3166   4073   7626    -44   -694    -53       O  
ATOM   5832  CB  LEU C 117     -51.516  -0.606  29.024  1.00 38.56           C  
ANISOU 5832  CB  LEU C 117     3066   4058   7527     12   -751    -46       C  
ATOM   5833  CG  LEU C 117     -51.541  -2.014  28.435  1.00 38.62           C  
ANISOU 5833  CG  LEU C 117     3123   4049   7502     21   -747    -23       C  
ATOM   5834  CD1 LEU C 117     -52.350  -2.055  27.156  1.00 38.29           C  
ANISOU 5834  CD1 LEU C 117     3071   3981   7496     -8   -755    -10       C  
ATOM   5835  CD2 LEU C 117     -50.126  -2.504  28.180  1.00 38.98           C  
ANISOU 5835  CD2 LEU C 117     3184   4124   7502     60   -763    -23       C  
ATOM   5836  N   LEU C 118     -53.235  -0.609  31.686  1.00 39.33           N  
ANISOU 5836  N   LEU C 118     3172   4149   7621     -3   -697    -76       N  
ATOM   5837  CA  LEU C 118     -53.830  -1.319  32.846  1.00 39.82           C  
ANISOU 5837  CA  LEU C 118     3272   4208   7650     -5   -664    -79       C  
ATOM   5838  C   LEU C 118     -55.283  -0.860  33.009  1.00 40.35           C  
ANISOU 5838  C   LEU C 118     3307   4259   7763    -50   -646    -99       C  
ATOM   5839  O   LEU C 118     -56.164  -1.734  33.201  1.00 40.54           O  
ANISOU 5839  O   LEU C 118     3365   4262   7775    -75   -614    -95       O  
ATOM   5840  CB  LEU C 118     -52.983  -1.040  34.093  1.00 40.02           C  
ANISOU 5840  CB  LEU C 118     3297   4274   7634     30   -662    -95       C  
ATOM   5841  CG  LEU C 118     -51.632  -1.757  34.125  1.00 40.22           C  
ANISOU 5841  CG  LEU C 118     3360   4322   7598     85   -677    -82       C  
ATOM   5842  CD1 LEU C 118     -50.648  -1.067  35.051  1.00 40.29           C  
ANISOU 5842  CD1 LEU C 118     3338   4389   7582    121   -689   -114       C  
ATOM   5843  CD2 LEU C 118     -51.799  -3.217  34.513  1.00 40.55           C  
ANISOU 5843  CD2 LEU C 118     3486   4338   7581    104   -653    -53       C  
ATOM   5844  N   THR C 119     -55.520   0.455  32.896  1.00 40.58           N  
ANISOU 5844  N   THR C 119     3276   4297   7846    -59   -664   -123       N  
ATOM   5845  CA  THR C 119     -56.860   1.103  32.961  1.00 40.49           C  
ANISOU 5845  CA  THR C 119     3221   4277   7885    -91   -658   -151       C  
ATOM   5846  C   THR C 119     -57.765   0.574  31.839  1.00 39.96           C  
ANISOU 5846  C   THR C 119     3156   4185   7839   -115   -660   -144       C  
ATOM   5847  O   THR C 119     -58.891   0.171  32.145  1.00 39.42           O  
ANISOU 5847  O   THR C 119     3086   4115   7778   -145   -634   -165       O  
ATOM   5848  CB  THR C 119     -56.735   2.629  32.874  1.00 40.36           C  
ANISOU 5848  CB  THR C 119     3148   4266   7919    -84   -684   -174       C  
ATOM   5849  OG1 THR C 119     -55.841   3.061  33.900  1.00 40.52           O  
ANISOU 5849  OG1 THR C 119     3163   4315   7918    -65   -679   -189       O  
ATOM   5850  CG2 THR C 119     -58.067   3.333  33.019  1.00 40.75           C  
ANISOU 5850  CG2 THR C 119     3153   4310   8018   -104   -682   -209       C  
ATOM   5851  N   LEU C 120     -57.285   0.588  30.592  1.00 39.95           N  
ANISOU 5851  N   LEU C 120     3158   4173   7848   -104   -688   -119       N  
ATOM   5852  CA  LEU C 120     -58.073   0.230  29.383  1.00 40.66           C  
ANISOU 5852  CA  LEU C 120     3242   4247   7959   -120   -698   -116       C  
ATOM   5853  C   LEU C 120     -58.606  -1.204  29.494  1.00 41.82           C  
ANISOU 5853  C   LEU C 120     3430   4383   8075   -146   -663   -115       C  
ATOM   5854  O   LEU C 120     -59.660  -1.488  28.895  1.00 42.69           O  
ANISOU 5854  O   LEU C 120     3522   4490   8207   -172   -658   -134       O  
ATOM   5855  CB  LEU C 120     -57.195   0.400  28.140  1.00 40.48           C  
ANISOU 5855  CB  LEU C 120     3224   4219   7936   -101   -732    -86       C  
ATOM   5856  CG  LEU C 120     -56.992   1.850  27.706  1.00 40.59           C  
ANISOU 5856  CG  LEU C 120     3200   4230   7989    -89   -762    -87       C  
ATOM   5857  CD1 LEU C 120     -55.728   2.023  26.885  1.00 40.51           C  
ANISOU 5857  CD1 LEU C 120     3206   4222   7963    -74   -782    -58       C  
ATOM   5858  CD2 LEU C 120     -58.204   2.342  26.928  1.00 40.51           C  
ANISOU 5858  CD2 LEU C 120     3158   4211   8019    -94   -782   -100       C  
ATOM   5859  N   GLN C 121     -57.924  -2.062  30.252  1.00 42.24           N  
ANISOU 5859  N   GLN C 121     3539   4432   8078   -136   -638    -97       N  
ATOM   5860  CA  GLN C 121     -58.329  -3.472  30.484  1.00 42.87           C  
ANISOU 5860  CA  GLN C 121     3676   4489   8122   -160   -596    -91       C  
ATOM   5861  C   GLN C 121     -59.456  -3.570  31.524  1.00 42.87           C  
ANISOU 5861  C   GLN C 121     3672   4490   8123   -201   -552   -123       C  
ATOM   5862  O   GLN C 121     -59.944  -4.694  31.731  1.00 43.45           O  
ANISOU 5862  O   GLN C 121     3796   4540   8171   -233   -508   -124       O  
ATOM   5863  CB  GLN C 121     -57.113  -4.279  30.945  1.00 43.49           C  
ANISOU 5863  CB  GLN C 121     3824   4559   8141   -123   -590    -58       C  
ATOM   5864  CG  GLN C 121     -56.054  -4.475  29.872  1.00 43.39           C  
ANISOU 5864  CG  GLN C 121     3819   4546   8119    -89   -626    -33       C  
ATOM   5865  CD  GLN C 121     -54.785  -5.015  30.474  1.00 43.60           C  
ANISOU 5865  CD  GLN C 121     3898   4579   8087    -40   -628    -12       C  
ATOM   5866  OE1 GLN C 121     -54.758  -6.098  31.033  1.00 45.34           O  
ANISOU 5866  OE1 GLN C 121     4188   4774   8262    -31   -599      1       O  
ATOM   5867  NE2 GLN C 121     -53.719  -4.252  30.382  1.00 43.75           N  
ANISOU 5867  NE2 GLN C 121     3885   4631   8104     -4   -662    -13       N  
ATOM   5868  N   GLN C 122     -59.853  -2.464  32.157  1.00 42.30           N  
ANISOU 5868  N   GLN C 122     3546   4445   8081   -202   -559   -153       N  
ATOM   5869  CA  GLN C 122     -60.780  -2.479  33.318  1.00 42.59           C  
ANISOU 5869  CA  GLN C 122     3576   4492   8112   -238   -516   -187       C  
ATOM   5870  C   GLN C 122     -61.996  -1.572  33.104  1.00 42.66           C  
ANISOU 5870  C   GLN C 122     3505   4524   8180   -262   -526   -240       C  
ATOM   5871  O   GLN C 122     -62.774  -1.458  34.055  1.00 42.34           O  
ANISOU 5871  O   GLN C 122     3446   4502   8139   -292   -493   -277       O  
ATOM   5872  CB  GLN C 122     -60.045  -2.010  34.570  1.00 42.35           C  
ANISOU 5872  CB  GLN C 122     3555   4482   8051   -209   -513   -181       C  
ATOM   5873  CG  GLN C 122     -58.932  -2.937  35.003  1.00 42.33           C  
ANISOU 5873  CG  GLN C 122     3633   4466   7981   -176   -502   -138       C  
ATOM   5874  CD  GLN C 122     -58.209  -2.365  36.197  1.00 42.36           C  
ANISOU 5874  CD  GLN C 122     3634   4504   7955   -141   -505   -141       C  
ATOM   5875  OE1 GLN C 122     -58.781  -2.207  37.267  1.00 42.56           O  
ANISOU 5875  OE1 GLN C 122     3655   4547   7968   -161   -475   -164       O  
ATOM   5876  NE2 GLN C 122     -56.943  -2.029  36.018  1.00 42.31           N  
ANISOU 5876  NE2 GLN C 122     3626   4513   7936    -90   -543   -124       N  
ATOM   5877  N   ILE C 123     -62.132  -0.938  31.936  1.00 43.30           N  
ANISOU 5877  N   ILE C 123     3540   4606   8304   -246   -571   -244       N  
ATOM   5878  CA  ILE C 123     -63.250  -0.005  31.600  1.00 44.46           C  
ANISOU 5878  CA  ILE C 123     3611   4774   8505   -251   -592   -294       C  
ATOM   5879  C   ILE C 123     -63.827  -0.430  30.248  1.00 45.95           C  
ANISOU 5879  C   ILE C 123     3786   4961   8712   -260   -609   -301       C  
ATOM   5880  O   ILE C 123     -63.025  -0.754  29.360  1.00 45.15           O  
ANISOU 5880  O   ILE C 123     3716   4841   8597   -239   -631   -257       O  
ATOM   5881  CB  ILE C 123     -62.815   1.480  31.611  1.00 44.11           C  
ANISOU 5881  CB  ILE C 123     3527   4736   8497   -208   -638   -294       C  
ATOM   5882  CG1 ILE C 123     -61.630   1.758  30.684  1.00 44.02           C  
ANISOU 5882  CG1 ILE C 123     3538   4703   8483   -171   -676   -243       C  
ATOM   5883  CG2 ILE C 123     -62.524   1.956  33.025  1.00 43.96           C  
ANISOU 5883  CG2 ILE C 123     3504   4730   8467   -206   -618   -308       C  
ATOM   5884  CD1 ILE C 123     -62.006   2.360  29.351  1.00 44.33           C  
ANISOU 5884  CD1 ILE C 123     3547   4736   8559   -152   -720   -242       C  
ATOM   5885  N   GLU C 124     -65.166  -0.460  30.136  1.00 48.93           N  
ANISOU 5885  N   GLU C 124     4113   5364   9113   -290   -597   -360       N  
ATOM   5886  CA  GLU C 124     -65.915  -0.942  28.942  1.00 50.71           C  
ANISOU 5886  CA  GLU C 124     4314   5600   9352   -303   -608   -384       C  
ATOM   5887  C   GLU C 124     -65.715   0.103  27.836  1.00 51.14           C  
ANISOU 5887  C   GLU C 124     4335   5658   9437   -246   -676   -369       C  
ATOM   5888  O   GLU C 124     -66.075   1.274  28.084  1.00 51.45           O  
ANISOU 5888  O   GLU C 124     4329   5711   9509   -216   -705   -393       O  
ATOM   5889  CB  GLU C 124     -67.397  -1.169  29.279  1.00 52.57           C  
ANISOU 5889  CB  GLU C 124     4496   5874   9603   -351   -574   -466       C  
ATOM   5890  CG  GLU C 124     -67.976  -2.508  28.791  1.00 54.23           C  
ANISOU 5890  CG  GLU C 124     4723   6086   9796   -408   -531   -491       C  
ATOM   5891  CD  GLU C 124     -68.074  -3.645  29.812  1.00 55.82           C  
ANISOU 5891  CD  GLU C 124     4983   6265   9959   -476   -450   -495       C  
ATOM   5892  OE1 GLU C 124     -68.106  -3.332  31.038  1.00 55.85           O  
ANISOU 5892  OE1 GLU C 124     4992   6273   9953   -488   -423   -502       O  
ATOM   5893  OE2 GLU C 124     -68.115  -4.845  29.388  1.00 54.87           O  
ANISOU 5893  OE2 GLU C 124     4907   6122   9818   -518   -413   -492       O  
ATOM   5894  N   LEU C 125     -65.141  -0.286  26.688  1.00 50.94           N  
ANISOU 5894  N   LEU C 125     4335   5619   9400   -229   -700   -330       N  
ATOM   5895  CA  LEU C 125     -64.790   0.661  25.597  1.00 50.93           C  
ANISOU 5895  CA  LEU C 125     4318   5614   9416   -176   -761   -302       C  
ATOM   5896  C   LEU C 125     -64.646  -0.077  24.263  1.00 51.25           C  
ANISOU 5896  C   LEU C 125     4373   5657   9440   -175   -776   -284       C  
ATOM   5897  O   LEU C 125     -64.187  -1.214  24.270  1.00 50.92           O  
ANISOU 5897  O   LEU C 125     4374   5602   9369   -204   -743   -266       O  
ATOM   5898  CB  LEU C 125     -63.484   1.352  25.982  1.00 50.67           C  
ANISOU 5898  CB  LEU C 125     4321   5552   9378   -149   -773   -249       C  
ATOM   5899  CG  LEU C 125     -63.169   2.633  25.221  1.00 50.77           C  
ANISOU 5899  CG  LEU C 125     4321   5553   9414   -100   -825   -226       C  
ATOM   5900  CD1 LEU C 125     -63.949   3.802  25.801  1.00 51.14           C  
ANISOU 5900  CD1 LEU C 125     4323   5607   9501    -80   -841   -266       C  
ATOM   5901  CD2 LEU C 125     -61.673   2.907  25.254  1.00 51.17           C  
ANISOU 5901  CD2 LEU C 125     4416   5577   9447    -89   -828   -171       C  
ATOM   5902  N   LYS C 126     -65.011   0.582  23.161  1.00 52.93           N  
ANISOU 5902  N   LYS C 126     4554   5886   9669   -136   -825   -287       N  
ATOM   5903  CA  LYS C 126     -64.891   0.064  21.775  1.00 54.72           C  
ANISOU 5903  CA  LYS C 126     4787   6124   9878   -126   -848   -271       C  
ATOM   5904  C   LYS C 126     -64.260   1.140  20.886  1.00 53.88           C  
ANISOU 5904  C   LYS C 126     4692   6005   9775    -72   -902   -223       C  
ATOM   5905  O   LYS C 126     -64.866   2.216  20.743  1.00 55.06           O  
ANISOU 5905  O   LYS C 126     4810   6161   9948    -32   -937   -239       O  
ATOM   5906  CB  LYS C 126     -66.273  -0.328  21.249  1.00 57.68           C  
ANISOU 5906  CB  LYS C 126     5105   6546  10263   -137   -852   -341       C  
ATOM   5907  CG  LYS C 126     -66.415  -0.400  19.733  1.00 60.00           C  
ANISOU 5907  CG  LYS C 126     5384   6865  10545   -106   -895   -337       C  
ATOM   5908  CD  LYS C 126     -67.778  -0.925  19.303  1.00 62.55           C  
ANISOU 5908  CD  LYS C 126     5644   7246  10876   -123   -893   -420       C  
ATOM   5909  CE  LYS C 126     -67.854  -1.293  17.833  1.00 63.94           C  
ANISOU 5909  CE  LYS C 126     5807   7453  11031   -101   -926   -421       C  
ATOM   5910  NZ  LYS C 126     -69.255  -1.524  17.390  1.00 65.35           N  
ANISOU 5910  NZ  LYS C 126     5909   7701  11217   -103   -936   -513       N  
ATOM   5911  N   PHE C 127     -63.109   0.840  20.283  1.00 52.30           N  
ANISOU 5911  N   PHE C 127     4536   5786   9547    -70   -905   -168       N  
ATOM   5912  CA  PHE C 127     -62.402   1.754  19.348  1.00 51.70           C  
ANISOU 5912  CA  PHE C 127     4481   5696   9465    -29   -946   -118       C  
ATOM   5913  C   PHE C 127     -63.074   1.706  17.976  1.00 51.63           C  
ANISOU 5913  C   PHE C 127     4450   5719   9447     -2   -984   -128       C  
ATOM   5914  O   PHE C 127     -63.487   0.620  17.532  1.00 51.97           O  
ANISOU 5914  O   PHE C 127     4477   5791   9475    -25   -972   -156       O  
ATOM   5915  CB  PHE C 127     -60.907   1.426  19.290  1.00 50.69           C  
ANISOU 5915  CB  PHE C 127     4402   5546   9310    -43   -932    -67       C  
ATOM   5916  CG  PHE C 127     -60.193   1.808  20.557  1.00 49.35           C  
ANISOU 5916  CG  PHE C 127     4250   5352   9148    -53   -907    -58       C  
ATOM   5917  CD1 PHE C 127     -60.075   3.140  20.910  1.00 48.84           C  
ANISOU 5917  CD1 PHE C 127     4181   5267   9108    -32   -922    -49       C  
ATOM   5918  CD2 PHE C 127     -59.707   0.838  21.418  1.00 49.10           C  
ANISOU 5918  CD2 PHE C 127     4240   5318   9098    -81   -868    -61       C  
ATOM   5919  CE1 PHE C 127     -59.472   3.499  22.102  1.00 48.80           C  
ANISOU 5919  CE1 PHE C 127     4183   5246   9111    -42   -899    -51       C  
ATOM   5920  CE2 PHE C 127     -59.091   1.200  22.603  1.00 48.93           C  
ANISOU 5920  CE2 PHE C 127     4228   5283   9077    -84   -849    -58       C  
ATOM   5921  CZ  PHE C 127     -58.975   2.531  22.939  1.00 49.19           C  
ANISOU 5921  CZ  PHE C 127     4248   5303   9137    -67   -864    -56       C  
ATOM   5922  N   ASN C 128     -63.187   2.867  17.335  1.00 51.37           N  
ANISOU 5922  N   ASN C 128     4418   5680   9420     45  -1027   -106       N  
ATOM   5923  CA  ASN C 128     -63.806   3.014  15.996  1.00 52.04           C  
ANISOU 5923  CA  ASN C 128     4487   5797   9489     87  -1072   -110       C  
ATOM   5924  C   ASN C 128     -62.815   2.570  14.929  1.00 51.43           C  
ANISOU 5924  C   ASN C 128     4448   5720   9372     80  -1076    -60       C  
ATOM   5925  O   ASN C 128     -63.213   1.886  13.994  1.00 51.67           O  
ANISOU 5925  O   ASN C 128     4459   5791   9380     84  -1090    -78       O  
ATOM   5926  CB  ASN C 128     -64.384   4.414  15.803  1.00 53.23           C  
ANISOU 5926  CB  ASN C 128     4631   5935   9656    149  -1117   -108       C  
ATOM   5927  CG  ASN C 128     -65.719   4.532  16.510  1.00 54.29           C  
ANISOU 5927  CG  ASN C 128     4706   6100   9823    161  -1121   -183       C  
ATOM   5928  OD1 ASN C 128     -65.816   5.153  17.568  1.00 55.32           O  
ANISOU 5928  OD1 ASN C 128     4830   6204   9984    159  -1109   -196       O  
ATOM   5929  ND2 ASN C 128     -66.725   3.839  15.999  1.00 54.96           N  
ANISOU 5929  ND2 ASN C 128     4739   6244   9899    165  -1132   -241       N  
ATOM   5930  N   PRO C 129     -61.508   2.903  15.019  1.00 51.23           N  
ANISOU 5930  N   PRO C 129     4472   5657   9336     67  -1063     -4       N  
ATOM   5931  CA  PRO C 129     -60.522   2.328  14.099  1.00 50.65           C  
ANISOU 5931  CA  PRO C 129     4428   5592   9223     53  -1060     32       C  
ATOM   5932  C   PRO C 129     -60.355   0.825  14.344  1.00 48.78           C  
ANISOU 5932  C   PRO C 129     4182   5375   8976     11  -1026      4       C  
ATOM   5933  O   PRO C 129     -60.144   0.398  15.477  1.00 48.08           O  
ANISOU 5933  O   PRO C 129     4097   5269   8902    -17   -992     -9       O  
ATOM   5934  CB  PRO C 129     -59.210   3.085  14.399  1.00 50.56           C  
ANISOU 5934  CB  PRO C 129     4462   5539   9209     42  -1046     82       C  
ATOM   5935  CG  PRO C 129     -59.649   4.303  15.194  1.00 50.94           C  
ANISOU 5935  CG  PRO C 129     4508   5552   9294     64  -1053     77       C  
ATOM   5936  CD  PRO C 129     -60.898   3.867  15.945  1.00 51.09           C  
ANISOU 5936  CD  PRO C 129     4478   5593   9341     65  -1050     17       C  
ATOM   5937  N   PRO C 130     -60.471  -0.030  13.300  1.00 47.69           N  
ANISOU 5937  N   PRO C 130     4035   5272   8811      8  -1035     -4       N  
ATOM   5938  CA  PRO C 130     -60.131  -1.446  13.429  1.00 47.30           C  
ANISOU 5938  CA  PRO C 130     3990   5230   8749    -30  -1002    -24       C  
ATOM   5939  C   PRO C 130     -58.733  -1.626  14.045  1.00 46.53           C  
ANISOU 5939  C   PRO C 130     3935   5102   8640    -48   -976     10       C  
ATOM   5940  O   PRO C 130     -58.613  -2.333  15.021  1.00 45.70           O  
ANISOU 5940  O   PRO C 130     3840   4980   8542    -71   -942     -5       O  
ATOM   5941  CB  PRO C 130     -60.171  -1.966  11.985  1.00 47.25           C  
ANISOU 5941  CB  PRO C 130     3975   5265   8711    -21  -1025    -26       C  
ATOM   5942  CG  PRO C 130     -61.129  -1.041  11.280  1.00 47.22           C  
ANISOU 5942  CG  PRO C 130     3943   5288   8709     22  -1069    -32       C  
ATOM   5943  CD  PRO C 130     -60.957   0.307  11.953  1.00 47.82           C  
ANISOU 5943  CD  PRO C 130     4039   5323   8805     45  -1078      0       C  
ATOM   5944  N   ALA C 131     -57.726  -0.954  13.480  1.00 46.03           N  
ANISOU 5944  N   ALA C 131     3896   5036   8557    -36   -991     55       N  
ATOM   5945  CA  ALA C 131     -56.312  -1.002  13.920  1.00 45.68           C  
ANISOU 5945  CA  ALA C 131     3882   4975   8497    -49   -970     80       C  
ATOM   5946  C   ALA C 131     -56.228  -0.999  15.442  1.00 45.52           C  
ANISOU 5946  C   ALA C 131     3867   4928   8500    -59   -943     67       C  
ATOM   5947  O   ALA C 131     -55.508  -1.859  16.004  1.00 44.63           O  
ANISOU 5947  O   ALA C 131     3772   4812   8372    -71   -919     62       O  
ATOM   5948  CB  ALA C 131     -55.537   0.137  13.318  1.00 45.67           C  
ANISOU 5948  CB  ALA C 131     3899   4968   8482    -40   -986    122       C  
ATOM   5949  N   LEU C 132     -56.969  -0.086  16.071  1.00 46.41           N  
ANISOU 5949  N   LEU C 132     3964   5023   8644    -51   -948     59       N  
ATOM   5950  CA  LEU C 132     -56.968   0.119  17.543  1.00 47.09           C  
ANISOU 5950  CA  LEU C 132     4050   5088   8752    -59   -923     45       C  
ATOM   5951  C   LEU C 132     -57.758  -0.990  18.242  1.00 47.28           C  
ANISOU 5951  C   LEU C 132     4068   5115   8782    -77   -897      8       C  
ATOM   5952  O   LEU C 132     -57.292  -1.436  19.298  1.00 48.01           O  
ANISOU 5952  O   LEU C 132     4179   5195   8867    -88   -869      4       O  
ATOM   5953  CB  LEU C 132     -57.566   1.486  17.881  1.00 47.47           C  
ANISOU 5953  CB  LEU C 132     4082   5119   8834    -42   -939     44       C  
ATOM   5954  CG  LEU C 132     -56.583   2.652  17.961  1.00 47.46           C  
ANISOU 5954  CG  LEU C 132     4100   5095   8835    -38   -942     75       C  
ATOM   5955  CD1 LEU C 132     -57.253   3.857  18.607  1.00 48.05           C  
ANISOU 5955  CD1 LEU C 132     4162   5145   8949    -23   -950     64       C  
ATOM   5956  CD2 LEU C 132     -55.312   2.280  18.715  1.00 46.91           C  
ANISOU 5956  CD2 LEU C 132     4046   5027   8747    -56   -915     77       C  
ATOM   5957  N   GLN C 133     -58.916  -1.391  17.709  1.00 47.19           N  
ANISOU 5957  N   GLN C 133     4030   5120   8779    -81   -904    -21       N  
ATOM   5958  CA  GLN C 133     -59.756  -2.456  18.324  1.00 47.68           C  
ANISOU 5958  CA  GLN C 133     4084   5183   8846   -111   -870    -63       C  
ATOM   5959  C   GLN C 133     -58.976  -3.782  18.248  1.00 47.06           C  
ANISOU 5959  C   GLN C 133     4047   5095   8737   -127   -845    -54       C  
ATOM   5960  O   GLN C 133     -58.775  -4.419  19.306  1.00 46.46           O  
ANISOU 5960  O   GLN C 133     4001   4996   8653   -143   -809    -59       O  
ATOM   5961  CB  GLN C 133     -61.148  -2.512  17.673  1.00 48.07           C  
ANISOU 5961  CB  GLN C 133     4088   5263   8913   -113   -884   -108       C  
ATOM   5962  CG  GLN C 133     -62.150  -3.429  18.378  1.00 48.32           C  
ANISOU 5962  CG  GLN C 133     4105   5297   8955   -154   -843   -162       C  
ATOM   5963  CD  GLN C 133     -62.451  -3.026  19.804  1.00 48.82           C  
ANISOU 5963  CD  GLN C 133     4167   5344   9038   -167   -817   -176       C  
ATOM   5964  OE1 GLN C 133     -62.539  -1.844  20.136  1.00 49.69           O  
ANISOU 5964  OE1 GLN C 133     4257   5454   9167   -140   -840   -169       O  
ATOM   5965  NE2 GLN C 133     -62.598  -4.014  20.676  1.00 48.86           N  
ANISOU 5965  NE2 GLN C 133     4198   5331   9034   -208   -765   -195       N  
ATOM   5966  N   ASP C 134     -58.511  -4.156  17.055  1.00 46.99           N  
ANISOU 5966  N   ASP C 134     4042   5102   8707   -119   -864    -41       N  
ATOM   5967  CA  ASP C 134     -57.701  -5.383  16.829  1.00 47.05           C  
ANISOU 5967  CA  ASP C 134     4088   5103   8686   -127   -846    -35       C  
ATOM   5968  C   ASP C 134     -56.585  -5.423  17.879  1.00 46.06           C  
ANISOU 5968  C   ASP C 134     4002   4954   8544   -116   -830    -11       C  
ATOM   5969  O   ASP C 134     -56.546  -6.387  18.649  1.00 46.01           O  
ANISOU 5969  O   ASP C 134     4031   4922   8526   -127   -797    -21       O  
ATOM   5970  CB  ASP C 134     -57.169  -5.456  15.394  1.00 47.61           C  
ANISOU 5970  CB  ASP C 134     4151   5201   8735   -114   -876    -21       C  
ATOM   5971  CG  ASP C 134     -58.160  -5.969  14.352  1.00 48.22           C  
ANISOU 5971  CG  ASP C 134     4198   5307   8816   -125   -885    -55       C  
ATOM   5972  OD1 ASP C 134     -57.779  -6.038  13.163  1.00 48.18           O  
ANISOU 5972  OD1 ASP C 134     4186   5330   8790   -113   -910    -45       O  
ATOM   5973  OD2 ASP C 134     -59.303  -6.308  14.730  1.00 48.89           O  
ANISOU 5973  OD2 ASP C 134     4263   5390   8922   -147   -866    -96       O  
ATOM   5974  N   ALA C 135     -55.746  -4.391  17.953  1.00 46.00           N  
ANISOU 5974  N   ALA C 135     3989   4954   8533    -96   -849     15       N  
ATOM   5975  CA  ALA C 135     -54.557  -4.353  18.841  1.00 46.21           C  
ANISOU 5975  CA  ALA C 135     4043   4973   8540    -81   -839     30       C  
ATOM   5976  C   ALA C 135     -54.979  -4.404  20.320  1.00 46.67           C  
ANISOU 5976  C   ALA C 135     4114   5010   8608    -86   -811     18       C  
ATOM   5977  O   ALA C 135     -54.230  -4.993  21.131  1.00 46.92           O  
ANISOU 5977  O   ALA C 135     4181   5032   8611    -72   -794     21       O  
ATOM   5978  CB  ALA C 135     -53.741  -3.130  18.540  1.00 45.76           C  
ANISOU 5978  CB  ALA C 135     3969   4932   8484    -70   -861     50       C  
ATOM   5979  N   TYR C 136     -56.137  -3.824  20.655  1.00 47.10           N  
ANISOU 5979  N   TYR C 136     4141   5059   8695   -102   -807      1       N  
ATOM   5980  CA  TYR C 136     -56.715  -3.774  22.026  1.00 47.36           C  
ANISOU 5980  CA  TYR C 136     4178   5077   8739   -113   -779    -15       C  
ATOM   5981  C   TYR C 136     -57.107  -5.183  22.492  1.00 47.27           C  
ANISOU 5981  C   TYR C 136     4207   5044   8709   -134   -739    -29       C  
ATOM   5982  O   TYR C 136     -56.968  -5.479  23.694  1.00 47.38           O  
ANISOU 5982  O   TYR C 136     4253   5042   8706   -134   -711    -29       O  
ATOM   5983  CB  TYR C 136     -57.907  -2.815  22.027  1.00 47.70           C  
ANISOU 5983  CB  TYR C 136     4172   5127   8823   -124   -789    -38       C  
ATOM   5984  CG  TYR C 136     -58.621  -2.574  23.330  1.00 48.16           C  
ANISOU 5984  CG  TYR C 136     4222   5179   8897   -138   -763    -63       C  
ATOM   5985  CD1 TYR C 136     -57.973  -2.596  24.557  1.00 48.36           C  
ANISOU 5985  CD1 TYR C 136     4273   5196   8904   -132   -742    -55       C  
ATOM   5986  CD2 TYR C 136     -59.964  -2.239  23.317  1.00 48.59           C  
ANISOU 5986  CD2 TYR C 136     4233   5243   8983   -155   -762   -100       C  
ATOM   5987  CE1 TYR C 136     -58.654  -2.335  25.736  1.00 48.53           C  
ANISOU 5987  CE1 TYR C 136     4284   5217   8937   -147   -717    -80       C  
ATOM   5988  CE2 TYR C 136     -60.656  -1.964  24.483  1.00 49.08           C  
ANISOU 5988  CE2 TYR C 136     4280   5306   9060   -171   -738   -130       C  
ATOM   5989  CZ  TYR C 136     -60.001  -2.023  25.698  1.00 49.06           C  
ANISOU 5989  CZ  TYR C 136     4308   5293   9038   -169   -713   -117       C  
ATOM   5990  OH  TYR C 136     -60.715  -1.763  26.830  1.00 50.34           O  
ANISOU 5990  OH  TYR C 136     4454   5460   9211   -187   -688   -149       O  
ATOM   5991  N   TYR C 137     -57.589  -6.029  21.580  1.00 46.94           N  
ANISOU 5991  N   TYR C 137     4168   5000   8666   -152   -735    -42       N  
ATOM   5992  CA  TYR C 137     -57.878  -7.456  21.876  1.00 47.45           C  
ANISOU 5992  CA  TYR C 137     4281   5034   8711   -177   -692    -56       C  
ATOM   5993  C   TYR C 137     -56.557  -8.174  22.159  1.00 48.61           C  
ANISOU 5993  C   TYR C 137     4489   5162   8816   -144   -689    -26       C  
ATOM   5994  O   TYR C 137     -56.433  -8.772  23.251  1.00 49.32           O  
ANISOU 5994  O   TYR C 137     4634   5223   8882   -142   -656    -20       O  
ATOM   5995  CB  TYR C 137     -58.658  -8.145  20.751  1.00 46.80           C  
ANISOU 5995  CB  TYR C 137     4181   4958   8641   -206   -689    -85       C  
ATOM   5996  CG  TYR C 137     -60.134  -7.853  20.750  1.00 46.42           C  
ANISOU 5996  CG  TYR C 137     4083   4927   8626   -243   -677   -130       C  
ATOM   5997  CD1 TYR C 137     -60.892  -8.004  21.899  1.00 46.47           C  
ANISOU 5997  CD1 TYR C 137     4098   4916   8639   -277   -634   -154       C  
ATOM   5998  CD2 TYR C 137     -60.772  -7.410  19.604  1.00 46.49           C  
ANISOU 5998  CD2 TYR C 137     4032   4974   8655   -242   -711   -154       C  
ATOM   5999  CE1 TYR C 137     -62.244  -7.706  21.914  1.00 47.11           C  
ANISOU 5999  CE1 TYR C 137     4124   5023   8751   -312   -623   -207       C  
ATOM   6000  CE2 TYR C 137     -62.127  -7.122  19.595  1.00 46.99           C  
ANISOU 6000  CE2 TYR C 137     4042   5063   8747   -268   -705   -205       C  
ATOM   6001  CZ  TYR C 137     -62.866  -7.277  20.755  1.00 47.27           C  
ANISOU 6001  CZ  TYR C 137     4080   5085   8793   -305   -660   -235       C  
ATOM   6002  OH  TYR C 137     -64.201  -7.010  20.762  1.00 47.84           O  
ANISOU 6002  OH  TYR C 137     4093   5192   8892   -332   -653   -296       O  
ATOM   6003  N   ARG C 138     -55.598  -8.083  21.230  1.00 49.46           N  
ANISOU 6003  N   ARG C 138     4590   5291   8911   -115   -724    -10       N  
ATOM   6004  CA  ARG C 138     -54.303  -8.810  21.311  1.00 50.59           C  
ANISOU 6004  CA  ARG C 138     4781   5426   9012    -76   -728      7       C  
ATOM   6005  C   ARG C 138     -53.471  -8.258  22.477  1.00 50.66           C  
ANISOU 6005  C   ARG C 138     4802   5443   9000    -42   -731     22       C  
ATOM   6006  O   ARG C 138     -52.608  -9.000  22.967  1.00 50.90           O  
ANISOU 6006  O   ARG C 138     4884   5463   8990     -6   -725     30       O  
ATOM   6007  CB  ARG C 138     -53.603  -8.791  19.946  1.00 52.04           C  
ANISOU 6007  CB  ARG C 138     4941   5640   9190    -62   -762     11       C  
ATOM   6008  CG  ARG C 138     -54.322  -9.645  18.902  1.00 54.25           C  
ANISOU 6008  CG  ARG C 138     5220   5912   9479    -89   -755     -8       C  
ATOM   6009  CD  ARG C 138     -53.484 -10.361  17.851  1.00 56.68           C  
ANISOU 6009  CD  ARG C 138     5539   6234   9764    -69   -773    -10       C  
ATOM   6010  NE  ARG C 138     -52.675  -9.462  17.026  1.00 59.28           N  
ANISOU 6010  NE  ARG C 138     5824   6611  10086    -52   -812      2       N  
ATOM   6011  CZ  ARG C 138     -51.946  -9.818  15.955  1.00 60.77           C  
ANISOU 6011  CZ  ARG C 138     6006   6827  10255    -39   -832     -1       C  
ATOM   6012  NH1 ARG C 138     -51.916 -11.077  15.536  1.00 61.47           N  
ANISOU 6012  NH1 ARG C 138     6125   6899  10331    -36   -821    -19       N  
ATOM   6013  NH2 ARG C 138     -51.238  -8.905  15.304  1.00 60.48           N  
ANISOU 6013  NH2 ARG C 138     5933   6833  10210    -31   -860     11       N  
ATOM   6014  N   ALA C 139     -53.756  -7.037  22.943  1.00 51.61           N  
ANISOU 6014  N   ALA C 139     4880   5581   9146    -51   -738     20       N  
ATOM   6015  CA  ALA C 139     -53.184  -6.441  24.176  1.00 52.82           C  
ANISOU 6015  CA  ALA C 139     5037   5746   9285    -27   -736     24       C  
ATOM   6016  C   ALA C 139     -53.646  -7.220  25.415  1.00 54.57           C  
ANISOU 6016  C   ALA C 139     5313   5936   9485    -30   -696     23       C  
ATOM   6017  O   ALA C 139     -52.779  -7.701  26.169  1.00 53.48           O  
ANISOU 6017  O   ALA C 139     5220   5797   9302     10   -692     33       O  
ATOM   6018  CB  ALA C 139     -53.579  -4.993  24.284  1.00 52.68           C  
ANISOU 6018  CB  ALA C 139     4961   5746   9307    -43   -750     17       C  
ATOM   6019  N   ARG C 140     -54.964  -7.331  25.618  1.00 58.41           N  
ANISOU 6019  N   ARG C 140     5795   6401   9998    -75   -667      9       N  
ATOM   6020  CA  ARG C 140     -55.588  -8.028  26.784  1.00 61.02           C  
ANISOU 6020  CA  ARG C 140     6177   6698  10308    -94   -619      5       C  
ATOM   6021  C   ARG C 140     -55.032  -9.454  26.894  1.00 60.40           C  
ANISOU 6021  C   ARG C 140     6186   6581  10181    -71   -598     24       C  
ATOM   6022  O   ARG C 140     -54.843  -9.927  28.032  1.00 60.36           O  
ANISOU 6022  O   ARG C 140     6243   6555  10135    -53   -571     37       O  
ATOM   6023  CB  ARG C 140     -57.117  -8.085  26.659  1.00 64.02           C  
ANISOU 6023  CB  ARG C 140     6532   7066  10724   -156   -589    -23       C  
ATOM   6024  CG  ARG C 140     -57.871  -7.554  27.874  1.00 67.56           C  
ANISOU 6024  CG  ARG C 140     6967   7519  11180   -180   -561    -40       C  
ATOM   6025  CD  ARG C 140     -58.266  -6.096  27.678  1.00 69.36           C  
ANISOU 6025  CD  ARG C 140     7110   7787  11456   -182   -594    -60       C  
ATOM   6026  NE  ARG C 140     -59.472  -5.964  26.862  1.00 70.27           N  
ANISOU 6026  NE  ARG C 140     7175   7911  11614   -221   -595    -94       N  
ATOM   6027  CZ  ARG C 140     -60.707  -5.782  27.333  1.00 71.74           C  
ANISOU 6027  CZ  ARG C 140     7329   8104  11822   -262   -568   -134       C  
ATOM   6028  NH1 ARG C 140     -60.926  -5.676  28.637  1.00 71.41           N  
ANISOU 6028  NH1 ARG C 140     7303   8062  11768   -275   -535   -142       N  
ATOM   6029  NH2 ARG C 140     -61.721  -5.687  26.483  1.00 73.18           N  
ANISOU 6029  NH2 ARG C 140     7460   8304  12038   -289   -575   -172       N  
ATOM   6030  N   ALA C 141     -54.797 -10.099  25.746  1.00 58.98           N  
ANISOU 6030  N   ALA C 141     6014   6391  10003    -69   -611     24       N  
ATOM   6031  CA  ALA C 141     -54.216 -11.453  25.613  1.00 59.10           C  
ANISOU 6031  CA  ALA C 141     6110   6367   9978    -41   -598     37       C  
ATOM   6032  C   ALA C 141     -52.794 -11.486  26.194  1.00 59.67           C  
ANISOU 6032  C   ALA C 141     6215   6456  10000     34   -624     57       C  
ATOM   6033  O   ALA C 141     -52.492 -12.419  26.965  1.00 61.07           O  
ANISOU 6033  O   ALA C 141     6478   6594  10130     67   -601     73       O  
ATOM   6034  CB  ALA C 141     -54.225 -11.857  24.162  1.00 59.46           C  
ANISOU 6034  CB  ALA C 141     6132   6414  10043    -54   -616     25       C  
ATOM   6035  N   GLY C 142     -51.953 -10.508  25.844  1.00 58.38           N  
ANISOU 6035  N   GLY C 142     5988   6350   9843     63   -669     54       N  
ATOM   6036  CA  GLY C 142     -50.550 -10.434  26.299  1.00 56.35           C  
ANISOU 6036  CA  GLY C 142     5743   6127   9541    134   -698     58       C  
ATOM   6037  C   GLY C 142     -49.641  -9.772  25.276  1.00 55.34           C  
ANISOU 6037  C   GLY C 142     5549   6053   9424    149   -742     45       C  
ATOM   6038  O   GLY C 142     -48.575  -9.261  25.696  1.00 55.65           O  
ANISOU 6038  O   GLY C 142     5566   6139   9437    192   -766     36       O  
ATOM   6039  N   GLU C 143     -50.032  -9.794  23.994  1.00 53.61           N  
ANISOU 6039  N   GLU C 143     5299   5832   9238    112   -749     41       N  
ATOM   6040  CA  GLU C 143     -49.302  -9.166  22.858  1.00 53.28           C  
ANISOU 6040  CA  GLU C 143     5198   5838   9206    114   -785     32       C  
ATOM   6041  C   GLU C 143     -49.712  -7.685  22.742  1.00 51.60           C  
ANISOU 6041  C   GLU C 143     4918   5651   9036     76   -793     31       C  
ATOM   6042  O   GLU C 143     -50.539  -7.351  21.858  1.00 51.03           O  
ANISOU 6042  O   GLU C 143     4817   5572   9000     35   -795     33       O  
ATOM   6043  CB  GLU C 143     -49.573  -9.991  21.594  1.00 54.25           C  
ANISOU 6043  CB  GLU C 143     5329   5945   9336     97   -787     28       C  
ATOM   6044  CG  GLU C 143     -49.097  -9.351  20.285  1.00 55.19           C  
ANISOU 6044  CG  GLU C 143     5389   6111   9468     85   -817     22       C  
ATOM   6045  CD  GLU C 143     -49.929  -9.670  19.048  1.00 55.39           C  
ANISOU 6045  CD  GLU C 143     5400   6127   9519     46   -816     19       C  
ATOM   6046  OE1 GLU C 143     -50.233 -10.874  18.827  1.00 55.91           O  
ANISOU 6046  OE1 GLU C 143     5508   6158   9576     47   -801     11       O  
ATOM   6047  OE2 GLU C 143     -50.240  -8.728  18.276  1.00 54.52           O  
ANISOU 6047  OE2 GLU C 143     5238   6042   9433     18   -832     22       O  
ATOM   6048  N   ALA C 144     -49.127  -6.834  23.591  1.00 50.04           N  
ANISOU 6048  N   ALA C 144     4699   5481   8830     93   -799     24       N  
ATOM   6049  CA  ALA C 144     -49.507  -5.418  23.798  1.00 49.01           C  
ANISOU 6049  CA  ALA C 144     4518   5364   8740     63   -801     22       C  
ATOM   6050  C   ALA C 144     -48.486  -4.470  23.161  1.00 47.61           C  
ANISOU 6050  C   ALA C 144     4293   5230   8563     62   -824     12       C  
ATOM   6051  O   ALA C 144     -48.597  -3.247  23.388  1.00 47.68           O  
ANISOU 6051  O   ALA C 144     4266   5247   8601     41   -824      8       O  
ATOM   6052  CB  ALA C 144     -49.634  -5.155  25.276  1.00 49.28           C  
ANISOU 6052  CB  ALA C 144     4562   5396   8766     76   -785     15       C  
ATOM   6053  N   ALA C 145     -47.522  -4.999  22.413  1.00 47.22           N  
ANISOU 6053  N   ALA C 145     4246   5208   8484     83   -839      5       N  
ATOM   6054  CA  ALA C 145     -46.493  -4.194  21.717  1.00 46.99           C  
ANISOU 6054  CA  ALA C 145     4175   5227   8452     74   -854     -8       C  
ATOM   6055  C   ALA C 145     -47.186  -3.299  20.697  1.00 45.99           C  
ANISOU 6055  C   ALA C 145     4023   5084   8365     26   -856     10       C  
ATOM   6056  O   ALA C 145     -47.038  -2.081  20.781  1.00 45.71           O  
ANISOU 6056  O   ALA C 145     3960   5056   8351      3   -854      8       O  
ATOM   6057  CB  ALA C 145     -45.468  -5.086  21.061  1.00 47.34           C  
ANISOU 6057  CB  ALA C 145     4228   5305   8455    104   -868    -24       C  
ATOM   6058  N   ASN C 146     -47.946  -3.906  19.791  1.00 46.05           N  
ANISOU 6058  N   ASN C 146     4044   5070   8381     14   -860     27       N  
ATOM   6059  CA  ASN C 146     -48.641  -3.182  18.697  1.00 45.90           C  
ANISOU 6059  CA  ASN C 146     4006   5041   8390    -19   -869     46       C  
ATOM   6060  C   ASN C 146     -49.513  -2.082  19.280  1.00 45.25           C  
ANISOU 6060  C   ASN C 146     3911   4933   8350    -37   -863     54       C  
ATOM   6061  O   ASN C 146     -49.347  -0.919  18.880  1.00 46.69           O  
ANISOU 6061  O   ASN C 146     4075   5117   8548    -55   -868     63       O  
ATOM   6062  CB  ASN C 146     -49.496  -4.105  17.836  1.00 46.03           C  
ANISOU 6062  CB  ASN C 146     4036   5043   8409    -24   -873     53       C  
ATOM   6063  CG  ASN C 146     -48.743  -4.482  16.587  1.00 46.77           C  
ANISOU 6063  CG  ASN C 146     4124   5170   8476    -24   -887     52       C  
ATOM   6064  OD1 ASN C 146     -48.900  -3.830  15.561  1.00 47.41           O  
ANISOU 6064  OD1 ASN C 146     4188   5262   8563    -45   -898     66       O  
ATOM   6065  ND2 ASN C 146     -47.856  -5.460  16.694  1.00 47.44           N  
ANISOU 6065  ND2 ASN C 146     4225   5273   8527      2   -887     34       N  
ATOM   6066  N   PHE C 147     -50.413  -2.457  20.181  1.00 43.55           N  
ANISOU 6066  N   PHE C 147     3706   4690   8148    -32   -851     49       N  
ATOM   6067  CA  PHE C 147     -51.402  -1.544  20.793  1.00 42.25           C  
ANISOU 6067  CA  PHE C 147     3525   4502   8023    -46   -846     49       C  
ATOM   6068  C   PHE C 147     -50.700  -0.284  21.301  1.00 41.97           C  
ANISOU 6068  C   PHE C 147     3471   4475   7999    -49   -846     44       C  
ATOM   6069  O   PHE C 147     -51.216   0.825  21.036  1.00 42.84           O  
ANISOU 6069  O   PHE C 147     3566   4569   8143    -63   -853     51       O  
ATOM   6070  CB  PHE C 147     -52.148  -2.249  21.920  1.00 41.88           C  
ANISOU 6070  CB  PHE C 147     3496   4436   7978    -42   -825     37       C  
ATOM   6071  CG  PHE C 147     -53.278  -1.433  22.478  1.00 41.97           C  
ANISOU 6071  CG  PHE C 147     3485   4429   8029    -56   -820     28       C  
ATOM   6072  CD1 PHE C 147     -54.213  -0.861  21.632  1.00 42.00           C  
ANISOU 6072  CD1 PHE C 147     3465   4425   8065    -68   -837     31       C  
ATOM   6073  CD2 PHE C 147     -53.395  -1.232  23.837  1.00 42.25           C  
ANISOU 6073  CD2 PHE C 147     3522   4462   8069    -53   -802     14       C  
ATOM   6074  CE1 PHE C 147     -55.240  -0.095  22.138  1.00 42.41           C  
ANISOU 6074  CE1 PHE C 147     3494   4466   8154    -74   -836     17       C  
ATOM   6075  CE2 PHE C 147     -54.436  -0.476  24.348  1.00 42.79           C  
ANISOU 6075  CE2 PHE C 147     3564   4518   8174    -66   -798      0       C  
ATOM   6076  CZ  PHE C 147     -55.355   0.091  23.496  1.00 42.89           C  
ANISOU 6076  CZ  PHE C 147     3553   4523   8221    -76   -816      0       C  
ATOM   6077  N   CYS C 148     -49.565  -0.454  21.988  1.00 40.58           N  
ANISOU 6077  N   CYS C 148     3296   4326   7794    -33   -839     27       N  
ATOM   6078  CA  CYS C 148     -48.759   0.648  22.565  1.00 40.04           C  
ANISOU 6078  CA  CYS C 148     3205   4275   7732    -39   -833      9       C  
ATOM   6079  C   CYS C 148     -48.267   1.543  21.418  1.00 39.37           C  
ANISOU 6079  C   CYS C 148     3108   4193   7656    -67   -839     20       C  
ATOM   6080  O   CYS C 148     -48.559   2.753  21.431  1.00 39.26           O  
ANISOU 6080  O   CYS C 148     3085   4156   7677    -87   -835     24       O  
ATOM   6081  CB  CYS C 148     -47.633   0.095  23.429  1.00 40.42           C  
ANISOU 6081  CB  CYS C 148     3253   4364   7738    -10   -828    -18       C  
ATOM   6082  SG  CYS C 148     -48.206  -0.590  25.014  1.00 41.07           S  
ANISOU 6082  SG  CYS C 148     3358   4437   7809     20   -815    -27       S  
ATOM   6083  N   ALA C 149     -47.610   0.955  20.423  1.00 39.07           N  
ANISOU 6083  N   ALA C 149     3076   4181   7588    -67   -846     25       N  
ATOM   6084  CA  ALA C 149     -47.126   1.649  19.207  1.00 39.48           C  
ANISOU 6084  CA  ALA C 149     3124   4238   7636    -97   -848     39       C  
ATOM   6085  C   ALA C 149     -48.239   2.532  18.634  1.00 39.32           C  
ANISOU 6085  C   ALA C 149     3114   4171   7653   -112   -855     71       C  
ATOM   6086  O   ALA C 149     -48.004   3.730  18.381  1.00 39.50           O  
ANISOU 6086  O   ALA C 149     3138   4176   7692   -137   -847     79       O  
ATOM   6087  CB  ALA C 149     -46.654   0.645  18.181  1.00 39.74           C  
ANISOU 6087  CB  ALA C 149     3164   4302   7632    -90   -858     42       C  
ATOM   6088  N   LEU C 150     -49.416   1.947  18.435  1.00 39.46           N  
ANISOU 6088  N   LEU C 150     3139   4169   7682    -96   -869     86       N  
ATOM   6089  CA  LEU C 150     -50.586   2.652  17.863  1.00 39.45           C  
ANISOU 6089  CA  LEU C 150     3143   4133   7711    -97   -884    110       C  
ATOM   6090  C   LEU C 150     -50.957   3.805  18.789  1.00 40.34           C  
ANISOU 6090  C   LEU C 150     3249   4214   7864   -100   -876    103       C  
ATOM   6091  O   LEU C 150     -51.172   4.910  18.267  1.00 41.47           O  
ANISOU 6091  O   LEU C 150     3403   4327   8025   -107   -882    122       O  
ATOM   6092  CB  LEU C 150     -51.739   1.671  17.673  1.00 38.83           C  
ANISOU 6092  CB  LEU C 150     3063   4054   7637    -81   -896    109       C  
ATOM   6093  CG  LEU C 150     -51.565   0.706  16.506  1.00 38.38           C  
ANISOU 6093  CG  LEU C 150     3012   4022   7547    -80   -907    117       C  
ATOM   6094  CD1 LEU C 150     -52.683  -0.308  16.472  1.00 38.50           C  
ANISOU 6094  CD1 LEU C 150     3023   4035   7568    -71   -911    105       C  
ATOM   6095  CD2 LEU C 150     -51.476   1.442  15.180  1.00 38.30           C  
ANISOU 6095  CD2 LEU C 150     3010   4014   7526    -87   -922    146       C  
ATOM   6096  N   ILE C 151     -50.971   3.582  20.106  1.00 40.96           N  
ANISOU 6096  N   ILE C 151     3313   4296   7951    -93   -863     75       N  
ATOM   6097  CA  ILE C 151     -51.307   4.667  21.076  1.00 42.16           C  
ANISOU 6097  CA  ILE C 151     3454   4423   8142    -95   -855     60       C  
ATOM   6098  C   ILE C 151     -50.314   5.815  20.867  1.00 43.10           C  
ANISOU 6098  C   ILE C 151     3576   4533   8264   -120   -843     60       C  
ATOM   6099  O   ILE C 151     -50.784   6.932  20.567  1.00 44.26           O  
ANISOU 6099  O   ILE C 151     3735   4638   8443   -125   -846     75       O  
ATOM   6100  CB  ILE C 151     -51.344   4.158  22.530  1.00 42.40           C  
ANISOU 6100  CB  ILE C 151     3470   4469   8170    -85   -840     28       C  
ATOM   6101  CG1 ILE C 151     -52.508   3.190  22.753  1.00 42.90           C  
ANISOU 6101  CG1 ILE C 151     3535   4528   8235    -72   -844     27       C  
ATOM   6102  CG2 ILE C 151     -51.409   5.313  23.509  1.00 42.54           C  
ANISOU 6102  CG2 ILE C 151     3469   4469   8221    -90   -830      6       C  
ATOM   6103  CD1 ILE C 151     -52.425   2.418  24.048  1.00 42.96           C  
ANISOU 6103  CD1 ILE C 151     3545   4553   8225    -62   -825      5       C  
ATOM   6104  N   LEU C 152     -49.008   5.540  20.973  1.00 43.76           N  
ANISOU 6104  N   LEU C 152     3653   4655   8317   -133   -827     42       N  
ATOM   6105  CA  LEU C 152     -47.913   6.529  20.748  1.00 44.48           C  
ANISOU 6105  CA  LEU C 152     3744   4749   8408   -169   -807     31       C  
ATOM   6106  C   LEU C 152     -48.147   7.239  19.413  1.00 45.73           C  
ANISOU 6106  C   LEU C 152     3934   4868   8570   -188   -811     73       C  
ATOM   6107  O   LEU C 152     -48.082   8.485  19.378  1.00 45.72           O  
ANISOU 6107  O   LEU C 152     3948   4825   8595   -212   -796     77       O  
ATOM   6108  CB  LEU C 152     -46.555   5.821  20.747  1.00 44.29           C  
ANISOU 6108  CB  LEU C 152     3703   4787   8338   -175   -796      2       C  
ATOM   6109  CG  LEU C 152     -46.053   5.331  22.107  1.00 43.92           C  
ANISOU 6109  CG  LEU C 152     3628   4782   8277   -152   -791    -43       C  
ATOM   6110  CD1 LEU C 152     -44.877   4.383  21.945  1.00 43.37           C  
ANISOU 6110  CD1 LEU C 152     3546   4777   8156   -139   -792    -68       C  
ATOM   6111  CD2 LEU C 152     -45.676   6.494  23.010  1.00 44.10           C  
ANISOU 6111  CD2 LEU C 152     3628   4800   8326   -174   -769    -80       C  
ATOM   6112  N   ALA C 153     -48.433   6.470  18.362  1.00 47.16           N  
ANISOU 6112  N   ALA C 153     4129   5061   8725   -176   -830    102       N  
ATOM   6113  CA  ALA C 153     -48.700   6.987  17.001  1.00 49.08           C  
ANISOU 6113  CA  ALA C 153     4407   5277   8961   -186   -839    146       C  
ATOM   6114  C   ALA C 153     -49.878   7.964  17.033  1.00 49.65           C  
ANISOU 6114  C   ALA C 153     4499   5288   9074   -166   -853    168       C  
ATOM   6115  O   ALA C 153     -49.680   9.134  16.681  1.00 50.31           O  
ANISOU 6115  O   ALA C 153     4617   5329   9170   -186   -841    187       O  
ATOM   6116  CB  ALA C 153     -48.970   5.840  16.058  1.00 49.73           C  
ANISOU 6116  CB  ALA C 153     4491   5392   9011   -168   -861    163       C  
ATOM   6117  N   TYR C 154     -51.046   7.499  17.480  1.00 50.46           N  
ANISOU 6117  N   TYR C 154     4585   5388   9197   -130   -877    162       N  
ATOM   6118  CA  TYR C 154     -52.329   8.250  17.436  1.00 51.88           C  
ANISOU 6118  CA  TYR C 154     4776   5523   9412    -99   -899    175       C  
ATOM   6119  C   TYR C 154     -52.255   9.525  18.283  1.00 53.59           C  
ANISOU 6119  C   TYR C 154     4998   5693   9669   -108   -883    161       C  
ATOM   6120  O   TYR C 154     -53.048  10.433  18.004  1.00 55.60           O  
ANISOU 6120  O   TYR C 154     5276   5899   9948    -83   -900    179       O  
ATOM   6121  CB  TYR C 154     -53.498   7.369  17.880  1.00 51.55           C  
ANISOU 6121  CB  TYR C 154     4702   5502   9381    -68   -920    154       C  
ATOM   6122  CG  TYR C 154     -54.125   6.577  16.761  1.00 52.31           C  
ANISOU 6122  CG  TYR C 154     4799   5621   9452    -48   -946    172       C  
ATOM   6123  CD1 TYR C 154     -54.767   7.218  15.711  1.00 52.91           C  
ANISOU 6123  CD1 TYR C 154     4899   5678   9525    -22   -973    202       C  
ATOM   6124  CD2 TYR C 154     -54.076   5.191  16.741  1.00 52.13           C  
ANISOU 6124  CD2 TYR C 154     4758   5642   9406    -53   -943    156       C  
ATOM   6125  CE1 TYR C 154     -55.346   6.509  14.671  1.00 53.02           C  
ANISOU 6125  CE1 TYR C 154     4909   5722   9512     -2   -999    211       C  
ATOM   6126  CE2 TYR C 154     -54.668   4.465  15.719  1.00 52.38           C  
ANISOU 6126  CE2 TYR C 154     4787   5698   9417    -38   -965    164       C  
ATOM   6127  CZ  TYR C 154     -55.293   5.128  14.674  1.00 53.03           C  
ANISOU 6127  CZ  TYR C 154     4884   5768   9495    -14   -994    189       C  
ATOM   6128  OH  TYR C 154     -55.882   4.436  13.661  1.00 54.04           O  
ANISOU 6128  OH  TYR C 154     5003   5928   9599      2  -1017    191       O  
ATOM   6129  N   CYS C 155     -51.355   9.593  19.271  1.00 54.45           N  
ANISOU 6129  N   CYS C 155     5087   5817   9784   -136   -853    127       N  
ATOM   6130  CA  CYS C 155     -51.206  10.747  20.199  1.00 55.64           C  
ANISOU 6130  CA  CYS C 155     5234   5930   9974   -150   -833    102       C  
ATOM   6131  C   CYS C 155     -50.010  11.629  19.806  1.00 57.84           C  
ANISOU 6131  C   CYS C 155     5542   6188  10247   -198   -799    106       C  
ATOM   6132  O   CYS C 155     -49.694  12.578  20.563  1.00 57.68           O  
ANISOU 6132  O   CYS C 155     5518   6138  10258   -220   -775     77       O  
ATOM   6133  CB  CYS C 155     -51.037  10.263  21.633  1.00 54.96           C  
ANISOU 6133  CB  CYS C 155     5102   5882   9896   -149   -821     52       C  
ATOM   6134  SG  CYS C 155     -52.312   9.078  22.138  1.00 53.95           S  
ANISOU 6134  SG  CYS C 155     4946   5783   9768   -109   -846     43       S  
ATOM   6135  N   ASN C 156     -49.363  11.317  18.680  1.00 60.46           N  
ANISOU 6135  N   ASN C 156     5897   6536  10537   -219   -794    135       N  
ATOM   6136  CA  ASN C 156     -48.188  12.044  18.130  1.00 62.74           C  
ANISOU 6136  CA  ASN C 156     6215   6812  10811   -276   -756    138       C  
ATOM   6137  C   ASN C 156     -47.071  12.141  19.177  1.00 60.36           C  
ANISOU 6137  C   ASN C 156     5870   6548  10513   -315   -720     76       C  
ATOM   6138  O   ASN C 156     -46.266  13.088  19.090  1.00 60.72           O  
ANISOU 6138  O   ASN C 156     5934   6570  10566   -368   -680     61       O  
ATOM   6139  CB  ASN C 156     -48.569  13.429  17.608  1.00 66.70           C  
ANISOU 6139  CB  ASN C 156     6779   7226  11337   -284   -747    174       C  
ATOM   6140  CG  ASN C 156     -47.824  13.762  16.331  1.00 70.62           C  
ANISOU 6140  CG  ASN C 156     7328   7708  11794   -327   -723    212       C  
ATOM   6141  OD1 ASN C 156     -46.612  13.563  16.235  1.00 71.26           O  
ANISOU 6141  OD1 ASN C 156     7393   7832  11848   -381   -688    185       O  
ATOM   6142  ND2 ASN C 156     -48.551  14.229  15.326  1.00 74.82           N  
ANISOU 6142  ND2 ASN C 156     7923   8187  12318   -300   -743    271       N  
ATOM   6143  N   LYS C 157     -46.996  11.176  20.096  1.00 57.50           N  
ANISOU 6143  N   LYS C 157     5456   6246  10142   -291   -732     38       N  
ATOM   6144  CA  LYS C 157     -45.854  11.023  21.033  1.00 56.28           C  
ANISOU 6144  CA  LYS C 157     5255   6149   9976   -314   -706    -24       C  
ATOM   6145  C   LYS C 157     -44.784  10.135  20.381  1.00 54.68           C  
ANISOU 6145  C   LYS C 157     5039   6016   9720   -330   -700    -34       C  
ATOM   6146  O   LYS C 157     -45.109   9.435  19.398  1.00 54.99           O  
ANISOU 6146  O   LYS C 157     5100   6059   9734   -313   -722      7       O  
ATOM   6147  CB  LYS C 157     -46.340  10.435  22.358  1.00 55.78           C  
ANISOU 6147  CB  LYS C 157     5153   6116   9924   -272   -722    -55       C  
ATOM   6148  CG  LYS C 157     -47.474  11.202  23.016  1.00 56.40           C  
ANISOU 6148  CG  LYS C 157     5237   6136  10054   -253   -731    -52       C  
ATOM   6149  CD  LYS C 157     -47.295  11.307  24.529  1.00 56.94           C  
ANISOU 6149  CD  LYS C 157     5261   6235  10137   -246   -720   -110       C  
ATOM   6150  CE  LYS C 157     -46.609  12.586  24.974  1.00 57.53           C  
ANISOU 6150  CE  LYS C 157     5326   6290  10241   -291   -684   -153       C  
ATOM   6151  NZ  LYS C 157     -47.530  13.751  24.853  1.00 58.81           N  
ANISOU 6151  NZ  LYS C 157     5521   6365  10458   -292   -685   -132       N  
ATOM   6152  N   THR C 158     -43.550  10.188  20.888  1.00 52.91           N  
ANISOU 6152  N   THR C 158     4777   5848   9478   -359   -673    -94       N  
ATOM   6153  CA  THR C 158     -42.437   9.275  20.506  1.00 51.62           C  
ANISOU 6153  CA  THR C 158     4586   5766   9261   -364   -671   -123       C  
ATOM   6154  C   THR C 158     -41.916   8.599  21.777  1.00 51.19           C  
ANISOU 6154  C   THR C 158     4479   5782   9190   -328   -679   -184       C  
ATOM   6155  O   THR C 158     -42.232   9.069  22.898  1.00 51.01           O  
ANISOU 6155  O   THR C 158     4439   5746   9196   -317   -676   -209       O  
ATOM   6156  CB  THR C 158     -41.316  10.002  19.750  1.00 50.95           C  
ANISOU 6156  CB  THR C 158     4502   5694   9160   -436   -629   -146       C  
ATOM   6157  OG1 THR C 158     -40.720  10.917  20.665  1.00 50.36           O  
ANISOU 6157  OG1 THR C 158     4398   5626   9110   -473   -594   -208       O  
ATOM   6158  CG2 THR C 158     -41.796  10.738  18.518  1.00 51.08           C  
ANISOU 6158  CG2 THR C 158     4583   5636   9186   -471   -617    -81       C  
ATOM   6159  N   VAL C 159     -41.170   7.514  21.608  1.00 50.85           N  
ANISOU 6159  N   VAL C 159     4412   5810   9097   -303   -692   -207       N  
ATOM   6160  CA  VAL C 159     -40.625   6.729  22.751  1.00 51.33           C  
ANISOU 6160  CA  VAL C 159     4431   5942   9128   -253   -706   -262       C  
ATOM   6161  C   VAL C 159     -39.690   7.648  23.543  1.00 51.28           C  
ANISOU 6161  C   VAL C 159     4378   5977   9129   -288   -675   -338       C  
ATOM   6162  O   VAL C 159     -39.038   8.493  22.912  1.00 51.01           O  
ANISOU 6162  O   VAL C 159     4337   5941   9101   -355   -640   -359       O  
ATOM   6163  CB  VAL C 159     -39.912   5.457  22.256  1.00 51.62           C  
ANISOU 6163  CB  VAL C 159     4457   6045   9109   -218   -726   -274       C  
ATOM   6164  CG1 VAL C 159     -39.333   4.664  23.417  1.00 51.75           C  
ANISOU 6164  CG1 VAL C 159     4441   6132   9089   -156   -744   -327       C  
ATOM   6165  CG2 VAL C 159     -40.835   4.598  21.403  1.00 51.04           C  
ANISOU 6165  CG2 VAL C 159     4429   5929   9032   -193   -752   -205       C  
ATOM   6166  N   GLY C 160     -39.665   7.519  24.872  1.00 51.42           N  
ANISOU 6166  N   GLY C 160     4364   6027   9143   -248   -683   -378       N  
ATOM   6167  CA  GLY C 160     -38.792   8.324  25.748  1.00 51.85           C  
ANISOU 6167  CA  GLY C 160     4364   6132   9201   -275   -657   -462       C  
ATOM   6168  C   GLY C 160     -39.441   9.640  26.145  1.00 52.20           C  
ANISOU 6168  C   GLY C 160     4419   6104   9308   -319   -630   -457       C  
ATOM   6169  O   GLY C 160     -39.223  10.090  27.289  1.00 53.27           O  
ANISOU 6169  O   GLY C 160     4515   6270   9453   -314   -621   -515       O  
ATOM   6170  N   GLU C 161     -40.197  10.250  25.228  1.00 52.47           N  
ANISOU 6170  N   GLU C 161     4506   6048   9381   -357   -621   -393       N  
ATOM   6171  CA  GLU C 161     -41.041  11.449  25.484  1.00 52.45           C  
ANISOU 6171  CA  GLU C 161     4529   5959   9441   -386   -604   -374       C  
ATOM   6172  C   GLU C 161     -41.830  11.212  26.776  1.00 50.99           C  
ANISOU 6172  C   GLU C 161     4327   5776   9270   -331   -627   -381       C  
ATOM   6173  O   GLU C 161     -42.409  10.125  26.923  1.00 48.94           O  
ANISOU 6173  O   GLU C 161     4078   5528   8986   -274   -661   -346       O  
ATOM   6174  CB  GLU C 161     -41.964  11.705  24.285  1.00 53.23           C  
ANISOU 6174  CB  GLU C 161     4694   5968   9563   -398   -610   -288       C  
ATOM   6175  CG  GLU C 161     -42.561  13.103  24.228  1.00 54.27           C  
ANISOU 6175  CG  GLU C 161     4861   6005   9753   -436   -587   -271       C  
ATOM   6176  CD  GLU C 161     -43.349  13.412  22.956  1.00 55.02           C  
ANISOU 6176  CD  GLU C 161     5026   6017   9861   -442   -595   -190       C  
ATOM   6177  OE1 GLU C 161     -44.225  14.320  22.998  1.00 54.64           O  
ANISOU 6177  OE1 GLU C 161     5015   5886   9859   -441   -595   -162       O  
ATOM   6178  OE2 GLU C 161     -43.101  12.741  21.916  1.00 54.85           O  
ANISOU 6178  OE2 GLU C 161     5023   6016   9799   -443   -604   -155       O  
ATOM   6179  N   LEU C 162     -41.797  12.184  27.691  1.00 51.18           N  
ANISOU 6179  N   LEU C 162     4324   5791   9330   -352   -605   -431       N  
ATOM   6180  CA  LEU C 162     -42.624  12.228  28.927  1.00 49.91           C  
ANISOU 6180  CA  LEU C 162     4148   5623   9190   -312   -620   -441       C  
ATOM   6181  C   LEU C 162     -44.085  12.298  28.516  1.00 48.70           C  
ANISOU 6181  C   LEU C 162     4045   5383   9074   -293   -640   -367       C  
ATOM   6182  O   LEU C 162     -44.365  12.795  27.409  1.00 48.38           O  
ANISOU 6182  O   LEU C 162     4049   5276   9056   -323   -634   -321       O  
ATOM   6183  CB  LEU C 162     -42.255  13.455  29.756  1.00 50.75           C  
ANISOU 6183  CB  LEU C 162     4219   5729   9335   -352   -586   -512       C  
ATOM   6184  CG  LEU C 162     -40.867  13.392  30.391  1.00 51.23           C  
ANISOU 6184  CG  LEU C 162     4213   5893   9357   -364   -568   -605       C  
ATOM   6185  CD1 LEU C 162     -40.241  14.780  30.485  1.00 52.02           C  
ANISOU 6185  CD1 LEU C 162     4290   5974   9499   -441   -518   -671       C  
ATOM   6186  CD2 LEU C 162     -40.940  12.716  31.753  1.00 50.85           C  
ANISOU 6186  CD2 LEU C 162     4125   5919   9276   -298   -593   -641       C  
ATOM   6187  N   GLY C 163     -44.972  11.816  29.383  1.00 48.31           N  
ANISOU 6187  N   GLY C 163     3990   5339   9027   -246   -662   -359       N  
ATOM   6188  CA  GLY C 163     -46.365  11.527  29.010  1.00 48.27           C  
ANISOU 6188  CA  GLY C 163     4022   5274   9043   -219   -687   -297       C  
ATOM   6189  C   GLY C 163     -47.321  11.791  30.150  1.00 48.14           C  
ANISOU 6189  C   GLY C 163     3989   5246   9055   -196   -692   -315       C  
ATOM   6190  O   GLY C 163     -46.877  11.802  31.310  1.00 47.87           O  
ANISOU 6190  O   GLY C 163     3915   5265   9007   -187   -682   -369       O  
ATOM   6191  N   ASP C 164     -48.589  11.997  29.799  1.00 48.13           N  
ANISOU 6191  N   ASP C 164     4013   5183   9090   -184   -708   -276       N  
ATOM   6192  CA  ASP C 164     -49.710  12.250  30.731  1.00 48.40           C  
ANISOU 6192  CA  ASP C 164     4030   5202   9155   -162   -714   -292       C  
ATOM   6193  C   ASP C 164     -50.787  11.190  30.471  1.00 47.70           C  
ANISOU 6193  C   ASP C 164     3961   5113   9051   -131   -738   -249       C  
ATOM   6194  O   ASP C 164     -51.238  11.064  29.316  1.00 47.99           O  
ANISOU 6194  O   ASP C 164     4029   5111   9094   -129   -753   -203       O  
ATOM   6195  CB  ASP C 164     -50.213  13.686  30.562  1.00 49.35           C  
ANISOU 6195  CB  ASP C 164     4159   5250   9341   -180   -709   -300       C  
ATOM   6196  CG  ASP C 164     -51.292  14.072  31.556  1.00 50.52           C  
ANISOU 6196  CG  ASP C 164     4282   5388   9524   -158   -715   -329       C  
ATOM   6197  OD1 ASP C 164     -52.495  13.978  31.165  1.00 51.03           O  
ANISOU 6197  OD1 ASP C 164     4362   5418   9609   -134   -738   -300       O  
ATOM   6198  OD2 ASP C 164     -50.939  14.431  32.699  1.00 51.28           O  
ANISOU 6198  OD2 ASP C 164     4339   5518   9625   -165   -698   -386       O  
ATOM   6199  N   VAL C 165     -51.188  10.453  31.502  1.00 47.39           N  
ANISOU 6199  N   VAL C 165     3903   5114   8987   -109   -737   -267       N  
ATOM   6200  CA  VAL C 165     -52.281   9.438  31.420  1.00 47.81           C  
ANISOU 6200  CA  VAL C 165     3973   5166   9027    -89   -750   -237       C  
ATOM   6201  C   VAL C 165     -53.551  10.127  30.907  1.00 48.16           C  
ANISOU 6201  C   VAL C 165     4017   5155   9124    -87   -765   -227       C  
ATOM   6202  O   VAL C 165     -54.078   9.671  29.873  1.00 47.49           O  
ANISOU 6202  O   VAL C 165     3957   5050   9037    -81   -781   -188       O  
ATOM   6203  CB  VAL C 165     -52.500   8.748  32.781  1.00 47.58           C  
ANISOU 6203  CB  VAL C 165     3928   5184   8965    -73   -737   -264       C  
ATOM   6204  CG1 VAL C 165     -53.831   8.016  32.862  1.00 47.50           C  
ANISOU 6204  CG1 VAL C 165     3928   5165   8955    -67   -739   -249       C  
ATOM   6205  CG2 VAL C 165     -51.340   7.815  33.106  1.00 47.15           C  
ANISOU 6205  CG2 VAL C 165     3885   5183   8846    -58   -731   -264       C  
ATOM   6206  N   ARG C 166     -53.990  11.202  31.574  1.00 49.30           N  
ANISOU 6206  N   ARG C 166     4136   5281   9314    -88   -761   -264       N  
ATOM   6207  CA  ARG C 166     -55.261  11.919  31.285  1.00 50.65           C  
ANISOU 6207  CA  ARG C 166     4303   5405   9536    -75   -779   -267       C  
ATOM   6208  C   ARG C 166     -55.268  12.434  29.844  1.00 49.82           C  
ANISOU 6208  C   ARG C 166     4234   5244   9448    -72   -798   -224       C  
ATOM   6209  O   ARG C 166     -56.294  12.287  29.170  1.00 48.87           O  
ANISOU 6209  O   ARG C 166     4122   5106   9340    -50   -822   -204       O  
ATOM   6210  CB  ARG C 166     -55.459  13.085  32.251  1.00 52.66           C  
ANISOU 6210  CB  ARG C 166     4526   5647   9835    -76   -770   -319       C  
ATOM   6211  CG  ARG C 166     -56.794  13.805  32.099  1.00 54.45           C  
ANISOU 6211  CG  ARG C 166     4742   5833  10112    -52   -791   -333       C  
ATOM   6212  CD  ARG C 166     -56.899  15.083  32.918  1.00 56.48           C  
ANISOU 6212  CD  ARG C 166     4973   6065  10419    -51   -784   -385       C  
ATOM   6213  NE  ARG C 166     -55.711  15.930  32.873  1.00 58.50           N  
ANISOU 6213  NE  ARG C 166     5244   6293  10688    -76   -765   -392       N  
ATOM   6214  CZ  ARG C 166     -55.259  16.559  31.786  1.00 60.72           C  
ANISOU 6214  CZ  ARG C 166     5571   6513  10985    -83   -768   -356       C  
ATOM   6215  NH1 ARG C 166     -55.896  16.456  30.628  1.00 61.05           N  
ANISOU 6215  NH1 ARG C 166     5650   6517  11029    -60   -796   -307       N  
ATOM   6216  NH2 ARG C 166     -54.152  17.283  31.861  1.00 60.99           N  
ANISOU 6216  NH2 ARG C 166     5615   6529  11030   -118   -742   -372       N  
ATOM   6217  N   GLU C 167     -54.167  13.030  29.402  1.00 50.06           N  
ANISOU 6217  N   GLU C 167     4285   5254   9479    -94   -786   -213       N  
ATOM   6218  CA  GLU C 167     -54.023  13.553  28.023  1.00 50.98           C  
ANISOU 6218  CA  GLU C 167     4448   5317   9606    -96   -798   -168       C  
ATOM   6219  C   GLU C 167     -54.201  12.387  27.042  1.00 50.14           C  
ANISOU 6219  C   GLU C 167     4360   5232   9458    -86   -815   -123       C  
ATOM   6220  O   GLU C 167     -55.003  12.534  26.097  1.00 50.14           O  
ANISOU 6220  O   GLU C 167     4381   5199   9467    -63   -841    -92       O  
ATOM   6221  CB  GLU C 167     -52.670  14.244  27.869  1.00 51.90           C  
ANISOU 6221  CB  GLU C 167     4579   5418   9720   -135   -770   -174       C  
ATOM   6222  CG  GLU C 167     -52.508  14.954  26.538  1.00 53.41           C  
ANISOU 6222  CG  GLU C 167     4826   5545   9920   -145   -773   -128       C  
ATOM   6223  CD  GLU C 167     -51.205  15.716  26.365  1.00 54.52           C  
ANISOU 6223  CD  GLU C 167     4985   5667  10062   -196   -736   -139       C  
ATOM   6224  OE1 GLU C 167     -50.541  16.004  27.393  1.00 54.89           O  
ANISOU 6224  OE1 GLU C 167     4995   5742  10118   -221   -709   -195       O  
ATOM   6225  OE2 GLU C 167     -50.855  16.010  25.196  1.00 55.58           O  
ANISOU 6225  OE2 GLU C 167     5169   5762  10185   -213   -731    -96       O  
ATOM   6226  N   THR C 168     -53.499  11.276  27.289  1.00 49.13           N  
ANISOU 6226  N   THR C 168     4223   5160   9284    -97   -804   -123       N  
ATOM   6227  CA  THR C 168     -53.513  10.033  26.470  1.00 48.23           C  
ANISOU 6227  CA  THR C 168     4125   5071   9127    -91   -815    -87       C  
ATOM   6228  C   THR C 168     -54.935   9.481  26.381  1.00 47.22           C  
ANISOU 6228  C   THR C 168     3989   4943   9008    -67   -835    -84       C  
ATOM   6229  O   THR C 168     -55.378   9.216  25.258  1.00 47.08           O  
ANISOU 6229  O   THR C 168     3989   4913   8984    -56   -856    -53       O  
ATOM   6230  CB  THR C 168     -52.591   8.947  27.043  1.00 47.92           C  
ANISOU 6230  CB  THR C 168     4077   5088   9039    -97   -799    -99       C  
ATOM   6231  OG1 THR C 168     -51.314   9.514  27.312  1.00 47.45           O  
ANISOU 6231  OG1 THR C 168     4012   5044   8974   -119   -780   -120       O  
ATOM   6232  CG2 THR C 168     -52.418   7.770  26.109  1.00 47.52           C  
ANISOU 6232  CG2 THR C 168     4049   5057   8948    -93   -809    -65       C  
ATOM   6233  N   MET C 169     -55.605   9.297  27.520  1.00 46.81           N  
ANISOU 6233  N   MET C 169     3907   4911   8967    -61   -827   -121       N  
ATOM   6234  CA  MET C 169     -57.004   8.790  27.573  1.00 47.81           C  
ANISOU 6234  CA  MET C 169     4017   5045   9103    -47   -838   -132       C  
ATOM   6235  C   MET C 169     -57.880   9.664  26.666  1.00 48.91           C  
ANISOU 6235  C   MET C 169     4158   5145   9278    -22   -870   -124       C  
ATOM   6236  O   MET C 169     -58.630   9.095  25.848  1.00 49.10           O  
ANISOU 6236  O   MET C 169     4183   5177   9294     -9   -889   -112       O  
ATOM   6237  CB  MET C 169     -57.592   8.799  28.989  1.00 47.44           C  
ANISOU 6237  CB  MET C 169     3935   5020   9067    -49   -821   -180       C  
ATOM   6238  CG  MET C 169     -56.854   7.910  29.991  1.00 47.26           C  
ANISOU 6238  CG  MET C 169     3916   5037   9000    -63   -792   -188       C  
ATOM   6239  SD  MET C 169     -56.421   6.246  29.435  1.00 46.44           S  
ANISOU 6239  SD  MET C 169     3850   4956   8838    -69   -784   -151       S  
ATOM   6240  CE  MET C 169     -57.768   5.300  30.150  1.00 46.95           C  
ANISOU 6240  CE  MET C 169     3904   5038   8894    -80   -764   -175       C  
ATOM   6241  N   SER C 170     -57.764  10.989  26.773  1.00 50.69           N  
ANISOU 6241  N   SER C 170     4387   5330   9541    -13   -875   -132       N  
ATOM   6242  CA  SER C 170     -58.545  11.955  25.960  1.00 52.88           C  
ANISOU 6242  CA  SER C 170     4678   5561   9852     21   -907   -122       C  
ATOM   6243  C   SER C 170     -58.393  11.614  24.476  1.00 54.69           C  
ANISOU 6243  C   SER C 170     4944   5781  10053     30   -927    -70       C  
ATOM   6244  O   SER C 170     -59.398  11.226  23.876  1.00 57.33           O  
ANISOU 6244  O   SER C 170     5268   6130  10383     58   -954    -70       O  
ATOM   6245  CB  SER C 170     -58.155  13.376  26.223  1.00 53.31           C  
ANISOU 6245  CB  SER C 170     4748   5562   9945     24   -903   -129       C  
ATOM   6246  OG  SER C 170     -59.071  14.251  25.590  1.00 53.28           O  
ANISOU 6246  OG  SER C 170     4760   5512   9971     70   -937   -124       O  
ATOM   6247  N   TYR C 171     -57.185  11.721  23.918  1.00 56.39           N  
ANISOU 6247  N   TYR C 171     5196   5981  10245      5   -913    -33       N  
ATOM   6248  CA  TYR C 171     -56.886  11.413  22.491  1.00 58.10           C  
ANISOU 6248  CA  TYR C 171     5452   6193  10430      8   -928     17       C  
ATOM   6249  C   TYR C 171     -57.502  10.060  22.098  1.00 57.23           C  
ANISOU 6249  C   TYR C 171     5320   6133  10290     16   -941     16       C  
ATOM   6250  O   TYR C 171     -58.050   9.966  20.981  1.00 56.86           O  
ANISOU 6250  O   TYR C 171     5287   6084  10231     42   -970     40       O  
ATOM   6251  CB  TYR C 171     -55.377  11.352  22.223  1.00 59.49           C  
ANISOU 6251  CB  TYR C 171     5654   6371  10578    -33   -900     40       C  
ATOM   6252  CG  TYR C 171     -54.649  12.657  22.030  1.00 61.80           C  
ANISOU 6252  CG  TYR C 171     5985   6608  10889    -51   -884     53       C  
ATOM   6253  CD1 TYR C 171     -54.399  13.148  20.758  1.00 63.08           C  
ANISOU 6253  CD1 TYR C 171     6200   6732  11034    -50   -891    101       C  
ATOM   6254  CD2 TYR C 171     -54.118  13.359  23.106  1.00 62.81           C  
ANISOU 6254  CD2 TYR C 171     6098   6723  11045    -75   -856     15       C  
ATOM   6255  CE1 TYR C 171     -53.671  14.314  20.561  1.00 63.91           C  
ANISOU 6255  CE1 TYR C 171     6350   6780  11153    -78   -866    114       C  
ATOM   6256  CE2 TYR C 171     -53.411  14.537  22.929  1.00 63.44           C  
ANISOU 6256  CE2 TYR C 171     6213   6747  11142   -101   -833     21       C  
ATOM   6257  CZ  TYR C 171     -53.184  15.014  21.651  1.00 63.90           C  
ANISOU 6257  CZ  TYR C 171     6332   6761  11186   -105   -835     72       C  
ATOM   6258  OH  TYR C 171     -52.479  16.169  21.477  1.00 65.90           O  
ANISOU 6258  OH  TYR C 171     6629   6953  11454   -140   -805     79       O  
ATOM   6259  N   LEU C 172     -57.397   9.042  22.967  1.00 56.06           N  
ANISOU 6259  N   LEU C 172     5144   6027  10128     -4   -920     -9       N  
ATOM   6260  CA  LEU C 172     -57.865   7.658  22.682  1.00 55.53           C  
ANISOU 6260  CA  LEU C 172     5064   6001  10033     -7   -921    -13       C  
ATOM   6261  C   LEU C 172     -59.394   7.630  22.658  1.00 56.69           C  
ANISOU 6261  C   LEU C 172     5179   6158  10202     17   -942    -44       C  
ATOM   6262  O   LEU C 172     -59.946   6.908  21.812  1.00 57.74           O  
ANISOU 6262  O   LEU C 172     5306   6313  10317     25   -958    -40       O  
ATOM   6263  CB  LEU C 172     -57.325   6.681  23.729  1.00 55.14           C  
ANISOU 6263  CB  LEU C 172     5005   5982   9960    -34   -888    -31       C  
ATOM   6264  CG  LEU C 172     -55.847   6.314  23.592  1.00 55.47           C  
ANISOU 6264  CG  LEU C 172     5072   6034   9968    -52   -872     -8       C  
ATOM   6265  CD1 LEU C 172     -55.375   5.539  24.816  1.00 55.63           C  
ANISOU 6265  CD1 LEU C 172     5087   6083   9967    -63   -845    -30       C  
ATOM   6266  CD2 LEU C 172     -55.583   5.520  22.315  1.00 55.08           C  
ANISOU 6266  CD2 LEU C 172     5044   5997   9886    -53   -884     22       C  
ATOM   6267  N   PHE C 173     -60.049   8.383  23.549  1.00 55.69           N  
ANISOU 6267  N   PHE C 173     5025   6021  10111     29   -943    -81       N  
ATOM   6268  CA  PHE C 173     -61.531   8.452  23.668  1.00 54.32           C  
ANISOU 6268  CA  PHE C 173     4810   5866   9962     55   -963   -126       C  
ATOM   6269  C   PHE C 173     -62.134   9.174  22.453  1.00 56.04           C  
ANISOU 6269  C   PHE C 173     5037   6065  10187    105  -1009   -110       C  
ATOM   6270  O   PHE C 173     -63.335   8.976  22.201  1.00 56.65           O  
ANISOU 6270  O   PHE C 173     5077   6172  10272    130  -1032   -147       O  
ATOM   6271  CB  PHE C 173     -61.946   9.088  24.999  1.00 52.65           C  
ANISOU 6271  CB  PHE C 173     4566   5651   9785     54   -949   -173       C  
ATOM   6272  CG  PHE C 173     -61.677   8.250  26.232  1.00 50.84           C  
ANISOU 6272  CG  PHE C 173     4323   5452   9540     12   -906   -196       C  
ATOM   6273  CD1 PHE C 173     -61.359   6.898  26.148  1.00 49.39           C  
ANISOU 6273  CD1 PHE C 173     4154   5294   9316    -17   -883   -182       C  
ATOM   6274  CD2 PHE C 173     -61.770   8.817  27.498  1.00 49.96           C  
ANISOU 6274  CD2 PHE C 173     4188   5342   9452      6   -889   -234       C  
ATOM   6275  CE1 PHE C 173     -61.124   6.153  27.294  1.00 48.61           C  
ANISOU 6275  CE1 PHE C 173     4054   5216   9197    -48   -844   -198       C  
ATOM   6276  CE2 PHE C 173     -61.536   8.064  28.640  1.00 48.85           C  
ANISOU 6276  CE2 PHE C 173     4040   5231   9289    -26   -850   -252       C  
ATOM   6277  CZ  PHE C 173     -61.221   6.732  28.537  1.00 48.40           C  
ANISOU 6277  CZ  PHE C 173     4006   5194   9189    -52   -827   -232       C  
ATOM   6278  N   GLN C 174     -61.343   9.963  21.717  1.00 57.59           N  
ANISOU 6278  N   GLN C 174     5283   6218  10380    118  -1021    -60       N  
ATOM   6279  CA  GLN C 174     -61.741  10.555  20.408  1.00 59.80           C  
ANISOU 6279  CA  GLN C 174     5591   6477  10652    167  -1064    -29       C  
ATOM   6280  C   GLN C 174     -62.125   9.435  19.442  1.00 59.98           C  
ANISOU 6280  C   GLN C 174     5601   6550  10638    169  -1078    -25       C  
ATOM   6281  O   GLN C 174     -63.122   9.603  18.708  1.00 61.92           O  
ANISOU 6281  O   GLN C 174     5831   6813  10881    219  -1119    -39       O  
ATOM   6282  CB  GLN C 174     -60.605  11.332  19.740  1.00 62.05           C  
ANISOU 6282  CB  GLN C 174     5942   6708  10924    162  -1059     31       C  
ATOM   6283  CG  GLN C 174     -60.016  12.447  20.590  1.00 63.87           C  
ANISOU 6283  CG  GLN C 174     6192   6884  11190    149  -1037     28       C  
ATOM   6284  CD  GLN C 174     -61.075  13.427  21.025  1.00 65.96           C  
ANISOU 6284  CD  GLN C 174     6442   7122  11498    200  -1064     -6       C  
ATOM   6285  OE1 GLN C 174     -62.027  13.702  20.293  1.00 67.15           O  
ANISOU 6285  OE1 GLN C 174     6595   7272  11647    259  -1107     -6       O  
ATOM   6286  NE2 GLN C 174     -60.921  13.951  22.234  1.00 67.48           N  
ANISOU 6286  NE2 GLN C 174     6614   7296  11726    183  -1041    -42       N  
ATOM   6287  N   HIS C 175     -61.338   8.353  19.445  1.00 59.29           N  
ANISOU 6287  N   HIS C 175     5519   6486  10522    121  -1048    -11       N  
ATOM   6288  CA  HIS C 175     -61.449   7.181  18.534  1.00 59.33           C  
ANISOU 6288  CA  HIS C 175     5517   6533  10490    112  -1053     -5       C  
ATOM   6289  C   HIS C 175     -62.300   6.074  19.184  1.00 58.70           C  
ANISOU 6289  C   HIS C 175     5387   6499  10415     89  -1035    -62       C  
ATOM   6290  O   HIS C 175     -62.531   5.052  18.521  1.00 58.76           O  
ANISOU 6290  O   HIS C 175     5385   6542  10398     77  -1035    -70       O  
ATOM   6291  CB  HIS C 175     -60.055   6.672  18.136  1.00 58.91           C  
ANISOU 6291  CB  HIS C 175     5504   6476  10403     76  -1030     39       C  
ATOM   6292  CG  HIS C 175     -59.133   7.730  17.616  1.00 59.91           C  
ANISOU 6292  CG  HIS C 175     5680   6558  10524     82  -1035     89       C  
ATOM   6293  ND1 HIS C 175     -58.169   8.324  18.416  1.00 59.43           N  
ANISOU 6293  ND1 HIS C 175     5636   6465  10477     55  -1006     96       N  
ATOM   6294  CD2 HIS C 175     -59.012   8.302  16.395  1.00 59.75           C  
ANISOU 6294  CD2 HIS C 175     5697   6521  10482    107  -1060    131       C  
ATOM   6295  CE1 HIS C 175     -57.495   9.212  17.713  1.00 59.12           C  
ANISOU 6295  CE1 HIS C 175     5643   6389  10429     56  -1009    138       C  
ATOM   6296  NE2 HIS C 175     -57.988   9.210  16.468  1.00 59.52           N  
ANISOU 6296  NE2 HIS C 175     5712   6445  10456     88  -1041    165       N  
ATOM   6297  N   ALA C 176     -62.727   6.250  20.437  1.00 57.68           N  
ANISOU 6297  N   ALA C 176     5230   6369  10315     77  -1015   -103       N  
ATOM   6298  CA  ALA C 176     -63.695   5.363  21.118  1.00 57.17           C  
ANISOU 6298  CA  ALA C 176     5119   6344  10257     52   -993   -164       C  
ATOM   6299  C   ALA C 176     -65.094   5.742  20.641  1.00 58.80           C  
ANISOU 6299  C   ALA C 176     5278   6582  10481     93  -1030   -212       C  
ATOM   6300  O   ALA C 176     -65.286   6.913  20.264  1.00 60.13           O  
ANISOU 6300  O   ALA C 176     5452   6729  10665    147  -1070   -201       O  
ATOM   6301  CB  ALA C 176     -63.588   5.481  22.616  1.00 56.20           C  
ANISOU 6301  CB  ALA C 176     4986   6213  10153     25   -957   -188       C  
ATOM   6302  N   ASN C 177     -66.017   4.782  20.625  1.00 59.12           N  
ANISOU 6302  N   ASN C 177     5274   6671  10515     71  -1018   -267       N  
ATOM   6303  CA  ASN C 177     -67.440   5.039  20.315  1.00 59.94           C  
ANISOU 6303  CA  ASN C 177     5316   6821  10634    107  -1050   -335       C  
ATOM   6304  C   ASN C 177     -68.128   5.426  21.625  1.00 60.03           C  
ANISOU 6304  C   ASN C 177     5286   6842  10679     95  -1030   -394       C  
ATOM   6305  O   ASN C 177     -68.551   4.515  22.349  1.00 60.10           O  
ANISOU 6305  O   ASN C 177     5267   6879  10686     38   -984   -440       O  
ATOM   6306  CB  ASN C 177     -68.099   3.840  19.631  1.00 60.89           C  
ANISOU 6306  CB  ASN C 177     5402   6997  10733     81  -1042   -377       C  
ATOM   6307  CG  ASN C 177     -69.517   4.143  19.202  1.00 62.71           C  
ANISOU 6307  CG  ASN C 177     5563   7288  10976    124  -1080   -454       C  
ATOM   6308  OD1 ASN C 177     -69.992   5.265  19.372  1.00 64.77           O  
ANISOU 6308  OD1 ASN C 177     5804   7545  11258    182  -1117   -471       O  
ATOM   6309  ND2 ASN C 177     -70.197   3.153  18.648  1.00 63.61           N  
ANISOU 6309  ND2 ASN C 177     5635   7457  11074     99  -1071   -506       N  
ATOM   6310  N   LEU C 178     -68.193   6.728  21.920  1.00 60.23           N  
ANISOU 6310  N   LEU C 178     5311   6839  10731    145  -1060   -391       N  
ATOM   6311  CA  LEU C 178     -68.785   7.275  23.169  1.00 60.62           C  
ANISOU 6311  CA  LEU C 178     5320   6895  10815    142  -1046   -447       C  
ATOM   6312  C   LEU C 178     -69.967   8.200  22.835  1.00 62.42           C  
ANISOU 6312  C   LEU C 178     5497   7151  11068    215  -1100   -505       C  
ATOM   6313  O   LEU C 178     -70.404   8.933  23.739  1.00 60.43           O  
ANISOU 6313  O   LEU C 178     5215   6897  10847    230  -1100   -548       O  
ATOM   6314  CB  LEU C 178     -67.690   8.014  23.943  1.00 59.10           C  
ANISOU 6314  CB  LEU C 178     5175   6643  10636    135  -1030   -398       C  
ATOM   6315  CG  LEU C 178     -66.534   7.146  24.436  1.00 57.75           C  
ANISOU 6315  CG  LEU C 178     5047   6455  10439     72   -979   -352       C  
ATOM   6316  CD1 LEU C 178     -65.449   8.001  25.079  1.00 57.70           C  
ANISOU 6316  CD1 LEU C 178     5079   6397  10444     74   -971   -312       C  
ATOM   6317  CD2 LEU C 178     -67.019   6.085  25.415  1.00 57.10           C  
ANISOU 6317  CD2 LEU C 178     4936   6411  10347     12   -928   -401       C  
ATOM   6318  N   ASP C 179     -70.495   8.113  21.606  1.00 65.50           N  
ANISOU 6318  N   ASP C 179     5875   7572  11440    262  -1144   -511       N  
ATOM   6319  CA  ASP C 179     -71.574   8.991  21.070  1.00 68.25           C  
ANISOU 6319  CA  ASP C 179     6181   7949  11801    352  -1208   -561       C  
ATOM   6320  C   ASP C 179     -72.798   8.993  21.998  1.00 68.25           C  
ANISOU 6320  C   ASP C 179     6092   8010  11828    345  -1199   -671       C  
ATOM   6321  O   ASP C 179     -73.336  10.092  22.258  1.00 68.49           O  
ANISOU 6321  O   ASP C 179     6101   8034  11886    412  -1238   -705       O  
ATOM   6322  CB  ASP C 179     -71.989   8.566  19.658  1.00 70.34           C  
ANISOU 6322  CB  ASP C 179     6435   8259  12031    391  -1249   -563       C  
ATOM   6323  CG  ASP C 179     -70.841   8.555  18.662  1.00 72.71           C  
ANISOU 6323  CG  ASP C 179     6818   8508  12300    398  -1259   -460       C  
ATOM   6324  OD1 ASP C 179     -69.720   9.011  19.030  1.00 72.82           O  
ANISOU 6324  OD1 ASP C 179     6899   8449  12321    378  -1238   -388       O  
ATOM   6325  OD2 ASP C 179     -71.072   8.082  17.531  1.00 74.69           O  
ANISOU 6325  OD2 ASP C 179     7063   8798  12517    420  -1286   -458       O  
ATOM   6326  N   SER C 180     -73.225   7.817  22.472  1.00 67.43           N  
ANISOU 6326  N   SER C 180     5941   7960  11715    265  -1146   -727       N  
ATOM   6327  CA  SER C 180     -74.470   7.629  23.267  1.00 67.87           C  
ANISOU 6327  CA  SER C 180     5907   8090  11791    243  -1127   -843       C  
ATOM   6328  C   SER C 180     -74.239   7.961  24.749  1.00 66.80           C  
ANISOU 6328  C   SER C 180     5772   7926  11680    201  -1083   -853       C  
ATOM   6329  O   SER C 180     -75.204   7.839  25.526  1.00 67.95           O  
ANISOU 6329  O   SER C 180     5844   8131  11840    174  -1060   -949       O  
ATOM   6330  CB  SER C 180     -75.017   6.236  23.095  1.00 68.07           C  
ANISOU 6330  CB  SER C 180     5889   8179  11793    168  -1083   -900       C  
ATOM   6331  OG  SER C 180     -74.123   5.276  23.632  1.00 68.03           O  
ANISOU 6331  OG  SER C 180     5941   8134  11773     77  -1014   -846       O  
ATOM   6332  N   CYS C 181     -73.019   8.350  25.132  1.00 65.12           N  
ANISOU 6332  N   CYS C 181     5634   7637  11471    192  -1070   -766       N  
ATOM   6333  CA  CYS C 181     -72.689   8.856  26.493  1.00 64.25           C  
ANISOU 6333  CA  CYS C 181     5528   7499  11384    167  -1037   -771       C  
ATOM   6334  C   CYS C 181     -73.209  10.291  26.638  1.00 63.35           C  
ANISOU 6334  C   CYS C 181     5385   7374  11308    251  -1090   -807       C  
ATOM   6335  O   CYS C 181     -73.148  11.063  25.641  1.00 62.88           O  
ANISOU 6335  O   CYS C 181     5354   7283  11253    332  -1151   -773       O  
ATOM   6336  CB  CYS C 181     -71.191   8.822  26.781  1.00 63.45           C  
ANISOU 6336  CB  CYS C 181     5509   7326  11270    136  -1009   -674       C  
ATOM   6337  SG  CYS C 181     -70.520   7.145  26.875  1.00 62.03           S  
ANISOU 6337  SG  CYS C 181     5369   7153  11046     42   -943   -635       S  
ATOM   6338  N   LYS C 182     -73.664  10.637  27.843  1.00 62.05           N  
ANISOU 6338  N   LYS C 182     5174   7231  11168    233  -1067   -872       N  
ATOM   6339  CA  LYS C 182     -74.358  11.913  28.118  1.00 62.99           C  
ANISOU 6339  CA  LYS C 182     5252   7352  11327    310  -1114   -930       C  
ATOM   6340  C   LYS C 182     -74.165  12.281  29.591  1.00 62.11           C  
ANISOU 6340  C   LYS C 182     5125   7233  11238    271  -1072   -959       C  
ATOM   6341  O   LYS C 182     -74.283  11.388  30.446  1.00 61.71           O  
ANISOU 6341  O   LYS C 182     5049   7226  11170    187  -1011   -990       O  
ATOM   6342  CB  LYS C 182     -75.838  11.757  27.760  1.00 64.91           C  
ANISOU 6342  CB  LYS C 182     5403   7685  11572    345  -1144  -1038       C  
ATOM   6343  CG  LYS C 182     -76.605  13.049  27.507  1.00 66.30           C  
ANISOU 6343  CG  LYS C 182     5545   7864  11781    459  -1218  -1091       C  
ATOM   6344  CD  LYS C 182     -78.082  12.814  27.189  1.00 67.88           C  
ANISOU 6344  CD  LYS C 182     5642   8171  11979    493  -1247  -1211       C  
ATOM   6345  CE  LYS C 182     -78.968  12.611  28.408  1.00 67.84           C  
ANISOU 6345  CE  LYS C 182     5542   8243  11990    439  -1205  -1329       C  
ATOM   6346  NZ  LYS C 182     -80.301  12.081  28.038  1.00 67.91           N  
ANISOU 6346  NZ  LYS C 182     5448   8366  11987    445  -1217  -1449       N  
ATOM   6347  N   ARG C 183     -73.890  13.559  29.853  1.00 62.20           N  
ANISOU 6347  N   ARG C 183     5157   7190  11286    330  -1104   -949       N  
ATOM   6348  CA  ARG C 183     -73.727  14.141  31.211  1.00 62.77           C  
ANISOU 6348  CA  ARG C 183     5210   7254  11385    307  -1075   -983       C  
ATOM   6349  C   ARG C 183     -74.545  15.438  31.286  1.00 63.04           C  
ANISOU 6349  C   ARG C 183     5201   7284  11465    398  -1131  -1052       C  
ATOM   6350  O   ARG C 183     -74.660  16.122  30.252  1.00 63.37           O  
ANISOU 6350  O   ARG C 183     5274   7285  11517    484  -1192  -1026       O  
ATOM   6351  CB  ARG C 183     -72.238  14.369  31.487  1.00 62.85           C  
ANISOU 6351  CB  ARG C 183     5301   7186  11392    278  -1049   -891       C  
ATOM   6352  CG  ARG C 183     -71.916  15.014  32.827  1.00 63.88           C  
ANISOU 6352  CG  ARG C 183     5417   7305  11548    258  -1021   -921       C  
ATOM   6353  CD  ARG C 183     -70.415  15.100  33.054  1.00 65.25           C  
ANISOU 6353  CD  ARG C 183     5664   7416  11711    224   -993   -837       C  
ATOM   6354  NE  ARG C 183     -69.932  14.076  33.978  1.00 66.26           N  
ANISOU 6354  NE  ARG C 183     5791   7583  11801    142   -930   -830       N  
ATOM   6355  CZ  ARG C 183     -68.674  13.659  34.099  1.00 65.59           C  
ANISOU 6355  CZ  ARG C 183     5764   7470  11687    103   -900   -761       C  
ATOM   6356  NH1 ARG C 183     -67.718  14.152  33.333  1.00 66.43           N  
ANISOU 6356  NH1 ARG C 183     5930   7510  11800    127   -922   -692       N  
ATOM   6357  NH2 ARG C 183     -68.383  12.730  34.990  1.00 66.29           N  
ANISOU 6357  NH2 ARG C 183     5851   7599  11737     40   -848   -762       N  
ATOM   6358  N   VAL C 184     -75.104  15.752  32.458  1.00 63.05           N  
ANISOU 6358  N   VAL C 184     5138   7327  11490    383  -1111  -1137       N  
ATOM   6359  CA  VAL C 184     -75.866  17.011  32.716  1.00 64.61           C  
ANISOU 6359  CA  VAL C 184     5291   7522  11735    469  -1160  -1213       C  
ATOM   6360  C   VAL C 184     -75.383  17.606  34.046  1.00 65.67           C  
ANISOU 6360  C   VAL C 184     5420   7633  11895    437  -1124  -1232       C  
ATOM   6361  O   VAL C 184     -75.546  16.940  35.090  1.00 64.71           O  
ANISOU 6361  O   VAL C 184     5252   7575  11757    358  -1067  -1278       O  
ATOM   6362  CB  VAL C 184     -77.391  16.768  32.681  1.00 64.47           C  
ANISOU 6362  CB  VAL C 184     5168   7609  11718    496  -1182  -1335       C  
ATOM   6363  CG1 VAL C 184     -78.194  18.020  33.013  1.00 64.23           C  
ANISOU 6363  CG1 VAL C 184     5086   7584  11735    588  -1234  -1423       C  
ATOM   6364  CG2 VAL C 184     -77.815  16.217  31.329  1.00 64.52           C  
ANISOU 6364  CG2 VAL C 184     5176   7640  11695    532  -1220  -1319       C  
ATOM   6365  N   LEU C 185     -74.795  18.809  33.979  1.00 68.36           N  
ANISOU 6365  N   LEU C 185     5813   7884  12274    494  -1154  -1197       N  
ATOM   6366  CA  LEU C 185     -74.172  19.559  35.109  1.00 70.80           C  
ANISOU 6366  CA  LEU C 185     6130   8156  12614    473  -1126  -1208       C  
ATOM   6367  C   LEU C 185     -74.955  20.849  35.367  1.00 74.23           C  
ANISOU 6367  C   LEU C 185     6525   8575  13104    562  -1175  -1290       C  
ATOM   6368  O   LEU C 185     -75.426  21.463  34.389  1.00 73.39           O  
ANISOU 6368  O   LEU C 185     6439   8431  13013    656  -1238  -1286       O  
ATOM   6369  CB  LEU C 185     -72.721  19.899  34.754  1.00 71.28           C  
ANISOU 6369  CB  LEU C 185     6291   8116  12674    459  -1115  -1099       C  
ATOM   6370  CG  LEU C 185     -71.717  18.759  34.925  1.00 71.05           C  
ANISOU 6370  CG  LEU C 185     6297   8102  12597    366  -1058  -1030       C  
ATOM   6371  CD1 LEU C 185     -70.452  19.025  34.120  1.00 70.66           C  
ANISOU 6371  CD1 LEU C 185     6344   7961  12541    368  -1062   -924       C  
ATOM   6372  CD2 LEU C 185     -71.394  18.524  36.399  1.00 70.94           C  
ANISOU 6372  CD2 LEU C 185     6246   8131  12576    296  -1001  -1069       C  
ATOM   6373  N   ASN C 186     -75.053  21.255  36.636  1.00 77.24           N  
ANISOU 6373  N   ASN C 186     6855   8982  13510    536  -1147  -1360       N  
ATOM   6374  CA  ASN C 186     -75.823  22.448  37.075  1.00 79.01           C  
ANISOU 6374  CA  ASN C 186     7030   9200  13788    615  -1187  -1454       C  
ATOM   6375  C   ASN C 186     -74.965  23.273  38.039  1.00 80.17           C  
ANISOU 6375  C   ASN C 186     7202   9289  13970    591  -1157  -1452       C  
ATOM   6376  O   ASN C 186     -74.474  22.684  39.020  1.00 81.83           O  
ANISOU 6376  O   ASN C 186     7390   9546  14156    501  -1096  -1456       O  
ATOM   6377  CB  ASN C 186     -77.139  22.036  37.738  1.00 80.26           C  
ANISOU 6377  CB  ASN C 186     7070   9483  13942    605  -1182  -1580       C  
ATOM   6378  CG  ASN C 186     -78.238  23.059  37.555  1.00 81.57           C  
ANISOU 6378  CG  ASN C 186     7184   9655  14152    720  -1250  -1675       C  
ATOM   6379  OD1 ASN C 186     -78.014  24.121  36.971  1.00 82.81           O  
ANISOU 6379  OD1 ASN C 186     7403   9714  14346    810  -1302  -1643       O  
ATOM   6380  ND2 ASN C 186     -79.428  22.734  38.032  1.00 82.68           N  
ANISOU 6380  ND2 ASN C 186     7215   9911  14288    717  -1250  -1794       N  
ATOM   6381  N   VAL C 187     -74.807  24.576  37.769  1.00 81.39           N  
ANISOU 6381  N   VAL C 187     7401   9346  14176    670  -1199  -1449       N  
ATOM   6382  CA  VAL C 187     -74.006  25.540  38.587  1.00 82.04           C  
ANISOU 6382  CA  VAL C 187     7510   9360  14301    656  -1175  -1456       C  
ATOM   6383  C   VAL C 187     -74.954  26.587  39.192  1.00 82.46           C  
ANISOU 6383  C   VAL C 187     7500   9420  14410    730  -1210  -1571       C  
ATOM   6384  O   VAL C 187     -75.495  27.403  38.423  1.00 80.75           O  
ANISOU 6384  O   VAL C 187     7313   9143  14225    836  -1272  -1580       O  
ATOM   6385  CB  VAL C 187     -72.890  26.193  37.745  1.00 82.05           C  
ANISOU 6385  CB  VAL C 187     7631   9226  14317    674  -1182  -1351       C  
ATOM   6386  CG1 VAL C 187     -71.978  27.068  38.591  1.00 81.81           C  
ANISOU 6386  CG1 VAL C 187     7624   9131  14327    642  -1147  -1361       C  
ATOM   6387  CG2 VAL C 187     -72.079  25.149  36.982  1.00 81.13           C  
ANISOU 6387  CG2 VAL C 187     7571   9108  14143    614  -1158  -1243       C  
ATOM   6388  N   VAL C 188     -75.122  26.564  40.520  1.00 84.32           N  
ANISOU 6388  N   VAL C 188     7655   9728  14653    680  -1171  -1656       N  
ATOM   6389  CA  VAL C 188     -76.102  27.395  41.284  1.00 88.35           C  
ANISOU 6389  CA  VAL C 188     8082  10274  15211    737  -1197  -1786       C  
ATOM   6390  C   VAL C 188     -75.359  28.505  42.046  1.00 89.99           C  
ANISOU 6390  C   VAL C 188     8316  10403  15471    735  -1179  -1804       C  
ATOM   6391  O   VAL C 188     -74.652  28.170  43.014  1.00 89.88           O  
ANISOU 6391  O   VAL C 188     8282  10427  15440    646  -1119  -1806       O  
ATOM   6392  CB  VAL C 188     -76.943  26.524  42.242  1.00 88.73           C  
ANISOU 6392  CB  VAL C 188     8013  10474  15226    678  -1162  -1881       C  
ATOM   6393  CG1 VAL C 188     -77.903  27.359  43.076  1.00 89.15           C  
ANISOU 6393  CG1 VAL C 188     7973  10572  15325    730  -1185  -2021       C  
ATOM   6394  CG2 VAL C 188     -77.701  25.428  41.503  1.00 88.03           C  
ANISOU 6394  CG2 VAL C 188     7896  10463  15089    671  -1173  -1874       C  
ATOM   6395  N   CYS C 189     -75.511  29.765  41.611  1.00 93.15           N  
ANISOU 6395  N   CYS C 189     8763  10699  15931    833  -1229  -1818       N  
ATOM   6396  CA  CYS C 189     -75.073  30.997  42.328  1.00 95.95           C  
ANISOU 6396  CA  CYS C 189     9132  10975  16349    848  -1220  -1863       C  
ATOM   6397  C   CYS C 189     -76.318  31.808  42.711  1.00 97.89           C  
ANISOU 6397  C   CYS C 189     9303  11246  16643    944  -1270  -1992       C  
ATOM   6398  O   CYS C 189     -77.244  31.899  41.872  1.00101.20           O  
ANISOU 6398  O   CYS C 189     9721  11666  17063   1040  -1334  -2005       O  
ATOM   6399  CB  CYS C 189     -74.121  31.847  41.484  1.00 97.47           C  
ANISOU 6399  CB  CYS C 189     9458  11003  16573    877  -1229  -1769       C  
ATOM   6400  SG  CYS C 189     -73.343  33.220  42.382  1.00 99.47           S  
ANISOU 6400  SG  CYS C 189     9738  11155  16900    865  -1198  -1816       S  
ATOM   6401  N   LYS C 190     -76.344  32.375  43.925  1.00 97.07           N  
ANISOU 6401  N   LYS C 190     9136  11170  16577    923  -1245  -2088       N  
ATOM   6402  CA  LYS C 190     -77.461  33.210  44.446  1.00 96.98           C  
ANISOU 6402  CA  LYS C 190     9045  11187  16616   1011  -1289  -2224       C  
ATOM   6403  C   LYS C 190     -77.557  34.517  43.643  1.00 97.46           C  
ANISOU 6403  C   LYS C 190     9197  11093  16739   1136  -1351  -2211       C  
ATOM   6404  O   LYS C 190     -78.668  35.098  43.610  1.00 94.53           O  
ANISOU 6404  O   LYS C 190     8777  10739  16400   1244  -1411  -2306       O  
ATOM   6405  CB  LYS C 190     -77.265  33.480  45.941  1.00 96.27           C  
ANISOU 6405  CB  LYS C 190     8875  11156  16547    946  -1239  -2319       C  
ATOM   6406  CG  LYS C 190     -77.528  32.285  46.844  1.00 95.46           C  
ANISOU 6406  CG  LYS C 190     8668  11220  16381    845  -1187  -2361       C  
ATOM   6407  CD  LYS C 190     -77.743  32.678  48.282  1.00 95.42           C  
ANISOU 6407  CD  LYS C 190     8566  11291  16397    814  -1156  -2484       C  
ATOM   6408  CE  LYS C 190     -78.279  31.544  49.131  1.00 95.44           C  
ANISOU 6408  CE  LYS C 190     8463  11463  16334    729  -1110  -2539       C  
ATOM   6409  NZ  LYS C 190     -78.337  31.929  50.560  1.00 95.93           N  
ANISOU 6409  NZ  LYS C 190     8439  11598  16409    690  -1074  -2650       N  
ATOM   6410  N   THR C 191     -76.447  34.948  43.021  1.00 97.86           N  
ANISOU 6410  N   THR C 191     9377  11002  16803   1122  -1335  -2100       N  
ATOM   6411  CA  THR C 191     -76.370  36.123  42.108  1.00100.50           C  
ANISOU 6411  CA  THR C 191     9831  11168  17187   1230  -1384  -2058       C  
ATOM   6412  C   THR C 191     -76.885  35.727  40.715  1.00100.80           C  
ANISOU 6412  C   THR C 191     9923  11190  17184   1311  -1443  -1984       C  
ATOM   6413  O   THR C 191     -77.980  36.195  40.338  1.00103.17           O  
ANISOU 6413  O   THR C 191    10204  11493  17501   1439  -1516  -2045       O  
ATOM   6414  CB  THR C 191     -74.944  36.696  42.010  1.00101.50           C  
ANISOU 6414  CB  THR C 191    10073  11153  17338   1167  -1333  -1972       C  
ATOM   6415  OG1 THR C 191     -74.298  36.611  43.281  1.00102.45           O  
ANISOU 6415  OG1 THR C 191    10128  11330  17469   1060  -1265  -2025       O  
ATOM   6416  CG2 THR C 191     -74.927  38.137  41.539  1.00102.19           C  
ANISOU 6416  CG2 THR C 191    10269  11066  17492   1267  -1367  -1970       C  
ATOM   6417  N   CYS C 192     -76.128  34.888  39.987  1.00 98.93           N  
ANISOU 6417  N   CYS C 192     9748  10946  16893   1243  -1415  -1862       N  
ATOM   6418  CA  CYS C 192     -76.295  34.620  38.528  1.00 98.54           C  
ANISOU 6418  CA  CYS C 192     9783  10852  16805   1310  -1464  -1766       C  
ATOM   6419  C   CYS C 192     -77.193  33.403  38.271  1.00 95.79           C  
ANISOU 6419  C   CYS C 192     9338  10658  16397   1309  -1487  -1792       C  
ATOM   6420  O   CYS C 192     -77.167  32.899  37.127  1.00 94.75           O  
ANISOU 6420  O   CYS C 192     9264  10513  16221   1333  -1512  -1706       O  
ATOM   6421  CB  CYS C 192     -74.946  34.406  37.856  1.00 99.50           C  
ANISOU 6421  CB  CYS C 192    10024  10880  16902   1233  -1418  -1625       C  
ATOM   6422  SG  CYS C 192     -73.746  35.684  38.310  1.00102.03           S  
ANISOU 6422  SG  CYS C 192    10441  11036  17288   1194  -1368  -1606       S  
ATOM   6423  N   GLY C 193     -77.970  32.963  39.270  1.00 93.65           N  
ANISOU 6423  N   GLY C 193     8929  10527  16125   1281  -1476  -1910       N  
ATOM   6424  CA  GLY C 193     -79.040  31.949  39.128  1.00 91.37           C  
ANISOU 6424  CA  GLY C 193     8536  10390  15790   1288  -1499  -1967       C  
ATOM   6425  C   GLY C 193     -78.494  30.562  38.834  1.00 88.15           C  
ANISOU 6425  C   GLY C 193     8132  10045  15315   1176  -1449  -1882       C  
ATOM   6426  O   GLY C 193     -77.470  30.215  39.419  1.00 86.29           O  
ANISOU 6426  O   GLY C 193     7917   9798  15069   1065  -1381  -1832       O  
ATOM   6427  N   GLN C 194     -79.142  29.812  37.933  1.00 87.04           N  
ANISOU 6427  N   GLN C 194     7973   9966  15129   1208  -1484  -1867       N  
ATOM   6428  CA  GLN C 194     -78.751  28.437  37.514  1.00 85.34           C  
ANISOU 6428  CA  GLN C 194     7763   9812  14849   1113  -1443  -1791       C  
ATOM   6429  C   GLN C 194     -78.031  28.466  36.154  1.00 83.54           C  
ANISOU 6429  C   GLN C 194     7664   9477  14601   1144  -1467  -1654       C  
ATOM   6430  O   GLN C 194     -78.261  29.420  35.375  1.00 84.01           O  
ANISOU 6430  O   GLN C 194     7789   9445  14683   1263  -1530  -1637       O  
ATOM   6431  CB  GLN C 194     -79.993  27.557  37.395  1.00 86.59           C  
ANISOU 6431  CB  GLN C 194     7809  10116  14972   1122  -1463  -1877       C  
ATOM   6432  CG  GLN C 194     -80.514  26.999  38.712  1.00 86.56           C  
ANISOU 6432  CG  GLN C 194     7681  10243  14963   1036  -1410  -1988       C  
ATOM   6433  CD  GLN C 194     -81.424  25.806  38.486  1.00 86.65           C  
ANISOU 6433  CD  GLN C 194     7605  10393  14925    999  -1403  -2041       C  
ATOM   6434  OE1 GLN C 194     -81.661  25.356  37.362  1.00 84.82           O  
ANISOU 6434  OE1 GLN C 194     7398  10166  14663   1037  -1437  -1999       O  
ATOM   6435  NE2 GLN C 194     -81.931  25.244  39.570  1.00 87.01           N  
ANISOU 6435  NE2 GLN C 194     7547  10554  14957    918  -1351  -2137       N  
ATOM   6436  N   GLN C 195     -77.203  27.445  35.892  1.00 80.89           N  
ANISOU 6436  N   GLN C 195     7362   9154  14217   1044  -1417  -1562       N  
ATOM   6437  CA  GLN C 195     -76.471  27.215  34.610  1.00 78.97           C  
ANISOU 6437  CA  GLN C 195     7230   8832  13942   1051  -1428  -1432       C  
ATOM   6438  C   GLN C 195     -76.249  25.708  34.402  1.00 75.91           C  
ANISOU 6438  C   GLN C 195     6816   8532  13492    954  -1386  -1389       C  
ATOM   6439  O   GLN C 195     -75.317  25.153  35.025  1.00 73.06           O  
ANISOU 6439  O   GLN C 195     6465   8177  13117    845  -1319  -1349       O  
ATOM   6440  CB  GLN C 195     -75.126  27.946  34.609  1.00 78.69           C  
ANISOU 6440  CB  GLN C 195     7306   8661  13931   1020  -1396  -1342       C  
ATOM   6441  CG  GLN C 195     -74.373  27.816  33.292  1.00 78.83           C  
ANISOU 6441  CG  GLN C 195     7440   8595  13915   1028  -1405  -1213       C  
ATOM   6442  CD  GLN C 195     -72.919  28.215  33.395  1.00 77.84           C  
ANISOU 6442  CD  GLN C 195     7408   8364  13802    958  -1352  -1130       C  
ATOM   6443  OE1 GLN C 195     -72.481  28.832  34.364  1.00 78.05           O  
ANISOU 6443  OE1 GLN C 195     7426   8358  13871    923  -1318  -1168       O  
ATOM   6444  NE2 GLN C 195     -72.150  27.856  32.382  1.00 76.43           N  
ANISOU 6444  NE2 GLN C 195     7315   8136  13585    935  -1344  -1020       N  
ATOM   6445  N   GLN C 196     -77.064  25.074  33.553  1.00 75.01           N  
ANISOU 6445  N   GLN C 196     6670   8484  13343    996  -1425  -1401       N  
ATOM   6446  CA  GLN C 196     -76.958  23.621  33.253  1.00 74.08           C  
ANISOU 6446  CA  GLN C 196     6529   8447  13168    909  -1388  -1367       C  
ATOM   6447  C   GLN C 196     -76.405  23.442  31.837  1.00 73.16           C  
ANISOU 6447  C   GLN C 196     6510   8266  13019    939  -1415  -1253       C  
ATOM   6448  O   GLN C 196     -76.746  24.261  30.956  1.00 72.14           O  
ANISOU 6448  O   GLN C 196     6429   8080  12901   1052  -1481  -1238       O  
ATOM   6449  CB  GLN C 196     -78.297  22.909  33.470  1.00 74.10           C  
ANISOU 6449  CB  GLN C 196     6409   8590  13154    911  -1398  -1482       C  
ATOM   6450  CG  GLN C 196     -79.042  22.509  32.207  1.00 74.09           C  
ANISOU 6450  CG  GLN C 196     6398   8631  13120    980  -1454  -1484       C  
ATOM   6451  CD  GLN C 196     -80.359  21.861  32.560  1.00 73.59           C  
ANISOU 6451  CD  GLN C 196     6202   8713  13045    971  -1455  -1616       C  
ATOM   6452  OE1 GLN C 196     -80.912  22.071  33.638  1.00 72.81           O  
ANISOU 6452  OE1 GLN C 196     6021   8671  12971    952  -1436  -1718       O  
ATOM   6453  NE2 GLN C 196     -80.875  21.049  31.652  1.00 73.87           N  
ANISOU 6453  NE2 GLN C 196     6211   8814  13040    979  -1475  -1622       N  
ATOM   6454  N   THR C 197     -75.575  22.408  31.652  1.00 72.03           N  
ANISOU 6454  N   THR C 197     6398   8133  12836    842  -1364  -1176       N  
ATOM   6455  CA  THR C 197     -74.878  22.065  30.381  1.00 71.57           C  
ANISOU 6455  CA  THR C 197     6430   8022  12740    846  -1375  -1063       C  
ATOM   6456  C   THR C 197     -75.177  20.603  30.015  1.00 69.36           C  
ANISOU 6456  C   THR C 197     6103   7841  12409    787  -1355  -1065       C  
ATOM   6457  O   THR C 197     -75.249  19.770  30.937  1.00 66.04           O  
ANISOU 6457  O   THR C 197     5620   7492  11978    697  -1300  -1108       O  
ATOM   6458  CB  THR C 197     -73.365  22.315  30.498  1.00 71.75           C  
ANISOU 6458  CB  THR C 197     6547   7947  12766    784  -1329   -964       C  
ATOM   6459  OG1 THR C 197     -72.875  21.484  31.548  1.00 71.94           O  
ANISOU 6459  OG1 THR C 197     6528   8025  12778    673  -1261   -978       O  
ATOM   6460  CG2 THR C 197     -72.988  23.752  30.792  1.00 71.98           C  
ANISOU 6460  CG2 THR C 197     6632   7869  12847    832  -1342   -960       C  
ATOM   6461  N   THR C 198     -75.332  20.312  28.718  1.00 69.70           N  
ANISOU 6461  N   THR C 198     6181   7883  12419    834  -1395  -1019       N  
ATOM   6462  CA  THR C 198     -75.591  18.953  28.168  1.00 71.32           C  
ANISOU 6462  CA  THR C 198     6349   8172  12575    784  -1380  -1016       C  
ATOM   6463  C   THR C 198     -74.444  18.555  27.226  1.00 73.36           C  
ANISOU 6463  C   THR C 198     6706   8368  12799    753  -1367   -892       C  
ATOM   6464  O   THR C 198     -74.487  18.940  26.031  1.00 74.49           O  
ANISOU 6464  O   THR C 198     6902   8474  12924    832  -1420   -844       O  
ATOM   6465  CB  THR C 198     -76.974  18.892  27.513  1.00 71.21           C  
ANISOU 6465  CB  THR C 198     6264   8241  12551    869  -1442  -1101       C  
ATOM   6466  OG1 THR C 198     -77.900  18.797  28.595  1.00 72.09           O  
ANISOU 6466  OG1 THR C 198     6267   8437  12685    848  -1424  -1223       O  
ATOM   6467  CG2 THR C 198     -77.158  17.725  26.565  1.00 70.75           C  
ANISOU 6467  CG2 THR C 198     6192   8246  12442    842  -1441  -1084       C  
ATOM   6468  N   LEU C 199     -73.478  17.801  27.766  1.00 74.05           N  
ANISOU 6468  N   LEU C 199     6812   8449  12871    646  -1300   -846       N  
ATOM   6469  CA  LEU C 199     -72.274  17.280  27.066  1.00 74.38           C  
ANISOU 6469  CA  LEU C 199     6937   8444  12879    598  -1276   -737       C  
ATOM   6470  C   LEU C 199     -72.596  15.894  26.495  1.00 73.99           C  
ANISOU 6470  C   LEU C 199     6854   8473  12785    557  -1264   -741       C  
ATOM   6471  O   LEU C 199     -73.339  15.136  27.156  1.00 72.94           O  
ANISOU 6471  O   LEU C 199     6641   8423  12649    512  -1237   -818       O  
ATOM   6472  CB  LEU C 199     -71.109  17.203  28.064  1.00 74.06           C  
ANISOU 6472  CB  LEU C 199     6925   8367  12847    513  -1213   -702       C  
ATOM   6473  CG  LEU C 199     -70.784  18.485  28.836  1.00 74.75           C  
ANISOU 6473  CG  LEU C 199     7031   8386  12982    536  -1212   -715       C  
ATOM   6474  CD1 LEU C 199     -69.888  18.196  30.034  1.00 73.54           C  
ANISOU 6474  CD1 LEU C 199     6873   8236  12832    447  -1147   -713       C  
ATOM   6475  CD2 LEU C 199     -70.132  19.521  27.931  1.00 75.14           C  
ANISOU 6475  CD2 LEU C 199     7177   8330  13042    591  -1242   -640       C  
ATOM   6476  N   LYS C 200     -72.080  15.607  25.298  1.00 75.30           N  
ANISOU 6476  N   LYS C 200     7080   8612  12917    569  -1281   -664       N  
ATOM   6477  CA  LYS C 200     -72.100  14.274  24.640  1.00 77.23           C  
ANISOU 6477  CA  LYS C 200     7311   8915  13118    523  -1265   -650       C  
ATOM   6478  C   LYS C 200     -70.649  13.907  24.303  1.00 76.44           C  
ANISOU 6478  C   LYS C 200     7293   8756  12992    467  -1231   -546       C  
ATOM   6479  O   LYS C 200     -69.789  14.808  24.364  1.00 76.27           O  
ANISOU 6479  O   LYS C 200     7336   8655  12987    480  -1231   -491       O  
ATOM   6480  CB  LYS C 200     -72.975  14.313  23.382  1.00 79.26           C  
ANISOU 6480  CB  LYS C 200     7551   9208  13353    606  -1329   -668       C  
ATOM   6481  CG  LYS C 200     -73.837  13.085  23.134  1.00 81.45           C  
ANISOU 6481  CG  LYS C 200     7751   9589  13605    572  -1320   -735       C  
ATOM   6482  CD  LYS C 200     -74.317  12.972  21.695  1.00 82.51           C  
ANISOU 6482  CD  LYS C 200     7887   9756  13705    644  -1378   -729       C  
ATOM   6483  CE  LYS C 200     -75.619  12.204  21.565  1.00 82.46           C  
ANISOU 6483  CE  LYS C 200     7776   9866  13688    644  -1387   -840       C  
ATOM   6484  NZ  LYS C 200     -75.878  11.779  20.168  1.00 82.33           N  
ANISOU 6484  NZ  LYS C 200     7761   9890  13629    688  -1429   -828       N  
ATOM   6485  N   GLY C 201     -70.400  12.645  23.948  1.00 76.09           N  
ANISOU 6485  N   GLY C 201     7246   8752  12912    409  -1202   -528       N  
ATOM   6486  CA  GLY C 201     -69.087  12.159  23.474  1.00 75.61           C  
ANISOU 6486  CA  GLY C 201     7255   8650  12821    362  -1175   -437       C  
ATOM   6487  C   GLY C 201     -68.041  12.135  24.581  1.00 74.95           C  
ANISOU 6487  C   GLY C 201     7196   8533  12747    297  -1121   -414       C  
ATOM   6488  O   GLY C 201     -68.415  11.858  25.739  1.00 77.74           O  
ANISOU 6488  O   GLY C 201     7501   8920  13114    260  -1089   -470       O  
ATOM   6489  N   VAL C 202     -66.782  12.436  24.243  1.00 73.03           N  
ANISOU 6489  N   VAL C 202     7022   8230  12493    284  -1112   -337       N  
ATOM   6490  CA  VAL C 202     -65.601  12.374  25.161  1.00 72.13           C  
ANISOU 6490  CA  VAL C 202     6933   8090  12380    224  -1063   -312       C  
ATOM   6491  C   VAL C 202     -65.837  13.263  26.393  1.00 71.07           C  
ANISOU 6491  C   VAL C 202     6771   7942  12289    230  -1053   -362       C  
ATOM   6492  O   VAL C 202     -65.510  12.811  27.509  1.00 71.60           O  
ANISOU 6492  O   VAL C 202     6817   8033  12353    179  -1010   -384       O  
ATOM   6493  CB  VAL C 202     -64.296  12.763  24.432  1.00 71.57           C  
ANISOU 6493  CB  VAL C 202     6937   7961  12294    218  -1060   -233       C  
ATOM   6494  CG1 VAL C 202     -63.089  12.707  25.359  1.00 70.67           C  
ANISOU 6494  CG1 VAL C 202     6839   7833  12179    162  -1013   -220       C  
ATOM   6495  CG2 VAL C 202     -64.059  11.900  23.201  1.00 71.91           C  
ANISOU 6495  CG2 VAL C 202     7006   8023  12294    213  -1070   -187       C  
ATOM   6496  N   GLU C 203     -66.378  14.471  26.202  1.00 69.87           N  
ANISOU 6496  N   GLU C 203     6622   7752  12172    294  -1092   -379       N  
ATOM   6497  CA  GLU C 203     -66.531  15.518  27.253  1.00 69.56           C  
ANISOU 6497  CA  GLU C 203     6563   7686  12179    308  -1088   -425       C  
ATOM   6498  C   GLU C 203     -67.487  15.038  28.361  1.00 68.74           C  
ANISOU 6498  C   GLU C 203     6376   7654  12085    289  -1071   -510       C  
ATOM   6499  O   GLU C 203     -67.503  15.677  29.439  1.00 68.03           O  
ANISOU 6499  O   GLU C 203     6262   7557  12027    283  -1055   -553       O  
ATOM   6500  CB  GLU C 203     -67.025  16.831  26.631  1.00 70.13           C  
ANISOU 6500  CB  GLU C 203     6664   7699  12283    392  -1139   -424       C  
ATOM   6501  CG  GLU C 203     -65.932  17.865  26.367  1.00 70.91           C  
ANISOU 6501  CG  GLU C 203     6843   7702  12396    393  -1131   -365       C  
ATOM   6502  CD  GLU C 203     -66.208  19.244  26.957  1.00 72.52           C  
ANISOU 6502  CD  GLU C 203     7053   7847  12654    437  -1144   -403       C  
ATOM   6503  OE1 GLU C 203     -66.553  19.331  28.166  1.00 72.58           O  
ANISOU 6503  OE1 GLU C 203     6999   7887  12689    420  -1127   -472       O  
ATOM   6504  OE2 GLU C 203     -66.069  20.239  26.214  1.00 74.12           O  
ANISOU 6504  OE2 GLU C 203     7325   7968  12868    487  -1170   -363       O  
ATOM   6505  N   ALA C 204     -68.247  13.965  28.107  1.00 68.10           N  
ANISOU 6505  N   ALA C 204     6256   7641  11978    274  -1070   -537       N  
ATOM   6506  CA  ALA C 204     -69.317  13.427  28.983  1.00 67.00           C  
ANISOU 6506  CA  ALA C 204     6037   7576  11842    251  -1051   -623       C  
ATOM   6507  C   ALA C 204     -68.717  12.595  30.125  1.00 65.41           C  
ANISOU 6507  C   ALA C 204     5832   7400  11619    170   -987   -624       C  
ATOM   6508  O   ALA C 204     -69.303  12.614  31.229  1.00 63.27           O  
ANISOU 6508  O   ALA C 204     5509   7170  11361    149   -963   -691       O  
ATOM   6509  CB  ALA C 204     -70.291  12.607  28.164  1.00 66.81           C  
ANISOU 6509  CB  ALA C 204     5977   7611  11797    261  -1070   -653       C  
ATOM   6510  N   VAL C 205     -67.597  11.903  29.863  1.00 64.27           N  
ANISOU 6510  N   VAL C 205     5743   7235  11441    130   -962   -553       N  
ATOM   6511  CA  VAL C 205     -66.977  10.884  30.767  1.00 62.42           C  
ANISOU 6511  CA  VAL C 205     5518   7027  11172     61   -904   -543       C  
ATOM   6512  C   VAL C 205     -65.813  11.490  31.564  1.00 61.77           C  
ANISOU 6512  C   VAL C 205     5463   6910  11094     50   -885   -518       C  
ATOM   6513  O   VAL C 205     -65.561  10.998  32.672  1.00 62.57           O  
ANISOU 6513  O   VAL C 205     5556   7042  11175      9   -844   -535       O  
ATOM   6514  CB  VAL C 205     -66.531   9.634  29.982  1.00 60.91           C  
ANISOU 6514  CB  VAL C 205     5364   6841  10935     31   -891   -491       C  
ATOM   6515  CG1 VAL C 205     -67.719   8.881  29.410  1.00 60.16           C  
ANISOU 6515  CG1 VAL C 205     5231   6792  10831     27   -897   -531       C  
ATOM   6516  CG2 VAL C 205     -65.520   9.949  28.889  1.00 59.79           C  
ANISOU 6516  CG2 VAL C 205     5280   6649  10786     55   -917   -417       C  
ATOM   6517  N   MET C 206     -65.130  12.511  31.037  1.00 62.43           N  
ANISOU 6517  N   MET C 206     5582   6935  11201     83   -912   -482       N  
ATOM   6518  CA  MET C 206     -63.921  13.126  31.659  1.00 61.21           C  
ANISOU 6518  CA  MET C 206     5454   6749  11052     68   -892   -463       C  
ATOM   6519  C   MET C 206     -64.310  14.416  32.386  1.00 61.81           C  
ANISOU 6519  C   MET C 206     5500   6805  11181     94   -902   -517       C  
ATOM   6520  O   MET C 206     -65.097  15.202  31.832  1.00 62.60           O  
ANISOU 6520  O   MET C 206     5592   6877  11316    145   -941   -535       O  
ATOM   6521  CB  MET C 206     -62.860  13.450  30.606  1.00 60.41           C  
ANISOU 6521  CB  MET C 206     5413   6593  10945     75   -905   -395       C  
ATOM   6522  CG  MET C 206     -62.217  12.225  30.017  1.00 60.37           C  
ANISOU 6522  CG  MET C 206     5439   6608  10888     46   -891   -344       C  
ATOM   6523  SD  MET C 206     -60.994  12.615  28.747  1.00 62.31           S  
ANISOU 6523  SD  MET C 206     5751   6800  11124     50   -904   -271       S  
ATOM   6524  CE  MET C 206     -59.686  13.352  29.725  1.00 61.56           C  
ANISOU 6524  CE  MET C 206     5663   6688  11039     21   -871   -281       C  
ATOM   6525  N   TYR C 207     -63.767  14.620  33.587  1.00 61.73           N  
ANISOU 6525  N   TYR C 207     5472   6809  11171     67   -870   -545       N  
ATOM   6526  CA  TYR C 207     -63.824  15.902  34.334  1.00 62.18           C  
ANISOU 6526  CA  TYR C 207     5506   6841  11277     85   -874   -594       C  
ATOM   6527  C   TYR C 207     -62.452  16.175  34.949  1.00 61.74           C  
ANISOU 6527  C   TYR C 207     5470   6774  11212     52   -843   -582       C  
ATOM   6528  O   TYR C 207     -61.823  15.226  35.465  1.00 63.44           O  
ANISOU 6528  O   TYR C 207     5687   7037  11380     16   -812   -568       O  
ATOM   6529  CB  TYR C 207     -64.921  15.871  35.399  1.00 63.43           C  
ANISOU 6529  CB  TYR C 207     5596   7055  11448     85   -865   -673       C  
ATOM   6530  CG  TYR C 207     -64.996  17.098  36.275  1.00 64.12           C  
ANISOU 6530  CG  TYR C 207     5652   7125  11583    102   -866   -733       C  
ATOM   6531  CD1 TYR C 207     -65.655  18.243  35.857  1.00 65.17           C  
ANISOU 6531  CD1 TYR C 207     5780   7207  11771    157   -905   -761       C  
ATOM   6532  CD2 TYR C 207     -64.414  17.110  37.534  1.00 64.63           C  
ANISOU 6532  CD2 TYR C 207     5694   7225  11637     66   -829   -765       C  
ATOM   6533  CE1 TYR C 207     -65.731  19.369  36.666  1.00 67.16           C  
ANISOU 6533  CE1 TYR C 207     6005   7439  12071    174   -905   -820       C  
ATOM   6534  CE2 TYR C 207     -64.480  18.223  38.355  1.00 65.68           C  
ANISOU 6534  CE2 TYR C 207     5794   7345  11814     79   -828   -826       C  
ATOM   6535  CZ  TYR C 207     -65.143  19.358  37.923  1.00 67.30           C  
ANISOU 6535  CZ  TYR C 207     5995   7495  12080    131   -865   -855       C  
ATOM   6536  OH  TYR C 207     -65.195  20.448  38.751  1.00 69.41           O  
ANISOU 6536  OH  TYR C 207     6231   7746  12394    143   -862   -919       O  
ATOM   6537  N   MET C 208     -62.014  17.436  34.878  1.00 61.01           N  
ANISOU 6537  N   MET C 208     5394   6621  11165     67   -850   -590       N  
ATOM   6538  CA  MET C 208     -60.784  17.958  35.525  1.00 60.15           C  
ANISOU 6538  CA  MET C 208     5292   6501  11059     36   -820   -600       C  
ATOM   6539  C   MET C 208     -61.208  18.961  36.607  1.00 58.84           C  
ANISOU 6539  C   MET C 208     5080   6335  10941     46   -816   -677       C  
ATOM   6540  O   MET C 208     -61.775  19.998  36.231  1.00 58.42           O  
ANISOU 6540  O   MET C 208     5035   6219  10940     84   -841   -693       O  
ATOM   6541  CB  MET C 208     -59.895  18.630  34.473  1.00 61.39           C  
ANISOU 6541  CB  MET C 208     5512   6582  11231     34   -825   -549       C  
ATOM   6542  CG  MET C 208     -58.596  19.211  35.016  1.00 62.67           C  
ANISOU 6542  CG  MET C 208     5678   6734  11399     -4   -791   -567       C  
ATOM   6543  SD  MET C 208     -57.474  17.984  35.754  1.00 64.37           S  
ANISOU 6543  SD  MET C 208     5872   7042  11544    -46   -757   -565       S  
ATOM   6544  CE  MET C 208     -55.917  18.852  35.560  1.00 64.28           C  
ANISOU 6544  CE  MET C 208     5886   6992  11544    -85   -729   -568       C  
ATOM   6545  N   GLY C 209     -60.989  18.649  37.894  1.00 57.85           N  
ANISOU 6545  N   GLY C 209     4909   6276  10794     20   -786   -724       N  
ATOM   6546  CA  GLY C 209     -61.348  19.534  39.024  1.00 57.75           C  
ANISOU 6546  CA  GLY C 209     4844   6275  10821     25   -778   -805       C  
ATOM   6547  C   GLY C 209     -61.259  18.867  40.393  1.00 56.99           C  
ANISOU 6547  C   GLY C 209     4699   6271  10681     -2   -747   -848       C  
ATOM   6548  O   GLY C 209     -60.732  19.511  41.316  1.00 55.53           O  
ANISOU 6548  O   GLY C 209     4485   6101  10510    -14   -728   -899       O  
ATOM   6549  N   THR C 210     -61.801  17.652  40.544  1.00 57.23           N  
ANISOU 6549  N   THR C 210     4721   6361  10661    -11   -740   -831       N  
ATOM   6550  CA  THR C 210     -61.770  16.848  41.801  1.00 57.62           C  
ANISOU 6550  CA  THR C 210     4741   6497  10655    -37   -707   -860       C  
ATOM   6551  C   THR C 210     -61.794  15.358  41.450  1.00 57.04           C  
ANISOU 6551  C   THR C 210     4701   6454  10514    -54   -695   -801       C  
ATOM   6552  O   THR C 210     -62.188  15.037  40.318  1.00 58.55           O  
ANISOU 6552  O   THR C 210     4921   6610  10715    -44   -716   -758       O  
ATOM   6553  CB  THR C 210     -62.949  17.154  42.732  1.00 58.85           C  
ANISOU 6553  CB  THR C 210     4833   6694  10830    -33   -702   -937       C  
ATOM   6554  OG1 THR C 210     -62.736  16.400  43.929  1.00 59.93           O  
ANISOU 6554  OG1 THR C 210     4953   6911  10905    -61   -665   -956       O  
ATOM   6555  CG2 THR C 210     -64.291  16.804  42.124  1.00 58.46           C  
ANISOU 6555  CG2 THR C 210     4773   6643  10795    -19   -720   -941       C  
ATOM   6556  N   LEU C 211     -61.418  14.494  42.398  1.00 55.51           N  
ANISOU 6556  N   LEU C 211     4508   6325  10256    -75   -663   -802       N  
ATOM   6557  CA  LEU C 211     -61.253  13.030  42.183  1.00 54.38           C  
ANISOU 6557  CA  LEU C 211     4412   6206  10043    -91   -646   -744       C  
ATOM   6558  C   LEU C 211     -62.474  12.258  42.702  1.00 53.43           C  
ANISOU 6558  C   LEU C 211     4275   6127   9897   -112   -623   -767       C  
ATOM   6559  O   LEU C 211     -62.787  11.199  42.119  1.00 53.04           O  
ANISOU 6559  O   LEU C 211     4261   6073   9815   -126   -615   -724       O  
ATOM   6560  CB  LEU C 211     -59.977  12.572  42.896  1.00 54.56           C  
ANISOU 6560  CB  LEU C 211     4456   6268  10003    -94   -626   -728       C  
ATOM   6561  CG  LEU C 211     -58.691  13.305  42.519  1.00 53.94           C  
ANISOU 6561  CG  LEU C 211     4384   6164   9944    -82   -641   -720       C  
ATOM   6562  CD1 LEU C 211     -57.583  12.962  43.507  1.00 53.33           C  
ANISOU 6562  CD1 LEU C 211     4307   6149   9804    -79   -622   -732       C  
ATOM   6563  CD2 LEU C 211     -58.296  12.986  41.083  1.00 53.42           C  
ANISOU 6563  CD2 LEU C 211     4367   6044   9885    -78   -661   -654       C  
ATOM   6564  N   SER C 212     -63.130  12.758  43.756  1.00 53.54           N  
ANISOU 6564  N   SER C 212     4235   6182   9923   -119   -608   -837       N  
ATOM   6565  CA  SER C 212     -64.288  12.099  44.421  1.00 53.48           C  
ANISOU 6565  CA  SER C 212     4206   6225   9888   -148   -577   -873       C  
ATOM   6566  C   SER C 212     -65.546  12.269  43.570  1.00 53.27           C  
ANISOU 6566  C   SER C 212     4150   6178   9913   -145   -598   -897       C  
ATOM   6567  O   SER C 212     -65.961  13.428  43.358  1.00 52.70           O  
ANISOU 6567  O   SER C 212     4032   6082   9907   -115   -630   -943       O  
ATOM   6568  CB  SER C 212     -64.520  12.614  45.813  1.00 53.29           C  
ANISOU 6568  CB  SER C 212     4130   6258   9857   -157   -554   -944       C  
ATOM   6569  OG  SER C 212     -65.697  12.036  46.353  1.00 52.21           O  
ANISOU 6569  OG  SER C 212     3969   6169   9698   -191   -521   -983       O  
ATOM   6570  N   TYR C 213     -66.125  11.146  43.138  1.00 53.12           N  
ANISOU 6570  N   TYR C 213     4155   6166   9859   -173   -579   -872       N  
ATOM   6571  CA  TYR C 213     -67.350  11.075  42.301  1.00 53.46           C  
ANISOU 6571  CA  TYR C 213     4168   6204   9938   -174   -596   -899       C  
ATOM   6572  C   TYR C 213     -68.568  11.384  43.170  1.00 53.74           C  
ANISOU 6572  C   TYR C 213     4131   6298   9988   -192   -576   -992       C  
ATOM   6573  O   TYR C 213     -69.470  12.084  42.691  1.00 52.44           O  
ANISOU 6573  O   TYR C 213     3913   6131   9880   -165   -610  -1046       O  
ATOM   6574  CB  TYR C 213     -67.479   9.695  41.653  1.00 53.02           C  
ANISOU 6574  CB  TYR C 213     4163   6145   9837   -206   -573   -848       C  
ATOM   6575  CG  TYR C 213     -68.520   9.577  40.572  1.00 52.98           C  
ANISOU 6575  CG  TYR C 213     4131   6132   9865   -202   -596   -869       C  
ATOM   6576  CD1 TYR C 213     -68.759  10.598  39.665  1.00 52.86           C  
ANISOU 6576  CD1 TYR C 213     4087   6083   9911   -148   -654   -881       C  
ATOM   6577  CD2 TYR C 213     -69.249   8.407  40.438  1.00 53.76           C  
ANISOU 6577  CD2 TYR C 213     4239   6258   9930   -251   -558   -876       C  
ATOM   6578  CE1 TYR C 213     -69.706  10.463  38.663  1.00 53.20           C  
ANISOU 6578  CE1 TYR C 213     4105   6130   9978   -135   -679   -902       C  
ATOM   6579  CE2 TYR C 213     -70.206   8.258  39.448  1.00 54.07           C  
ANISOU 6579  CE2 TYR C 213     4246   6302   9996   -248   -579   -904       C  
ATOM   6580  CZ  TYR C 213     -70.433   9.288  38.554  1.00 53.78           C  
ANISOU 6580  CZ  TYR C 213     4176   6241  10017   -185   -643   -918       C  
ATOM   6581  OH  TYR C 213     -71.365   9.120  37.574  1.00 53.44           O  
ANISOU 6581  OH  TYR C 213     4100   6211   9993   -174   -667   -948       O  
ATOM   6582  N   GLU C 214     -68.572  10.875  44.404  1.00 55.42           N  
ANISOU 6582  N   GLU C 214     4344   6563  10148   -234   -525  -1013       N  
ATOM   6583  CA  GLU C 214     -69.653  11.116  45.389  1.00 58.13           C  
ANISOU 6583  CA  GLU C 214     4619   6973  10496   -261   -497  -1105       C  
ATOM   6584  C   GLU C 214     -69.766  12.629  45.605  1.00 58.22           C  
ANISOU 6584  C   GLU C 214     4565   6979  10577   -212   -539  -1168       C  
ATOM   6585  O   GLU C 214     -70.888  13.156  45.535  1.00 60.37           O  
ANISOU 6585  O   GLU C 214     4768   7276  10894   -201   -555  -1246       O  
ATOM   6586  CB  GLU C 214     -69.385  10.383  46.710  1.00 59.69           C  
ANISOU 6586  CB  GLU C 214     4841   7220  10615   -309   -434  -1103       C  
ATOM   6587  CG  GLU C 214     -70.611   9.694  47.289  1.00 61.60           C  
ANISOU 6587  CG  GLU C 214     5055   7523  10825   -373   -379  -1161       C  
ATOM   6588  CD  GLU C 214     -70.843   9.884  48.787  1.00 63.53           C  
ANISOU 6588  CD  GLU C 214     5265   7837  11033   -402   -336  -1221       C  
ATOM   6589  OE1 GLU C 214     -69.869   9.845  49.569  1.00 63.81           O  
ANISOU 6589  OE1 GLU C 214     5341   7880  11022   -393   -323  -1185       O  
ATOM   6590  OE2 GLU C 214     -72.006  10.095  49.164  1.00 65.62           O  
ANISOU 6590  OE2 GLU C 214     5460   8156  11316   -432   -317  -1309       O  
ATOM   6591  N   GLN C 215     -68.638  13.294  45.835  1.00 57.61           N  
ANISOU 6591  N   GLN C 215     4507   6870  10509   -182   -557  -1140       N  
ATOM   6592  CA  GLN C 215     -68.588  14.754  46.097  1.00 58.28           C  
ANISOU 6592  CA  GLN C 215     4541   6940  10661   -139   -591  -1198       C  
ATOM   6593  C   GLN C 215     -69.097  15.508  44.866  1.00 58.24           C  
ANISOU 6593  C   GLN C 215     4524   6876  10729    -88   -648  -1203       C  
ATOM   6594  O   GLN C 215     -69.779  16.521  45.049  1.00 58.46           O  
ANISOU 6594  O   GLN C 215     4492   6905  10812    -56   -673  -1278       O  
ATOM   6595  CB  GLN C 215     -67.188  15.213  46.513  1.00 58.29           C  
ANISOU 6595  CB  GLN C 215     4572   6920  10653   -126   -593  -1166       C  
ATOM   6596  CG  GLN C 215     -67.219  16.567  47.204  1.00 58.71           C  
ANISOU 6596  CG  GLN C 215     4566   6976  10762   -100   -608  -1244       C  
ATOM   6597  CD  GLN C 215     -67.806  16.468  48.595  1.00 60.05           C  
ANISOU 6597  CD  GLN C 215     4681   7235  10901   -130   -569  -1319       C  
ATOM   6598  OE1 GLN C 215     -67.133  16.050  49.531  1.00 60.14           O  
ANISOU 6598  OE1 GLN C 215     4705   7291  10851   -154   -535  -1310       O  
ATOM   6599  NE2 GLN C 215     -69.075  16.835  48.741  1.00 60.52           N  
ANISOU 6599  NE2 GLN C 215     4676   7323  10997   -127   -575  -1398       N  
ATOM   6600  N   PHE C 216     -68.801  15.015  43.666  1.00 58.49           N  
ANISOU 6600  N   PHE C 216     4610   6859  10755    -79   -667  -1129       N  
ATOM   6601  CA  PHE C 216     -69.210  15.626  42.378  1.00 60.39           C  
ANISOU 6601  CA  PHE C 216     4852   7041  11051    -26   -722  -1121       C  
ATOM   6602  C   PHE C 216     -70.735  15.637  42.262  1.00 64.66           C  
ANISOU 6602  C   PHE C 216     5325   7626  11613    -16   -734  -1199       C  
ATOM   6603  O   PHE C 216     -71.259  16.459  41.500  1.00 67.05           O  
ANISOU 6603  O   PHE C 216     5610   7895  11970     43   -786  -1222       O  
ATOM   6604  CB  PHE C 216     -68.608  14.837  41.221  1.00 59.61           C  
ANISOU 6604  CB  PHE C 216     4822   6900  10924    -30   -730  -1027       C  
ATOM   6605  CG  PHE C 216     -68.759  15.451  39.858  1.00 59.55           C  
ANISOU 6605  CG  PHE C 216     4833   6829  10962     24   -785  -1000       C  
ATOM   6606  CD1 PHE C 216     -69.297  14.719  38.814  1.00 58.94           C  
ANISOU 6606  CD1 PHE C 216     4769   6753  10870     28   -800   -974       C  
ATOM   6607  CD2 PHE C 216     -68.309  16.737  39.606  1.00 60.51           C  
ANISOU 6607  CD2 PHE C 216     4967   6885  11136     72   -819   -998       C  
ATOM   6608  CE1 PHE C 216     -69.393  15.268  37.544  1.00 59.59           C  
ANISOU 6608  CE1 PHE C 216     4874   6780  10986     84   -852   -944       C  
ATOM   6609  CE2 PHE C 216     -68.407  17.287  38.336  1.00 60.87           C  
ANISOU 6609  CE2 PHE C 216     5045   6867  11216    125   -868   -965       C  
ATOM   6610  CZ  PHE C 216     -68.954  16.553  37.308  1.00 60.73           C  
ANISOU 6610  CZ  PHE C 216     5038   6858  11178    134   -886   -937       C  
ATOM   6611  N   LYS C 217     -71.420  14.725  42.961  1.00 67.37           N  
ANISOU 6611  N   LYS C 217     5638   8046  11914    -72   -687  -1239       N  
ATOM   6612  CA  LYS C 217     -72.902  14.607  42.952  1.00 69.48           C  
ANISOU 6612  CA  LYS C 217     5830   8374  12194    -76   -688  -1328       C  
ATOM   6613  C   LYS C 217     -73.492  15.582  43.973  1.00 72.24           C  
ANISOU 6613  C   LYS C 217     6103   8766  12579    -60   -691  -1430       C  
ATOM   6614  O   LYS C 217     -74.567  16.163  43.675  1.00 76.41           O  
ANISOU 6614  O   LYS C 217     6564   9315  13150    -18   -727  -1510       O  
ATOM   6615  CB  LYS C 217     -73.348  13.175  43.268  1.00 69.93           C  
ANISOU 6615  CB  LYS C 217     5892   8490  12186   -157   -626  -1330       C  
ATOM   6616  CG  LYS C 217     -73.018  12.142  42.203  1.00 69.25           C  
ANISOU 6616  CG  LYS C 217     5870   8369  12069   -174   -623  -1247       C  
ATOM   6617  CD  LYS C 217     -73.015  10.730  42.730  1.00 69.53           C  
ANISOU 6617  CD  LYS C 217     5943   8441  12033   -257   -551  -1225       C  
ATOM   6618  CE  LYS C 217     -72.764   9.711  41.637  1.00 70.26           C  
ANISOU 6618  CE  LYS C 217     6096   8499  12101   -273   -549  -1154       C  
ATOM   6619  NZ  LYS C 217     -72.959   8.326  42.124  1.00 71.22           N  
ANISOU 6619  NZ  LYS C 217     6252   8650  12156   -356   -475  -1144       N  
ATOM   6620  N   LYS C 218     -72.834  15.740  45.127  1.00 71.55           N  
ANISOU 6620  N   LYS C 218     6020   8695  12471    -87   -656  -1433       N  
ATOM   6621  CA  LYS C 218     -73.306  16.609  46.236  1.00 71.85           C  
ANISOU 6621  CA  LYS C 218     5983   8780  12536    -80   -651  -1533       C  
ATOM   6622  C   LYS C 218     -73.073  18.074  45.851  1.00 72.96           C  
ANISOU 6622  C   LYS C 218     6114   8852  12755      0   -712  -1550       C  
ATOM   6623  O   LYS C 218     -74.058  18.747  45.523  1.00 77.42           O  
ANISOU 6623  O   LYS C 218     6623   9422  13369     50   -752  -1622       O  
ATOM   6624  CB  LYS C 218     -72.629  16.207  47.549  1.00 69.80           C  
ANISOU 6624  CB  LYS C 218     5736   8564  12218   -135   -593  -1525       C  
ATOM   6625  CG  LYS C 218     -72.815  14.747  47.924  1.00 68.90           C  
ANISOU 6625  CG  LYS C 218     5651   8504  12022   -212   -529  -1498       C  
ATOM   6626  CD  LYS C 218     -72.345  14.442  49.328  1.00 68.48           C  
ANISOU 6626  CD  LYS C 218     5605   8505  11908   -258   -474  -1505       C  
ATOM   6627  CE  LYS C 218     -72.271  12.960  49.620  1.00 67.80           C  
ANISOU 6627  CE  LYS C 218     5580   8448  11732   -327   -410  -1451       C  
ATOM   6628  NZ  LYS C 218     -72.306  12.687  51.078  1.00 68.28           N  
ANISOU 6628  NZ  LYS C 218     5629   8583  11730   -374   -351  -1488       N  
ATOM   6629  N   GLY C 219     -71.825  18.540  45.849  1.00 74.04           N  
ANISOU 6629  N   GLY C 219     6305   8925  12899     13   -719  -1489       N  
ATOM   6630  CA  GLY C 219     -71.489  19.948  45.569  1.00 75.59           C  
ANISOU 6630  CA  GLY C 219     6505   9046  13168     78   -765  -1504       C  
ATOM   6631  C   GLY C 219     -69.992  20.172  45.462  1.00 75.98           C  
ANISOU 6631  C   GLY C 219     6624   9031  13213     71   -759  -1426       C  
ATOM   6632  O   GLY C 219     -69.243  19.488  46.170  1.00 74.58           O  
ANISOU 6632  O   GLY C 219     6464   8893  12978     20   -715  -1397       O  
ATOM   6633  N   VAL C 220     -69.587  21.113  44.605  1.00 78.58           N  
ANISOU 6633  N   VAL C 220     6993   9265  13597    122   -800  -1397       N  
ATOM   6634  CA  VAL C 220     -68.176  21.542  44.367  1.00 81.00           C  
ANISOU 6634  CA  VAL C 220     7363   9500  13911    117   -796  -1334       C  
ATOM   6635  C   VAL C 220     -68.187  23.062  44.126  1.00 83.93           C  
ANISOU 6635  C   VAL C 220     7738   9786  14363    172   -830  -1371       C  
ATOM   6636  O   VAL C 220     -69.089  23.522  43.407  1.00 85.47           O  
ANISOU 6636  O   VAL C 220     7929   9944  14598    230   -874  -1388       O  
ATOM   6637  CB  VAL C 220     -67.576  20.758  43.177  1.00 80.28           C  
ANISOU 6637  CB  VAL C 220     7348   9368  13786    109   -802  -1227       C  
ATOM   6638  CG1 VAL C 220     -66.239  21.314  42.706  1.00 81.31           C  
ANISOU 6638  CG1 VAL C 220     7542   9419  13932    108   -803  -1169       C  
ATOM   6639  CG2 VAL C 220     -67.451  19.272  43.492  1.00 78.73           C  
ANISOU 6639  CG2 VAL C 220     7157   9246  13510     54   -764  -1191       C  
ATOM   6640  N   GLN C 221     -67.229  23.809  44.690  1.00 85.55           N  
ANISOU 6640  N   GLN C 221     7952   9960  14591    158   -812  -1385       N  
ATOM   6641  CA  GLN C 221     -67.192  25.301  44.648  1.00 86.18           C  
ANISOU 6641  CA  GLN C 221     8038   9955  14751    201   -834  -1431       C  
ATOM   6642  C   GLN C 221     -66.272  25.759  43.511  1.00 86.45           C  
ANISOU 6642  C   GLN C 221     8164   9876  14806    211   -845  -1349       C  
ATOM   6643  O   GLN C 221     -65.173  25.192  43.401  1.00 86.15           O  
ANISOU 6643  O   GLN C 221     8162   9844  14726    163   -816  -1289       O  
ATOM   6644  CB  GLN C 221     -66.762  25.849  46.014  1.00 86.24           C  
ANISOU 6644  CB  GLN C 221     7992  10004  14771    172   -801  -1511       C  
ATOM   6645  CG  GLN C 221     -67.786  25.627  47.121  1.00 86.79           C  
ANISOU 6645  CG  GLN C 221     7970  10176  14827    169   -792  -1603       C  
ATOM   6646  CD  GLN C 221     -67.984  24.172  47.477  1.00 86.17           C  
ANISOU 6646  CD  GLN C 221     7873  10201  14664    122   -763  -1576       C  
ATOM   6647  OE1 GLN C 221     -67.030  23.407  47.636  1.00 87.26           O  
ANISOU 6647  OE1 GLN C 221     8043  10365  14744     77   -732  -1518       O  
ATOM   6648  NE2 GLN C 221     -69.240  23.779  47.612  1.00 84.84           N  
ANISOU 6648  NE2 GLN C 221     7653  10093  14487    132   -772  -1622       N  
ATOM   6649  N   ILE C 222     -66.723  26.723  42.694  1.00 89.23           N  
ANISOU 6649  N   ILE C 222     8555  10131  15217    274   -885  -1347       N  
ATOM   6650  CA  ILE C 222     -65.961  27.320  41.551  1.00 91.22           C  
ANISOU 6650  CA  ILE C 222     8904  10261  15492    288   -895  -1271       C  
ATOM   6651  C   ILE C 222     -66.298  28.809  41.439  1.00 94.90           C  
ANISOU 6651  C   ILE C 222     9395  10623  16038    347   -920  -1316       C  
ATOM   6652  O   ILE C 222     -67.304  29.252  41.991  1.00 96.46           O  
ANISOU 6652  O   ILE C 222     9535  10845  16269    393   -943  -1399       O  
ATOM   6653  CB  ILE C 222     -66.250  26.559  40.236  1.00 90.57           C  
ANISOU 6653  CB  ILE C 222     8873  10165  15373    312   -925  -1183       C  
ATOM   6654  CG1 ILE C 222     -67.745  26.476  39.918  1.00 90.21           C  
ANISOU 6654  CG1 ILE C 222     8789  10147  15337    382   -974  -1219       C  
ATOM   6655  CG2 ILE C 222     -65.613  25.175  40.263  1.00 89.81           C  
ANISOU 6655  CG2 ILE C 222     8773  10145  15202    247   -894  -1127       C  
ATOM   6656  CD1 ILE C 222     -68.045  25.931  38.542  1.00 89.33           C  
ANISOU 6656  CD1 ILE C 222     8731  10013  15197    416  -1009  -1140       C  
ATOM   6657  N   PRO C 223     -65.459  29.640  40.771  1.00 97.60           N  
ANISOU 6657  N   PRO C 223     9825  10845  16412    345   -911  -1270       N  
ATOM   6658  CA  PRO C 223     -65.824  31.030  40.478  1.00 98.56           C  
ANISOU 6658  CA  PRO C 223     9994  10847  16606    409   -936  -1299       C  
ATOM   6659  C   PRO C 223     -66.957  31.159  39.437  1.00 99.54           C  
ANISOU 6659  C   PRO C 223    10155  10928  16738    507  -1001  -1270       C  
ATOM   6660  O   PRO C 223     -67.081  30.288  38.579  1.00 98.15           O  
ANISOU 6660  O   PRO C 223    10001  10780  16511    512  -1019  -1199       O  
ATOM   6661  CB  PRO C 223     -64.512  31.663  39.964  1.00 98.11           C  
ANISOU 6661  CB  PRO C 223    10031  10679  16566    362   -898  -1244       C  
ATOM   6662  CG  PRO C 223     -63.666  30.497  39.491  1.00 96.32           C  
ANISOU 6662  CG  PRO C 223     9821  10507  16268    298   -874  -1161       C  
ATOM   6663  CD  PRO C 223     -64.091  29.310  40.332  1.00 96.31           C  
ANISOU 6663  CD  PRO C 223     9720  10656  16216    277   -872  -1195       C  
ATOM   6664  N   CYS C 224     -67.732  32.250  39.520  1.00100.02           N  
ANISOU 6664  N   CYS C 224    10221  10923  16859    586  -1037  -1330       N  
ATOM   6665  CA  CYS C 224     -68.850  32.604  38.595  1.00 99.28           C  
ANISOU 6665  CA  CYS C 224    10161  10781  16777    700  -1106  -1319       C  
ATOM   6666  C   CYS C 224     -68.299  33.323  37.352  1.00 97.84           C  
ANISOU 6666  C   CYS C 224    10121  10445  16607    733  -1115  -1225       C  
ATOM   6667  O   CYS C 224     -67.766  34.441  37.518  1.00 95.49           O  
ANISOU 6667  O   CYS C 224     9885  10033  16362    729  -1092  -1237       O  
ATOM   6668  CB  CYS C 224     -69.894  33.465  39.305  1.00 99.82           C  
ANISOU 6668  CB  CYS C 224    10171  10850  16903    777  -1141  -1432       C  
ATOM   6669  SG  CYS C 224     -71.222  34.070  38.229  1.00100.40           S  
ANISOU 6669  SG  CYS C 224    10290  10861  16995    935  -1232  -1432       S  
ATOM   6670  N   GLY C 227     -67.647  37.593  39.685  1.00 90.21           N  
ANISOU 6670  N   GLY C 227     9209   9177  15889    753  -1047  -1464       N  
ATOM   6671  CA  GLY C 227     -67.136  38.067  40.996  1.00 90.58           C  
ANISOU 6671  CA  GLY C 227     9189   9247  15980    685   -995  -1562       C  
ATOM   6672  C   GLY C 227     -67.893  37.434  42.152  1.00 91.55           C  
ANISOU 6672  C   GLY C 227     9160   9536  16090    684  -1008  -1661       C  
ATOM   6673  O   GLY C 227     -68.588  38.184  42.872  1.00 91.12           O  
ANISOU 6673  O   GLY C 227     9055   9477  16089    736  -1027  -1764       O  
ATOM   6674  N   LYS C 228     -67.780  36.103  42.296  1.00 91.96           N  
ANISOU 6674  N   LYS C 228     9146   9725  16069    628   -997  -1631       N  
ATOM   6675  CA  LYS C 228     -68.316  35.274  43.420  1.00 91.86           C  
ANISOU 6675  CA  LYS C 228     8994   9882  16024    601   -992  -1709       C  
ATOM   6676  C   LYS C 228     -67.883  33.809  43.223  1.00 92.47           C  
ANISOU 6676  C   LYS C 228     9051  10065  16017    532   -971  -1635       C  
ATOM   6677  O   LYS C 228     -67.174  33.542  42.233  1.00 92.45           O  
ANISOU 6677  O   LYS C 228     9136  10001  15987    511   -963  -1532       O  
ATOM   6678  CB  LYS C 228     -69.843  35.401  43.504  1.00 90.93           C  
ANISOU 6678  CB  LYS C 228     8816   9808  15925    701  -1054  -1780       C  
ATOM   6679  CG  LYS C 228     -70.419  35.295  44.913  1.00 89.55           C  
ANISOU 6679  CG  LYS C 228     8508   9760  15757    683  -1043  -1906       C  
ATOM   6680  CD  LYS C 228     -71.358  36.427  45.283  1.00 89.40           C  
ANISOU 6680  CD  LYS C 228     8459   9698  15810    775  -1083  -2013       C  
ATOM   6681  CE  LYS C 228     -71.167  36.912  46.707  1.00 88.46           C  
ANISOU 6681  CE  LYS C 228     8255   9629  15725    730  -1045  -2127       C  
ATOM   6682  NZ  LYS C 228     -71.732  38.272  46.896  1.00 89.55           N  
ANISOU 6682  NZ  LYS C 228     8401   9674  15948    816  -1077  -2216       N  
ATOM   6683  N   GLN C 229     -68.251  32.904  44.141  1.00 92.19           N  
ANISOU 6683  N   GLN C 229     8910  10178  15938    496   -958  -1685       N  
ATOM   6684  CA  GLN C 229     -68.090  31.434  43.952  1.00 91.16           C  
ANISOU 6684  CA  GLN C 229     8761  10150  15726    445   -945  -1620       C  
ATOM   6685  C   GLN C 229     -69.466  30.760  43.930  1.00 90.03           C  
ANISOU 6685  C   GLN C 229     8550  10098  15556    492   -983  -1654       C  
ATOM   6686  O   GLN C 229     -70.370  31.261  44.630  1.00 90.10           O  
ANISOU 6686  O   GLN C 229     8488  10144  15601    532  -1002  -1756       O  
ATOM   6687  CB  GLN C 229     -67.193  30.820  45.025  1.00 91.84           C  
ANISOU 6687  CB  GLN C 229     8796  10329  15769    352   -886  -1638       C  
ATOM   6688  CG  GLN C 229     -67.930  30.424  46.294  1.00 92.29           C  
ANISOU 6688  CG  GLN C 229     8740  10517  15806    340   -876  -1734       C  
ATOM   6689  CD  GLN C 229     -66.973  30.146  47.424  1.00 91.86           C  
ANISOU 6689  CD  GLN C 229     8645  10537  15719    262   -822  -1763       C  
ATOM   6690  OE1 GLN C 229     -65.776  29.945  47.221  1.00 92.87           O  
ANISOU 6690  OE1 GLN C 229     8820  10642  15823    214   -792  -1704       O  
ATOM   6691  NE2 GLN C 229     -67.502  30.140  48.636  1.00 91.47           N  
ANISOU 6691  NE2 GLN C 229     8504  10585  15665    253   -809  -1859       N  
ATOM   6692  N   ALA C 230     -69.590  29.648  43.191  1.00 88.36           N  
ANISOU 6692  N   ALA C 230     8356   9929  15286    480   -991  -1579       N  
ATOM   6693  CA  ALA C 230     -70.859  28.943  42.878  1.00 87.99           C  
ANISOU 6693  CA  ALA C 230     8259   9960  15213    521  -1028  -1600       C  
ATOM   6694  C   ALA C 230     -70.786  27.483  43.345  1.00 85.36           C  
ANISOU 6694  C   ALA C 230     7877   9750  14803    442   -988  -1583       C  
ATOM   6695  O   ALA C 230     -69.733  27.093  43.896  1.00 85.59           O  
ANISOU 6695  O   ALA C 230     7918   9800  14802    368   -939  -1552       O  
ATOM   6696  CB  ALA C 230     -71.114  29.036  41.393  1.00 88.65           C  
ANISOU 6696  CB  ALA C 230     8420   9963  15298    588  -1077  -1524       C  
ATOM   6697  N   THR C 231     -71.868  26.719  43.149  1.00 81.94           N  
ANISOU 6697  N   THR C 231     7394   9397  14341    457  -1007  -1607       N  
ATOM   6698  CA  THR C 231     -71.971  25.277  43.505  1.00 79.17           C  
ANISOU 6698  CA  THR C 231     7006   9157  13917    384   -968  -1592       C  
ATOM   6699  C   THR C 231     -72.256  24.457  42.239  1.00 77.50           C  
ANISOU 6699  C   THR C 231     6834   8939  13672    400   -992  -1518       C  
ATOM   6700  O   THR C 231     -73.290  24.706  41.592  1.00 77.83           O  
ANISOU 6700  O   THR C 231     6855   8980  13734    469  -1042  -1553       O  
ATOM   6701  CB  THR C 231     -73.030  25.049  44.589  1.00 79.51           C  
ANISOU 6701  CB  THR C 231     6941   9315  13953    370   -953  -1705       C  
ATOM   6702  OG1 THR C 231     -72.681  25.885  45.691  1.00 78.78           O  
ANISOU 6702  OG1 THR C 231     6817   9222  13894    360   -933  -1770       O  
ATOM   6703  CG2 THR C 231     -73.124  23.607  45.040  1.00 78.96           C  
ANISOU 6703  CG2 THR C 231     6844   9349  13806    288   -904  -1691       C  
ATOM   6704  N   LYS C 232     -71.347  23.537  41.903  1.00 75.55           N  
ANISOU 6704  N   LYS C 232     6641   8690  13373    341   -961  -1426       N  
ATOM   6705  CA  LYS C 232     -71.411  22.606  40.745  1.00 73.60           C  
ANISOU 6705  CA  LYS C 232     6436   8440  13085    339   -974  -1348       C  
ATOM   6706  C   LYS C 232     -71.783  21.213  41.269  1.00 71.55           C  
ANISOU 6706  C   LYS C 232     6131   8289  12763    270   -932  -1361       C  
ATOM   6707  O   LYS C 232     -71.180  20.780  42.275  1.00 70.76           O  
ANISOU 6707  O   LYS C 232     6022   8230  12631    206   -881  -1362       O  
ATOM   6708  CB  LYS C 232     -70.046  22.595  40.045  1.00 73.13           C  
ANISOU 6708  CB  LYS C 232     6471   8298  13014    320   -965  -1240       C  
ATOM   6709  CG  LYS C 232     -70.013  22.173  38.588  1.00 73.13           C  
ANISOU 6709  CG  LYS C 232     6533   8256  12994    347   -996  -1157       C  
ATOM   6710  CD  LYS C 232     -68.597  22.271  38.033  1.00 72.15           C  
ANISOU 6710  CD  LYS C 232     6497   8055  12860    321   -980  -1062       C  
ATOM   6711  CE  LYS C 232     -68.543  22.283  36.523  1.00 71.74           C  
ANISOU 6711  CE  LYS C 232     6514   7938  12802    363  -1018   -985       C  
ATOM   6712  NZ  LYS C 232     -67.202  22.689  36.033  1.00 70.75           N  
ANISOU 6712  NZ  LYS C 232     6473   7728  12679    341  -1002   -908       N  
ATOM   6713  N   TYR C 233     -72.749  20.548  40.631  1.00 69.85           N  
ANISOU 6713  N   TYR C 233     5890   8118  12530    283   -950  -1374       N  
ATOM   6714  CA  TYR C 233     -73.160  19.157  40.958  1.00 69.33           C  
ANISOU 6714  CA  TYR C 233     5793   8144  12404    212   -905  -1383       C  
ATOM   6715  C   TYR C 233     -73.626  18.426  39.694  1.00 68.26           C  
ANISOU 6715  C   TYR C 233     5675   8010  12248    227   -930  -1345       C  
ATOM   6716  O   TYR C 233     -74.028  19.092  38.706  1.00 68.67           O  
ANISOU 6716  O   TYR C 233     5737   8019  12334    306   -990  -1344       O  
ATOM   6717  CB  TYR C 233     -74.252  19.131  42.030  1.00 71.12           C  
ANISOU 6717  CB  TYR C 233     5923   8467  12633    192   -884  -1500       C  
ATOM   6718  CG  TYR C 233     -75.524  19.860  41.683  1.00 73.33           C  
ANISOU 6718  CG  TYR C 233     6136   8767  12960    267   -937  -1593       C  
ATOM   6719  CD1 TYR C 233     -75.788  21.112  42.212  1.00 74.64           C  
ANISOU 6719  CD1 TYR C 233     6263   8914  13181    323   -966  -1665       C  
ATOM   6720  CD2 TYR C 233     -76.467  19.303  40.835  1.00 74.00           C  
ANISOU 6720  CD2 TYR C 233     6192   8893  13032    286   -961  -1615       C  
ATOM   6721  CE1 TYR C 233     -76.953  21.795  41.905  1.00 76.62           C  
ANISOU 6721  CE1 TYR C 233     6453   9186  13473    403  -1020  -1755       C  
ATOM   6722  CE2 TYR C 233     -77.637  19.970  40.515  1.00 76.28           C  
ANISOU 6722  CE2 TYR C 233     6413   9209  13358    364  -1015  -1708       C  
ATOM   6723  CZ  TYR C 233     -77.882  21.222  41.054  1.00 77.25           C  
ANISOU 6723  CZ  TYR C 233     6502   9313  13536    427  -1046  -1777       C  
ATOM   6724  OH  TYR C 233     -79.024  21.898  40.745  1.00 78.52           O  
ANISOU 6724  OH  TYR C 233     6598   9501  13733    516  -1105  -1872       O  
ATOM   6725  N   LEU C 234     -73.574  17.092  39.750  1.00 65.80           N  
ANISOU 6725  N   LEU C 234     5372   7748  11879    155   -884  -1316       N  
ATOM   6726  CA  LEU C 234     -74.009  16.173  38.669  1.00 65.29           C  
ANISOU 6726  CA  LEU C 234     5320   7700  11788    150   -894  -1287       C  
ATOM   6727  C   LEU C 234     -75.531  15.986  38.742  1.00 65.12           C  
ANISOU 6727  C   LEU C 234     5205   7765  11772    156   -901  -1397       C  
ATOM   6728  O   LEU C 234     -76.035  15.623  39.835  1.00 63.99           O  
ANISOU 6728  O   LEU C 234     5006   7695  11612     99   -853  -1468       O  
ATOM   6729  CB  LEU C 234     -73.280  14.834  38.820  1.00 64.42           C  
ANISOU 6729  CB  LEU C 234     5260   7602  11616     67   -836  -1217       C  
ATOM   6730  CG  LEU C 234     -73.594  13.795  37.741  1.00 64.63           C  
ANISOU 6730  CG  LEU C 234     5304   7640  11612     51   -838  -1184       C  
ATOM   6731  CD1 LEU C 234     -73.095  14.253  36.374  1.00 64.04           C  
ANISOU 6731  CD1 LEU C 234     5284   7491  11555    117   -896  -1112       C  
ATOM   6732  CD2 LEU C 234     -73.000  12.437  38.099  1.00 64.14           C  
ANISOU 6732  CD2 LEU C 234     5289   7593  11488    -33   -773  -1130       C  
ATOM   6733  N   VAL C 235     -76.217  16.225  37.617  1.00 64.70           N  
ANISOU 6733  N   VAL C 235     5136   7708  11738    224   -959  -1414       N  
ATOM   6734  CA  VAL C 235     -77.694  16.072  37.464  1.00 66.07           C  
ANISOU 6734  CA  VAL C 235     5215   7971  11917    244   -977  -1526       C  
ATOM   6735  C   VAL C 235     -77.992  14.669  36.930  1.00 65.90           C  
ANISOU 6735  C   VAL C 235     5192   7999  11847    177   -942  -1514       C  
ATOM   6736  O   VAL C 235     -78.706  13.909  37.619  1.00 65.99           O  
ANISOU 6736  O   VAL C 235     5144   8095  11834    103   -887  -1588       O  
ATOM   6737  CB  VAL C 235     -78.290  17.136  36.526  1.00 66.78           C  
ANISOU 6737  CB  VAL C 235     5287   8035  12049    367  -1065  -1557       C  
ATOM   6738  CG1 VAL C 235     -79.806  17.064  36.512  1.00 67.91           C  
ANISOU 6738  CG1 VAL C 235     5319   8283  12198    393  -1086  -1691       C  
ATOM   6739  CG2 VAL C 235     -77.822  18.538  36.877  1.00 66.96           C  
ANISOU 6739  CG2 VAL C 235     5337   7981  12121    435  -1100  -1549       C  
ATOM   6740  N   GLN C 236     -77.473  14.360  35.740  1.00 64.88           N  
ANISOU 6740  N   GLN C 236     5127   7819  11704    202   -969  -1427       N  
ATOM   6741  CA  GLN C 236     -77.634  13.045  35.068  1.00 64.96           C  
ANISOU 6741  CA  GLN C 236     5147   7862  11671    145   -940  -1406       C  
ATOM   6742  C   GLN C 236     -76.284  12.608  34.471  1.00 64.04           C  
ANISOU 6742  C   GLN C 236     5138   7664  11530    127   -932  -1271       C  
ATOM   6743  O   GLN C 236     -75.621  13.454  33.828  1.00 65.25           O  
ANISOU 6743  O   GLN C 236     5344   7742  11705    198   -983  -1206       O  
ATOM   6744  CB  GLN C 236     -78.738  13.124  34.004  1.00 66.02           C  
ANISOU 6744  CB  GLN C 236     5222   8047  11815    209   -997  -1473       C  
ATOM   6745  CG  GLN C 236     -78.881  11.833  33.195  1.00 65.92           C  
ANISOU 6745  CG  GLN C 236     5218   8066  11762    156   -972  -1454       C  
ATOM   6746  CD  GLN C 236     -80.229  11.583  32.573  1.00 66.79           C  
ANISOU 6746  CD  GLN C 236     5235   8270  11871    180   -999  -1564       C  
ATOM   6747  OE1 GLN C 236     -80.391  11.699  31.358  1.00 67.10           O  
ANISOU 6747  OE1 GLN C 236     5280   8306  11909    250  -1058  -1548       O  
ATOM   6748  NE2 GLN C 236     -81.184  11.188  33.403  1.00 67.33           N  
ANISOU 6748  NE2 GLN C 236     5216   8428  11936    117   -951  -1679       N  
ATOM   6749  N   GLN C 237     -75.915  11.333  34.672  1.00 61.77           N  
ANISOU 6749  N   GLN C 237     4882   7389  11197     37   -869  -1234       N  
ATOM   6750  CA  GLN C 237     -74.791  10.636  33.997  1.00 58.24           C  
ANISOU 6750  CA  GLN C 237     4526   6883  10719     15   -858  -1120       C  
ATOM   6751  C   GLN C 237     -75.292   9.361  33.314  1.00 57.29           C  
ANISOU 6751  C   GLN C 237     4398   6804  10565    -33   -833  -1131       C  
ATOM   6752  O   GLN C 237     -75.894   8.527  34.014  1.00 57.01           O  
ANISOU 6752  O   GLN C 237     4328   6824  10508   -110   -772  -1189       O  
ATOM   6753  CB  GLN C 237     -73.724  10.268  35.027  1.00 57.56           C  
ANISOU 6753  CB  GLN C 237     4496   6767  10607    -45   -801  -1063       C  
ATOM   6754  CG  GLN C 237     -72.404   9.827  34.407  1.00 56.34           C  
ANISOU 6754  CG  GLN C 237     4433   6546  10426    -49   -800   -949       C  
ATOM   6755  CD  GLN C 237     -71.752  10.983  33.700  1.00 55.53           C  
ANISOU 6755  CD  GLN C 237     4362   6378  10356     27   -861   -899       C  
ATOM   6756  OE1 GLN C 237     -71.516  12.036  34.295  1.00 55.72           O  
ANISOU 6756  OE1 GLN C 237     4379   6379  10412     58   -875   -912       O  
ATOM   6757  NE2 GLN C 237     -71.492  10.802  32.415  1.00 54.75           N  
ANISOU 6757  NE2 GLN C 237     4300   6250  10250     57   -895   -845       N  
ATOM   6758  N   GLU C 238     -75.040   9.215  32.009  1.00 56.50           N  
ANISOU 6758  N   GLU C 238     4330   6676  10460      5   -874  -1079       N  
ATOM   6759  CA  GLU C 238     -75.237   7.951  31.243  1.00 56.21           C  
ANISOU 6759  CA  GLU C 238     4303   6664  10390    -41   -850  -1072       C  
ATOM   6760  C   GLU C 238     -73.937   7.614  30.511  1.00 54.63           C  
ANISOU 6760  C   GLU C 238     4196   6391  10167    -37   -857   -953       C  
ATOM   6761  O   GLU C 238     -73.677   8.244  29.459  1.00 54.99           O  
ANISOU 6761  O   GLU C 238     4262   6405  10225     35   -919   -912       O  
ATOM   6762  CB  GLU C 238     -76.386   8.073  30.240  1.00 58.08           C  
ANISOU 6762  CB  GLU C 238     4468   6959  10638      7   -899  -1147       C  
ATOM   6763  CG  GLU C 238     -77.741   8.256  30.897  1.00 60.57           C  
ANISOU 6763  CG  GLU C 238     4679   7361  10971     -2   -889  -1280       C  
ATOM   6764  CD  GLU C 238     -78.945   8.144  29.983  1.00 62.65           C  
ANISOU 6764  CD  GLU C 238     4861   7704  11237     34   -928  -1373       C  
ATOM   6765  OE1 GLU C 238     -78.767   7.772  28.796  1.00 62.80           O  
ANISOU 6765  OE1 GLU C 238     4906   7714  11241     59   -958  -1332       O  
ATOM   6766  OE2 GLU C 238     -80.061   8.424  30.473  1.00 65.68           O  
ANISOU 6766  OE2 GLU C 238     5151   8166  11638     37   -928  -1491       O  
ATOM   6767  N   SER C 239     -73.155   6.672  31.061  1.00 52.88           N  
ANISOU 6767  N   SER C 239     4032   6147   9912   -109   -796   -901       N  
ATOM   6768  CA  SER C 239     -71.890   6.130  30.485  1.00 50.00           C  
ANISOU 6768  CA  SER C 239     3753   5723   9519   -116   -792   -797       C  
ATOM   6769  C   SER C 239     -71.446   4.913  31.292  1.00 48.07           C  
ANISOU 6769  C   SER C 239     3555   5475   9234   -199   -717   -774       C  
ATOM   6770  O   SER C 239     -71.839   4.783  32.451  1.00 47.87           O  
ANISOU 6770  O   SER C 239     3508   5477   9202   -242   -671   -820       O  
ATOM   6771  CB  SER C 239     -70.822   7.192  30.456  1.00 50.02           C  
ANISOU 6771  CB  SER C 239     3800   5666   9539    -61   -830   -730       C  
ATOM   6772  OG  SER C 239     -70.540   7.671  31.768  1.00 50.13           O  
ANISOU 6772  OG  SER C 239     3811   5676   9561    -76   -803   -743       O  
ATOM   6773  N   PRO C 240     -70.617   4.004  30.715  1.00 46.83           N  
ANISOU 6773  N   PRO C 240     3464   5283   9044   -219   -703   -704       N  
ATOM   6774  CA  PRO C 240     -70.160   2.794  31.418  1.00 46.12           C  
ANISOU 6774  CA  PRO C 240     3431   5181   8910   -287   -635   -677       C  
ATOM   6775  C   PRO C 240     -69.109   3.048  32.514  1.00 46.00           C  
ANISOU 6775  C   PRO C 240     3464   5136   8876   -286   -615   -628       C  
ATOM   6776  O   PRO C 240     -69.043   2.300  33.487  1.00 45.54           O  
ANISOU 6776  O   PRO C 240     3438   5082   8784   -338   -556   -629       O  
ATOM   6777  CB  PRO C 240     -69.584   1.902  30.309  1.00 44.92           C  
ANISOU 6777  CB  PRO C 240     3330   5001   8735   -291   -640   -621       C  
ATOM   6778  CG  PRO C 240     -69.251   2.843  29.174  1.00 44.96           C  
ANISOU 6778  CG  PRO C 240     3324   4991   8766   -217   -714   -590       C  
ATOM   6779  CD  PRO C 240     -70.109   4.078  29.336  1.00 45.84           C  
ANISOU 6779  CD  PRO C 240     3365   5131   8920   -174   -752   -650       C  
ATOM   6780  N   PHE C 241     -68.312   4.108  32.351  1.00 46.60           N  
ANISOU 6780  N   PHE C 241     3547   5184   8974   -228   -663   -590       N  
ATOM   6781  CA  PHE C 241     -67.341   4.610  33.359  1.00 46.69           C  
ANISOU 6781  CA  PHE C 241     3586   5177   8975   -218   -653   -559       C  
ATOM   6782  C   PHE C 241     -67.414   6.138  33.413  1.00 47.55           C  
ANISOU 6782  C   PHE C 241     3651   5280   9134   -166   -700   -583       C  
ATOM   6783  O   PHE C 241     -68.007   6.776  32.510  1.00 47.30           O  
ANISOU 6783  O   PHE C 241     3585   5247   9138   -126   -746   -602       O  
ATOM   6784  CB  PHE C 241     -65.915   4.184  33.007  1.00 45.44           C  
ANISOU 6784  CB  PHE C 241     3500   4979   8786   -207   -657   -477       C  
ATOM   6785  CG  PHE C 241     -65.468   4.706  31.667  1.00 44.90           C  
ANISOU 6785  CG  PHE C 241     3438   4882   8739   -162   -711   -439       C  
ATOM   6786  CD1 PHE C 241     -64.792   5.909  31.555  1.00 44.59           C  
ANISOU 6786  CD1 PHE C 241     3397   4817   8727   -120   -747   -419       C  
ATOM   6787  CD2 PHE C 241     -65.787   4.023  30.509  1.00 44.89           C  
ANISOU 6787  CD2 PHE C 241     3444   4880   8731   -166   -722   -428       C  
ATOM   6788  CE1 PHE C 241     -64.397   6.383  30.313  1.00 44.39           C  
ANISOU 6788  CE1 PHE C 241     3387   4763   8716    -84   -790   -381       C  
ATOM   6789  CE2 PHE C 241     -65.410   4.513  29.268  1.00 44.76           C  
ANISOU 6789  CE2 PHE C 241     3435   4841   8729   -125   -770   -392       C  
ATOM   6790  CZ  PHE C 241     -64.706   5.691  29.172  1.00 44.22           C  
ANISOU 6790  CZ  PHE C 241     3374   4744   8683    -85   -803   -365       C  
ATOM   6791  N   VAL C 242     -66.801   6.706  34.449  1.00 48.55           N  
ANISOU 6791  N   VAL C 242     3783   5403   9260   -162   -689   -581       N  
ATOM   6792  CA  VAL C 242     -66.428   8.147  34.497  1.00 49.11           C  
ANISOU 6792  CA  VAL C 242     3833   5449   9374   -113   -729   -585       C  
ATOM   6793  C   VAL C 242     -64.976   8.236  34.962  1.00 48.52           C  
ANISOU 6793  C   VAL C 242     3807   5352   9276   -112   -718   -534       C  
ATOM   6794  O   VAL C 242     -64.582   7.445  35.848  1.00 49.21           O  
ANISOU 6794  O   VAL C 242     3918   5461   9316   -144   -676   -525       O  
ATOM   6795  CB  VAL C 242     -67.367   8.980  35.396  1.00 49.96           C  
ANISOU 6795  CB  VAL C 242     3875   5589   9516   -107   -728   -665       C  
ATOM   6796  CG1 VAL C 242     -68.737   9.158  34.768  1.00 50.51           C  
ANISOU 6796  CG1 VAL C 242     3889   5684   9617    -89   -754   -723       C  
ATOM   6797  CG2 VAL C 242     -67.483   8.409  36.804  1.00 50.12           C  
ANISOU 6797  CG2 VAL C 242     3888   5652   9501   -156   -672   -696       C  
ATOM   6798  N   MET C 243     -64.238   9.184  34.382  1.00 48.72           N  
ANISOU 6798  N   MET C 243     3845   5336   9328    -76   -754   -505       N  
ATOM   6799  CA  MET C 243     -62.854   9.553  34.763  1.00 48.31           C  
ANISOU 6799  CA  MET C 243     3823   5266   9265    -73   -748   -473       C  
ATOM   6800  C   MET C 243     -62.891  10.873  35.528  1.00 49.10           C  
ANISOU 6800  C   MET C 243     3886   5361   9408    -56   -756   -519       C  
ATOM   6801  O   MET C 243     -63.397  11.855  34.971  1.00 48.89           O  
ANISOU 6801  O   MET C 243     3842   5303   9432    -24   -789   -536       O  
ATOM   6802  CB  MET C 243     -61.991   9.717  33.513  1.00 47.63           C  
ANISOU 6802  CB  MET C 243     3778   5137   9180    -55   -775   -414       C  
ATOM   6803  CG  MET C 243     -60.521   9.823  33.808  1.00 47.11           C  
ANISOU 6803  CG  MET C 243     3742   5065   9092    -60   -764   -385       C  
ATOM   6804  SD  MET C 243     -59.602   9.818  32.269  1.00 46.94           S  
ANISOU 6804  SD  MET C 243     3768   5002   9064    -50   -788   -320       S  
ATOM   6805  CE  MET C 243     -57.937   9.977  32.923  1.00 48.07           C  
ANISOU 6805  CE  MET C 243     3926   5157   9179    -61   -768   -313       C  
ATOM   6806  N   MET C 244     -62.380  10.868  36.760  1.00 50.85           N  
ANISOU 6806  N   MET C 244     4099   5613   9608    -72   -727   -541       N  
ATOM   6807  CA  MET C 244     -62.248  12.063  37.628  1.00 51.98           C  
ANISOU 6807  CA  MET C 244     4205   5755   9787    -61   -728   -590       C  
ATOM   6808  C   MET C 244     -60.761  12.397  37.784  1.00 52.13           C  
ANISOU 6808  C   MET C 244     4250   5763   9793    -62   -722   -566       C  
ATOM   6809  O   MET C 244     -60.058  11.685  38.508  1.00 51.03           O  
ANISOU 6809  O   MET C 244     4124   5664   9601    -76   -697   -558       O  
ATOM   6810  CB  MET C 244     -62.882  11.816  38.999  1.00 52.92           C  
ANISOU 6810  CB  MET C 244     4285   5933   9888    -81   -696   -647       C  
ATOM   6811  CG  MET C 244     -64.351  11.428  38.932  1.00 54.32           C  
ANISOU 6811  CG  MET C 244     4430   6134  10075    -91   -693   -684       C  
ATOM   6812  SD  MET C 244     -65.370  12.579  37.942  1.00 55.48           S  
ANISOU 6812  SD  MET C 244     4539   6241  10298    -46   -745   -717       S  
ATOM   6813  CE  MET C 244     -65.331  14.032  38.991  1.00 55.82           C  
ANISOU 6813  CE  MET C 244     4535   6282  10390    -26   -750   -784       C  
ATOM   6814  N   SER C 245     -60.310  13.449  37.105  1.00 53.84           N  
ANISOU 6814  N   SER C 245     4475   5926  10054    -45   -745   -557       N  
ATOM   6815  CA  SER C 245     -58.922  13.971  37.172  1.00 54.54           C  
ANISOU 6815  CA  SER C 245     4581   6001  10141    -53   -738   -548       C  
ATOM   6816  C   SER C 245     -58.882  15.243  38.022  1.00 54.43           C  
ANISOU 6816  C   SER C 245     4527   5978  10172    -50   -732   -611       C  
ATOM   6817  O   SER C 245     -59.903  15.955  38.066  1.00 54.38           O  
ANISOU 6817  O   SER C 245     4496   5949  10216    -32   -748   -646       O  
ATOM   6818  CB  SER C 245     -58.382  14.230  35.791  1.00 55.20           C  
ANISOU 6818  CB  SER C 245     4708   6027  10237    -48   -757   -495       C  
ATOM   6819  OG  SER C 245     -58.814  13.232  34.875  1.00 55.85           O  
ANISOU 6819  OG  SER C 245     4817   6110  10293    -43   -769   -447       O  
ATOM   6820  N   ALA C 246     -57.741  15.500  38.665  1.00 53.27           N  
ANISOU 6820  N   ALA C 246     4373   5854  10010    -65   -713   -630       N  
ATOM   6821  CA  ALA C 246     -57.431  16.725  39.441  1.00 53.78           C  
ANISOU 6821  CA  ALA C 246     4403   5912  10118    -70   -703   -694       C  
ATOM   6822  C   ALA C 246     -55.914  16.844  39.567  1.00 54.27           C  
ANISOU 6822  C   ALA C 246     4472   5991  10156    -91   -684   -697       C  
ATOM   6823  O   ALA C 246     -55.226  15.828  39.638  1.00 54.97           O  
ANISOU 6823  O   ALA C 246     4573   6129  10181    -94   -676   -669       O  
ATOM   6824  CB  ALA C 246     -58.089  16.653  40.793  1.00 52.86           C  
ANISOU 6824  CB  ALA C 246     4234   5855   9992    -68   -689   -754       C  
ATOM   6825  N   PRO C 247     -55.325  18.061  39.590  1.00 54.03           N  
ANISOU 6825  N   PRO C 247     4433   5922  10174   -106   -675   -734       N  
ATOM   6826  CA  PRO C 247     -53.894  18.199  39.858  1.00 53.64           C  
ANISOU 6826  CA  PRO C 247     4374   5904  10100   -131   -652   -757       C  
ATOM   6827  C   PRO C 247     -53.451  17.300  41.013  1.00 52.75           C  
ANISOU 6827  C   PRO C 247     4228   5896   9917   -124   -641   -784       C  
ATOM   6828  O   PRO C 247     -54.105  17.254  42.058  1.00 52.52           O  
ANISOU 6828  O   PRO C 247     4162   5909   9882   -112   -637   -824       O  
ATOM   6829  CB  PRO C 247     -53.755  19.690  40.171  1.00 54.62           C  
ANISOU 6829  CB  PRO C 247     4477   5981  10293   -149   -638   -820       C  
ATOM   6830  CG  PRO C 247     -54.799  20.313  39.281  1.00 55.43           C  
ANISOU 6830  CG  PRO C 247     4617   5988  10455   -131   -661   -788       C  
ATOM   6831  CD  PRO C 247     -55.978  19.354  39.335  1.00 54.88           C  
ANISOU 6831  CD  PRO C 247     4540   5950  10358    -98   -684   -760       C  
ATOM   6832  N   PRO C 248     -52.341  16.541  40.846  1.00 51.44           N  
ANISOU 6832  N   PRO C 248     4075   5776   9692   -127   -635   -763       N  
ATOM   6833  CA  PRO C 248     -51.941  15.523  41.816  1.00 50.88           C  
ANISOU 6833  CA  PRO C 248     3987   5800   9542   -106   -630   -774       C  
ATOM   6834  C   PRO C 248     -51.999  16.074  43.237  1.00 50.81           C  
ANISOU 6834  C   PRO C 248     3921   5848   9534   -104   -616   -854       C  
ATOM   6835  O   PRO C 248     -51.508  17.156  43.453  1.00 51.35           O  
ANISOU 6835  O   PRO C 248     3955   5907   9645   -125   -604   -913       O  
ATOM   6836  CB  PRO C 248     -50.496  15.179  41.429  1.00 51.03           C  
ANISOU 6836  CB  PRO C 248     4015   5855   9518   -111   -627   -770       C  
ATOM   6837  CG  PRO C 248     -50.441  15.465  39.939  1.00 51.11           C  
ANISOU 6837  CG  PRO C 248     4067   5782   9569   -133   -634   -719       C  
ATOM   6838  CD  PRO C 248     -51.409  16.614  39.707  1.00 51.43           C  
ANISOU 6838  CD  PRO C 248     4107   5741   9692   -147   -635   -729       C  
ATOM   6839  N   ALA C 249     -52.604  15.322  44.149  1.00 50.37           N  
ANISOU 6839  N   ALA C 249     3859   5848   9430    -82   -614   -855       N  
ATOM   6840  CA  ALA C 249     -52.800  15.733  45.553  1.00 51.36           C  
ANISOU 6840  CA  ALA C 249     3931   6036   9547    -76   -601   -928       C  
ATOM   6841  C   ALA C 249     -52.918  14.484  46.425  1.00 51.75           C  
ANISOU 6841  C   ALA C 249     3996   6163   9503    -48   -596   -908       C  
ATOM   6842  O   ALA C 249     -53.473  13.491  45.944  1.00 51.86           O  
ANISOU 6842  O   ALA C 249     4060   6154   9488    -42   -600   -841       O  
ATOM   6843  CB  ALA C 249     -54.021  16.621  45.646  1.00 51.19           C  
ANISOU 6843  CB  ALA C 249     3885   5962   9600    -89   -601   -957       C  
ATOM   6844  N   GLN C 250     -52.420  14.551  47.661  1.00 52.83           N  
ANISOU 6844  N   GLN C 250     4093   6385   9592    -33   -585   -966       N  
ATOM   6845  CA  GLN C 250     -52.634  13.529  48.719  1.00 54.08           C  
ANISOU 6845  CA  GLN C 250     4268   6619   9659     -4   -576   -956       C  
ATOM   6846  C   GLN C 250     -54.127  13.182  48.782  1.00 55.17           C  
ANISOU 6846  C   GLN C 250     4426   6724   9812    -19   -565   -928       C  
ATOM   6847  O   GLN C 250     -54.963  14.119  48.896  1.00 55.99           O  
ANISOU 6847  O   GLN C 250     4486   6799   9987    -42   -562   -973       O  
ATOM   6848  CB  GLN C 250     -52.144  14.060  50.074  1.00 54.75           C  
ANISOU 6848  CB  GLN C 250     4292   6796   9714      9   -566  -1041       C  
ATOM   6849  CG  GLN C 250     -50.655  13.867  50.306  1.00 55.30           C  
ANISOU 6849  CG  GLN C 250     4349   6937   9723     40   -575  -1066       C  
ATOM   6850  CD  GLN C 250     -50.305  12.401  50.236  1.00 55.50           C  
ANISOU 6850  CD  GLN C 250     4444   6991   9650     84   -583   -995       C  
ATOM   6851  OE1 GLN C 250     -50.983  11.578  50.843  1.00 55.30           O  
ANISOU 6851  OE1 GLN C 250     4459   6985   9567    101   -573   -960       O  
ATOM   6852  NE2 GLN C 250     -49.303  12.063  49.433  1.00 55.12           N  
ANISOU 6852  NE2 GLN C 250     4416   6938   9587     99   -599   -971       N  
ATOM   6853  N   TYR C 251     -54.457  11.893  48.689  1.00 55.49           N  
ANISOU 6853  N   TYR C 251     4529   6766   9787     -8   -559   -862       N  
ATOM   6854  CA  TYR C 251     -55.851  11.388  48.672  1.00 56.20           C  
ANISOU 6854  CA  TYR C 251     4642   6828   9883    -31   -543   -835       C  
ATOM   6855  C   TYR C 251     -55.868   9.941  49.168  1.00 56.82           C  
ANISOU 6855  C   TYR C 251     4788   6941   9859    -15   -523   -783       C  
ATOM   6856  O   TYR C 251     -54.962   9.176  48.779  1.00 56.31           O  
ANISOU 6856  O   TYR C 251     4774   6877   9743     13   -533   -735       O  
ATOM   6857  CB  TYR C 251     -56.435  11.528  47.264  1.00 56.02           C  
ANISOU 6857  CB  TYR C 251     4635   6716   9933    -52   -559   -797       C  
ATOM   6858  CG  TYR C 251     -57.899  11.197  47.139  1.00 56.09           C  
ANISOU 6858  CG  TYR C 251     4650   6699   9961    -77   -545   -788       C  
ATOM   6859  CD1 TYR C 251     -58.792  11.481  48.161  1.00 57.47           C  
ANISOU 6859  CD1 TYR C 251     4784   6915  10137    -93   -524   -843       C  
ATOM   6860  CD2 TYR C 251     -58.402  10.635  45.979  1.00 56.12           C  
ANISOU 6860  CD2 TYR C 251     4693   6645   9984    -88   -554   -733       C  
ATOM   6861  CE1 TYR C 251     -60.143  11.196  48.040  1.00 58.04           C  
ANISOU 6861  CE1 TYR C 251     4853   6972  10227   -120   -509   -846       C  
ATOM   6862  CE2 TYR C 251     -59.748  10.341  45.841  1.00 56.83           C  
ANISOU 6862  CE2 TYR C 251     4779   6720  10092   -114   -541   -737       C  
ATOM   6863  CZ  TYR C 251     -60.622  10.623  46.875  1.00 57.30           C  
ANISOU 6863  CZ  TYR C 251     4795   6822  10152   -131   -518   -796       C  
ATOM   6864  OH  TYR C 251     -61.947  10.331  46.765  1.00 57.00           O  
ANISOU 6864  OH  TYR C 251     4746   6780  10130   -160   -502   -810       O  
ATOM   6865  N   GLU C 252     -56.866   9.598  49.993  1.00 57.66           N  
ANISOU 6865  N   GLU C 252     4898   7073   9936    -34   -493   -795       N  
ATOM   6866  CA  GLU C 252     -57.050   8.256  50.610  1.00 57.08           C  
ANISOU 6866  CA  GLU C 252     4898   7026   9762    -28   -462   -748       C  
ATOM   6867  C   GLU C 252     -57.998   7.447  49.722  1.00 55.34           C  
ANISOU 6867  C   GLU C 252     4728   6739   9558    -63   -447   -694       C  
ATOM   6868  O   GLU C 252     -59.117   7.906  49.509  1.00 56.20           O  
ANISOU 6868  O   GLU C 252     4796   6825   9729   -102   -439   -725       O  
ATOM   6869  CB  GLU C 252     -57.588   8.424  52.032  1.00 58.04           C  
ANISOU 6869  CB  GLU C 252     4993   7217   9842    -37   -431   -799       C  
ATOM   6870  CG  GLU C 252     -57.854   7.111  52.749  1.00 59.35           C  
ANISOU 6870  CG  GLU C 252     5242   7407   9900    -36   -392   -751       C  
ATOM   6871  CD  GLU C 252     -58.111   7.275  54.247  1.00 60.54           C  
ANISOU 6871  CD  GLU C 252     5371   7640   9990    -36   -362   -799       C  
ATOM   6872  OE1 GLU C 252     -58.915   8.164  54.622  1.00 60.12           O  
ANISOU 6872  OE1 GLU C 252     5242   7606   9994    -71   -353   -868       O  
ATOM   6873  OE2 GLU C 252     -57.502   6.519  55.054  1.00 60.97           O  
ANISOU 6873  OE2 GLU C 252     5486   7742   9936      2   -350   -771       O  
ATOM   6874  N   LEU C 253     -57.536   6.321  49.177  1.00 54.08           N  
ANISOU 6874  N   LEU C 253     4649   6550   9348    -46   -447   -623       N  
ATOM   6875  CA  LEU C 253     -58.358   5.383  48.367  1.00 53.39           C  
ANISOU 6875  CA  LEU C 253     4616   6402   9264    -81   -428   -573       C  
ATOM   6876  C   LEU C 253     -58.896   4.287  49.287  1.00 53.99           C  
ANISOU 6876  C   LEU C 253     4761   6498   9253    -98   -377   -549       C  
ATOM   6877  O   LEU C 253     -58.092   3.583  49.923  1.00 53.05           O  
ANISOU 6877  O   LEU C 253     4705   6406   9044    -57   -370   -516       O  
ATOM   6878  CB  LEU C 253     -57.534   4.796  47.216  1.00 52.60           C  
ANISOU 6878  CB  LEU C 253     4566   6256   9162    -54   -455   -513       C  
ATOM   6879  CG  LEU C 253     -57.207   5.772  46.083  1.00 51.76           C  
ANISOU 6879  CG  LEU C 253     4405   6115   9144    -52   -498   -526       C  
ATOM   6880  CD1 LEU C 253     -56.338   5.106  45.021  1.00 50.92           C  
ANISOU 6880  CD1 LEU C 253     4349   5973   9023    -27   -520   -469       C  
ATOM   6881  CD2 LEU C 253     -58.481   6.340  45.463  1.00 51.59           C  
ANISOU 6881  CD2 LEU C 253     4340   6055   9206    -96   -497   -550       C  
ATOM   6882  N   LYS C 254     -60.225   4.191  49.369  1.00 55.44           N  
ANISOU 6882  N   LYS C 254     4931   6670   9461   -157   -341   -571       N  
ATOM   6883  CA  LYS C 254     -60.939   3.147  50.143  1.00 55.68           C  
ANISOU 6883  CA  LYS C 254     5029   6710   9416   -195   -279   -553       C  
ATOM   6884  C   LYS C 254     -61.323   2.025  49.175  1.00 55.31           C  
ANISOU 6884  C   LYS C 254     5054   6593   9365   -225   -260   -497       C  
ATOM   6885  O   LYS C 254     -61.826   2.324  48.071  1.00 54.90           O  
ANISOU 6885  O   LYS C 254     4961   6503   9392   -248   -280   -508       O  
ATOM   6886  CB  LYS C 254     -62.152   3.723  50.879  1.00 56.05           C  
ANISOU 6886  CB  LYS C 254     5011   6798   9489   -249   -246   -624       C  
ATOM   6887  CG  LYS C 254     -62.299   3.205  52.307  1.00 57.80           C  
ANISOU 6887  CG  LYS C 254     5278   7072   9612   -260   -193   -627       C  
ATOM   6888  CD  LYS C 254     -63.743   3.119  52.830  1.00 59.10           C  
ANISOU 6888  CD  LYS C 254     5416   7257   9778   -339   -134   -676       C  
ATOM   6889  CE  LYS C 254     -63.945   2.025  53.866  1.00 59.67           C  
ANISOU 6889  CE  LYS C 254     5586   7347   9735   -367    -64   -642       C  
ATOM   6890  NZ  LYS C 254     -64.721   2.506  55.035  1.00 60.34           N  
ANISOU 6890  NZ  LYS C 254     5619   7505   9801   -408    -23   -712       N  
ATOM   6891  N   HIS C 255     -61.051   0.787  49.583  1.00 55.14           N  
ANISOU 6891  N   HIS C 255     5142   6557   9251   -219   -223   -439       N  
ATOM   6892  CA  HIS C 255     -61.324  -0.462  48.826  1.00 54.62           C  
ANISOU 6892  CA  HIS C 255     5165   6423   9166   -246   -194   -383       C  
ATOM   6893  C   HIS C 255     -62.772  -0.477  48.310  1.00 53.87           C  
ANISOU 6893  C   HIS C 255     5029   6305   9132   -331   -160   -422       C  
ATOM   6894  O   HIS C 255     -63.707  -0.219  49.100  1.00 53.80           O  
ANISOU 6894  O   HIS C 255     4985   6335   9120   -382   -119   -473       O  
ATOM   6895  CB  HIS C 255     -60.983  -1.669  49.710  1.00 55.78           C  
ANISOU 6895  CB  HIS C 255     5437   6561   9194   -232   -148   -327       C  
ATOM   6896  CG  HIS C 255     -61.453  -2.964  49.151  1.00 56.43           C  
ANISOU 6896  CG  HIS C 255     5617   6570   9253   -275   -102   -279       C  
ATOM   6897  ND1 HIS C 255     -62.224  -3.836  49.884  1.00 58.25           N  
ANISOU 6897  ND1 HIS C 255     5928   6785   9418   -334    -23   -266       N  
ATOM   6898  CD2 HIS C 255     -61.298  -3.520  47.933  1.00 56.28           C  
ANISOU 6898  CD2 HIS C 255     5627   6489   9267   -275   -118   -244       C  
ATOM   6899  CE1 HIS C 255     -62.515  -4.889  49.146  1.00 58.33           C  
ANISOU 6899  CE1 HIS C 255     6014   6721   9424   -369      8   -228       C  
ATOM   6900  NE2 HIS C 255     -61.956  -4.718  47.945  1.00 57.04           N  
ANISOU 6900  NE2 HIS C 255     5819   6531   9322   -331    -51   -215       N  
ATOM   6901  N   GLY C 256     -62.935  -0.734  47.010  1.00 52.37           N  
ANISOU 6901  N   GLY C 256     4837   6064   8996   -343   -180   -405       N  
ATOM   6902  CA  GLY C 256     -64.225  -1.046  46.364  1.00 51.33           C  
ANISOU 6902  CA  GLY C 256     4683   5908   8910   -418   -146   -436       C  
ATOM   6903  C   GLY C 256     -65.137   0.161  46.226  1.00 49.99           C  
ANISOU 6903  C   GLY C 256     4390   5779   8825   -442   -167   -518       C  
ATOM   6904  O   GLY C 256     -66.319  -0.066  45.955  1.00 50.74           O  
ANISOU 6904  O   GLY C 256     4456   5874   8948   -506   -133   -560       O  
ATOM   6905  N   THR C 257     -64.613   1.385  46.371  1.00 48.31           N  
ANISOU 6905  N   THR C 257     4105   5596   8652   -391   -221   -543       N  
ATOM   6906  CA  THR C 257     -65.325   2.677  46.138  1.00 46.87           C  
ANISOU 6906  CA  THR C 257     3809   5442   8557   -394   -254   -618       C  
ATOM   6907  C   THR C 257     -64.935   3.269  44.776  1.00 44.72           C  
ANISOU 6907  C   THR C 257     3503   5131   8357   -354   -319   -602       C  
ATOM   6908  O   THR C 257     -65.353   4.396  44.470  1.00 43.40           O  
ANISOU 6908  O   THR C 257     3253   4974   8261   -341   -356   -653       O  
ATOM   6909  CB  THR C 257     -64.992   3.690  47.239  1.00 47.39           C  
ANISOU 6909  CB  THR C 257     3822   5561   8620   -366   -266   -659       C  
ATOM   6910  OG1 THR C 257     -63.598   3.999  47.140  1.00 46.90           O  
ANISOU 6910  OG1 THR C 257     3781   5490   8546   -302   -309   -618       O  
ATOM   6911  CG2 THR C 257     -65.320   3.182  48.627  1.00 48.11           C  
ANISOU 6911  CG2 THR C 257     3946   5699   8634   -401   -203   -674       C  
ATOM   6912  N   PHE C 258     -64.126   2.539  44.007  1.00 43.19           N  
ANISOU 6912  N   PHE C 258     3377   4893   8140   -332   -333   -534       N  
ATOM   6913  CA  PHE C 258     -63.611   2.942  42.676  1.00 41.73           C  
ANISOU 6913  CA  PHE C 258     3176   4669   8008   -296   -390   -508       C  
ATOM   6914  C   PHE C 258     -63.145   1.680  41.952  1.00 40.76           C  
ANISOU 6914  C   PHE C 258     3137   4503   7844   -297   -380   -443       C  
ATOM   6915  O   PHE C 258     -63.013   0.639  42.618  1.00 40.10           O  
ANISOU 6915  O   PHE C 258     3129   4417   7690   -313   -334   -414       O  
ATOM   6916  CB  PHE C 258     -62.486   3.971  42.831  1.00 41.35           C  
ANISOU 6916  CB  PHE C 258     3101   4631   7977   -240   -435   -505       C  
ATOM   6917  CG  PHE C 258     -61.204   3.416  43.404  1.00 41.07           C  
ANISOU 6917  CG  PHE C 258     3130   4606   7869   -205   -430   -459       C  
ATOM   6918  CD1 PHE C 258     -60.128   3.127  42.580  1.00 40.28           C  
ANISOU 6918  CD1 PHE C 258     3067   4476   7759   -169   -461   -409       C  
ATOM   6919  CD2 PHE C 258     -61.092   3.150  44.762  1.00 41.42           C  
ANISOU 6919  CD2 PHE C 258     3196   4691   7848   -206   -396   -469       C  
ATOM   6920  CE1 PHE C 258     -58.970   2.581  43.104  1.00 40.49           C  
ANISOU 6920  CE1 PHE C 258     3148   4519   7715   -129   -461   -374       C  
ATOM   6921  CE2 PHE C 258     -59.930   2.604  45.283  1.00 41.48           C  
ANISOU 6921  CE2 PHE C 258     3265   4713   7781   -163   -396   -429       C  
ATOM   6922  CZ  PHE C 258     -58.871   2.326  44.454  1.00 40.90           C  
ANISOU 6922  CZ  PHE C 258     3223   4613   7701   -122   -430   -385       C  
ATOM   6923  N   THR C 259     -62.934   1.780  40.641  1.00 40.34           N  
ANISOU 6923  N   THR C 259     3075   4416   7833   -280   -420   -421       N  
ATOM   6924  CA  THR C 259     -62.387   0.694  39.789  1.00 40.85           C  
ANISOU 6924  CA  THR C 259     3212   4440   7869   -274   -419   -362       C  
ATOM   6925  C   THR C 259     -60.855   0.701  39.909  1.00 41.00           C  
ANISOU 6925  C   THR C 259     3270   4457   7850   -217   -447   -316       C  
ATOM   6926  O   THR C 259     -60.302  -0.183  40.590  1.00 41.18           O  
ANISOU 6926  O   THR C 259     3364   4479   7801   -205   -420   -284       O  
ATOM   6927  CB  THR C 259     -62.819   0.858  38.329  1.00 40.63           C  
ANISOU 6927  CB  THR C 259     3151   4387   7899   -278   -452   -364       C  
ATOM   6928  OG1 THR C 259     -64.241   0.897  38.282  1.00 42.05           O  
ANISOU 6928  OG1 THR C 259     3284   4582   8111   -326   -430   -419       O  
ATOM   6929  CG2 THR C 259     -62.304  -0.257  37.451  1.00 40.41           C  
ANISOU 6929  CG2 THR C 259     3190   4320   7841   -275   -451   -311       C  
ATOM   6930  N   CYS C 260     -60.209   1.680  39.273  1.00 40.65           N  
ANISOU 6930  N   CYS C 260     3181   4413   7851   -182   -497   -317       N  
ATOM   6931  CA  CYS C 260     -58.750   1.894  39.288  1.00 40.63           C  
ANISOU 6931  CA  CYS C 260     3194   4418   7823   -132   -526   -291       C  
ATOM   6932  C   CYS C 260     -58.451   3.394  39.367  1.00 41.28           C  
ANISOU 6932  C   CYS C 260     3206   4520   7960   -115   -559   -328       C  
ATOM   6933  O   CYS C 260     -59.360   4.207  39.123  1.00 41.80           O  
ANISOU 6933  O   CYS C 260     3216   4577   8085   -135   -567   -363       O  
ATOM   6934  CB  CYS C 260     -58.110   1.274  38.056  1.00 40.15           C  
ANISOU 6934  CB  CYS C 260     3172   4324   7758   -116   -549   -245       C  
ATOM   6935  SG  CYS C 260     -58.643   2.019  36.492  1.00 39.12           S  
ANISOU 6935  SG  CYS C 260     2990   4163   7709   -129   -586   -251       S  
ATOM   6936  N   ALA C 261     -57.210   3.729  39.711  1.00 42.07           N  
ANISOU 6936  N   ALA C 261     3306   4643   8036    -79   -576   -325       N  
ATOM   6937  CA  ALA C 261     -56.697   5.107  39.874  1.00 42.39           C  
ANISOU 6937  CA  ALA C 261     3286   4700   8120    -66   -600   -363       C  
ATOM   6938  C   ALA C 261     -55.334   5.226  39.180  1.00 42.76           C  
ANISOU 6938  C   ALA C 261     3342   4745   8158    -38   -627   -341       C  
ATOM   6939  O   ALA C 261     -54.794   4.195  38.692  1.00 43.23           O  
ANISOU 6939  O   ALA C 261     3453   4797   8173    -23   -629   -299       O  
ATOM   6940  CB  ALA C 261     -56.598   5.439  41.342  1.00 42.76           C  
ANISOU 6940  CB  ALA C 261     3311   4798   8137    -58   -581   -404       C  
ATOM   6941  N   SER C 262     -54.821   6.451  39.112  1.00 42.54           N  
ANISOU 6941  N   SER C 262     3266   4721   8174    -36   -644   -374       N  
ATOM   6942  CA  SER C 262     -53.485   6.788  38.578  1.00 42.15           C  
ANISOU 6942  CA  SER C 262     3213   4680   8122    -19   -664   -370       C  
ATOM   6943  C   SER C 262     -52.779   7.676  39.616  1.00 42.65           C  
ANISOU 6943  C   SER C 262     3230   4791   8183    -10   -660   -427       C  
ATOM   6944  O   SER C 262     -53.319   8.749  39.959  1.00 41.18           O  
ANISOU 6944  O   SER C 262     3000   4595   8051    -28   -657   -468       O  
ATOM   6945  CB  SER C 262     -53.609   7.423  37.216  1.00 41.57           C  
ANISOU 6945  CB  SER C 262     3132   4553   8108    -38   -683   -353       C  
ATOM   6946  OG  SER C 262     -53.777   8.830  37.335  1.00 41.90           O  
ANISOU 6946  OG  SER C 262     3129   4579   8213    -52   -687   -393       O  
ATOM   6947  N   GLU C 263     -51.658   7.185  40.155  1.00 43.31           N  
ANISOU 6947  N   GLU C 263     3323   4929   8201     21   -660   -435       N  
ATOM   6948  CA  GLU C 263     -50.799   7.904  41.130  1.00 44.20           C  
ANISOU 6948  CA  GLU C 263     3389   5104   8300     36   -658   -497       C  
ATOM   6949  C   GLU C 263     -49.692   8.635  40.371  1.00 43.99           C  
ANISOU 6949  C   GLU C 263     3333   5077   8302     25   -671   -518       C  
ATOM   6950  O   GLU C 263     -49.272   8.116  39.328  1.00 43.36           O  
ANISOU 6950  O   GLU C 263     3285   4976   8213     27   -682   -478       O  
ATOM   6951  CB  GLU C 263     -50.172   6.921  42.114  1.00 44.77           C  
ANISOU 6951  CB  GLU C 263     3487   5244   8278     84   -656   -497       C  
ATOM   6952  CG  GLU C 263     -49.502   7.598  43.287  1.00 45.26           C  
ANISOU 6952  CG  GLU C 263     3496   5381   8318    103   -653   -567       C  
ATOM   6953  CD  GLU C 263     -48.395   6.777  43.896  1.00 46.11           C  
ANISOU 6953  CD  GLU C 263     3623   5565   8331    164   -663   -574       C  
ATOM   6954  OE1 GLU C 263     -47.393   6.520  43.194  1.00 46.08           O  
ANISOU 6954  OE1 GLU C 263     3623   5573   8310    183   -681   -570       O  
ATOM   6955  OE2 GLU C 263     -48.540   6.416  45.069  1.00 47.31           O  
ANISOU 6955  OE2 GLU C 263     3786   5766   8424    196   -654   -586       O  
ATOM   6956  N   TYR C 264     -49.255   9.792  40.877  1.00 44.56           N  
ANISOU 6956  N   TYR C 264     3350   5174   8407     11   -664   -583       N  
ATOM   6957  CA  TYR C 264     -48.186  10.624  40.271  1.00 45.65           C  
ANISOU 6957  CA  TYR C 264     3456   5314   8574    -11   -665   -616       C  
ATOM   6958  C   TYR C 264     -47.335  11.262  41.371  1.00 47.73           C  
ANISOU 6958  C   TYR C 264     3660   5654   8821     -4   -656   -700       C  
ATOM   6959  O   TYR C 264     -47.807  12.225  42.011  1.00 49.02           O  
ANISOU 6959  O   TYR C 264     3785   5809   9030    -25   -643   -746       O  
ATOM   6960  CB  TYR C 264     -48.773  11.709  39.370  1.00 45.05           C  
ANISOU 6960  CB  TYR C 264     3377   5151   8586    -57   -661   -608       C  
ATOM   6961  CG  TYR C 264     -47.786  12.291  38.394  1.00 44.94           C  
ANISOU 6961  CG  TYR C 264     3359   5119   8596    -88   -657   -616       C  
ATOM   6962  CD1 TYR C 264     -47.038  13.422  38.694  1.00 45.78           C  
ANISOU 6962  CD1 TYR C 264     3420   5239   8733   -119   -639   -685       C  
ATOM   6963  CD2 TYR C 264     -47.595  11.697  37.164  1.00 44.71           C  
ANISOU 6963  CD2 TYR C 264     3372   5059   8555    -91   -668   -558       C  
ATOM   6964  CE1 TYR C 264     -46.133  13.951  37.788  1.00 46.17           C  
ANISOU 6964  CE1 TYR C 264     3470   5271   8802   -157   -627   -695       C  
ATOM   6965  CE2 TYR C 264     -46.688  12.208  36.253  1.00 45.30           C  
ANISOU 6965  CE2 TYR C 264     3444   5119   8645   -124   -660   -566       C  
ATOM   6966  CZ  TYR C 264     -45.953  13.334  36.560  1.00 45.71           C  
ANISOU 6966  CZ  TYR C 264     3454   5183   8727   -160   -637   -634       C  
ATOM   6967  OH  TYR C 264     -45.073  13.781  35.615  1.00 45.46           O  
ANISOU 6967  OH  TYR C 264     3427   5137   8708   -202   -623   -640       O  
ATOM   6968  N   THR C 265     -46.132  10.723  41.587  1.00 49.06           N  
ANISOU 6968  N   THR C 265     3817   5898   8922     28   -663   -725       N  
ATOM   6969  CA  THR C 265     -45.075  11.314  42.444  1.00 50.80           C  
ANISOU 6969  CA  THR C 265     3973   6207   9122     35   -657   -816       C  
ATOM   6970  C   THR C 265     -44.125  12.077  41.527  1.00 51.79           C  
ANISOU 6970  C   THR C 265     4070   6320   9287    -10   -647   -851       C  
ATOM   6971  O   THR C 265     -44.180  11.798  40.314  1.00 51.54           O  
ANISOU 6971  O   THR C 265     4080   6230   9273    -29   -652   -793       O  
ATOM   6972  CB  THR C 265     -44.331  10.241  43.246  1.00 51.74           C  
ANISOU 6972  CB  THR C 265     4096   6425   9137    107   -674   -829       C  
ATOM   6973  OG1 THR C 265     -45.314   9.332  43.739  1.00 51.71           O  
ANISOU 6973  OG1 THR C 265     4147   6403   9095    141   -679   -769       O  
ATOM   6974  CG2 THR C 265     -43.524  10.821  44.391  1.00 52.57           C  
ANISOU 6974  CG2 THR C 265     4129   6631   9214    125   -670   -928       C  
ATOM   6975  N   GLY C 266     -43.310  12.989  42.079  1.00 53.12           N  
ANISOU 6975  N   GLY C 266     4170   6543   9467    -32   -631   -944       N  
ATOM   6976  CA  GLY C 266     -42.315  13.782  41.326  1.00 54.35           C  
ANISOU 6976  CA  GLY C 266     4294   6696   9658    -87   -611   -993       C  
ATOM   6977  C   GLY C 266     -42.955  15.022  40.724  1.00 55.06           C  
ANISOU 6977  C   GLY C 266     4395   6677   9847   -158   -585   -985       C  
ATOM   6978  O   GLY C 266     -44.213  15.090  40.723  1.00 57.15           O  
ANISOU 6978  O   GLY C 266     4696   6869  10149   -154   -591   -931       O  
ATOM   6979  N   ASN C 267     -42.155  15.962  40.207  1.00 55.13           N  
ANISOU 6979  N   ASN C 267     4377   6671   9895   -221   -555  -1037       N  
ATOM   6980  CA  ASN C 267     -42.634  17.360  40.022  1.00 55.59           C  
ANISOU 6980  CA  ASN C 267     4439   6637  10046   -284   -524  -1057       C  
ATOM   6981  C   ASN C 267     -42.495  17.844  38.580  1.00 55.44           C  
ANISOU 6981  C   ASN C 267     4470   6524  10071   -342   -504  -1012       C  
ATOM   6982  O   ASN C 267     -43.492  18.413  38.079  1.00 59.33           O  
ANISOU 6982  O   ASN C 267     5011   6906  10624   -358   -503   -958       O  
ATOM   6983  CB  ASN C 267     -41.951  18.329  40.988  1.00 55.88           C  
ANISOU 6983  CB  ASN C 267     4399   6730  10100   -316   -493  -1176       C  
ATOM   6984  CG  ASN C 267     -42.610  18.311  42.344  1.00 55.28           C  
ANISOU 6984  CG  ASN C 267     4289   6699  10015   -272   -507  -1209       C  
ATOM   6985  OD1 ASN C 267     -43.590  17.591  42.525  1.00 54.60           O  
ANISOU 6985  OD1 ASN C 267     4239   6596   9909   -223   -535  -1140       O  
ATOM   6986  ND2 ASN C 267     -42.056  19.044  43.292  1.00 55.70           N  
ANISOU 6986  ND2 ASN C 267     4271   6816  10076   -290   -485  -1316       N  
ATOM   6987  N   TYR C 268     -41.327  17.704  37.967  1.00 52.99           N  
ANISOU 6987  N   TYR C 268     4146   6255   9731   -373   -488  -1038       N  
ATOM   6988  CA  TYR C 268     -41.010  18.390  36.688  1.00 52.80           C  
ANISOU 6988  CA  TYR C 268     4164   6148   9749   -445   -456  -1015       C  
ATOM   6989  C   TYR C 268     -40.783  17.316  35.629  1.00 52.33           C  
ANISOU 6989  C   TYR C 268     4143   6098   9639   -424   -479   -942       C  
ATOM   6990  O   TYR C 268     -41.785  16.883  35.074  1.00 53.17           O  
ANISOU 6990  O   TYR C 268     4310   6137   9755   -394   -506   -849       O  
ATOM   6991  CB  TYR C 268     -39.882  19.404  36.898  1.00 53.40           C  
ANISOU 6991  CB  TYR C 268     4186   6255   9846   -520   -404  -1123       C  
ATOM   6992  CG  TYR C 268     -40.203  20.407  37.979  1.00 53.40           C  
ANISOU 6992  CG  TYR C 268     4148   6243   9897   -535   -384  -1196       C  
ATOM   6993  CD1 TYR C 268     -39.674  20.270  39.250  1.00 53.50           C  
ANISOU 6993  CD1 TYR C 268     4076   6375   9874   -508   -388  -1292       C  
ATOM   6994  CD2 TYR C 268     -41.087  21.453  37.763  1.00 53.44           C  
ANISOU 6994  CD2 TYR C 268     4200   6120   9982   -567   -366  -1168       C  
ATOM   6995  CE1 TYR C 268     -39.986  21.160  40.267  1.00 53.77           C  
ANISOU 6995  CE1 TYR C 268     4070   6406   9953   -520   -371  -1362       C  
ATOM   6996  CE2 TYR C 268     -41.417  22.346  38.770  1.00 53.63           C  
ANISOU 6996  CE2 TYR C 268     4188   6134  10054   -577   -350  -1237       C  
ATOM   6997  CZ  TYR C 268     -40.866  22.200  40.030  1.00 53.66           C  
ANISOU 6997  CZ  TYR C 268     4103   6261  10024   -557   -351  -1336       C  
ATOM   6998  OH  TYR C 268     -41.164  23.082  41.028  1.00 53.06           O  
ANISOU 6998  OH  TYR C 268     3985   6180   9993   -568   -334  -1411       O  
ATOM   6999  N   GLN C 269     -39.543  16.882  35.396  1.00 51.90           N  
ANISOU 6999  N   GLN C 269     4054   6131   9535   -435   -471   -989       N  
ATOM   7000  CA  GLN C 269     -39.218  15.753  34.480  1.00 50.80           C  
ANISOU 7000  CA  GLN C 269     3942   6018   9340   -407   -495   -932       C  
ATOM   7001  C   GLN C 269     -38.964  14.477  35.300  1.00 49.95           C  
ANISOU 7001  C   GLN C 269     3802   6020   9156   -319   -538   -946       C  
ATOM   7002  O   GLN C 269     -38.619  13.455  34.684  1.00 50.05           O  
ANISOU 7002  O   GLN C 269     3833   6065   9118   -286   -561   -910       O  
ATOM   7003  CB  GLN C 269     -38.036  16.129  33.575  1.00 50.57           C  
ANISOU 7003  CB  GLN C 269     3899   6009   9306   -479   -457   -974       C  
ATOM   7004  CG  GLN C 269     -36.669  16.224  34.251  1.00 51.05           C  
ANISOU 7004  CG  GLN C 269     3869   6198   9328   -494   -437  -1101       C  
ATOM   7005  CD  GLN C 269     -36.411  17.516  34.987  1.00 51.64           C  
ANISOU 7005  CD  GLN C 269     3897   6268   9453   -556   -391  -1194       C  
ATOM   7006  OE1 GLN C 269     -37.320  18.303  35.238  1.00 52.40           O  
ANISOU 7006  OE1 GLN C 269     4026   6270   9611   -573   -380  -1168       O  
ATOM   7007  NE2 GLN C 269     -35.163  17.729  35.373  1.00 52.00           N  
ANISOU 7007  NE2 GLN C 269     3863   6423   9472   -587   -365  -1313       N  
ATOM   7008  N   CYS C 270     -39.133  14.553  36.626  1.00 49.19           N  
ANISOU 7008  N   CYS C 270     3664   5974   9049   -281   -546   -996       N  
ATOM   7009  CA  CYS C 270     -38.814  13.489  37.615  1.00 48.32           C  
ANISOU 7009  CA  CYS C 270     3524   5974   8860   -195   -582  -1021       C  
ATOM   7010  C   CYS C 270     -40.106  12.791  38.055  1.00 47.94           C  
ANISOU 7010  C   CYS C 270     3528   5882   8805   -136   -612   -939       C  
ATOM   7011  O   CYS C 270     -40.089  12.109  39.088  1.00 48.00           O  
ANISOU 7011  O   CYS C 270     3520   5961   8754    -69   -635   -956       O  
ATOM   7012  CB  CYS C 270     -38.102  14.078  38.832  1.00 48.78           C  
ANISOU 7012  CB  CYS C 270     3498   6128   8904   -193   -568  -1139       C  
ATOM   7013  SG  CYS C 270     -36.414  14.569  38.548  1.00 48.59           S  
ANISOU 7013  SG  CYS C 270     3396   6202   8864   -246   -537  -1260       S  
ATOM   7014  N   GLY C 271     -41.189  12.964  37.291  1.00 47.96           N  
ANISOU 7014  N   GLY C 271     3589   5770   8860   -162   -611   -856       N  
ATOM   7015  CA  GLY C 271     -42.533  12.457  37.618  1.00 47.32           C  
ANISOU 7015  CA  GLY C 271     3554   5640   8785   -123   -631   -786       C  
ATOM   7016  C   GLY C 271     -42.687  10.981  37.304  1.00 46.82           C  
ANISOU 7016  C   GLY C 271     3537   5591   8659    -66   -662   -719       C  
ATOM   7017  O   GLY C 271     -42.220  10.541  36.239  1.00 47.88           O  
ANISOU 7017  O   GLY C 271     3694   5716   8780    -74   -667   -689       O  
ATOM   7018  N   HIS C 272     -43.346  10.236  38.189  1.00 46.05           N  
ANISOU 7018  N   HIS C 272     3458   5512   8526    -13   -677   -696       N  
ATOM   7019  CA  HIS C 272     -43.626   8.787  38.009  1.00 45.24           C  
ANISOU 7019  CA  HIS C 272     3412   5412   8365     40   -701   -630       C  
ATOM   7020  C   HIS C 272     -45.105   8.478  38.266  1.00 44.64           C  
ANISOU 7020  C   HIS C 272     3379   5273   8309     45   -701   -572       C  
ATOM   7021  O   HIS C 272     -45.608   8.867  39.343  1.00 44.17           O  
ANISOU 7021  O   HIS C 272     3298   5229   8255     50   -692   -601       O  
ATOM   7022  CB  HIS C 272     -42.705   7.965  38.914  1.00 45.48           C  
ANISOU 7022  CB  HIS C 272     3428   5545   8306    110   -717   -670       C  
ATOM   7023  CG  HIS C 272     -42.801   6.502  38.666  1.00 45.10           C  
ANISOU 7023  CG  HIS C 272     3444   5494   8196    167   -739   -607       C  
ATOM   7024  ND1 HIS C 272     -42.682   5.964  37.391  1.00 44.88           N  
ANISOU 7024  ND1 HIS C 272     3451   5426   8174    156   -747   -559       N  
ATOM   7025  CD2 HIS C 272     -43.011   5.469  39.506  1.00 45.01           C  
ANISOU 7025  CD2 HIS C 272     3475   5510   8116    233   -751   -584       C  
ATOM   7026  CE1 HIS C 272     -42.809   4.657  37.459  1.00 44.61           C  
ANISOU 7026  CE1 HIS C 272     3475   5392   8081    213   -764   -513       C  
ATOM   7027  NE2 HIS C 272     -43.008   4.326  38.751  1.00 44.71           N  
ANISOU 7027  NE2 HIS C 272     3497   5443   8046    261   -765   -525       N  
ATOM   7028  N   TYR C 273     -45.757   7.810  37.301  1.00 44.21           N  
ANISOU 7028  N   TYR C 273     3378   5156   8262     40   -709   -500       N  
ATOM   7029  CA  TYR C 273     -47.112   7.208  37.434  1.00 43.78           C  
ANISOU 7029  CA  TYR C 273     3367   5051   8213     47   -708   -446       C  
ATOM   7030  C   TYR C 273     -47.017   5.773  37.947  1.00 44.73           C  
ANISOU 7030  C   TYR C 273     3535   5206   8254    102   -716   -418       C  
ATOM   7031  O   TYR C 273     -46.257   4.990  37.361  1.00 45.37           O  
ANISOU 7031  O   TYR C 273     3640   5303   8293    129   -730   -400       O  
ATOM   7032  CB  TYR C 273     -47.831   7.062  36.099  1.00 42.40           C  
ANISOU 7032  CB  TYR C 273     3228   4801   8080     18   -714   -387       C  
ATOM   7033  CG  TYR C 273     -48.496   8.306  35.583  1.00 42.09           C  
ANISOU 7033  CG  TYR C 273     3169   4702   8122    -27   -708   -391       C  
ATOM   7034  CD1 TYR C 273     -47.936   9.028  34.545  1.00 41.56           C  
ANISOU 7034  CD1 TYR C 273     3095   4607   8088    -59   -708   -390       C  
ATOM   7035  CD2 TYR C 273     -49.719   8.723  36.087  1.00 41.94           C  
ANISOU 7035  CD2 TYR C 273     3142   4649   8140    -36   -702   -393       C  
ATOM   7036  CE1 TYR C 273     -48.556  10.154  34.038  1.00 41.57           C  
ANISOU 7036  CE1 TYR C 273     3092   4543   8157    -94   -703   -387       C  
ATOM   7037  CE2 TYR C 273     -50.354   9.849  35.592  1.00 41.58           C  
ANISOU 7037  CE2 TYR C 273     3084   4546   8167    -67   -702   -396       C  
ATOM   7038  CZ  TYR C 273     -49.764  10.567  34.566  1.00 41.71           C  
ANISOU 7038  CZ  TYR C 273     3103   4528   8214    -93   -703   -390       C  
ATOM   7039  OH  TYR C 273     -50.362  11.676  34.049  1.00 41.93           O  
ANISOU 7039  OH  TYR C 273     3131   4490   8307   -116   -703   -388       O  
ATOM   7040  N   LYS C 274     -47.785   5.447  38.986  1.00 45.65           N  
ANISOU 7040  N   LYS C 274     3668   5329   8348    118   -705   -414       N  
ATOM   7041  CA  LYS C 274     -48.147   4.056  39.359  1.00 46.19           C  
ANISOU 7041  CA  LYS C 274     3804   5395   8351    156   -702   -369       C  
ATOM   7042  C   LYS C 274     -49.648   3.886  39.131  1.00 46.99           C  
ANISOU 7042  C   LYS C 274     3932   5429   8493    117   -685   -330       C  
ATOM   7043  O   LYS C 274     -50.357   4.911  39.032  1.00 46.10           O  
ANISOU 7043  O   LYS C 274     3777   5289   8447     75   -679   -350       O  
ATOM   7044  CB  LYS C 274     -47.825   3.757  40.823  1.00 46.21           C  
ANISOU 7044  CB  LYS C 274     3810   5464   8283    204   -697   -397       C  
ATOM   7045  CG  LYS C 274     -46.361   3.886  41.211  1.00 46.21           C  
ANISOU 7045  CG  LYS C 274     3776   5548   8234    253   -717   -448       C  
ATOM   7046  CD  LYS C 274     -46.110   3.429  42.630  1.00 46.51           C  
ANISOU 7046  CD  LYS C 274     3829   5653   8189    313   -716   -468       C  
ATOM   7047  CE  LYS C 274     -44.806   3.925  43.210  1.00 46.98           C  
ANISOU 7047  CE  LYS C 274     3826   5811   8211    355   -734   -543       C  
ATOM   7048  NZ  LYS C 274     -45.041   4.607  44.509  1.00 47.52           N  
ANISOU 7048  NZ  LYS C 274     3853   5931   8271    356   -722   -594       N  
ATOM   7049  N   HIS C 275     -50.109   2.640  39.059  1.00 48.34           N  
ANISOU 7049  N   HIS C 275     4170   5574   8622    130   -676   -282       N  
ATOM   7050  CA  HIS C 275     -51.539   2.291  38.863  1.00 49.18           C  
ANISOU 7050  CA  HIS C 275     4303   5624   8757     91   -654   -253       C  
ATOM   7051  C   HIS C 275     -52.049   1.569  40.110  1.00 49.53           C  
ANISOU 7051  C   HIS C 275     4391   5684   8744    104   -626   -247       C  
ATOM   7052  O   HIS C 275     -51.383   0.630  40.553  1.00 49.79           O  
ANISOU 7052  O   HIS C 275     4480   5737   8701    151   -625   -227       O  
ATOM   7053  CB  HIS C 275     -51.707   1.456  37.594  1.00 49.56           C  
ANISOU 7053  CB  HIS C 275     4394   5623   8812     81   -661   -206       C  
ATOM   7054  CG  HIS C 275     -53.125   1.117  37.299  1.00 49.94           C  
ANISOU 7054  CG  HIS C 275     4460   5622   8892     38   -639   -187       C  
ATOM   7055  ND1 HIS C 275     -53.991   2.034  36.732  1.00 50.06           N  
ANISOU 7055  ND1 HIS C 275     4425   5612   8980     -1   -644   -203       N  
ATOM   7056  CD2 HIS C 275     -53.828  -0.019  37.490  1.00 50.09           C  
ANISOU 7056  CD2 HIS C 275     4538   5614   8876     28   -611   -160       C  
ATOM   7057  CE1 HIS C 275     -55.164   1.467  36.569  1.00 49.76           C  
ANISOU 7057  CE1 HIS C 275     4408   5544   8953    -32   -623   -192       C  
ATOM   7058  NE2 HIS C 275     -55.096   0.209  37.032  1.00 49.63           N  
ANISOU 7058  NE2 HIS C 275     4458   5524   8873    -21   -599   -167       N  
ATOM   7059  N   ILE C 276     -53.168   2.026  40.671  1.00 49.90           N  
ANISOU 7059  N   ILE C 276     4414   5723   8821     65   -603   -267       N  
ATOM   7060  CA  ILE C 276     -53.850   1.337  41.799  1.00 50.87           C  
ANISOU 7060  CA  ILE C 276     4581   5855   8890     62   -566   -261       C  
ATOM   7061  C   ILE C 276     -55.181   0.804  41.275  1.00 50.83           C  
ANISOU 7061  C   ILE C 276     4601   5795   8916      8   -538   -240       C  
ATOM   7062  O   ILE C 276     -55.872   1.535  40.559  1.00 50.71           O  
ANISOU 7062  O   ILE C 276     4533   5757   8975    -27   -548   -258       O  
ATOM   7063  CB  ILE C 276     -54.018   2.250  43.026  1.00 52.00           C  
ANISOU 7063  CB  ILE C 276     4671   6050   9035     60   -556   -313       C  
ATOM   7064  CG1 ILE C 276     -52.677   2.559  43.697  1.00 52.63           C  
ANISOU 7064  CG1 ILE C 276     4732   6195   9067    117   -578   -339       C  
ATOM   7065  CG2 ILE C 276     -54.987   1.618  44.013  1.00 52.72           C  
ANISOU 7065  CG2 ILE C 276     4804   6144   9083     38   -512   -307       C  
ATOM   7066  CD1 ILE C 276     -51.870   3.625  43.014  1.00 52.58           C  
ANISOU 7066  CD1 ILE C 276     4658   6200   9118    118   -611   -373       C  
ATOM   7067  N   THR C 277     -55.490  -0.446  41.609  1.00 50.58           N  
ANISOU 7067  N   THR C 277     4651   5742   8824      7   -505   -205       N  
ATOM   7068  CA  THR C 277     -56.719  -1.160  41.198  1.00 50.40           C  
ANISOU 7068  CA  THR C 277     4660   5671   8817    -49   -469   -190       C  
ATOM   7069  C   THR C 277     -57.383  -1.721  42.461  1.00 50.51           C  
ANISOU 7069  C   THR C 277     4722   5695   8774    -71   -415   -192       C  
ATOM   7070  O   THR C 277     -56.662  -2.213  43.339  1.00 51.68           O  
ANISOU 7070  O   THR C 277     4927   5863   8843    -25   -408   -171       O  
ATOM   7071  CB  THR C 277     -56.385  -2.215  40.137  1.00 50.17           C  
ANISOU 7071  CB  THR C 277     4693   5593   8774    -39   -475   -143       C  
ATOM   7072  OG1 THR C 277     -57.604  -2.678  39.567  1.00 49.85           O  
ANISOU 7072  OG1 THR C 277     4661   5512   8767   -101   -444   -144       O  
ATOM   7073  CG2 THR C 277     -55.645  -3.416  40.677  1.00 51.02           C  
ANISOU 7073  CG2 THR C 277     4901   5692   8791      6   -460   -101       C  
ATOM   7074  N   SER C 278     -58.705  -1.602  42.565  1.00 49.70           N  
ANISOU 7074  N   SER C 278     4593   5583   8706   -136   -380   -220       N  
ATOM   7075  CA  SER C 278     -59.524  -2.202  43.645  1.00 49.45           C  
ANISOU 7075  CA  SER C 278     4608   5556   8624   -176   -318   -226       C  
ATOM   7076  C   SER C 278     -60.002  -3.580  43.176  1.00 49.01           C  
ANISOU 7076  C   SER C 278     4641   5439   8539   -214   -274   -187       C  
ATOM   7077  O   SER C 278     -60.669  -3.639  42.138  1.00 47.62           O  
ANISOU 7077  O   SER C 278     4435   5234   8422   -255   -276   -199       O  
ATOM   7078  CB  SER C 278     -60.664  -1.298  44.023  1.00 49.46           C  
ANISOU 7078  CB  SER C 278     4524   5589   8679   -229   -302   -289       C  
ATOM   7079  OG  SER C 278     -61.317  -1.769  45.194  1.00 50.26           O  
ANISOU 7079  OG  SER C 278     4664   5707   8723   -266   -241   -300       O  
ATOM   7080  N   LYS C 279     -59.595  -4.634  43.883  1.00 49.82           N  
ANISOU 7080  N   LYS C 279     4853   5522   8554   -193   -240   -142       N  
ATOM   7081  CA  LYS C 279     -59.990  -6.043  43.621  1.00 51.71           C  
ANISOU 7081  CA  LYS C 279     5199   5693   8754   -229   -187   -103       C  
ATOM   7082  C   LYS C 279     -60.457  -6.629  44.961  1.00 52.32           C  
ANISOU 7082  C   LYS C 279     5355   5771   8751   -258   -117    -93       C  
ATOM   7083  O   LYS C 279     -61.227  -5.934  45.637  1.00 52.53           O  
ANISOU 7083  O   LYS C 279     5319   5843   8795   -302    -95   -142       O  
ATOM   7084  CB  LYS C 279     -58.842  -6.785  42.927  1.00 52.40           C  
ANISOU 7084  CB  LYS C 279     5355   5741   8811   -161   -222    -48       C  
ATOM   7085  CG  LYS C 279     -58.422  -6.187  41.598  1.00 52.41           C  
ANISOU 7085  CG  LYS C 279     5278   5747   8887   -142   -285    -60       C  
ATOM   7086  CD  LYS C 279     -57.850  -7.196  40.656  1.00 53.29           C  
ANISOU 7086  CD  LYS C 279     5459   5805   8984   -115   -296    -17       C  
ATOM   7087  CE  LYS C 279     -58.117  -6.823  39.213  1.00 53.92           C  
ANISOU 7087  CE  LYS C 279     5465   5873   9146   -142   -329    -36       C  
ATOM   7088  NZ  LYS C 279     -57.386  -7.711  38.268  1.00 54.78           N  
ANISOU 7088  NZ  LYS C 279     5632   5940   9240   -107   -348      0       N  
ATOM   7089  N   GLU C 280     -60.046  -7.841  45.343  1.00 52.63           N  
ANISOU 7089  N   GLU C 280     5530   5761   8705   -234    -83    -35       N  
ATOM   7090  CA  GLU C 280     -60.429  -8.421  46.657  1.00 54.15           C  
ANISOU 7090  CA  GLU C 280     5814   5950   8809   -258    -13    -17       C  
ATOM   7091  C   GLU C 280     -59.846  -7.534  47.762  1.00 54.01           C  
ANISOU 7091  C   GLU C 280     5752   6014   8753   -198    -44    -33       C  
ATOM   7092  O   GLU C 280     -60.504  -7.385  48.796  1.00 54.16           O  
ANISOU 7092  O   GLU C 280     5775   6064   8738   -240      4    -55       O  
ATOM   7093  CB  GLU C 280     -60.003  -9.885  46.772  1.00 55.51           C  
ANISOU 7093  CB  GLU C 280     6152   6043   8895   -231     23     54       C  
ATOM   7094  CG  GLU C 280     -58.525 -10.099  47.036  1.00 56.25           C  
ANISOU 7094  CG  GLU C 280     6305   6147   8919   -104    -33    103       C  
ATOM   7095  CD  GLU C 280     -57.616 -10.055  45.820  1.00 56.53           C  
ANISOU 7095  CD  GLU C 280     6305   6171   9001    -43   -105    111       C  
ATOM   7096  OE1 GLU C 280     -58.047  -9.576  44.746  1.00 56.57           O  
ANISOU 7096  OE1 GLU C 280     6217   6174   9101    -92   -125     76       O  
ATOM   7097  OE2 GLU C 280     -56.468 -10.513  45.951  1.00 57.89           O  
ANISOU 7097  OE2 GLU C 280     6545   6340   9109     55   -142    151       O  
ATOM   7098  N   THR C 281     -58.657  -6.975  47.522  1.00 54.76           N  
ANISOU 7098  N   THR C 281     5804   6146   8854   -107   -121    -30       N  
ATOM   7099  CA  THR C 281     -57.999  -5.892  48.311  1.00 55.30           C  
ANISOU 7099  CA  THR C 281     5795   6303   8911    -49   -165    -63       C  
ATOM   7100  C   THR C 281     -57.420  -4.870  47.322  1.00 54.53           C  
ANISOU 7100  C   THR C 281     5582   6232   8904    -21   -238    -97       C  
ATOM   7101  O   THR C 281     -57.717  -5.006  46.122  1.00 54.62           O  
ANISOU 7101  O   THR C 281     5574   6196   8981    -54   -248    -93       O  
ATOM   7102  CB  THR C 281     -56.931  -6.464  49.253  1.00 56.44           C  
ANISOU 7102  CB  THR C 281     6036   6469   8939     46   -175    -20       C  
ATOM   7103  OG1 THR C 281     -56.506  -5.423  50.135  1.00 56.69           O  
ANISOU 7103  OG1 THR C 281     5987   6593   8958     85   -205    -65       O  
ATOM   7104  CG2 THR C 281     -55.742  -7.041  48.515  1.00 56.31           C  
ANISOU 7104  CG2 THR C 281     6067   6424   8901    131   -226     20       C  
ATOM   7105  N   LEU C 282     -56.628  -3.897  47.790  1.00 54.22           N  
ANISOU 7105  N   LEU C 282     5470   6265   8864     34   -285   -130       N  
ATOM   7106  CA  LEU C 282     -55.978  -2.875  46.919  1.00 53.27           C  
ANISOU 7106  CA  LEU C 282     5246   6168   8823     58   -349   -163       C  
ATOM   7107  C   LEU C 282     -54.627  -3.392  46.428  1.00 52.44           C  
ANISOU 7107  C   LEU C 282     5185   6059   8678    140   -394   -128       C  
ATOM   7108  O   LEU C 282     -53.818  -3.810  47.271  1.00 53.05           O  
ANISOU 7108  O   LEU C 282     5318   6172   8665    211   -401   -112       O  
ATOM   7109  CB  LEU C 282     -55.776  -1.569  47.689  1.00 53.84           C  
ANISOU 7109  CB  LEU C 282     5220   6320   8917     70   -371   -224       C  
ATOM   7110  CG  LEU C 282     -57.046  -0.808  48.043  1.00 55.17           C  
ANISOU 7110  CG  LEU C 282     5319   6500   9142     -4   -340   -274       C  
ATOM   7111  CD1 LEU C 282     -56.704   0.399  48.906  1.00 55.57           C  
ANISOU 7111  CD1 LEU C 282     5282   6628   9202     17   -361   -335       C  
ATOM   7112  CD2 LEU C 282     -57.813  -0.401  46.786  1.00 54.80           C  
ANISOU 7112  CD2 LEU C 282     5215   6406   9199    -60   -350   -289       C  
ATOM   7113  N   TYR C 283     -54.403  -3.324  45.115  1.00 50.96           N  
ANISOU 7113  N   TYR C 283     4969   5837   8554    132   -424   -122       N  
ATOM   7114  CA  TYR C 283     -53.128  -3.664  44.445  1.00 50.52           C  
ANISOU 7114  CA  TYR C 283     4933   5784   8477    202   -471   -101       C  
ATOM   7115  C   TYR C 283     -52.556  -2.398  43.805  1.00 49.83           C  
ANISOU 7115  C   TYR C 283     4732   5737   8464    204   -519   -148       C  
ATOM   7116  O   TYR C 283     -53.299  -1.717  43.089  1.00 49.02           O  
ANISOU 7116  O   TYR C 283     4568   5609   8448    143   -518   -166       O  
ATOM   7117  CB  TYR C 283     -53.348  -4.721  43.365  1.00 50.73           C  
ANISOU 7117  CB  TYR C 283     5028   5733   8513    185   -461    -55       C  
ATOM   7118  CG  TYR C 283     -53.671  -6.104  43.858  1.00 52.13           C  
ANISOU 7118  CG  TYR C 283     5336   5859   8613    192   -415     -4       C  
ATOM   7119  CD1 TYR C 283     -54.945  -6.453  44.271  1.00 53.58           C  
ANISOU 7119  CD1 TYR C 283     5556   6004   8797    116   -352      1       C  
ATOM   7120  CD2 TYR C 283     -52.707  -7.088  43.856  1.00 52.88           C  
ANISOU 7120  CD2 TYR C 283     5521   5937   8632    271   -431     35       C  
ATOM   7121  CE1 TYR C 283     -55.239  -7.738  44.704  1.00 54.32           C  
ANISOU 7121  CE1 TYR C 283     5780   6041   8818    113   -300     49       C  
ATOM   7122  CE2 TYR C 283     -52.980  -8.379  44.269  1.00 53.94           C  
ANISOU 7122  CE2 TYR C 283     5790   6011   8694    280   -387     86       C  
ATOM   7123  CZ  TYR C 283     -54.252  -8.709  44.691  1.00 54.73           C  
ANISOU 7123  CZ  TYR C 283     5931   6066   8795    197   -318     95       C  
ATOM   7124  OH  TYR C 283     -54.504  -9.986  45.097  1.00 56.01           O  
ANISOU 7124  OH  TYR C 283     6236   6161   8884    199   -266    147       O  
ATOM   7125  N   CYS C 284     -51.278  -2.106  44.060  1.00 49.59           N  
ANISOU 7125  N   CYS C 284     4677   5765   8397    273   -558   -169       N  
ATOM   7126  CA  CYS C 284     -50.499  -1.034  43.389  1.00 48.06           C  
ANISOU 7126  CA  CYS C 284     4389   5607   8263    277   -599   -212       C  
ATOM   7127  C   CYS C 284     -49.590  -1.678  42.340  1.00 47.52           C  
ANISOU 7127  C   CYS C 284     4350   5523   8183    315   -630   -187       C  
ATOM   7128  O   CYS C 284     -48.652  -2.398  42.723  1.00 47.66           O  
ANISOU 7128  O   CYS C 284     4415   5571   8120    392   -647   -177       O  
ATOM   7129  CB  CYS C 284     -49.687  -0.230  44.395  1.00 48.28           C  
ANISOU 7129  CB  CYS C 284     4358   5722   8261    320   -617   -267       C  
ATOM   7130  SG  CYS C 284     -48.734   1.095  43.617  1.00 47.65           S  
ANISOU 7130  SG  CYS C 284     4168   5681   8254    310   -656   -327       S  
ATOM   7131  N   ILE C 285     -49.893  -1.455  41.066  1.00 46.82           N  
ANISOU 7131  N   ILE C 285     4235   5387   8167    268   -637   -177       N  
ATOM   7132  CA  ILE C 285     -49.087  -1.960  39.920  1.00 47.03           C  
ANISOU 7132  CA  ILE C 285     4277   5399   8193    294   -664   -159       C  
ATOM   7133  C   ILE C 285     -48.120  -0.852  39.494  1.00 46.60           C  
ANISOU 7133  C   ILE C 285     4133   5396   8175    297   -697   -208       C  
ATOM   7134  O   ILE C 285     -48.582   0.203  38.991  1.00 47.04           O  
ANISOU 7134  O   ILE C 285     4127   5437   8309    239   -695   -227       O  
ATOM   7135  CB  ILE C 285     -49.989  -2.417  38.758  1.00 47.19           C  
ANISOU 7135  CB  ILE C 285     4323   5343   8264    239   -651   -121       C  
ATOM   7136  CG1 ILE C 285     -51.008  -3.466  39.213  1.00 47.87           C  
ANISOU 7136  CG1 ILE C 285     4492   5376   8317    221   -609    -82       C  
ATOM   7137  CG2 ILE C 285     -49.143  -2.899  37.583  1.00 46.96           C  
ANISOU 7137  CG2 ILE C 285     4305   5305   8232    264   -680   -106       C  
ATOM   7138  CD1 ILE C 285     -51.949  -3.910  38.123  1.00 47.72           C  
ANISOU 7138  CD1 ILE C 285     4490   5291   8348    163   -593    -58       C  
ATOM   7139  N   ASP C 286     -46.828  -1.096  39.709  1.00 46.19           N  
ANISOU 7139  N   ASP C 286     4079   5405   8065    364   -723   -230       N  
ATOM   7140  CA  ASP C 286     -45.705  -0.192  39.353  1.00 45.29           C  
ANISOU 7140  CA  ASP C 286     3885   5351   7971    371   -750   -286       C  
ATOM   7141  C   ASP C 286     -44.860  -0.891  38.285  1.00 43.95           C  
ANISOU 7141  C   ASP C 286     3735   5180   7783    400   -774   -273       C  
ATOM   7142  O   ASP C 286     -43.769  -1.346  38.604  1.00 43.17           O  
ANISOU 7142  O   ASP C 286     3640   5143   7618    472   -798   -298       O  
ATOM   7143  CB  ASP C 286     -44.903   0.151  40.608  1.00 46.30           C  
ANISOU 7143  CB  ASP C 286     3978   5569   8042    425   -760   -341       C  
ATOM   7144  CG  ASP C 286     -43.791   1.141  40.363  1.00 47.39           C  
ANISOU 7144  CG  ASP C 286     4026   5776   8202    421   -779   -413       C  
ATOM   7145  OD1 ASP C 286     -43.606   1.523  39.191  1.00 48.31           O  
ANISOU 7145  OD1 ASP C 286     4115   5865   8374    377   -783   -413       O  
ATOM   7146  OD2 ASP C 286     -43.122   1.517  41.347  1.00 49.22           O  
ANISOU 7146  OD2 ASP C 286     4217   6090   8393    461   -787   -470       O  
ATOM   7147  N   GLY C 287     -45.375  -0.981  37.062  1.00 43.29           N  
ANISOU 7147  N   GLY C 287     3660   5033   7753    350   -770   -238       N  
ATOM   7148  CA  GLY C 287     -44.720  -1.682  35.943  1.00 43.00           C  
ANISOU 7148  CA  GLY C 287     3644   4989   7704    370   -790   -223       C  
ATOM   7149  C   GLY C 287     -44.740  -3.181  36.163  1.00 43.81           C  
ANISOU 7149  C   GLY C 287     3840   5066   7739    430   -791   -182       C  
ATOM   7150  O   GLY C 287     -45.814  -3.774  36.049  1.00 45.39           O  
ANISOU 7150  O   GLY C 287     4097   5195   7952    401   -767   -134       O  
ATOM   7151  N   ALA C 288     -43.600  -3.779  36.506  1.00 44.69           N  
ANISOU 7151  N   ALA C 288     3968   5234   7778    514   -818   -203       N  
ATOM   7152  CA  ALA C 288     -43.450  -5.232  36.777  1.00 44.91           C  
ANISOU 7152  CA  ALA C 288     4095   5237   7730    589   -824   -166       C  
ATOM   7153  C   ALA C 288     -43.571  -5.507  38.278  1.00 45.15           C  
ANISOU 7153  C   ALA C 288     4173   5288   7692    644   -814   -161       C  
ATOM   7154  O   ALA C 288     -43.594  -6.688  38.644  1.00 45.19           O  
ANISOU 7154  O   ALA C 288     4278   5260   7632    704   -812   -122       O  
ATOM   7155  CB  ALA C 288     -42.128  -5.743  36.246  1.00 45.11           C  
ANISOU 7155  CB  ALA C 288     4113   5314   7711    661   -863   -195       C  
ATOM   7156  N   LEU C 289     -43.618  -4.471  39.114  1.00 45.35           N  
ANISOU 7156  N   LEU C 289     4135   5365   7729    625   -809   -200       N  
ATOM   7157  CA  LEU C 289     -43.672  -4.619  40.594  1.00 46.16           C  
ANISOU 7157  CA  LEU C 289     4273   5503   7762    678   -801   -203       C  
ATOM   7158  C   LEU C 289     -45.130  -4.530  41.028  1.00 46.30           C  
ANISOU 7158  C   LEU C 289     4325   5453   7812    607   -755   -163       C  
ATOM   7159  O   LEU C 289     -45.911  -3.909  40.286  1.00 46.60           O  
ANISOU 7159  O   LEU C 289     4319   5447   7937    519   -737   -159       O  
ATOM   7160  CB  LEU C 289     -42.835  -3.529  41.266  1.00 46.53           C  
ANISOU 7160  CB  LEU C 289     4221   5656   7800    699   -822   -281       C  
ATOM   7161  CG  LEU C 289     -41.467  -3.278  40.636  1.00 46.71           C  
ANISOU 7161  CG  LEU C 289     4176   5754   7817    736   -861   -341       C  
ATOM   7162  CD1 LEU C 289     -40.679  -2.266  41.454  1.00 47.38           C  
ANISOU 7162  CD1 LEU C 289     4166   5948   7887    756   -875   -426       C  
ATOM   7163  CD2 LEU C 289     -40.700  -4.579  40.485  1.00 47.12           C  
ANISOU 7163  CD2 LEU C 289     4301   5814   7788    837   -892   -323       C  
ATOM   7164  N   LEU C 290     -45.458  -5.140  42.171  1.00 46.52           N  
ANISOU 7164  N   LEU C 290     4429   5476   7768    647   -735   -137       N  
ATOM   7165  CA  LEU C 290     -46.844  -5.338  42.665  1.00 45.66           C  
ANISOU 7165  CA  LEU C 290     4373   5303   7672    584   -684    -97       C  
ATOM   7166  C   LEU C 290     -46.850  -5.267  44.186  1.00 46.60           C  
ANISOU 7166  C   LEU C 290     4515   5472   7717    627   -672   -107       C  
ATOM   7167  O   LEU C 290     -46.124  -6.043  44.798  1.00 47.46           O  
ANISOU 7167  O   LEU C 290     4693   5608   7729    722   -689    -93       O  
ATOM   7168  CB  LEU C 290     -47.341  -6.712  42.212  1.00 45.43           C  
ANISOU 7168  CB  LEU C 290     4461   5180   7617    585   -659    -30       C  
ATOM   7169  CG  LEU C 290     -48.784  -7.041  42.605  1.00 45.42           C  
ANISOU 7169  CG  LEU C 290     4518   5109   7629    510   -599      6       C  
ATOM   7170  CD1 LEU C 290     -49.765  -6.146  41.854  1.00 44.72           C  
ANISOU 7170  CD1 LEU C 290     4344   4998   7650    404   -583    -14       C  
ATOM   7171  CD2 LEU C 290     -49.109  -8.504  42.355  1.00 45.52           C  
ANISOU 7171  CD2 LEU C 290     4662   5033   7599    520   -570     66       C  
ATOM   7172  N   THR C 291     -47.687  -4.414  44.762  1.00 47.96           N  
ANISOU 7172  N   THR C 291     4637   5656   7930    562   -644   -128       N  
ATOM   7173  CA  THR C 291     -47.869  -4.297  46.230  1.00 50.39           C  
ANISOU 7173  CA  THR C 291     4962   6012   8170    588   -626   -139       C  
ATOM   7174  C   THR C 291     -49.344  -4.541  46.562  1.00 52.93           C  
ANISOU 7174  C   THR C 291     5332   6266   8509    508   -565   -104       C  
ATOM   7175  O   THR C 291     -50.147  -4.534  45.621  1.00 53.07           O  
ANISOU 7175  O   THR C 291     5340   6217   8605    431   -546    -89       O  
ATOM   7176  CB  THR C 291     -47.292  -2.963  46.710  1.00 49.97           C  
ANISOU 7176  CB  THR C 291     4787   6056   8141    595   -652   -217       C  
ATOM   7177  OG1 THR C 291     -45.883  -3.156  46.640  1.00 50.23           O  
ANISOU 7177  OG1 THR C 291     4809   6154   8120    687   -700   -244       O  
ATOM   7178  CG2 THR C 291     -47.674  -2.573  48.120  1.00 50.36           C  
ANISOU 7178  CG2 THR C 291     4829   6157   8146    599   -630   -240       C  
ATOM   7179  N   LYS C 292     -49.650  -4.828  47.834  1.00 55.80           N  
ANISOU 7179  N   LYS C 292     5752   6651   8795    528   -536    -92       N  
ATOM   7180  CA  LYS C 292     -51.022  -4.981  48.378  1.00 57.05           C  
ANISOU 7180  CA  LYS C 292     5949   6766   8959    449   -473    -72       C  
ATOM   7181  C   LYS C 292     -51.119  -4.295  49.740  1.00 59.26           C  
ANISOU 7181  C   LYS C 292     6191   7126   9198    459   -462   -112       C  
ATOM   7182  O   LYS C 292     -50.192  -4.460  50.548  1.00 59.87           O  
ANISOU 7182  O   LYS C 292     6294   7269   9185    552   -488   -117       O  
ATOM   7183  CB  LYS C 292     -51.369  -6.453  48.606  1.00 57.92           C  
ANISOU 7183  CB  LYS C 292     6216   6801   8990    463   -430      0       C  
ATOM   7184  CG  LYS C 292     -51.334  -7.342  47.375  1.00 57.80           C  
ANISOU 7184  CG  LYS C 292     6258   6699   9001    455   -432     43       C  
ATOM   7185  CD  LYS C 292     -51.887  -8.730  47.635  1.00 58.58           C  
ANISOU 7185  CD  LYS C 292     6514   6711   9033    447   -376    110       C  
ATOM   7186  CE  LYS C 292     -51.338  -9.348  48.907  1.00 59.76           C  
ANISOU 7186  CE  LYS C 292     6768   6885   9050    539   -370    142       C  
ATOM   7187  NZ  LYS C 292     -52.148 -10.502  49.363  1.00 61.14           N  
ANISOU 7187  NZ  LYS C 292     7095   6971   9162    504   -296    205       N  
ATOM   7188  N   SER C 293     -52.230  -3.601  49.993  1.00 61.65           N  
ANISOU 7188  N   SER C 293     6436   7426   9559    370   -425   -141       N  
ATOM   7189  CA  SER C 293     -52.612  -3.051  51.321  1.00 64.07           C  
ANISOU 7189  CA  SER C 293     6716   7800   9828    362   -401   -176       C  
ATOM   7190  C   SER C 293     -54.136  -3.096  51.466  1.00 65.92           C  
ANISOU 7190  C   SER C 293     6959   7986  10099    257   -337   -172       C  
ATOM   7191  O   SER C 293     -54.832  -3.181  50.423  1.00 67.19           O  
ANISOU 7191  O   SER C 293     7108   8080  10341    190   -324   -163       O  
ATOM   7192  CB  SER C 293     -52.077  -1.652  51.520  1.00 64.62           C  
ANISOU 7192  CB  SER C 293     6648   7954   9948    374   -442   -256       C  
ATOM   7193  OG  SER C 293     -52.497  -0.777  50.479  1.00 64.97           O  
ANISOU 7193  OG  SER C 293     6599   7966  10118    306   -454   -288       O  
ATOM   7194  N   SER C 294     -54.633  -3.041  52.705  1.00 66.63           N  
ANISOU 7194  N   SER C 294     7068   8118  10130    244   -297   -185       N  
ATOM   7195  CA  SER C 294     -56.081  -2.968  53.025  1.00 66.24           C  
ANISOU 7195  CA  SER C 294     7012   8045  10109    142   -233   -199       C  
ATOM   7196  C   SER C 294     -56.609  -1.564  52.700  1.00 66.59           C  
ANISOU 7196  C   SER C 294     6907   8123  10272     86   -251   -277       C  
ATOM   7197  O   SER C 294     -57.810  -1.452  52.395  1.00 68.23           O  
ANISOU 7197  O   SER C 294     7088   8296  10540      0   -213   -294       O  
ATOM   7198  CB  SER C 294     -56.345  -3.359  54.456  1.00 66.89           C  
ANISOU 7198  CB  SER C 294     7164   8168  10082    150   -185   -188       C  
ATOM   7199  OG  SER C 294     -55.801  -2.407  55.363  1.00 67.16           O  
ANISOU 7199  OG  SER C 294     7116   8304  10095    197   -216   -245       O  
ATOM   7200  N   GLU C 295     -55.749  -0.535  52.751  1.00 67.03           N  
ANISOU 7200  N   GLU C 295     6868   8241  10358    135   -306   -326       N  
ATOM   7201  CA  GLU C 295     -56.065   0.864  52.338  1.00 65.40           C  
ANISOU 7201  CA  GLU C 295     6525   8054  10267     94   -332   -398       C  
ATOM   7202  C   GLU C 295     -54.820   1.506  51.710  1.00 61.33           C  
ANISOU 7202  C   GLU C 295     5952   7561   9788    151   -395   -418       C  
ATOM   7203  O   GLU C 295     -53.723   0.978  51.906  1.00 58.40           O  
ANISOU 7203  O   GLU C 295     5629   7217   9343    227   -419   -393       O  
ATOM   7204  CB  GLU C 295     -56.552   1.686  53.538  1.00 67.44           C  
ANISOU 7204  CB  GLU C 295     6719   8386  10518     74   -311   -462       C  
ATOM   7205  CG  GLU C 295     -55.657   1.584  54.775  1.00 70.40           C  
ANISOU 7205  CG  GLU C 295     7118   8845  10785    148   -319   -470       C  
ATOM   7206  CD  GLU C 295     -55.232   2.926  55.373  1.00 72.53           C  
ANISOU 7206  CD  GLU C 295     7268   9200  11089    166   -349   -557       C  
ATOM   7207  OE1 GLU C 295     -56.130   3.783  55.583  1.00 73.81           O  
ANISOU 7207  OE1 GLU C 295     7351   9373  11319    106   -332   -614       O  
ATOM   7208  OE2 GLU C 295     -54.004   3.128  55.599  1.00 70.75           O  
ANISOU 7208  OE2 GLU C 295     7024   9032  10825    240   -391   -575       O  
ATOM   7209  N   TYR C 296     -55.013   2.609  50.984  1.00 59.98           N  
ANISOU 7209  N   TYR C 296     5683   7378   9727    115   -419   -464       N  
ATOM   7210  CA  TYR C 296     -53.962   3.320  50.210  1.00 60.07           C  
ANISOU 7210  CA  TYR C 296     5636   7396   9789    147   -470   -486       C  
ATOM   7211  C   TYR C 296     -54.096   4.839  50.359  1.00 60.97           C  
ANISOU 7211  C   TYR C 296     5635   7541   9987    120   -484   -565       C  
ATOM   7212  O   TYR C 296     -55.226   5.362  50.232  1.00 62.39           O  
ANISOU 7212  O   TYR C 296     5776   7691  10235     63   -465   -588       O  
ATOM   7213  CB  TYR C 296     -54.056   2.993  48.721  1.00 58.97           C  
ANISOU 7213  CB  TYR C 296     5518   7178   9710    125   -484   -443       C  
ATOM   7214  CG  TYR C 296     -52.856   3.452  47.942  1.00 58.76           C  
ANISOU 7214  CG  TYR C 296     5454   7158   9711    160   -530   -454       C  
ATOM   7215  CD1 TYR C 296     -51.770   2.611  47.773  1.00 58.85           C  
ANISOU 7215  CD1 TYR C 296     5522   7185   9654    223   -550   -420       C  
ATOM   7216  CD2 TYR C 296     -52.781   4.733  47.421  1.00 59.00           C  
ANISOU 7216  CD2 TYR C 296     5396   7186   9834    133   -550   -503       C  
ATOM   7217  CE1 TYR C 296     -50.638   3.020  47.093  1.00 58.63           C  
ANISOU 7217  CE1 TYR C 296     5454   7175   9647    252   -589   -440       C  
ATOM   7218  CE2 TYR C 296     -51.658   5.158  46.731  1.00 58.66           C  
ANISOU 7218  CE2 TYR C 296     5322   7152   9813    156   -584   -517       C  
ATOM   7219  CZ  TYR C 296     -50.587   4.295  46.566  1.00 58.58           C  
ANISOU 7219  CZ  TYR C 296     5360   7164   9733    213   -602   -489       C  
ATOM   7220  OH  TYR C 296     -49.470   4.683  45.890  1.00 59.31           O  
ANISOU 7220  OH  TYR C 296     5418   7275   9843    231   -632   -510       O  
ATOM   7221  N   LYS C 297     -52.959   5.515  50.571  1.00 62.08           N  
ANISOU 7221  N   LYS C 297     5723   7737  10125    162   -515   -610       N  
ATOM   7222  CA  LYS C 297     -52.831   6.996  50.699  1.00 60.91           C  
ANISOU 7222  CA  LYS C 297     5469   7616  10055    141   -529   -691       C  
ATOM   7223  C   LYS C 297     -51.644   7.465  49.851  1.00 56.93           C  
ANISOU 7223  C   LYS C 297     4934   7111   9586    161   -564   -705       C  
ATOM   7224  O   LYS C 297     -50.555   6.881  50.004  1.00 56.83           O  
ANISOU 7224  O   LYS C 297     4947   7144   9500    217   -581   -696       O  
ATOM   7225  CB  LYS C 297     -52.601   7.371  52.166  1.00 64.25           C  
ANISOU 7225  CB  LYS C 297     5854   8134  10421    167   -520   -751       C  
ATOM   7226  CG  LYS C 297     -52.447   8.860  52.451  1.00 66.98           C  
ANISOU 7226  CG  LYS C 297     6094   8513  10843    147   -529   -842       C  
ATOM   7227  CD  LYS C 297     -51.446   9.164  53.563  1.00 68.03           C  
ANISOU 7227  CD  LYS C 297     6184   8753  10909    196   -538   -906       C  
ATOM   7228  CE  LYS C 297     -51.376  10.634  53.911  1.00 68.58           C  
ANISOU 7228  CE  LYS C 297     6148   8852  11055    168   -540  -1004       C  
ATOM   7229  NZ  LYS C 297     -52.694  11.172  54.332  1.00 69.23           N  
ANISOU 7229  NZ  LYS C 297     6201   8913  11189    120   -515  -1030       N  
ATOM   7230  N   GLY C 298     -51.840   8.473  49.000  1.00 53.13           N  
ANISOU 7230  N   GLY C 298     4399   6578   9207    118   -573   -730       N  
ATOM   7231  CA  GLY C 298     -50.792   8.916  48.066  1.00 51.94           C  
ANISOU 7231  CA  GLY C 298     4225   6414   9093    123   -598   -739       C  
ATOM   7232  C   GLY C 298     -51.272   9.959  47.064  1.00 50.09           C  
ANISOU 7232  C   GLY C 298     3955   6104   8971     70   -602   -750       C  
ATOM   7233  O   GLY C 298     -52.455  10.248  46.968  1.00 49.96           O  
ANISOU 7233  O   GLY C 298     3934   6041   9006     37   -591   -744       O  
ATOM   7234  N   PRO C 299     -50.346  10.556  46.288  1.00 49.07           N  
ANISOU 7234  N   PRO C 299     3800   5962   8879     63   -617   -767       N  
ATOM   7235  CA  PRO C 299     -50.709  11.560  45.292  1.00 48.95           C  
ANISOU 7235  CA  PRO C 299     3765   5869   8965     17   -619   -771       C  
ATOM   7236  C   PRO C 299     -51.414  10.963  44.065  1.00 48.09           C  
ANISOU 7236  C   PRO C 299     3712   5680   8879      4   -627   -693       C  
ATOM   7237  O   PRO C 299     -50.742  10.476  43.184  1.00 49.24           O  
ANISOU 7237  O   PRO C 299     3888   5811   9008     11   -638   -655       O  
ATOM   7238  CB  PRO C 299     -49.355  12.203  44.951  1.00 48.51           C  
ANISOU 7238  CB  PRO C 299     3674   5835   8920     13   -625   -814       C  
ATOM   7239  CG  PRO C 299     -48.375  11.091  45.162  1.00 48.55           C  
ANISOU 7239  CG  PRO C 299     3705   5909   8830     61   -636   -797       C  
ATOM   7240  CD  PRO C 299     -48.900  10.328  46.356  1.00 48.54           C  
ANISOU 7240  CD  PRO C 299     3723   5959   8758     98   -630   -790       C  
ATOM   7241  N   ILE C 300     -52.746  11.024  44.045  1.00 47.40           N  
ANISOU 7241  N   ILE C 300     3629   5550   8828    -14   -620   -679       N  
ATOM   7242  CA  ILE C 300     -53.611  10.508  42.943  1.00 46.75           C  
ANISOU 7242  CA  ILE C 300     3590   5400   8772    -28   -627   -617       C  
ATOM   7243  C   ILE C 300     -53.994  11.688  42.048  1.00 46.09           C  
ANISOU 7243  C   ILE C 300     3483   5247   8780    -53   -639   -629       C  
ATOM   7244  O   ILE C 300     -54.234  12.763  42.590  1.00 46.35           O  
ANISOU 7244  O   ILE C 300     3470   5280   8860    -62   -635   -685       O  
ATOM   7245  CB  ILE C 300     -54.860   9.789  43.498  1.00 46.79           C  
ANISOU 7245  CB  ILE C 300     3613   5409   8753    -34   -609   -604       C  
ATOM   7246  CG1 ILE C 300     -54.539   8.891  44.700  1.00 47.01           C  
ANISOU 7246  CG1 ILE C 300     3664   5506   8690    -10   -590   -606       C  
ATOM   7247  CG2 ILE C 300     -55.563   9.010  42.396  1.00 46.44           C  
ANISOU 7247  CG2 ILE C 300     3615   5311   8718    -46   -614   -545       C  
ATOM   7248  CD1 ILE C 300     -53.463   7.859  44.433  1.00 46.69           C  
ANISOU 7248  CD1 ILE C 300     3677   5484   8577     23   -598   -560       C  
ATOM   7249  N   THR C 301     -54.064  11.474  40.731  1.00 45.79           N  
ANISOU 7249  N   THR C 301     3480   5154   8764    -59   -654   -576       N  
ATOM   7250  CA  THR C 301     -54.431  12.499  39.710  1.00 45.24           C  
ANISOU 7250  CA  THR C 301     3406   5011   8773    -75   -669   -573       C  
ATOM   7251  C   THR C 301     -55.593  12.021  38.822  1.00 44.54           C  
ANISOU 7251  C   THR C 301     3343   4876   8701    -74   -682   -528       C  
ATOM   7252  O   THR C 301     -56.229  12.884  38.199  1.00 46.21           O  
ANISOU 7252  O   THR C 301     3547   5034   8974    -76   -696   -532       O  
ATOM   7253  CB  THR C 301     -53.225  12.882  38.842  1.00 45.40           C  
ANISOU 7253  CB  THR C 301     3440   5010   8800    -84   -674   -558       C  
ATOM   7254  OG1 THR C 301     -53.606  14.028  38.079  1.00 44.84           O  
ANISOU 7254  OG1 THR C 301     3368   4865   8801    -98   -682   -560       O  
ATOM   7255  CG2 THR C 301     -52.766  11.774  37.911  1.00 45.30           C  
ANISOU 7255  CG2 THR C 301     3473   4997   8741    -77   -683   -497       C  
ATOM   7256  N   ASP C 302     -55.845  10.715  38.720  1.00 43.37           N  
ANISOU 7256  N   ASP C 302     3229   4749   8501    -70   -677   -488       N  
ATOM   7257  CA  ASP C 302     -57.032  10.167  38.012  1.00 42.55           C  
ANISOU 7257  CA  ASP C 302     3141   4614   8410    -75   -684   -459       C  
ATOM   7258  C   ASP C 302     -57.680   9.101  38.886  1.00 41.78           C  
ANISOU 7258  C   ASP C 302     3053   4558   8263    -82   -659   -463       C  
ATOM   7259  O   ASP C 302     -56.962   8.409  39.610  1.00 40.88           O  
ANISOU 7259  O   ASP C 302     2960   4484   8087    -74   -642   -456       O  
ATOM   7260  CB  ASP C 302     -56.696   9.579  36.641  1.00 42.77           C  
ANISOU 7260  CB  ASP C 302     3211   4609   8428    -73   -700   -401       C  
ATOM   7261  CG  ASP C 302     -56.036  10.565  35.701  1.00 43.77           C  
ANISOU 7261  CG  ASP C 302     3340   4693   8595    -72   -719   -390       C  
ATOM   7262  OD1 ASP C 302     -56.653  11.626  35.454  1.00 43.89           O  
ANISOU 7262  OD1 ASP C 302     3337   4669   8669    -70   -732   -410       O  
ATOM   7263  OD2 ASP C 302     -54.903  10.262  35.233  1.00 44.72           O  
ANISOU 7263  OD2 ASP C 302     3484   4819   8685    -73   -720   -364       O  
ATOM   7264  N   VAL C 303     -59.009   9.010  38.830  1.00 41.72           N  
ANISOU 7264  N   VAL C 303     3029   4541   8279    -94   -655   -478       N  
ATOM   7265  CA  VAL C 303     -59.781   7.888  39.428  1.00 41.37           C  
ANISOU 7265  CA  VAL C 303     3001   4526   8189   -114   -624   -479       C  
ATOM   7266  C   VAL C 303     -60.903   7.547  38.458  1.00 41.25           C  
ANISOU 7266  C   VAL C 303     2986   4484   8203   -129   -631   -471       C  
ATOM   7267  O   VAL C 303     -61.585   8.474  38.001  1.00 41.06           O  
ANISOU 7267  O   VAL C 303     2920   4440   8238   -120   -656   -500       O  
ATOM   7268  CB  VAL C 303     -60.297   8.235  40.832  1.00 41.56           C  
ANISOU 7268  CB  VAL C 303     2988   4595   8207   -125   -599   -535       C  
ATOM   7269  CG1 VAL C 303     -60.942   7.031  41.495  1.00 41.48           C  
ANISOU 7269  CG1 VAL C 303     3007   4613   8139   -152   -557   -530       C  
ATOM   7270  CG2 VAL C 303     -59.201   8.797  41.726  1.00 41.70           C  
ANISOU 7270  CG2 VAL C 303     2993   4644   8206   -106   -598   -555       C  
ATOM   7271  N   PHE C 304     -61.023   6.264  38.117  1.00 41.83           N  
ANISOU 7271  N   PHE C 304     3105   4555   8233   -145   -613   -435       N  
ATOM   7272  CA  PHE C 304     -62.090   5.713  37.245  1.00 42.12           C  
ANISOU 7272  CA  PHE C 304     3141   4577   8286   -165   -613   -434       C  
ATOM   7273  C   PHE C 304     -63.137   5.050  38.143  1.00 42.95           C  
ANISOU 7273  C   PHE C 304     3238   4713   8367   -205   -567   -471       C  
ATOM   7274  O   PHE C 304     -62.778   4.367  39.124  1.00 42.43           O  
ANISOU 7274  O   PHE C 304     3210   4667   8243   -218   -530   -460       O  
ATOM   7275  CB  PHE C 304     -61.487   4.771  36.205  1.00 41.78           C  
ANISOU 7275  CB  PHE C 304     3152   4506   8214   -162   -620   -375       C  
ATOM   7276  CG  PHE C 304     -60.499   5.445  35.291  1.00 41.90           C  
ANISOU 7276  CG  PHE C 304     3172   4494   8252   -130   -660   -343       C  
ATOM   7277  CD1 PHE C 304     -60.845   5.778  33.989  1.00 41.89           C  
ANISOU 7277  CD1 PHE C 304     3161   4466   8289   -121   -693   -331       C  
ATOM   7278  CD2 PHE C 304     -59.227   5.774  35.739  1.00 41.91           C  
ANISOU 7278  CD2 PHE C 304     3186   4504   8233   -111   -664   -330       C  
ATOM   7279  CE1 PHE C 304     -59.927   6.392  33.146  1.00 41.80           C  
ANISOU 7279  CE1 PHE C 304     3160   4427   8291    -98   -723   -299       C  
ATOM   7280  CE2 PHE C 304     -58.326   6.414  34.901  1.00 41.78           C  
ANISOU 7280  CE2 PHE C 304     3173   4465   8237    -92   -693   -307       C  
ATOM   7281  CZ  PHE C 304     -58.676   6.719  33.607  1.00 41.50           C  
ANISOU 7281  CZ  PHE C 304     3135   4396   8237    -88   -720   -289       C  
ATOM   7282  N   TYR C 305     -64.413   5.302  37.836  1.00 44.24           N  
ANISOU 7282  N   TYR C 305     3353   4885   8570   -222   -570   -518       N  
ATOM   7283  CA  TYR C 305     -65.589   4.747  38.551  1.00 44.90           C  
ANISOU 7283  CA  TYR C 305     3416   5004   8638   -270   -524   -568       C  
ATOM   7284  C   TYR C 305     -66.479   4.052  37.526  1.00 47.35           C  
ANISOU 7284  C   TYR C 305     3722   5308   8960   -295   -521   -577       C  
ATOM   7285  O   TYR C 305     -66.610   4.589  36.405  1.00 47.61           O  
ANISOU 7285  O   TYR C 305     3729   5323   9036   -263   -569   -575       O  
ATOM   7286  CB  TYR C 305     -66.340   5.865  39.267  1.00 43.71           C  
ANISOU 7286  CB  TYR C 305     3190   4887   8529   -264   -531   -642       C  
ATOM   7287  CG  TYR C 305     -65.543   6.611  40.304  1.00 42.79           C  
ANISOU 7287  CG  TYR C 305     3067   4783   8405   -243   -533   -646       C  
ATOM   7288  CD1 TYR C 305     -65.625   6.272  41.645  1.00 42.77           C  
ANISOU 7288  CD1 TYR C 305     3071   4821   8357   -271   -486   -669       C  
ATOM   7289  CD2 TYR C 305     -64.719   7.673  39.954  1.00 42.08           C  
ANISOU 7289  CD2 TYR C 305     2967   4667   8353   -197   -577   -632       C  
ATOM   7290  CE1 TYR C 305     -64.901   6.959  42.608  1.00 42.75           C  
ANISOU 7290  CE1 TYR C 305     3057   4840   8345   -249   -489   -680       C  
ATOM   7291  CE2 TYR C 305     -63.994   8.375  40.906  1.00 41.81           C  
ANISOU 7291  CE2 TYR C 305     2921   4649   8315   -181   -576   -647       C  
ATOM   7292  CZ  TYR C 305     -64.083   8.016  42.240  1.00 42.14           C  
ANISOU 7292  CZ  TYR C 305     2961   4738   8309   -204   -534   -673       C  
ATOM   7293  OH  TYR C 305     -63.372   8.688  43.193  1.00 41.97           O  
ANISOU 7293  OH  TYR C 305     2923   4741   8280   -187   -534   -694       O  
ATOM   7294  N   LYS C 306     -67.049   2.900  37.892  1.00 50.66           N  
ANISOU 7294  N   LYS C 306     4169   5740   9339   -351   -465   -587       N  
ATOM   7295  CA  LYS C 306     -68.086   2.197  37.083  1.00 53.31           C  
ANISOU 7295  CA  LYS C 306     4489   6081   9685   -390   -450   -618       C  
ATOM   7296  C   LYS C 306     -69.399   2.986  37.202  1.00 55.07           C  
ANISOU 7296  C   LYS C 306     4616   6351   9955   -397   -460   -709       C  
ATOM   7297  O   LYS C 306     -69.700   3.463  38.315  1.00 56.70           O  
ANISOU 7297  O   LYS C 306     4792   6591  10160   -409   -439   -752       O  
ATOM   7298  CB  LYS C 306     -68.236   0.743  37.543  1.00 54.67           C  
ANISOU 7298  CB  LYS C 306     4727   6246   9798   -455   -378   -603       C  
ATOM   7299  CG  LYS C 306     -68.523  -0.256  36.428  1.00 55.78           C  
ANISOU 7299  CG  LYS C 306     4893   6363   9936   -482   -368   -592       C  
ATOM   7300  CD  LYS C 306     -69.129  -1.567  36.898  1.00 57.87           C  
ANISOU 7300  CD  LYS C 306     5206   6625  10157   -563   -286   -608       C  
ATOM   7301  CE  LYS C 306     -70.402  -1.984  36.166  1.00 59.01           C  
ANISOU 7301  CE  LYS C 306     5297   6794  10328   -616   -267   -679       C  
ATOM   7302  NZ  LYS C 306     -70.245  -1.972  34.689  1.00 58.99           N  
ANISOU 7302  NZ  LYS C 306     5278   6777  10356   -578   -322   -663       N  
ATOM   7303  N   GLU C 307     -70.140   3.143  36.101  1.00 56.26           N  
ANISOU 7303  N   GLU C 307     4719   6511  10143   -384   -493   -742       N  
ATOM   7304  CA  GLU C 307     -71.484   3.787  36.101  1.00 56.85           C  
ANISOU 7304  CA  GLU C 307     4699   6640  10260   -385   -506   -840       C  
ATOM   7305  C   GLU C 307     -72.349   3.168  34.999  1.00 56.91           C  
ANISOU 7305  C   GLU C 307     4677   6667  10277   -404   -510   -876       C  
ATOM   7306  O   GLU C 307     -71.804   2.720  33.980  1.00 55.68           O  
ANISOU 7306  O   GLU C 307     4564   6476  10114   -387   -532   -819       O  
ATOM   7307  CB  GLU C 307     -71.353   5.301  35.908  1.00 57.36           C  
ANISOU 7307  CB  GLU C 307     4717   6699  10376   -306   -576   -851       C  
ATOM   7308  CG  GLU C 307     -72.639   6.090  36.167  1.00 57.55           C  
ANISOU 7308  CG  GLU C 307     4645   6779  10441   -294   -592   -955       C  
ATOM   7309  CD  GLU C 307     -73.147   6.089  37.603  1.00 57.60           C  
ANISOU 7309  CD  GLU C 307     4618   6833  10433   -343   -538  -1018       C  
ATOM   7310  OE1 GLU C 307     -73.807   5.110  37.995  1.00 58.94           O  
ANISOU 7310  OE1 GLU C 307     4784   7039  10571   -418   -475  -1056       O  
ATOM   7311  OE2 GLU C 307     -72.882   7.064  38.332  1.00 56.37           O  
ANISOU 7311  OE2 GLU C 307     4443   6677  10298   -311   -555  -1030       O  
ATOM   7312  N   ASN C 308     -73.664   3.149  35.211  1.00 58.61           N  
ANISOU 7312  N   ASN C 308     4817   6945  10507   -438   -490   -976       N  
ATOM   7313  CA  ASN C 308     -74.681   2.693  34.226  1.00 59.10           C  
ANISOU 7313  CA  ASN C 308     4827   7047  10582   -454   -496  -1039       C  
ATOM   7314  C   ASN C 308     -75.553   3.898  33.863  1.00 59.60           C  
ANISOU 7314  C   ASN C 308     4791   7159  10695   -387   -562  -1117       C  
ATOM   7315  O   ASN C 308     -75.487   4.360  32.694  1.00 59.82           O  
ANISOU 7315  O   ASN C 308     4807   7175  10745   -316   -630  -1099       O  
ATOM   7316  CB  ASN C 308     -75.520   1.543  34.788  1.00 59.02           C  
ANISOU 7316  CB  ASN C 308     4809   7075  10541   -560   -407  -1102       C  
ATOM   7317  CG  ASN C 308     -76.255   0.765  33.723  1.00 59.17           C  
ANISOU 7317  CG  ASN C 308     4798   7121  10562   -591   -400  -1150       C  
ATOM   7318  OD1 ASN C 308     -77.144  -0.022  34.036  1.00 60.95           O  
ANISOU 7318  OD1 ASN C 308     4996   7387  10772   -678   -332  -1225       O  
ATOM   7319  ND2 ASN C 308     -75.907   0.979  32.466  1.00 58.20           N  
ANISOU 7319  ND2 ASN C 308     4678   6978  10456   -526   -467  -1111       N  
ATOM   7320  N   SER C 309     -76.307   4.378  34.857  1.00 58.59           N  
ANISOU 7320  N   SER C 309     4600   7082  10580   -404   -541  -1200       N  
ATOM   7321  CA  SER C 309     -77.256   5.510  34.766  1.00 58.15           C  
ANISOU 7321  CA  SER C 309     4443   7080  10568   -342   -596  -1292       C  
ATOM   7322  C   SER C 309     -77.413   6.123  36.161  1.00 57.83           C  
ANISOU 7322  C   SER C 309     4373   7064  10534   -357   -570  -1336       C  
ATOM   7323  O   SER C 309     -77.800   5.379  37.087  1.00 59.02           O  
ANISOU 7323  O   SER C 309     4520   7251  10654   -447   -491  -1377       O  
ATOM   7324  CB  SER C 309     -78.573   5.052  34.209  1.00 58.88           C  
ANISOU 7324  CB  SER C 309     4452   7252  10666   -369   -590  -1400       C  
ATOM   7325  OG  SER C 309     -79.337   6.157  33.762  1.00 60.06           O  
ANISOU 7325  OG  SER C 309     4515   7446  10857   -279   -665  -1474       O  
ATOM   7326  N   TYR C 310     -77.084   7.411  36.312  1.00 55.77           N  
ANISOU 7326  N   TYR C 310     4099   6780  10310   -275   -629  -1326       N  
ATOM   7327  CA  TYR C 310     -77.330   8.204  37.544  1.00 54.96           C  
ANISOU 7327  CA  TYR C 310     3952   6707  10224   -273   -618  -1383       C  
ATOM   7328  C   TYR C 310     -78.346   9.313  37.264  1.00 56.61           C  
ANISOU 7328  C   TYR C 310     4062   6962  10483   -196   -682  -1483       C  
ATOM   7329  O   TYR C 310     -78.316   9.893  36.159  1.00 57.13           O  
ANISOU 7329  O   TYR C 310     4129   6999  10577   -111   -756  -1462       O  
ATOM   7330  CB  TYR C 310     -76.046   8.846  38.057  1.00 52.23           C  
ANISOU 7330  CB  TYR C 310     3672   6292   9881   -240   -631  -1296       C  
ATOM   7331  CG  TYR C 310     -76.225   9.688  39.297  1.00 50.58           C  
ANISOU 7331  CG  TYR C 310     3418   6111   9689   -235   -622  -1354       C  
ATOM   7332  CD1 TYR C 310     -76.377   9.102  40.541  1.00 49.90           C  
ANISOU 7332  CD1 TYR C 310     3328   6068   9562   -317   -546  -1385       C  
ATOM   7333  CD2 TYR C 310     -76.230  11.074  39.229  1.00 49.75           C  
ANISOU 7333  CD2 TYR C 310     3278   5986   9636   -149   -686  -1378       C  
ATOM   7334  CE1 TYR C 310     -76.508   9.868  41.689  1.00 49.76           C  
ANISOU 7334  CE1 TYR C 310     3267   6081   9556   -313   -537  -1439       C  
ATOM   7335  CE2 TYR C 310     -76.360  11.853  40.367  1.00 49.38           C  
ANISOU 7335  CE2 TYR C 310     3189   5965   9608   -145   -678  -1435       C  
ATOM   7336  CZ  TYR C 310     -76.504  11.249  41.600  1.00 49.38           C  
ANISOU 7336  CZ  TYR C 310     3178   6017   9567   -227   -604  -1468       C  
ATOM   7337  OH  TYR C 310     -76.644  12.016  42.716  1.00 49.56           O  
ANISOU 7337  OH  TYR C 310     3154   6070   9604   -222   -595  -1528       O  
ATOM   7338  N   THR C 311     -79.206   9.592  38.250  1.00 57.79           N  
ANISOU 7338  N   THR C 311     4133   7182  10640   -223   -655  -1588       N  
ATOM   7339  CA  THR C 311     -80.062  10.807  38.328  1.00 58.14           C  
ANISOU 7339  CA  THR C 311     4085   7271  10735   -144   -714  -1689       C  
ATOM   7340  C   THR C 311     -80.054  11.305  39.782  1.00 59.15           C  
ANISOU 7340  C   THR C 311     4185   7422  10866   -172   -677  -1734       C  
ATOM   7341  O   THR C 311     -80.166  10.458  40.698  1.00 58.25           O  
ANISOU 7341  O   THR C 311     4074   7348  10709   -273   -594  -1752       O  
ATOM   7342  CB  THR C 311     -81.453  10.525  37.752  1.00 58.11           C  
ANISOU 7342  CB  THR C 311     3983   7358  10737   -143   -726  -1808       C  
ATOM   7343  OG1 THR C 311     -81.296   9.868  36.495  1.00 56.78           O  
ANISOU 7343  OG1 THR C 311     3852   7167  10554   -134   -746  -1755       O  
ATOM   7344  CG2 THR C 311     -82.259  11.785  37.545  1.00 58.70           C  
ANISOU 7344  CG2 THR C 311     3971   7470  10861    -34   -806  -1901       C  
ATOM   7345  N   THR C 312     -79.868  12.615  39.980  1.00 60.93           N  
ANISOU 7345  N   THR C 312     4394   7618  11138    -86   -735  -1745       N  
ATOM   7346  CA  THR C 312     -79.744  13.271  41.309  1.00 62.78           C  
ANISOU 7346  CA  THR C 312     4603   7868  11382    -97   -712  -1784       C  
ATOM   7347  C   THR C 312     -81.129  13.522  41.904  1.00 65.23           C  
ANISOU 7347  C   THR C 312     4792   8286  11707   -107   -702  -1939       C  
ATOM   7348  O   THR C 312     -82.080  13.744  41.131  1.00 64.77           O  
ANISOU 7348  O   THR C 312     4666   8269  11672    -54   -750  -2014       O  
ATOM   7349  CB  THR C 312     -78.994  14.607  41.239  1.00 63.47           C  
ANISOU 7349  CB  THR C 312     4721   7875  11518     -3   -775  -1741       C  
ATOM   7350  OG1 THR C 312     -78.891  15.087  42.578  1.00 64.96           O  
ANISOU 7350  OG1 THR C 312     4881   8090  11711    -28   -743  -1787       O  
ATOM   7351  CG2 THR C 312     -79.678  15.661  40.399  1.00 63.71           C  
ANISOU 7351  CG2 THR C 312     4704   7898  11604    110   -863  -1796       C  
ATOM   7352  N   THR C 313     -81.203  13.513  43.237  1.00 67.92           N  
ANISOU 7352  N   THR C 313     5105   8672  12029   -169   -644  -1985       N  
ATOM   7353  CA  THR C 313     -82.413  13.807  44.049  1.00 70.75           C  
ANISOU 7353  CA  THR C 313     5346   9137  12397   -189   -625  -2137       C  
ATOM   7354  C   THR C 313     -82.293  15.245  44.580  1.00 74.14           C  
ANISOU 7354  C   THR C 313     5740   9548  12880   -103   -678  -2177       C  
ATOM   7355  O   THR C 313     -82.345  15.435  45.824  1.00 76.92           O  
ANISOU 7355  O   THR C 313     6059   9945  13220   -147   -634  -2228       O  
ATOM   7356  CB  THR C 313     -82.582  12.744  45.144  1.00 69.63           C  
ANISOU 7356  CB  THR C 313     5205   9058  12191   -323   -517  -2159       C  
ATOM   7357  OG1 THR C 313     -81.468  12.810  46.035  1.00 69.34           O  
ANISOU 7357  OG1 THR C 313     5244   8973  12130   -347   -485  -2075       O  
ATOM   7358  CG2 THR C 313     -82.677  11.340  44.589  1.00 68.88           C  
ANISOU 7358  CG2 THR C 313     5155   8967  12047   -408   -462  -2118       C  
ATOM   7359  N   ILE C 314     -82.124  16.214  43.665  1.00 76.03           N  
ANISOU 7359  N   ILE C 314     5993   9720  13173     14   -768  -2153       N  
ATOM   7360  CA  ILE C 314     -81.901  17.664  43.975  1.00 77.18           C  
ANISOU 7360  CA  ILE C 314     6125   9820  13377    108   -826  -2176       C  
ATOM   7361  C   ILE C 314     -82.859  18.534  43.141  1.00 78.01           C  
ANISOU 7361  C   ILE C 314     6165   9938  13534    226   -914  -2260       C  
ATOM   7362  O   ILE C 314     -83.055  18.316  41.948  1.00 78.38           O  
ANISOU 7362  O   ILE C 314     6232   9966  13581    272   -958  -2229       O  
ATOM   7363  CB  ILE C 314     -80.407  18.008  43.769  1.00 76.23           C  
ANISOU 7363  CB  ILE C 314     6120   9577  13264    130   -839  -2036       C  
ATOM   7364  CG1 ILE C 314     -79.583  17.559  44.984  1.00 75.77           C  
ANISOU 7364  CG1 ILE C 314     6097   9526  13163     39   -764  -1996       C  
ATOM   7365  CG2 ILE C 314     -80.191  19.484  43.447  1.00 76.12           C  
ANISOU 7365  CG2 ILE C 314     6118   9486  13319    247   -917  -2039       C  
ATOM   7366  CD1 ILE C 314     -78.078  17.487  44.745  1.00 74.90           C  
ANISOU 7366  CD1 ILE C 314     6100   9317  13041     35   -760  -1856       C  
TER    7367      ILE C 314                                                      
HETATM 7368 ZN    ZN A 501       1.616  34.502  41.678  1.00107.70          ZN  
ANISOU 7368 ZN    ZN A 501     8716  15006  17197    399  -1646   1627      ZN  
HETATM 7369 CL    CL A 502     -39.188  28.854  36.327  1.00 52.03          CL  
ANISOU 7369 CL    CL A 502     4758   6302   8707   -370   -373    340      CL  
HETATM 7370 ZN    ZN B 501     -34.608 -29.424  41.730  1.00103.41          ZN  
ANISOU 7370 ZN    ZN B 501    11623  11018  16650  -1454   2548   -411      ZN  
HETATM 7371 CL    CL B 502     -18.679   8.588  36.384  1.00 59.10          CL  
ANISOU 7371 CL    CL B 502     5766   6982   9707    -26   -398    169      CL  
HETATM 7372 ZN    ZN C 401     -35.337  13.022  37.125  1.00 53.87          ZN  
ANISOU 7372 ZN    ZN C 401     6839   5271   8356   -588  -1549    599      ZN  
HETATM 7373 ZN    ZN C 402     -72.359  34.497  40.498  1.00117.57          ZN  
ANISOU 7373 ZN    ZN C 402    12262  13176  19231    941  -1228  -1661      ZN  
HETATM 7374 CL    CL C 403     -47.139   1.680  36.120  1.00 58.54          CL  
ANISOU 7374 CL    CL C 403     5478   6886   9877    184   -741   -255      CL  
CONECT 1497 7368                                                                
CONECT 1519 7368                                                                
CONECT 2106 7372                                                                
CONECT 3966 7370                                                                
CONECT 3988 7370                                                                
CONECT 4560 7372                                                                
CONECT 6400 7373                                                                
CONECT 6422 7373                                                                
CONECT 6669 7373                                                                
CONECT 7013 7372                                                                
CONECT 7368 1497 1519                                                           
CONECT 7370 3966 3988                                                           
CONECT 7372 2106 4560 7013                                                      
CONECT 7373 6400 6422 6669                                                      
MASTER      441    0    7   27   66    0    0    6 7371    3   14   75          
END                                                                             
HEADER    VIRAL PROTEIN                           23-MAR-20   6W9Q              
TITLE     PEPTIDE-BOUND SARS-COV-2 NSP9 RNA-REPLICASE                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3C-LIKE PROTEINASE PEPTIDE, NON-STRUCTURAL PROTEIN 9       
COMPND   3 FUSION;                                                              
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: 3CL-PRO, 3CLP, NSP9;                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 VARIANT: SARS-COV-2;                                                 
SOURCE   7 GENE: REP, 1A-1B;                                                    
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    COVID-19, SARS-COV-2, NSP9, RNA REPLICASE, VIRAL PROTEIN              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.R.LITTLER,B.S.GULLY,A.RIBOLDI-TUNNICLIFFE,J.ROSSJOHN                
REVDAT   3   09-SEP-20 6W9Q    1       JRNL                                     
REVDAT   2   06-MAY-20 6W9Q    1       COMPND SOURCE DBREF                      
REVDAT   1   08-APR-20 6W9Q    0                                                
JRNL        AUTH   D.R.LITTLER,B.S.GULLY,R.N.COLSON,J.ROSSJOHN                  
JRNL        TITL   CRYSTAL STRUCTURE OF THE SARS-COV-2 NON-STRUCTURAL PROTEIN   
JRNL        TITL 2 9, NSP9.                                                     
JRNL        REF    ISCIENCE                      V.  23 01258 2020              
JRNL        REFN                   ESSN 2589-0042                               
JRNL        PMID   32592996                                                     
JRNL        DOI    10.1016/J.ISCI.2020.101258                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.17.1_3660                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 9967                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 499                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.5100 -  3.2500    1.00     2514   132  0.1985 0.2120        
REMARK   3     2  3.2500 -  2.5800    1.00     2357   124  0.2814 0.2836        
REMARK   3     3  2.5800 -  2.2600    0.99     2306   123  0.2994 0.3301        
REMARK   3     4  2.2600 -  2.0500    0.99     2291   120  0.3463 0.3641        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.272            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.479           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.013            962                                  
REMARK   3   ANGLE     :  1.291           1307                                  
REMARK   3   CHIRALITY :  0.086            150                                  
REMARK   3   PLANARITY :  0.007            168                                  
REMARK   3   DIHEDRAL  : 27.430            352                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1072 -19.8321  -8.1387              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4030 T22:   0.3975                                     
REMARK   3      T33:   0.3170 T12:   0.0141                                     
REMARK   3      T13:   0.0605 T23:  -0.0246                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2857 L22:   2.5675                                     
REMARK   3      L33:   6.9825 L12:   1.5417                                     
REMARK   3      L13:   2.6042 L23:   1.2634                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0646 S12:   0.4934 S13:  -0.1000                       
REMARK   3      S21:  -0.2403 S22:  -0.1695 S23:   0.1287                       
REMARK   3      S31:   0.0184 S32:  -0.5675 S33:   0.1003                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6W9Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000247870.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95372                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10055                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.02400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1QZ8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2M AMSO4, 0.1M CITRATE-PHOSPHATE       
REMARK 280  PH4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z+1/2                                             
REMARK 290       7555   Y,X,-Z+1/4                                              
REMARK 290       8555   -Y,-X,-Z+3/4                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.82450            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       64.23675            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       21.41225            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       42.82450            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       21.41225            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       64.23675            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 304  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -19                                                      
REMARK 465     ALA A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     ALA A   -10                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A   1     -141.94     51.06                                   
REMARK 500    ASN A   2       61.64   -115.96                                   
REMARK 500    CYS A  23       88.44    -65.52                                   
REMARK 500    THR A  24      -93.74    -90.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 201                 
DBREF  6W9Q A  -19     0  PDB    6W9Q     6W9Q           -19      0             
DBREF  6W9Q A    1   113  UNP    P0DTD1   R1AB_SARS2    4141   4253             
SEQRES   1 A  133  MET ALA HIS HIS HIS HIS HIS HIS SER ALA ALA LEU GLU          
SEQRES   2 A  133  VAL LEU PHE GLN GLY PRO GLY ASN ASN GLU LEU SER PRO          
SEQRES   3 A  133  VAL ALA LEU ARG GLN MET SER CYS ALA ALA GLY THR THR          
SEQRES   4 A  133  GLN THR ALA CYS THR ASP ASP ASN ALA LEU ALA TYR TYR          
SEQRES   5 A  133  ASN THR THR LYS GLY GLY ARG PHE VAL LEU ALA LEU LEU          
SEQRES   6 A  133  SER ASP LEU GLN ASP LEU LYS TRP ALA ARG PHE PRO LYS          
SEQRES   7 A  133  SER ASP GLY THR GLY THR ILE TYR THR GLU LEU GLU PRO          
SEQRES   8 A  133  PRO CYS ARG PHE VAL THR ASP THR PRO LYS GLY PRO LYS          
SEQRES   9 A  133  VAL LYS TYR LEU TYR PHE ILE LYS GLY LEU ASN ASN LEU          
SEQRES  10 A  133  ASN ARG GLY MET VAL LEU GLY SER LEU ALA ALA THR VAL          
SEQRES  11 A  133  ARG LEU GLN                                                  
HET    PO4  A 201       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   2  PO4    O4 P 3-                                                      
FORMUL   3  HOH   *4(H2 O)                                                      
HELIX    1 AA1 ASN A   95  LEU A  106  1                                  12    
HELIX    2 AA2 LEU A  106  LEU A  112  1                                   7    
SHEET    1 AA1 2 GLU A  -7  GLN A  -3  0                                        
SHEET    2 AA1 2 LEU A   4  ALA A   8 -1  O  SER A   5   N  PHE A  -4           
SHEET    1 AA2 7 THR A  64  GLU A  68  0                                        
SHEET    2 AA2 7 TRP A  53  PRO A  57 -1  N  PHE A  56   O  ILE A  65           
SHEET    3 AA2 7 ARG A  10  GLY A  17 -1  N  ALA A  15   O  ARG A  55           
SHEET    4 AA2 7 ALA A  28  THR A  34 -1  O  ALA A  30   N  MET A  12           
SHEET    5 AA2 7 ARG A  39  SER A  46 -1  O  PHE A  40   N  ASN A  33           
SHEET    6 AA2 7 GLY A  82  PHE A  90 -1  O  TYR A  89   N  LEU A  44           
SHEET    7 AA2 7 CYS A  73  THR A  79 -1  N  CYS A  73   O  LEU A  88           
CISPEP   1 GLY A   -2    PRO A   -1          0         7.63                     
SITE     1 AC1  3 ALA A  -9  ARG A 111  GLN A 113                               
CRYST1   59.011   59.011   85.649  90.00  90.00  90.00 P 43 2 2      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016946  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016946  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011676        0.00000                         
ATOM      1  N   ALA A  -9      -1.341  -7.391  -8.502  1.00 55.13           N  
ANISOU    1  N   ALA A  -9     8898   5578   6472   -952     73   1880       N  
ATOM      2  CA  ALA A  -9      -2.086  -7.883  -7.324  1.00 68.54           C  
ANISOU    2  CA  ALA A  -9    10498   7169   8375   -623    107   1538       C  
ATOM      3  C   ALA A  -9      -1.655  -9.317  -6.972  1.00 67.20           C  
ANISOU    3  C   ALA A  -9    10014   7371   8146   -600    358   1326       C  
ATOM      4  O   ALA A  -9      -0.468  -9.480  -6.824  1.00 85.76           O  
ANISOU    4  O   ALA A  -9    12268   9874  10443   -831    465   1363       O  
ATOM      5  CB  ALA A  -9      -3.575  -7.720  -7.485  1.00 67.01           C  
ANISOU    5  CB  ALA A  -9    10371   6827   8264   -271    -46   1453       C  
ATOM      6  N   LEU A  -8      -2.592 -10.266  -6.856  1.00 62.73           N  
ANISOU    6  N   LEU A  -8     9308   6927   7599   -342    415   1124       N  
ATOM      7  CA  LEU A  -8      -2.327 -11.655  -6.380  1.00 48.91           C  
ANISOU    7  CA  LEU A  -8     7321   5416   5846   -297    589    922       C  
ATOM      8  C   LEU A  -8      -1.094 -12.306  -7.017  1.00 57.91           C  
ANISOU    8  C   LEU A  -8     8302   6853   6850   -474    728    965       C  
ATOM      9  O   LEU A  -8      -0.970 -12.283  -8.240  1.00 45.62           O  
ANISOU    9  O   LEU A  -8     6728   5493   5112   -555    750   1076       O  
ATOM     10  CB  LEU A  -8      -3.578 -12.514  -6.565  1.00 47.70           C  
ANISOU   10  CB  LEU A  -8     7078   5359   5688    -75    596    767       C  
ATOM     11  CG  LEU A  -8      -4.797 -12.086  -5.757  1.00 51.52           C  
ANISOU   11  CG  LEU A  -8     7609   5671   6294    121    497    641       C  
ATOM     12  CD1 LEU A  -8      -5.864 -13.157  -5.805  1.00 55.27           C  
ANISOU   12  CD1 LEU A  -8     7929   6330   6742    254    540    477       C  
ATOM     13  CD2 LEU A  -8      -4.420 -11.791  -4.321  1.00 51.18           C  
ANISOU   13  CD2 LEU A  -8     7587   5489   6371     85    511    538       C  
ATOM     14  N   GLU A  -7      -0.260 -12.926  -6.180  1.00 43.05           N  
ANISOU   14  N   GLU A  -7     6281   5036   5038   -507    810    853       N  
ATOM     15  CA  GLU A  -7       0.985 -13.598  -6.624  1.00 52.51           C  
ANISOU   15  CA  GLU A  -7     7267   6543   6143   -610    932    822       C  
ATOM     16  C   GLU A  -7       1.196 -14.900  -5.850  1.00 53.12           C  
ANISOU   16  C   GLU A  -7     7187   6658   6340   -449    968    616       C  
ATOM     17  O   GLU A  -7       0.680 -15.025  -4.736  1.00 46.89           O  
ANISOU   17  O   GLU A  -7     6468   5665   5681   -374    906    567       O  
ATOM     18  CB  GLU A  -7       2.195 -12.721  -6.319  1.00 55.09           C  
ANISOU   18  CB  GLU A  -7     7582   6901   6448   -877    934    956       C  
ATOM     19  CG  GLU A  -7       2.231 -11.436  -7.109  1.00 55.64           C  
ANISOU   19  CG  GLU A  -7     7834   6914   6394  -1121    868   1216       C  
ATOM     20  CD  GLU A  -7       2.842 -11.576  -8.487  1.00 68.39           C  
ANISOU   20  CD  GLU A  -7     9306   8938   7740  -1300    975   1316       C  
ATOM     21  OE1 GLU A  -7       2.303 -10.986  -9.418  1.00 69.50           O  
ANISOU   21  OE1 GLU A  -7     9609   9060   7739  -1385    908   1508       O  
ATOM     22  OE2 GLU A  -7       3.845 -12.278  -8.615  1.00 71.28           O  
ANISOU   22  OE2 GLU A  -7     9388   9667   8028  -1344   1115   1189       O  
ATOM     23  N   VAL A  -6       1.943 -15.820  -6.453  1.00 40.07           N  
ANISOU   23  N   VAL A  -6     5326   5269   4629   -402   1052    497       N  
ATOM     24  CA  VAL A  -6       2.321 -17.119  -5.833  1.00 39.57           C  
ANISOU   24  CA  VAL A  -6     5125   5205   4705   -227   1036    311       C  
ATOM     25  C   VAL A  -6       3.774 -17.392  -6.217  1.00 42.68           C  
ANISOU   25  C   VAL A  -6     5253   5921   5044   -250   1110    225       C  
ATOM     26  O   VAL A  -6       4.203 -16.902  -7.258  1.00 49.70           O  
ANISOU   26  O   VAL A  -6     6047   7100   5737   -386   1212    261       O  
ATOM     27  CB  VAL A  -6       1.408 -18.266  -6.289  1.00 42.57           C  
ANISOU   27  CB  VAL A  -6     5527   5529   5118    -38   1016    150       C  
ATOM     28  CG1 VAL A  -6      -0.015 -18.075  -5.809  1.00 42.61           C  
ANISOU   28  CG1 VAL A  -6     5725   5297   5169    -28    948    210       C  
ATOM     29  CG2 VAL A  -6       1.444 -18.447  -7.793  1.00 48.59           C  
ANISOU   29  CG2 VAL A  -6     6196   6570   5698    -21   1105     56       C  
ATOM     30  N   LEU A  -5       4.505 -18.128  -5.387  1.00 48.28           N  
ANISOU   30  N   LEU A  -5     5830   6613   5903   -129   1048    124       N  
ATOM     31  CA  LEU A  -5       5.906 -18.436  -5.709  1.00 49.68           C  
ANISOU   31  CA  LEU A  -5     5688   7144   6044    -96   1104     -8       C  
ATOM     32  C   LEU A  -5       5.927 -19.762  -6.447  1.00 60.63           C  
ANISOU   32  C   LEU A  -5     6936   8627   7474    198   1108   -298       C  
ATOM     33  O   LEU A  -5       5.581 -20.747  -5.869  1.00 65.07           O  
ANISOU   33  O   LEU A  -5     7581   8907   8234    409    971   -388       O  
ATOM     34  CB  LEU A  -5       6.725 -18.531  -4.435  1.00 51.45           C  
ANISOU   34  CB  LEU A  -5     5823   7309   6417    -80    991     21       C  
ATOM     35  CG  LEU A  -5       7.114 -17.201  -3.834  1.00 51.05           C  
ANISOU   35  CG  LEU A  -5     5823   7275   6297   -395    999    230       C  
ATOM     36  CD1 LEU A  -5       7.895 -17.405  -2.573  1.00 43.56           C  
ANISOU   36  CD1 LEU A  -5     4770   6306   5473   -371    870    234       C  
ATOM     37  CD2 LEU A  -5       7.913 -16.391  -4.814  1.00 46.99           C  
ANISOU   37  CD2 LEU A  -5     5129   7151   5574   -646   1142    276       C  
ATOM     38  N   PHE A  -4       6.260 -19.721  -7.715  1.00 52.52           N  
ANISOU   38  N   PHE A  -4     5728   7985   6242    174   1254   -430       N  
ATOM     39  CA  PHE A  -4       6.381 -20.927  -8.529  1.00 62.21           C  
ANISOU   39  CA  PHE A  -4     6790   9361   7484    463   1269   -785       C  
ATOM     40  C   PHE A  -4       7.660 -21.686  -8.190  1.00 63.11           C  
ANISOU   40  C   PHE A  -4     6581   9656   7743    714   1216  -1038       C  
ATOM     41  O   PHE A  -4       8.754 -21.110  -8.171  1.00 62.31           O  
ANISOU   41  O   PHE A  -4     6200   9945   7532    587   1304  -1017       O  
ATOM     42  CB  PHE A  -4       6.374 -20.526 -10.007  1.00 59.08           C  
ANISOU   42  CB  PHE A  -4     6275   9422   6752    320   1459   -854       C  
ATOM     43  CG  PHE A  -4       6.398 -21.678 -10.979  1.00 70.77           C  
ANISOU   43  CG  PHE A  -4     7593  11105   8192    598   1494  -1275       C  
ATOM     44  CD1 PHE A  -4       5.246 -22.401 -11.250  1.00 73.76           C  
ANISOU   44  CD1 PHE A  -4     8204  11168   8652    736   1405  -1384       C  
ATOM     45  CD2 PHE A  -4       7.561 -21.991 -11.683  1.00 80.48           C  
ANISOU   45  CD2 PHE A  -4     8412  12892   9273    700   1624  -1592       C  
ATOM     46  CE1 PHE A  -4       5.258 -23.444 -12.180  1.00 74.76           C  
ANISOU   46  CE1 PHE A  -4     8202  11464   8740    978   1422  -1812       C  
ATOM     47  CE2 PHE A  -4       7.580 -23.040 -12.625  1.00 77.22           C  
ANISOU   47  CE2 PHE A  -4     7839  12689   8810    984   1657  -2056       C  
ATOM     48  CZ  PHE A  -4       6.428 -23.761 -12.869  1.00 72.27           C  
ANISOU   48  CZ  PHE A  -4     7492  11679   8288   1121   1547  -2166       C  
ATOM     49  N   GLN A  -3       7.529 -22.991  -7.957  1.00 68.68           N  
ANISOU   49  N   GLN A  -3     7316  10079   8698   1070   1050  -1283       N  
ATOM     50  CA  GLN A  -3       8.695 -23.844  -7.717  1.00 71.95           C  
ANISOU   50  CA  GLN A  -3     7423  10621   9293   1407    944  -1573       C  
ATOM     51  C   GLN A  -3       9.317 -24.169  -9.073  1.00 67.42           C  
ANISOU   51  C   GLN A  -3     6491  10597   8530   1562   1117  -1988       C  
ATOM     52  O   GLN A  -3       9.059 -25.204  -9.691  1.00 72.77           O  
ANISOU   52  O   GLN A  -3     7170  11184   9296   1864   1059  -2348       O  
ATOM     53  CB  GLN A  -3       8.300 -25.092  -6.934  1.00 74.60           C  
ANISOU   53  CB  GLN A  -3     7983  10376   9987   1717    646  -1643       C  
ATOM     54  CG  GLN A  -3       7.766 -24.767  -5.528  1.00 77.39           C  
ANISOU   54  CG  GLN A  -3     8643  10300  10463   1524    490  -1233       C  
ATOM     55  CD  GLN A  -3       7.609 -25.986  -4.626  1.00 84.76           C  
ANISOU   55  CD  GLN A  -3     9771  10714  11721   1774    162  -1233       C  
ATOM     56  OE1 GLN A  -3       6.949 -26.960  -4.988  1.00 89.47           O  
ANISOU   56  OE1 GLN A  -3    10552  10989  12452   1929     45  -1390       O  
ATOM     57  NE2 GLN A  -3       8.218 -25.928  -3.435  1.00 87.89           N  
ANISOU   57  NE2 GLN A  -3    10144  11019  12232   1780    -11  -1036       N  
ATOM     58  N   GLY A  -2      10.147 -23.249  -9.549  1.00 73.25           N  
ANISOU   58  N   GLY A  -2     6914  11940   8978   1316   1334  -1949       N  
ATOM     59  CA  GLY A  -2      10.724 -23.382 -10.864  1.00 82.20           C  
ANISOU   59  CA  GLY A  -2     7673  13731   9828   1364   1548  -2310       C  
ATOM     60  C   GLY A  -2      11.229 -22.065 -11.415  1.00 82.23           C  
ANISOU   60  C   GLY A  -2     7510  14304   9430    865   1782  -2053       C  
ATOM     61  O   GLY A  -2      11.162 -21.026 -10.754  1.00 72.10           O  
ANISOU   61  O   GLY A  -2     6373  12905   8116    516   1788  -1639       O  
ATOM     62  N   PRO A  -1      11.719 -22.078 -12.666  1.00 87.56           N  
ANISOU   62  N   PRO A  -1     8015  15434   9819    761   1877  -2212       N  
ATOM     63  CA  PRO A  -1      11.668 -23.212 -13.606  1.00 95.19           C  
ANISOU   63  CA  PRO A  -1     8920  16457  10792   1083   1826  -2648       C  
ATOM     64  C   PRO A  -1      12.714 -24.301 -13.376  1.00 96.87           C  
ANISOU   64  C   PRO A  -1     8836  16724  11244   1524   1679  -3070       C  
ATOM     65  O   PRO A  -1      12.475 -25.454 -13.732  1.00104.44           O  
ANISOU   65  O   PRO A  -1     9849  17462  12371   1888   1549  -3428       O  
ATOM     66  CB  PRO A  -1      11.908 -22.548 -14.978  1.00100.94           C  
ANISOU   66  CB  PRO A  -1     9531  17763  11057    709   1994  -2594       C  
ATOM     67  CG  PRO A  -1      11.869 -21.066 -14.737  1.00103.22           C  
ANISOU   67  CG  PRO A  -1     9931  18148  11139    189   2094  -2073       C  
ATOM     68  CD  PRO A  -1      12.261 -20.871 -13.304  1.00 97.48           C  
ANISOU   68  CD  PRO A  -1     9170  17173  10697    250   2026  -1936       C  
ATOM     69  N   GLY A   0      13.859 -23.950 -12.802  1.00 96.57           N  
ANISOU   69  N   GLY A   0     8501  16966  11225   1485   1675  -3030       N  
ATOM     70  CA  GLY A   0      14.948 -24.887 -12.629  1.00105.10           C  
ANISOU   70  CA  GLY A   0     9269  18168  12496   1894   1526  -3419       C  
ATOM     71  C   GLY A   0      15.420 -24.958 -11.193  1.00103.50           C  
ANISOU   71  C   GLY A   0     9010  17690  12626   2079   1349  -3300       C  
ATOM     72  O   GLY A   0      14.933 -24.246 -10.312  1.00 99.49           O  
ANISOU   72  O   GLY A   0     8676  16939  12188   1870   1357  -2927       O  
ATOM     73  N   ASN A   1      16.392 -25.850 -10.972  1.00108.98           N  
ANISOU   73  N   ASN A   1     9445  18442  13521   2488   1168  -3634       N  
ATOM     74  CA  ASN A   1      17.052 -25.979  -9.681  1.00116.40           C  
ANISOU   74  CA  ASN A   1    10266  19209  14752   2689    960  -3544       C  
ATOM     75  C   ASN A   1      16.037 -26.117  -8.565  1.00107.62           C  
ANISOU   75  C   ASN A   1     9544  17382  13965   2783    775  -3260       C  
ATOM     76  O   ASN A   1      14.995 -26.762  -8.715  1.00107.25           O  
ANISOU   76  O   ASN A   1     9855  16823  14073   2941    683  -3304       O  
ATOM     77  CB  ASN A   1      17.936 -24.760  -9.391  1.00124.29           C  
ANISOU   77  CB  ASN A   1    10958  20768  15496   2264   1120  -3301       C  
ATOM     78  CG  ASN A   1      19.267 -24.810 -10.111  1.00141.04           C  
ANISOU   78  CG  ASN A   1    12618  23589  17382   2270   1200  -3614       C  
ATOM     79  OD1 ASN A   1      20.162 -25.570  -9.732  1.00150.44           O  
ANISOU   79  OD1 ASN A   1    13554  24833  18774   2670   1009  -3890       O  
ATOM     80  ND2 ASN A   1      19.416 -23.986 -11.145  1.00143.49           N  
ANISOU   80  ND2 ASN A   1    12818  24448  17254   1817   1462  -3560       N  
ATOM     81  N   ASN A   2      16.355 -25.487  -7.442  1.00101.78           N  
ANISOU   81  N   ASN A   2     8724  16641  13307   2654    709  -2968       N  
ATOM     82  CA  ASN A   2      15.372 -25.184  -6.424  1.00 90.40           C  
ANISOU   82  CA  ASN A   2     7598  14704  12045   2577    606  -2629       C  
ATOM     83  C   ASN A   2      15.274 -23.671  -6.326  1.00 88.21           C  
ANISOU   83  C   ASN A   2     7345  14721  11450   1947    853  -2232       C  
ATOM     84  O   ASN A   2      15.587 -23.086  -5.287  1.00 92.62           O  
ANISOU   84  O   ASN A   2     7941  15199  12050   1733    748  -1928       O  
ATOM     85  CB  ASN A   2      15.761 -25.802  -5.088  1.00 90.84           C  
ANISOU   85  CB  ASN A   2     7671  14373  12471   2908    221  -2549       C  
ATOM     86  CG  ASN A   2      16.064 -27.274  -5.200  1.00100.27           C  
ANISOU   86  CG  ASN A   2     8938  15204  13957   3433    -72  -2857       C  
ATOM     87  OD1 ASN A   2      17.228 -27.673  -5.235  1.00106.71           O  
ANISOU   87  OD1 ASN A   2     9434  16303  14808   3653   -165  -3073       O  
ATOM     88  ND2 ASN A   2      15.019 -28.095  -5.269  1.00 97.88           N  
ANISOU   88  ND2 ASN A   2     9070  14264  13856   3605   -228  -2874       N  
ATOM     89  N   GLU A   3      14.875 -23.017  -7.410  1.00 78.54           N  
ANISOU   89  N   GLU A   3     6139  13809   9893   1617   1152  -2214       N  
ATOM     90  CA  GLU A   3      14.676 -21.578  -7.364  1.00 64.17           C  
ANISOU   90  CA  GLU A   3     4468  12115   7797    996   1327  -1787       C  
ATOM     91  C   GLU A   3      13.186 -21.269  -7.257  1.00 61.07           C  
ANISOU   91  C   GLU A   3     4682  11095   7428    814   1301  -1472       C  
ATOM     92  O   GLU A   3      12.335 -22.122  -7.500  1.00 67.29           O  
ANISOU   92  O   GLU A   3     5709  11504   8356   1094   1219  -1608       O  
ATOM     93  CB  GLU A   3      15.284 -20.892  -8.591  1.00 82.79           C  
ANISOU   93  CB  GLU A   3     6549  15161   9746    648   1601  -1844       C  
ATOM     94  CG  GLU A   3      14.363 -20.852  -9.797  1.00 84.96           C  
ANISOU   94  CG  GLU A   3     7076  15405   9798    537   1745  -1852       C  
ATOM     95  CD  GLU A   3      15.013 -20.165 -11.003  1.00 97.86           C  
ANISOU   95  CD  GLU A   3     8558  17606  11021    149   1908  -1821       C  
ATOM     96  OE1 GLU A   3      15.373 -20.874 -11.973  1.00100.49           O  
ANISOU   96  OE1 GLU A   3     8706  18234  11243    356   1933  -2172       O  
ATOM     97  OE2 GLU A   3      15.171 -18.920 -10.969  1.00 99.81           O  
ANISOU   97  OE2 GLU A   3     8882  17982  11059   -372   1983  -1447       O  
ATOM     98  N   LEU A   4      12.881 -20.035  -6.864  1.00 58.33           N  
ANISOU   98  N   LEU A   4     4571  10640   6953    345   1351  -1068       N  
ATOM     99  CA  LEU A   4      11.511 -19.601  -6.623  1.00 64.31           C  
ANISOU   99  CA  LEU A   4     5858  10837   7740    183   1309   -776       C  
ATOM    100  C   LEU A   4      11.274 -18.351  -7.451  1.00 48.96           C  
ANISOU  100  C   LEU A   4     4006   9121   5478   -283   1502   -541       C  
ATOM    101  O   LEU A   4      12.041 -17.392  -7.360  1.00 51.74           O  
ANISOU  101  O   LEU A   4     4211   9771   5678   -649   1570   -376       O  
ATOM    102  CB  LEU A   4      11.256 -19.328  -5.122  1.00 47.49           C  
ANISOU  102  CB  LEU A   4     3991   8235   5818    124   1108   -524       C  
ATOM    103  CG  LEU A   4      11.292 -20.560  -4.211  1.00 54.77           C  
ANISOU  103  CG  LEU A   4     4932   8834   7044    536    861   -652       C  
ATOM    104  CD1 LEU A   4      11.188 -20.173  -2.725  1.00 51.08           C  
ANISOU  104  CD1 LEU A   4     4670   8048   6688    400    683   -387       C  
ATOM    105  CD2 LEU A   4      10.191 -21.519  -4.585  1.00 50.61           C  
ANISOU  105  CD2 LEU A   4     4669   7924   6636    793    802   -761       C  
ATOM    106  N   SER A   5      10.218 -18.362  -8.264  1.00 55.20           N  
ANISOU  106  N   SER A   5     5045   9765   6164   -290   1562   -509       N  
ATOM    107  CA  SER A   5       9.876 -17.219  -9.076  1.00 53.28           C  
ANISOU  107  CA  SER A   5     4946   9669   5628   -704   1686   -244       C  
ATOM    108  C   SER A   5       8.463 -16.745  -8.766  1.00 47.76           C  
ANISOU  108  C   SER A   5     4738   8386   5023   -750   1576      8       C  
ATOM    109  O   SER A   5       7.513 -17.536  -8.846  1.00 46.90           O  
ANISOU  109  O   SER A   5     4788   8002   5032   -470   1516   -118       O  
ATOM    110  CB  SER A   5       9.988 -17.560 -10.588  1.00 56.36           C  
ANISOU  110  CB  SER A   5     5113  10594   5708   -703   1871   -447       C  
ATOM    111  OG  SER A   5      11.226 -18.207 -10.857  1.00 65.13           O  
ANISOU  111  OG  SER A   5     5713  12276   6757   -549   1973   -796       O  
ATOM    112  N   PRO A   6       8.279 -15.460  -8.448  1.00 44.94           N  
ANISOU  112  N   PRO A   6     4617   7840   4618  -1098   1535    342       N  
ATOM    113  CA  PRO A   6       6.921 -14.912  -8.278  1.00 47.21           C  
ANISOU  113  CA  PRO A   6     5330   7631   4977  -1108   1428    542       C  
ATOM    114  C   PRO A   6       6.219 -14.844  -9.622  1.00 52.09           C  
ANISOU  114  C   PRO A   6     6030   8397   5363  -1147   1492    588       C  
ATOM    115  O   PRO A   6       6.729 -14.229 -10.561  1.00 58.98           O  
ANISOU  115  O   PRO A   6     6815   9645   5950  -1450   1587    726       O  
ATOM    116  CB  PRO A   6       7.175 -13.508  -7.710  1.00 53.77           C  
ANISOU  116  CB  PRO A   6     6345   8277   5808  -1470   1354    834       C  
ATOM    117  CG  PRO A   6       8.629 -13.484  -7.330  1.00 59.14           C  
ANISOU  117  CG  PRO A   6     6696   9315   6459  -1637   1408    778       C  
ATOM    118  CD  PRO A   6       9.306 -14.438  -8.259  1.00 56.24           C  
ANISOU  118  CD  PRO A   6     5931   9505   5932  -1499   1567    528       C  
ATOM    119  N   VAL A   7       5.040 -15.476  -9.714  1.00 46.21           N  
ANISOU  119  N   VAL A   7     5450   7392   4715   -876   1433    487       N  
ATOM    120  CA  VAL A   7       4.175 -15.370 -10.883  1.00 62.36           C  
ANISOU  120  CA  VAL A   7     7612   9527   6554   -898   1448    545       C  
ATOM    121  C   VAL A   7       2.805 -14.891 -10.431  1.00 61.00           C  
ANISOU  121  C   VAL A   7     7778   8869   6530   -820   1291    700       C  
ATOM    122  O   VAL A   7       2.427 -15.026  -9.270  1.00 52.25           O  
ANISOU  122  O   VAL A   7     6768   7409   5675   -682   1206    659       O  
ATOM    123  CB  VAL A   7       4.035 -16.699 -11.654  1.00 60.64           C  
ANISOU  123  CB  VAL A   7     7203   9566   6269   -639   1527    199       C  
ATOM    124  CG1 VAL A   7       5.406 -17.279 -11.976  1.00 61.40           C  
ANISOU  124  CG1 VAL A   7     6910  10154   6264   -618   1672    -54       C  
ATOM    125  CG2 VAL A   7       3.210 -17.672 -10.859  1.00 55.01           C  
ANISOU  125  CG2 VAL A   7     6599   8447   5855   -324   1417     18       C  
ATOM    126  N   ALA A   8       2.060 -14.322 -11.376  1.00 60.47           N  
ANISOU  126  N   ALA A   8     7866   8832   6276   -911   1246    874       N  
ATOM    127  CA  ALA A   8       0.755 -13.755 -11.078  1.00 52.78           C  
ANISOU  127  CA  ALA A   8     7174   7457   5425   -812   1079   1008       C  
ATOM    128  C   ALA A   8      -0.283 -14.855 -10.912  1.00 53.68           C  
ANISOU  128  C   ALA A   8     7260   7476   5661   -512   1060    758       C  
ATOM    129  O   ALA A   8      -0.328 -15.798 -11.703  1.00 60.95           O  
ANISOU  129  O   ALA A   8     8039   8662   6458   -430   1135    564       O  
ATOM    130  CB  ALA A   8       0.327 -12.800 -12.184  1.00 57.74           C  
ANISOU  130  CB  ALA A   8     7972   8152   5813   -990    990   1298       C  
ATOM    131  N   LEU A   9      -1.107 -14.749  -9.862  1.00 44.58           N  
ANISOU  131  N   LEU A   9     6233   5966   4738   -373    960    739       N  
ATOM    132  CA  LEU A   9      -2.309 -15.580  -9.743  1.00 45.44           C  
ANISOU  132  CA  LEU A   9     6342   5995   4929   -167    917    567       C  
ATOM    133  C   LEU A   9      -3.458 -14.778 -10.345  1.00 53.58           C  
ANISOU  133  C   LEU A   9     7512   6967   5877   -130    788    710       C  
ATOM    134  O   LEU A   9      -4.112 -13.977  -9.664  1.00 49.43           O  
ANISOU  134  O   LEU A   9     7115   6183   5483    -61    674    787       O  
ATOM    135  CB  LEU A   9      -2.582 -15.967  -8.294  1.00 48.59           C  
ANISOU  135  CB  LEU A   9     6752   6146   5564    -74    890    464       C  
ATOM    136  CG  LEU A   9      -3.747 -16.933  -8.041  1.00 49.92           C  
ANISOU  136  CG  LEU A   9     6897   6266   5804     57    855    298       C  
ATOM    137  CD1 LEU A   9      -3.381 -18.341  -8.513  1.00 51.39           C  
ANISOU  137  CD1 LEU A   9     6968   6576   5982     97    907    102       C  
ATOM    138  CD2 LEU A   9      -4.127 -16.940  -6.548  1.00 60.44           C  
ANISOU  138  CD2 LEU A   9     8265   7399   7302     75    819    274       C  
ATOM    139  N   ARG A  10      -3.704 -14.996 -11.638  1.00 49.11           N  
ANISOU  139  N   ARG A  10     6910   6666   5085   -153    791    723       N  
ATOM    140  CA  ARG A  10      -4.627 -14.160 -12.398  1.00 48.31           C  
ANISOU  140  CA  ARG A  10     6939   6555   4860   -134    633    915       C  
ATOM    141  C   ARG A  10      -6.084 -14.529 -12.114  1.00 51.32           C  
ANISOU  141  C   ARG A  10     7298   6848   5354     84    533    770       C  
ATOM    142  O   ARG A  10      -6.399 -15.606 -11.595  1.00 50.60           O  
ANISOU  142  O   ARG A  10     7089   6770   5368    158    604    526       O  
ATOM    143  CB  ARG A  10      -4.326 -14.273 -13.893  1.00 51.52           C  
ANISOU  143  CB  ARG A  10     7297   7351   4925   -276    668    992       C  
ATOM    144  CG  ARG A  10      -2.915 -13.784 -14.259  1.00 63.59           C  
ANISOU  144  CG  ARG A  10     8810   9069   6281   -551    775   1161       C  
ATOM    145  CD  ARG A  10      -2.539 -14.137 -15.712  1.00 82.55           C  
ANISOU  145  CD  ARG A  10    11088  11995   8284   -710    867   1153       C  
ATOM    146  NE  ARG A  10      -1.261 -13.565 -16.149  1.00 94.10           N  
ANISOU  146  NE  ARG A  10    12503  13737   9515  -1034    973   1345       N  
ATOM    147  CZ  ARG A  10      -0.072 -14.149 -15.995  1.00104.25           C  
ANISOU  147  CZ  ARG A  10    13546  15295  10771  -1104   1180   1137       C  
ATOM    148  NH1 ARG A  10       1.024 -13.548 -16.446  1.00108.59           N  
ANISOU  148  NH1 ARG A  10    14017  16174  11068  -1444   1276   1327       N  
ATOM    149  NH2 ARG A  10       0.030 -15.329 -15.390  1.00105.45           N  
ANISOU  149  NH2 ARG A  10    13526  15397  11143   -844   1272    748       N  
ATOM    150  N   GLN A  11      -6.971 -13.600 -12.463  1.00 58.08           N  
ANISOU  150  N   GLN A  11     8267   7616   6183    175    343    935       N  
ATOM    151  CA  GLN A  11      -8.374 -13.623 -12.095  1.00 57.11           C  
ANISOU  151  CA  GLN A  11     8094   7426   6177    399    220    815       C  
ATOM    152  C   GLN A  11      -9.200 -13.465 -13.360  1.00 58.33           C  
ANISOU  152  C   GLN A  11     8245   7795   6121    455     63    912       C  
ATOM    153  O   GLN A  11      -8.857 -12.658 -14.229  1.00 53.91           O  
ANISOU  153  O   GLN A  11     7833   7258   5394    363    -49   1192       O  
ATOM    154  CB  GLN A  11      -8.708 -12.485 -11.105  1.00 64.47           C  
ANISOU  154  CB  GLN A  11     9147   8016   7333    545     87    874       C  
ATOM    155  CG  GLN A  11      -7.807 -12.471  -9.859  1.00 78.67           C  
ANISOU  155  CG  GLN A  11    10972   9619   9301    458    218    806       C  
ATOM    156  CD  GLN A  11      -8.053 -11.271  -8.959  1.00 88.48           C  
ANISOU  156  CD  GLN A  11    12351  10528  10739    589     80    825       C  
ATOM    157  OE1 GLN A  11      -9.206 -10.939  -8.657  1.00 91.02           O  
ANISOU  157  OE1 GLN A  11    12626  10805  11154    836    -45    701       O  
ATOM    158  NE2 GLN A  11      -6.968 -10.601  -8.529  1.00 89.05           N  
ANISOU  158  NE2 GLN A  11    12577  10384  10875    431     92    948       N  
ATOM    159  N   MET A  12     -10.240 -14.262 -13.494  1.00 53.68           N  
ANISOU  159  N   MET A  12     7489   7394   5514    558     46    703       N  
ATOM    160  CA  MET A  12     -11.103 -14.066 -14.669  1.00 62.00           C  
ANISOU  160  CA  MET A  12     8519   8679   6359    624   -137    791       C  
ATOM    161  C   MET A  12     -12.527 -14.392 -14.285  1.00 64.64           C  
ANISOU  161  C   MET A  12     8665   9097   6797    818   -231    583       C  
ATOM    162  O   MET A  12     -12.727 -15.242 -13.472  1.00 57.54           O  
ANISOU  162  O   MET A  12     7633   8207   6023    787    -94    344       O  
ATOM    163  CB  MET A  12     -10.693 -14.915 -15.868  1.00 58.64           C  
ANISOU  163  CB  MET A  12     8034   8615   5630    438    -44    740       C  
ATOM    164  CG  MET A  12     -11.263 -16.270 -15.864  1.00 64.22           C  
ANISOU  164  CG  MET A  12     8551   9512   6337    429     43    402       C  
ATOM    165  SD  MET A  12     -10.588 -17.227 -17.200  1.00 71.80           S  
ANISOU  165  SD  MET A  12     9461  10858   6963    238    160    259       S  
ATOM    166  CE  MET A  12     -10.557 -18.859 -16.493  1.00 70.87           C  
ANISOU  166  CE  MET A  12     9223  10654   7050    208    315   -160       C  
ATOM    167  N   SER A  13     -13.470 -13.720 -14.923  1.00 68.18           N  
ANISOU  167  N   SER A  13     9100   9636   7170    992   -480    696       N  
ATOM    168  CA  SER A  13     -14.881 -13.991 -14.703  1.00 69.79           C  
ANISOU  168  CA  SER A  13     9061  10024   7434   1179   -586    487       C  
ATOM    169  C   SER A  13     -15.223 -15.347 -15.305  1.00 69.30           C  
ANISOU  169  C   SER A  13     8821  10322   7190    994   -487    275       C  
ATOM    170  O   SER A  13     -14.596 -15.783 -16.265  1.00 65.86           O  
ANISOU  170  O   SER A  13     8460  10034   6528    815   -434    326       O  
ATOM    171  CB  SER A  13     -15.733 -12.893 -15.335  1.00 78.33           C  
ANISOU  171  CB  SER A  13    10167  11115   8480   1451   -924    672       C  
ATOM    172  OG  SER A  13     -17.077 -12.992 -14.898  1.00 85.08           O  
ANISOU  172  OG  SER A  13    10734  12153   9440   1686  -1027    433       O  
ATOM    173  N   CYS A  14     -16.202 -16.041 -14.723  1.00 66.34           N  
ANISOU  173  N   CYS A  14     8201  10106   6899   1010   -459     14       N  
ATOM    174  CA  CYS A  14     -16.606 -17.299 -15.339  1.00 66.30           C  
ANISOU  174  CA  CYS A  14     8053  10404   6733    807   -412   -188       C  
ATOM    175  C   CYS A  14     -17.987 -17.704 -14.854  1.00 66.38           C  
ANISOU  175  C   CYS A  14     7761  10659   6801    836   -472   -407       C  
ATOM    176  O   CYS A  14     -18.494 -17.193 -13.853  1.00 69.17           O  
ANISOU  176  O   CYS A  14     7992  10962   7326    991   -479   -452       O  
ATOM    177  CB  CYS A  14     -15.603 -18.414 -15.057  1.00 61.76           C  
ANISOU  177  CB  CYS A  14     7576   9693   6197    556   -180   -319       C  
ATOM    178  SG  CYS A  14     -15.572 -18.899 -13.343  1.00 62.25           S  
ANISOU  178  SG  CYS A  14     7591   9519   6543    480    -19   -447       S  
ATOM    179  N   ALA A  15     -18.570 -18.665 -15.570  1.00 55.96           N  
ANISOU  179  N   ALA A  15     6302   9643   5316    657   -506   -573       N  
ATOM    180  CA  ALA A  15     -19.934 -19.112 -15.334  1.00 61.40           C  
ANISOU  180  CA  ALA A  15     6666  10665   5998    613   -582   -776       C  
ATOM    181  C   ALA A  15     -19.919 -20.429 -14.577  1.00 63.07           C  
ANISOU  181  C   ALA A  15     6838  10828   6298    268   -403   -980       C  
ATOM    182  O   ALA A  15     -19.257 -21.382 -15.002  1.00 59.37           O  
ANISOU  182  O   ALA A  15     6535  10238   5784     42   -327  -1055       O  
ATOM    183  CB  ALA A  15     -20.689 -19.264 -16.654  1.00 72.47           C  
ANISOU  183  CB  ALA A  15     7933  12459   7144    607   -787   -815       C  
ATOM    184  N   ALA A  16     -20.631 -20.474 -13.451  1.00 58.42           N  
ANISOU  184  N   ALA A  16     6034  10335   5827    226   -349  -1073       N  
ATOM    185  CA  ALA A  16     -20.734 -21.671 -12.638  1.00 55.94           C  
ANISOU  185  CA  ALA A  16     5688   9988   5578   -153   -215  -1205       C  
ATOM    186  C   ALA A  16     -22.204 -21.945 -12.365  1.00 59.50           C  
ANISOU  186  C   ALA A  16     5738  10917   5951   -295   -277  -1372       C  
ATOM    187  O   ALA A  16     -23.071 -21.134 -12.696  1.00 71.62           O  
ANISOU  187  O   ALA A  16     7003  12793   7415    -26   -414  -1407       O  
ATOM    188  CB  ALA A  16     -19.944 -21.525 -11.328  1.00 56.02           C  
ANISOU  188  CB  ALA A  16     5848   9669   5766   -167    -46  -1114       C  
ATOM    189  N   GLY A  17     -22.487 -23.103 -11.785  1.00 56.13           N  
ANISOU  189  N   GLY A  17     5268  10525   5534   -729   -199  -1469       N  
ATOM    190  CA  GLY A  17     -23.856 -23.434 -11.431  1.00 54.95           C  
ANISOU  190  CA  GLY A  17     4709  10886   5284   -962   -231  -1621       C  
ATOM    191  C   GLY A  17     -23.917 -24.754 -10.696  1.00 65.77           C  
ANISOU  191  C   GLY A  17     6144  12170   6676  -1527   -144  -1645       C  
ATOM    192  O   GLY A  17     -22.894 -25.388 -10.421  1.00 64.31           O  
ANISOU  192  O   GLY A  17     6331  11490   6615  -1680    -83  -1548       O  
ATOM    193  N   THR A  18     -25.146 -25.161 -10.367  1.00 74.56           N  
ANISOU  193  N   THR A  18     6877  13786   7665  -1849   -161  -1768       N  
ATOM    194  CA  THR A  18     -25.366 -26.409  -9.645  1.00 68.59           C  
ANISOU  194  CA  THR A  18     6167  12996   6898  -2476   -112  -1751       C  
ATOM    195  C   THR A  18     -25.234 -27.633 -10.541  1.00 76.79           C  
ANISOU  195  C   THR A  18     7459  13768   7950  -2831   -253  -1816       C  
ATOM    196  O   THR A  18     -24.896 -28.715 -10.051  1.00 78.17           O  
ANISOU  196  O   THR A  18     7903  13586   8210  -3276   -257  -1744       O  
ATOM    197  CB  THR A  18     -26.751 -26.411  -9.019  1.00 72.23           C  
ANISOU  197  CB  THR A  18     6096  14166   7181  -2759    -76  -1864       C  
ATOM    198  OG1 THR A  18     -27.722 -26.289 -10.067  1.00 74.79           O  
ANISOU  198  OG1 THR A  18     6084  14959   7373  -2684   -232  -2049       O  
ATOM    199  CG2 THR A  18     -26.894 -25.241  -8.063  1.00 71.01           C  
ANISOU  199  CG2 THR A  18     5674  14292   7014  -2391     66  -1876       C  
ATOM    200  N   THR A  19     -25.544 -27.496 -11.829  1.00 78.99           N  
ANISOU  200  N   THR A  19     7655  14223   8136  -2654   -394  -1962       N  
ATOM    201  CA  THR A  19     -25.336 -28.540 -12.826  1.00 85.08           C  
ANISOU  201  CA  THR A  19     8676  14747   8904  -2904   -535  -2093       C  
ATOM    202  C   THR A  19     -24.584 -27.953 -14.009  1.00 81.58           C  
ANISOU  202  C   THR A  19     8410  14154   8431  -2427   -588  -2128       C  
ATOM    203  O   THR A  19     -24.448 -26.732 -14.136  1.00 78.19           O  
ANISOU  203  O   THR A  19     7874  13868   7966  -1958   -558  -2026       O  
ATOM    204  CB  THR A  19     -26.656 -29.142 -13.324  1.00 91.07           C  
ANISOU  204  CB  THR A  19     9100  16018   9485  -3313   -679  -2283       C  
ATOM    205  OG1 THR A  19     -27.534 -28.086 -13.745  1.00 96.03           O  
ANISOU  205  OG1 THR A  19     9266  17278   9942  -2968   -727  -2344       O  
ATOM    206  CG2 THR A  19     -27.317 -29.979 -12.243  1.00 97.39           C  
ANISOU  206  CG2 THR A  19     9795  16917  10291  -3925   -631  -2225       C  
ATOM    207  N   GLN A  20     -24.119 -28.840 -14.894  1.00 85.05           N  
ANISOU  207  N   GLN A  20     9125  14318   8873  -2572   -683  -2285       N  
ATOM    208  CA  GLN A  20     -23.460 -28.391 -16.116  1.00 79.43           C  
ANISOU  208  CA  GLN A  20     8547  13578   8054  -2202   -727  -2348       C  
ATOM    209  C   GLN A  20     -24.389 -27.509 -16.935  1.00 82.83           C  
ANISOU  209  C   GLN A  20     8621  14611   8238  -1982   -848  -2362       C  
ATOM    210  O   GLN A  20     -23.974 -26.483 -17.489  1.00 81.25           O  
ANISOU  210  O   GLN A  20     8443  14479   7949  -1560   -858  -2236       O  
ATOM    211  CB  GLN A  20     -23.002 -29.595 -16.936  1.00 89.87           C  
ANISOU  211  CB  GLN A  20    10152  14613   9382  -2431   -820  -2610       C  
ATOM    212  CG  GLN A  20     -22.152 -30.565 -16.154  1.00 91.83           C  
ANISOU  212  CG  GLN A  20    10760  14224   9909  -2631   -772  -2613       C  
ATOM    213  CD  GLN A  20     -21.381 -31.505 -17.059  1.00 98.42           C  
ANISOU  213  CD  GLN A  20    11904  14708  10782  -2647   -858  -2913       C  
ATOM    214  OE1 GLN A  20     -21.633 -31.567 -18.263  1.00102.58           O  
ANISOU  214  OE1 GLN A  20    12359  15527  11091  -2612   -950  -3150       O  
ATOM    215  NE2 GLN A  20     -20.430 -32.240 -16.482  1.00 97.58           N  
ANISOU  215  NE2 GLN A  20    12135  13993  10947  -2679   -844  -2926       N  
ATOM    216  N   THR A  21     -25.661 -27.889 -17.011  1.00 84.35           N  
ANISOU  216  N   THR A  21     8480  15255   8315  -2282   -966  -2496       N  
ATOM    217  CA  THR A  21     -26.631 -27.053 -17.703  1.00 87.18           C  
ANISOU  217  CA  THR A  21     8448  16224   8454  -2048  -1118  -2510       C  
ATOM    218  C   THR A  21     -26.835 -25.725 -16.979  1.00 85.45           C  
ANISOU  218  C   THR A  21     8005  16160   8301  -1617  -1061  -2306       C  
ATOM    219  O   THR A  21     -27.143 -24.711 -17.618  1.00 84.26           O  
ANISOU  219  O   THR A  21     7691  16295   8031  -1211  -1202  -2232       O  
ATOM    220  CB  THR A  21     -27.954 -27.806 -17.839  1.00 94.55           C  
ANISOU  220  CB  THR A  21     9040  17614   9272  -2482  -1236  -2703       C  
ATOM    221  OG1 THR A  21     -28.683 -27.705 -16.610  1.00101.63           O  
ANISOU  221  OG1 THR A  21     9647  18702  10265  -2625  -1119  -2628       O  
ATOM    222  CG2 THR A  21     -27.693 -29.278 -18.112  1.00 94.58           C  
ANISOU  222  CG2 THR A  21     9369  17220   9347  -2958  -1238  -2865       C  
ATOM    223  N   ALA A  22     -26.646 -25.708 -15.653  1.00 88.73           N  
ANISOU  223  N   ALA A  22     8434  16373   8905  -1691   -880  -2218       N  
ATOM    224  CA  ALA A  22     -26.950 -24.525 -14.853  1.00 93.36           C  
ANISOU  224  CA  ALA A  22     8772  17141   9558  -1312   -826  -2110       C  
ATOM    225  C   ALA A  22     -25.997 -23.364 -15.111  1.00 95.62           C  
ANISOU  225  C   ALA A  22     9320  17093   9919   -775   -827  -1910       C  
ATOM    226  O   ALA A  22     -26.338 -22.223 -14.776  1.00101.03           O  
ANISOU  226  O   ALA A  22     9806  17931  10647   -369   -872  -1848       O  
ATOM    227  CB  ALA A  22     -26.946 -24.879 -13.366  1.00 90.81           C  
ANISOU  227  CB  ALA A  22     8411  16727   9367  -1588   -622  -2086       C  
ATOM    228  N   CYS A  23     -24.815 -23.675 -15.640  1.00 91.48           N  
ANISOU  228  N   CYS A  23     9225  16118   9417   -794   -780  -1830       N  
ATOM    229  CA  CYS A  23     -23.810 -22.622 -15.878  1.00 84.21           C  
ANISOU  229  CA  CYS A  23     8568  14884   8544   -378   -766  -1612       C  
ATOM    230  C   CYS A  23     -24.312 -21.658 -16.934  1.00 93.42           C  
ANISOU  230  C   CYS A  23     9598  16361   9536    -33  -1003  -1528       C  
ATOM    231  O   CYS A  23     -23.991 -21.855 -18.080  1.00 95.06           O  
ANISOU  231  O   CYS A  23     9952  16610   9556    -69  -1095  -1514       O  
ATOM    232  CB  CYS A  23     -22.490 -23.226 -16.295  1.00 72.55           C  
ANISOU  232  CB  CYS A  23     7503  12980   7084   -500   -663  -1586       C  
ATOM    233  SG  CYS A  23     -21.872 -24.356 -15.044  1.00 69.60           S  
ANISOU  233  SG  CYS A  23     7321  12178   6945   -858   -458  -1646       S  
ATOM    234  N   THR A  24     -25.032 -20.635 -16.501  1.00106.47           N  
ANISOU  234  N   THR A  24    10989  18212  11253    305  -1106  -1480       N  
ATOM    235  CA  THR A  24     -25.664 -19.620 -17.380  1.00110.89           C  
ANISOU  235  CA  THR A  24    11391  19054  11689    696  -1403  -1378       C  
ATOM    236  C   THR A  24     -24.722 -18.445 -17.627  1.00103.35           C  
ANISOU  236  C   THR A  24    10783  17691  10795   1057  -1470  -1071       C  
ATOM    237  O   THR A  24     -23.936 -18.524 -18.536  1.00 98.23           O  
ANISOU  237  O   THR A  24    10427  16908   9990    973  -1489   -920       O  
ATOM    238  CB  THR A  24     -26.885 -19.041 -16.675  1.00119.23           C  
ANISOU  238  CB  THR A  24    11980  20483  12837    952  -1504  -1516       C  
ATOM    239  OG1 THR A  24     -26.397 -18.480 -15.464  1.00117.91           O  
ANISOU  239  OG1 THR A  24    11909  19981  12910   1119  -1331  -1483       O  
ATOM    240  CG2 THR A  24     -27.906 -20.086 -16.298  1.00119.66           C  
ANISOU  240  CG2 THR A  24    11626  21019  12818    558  -1432  -1803       C  
ATOM    241  N   ASP A  25     -24.834 -17.395 -16.825  1.00101.74           N  
ANISOU  241  N   ASP A  25    10531  17325  10801   1423  -1510  -1006       N  
ATOM    242  CA  ASP A  25     -24.000 -16.182 -16.992  1.00 98.62           C  
ANISOU  242  CA  ASP A  25    10482  16495  10495   1747  -1616   -700       C  
ATOM    243  C   ASP A  25     -22.895 -16.151 -15.940  1.00 79.62           C  
ANISOU  243  C   ASP A  25     8345  13611   8295   1655  -1336   -661       C  
ATOM    244  O   ASP A  25     -22.868 -17.035 -15.115  1.00 72.92           O  
ANISOU  244  O   ASP A  25     7402  12795   7511   1380  -1094   -856       O  
ATOM    245  CB  ASP A  25     -24.848 -14.923 -16.904  1.00117.69           C  
ANISOU  245  CB  ASP A  25    12708  18978  13031   2272  -1926   -661       C  
ATOM    246  CG  ASP A  25     -25.733 -14.757 -18.119  1.00138.09           C  
ANISOU  246  CG  ASP A  25    15105  21969  15396   2418  -2277   -597       C  
ATOM    247  OD1 ASP A  25     -25.476 -15.451 -19.117  1.00142.65           O  
ANISOU  247  OD1 ASP A  25    15789  22710  15700   2108  -2273   -526       O  
ATOM    248  OD2 ASP A  25     -26.654 -13.928 -18.063  1.00144.93           O  
ANISOU  248  OD2 ASP A  25    15713  22992  16359   2861  -2565   -638       O  
ATOM    249  N   ASP A  26     -22.118 -15.073 -15.944  1.00 74.39           N  
ANISOU  249  N   ASP A  26     7991  12539   7734   1888  -1414   -404       N  
ATOM    250  CA  ASP A  26     -20.910 -14.946 -15.138  1.00 71.30           C  
ANISOU  250  CA  ASP A  26     7893  11694   7503   1788  -1184   -322       C  
ATOM    251  C   ASP A  26     -21.289 -14.677 -13.691  1.00 73.86           C  
ANISOU  251  C   ASP A  26     8037  11959   8068   1936  -1077   -533       C  
ATOM    252  O   ASP A  26     -21.771 -13.593 -13.360  1.00 82.76           O  
ANISOU  252  O   ASP A  26     9094  13008   9343   2330  -1263   -549       O  
ATOM    253  CB  ASP A  26     -20.039 -13.820 -15.679  1.00 74.03           C  
ANISOU  253  CB  ASP A  26     8610  11664   7854   1944  -1338     31       C  
ATOM    254  CG  ASP A  26     -19.214 -14.250 -16.866  1.00 85.41           C  
ANISOU  254  CG  ASP A  26    10274  13158   9021   1664  -1305    230       C  
ATOM    255  OD1 ASP A  26     -19.406 -15.389 -17.346  1.00 94.44           O  
ANISOU  255  OD1 ASP A  26    11282  14617   9985   1413  -1200     56       O  
ATOM    256  OD2 ASP A  26     -18.368 -13.445 -17.309  1.00 85.01           O  
ANISOU  256  OD2 ASP A  26    10530  12846   8923   1676  -1386    545       O  
ATOM    257  N   ASN A  27     -21.047 -15.650 -12.823  1.00 61.55           N  
ANISOU  257  N   ASN A  27     6417  10428   6542   1623   -796   -699       N  
ATOM    258  CA  ASN A  27     -21.399 -15.479 -11.424  1.00 65.41           C  
ANISOU  258  CA  ASN A  27     6717  10950   7188   1694   -669   -901       C  
ATOM    259  C   ASN A  27     -20.280 -15.931 -10.489  1.00 67.97           C  
ANISOU  259  C   ASN A  27     7272  10956   7597   1428   -405   -863       C  
ATOM    260  O   ASN A  27     -20.563 -16.281  -9.334  1.00 61.84           O  
ANISOU  260  O   ASN A  27     6322  10309   6863   1305   -246  -1037       O  
ATOM    261  CB  ASN A  27     -22.689 -16.238 -11.145  1.00 63.53           C  
ANISOU  261  CB  ASN A  27     6023  11260   6854   1558   -638  -1174       C  
ATOM    262  CG  ASN A  27     -22.566 -17.704 -11.448  1.00 68.42           C  
ANISOU  262  CG  ASN A  27     6661  12001   7335   1062   -500  -1196       C  
ATOM    263  OD1 ASN A  27     -21.629 -18.118 -12.116  1.00 77.96           O  
ANISOU  263  OD1 ASN A  27     8185  12936   8501    904   -469  -1041       O  
ATOM    264  ND2 ASN A  27     -23.505 -18.502 -10.958  1.00 66.69           N  
ANISOU  264  ND2 ASN A  27     6098  12197   7042    802   -425  -1405       N  
ATOM    265  N   ALA A  28     -19.021 -15.932 -10.939  1.00 64.64           N  
ANISOU  265  N   ALA A  28     7213  10171   7177   1325   -360   -641       N  
ATOM    266  CA  ALA A  28     -17.913 -16.331 -10.070  1.00 60.69           C  
ANISOU  266  CA  ALA A  28     6911   9382   6766   1110   -142   -603       C  
ATOM    267  C   ALA A  28     -16.613 -15.779 -10.629  1.00 60.84           C  
ANISOU  267  C   ALA A  28     7274   9041   6800   1137   -158   -354       C  
ATOM    268  O   ALA A  28     -16.563 -15.265 -11.746  1.00 52.00           O  
ANISOU  268  O   ALA A  28     6255   7920   5582   1245   -317   -194       O  
ATOM    269  CB  ALA A  28     -17.825 -17.851  -9.922  1.00 60.73           C  
ANISOU  269  CB  ALA A  28     6876   9494   6705    720     14   -694       C  
ATOM    270  N   LEU A  29     -15.565 -15.906  -9.844  1.00 55.59           N  
ANISOU  270  N   LEU A  29     6774   8116   6232   1007      2   -311       N  
ATOM    271  CA  LEU A  29     -14.226 -15.447 -10.244  1.00 60.98           C  
ANISOU  271  CA  LEU A  29     7741   8509   6919    971     21    -93       C  
ATOM    272  C   LEU A  29     -13.288 -16.633 -10.138  1.00 60.05           C  
ANISOU  272  C   LEU A  29     7684   8350   6781    700    204   -125       C  
ATOM    273  O   LEU A  29     -13.209 -17.180  -9.084  1.00 67.12           O  
ANISOU  273  O   LEU A  29     8536   9195   7771    594    313   -223       O  
ATOM    274  CB  LEU A  29     -13.784 -14.395  -9.248  1.00 66.40           C  
ANISOU  274  CB  LEU A  29     8543   8911   7775   1100     16    -49       C  
ATOM    275  CG  LEU A  29     -13.024 -13.243  -9.857  1.00 74.45           C  
ANISOU  275  CG  LEU A  29     9821   9663   8805   1179   -112    207       C  
ATOM    276  CD1 LEU A  29     -13.939 -12.074 -10.101  1.00 82.37           C  
ANISOU  276  CD1 LEU A  29    10829  10595   9874   1499   -376    239       C  
ATOM    277  CD2 LEU A  29     -11.876 -12.848  -8.967  1.00 80.07           C  
ANISOU  277  CD2 LEU A  29    10701  10084   9639   1080    -10    264       C  
ATOM    278  N   ALA A  30     -12.652 -17.009 -11.228  1.00 53.99           N  
ANISOU  278  N   ALA A  30     7006   7630   5879    608    216    -56       N  
ATOM    279  CA  ALA A  30     -11.722 -18.127 -11.253  1.00 52.08           C  
ANISOU  279  CA  ALA A  30     6810   7343   5635    422    358   -137       C  
ATOM    280  C   ALA A  30     -10.304 -17.601 -11.152  1.00 53.62           C  
ANISOU  280  C   ALA A  30     7157   7358   5860    400    436     12       C  
ATOM    281  O   ALA A  30      -9.917 -16.691 -11.897  1.00 48.65           O  
ANISOU  281  O   ALA A  30     6618   6749   5117    431    381    196       O  
ATOM    282  CB  ALA A  30     -11.890 -18.952 -12.529  1.00 55.82           C  
ANISOU  282  CB  ALA A  30     7239   8047   5923    344    334   -246       C  
ATOM    283  N   TYR A  31      -9.543 -18.157 -10.215  1.00 41.36           N  
ANISOU  283  N   TYR A  31     5627   5642   4446    321    545    -43       N  
ATOM    284  CA  TYR A  31      -8.119 -17.880 -10.092  1.00 41.87           C  
ANISOU  284  CA  TYR A  31     5779   5594   4537    275    628     54       C  
ATOM    285  C   TYR A  31      -7.343 -18.941 -10.861  1.00 44.15           C  
ANISOU  285  C   TYR A  31     6026   6000   4746    214    705    -83       C  
ATOM    286  O   TYR A  31      -7.578 -20.136 -10.659  1.00 44.60           O  
ANISOU  286  O   TYR A  31     6044   6022   4881    190    707   -270       O  
ATOM    287  CB  TYR A  31      -7.709 -17.907  -8.628  1.00 42.07           C  
ANISOU  287  CB  TYR A  31     5827   5411   4748    248    675     53       C  
ATOM    288  CG  TYR A  31      -8.372 -16.843  -7.763  1.00 44.59           C  
ANISOU  288  CG  TYR A  31     6170   5632   5142    327    615    112       C  
ATOM    289  CD1 TYR A  31      -8.034 -15.503  -7.899  1.00 54.80           C  
ANISOU  289  CD1 TYR A  31     7575   6810   6436    385    554    268       C  
ATOM    290  CD2 TYR A  31      -9.309 -17.185  -6.801  1.00 53.37           C  
ANISOU  290  CD2 TYR A  31     7191   6772   6315    330    611     -5       C  
ATOM    291  CE1 TYR A  31      -8.617 -14.524  -7.104  1.00 49.03           C  
ANISOU  291  CE1 TYR A  31     6878   5949   5804    505    474    257       C  
ATOM    292  CE2 TYR A  31      -9.900 -16.206  -5.992  1.00 61.41           C  
ANISOU  292  CE2 TYR A  31     8191   7755   7387    439    568    -27       C  
ATOM    293  CZ  TYR A  31      -9.547 -14.874  -6.161  1.00 62.34           C  
ANISOU  293  CZ  TYR A  31     8434   7711   7542    557    492     81       C  
ATOM    294  OH  TYR A  31     -10.123 -13.880  -5.382  1.00 64.91           O  
ANISOU  294  OH  TYR A  31     8755   7958   7950    714    421     -1       O  
ATOM    295  N   TYR A  32      -6.411 -18.517 -11.719  1.00 40.70           N  
ANISOU  295  N   TYR A  32     5599   5710   4156    177    757     -4       N  
ATOM    296  CA  TYR A  32      -5.710 -19.494 -12.547  1.00 38.84           C  
ANISOU  296  CA  TYR A  32     5277   5668   3813    159    838   -208       C  
ATOM    297  C   TYR A  32      -4.233 -19.158 -12.707  1.00 44.83           C  
ANISOU  297  C   TYR A  32     5988   6540   4506    103    952   -154       C  
ATOM    298  O   TYR A  32      -3.805 -18.014 -12.573  1.00 49.73           O  
ANISOU  298  O   TYR A  32     6668   7147   5081     15    956     96       O  
ATOM    299  CB  TYR A  32      -6.341 -19.618 -13.936  1.00 50.47           C  
ANISOU  299  CB  TYR A  32     6713   7443   5022    142    799   -275       C  
ATOM    300  CG  TYR A  32      -6.242 -18.363 -14.771  1.00 54.35           C  
ANISOU  300  CG  TYR A  32     7256   8132   5264     66    768      4       C  
ATOM    301  CD1 TYR A  32      -7.152 -17.334 -14.615  1.00 52.93           C  
ANISOU  301  CD1 TYR A  32     7176   7831   5102    106    619    243       C  
ATOM    302  CD2 TYR A  32      -5.251 -18.215 -15.736  1.00 61.45           C  
ANISOU  302  CD2 TYR A  32     8098   9353   5896    -51    867     27       C  
ATOM    303  CE1 TYR A  32      -7.081 -16.190 -15.365  1.00 55.70           C  
ANISOU  303  CE1 TYR A  32     7628   8284   5251     34    529    540       C  
ATOM    304  CE2 TYR A  32      -5.172 -17.064 -16.510  1.00 56.66           C  
ANISOU  304  CE2 TYR A  32     7573   8924   5030   -190    811    347       C  
ATOM    305  CZ  TYR A  32      -6.091 -16.057 -16.318  1.00 56.69           C  
ANISOU  305  CZ  TYR A  32     7735   8713   5094   -146    621    624       C  
ATOM    306  OH  TYR A  32      -6.043 -14.906 -17.065  1.00 65.24           O  
ANISOU  306  OH  TYR A  32     8953   9888   5949   -282    503    984       O  
ATOM    307  N   ASN A  33      -3.464 -20.195 -13.001  1.00 53.94           N  
ANISOU  307  N   ASN A  33     7022   7809   5662    155   1028   -418       N  
ATOM    308  CA  ASN A  33      -2.098 -20.089 -13.482  1.00 56.81           C  
ANISOU  308  CA  ASN A  33     7244   8449   5891    115   1156   -468       C  
ATOM    309  C   ASN A  33      -2.081 -20.370 -14.978  1.00 58.29           C  
ANISOU  309  C   ASN A  33     7323   9072   5750     83   1220   -637       C  
ATOM    310  O   ASN A  33      -2.890 -21.154 -15.485  1.00 66.46           O  
ANISOU  310  O   ASN A  33     8372  10126   6755    156   1162   -853       O  
ATOM    311  CB  ASN A  33      -1.178 -21.090 -12.783  1.00 55.93           C  
ANISOU  311  CB  ASN A  33     7026   8214   6013    259   1180   -710       C  
ATOM    312  CG  ASN A  33      -0.789 -20.652 -11.426  1.00 67.24           C  
ANISOU  312  CG  ASN A  33     8516   9362   7670    239   1146   -518       C  
ATOM    313  OD1 ASN A  33      -0.588 -19.460 -11.187  1.00 79.04           O  
ANISOU  313  OD1 ASN A  33    10060  10873   9100     93   1168   -246       O  
ATOM    314  ND2 ASN A  33      -0.688 -21.601 -10.503  1.00 71.65           N  
ANISOU  314  ND2 ASN A  33     9093   9639   8494    368   1065   -647       N  
ATOM    315  N   THR A  34      -1.145 -19.739 -15.681  1.00 64.48           N  
ANISOU  315  N   THR A  34     7990  10246   6262    -64   1340   -547       N  
ATOM    316  CA  THR A  34      -0.822 -20.146 -17.044  1.00 77.52           C  
ANISOU  316  CA  THR A  34     9470  12424   7558   -103   1445   -780       C  
ATOM    317  C   THR A  34       0.278 -21.199 -16.970  1.00 80.14           C  
ANISOU  317  C   THR A  34     9560  12905   7987     78   1557  -1210       C  
ATOM    318  O   THR A  34       1.236 -21.052 -16.207  1.00 82.73           O  
ANISOU  318  O   THR A  34     9790  13164   8478    100   1606  -1172       O  
ATOM    319  CB  THR A  34      -0.401 -18.942 -17.898  1.00 82.89           C  
ANISOU  319  CB  THR A  34    10134  13526   7836   -406   1514   -447       C  
ATOM    320  OG1 THR A  34       0.613 -18.184 -17.221  1.00 78.21           O  
ANISOU  320  OG1 THR A  34     9505  12890   7321   -547   1577   -222       O  
ATOM    321  CG2 THR A  34      -1.603 -18.031 -18.176  1.00 73.82           C  
ANISOU  321  CG2 THR A  34     9238  12222   6590   -514   1340    -70       C  
ATOM    322  N   THR A  35       0.116 -22.290 -17.720  1.00 87.73           N  
ANISOU  322  N   THR A  35    10421  14041   8872    235   1568  -1648       N  
ATOM    323  CA  THR A  35       0.929 -23.479 -17.478  1.00 91.82           C  
ANISOU  323  CA  THR A  35    10763  14516   9609    516   1590  -2118       C  
ATOM    324  C   THR A  35       1.215 -24.207 -18.788  1.00104.22           C  
ANISOU  324  C   THR A  35    12155  16481  10965    582   1626  -2514       C  
ATOM    325  O   THR A  35       0.754 -23.811 -19.866  1.00106.93           O  
ANISOU  325  O   THR A  35    12507  17150  10970    388   1643  -2416       O  
ATOM    326  CB  THR A  35       0.245 -24.419 -16.478  1.00 88.96           C  
ANISOU  326  CB  THR A  35    10607  13492   9703    715   1390  -2218       C  
ATOM    327  OG1 THR A  35       1.191 -25.382 -15.995  1.00 92.63           O  
ANISOU  327  OG1 THR A  35    10940  13808  10446    996   1355  -2560       O  
ATOM    328  CG2 THR A  35      -0.919 -25.153 -17.136  1.00 84.70           C  
ANISOU  328  CG2 THR A  35    10195  12872   9114    732   1285  -2438       C  
ATOM    329  N   LYS A  36       1.982 -25.303 -18.671  1.00107.16           N  
ANISOU  329  N   LYS A  36    12382  16747  11588    862   1580  -2922       N  
ATOM    330  CA  LYS A  36       2.353 -26.129 -19.815  1.00117.60           C  
ANISOU  330  CA  LYS A  36    13530  18355  12797    963   1568  -3322       C  
ATOM    331  C   LYS A  36       1.138 -26.716 -20.520  1.00118.28           C  
ANISOU  331  C   LYS A  36    13788  18344  12809    946   1465  -3491       C  
ATOM    332  O   LYS A  36       1.238 -27.113 -21.685  1.00125.76           O  
ANISOU  332  O   LYS A  36    14601  19642  13540    933   1481  -3748       O  
ATOM    333  CB  LYS A  36       3.289 -27.255 -19.372  1.00121.10           C  
ANISOU  333  CB  LYS A  36    13834  18584  13594   1318   1478  -3719       C  
ATOM    334  CG  LYS A  36       4.648 -26.778 -18.887  1.00123.52           C  
ANISOU  334  CG  LYS A  36    13882  19122  13929   1346   1571  -3632       C  
ATOM    335  CD  LYS A  36       5.517 -27.943 -18.441  1.00126.79           C  
ANISOU  335  CD  LYS A  36    14164  19305  14707   1739   1430  -4025       C  
ATOM    336  CE  LYS A  36       6.885 -27.467 -17.978  1.00128.27           C  
ANISOU  336  CE  LYS A  36    14051  19785  14899   1764   1510  -3958       C  
ATOM    337  NZ  LYS A  36       7.737 -28.597 -17.515  1.00131.18           N  
ANISOU  337  NZ  LYS A  36    14287  19926  15628   2180   1332  -4328       N  
ATOM    338  N   GLY A  37       0.000 -26.811 -19.836  1.00111.56           N  
ANISOU  338  N   GLY A  37    13209  17053  12126    936   1355  -3380       N  
ATOM    339  CA  GLY A  37      -1.231 -27.219 -20.483  1.00108.73           C  
ANISOU  339  CA  GLY A  37    13001  16653  11658    856   1252  -3494       C  
ATOM    340  C   GLY A  37      -1.993 -26.028 -21.024  1.00107.32           C  
ANISOU  340  C   GLY A  37    12873  16817  11087    563   1309  -3098       C  
ATOM    341  O   GLY A  37      -2.676 -26.135 -22.047  1.00114.69           O  
ANISOU  341  O   GLY A  37    13812  17998  11768    454   1264  -3170       O  
ATOM    342  N   GLY A  38      -1.857 -24.881 -20.361  1.00103.83           N  
ANISOU  342  N   GLY A  38    12471  16388  10594    439   1386  -2667       N  
ATOM    343  CA  GLY A  38      -2.540 -23.655 -20.741  1.00101.35           C  
ANISOU  343  CA  GLY A  38    12246  16310   9951    183   1390  -2219       C  
ATOM    344  C   GLY A  38      -3.073 -22.906 -19.531  1.00 94.43           C  
ANISOU  344  C   GLY A  38    11566  14967   9346    144   1299  -1781       C  
ATOM    345  O   GLY A  38      -2.322 -22.568 -18.608  1.00 94.18           O  
ANISOU  345  O   GLY A  38    11526  14721   9537    174   1347  -1625       O  
ATOM    346  N   ARG A  39      -4.376 -22.710 -19.503  1.00 89.63           N  
ANISOU  346  N   ARG A  39    11115  14180   8762     92   1145  -1607       N  
ATOM    347  CA  ARG A  39      -4.980 -22.090 -18.312  1.00 78.72           C  
ANISOU  347  CA  ARG A  39     9892  12333   7683     91   1039  -1250       C  
ATOM    348  C   ARG A  39      -5.201 -23.221 -17.313  1.00 69.90           C  
ANISOU  348  C   ARG A  39     8825  10761   6972    227    972  -1494       C  
ATOM    349  O   ARG A  39      -5.785 -24.211 -17.675  1.00 78.22           O  
ANISOU  349  O   ARG A  39     9887  11785   8050    259    897  -1797       O  
ATOM    350  CB  ARG A  39      -6.319 -21.468 -18.692  1.00 77.61           C  
ANISOU  350  CB  ARG A  39     9846  12240   7404     14    888  -1012       C  
ATOM    351  CG  ARG A  39      -6.483 -20.020 -18.286  1.00 69.24           C  
ANISOU  351  CG  ARG A  39     8898  11063   6347    -47    825   -530       C  
ATOM    352  CD  ARG A  39      -6.383 -19.081 -19.460  1.00 80.98           C  
ANISOU  352  CD  ARG A  39    10401  12952   7416   -202    798   -267       C  
ATOM    353  NE  ARG A  39      -7.154 -17.860 -19.307  1.00 87.15           N  
ANISOU  353  NE  ARG A  39    11337  13565   8211   -210    611    150       N  
ATOM    354  CZ  ARG A  39      -6.909 -16.744 -19.965  1.00 95.69           C  
ANISOU  354  CZ  ARG A  39    12519  14813   9027   -362    539    528       C  
ATOM    355  NH1 ARG A  39      -5.905 -16.692 -20.812  1.00104.73           N  
ANISOU  355  NH1 ARG A  39    13596  16372   9825   -573    677    553       N  
ATOM    356  NH2 ARG A  39      -7.666 -15.683 -19.790  1.00 96.28           N  
ANISOU  356  NH2 ARG A  39    12757  14652   9173   -310    315    875       N  
ATOM    357  N   PHE A  40      -4.598 -23.112 -16.157  1.00 58.44           N  
ANISOU  357  N   PHE A  40     7406   8996   5803    282    994  -1375       N  
ATOM    358  CA  PHE A  40      -4.823 -24.037 -15.048  1.00 62.01           C  
ANISOU  358  CA  PHE A  40     7945   8988   6627    362    898  -1487       C  
ATOM    359  C   PHE A  40      -5.601 -23.280 -13.974  1.00 59.82           C  
ANISOU  359  C   PHE A  40     7777   8460   6491    281    834  -1139       C  
ATOM    360  O   PHE A  40      -5.080 -22.322 -13.390  1.00 53.33           O  
ANISOU  360  O   PHE A  40     6966   7600   5697    264    886   -882       O  
ATOM    361  CB  PHE A  40      -3.502 -24.585 -14.510  1.00 72.32           C  
ANISOU  361  CB  PHE A  40     9185  10162   8132    507    944  -1644       C  
ATOM    362  CG  PHE A  40      -3.652 -25.565 -13.368  1.00 75.80           C  
ANISOU  362  CG  PHE A  40     9751  10106   8946    574    801  -1708       C  
ATOM    363  CD1 PHE A  40      -4.614 -26.566 -13.408  1.00 75.48           C  
ANISOU  363  CD1 PHE A  40     9830   9833   9016    533    656  -1879       C  
ATOM    364  CD2 PHE A  40      -2.807 -25.495 -12.258  1.00 82.35           C  
ANISOU  364  CD2 PHE A  40    10583  10710   9995    640    790  -1577       C  
ATOM    365  CE1 PHE A  40      -4.746 -27.471 -12.363  1.00 76.80           C  
ANISOU  365  CE1 PHE A  40    10146   9533   9502    530    497  -1880       C  
ATOM    366  CE2 PHE A  40      -2.927 -26.405 -11.204  1.00 77.59           C  
ANISOU  366  CE2 PHE A  40    10119   9658   9702    673    626  -1583       C  
ATOM    367  CZ  PHE A  40      -3.901 -27.390 -11.258  1.00 77.81           C  
ANISOU  367  CZ  PHE A  40    10293   9439   9834    604    477  -1716       C  
ATOM    368  N   VAL A  41      -6.843 -23.704 -13.724  1.00 56.68           N  
ANISOU  368  N   VAL A  41     7441   7925   6169    220    721  -1161       N  
ATOM    369  CA  VAL A  41      -7.719 -23.057 -12.747  1.00 49.44           C  
ANISOU  369  CA  VAL A  41     6572   6860   5353    157    669   -909       C  
ATOM    370  C   VAL A  41      -7.569 -23.744 -11.398  1.00 51.60           C  
ANISOU  370  C   VAL A  41     6917   6783   5907    125    631   -904       C  
ATOM    371  O   VAL A  41      -7.664 -24.974 -11.292  1.00 47.47           O  
ANISOU  371  O   VAL A  41     6446   6077   5514     88    552  -1096       O  
ATOM    372  CB  VAL A  41      -9.179 -23.087 -13.221  1.00 50.11           C  
ANISOU  372  CB  VAL A  41     6620   7098   5323     85    572   -936       C  
ATOM    373  CG1 VAL A  41     -10.109 -22.604 -12.087  1.00 44.84           C  
ANISOU  373  CG1 VAL A  41     5943   6317   4777     41    526   -763       C  
ATOM    374  CG2 VAL A  41      -9.331 -22.230 -14.470  1.00 53.97           C  
ANISOU  374  CG2 VAL A  41     7058   7933   5514    117    570   -856       C  
ATOM    375  N   LEU A  42      -7.363 -22.951 -10.346  1.00 50.78           N  
ANISOU  375  N   LEU A  42     6835   6570   5889    121    662   -678       N  
ATOM    376  CA  LEU A  42      -7.186 -23.524  -9.030  1.00 47.93           C  
ANISOU  376  CA  LEU A  42     6542   5930   5739     63    620   -633       C  
ATOM    377  C   LEU A  42      -8.411 -23.397  -8.152  1.00 44.38           C  
ANISOU  377  C   LEU A  42     6090   5469   5306    -78    578   -532       C  
ATOM    378  O   LEU A  42      -8.736 -24.342  -7.436  1.00 49.76           O  
ANISOU  378  O   LEU A  42     6827   5983   6094   -222    503   -547       O  
ATOM    379  CB  LEU A  42      -6.000 -22.869  -8.324  1.00 47.43           C  
ANISOU  379  CB  LEU A  42     6484   5792   5744    127    682   -492       C  
ATOM    380  CG  LEU A  42      -4.642 -22.993  -8.999  1.00 57.94           C  
ANISOU  380  CG  LEU A  42     7756   7201   7058    248    741   -597       C  
ATOM    381  CD1 LEU A  42      -4.439 -21.837  -9.926  1.00 57.06           C  
ANISOU  381  CD1 LEU A  42     7582   7372   6727    250    838   -508       C  
ATOM    382  CD2 LEU A  42      -3.565 -23.004  -7.940  1.00 62.91           C  
ANISOU  382  CD2 LEU A  42     8388   7671   7844    281    734   -513       C  
ATOM    383  N   ALA A  43      -9.096 -22.263  -8.185  1.00 43.08           N  
ANISOU  383  N   ALA A  43     5852   5483   5031    -42    608   -433       N  
ATOM    384  CA  ALA A  43     -10.234 -22.069  -7.301  1.00 48.52           C  
ANISOU  384  CA  ALA A  43     6472   6244   5719   -140    588   -392       C  
ATOM    385  C   ALA A  43     -11.187 -21.081  -7.941  1.00 48.49           C  
ANISOU  385  C   ALA A  43     6355   6482   5586    -26    567   -392       C  
ATOM    386  O   ALA A  43     -10.812 -20.312  -8.832  1.00 45.71           O  
ANISOU  386  O   ALA A  43     6030   6179   5156    114    561   -336       O  
ATOM    387  CB  ALA A  43      -9.803 -21.567  -5.921  1.00 45.60           C  
ANISOU  387  CB  ALA A  43     6134   5765   5427   -160    631   -270       C  
ATOM    388  N   LEU A  44     -12.435 -21.135  -7.480  1.00 44.85           N  
ANISOU  388  N   LEU A  44     5755   6196   5092   -102    538   -445       N  
ATOM    389  CA  LEU A  44     -13.440 -20.135  -7.793  1.00 50.39           C  
ANISOU  389  CA  LEU A  44     6305   7131   5708     59    487   -463       C  
ATOM    390  C   LEU A  44     -13.802 -19.381  -6.515  1.00 55.11           C  
ANISOU  390  C   LEU A  44     6817   7770   6353    113    526   -463       C  
ATOM    391  O   LEU A  44     -13.810 -19.949  -5.422  1.00 53.25           O  
ANISOU  391  O   LEU A  44     6561   7531   6141    -79    591   -476       O  
ATOM    392  CB  LEU A  44     -14.703 -20.759  -8.405  1.00 46.07           C  
ANISOU  392  CB  LEU A  44     5581   6868   5056    -39    414   -597       C  
ATOM    393  CG  LEU A  44     -14.699 -20.806  -9.931  1.00 49.41           C  
ANISOU  393  CG  LEU A  44     6028   7383   5361     38    333   -621       C  
ATOM    394  CD1 LEU A  44     -13.644 -21.773 -10.423  1.00 48.68           C  
ANISOU  394  CD1 LEU A  44     6110   7096   5291    -74    374   -663       C  
ATOM    395  CD2 LEU A  44     -16.068 -21.138 -10.534  1.00 53.67           C  
ANISOU  395  CD2 LEU A  44     6352   8264   5776    -23    230   -753       C  
ATOM    396  N   LEU A  45     -14.089 -18.088  -6.662  1.00 54.98           N  
ANISOU  396  N   LEU A  45     6762   7787   6340    376    466   -453       N  
ATOM    397  CA  LEU A  45     -14.661 -17.277  -5.597  1.00 55.19           C  
ANISOU  397  CA  LEU A  45     6660   7909   6402    500    478   -550       C  
ATOM    398  C   LEU A  45     -16.047 -16.833  -6.039  1.00 57.25           C  
ANISOU  398  C   LEU A  45     6669   8480   6604    693    370   -691       C  
ATOM    399  O   LEU A  45     -16.195 -16.298  -7.140  1.00 54.00           O  
ANISOU  399  O   LEU A  45     6298   8041   6179    888    230   -625       O  
ATOM    400  CB  LEU A  45     -13.780 -16.057  -5.305  1.00 53.50           C  
ANISOU  400  CB  LEU A  45     6632   7401   6292    689    454   -463       C  
ATOM    401  CG  LEU A  45     -14.097 -15.332  -4.003  1.00 62.24           C  
ANISOU  401  CG  LEU A  45     7649   8554   7446    790    486   -615       C  
ATOM    402  CD1 LEU A  45     -13.698 -16.208  -2.798  1.00 52.09           C  
ANISOU  402  CD1 LEU A  45     6349   7328   6116    492    636   -626       C  
ATOM    403  CD2 LEU A  45     -13.418 -13.969  -3.973  1.00 59.32           C  
ANISOU  403  CD2 LEU A  45     7482   7858   7200   1013    394   -555       C  
ATOM    404  N   SER A  46     -17.060 -17.042  -5.192  1.00 53.42           N  
ANISOU  404  N   SER A  46     5903   8332   6062    633    423   -880       N  
ATOM    405  CA  SER A  46     -18.417 -16.676  -5.573  1.00 48.02           C  
ANISOU  405  CA  SER A  46     4905   8022   5319    831    317  -1056       C  
ATOM    406  C   SER A  46     -19.225 -16.262  -4.353  1.00 61.51           C  
ANISOU  406  C   SER A  46     6311  10062   6997    910    390  -1308       C  
ATOM    407  O   SER A  46     -18.859 -16.545  -3.208  1.00 65.51           O  
ANISOU  407  O   SER A  46     6836  10584   7469    697    543  -1332       O  
ATOM    408  CB  SER A  46     -19.137 -17.829  -6.275  1.00 53.40           C  
ANISOU  408  CB  SER A  46     5426   8992   5871    567    302  -1081       C  
ATOM    409  OG  SER A  46     -20.443 -17.438  -6.674  1.00 55.25           O  
ANISOU  409  OG  SER A  46     5315   9636   6040    771    182  -1254       O  
ATOM    410  N   ASP A  47     -20.352 -15.603  -4.624  1.00 60.58           N  
ANISOU  410  N   ASP A  47     5888  10257   6870   1226    268  -1512       N  
ATOM    411  CA  ASP A  47     -21.324 -15.326  -3.581  1.00 70.82           C  
ANISOU  411  CA  ASP A  47     6786  12028   8094   1308    346  -1834       C  
ATOM    412  C   ASP A  47     -22.242 -16.513  -3.350  1.00 70.12           C  
ANISOU  412  C   ASP A  47     6351  12500   7792    886    467  -1921       C  
ATOM    413  O   ASP A  47     -22.725 -16.705  -2.232  1.00 66.62           O  
ANISOU  413  O   ASP A  47     5632  12473   7209    704    627  -2107       O  
ATOM    414  CB  ASP A  47     -22.138 -14.084  -3.937  1.00 80.04           C  
ANISOU  414  CB  ASP A  47     7741  13299   9369   1885    135  -2059       C  
ATOM    415  CG  ASP A  47     -21.285 -12.823  -3.988  1.00 87.01           C  
ANISOU  415  CG  ASP A  47     8989  13594  10477   2267    -11  -1982       C  
ATOM    416  OD1 ASP A  47     -20.303 -12.740  -3.213  1.00 86.02           O  
ANISOU  416  OD1 ASP A  47     9118  13175  10391   2117    118  -1916       O  
ATOM    417  OD2 ASP A  47     -21.586 -11.922  -4.807  1.00 93.79           O  
ANISOU  417  OD2 ASP A  47     9892  14275  11468   2692   -280  -1968       O  
ATOM    418  N   LEU A  48     -22.465 -17.336  -4.364  1.00 59.90           N  
ANISOU  418  N   LEU A  48     5074  11240   6446    678    395  -1788       N  
ATOM    419  CA  LEU A  48     -23.373 -18.457  -4.203  1.00 68.32           C  
ANISOU  419  CA  LEU A  48     5829  12811   7319    231    476  -1864       C  
ATOM    420  C   LEU A  48     -22.670 -19.604  -3.496  1.00 67.27           C  
ANISOU  420  C   LEU A  48     5938  12497   7126   -323    631  -1671       C  
ATOM    421  O   LEU A  48     -21.453 -19.773  -3.612  1.00 62.63           O  
ANISOU  421  O   LEU A  48     5778  11359   6661   -352    631  -1452       O  
ATOM    422  CB  LEU A  48     -23.911 -18.915  -5.557  1.00 76.44           C  
ANISOU  422  CB  LEU A  48     6790  13941   8313    201    312  -1829       C  
ATOM    423  CG  LEU A  48     -24.864 -17.943  -6.258  1.00 85.62           C  
ANISOU  423  CG  LEU A  48     7630  15408   9493    701    114  -2014       C  
ATOM    424  CD1 LEU A  48     -24.108 -16.812  -6.946  1.00 83.88           C  
ANISOU  424  CD1 LEU A  48     7747  14664   9457   1203    -64  -1872       C  
ATOM    425  CD2 LEU A  48     -25.748 -18.685  -7.269  1.00 88.35           C  
ANISOU  425  CD2 LEU A  48     7742  16123   9705    502     -8  -2047       C  
ATOM    426  N   GLN A  49     -23.445 -20.395  -2.751  1.00 61.57           N  
ANISOU  426  N   GLN A  49     4929  12259   6205   -774    745  -1743       N  
ATOM    427  CA  GLN A  49     -22.912 -21.523  -2.000  1.00 59.10           C  
ANISOU  427  CA  GLN A  49     4843  11792   5819  -1341    845  -1527       C  
ATOM    428  C   GLN A  49     -23.331 -22.865  -2.571  1.00 69.83           C  
ANISOU  428  C   GLN A  49     6226  13193   7112  -1846    775  -1420       C  
ATOM    429  O   GLN A  49     -22.943 -23.904  -2.026  1.00 75.57           O  
ANISOU  429  O   GLN A  49     7180  13729   7803  -2340    799  -1216       O  
ATOM    430  CB  GLN A  49     -23.337 -21.440  -0.524  1.00 65.64           C  
ANISOU  430  CB  GLN A  49     5398  13110   6433  -1582   1024  -1628       C  
ATOM    431  CG  GLN A  49     -24.734 -20.925  -0.327  1.00 74.97           C  
ANISOU  431  CG  GLN A  49     6034  15010   7442  -1451   1047  -1957       C  
ATOM    432  CD  GLN A  49     -25.117 -20.805   1.143  1.00 92.90           C  
ANISOU  432  CD  GLN A  49     8214  17590   9494  -1628   1124  -2044       C  
ATOM    433  OE1 GLN A  49     -24.491 -21.410   2.024  1.00 94.25           O  
ANISOU  433  OE1 GLN A  49     8630  17603   9576  -2022   1193  -1822       O  
ATOM    434  NE2 GLN A  49     -26.149 -20.014   1.416  1.00 97.57           N  
ANISOU  434  NE2 GLN A  49     8448  18636   9988  -1327   1088  -2373       N  
ATOM    435  N   ASP A  50     -24.093 -22.871  -3.659  1.00 75.61           N  
ANISOU  435  N   ASP A  50     6756  14137   7836  -1736    657  -1548       N  
ATOM    436  CA  ASP A  50     -24.665 -24.073  -4.250  1.00 82.59           C  
ANISOU  436  CA  ASP A  50     7606  15132   8641  -2218    572  -1516       C  
ATOM    437  C   ASP A  50     -23.852 -24.602  -5.428  1.00 77.56           C  
ANISOU  437  C   ASP A  50     7395  13902   8171  -2162    426  -1402       C  
ATOM    438  O   ASP A  50     -24.276 -25.565  -6.076  1.00 79.65           O  
ANISOU  438  O   ASP A  50     7672  14196   8397  -2511    323  -1421       O  
ATOM    439  CB  ASP A  50     -26.098 -23.764  -4.709  1.00 94.41           C  
ANISOU  439  CB  ASP A  50     8547  17341   9985  -2151    524  -1775       C  
ATOM    440  CG  ASP A  50     -26.193 -22.422  -5.434  1.00105.31           C  
ANISOU  440  CG  ASP A  50     9796  18752  11466  -1421    424  -1927       C  
ATOM    441  OD1 ASP A  50     -25.857 -21.389  -4.809  1.00110.38           O  
ANISOU  441  OD1 ASP A  50    10430  19333  12178  -1017    491  -1983       O  
ATOM    442  OD2 ASP A  50     -26.571 -22.389  -6.628  1.00108.65           O  
ANISOU  442  OD2 ASP A  50    10156  19230  11898  -1260    253  -1980       O  
ATOM    443  N   LEU A  51     -22.700 -24.007  -5.715  1.00 69.65           N  
ANISOU  443  N   LEU A  51     6726  12400   7339  -1756    416  -1309       N  
ATOM    444  CA  LEU A  51     -21.999 -24.306  -6.953  1.00 67.99           C  
ANISOU  444  CA  LEU A  51     6824  11772   7236  -1624    296  -1266       C  
ATOM    445  C   LEU A  51     -21.368 -25.688  -6.893  1.00 68.66           C  
ANISOU  445  C   LEU A  51     7254  11434   7401  -2048    259  -1158       C  
ATOM    446  O   LEU A  51     -20.775 -26.078  -5.883  1.00 64.47           O  
ANISOU  446  O   LEU A  51     6911  10652   6930  -2250    321  -1008       O  
ATOM    447  CB  LEU A  51     -20.945 -23.242  -7.225  1.00 59.76           C  
ANISOU  447  CB  LEU A  51     6002  10385   6318  -1122    308  -1188       C  
ATOM    448  CG  LEU A  51     -21.581 -21.865  -7.402  1.00 65.91           C  
ANISOU  448  CG  LEU A  51     6501  11482   7062   -671    271  -1290       C  
ATOM    449  CD1 LEU A  51     -20.548 -20.829  -7.749  1.00 62.74           C  
ANISOU  449  CD1 LEU A  51     6363  10696   6781   -248    245  -1173       C  
ATOM    450  CD2 LEU A  51     -22.662 -21.926  -8.476  1.00 69.47           C  
ANISOU  450  CD2 LEU A  51     6677  12325   7393   -631    122  -1425       C  
ATOM    451  N   LYS A  52     -21.510 -26.426  -7.980  1.00 60.90           N  
ANISOU  451  N   LYS A  52     6356  10365   6419  -2170    131  -1249       N  
ATOM    452  CA  LYS A  52     -20.821 -27.725  -8.074  1.00 63.56           C  
ANISOU  452  CA  LYS A  52     7066  10201   6884  -2483     47  -1202       C  
ATOM    453  C   LYS A  52     -20.109 -27.784  -9.417  1.00 71.13           C  
ANISOU  453  C   LYS A  52     8229  10894   7904  -2196    -35  -1320       C  
ATOM    454  O   LYS A  52     -19.373 -28.691  -9.605  1.00 70.83           O  
ANISOU  454  O   LYS A  52     8496  10415   7998  -2307   -106  -1342       O  
ATOM    455  CB  LYS A  52     -21.764 -28.921  -7.967  1.00 74.38           C  
ANISOU  455  CB  LYS A  52     8370  11704   8186  -3078    -55  -1246       C  
ATOM    456  CG  LYS A  52     -22.446 -29.138  -6.626  1.00 93.94           C  
ANISOU  456  CG  LYS A  52    10666  14472  10554  -3519     22  -1105       C  
ATOM    457  CD  LYS A  52     -23.384 -30.326  -6.601  1.00106.65           C  
ANISOU  457  CD  LYS A  52    12220  16226  12078  -4185    -97  -1118       C  
ATOM    458  CE  LYS A  52     -24.045 -30.558  -5.261  1.00117.92           C  
ANISOU  458  CE  LYS A  52    13454  18015  13335  -4702     -8   -946       C  
ATOM    459  NZ  LYS A  52     -24.966 -31.713  -5.295  1.00129.63           N  
ANISOU  459  NZ  LYS A  52    14994  19533  14725  -5170   -111   -884       N  
ATOM    460  N   TRP A  53     -20.343 -26.829 -10.304  1.00 67.69           N  
ANISOU  460  N   TRP A  53     7619  10743   7358  -1836    -38  -1397       N  
ATOM    461  CA  TRP A  53     -19.723 -26.910 -11.641  1.00 65.68           C  
ANISOU  461  CA  TRP A  53     7531  10341   7082  -1627   -109  -1509       C  
ATOM    462  C   TRP A  53     -19.335 -25.531 -12.113  1.00 64.38           C  
ANISOU  462  C   TRP A  53     7315  10295   6852  -1163    -67  -1420       C  
ATOM    463  O   TRP A  53     -20.037 -24.622 -11.815  1.00 59.65           O  
ANISOU  463  O   TRP A  53     6474   9999   6193  -1010    -62  -1366       O  
ATOM    464  CB  TRP A  53     -20.691 -27.528 -12.653  1.00 65.77           C  
ANISOU  464  CB  TRP A  53     7395  10649   6944  -1840   -253  -1720       C  
ATOM    465  CG  TRP A  53     -20.864 -28.993 -12.487  1.00 67.19           C  
ANISOU  465  CG  TRP A  53     7732  10588   7210  -2312   -344  -1832       C  
ATOM    466  CD1 TRP A  53     -21.849 -29.628 -11.812  1.00 74.81           C  
ANISOU  466  CD1 TRP A  53     8550  11720   8154  -2776   -388  -1820       C  
ATOM    467  CD2 TRP A  53     -19.973 -30.004 -12.939  1.00 69.76           C  
ANISOU  467  CD2 TRP A  53     8409  10423   7674  -2375   -420  -1969       C  
ATOM    468  NE1 TRP A  53     -21.628 -30.967 -11.811  1.00 73.32           N  
ANISOU  468  NE1 TRP A  53     8651  11113   8096  -3154   -511  -1898       N  
ATOM    469  CE2 TRP A  53     -20.487 -31.226 -12.498  1.00 73.29           C  
ANISOU  469  CE2 TRP A  53     8957  10680   8211  -2880   -543  -2015       C  
ATOM    470  CE3 TRP A  53     -18.795 -29.988 -13.668  1.00 68.20           C  
ANISOU  470  CE3 TRP A  53     8435   9953   7526  -2057   -402  -2073       C  
ATOM    471  CZ2 TRP A  53     -19.867 -32.433 -12.771  1.00 80.84           C  
ANISOU  471  CZ2 TRP A  53    10267  11098   9350  -3029   -685  -2175       C  
ATOM    472  CZ3 TRP A  53     -18.172 -31.179 -13.932  1.00 74.16           C  
ANISOU  472  CZ3 TRP A  53     9482  10254   8441  -2175   -509  -2274       C  
ATOM    473  CH2 TRP A  53     -18.704 -32.383 -13.494  1.00 80.86           C  
ANISOU  473  CH2 TRP A  53    10464  10838   9421  -2630   -666  -2331       C  
ATOM    474  N   ALA A  54     -18.269 -25.472 -12.889  1.00 61.27           N  
ANISOU  474  N   ALA A  54     7142   9675   6461   -973    -57  -1427       N  
ATOM    475  CA  ALA A  54     -17.738 -24.243 -13.497  1.00 55.23           C  
ANISOU  475  CA  ALA A  54     6396   8981   5609   -608    -38  -1302       C  
ATOM    476  C   ALA A  54     -17.493 -24.548 -14.967  1.00 61.74           C  
ANISOU  476  C   ALA A  54     7282   9926   6250   -581   -110  -1438       C  
ATOM    477  O   ALA A  54     -17.115 -25.634 -15.260  1.00 55.43           O  
ANISOU  477  O   ALA A  54     6610   8964   5484   -749   -114  -1628       O  
ATOM    478  CB  ALA A  54     -16.459 -23.893 -12.828  1.00 51.51           C  
ANISOU  478  CB  ALA A  54     6130   8152   5290   -476     87  -1157       C  
ATOM    479  N   ARG A  55     -17.614 -23.555 -15.814  1.00 56.27           N  
ANISOU  479  N   ARG A  55     6523   9486   5370   -361   -174  -1331       N  
ATOM    480  CA  ARG A  55     -17.491 -23.828 -17.245  1.00 59.54           C  
ANISOU  480  CA  ARG A  55     6965  10125   5534   -376   -249  -1459       C  
ATOM    481  C   ARG A  55     -16.561 -22.817 -17.875  1.00 64.25           C  
ANISOU  481  C   ARG A  55     7681  10743   5987   -160   -214  -1250       C  
ATOM    482  O   ARG A  55     -16.745 -21.657 -17.657  1.00 65.77           O  
ANISOU  482  O   ARG A  55     7846  10959   6186     25   -266   -996       O  
ATOM    483  CB  ARG A  55     -18.883 -23.753 -17.858  1.00 65.40           C  
ANISOU  483  CB  ARG A  55     7460  11298   6091   -424   -431  -1526       C  
ATOM    484  CG  ARG A  55     -18.900 -23.359 -19.319  1.00 76.01           C  
ANISOU  484  CG  ARG A  55     8793  12984   7103   -336   -553  -1510       C  
ATOM    485  CD  ARG A  55     -20.262 -23.657 -19.877  1.00 88.82           C  
ANISOU  485  CD  ARG A  55    10161  15028   8560   -449   -745  -1655       C  
ATOM    486  NE  ARG A  55     -21.031 -22.448 -19.752  1.00 93.56           N  
ANISOU  486  NE  ARG A  55    10576  15836   9136   -191   -889  -1415       N  
ATOM    487  CZ  ARG A  55     -20.926 -21.452 -20.584  1.00 98.52           C  
ANISOU  487  CZ  ARG A  55    11244  16628   9560     32  -1028  -1185       C  
ATOM    488  NH1 ARG A  55     -21.638 -20.362 -20.406  1.00 99.14           N  
ANISOU  488  NH1 ARG A  55    11176  16818   9674    312  -1204   -981       N  
ATOM    489  NH2 ARG A  55     -20.107 -21.558 -21.604  1.00 97.96           N  
ANISOU  489  NH2 ARG A  55    11358  16622   9241    -28  -1005  -1168       N  
ATOM    490  N   PHE A  56     -15.618 -23.294 -18.663  1.00 58.27           N  
ANISOU  490  N   PHE A  56     7047   9997   5097   -204   -142  -1382       N  
ATOM    491  CA  PHE A  56     -14.673 -22.380 -19.328  1.00 56.53           C  
ANISOU  491  CA  PHE A  56     6922   9876   4680    -82    -92  -1173       C  
ATOM    492  C   PHE A  56     -14.645 -22.685 -20.813  1.00 65.35           C  
ANISOU  492  C   PHE A  56     8009  11405   5415   -160   -144  -1328       C  
ATOM    493  O   PHE A  56     -14.629 -23.807 -21.204  1.00 68.84           O  
ANISOU  493  O   PHE A  56     8436  11901   5819   -278   -124  -1685       O  
ATOM    494  CB  PHE A  56     -13.279 -22.635 -18.778  1.00 52.39           C  
ANISOU  494  CB  PHE A  56     6532   9051   4324    -67    101  -1205       C  
ATOM    495  CG  PHE A  56     -13.218 -22.615 -17.283  1.00 57.26           C  
ANISOU  495  CG  PHE A  56     7187   9271   5298    -37    158  -1116       C  
ATOM    496  CD1 PHE A  56     -13.131 -21.425 -16.605  1.00 63.38           C  
ANISOU  496  CD1 PHE A  56     7992   9924   6167     86    161   -810       C  
ATOM    497  CD2 PHE A  56     -13.252 -23.781 -16.565  1.00 57.44           C  
ANISOU  497  CD2 PHE A  56     7235   9041   5550   -148    185  -1336       C  
ATOM    498  CE1 PHE A  56     -13.099 -21.395 -15.228  1.00 62.57           C  
ANISOU  498  CE1 PHE A  56     7909   9519   6346    100    216   -757       C  
ATOM    499  CE2 PHE A  56     -13.204 -23.750 -15.188  1.00 70.97           C  
ANISOU  499  CE2 PHE A  56     8984  10447   7536   -158    229  -1221       C  
ATOM    500  CZ  PHE A  56     -13.137 -22.559 -14.524  1.00 65.94           C  
ANISOU  500  CZ  PHE A  56     8342   9760   6953    -33    257   -949       C  
ATOM    501  N   PRO A  57     -14.729 -21.682 -21.672  1.00 73.46           N  
ANISOU  501  N   PRO A  57     9036  12736   6140   -107   -245  -1062       N  
ATOM    502  CA  PRO A  57     -14.606 -21.916 -23.073  1.00 80.30           C  
ANISOU  502  CA  PRO A  57     9875  14055   6579   -211   -282  -1185       C  
ATOM    503  C   PRO A  57     -13.108 -21.996 -23.345  1.00 87.29           C  
ANISOU  503  C   PRO A  57    10851  14961   7356   -249    -61  -1240       C  
ATOM    504  O   PRO A  57     -12.401 -21.239 -22.801  1.00 86.81           O  
ANISOU  504  O   PRO A  57    10877  14693   7414   -192     20   -964       O  
ATOM    505  CB  PRO A  57     -15.093 -20.592 -23.632  1.00 78.30           C  
ANISOU  505  CB  PRO A  57     9632  14029   6089   -135   -485   -748       C  
ATOM    506  CG  PRO A  57     -15.950 -20.057 -22.547  1.00 80.61           C  
ANISOU  506  CG  PRO A  57     9878  14017   6733     35   -600   -584       C  
ATOM    507  CD  PRO A  57     -15.093 -20.337 -21.346  1.00 78.73           C  
ANISOU  507  CD  PRO A  57     9728  13330   6856     48   -373   -652       C  
ATOM    508  N   LYS A  58     -12.683 -22.921 -24.193  1.00 93.87           N  
ANISOU  508  N   LYS A  58    11636  16073   7956   -345     23  -1633       N  
ATOM    509  CA  LYS A  58     -11.249 -23.016 -24.542  1.00104.15           C  
ANISOU  509  CA  LYS A  58    12950  17514   9107   -363    244  -1749       C  
ATOM    510  C   LYS A  58     -10.807 -21.744 -25.260  1.00112.09           C  
ANISOU  510  C   LYS A  58    13986  18854   9749   -448    240  -1296       C  
ATOM    511  O   LYS A  58     -11.576 -21.171 -26.045  1.00102.78           O  
ANISOU  511  O   LYS A  58    12807  17929   8316   -512     50  -1051       O  
ATOM    512  CB  LYS A  58     -10.987 -24.190 -25.478  1.00106.18           C  
ANISOU  512  CB  LYS A  58    13117  17963   9264   -409    300  -2243       C  
ATOM    513  CG  LYS A  58     -11.458 -25.543 -24.990  1.00102.57           C  
ANISOU  513  CG  LYS A  58    12674  17187   9109   -380    250  -2715       C  
ATOM    514  CD  LYS A  58     -11.786 -26.463 -26.127  1.00104.52           C  
ANISOU  514  CD  LYS A  58    12849  17642   9222   -455    185  -3083       C  
ATOM    515  CE  LYS A  58     -11.600 -27.918 -25.755  1.00101.53           C  
ANISOU  515  CE  LYS A  58    12527  16865   9185   -403    184  -3594       C  
ATOM    516  NZ  LYS A  58     -11.091 -28.749 -26.872  1.00 98.11           N  
ANISOU  516  NZ  LYS A  58    12023  16615   8638   -381    225  -3986       N  
ATOM    517  N   SER A  59      -9.579 -21.339 -24.975  1.00118.95           N  
ANISOU  517  N   SER A  59    14881  19653  10661   -461    423  -1166       N  
ATOM    518  CA  SER A  59      -8.908 -20.160 -25.578  1.00125.95           C  
ANISOU  518  CA  SER A  59    15815  20746  11295   -610    438   -712       C  
ATOM    519  C   SER A  59      -9.130 -20.160 -27.089  1.00127.86           C  
ANISOU  519  C   SER A  59    15983  21430  11169   -760    364   -713       C  
ATOM    520  O   SER A  59      -9.675 -19.170 -27.610  1.00128.81           O  
ANISOU  520  O   SER A  59    16201  21669  11071   -850    169   -275       O  
ATOM    521  CB  SER A  59      -7.453 -20.264 -25.299  1.00131.73           C  
ANISOU  521  CB  SER A  59    16482  21441  12128   -638    683   -807       C  
ATOM    522  OG  SER A  59      -7.023 -21.602 -25.478  1.00137.25           O  
ANISOU  522  OG  SER A  59    17026  22177  12944   -541    813  -1376       O  
ATOM    523  N   ASP A  60      -8.618 -21.208 -27.737  1.00125.39           N  
ANISOU  523  N   ASP A  60    15507  21331  10806   -773    508  -1182       N  
ATOM    524  CA  ASP A  60      -8.746 -21.486 -29.190  1.00124.99           C  
ANISOU  524  CA  ASP A  60    15337  21749  10404   -909    479  -1319       C  
ATOM    525  C   ASP A  60     -10.174 -21.200 -29.664  1.00117.66           C  
ANISOU  525  C   ASP A  60    14472  20922   9310   -936    210  -1135       C  
ATOM    526  O   ASP A  60     -10.328 -20.476 -30.641  1.00124.50           O  
ANISOU  526  O   ASP A  60    15356  22109   9840  -1093    105   -821       O  
ATOM    527  CB  ASP A  60      -8.434 -22.951 -29.473  1.00132.86           C  
ANISOU  527  CB  ASP A  60    16176  22801  11505   -816    600  -1971       C  
ATOM    528  CG  ASP A  60      -6.968 -23.281 -29.310  1.00144.99           C  
ANISOU  528  CG  ASP A  60    17584  24361  13146   -767    834  -2194       C  
ATOM    529  OD1 ASP A  60      -6.184 -22.334 -29.264  1.00150.07           O  
ANISOU  529  OD1 ASP A  60    18224  25115  13682   -886    918  -1836       O  
ATOM    530  OD2 ASP A  60      -6.635 -24.467 -29.224  1.00150.14           O  
ANISOU  530  OD2 ASP A  60    18142  24907  13998   -613    905  -2715       O  
ATOM    531  N   GLY A  61     -11.176 -21.764 -29.004  1.00114.33           N  
ANISOU  531  N   GLY A  61    14070  20252   9118   -802     90  -1327       N  
ATOM    532  CA  GLY A  61     -12.578 -21.559 -29.423  1.00105.62           C  
ANISOU  532  CA  GLY A  61    12967  19282   7881   -810   -184  -1194       C  
ATOM    533  C   GLY A  61     -13.163 -22.842 -29.971  1.00103.19           C  
ANISOU  533  C   GLY A  61    12532  19109   7566   -836   -206  -1717       C  
ATOM    534  O   GLY A  61     -14.284 -22.834 -30.453  1.00102.59           O  
ANISOU  534  O   GLY A  61    12411  19208   7362   -870   -418  -1681       O  
ATOM    535  N   THR A  62     -12.419 -23.926 -29.808  1.00104.82           N  
ANISOU  535  N   THR A  62    12691  19186   7950   -801    -12  -2193       N  
ATOM    536  CA  THR A  62     -12.758 -25.269 -30.319  1.00103.16           C  
ANISOU  536  CA  THR A  62    12398  19020   7778   -823    -24  -2745       C  
ATOM    537  C   THR A  62     -13.584 -26.060 -29.314  1.00 94.16           C  
ANISOU  537  C   THR A  62    11309  17462   7006   -770   -126  -2985       C  
ATOM    538  O   THR A  62     -13.660 -27.254 -29.490  1.00 87.10           O  
ANISOU  538  O   THR A  62    10402  16448   6242   -785   -124  -3453       O  
ATOM    539  CB  THR A  62     -11.450 -26.010 -30.588  1.00104.55           C  
ANISOU  539  CB  THR A  62    12511  19207   8005   -770    202  -3129       C  
ATOM    540  OG1 THR A  62     -10.933 -26.438 -29.337  1.00 91.34           O  
ANISOU  540  OG1 THR A  62    10918  17037   6749   -618    292  -3269       O  
ATOM    541  CG2 THR A  62     -10.407 -25.107 -31.198  1.00104.75           C  
ANISOU  541  CG2 THR A  62    12471  19589   7740   -844    346  -2840       C  
ATOM    542  N   GLY A  63     -14.152 -25.426 -28.292  1.00 81.69           N  
ANISOU  542  N   GLY A  63     9784  15663   5589   -722   -218  -2680       N  
ATOM    543  CA  GLY A  63     -14.951 -26.198 -27.332  1.00 72.22           C  
ANISOU  543  CA  GLY A  63     8604  14115   4721   -733   -312  -2909       C  
ATOM    544  C   GLY A  63     -14.986 -25.581 -25.954  1.00 83.85           C  
ANISOU  544  C   GLY A  63    10139  15290   6429   -642   -303  -2644       C  
ATOM    545  O   GLY A  63     -14.562 -24.454 -25.784  1.00 81.91           O  
ANISOU  545  O   GLY A  63     9930  15114   6077   -556   -264  -2246       O  
ATOM    546  N   THR A  64     -15.658 -26.251 -25.027  1.00 84.58           N  
ANISOU  546  N   THR A  64    10235  15087   6813   -699   -375  -2830       N  
ATOM    547  CA  THR A  64     -15.758 -25.804 -23.645  1.00 85.73           C  
ANISOU  547  CA  THR A  64    10420  14783   7372   -610   -341  -2518       C  
ATOM    548  C   THR A  64     -15.397 -26.943 -22.700  1.00 73.48           C  
ANISOU  548  C   THR A  64     8978  12708   6234   -664   -266  -2795       C  
ATOM    549  O   THR A  64     -15.444 -28.125 -23.058  1.00 77.30           O  
ANISOU  549  O   THR A  64     9504  13124   6741   -787   -312  -3229       O  
ATOM    550  CB  THR A  64     -17.163 -25.266 -23.303  1.00 91.27           C  
ANISOU  550  CB  THR A  64    10972  15592   8114   -631   -529  -2279       C  
ATOM    551  OG1 THR A  64     -18.046 -26.354 -23.011  1.00104.32           O  
ANISOU  551  OG1 THR A  64    12555  17159   9922   -839   -622  -2581       O  
ATOM    552  CG2 THR A  64     -17.736 -24.453 -24.456  1.00 75.93           C  
ANISOU  552  CG2 THR A  64     8919  14192   5741   -598   -702  -2097       C  
ATOM    553  N   ILE A  65     -15.002 -26.544 -21.500  1.00 65.31           N  
ANISOU  553  N   ILE A  65     8010  11288   5516   -568   -174  -2533       N  
ATOM    554  CA  ILE A  65     -14.610 -27.490 -20.425  1.00 73.38           C  
ANISOU  554  CA  ILE A  65     9162  11775   6945   -613   -129  -2681       C  
ATOM    555  C   ILE A  65     -15.504 -27.279 -19.211  1.00 68.37           C  
ANISOU  555  C   ILE A  65     8482  10941   6555   -708   -183  -2430       C  
ATOM    556  O   ILE A  65     -15.705 -26.155 -18.837  1.00 62.93           O  
ANISOU  556  O   ILE A  65     7715  10356   5841   -590   -157  -2099       O  
ATOM    557  CB  ILE A  65     -13.152 -27.246 -20.020  1.00 76.20           C  
ANISOU  557  CB  ILE A  65     9620  11902   7429   -423     45  -2610       C  
ATOM    558  CG1 ILE A  65     -12.221 -27.293 -21.223  1.00 81.28           C  
ANISOU  558  CG1 ILE A  65    10239  12874   7770   -329    137  -2849       C  
ATOM    559  CG2 ILE A  65     -12.732 -28.224 -18.959  1.00 61.95           C  
ANISOU  559  CG2 ILE A  65     7960   9550   6029   -446     42  -2740       C  
ATOM    560  CD1 ILE A  65     -10.898 -26.661 -20.975  1.00 83.40           C  
ANISOU  560  CD1 ILE A  65    10520  13114   8054   -168    315  -2686       C  
ATOM    561  N   TYR A  66     -16.003 -28.359 -18.643  1.00 67.00           N  
ANISOU  561  N   TYR A  66     8361  10497   6599   -932   -265  -2605       N  
ATOM    562  CA  TYR A  66     -16.813 -28.298 -17.415  1.00 59.77           C  
ANISOU  562  CA  TYR A  66     7381   9444   5883  -1090   -292  -2392       C  
ATOM    563  C   TYR A  66     -15.960 -28.922 -16.333  1.00 59.24           C  
ANISOU  563  C   TYR A  66     7526   8841   6141  -1115   -236  -2362       C  
ATOM    564  O   TYR A  66     -15.589 -30.044 -16.490  1.00 57.03           O  
ANISOU  564  O   TYR A  66     7416   8260   5991  -1213   -310  -2623       O  
ATOM    565  CB  TYR A  66     -18.125 -29.055 -17.578  1.00 58.03           C  
ANISOU  565  CB  TYR A  66     7044   9389   5615  -1422   -451  -2561       C  
ATOM    566  CG  TYR A  66     -19.145 -28.337 -18.410  1.00 65.72           C  
ANISOU  566  CG  TYR A  66     7751  10932   6288  -1391   -538  -2531       C  
ATOM    567  CD1 TYR A  66     -19.972 -27.383 -17.873  1.00 68.61           C  
ANISOU  567  CD1 TYR A  66     7880  11563   6626  -1318   -545  -2278       C  
ATOM    568  CD2 TYR A  66     -19.265 -28.589 -19.752  1.00 73.07           C  
ANISOU  568  CD2 TYR A  66     8654  12159   6948  -1405   -632  -2775       C  
ATOM    569  CE1 TYR A  66     -20.889 -26.696 -18.636  1.00 66.44           C  
ANISOU  569  CE1 TYR A  66     7352  11793   6097  -1229   -670  -2244       C  
ATOM    570  CE2 TYR A  66     -20.183 -27.922 -20.534  1.00 79.05           C  
ANISOU  570  CE2 TYR A  66     9171  13453   7413  -1366   -750  -2718       C  
ATOM    571  CZ  TYR A  66     -21.003 -26.973 -19.976  1.00 77.69           C  
ANISOU  571  CZ  TYR A  66     8767  13502   7250  -1264   -784  -2441       C  
ATOM    572  OH  TYR A  66     -21.902 -26.320 -20.752  1.00 79.55           O  
ANISOU  572  OH  TYR A  66     8758  14247   7220  -1178   -946  -2386       O  
ATOM    573  N   THR A  67     -15.632 -28.163 -15.300  1.00 63.27           N  
ANISOU  573  N   THR A  67     8031   9235   6772  -1004   -131  -2061       N  
ATOM    574  CA  THR A  67     -14.776 -28.674 -14.206  1.00 66.24           C  
ANISOU  574  CA  THR A  67     8602   9132   7436  -1018    -96  -1987       C  
ATOM    575  C   THR A  67     -15.588 -28.802 -12.935  1.00 62.11           C  
ANISOU  575  C   THR A  67     8036   8536   7029  -1281   -122  -1790       C  
ATOM    576  O   THR A  67     -16.352 -27.935 -12.656  1.00 56.50           O  
ANISOU  576  O   THR A  67     7119   8146   6203  -1270    -76  -1638       O  
ATOM    577  CB  THR A  67     -13.651 -27.712 -13.855  1.00 64.45           C  
ANISOU  577  CB  THR A  67     8402   8845   7241   -730     52  -1788       C  
ATOM    578  OG1 THR A  67     -13.029 -27.307 -15.060  1.00 75.81           O  
ANISOU  578  OG1 THR A  67     9812  10512   8481   -528    106  -1905       O  
ATOM    579  CG2 THR A  67     -12.588 -28.381 -13.031  1.00 63.61           C  
ANISOU  579  CG2 THR A  67     8489   8279   7401   -699     55  -1785       C  
ATOM    580  N   GLU A  68     -15.352 -29.884 -12.204  1.00 56.72           N  
ANISOU  580  N   GLU A  68     7553   7432   6565  -1498   -209  -1803       N  
ATOM    581  CA  GLU A  68     -16.077 -30.188 -10.951  1.00 54.74           C  
ANISOU  581  CA  GLU A  68     7288   7123   6388  -1846   -243  -1598       C  
ATOM    582  C   GLU A  68     -15.452 -29.409  -9.791  1.00 59.27           C  
ANISOU  582  C   GLU A  68     7866   7624   7029  -1700   -114  -1320       C  
ATOM    583  O   GLU A  68     -14.225 -29.394  -9.685  1.00 52.21           O  
ANISOU  583  O   GLU A  68     7138   6430   6269  -1463    -89  -1299       O  
ATOM    584  CB  GLU A  68     -16.006 -31.691 -10.702  1.00 56.14           C  
ANISOU  584  CB  GLU A  68     7741   6822   6767  -2168   -438  -1684       C  
ATOM    585  CG  GLU A  68     -16.649 -32.119  -9.406  1.00 71.90           C  
ANISOU  585  CG  GLU A  68     9765   8745   8808  -2607   -491  -1425       C  
ATOM    586  CD  GLU A  68     -17.417 -33.418  -9.507  1.00 86.01           C  
ANISOU  586  CD  GLU A  68    11691  10334  10653  -3108   -710  -1516       C  
ATOM    587  OE1 GLU A  68     -16.872 -34.376 -10.066  1.00 93.62           O  
ANISOU  587  OE1 GLU A  68    12938  10826  11806  -3080   -889  -1727       O  
ATOM    588  OE2 GLU A  68     -18.554 -33.459  -9.030  1.00 93.69           O  
ANISOU  588  OE2 GLU A  68    12478  11638  11480  -3526   -705  -1398       O  
ATOM    589  N   LEU A  69     -16.293 -28.811  -8.947  1.00 65.37           N  
ANISOU  589  N   LEU A  69     8436   8704   7699  -1843    -40  -1151       N  
ATOM    590  CA  LEU A  69     -15.819 -28.021  -7.783  1.00 59.73           C  
ANISOU  590  CA  LEU A  69     7705   7976   7014  -1730     82   -926       C  
ATOM    591  C   LEU A  69     -15.978 -28.836  -6.504  1.00 56.06           C  
ANISOU  591  C   LEU A  69     7351   7335   6615  -2127     25   -750       C  
ATOM    592  O   LEU A  69     -16.886 -29.660  -6.435  1.00 55.43           O  
ANISOU  592  O   LEU A  69     7244   7329   6488  -2532    -70   -769       O  
ATOM    593  CB  LEU A  69     -16.671 -26.760  -7.665  1.00 57.39           C  
ANISOU  593  CB  LEU A  69     7090   8172   6543  -1592    192   -905       C  
ATOM    594  CG  LEU A  69     -16.695 -25.869  -8.895  1.00 55.15           C  
ANISOU  594  CG  LEU A  69     6701   8089   6164  -1241    201  -1010       C  
ATOM    595  CD1 LEU A  69     -17.542 -24.641  -8.638  1.00 53.08           C  
ANISOU  595  CD1 LEU A  69     6153   8231   5786  -1067    253   -982       C  
ATOM    596  CD2 LEU A  69     -15.287 -25.477  -9.285  1.00 54.02           C  
ANISOU  596  CD2 LEU A  69     6761   7661   6105   -942    246   -967       C  
ATOM    597  N   GLU A  70     -15.122 -28.567  -5.523  1.00 58.78           N  
ANISOU  597  N   GLU A  70     7811   7485   7038  -2043     74   -566       N  
ATOM    598  CA  GLU A  70     -15.219 -29.219  -4.198  1.00 65.62           C  
ANISOU  598  CA  GLU A  70     8788   8230   7916  -2431     15   -336       C  
ATOM    599  C   GLU A  70     -16.247 -28.460  -3.361  1.00 62.90           C  
ANISOU  599  C   GLU A  70     8129   8438   7334  -2603    165   -273       C  
ATOM    600  O   GLU A  70     -16.611 -27.340  -3.732  1.00 58.56           O  
ANISOU  600  O   GLU A  70     7323   8240   6685  -2306    294   -403       O  
ATOM    601  CB  GLU A  70     -13.908 -29.061  -3.438  1.00 57.82           C  
ANISOU  601  CB  GLU A  70     7996   6915   7059  -2240     12   -171       C  
ATOM    602  CG  GLU A  70     -12.721 -29.660  -4.141  1.00 66.84           C  
ANISOU  602  CG  GLU A  70     9388   7570   8440  -1978   -116   -267       C  
ATOM    603  CD  GLU A  70     -12.385 -31.035  -3.615  1.00 81.89           C  
ANISOU  603  CD  GLU A  70    11607   8978  10532  -2242   -365   -136       C  
ATOM    604  OE1 GLU A  70     -13.305 -31.711  -3.132  1.00 88.59           O  
ANISOU  604  OE1 GLU A  70    12498   9854  11309  -2710   -460     -9       O  
ATOM    605  OE2 GLU A  70     -11.214 -31.416  -3.686  1.00 85.41           O  
ANISOU  605  OE2 GLU A  70    12245   9019  11190  -1986   -478   -157       O  
ATOM    606  N   PRO A  71     -16.689 -29.002  -2.211  1.00 64.60           N  
ANISOU  606  N   PRO A  71     8350   8748   7444  -3061    142    -77       N  
ATOM    607  CA  PRO A  71     -17.605 -28.288  -1.334  1.00 65.06           C  
ANISOU  607  CA  PRO A  71     8068   9409   7243  -3218    309    -65       C  
ATOM    608  C   PRO A  71     -16.895 -26.988  -0.932  1.00 59.03           C  
ANISOU  608  C   PRO A  71     7239   8705   6484  -2759    454    -96       C  
ATOM    609  O   PRO A  71     -15.757 -27.032  -0.540  1.00 59.65           O  
ANISOU  609  O   PRO A  71     7569   8406   6690  -2637    414     42       O  
ATOM    610  CB  PRO A  71     -17.747 -29.225  -0.136  1.00 71.26           C  
ANISOU  610  CB  PRO A  71     8988  10162   7926  -3800    232    216       C  
ATOM    611  CG  PRO A  71     -17.404 -30.580  -0.687  1.00 77.08           C  
ANISOU  611  CG  PRO A  71    10097  10311   8880  -4025    -23    305       C  
ATOM    612  CD  PRO A  71     -16.326 -30.315  -1.709  1.00 68.45           C  
ANISOU  612  CD  PRO A  71     9175   8786   8046  -3450    -62    137       C  
ATOM    613  N   PRO A  72     -17.582 -25.834  -0.939  1.00 52.72           N  
ANISOU  613  N   PRO A  72     6099   8381   5550  -2519    600   -279       N  
ATOM    614  CA  PRO A  72     -16.935 -24.556  -0.690  1.00 50.84           C  
ANISOU  614  CA  PRO A  72     5837   8128   5352  -2075    699   -338       C  
ATOM    615  C   PRO A  72     -16.449 -24.261   0.731  1.00 61.41           C  
ANISOU  615  C   PRO A  72     7212   9521   6598  -2176    778   -220       C  
ATOM    616  O   PRO A  72     -16.695 -25.036   1.620  1.00 63.07           O  
ANISOU  616  O   PRO A  72     7443   9853   6670  -2621    766    -64       O  
ATOM    617  CB  PRO A  72     -18.046 -23.559  -1.026  1.00 51.31           C  
ANISOU  617  CB  PRO A  72     5512   8688   5297  -1839    779   -588       C  
ATOM    618  CG  PRO A  72     -19.293 -24.296  -0.663  1.00 58.23           C  
ANISOU  618  CG  PRO A  72     6122  10035   5967  -2300    799   -622       C  
ATOM    619  CD  PRO A  72     -19.020 -25.713  -1.103  1.00 60.16           C  
ANISOU  619  CD  PRO A  72     6656   9898   6303  -2675    654   -448       C  
ATOM    620  N   CYS A  73     -15.735 -23.143   0.857  1.00 60.07           N  
ANISOU  620  N   CYS A  73     7073   9249   6502  -1780    835   -285       N  
ATOM    621  CA  CYS A  73     -15.244 -22.611   2.138  1.00 60.87           C  
ANISOU  621  CA  CYS A  73     7186   9434   6508  -1800    913   -241       C  
ATOM    622  C   CYS A  73     -15.715 -21.182   2.210  1.00 58.49           C  
ANISOU  622  C   CYS A  73     6637   9426   6161  -1432   1015   -516       C  
ATOM    623  O   CYS A  73     -15.659 -20.516   1.241  1.00 59.07           O  
ANISOU  623  O   CYS A  73     6717   9348   6379  -1073    976   -617       O  
ATOM    624  CB  CYS A  73     -13.741 -22.565   2.188  1.00 70.87           C  
ANISOU  624  CB  CYS A  73     8765  10208   7955  -1644    844    -83       C  
ATOM    625  SG  CYS A  73     -13.067 -24.214   2.378  1.00 87.40           S  
ANISOU  625  SG  CYS A  73    11166  11910  10132  -2013    673    224       S  
ATOM    626  N   ARG A  74     -16.168 -20.779   3.366  1.00 63.00           N  
ANISOU  626  N   ARG A  74     7005  10412   6521  -1541   1125   -631       N  
ATOM    627  CA  ARG A  74     -16.737 -19.455   3.528  1.00 62.83           C  
ANISOU  627  CA  ARG A  74     6722  10687   6464  -1169   1202   -964       C  
ATOM    628  C   ARG A  74     -15.782 -18.581   4.329  1.00 66.53           C  
ANISOU  628  C   ARG A  74     7341  10972   6965   -990   1225  -1003       C  
ATOM    629  O   ARG A  74     -15.133 -19.043   5.277  1.00 61.89           O  
ANISOU  629  O   ARG A  74     6888  10363   6264  -1282   1247   -832       O  
ATOM    630  CB  ARG A  74     -18.118 -19.518   4.214  1.00 68.49           C  
ANISOU  630  CB  ARG A  74     7000  12134   6888  -1372   1326  -1193       C  
ATOM    631  CG  ARG A  74     -18.199 -20.408   5.460  1.00 80.07           C  
ANISOU  631  CG  ARG A  74     8430  13939   8052  -1951   1414  -1027       C  
ATOM    632  CD  ARG A  74     -19.575 -20.334   6.147  1.00 79.25           C  
ANISOU  632  CD  ARG A  74     7933  14462   7714  -2075   1431  -1262       C  
ATOM    633  NE  ARG A  74     -19.959 -18.959   6.455  1.00 90.26           N  
ANISOU  633  NE  ARG A  74     9083  16080   9131  -1595   1468  -1668       N  
ATOM    634  CZ  ARG A  74     -19.432 -18.240   7.450  1.00 97.77           C  
ANISOU  634  CZ  ARG A  74    10086  17028  10034  -1479   1502  -1784       C  
ATOM    635  NH1 ARG A  74     -19.837 -16.991   7.661  1.00 93.29           N  
ANISOU  635  NH1 ARG A  74     9316  16604   9527  -1027   1499  -2179       N  
ATOM    636  NH2 ARG A  74     -18.483 -18.760   8.229  1.00102.78           N  
ANISOU  636  NH2 ARG A  74    10989  17489  10574  -1803   1508  -1508       N  
ATOM    637  N   PHE A  75     -15.691 -17.317   3.933  1.00 56.82           N  
ANISOU  637  N   PHE A  75     6106   9590   5894   -526   1190  -1215       N  
ATOM    638  CA  PHE A  75     -15.028 -16.335   4.765  1.00 63.71           C  
ANISOU  638  CA  PHE A  75     7065  10363   6778   -358   1210  -1347       C  
ATOM    639  C   PHE A  75     -15.738 -15.016   4.569  1.00 65.23           C  
ANISOU  639  C   PHE A  75     7072  10657   7055    109   1179  -1724       C  
ATOM    640  O   PHE A  75     -16.542 -14.851   3.650  1.00 62.34           O  
ANISOU  640  O   PHE A  75     6560  10353   6773    335   1114  -1813       O  
ATOM    641  CB  PHE A  75     -13.540 -16.195   4.437  1.00 57.03           C  
ANISOU  641  CB  PHE A  75     6598   8933   6140   -304   1118  -1100       C  
ATOM    642  CG  PHE A  75     -13.261 -15.827   3.006  1.00 60.40           C  
ANISOU  642  CG  PHE A  75     7174   8964   6811    -24   1004  -1016       C  
ATOM    643  CD1 PHE A  75     -13.233 -14.500   2.613  1.00 61.56           C  
ANISOU  643  CD1 PHE A  75     7372   8907   7111    357    921  -1174       C  
ATOM    644  CD2 PHE A  75     -13.008 -16.803   2.064  1.00 60.41           C  
ANISOU  644  CD2 PHE A  75     7285   8793   6877   -156    962   -779       C  
ATOM    645  CE1 PHE A  75     -12.969 -14.150   1.303  1.00 49.94           C  
ANISOU  645  CE1 PHE A  75     6053   7107   5816    557    802  -1043       C  
ATOM    646  CE2 PHE A  75     -12.742 -16.457   0.739  1.00 60.75           C  
ANISOU  646  CE2 PHE A  75     7448   8553   7083     70    870   -707       C  
ATOM    647  CZ  PHE A  75     -12.722 -15.132   0.371  1.00 54.15           C  
ANISOU  647  CZ  PHE A  75     6659   7557   6360    403    793   -812       C  
ATOM    648  N   VAL A  76     -15.429 -14.081   5.453  1.00 61.44           N  
ANISOU  648  N   VAL A  76     6605  10182   6556    263   1200  -1956       N  
ATOM    649  CA  VAL A  76     -16.002 -12.747   5.426  1.00 59.20           C  
ANISOU  649  CA  VAL A  76     6191   9915   6390    748   1131  -2362       C  
ATOM    650  C   VAL A  76     -14.903 -11.789   5.011  1.00 65.20           C  
ANISOU  650  C   VAL A  76     7335  10007   7431    989    971  -2269       C  
ATOM    651  O   VAL A  76     -13.749 -11.934   5.424  1.00 63.97           O  
ANISOU  651  O   VAL A  76     7432   9598   7275    765    986  -2066       O  
ATOM    652  CB  VAL A  76     -16.594 -12.369   6.798  1.00 68.48           C  
ANISOU  652  CB  VAL A  76     7063  11643   7313    740   1265  -2781       C  
ATOM    653  CG1 VAL A  76     -17.416 -11.105   6.687  1.00 70.25           C  
ANISOU  653  CG1 VAL A  76     7141  11824   7726   1248   1107  -3151       C  
ATOM    654  CG2 VAL A  76     -17.426 -13.517   7.340  1.00 76.10           C  
ANISOU  654  CG2 VAL A  76     7742  13188   7985    286   1379  -2665       C  
ATOM    655  N   THR A  77     -15.251 -10.836   4.168  1.00 73.12           N  
ANISOU  655  N   THR A  77     8383  10731   8668   1420    798  -2389       N  
ATOM    656  CA  THR A  77     -14.315  -9.827   3.717  1.00 83.67           C  
ANISOU  656  CA  THR A  77    10093  11432  10266   1618    616  -2286       C  
ATOM    657  C   THR A  77     -15.087  -8.526   3.601  1.00 91.81           C  
ANISOU  657  C   THR A  77    11058  12344  11480   2143    431  -2664       C  
ATOM    658  O   THR A  77     -16.250  -8.528   3.188  1.00 98.02           O  
ANISOU  658  O   THR A  77    11559  13421  12262   2400    387  -2843       O  
ATOM    659  CB  THR A  77     -13.665 -10.229   2.375  1.00 87.46           C  
ANISOU  659  CB  THR A  77    10824  11538  10869   1516    528  -1834       C  
ATOM    660  OG1 THR A  77     -12.719  -9.230   1.977  1.00 93.14           O  
ANISOU  660  OG1 THR A  77    11897  11692  11800   1627    361  -1705       O  
ATOM    661  CG2 THR A  77     -14.719 -10.422   1.275  1.00 84.84           C  
ANISOU  661  CG2 THR A  77    10321  11352  10564   1716    443  -1818       C  
ATOM    662  N   ASP A  78     -14.463  -7.427   4.022  1.00 96.14           N  
ANISOU  662  N   ASP A  78    11858  12478  12194   2306    303  -2813       N  
ATOM    663  CA  ASP A  78     -15.135  -6.127   4.053  1.00108.77           C  
ANISOU  663  CA  ASP A  78    13443  13877  14007   2820     80  -3201       C  
ATOM    664  C   ASP A  78     -15.031  -5.531   2.658  1.00110.88           C  
ANISOU  664  C   ASP A  78    14000  13577  14554   3071   -212  -2920       C  
ATOM    665  O   ASP A  78     -13.987  -4.996   2.276  1.00112.61           O  
ANISOU  665  O   ASP A  78    14635  13221  14932   2957   -354  -2635       O  
ATOM    666  CB  ASP A  78     -14.523  -5.218   5.115  1.00118.78           C  
ANISOU  666  CB  ASP A  78    14889  14910  15330   2798     40  -3423       C  
ATOM    667  CG  ASP A  78     -15.503  -4.150   5.626  1.00130.38           C  
ANISOU  667  CG  ASP A  78    16191  16450  16896   3140   -104  -3804       C  
ATOM    668  OD1 ASP A  78     -16.611  -4.012   5.047  1.00133.18           O  
ANISOU  668  OD1 ASP A  78    16327  16963  17313   3425   -216  -3874       O  
ATOM    669  OD2 ASP A  78     -15.163  -3.451   6.614  1.00129.20           O  
ANISOU  669  OD2 ASP A  78    16121  16216  16753   3131   -116  -4058       O  
ATOM    670  N   THR A  79     -16.110  -5.643   1.889  1.00107.69           N  
ANISOU  670  N   THR A  79    13368  13382  14166   3309   -304  -2918       N  
ATOM    671  CA  THR A  79     -16.160  -5.175   0.510  1.00107.60           C  
ANISOU  671  CA  THR A  79    13591  12935  14359   3531   -594  -2619       C  
ATOM    672  C   THR A  79     -16.607  -3.718   0.472  1.00113.59           C  
ANISOU  672  C   THR A  79    14481  13312  15364   3871   -910  -2752       C  
ATOM    673  O   THR A  79     -17.039  -3.164   1.490  1.00115.56           O  
ANISOU  673  O   THR A  79    14574  13713  15621   3991   -888  -3137       O  
ATOM    674  CB  THR A  79     -17.095  -6.080  -0.308  1.00 98.83           C  
ANISOU  674  CB  THR A  79    12155  12289  13107   3560   -545  -2529       C  
ATOM    675  OG1 THR A  79     -18.453  -5.630  -0.205  1.00 99.85           O  
ANISOU  675  OG1 THR A  79    11946  12732  13260   3887   -660  -2840       O  
ATOM    676  CG2 THR A  79     -17.008  -7.536   0.166  1.00 89.89           C  
ANISOU  676  CG2 THR A  79    10777  11708  11668   3068   -182  -2453       C  
ATOM    677  N   PRO A  80     -16.478  -3.048  -0.685  1.00112.65           N  
ANISOU  677  N   PRO A  80    14673  12693  15437   4012  -1220  -2426       N  
ATOM    678  CA  PRO A  80     -16.949  -1.653  -0.773  1.00114.18           C  
ANISOU  678  CA  PRO A  80    15007  12506  15870   4334  -1549  -2538       C  
ATOM    679  C   PRO A  80     -18.405  -1.464  -0.389  1.00114.96           C  
ANISOU  679  C   PRO A  80    14670  13061  15950   4702  -1587  -2975       C  
ATOM    680  O   PRO A  80     -18.777  -0.365   0.043  1.00124.73           O  
ANISOU  680  O   PRO A  80    15953  14079  17359   4977  -1786  -3242       O  
ATOM    681  CB  PRO A  80     -16.705  -1.301  -2.245  1.00113.40           C  
ANISOU  681  CB  PRO A  80    15241  11962  15883   4346  -1840  -2037       C  
ATOM    682  CG  PRO A  80     -15.537  -2.125  -2.620  1.00108.45           C  
ANISOU  682  CG  PRO A  80    14826  11252  15129   3939  -1671  -1658       C  
ATOM    683  CD  PRO A  80     -15.701  -3.430  -1.881  1.00106.91           C  
ANISOU  683  CD  PRO A  80    14250  11667  14703   3822  -1297  -1912       C  
ATOM    684  N   LYS A  81     -19.241  -2.490  -0.532  1.00107.57           N  
ANISOU  684  N   LYS A  81    13307  12761  14804   4701  -1412  -3065       N  
ATOM    685  CA  LYS A  81     -20.629  -2.424  -0.100  1.00113.67           C  
ANISOU  685  CA  LYS A  81    13611  14073  15504   4974  -1414  -3489       C  
ATOM    686  C   LYS A  81     -20.843  -3.017   1.293  1.00108.77           C  
ANISOU  686  C   LYS A  81    12627  14060  14642   4770  -1073  -3866       C  
ATOM    687  O   LYS A  81     -21.990  -3.274   1.672  1.00113.24           O  
ANISOU  687  O   LYS A  81    12737  15233  15057   4874  -1005  -4184       O  
ATOM    688  CB  LYS A  81     -21.530  -3.135  -1.114  1.00118.60           C  
ANISOU  688  CB  LYS A  81    13956  15086  16021   5054  -1454  -3362       C  
ATOM    689  CG  LYS A  81     -21.601  -2.428  -2.466  1.00128.28           C  
ANISOU  689  CG  LYS A  81    15478  15808  17453   5308  -1841  -3029       C  
ATOM    690  CD  LYS A  81     -22.483  -3.173  -3.454  1.00132.22           C  
ANISOU  690  CD  LYS A  81    15680  16743  17815   5369  -1880  -2914       C  
ATOM    691  CE  LYS A  81     -22.558  -2.441  -4.782  1.00137.66           C  
ANISOU  691  CE  LYS A  81    16670  16957  18676   5598  -2283  -2554       C  
ATOM    692  NZ  LYS A  81     -23.406  -3.189  -5.752  1.00138.97           N  
ANISOU  692  NZ  LYS A  81    16534  17587  18683   5644  -2330  -2444       N  
ATOM    693  N   GLY A  82     -19.772  -3.227   2.062  1.00 98.59           N  
ANISOU  693  N   GLY A  82    11527  12642  13290   4457   -872  -3824       N  
ATOM    694  CA  GLY A  82     -19.890  -3.748   3.406  1.00 92.25           C  
ANISOU  694  CA  GLY A  82    10423  12397  12231   4218   -571  -4126       C  
ATOM    695  C   GLY A  82     -19.488  -5.205   3.497  1.00 84.39           C  
ANISOU  695  C   GLY A  82     9307  11796  10959   3754   -248  -3903       C  
ATOM    696  O   GLY A  82     -19.088  -5.822   2.505  1.00 81.53           O  
ANISOU  696  O   GLY A  82     9088  11271  10617   3647   -248  -3551       O  
ATOM    697  N   PRO A  83     -19.590  -5.793   4.690  1.00 82.27           N  
ANISOU  697  N   PRO A  83     8780  12063  10416   3455     18  -4094       N  
ATOM    698  CA  PRO A  83     -19.139  -7.179   4.859  1.00 76.13           C  
ANISOU  698  CA  PRO A  83     7937  11617   9372   2962    306  -3848       C  
ATOM    699  C   PRO A  83     -20.050  -8.158   4.137  1.00 64.56           C  
ANISOU  699  C   PRO A  83     6161  10601   7768   2858    365  -3729       C  
ATOM    700  O   PRO A  83     -21.277  -8.044   4.174  1.00 79.97           O  
ANISOU  700  O   PRO A  83     7754  12974   9656   3012    307  -3964       O  
ATOM    701  CB  PRO A  83     -19.179  -7.388   6.382  1.00 72.85           C  
ANISOU  701  CB  PRO A  83     7319  11672   8688   2681    510  -4081       C  
ATOM    702  CG  PRO A  83     -20.153  -6.387   6.889  1.00 79.24           C  
ANISOU  702  CG  PRO A  83     7889  12665   9555   3041    370  -4519       C  
ATOM    703  CD  PRO A  83     -20.048  -5.197   5.963  1.00 90.85           C  
ANISOU  703  CD  PRO A  83     9653  13454  11412   3530     50  -4525       C  
ATOM    704  N   LYS A  84     -19.436  -9.127   3.472  1.00 62.37           N  
ANISOU  704  N   LYS A  84     6017  10243   7436   2589    472  -3384       N  
ATOM    705  CA  LYS A  84     -20.176 -10.172   2.782  1.00 74.05           C  
ANISOU  705  CA  LYS A  84     7233  12131   8773   2411    540  -3248       C  
ATOM    706  C   LYS A  84     -19.461 -11.496   2.959  1.00 65.71           C  
ANISOU  706  C   LYS A  84     6250  11209   7508   1875    784  -2965       C  
ATOM    707  O   LYS A  84     -18.235 -11.547   3.089  1.00 67.58           O  
ANISOU  707  O   LYS A  84     6860  11014   7805   1704    805  -2724       O  
ATOM    708  CB  LYS A  84     -20.349  -9.868   1.284  1.00 75.04           C  
ANISOU  708  CB  LYS A  84     7460  11938   9113   2760    308  -3100       C  
ATOM    709  CG  LYS A  84     -21.665  -9.179   0.958  1.00 87.28           C  
ANISOU  709  CG  LYS A  84     8733  13694  10737   3143     92  -3344       C  
ATOM    710  CD  LYS A  84     -21.859  -9.016  -0.549  1.00 96.77           C  
ANISOU  710  CD  LYS A  84    10027  14642  12099   3429   -154  -3136       C  
ATOM    711  CE  LYS A  84     -23.193  -9.602  -1.002  1.00 99.16           C  
ANISOU  711  CE  LYS A  84     9886  15546  12243   3408   -170  -3236       C  
ATOM    712  NZ  LYS A  84     -23.308  -9.560  -2.482  1.00 99.90           N  
ANISOU  712  NZ  LYS A  84    10068  15440  12450   3634   -408  -2998       N  
ATOM    713  N   VAL A  85     -20.248 -12.570   2.994  1.00 65.42           N  
ANISOU  713  N   VAL A  85     5916  11697   7245   1523    902  -2907       N  
ATOM    714  CA  VAL A  85     -19.679 -13.907   2.940  1.00 66.86           C  
ANISOU  714  CA  VAL A  85     6224  11904   7274    987   1052  -2558       C  
ATOM    715  C   VAL A  85     -19.282 -14.214   1.498  1.00 67.91           C  
ANISOU  715  C   VAL A  85     6633  11571   7599   1024    894  -2218       C  
ATOM    716  O   VAL A  85     -20.011 -13.897   0.548  1.00 69.87           O  
ANISOU  716  O   VAL A  85     6740  11872   7936   1316    753  -2292       O  
ATOM    717  CB  VAL A  85     -20.670 -14.943   3.495  1.00 76.39           C  
ANISOU  717  CB  VAL A  85     7081  13753   8190    534   1175  -2574       C  
ATOM    718  CG1 VAL A  85     -21.899 -15.075   2.586  1.00 76.60           C  
ANISOU  718  CG1 VAL A  85     6795  14084   8224    667   1070  -2676       C  
ATOM    719  CG2 VAL A  85     -19.987 -16.289   3.707  1.00 77.92           C  
ANISOU  719  CG2 VAL A  85     7461  13916   8228    -56   1310  -2213       C  
ATOM    720  N   LYS A  86     -18.095 -14.781   1.326  1.00 61.16           N  
ANISOU  720  N   LYS A  86     6159  10279   6799    754    906  -1864       N  
ATOM    721  CA  LYS A  86     -17.645 -15.268   0.030  1.00 63.30           C  
ANISOU  721  CA  LYS A  86     6666  10197   7188    712    800  -1566       C  
ATOM    722  C   LYS A  86     -17.338 -16.745   0.179  1.00 61.39           C  
ANISOU  722  C   LYS A  86     6496  10004   6826    206    897  -1333       C  
ATOM    723  O   LYS A  86     -16.959 -17.202   1.261  1.00 66.09           O  
ANISOU  723  O   LYS A  86     7126  10679   7308    -88   1006  -1283       O  
ATOM    724  CB  LYS A  86     -16.401 -14.509  -0.476  1.00 62.44           C  
ANISOU  724  CB  LYS A  86     6953   9486   7286    910    691  -1381       C  
ATOM    725  CG  LYS A  86     -16.597 -13.005  -0.721  1.00 65.15           C  
ANISOU  725  CG  LYS A  86     7330   9630   7795   1394    526  -1548       C  
ATOM    726  CD  LYS A  86     -17.416 -12.710  -1.960  1.00 72.52           C  
ANISOU  726  CD  LYS A  86     8164  10602   8787   1674    345  -1548       C  
ATOM    727  CE  LYS A  86     -16.999 -11.370  -2.577  1.00 77.24           C  
ANISOU  727  CE  LYS A  86     9035  10716   9597   2050    110  -1476       C  
ATOM    728  NZ  LYS A  86     -18.083 -10.712  -3.388  1.00 78.68           N  
ANISOU  728  NZ  LYS A  86     9053  10991   9850   2463   -126  -1589       N  
ATOM    729  N   TYR A  87     -17.532 -17.507  -0.896  1.00 48.95           N  
ANISOU  729  N   TYR A  87     4952   8378   5268     99    831  -1199       N  
ATOM    730  CA  TYR A  87     -17.285 -18.943  -0.866  1.00 45.12           C  
ANISOU  730  CA  TYR A  87     4571   7858   4715   -354    869  -1004       C  
ATOM    731  C   TYR A  87     -16.128 -19.249  -1.804  1.00 51.62           C  
ANISOU  731  C   TYR A  87     5741   8175   5696   -311    790   -790       C  
ATOM    732  O   TYR A  87     -16.098 -18.755  -2.928  1.00 63.90           O  
ANISOU  732  O   TYR A  87     7343   9606   7328    -51    700   -792       O  
ATOM    733  CB  TYR A  87     -18.553 -19.734  -1.242  1.00 47.68           C  
ANISOU  733  CB  TYR A  87     4609   8604   4902   -583    861  -1089       C  
ATOM    734  CG  TYR A  87     -19.701 -19.481  -0.263  1.00 61.72           C  
ANISOU  734  CG  TYR A  87     5971  11001   6480   -666    967  -1326       C  
ATOM    735  CD1 TYR A  87     -20.528 -18.364  -0.395  1.00 65.49           C  
ANISOU  735  CD1 TYR A  87     6138  11784   6961   -240    940  -1619       C  
ATOM    736  CD2 TYR A  87     -19.926 -20.334   0.808  1.00 63.60           C  
ANISOU  736  CD2 TYR A  87     6122  11530   6514  -1160   1081  -1261       C  
ATOM    737  CE1 TYR A  87     -21.557 -18.117   0.513  1.00 70.54           C  
ANISOU  737  CE1 TYR A  87     6339  13059   7402   -277   1053  -1905       C  
ATOM    738  CE2 TYR A  87     -20.951 -20.095   1.714  1.00 76.60           C  
ANISOU  738  CE2 TYR A  87     7345  13840   7919  -1271   1208  -1498       C  
ATOM    739  CZ  TYR A  87     -21.767 -18.985   1.557  1.00 75.24           C  
ANISOU  739  CZ  TYR A  87     6817  14019   7752   -810   1207  -1852       C  
ATOM    740  OH  TYR A  87     -22.786 -18.747   2.463  1.00 77.04           O  
ANISOU  740  OH  TYR A  87     6689  14806   7778   -872   1248  -2096       O  
ATOM    741  N   LEU A  88     -15.169 -20.032  -1.328  1.00 47.97           N  
ANISOU  741  N   LEU A  88     5505   7456   5266   -556    814   -613       N  
ATOM    742  CA  LEU A  88     -13.987 -20.401  -2.090  1.00 44.33           C  
ANISOU  742  CA  LEU A  88     5325   6574   4946   -512    756   -460       C  
ATOM    743  C   LEU A  88     -14.105 -21.864  -2.472  1.00 50.21           C  
ANISOU  743  C   LEU A  88     6138   7248   5690   -807    701   -396       C  
ATOM    744  O   LEU A  88     -14.130 -22.732  -1.594  1.00 46.76           O  
ANISOU  744  O   LEU A  88     5744   6811   5214  -1128    699   -304       O  
ATOM    745  CB  LEU A  88     -12.714 -20.163  -1.281  1.00 51.93           C  
ANISOU  745  CB  LEU A  88     6479   7273   5980   -507    784   -339       C  
ATOM    746  CG  LEU A  88     -11.378 -20.451  -1.983  1.00 47.04           C  
ANISOU  746  CG  LEU A  88     6088   6287   5497   -431    738   -216       C  
ATOM    747  CD1 LEU A  88     -11.132 -19.469  -3.091  1.00 48.80           C  
ANISOU  747  CD1 LEU A  88     6336   6445   5761   -150    720   -242       C  
ATOM    748  CD2 LEU A  88     -10.249 -20.381  -0.973  1.00 55.16           C  
ANISOU  748  CD2 LEU A  88     7244   7142   6574   -485    752   -104       C  
ATOM    749  N   TYR A  89     -14.180 -22.140  -3.784  1.00 44.92           N  
ANISOU  749  N   TYR A  89     5500   6510   5058   -716    634   -444       N  
ATOM    750  CA  TYR A  89     -14.302 -23.507  -4.276  1.00 49.44           C  
ANISOU  750  CA  TYR A  89     6158   6974   5653   -967    554   -445       C  
ATOM    751  C   TYR A  89     -12.990 -23.930  -4.918  1.00 51.31           C  
ANISOU  751  C   TYR A  89     6639   6827   6030   -846    508   -410       C  
ATOM    752  O   TYR A  89     -12.627 -23.418  -5.986  1.00 56.90           O  
ANISOU  752  O   TYR A  89     7357   7529   6734   -606    512   -468       O  
ATOM    753  CB  TYR A  89     -15.420 -23.624  -5.295  1.00 48.26           C  
ANISOU  753  CB  TYR A  89     5831   7096   5411   -978    504   -590       C  
ATOM    754  CG  TYR A  89     -16.816 -23.223  -4.861  1.00 50.12           C  
ANISOU  754  CG  TYR A  89     5742   7802   5498  -1058    538   -685       C  
ATOM    755  CD1 TYR A  89     -17.204 -21.888  -4.854  1.00 50.74           C  
ANISOU  755  CD1 TYR A  89     5635   8104   5539   -724    569   -764       C  
ATOM    756  CD2 TYR A  89     -17.772 -24.188  -4.551  1.00 51.15           C  
ANISOU  756  CD2 TYR A  89     5739   8165   5532  -1462    515   -716       C  
ATOM    757  CE1 TYR A  89     -18.490 -21.525  -4.543  1.00 54.41           C  
ANISOU  757  CE1 TYR A  89     5752   9041   5881   -728    585   -913       C  
ATOM    758  CE2 TYR A  89     -19.060 -23.833  -4.245  1.00 52.64           C  
ANISOU  758  CE2 TYR A  89     5561   8879   5561  -1534    556   -841       C  
ATOM    759  CZ  TYR A  89     -19.407 -22.496  -4.234  1.00 57.91           C  
ANISOU  759  CZ  TYR A  89     6010   9793   6201  -1133    596   -960       C  
ATOM    760  OH  TYR A  89     -20.684 -22.108  -3.905  1.00 57.55           O  
ANISOU  760  OH  TYR A  89     5549  10309   6007  -1136    629  -1140       O  
ATOM    761  N   PHE A  90     -12.302 -24.878  -4.295  1.00 47.13           N  
ANISOU  761  N   PHE A  90     6289   6010   5608  -1014    451   -317       N  
ATOM    762  CA  PHE A  90     -11.157 -25.498  -4.937  1.00 49.04           C  
ANISOU  762  CA  PHE A  90     6715   5920   5997   -886    382   -354       C  
ATOM    763  C   PHE A  90     -11.620 -26.467  -6.014  1.00 54.58           C  
ANISOU  763  C   PHE A  90     7452   6572   6713   -967    285   -527       C  
ATOM    764  O   PHE A  90     -12.633 -27.149  -5.852  1.00 54.34           O  
ANISOU  764  O   PHE A  90     7395   6611   6642  -1258    215   -542       O  
ATOM    765  CB  PHE A  90     -10.304 -26.225  -3.908  1.00 47.91           C  
ANISOU  765  CB  PHE A  90     6751   5460   5990   -994    297   -208       C  
ATOM    766  CG  PHE A  90      -9.530 -25.305  -3.035  1.00 53.37           C  
ANISOU  766  CG  PHE A  90     7428   6176   6676   -873    379    -78       C  
ATOM    767  CD1 PHE A  90      -8.650 -24.392  -3.592  1.00 53.86           C  
ANISOU  767  CD1 PHE A  90     7456   6254   6755   -587    461   -122       C  
ATOM    768  CD2 PHE A  90      -9.666 -25.345  -1.673  1.00 61.25           C  
ANISOU  768  CD2 PHE A  90     8444   7207   7622  -1084    368     89       C  
ATOM    769  CE1 PHE A  90      -7.935 -23.520  -2.800  1.00 51.12           C  
ANISOU  769  CE1 PHE A  90     7101   5919   6405   -511    520    -16       C  
ATOM    770  CE2 PHE A  90      -8.952 -24.480  -0.878  1.00 59.28           C  
ANISOU  770  CE2 PHE A  90     8178   6996   7350   -981    433    174       C  
ATOM    771  CZ  PHE A  90      -8.091 -23.574  -1.441  1.00 57.51           C  
ANISOU  771  CZ  PHE A  90     7928   6748   7175   -694    503    113       C  
ATOM    772  N   ILE A  91     -10.872 -26.506  -7.119  1.00 49.42           N  
ANISOU  772  N   ILE A  91     6842   5842   6093   -735    284   -674       N  
ATOM    773  CA  ILE A  91     -11.098 -27.501  -8.160  1.00 51.55           C  
ANISOU  773  CA  ILE A  91     7169   6034   6382   -781    180   -900       C  
ATOM    774  C   ILE A  91     -11.020 -28.895  -7.568  1.00 59.57           C  
ANISOU  774  C   ILE A  91     8391   6652   7590  -1004      4   -901       C  
ATOM    775  O   ILE A  91     -10.135 -29.197  -6.753  1.00 58.90           O  
ANISOU  775  O   ILE A  91     8445   6270   7665   -961    -54   -779       O  
ATOM    776  CB  ILE A  91     -10.057 -27.336  -9.282  1.00 52.70           C  
ANISOU  776  CB  ILE A  91     7319   6192   6514   -486    227  -1077       C  
ATOM    777  CG1 ILE A  91     -10.156 -25.945  -9.888  1.00 58.73           C  
ANISOU  777  CG1 ILE A  91     7926   7317   7072   -329    361  -1007       C  
ATOM    778  CG2 ILE A  91     -10.279 -28.362 -10.349  1.00 66.67           C  
ANISOU  778  CG2 ILE A  91     9140   7908   8284   -517    122  -1375       C  
ATOM    779  CD1 ILE A  91     -11.533 -25.575 -10.326  1.00 64.37           C  
ANISOU  779  CD1 ILE A  91     8506   8333   7618   -428    341  -1015       C  
ATOM    780  N   LYS A  92     -11.952 -29.755  -7.974  1.00 56.22           N  
ANISOU  780  N   LYS A  92     8002   6205   7153  -1258   -114  -1024       N  
ATOM    781  CA  LYS A  92     -11.968 -31.117  -7.460  1.00 58.86           C  
ANISOU  781  CA  LYS A  92     8584   6096   7682  -1525   -334  -1001       C  
ATOM    782  C   LYS A  92     -10.646 -31.798  -7.784  1.00 66.55           C  
ANISOU  782  C   LYS A  92     9757   6633   8895  -1233   -455  -1165       C  
ATOM    783  O   LYS A  92     -10.190 -31.781  -8.928  1.00 74.66           O  
ANISOU  783  O   LYS A  92    10733   7729   9906   -960   -417  -1465       O  
ATOM    784  CB  LYS A  92     -13.145 -31.910  -8.050  1.00 72.16           C  
ANISOU  784  CB  LYS A  92    10276   7827   9313  -1859   -454  -1155       C  
ATOM    785  CG  LYS A  92     -13.456 -33.246  -7.335  1.00 81.28           C  
ANISOU  785  CG  LYS A  92    11706   8535  10641  -2286   -707  -1040       C  
ATOM    786  CD  LYS A  92     -12.672 -34.413  -7.934  1.00 98.29           C  
ANISOU  786  CD  LYS A  92    14163  10108  13075  -2141   -948  -1294       C  
ATOM    787  CE  LYS A  92     -12.086 -35.340  -6.860  1.00105.14           C  
ANISOU  787  CE  LYS A  92    15368  10367  14212  -2281  -1203  -1057       C  
ATOM    788  NZ  LYS A  92     -10.962 -36.189  -7.384  1.00108.79           N  
ANISOU  788  NZ  LYS A  92    16077  10266  14991  -1913  -1420  -1340       N  
ATOM    789  N   GLY A  93     -10.023 -32.385  -6.768  1.00 66.46           N  
ANISOU  789  N   GLY A  93     9951   6213   9087  -1281   -608   -977       N  
ATOM    790  CA  GLY A  93      -8.759 -33.057  -6.955  1.00 60.75           C  
ANISOU  790  CA  GLY A  93     9390   5068   8624   -958   -761  -1140       C  
ATOM    791  C   GLY A  93      -7.538 -32.180  -6.837  1.00 61.31           C  
ANISOU  791  C   GLY A  93     9313   5295   8687   -575   -604  -1117       C  
ATOM    792  O   GLY A  93      -6.425 -32.670  -7.067  1.00 71.28           O  
ANISOU  792  O   GLY A  93    10633   6300  10148   -257   -711  -1301       O  
ATOM    793  N   LEU A  94      -7.744 -30.914  -6.484  1.00 54.29           N  
ANISOU  793  N   LEU A  94     8227   4821   7581   -603   -372   -918       N  
ATOM    794  CA  LEU A  94      -6.587 -30.005  -6.403  1.00 54.85           C  
ANISOU  794  CA  LEU A  94     8159   5052   7630   -296   -226   -888       C  
ATOM    795  C   LEU A  94      -5.666 -30.498  -5.302  1.00 66.01           C  
ANISOU  795  C   LEU A  94     9711   6116   9255   -239   -395   -715       C  
ATOM    796  O   LEU A  94      -6.129 -30.724  -4.220  1.00 64.76           O  
ANISOU  796  O   LEU A  94     9675   5827   9105   -514   -494   -439       O  
ATOM    797  CB  LEU A  94      -7.062 -28.589  -6.132  1.00 48.06           C  
ANISOU  797  CB  LEU A  94     7120   4608   6534   -366     -2   -701       C  
ATOM    798  CG  LEU A  94      -5.957 -27.549  -6.149  1.00 51.52           C  
ANISOU  798  CG  LEU A  94     7427   5220   6927   -119    146   -664       C  
ATOM    799  CD1 LEU A  94      -5.492 -27.290  -7.556  1.00 56.23           C  
ANISOU  799  CD1 LEU A  94     7902   6031   7431    100    249   -916       C  
ATOM    800  CD2 LEU A  94      -6.415 -26.261  -5.513  1.00 49.92           C  
ANISOU  800  CD2 LEU A  94     7128   5274   6564   -216    290   -449       C  
ATOM    801  N   ASN A  95      -4.383 -30.568  -5.590  1.00 62.89           N  
ANISOU  801  N   ASN A  95     9258   5652   8987    107   -415   -873       N  
ATOM    802  CA  ASN A  95      -3.404 -31.073  -4.609  1.00 60.12           C  
ANISOU  802  CA  ASN A  95     9013   4975   8856    225   -619   -731       C  
ATOM    803  C   ASN A  95      -3.195 -30.071  -3.477  1.00 55.22           C  
ANISOU  803  C   ASN A  95     8313   4565   8103    107   -508   -395       C  
ATOM    804  O   ASN A  95      -3.440 -28.913  -3.647  1.00 50.72           O  
ANISOU  804  O   ASN A  95     7575   4376   7320     64   -263   -360       O  
ATOM    805  CB  ASN A  95      -2.129 -31.547  -5.292  1.00 61.17           C  
ANISOU  805  CB  ASN A  95     9059   5007   9177    662   -696  -1064       C  
ATOM    806  CG  ASN A  95      -1.342 -30.402  -5.849  1.00 67.99           C  
ANISOU  806  CG  ASN A  95     9612   6363   9857    860   -415  -1169       C  
ATOM    807  OD1 ASN A  95      -1.592 -29.279  -5.490  1.00 69.32           O  
ANISOU  807  OD1 ASN A  95     9688   6825   9823    690   -223   -937       O  
ATOM    808  ND2 ASN A  95      -0.381 -30.680  -6.696  1.00 69.27           N  
ANISOU  808  ND2 ASN A  95     9611   6622  10088   1203   -401  -1524       N  
ATOM    809  N   ASN A  96      -2.650 -30.548  -2.380  1.00 55.36           N  
ANISOU  809  N   ASN A  96     8462   4312   8262     88   -721   -176       N  
ATOM    810  CA  ASN A  96      -2.445 -29.728  -1.172  1.00 52.00           C  
ANISOU  810  CA  ASN A  96     7985   4072   7700    -56   -657    134       C  
ATOM    811  C   ASN A  96      -1.467 -28.583  -1.417  1.00 48.35           C  
ANISOU  811  C   ASN A  96     7266   3947   7156    180   -449     44       C  
ATOM    812  O   ASN A  96      -1.615 -27.597  -0.794  1.00 50.97           O  
ANISOU  812  O   ASN A  96     7526   4524   7316     36   -307    205       O  
ATOM    813  CB  ASN A  96      -1.968 -30.605  -0.033  1.00 58.81           C  
ANISOU  813  CB  ASN A  96     9053   4567   8724   -114   -980    389       C  
ATOM    814  CG  ASN A  96      -3.064 -31.487   0.498  1.00 63.35           C  
ANISOU  814  CG  ASN A  96     9898   4881   9290   -513  -1165    610       C  
ATOM    815  OD1 ASN A  96      -4.214 -31.094   0.535  1.00 62.57           O  
ANISOU  815  OD1 ASN A  96     9765   5035   8974   -830   -994    668       O  
ATOM    816  ND2 ASN A  96      -2.698 -32.681   0.912  1.00 69.19           N  
ANISOU  816  ND2 ASN A  96    10899   5120  10269   -502  -1537    736       N  
ATOM    817  N   LEU A  97      -0.484 -28.746  -2.273  1.00 51.79           N  
ANISOU  817  N   LEU A  97     7566   4401   7709    514   -444   -221       N  
ATOM    818  CA  LEU A  97       0.453 -27.635  -2.462  1.00 47.72           C  
ANISOU  818  CA  LEU A  97     6798   4250   7086    650   -246   -266       C  
ATOM    819  C   LEU A  97      -0.271 -26.476  -3.128  1.00 52.25           C  
ANISOU  819  C   LEU A  97     7282   5159   7414    507     34   -281       C  
ATOM    820  O   LEU A  97      -0.140 -25.398  -2.684  1.00 44.98           O  
ANISOU  820  O   LEU A  97     6290   4438   6364    407    158   -138       O  
ATOM    821  CB  LEU A  97       1.603 -28.092  -3.340  1.00 54.21           C  
ANISOU  821  CB  LEU A  97     7438   5117   8041   1015   -277   -585       C  
ATOM    822  CG  LEU A  97       2.605 -26.994  -3.640  1.00 60.21           C  
ANISOU  822  CG  LEU A  97     7906   6310   8660   1094    -66   -634       C  
ATOM    823  CD1 LEU A  97       3.504 -26.772  -2.463  1.00 54.71           C  
ANISOU  823  CD1 LEU A  97     7150   5606   8031   1108   -182   -438       C  
ATOM    824  CD2 LEU A  97       3.407 -27.308  -4.874  1.00 62.87           C  
ANISOU  824  CD2 LEU A  97     8006   6867   9013   1385      6  -1015       C  
ATOM    825  N   ASN A  98      -1.026 -26.753  -4.172  1.00 49.75           N  
ANISOU  825  N   ASN A  98     6987   4869   7048    506     92   -459       N  
ATOM    826  CA  ASN A  98      -1.724 -25.670  -4.843  1.00 48.80           C  
ANISOU  826  CA  ASN A  98     6789   5052   6699    398    307   -450       C  
ATOM    827  C   ASN A  98      -2.826 -25.109  -3.979  1.00 37.87           C  
ANISOU  827  C   ASN A  98     5494   3677   5218    150    332   -225       C  
ATOM    828  O   ASN A  98      -3.097 -23.910  -4.030  1.00 40.97           O  
ANISOU  828  O   ASN A  98     5820   4284   5462     98    474   -149       O  
ATOM    829  CB  ASN A  98      -2.310 -26.151  -6.157  1.00 55.80           C  
ANISOU  829  CB  ASN A  98     7670   6002   7532    449    335   -694       C  
ATOM    830  CG  ASN A  98      -1.266 -26.357  -7.200  1.00 55.89           C  
ANISOU  830  CG  ASN A  98     7521   6178   7537    691    390   -970       C  
ATOM    831  OD1 ASN A  98      -0.498 -25.449  -7.516  1.00 53.14           O  
ANISOU  831  OD1 ASN A  98     7004   6130   7057    731    541   -947       O  
ATOM    832  ND2 ASN A  98      -1.210 -27.570  -7.742  1.00 60.17           N  
ANISOU  832  ND2 ASN A  98     8108   6538   8216    840    260  -1254       N  
ATOM    833  N   ARG A  99      -3.474 -25.961  -3.209  1.00 40.00           N  
ANISOU  833  N   ARG A  99     5910   3727   5563    -10    185   -130       N  
ATOM    834  CA  ARG A  99      -4.501 -25.514  -2.252  1.00 47.06           C  
ANISOU  834  CA  ARG A  99     6840   4711   6331   -268    219     58       C  
ATOM    835  C   ARG A  99      -3.849 -24.535  -1.271  1.00 40.43           C  
ANISOU  835  C   ARG A  99     5947   3982   5434   -272    279    205       C  
ATOM    836  O   ARG A  99      -4.395 -23.512  -1.060  1.00 39.22           O  
ANISOU  836  O   ARG A  99     5731   4028   5145   -334    403    231       O  
ATOM    837  CB  ARG A  99      -5.127 -26.744  -1.591  1.00 56.24           C  
ANISOU  837  CB  ARG A  99     8169   5636   7563   -498     31    163       C  
ATOM    838  CG  ARG A  99      -6.122 -26.449  -0.483  1.00 72.87           C  
ANISOU  838  CG  ARG A  99    10278   7911   9500   -813     66    352       C  
ATOM    839  CD  ARG A  99      -6.955 -27.601   0.034  1.00 80.87           C  
ANISOU  839  CD  ARG A  99    11440   8775  10513  -1150    -97    483       C  
ATOM    840  NE  ARG A  99      -7.142 -28.626  -0.976  1.00 91.42           N  
ANISOU  840  NE  ARG A  99    12881   9852  12003  -1118   -223    329       N  
ATOM    841  CZ  ARG A  99      -8.314 -29.048  -1.408  1.00 93.65           C  
ANISOU  841  CZ  ARG A  99    13162  10204  12216  -1348   -227    265       C  
ATOM    842  NH1 ARG A  99      -8.376 -29.979  -2.335  1.00 89.33           N  
ANISOU  842  NH1 ARG A  99    12728   9395  11819  -1309   -360     89       N  
ATOM    843  NH2 ARG A  99      -9.420 -28.550  -0.905  1.00 96.83           N  
ANISOU  843  NH2 ARG A  99    13429  10965  12396  -1616   -103    344       N  
ATOM    844  N   GLY A 100      -2.670 -24.848  -0.757  1.00 43.45           N  
ANISOU  844  N   GLY A 100     6344   4234   5930   -179    172    265       N  
ATOM    845  CA  GLY A 100      -1.991 -23.941   0.171  1.00 41.33           C  
ANISOU  845  CA  GLY A 100     6019   4088   5598   -206    211    386       C  
ATOM    846  C   GLY A 100      -1.553 -22.662  -0.508  1.00 45.65           C  
ANISOU  846  C   GLY A 100     6435   4838   6073   -102    387    300       C  
ATOM    847  O   GLY A 100      -1.686 -21.642   0.067  1.00 36.99           O  
ANISOU  847  O   GLY A 100     5324   3856   4876   -191    461    360       O  
ATOM    848  N   MET A 101      -1.068 -22.746  -1.731  1.00 36.96           N  
ANISOU  848  N   MET A 101     5252   3782   5010     62    440    154       N  
ATOM    849  CA  MET A 101      -0.614 -21.545  -2.458  1.00 31.45           C  
ANISOU  849  CA  MET A 101     4449   3290   4212     94    590    124       C  
ATOM    850  C   MET A 101      -1.757 -20.535  -2.543  1.00 35.15           C  
ANISOU  850  C   MET A 101     4977   3825   4555     -4    676    171       C  
ATOM    851  O   MET A 101      -1.544 -19.417  -2.253  1.00 40.76           O  
ANISOU  851  O   MET A 101     5688   4587   5213    -56    723    239       O  
ATOM    852  CB  MET A 101      -0.144 -21.922  -3.858  1.00 39.55           C  
ANISOU  852  CB  MET A 101     5368   4429   5230    241    644    -50       C  
ATOM    853  CG  MET A 101       1.352 -21.969  -3.994  1.00 61.60           C  
ANISOU  853  CG  MET A 101     7988   7352   8066    349    651   -116       C  
ATOM    854  SD  MET A 101       1.878 -22.947  -5.393  1.00 73.58           S  
ANISOU  854  SD  MET A 101     9351   9006   9600    576    673   -423       S  
ATOM    855  CE  MET A 101       0.937 -22.182  -6.699  1.00 88.92           C  
ANISOU  855  CE  MET A 101    11324  11161  11299    461    833   -430       C  
ATOM    856  N   VAL A 102      -2.949 -20.980  -2.886  1.00 36.34           N  
ANISOU  856  N   VAL A 102     5172   3959   4676    -22    667    120       N  
ATOM    857  CA  VAL A 102      -4.122 -20.086  -2.989  1.00 37.59           C  
ANISOU  857  CA  VAL A 102     5343   4208   4730    -60    720    129       C  
ATOM    858  C   VAL A 102      -4.456 -19.494  -1.626  1.00 40.65           C  
ANISOU  858  C   VAL A 102     5755   4598   5094   -154    715    191       C  
ATOM    859  O   VAL A 102      -4.613 -18.338  -1.536  1.00 43.54           O  
ANISOU  859  O   VAL A 102     6126   4998   5420   -125    750    192       O  
ATOM    860  CB  VAL A 102      -5.299 -20.866  -3.569  1.00 43.72           C  
ANISOU  860  CB  VAL A 102     6116   5019   5478    -78    695     40       C  
ATOM    861  CG1 VAL A 102      -6.576 -20.096  -3.423  1.00 46.40           C  
ANISOU  861  CG1 VAL A 102     6418   5488   5725    -97    721     30       C  
ATOM    862  CG2 VAL A 102      -5.046 -21.247  -5.004  1.00 37.43           C  
ANISOU  862  CG2 VAL A 102     5290   4274   4658     21    710    -66       C  
ATOM    863  N   LEU A 103      -4.491 -20.314  -0.601  1.00 39.86           N  
ANISOU  863  N   LEU A 103     5680   4454   5013   -272    653    239       N  
ATOM    864  CA  LEU A 103      -4.849 -19.881   0.762  1.00 46.34           C  
ANISOU  864  CA  LEU A 103     6502   5358   5749   -401    657    277       C  
ATOM    865  C   LEU A 103      -3.856 -18.840   1.266  1.00 48.30           C  
ANISOU  865  C   LEU A 103     6758   5592   6003   -372    672    299       C  
ATOM    866  O   LEU A 103      -4.271 -17.945   1.925  1.00 48.66           O  
ANISOU  866  O   LEU A 103     6796   5719   5974   -398    707    240       O  
ATOM    867  CB  LEU A 103      -4.861 -21.116   1.658  1.00 38.78           C  
ANISOU  867  CB  LEU A 103     5595   4353   4785   -579    554    389       C  
ATOM    868  CG  LEU A 103      -6.079 -22.014   1.528  1.00 43.64           C  
ANISOU  868  CG  LEU A 103     6214   5016   5352   -727    532    382       C  
ATOM    869  CD1 LEU A 103      -6.025 -23.120   2.533  1.00 48.34           C  
ANISOU  869  CD1 LEU A 103     6908   5534   5925   -968    396    559       C  
ATOM    870  CD2 LEU A 103      -7.356 -21.238   1.660  1.00 47.60           C  
ANISOU  870  CD2 LEU A 103     6592   5790   5704   -764    645    266       C  
ATOM    871  N   GLY A 104      -2.587 -19.005   0.970  1.00 41.98           N  
ANISOU  871  N   GLY A 104     5954   4710   5288   -324    638    354       N  
ATOM    872  CA  GLY A 104      -1.584 -18.030   1.387  1.00 29.88           C  
ANISOU  872  CA  GLY A 104     4411   3186   3756   -347    643    379       C  
ATOM    873  C   GLY A 104      -1.634 -16.797   0.534  1.00 39.32           C  
ANISOU  873  C   GLY A 104     5629   4369   4944   -294    709    342       C  
ATOM    874  O   GLY A 104      -1.538 -15.736   1.059  1.00 47.90           O  
ANISOU  874  O   GLY A 104     6763   5427   6010   -344    705    322       O  
ATOM    875  N   SER A 105      -1.881 -16.963  -0.742  1.00 36.81           N  
ANISOU  875  N   SER A 105     5297   4059   4631   -207    746    331       N  
ATOM    876  CA  SER A 105      -1.868 -15.824  -1.648  1.00 32.67           C  
ANISOU  876  CA  SER A 105     4820   3516   4077   -189    772    361       C  
ATOM    877  C   SER A 105      -3.044 -14.893  -1.374  1.00 33.87           C  
ANISOU  877  C   SER A 105     5057   3597   4216   -132    743    305       C  
ATOM    878  O   SER A 105      -2.897 -13.666  -1.475  1.00 40.93           O  
ANISOU  878  O   SER A 105     6051   4373   5127   -141    701    338       O  
ATOM    879  CB  SER A 105      -1.869 -16.314  -3.100  1.00 37.01           C  
ANISOU  879  CB  SER A 105     5321   4157   4583   -126    811    364       C  
ATOM    880  OG  SER A 105      -1.849 -15.228  -4.011  1.00 40.39           O  
ANISOU  880  OG  SER A 105     5815   4587   4943   -152    813    454       O  
ATOM    881  N   LEU A 106      -4.234 -15.441  -1.077  1.00 31.68           N  
ANISOU  881  N   LEU A 106     4735   3390   3913    -71    747    210       N  
ATOM    882  CA  LEU A 106      -5.394 -14.566  -0.879  1.00 38.22           C  
ANISOU  882  CA  LEU A 106     5578   4213   4729     40    717    100       C  
ATOM    883  C   LEU A 106      -5.420 -13.914   0.481  1.00 47.15           C  
ANISOU  883  C   LEU A 106     6724   5333   5857     11    706    -13       C  
ATOM    884  O   LEU A 106      -6.242 -13.015   0.693  1.00 44.52           O  
ANISOU  884  O   LEU A 106     6400   4978   5537    150    666   -160       O  
ATOM    885  CB  LEU A 106      -6.715 -15.326  -1.020  1.00 42.31           C  
ANISOU  885  CB  LEU A 106     5981   4905   5191     91    735      5       C  
ATOM    886  CG  LEU A 106      -6.974 -16.101  -2.294  1.00 53.27           C  
ANISOU  886  CG  LEU A 106     7337   6346   6558    116    736     51       C  
ATOM    887  CD1 LEU A 106      -8.332 -16.788  -2.122  1.00 50.97           C  
ANISOU  887  CD1 LEU A 106     6914   6248   6204    104    743    -63       C  
ATOM    888  CD2 LEU A 106      -6.947 -15.133  -3.454  1.00 49.89           C  
ANISOU  888  CD2 LEU A 106     6983   5844   6130    238    680    119       C  
ATOM    889  N   ALA A 107      -4.566 -14.356   1.400  1.00 45.22           N  
ANISOU  889  N   ALA A 107     6472   5121   5589   -144    724     28       N  
ATOM    890  CA  ALA A 107      -4.772 -14.074   2.822  1.00 50.03           C  
ANISOU  890  CA  ALA A 107     7056   5832   6122   -212    729   -103       C  
ATOM    891  C   ALA A 107      -4.698 -12.588   3.148  1.00 48.66           C  
ANISOU  891  C   ALA A 107     6979   5512   5998   -134    676   -247       C  
ATOM    892  O   ALA A 107      -5.540 -12.074   3.888  1.00 43.66           O  
ANISOU  892  O   ALA A 107     6300   4976   5312    -49    680   -477       O  
ATOM    893  CB  ALA A 107      -3.754 -14.847   3.631  1.00 42.83           C  
ANISOU  893  CB  ALA A 107     6132   4975   5166   -397    717     17       C  
ATOM    894  N   ALA A 108      -3.707 -11.872   2.612  1.00 47.60           N  
ANISOU  894  N   ALA A 108     6972   5151   5962   -172    617   -135       N  
ATOM    895  CA  ALA A 108      -3.589 -10.459   2.943  1.00 41.21           C  
ANISOU  895  CA  ALA A 108     6308   4122   5228   -137    523   -262       C  
ATOM    896  C   ALA A 108      -4.785  -9.654   2.455  1.00 47.31           C  
ANISOU  896  C   ALA A 108     7135   4761   6080    126    447   -409       C  
ATOM    897  O   ALA A 108      -5.170  -8.679   3.112  1.00 47.57           O  
ANISOU  897  O   ALA A 108     7236   4672   6166    245    367   -651       O  
ATOM    898  CB  ALA A 108      -2.276  -9.902   2.389  1.00 44.04           C  
ANISOU  898  CB  ALA A 108     6793   4280   5659   -309    464    -66       C  
ATOM    899  N   THR A 109      -5.406 -10.043   1.332  1.00 38.18           N  
ANISOU  899  N   THR A 109     5940   3635   4933    245    451   -298       N  
ATOM    900  CA  THR A 109      -6.533  -9.269   0.830  1.00 42.43           C  
ANISOU  900  CA  THR A 109     6512   4055   5552    526    337   -422       C  
ATOM    901  C   THR A 109      -7.842  -9.609   1.543  1.00 47.13           C  
ANISOU  901  C   THR A 109     6884   4952   6072    702    399   -716       C  
ATOM    902  O   THR A 109      -8.700  -8.728   1.673  1.00 57.89           O  
ANISOU  902  O   THR A 109     8239   6240   7515    977    292   -956       O  
ATOM    903  CB  THR A 109      -6.666  -9.444  -0.698  1.00 51.44           C  
ANISOU  903  CB  THR A 109     7698   5144   6702    568    288   -178       C  
ATOM    904  OG1 THR A 109      -7.104 -10.767  -1.018  1.00 61.91           O  
ANISOU  904  OG1 THR A 109     8827   6783   7912    534    416   -151       O  
ATOM    905  CG2 THR A 109      -5.333  -9.223  -1.354  1.00 45.93           C  
ANISOU  905  CG2 THR A 109     7161   4281   6011    332    270    103       C  
ATOM    906  N   VAL A 110      -8.018 -10.842   2.035  1.00 44.77           N  
ANISOU  906  N   VAL A 110     6394   4997   5618    544    553   -713       N  
ATOM    907  CA  VAL A 110      -9.167 -11.136   2.893  1.00 56.88           C  
ANISOU  907  CA  VAL A 110     7693   6896   7024    610    632   -986       C  
ATOM    908  C   VAL A 110      -9.104 -10.296   4.165  1.00 55.21           C  
ANISOU  908  C   VAL A 110     7483   6712   6782    650    627  -1278       C  
ATOM    909  O   VAL A 110     -10.109  -9.732   4.617  1.00 59.33           O  
ANISOU  909  O   VAL A 110     7856   7405   7281    878    617  -1621       O  
ATOM    910  CB  VAL A 110      -9.220 -12.637   3.240  1.00 57.49           C  
ANISOU  910  CB  VAL A 110     7626   7289   6930    336    767   -858       C  
ATOM    911  CG1 VAL A 110     -10.406 -12.914   4.154  1.00 57.17           C  
ANISOU  911  CG1 VAL A 110     7324   7695   6703    318    861  -1112       C  
ATOM    912  CG2 VAL A 110      -9.319 -13.480   1.991  1.00 58.89           C  
ANISOU  912  CG2 VAL A 110     7806   7426   7144    311    760   -642       C  
ATOM    913  N   ARG A 111      -7.902 -10.191   4.739  1.00 58.77           N  
ANISOU  913  N   ARG A 111     8080   7023   7226    440    625  -1179       N  
ATOM    914  CA  ARG A 111      -7.664  -9.525   6.014  1.00 54.97           C  
ANISOU  914  CA  ARG A 111     7611   6599   6676    405    622  -1448       C  
ATOM    915  C   ARG A 111      -7.834  -8.010   5.936  1.00 64.58           C  
ANISOU  915  C   ARG A 111     8983   7465   8088    685    460  -1716       C  
ATOM    916  O   ARG A 111      -8.206  -7.376   6.940  1.00 65.32           O  
ANISOU  916  O   ARG A 111     9017   7676   8125    793    454  -2107       O  
ATOM    917  CB  ARG A 111      -6.254  -9.883   6.480  1.00 46.28           C  
ANISOU  917  CB  ARG A 111     6623   5434   5527     93    630  -1223       C  
ATOM    918  CG  ARG A 111      -5.675  -8.976   7.556  1.00 51.20           C  
ANISOU  918  CG  ARG A 111     7337   5996   6121     28    574  -1454       C  
ATOM    919  CD  ARG A 111      -6.266  -9.279   8.920  1.00 55.64           C  
ANISOU  919  CD  ARG A 111     7702   7034   6407    -47    681  -1730       C  
ATOM    920  NE  ARG A 111      -5.649  -8.428   9.933  1.00 56.23           N  
ANISOU  920  NE  ARG A 111     7865   7068   6430   -124    620  -1976       N  
ATOM    921  CZ  ARG A 111      -6.043  -8.364  11.198  1.00 64.27           C  
ANISOU  921  CZ  ARG A 111     8739   8494   7187   -186    692  -2297       C  
ATOM    922  NH1 ARG A 111      -5.417  -7.558  12.042  1.00 59.70           N  
ANISOU  922  NH1 ARG A 111     8261   7854   6566   -261    619  -2538       N  
ATOM    923  NH2 ARG A 111      -7.059  -9.105  11.617  1.00 53.27           N  
ANISOU  923  NH2 ARG A 111     7092   7603   5546   -210    839  -2383       N  
ATOM    924  N   LEU A 112      -7.539  -7.419   4.781  1.00 65.10           N  
ANISOU  924  N   LEU A 112     9264   7100   8373    788    310  -1516       N  
ATOM    925  CA  LEU A 112      -7.615  -5.979   4.573  1.00 67.60           C  
ANISOU  925  CA  LEU A 112     9808   6959   8916   1027     88  -1685       C  
ATOM    926  C   LEU A 112      -9.067  -5.523   4.625  1.00 73.62           C  
ANISOU  926  C   LEU A 112    10413   7825   9735   1458     22  -2062       C  
ATOM    927  O   LEU A 112      -9.978  -6.249   4.215  1.00 80.00           O  
ANISOU  927  O   LEU A 112    10979   8966  10453   1565    112  -2046       O  
ATOM    928  CB  LEU A 112      -6.992  -5.608   3.217  1.00 67.92           C  
ANISOU  928  CB  LEU A 112    10110   6572   9123    965    -61  -1286       C  
ATOM    929  CG  LEU A 112      -6.504  -4.175   2.970  1.00 73.04           C  
ANISOU  929  CG  LEU A 112    11116   6630  10005   1004   -328  -1276       C  
ATOM    930  CD1 LEU A 112      -5.334  -3.822   3.900  1.00 67.81           C  
ANISOU  930  CD1 LEU A 112    10578   5863   9323    694   -320  -1331       C  
ATOM    931  CD2 LEU A 112      -6.104  -3.977   1.522  1.00 78.25           C  
ANISOU  931  CD2 LEU A 112    11984   7001  10747    905   -454   -830       C  
ATOM    932  N   GLN A 113      -9.273  -4.303   5.130  1.00 73.19           N  
ANISOU  932  N   GLN A 113    10485   7483   9839   1714   -153  -2430       N  
ATOM    933  CA  GLN A 113     -10.614  -3.739   5.300  1.00 79.80           C  
ANISOU  933  CA  GLN A 113    11144   8421  10757   2199   -244  -2888       C  
ATOM    934  C   GLN A 113     -10.917  -2.623   4.291  1.00 90.50           C  
ANISOU  934  C   GLN A 113    12763   9184  12440   2537   -579  -2812       C  
ATOM    935  O   GLN A 113     -10.011  -1.949   3.783  1.00 93.74           O  
ANISOU  935  O   GLN A 113    13558   9032  13026   2384   -769  -2522       O  
ATOM    936  CB  GLN A 113     -10.791  -3.218   6.735  1.00 75.12           C  
ANISOU  936  CB  GLN A 113    10434   8033  10076   2277   -193  -3425       C  
ATOM    937  CG  GLN A 113     -10.731  -4.319   7.771  1.00 66.25           C  
ANISOU  937  CG  GLN A 113     9011   7587   8575   1962    118  -3513       C  
ATOM    938  CD  GLN A 113     -11.045  -3.834   9.188  1.00 75.51           C  
ANISOU  938  CD  GLN A 113    10013   9093   9582   1990    188  -3978       C  
ATOM    939  OE1 GLN A 113     -10.413  -2.907   9.697  1.00 73.61           O  
ANISOU  939  OE1 GLN A 113    10009   8509   9452   1973     59  -4125       O  
ATOM    940  NE2 GLN A 113     -12.014  -4.478   9.833  1.00 80.24           N  
ANISOU  940  NE2 GLN A 113    10199  10389   9897   1967    389  -4144       N  
TER     941      GLN A 113                                                      
HETATM  942  P   PO4 A 201      -6.121  -2.444  11.233  1.00148.73           P  
ANISOU  942  P   PO4 A 201    20284  17364  18863    817    -68  -3818       P  
HETATM  943  O1  PO4 A 201      -5.255  -3.110  10.192  1.00142.87           O  
ANISOU  943  O1  PO4 A 201    19654  16434  18198    534    -59  -3152       O  
HETATM  944  O2  PO4 A 201      -7.187  -1.616  10.549  1.00153.99           O  
ANISOU  944  O2  PO4 A 201    21003  17694  19812   1309   -224  -4032       O  
HETATM  945  O3  PO4 A 201      -6.772  -3.507  12.084  1.00145.81           O  
ANISOU  945  O3  PO4 A 201    19518  17792  18092    742    203  -3943       O  
HETATM  946  O4  PO4 A 201      -5.256  -1.570  12.109  1.00152.42           O  
ANISOU  946  O4  PO4 A 201    20959  17610  19343    639   -201  -4094       O  
HETATM  947  O   HOH A 301      -1.449 -13.207   1.735  1.00 40.79           O  
ANISOU  947  O   HOH A 301     6034   4346   5120   -409    655    227       O  
HETATM  948  O   HOH A 302      -3.755 -11.202  -0.860  1.00 48.33           O  
ANISOU  948  O   HOH A 302     7236   4960   6168    -20    528    222       O  
HETATM  949  O   HOH A 303      -0.733 -12.397  -3.271  1.00 39.87           O  
ANISOU  949  O   HOH A 303     6001   4223   4925   -423    698    664       O  
HETATM  950  O   HOH A 304       0.000 -11.280   0.000  0.50 59.52           O  
ANISOU  950  O   HOH A 304     8588   6465   7562      0    588      0       O  
CONECT  942  943  944  945  946                                                 
CONECT  943  942                                                                
CONECT  944  942                                                                
CONECT  945  942                                                                
CONECT  946  942                                                                
MASTER      280    0    1    2    9    0    1    6  949    1    5   11          
END                                                                             
HEADER    VIRAL PROTEIN                           03-APR-20   6WEY              
TITLE     HIGH-RESOLUTION STRUCTURE OF THE SARS-COV-2 NSP3 MACRO X DOMAIN       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NON-STRUCTURAL PROTEIN 3;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: MACRO X DOMAIN (RESIDUES 207-377);                         
COMPND   5 SYNONYM: NSP3;                                                       
COMPND   6 EC: 3.2.2.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2, COVID-19 VIRUS;              
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 GENE: REP, 1A-1B;                                                    
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: DE3;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET21                                     
KEYWDS    MACRO DOMAIN, ADP-RIBOSE-BINDING, SARS-COV-2, VIRAL PROTEIN           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.VUKSANOVIC,N.R.SILVAGGI                                             
REVDAT   4   02-SEP-20 6WEY    1       SOURCE                                   
REVDAT   3   26-AUG-20 6WEY    1       JRNL                                     
REVDAT   2   06-MAY-20 6WEY    1       COMPND SOURCE DBREF  SEQADV              
REVDAT   1   29-APR-20 6WEY    0                                                
JRNL        AUTH   D.N.FRICK,R.S.VIRDI,N.VUKSANOVIC,N.DAHAL,N.R.SILVAGGI        
JRNL        TITL   MOLECULAR BASIS FOR ADP-RIBOSE BINDING TO THE MAC1 DOMAIN OF 
JRNL        TITL 2 SARS-COV-2 NSP3.                                             
JRNL        REF    BIOCHEMISTRY                  V.  59  2608 2020              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   32578982                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.0C00309                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    0.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.17.1_3660                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.30                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.390                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 99335                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.120                           
REMARK   3   R VALUE            (WORKING SET) : 0.119                           
REMARK   3   FREE R VALUE                     : 0.136                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5046                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 30.3000 -  2.9500    0.93     3216   158  0.1497 0.1681        
REMARK   3     2  2.9500 -  2.3400    1.00     3293   174  0.1262 0.1379        
REMARK   3     3  2.3400 -  2.0500    1.00     3270   163  0.1144 0.1377        
REMARK   3     4  2.0500 -  1.8600    1.00     3239   176  0.1110 0.1455        
REMARK   3     5  1.8600 -  1.7300    1.00     3236   179  0.1108 0.1130        
REMARK   3     6  1.7300 -  1.6200    1.00     3252   154  0.1042 0.1100        
REMARK   3     7  1.6200 -  1.5400    1.00     3192   168  0.0995 0.1320        
REMARK   3     8  1.5400 -  1.4800    1.00     3223   160  0.1041 0.1254        
REMARK   3     9  1.4800 -  1.4200    1.00     3233   154  0.1023 0.1125        
REMARK   3    10  1.4200 -  1.3700    1.00     3204   173  0.1052 0.1208        
REMARK   3    11  1.3700 -  1.3300    1.00     3177   177  0.1054 0.1141        
REMARK   3    12  1.3300 -  1.2900    1.00     3158   193  0.1046 0.1215        
REMARK   3    13  1.2900 -  1.2600    1.00     3179   190  0.1031 0.1180        
REMARK   3    14  1.2600 -  1.2200    1.00     3154   185  0.1046 0.1253        
REMARK   3    15  1.2200 -  1.2000    1.00     3175   167  0.0991 0.1281        
REMARK   3    16  1.2000 -  1.1700    1.00     3183   163  0.0980 0.1164        
REMARK   3    17  1.1700 -  1.1500    1.00     3189   164  0.1035 0.0965        
REMARK   3    18  1.1500 -  1.1300    1.00     3150   161  0.1031 0.1090        
REMARK   3    19  1.1300 -  1.1100    1.00     3182   163  0.1016 0.1247        
REMARK   3    20  1.1100 -  1.0900    1.00     3139   167  0.1026 0.1135        
REMARK   3    21  1.0900 -  1.0700    0.99     3143   172  0.1107 0.1307        
REMARK   3    22  1.0700 -  1.0500    0.99     3179   153  0.1168 0.1779        
REMARK   3    23  1.0500 -  1.0400    0.99     3122   181  0.1224 0.1386        
REMARK   3    24  1.0400 -  1.0200    0.99     3117   180  0.1328 0.1508        
REMARK   3    25  1.0200 -  1.0100    0.98     3070   174  0.1304 0.1511        
REMARK   3    26  1.0100 -  1.0000    0.98     3142   156  0.1397 0.1612        
REMARK   3    27  1.0000 -  0.9800    0.96     3013   172  0.1591 0.1768        
REMARK   3    28  0.9800 -  0.9700    0.95     3010   177  0.1900 0.2150        
REMARK   3    29  0.9700 -  0.9600    0.90     2843   167  0.2212 0.2208        
REMARK   3    30  0.9600 -  0.9500    0.82     2606   125  0.2462 0.2573        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.065            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 10.680           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 7.42                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           1497                                  
REMARK   3   ANGLE     :  1.133           2041                                  
REMARK   3   CHIRALITY :  0.079            237                                  
REMARK   3   PLANARITY :  0.008            269                                  
REMARK   3   DIHEDRAL  : 13.525            548                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6WEY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000248067.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAR-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : SI-111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DIALS                              
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 99442                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.320                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 0.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2FAV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MORPHEUS SCREEN D9 (0.12M ALCOHOLS,      
REMARK 280  0.1M BUFFER SYSTEM 3, PH 8.5, 30% PPT MIX 1 [40% PEG 500 MME/20%    
REMARK 280  PEG 20K]), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       21.66100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       33.78350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.21200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       33.78350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.66100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       27.21200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   406     O    HOH A   606              1.86            
REMARK 500   O    HOH A   481     O    HOH A   624              1.95            
REMARK 500   O    HOH A   528     O    HOH A   608              2.01            
REMARK 500   O    HOH A   504     O    HOH A   709              2.01            
REMARK 500   O    HOH A   453     O    HOH A   515              2.05            
REMARK 500   O    HOH A   444     O    HOH A   619              2.07            
REMARK 500   O    HOH A   757     O    HOH A   758              2.09            
REMARK 500   O    HOH A   698     O    HOH A   750              2.10            
REMARK 500   O    HOH A   635     O    HOH A   649              2.10            
REMARK 500   O    HOH A   402     O    HOH A   642              2.10            
REMARK 500   O    HOH A   714     O    HOH A   750              2.11            
REMARK 500   O    HOH A   621     O    HOH A   757              2.12            
REMARK 500   O    HOH A   577     O    HOH A   584              2.15            
REMARK 500   O    HOH A   403     O    HOH A   579              2.17            
REMARK 500   O    HOH A   693     O    HOH A   760              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   H    GLY A   252    HD22  ASN A   354     3554     1.33            
REMARK 500   O    HOH A   612     O    HOH A   667     3554     1.89            
REMARK 500   O    HOH A   418     O    HOH A   528     3554     1.97            
REMARK 500   O    HOH A   404     O    HOH A   754     3554     2.01            
REMARK 500   O    HOH A   600     O    HOH A   714     4555     2.01            
REMARK 500   O    HOH A   434     O    HOH A   720     4555     2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A 290     -133.04     56.18                                   
REMARK 500    ALA A 333     -147.18    -95.26                                   
REMARK 500    THR A 353     -139.78   -100.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 759        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A 760        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH A 761        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH A 762        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH A 763        DISTANCE =  6.76 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6VXS   RELATED DB: PDB                                   
REMARK 900 LOWER RESOLUTION STRUCTURE OF A SIMILAR PROTEIN CONSTRUCT.           
DBREF  6WEY A  207   377  UNP    P0DTD1   R1AB_SARS2    1025   1195             
SEQADV 6WEY GLY A  206  UNP  P0DTD1              EXPRESSION TAG                 
SEQRES   1 A  172  GLY VAL ASN SER PHE SER GLY TYR LEU LYS LEU THR ASP          
SEQRES   2 A  172  ASN VAL TYR ILE LYS ASN ALA ASP ILE VAL GLU GLU ALA          
SEQRES   3 A  172  LYS LYS VAL LYS PRO THR VAL VAL VAL ASN ALA ALA ASN          
SEQRES   4 A  172  VAL TYR LEU LYS HIS GLY GLY GLY VAL ALA GLY ALA LEU          
SEQRES   5 A  172  ASN LYS ALA THR ASN ASN ALA MET GLN VAL GLU SER ASP          
SEQRES   6 A  172  ASP TYR ILE ALA THR ASN GLY PRO LEU LYS VAL GLY GLY          
SEQRES   7 A  172  SER CYS VAL LEU SER GLY HIS ASN LEU ALA LYS HIS CYS          
SEQRES   8 A  172  LEU HIS VAL VAL GLY PRO ASN VAL ASN LYS GLY GLU ASP          
SEQRES   9 A  172  ILE GLN LEU LEU LYS SER ALA TYR GLU ASN PHE ASN GLN          
SEQRES  10 A  172  HIS GLU VAL LEU LEU ALA PRO LEU LEU SER ALA GLY ILE          
SEQRES  11 A  172  PHE GLY ALA ASP PRO ILE HIS SER LEU ARG VAL CYS VAL          
SEQRES  12 A  172  ASP THR VAL ARG THR ASN VAL TYR LEU ALA VAL PHE ASP          
SEQRES  13 A  172  LYS ASN LEU TYR ASP LYS LEU VAL SER SER PHE LEU GLU          
SEQRES  14 A  172  MET LYS SER                                                  
FORMUL   2  HOH   *363(H2 O)                                                    
HELIX    1 AA1 ASP A  226  LYS A  235  1                                  10    
HELIX    2 AA2 GLY A  251  THR A  261  1                                  11    
HELIX    3 AA3 ASN A  263  GLY A  277  1                                  15    
HELIX    4 AA4 ASN A  303  GLY A  307  5                                   5    
HELIX    5 AA5 ASP A  309  GLN A  311  5                                   3    
HELIX    6 AA6 LEU A  312  ASN A  319  1                                   8    
HELIX    7 AA7 PHE A  320  HIS A  323  5                                   4    
HELIX    8 AA8 ASP A  339  VAL A  351  1                                  13    
HELIX    9 AA9 ASP A  361  GLU A  374  1                                  14    
SHEET    1 AA1 4 LEU A 214  LYS A 215  0                                        
SHEET    2 AA1 4 VAL A 220  ASN A 224 -1  O  ILE A 222   N  LEU A 214           
SHEET    3 AA1 4 ASN A 354  VAL A 359  1  O  LEU A 357   N  TYR A 221           
SHEET    4 AA1 4 VAL A 325  ALA A 328  1  N  LEU A 326   O  TYR A 356           
SHEET    1 AA2 3 VAL A 238  ALA A 242  0                                        
SHEET    2 AA2 3 HIS A 295  VAL A 299  1  O  VAL A 299   N  ASN A 241           
SHEET    3 AA2 3 SER A 284  SER A 288 -1  N  LEU A 287   O  CYS A 296           
CRYST1   43.322   54.424   67.567  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.023083  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018374  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014800        0.00000                         
ATOM      1  N   GLY A 206       3.537  -6.891 -31.593  1.00  9.51           N  
ANISOU    1  N   GLY A 206     1225   1499    890     12    322     55       N  
ATOM      2  CA  GLY A 206       2.394  -7.456 -30.910  1.00  8.76           C  
ANISOU    2  CA  GLY A 206     1186   1316    827    -31    257   -112       C  
ATOM      3  C   GLY A 206       1.948  -6.610 -29.727  1.00  7.60           C  
ANISOU    3  C   GLY A 206      879   1105    904      9    187   -101       C  
ATOM      4  O   GLY A 206       2.435  -5.504 -29.521  1.00  9.19           O  
ANISOU    4  O   GLY A 206     1120   1164   1209   -123    260   -173       O  
ATOM      5  HA2 GLY A 206       1.652  -7.528 -31.531  1.00 10.52           H  
ATOM      6  HA3 GLY A 206       2.620  -8.341 -30.584  1.00 10.52           H  
ATOM      7  N   VAL A 207       1.022  -7.142 -28.956  1.00  7.73           N  
ANISOU    7  N   VAL A 207     1075   1077    785    -85    235   -112       N  
ATOM      8  CA  VAL A 207       0.477  -6.399 -27.833  1.00  7.37           C  
ANISOU    8  CA  VAL A 207      788   1163    847    -33    156    -93       C  
ATOM      9  C   VAL A 207       1.481  -6.386 -26.678  1.00  6.58           C  
ANISOU    9  C   VAL A 207      705   1012    784     59    216    -49       C  
ATOM     10  O   VAL A 207       2.371  -7.239 -26.531  1.00  7.05           O  
ANISOU   10  O   VAL A 207      864   1002    812    -56    288   -142       O  
ATOM     11  CB  VAL A 207      -0.901  -6.934 -27.393  1.00  8.82           C  
ANISOU   11  CB  VAL A 207      848   1363   1141   -107     84    -59       C  
ATOM     12  CG1 VAL A 207      -1.915  -6.834 -28.536  1.00 10.00           C  
ANISOU   12  CG1 VAL A 207      968   1473   1360   -102     37    -83       C  
ATOM     13  CG2 VAL A 207      -0.796  -8.335 -26.829  1.00  9.80           C  
ANISOU   13  CG2 VAL A 207     1035   1403   1285   -215     -8     24       C  
ATOM     14  H   VAL A 207       0.690  -7.929 -29.059  1.00  9.28           H  
ATOM     15  HA  VAL A 207       0.343  -5.481 -28.116  1.00  8.85           H  
ATOM     16  HB  VAL A 207      -1.235  -6.377 -26.673  1.00 10.59           H  
ATOM     17 HG11 VAL A 207      -2.769  -7.178 -28.231  1.00 12.01           H  
ATOM     18 HG12 VAL A 207      -2.006  -5.904 -28.796  1.00 12.01           H  
ATOM     19 HG13 VAL A 207      -1.596  -7.358 -29.287  1.00 12.01           H  
ATOM     20 HG21 VAL A 207      -1.689  -8.688 -26.693  1.00 11.77           H  
ATOM     21 HG22 VAL A 207      -0.311  -8.893 -27.457  1.00 11.77           H  
ATOM     22 HG23 VAL A 207      -0.322  -8.300 -25.984  1.00 11.77           H  
ATOM     23  N   ASN A 208       1.307  -5.406 -25.812  1.00  6.48           N  
ANISOU   23  N   ASN A 208      771    968    725     90     33    -28       N  
ATOM     24  CA  ASN A 208       2.133  -5.247 -24.618  1.00  6.49           C  
ANISOU   24  CA  ASN A 208      807    888    769    164     28    -61       C  
ATOM     25  C   ASN A 208       3.628  -5.167 -24.952  1.00  6.54           C  
ANISOU   25  C   ASN A 208      831    897    755     57    -20    -83       C  
ATOM     26  O   ASN A 208       4.467  -5.756 -24.270  1.00  6.85           O  
ANISOU   26  O   ASN A 208      736   1016    852    174     32    -13       O  
ATOM     27  CB  ASN A 208       1.885  -6.337 -23.583  1.00  7.08           C  
ANISOU   27  CB  ASN A 208      903    998    791    196     75     15       C  
ATOM     28  CG  ASN A 208       0.546  -6.241 -22.938  1.00  7.87           C  
ANISOU   28  CG  ASN A 208      880   1228    882    115    105    -10       C  
ATOM     29  OD1 ASN A 208      -0.050  -5.165 -22.841  1.00  7.86           O  
ANISOU   29  OD1 ASN A 208      816   1338    833    218    126    -53       O  
ATOM     30  ND2 ASN A 208       0.087  -7.350 -22.406  1.00 10.08           N  
ANISOU   30  ND2 ASN A 208     1260   1331   1240   -136    269     27       N  
ATOM     31  H   ASN A 208       0.702  -4.800 -25.891  1.00  7.79           H  
ATOM     32  HA  ASN A 208       1.871  -4.400 -24.224  1.00  7.79           H  
ATOM     33  HB2 ASN A 208       1.946  -7.202 -24.017  1.00  8.51           H  
ATOM     34  HB3 ASN A 208       2.557  -6.267 -22.887  1.00  8.51           H  
ATOM     35 HD21 ASN A 208      -0.681  -7.356 -22.020  1.00 12.11           H  
ATOM     36 HD22 ASN A 208       0.554  -8.071 -22.444  1.00 12.11           H  
ATOM     37  N   SER A 209       3.954  -4.366 -25.960  1.00  6.69           N  
ANISOU   37  N   SER A 209      826    911    805    109      1    -51       N  
ATOM     38  CA  SER A 209       5.336  -4.201 -26.375  1.00  7.23           C  
ANISOU   38  CA  SER A 209      866    976    905    -12     91   -106       C  
ATOM     39  C   SER A 209       6.000  -3.103 -25.538  1.00  7.48           C  
ANISOU   39  C   SER A 209      809   1004   1030     31     98    -93       C  
ATOM     40  O   SER A 209       6.294  -2.007 -25.991  1.00  9.51           O  
ANISOU   40  O   SER A 209     1262   1189   1164   -159     67    -18       O  
ATOM     41  CB  SER A 209       5.365  -3.915 -27.856  1.00  8.24           C  
ANISOU   41  CB  SER A 209     1012   1218    899    -92    158    -60       C  
ATOM     42  OG  SER A 209       6.646  -4.071 -28.305  1.00  9.72           O  
ANISOU   42  OG  SER A 209     1152   1424   1116    -22    256    -76       O  
ATOM     43  H   SER A 209       3.389  -3.907 -26.419  1.00  8.03           H  
ATOM     44  HA  SER A 209       5.838  -5.014 -26.208  1.00  8.69           H  
ATOM     45  HB2 SER A 209       4.781  -4.536 -28.318  1.00  9.89           H  
ATOM     46  HB3 SER A 209       5.073  -3.004 -28.016  1.00  9.89           H  
ATOM     47  HG  SER A 209       6.680  -3.926 -29.132  1.00 11.67           H  
ATOM     48  N   PHE A 210       6.192  -3.411 -24.270  1.00  7.15           N  
ANISOU   48  N   PHE A 210      730   1059    925     63     24   -173       N  
ATOM     49  CA  PHE A 210       6.824  -2.511 -23.311  1.00  8.00           C  
ANISOU   49  CA  PHE A 210      687   1334   1017    167   -102   -328       C  
ATOM     50  C   PHE A 210       8.331  -2.712 -23.347  1.00  9.58           C  
ANISOU   50  C   PHE A 210      786   1588   1265    141    -71   -497       C  
ATOM     51  O   PHE A 210       8.824  -3.842 -23.217  1.00 11.11           O  
ANISOU   51  O   PHE A 210      833   1740   1647    367   -171   -513       O  
ATOM     52  CB  PHE A 210       6.340  -2.814 -21.894  1.00  8.52           C  
ANISOU   52  CB  PHE A 210      809   1468    958    338    -97   -313       C  
ATOM     53  CG  PHE A 210       4.906  -2.502 -21.642  1.00  7.51           C  
ANISOU   53  CG  PHE A 210      732   1291    832    227    -71   -192       C  
ATOM     54  CD1 PHE A 210       4.507  -1.215 -21.289  1.00  7.20           C  
ANISOU   54  CD1 PHE A 210      712   1129    896     51   -106   -164       C  
ATOM     55  CD2 PHE A 210       3.932  -3.486 -21.718  1.00  7.35           C  
ANISOU   55  CD2 PHE A 210      859   1093    841    158     38    -88       C  
ATOM     56  CE1 PHE A 210       3.177  -0.928 -21.012  1.00  6.85           C  
ANISOU   56  CE1 PHE A 210      666   1096    839     81   -119   -176       C  
ATOM     57  CE2 PHE A 210       2.600  -3.211 -21.453  1.00  7.24           C  
ANISOU   57  CE2 PHE A 210      898   1046    807     60     61    -44       C  
ATOM     58  CZ  PHE A 210       2.227  -1.919 -21.087  1.00  6.75           C  
ANISOU   58  CZ  PHE A 210      761   1053    751    122    -49   -107       C  
ATOM     59  H   PHE A 210       5.957  -4.162 -23.922  1.00  8.58           H  
ATOM     60  HA  PHE A 210       6.604  -1.596 -23.543  1.00  9.61           H  
ATOM     61  HB2 PHE A 210       6.467  -3.760 -21.722  1.00 10.23           H  
ATOM     62  HB3 PHE A 210       6.866  -2.289 -21.271  1.00 10.23           H  
ATOM     63  HD1 PHE A 210       5.142  -0.537 -21.238  1.00  8.65           H  
ATOM     64  HD2 PHE A 210       4.179  -4.351 -21.953  1.00  8.83           H  
ATOM     65  HE1 PHE A 210       2.928  -0.063 -20.775  1.00  8.23           H  
ATOM     66  HE2 PHE A 210       1.960  -3.883 -21.518  1.00  8.70           H  
ATOM     67  HZ  PHE A 210       1.338  -1.728 -20.893  1.00  8.11           H  
ATOM     68  N   SER A 211       9.064  -1.612 -23.494  1.00 10.05           N  
ANISOU   68  N   SER A 211      693   1863   1262     64    126   -444       N  
ATOM     69  CA  SER A 211      10.519  -1.649 -23.460  1.00 11.33           C  
ANISOU   69  CA  SER A 211      652   2209   1446     28    192   -369       C  
ATOM     70  C   SER A 211      11.018  -0.255 -23.096  1.00 11.15           C  
ANISOU   70  C   SER A 211      602   2160   1476   -173    188    -92       C  
ATOM     71  O   SER A 211      10.308   0.733 -23.268  1.00 11.95           O  
ANISOU   71  O   SER A 211      761   2188   1591   -210    163    176       O  
ATOM     72  CB  SER A 211      11.077  -2.134 -24.796  1.00 14.24           C  
ANISOU   72  CB  SER A 211     1116   2719   1577    304    425   -317       C  
ATOM     73  OG  SER A 211      10.558  -1.370 -25.860  1.00 16.99           O  
ANISOU   73  OG  SER A 211     1536   3245   1673    346    512    -68       O  
ATOM     74  H   SER A 211       8.738  -0.825 -23.615  1.00 12.07           H  
ATOM     75  HA  SER A 211      10.835  -2.257 -22.773  1.00 13.61           H  
ATOM     76  HB2 SER A 211      12.043  -2.047 -24.786  1.00 17.10           H  
ATOM     77  HB3 SER A 211      10.829  -3.063 -24.923  1.00 17.10           H  
ATOM     78  HG  SER A 211       9.756  -1.580 -26.000  1.00 20.39           H  
ATOM     79  N   GLY A 212      12.245  -0.179 -22.596  1.00 11.26           N  
ANISOU   79  N   GLY A 212      677   2068   1534   -113    182    -22       N  
ATOM     80  CA  GLY A 212      12.821   1.110 -22.246  1.00 10.87           C  
ANISOU   80  CA  GLY A 212      692   1931   1509   -246    176     73       C  
ATOM     81  C   GLY A 212      12.471   1.626 -20.866  1.00  9.68           C  
ANISOU   81  C   GLY A 212      592   1503   1584   -171     92    161       C  
ATOM     82  O   GLY A 212      12.748   2.791 -20.574  1.00 10.50           O  
ANISOU   82  O   GLY A 212      860   1503   1628   -301    141    210       O  
ATOM     83  H   GLY A 212      12.759  -0.853 -22.453  1.00 13.53           H  
ATOM     84  HA2 GLY A 212      13.787   1.039 -22.295  1.00 13.06           H  
ATOM     85  HA3 GLY A 212      12.519   1.768 -22.891  1.00 13.06           H  
ATOM     86  N   TYR A 213      11.855   0.808 -20.019  1.00  8.45           N  
ANISOU   86  N   TYR A 213      483   1186   1542   -140     61    162       N  
ATOM     87  CA  TYR A 213      11.456   1.195 -18.675  1.00  7.75           C  
ANISOU   87  CA  TYR A 213      406   1066   1472    -87     64    106       C  
ATOM     88  C   TYR A 213      12.573   0.932 -17.666  1.00  7.79           C  
ANISOU   88  C   TYR A 213      411    974   1574    -67     -1     94       C  
ATOM     89  O   TYR A 213      13.494   0.136 -17.895  1.00  8.87           O  
ANISOU   89  O   TYR A 213      514   1078   1778     33   -120    -22       O  
ATOM     90  CB  TYR A 213      10.203   0.412 -18.224  1.00  7.39           C  
ANISOU   90  CB  TYR A 213      370   1118   1321   -115    -52    145       C  
ATOM     91  CG  TYR A 213       8.953   0.862 -18.921  1.00  6.96           C  
ANISOU   91  CG  TYR A 213      458    946   1241   -111     13    121       C  
ATOM     92  CD1 TYR A 213       8.680   0.497 -20.237  1.00  7.48           C  
ANISOU   92  CD1 TYR A 213      462   1161   1219    -63     31     18       C  
ATOM     93  CD2 TYR A 213       8.024   1.652 -18.268  1.00  6.90           C  
ANISOU   93  CD2 TYR A 213      464    864   1295   -150    -24    -14       C  
ATOM     94  CE1 TYR A 213       7.547   0.943 -20.892  1.00  7.57           C  
ANISOU   94  CE1 TYR A 213      451   1302   1125    -15     89    125       C  
ATOM     95  CE2 TYR A 213       6.871   2.102 -18.919  1.00  7.04           C  
ANISOU   95  CE2 TYR A 213      512    864   1299    -96     15     21       C  
ATOM     96  CZ  TYR A 213       6.642   1.772 -20.230  1.00  7.48           C  
ANISOU   96  CZ  TYR A 213      466   1158   1220    -91    -35    163       C  
ATOM     97  OH  TYR A 213       5.526   2.226 -20.857  1.00  8.09           O  
ANISOU   97  OH  TYR A 213      541   1280   1254    -10   -124    182       O  
ATOM     98  H   TYR A 213      11.650  -0.006 -20.209  1.00 10.15           H  
ATOM     99  HA  TYR A 213      11.256   2.144 -18.684  1.00  9.31           H  
ATOM    100  HB2 TYR A 213      10.332  -0.529 -18.419  1.00  8.88           H  
ATOM    101  HB3 TYR A 213      10.077   0.540 -17.271  1.00  8.88           H  
ATOM    102  HD1 TYR A 213       9.274  -0.061 -20.685  1.00  8.98           H  
ATOM    103  HD2 TYR A 213       8.169   1.889 -17.380  1.00  8.29           H  
ATOM    104  HE1 TYR A 213       7.389   0.690 -21.773  1.00  9.10           H  
ATOM    105  HE2 TYR A 213       6.256   2.627 -18.461  1.00  8.46           H  
ATOM    106  HH  TYR A 213       5.507   1.947 -21.649  1.00  9.72           H  
ATOM    107  N   LEU A 214      12.456   1.601 -16.528  1.00  7.54           N  
ANISOU  107  N   LEU A 214      407    959   1499     -3   -114     89       N  
ATOM    108  CA  LEU A 214      13.220   1.294 -15.331  1.00  7.78           C  
ANISOU  108  CA  LEU A 214      416   1034   1508    -10   -182     64       C  
ATOM    109  C   LEU A 214      12.365   0.424 -14.413  1.00  7.74           C  
ANISOU  109  C   LEU A 214      448    985   1506    -56   -240     88       C  
ATOM    110  O   LEU A 214      11.246   0.802 -14.067  1.00  7.52           O  
ANISOU  110  O   LEU A 214      395    989   1472     -5   -130    129       O  
ATOM    111  CB  LEU A 214      13.597   2.579 -14.591  1.00  8.86           C  
ANISOU  111  CB  LEU A 214      588   1120   1658    -90   -180     60       C  
ATOM    112  CG  LEU A 214      14.204   2.379 -13.200  1.00  9.23           C  
ANISOU  112  CG  LEU A 214      625   1174   1708   -215   -159     42       C  
ATOM    113  CD1 LEU A 214      15.488   1.557 -13.266  1.00  9.47           C  
ANISOU  113  CD1 LEU A 214      511   1369   1717    -70   -251     75       C  
ATOM    114  CD2 LEU A 214      14.437   3.729 -12.539  1.00 11.29           C  
ANISOU  114  CD2 LEU A 214     1086   1345   1859   -232   -266   -154       C  
ATOM    115  H   LEU A 214      11.918   2.263 -16.422  1.00  9.05           H  
ATOM    116  HA  LEU A 214      14.030   0.817 -15.572  1.00  9.35           H  
ATOM    117  HB2 LEU A 214      14.249   3.059 -15.125  1.00 10.64           H  
ATOM    118  HB3 LEU A 214      12.796   3.115 -14.483  1.00 10.64           H  
ATOM    119  HG  LEU A 214      13.583   1.875 -12.651  1.00 11.08           H  
ATOM    120 HD11 LEU A 214      15.915   1.568 -12.395  1.00 11.37           H  
ATOM    121 HD12 LEU A 214      15.268   0.646 -13.515  1.00 11.37           H  
ATOM    122 HD13 LEU A 214      16.079   1.947 -13.929  1.00 11.37           H  
ATOM    123 HD21 LEU A 214      14.826   3.588 -11.662  1.00 13.56           H  
ATOM    124 HD22 LEU A 214      15.041   4.250 -13.090  1.00 13.56           H  
ATOM    125 HD23 LEU A 214      13.587   4.189 -12.454  1.00 13.56           H  
ATOM    126  N   LYS A 215      12.903  -0.730 -14.016  1.00  7.76           N  
ANISOU  126  N   LYS A 215      521    919   1510     30   -170     92       N  
ATOM    127  CA  LYS A 215      12.262  -1.574 -13.027  1.00  8.19           C  
ANISOU  127  CA  LYS A 215      636    959   1516     32   -274     52       C  
ATOM    128  C   LYS A 215      12.522  -1.006 -11.641  1.00  8.28           C  
ANISOU  128  C   LYS A 215      589   1048   1508    -47   -387     16       C  
ATOM    129  O   LYS A 215      13.665  -0.950 -11.184  1.00 10.01           O  
ANISOU  129  O   LYS A 215      608   1621   1573     28   -441      5       O  
ATOM    130  CB  LYS A 215      12.816  -2.987 -13.133  1.00  9.70           C  
ANISOU  130  CB  LYS A 215      989    947   1747    107   -212     70       C  
ATOM    131  CG  LYS A 215      12.155  -3.958 -12.160  1.00 12.01           C  
ANISOU  131  CG  LYS A 215     1639    946   1979     70      0    246       C  
ATOM    132  CD  LYS A 215      12.899  -5.259 -11.984  1.00 18.03           C  
ANISOU  132  CD  LYS A 215     2949   1333   2570    102    329    434       C  
ATOM    133  CE  LYS A 215      13.041  -6.024 -13.254  1.00 23.42           C  
ANISOU  133  CE  LYS A 215     3855   1994   3048    -47    194    406       C  
ATOM    134  NZ  LYS A 215      13.765  -7.302 -13.007  1.00 24.90           N  
ANISOU  134  NZ  LYS A 215     4218   1949   3292     62    189    277       N  
ATOM    135  H   LYS A 215      13.647  -1.044 -14.312  1.00  9.33           H  
ATOM    136  HA  LYS A 215      11.304  -1.598 -13.177  1.00  9.83           H  
ATOM    137  HB2 LYS A 215      12.667  -3.316 -14.033  1.00 11.64           H  
ATOM    138  HB3 LYS A 215      13.766  -2.968 -12.939  1.00 11.64           H  
ATOM    139  HG2 LYS A 215      12.094  -3.534 -11.290  1.00 14.42           H  
ATOM    140  HG3 LYS A 215      11.267  -4.171 -12.488  1.00 14.42           H  
ATOM    141  HD2 LYS A 215      13.789  -5.071 -11.647  1.00 21.65           H  
ATOM    142  HD3 LYS A 215      12.416  -5.816 -11.352  1.00 21.65           H  
ATOM    143  HE2 LYS A 215      12.163  -6.229 -13.612  1.00 28.11           H  
ATOM    144  HE3 LYS A 215      13.547  -5.500 -13.895  1.00 28.11           H  
ATOM    145  HZ1 LYS A 215      14.574  -7.135 -12.676  1.00 29.88           H  
ATOM    146  HZ2 LYS A 215      13.313  -7.802 -12.426  1.00 29.88           H  
ATOM    147  HZ3 LYS A 215      13.854  -7.754 -13.769  1.00 29.88           H  
ATOM    148  N   LEU A 216      11.462  -0.603 -10.962  1.00  7.76           N  
ANISOU  148  N   LEU A 216      572    959   1419    -18   -418     82       N  
ATOM    149  CA  LEU A 216      11.556  -0.175  -9.576  1.00  7.96           C  
ANISOU  149  CA  LEU A 216      636   1018   1369    -47   -466     26       C  
ATOM    150  C   LEU A 216      11.445  -1.351  -8.621  1.00  8.84           C  
ANISOU  150  C   LEU A 216      786   1102   1470    -67   -569    138       C  
ATOM    151  O   LEU A 216      12.207  -1.444  -7.658  1.00 10.49           O  
ANISOU  151  O   LEU A 216      993   1343   1650   -151   -693    295       O  
ATOM    152  CB  LEU A 216      10.487   0.861  -9.239  1.00  8.55           C  
ANISOU  152  CB  LEU A 216      814   1137   1299    -25   -338      4       C  
ATOM    153  CG  LEU A 216      10.559   2.178 -10.017  1.00  8.84           C  
ANISOU  153  CG  LEU A 216      927   1111   1320     51   -359    -15       C  
ATOM    154  CD1 LEU A 216       9.437   3.083  -9.585  1.00  9.79           C  
ANISOU  154  CD1 LEU A 216     1137   1153   1430    114   -228    -16       C  
ATOM    155  CD2 LEU A 216      11.903   2.875  -9.833  1.00  9.74           C  
ANISOU  155  CD2 LEU A 216     1119   1178   1402    -85   -389     75       C  
ATOM    156  H   LEU A 216      10.666  -0.568 -11.284  1.00  9.33           H  
ATOM    157  HA  LEU A 216      12.415   0.256  -9.449  1.00  9.56           H  
ATOM    158  HB2 LEU A 216       9.618   0.469  -9.419  1.00 10.27           H  
ATOM    159  HB3 LEU A 216      10.564   1.080  -8.297  1.00 10.27           H  
ATOM    160  HG  LEU A 216      10.468   1.982 -10.963  1.00 10.62           H  
ATOM    161 HD11 LEU A 216       9.504   3.921 -10.068  1.00 11.76           H  
ATOM    162 HD12 LEU A 216       8.590   2.653  -9.783  1.00 11.76           H  
ATOM    163 HD13 LEU A 216       9.511   3.244  -8.631  1.00 11.76           H  
ATOM    164 HD21 LEU A 216      11.864   3.750 -10.249  1.00 11.69           H  
ATOM    165 HD22 LEU A 216      12.083   2.967  -8.885  1.00 11.69           H  
ATOM    166 HD23 LEU A 216      12.596   2.341 -10.251  1.00 11.69           H  
ATOM    167  N   THR A 217      10.485  -2.234  -8.887  1.00  9.25           N  
ANISOU  167  N   THR A 217      836   1202   1477    -88   -467    172       N  
ATOM    168  CA  THR A 217      10.329  -3.527  -8.242  1.00 10.04           C  
ANISOU  168  CA  THR A 217      984   1346   1485    -91   -508    268       C  
ATOM    169  C   THR A 217       9.916  -4.528  -9.340  1.00 10.15           C  
ANISOU  169  C   THR A 217     1093   1171   1591   -155   -318     69       C  
ATOM    170  O   THR A 217       9.639  -4.157 -10.476  1.00 11.57           O  
ANISOU  170  O   THR A 217     1292   1431   1672   -290   -294   -138       O  
ATOM    171  CB  THR A 217       9.254  -3.464  -7.150  1.00 11.11           C  
ANISOU  171  CB  THR A 217     1103   1789   1329   -220   -576    344       C  
ATOM    172  OG1 THR A 217       7.973  -3.317  -7.777  1.00 10.86           O  
ANISOU  172  OG1 THR A 217      923   1875   1327   -282   -488    529       O  
ATOM    173  CG2 THR A 217       9.468  -2.312  -6.196  1.00 12.77           C  
ANISOU  173  CG2 THR A 217     1294   2165   1391   -195   -447    196       C  
ATOM    174  H   THR A 217       9.874  -2.094  -9.476  1.00 11.11           H  
ATOM    175  HA  THR A 217      11.160  -3.814  -7.833  1.00 12.06           H  
ATOM    176  HB  THR A 217       9.295  -4.279  -6.626  1.00 13.34           H  
ATOM    177  HG1 THR A 217       7.372  -3.259  -7.193  1.00 13.04           H  
ATOM    178 HG21 THR A 217       8.827  -2.360  -5.469  1.00 15.33           H  
ATOM    179 HG22 THR A 217      10.364  -2.347  -5.829  1.00 15.33           H  
ATOM    180 HG23 THR A 217       9.351  -1.469  -6.663  1.00 15.33           H  
ATOM    181  N   ASP A 218       9.817  -5.817  -9.001  1.00 11.02           N  
ANISOU  181  N   ASP A 218     1393   1292   1500   -202   -319     55       N  
ATOM    182  CA  ASP A 218       9.384  -6.780 -10.007  1.00 12.16           C  
ANISOU  182  CA  ASP A 218     2007   1341   1271   -446   -394    -11       C  
ATOM    183  C   ASP A 218       8.030  -6.411 -10.603  1.00 12.45           C  
ANISOU  183  C   ASP A 218     1934   1508   1289   -773   -770    375       C  
ATOM    184  O   ASP A 218       7.716  -6.850 -11.727  1.00 16.03           O  
ANISOU  184  O   ASP A 218     2855   1814   1423  -1024   -899    416       O  
ATOM    185  CB  ASP A 218       9.331  -8.196  -9.418  1.00 12.50           C  
ANISOU  185  CB  ASP A 218     2176   1276   1297   -254   -345   -106       C  
ATOM    186  CG  ASP A 218       9.132  -9.257 -10.484  1.00 13.04           C  
ANISOU  186  CG  ASP A 218     2217   1346   1391   -222   -327    -29       C  
ATOM    187  OD1 ASP A 218       9.987  -9.368 -11.389  1.00 15.05           O  
ANISOU  187  OD1 ASP A 218     2521   1822   1375   -300   -220   -273       O  
ATOM    188  OD2 ASP A 218       8.109  -9.988 -10.440  1.00 12.67           O  
ANISOU  188  OD2 ASP A 218     2104   1165   1545    -85   -557      2       O  
ATOM    189  H   ASP A 218       9.988  -6.145  -8.224  1.00 13.23           H  
ATOM    190  HA  ASP A 218      10.038  -6.786 -10.723  1.00 14.60           H  
ATOM    191  HB2 ASP A 218      10.166  -8.382  -8.960  1.00 15.00           H  
ATOM    192  HB3 ASP A 218       8.590  -8.254  -8.794  1.00 15.00           H  
ATOM    193  N  AASN A 219       7.192  -5.680  -9.800  0.61 10.50           N  
ATOM    194  N  BASN A 219       7.215  -5.618  -9.957  0.39 10.44           N  
ATOM    195  CA AASN A 219       5.827  -5.314 -10.162  0.61 10.29           C  
ATOM    196  CA BASN A 219       5.944  -5.395 -10.613  0.39 10.69           C  
ATOM    197  C  AASN A 219       5.739  -4.015 -10.909  0.61  8.14           C  
ATOM    198  C  BASN A 219       5.623  -3.913 -10.792  0.39  8.85           C  
ATOM    199  O  AASN A 219       4.847  -3.898 -11.746  0.61  7.41           O  
ATOM    200  O  BASN A 219       4.499  -3.564 -11.222  0.39  5.62           O  
ATOM    201  CB AASN A 219       4.912  -5.157  -8.961  0.61 10.45           C  
ATOM    202  CB BASN A 219       4.876  -6.161  -9.874  0.39 10.22           C  
ATOM    203  CG AASN A 219       4.930  -6.335  -8.067  0.61 10.67           C  
ATOM    204  CG BASN A 219       4.538  -5.494  -8.640  0.39  6.75           C  
ATOM    205  OD1AASN A 219       5.458  -6.277  -6.943  0.61 11.21           O  
ATOM    206  OD1BASN A 219       5.296  -5.526  -7.665  0.39 22.53           O  
ATOM    207  ND2AASN A 219       4.346  -7.425  -8.531  0.61 10.83           N  
ATOM    208  ND2BASN A 219       3.389  -4.875  -8.620  0.39 11.26           N  
ATOM    209  H  AASN A 219       7.417  -5.387  -9.023  0.61 12.61           H  
ATOM    210  H  BASN A 219       7.358  -5.228  -9.203  0.39 12.53           H  
ATOM    211  HA AASN A 219       5.504  -6.051 -10.703  0.61 12.35           H  
ATOM    212  HA BASN A 219       5.953  -5.743 -11.518  0.39 12.83           H  
ATOM    213  HB2AASN A 219       5.196  -4.386  -8.445  0.61 12.55           H  
ATOM    214  HB2BASN A 219       4.078  -6.218 -10.423  0.39 12.27           H  
ATOM    215  HB3AASN A 219       4.001  -5.031  -9.271  0.61 12.55           H  
ATOM    216  HB3BASN A 219       5.200  -7.051  -9.665  0.39 12.27           H  
ATOM    217 HD21AASN A 219       4.327  -8.139  -8.053  0.61 13.00           H  
ATOM    218 HD21BASN A 219       2.885  -4.882  -9.316  0.39 13.52           H  
ATOM    219 HD22AASN A 219       3.984  -7.420  -9.311  0.61 13.00           H  
ATOM    220 HD22BASN A 219       3.136  -4.460  -7.910  0.39 13.52           H  
ATOM    221  N   VAL A 220       6.607  -3.038 -10.599  1.00  8.32           N  
ANISOU  221  N   VAL A 220      751   1271   1138   -398   -394    320       N  
ATOM    222  CA  VAL A 220       6.419  -1.647 -10.972  1.00  7.39           C  
ANISOU  222  CA  VAL A 220      617   1285    905   -219   -267    180       C  
ATOM    223  C   VAL A 220       7.592  -1.186 -11.808  1.00  6.54           C  
ANISOU  223  C   VAL A 220      529   1030    928   -104   -247     51       C  
ATOM    224  O   VAL A 220       8.752  -1.262 -11.381  1.00  7.10           O  
ANISOU  224  O   VAL A 220      533   1134   1032    -93   -279    133       O  
ATOM    225  CB  VAL A 220       6.216  -0.732  -9.752  1.00  8.92           C  
ANISOU  225  CB  VAL A 220      753   1726    910   -281   -229     69       C  
ATOM    226  CG1 VAL A 220       6.030   0.718 -10.202  1.00  8.91           C  
ANISOU  226  CG1 VAL A 220      900   1498    988    -50   -127   -107       C  
ATOM    227  CG2 VAL A 220       5.039  -1.200  -8.922  1.00 10.96           C  
ANISOU  227  CG2 VAL A 220      930   2277    956   -444   -180     40       C  
ATOM    228  H   VAL A 220       7.334  -3.169 -10.159  1.00  9.99           H  
ATOM    229  HA  VAL A 220       5.625  -1.586 -11.525  1.00  8.87           H  
ATOM    230  HB  VAL A 220       7.006  -0.772  -9.191  1.00 10.71           H  
ATOM    231 HG11 VAL A 220       5.735   1.248  -9.446  1.00 10.70           H  
ATOM    232 HG12 VAL A 220       6.877   1.057 -10.533  1.00 10.70           H  
ATOM    233 HG13 VAL A 220       5.364   0.747 -10.907  1.00 10.70           H  
ATOM    234 HG21 VAL A 220       4.870  -0.553  -8.220  1.00 13.16           H  
ATOM    235 HG22 VAL A 220       4.260  -1.279  -9.494  1.00 13.16           H  
ATOM    236 HG23 VAL A 220       5.251  -2.063  -8.532  1.00 13.16           H  
ATOM    237  N   TYR A 221       7.267  -0.654 -12.972  1.00  5.97           N  
ANISOU  237  N   TYR A 221      431    876    963    -14   -163     90       N  
ATOM    238  CA  TYR A 221       8.192  -0.139 -13.967  1.00  5.98           C  
ANISOU  238  CA  TYR A 221      356    929    987    -42   -127    114       C  
ATOM    239  C   TYR A 221       7.819   1.310 -14.238  1.00  6.07           C  
ANISOU  239  C   TYR A 221      360    877   1069    -37   -229     94       C  
ATOM    240  O   TYR A 221       6.644   1.672 -14.136  1.00  6.76           O  
ANISOU  240  O   TYR A 221      380    874   1315    -70   -158    152       O  
ATOM    241  CB  TYR A 221       8.071  -0.966 -15.262  1.00  6.27           C  
ANISOU  241  CB  TYR A 221      516    883    985      2   -106    120       C  
ATOM    242  CG  TYR A 221       8.371  -2.420 -15.024  1.00  6.58           C  
ANISOU  242  CG  TYR A 221      600    905    993     -3    -99     41       C  
ATOM    243  CD1 TYR A 221       7.393  -3.273 -14.515  1.00  7.10           C  
ANISOU  243  CD1 TYR A 221      738    954   1004   -165    -85     46       C  
ATOM    244  CD2 TYR A 221       9.631  -2.928 -15.248  1.00  7.38           C  
ANISOU  244  CD2 TYR A 221      716    931   1157    -17     10     42       C  
ATOM    245  CE1 TYR A 221       7.699  -4.584 -14.195  1.00  8.61           C  
ANISOU  245  CE1 TYR A 221     1018    935   1318   -160    -71    117       C  
ATOM    246  CE2 TYR A 221       9.939  -4.253 -14.947  1.00  8.97           C  
ANISOU  246  CE2 TYR A 221      979    985   1445    202    -82    -28       C  
ATOM    247  CZ  TYR A 221       8.978  -5.064 -14.414  1.00  9.92           C  
ANISOU  247  CZ  TYR A 221     1333    831   1605     15   -215     29       C  
ATOM    248  OH  TYR A 221       9.325  -6.366 -14.100  1.00 12.82           O  
ANISOU  248  OH  TYR A 221     1891    833   2148    118   -318     55       O  
ATOM    249  H   TYR A 221       6.451  -0.573 -13.230  1.00  7.18           H  
ATOM    250  HA  TYR A 221       9.112  -0.178 -13.662  1.00  7.18           H  
ATOM    251  HB2 TYR A 221       7.166  -0.893 -15.604  1.00  7.54           H  
ATOM    252  HB3 TYR A 221       8.701  -0.627 -15.918  1.00  7.54           H  
ATOM    253  HD1 TYR A 221       6.527  -2.958 -14.389  1.00  8.52           H  
ATOM    254  HD2 TYR A 221      10.288  -2.377 -15.608  1.00  8.87           H  
ATOM    255  HE1 TYR A 221       7.047  -5.140 -13.834  1.00 10.34           H  
ATOM    256  HE2 TYR A 221      10.793  -4.583 -15.109  1.00 10.78           H  
ATOM    257  HH  TYR A 221       8.668  -6.764 -13.760  1.00 15.39           H  
ATOM    258  N   ILE A 222       8.790   2.142 -14.626  1.00  6.06           N  
ANISOU  258  N   ILE A 222      335    851   1117    -11   -177     98       N  
ATOM    259  CA  ILE A 222       8.511   3.563 -14.820  1.00  6.07           C  
ANISOU  259  CA  ILE A 222      384    780   1141     -9   -146     22       C  
ATOM    260  C   ILE A 222       9.298   4.080 -16.024  1.00  6.26           C  
ANISOU  260  C   ILE A 222      360    839   1179    -63   -161      8       C  
ATOM    261  O   ILE A 222      10.431   3.673 -16.298  1.00  7.20           O  
ANISOU  261  O   ILE A 222      368    956   1414     33    -44    139       O  
ATOM    262  CB  ILE A 222       8.821   4.342 -13.518  1.00  7.26           C  
ANISOU  262  CB  ILE A 222      693    827   1239      1   -236     -1       C  
ATOM    263  CG1 ILE A 222       8.240   5.756 -13.569  1.00  8.79           C  
ANISOU  263  CG1 ILE A 222     1000    952   1386     50   -457    -42       C  
ATOM    264  CG2 ILE A 222      10.317   4.333 -13.205  1.00  8.08           C  
ANISOU  264  CG2 ILE A 222      783    945   1341    -29   -468     75       C  
ATOM    265  CD1 ILE A 222       8.279   6.436 -12.233  1.00 11.81           C  
ANISOU  265  CD1 ILE A 222     1755   1224   1509    321   -576   -301       C  
ATOM    266  H   ILE A 222       9.603   1.908 -14.780  1.00  7.28           H  
ATOM    267  HA  ILE A 222       7.578   3.703 -15.044  1.00  7.29           H  
ATOM    268  HB  ILE A 222       8.380   3.885 -12.784  1.00  8.72           H  
ATOM    269 HG12 ILE A 222       8.755   6.288 -14.194  1.00 10.55           H  
ATOM    270 HG13 ILE A 222       7.315   5.708 -13.857  1.00 10.55           H  
ATOM    271 HG21 ILE A 222      10.457   4.706 -12.320  1.00  9.70           H  
ATOM    272 HG22 ILE A 222      10.639   3.418 -13.233  1.00  9.70           H  
ATOM    273 HG23 ILE A 222      10.781   4.868 -13.867  1.00  9.70           H  
ATOM    274 HD11 ILE A 222       7.819   7.287 -12.299  1.00 14.18           H  
ATOM    275 HD12 ILE A 222       7.839   5.872 -11.578  1.00 14.18           H  
ATOM    276 HD13 ILE A 222       9.204   6.578 -11.978  1.00 14.18           H  
ATOM    277  N   LYS A 223       8.699   5.045 -16.720  1.00  6.26           N  
ANISOU  277  N   LYS A 223      377    898   1104     -6    -52    126       N  
ATOM    278  CA  LYS A 223       9.299   5.674 -17.880  1.00  6.15           C  
ANISOU  278  CA  LYS A 223      337    918   1079    -18     59     26       C  
ATOM    279  C   LYS A 223       8.828   7.116 -17.953  1.00  5.77           C  
ANISOU  279  C   LYS A 223      315    890    985    -44     -1     27       C  
ATOM    280  O   LYS A 223       7.692   7.430 -17.593  1.00  6.08           O  
ANISOU  280  O   LYS A 223      346    907   1058    -22     40     92       O  
ATOM    281  CB  LYS A 223       8.888   4.941 -19.165  1.00  7.34           C  
ANISOU  281  CB  LYS A 223      628    943   1218    -44    168     12       C  
ATOM    282  CG  LYS A 223       9.534   5.468 -20.434  1.00  9.49           C  
ANISOU  282  CG  LYS A 223     1012   1249   1347   -156    232   -222       C  
ATOM    283  CD  LYS A 223       8.950   4.819 -21.683  1.00 11.77           C  
ANISOU  283  CD  LYS A 223     1090   1812   1571     50    332    -76       C  
ATOM    284  CE  LYS A 223       9.561   3.513 -21.964  1.00 12.79           C  
ANISOU  284  CE  LYS A 223     1362   1778   1721   -112     81   -178       C  
ATOM    285  NZ  LYS A 223       9.099   3.085 -23.291  1.00 12.49           N  
ANISOU  285  NZ  LYS A 223     1246   1825   1675   -214    188   -606       N  
ATOM    286  H   LYS A 223       7.921   5.358 -16.530  1.00  7.52           H  
ATOM    287  HA  LYS A 223      10.265   5.666 -17.798  1.00  7.38           H  
ATOM    288  HB2 LYS A 223       9.134   4.007 -19.079  1.00  8.82           H  
ATOM    289  HB3 LYS A 223       7.927   5.022 -19.272  1.00  8.82           H  
ATOM    290  HG2 LYS A 223       9.387   6.425 -20.494  1.00 11.40           H  
ATOM    291  HG3 LYS A 223      10.485   5.279 -20.411  1.00 11.40           H  
ATOM    292  HD2 LYS A 223       7.998   4.686 -21.558  1.00 14.14           H  
ATOM    293  HD3 LYS A 223       9.107   5.397 -22.446  1.00 14.14           H  
ATOM    294  HE2 LYS A 223      10.528   3.589 -21.970  1.00 15.36           H  
ATOM    295  HE3 LYS A 223       9.283   2.862 -21.301  1.00 15.36           H  
ATOM    296  HZ1 LYS A 223       9.467   2.303 -23.504  1.00 15.00           H  
ATOM    297  HZ2 LYS A 223       8.213   2.996 -23.291  1.00 15.00           H  
ATOM    298  HZ3 LYS A 223       9.329   3.688 -23.903  1.00 15.00           H  
ATOM    299  N   ASN A 224       9.712   7.984 -18.446  1.00  5.76           N  
ANISOU  299  N   ASN A 224      392    832    967     62     13     41       N  
ATOM    300  CA  ASN A 224       9.344   9.373 -18.758  1.00  6.00           C  
ANISOU  300  CA  ASN A 224      359    909   1013      0     16    115       C  
ATOM    301  C   ASN A 224       8.721   9.350 -20.145  1.00  6.27           C  
ANISOU  301  C   ASN A 224      481    962    938     17     40     62       C  
ATOM    302  O   ASN A 224       9.425   9.166 -21.143  1.00  7.95           O  
ANISOU  302  O   ASN A 224      586   1411   1022    156    168     48       O  
ATOM    303  CB  ASN A 224      10.629  10.199 -18.728  1.00  6.91           C  
ANISOU  303  CB  ASN A 224      505    864   1254     -9    -13    136       C  
ATOM    304  CG  ASN A 224      10.441  11.707 -18.896  1.00  8.32           C  
ANISOU  304  CG  ASN A 224      552    870   1738   -100    199     96       C  
ATOM    305  OD1 ASN A 224      11.431  12.392 -19.095  1.00 11.35           O  
ANISOU  305  OD1 ASN A 224      766   1038   2507    -40    422    157       O  
ATOM    306  ND2 ASN A 224       9.259  12.217 -18.749  1.00  7.29           N  
ANISOU  306  ND2 ASN A 224      458    862   1449    -45    103    113       N  
ATOM    307  H   ASN A 224      10.534   7.795 -18.611  1.00  6.93           H  
ATOM    308  HA  ASN A 224       8.701   9.746 -18.135  1.00  7.21           H  
ATOM    309  HB2 ASN A 224      11.066  10.056 -17.874  1.00  8.29           H  
ATOM    310  HB3 ASN A 224      11.204   9.898 -19.449  1.00  8.29           H  
ATOM    311 HD21 ASN A 224       9.142  13.064 -18.841  1.00  8.75           H  
ATOM    312 HD22 ASN A 224       8.592  11.708 -18.560  1.00  8.75           H  
ATOM    313  N   ALA A 225       7.395   9.461 -20.221  1.00  5.90           N  
ANISOU  313  N   ALA A 225      420    955    866     16     48     48       N  
ATOM    314  CA  ALA A 225       6.692   9.277 -21.477  1.00  6.67           C  
ANISOU  314  CA  ALA A 225      591   1068    877     45      4     15       C  
ATOM    315  C   ALA A 225       5.328   9.940 -21.424  1.00  6.06           C  
ANISOU  315  C   ALA A 225      501   1014    786    -16      4    -41       C  
ATOM    316  O   ALA A 225       4.755  10.159 -20.355  1.00  6.28           O  
ANISOU  316  O   ALA A 225      537   1063    785     14    -38    -35       O  
ATOM    317  CB  ALA A 225       6.499   7.792 -21.777  1.00  8.29           C  
ANISOU  317  CB  ALA A 225      888   1110   1151    141   -178   -152       C  
ATOM    318  H   ALA A 225       6.883   9.643 -19.554  1.00  7.09           H  
ATOM    319  HA  ALA A 225       7.212   9.704 -22.175  1.00  8.02           H  
ATOM    320  HB1 ALA A 225       6.026   7.699 -22.619  1.00  9.96           H  
ATOM    321  HB2 ALA A 225       7.368   7.367 -21.837  1.00  9.96           H  
ATOM    322  HB3 ALA A 225       5.982   7.390 -21.062  1.00  9.96           H  
ATOM    323  N   ASP A 226       4.819  10.210 -22.633  1.00  6.12           N  
ANISOU  323  N   ASP A 226      494   1050    780     -4    -31     26       N  
ATOM    324  CA  ASP A 226       3.445  10.625 -22.896  1.00  6.17           C  
ANISOU  324  CA  ASP A 226      554    947    844     -2    -40     32       C  
ATOM    325  C   ASP A 226       2.608   9.363 -23.047  1.00  5.87           C  
ANISOU  325  C   ASP A 226      530    949    751     68    -27     43       C  
ATOM    326  O   ASP A 226       2.809   8.590 -23.987  1.00  6.58           O  
ANISOU  326  O   ASP A 226      649   1074    778    -23      4    -47       O  
ATOM    327  CB  ASP A 226       3.445  11.441 -24.192  1.00  7.00           C  
ANISOU  327  CB  ASP A 226      718    973    967    -14   -120     61       C  
ATOM    328  CG  ASP A 226       2.095  11.899 -24.651  1.00  8.32           C  
ANISOU  328  CG  ASP A 226      976   1034   1152     21   -239    154       C  
ATOM    329  OD1 ASP A 226       1.069  11.407 -24.164  1.00  9.28           O  
ANISOU  329  OD1 ASP A 226      854   1158   1514     -5   -243    364       O  
ATOM    330  OD2 ASP A 226       2.098  12.818 -25.520  1.00 11.18           O  
ANISOU  330  OD2 ASP A 226     1376   1401   1470      4   -261    339       O  
ATOM    331  H   ASP A 226       5.282  10.156 -23.356  1.00  7.35           H  
ATOM    332  HA  ASP A 226       3.078  11.153 -22.169  1.00  7.41           H  
ATOM    333  HB2 ASP A 226       3.989  12.232 -24.057  1.00  8.40           H  
ATOM    334  HB3 ASP A 226       3.822  10.895 -24.899  1.00  8.40           H  
ATOM    335  N   ILE A 227       1.674   9.154 -22.125  1.00  5.88           N  
ANISOU  335  N   ILE A 227      625    791    818     30    -40    -68       N  
ATOM    336  CA  ILE A 227       0.905   7.911 -22.098  1.00  5.98           C  
ANISOU  336  CA  ILE A 227      628    779    867     42    -29    -38       C  
ATOM    337  C   ILE A 227       0.154   7.661 -23.396  1.00  5.95           C  
ANISOU  337  C   ILE A 227      587    869    804     23    -28    -14       C  
ATOM    338  O   ILE A 227      -0.020   6.503 -23.786  1.00  6.25           O  
ANISOU  338  O   ILE A 227      696    900    780    -20     24    -62       O  
ATOM    339  CB  ILE A 227      -0.022   7.886 -20.865  1.00  6.29           C  
ANISOU  339  CB  ILE A 227      668    902    819     -5     16    -76       C  
ATOM    340  CG1 ILE A 227      -0.600   6.476 -20.649  1.00  7.02           C  
ANISOU  340  CG1 ILE A 227      868    953    848    -76    148    -79       C  
ATOM    341  CG2 ILE A 227      -1.123   8.942 -20.958  1.00  7.15           C  
ANISOU  341  CG2 ILE A 227      782    982    951     26     90   -102       C  
ATOM    342  CD1 ILE A 227      -1.320   6.322 -19.335  1.00  8.66           C  
ANISOU  342  CD1 ILE A 227     1182   1164    944   -223    145    -76       C  
ATOM    343  H   ILE A 227       1.464   9.712 -21.506  1.00  7.06           H  
ATOM    344  HA  ILE A 227       1.536   7.179 -22.013  1.00  7.19           H  
ATOM    345  HB  ILE A 227       0.515   8.111 -20.090  1.00  7.55           H  
ATOM    346 HG12 ILE A 227      -1.232   6.284 -21.360  1.00  8.44           H  
ATOM    347 HG13 ILE A 227       0.126   5.834 -20.668  1.00  8.44           H  
ATOM    348 HG21 ILE A 227      -1.580   8.997 -20.104  1.00  8.58           H  
ATOM    349 HG22 ILE A 227      -0.722   9.798 -21.175  1.00  8.58           H  
ATOM    350 HG23 ILE A 227      -1.750   8.684 -21.652  1.00  8.58           H  
ATOM    351 HD11 ILE A 227      -1.560   5.390 -19.214  1.00 10.40           H  
ATOM    352 HD12 ILE A 227      -0.734   6.608 -18.618  1.00 10.40           H  
ATOM    353 HD13 ILE A 227      -2.120   6.871 -19.347  1.00 10.40           H  
ATOM    354  N   VAL A 228      -0.331   8.703 -24.071  1.00  6.16           N  
ANISOU  354  N   VAL A 228      688    818    834     25   -111    -58       N  
ATOM    355  CA  VAL A 228      -1.040   8.493 -25.332  1.00  6.70           C  
ANISOU  355  CA  VAL A 228      694    885    967     -1   -139     38       C  
ATOM    356  C   VAL A 228      -0.107   7.940 -26.401  1.00  6.86           C  
ANISOU  356  C   VAL A 228      857    923    826     20   -196    101       C  
ATOM    357  O   VAL A 228      -0.421   6.966 -27.096  1.00  7.74           O  
ANISOU  357  O   VAL A 228     1031   1068    842      5   -194     11       O  
ATOM    358  CB  VAL A 228      -1.713   9.803 -25.796  1.00  7.96           C  
ANISOU  358  CB  VAL A 228      780   1018   1227    159   -209     79       C  
ATOM    359  CG1 VAL A 228      -2.236   9.675 -27.235  1.00  9.66           C  
ANISOU  359  CG1 VAL A 228     1190   1208   1274    183   -434     43       C  
ATOM    360  CG2 VAL A 228      -2.820  10.181 -24.833  1.00  9.62           C  
ANISOU  360  CG2 VAL A 228      882   1269   1505    290     10     84       C  
ATOM    361  H   VAL A 228      -0.266   9.525 -23.825  1.00  7.40           H  
ATOM    362  HA  VAL A 228      -1.733   7.832 -25.179  1.00  8.05           H  
ATOM    363  HB  VAL A 228      -1.057  10.517 -25.797  1.00  9.56           H  
ATOM    364 HG11 VAL A 228      -2.865  10.393 -27.407  1.00 11.60           H  
ATOM    365 HG12 VAL A 228      -1.488   9.736 -27.849  1.00 11.60           H  
ATOM    366 HG13 VAL A 228      -2.678   8.817 -27.335  1.00 11.60           H  
ATOM    367 HG21 VAL A 228      -3.213  11.021 -25.118  1.00 11.55           H  
ATOM    368 HG22 VAL A 228      -3.493   9.483 -24.836  1.00 11.55           H  
ATOM    369 HG23 VAL A 228      -2.445  10.276 -23.944  1.00 11.55           H  
ATOM    370  N   GLU A 229       1.065   8.564 -26.551  1.00  7.07           N  
ANISOU  370  N   GLU A 229      872    939    876     -6    -39     13       N  
ATOM    371  CA  GLU A 229       2.035   8.083 -27.534  1.00  7.92           C  
ANISOU  371  CA  GLU A 229     1050    997    964     55    115     77       C  
ATOM    372  C   GLU A 229       2.534   6.696 -27.155  1.00  7.31           C  
ANISOU  372  C   GLU A 229      858   1057    863    -20     47     22       C  
ATOM    373  O   GLU A 229       2.726   5.834 -28.018  1.00  8.02           O  
ANISOU  373  O   GLU A 229     1166   1041    839     83    126    -85       O  
ATOM    374  CB  GLU A 229       3.188   9.076 -27.664  1.00  9.85           C  
ANISOU  374  CB  GLU A 229     1267   1163   1312     -7    306    204       C  
ATOM    375  CG  GLU A 229       2.736  10.407 -28.220  1.00 13.41           C  
ANISOU  375  CG  GLU A 229     2004   1495   1595   -108    302    247       C  
ATOM    376  CD  GLU A 229       1.897  10.252 -29.473  1.00 16.64           C  
ANISOU  376  CD  GLU A 229     2771   1884   1668    186    348    297       C  
ATOM    377  OE1 GLU A 229       2.392   9.613 -30.435  1.00 18.50           O  
ANISOU  377  OE1 GLU A 229     3364   2112   1552    236    435    336       O  
ATOM    378  OE2 GLU A 229       0.738  10.744 -29.494  1.00 19.02           O  
ANISOU  378  OE2 GLU A 229     3064   2354   1808    497    178    208       O  
ATOM    379  H   GLU A 229       1.317   9.255 -26.105  1.00  8.50           H  
ATOM    380  HA  GLU A 229       1.612   8.021 -28.404  1.00  9.52           H  
ATOM    381  HB2 GLU A 229       3.575   9.229 -26.788  1.00 11.82           H  
ATOM    382  HB3 GLU A 229       3.857   8.709 -28.263  1.00 11.82           H  
ATOM    383  HG2 GLU A 229       2.201  10.865 -27.553  1.00 16.10           H  
ATOM    384  HG3 GLU A 229       3.515  10.940 -28.443  1.00 16.10           H  
ATOM    385  N   GLU A 230       2.737   6.466 -25.858  1.00  6.79           N  
ANISOU  385  N   GLU A 230      746    996    837     38      9     -5       N  
ATOM    386  CA  GLU A 230       3.191   5.160 -25.403  1.00  6.66           C  
ANISOU  386  CA  GLU A 230      714   1001    815    108    -14    -69       C  
ATOM    387  C   GLU A 230       2.148   4.087 -25.696  1.00  6.74           C  
ANISOU  387  C   GLU A 230      869    911    782    111     11     17       C  
ATOM    388  O   GLU A 230       2.499   2.994 -26.152  1.00  7.58           O  
ANISOU  388  O   GLU A 230     1031    909    940    187    -16    -84       O  
ATOM    389  CB  GLU A 230       3.573   5.250 -23.930  1.00  7.04           C  
ANISOU  389  CB  GLU A 230      728   1121    825    107    -19    -88       C  
ATOM    390  CG  GLU A 230       4.232   4.001 -23.362  1.00  7.35           C  
ANISOU  390  CG  GLU A 230      811   1048    933     44     -3     22       C  
ATOM    391  CD  GLU A 230       5.641   3.734 -23.844  1.00  8.51           C  
ANISOU  391  CD  GLU A 230      812   1217   1205     98   -108     55       C  
ATOM    392  OE1 GLU A 230       6.204   4.502 -24.656  1.00  9.99           O  
ANISOU  392  OE1 GLU A 230      881   1346   1569    141    150    250       O  
ATOM    393  OE2 GLU A 230       6.185   2.693 -23.408  1.00  9.16           O  
ANISOU  393  OE2 GLU A 230     1080   1188   1211    121   -208     61       O  
ATOM    394  H   GLU A 230       2.619   7.043 -25.231  1.00  8.15           H  
ATOM    395  HA  GLU A 230       3.991   4.890 -25.881  1.00  8.00           H  
ATOM    396  HB2 GLU A 230       4.196   5.985 -23.818  1.00  8.45           H  
ATOM    397  HB3 GLU A 230       2.769   5.415 -23.414  1.00  8.45           H  
ATOM    398  HG2 GLU A 230       4.269   4.087 -22.397  1.00  8.83           H  
ATOM    399  HG3 GLU A 230       3.693   3.233 -23.606  1.00  8.83           H  
ATOM    400  N   ALA A 231       0.867   4.379 -25.477  1.00  6.27           N  
ANISOU  400  N   ALA A 231      719    868    797     22      0    -51       N  
ATOM    401  CA  ALA A 231      -0.173   3.405 -25.784  1.00  6.65           C  
ANISOU  401  CA  ALA A 231      857    872    796     42    -83     -4       C  
ATOM    402  C   ALA A 231      -0.160   3.050 -27.261  1.00  7.00           C  
ANISOU  402  C   ALA A 231      919    958    782     60    -80    -42       C  
ATOM    403  O   ALA A 231      -0.312   1.884 -27.630  1.00  7.40           O  
ANISOU  403  O   ALA A 231     1025    925    862     24   -113    -70       O  
ATOM    404  CB  ALA A 231      -1.532   3.950 -25.364  1.00  6.72           C  
ANISOU  404  CB  ALA A 231      787    981    784    -24    -82    -47       C  
ATOM    405  H   ALA A 231       0.579   5.123 -25.156  1.00  7.54           H  
ATOM    406  HA  ALA A 231      -0.012   2.593 -25.280  1.00  7.98           H  
ATOM    407  HB1 ALA A 231      -2.216   3.304 -25.597  1.00  8.07           H  
ATOM    408  HB2 ALA A 231      -1.530   4.099 -24.406  1.00  8.07           H  
ATOM    409  HB3 ALA A 231      -1.694   4.786 -25.829  1.00  8.07           H  
ATOM    410  N   LYS A 232      -0.004   4.043 -28.128  1.00  7.43           N  
ANISOU  410  N   LYS A 232     1122    950    752     48   -108    -25       N  
ATOM    411  CA  LYS A 232       0.012   3.764 -29.561  1.00  8.66           C  
ANISOU  411  CA  LYS A 232     1334   1170    788     87   -120    -27       C  
ATOM    412  C   LYS A 232       1.173   2.851 -29.934  1.00  9.16           C  
ANISOU  412  C   LYS A 232     1486   1144    850     22    -58    -54       C  
ATOM    413  O   LYS A 232       1.044   2.007 -30.824  1.00 10.93           O  
ANISOU  413  O   LYS A 232     1884   1295    973    162    -22   -253       O  
ATOM    414  CB  LYS A 232       0.091   5.072 -30.347  1.00 10.04           C  
ANISOU  414  CB  LYS A 232     1684   1334    798    206    -63     42       C  
ATOM    415  CG  LYS A 232      -1.151   5.937 -30.270  1.00 12.13           C  
ANISOU  415  CG  LYS A 232     2132   1594    883    625   -154    148       C  
ATOM    416  CD  LYS A 232      -0.887   7.289 -30.934  1.00 16.35           C  
ANISOU  416  CD  LYS A 232     3054   1934   1225    907     52    362       C  
ATOM    417  CE  LYS A 232      -2.067   8.217 -30.859  1.00 19.86           C  
ANISOU  417  CE  LYS A 232     3892   2091   1561    787    159    442       C  
ATOM    418  NZ  LYS A 232      -1.673   9.558 -31.383  1.00 22.36           N  
ANISOU  418  NZ  LYS A 232     4481   2215   1799    611    193    518       N  
ATOM    419  H   LYS A 232       0.092   4.872 -27.919  1.00  8.93           H  
ATOM    420  HA  LYS A 232      -0.813   3.314 -29.800  1.00 10.40           H  
ATOM    421  HB2 LYS A 232       0.832   5.594 -30.002  1.00 12.06           H  
ATOM    422  HB3 LYS A 232       0.241   4.861 -31.282  1.00 12.06           H  
ATOM    423  HG2 LYS A 232      -1.883   5.500 -30.732  1.00 14.57           H  
ATOM    424  HG3 LYS A 232      -1.388   6.088 -29.341  1.00 14.57           H  
ATOM    425  HD2 LYS A 232      -0.139   7.718 -30.490  1.00 19.63           H  
ATOM    426  HD3 LYS A 232      -0.678   7.145 -31.871  1.00 19.63           H  
ATOM    427  HE2 LYS A 232      -2.794   7.870 -31.398  1.00 23.84           H  
ATOM    428  HE3 LYS A 232      -2.353   8.312 -29.937  1.00 23.84           H  
ATOM    429  HZ1 LYS A 232      -2.360  10.121 -31.324  1.00 26.84           H  
ATOM    430  HZ2 LYS A 232      -0.993   9.882 -30.909  1.00 26.84           H  
ATOM    431  HZ3 LYS A 232      -1.426   9.491 -32.235  1.00 26.84           H  
ATOM    432  N   LYS A 233       2.324   3.014 -29.283  1.00  8.41           N  
ANISOU  432  N   LYS A 233     1276   1067    851    102    207     31       N  
ATOM    433  CA  LYS A 233       3.489   2.184 -29.591  1.00  9.59           C  
ANISOU  433  CA  LYS A 233     1276   1156   1211     71    479    114       C  
ATOM    434  C   LYS A 233       3.395   0.789 -28.977  1.00  8.38           C  
ANISOU  434  C   LYS A 233     1112   1089    984     58    313    -13       C  
ATOM    435  O   LYS A 233       3.768  -0.208 -29.607  1.00  9.35           O  
ANISOU  435  O   LYS A 233     1427   1110   1015     96    375   -108       O  
ATOM    436  CB  LYS A 233       4.765   2.872 -29.093  1.00 12.63           C  
ANISOU  436  CB  LYS A 233     1327   1365   2107      6    630    314       C  
ATOM    437  CG  LYS A 233       5.140   4.124 -29.838  1.00 18.02           C  
ANISOU  437  CG  LYS A 233     1988   1993   2866   -316    594    275       C  
ATOM    438  CD  LYS A 233       6.386   4.763 -29.225  1.00 24.92           C  
ANISOU  438  CD  LYS A 233     3104   2874   3489   -757    301    213       C  
ATOM    439  CE  LYS A 233       6.403   6.283 -29.386  1.00 29.26           C  
ANISOU  439  CE  LYS A 233     3827   3452   3840   -989    120     41       C  
ATOM    440  NZ  LYS A 233       7.367   6.949 -28.454  1.00 30.80           N  
ANISOU  440  NZ  LYS A 233     4059   3706   3939  -1058    114    -60       N  
ATOM    441  H   LYS A 233       2.458   3.595 -28.662  1.00 10.10           H  
ATOM    442  HA  LYS A 233       3.535   2.082 -30.555  1.00 11.51           H  
ATOM    443  HB2 LYS A 233       4.640   3.114 -28.162  1.00 15.17           H  
ATOM    444  HB3 LYS A 233       5.504   2.250 -29.178  1.00 15.17           H  
ATOM    445  HG2 LYS A 233       5.329   3.905 -30.764  1.00 21.63           H  
ATOM    446  HG3 LYS A 233       4.410   4.761 -29.790  1.00 21.63           H  
ATOM    447  HD2 LYS A 233       6.412   4.561 -28.277  1.00 29.91           H  
ATOM    448  HD3 LYS A 233       7.174   4.406 -29.663  1.00 29.91           H  
ATOM    449  HE2 LYS A 233       6.662   6.503 -30.294  1.00 35.12           H  
ATOM    450  HE3 LYS A 233       5.516   6.631 -29.201  1.00 35.12           H  
ATOM    451  HZ1 LYS A 233       7.347   7.830 -28.573  1.00 36.97           H  
ATOM    452  HZ2 LYS A 233       7.149   6.767 -27.610  1.00 36.97           H  
ATOM    453  HZ3 LYS A 233       8.193   6.654 -28.609  1.00 36.97           H  
ATOM    454  N   VAL A 234       2.951   0.714 -27.727  1.00  7.17           N  
ANISOU  454  N   VAL A 234      835    994    896     17    186      2       N  
ATOM    455  CA  VAL A 234       2.947  -0.524 -26.954  1.00  6.92           C  
ANISOU  455  CA  VAL A 234      830    939    860     52    110     -4       C  
ATOM    456  C   VAL A 234       1.814  -1.449 -27.343  1.00  6.58           C  
ANISOU  456  C   VAL A 234      775   1022    702     69    128    -36       C  
ATOM    457  O   VAL A 234       1.947  -2.670 -27.225  1.00  7.04           O  
ANISOU  457  O   VAL A 234      821    915    938     -4     71    -62       O  
ATOM    458  CB  VAL A 234       2.821  -0.151 -25.453  1.00  7.91           C  
ANISOU  458  CB  VAL A 234     1016    986   1004     71   -121    -32       C  
ATOM    459  CG1 VAL A 234       2.501  -1.365 -24.577  1.00  7.83           C  
ANISOU  459  CG1 VAL A 234     1072   1020    882     92    -26    -58       C  
ATOM    460  CG2 VAL A 234       4.110   0.516 -24.984  1.00  8.91           C  
ANISOU  460  CG2 VAL A 234     1106   1096   1185     -5   -248    -85       C  
ATOM    461  H   VAL A 234       2.637   1.384 -27.289  1.00  8.62           H  
ATOM    462  HA  VAL A 234       3.776  -0.996 -27.132  1.00  8.31           H  
ATOM    463  HB  VAL A 234       2.079   0.466 -25.357  1.00  9.50           H  
ATOM    464 HG11 VAL A 234       2.676  -1.141 -23.650  1.00  9.40           H  
ATOM    465 HG12 VAL A 234       1.566  -1.598 -24.689  1.00  9.40           H  
ATOM    466 HG13 VAL A 234       3.062  -2.108 -24.849  1.00  9.40           H  
ATOM    467 HG21 VAL A 234       4.019   0.755 -24.048  1.00 10.71           H  
ATOM    468 HG22 VAL A 234       4.847  -0.106 -25.096  1.00 10.71           H  
ATOM    469 HG23 VAL A 234       4.266   1.312 -25.515  1.00 10.71           H  
ATOM    470  N   LYS A 235       0.671  -0.888 -27.704  1.00  6.84           N  
ANISOU  470  N   LYS A 235      828    998    772     62     26      4       N  
ATOM    471  CA  LYS A 235      -0.545  -1.661 -27.922  1.00  7.25           C  
ANISOU  471  CA  LYS A 235      849   1109    796     26    -34    -52       C  
ATOM    472  C   LYS A 235      -0.863  -2.470 -26.661  1.00  6.69           C  
ANISOU  472  C   LYS A 235      721   1000    823     62   -105    -52       C  
ATOM    473  O   LYS A 235      -0.976  -3.704 -26.697  1.00  7.07           O  
ANISOU  473  O   LYS A 235      850    986    852     10    -25   -128       O  
ATOM    474  CB  LYS A 235      -0.454  -2.541 -29.163  1.00  8.54           C  
ANISOU  474  CB  LYS A 235     1112   1301    832    -18    -31    -80       C  
ATOM    475  CG  LYS A 235      -0.152  -1.757 -30.424  1.00 11.41           C  
ANISOU  475  CG  LYS A 235     1724   1782    831    102     62   -121       C  
ATOM    476  CD  LYS A 235      -0.035  -2.675 -31.627  1.00 16.53           C  
ANISOU  476  CD  LYS A 235     2562   2630   1088    340    206   -145       C  
ATOM    477  CE  LYS A 235       0.573  -1.964 -32.822  1.00 22.11           C  
ANISOU  477  CE  LYS A 235     3670   3368   1362    407    389   -108       C  
ATOM    478  NZ  LYS A 235       0.553  -2.835 -34.020  1.00 25.79           N  
ANISOU  478  NZ  LYS A 235     4303   3827   1670    339    452   -134       N  
ATOM    479  H   LYS A 235       0.569  -0.044 -27.833  1.00  8.22           H  
ATOM    480  HA  LYS A 235      -1.284  -1.055 -28.087  1.00  8.71           H  
ATOM    481  HB2 LYS A 235       0.256  -3.190 -29.037  1.00 10.26           H  
ATOM    482  HB3 LYS A 235      -1.301  -2.996 -29.289  1.00 10.26           H  
ATOM    483  HG2 LYS A 235      -0.869  -1.125 -30.590  1.00 13.71           H  
ATOM    484  HG3 LYS A 235       0.688  -1.284 -30.316  1.00 13.71           H  
ATOM    485  HD2 LYS A 235       0.534  -3.428 -31.401  1.00 19.84           H  
ATOM    486  HD3 LYS A 235      -0.917  -2.989 -31.878  1.00 19.84           H  
ATOM    487  HE2 LYS A 235       0.062  -1.163 -33.016  1.00 26.54           H  
ATOM    488  HE3 LYS A 235       1.494  -1.732 -32.626  1.00 26.54           H  
ATOM    489  HZ1 LYS A 235       0.915  -2.408 -34.712  1.00 30.96           H  
ATOM    490  HZ2 LYS A 235       1.017  -3.578 -33.864  1.00 30.96           H  
ATOM    491  HZ3 LYS A 235      -0.285  -3.054 -34.223  1.00 30.96           H  
ATOM    492  N   PRO A 236      -1.038  -1.807 -25.529  1.00  6.42           N  
ANISOU  492  N   PRO A 236      654   1027    758     69      3    -30       N  
ATOM    493  CA  PRO A 236      -1.271  -2.541 -24.295  1.00  6.37           C  
ANISOU  493  CA  PRO A 236      545   1076    799    -10    -12    -73       C  
ATOM    494  C   PRO A 236      -2.625  -3.211 -24.310  1.00  6.52           C  
ANISOU  494  C   PRO A 236      563   1078    837     54    -28   -120       C  
ATOM    495  O   PRO A 236      -3.587  -2.718 -24.882  1.00  7.59           O  
ANISOU  495  O   PRO A 236      697   1187   1000     28    -93    -33       O  
ATOM    496  CB  PRO A 236      -1.214  -1.445 -23.224  1.00  7.42           C  
ANISOU  496  CB  PRO A 236      707   1262    851   -172     38   -164       C  
ATOM    497  CG  PRO A 236      -1.673  -0.205 -23.948  1.00  7.61           C  
ANISOU  497  CG  PRO A 236      822   1117    954      9     33   -144       C  
ATOM    498  CD  PRO A 236      -1.148  -0.344 -25.349  1.00  7.17           C  
ANISOU  498  CD  PRO A 236      784   1027    912    101     13    -80       C  
ATOM    499  HA  PRO A 236      -0.575  -3.198 -24.137  1.00  7.65           H  
ATOM    500  HB2 PRO A 236      -1.810  -1.664 -22.490  1.00  8.91           H  
ATOM    501  HB3 PRO A 236      -0.307  -1.345 -22.896  1.00  8.91           H  
ATOM    502  HG2 PRO A 236      -2.642  -0.162 -23.945  1.00  9.15           H  
ATOM    503  HG3 PRO A 236      -1.305   0.583 -23.518  1.00  9.15           H  
ATOM    504  HD2 PRO A 236      -1.768   0.037 -25.990  1.00  8.61           H  
ATOM    505  HD3 PRO A 236      -0.280   0.080 -25.436  1.00  8.61           H  
ATOM    506  N  ATHR A 237      -2.725  -4.340 -23.619  0.54  5.76           N  
ANISOU  506  N  ATHR A 237      471   1005    712     74     97   -221       N  
ATOM    507  N  BTHR A 237      -2.703  -4.342 -23.606  0.46  7.24           N  
ANISOU  507  N  BTHR A 237      749   1039    961    -12   -183   -130       N  
ATOM    508  CA ATHR A 237      -4.044  -4.914 -23.391  0.54  6.41           C  
ANISOU  508  CA ATHR A 237      576    900    961    -58    167   -312       C  
ATOM    509  CA BTHR A 237      -3.993  -4.961 -23.335  0.46  8.42           C  
ANISOU  509  CA BTHR A 237      898    990   1311    -21   -208   -210       C  
ATOM    510  C  ATHR A 237      -4.877  -4.049 -22.459  0.54  5.53           C  
ANISOU  510  C  ATHR A 237      507    719    874     35    -73    -55       C  
ATOM    511  C  BTHR A 237      -4.858  -4.083 -22.444  0.46  6.58           C  
ANISOU  511  C  BTHR A 237      687    792   1019     13    -73    -99       C  
ATOM    512  O  ATHR A 237      -6.103  -4.039 -22.580  0.54  6.26           O  
ANISOU  512  O  ATHR A 237      472    912    994   -150   -309    -73       O  
ATOM    513  O  BTHR A 237      -6.084  -4.125 -22.558  0.46  6.73           O  
ANISOU  513  O  BTHR A 237      708    838   1011    100    170   -247       O  
ATOM    514  CB ATHR A 237      -3.904  -6.335 -22.867  0.54  8.57           C  
ANISOU  514  CB ATHR A 237      861    674   1719     47    400   -185       C  
ATOM    515  CB BTHR A 237      -3.805  -6.329 -22.680  0.46 11.90           C  
ANISOU  515  CB BTHR A 237     1164   1085   2272     90   -126   -234       C  
ATOM    516  OG1ATHR A 237      -3.054  -6.314 -21.725  0.54  8.55           O  
ANISOU  516  OG1ATHR A 237     1364    619   1266    191    525    213       O  
ATOM    517  OG1BTHR A 237      -3.027  -7.176 -23.532  0.46 15.21           O  
ANISOU  517  OG1BTHR A 237     1614   1358   2805    213     29   -317       O  
ATOM    518  CG2ATHR A 237      -3.303  -7.248 -23.947  0.54 11.12           C  
ANISOU  518  CG2ATHR A 237      951   1012   2261     69    357   -582       C  
ATOM    519  CG2BTHR A 237      -5.159  -6.969 -22.423  0.46 13.08           C  
ANISOU  519  CG2BTHR A 237     1137   1391   2440    123   -190    -88       C  
ATOM    520  H  ATHR A 237      -2.067  -4.780 -23.283  0.54  6.92           H  
ATOM    521  H  BTHR A 237      -2.029  -4.765 -23.278  0.46  8.69           H  
ATOM    522  HA ATHR A 237      -4.524  -4.966 -24.232  0.54  7.71           H  
ATOM    523  HA BTHR A 237      -4.450  -5.091 -24.181  0.46 10.11           H  
ATOM    524  HB ATHR A 237      -4.772  -6.694 -22.626  0.54 10.29           H  
ATOM    525  HB BTHR A 237      -3.343  -6.226 -21.834  0.46 14.29           H  
ATOM    526  HG1ATHR A 237      -2.964  -7.092 -21.419  0.54 10.27           H  
ATOM    527  HG1BTHR A 237      -2.952  -7.939 -23.188  0.46 18.26           H  
ATOM    528 HG21ATHR A 237      -3.233  -8.156 -23.612  0.54 13.35           H  
ATOM    529 HG21BTHR A 237      -5.128  -7.912 -22.649  0.46 15.70           H  
ATOM    530 HG22ATHR A 237      -3.868  -7.246 -24.735  0.54 13.35           H  
ATOM    531 HG22BTHR A 237      -5.398  -6.877 -21.488  0.46 15.70           H  
ATOM    532 HG23ATHR A 237      -2.419  -6.935 -24.192  0.54 13.35           H  
ATOM    533 HG23BTHR A 237      -5.838  -6.538 -22.966  0.46 15.70           H  
ATOM    534  N   VAL A 238      -4.242  -3.322 -21.537  1.00  5.62           N  
ANISOU  534  N   VAL A 238      463    836    838      5    -77    -80       N  
ATOM    535  CA  VAL A 238      -4.971  -2.471 -20.600  1.00  5.34           C  
ANISOU  535  CA  VAL A 238      349    887    793     25     -4   -119       C  
ATOM    536  C   VAL A 238      -4.242  -1.145 -20.468  1.00  5.39           C  
ANISOU  536  C   VAL A 238      387    926    734     -9    -70    -84       C  
ATOM    537  O   VAL A 238      -3.087  -1.127 -20.029  1.00  6.15           O  
ANISOU  537  O   VAL A 238      493    890    953     33   -187   -126       O  
ATOM    538  CB  VAL A 238      -5.107  -3.105 -19.210  1.00  6.77           C  
ANISOU  538  CB  VAL A 238      576   1124    872    -54      6      6       C  
ATOM    539  CG1 VAL A 238      -5.903  -2.196 -18.277  1.00  7.97           C  
ANISOU  539  CG1 VAL A 238      695   1462    872     39     47      4       C  
ATOM    540  CG2 VAL A 238      -5.758  -4.479 -19.290  1.00  7.61           C  
ANISOU  540  CG2 VAL A 238      764   1143    983    -82    -23     99       C  
ATOM    541  H   VAL A 238      -3.388  -3.305 -21.434  1.00  6.76           H  
ATOM    542  HA  VAL A 238      -5.854  -2.307 -20.966  1.00  6.42           H  
ATOM    543  HB  VAL A 238      -4.216  -3.219 -18.844  1.00  8.13           H  
ATOM    544 HG11 VAL A 238      -6.131  -2.690 -17.474  1.00  9.57           H  
ATOM    545 HG12 VAL A 238      -5.361  -1.425 -18.050  1.00  9.57           H  
ATOM    546 HG13 VAL A 238      -6.712  -1.910 -18.730  1.00  9.57           H  
ATOM    547 HG21 VAL A 238      -5.867  -4.829 -18.392  1.00  9.14           H  
ATOM    548 HG22 VAL A 238      -6.624  -4.394 -19.719  1.00  9.14           H  
ATOM    549 HG23 VAL A 238      -5.188  -5.069 -19.808  1.00  9.14           H  
ATOM    550  N   VAL A 239      -4.920  -0.046 -20.796  1.00  5.13           N  
ANISOU  550  N   VAL A 239      380    829    741     26   -142   -138       N  
ATOM    551  CA  VAL A 239      -4.466   1.287 -20.430  1.00  5.18           C  
ANISOU  551  CA  VAL A 239      336    873    761     21    -99   -107       C  
ATOM    552  C   VAL A 239      -5.369   1.787 -19.317  1.00  5.00           C  
ANISOU  552  C   VAL A 239      334    832    732     18    -78    -66       C  
ATOM    553  O   VAL A 239      -6.589   1.647 -19.391  1.00  5.75           O  
ANISOU  553  O   VAL A 239      334   1030    821    -27    -84   -205       O  
ATOM    554  CB  VAL A 239      -4.401   2.257 -21.631  1.00  5.71           C  
ANISOU  554  CB  VAL A 239      536    879    754      8    -34    -80       C  
ATOM    555  CG1 VAL A 239      -5.776   2.583 -22.213  1.00  6.41           C  
ANISOU  555  CG1 VAL A 239      685   1003    748     19    -99    -27       C  
ATOM    556  CG2 VAL A 239      -3.649   3.518 -21.246  1.00  6.34           C  
ANISOU  556  CG2 VAL A 239      733    900    774    -59      6    -18       C  
ATOM    557  H   VAL A 239      -5.657  -0.051 -21.238  1.00  6.17           H  
ATOM    558  HA  VAL A 239      -3.559   1.239 -20.089  1.00  6.23           H  
ATOM    559  HB  VAL A 239      -3.915   1.809 -22.342  1.00  6.86           H  
ATOM    560 HG11 VAL A 239      -5.659   3.070 -23.044  1.00  7.70           H  
ATOM    561 HG12 VAL A 239      -6.252   1.754 -22.380  1.00  7.70           H  
ATOM    562 HG13 VAL A 239      -6.267   3.125 -21.577  1.00  7.70           H  
ATOM    563 HG21 VAL A 239      -3.569   4.088 -22.027  1.00  7.61           H  
ATOM    564 HG22 VAL A 239      -4.141   3.979 -20.549  1.00  7.61           H  
ATOM    565 HG23 VAL A 239      -2.767   3.274 -20.923  1.00  7.61           H  
ATOM    566  N   VAL A 240      -4.773   2.381 -18.289  1.00  5.15           N  
ANISOU  566  N   VAL A 240      302    938    714    -17    -19    -94       N  
ATOM    567  CA  VAL A 240      -5.520   2.967 -17.186  1.00  5.06           C  
ANISOU  567  CA  VAL A 240      312    858    752    -22      5    -89       C  
ATOM    568  C   VAL A 240      -5.816   4.432 -17.486  1.00  5.07           C  
ANISOU  568  C   VAL A 240      390    896    640    -27    -92    -45       C  
ATOM    569  O   VAL A 240      -4.917   5.203 -17.860  1.00  5.45           O  
ANISOU  569  O   VAL A 240      367    881    821    -21    -37     20       O  
ATOM    570  CB  VAL A 240      -4.739   2.832 -15.880  1.00  4.89           C  
ANISOU  570  CB  VAL A 240      344    767    748    -52    -16    -67       C  
ATOM    571  CG1 VAL A 240      -5.431   3.568 -14.737  1.00  5.54           C  
ANISOU  571  CG1 VAL A 240      517    898    689     38    -52    -19       C  
ATOM    572  CG2 VAL A 240      -4.536   1.368 -15.538  1.00  5.69           C  
ANISOU  572  CG2 VAL A 240      477    892    791    -68    -72    -40       C  
ATOM    573  H   VAL A 240      -3.920   2.460 -18.208  1.00  6.18           H  
ATOM    574  HA  VAL A 240      -6.367   2.502 -17.101  1.00  6.08           H  
ATOM    575  HB  VAL A 240      -3.868   3.243 -15.998  1.00  5.88           H  
ATOM    576 HG11 VAL A 240      -5.017   3.310 -13.899  1.00  6.65           H  
ATOM    577 HG12 VAL A 240      -5.336   4.523 -14.873  1.00  6.65           H  
ATOM    578 HG13 VAL A 240      -6.371   3.326 -14.730  1.00  6.65           H  
ATOM    579 HG21 VAL A 240      -4.073   1.304 -14.688  1.00  6.83           H  
ATOM    580 HG22 VAL A 240      -5.402   0.935 -15.476  1.00  6.83           H  
ATOM    581 HG23 VAL A 240      -4.006   0.952 -16.236  1.00  6.83           H  
ATOM    582  N   ASN A 241      -7.081   4.804 -17.288  1.00  5.01           N  
ANISOU  582  N   ASN A 241      339    835    732     -7    -36    -51       N  
ATOM    583  CA  ASN A 241      -7.498   6.191 -17.323  1.00  5.26           C  
ANISOU  583  CA  ASN A 241      396    796    809     24     -8    -39       C  
ATOM    584  C   ASN A 241      -7.650   6.731 -15.902  1.00  5.30           C  
ANISOU  584  C   ASN A 241      337    868    808     10     -5    -65       C  
ATOM    585  O   ASN A 241      -8.178   6.059 -15.013  1.00  5.91           O  
ANISOU  585  O   ASN A 241      503    921    820     12     26    -57       O  
ATOM    586  CB  ASN A 241      -8.805   6.340 -18.079  1.00  5.46           C  
ANISOU  586  CB  ASN A 241      422    817    836     21    -79    -30       C  
ATOM    587  CG  ASN A 241      -9.253   7.784 -18.177  1.00  5.77           C  
ANISOU  587  CG  ASN A 241      508    855    830      8   -119    -88       C  
ATOM    588  OD1 ASN A 241      -8.428   8.702 -18.235  1.00  6.12           O  
ANISOU  588  OD1 ASN A 241      552    842    933      8   -124    -36       O  
ATOM    589  ND2 ASN A 241     -10.565   7.979 -18.235  1.00  6.51           N  
ANISOU  589  ND2 ASN A 241      508    921   1045     32   -165    -67       N  
ATOM    590  H   ASN A 241      -7.723   4.255 -17.128  1.00  6.03           H  
ATOM    591  HA  ASN A 241      -6.823   6.721 -17.776  1.00  6.33           H  
ATOM    592  HB2 ASN A 241      -8.693   5.998 -18.979  1.00  6.56           H  
ATOM    593  HB3 ASN A 241      -9.497   5.841 -17.618  1.00  6.56           H  
ATOM    594 HD21 ASN A 241     -10.879   8.777 -18.292  1.00  7.82           H  
ATOM    595 HD22 ASN A 241     -11.100   7.306 -18.216  1.00  7.82           H  
ATOM    596  N   ALA A 242      -7.175   7.965 -15.709  1.00  5.47           N  
ANISOU  596  N   ALA A 242      434    858    784    -36    -46    -98       N  
ATOM    597  CA  ALA A 242      -7.392   8.746 -14.487  1.00  5.87           C  
ANISOU  597  CA  ALA A 242      534    958    736   -108     -1   -150       C  
ATOM    598  C   ALA A 242      -8.779   9.371 -14.574  1.00  5.81           C  
ANISOU  598  C   ALA A 242      456    934    816    -58     -2   -146       C  
ATOM    599  O   ALA A 242      -8.971  10.534 -14.938  1.00  6.35           O  
ANISOU  599  O   ALA A 242      547    891    974    -85      5    -47       O  
ATOM    600  CB  ALA A 242      -6.303   9.790 -14.367  1.00  6.59           C  
ANISOU  600  CB  ALA A 242      514   1085    905    -71    -17   -185       C  
ATOM    601  H   ALA A 242      -6.707   8.388 -16.294  1.00  6.57           H  
ATOM    602  HA  ALA A 242      -7.366   8.176 -13.703  1.00  7.05           H  
ATOM    603  HB1 ALA A 242      -6.456  10.315 -13.565  1.00  7.92           H  
ATOM    604  HB2 ALA A 242      -5.443   9.344 -14.311  1.00  7.92           H  
ATOM    605  HB3 ALA A 242      -6.328  10.364 -15.148  1.00  7.92           H  
ATOM    606  N   ALA A 243      -9.776   8.548 -14.254  1.00  6.00           N  
ANISOU  606  N   ALA A 243      448    923    911    -26     35   -117       N  
ATOM    607  CA  ALA A 243     -11.171   8.875 -14.445  1.00  6.52           C  
ANISOU  607  CA  ALA A 243      467   1005   1006    -76     -9    -88       C  
ATOM    608  C   ALA A 243     -11.782   9.606 -13.246  1.00  6.51           C  
ANISOU  608  C   ALA A 243      526    942   1004   -111     55   -157       C  
ATOM    609  O   ALA A 243     -11.203   9.722 -12.168  1.00  6.92           O  
ANISOU  609  O   ALA A 243      536   1067   1025     11     40   -221       O  
ATOM    610  CB  ALA A 243     -11.948   7.572 -14.707  1.00  7.07           C  
ANISOU  610  CB  ALA A 243      549   1002   1137   -113      9   -216       C  
ATOM    611  H   ALA A 243      -9.658   7.768 -13.912  1.00  7.21           H  
ATOM    612  HA  ALA A 243     -11.245   9.478 -15.201  1.00  7.84           H  
ATOM    613  HB1 ALA A 243     -12.883   7.785 -14.851  1.00  8.50           H  
ATOM    614  HB2 ALA A 243     -11.582   7.139 -15.494  1.00  8.50           H  
ATOM    615  HB3 ALA A 243     -11.857   6.989 -13.937  1.00  8.50           H  
ATOM    616  N   ASN A 244     -13.009  10.057 -13.462  1.00  7.09           N  
ANISOU  616  N   ASN A 244      424   1215   1057     34     31   -161       N  
ATOM    617  CA  ASN A 244     -13.864  10.563 -12.405  1.00  7.36           C  
ANISOU  617  CA  ASN A 244      562   1080   1156      7    143   -172       C  
ATOM    618  C   ASN A 244     -15.163   9.754 -12.398  1.00  7.41           C  
ANISOU  618  C   ASN A 244      542   1013   1262     13     71   -180       C  
ATOM    619  O   ASN A 244     -15.417   8.943 -13.292  1.00  7.43           O  
ANISOU  619  O   ASN A 244      540   1056   1227     -2     25   -228       O  
ATOM    620  CB  ASN A 244     -14.089  12.078 -12.537  1.00  8.09           C  
ANISOU  620  CB  ASN A 244      695   1120   1259    -91     36   -189       C  
ATOM    621  CG  ASN A 244     -14.608  12.481 -13.882  1.00  9.34           C  
ANISOU  621  CG  ASN A 244      925   1198   1427   -118    -68   -119       C  
ATOM    622  OD1 ASN A 244     -15.649  12.018 -14.312  1.00 13.19           O  
ANISOU  622  OD1 ASN A 244     1756   1669   1585   -546   -467    157       O  
ATOM    623  ND2 ASN A 244     -13.959  13.410 -14.516  1.00 13.24           N  
ANISOU  623  ND2 ASN A 244     1553   1787   1691   -542   -154    286       N  
ATOM    624  H   ASN A 244     -13.378  10.079 -14.238  1.00  8.52           H  
ATOM    625  HA  ASN A 244     -13.449  10.442 -11.537  1.00  8.84           H  
ATOM    626  HB2 ASN A 244     -14.736  12.359 -11.871  1.00  9.72           H  
ATOM    627  HB3 ASN A 244     -13.245  12.535 -12.393  1.00  9.72           H  
ATOM    628 HD21 ASN A 244     -14.227  13.669 -15.291  1.00 15.89           H  
ATOM    629 HD22 ASN A 244     -13.262  13.767 -14.160  1.00 15.89           H  
ATOM    630  N   VAL A 245     -15.988   9.966 -11.367  1.00  7.96           N  
ANISOU  630  N   VAL A 245      550   1123   1350    -24    247   -155       N  
ATOM    631  CA  VAL A 245     -17.090   9.031 -11.124  1.00  8.75           C  
ANISOU  631  CA  VAL A 245      659   1211   1456   -121    166   -156       C  
ATOM    632  C   VAL A 245     -18.145   9.020 -12.225  1.00  8.42           C  
ANISOU  632  C   VAL A 245      525   1128   1547     14    117   -175       C  
ATOM    633  O   VAL A 245     -18.804   7.991 -12.413  1.00  9.51           O  
ANISOU  633  O   VAL A 245      723   1236   1654   -125     13    -64       O  
ATOM    634  CB  VAL A 245     -17.747   9.221  -9.740  1.00  9.32           C  
ANISOU  634  CB  VAL A 245      652   1444   1446   -114    276   -139       C  
ATOM    635  CG1 VAL A 245     -16.794   8.837  -8.627  1.00  9.82           C  
ANISOU  635  CG1 VAL A 245      699   1593   1440   -129    180   -128       C  
ATOM    636  CG2 VAL A 245     -18.293  10.639  -9.576  1.00 10.55           C  
ANISOU  636  CG2 VAL A 245      839   1694   1477    132    265   -156       C  
ATOM    637  H   VAL A 245     -15.933  10.621 -10.812  1.00  9.56           H  
ATOM    638  HA  VAL A 245     -16.661   8.161 -11.131  1.00 10.51           H  
ATOM    639  HB  VAL A 245     -18.507   8.622  -9.674  1.00 11.20           H  
ATOM    640 HG11 VAL A 245     -17.246   8.941  -7.775  1.00 11.79           H  
ATOM    641 HG12 VAL A 245     -16.523   7.914  -8.747  1.00 11.79           H  
ATOM    642 HG13 VAL A 245     -16.017   9.417  -8.663  1.00 11.79           H  
ATOM    643 HG21 VAL A 245     -18.721  10.715  -8.708  1.00 12.67           H  
ATOM    644 HG22 VAL A 245     -17.559  11.270  -9.639  1.00 12.67           H  
ATOM    645 HG23 VAL A 245     -18.939  10.812 -10.279  1.00 12.67           H  
ATOM    646  N   TYR A 246     -18.342  10.124 -12.952  1.00  8.55           N  
ANISOU  646  N   TYR A 246      572   1111   1567     58     83   -202       N  
ATOM    647  CA  TYR A 246     -19.274  10.157 -14.070  1.00  8.54           C  
ANISOU  647  CA  TYR A 246      443   1150   1653     46     -8   -146       C  
ATOM    648  C   TYR A 246     -18.588   9.952 -15.412  1.00  8.06           C  
ANISOU  648  C   TYR A 246      452   1091   1520    -14   -114    -63       C  
ATOM    649  O   TYR A 246     -19.219  10.118 -16.461  1.00  8.73           O  
ANISOU  649  O   TYR A 246      542   1140   1634     -3   -136   -114       O  
ATOM    650  CB  TYR A 246     -20.140  11.432 -14.061  1.00  9.88           C  
ANISOU  650  CB  TYR A 246      618   1219   1917    137    -82   -330       C  
ATOM    651  CG  TYR A 246     -21.240  11.373 -13.033  1.00 10.61           C  
ANISOU  651  CG  TYR A 246      581   1496   1954    138    -61   -456       C  
ATOM    652  CD1 TYR A 246     -22.428  10.719 -13.305  1.00 10.66           C  
ANISOU  652  CD1 TYR A 246      597   1529   1925     95     -5   -482       C  
ATOM    653  CD2 TYR A 246     -21.091  11.946 -11.781  1.00 11.58           C  
ANISOU  653  CD2 TYR A 246      699   1744   1956     24    -62   -703       C  
ATOM    654  CE1 TYR A 246     -23.445  10.650 -12.366  1.00 11.26           C  
ANISOU  654  CE1 TYR A 246      698   1666   1914     55   -102   -478       C  
ATOM    655  CE2 TYR A 246     -22.109  11.886 -10.841  1.00 11.90           C  
ANISOU  655  CE2 TYR A 246      822   1774   1925     23      6   -705       C  
ATOM    656  CZ  TYR A 246     -23.277  11.235 -11.141  1.00 11.45           C  
ANISOU  656  CZ  TYR A 246      685   1779   1887    139    -28   -599       C  
ATOM    657  OH  TYR A 246     -24.273  11.164 -10.200  1.00 12.77           O  
ANISOU  657  OH  TYR A 246      827   2106   1918    -12    184   -658       O  
ATOM    658  H   TYR A 246     -17.940  10.871 -12.812  1.00 10.27           H  
ATOM    659  HA  TYR A 246     -19.899   9.425 -13.955  1.00 10.26           H  
ATOM    660  HB2 TYR A 246     -19.577  12.196 -13.857  1.00 11.87           H  
ATOM    661  HB3 TYR A 246     -20.548  11.544 -14.934  1.00 11.87           H  
ATOM    662  HD1 TYR A 246     -22.546  10.316 -14.135  1.00 12.80           H  
ATOM    663  HD2 TYR A 246     -20.296  12.378 -11.568  1.00 13.90           H  
ATOM    664  HE1 TYR A 246     -24.238  10.209 -12.568  1.00 13.52           H  
ATOM    665  HE2 TYR A 246     -21.999  12.287 -10.009  1.00 14.29           H  
ATOM    666  HH  TYR A 246     -24.919  10.718 -10.499  1.00 15.33           H  
ATOM    667  N   LEU A 247     -17.308   9.575 -15.404  1.00  7.54           N  
ANISOU  667  N   LEU A 247      446   1097   1322     10    -28    -69       N  
ATOM    668  CA  LEU A 247     -16.594   9.300 -16.646  1.00  7.39           C  
ANISOU  668  CA  LEU A 247      430   1074   1302     27   -148    -78       C  
ATOM    669  C   LEU A 247     -16.689  10.451 -17.628  1.00  7.60           C  
ANISOU  669  C   LEU A 247      494   1086   1307     63   -171   -105       C  
ATOM    670  O   LEU A 247     -16.886  10.255 -18.823  1.00  8.74           O  
ANISOU  670  O   LEU A 247      879   1104   1336     49   -134    -18       O  
ATOM    671  CB  LEU A 247     -17.002   7.977 -17.298  1.00  7.32           C  
ANISOU  671  CB  LEU A 247      482   1026   1274    -44   -107   -134       C  
ATOM    672  CG  LEU A 247     -16.843   6.723 -16.445  1.00  7.75           C  
ANISOU  672  CG  LEU A 247      525   1061   1357    -58    -87   -118       C  
ATOM    673  CD1 LEU A 247     -17.315   5.521 -17.228  1.00  8.56           C  
ANISOU  673  CD1 LEU A 247      595   1121   1537     40   -116   -110       C  
ATOM    674  CD2 LEU A 247     -15.426   6.520 -15.963  1.00  7.48           C  
ANISOU  674  CD2 LEU A 247      512   1004   1326     -1     27    -66       C  
ATOM    675  H   LEU A 247     -16.835   9.473 -14.692  1.00  9.06           H  
ATOM    676  HA  LEU A 247     -15.660   9.206 -16.401  1.00  8.87           H  
ATOM    677  HB2 LEU A 247     -17.938   8.039 -17.544  1.00  8.80           H  
ATOM    678  HB3 LEU A 247     -16.459   7.853 -18.092  1.00  8.80           H  
ATOM    679  HG  LEU A 247     -17.386   6.827 -15.647  1.00  9.30           H  
ATOM    680 HD11 LEU A 247     -17.233   4.730 -16.673  1.00 10.28           H  
ATOM    681 HD12 LEU A 247     -18.242   5.653 -17.482  1.00 10.28           H  
ATOM    682 HD13 LEU A 247     -16.765   5.426 -18.022  1.00 10.28           H  
ATOM    683 HD21 LEU A 247     -15.363   5.659 -15.520  1.00  8.98           H  
ATOM    684 HD22 LEU A 247     -14.827   6.544 -16.726  1.00  8.98           H  
ATOM    685 HD23 LEU A 247     -15.199   7.229 -15.341  1.00  8.98           H  
ATOM    686  N   LYS A 248     -16.503  11.673 -17.127  1.00  7.94           N  
ANISOU  686  N   LYS A 248      557   1079   1382     -2    -77   -123       N  
ATOM    687  CA  LYS A 248     -16.481  12.875 -17.961  1.00  8.64           C  
ANISOU  687  CA  LYS A 248      739   1017   1526     83     -6    -38       C  
ATOM    688  C   LYS A 248     -15.020  13.156 -18.258  1.00  8.01           C  
ANISOU  688  C   LYS A 248      632   1006   1405     34   -140    -41       C  
ATOM    689  O   LYS A 248     -14.265  13.596 -17.390  1.00  9.09           O  
ANISOU  689  O   LYS A 248      841   1187   1426   -174   -161    -24       O  
ATOM    690  CB  LYS A 248     -17.190  14.029 -17.264  1.00 11.32           C  
ANISOU  690  CB  LYS A 248     1064   1116   2120    222    347     -2       C  
ATOM    691  CG  LYS A 248     -18.685  13.761 -17.151  1.00 16.75           C  
ANISOU  691  CG  LYS A 248     1689   1715   2960    474    730    231       C  
ATOM    692  CD  LYS A 248     -19.460  14.873 -16.482  1.00 25.02           C  
ANISOU  692  CD  LYS A 248     2958   2856   3691    271    678    564       C  
ATOM    693  CE  LYS A 248     -20.975  14.667 -16.645  1.00 30.63           C  
ANISOU  693  CE  LYS A 248     3770   3725   4142    244    617    878       C  
ATOM    694  NZ  LYS A 248     -21.664  14.146 -15.424  1.00 34.13           N  
ANISOU  694  NZ  LYS A 248     4387   4213   4367    296    518   1019       N  
ATOM    695  H   LYS A 248     -16.386  11.833 -16.290  1.00  9.54           H  
ATOM    696  HA  LYS A 248     -16.944  12.730 -18.801  1.00 10.37           H  
ATOM    697  HB2 LYS A 248     -16.828  14.138 -16.371  1.00 13.59           H  
ATOM    698  HB3 LYS A 248     -17.061  14.843 -17.775  1.00 13.59           H  
ATOM    699  HG2 LYS A 248     -19.048  13.644 -18.043  1.00 20.11           H  
ATOM    700  HG3 LYS A 248     -18.818  12.954 -16.630  1.00 20.11           H  
ATOM    701  HD2 LYS A 248     -19.253  14.886 -15.535  1.00 30.03           H  
ATOM    702  HD3 LYS A 248     -19.221  15.722 -16.886  1.00 30.03           H  
ATOM    703  HE2 LYS A 248     -21.381  15.519 -16.869  1.00 36.76           H  
ATOM    704  HE3 LYS A 248     -21.126  14.029 -17.360  1.00 36.76           H  
ATOM    705  HZ1 LYS A 248     -21.196  13.475 -15.074  1.00 40.96           H  
ATOM    706  HZ2 LYS A 248     -21.738  14.794 -14.817  1.00 40.96           H  
ATOM    707  HZ3 LYS A 248     -22.477  13.853 -15.634  1.00 40.96           H  
ATOM    708  N   HIS A 249     -14.605  12.855 -19.484  1.00  7.96           N  
ANISOU  708  N   HIS A 249      544   1055   1425    -13   -173     91       N  
ATOM    709  CA  HIS A 249     -13.183  12.824 -19.819  1.00  8.50           C  
ANISOU  709  CA  HIS A 249      627   1139   1464     43   -170    220       C  
ATOM    710  C   HIS A 249     -12.721  14.167 -20.360  1.00  9.67           C  
ANISOU  710  C   HIS A 249      762   1267   1645     22   -126    373       C  
ATOM    711  O   HIS A 249     -12.479  14.353 -21.554  1.00 12.20           O  
ANISOU  711  O   HIS A 249     1334   1500   1802     57     10    465       O  
ATOM    712  CB  HIS A 249     -12.910  11.736 -20.836  1.00  8.49           C  
ANISOU  712  CB  HIS A 249      646   1223   1356    216    -70    204       C  
ATOM    713  CG  HIS A 249     -13.406  10.403 -20.405  1.00  7.84           C  
ANISOU  713  CG  HIS A 249      534   1212   1233    180    -88     40       C  
ATOM    714  ND1 HIS A 249     -13.064   9.838 -19.191  1.00  7.94           N  
ANISOU  714  ND1 HIS A 249      592   1148   1276     81   -125    -31       N  
ATOM    715  CD2 HIS A 249     -14.221   9.527 -21.038  1.00  8.20           C  
ANISOU  715  CD2 HIS A 249      577   1330   1209    133   -202    -69       C  
ATOM    716  CE1 HIS A 249     -13.675   8.665 -19.107  1.00  7.45           C  
ANISOU  716  CE1 HIS A 249      426   1124   1281     55   -122    -68       C  
ATOM    717  NE2 HIS A 249     -14.363   8.447 -20.215  1.00  7.70           N  
ANISOU  717  NE2 HIS A 249      441   1179   1306    122   -124   -137       N  
ATOM    718  H   HIS A 249     -15.127  12.664 -20.140  1.00  9.56           H  
ATOM    719  HA  HIS A 249     -12.697  12.642 -18.999  1.00 10.21           H  
ATOM    720  HB2 HIS A 249     -13.352  11.965 -21.669  1.00 10.20           H  
ATOM    721  HB3 HIS A 249     -11.952  11.669 -20.976  1.00 10.20           H  
ATOM    722  HD2 HIS A 249     -14.610   9.640 -21.875  1.00  9.85           H  
ATOM    723  HE1 HIS A 249     -13.627   8.085 -18.382  1.00  8.95           H  
ATOM    724  HE2 HIS A 249     -14.824   7.742 -20.388  1.00  9.25           H  
ATOM    725  N   GLY A 250     -12.596  15.111 -19.443  1.00 10.24           N  
ANISOU  725  N   GLY A 250      941   1222   1727   -178   -233    335       N  
ATOM    726  CA  GLY A 250     -12.093  16.415 -19.788  1.00 11.69           C  
ANISOU  726  CA  GLY A 250     1146   1535   1759   -239   -400    250       C  
ATOM    727  C   GLY A 250     -10.805  16.652 -19.036  1.00 10.67           C  
ANISOU  727  C   GLY A 250     1135   1508   1412     -5   -191     66       C  
ATOM    728  O   GLY A 250     -10.768  16.427 -17.823  1.00 12.79           O  
ANISOU  728  O   GLY A 250     1219   2130   1510    447     93    199       O  
ATOM    729  H   GLY A 250     -12.798  15.015 -18.612  1.00 12.30           H  
ATOM    730  HA2 GLY A 250     -11.922  16.467 -20.742  1.00 14.03           H  
ATOM    731  HA3 GLY A 250     -12.737  17.098 -19.545  1.00 14.03           H  
ATOM    732  N   GLY A 251      -9.800  17.122 -19.740  1.00  9.48           N  
ANISOU  732  N   GLY A 251     1107   1146   1348     74   -112   -193       N  
ATOM    733  CA  GLY A 251      -8.579  17.505 -19.124  1.00  9.29           C  
ANISOU  733  CA  GLY A 251     1034   1120   1377    152    -86   -220       C  
ATOM    734  C   GLY A 251      -7.706  16.327 -18.760  1.00  7.73           C  
ANISOU  734  C   GLY A 251     1019    905   1014    161   -105   -196       C  
ATOM    735  O   GLY A 251      -8.153  15.183 -18.580  1.00  7.71           O  
ANISOU  735  O   GLY A 251     1002    886   1040    -40   -178   -194       O  
ATOM    736  H   GLY A 251      -9.812  17.227 -20.594  1.00 11.38           H  
ATOM    737  HA2 GLY A 251      -8.081  18.075 -19.731  1.00 11.16           H  
ATOM    738  HA3 GLY A 251      -8.773  18.001 -18.313  1.00 11.16           H  
ATOM    739  N   GLY A 252      -6.434  16.638 -18.632  1.00  7.04           N  
ANISOU  739  N   GLY A 252      838    874    962    -82    -71   -170       N  
ATOM    740  CA  GLY A 252      -5.504  15.659 -18.172  1.00  7.37           C  
ANISOU  740  CA  GLY A 252      984    904    911    -86   -171    -37       C  
ATOM    741  C   GLY A 252      -5.459  14.440 -19.065  1.00  6.33           C  
ANISOU  741  C   GLY A 252      654    920    832   -118   -186    -52       C  
ATOM    742  O   GLY A 252      -5.762  14.480 -20.255  1.00  6.70           O  
ANISOU  742  O   GLY A 252      785    908    854    -32   -164    -38       O  
ATOM    743  H   GLY A 252      -6.093  17.408 -18.806  1.00  8.46           H  
ATOM    744  HA2 GLY A 252      -4.616  16.049 -18.143  1.00  8.85           H  
ATOM    745  HA3 GLY A 252      -5.754  15.374 -17.279  1.00  8.85           H  
ATOM    746  N   VAL A 253      -5.048  13.334 -18.449  1.00  6.06           N  
ANISOU  746  N   VAL A 253      597    912    795    -99   -158    -21       N  
ATOM    747  CA  VAL A 253      -4.965  12.060 -19.147  1.00  5.95           C  
ANISOU  747  CA  VAL A 253      583    860    818    -12    -92    -23       C  
ATOM    748  C   VAL A 253      -6.315  11.694 -19.751  1.00  5.78           C  
ANISOU  748  C   VAL A 253      627    744    824     50   -132    -31       C  
ATOM    749  O   VAL A 253      -6.372  11.211 -20.881  1.00  6.15           O  
ANISOU  749  O   VAL A 253      620    893    824     85   -103    -51       O  
ATOM    750  CB  VAL A 253      -4.440  10.979 -18.182  1.00  6.75           C  
ANISOU  750  CB  VAL A 253      613   1021    932     73   -145    -53       C  
ATOM    751  CG1 VAL A 253      -4.683   9.571 -18.713  1.00  7.59           C  
ANISOU  751  CG1 VAL A 253      792   1034   1057    115   -168     28       C  
ATOM    752  CG2 VAL A 253      -2.976  11.186 -17.902  1.00  8.22           C  
ANISOU  752  CG2 VAL A 253      745   1247   1129    146   -198     40       C  
ATOM    753  H   VAL A 253      -4.811  13.296 -17.623  1.00  7.29           H  
ATOM    754  HA  VAL A 253      -4.337  12.136 -19.882  1.00  7.15           H  
ATOM    755  HB  VAL A 253      -4.933  11.064 -17.351  1.00  8.11           H  
ATOM    756 HG11 VAL A 253      -4.159   8.942 -18.192  1.00  9.11           H  
ATOM    757 HG12 VAL A 253      -5.627   9.361 -18.631  1.00  9.11           H  
ATOM    758 HG13 VAL A 253      -4.415   9.533 -19.644  1.00  9.11           H  
ATOM    759 HG21 VAL A 253      -2.680  10.520 -17.262  1.00  9.87           H  
ATOM    760 HG22 VAL A 253      -2.480  11.092 -18.731  1.00  9.87           H  
ATOM    761 HG23 VAL A 253      -2.847  12.076 -17.538  1.00  9.87           H  
ATOM    762  N   ALA A 254      -7.408  11.852 -19.009  1.00  5.62           N  
ANISOU  762  N   ALA A 254      501    838    797     18    -92    -98       N  
ATOM    763  CA  ALA A 254      -8.704  11.430 -19.524  1.00  6.07           C  
ANISOU  763  CA  ALA A 254      538    882    886    -10    -90    -79       C  
ATOM    764  C   ALA A 254      -9.047  12.171 -20.814  1.00  6.25           C  
ANISOU  764  C   ALA A 254      577    905    894     -9    -99   -127       C  
ATOM    765  O   ALA A 254      -9.493  11.572 -21.797  1.00  6.46           O  
ANISOU  765  O   ALA A 254      616    946    894    -11   -197   -113       O  
ATOM    766  CB  ALA A 254      -9.785  11.631 -18.476  1.00  6.28           C  
ANISOU  766  CB  ALA A 254      546    917    924    -33    -72   -119       C  
ATOM    767  H   ALA A 254      -7.426  12.194 -18.220  1.00  6.76           H  
ATOM    768  HA  ALA A 254      -8.665  10.481 -19.723  1.00  7.29           H  
ATOM    769  HB1 ALA A 254     -10.635  11.334 -18.838  1.00  7.55           H  
ATOM    770  HB2 ALA A 254      -9.561  11.111 -17.688  1.00  7.55           H  
ATOM    771  HB3 ALA A 254      -9.833  12.572 -18.248  1.00  7.55           H  
ATOM    772  N   GLY A 255      -8.870  13.494 -20.812  1.00  6.29           N  
ANISOU  772  N   GLY A 255      648    832    911     51   -149   -127       N  
ATOM    773  CA  GLY A 255      -9.161  14.256 -22.012  1.00  6.55           C  
ANISOU  773  CA  GLY A 255      734    809    945     72   -166    -63       C  
ATOM    774  C   GLY A 255      -8.264  13.867 -23.172  1.00  6.56           C  
ANISOU  774  C   GLY A 255      762    766    964      8   -184    -16       C  
ATOM    775  O   GLY A 255      -8.692  13.846 -24.333  1.00  7.36           O  
ANISOU  775  O   GLY A 255      861   1005    928     39   -254    -26       O  
ATOM    776  H   GLY A 255      -8.590  13.957 -20.144  1.00  7.56           H  
ATOM    777  HA2 GLY A 255     -10.083  14.104 -22.273  1.00  7.87           H  
ATOM    778  HA3 GLY A 255      -9.036  15.201 -21.831  1.00  7.87           H  
ATOM    779  N   ALA A 256      -6.995  13.592 -22.871  1.00  6.33           N  
ANISOU  779  N   ALA A 256      710    828    868     -5   -140    -49       N  
ATOM    780  CA  ALA A 256      -6.038  13.241 -23.910  1.00  6.41           C  
ANISOU  780  CA  ALA A 256      708    876    850    -58    -77    -46       C  
ATOM    781  C   ALA A 256      -6.347  11.861 -24.499  1.00  6.38           C  
ANISOU  781  C   ALA A 256      699    895    829      8   -158    -42       C  
ATOM    782  O   ALA A 256      -6.312  11.684 -25.720  1.00  6.77           O  
ANISOU  782  O   ALA A 256      841    916    815     13   -127    -47       O  
ATOM    783  CB  ALA A 256      -4.629  13.273 -23.331  1.00  7.15           C  
ANISOU  783  CB  ALA A 256      726    973   1017    -66    -63   -174       C  
ATOM    784  H   ALA A 256      -6.667  13.603 -22.076  1.00  7.61           H  
ATOM    785  HA  ALA A 256      -6.090  13.891 -24.628  1.00  7.70           H  
ATOM    786  HB1 ALA A 256      -3.996  13.038 -24.028  1.00  8.59           H  
ATOM    787  HB2 ALA A 256      -4.443  14.167 -23.003  1.00  8.59           H  
ATOM    788  HB3 ALA A 256      -4.572  12.634 -22.603  1.00  8.59           H  
ATOM    789  N   LEU A 257      -6.635  10.875 -23.650  1.00  6.34           N  
ANISOU  789  N   LEU A 257      711    875    821     12   -161   -127       N  
ATOM    790  CA  LEU A 257      -7.038   9.564 -24.155  1.00  6.19           C  
ANISOU  790  CA  LEU A 257      675    871    805     -6   -137   -162       C  
ATOM    791  C   LEU A 257      -8.290   9.701 -24.992  1.00  6.49           C  
ANISOU  791  C   LEU A 257      765    878    822    -30   -104   -127       C  
ATOM    792  O   LEU A 257      -8.375   9.163 -26.099  1.00  7.29           O  
ANISOU  792  O   LEU A 257      832   1003    935      4   -216   -127       O  
ATOM    793  CB  LEU A 257      -7.271   8.581 -23.005  1.00  6.70           C  
ANISOU  793  CB  LEU A 257      766    888    893      5   -137   -116       C  
ATOM    794  CG  LEU A 257      -6.055   8.158 -22.181  1.00  7.04           C  
ANISOU  794  CG  LEU A 257      814    897    965     53   -173    -65       C  
ATOM    795  CD1 LEU A 257      -6.513   7.345 -20.998  1.00  7.87           C  
ANISOU  795  CD1 LEU A 257     1031   1030    928     50     -4     -3       C  
ATOM    796  CD2 LEU A 257      -5.047   7.366 -23.004  1.00  8.28           C  
ANISOU  796  CD2 LEU A 257     1010   1040   1096    111    -44     75       C  
ATOM    797  H   LEU A 257      -6.606  10.937 -22.793  1.00  7.61           H  
ATOM    798  HA  LEU A 257      -6.321   9.202 -24.699  1.00  7.43           H  
ATOM    799  HB2 LEU A 257      -7.899   8.989 -22.389  1.00  8.05           H  
ATOM    800  HB3 LEU A 257      -7.652   7.771 -23.379  1.00  8.05           H  
ATOM    801  HG  LEU A 257      -5.599   8.957 -21.875  1.00  8.46           H  
ATOM    802 HD11 LEU A 257      -5.739   7.092 -20.470  1.00  9.45           H  
ATOM    803 HD12 LEU A 257      -7.118   7.880 -20.461  1.00  9.45           H  
ATOM    804 HD13 LEU A 257      -6.969   6.551 -21.317  1.00  9.45           H  
ATOM    805 HD21 LEU A 257      -4.302   7.116 -22.436  1.00  9.94           H  
ATOM    806 HD22 LEU A 257      -5.480   6.570 -23.352  1.00  9.94           H  
ATOM    807 HD23 LEU A 257      -4.734   7.918 -23.737  1.00  9.94           H  
ATOM    808  N   ASN A 258      -9.286  10.425 -24.474  1.00  6.53           N  
ANISOU  808  N   ASN A 258      658    955    869    -10   -161   -170       N  
ATOM    809  CA  ASN A 258     -10.534  10.524 -25.202  1.00  7.10           C  
ANISOU  809  CA  ASN A 258      694   1080    924    -10   -216   -131       C  
ATOM    810  C   ASN A 258     -10.322  11.182 -26.557  1.00  7.33           C  
ANISOU  810  C   ASN A 258      760   1104    920     90   -227   -114       C  
ATOM    811  O   ASN A 258     -10.865  10.721 -27.568  1.00  8.11           O  
ANISOU  811  O   ASN A 258      881   1200   1002      2   -317   -133       O  
ATOM    812  CB  ASN A 258     -11.577  11.288 -24.396  1.00  7.47           C  
ANISOU  812  CB  ASN A 258      705   1137    996    -10   -166   -143       C  
ATOM    813  CG  ASN A 258     -12.860  11.416 -25.160  1.00  8.40           C  
ANISOU  813  CG  ASN A 258      850   1150   1192     40   -231    -98       C  
ATOM    814  OD1 ASN A 258     -13.445  10.417 -25.578  1.00  8.29           O  
ANISOU  814  OD1 ASN A 258      716   1210   1222     57   -316    -92       O  
ATOM    815  ND2 ASN A 258     -13.279  12.637 -25.409  1.00  9.85           N  
ANISOU  815  ND2 ASN A 258     1072   1205   1467    106   -389    -90       N  
ATOM    816  H   ASN A 258      -9.258  10.851 -23.728  1.00  7.85           H  
ATOM    817  HA  ASN A 258     -10.878   9.628 -25.342  1.00  8.53           H  
ATOM    818  HB2 ASN A 258     -11.758  10.813 -23.569  1.00  8.97           H  
ATOM    819  HB3 ASN A 258     -11.245  12.179 -24.201  1.00  8.97           H  
ATOM    820 HD21 ASN A 258     -14.010  12.760 -25.844  1.00 11.83           H  
ATOM    821 HD22 ASN A 258     -12.821  13.312 -25.137  1.00 11.83           H  
ATOM    822  N   LYS A 259      -9.543  12.269 -26.605  1.00  7.62           N  
ANISOU  822  N   LYS A 259      857   1113    925     18   -225    -29       N  
ATOM    823  CA  LYS A 259      -9.293  12.941 -27.873  1.00  8.23           C  
ANISOU  823  CA  LYS A 259     1012   1150    966     28   -248      0       C  
ATOM    824  C   LYS A 259      -8.653  11.994 -28.866  1.00  8.24           C  
ANISOU  824  C   LYS A 259     1018   1211    901    -98   -192     59       C  
ATOM    825  O   LYS A 259      -8.989  11.998 -30.055  1.00  8.88           O  
ANISOU  825  O   LYS A 259     1250   1282    841    -71   -222     63       O  
ATOM    826  CB  LYS A 259      -8.411  14.172 -27.646  1.00  9.84           C  
ANISOU  826  CB  LYS A 259     1386   1227   1125    -77   -256    137       C  
ATOM    827  CG  LYS A 259      -8.084  14.930 -28.904  1.00 14.01           C  
ANISOU  827  CG  LYS A 259     2128   1636   1560   -394   -464    332       C  
ATOM    828  CD  LYS A 259      -7.165  16.107 -28.625  1.00 20.82           C  
ANISOU  828  CD  LYS A 259     3340   2434   2136   -275   -303    499       C  
ATOM    829  CE  LYS A 259      -7.084  17.044 -29.806  1.00 27.03           C  
ANISOU  829  CE  LYS A 259     4399   3283   2589    114   -242    634       C  
ATOM    830  NZ  LYS A 259      -8.406  17.672 -30.078  1.00 30.54           N  
ANISOU  830  NZ  LYS A 259     4983   3774   2848    364   -265    732       N  
ATOM    831  H   LYS A 259      -9.155  12.627 -25.926  1.00  9.15           H  
ATOM    832  HA  LYS A 259     -10.136  13.244 -28.246  1.00  9.89           H  
ATOM    833  HB2 LYS A 259      -8.873  14.780 -27.047  1.00 11.81           H  
ATOM    834  HB3 LYS A 259      -7.575  13.886 -27.247  1.00 11.81           H  
ATOM    835  HG2 LYS A 259      -7.637  14.337 -29.529  1.00 16.82           H  
ATOM    836  HG3 LYS A 259      -8.903  15.270 -29.297  1.00 16.82           H  
ATOM    837  HD2 LYS A 259      -7.504  16.604 -27.864  1.00 24.99           H  
ATOM    838  HD3 LYS A 259      -6.272  15.778 -28.436  1.00 24.99           H  
ATOM    839  HE2 LYS A 259      -6.443  17.747 -29.617  1.00 32.45           H  
ATOM    840  HE3 LYS A 259      -6.811  16.549 -30.594  1.00 32.45           H  
ATOM    841  HZ1 LYS A 259      -8.741  18.013 -29.327  1.00 36.66           H  
ATOM    842  HZ2 LYS A 259      -8.316  18.324 -30.677  1.00 36.66           H  
ATOM    843  HZ3 LYS A 259      -8.972  17.064 -30.397  1.00 36.66           H  
ATOM    844  N   ALA A 260      -7.709  11.177 -28.401  1.00  7.87           N  
ANISOU  844  N   ALA A 260      986   1167    839    -33   -216     30       N  
ATOM    845  CA  ALA A 260      -7.024  10.250 -29.290  1.00  8.33           C  
ANISOU  845  CA  ALA A 260     1006   1271    887    -29   -107    -26       C  
ATOM    846  C   ALA A 260      -7.957   9.170 -29.830  1.00  8.75           C  
ANISOU  846  C   ALA A 260     1116   1310    900     19   -161   -133       C  
ATOM    847  O   ALA A 260      -7.641   8.567 -30.859  1.00 10.72           O  
ANISOU  847  O   ALA A 260     1339   1598   1137   -182     87   -354       O  
ATOM    848  CB  ALA A 260      -5.824   9.638 -28.563  1.00  9.42           C  
ANISOU  848  CB  ALA A 260     1100   1506    972     86   -113    -84       C  
ATOM    849  H   ALA A 260      -7.450  11.142 -27.581  1.00  9.46           H  
ATOM    850  HA  ALA A 260      -6.682  10.731 -30.059  1.00 10.00           H  
ATOM    851  HB1 ALA A 260      -5.376   9.019 -29.160  1.00 11.31           H  
ATOM    852  HB2 ALA A 260      -5.216  10.348 -28.305  1.00 11.31           H  
ATOM    853  HB3 ALA A 260      -6.138   9.169 -27.774  1.00 11.31           H  
ATOM    854  N   THR A 261      -9.105   8.935 -29.182  1.00  8.14           N  
ANISOU  854  N   THR A 261      954   1263    875    -54    -98   -180       N  
ATOM    855  CA  THR A 261     -10.127   8.014 -29.676  1.00  8.72           C  
ANISOU  855  CA  THR A 261      998   1346    970    -86   -145   -214       C  
ATOM    856  C   THR A 261     -11.188   8.727 -30.513  1.00  9.40           C  
ANISOU  856  C   THR A 261     1152   1491    928   -118   -187   -186       C  
ATOM    857  O   THR A 261     -12.211   8.118 -30.855  1.00 10.53           O  
ANISOU  857  O   THR A 261     1232   1728   1041   -158   -362   -233       O  
ATOM    858  CB  THR A 261     -10.828   7.243 -28.542  1.00  8.72           C  
ANISOU  858  CB  THR A 261     1030   1328    954   -137   -173   -275       C  
ATOM    859  OG1 THR A 261     -11.762   8.079 -27.839  1.00  8.67           O  
ANISOU  859  OG1 THR A 261      941   1273   1081    -88   -173   -254       O  
ATOM    860  CG2 THR A 261      -9.847   6.600 -27.609  1.00  8.69           C  
ANISOU  860  CG2 THR A 261      952   1349    999   -124    -96   -264       C  
ATOM    861  H   THR A 261      -9.316   9.307 -28.436  1.00  9.77           H  
ATOM    862  HA  THR A 261      -9.669   7.353 -30.219  1.00 10.47           H  
ATOM    863  HB  THR A 261     -11.338   6.520 -28.940  1.00 10.47           H  
ATOM    864  HG1 THR A 261     -11.361   8.734 -27.498  1.00 10.42           H  
ATOM    865 HG21 THR A 261     -10.319   6.111 -26.917  1.00 10.43           H  
ATOM    866 HG22 THR A 261      -9.278   5.985 -28.098  1.00 10.43           H  
ATOM    867 HG23 THR A 261      -9.292   7.278 -27.193  1.00 10.43           H  
ATOM    868  N   ASN A 262     -10.988  10.002 -30.834  1.00  9.96           N  
ANISOU  868  N   ASN A 262     1241   1653    889    -96   -302    -47       N  
ATOM    869  CA  ASN A 262     -11.986  10.775 -31.572  1.00 10.76           C  
ANISOU  869  CA  ASN A 262     1380   1766    941    -23   -313     34       C  
ATOM    870  C   ASN A 262     -13.330  10.782 -30.857  1.00 10.55           C  
ANISOU  870  C   ASN A 262     1216   1717   1078     34   -395    -16       C  
ATOM    871  O   ASN A 262     -14.381  10.699 -31.486  1.00 11.69           O  
ANISOU  871  O   ASN A 262     1235   1980   1228     54   -567    -45       O  
ATOM    872  CB  ASN A 262     -12.141  10.256 -32.999  1.00 13.08           C  
ANISOU  872  CB  ASN A 262     1748   2129   1092    128   -417     35       C  
ATOM    873  CG  ASN A 262     -10.878  10.368 -33.790  1.00 16.99           C  
ANISOU  873  CG  ASN A 262     2452   2590   1414     58   -194    -94       C  
ATOM    874  OD1 ASN A 262     -10.092  11.292 -33.597  1.00 18.24           O  
ANISOU  874  OD1 ASN A 262     2486   2810   1635    -50     12    -61       O  
ATOM    875  ND2 ASN A 262     -10.667   9.427 -34.692  1.00 19.25           N  
ANISOU  875  ND2 ASN A 262     2889   2829   1595     11    150   -328       N  
ATOM    876  H   ASN A 262     -10.279  10.446 -30.635  1.00 11.96           H  
ATOM    877  HA  ASN A 262     -11.678  11.694 -31.616  1.00 12.92           H  
ATOM    878  HB2 ASN A 262     -12.396   9.321 -32.970  1.00 15.70           H  
ATOM    879  HB3 ASN A 262     -12.826  10.773 -33.452  1.00 15.70           H  
ATOM    880 HD21 ASN A 262     -11.241   8.796 -34.798  1.00 23.11           H  
ATOM    881 HD22 ASN A 262      -9.955   9.445 -35.174  1.00 23.11           H  
ATOM    882  N   ASN A 263     -13.298  10.888 -29.531  1.00  9.64           N  
ANISOU  882  N   ASN A 263     1230   1377   1056     27   -464    -28       N  
ATOM    883  CA  ASN A 263     -14.463  10.987 -28.671  1.00  9.59           C  
ANISOU  883  CA  ASN A 263     1050   1448   1145    121   -329    -56       C  
ATOM    884  C   ASN A 263     -15.212   9.668 -28.517  1.00  9.48           C  
ANISOU  884  C   ASN A 263     1021   1475   1107    107   -384   -114       C  
ATOM    885  O   ASN A 263     -16.233   9.636 -27.832  1.00  9.98           O  
ANISOU  885  O   ASN A 263      948   1568   1274    164   -359   -150       O  
ATOM    886  CB  ASN A 263     -15.430  12.098 -29.107  1.00 11.06           C  
ANISOU  886  CB  ASN A 263     1284   1516   1404    180   -487     35       C  
ATOM    887  CG  ASN A 263     -16.252  12.627 -27.964  1.00 11.88           C  
ANISOU  887  CG  ASN A 263     1300   1574   1640    270   -537    173       C  
ATOM    888  OD1 ASN A 263     -15.718  13.007 -26.924  1.00 11.92           O  
ANISOU  888  OD1 ASN A 263     1361   1563   1604    354   -553    105       O  
ATOM    889  ND2 ASN A 263     -17.557  12.689 -28.159  1.00 12.88           N  
ANISOU  889  ND2 ASN A 263     1215   1857   1822    378   -408    277       N  
ATOM    890  H   ASN A 263     -12.563  10.905 -29.086  1.00 11.58           H  
ATOM    891  HA  ASN A 263     -14.149  11.224 -27.784  1.00 11.52           H  
ATOM    892  HB2 ASN A 263     -14.920  12.836 -29.478  1.00 13.28           H  
ATOM    893  HB3 ASN A 263     -16.037  11.745 -29.776  1.00 13.28           H  
ATOM    894 HD21 ASN A 263     -18.072  12.984 -27.537  1.00 15.47           H  
ATOM    895 HD22 ASN A 263     -17.892  12.434 -28.909  1.00 15.47           H  
ATOM    896  N   ALA A 264     -14.722   8.571 -29.106  1.00  9.46           N  
ANISOU  896  N   ALA A 264      955   1551   1089     28   -328   -149       N  
ATOM    897  CA  ALA A 264     -15.419   7.296 -28.960  1.00  9.60           C  
ANISOU  897  CA  ALA A 264      959   1550   1140    -88   -290   -244       C  
ATOM    898  C   ALA A 264     -15.447   6.851 -27.510  1.00  8.95           C  
ANISOU  898  C   ALA A 264      884   1341   1176     51   -265   -234       C  
ATOM    899  O   ALA A 264     -16.422   6.244 -27.055  1.00  9.42           O  
ANISOU  899  O   ALA A 264      801   1481   1298    -88   -282   -264       O  
ATOM    900  CB  ALA A 264     -14.778   6.223 -29.838  1.00 10.65           C  
ANISOU  900  CB  ALA A 264     1183   1670   1195   -141   -264   -264       C  
ATOM    901  H   ALA A 264     -14.007   8.541 -29.582  1.00 11.36           H  
ATOM    902  HA  ALA A 264     -16.334   7.411 -29.262  1.00 11.53           H  
ATOM    903  HB1 ALA A 264     -15.257   5.388 -29.717  1.00 12.79           H  
ATOM    904  HB2 ALA A 264     -14.828   6.502 -30.765  1.00 12.79           H  
ATOM    905  HB3 ALA A 264     -13.851   6.113 -29.575  1.00 12.79           H  
ATOM    906  N   MET A 265     -14.370   7.125 -26.772  1.00  8.35           N  
ANISOU  906  N   MET A 265      718   1322   1132    -31   -273   -239       N  
ATOM    907  CA  MET A 265     -14.338   6.780 -25.354  1.00  7.82           C  
ANISOU  907  CA  MET A 265      726   1167   1077      6   -287   -197       C  
ATOM    908  C   MET A 265     -15.462   7.487 -24.594  1.00  7.76           C  
ANISOU  908  C   MET A 265      611   1185   1155     59   -312   -172       C  
ATOM    909  O   MET A 265     -16.133   6.872 -23.749  1.00  7.98           O  
ANISOU  909  O   MET A 265      605   1186   1243     -2   -194   -123       O  
ATOM    910  CB  MET A 265     -12.954   7.143 -24.801  1.00  7.85           C  
ANISOU  910  CB  MET A 265      767   1114   1099     36   -215   -167       C  
ATOM    911  CG  MET A 265     -12.828   6.901 -23.332  1.00  7.91           C  
ANISOU  911  CG  MET A 265      841   1142   1024    -51   -202    -59       C  
ATOM    912  SD  MET A 265     -11.176   7.293 -22.702  1.00  8.62           S  
ANISOU  912  SD  MET A 265      802   1351   1123   -175   -285     46       S  
ATOM    913  CE  MET A 265     -10.297   5.866 -23.311  1.00  9.54           C  
ANISOU  913  CE  MET A 265      879   1570   1174     -3   -236    182       C  
ATOM    914  H   MET A 265     -13.655   7.504 -27.064  1.00 10.03           H  
ATOM    915  HA  MET A 265     -14.466   5.826 -25.235  1.00  9.39           H  
ATOM    916  HB2 MET A 265     -12.284   6.605 -25.251  1.00  9.42           H  
ATOM    917  HB3 MET A 265     -12.787   8.085 -24.964  1.00  9.42           H  
ATOM    918  HG2 MET A 265     -13.469   7.458 -22.863  1.00  9.50           H  
ATOM    919  HG3 MET A 265     -13.005   5.965 -23.149  1.00  9.50           H  
ATOM    920  HE1 MET A 265      -9.375   5.912 -23.013  1.00 11.45           H  
ATOM    921  HE2 MET A 265     -10.717   5.064 -22.962  1.00 11.45           H  
ATOM    922  HE3 MET A 265     -10.332   5.863 -24.280  1.00 11.45           H  
ATOM    923  N   GLN A 266     -15.691   8.776 -24.879  1.00  8.15           N  
ANISOU  923  N   GLN A 266      706   1185   1206     12   -223   -167       N  
ATOM    924  CA  GLN A 266     -16.749   9.495 -24.172  1.00  8.34           C  
ANISOU  924  CA  GLN A 266      710   1249   1210    131   -204   -136       C  
ATOM    925  C   GLN A 266     -18.130   8.935 -24.503  1.00  8.23           C  
ANISOU  925  C   GLN A 266      717   1138   1273    108   -258   -142       C  
ATOM    926  O   GLN A 266     -18.972   8.798 -23.607  1.00  8.70           O  
ANISOU  926  O   GLN A 266      623   1263   1421     76   -185    -83       O  
ATOM    927  CB  GLN A 266     -16.690  10.992 -24.492  1.00  8.83           C  
ANISOU  927  CB  GLN A 266      834   1218   1301     81   -194    -85       C  
ATOM    928  CG  GLN A 266     -17.627  11.813 -23.616  1.00  8.92           C  
ANISOU  928  CG  GLN A 266      757   1223   1410    107   -220    -91       C  
ATOM    929  CD  GLN A 266     -17.188  11.751 -22.173  1.00  8.39           C  
ANISOU  929  CD  GLN A 266      681   1111   1398    180   -254    -13       C  
ATOM    930  OE1 GLN A 266     -16.136  12.286 -21.827  1.00  8.91           O  
ANISOU  930  OE1 GLN A 266      722   1317   1348     40   -269      9       O  
ATOM    931  NE2 GLN A 266     -17.912  11.016 -21.349  1.00  8.84           N  
ANISOU  931  NE2 GLN A 266      810   1175   1374    -14   -259    -62       N  
ATOM    932  H   GLN A 266     -15.260   9.240 -25.460  1.00  9.79           H  
ATOM    933  HA  GLN A 266     -16.600   9.387 -23.219  1.00 10.02           H  
ATOM    934  HB2 GLN A 266     -15.786  11.311 -24.348  1.00 10.60           H  
ATOM    935  HB3 GLN A 266     -16.947  11.128 -25.417  1.00 10.60           H  
ATOM    936  HG2 GLN A 266     -17.613  12.739 -23.904  1.00 10.71           H  
ATOM    937  HG3 GLN A 266     -18.527  11.458 -23.681  1.00 10.71           H  
ATOM    938 HE21 GLN A 266     -18.603  10.596 -21.642  1.00 10.62           H  
ATOM    939 HE22 GLN A 266     -17.693  10.957 -20.520  1.00 10.62           H  
ATOM    940  N   VAL A 267     -18.385   8.640 -25.782  1.00  8.91           N  
ANISOU  940  N   VAL A 267      746   1351   1288     96   -303   -103       N  
ATOM    941  CA  VAL A 267     -19.692   8.108 -26.159  1.00  9.49           C  
ANISOU  941  CA  VAL A 267      686   1478   1441     61   -365   -162       C  
ATOM    942  C   VAL A 267     -19.949   6.796 -25.428  1.00  9.56           C  
ANISOU  942  C   VAL A 267      718   1388   1525     70   -413   -260       C  
ATOM    943  O   VAL A 267     -21.034   6.557 -24.882  1.00  9.86           O  
ANISOU  943  O   VAL A 267      637   1411   1699     14   -302   -192       O  
ATOM    944  CB  VAL A 267     -19.791   7.951 -27.686  1.00 10.95           C  
ANISOU  944  CB  VAL A 267      980   1731   1449    -15   -516   -114       C  
ATOM    945  CG1 VAL A 267     -21.081   7.248 -28.072  1.00 11.94           C  
ANISOU  945  CG1 VAL A 267     1179   1857   1501   -204   -521    -66       C  
ATOM    946  CG2 VAL A 267     -19.704   9.314 -28.363  1.00 12.15           C  
ANISOU  946  CG2 VAL A 267     1264   1855   1496     39   -618     14       C  
ATOM    947  H   VAL A 267     -17.830   8.736 -26.432  1.00 10.70           H  
ATOM    948  HA  VAL A 267     -20.379   8.738 -25.889  1.00 11.40           H  
ATOM    949  HB  VAL A 267     -19.050   7.407 -27.994  1.00 13.15           H  
ATOM    950 HG11 VAL A 267     -21.225   7.353 -29.025  1.00 14.34           H  
ATOM    951 HG12 VAL A 267     -21.005   6.306 -27.851  1.00 14.34           H  
ATOM    952 HG13 VAL A 267     -21.816   7.645 -27.579  1.00 14.34           H  
ATOM    953 HG21 VAL A 267     -19.757   9.193 -29.324  1.00 14.58           H  
ATOM    954 HG22 VAL A 267     -20.441   9.866 -28.058  1.00 14.58           H  
ATOM    955 HG23 VAL A 267     -18.860   9.730 -28.128  1.00 14.58           H  
ATOM    956  N   GLU A 268     -18.944   5.917 -25.423  1.00  9.29           N  
ANISOU  956  N   GLU A 268      661   1376   1492     19   -210   -264       N  
ATOM    957  CA  GLU A 268     -19.061   4.634 -24.748  1.00  8.85           C  
ANISOU  957  CA  GLU A 268      584   1271   1509      6   -229   -221       C  
ATOM    958  C   GLU A 268     -19.256   4.819 -23.257  1.00  8.40           C  
ANISOU  958  C   GLU A 268      482   1172   1536    -16   -177   -260       C  
ATOM    959  O   GLU A 268     -20.055   4.114 -22.632  1.00  8.94           O  
ANISOU  959  O   GLU A 268      565   1199   1633    -39   -106   -259       O  
ATOM    960  CB  GLU A 268     -17.802   3.809 -25.034  1.00  9.09           C  
ANISOU  960  CB  GLU A 268      691   1336   1426     29   -373   -254       C  
ATOM    961  CG  GLU A 268     -17.770   2.471 -24.341  1.00  9.21           C  
ANISOU  961  CG  GLU A 268      671   1443   1384     34   -227   -256       C  
ATOM    962  CD  GLU A 268     -16.390   1.863 -24.316  1.00  9.77           C  
ANISOU  962  CD  GLU A 268      799   1594   1320     93   -328   -268       C  
ATOM    963  OE1 GLU A 268     -15.407   2.638 -24.285  1.00  9.90           O  
ANISOU  963  OE1 GLU A 268      637   1825   1301     18   -277   -160       O  
ATOM    964  OE2 GLU A 268     -16.308   0.619 -24.289  1.00 10.80           O  
ANISOU  964  OE2 GLU A 268      999   1514   1591    306   -496   -336       O  
ATOM    965  H   GLU A 268     -18.184   6.043 -25.806  1.00 11.15           H  
ATOM    966  HA  GLU A 268     -19.833   4.154 -25.086  1.00 10.63           H  
ATOM    967  HB2 GLU A 268     -17.747   3.647 -25.989  1.00 10.91           H  
ATOM    968  HB3 GLU A 268     -17.027   4.313 -24.738  1.00 10.91           H  
ATOM    969  HG2 GLU A 268     -18.066   2.583 -23.424  1.00 11.05           H  
ATOM    970  HG3 GLU A 268     -18.361   1.859 -24.807  1.00 11.05           H  
ATOM    971  N   SER A 269     -18.500   5.755 -22.670  1.00  8.50           N  
ANISOU  971  N   SER A 269      550   1194   1486    -14   -112   -194       N  
ATOM    972  CA  SER A 269     -18.596   6.026 -21.245  1.00  7.98           C  
ANISOU  972  CA  SER A 269      466   1204   1361    -17   -156   -170       C  
ATOM    973  C   SER A 269     -19.980   6.538 -20.861  1.00  8.26           C  
ANISOU  973  C   SER A 269      564   1144   1432    -34   -190   -166       C  
ATOM    974  O   SER A 269     -20.512   6.167 -19.811  1.00  8.49           O  
ANISOU  974  O   SER A 269      555   1248   1424     19    -75   -125       O  
ATOM    975  CB  SER A 269     -17.516   7.044 -20.860  1.00  8.32           C  
ANISOU  975  CB  SER A 269      492   1306   1365      3   -178    -95       C  
ATOM    976  OG  SER A 269     -16.224   6.471 -20.995  1.00  8.22           O  
ANISOU  976  OG  SER A 269      464   1337   1322     42   -106   -160       O  
ATOM    977  H   SER A 269     -17.924   6.244 -23.080  1.00 10.21           H  
ATOM    978  HA  SER A 269     -18.446   5.205 -20.751  1.00  9.58           H  
ATOM    979  HB2 SER A 269     -17.584   7.815 -21.444  1.00 10.00           H  
ATOM    980  HB3 SER A 269     -17.649   7.314 -19.937  1.00 10.00           H  
ATOM    981  HG  SER A 269     -16.063   6.312 -21.804  1.00  9.87           H  
ATOM    982  N   ASP A 270     -20.550   7.421 -21.684  1.00  8.79           N  
ANISOU  982  N   ASP A 270      580   1252   1508     80   -246    -61       N  
ATOM    983  CA  ASP A 270     -21.885   7.922 -21.391  1.00  8.99           C  
ANISOU  983  CA  ASP A 270      545   1189   1684     54   -131   -134       C  
ATOM    984  C   ASP A 270     -22.888   6.767 -21.362  1.00  9.18           C  
ANISOU  984  C   ASP A 270      520   1214   1754     78   -101   -205       C  
ATOM    985  O   ASP A 270     -23.784   6.726 -20.509  1.00  9.52           O  
ANISOU  985  O   ASP A 270      489   1296   1832     16   -101   -196       O  
ATOM    986  CB  ASP A 270     -22.295   8.950 -22.439  1.00 10.24           C  
ANISOU  986  CB  ASP A 270      685   1268   1938    159   -200    -68       C  
ATOM    987  CG  ASP A 270     -21.534  10.261 -22.340  1.00 12.00           C  
ANISOU  987  CG  ASP A 270      876   1410   2274    216   -306    -22       C  
ATOM    988  OD1 ASP A 270     -20.767  10.478 -21.386  1.00 11.96           O  
ANISOU  988  OD1 ASP A 270      886   1458   2201      2   -105   -191       O  
ATOM    989  OD2 ASP A 270     -21.732  11.085 -23.258  1.00 15.39           O  
ANISOU  989  OD2 ASP A 270     1615   1637   2596    -17   -492    347       O  
ATOM    990  H   ASP A 270     -20.192   7.735 -22.400  1.00 10.56           H  
ATOM    991  HA  ASP A 270     -21.883   8.360 -20.525  1.00 10.80           H  
ATOM    992  HB2 ASP A 270     -22.132   8.580 -23.320  1.00 12.30           H  
ATOM    993  HB3 ASP A 270     -23.238   9.147 -22.331  1.00 12.30           H  
ATOM    994  N   ASP A 271     -22.743   5.814 -22.287  1.00  9.84           N  
ANISOU  994  N   ASP A 271      565   1412   1761     38   -227   -304       N  
ATOM    995  CA  ASP A 271     -23.614   4.644 -22.272  1.00 10.00           C  
ANISOU  995  CA  ASP A 271      565   1378   1855    -30   -214   -374       C  
ATOM    996  C   ASP A 271     -23.386   3.783 -21.041  1.00  9.44           C  
ANISOU  996  C   ASP A 271      502   1247   1836     -3    -65   -338       C  
ATOM    997  O   ASP A 271     -24.346   3.278 -20.449  1.00  9.73           O  
ANISOU  997  O   ASP A 271      504   1320   1872    -83     -2   -265       O  
ATOM    998  CB  ASP A 271     -23.462   3.842 -23.556  1.00 11.49           C  
ANISOU  998  CB  ASP A 271      757   1502   2104    -17   -253   -394       C  
ATOM    999  CG  ASP A 271     -24.268   2.562 -23.533  1.00 13.31           C  
ANISOU  999  CG  ASP A 271      923   1676   2460    -79   -276   -586       C  
ATOM   1000  OD1 ASP A 271     -25.503   2.603 -23.627  1.00 14.49           O  
ANISOU 1000  OD1 ASP A 271      945   1930   2629   -158   -250   -694       O  
ATOM   1001  OD2 ASP A 271     -23.638   1.503 -23.374  1.00 14.15           O  
ANISOU 1001  OD2 ASP A 271     1049   1574   2754   -139   -128   -497       O  
ATOM   1002  H   ASP A 271     -22.160   5.823 -22.919  1.00 11.81           H  
ATOM   1003  HA  ASP A 271     -24.533   4.951 -22.236  1.00 12.00           H  
ATOM   1004  HB2 ASP A 271     -23.770   4.378 -24.304  1.00 13.79           H  
ATOM   1005  HB3 ASP A 271     -22.529   3.609 -23.677  1.00 13.79           H  
ATOM   1006  N   TYR A 272     -22.124   3.607 -20.644  1.00  9.36           N  
ANISOU 1006  N   TYR A 272      491   1206   1859    -43    -57   -238       N  
ATOM   1007  CA  TYR A 272     -21.828   2.896 -19.405  1.00  9.19           C  
ANISOU 1007  CA  TYR A 272      478   1159   1857      5     28   -193       C  
ATOM   1008  C   TYR A 272     -22.566   3.541 -18.229  1.00  8.65           C  
ANISOU 1008  C   TYR A 272      428   1172   1687     40      2    -93       C  
ATOM   1009  O   TYR A 272     -23.198   2.852 -17.418  1.00  8.78           O  
ANISOU 1009  O   TYR A 272      435   1191   1709    -28    -41   -103       O  
ATOM   1010  CB  TYR A 272     -20.306   2.854 -19.149  1.00  9.29           C  
ANISOU 1010  CB  TYR A 272      503   1176   1852     25     -8   -164       C  
ATOM   1011  CG  TYR A 272     -20.008   2.274 -17.780  1.00  9.02           C  
ANISOU 1011  CG  TYR A 272      439   1252   1736     40     48    -25       C  
ATOM   1012  CD1 TYR A 272     -19.959   3.085 -16.656  1.00  9.47           C  
ANISOU 1012  CD1 TYR A 272      462   1352   1785   -116     22    -31       C  
ATOM   1013  CD2 TYR A 272     -19.833   0.911 -17.597  1.00 10.20           C  
ANISOU 1013  CD2 TYR A 272      518   1315   2043    -15     91     27       C  
ATOM   1014  CE1 TYR A 272     -19.777   2.562 -15.393  1.00 10.48           C  
ANISOU 1014  CE1 TYR A 272      521   1476   1987    -23    -30     70       C  
ATOM   1015  CE2 TYR A 272     -19.636   0.383 -16.335  1.00 10.44           C  
ANISOU 1015  CE2 TYR A 272      528   1365   2072     38     37    140       C  
ATOM   1016  CZ  TYR A 272     -19.615   1.214 -15.241  1.00 10.83           C  
ANISOU 1016  CZ  TYR A 272      525   1548   2043    -57    -46    140       C  
ATOM   1017  OH  TYR A 272     -19.445   0.685 -13.990  1.00 11.95           O  
ANISOU 1017  OH  TYR A 272      703   1640   2196     42    -76    361       O  
ATOM   1018  H   TYR A 272     -21.431   3.886 -21.069  1.00 11.24           H  
ATOM   1019  HA  TYR A 272     -22.129   1.978 -19.492  1.00 11.04           H  
ATOM   1020  HB2 TYR A 272     -19.881   2.297 -19.819  1.00 11.16           H  
ATOM   1021  HB3 TYR A 272     -19.946   3.754 -19.188  1.00 11.16           H  
ATOM   1022  HD1 TYR A 272     -20.052   4.005 -16.756  1.00 11.38           H  
ATOM   1023  HD2 TYR A 272     -19.847   0.344 -18.334  1.00 12.25           H  
ATOM   1024  HE1 TYR A 272     -19.764   3.123 -14.650  1.00 12.59           H  
ATOM   1025  HE2 TYR A 272     -19.519  -0.534 -16.227  1.00 12.53           H  
ATOM   1026  HH  TYR A 272     -19.382  -0.152 -14.038  1.00 14.34           H  
ATOM   1027  N   ILE A 273     -22.487   4.869 -18.108  1.00  8.74           N  
ANISOU 1027  N   ILE A 273      444   1162   1715    -35    -85   -118       N  
ATOM   1028  CA  ILE A 273     -23.129   5.535 -16.978  1.00  8.80           C  
ANISOU 1028  CA  ILE A 273      452   1147   1743      8     26   -202       C  
ATOM   1029  C   ILE A 273     -24.645   5.361 -17.036  1.00  8.60           C  
ANISOU 1029  C   ILE A 273      469   1071   1729     54    -92   -224       C  
ATOM   1030  O   ILE A 273     -25.294   5.142 -16.008  1.00  8.91           O  
ANISOU 1030  O   ILE A 273      448   1200   1739     31    -12   -166       O  
ATOM   1031  CB  ILE A 273     -22.714   7.019 -16.948  1.00  9.41           C  
ANISOU 1031  CB  ILE A 273      579   1190   1808    -40    -61   -253       C  
ATOM   1032  CG1 ILE A 273     -21.219   7.184 -16.618  1.00  9.47           C  
ANISOU 1032  CG1 ILE A 273      566   1279   1755   -149    -10   -174       C  
ATOM   1033  CG2 ILE A 273     -23.571   7.794 -15.938  1.00  9.72           C  
ANISOU 1033  CG2 ILE A 273      608   1172   1912    -46     21   -313       C  
ATOM   1034  CD1 ILE A 273     -20.818   6.770 -15.219  1.00  9.88           C  
ANISOU 1034  CD1 ILE A 273      536   1480   1740   -139   -159   -102       C  
ATOM   1035  H   ILE A 273     -22.077   5.393 -18.653  1.00 10.50           H  
ATOM   1036  HA  ILE A 273     -22.828   5.120 -16.155  1.00 10.56           H  
ATOM   1037  HB  ILE A 273     -22.863   7.381 -17.835  1.00 11.31           H  
ATOM   1038 HG12 ILE A 273     -20.707   6.642 -17.239  1.00 11.38           H  
ATOM   1039 HG13 ILE A 273     -20.984   8.120 -16.722  1.00 11.38           H  
ATOM   1040 HG21 ILE A 273     -23.139   8.640 -15.741  1.00 11.67           H  
ATOM   1041 HG22 ILE A 273     -24.447   7.952 -16.323  1.00 11.67           H  
ATOM   1042 HG23 ILE A 273     -23.655   7.268 -15.127  1.00 11.67           H  
ATOM   1043 HD11 ILE A 273     -19.864   6.906 -15.110  1.00 11.87           H  
ATOM   1044 HD12 ILE A 273     -21.305   7.311 -14.578  1.00 11.87           H  
ATOM   1045 HD13 ILE A 273     -21.035   5.833 -15.093  1.00 11.87           H  
ATOM   1046  N   ALA A 274     -25.225   5.457 -18.234  1.00  8.77           N  
ANISOU 1046  N   ALA A 274      449   1182   1702     39    -84   -192       N  
ATOM   1047  CA  ALA A 274     -26.667   5.290 -18.377  1.00  9.05           C  
ANISOU 1047  CA  ALA A 274      460   1273   1704    125    -95   -120       C  
ATOM   1048  C   ALA A 274     -27.131   3.904 -17.958  1.00  9.25           C  
ANISOU 1048  C   ALA A 274      458   1312   1744     52   -123    -99       C  
ATOM   1049  O   ALA A 274     -28.269   3.744 -17.513  1.00  9.97           O  
ANISOU 1049  O   ALA A 274      481   1409   1898     78     20     -9       O  
ATOM   1050  CB  ALA A 274     -27.086   5.556 -19.821  1.00 10.38           C  
ANISOU 1050  CB  ALA A 274      526   1442   1975     34   -160   -122       C  
ATOM   1051  H   ALA A 274     -24.809   5.616 -18.970  1.00 10.54           H  
ATOM   1052  HA  ALA A 274     -27.102   5.939 -17.802  1.00 10.86           H  
ATOM   1053  HB1 ALA A 274     -28.045   5.432 -19.900  1.00 12.46           H  
ATOM   1054  HB2 ALA A 274     -26.850   6.467 -20.056  1.00 12.46           H  
ATOM   1055  HB3 ALA A 274     -26.623   4.934 -20.404  1.00 12.46           H  
ATOM   1056  N   THR A 275     -26.269   2.888 -18.100  1.00  9.03           N  
ANISOU 1056  N   THR A 275      465   1193   1773     63    -70   -176       N  
ATOM   1057  CA  THR A 275     -26.654   1.518 -17.825  1.00  9.53           C  
ANISOU 1057  CA  THR A 275      493   1202   1927    -16    -10   -179       C  
ATOM   1058  C   THR A 275     -26.076   0.963 -16.536  1.00 10.03           C  
ANISOU 1058  C   THR A 275      522   1311   1977   -131     39   -122       C  
ATOM   1059  O   THR A 275     -26.411  -0.166 -16.171  1.00 11.87           O  
ANISOU 1059  O   THR A 275      825   1370   2314   -303   -144     33       O  
ATOM   1060  CB  THR A 275     -26.335   0.612 -19.018  1.00 10.89           C  
ANISOU 1060  CB  THR A 275      608   1374   2156    -64    -56   -295       C  
ATOM   1061  OG1 THR A 275     -24.944   0.701 -19.341  1.00 11.79           O  
ANISOU 1061  OG1 THR A 275      657   1488   2335    115   -100   -483       O  
ATOM   1062  CG2 THR A 275     -27.169   1.009 -20.231  1.00 11.83           C  
ANISOU 1062  CG2 THR A 275      748   1632   2114   -105   -114   -407       C  
ATOM   1063  H   THR A 275     -25.453   2.979 -18.355  1.00 10.84           H  
ATOM   1064  HA  THR A 275     -27.617   1.482 -17.719  1.00 11.45           H  
ATOM   1065  HB  THR A 275     -26.549  -0.306 -18.790  1.00 13.08           H  
ATOM   1066  HG1 THR A 275     -24.778   0.245 -20.027  1.00 14.16           H  
ATOM   1067 HG21 THR A 275     -26.965   0.426 -20.979  1.00 14.21           H  
ATOM   1068 HG22 THR A 275     -28.114   0.936 -20.023  1.00 14.21           H  
ATOM   1069 HG23 THR A 275     -26.972   1.925 -20.484  1.00 14.21           H  
ATOM   1070  N   ASN A 276     -25.190   1.703 -15.859  1.00  9.66           N  
ANISOU 1070  N   ASN A 276      483   1308   1878    -60    -76    -87       N  
ATOM   1071  CA  ASN A 276     -24.538   1.234 -14.635  1.00 10.26           C  
ANISOU 1071  CA  ASN A 276      529   1387   1983   -116   -143     67       C  
ATOM   1072  C   ASN A 276     -24.531   2.245 -13.509  1.00 10.31           C  
ANISOU 1072  C   ASN A 276      526   1466   1925   -140   -159     78       C  
ATOM   1073  O   ASN A 276     -24.294   1.858 -12.357  1.00 11.78           O  
ANISOU 1073  O   ASN A 276      630   1692   2154   -148   -267    168       O  
ATOM   1074  CB  ASN A 276     -23.092   0.816 -14.909  1.00 11.42           C  
ANISOU 1074  CB  ASN A 276      568   1572   2200    -31   -121    130       C  
ATOM   1075  CG  ASN A 276     -22.999  -0.381 -15.802  1.00 12.77           C  
ANISOU 1075  CG  ASN A 276      756   1522   2576     92    143     72       C  
ATOM   1076  OD1 ASN A 276     -22.919  -1.521 -15.329  1.00 15.28           O  
ANISOU 1076  OD1 ASN A 276     1526   1491   2789    151    142    185       O  
ATOM   1077  ND2 ASN A 276     -23.002  -0.148 -17.098  1.00 12.39           N  
ANISOU 1077  ND2 ASN A 276      682   1478   2546    144    168    -63       N  
ATOM   1078  H   ASN A 276     -24.947   2.494 -16.095  1.00 11.60           H  
ATOM   1079  HA  ASN A 276     -25.017   0.448 -14.329  1.00 12.33           H  
ATOM   1080  HB2 ASN A 276     -22.626   1.550 -15.341  1.00 13.71           H  
ATOM   1081  HB3 ASN A 276     -22.660   0.599 -14.068  1.00 13.71           H  
ATOM   1082 HD21 ASN A 276     -22.951  -0.803 -17.653  1.00 14.87           H  
ATOM   1083 HD22 ASN A 276     -23.056   0.659 -17.389  1.00 14.87           H  
ATOM   1084  N   GLY A 277     -24.769   3.519 -13.791  1.00 10.63           N  
ANISOU 1084  N   GLY A 277      546   1456   2035   -110   -173      4       N  
ATOM   1085  CA  GLY A 277     -24.644   4.549 -12.792  1.00 10.72           C  
ANISOU 1085  CA  GLY A 277      551   1433   2091    -42   -128    -43       C  
ATOM   1086  C   GLY A 277     -23.209   4.945 -12.541  1.00 10.19           C  
ANISOU 1086  C   GLY A 277      580   1355   1937     12    -18   -117       C  
ATOM   1087  O   GLY A 277     -22.277   4.326 -13.055  1.00  9.97           O  
ANISOU 1087  O   GLY A 277      522   1404   1865    -78    -56   -135       O  
ATOM   1088  H   GLY A 277     -25.006   3.808 -14.565  1.00 12.76           H  
ATOM   1089  HA2 GLY A 277     -25.132   5.336 -13.081  1.00 12.88           H  
ATOM   1090  HA3 GLY A 277     -25.023   4.232 -11.957  1.00 12.88           H  
ATOM   1091  N   PRO A 278     -23.007   5.996 -11.748  1.00 10.76           N  
ANISOU 1091  N   PRO A 278      635   1444   2010     40    -12   -236       N  
ATOM   1092  CA  PRO A 278     -21.651   6.487 -11.490  1.00 10.93           C  
ANISOU 1092  CA  PRO A 278      790   1437   1925    -96    -64   -283       C  
ATOM   1093  C   PRO A 278     -20.835   5.484 -10.700  1.00 10.39           C  
ANISOU 1093  C   PRO A 278      807   1308   1834   -104     22   -168       C  
ATOM   1094  O   PRO A 278     -21.351   4.666  -9.924  1.00 11.21           O  
ANISOU 1094  O   PRO A 278      822   1520   1916   -154     76    -14       O  
ATOM   1095  CB  PRO A 278     -21.888   7.769 -10.684  1.00 11.98           C  
ANISOU 1095  CB  PRO A 278     1000   1518   2033      7    -60   -362       C  
ATOM   1096  CG  PRO A 278     -23.237   7.549 -10.040  1.00 13.03           C  
ANISOU 1096  CG  PRO A 278     1174   1632   2144    191     43   -330       C  
ATOM   1097  CD  PRO A 278     -24.041   6.777 -11.038  1.00 12.18           C  
ANISOU 1097  CD  PRO A 278      896   1638   2093     21    104   -268       C  
ATOM   1098  HA  PRO A 278     -21.195   6.698 -12.319  1.00 13.12           H  
ATOM   1099  HB2 PRO A 278     -21.193   7.877 -10.017  1.00 14.38           H  
ATOM   1100  HB3 PRO A 278     -21.902   8.538 -11.276  1.00 14.38           H  
ATOM   1101  HG2 PRO A 278     -23.129   7.042  -9.219  1.00 15.64           H  
ATOM   1102  HG3 PRO A 278     -23.653   8.404  -9.850  1.00 15.64           H  
ATOM   1103  HD2 PRO A 278     -24.676   6.192 -10.596  1.00 14.62           H  
ATOM   1104  HD3 PRO A 278     -24.506   7.372 -11.646  1.00 14.62           H  
ATOM   1105  N   LEU A 279     -19.529   5.583 -10.902  1.00  9.50           N  
ANISOU 1105  N   LEU A 279      561   1289   1760   -139    -41   -136       N  
ATOM   1106  CA  LEU A 279     -18.585   4.875 -10.071  1.00  9.71           C  
ANISOU 1106  CA  LEU A 279      723   1299   1669    -82     11   -108       C  
ATOM   1107  C   LEU A 279     -18.523   5.526  -8.693  1.00  9.73           C  
ANISOU 1107  C   LEU A 279      720   1368   1610   -122    144    -78       C  
ATOM   1108  O   LEU A 279     -19.102   6.592  -8.453  1.00 10.59           O  
ANISOU 1108  O   LEU A 279      994   1354   1674    -78    133   -144       O  
ATOM   1109  CB  LEU A 279     -17.196   4.885 -10.729  1.00  9.57           C  
ANISOU 1109  CB  LEU A 279      781   1244   1610    -53    -64   -228       C  
ATOM   1110  CG  LEU A 279     -17.070   4.120 -12.043  1.00 10.62           C  
ANISOU 1110  CG  LEU A 279      895   1440   1700    -22    -55   -330       C  
ATOM   1111  CD1 LEU A 279     -15.667   4.324 -12.632  1.00 12.02           C  
ANISOU 1111  CD1 LEU A 279     1204   1746   1617   -169     23   -355       C  
ATOM   1112  CD2 LEU A 279     -17.322   2.645 -11.871  1.00 13.17           C  
ANISOU 1112  CD2 LEU A 279     1303   1647   2056   -189    165   -404       C  
ATOM   1113  H   LEU A 279     -19.166   6.058 -11.520  1.00 11.41           H  
ATOM   1114  HA  LEU A 279     -18.863   3.952  -9.964  1.00 11.67           H  
ATOM   1115  HB2 LEU A 279     -16.954   5.807 -10.910  1.00 11.49           H  
ATOM   1116  HB3 LEU A 279     -16.564   4.492 -10.107  1.00 11.49           H  
ATOM   1117  HG  LEU A 279     -17.741   4.465 -12.652  1.00 12.75           H  
ATOM   1118 HD11 LEU A 279     -15.605   3.845 -13.474  1.00 14.43           H  
ATOM   1119 HD12 LEU A 279     -15.521   5.272 -12.780  1.00 14.43           H  
ATOM   1120 HD13 LEU A 279     -15.009   3.982 -12.007  1.00 14.43           H  
ATOM   1121 HD21 LEU A 279     -17.175   2.199 -12.719  1.00 15.81           H  
ATOM   1122 HD22 LEU A 279     -16.711   2.296 -11.203  1.00 15.81           H  
ATOM   1123 HD23 LEU A 279     -18.238   2.513 -11.582  1.00 15.81           H  
ATOM   1124  N   LYS A 280     -17.810   4.868  -7.786  1.00 10.77           N  
ANISOU 1124  N   LYS A 280      894   1601   1597    -45    224   -139       N  
ATOM   1125  CA  LYS A 280     -17.445   5.426  -6.497  1.00 11.51           C  
ANISOU 1125  CA  LYS A 280     1060   1801   1513   -165    298    -40       C  
ATOM   1126  C   LYS A 280     -15.959   5.765  -6.531  1.00  9.80           C  
ANISOU 1126  C   LYS A 280      956   1509   1260     16    348    -44       C  
ATOM   1127  O   LYS A 280     -15.187   5.169  -7.278  1.00  9.75           O  
ANISOU 1127  O   LYS A 280      933   1490   1282   -111    282   -119       O  
ATOM   1128  CB  LYS A 280     -17.712   4.416  -5.362  1.00 16.00           C  
ANISOU 1128  CB  LYS A 280     1603   2461   2017   -671    649    186       C  
ATOM   1129  CG  LYS A 280     -19.090   3.785  -5.366  1.00 21.36           C  
ANISOU 1129  CG  LYS A 280     2311   3153   2650   -836    621    314       C  
ATOM   1130  CD  LYS A 280     -19.985   4.424  -4.340  1.00 26.71           C  
ANISOU 1130  CD  LYS A 280     3190   3776   3183   -481    361    248       C  
ATOM   1131  CE  LYS A 280     -21.222   3.584  -4.073  1.00 30.33           C  
ANISOU 1131  CE  LYS A 280     3788   4181   3554   -255    216    254       C  
ATOM   1132  NZ  LYS A 280     -22.453   4.245  -4.569  1.00 32.62           N  
ANISOU 1132  NZ  LYS A 280     4186   4434   3772   -116    196    215       N  
ATOM   1133  H   LYS A 280     -17.516   4.068  -7.902  1.00 12.93           H  
ATOM   1134  HA  LYS A 280     -17.962   6.226  -6.311  1.00 13.82           H  
ATOM   1135  HB2 LYS A 280     -17.064   3.697  -5.433  1.00 19.21           H  
ATOM   1136  HB3 LYS A 280     -17.606   4.874  -4.513  1.00 19.21           H  
ATOM   1137  HG2 LYS A 280     -19.495   3.900  -6.239  1.00 25.64           H  
ATOM   1138  HG3 LYS A 280     -19.012   2.840  -5.158  1.00 25.64           H  
ATOM   1139  HD2 LYS A 280     -19.498   4.522  -3.506  1.00 32.06           H  
ATOM   1140  HD3 LYS A 280     -20.271   5.294  -4.661  1.00 32.06           H  
ATOM   1141  HE2 LYS A 280     -21.132   2.730  -4.524  1.00 36.40           H  
ATOM   1142  HE3 LYS A 280     -21.315   3.446  -3.117  1.00 36.40           H  
ATOM   1143  HZ1 LYS A 280     -22.396   4.375  -5.448  1.00 39.15           H  
ATOM   1144  HZ2 LYS A 280     -23.162   3.735  -4.399  1.00 39.15           H  
ATOM   1145  HZ3 LYS A 280     -22.560   5.032  -4.167  1.00 39.15           H  
ATOM   1146  N   VAL A 281     -15.554   6.717  -5.700  1.00  9.66           N  
ANISOU 1146  N   VAL A 281     1058   1326   1285    -36    411    -62       N  
ATOM   1147  CA  VAL A 281     -14.134   6.989  -5.545  1.00  9.56           C  
ANISOU 1147  CA  VAL A 281     1084   1379   1169   -127    483    -90       C  
ATOM   1148  C   VAL A 281     -13.467   5.731  -5.016  1.00  9.06           C  
ANISOU 1148  C   VAL A 281      958   1406   1080   -131    369    -95       C  
ATOM   1149  O   VAL A 281     -13.938   5.111  -4.055  1.00 10.04           O  
ANISOU 1149  O   VAL A 281     1116   1520   1180    -81    489     81       O  
ATOM   1150  CB  VAL A 281     -13.906   8.209  -4.643  1.00 10.73           C  
ANISOU 1150  CB  VAL A 281     1406   1442   1227   -297    601   -231       C  
ATOM   1151  CG1 VAL A 281     -12.415   8.447  -4.439  1.00 11.72           C  
ANISOU 1151  CG1 VAL A 281     1364   1763   1325   -409    623   -362       C  
ATOM   1152  CG2 VAL A 281     -14.556   9.449  -5.263  1.00 12.10           C  
ANISOU 1152  CG2 VAL A 281     1809   1343   1447   -172    499   -140       C  
ATOM   1153  H   VAL A 281     -16.072   7.211  -5.223  1.00 11.59           H  
ATOM   1154  HA  VAL A 281     -13.742   7.207  -6.405  1.00 11.48           H  
ATOM   1155  HB  VAL A 281     -14.312   8.043  -3.778  1.00 12.88           H  
ATOM   1156 HG11 VAL A 281     -12.288   9.313  -4.020  1.00 14.07           H  
ATOM   1157 HG12 VAL A 281     -12.059   7.748  -3.868  1.00 14.07           H  
ATOM   1158 HG13 VAL A 281     -11.971   8.428  -5.301  1.00 14.07           H  
ATOM   1159 HG21 VAL A 281     -14.364  10.219  -4.704  1.00 14.53           H  
ATOM   1160 HG22 VAL A 281     -14.191   9.587  -6.151  1.00 14.53           H  
ATOM   1161 HG23 VAL A 281     -15.514   9.310  -5.317  1.00 14.53           H  
ATOM   1162  N   GLY A 282     -12.369   5.339  -5.661  1.00  9.05           N  
ANISOU 1162  N   GLY A 282      965   1367   1107   -119    356    -90       N  
ATOM   1163  CA  GLY A 282     -11.710   4.090  -5.389  1.00  9.66           C  
ANISOU 1163  CA  GLY A 282      977   1519   1174    -46    277   -101       C  
ATOM   1164  C   GLY A 282     -12.144   2.955  -6.278  1.00  9.23           C  
ANISOU 1164  C   GLY A 282      898   1404   1206    -26    331    -85       C  
ATOM   1165  O   GLY A 282     -11.530   1.885  -6.231  1.00 10.70           O  
ANISOU 1165  O   GLY A 282     1182   1501   1382    163    326    -76       O  
ATOM   1166  H   GLY A 282     -11.985   5.800  -6.277  1.00 10.87           H  
ATOM   1167  HA2 GLY A 282     -10.754   4.209  -5.501  1.00 11.60           H  
ATOM   1168  HA3 GLY A 282     -11.891   3.835  -4.470  1.00 11.60           H  
ATOM   1169  N   GLY A 283     -13.171   3.163  -7.092  1.00  8.68           N  
ANISOU 1169  N   GLY A 283      939   1244   1116    -81    296   -145       N  
ATOM   1170  CA  GLY A 283     -13.694   2.142  -7.963  1.00  8.93           C  
ANISOU 1170  CA  GLY A 283      972   1253   1167   -144    376    -40       C  
ATOM   1171  C   GLY A 283     -13.184   2.233  -9.391  1.00  7.70           C  
ANISOU 1171  C   GLY A 283      805   1022   1099    -66    207    -50       C  
ATOM   1172  O   GLY A 283     -12.403   3.106  -9.762  1.00  8.29           O  
ANISOU 1172  O   GLY A 283      881   1165   1104   -194    213    -63       O  
ATOM   1173  H   GLY A 283     -13.589   3.912  -7.154  1.00 10.43           H  
ATOM   1174  HA2 GLY A 283     -13.449   1.272  -7.613  1.00 10.72           H  
ATOM   1175  HA3 GLY A 283     -14.662   2.212  -7.986  1.00 10.72           H  
ATOM   1176  N   SER A 284     -13.640   1.283 -10.201  1.00  7.66           N  
ANISOU 1176  N   SER A 284      792   1048   1069   -204    228    -46       N  
ATOM   1177  CA  SER A 284     -13.216   1.219 -11.587  1.00  7.21           C  
ANISOU 1177  CA  SER A 284      617   1010   1112   -136    141    -15       C  
ATOM   1178  C   SER A 284     -14.259   0.507 -12.435  1.00  7.24           C  
ANISOU 1178  C   SER A 284      481   1123   1149    -86    104    -58       C  
ATOM   1179  O   SER A 284     -15.140  -0.189 -11.937  1.00  8.60           O  
ANISOU 1179  O   SER A 284      689   1316   1261   -204    208    -65       O  
ATOM   1180  CB  SER A 284     -11.881   0.475 -11.730  1.00  7.42           C  
ANISOU 1180  CB  SER A 284      680   1036   1104    -75     80    -63       C  
ATOM   1181  OG  SER A 284     -12.028  -0.921 -11.478  1.00  8.74           O  
ANISOU 1181  OG  SER A 284      964   1137   1219     35     81     37       O  
ATOM   1182  H   SER A 284     -14.194   0.668  -9.968  1.00  9.20           H  
ATOM   1183  HA  SER A 284     -13.135   2.134 -11.900  1.00  8.66           H  
ATOM   1184  HB2 SER A 284     -11.551   0.596 -12.634  1.00  8.91           H  
ATOM   1185  HB3 SER A 284     -11.249   0.843 -11.094  1.00  8.91           H  
ATOM   1186  HG  SER A 284     -12.303  -1.043 -10.694  1.00 10.49           H  
ATOM   1187  N   CYS A 285     -14.092   0.645 -13.748  1.00  7.16           N  
ANISOU 1187  N   CYS A 285      501   1079   1141   -111     34    -92       N  
ATOM   1188  CA  CYS A 285     -14.789  -0.204 -14.711  1.00  7.29           C  
ANISOU 1188  CA  CYS A 285      418   1048   1302    -72     38   -155       C  
ATOM   1189  C   CYS A 285     -13.865  -0.455 -15.896  1.00  6.82           C  
ANISOU 1189  C   CYS A 285      332   1001   1257    -81    -53    -64       C  
ATOM   1190  O   CYS A 285     -12.959   0.327 -16.190  1.00  7.54           O  
ANISOU 1190  O   CYS A 285      446   1092   1328   -110     62   -198       O  
ATOM   1191  CB  CYS A 285     -16.119   0.411 -15.171  1.00  7.90           C  
ANISOU 1191  CB  CYS A 285      471   1176   1353    -39     44   -177       C  
ATOM   1192  SG  CYS A 285     -15.890   1.927 -16.143  1.00  8.33           S  
ANISOU 1192  SG  CYS A 285      498   1205   1461     -1    -91   -100       S  
ATOM   1193  H   CYS A 285     -13.575   1.229 -14.110  1.00  8.60           H  
ATOM   1194  HA  CYS A 285     -14.997  -1.059 -14.303  1.00  8.75           H  
ATOM   1195  HB2 CYS A 285     -16.591  -0.232 -15.723  1.00  9.48           H  
ATOM   1196  HB3 CYS A 285     -16.651   0.632 -14.391  1.00  9.48           H  
ATOM   1197  HG  CYS A 285     -16.961   2.309 -16.528  1.00 10.00           H  
ATOM   1198  N   VAL A 286     -14.128  -1.553 -16.598  1.00  7.55           N  
ANISOU 1198  N   VAL A 286      561   1012   1296   -156     63   -104       N  
ATOM   1199  CA  VAL A 286     -13.399  -1.936 -17.794  1.00  7.39           C  
ANISOU 1199  CA  VAL A 286      530   1002   1276    -78    -34   -111       C  
ATOM   1200  C   VAL A 286     -14.259  -1.637 -19.000  1.00  7.56           C  
ANISOU 1200  C   VAL A 286      522   1095   1257   -107    -58   -208       C  
ATOM   1201  O   VAL A 286     -15.375  -2.168 -19.126  1.00  8.90           O  
ANISOU 1201  O   VAL A 286      636   1353   1392   -317   -140    -49       O  
ATOM   1202  CB  VAL A 286     -13.029  -3.425 -17.787  1.00  9.03           C  
ANISOU 1202  CB  VAL A 286      876   1156   1397     94     14   -109       C  
ATOM   1203  CG1 VAL A 286     -12.307  -3.781 -19.079  1.00 10.38           C  
ANISOU 1203  CG1 VAL A 286     1278   1255   1410    163    137    -65       C  
ATOM   1204  CG2 VAL A 286     -12.192  -3.786 -16.582  1.00 10.00           C  
ANISOU 1204  CG2 VAL A 286     1062   1312   1426    109    -84    -78       C  
ATOM   1205  H   VAL A 286     -14.749  -2.110 -16.391  1.00  9.07           H  
ATOM   1206  HA  VAL A 286     -12.588  -1.404 -17.835  1.00  8.88           H  
ATOM   1207  HB  VAL A 286     -13.843  -3.949 -17.730  1.00 10.84           H  
ATOM   1208 HG11 VAL A 286     -11.867  -4.638 -18.969  1.00 12.46           H  
ATOM   1209 HG12 VAL A 286     -12.955  -3.832 -19.799  1.00 12.46           H  
ATOM   1210 HG13 VAL A 286     -11.650  -3.094 -19.273  1.00 12.46           H  
ATOM   1211 HG21 VAL A 286     -11.939  -4.720 -16.642  1.00 12.01           H  
ATOM   1212 HG22 VAL A 286     -11.398  -3.228 -16.570  1.00 12.01           H  
ATOM   1213 HG23 VAL A 286     -12.714  -3.635 -15.779  1.00 12.01           H  
ATOM   1214  N   LEU A 287     -13.746  -0.822 -19.899  1.00  6.74           N  
ANISOU 1214  N   LEU A 287      441   1000   1120    -34    -71   -152       N  
ATOM   1215  CA  LEU A 287     -14.393  -0.495 -21.154  1.00  6.92           C  
ANISOU 1215  CA  LEU A 287      465   1027   1138    -77   -162   -150       C  
ATOM   1216  C   LEU A 287     -13.400  -0.729 -22.279  1.00  6.95           C  
ANISOU 1216  C   LEU A 287      501   1030   1111    -30   -174   -214       C  
ATOM   1217  O   LEU A 287     -12.283  -1.216 -22.063  1.00  6.94           O  
ANISOU 1217  O   LEU A 287      427   1044   1165     10   -150   -214       O  
ATOM   1218  CB  LEU A 287     -14.942   0.943 -21.117  1.00  7.33           C  
ANISOU 1218  CB  LEU A 287      535   1052   1198    -16   -137   -160       C  
ATOM   1219  CG  LEU A 287     -16.095   1.172 -20.163  1.00  8.37           C  
ANISOU 1219  CG  LEU A 287      635   1136   1407    141    -46   -215       C  
ATOM   1220  CD1 LEU A 287     -16.445   2.659 -20.078  1.00  8.96           C  
ANISOU 1220  CD1 LEU A 287      711   1257   1437    134    -87   -258       C  
ATOM   1221  CD2 LEU A 287     -17.332   0.381 -20.571  1.00  9.83           C  
ANISOU 1221  CD2 LEU A 287      629   1395   1711     91     24   -199       C  
ATOM   1222  H   LEU A 287     -12.989  -0.426 -19.801  1.00  8.09           H  
ATOM   1223  HA  LEU A 287     -15.148  -1.082 -21.318  1.00  8.31           H  
ATOM   1224  HB2 LEU A 287     -14.223   1.538 -20.851  1.00  8.81           H  
ATOM   1225  HB3 LEU A 287     -15.251   1.175 -22.007  1.00  8.81           H  
ATOM   1226  HG  LEU A 287     -15.816   0.863 -19.287  1.00 10.05           H  
ATOM   1227 HD11 LEU A 287     -17.165   2.778 -19.438  1.00 10.76           H  
ATOM   1228 HD12 LEU A 287     -15.661   3.152 -19.790  1.00 10.76           H  
ATOM   1229 HD13 LEU A 287     -16.727   2.967 -20.954  1.00 10.76           H  
ATOM   1230 HD21 LEU A 287     -18.078   0.651 -20.013  1.00 11.81           H  
ATOM   1231 HD22 LEU A 287     -17.531   0.565 -21.502  1.00 11.81           H  
ATOM   1232 HD23 LEU A 287     -17.154  -0.565 -20.451  1.00 11.81           H  
ATOM   1233  N   SER A 288     -13.809  -0.442 -23.503  1.00  7.35           N  
ANISOU 1233  N   SER A 288      535   1128   1129     47   -142   -162       N  
ATOM   1234  CA  SER A 288     -12.904  -0.590 -24.624  1.00  7.75           C  
ANISOU 1234  CA  SER A 288      671   1149   1123     29   -133   -147       C  
ATOM   1235  C   SER A 288     -11.731   0.377 -24.547  1.00  7.47           C  
ANISOU 1235  C   SER A 288      664   1166   1008    101   -187    -82       C  
ATOM   1236  O   SER A 288     -11.850   1.508 -24.076  1.00  7.59           O  
ANISOU 1236  O   SER A 288      710   1081   1092     29   -203   -146       O  
ATOM   1237  CB  SER A 288     -13.646  -0.325 -25.931  1.00  8.34           C  
ANISOU 1237  CB  SER A 288      767   1325   1076   -134   -109   -317       C  
ATOM   1238  OG  SER A 288     -12.791  -0.507 -27.031  1.00  9.93           O  
ANISOU 1238  OG  SER A 288     1110   1509   1154   -204   -180   -340       O  
ATOM   1239  H   SER A 288     -14.597  -0.163 -23.708  1.00  8.82           H  
ATOM   1240  HA  SER A 288     -12.555  -1.496 -24.610  1.00  9.30           H  
ATOM   1241  HB2 SER A 288     -14.391  -0.943 -26.003  1.00 10.02           H  
ATOM   1242  HB3 SER A 288     -13.972   0.588 -25.930  1.00 10.02           H  
ATOM   1243  HG  SER A 288     -12.510  -1.298 -27.049  1.00 11.92           H  
ATOM   1244  N   GLY A 289     -10.589  -0.068 -25.062  1.00  7.58           N  
ANISOU 1244  N   GLY A 289      687   1189   1003     81   -136    -42       N  
ATOM   1245  CA  GLY A 289      -9.465   0.818 -25.275  1.00  7.83           C  
ANISOU 1245  CA  GLY A 289      650   1254   1072     43   -263    -40       C  
ATOM   1246  C   GLY A 289      -9.420   1.443 -26.646  1.00  7.53           C  
ANISOU 1246  C   GLY A 289      738   1138    984     54   -189   -121       C  
ATOM   1247  O   GLY A 289      -8.498   2.213 -26.952  1.00  7.87           O  
ANISOU 1247  O   GLY A 289      815   1176    998    -44   -233    -94       O  
ATOM   1248  H   GLY A 289     -10.447  -0.884 -25.295  1.00  9.10           H  
ATOM   1249  HA2 GLY A 289      -9.503   1.534 -24.622  1.00  9.41           H  
ATOM   1250  HA3 GLY A 289      -8.644   0.317 -25.148  1.00  9.41           H  
ATOM   1251  N   HIS A 290     -10.401   1.136 -27.490  1.00  7.63           N  
ANISOU 1251  N   HIS A 290      807   1130    964     18   -267   -159       N  
ATOM   1252  CA  HIS A 290     -10.513   1.766 -28.796  1.00  8.26           C  
ANISOU 1252  CA  HIS A 290      922   1307    911     28   -318   -148       C  
ATOM   1253  C   HIS A 290      -9.216   1.546 -29.555  1.00  8.93           C  
ANISOU 1253  C   HIS A 290     1088   1366    940    -29   -161   -267       C  
ATOM   1254  O   HIS A 290      -8.722   0.403 -29.595  1.00  9.81           O  
ANISOU 1254  O   HIS A 290     1208   1398   1122     26    -91   -304       O  
ATOM   1255  CB  HIS A 290     -10.973   3.218 -28.644  1.00  9.15           C  
ANISOU 1255  CB  HIS A 290     1102   1358   1015    143   -225     22       C  
ATOM   1256  CG  HIS A 290     -12.273   3.310 -27.936  1.00  9.27           C  
ANISOU 1256  CG  HIS A 290      921   1478   1125    211   -158     35       C  
ATOM   1257  ND1 HIS A 290     -13.476   3.151 -28.589  1.00 11.55           N  
ANISOU 1257  ND1 HIS A 290     1000   2142   1245    240   -302      2       N  
ATOM   1258  CD2 HIS A 290     -12.552   3.429 -26.622  1.00  8.97           C  
ANISOU 1258  CD2 HIS A 290      966   1294   1148    200   -204    -72       C  
ATOM   1259  CE1 HIS A 290     -14.447   3.195 -27.695  1.00 11.58           C  
ANISOU 1259  CE1 HIS A 290     1020   2145   1235    310   -238    -20       C  
ATOM   1260  NE2 HIS A 290     -13.913   3.360 -26.498  1.00 10.06           N  
ANISOU 1260  NE2 HIS A 290     1007   1579   1237    248   -196    -28       N  
ATOM   1261  H   HIS A 290     -11.018   0.561 -27.324  1.00  9.17           H  
ATOM   1262  HA  HIS A 290     -11.197   1.292 -29.294  1.00  9.93           H  
ATOM   1263  HB2 HIS A 290     -10.312   3.711 -28.132  1.00 10.98           H  
ATOM   1264  HB3 HIS A 290     -11.075   3.615 -29.523  1.00 10.98           H  
ATOM   1265  HD2 HIS A 290     -11.938   3.537 -25.932  1.00 10.77           H  
ATOM   1266  HE1 HIS A 290     -15.356   3.122 -27.878  1.00 13.91           H  
ATOM   1267  HE2 HIS A 290     -14.351   3.415 -25.759  1.00 12.08           H  
ATOM   1268  N   ASN A 291      -8.655   2.572 -30.168  1.00  9.25           N  
ANISOU 1268  N   ASN A 291     1172   1399    946     36    -60   -135       N  
ATOM   1269  CA  ASN A 291      -7.431   2.455 -30.935  1.00 10.23           C  
ANISOU 1269  CA  ASN A 291     1331   1408   1150     29    122   -169       C  
ATOM   1270  C   ASN A 291      -6.186   2.477 -30.066  1.00 10.46           C  
ANISOU 1270  C   ASN A 291     1057   1513   1403     98    225   -215       C  
ATOM   1271  O   ASN A 291      -5.082   2.276 -30.585  1.00 13.04           O  
ANISOU 1271  O   ASN A 291     1322   2015   1616    110    286   -298       O  
ATOM   1272  CB  ASN A 291      -7.379   3.600 -31.949  1.00 11.55           C  
ANISOU 1272  CB  ASN A 291     1698   1489   1202    -13    290   -152       C  
ATOM   1273  CG  ASN A 291      -7.556   4.958 -31.299  1.00 12.27           C  
ANISOU 1273  CG  ASN A 291     1799   1507   1355     34    296   -140       C  
ATOM   1274  OD1 ASN A 291      -8.507   5.188 -30.553  1.00 13.77           O  
ANISOU 1274  OD1 ASN A 291     2165   1464   1603    213    666    -18       O  
ATOM   1275  ND2 ASN A 291      -6.618   5.845 -31.536  1.00 13.08           N  
ANISOU 1275  ND2 ASN A 291     1895   1593   1480    -28    251   -185       N  
ATOM   1276  H   ASN A 291      -8.973   3.370 -30.154  1.00 11.11           H  
ATOM   1277  HA  ASN A 291      -7.427   1.614 -31.418  1.00 12.29           H  
ATOM   1278  HB2 ASN A 291      -6.518   3.589 -32.395  1.00 13.87           H  
ATOM   1279  HB3 ASN A 291      -8.090   3.481 -32.598  1.00 13.87           H  
ATOM   1280 HD21 ASN A 291      -6.672   6.630 -31.191  1.00 15.70           H  
ATOM   1281 HD22 ASN A 291      -5.949   5.640 -32.037  1.00 15.70           H  
ATOM   1282  N   LEU A 292      -6.322   2.701 -28.766  1.00  9.23           N  
ANISOU 1282  N   LEU A 292     1008   1218   1279    111     68   -121       N  
ATOM   1283  CA  LEU A 292      -5.170   2.874 -27.896  1.00  9.23           C  
ANISOU 1283  CA  LEU A 292      800   1184   1525    -21   -119    -60       C  
ATOM   1284  C   LEU A 292      -4.746   1.612 -27.175  1.00  8.78           C  
ANISOU 1284  C   LEU A 292      697   1181   1457     38    -88   -154       C  
ATOM   1285  O   LEU A 292      -3.576   1.499 -26.806  1.00  9.94           O  
ANISOU 1285  O   LEU A 292      808   1195   1775      6   -115      2       O  
ATOM   1286  CB  LEU A 292      -5.477   3.949 -26.858  1.00 10.17           C  
ANISOU 1286  CB  LEU A 292     1008   1138   1720     24   -398   -277       C  
ATOM   1287  CG  LEU A 292      -5.801   5.321 -27.448  1.00 11.71           C  
ANISOU 1287  CG  LEU A 292     1215   1160   2073    104   -371   -254       C  
ATOM   1288  CD1 LEU A 292      -6.226   6.245 -26.330  1.00 13.70           C  
ANISOU 1288  CD1 LEU A 292     1777   1369   2060    298   -554   -425       C  
ATOM   1289  CD2 LEU A 292      -4.628   5.888 -28.255  1.00 14.07           C  
ANISOU 1289  CD2 LEU A 292     1776   1272   2298    -10   -120    -48       C  
ATOM   1290  H   LEU A 292      -7.079   2.757 -28.360  1.00 11.08           H  
ATOM   1291  HA  LEU A 292      -4.416   3.161 -28.434  1.00 11.09           H  
ATOM   1292  HB2 LEU A 292      -6.245   3.665 -26.337  1.00 12.22           H  
ATOM   1293  HB3 LEU A 292      -4.704   4.052 -26.281  1.00 12.22           H  
ATOM   1294  HG  LEU A 292      -6.533   5.242 -28.080  1.00 14.06           H  
ATOM   1295 HD11 LEU A 292      -6.445   7.113 -26.704  1.00 16.45           H  
ATOM   1296 HD12 LEU A 292      -7.004   5.870 -25.888  1.00 16.45           H  
ATOM   1297 HD13 LEU A 292      -5.496   6.332 -25.697  1.00 16.45           H  
ATOM   1298 HD21 LEU A 292      -4.822   6.810 -28.487  1.00 16.89           H  
ATOM   1299 HD22 LEU A 292      -3.823   5.844 -27.717  1.00 16.89           H  
ATOM   1300 HD23 LEU A 292      -4.516   5.361 -29.062  1.00 16.89           H  
ATOM   1301  N   ALA A 293      -5.661   0.678 -26.971  1.00  7.90           N  
ANISOU 1301  N   ALA A 293      693   1154   1155     46   -145   -128       N  
ATOM   1302  CA  ALA A 293      -5.430  -0.492 -26.137  1.00  7.59           C  
ANISOU 1302  CA  ALA A 293      719   1140   1025    -14   -158   -136       C  
ATOM   1303  C   ALA A 293      -6.582  -1.439 -26.386  1.00  7.43           C  
ANISOU 1303  C   ALA A 293      716   1168    939     24   -156   -199       C  
ATOM   1304  O   ALA A 293      -7.621  -1.032 -26.879  1.00  8.47           O  
ANISOU 1304  O   ALA A 293      818   1201   1200    -56   -360    -64       O  
ATOM   1305  CB  ALA A 293      -5.412  -0.098 -24.661  1.00  7.98           C  
ANISOU 1305  CB  ALA A 293      678   1295   1059     10   -104   -336       C  
ATOM   1306  H   ALA A 293      -6.449   0.699 -27.315  1.00  9.49           H  
ATOM   1307  HA  ALA A 293      -4.592  -0.918 -26.374  1.00  9.12           H  
ATOM   1308  HB1 ALA A 293      -5.208  -0.881 -24.127  1.00  9.59           H  
ATOM   1309  HB2 ALA A 293      -4.734   0.582 -24.524  1.00  9.59           H  
ATOM   1310  HB3 ALA A 293      -6.284   0.250 -24.417  1.00  9.59           H  
ATOM   1311  N   LYS A 294      -6.440  -2.690 -25.959  1.00  7.35           N  
ANISOU 1311  N   LYS A 294      718   1166    908     29   -149   -250       N  
ATOM   1312  CA  LYS A 294      -7.595  -3.583 -26.032  1.00  7.34           C  
ANISOU 1312  CA  LYS A 294      756   1124    910    -22   -138   -313       C  
ATOM   1313  C   LYS A 294      -8.715  -3.075 -25.132  1.00  7.28           C  
ANISOU 1313  C   LYS A 294      718   1046   1001    -50   -231   -212       C  
ATOM   1314  O   LYS A 294      -9.866  -2.927 -25.572  1.00  7.94           O  
ANISOU 1314  O   LYS A 294      692   1294   1029     26   -282   -233       O  
ATOM   1315  CB  LYS A 294      -7.195  -5.016 -25.697  1.00  8.37           C  
ANISOU 1315  CB  LYS A 294      928   1164   1087     72   -184   -408       C  
ATOM   1316  CG  LYS A 294      -8.266  -5.985 -26.037  1.00 13.42           C  
ANISOU 1316  CG  LYS A 294     2001   1428   1672   -121   -370   -370       C  
ATOM   1317  CD  LYS A 294      -7.826  -7.410 -25.737  1.00 20.88           C  
ANISOU 1317  CD  LYS A 294     3612   2243   2079    -87    -94   -263       C  
ATOM   1318  CE  LYS A 294      -8.045  -8.366 -26.906  1.00 28.31           C  
ANISOU 1318  CE  LYS A 294     4950   3381   2424    143    205   -108       C  
ATOM   1319  NZ  LYS A 294      -7.053  -8.111 -27.999  1.00 32.54           N  
ANISOU 1319  NZ  LYS A 294     5654   4084   2624    207    383    -19       N  
ATOM   1320  H   LYS A 294      -5.721  -3.033 -25.636  1.00  8.83           H  
ATOM   1321  HA  LYS A 294      -7.929  -3.600 -26.943  1.00  8.82           H  
ATOM   1322  HB2 LYS A 294      -6.401  -5.252 -26.201  1.00 10.05           H  
ATOM   1323  HB3 LYS A 294      -7.017  -5.083 -24.746  1.00 10.05           H  
ATOM   1324  HG2 LYS A 294      -9.057  -5.791 -25.512  1.00 16.12           H  
ATOM   1325  HG3 LYS A 294      -8.472  -5.920 -26.983  1.00 16.12           H  
ATOM   1326  HD2 LYS A 294      -6.879  -7.409 -25.526  1.00 25.07           H  
ATOM   1327  HD3 LYS A 294      -8.334  -7.743 -24.981  1.00 25.07           H  
ATOM   1328  HE2 LYS A 294      -7.937  -9.280 -26.600  1.00 33.98           H  
ATOM   1329  HE3 LYS A 294      -8.937  -8.240 -27.265  1.00 33.98           H  
ATOM   1330  HZ1 LYS A 294      -7.193  -8.674 -28.674  1.00 39.05           H  
ATOM   1331  HZ2 LYS A 294      -7.137  -7.277 -28.297  1.00 39.05           H  
ATOM   1332  HZ3 LYS A 294      -6.226  -8.227 -27.692  1.00 39.05           H  
ATOM   1333  N   HIS A 295      -8.384  -2.796 -23.877  1.00  6.88           N  
ANISOU 1333  N   HIS A 295      608   1024    983    -20   -249   -216       N  
ATOM   1334  CA  HIS A 295      -9.305  -2.321 -22.868  1.00  6.35           C  
ANISOU 1334  CA  HIS A 295      509    960    942     42   -143   -227       C  
ATOM   1335  C   HIS A 295      -8.739  -1.097 -22.174  1.00  5.97           C  
ANISOU 1335  C   HIS A 295      442    952    873     32   -173   -140       C  
ATOM   1336  O   HIS A 295      -7.531  -0.917 -22.094  1.00  6.35           O  
ANISOU 1336  O   HIS A 295      456   1007    950     64   -144   -222       O  
ATOM   1337  CB  HIS A 295      -9.596  -3.402 -21.842  1.00  7.94           C  
ANISOU 1337  CB  HIS A 295      861    992   1163      7    -73   -117       C  
ATOM   1338  CG  HIS A 295     -10.435  -4.509 -22.405  1.00 11.09           C  
ANISOU 1338  CG  HIS A 295     1439   1160   1616   -189    -23   -126       C  
ATOM   1339  ND1 HIS A 295      -9.940  -5.750 -22.725  1.00 13.37           N  
ANISOU 1339  ND1 HIS A 295     1738   1200   2143    -38    -57   -235       N  
ATOM   1340  CD2 HIS A 295     -11.730  -4.505 -22.803  1.00 12.51           C  
ANISOU 1340  CD2 HIS A 295     1440   1523   1790   -545   -138   -218       C  
ATOM   1341  CE1 HIS A 295     -10.910  -6.475 -23.256  1.00 12.94           C  
ANISOU 1341  CE1 HIS A 295     1483   1172   2264   -405   -147   -406       C  
ATOM   1342  NE2 HIS A 295     -12.009  -5.750 -23.305  1.00 14.55           N  
ANISOU 1342  NE2 HIS A 295     1736   1622   2170   -644   -110   -346       N  
ATOM   1343  H   HIS A 295      -7.584  -2.880 -23.573  1.00  8.27           H  
ATOM   1344  HA  HIS A 295     -10.138  -2.060 -23.293  1.00  7.62           H  
ATOM   1345  HB2 HIS A 295      -8.758  -3.784 -21.536  1.00  9.54           H  
ATOM   1346  HB3 HIS A 295     -10.074  -3.010 -21.094  1.00  9.54           H  
ATOM   1347  HD2 HIS A 295     -12.321  -3.790 -22.747  1.00 15.02           H  
ATOM   1348  HE1 HIS A 295     -10.830  -7.355 -23.549  1.00 15.54           H  
ATOM   1349  HE2 HIS A 295     -12.773  -6.013 -23.601  1.00 17.47           H  
ATOM   1350  N   CYS A 296      -9.654  -0.273 -21.660  1.00  6.23           N  
ANISOU 1350  N   CYS A 296      395   1027    945     20   -152   -232       N  
ATOM   1351  CA  CYS A 296      -9.326   0.825 -20.770  1.00  5.95           C  
ANISOU 1351  CA  CYS A 296      383    962    916     19   -157   -169       C  
ATOM   1352  C   CYS A 296      -9.927   0.542 -19.409  1.00  5.93           C  
ANISOU 1352  C   CYS A 296      371    912    972    -53    -92   -165       C  
ATOM   1353  O   CYS A 296     -11.130   0.313 -19.291  1.00  6.60           O  
ANISOU 1353  O   CYS A 296      375   1084   1047    -58   -112   -164       O  
ATOM   1354  CB  CYS A 296      -9.810   2.159 -21.319  1.00  6.06           C  
ANISOU 1354  CB  CYS A 296      488    908    905     35   -173   -147       C  
ATOM   1355  SG  CYS A 296      -9.465   3.546 -20.198  1.00  6.43           S  
ANISOU 1355  SG  CYS A 296      555    917    970     44   -160   -180       S  
ATOM   1356  H   CYS A 296     -10.496  -0.338 -21.821  1.00  7.49           H  
ATOM   1357  HA  CYS A 296      -8.362   0.882 -20.675  1.00  7.15           H  
ATOM   1358  HB2 CYS A 296      -9.362   2.334 -22.161  1.00  7.28           H  
ATOM   1359  HB3 CYS A 296     -10.769   2.114 -21.456  1.00  7.28           H  
ATOM   1360  HG  CYS A 296      -9.881   4.559 -20.690  1.00  7.72           H  
ATOM   1361  N   LEU A 297      -9.075   0.527 -18.393  1.00  5.59           N  
ANISOU 1361  N   LEU A 297      327    884    911    -24    -58    -73       N  
ATOM   1362  CA  LEU A 297      -9.498   0.437 -17.002  1.00  5.57           C  
ANISOU 1362  CA  LEU A 297      307    943    868    -82     37   -102       C  
ATOM   1363  C   LEU A 297      -9.644   1.870 -16.494  1.00  5.45           C  
ANISOU 1363  C   LEU A 297      285    942    842    -97     -9    -31       C  
ATOM   1364  O   LEU A 297      -8.647   2.556 -16.267  1.00  5.65           O  
ANISOU 1364  O   LEU A 297      346    902    898      0    -15    -80       O  
ATOM   1365  CB  LEU A 297      -8.496  -0.361 -16.176  1.00  5.90           C  
ANISOU 1365  CB  LEU A 297      387    896    958    -49    -31    -79       C  
ATOM   1366  CG  LEU A 297      -8.879  -0.533 -14.703  1.00  6.34           C  
ANISOU 1366  CG  LEU A 297      521    921    966    -27     52     21       C  
ATOM   1367  CD1 LEU A 297     -10.071  -1.459 -14.535  1.00  7.49           C  
ANISOU 1367  CD1 LEU A 297      604   1077   1166    -45     92    160       C  
ATOM   1368  CD2 LEU A 297      -7.678  -1.038 -13.915  1.00  6.95           C  
ANISOU 1368  CD2 LEU A 297      596   1090    952    -13      5    100       C  
ATOM   1369  H   LEU A 297      -8.221   0.570 -18.486  1.00  6.71           H  
ATOM   1370  HA  LEU A 297     -10.351  -0.020 -16.931  1.00  6.70           H  
ATOM   1371  HB2 LEU A 297      -8.414  -1.247 -16.563  1.00  7.09           H  
ATOM   1372  HB3 LEU A 297      -7.640   0.094 -16.205  1.00  7.09           H  
ATOM   1373  HG  LEU A 297      -9.146   0.328 -14.345  1.00  7.61           H  
ATOM   1374 HD11 LEU A 297     -10.261  -1.560 -13.590  1.00  9.00           H  
ATOM   1375 HD12 LEU A 297     -10.837  -1.072 -14.987  1.00  9.00           H  
ATOM   1376 HD13 LEU A 297      -9.858  -2.321 -14.925  1.00  9.00           H  
ATOM   1377 HD21 LEU A 297      -7.936  -1.158 -12.988  1.00  8.34           H  
ATOM   1378 HD22 LEU A 297      -7.388  -1.885 -14.290  1.00  8.34           H  
ATOM   1379 HD23 LEU A 297      -6.963  -0.386 -13.978  1.00  8.34           H  
ATOM   1380  N   HIS A 298     -10.882   2.324 -16.340  1.00  5.63           N  
ANISOU 1380  N   HIS A 298      350    854    934    -63    -11   -126       N  
ATOM   1381  CA  HIS A 298     -11.171   3.650 -15.815  1.00  5.74           C  
ANISOU 1381  CA  HIS A 298      379    864    938    -76     42   -114       C  
ATOM   1382  C   HIS A 298     -11.156   3.564 -14.299  1.00  5.97           C  
ANISOU 1382  C   HIS A 298      415    940    916    -10    -12    -98       C  
ATOM   1383  O   HIS A 298     -12.004   2.884 -13.720  1.00  7.07           O  
ANISOU 1383  O   HIS A 298      547   1169    968   -213     63     -3       O  
ATOM   1384  CB  HIS A 298     -12.539   4.111 -16.306  1.00  6.09           C  
ANISOU 1384  CB  HIS A 298      404    941    970    -20    -42    -99       C  
ATOM   1385  CG  HIS A 298     -12.617   4.315 -17.778  1.00  5.88           C  
ANISOU 1385  CG  HIS A 298      400    813   1020     52   -111    -94       C  
ATOM   1386  ND1 HIS A 298     -12.240   5.498 -18.388  1.00  6.48           N  
ANISOU 1386  ND1 HIS A 298      480    956   1027     43   -142   -104       N  
ATOM   1387  CD2 HIS A 298     -12.983   3.451 -18.757  1.00  6.38           C  
ANISOU 1387  CD2 HIS A 298      578    866    983     44   -163    -45       C  
ATOM   1388  CE1 HIS A 298     -12.397   5.335 -19.689  1.00  6.43           C  
ANISOU 1388  CE1 HIS A 298      527    958    960     -6   -145    -56       C  
ATOM   1389  NE2 HIS A 298     -12.850   4.111 -19.941  1.00  6.75           N  
ANISOU 1389  NE2 HIS A 298      561   1017    987     32   -240   -169       N  
ATOM   1390  H   HIS A 298     -11.587   1.871 -16.536  1.00  6.76           H  
ATOM   1391  HA  HIS A 298     -10.499   4.284 -16.112  1.00  6.90           H  
ATOM   1392  HB2 HIS A 298     -13.198   3.440 -16.067  1.00  7.32           H  
ATOM   1393  HB3 HIS A 298     -12.755   4.955 -15.880  1.00  7.32           H  
ATOM   1394  HD2 HIS A 298     -13.269   2.574 -18.642  1.00  7.67           H  
ATOM   1395  HE1 HIS A 298     -12.216   5.981 -20.333  1.00  7.73           H  
ATOM   1396  HE2 HIS A 298     -13.030   3.791 -20.718  1.00  8.11           H  
ATOM   1397  N   VAL A 299     -10.177   4.201 -13.655  1.00  5.73           N  
ANISOU 1397  N   VAL A 299      411    873    892    -60     29    -90       N  
ATOM   1398  CA  VAL A 299      -9.994   4.120 -12.209  1.00  6.00           C  
ANISOU 1398  CA  VAL A 299      555    904    819    -51     52    -18       C  
ATOM   1399  C   VAL A 299     -10.196   5.500 -11.613  1.00  6.11           C  
ANISOU 1399  C   VAL A 299      533    947    840    -59     14    -95       C  
ATOM   1400  O   VAL A 299      -9.596   6.464 -12.102  1.00  6.44           O  
ANISOU 1400  O   VAL A 299      619    964    864    -81    120   -120       O  
ATOM   1401  CB  VAL A 299      -8.591   3.602 -11.849  1.00  6.26           C  
ANISOU 1401  CB  VAL A 299      516    960    901   -100     62    -26       C  
ATOM   1402  CG1 VAL A 299      -8.417   3.573 -10.333  1.00  7.44           C  
ANISOU 1402  CG1 VAL A 299      741   1132    954     15    -23    -95       C  
ATOM   1403  CG2 VAL A 299      -8.372   2.247 -12.467  1.00  6.84           C  
ANISOU 1403  CG2 VAL A 299      574    984   1042    -32     38     -3       C  
ATOM   1404  H   VAL A 299      -9.593   4.697 -14.046  1.00  6.88           H  
ATOM   1405  HA  VAL A 299     -10.663   3.522 -11.842  1.00  7.20           H  
ATOM   1406  HB  VAL A 299      -7.915   4.198 -12.206  1.00  7.52           H  
ATOM   1407 HG11 VAL A 299      -7.629   3.049 -10.116  1.00  8.94           H  
ATOM   1408 HG12 VAL A 299      -8.310   4.481 -10.010  1.00  8.94           H  
ATOM   1409 HG13 VAL A 299      -9.203   3.169  -9.933  1.00  8.94           H  
ATOM   1410 HG21 VAL A 299      -7.511   1.904 -12.181  1.00  8.22           H  
ATOM   1411 HG22 VAL A 299      -9.079   1.649 -12.177  1.00  8.22           H  
ATOM   1412 HG23 VAL A 299      -8.389   2.334 -13.433  1.00  8.22           H  
ATOM   1413  N   VAL A 300     -10.980   5.589 -10.549  1.00  6.42           N  
ANISOU 1413  N   VAL A 300      599   1003    837    -87    150    -90       N  
ATOM   1414  CA  VAL A 300     -11.220   6.862  -9.875  1.00  6.52           C  
ANISOU 1414  CA  VAL A 300      662    978    836    -64    197   -137       C  
ATOM   1415  C   VAL A 300     -10.363   6.939  -8.616  1.00  6.70           C  
ANISOU 1415  C   VAL A 300      678   1057    810    -14    175   -146       C  
ATOM   1416  O   VAL A 300     -10.660   6.315  -7.591  1.00  7.55           O  
ANISOU 1416  O   VAL A 300      754   1212    902    -50    207    -70       O  
ATOM   1417  CB  VAL A 300     -12.696   7.067  -9.535  1.00  7.35           C  
ANISOU 1417  CB  VAL A 300      634   1142   1015     -4    208   -152       C  
ATOM   1418  CG1 VAL A 300     -12.867   8.453  -8.927  1.00  7.85           C  
ANISOU 1418  CG1 VAL A 300      718   1249   1015     63    241   -115       C  
ATOM   1419  CG2 VAL A 300     -13.553   6.895 -10.760  1.00  7.98           C  
ANISOU 1419  CG2 VAL A 300      640   1246   1146    -28     66   -182       C  
ATOM   1420  H   VAL A 300     -11.390   4.921 -10.195  1.00  7.71           H  
ATOM   1421  HA  VAL A 300     -10.921   7.560 -10.478  1.00  7.83           H  
ATOM   1422  HB  VAL A 300     -12.989   6.402  -8.893  1.00  8.82           H  
ATOM   1423 HG11 VAL A 300     -13.813   8.664  -8.881  1.00  9.43           H  
ATOM   1424 HG12 VAL A 300     -12.484   8.456  -8.035  1.00  9.43           H  
ATOM   1425 HG13 VAL A 300     -12.411   9.102  -9.485  1.00  9.43           H  
ATOM   1426 HG21 VAL A 300     -14.475   7.090 -10.531  1.00  9.58           H  
ATOM   1427 HG22 VAL A 300     -13.247   7.506 -11.448  1.00  9.58           H  
ATOM   1428 HG23 VAL A 300     -13.477   5.979 -11.073  1.00  9.58           H  
ATOM   1429  N   GLY A 301      -9.284   7.714  -8.673  1.00  6.59           N  
ANISOU 1429  N   GLY A 301      656   1021    825     -6    139    -73       N  
ATOM   1430  CA  GLY A 301      -8.556   8.044  -7.474  1.00  6.92           C  
ANISOU 1430  CA  GLY A 301      791   1016    822    -48     84    -90       C  
ATOM   1431  C   GLY A 301      -9.189   9.228  -6.766  1.00  6.86           C  
ANISOU 1431  C   GLY A 301      742   1031    834    -82    191    -43       C  
ATOM   1432  O   GLY A 301      -9.955   9.983  -7.361  1.00  7.30           O  
ANISOU 1432  O   GLY A 301      826   1050    900     -8    202    -82       O  
ATOM   1433  H   GLY A 301      -8.962   8.054  -9.394  1.00  7.91           H  
ATOM   1434  HA2 GLY A 301      -8.556   7.283  -6.872  1.00  8.32           H  
ATOM   1435  HA3 GLY A 301      -7.639   8.268  -7.700  1.00  8.32           H  
ATOM   1436  N   PRO A 302      -8.874   9.408  -5.484  1.00  7.27           N  
ANISOU 1436  N   PRO A 302     1004    937    823    -70    249    -98       N  
ATOM   1437  CA  PRO A 302      -9.405  10.559  -4.757  1.00  7.84           C  
ANISOU 1437  CA  PRO A 302     1080   1034    864    -78    323   -128       C  
ATOM   1438  C   PRO A 302      -8.841  11.860  -5.295  1.00  7.51           C  
ANISOU 1438  C   PRO A 302      937   1069    846    -69    396   -143       C  
ATOM   1439  O   PRO A 302      -7.648  11.999  -5.552  1.00  7.70           O  
ANISOU 1439  O   PRO A 302      985   1076    865    -61    313   -108       O  
ATOM   1440  CB  PRO A 302      -8.952  10.306  -3.310  1.00  8.69           C  
ANISOU 1440  CB  PRO A 302     1321   1150    831   -151    396   -146       C  
ATOM   1441  CG  PRO A 302      -7.713   9.447  -3.442  1.00  8.52           C  
ANISOU 1441  CG  PRO A 302     1259   1202    777   -184    271   -120       C  
ATOM   1442  CD  PRO A 302      -8.009   8.558  -4.636  1.00  7.86           C  
ANISOU 1442  CD  PRO A 302     1123   1027    835    -49    200    -41       C  
ATOM   1443  HA  PRO A 302     -10.374  10.579  -4.800  1.00  9.41           H  
ATOM   1444  HB2 PRO A 302      -8.748  11.148  -2.875  1.00 10.44           H  
ATOM   1445  HB3 PRO A 302      -9.649   9.840  -2.821  1.00 10.44           H  
ATOM   1446  HG2 PRO A 302      -6.935  10.004  -3.604  1.00 10.24           H  
ATOM   1447  HG3 PRO A 302      -7.583   8.921  -2.638  1.00 10.24           H  
ATOM   1448  HD2 PRO A 302      -7.191   8.323  -5.103  1.00  9.44           H  
ATOM   1449  HD3 PRO A 302      -8.477   7.754  -4.361  1.00  9.44           H  
ATOM   1450  N   ASN A 303      -9.727  12.835  -5.420  1.00  7.86           N  
ANISOU 1450  N   ASN A 303     1012    970   1005    -44    396    -83       N  
ATOM   1451  CA  ASN A 303      -9.350  14.201  -5.763  1.00  8.14           C  
ANISOU 1451  CA  ASN A 303     1104    899   1090    -53    494    -59       C  
ATOM   1452  C   ASN A 303      -9.168  14.954  -4.452  1.00  8.69           C  
ANISOU 1452  C   ASN A 303     1400    864   1039    -26    592    -58       C  
ATOM   1453  O   ASN A 303     -10.131  15.482  -3.869  1.00  9.38           O  
ANISOU 1453  O   ASN A 303     1255   1056   1255     54    718   -118       O  
ATOM   1454  CB  ASN A 303     -10.397  14.801  -6.678  1.00  9.57           C  
ANISOU 1454  CB  ASN A 303     1276   1005   1356    -77    525     67       C  
ATOM   1455  CG  ASN A 303      -9.967  16.129  -7.221  1.00 10.89           C  
ANISOU 1455  CG  ASN A 303     1267   1230   1642     87    633    132       C  
ATOM   1456  OD1 ASN A 303      -9.293  16.897  -6.541  1.00 11.03           O  
ANISOU 1456  OD1 ASN A 303     1157   1096   1936    -85    692     38       O  
ATOM   1457  ND2 ASN A 303     -10.312  16.397  -8.459  1.00 12.89           N  
ANISOU 1457  ND2 ASN A 303     1818   1418   1663     74    456    395       N  
ATOM   1458  H   ASN A 303     -10.574  12.730  -5.309  1.00  9.44           H  
ATOM   1459  HA  ASN A 303      -8.503  14.233  -6.235  1.00  9.78           H  
ATOM   1460  HB2 ASN A 303     -10.549  14.202  -7.426  1.00 11.50           H  
ATOM   1461  HB3 ASN A 303     -11.221  14.928  -6.182  1.00 11.50           H  
ATOM   1462 HD21 ASN A 303     -10.088  17.148  -8.814  1.00 15.48           H  
ATOM   1463 HD22 ASN A 303     -10.762  15.823  -8.914  1.00 15.48           H  
ATOM   1464  N  AVAL A 304      -7.925  14.934  -3.937  0.59  7.52           N  
ATOM   1465  N  BVAL A 304      -7.938  14.948  -3.963  0.42  7.52           N  
ATOM   1466  CA AVAL A 304      -7.661  15.482  -2.606  0.59  8.52           C  
ATOM   1467  CA BVAL A 304      -7.636  15.700  -2.755  0.42 10.99           C  
ATOM   1468  C  AVAL A 304      -7.717  17.003  -2.589  0.59  7.19           C  
ATOM   1469  C  BVAL A 304      -8.087  17.156  -2.916  0.42  5.96           C  
ATOM   1470  O  AVAL A 304      -8.036  17.607  -1.569  0.59  7.04           O  
ATOM   1471  O  BVAL A 304      -8.717  17.730  -2.018  0.42  7.53           O  
ATOM   1472  CB AVAL A 304      -6.328  15.023  -1.997  0.59 12.77           C  
ATOM   1473  CB BVAL A 304      -6.138  15.548  -2.427  0.42 15.12           C  
ATOM   1474  CG1AVAL A 304      -6.258  13.526  -1.984  0.59 13.42           C  
ATOM   1475  CG1BVAL A 304      -5.809  16.180  -1.100  0.42 16.25           C  
ATOM   1476  CG2AVAL A 304      -5.161  15.637  -2.748  0.59 15.54           C  
ATOM   1477  CG2BVAL A 304      -5.724  14.071  -2.427  0.42 17.04           C  
ATOM   1478  H  AVAL A 304      -7.233  14.613  -4.335  0.59  9.03           H  
ATOM   1479  H  BVAL A 304      -7.271  14.526  -4.305  0.42  9.03           H  
ATOM   1480  HA AVAL A 304      -8.375  15.119  -2.059  0.59 10.23           H  
ATOM   1481  HA BVAL A 304      -8.132  15.343  -2.002  0.42 13.19           H  
ATOM   1482  HB AVAL A 304      -6.268  15.328  -1.078  0.59 15.33           H  
ATOM   1483  HB BVAL A 304      -5.631  16.007  -3.115  0.42 18.15           H  
ATOM   1484 HG11AVAL A 304      -5.529  13.250  -1.406  0.59 16.11           H  
ATOM   1485 HG11BVAL A 304      -5.498  15.493  -0.491  0.42 19.51           H  
ATOM   1486 HG12AVAL A 304      -7.098  13.174  -1.649  0.59 16.11           H  
ATOM   1487 HG12BVAL A 304      -5.116  16.846  -1.230  0.42 19.51           H  
ATOM   1488 HG13AVAL A 304      -6.103  13.209  -2.887  0.59 16.11           H  
ATOM   1489 HG13BVAL A 304      -6.608  16.600  -0.744  0.42 19.51           H  
ATOM   1490 HG21AVAL A 304      -4.353  15.146  -2.531  0.59 18.65           H  
ATOM   1491 HG21BVAL A 304      -4.846  13.989  -2.024  0.42 20.45           H  
ATOM   1492 HG22AVAL A 304      -5.335  15.583  -3.700  0.59 18.65           H  
ATOM   1493 HG22BVAL A 304      -6.372  13.562  -1.915  0.42 20.45           H  
ATOM   1494 HG23AVAL A 304      -5.066  16.564  -2.480  0.59 18.65           H  
ATOM   1495 HG23BVAL A 304      -5.700  13.750  -3.342  0.42 20.45           H  
ATOM   1496  N  AASN A 305      -7.454  17.655  -3.709  0.59  7.32           N  
ATOM   1497  N  BASN A 305      -7.851  17.744  -4.093  0.42  4.87           N  
ATOM   1498  CA AASN A 305      -7.699  19.098  -3.783  0.59  6.60           C  
ATOM   1499  CA BASN A 305      -8.113  19.185  -4.283  0.42  5.08           C  
ATOM   1500  C  AASN A 305      -9.167  19.463  -3.609  0.59  6.25           C  
ATOM   1501  C  BASN A 305      -9.591  19.490  -4.173  0.42  5.48           C  
ATOM   1502  O  AASN A 305      -9.501  20.603  -3.284  0.59  6.98           O  
ATOM   1503  O  BASN A 305     -10.004  20.651  -4.119  0.42  6.61           O  
ATOM   1504  CB AASN A 305      -7.223  19.591  -5.139  0.59  5.59           C  
ATOM   1505  CB BASN A 305      -7.545  19.625  -5.625  0.42  5.09           C  
ATOM   1506  CG AASN A 305      -5.746  19.637  -5.233  0.59  6.26           C  
ATOM   1507  CG BASN A 305      -6.052  19.743  -5.580  0.42  5.36           C  
ATOM   1508  OD1AASN A 305      -5.074  19.697  -4.218  0.59  7.51           O  
ATOM   1509  OD1BASN A 305      -5.445  19.870  -4.502  0.42  8.93           O  
ATOM   1510  ND2AASN A 305      -5.212  19.673  -6.438  0.59  5.26           N  
ATOM   1511  ND2BASN A 305      -5.442  19.748  -6.758  0.42  5.96           N  
ATOM   1512  H  AASN A 305      -7.141  17.301  -4.428  0.59  8.79           H  
ATOM   1513  H  BASN A 305      -7.544  17.342  -4.788  0.42  5.85           H  
ATOM   1514  HA AASN A 305      -7.206  19.539  -3.074  0.59  7.93           H  
ATOM   1515  HA BASN A 305      -7.660  19.712  -3.607  0.42  6.10           H  
ATOM   1516  HB2AASN A 305      -7.552  18.993  -5.828  0.59  6.71           H  
ATOM   1517  HB2BASN A 305      -7.779  18.971  -6.302  0.42  6.11           H  
ATOM   1518  HB3AASN A 305      -7.563  20.487  -5.288  0.59  6.71           H  
ATOM   1519  HB3BASN A 305      -7.913  20.492  -5.859  0.42  6.11           H  
ATOM   1520 HD21AASN A 305      -4.357  19.700  -6.529  0.59  6.32           H  
ATOM   1521 HD21BASN A 305      -4.585  19.813  -6.798  0.42  7.16           H  
ATOM   1522 HD22AASN A 305      -5.718  19.670  -7.133  0.59  6.32           H  
ATOM   1523 HD22BASN A 305      -5.903  19.686  -7.481  0.42  7.16           H  
ATOM   1524  N  ALYS A 306     -10.076  18.543  -3.872  0.59  8.11           N  
ATOM   1525  N  BLYS A 306     -10.381  18.450  -4.067  0.42  6.84           N  
ATOM   1526  CA ALYS A 306     -11.522  18.741  -3.753  0.59  7.31           C  
ATOM   1527  CA BLYS A 306     -11.736  18.576  -3.587  0.42 11.47           C  
ATOM   1528  C  ALYS A 306     -12.100  18.085  -2.518  0.59  7.64           C  
ATOM   1529  C  BLYS A 306     -11.942  17.951  -2.206  0.42  8.59           C  
ATOM   1530  O  ALYS A 306     -13.318  18.019  -2.336  0.59 10.37           O  
ATOM   1531  O  BLYS A 306     -13.092  17.782  -1.788  0.42 12.66           O  
ATOM   1532  CB ALYS A 306     -12.266  18.213  -4.984  0.59  9.13           C  
ATOM   1533  CB BLYS A 306     -12.669  18.033  -4.662  0.42 14.80           C  
ATOM   1534  CG ALYS A 306     -12.113  18.995  -6.345  0.59 15.37           C  
ATOM   1535  CG BLYS A 306     -12.427  18.683  -6.035  0.42 15.39           C  
ATOM   1536  CD ALYS A 306     -12.701  20.413  -6.327  0.59 16.16           C  
ATOM   1537  CD BLYS A 306     -12.694  20.195  -5.993  0.42 15.60           C  
ATOM   1538  CE ALYS A 306     -12.625  21.107  -7.701  0.59 19.27           C  
ATOM   1539  CE BLYS A 306     -12.695  20.825  -7.386  0.42 21.73           C  
ATOM   1540  NZ ALYS A 306     -12.991  22.556  -7.617  0.59 22.68           N  
ATOM   1541  NZ BLYS A 306     -13.255  22.212  -7.363  0.42 19.71           N  
ATOM   1542  H  ALYS A 306      -9.876  17.749  -4.136  0.59  9.74           H  
ATOM   1543  H  BLYS A 306     -10.153  17.646  -4.271  0.42  8.21           H  
ATOM   1544  HA ALYS A 306     -11.674  19.698  -3.703  0.59  8.78           H  
ATOM   1545  HA BLYS A 306     -11.969  19.508  -3.451  0.42 13.77           H  
ATOM   1546  HB2ALYS A 306     -11.956  17.309  -5.149  0.59 10.96           H  
ATOM   1547  HB2BLYS A 306     -12.527  17.078  -4.752  0.42 17.77           H  
ATOM   1548  HB3ALYS A 306     -13.213  18.207  -4.775  0.59 10.96           H  
ATOM   1549  HB3BLYS A 306     -13.587  18.209  -4.403  0.42 17.77           H  
ATOM   1550  HG2ALYS A 306     -11.169  19.073  -6.555  0.59 18.45           H  
ATOM   1551  HG2BLYS A 306     -11.504  18.544  -6.298  0.42 18.47           H  
ATOM   1552  HG3ALYS A 306     -12.568  18.498  -7.043  0.59 18.45           H  
ATOM   1553  HG3BLYS A 306     -13.022  18.286  -6.689  0.42 18.47           H  
ATOM   1554  HD2ALYS A 306     -13.635  20.365  -6.067  0.59 19.40           H  
ATOM   1555  HD2BLYS A 306     -13.563  20.353  -5.591  0.42 18.73           H  
ATOM   1556  HD3ALYS A 306     -12.207  20.953  -5.691  0.59 19.40           H  
ATOM   1557  HD3BLYS A 306     -12.002  20.626  -5.468  0.42 18.73           H  
ATOM   1558  HE2ALYS A 306     -11.719  21.042  -8.042  0.59 23.13           H  
ATOM   1559  HE2BLYS A 306     -11.785  20.870  -7.719  0.42 26.08           H  
ATOM   1560  HE3ALYS A 306     -13.241  20.674  -8.313  0.59 23.13           H  
ATOM   1561  HE3BLYS A 306     -13.240  20.287  -7.982  0.42 26.08           H  
ATOM   1562  HZ1ALYS A 306     -13.830  22.642  -7.333  0.59 27.22           H  
ATOM   1563  HZ1BLYS A 306     -12.655  22.776  -7.025  0.42 23.66           H  
ATOM   1564  HZ2ALYS A 306     -12.450  22.974  -7.047  0.59 27.22           H  
ATOM   1565  HZ2BLYS A 306     -13.461  22.471  -8.189  0.42 23.66           H  
ATOM   1566  HZ3ALYS A 306     -12.917  22.936  -8.418  0.59 27.22           H  
ATOM   1567  HZ3BLYS A 306     -13.989  22.236  -6.861  0.42 23.66           H  
ATOM   1568  N  AGLY A 307     -11.283  17.655  -1.618  0.59 11.04           N  
ANISOU 1568  N  AGLY A 307     1227   1360   1609   -307    788   -335       N  
ATOM   1569  N  BGLY A 307     -10.889  17.753  -1.425  0.42  6.08           N  
ANISOU 1569  N  BGLY A 307      407   1139    764     37   -117    -88       N  
ATOM   1570  CA AGLY A 307     -11.860  17.168  -0.406  0.59 12.44           C  
ANISOU 1570  CA AGLY A 307     1766   1168   1793   -202    798   -386       C  
ATOM   1571  CA BGLY A 307     -11.131  17.242  -0.087  0.42  6.04           C  
ANISOU 1571  CA BGLY A 307      684    936    673     79    225   -145       C  
ATOM   1572  C  AGLY A 307     -12.323  15.743  -0.497  0.59 11.96           C  
ANISOU 1572  C  AGLY A 307     1572   1332   1641   -160    876   -457       C  
ATOM   1573  C  BGLY A 307     -11.477  15.769   0.002  0.42  5.82           C  
ANISOU 1573  C  BGLY A 307      495   1020    695     79    181   -249       C  
ATOM   1574  O  AGLY A 307     -13.301  15.386   0.157  0.59 14.83           O  
ANISOU 1574  O  AGLY A 307     2136   1693   1807   -480   1124   -399       O  
ATOM   1575  O  BGLY A 307     -11.863  15.292   1.080  0.42  6.61           O  
ANISOU 1575  O  BGLY A 307      913    988    612    148    393    -97       O  
ATOM   1576  H  AGLY A 307     -10.426  17.632  -1.677  0.59 13.26           H  
ATOM   1577  H  BGLY A 307     -10.068  17.899  -1.637  0.42  7.31           H  
ATOM   1578  HA2AGLY A 307     -11.202  17.227   0.304  0.59 14.94           H  
ATOM   1579  HA2BGLY A 307     -10.335  17.388   0.447  0.42  7.25           H  
ATOM   1580  HA3AGLY A 307     -12.624  17.720  -0.175  0.59 14.94           H  
ATOM   1581  HA3BGLY A 307     -11.868  17.739   0.303  0.42  7.25           H  
ATOM   1582  N  AGLU A 308     -11.663  14.922  -1.301  0.59  8.41           N  
ATOM   1583  N  BGLU A 308     -11.347  15.036  -1.090  0.42  8.70           N  
ATOM   1584  CA AGLU A 308     -11.810  13.475  -1.213  0.59 10.29           C  
ATOM   1585  CA BGLU A 308     -11.618  13.610  -1.065  0.42 10.04           C  
ATOM   1586  C  AGLU A 308     -10.617  12.914  -0.434  0.59  9.20           C  
ATOM   1587  C  BGLU A 308     -10.506  12.924  -0.303  0.42  9.28           C  
ATOM   1588  O  AGLU A 308      -9.516  13.463  -0.490  0.59 10.51           O  
ATOM   1589  O  BGLU A 308      -9.369  13.405  -0.212  0.42 10.46           O  
ATOM   1590  CB AGLU A 308     -11.959  12.869  -2.620  0.59  9.28           C  
ATOM   1591  CB BGLU A 308     -11.782  13.053  -2.481  0.42  9.23           C  
ATOM   1592  CG AGLU A 308     -13.192  13.432  -3.329  0.59 10.43           C  
ATOM   1593  CG BGLU A 308     -12.980  13.652  -3.203  0.42 10.72           C  
ATOM   1594  CD AGLU A 308     -13.431  12.989  -4.771  0.59  9.83           C  
ATOM   1595  CD BGLU A 308     -13.157  13.145  -4.619  0.42  9.52           C  
ATOM   1596  OE1AGLU A 308     -12.526  12.445  -5.453  0.59  8.69           O  
ATOM   1597  OE1BGLU A 308     -12.323  12.318  -5.070  0.42  8.22           O  
ATOM   1598  OE2AGLU A 308     -14.567  13.230  -5.230  0.59 13.74           O  
ATOM   1599  OE2BGLU A 308     -14.122  13.587  -5.295  0.42 13.74           O  
ATOM   1600  H  AGLU A 308     -11.118  15.182  -1.914  0.59 10.10           H  
ATOM   1601  H  BGLU A 308     -11.104  15.339  -1.858  0.42 10.45           H  
ATOM   1602  HA AGLU A 308     -12.611  13.214  -0.732  0.59 12.35           H  
ATOM   1603  HA BGLU A 308     -12.457  13.421  -0.618  0.42 12.05           H  
ATOM   1604  HB2AGLU A 308     -11.174  13.083  -3.148  0.59 11.14           H  
ATOM   1605  HB2BGLU A 308     -10.986  13.257  -2.997  0.42 11.08           H  
ATOM   1606  HB3AGLU A 308     -12.057  11.907  -2.547  0.59 11.14           H  
ATOM   1607  HB3BGLU A 308     -11.908  12.093  -2.432  0.42 11.08           H  
ATOM   1608  HG2AGLU A 308     -13.975  13.170  -2.821  0.59 12.52           H  
ATOM   1609  HG2BGLU A 308     -13.785  13.433  -2.707  0.42 12.87           H  
ATOM   1610  HG3AGLU A 308     -13.114  14.399  -3.342  0.59 12.52           H  
ATOM   1611  HG3BGLU A 308     -12.869  14.615  -3.245  0.42 12.87           H  
ATOM   1612  N   ASP A 309     -10.838  11.813   0.297  1.00 10.83           N  
ANISOU 1612  N   ASP A 309     1572   1358   1184   -162    614     75       N  
ATOM   1613  CA  ASP A 309      -9.899  11.261   1.258  1.00 11.86           C  
ANISOU 1613  CA  ASP A 309     1755   1754    996    -77    470     22       C  
ATOM   1614  C   ASP A 309      -8.735  10.564   0.570  1.00 10.58           C  
ANISOU 1614  C   ASP A 309     1700   1501    820   -131    483   -158       C  
ATOM   1615  O   ASP A 309      -8.927   9.582  -0.147  1.00 10.77           O  
ANISOU 1615  O   ASP A 309     1760   1508    824   -279    398   -109       O  
ATOM   1616  CB  ASP A 309     -10.648  10.286   2.150  1.00 14.35           C  
ANISOU 1616  CB  ASP A 309     2033   2306   1112    -11    626    264       C  
ATOM   1617  CG  ASP A 309      -9.853   9.892   3.364  1.00 17.42           C  
ANISOU 1617  CG  ASP A 309     2433   3034   1152    -67    685    264       C  
ATOM   1618  OD1 ASP A 309      -8.615  10.017   3.386  1.00 16.71           O  
ANISOU 1618  OD1 ASP A 309     2385   3006    957    216    492    -62       O  
ATOM   1619  OD2 ASP A 309     -10.497   9.478   4.340  1.00 20.40           O  
ANISOU 1619  OD2 ASP A 309     2817   3560   1375   -187    748    497       O  
ATOM   1620  H   ASP A 309     -11.561  11.350   0.248  1.00 13.01           H  
ATOM   1621  HA  ASP A 309      -9.520  11.981   1.786  1.00 14.24           H  
ATOM   1622  HB2 ASP A 309     -11.473  10.699   2.451  1.00 17.23           H  
ATOM   1623  HB3 ASP A 309     -10.846   9.481   1.645  1.00 17.23           H  
ATOM   1624  N   ILE A 310      -7.527  11.076   0.813  1.00 10.75           N  
ANISOU 1624  N   ILE A 310     1602   1489    995   -113    369   -305       N  
ATOM   1625  CA  ILE A 310      -6.309  10.476   0.274  1.00 10.61           C  
ANISOU 1625  CA  ILE A 310     1574   1387   1072     -9    308   -265       C  
ATOM   1626  C   ILE A 310      -6.207   9.002   0.628  1.00 10.56           C  
ANISOU 1626  C   ILE A 310     1660   1407    944   -110    307   -213       C  
ATOM   1627  O   ILE A 310      -5.580   8.237  -0.105  1.00 10.56           O  
ANISOU 1627  O   ILE A 310     1646   1402    964    -73    396   -258       O  
ATOM   1628  CB  ILE A 310      -5.087  11.285   0.763  1.00 12.46           C  
ANISOU 1628  CB  ILE A 310     1693   1498   1542   -234    287   -354       C  
ATOM   1629  CG1 ILE A 310      -3.790  10.830   0.109  1.00 14.62           C  
ANISOU 1629  CG1 ILE A 310     2024   1603   1929   -269    460   -360       C  
ATOM   1630  CG2 ILE A 310      -4.931  11.188   2.276  1.00 13.41           C  
ANISOU 1630  CG2 ILE A 310     1888   1539   1667   -215     96   -303       C  
ATOM   1631  CD1 ILE A 310      -3.765  10.945  -1.380  1.00 16.49           C  
ANISOU 1631  CD1 ILE A 310     2444   1669   2153    -70    521   -229       C  
ATOM   1632  H   ILE A 310      -7.384  11.777   1.290  1.00 12.91           H  
ATOM   1633  HA  ILE A 310      -6.336  10.521  -0.694  1.00 12.74           H  
ATOM   1634  HB  ILE A 310      -5.259  12.203   0.504  1.00 14.96           H  
ATOM   1635 HG12 ILE A 310      -3.064  11.371   0.456  1.00 17.56           H  
ATOM   1636 HG13 ILE A 310      -3.643   9.897   0.332  1.00 17.56           H  
ATOM   1637 HG21 ILE A 310      -4.217  11.780   2.558  1.00 16.10           H  
ATOM   1638 HG22 ILE A 310      -5.765  11.452   2.696  1.00 16.10           H  
ATOM   1639 HG23 ILE A 310      -4.716  10.273   2.513  1.00 16.10           H  
ATOM   1640 HD11 ILE A 310      -2.897  10.659  -1.705  1.00 19.80           H  
ATOM   1641 HD12 ILE A 310      -4.461  10.380  -1.753  1.00 19.80           H  
ATOM   1642 HD13 ILE A 310      -3.922  11.870  -1.628  1.00 19.80           H  
ATOM   1643  N   GLN A 311      -6.807   8.583   1.747  1.00 11.02           N  
ANISOU 1643  N   GLN A 311     1868   1450    868   -136    295   -203       N  
ATOM   1644  CA  GLN A 311      -6.725   7.191   2.164  1.00 12.60           C  
ANISOU 1644  CA  GLN A 311     2143   1623   1022   -299    343    -43       C  
ATOM   1645  C   GLN A 311      -7.336   6.241   1.143  1.00 12.48           C  
ANISOU 1645  C   GLN A 311     2001   1578   1164   -183    428   -137       C  
ATOM   1646  O   GLN A 311      -6.982   5.062   1.134  1.00 13.98           O  
ANISOU 1646  O   GLN A 311     2292   1518   1502   -203    270   -160       O  
ATOM   1647  CB  GLN A 311      -7.437   7.009   3.505  1.00 17.29           C  
ANISOU 1647  CB  GLN A 311     3072   2104   1394   -488    367    210       C  
ATOM   1648  CG  GLN A 311      -7.374   5.604   4.055  1.00 24.11           C  
ANISOU 1648  CG  GLN A 311     4183   2904   2073   -303    272    358       C  
ATOM   1649  CD  GLN A 311      -5.962   5.188   4.394  1.00 30.45           C  
ANISOU 1649  CD  GLN A 311     5134   3659   2776   -154     92    399       C  
ATOM   1650  OE1 GLN A 311      -5.148   6.010   4.818  1.00 33.27           O  
ANISOU 1650  OE1 GLN A 311     5589   4037   3015   -134     63    474       O  
ATOM   1651  NE2 GLN A 311      -5.659   3.907   4.208  1.00 32.76           N  
ANISOU 1651  NE2 GLN A 311     5463   3908   3077     12     33    297       N  
ATOM   1652  H   GLN A 311      -7.263   9.086   2.276  1.00 13.23           H  
ATOM   1653  HA  GLN A 311      -5.790   6.960   2.272  1.00 15.13           H  
ATOM   1654  HB2 GLN A 311      -7.027   7.598   4.157  1.00 20.76           H  
ATOM   1655  HB3 GLN A 311      -8.373   7.239   3.393  1.00 20.76           H  
ATOM   1656  HG2 GLN A 311      -7.907   5.555   4.864  1.00 28.94           H  
ATOM   1657  HG3 GLN A 311      -7.720   4.987   3.391  1.00 28.94           H  
ATOM   1658 HE21 GLN A 311      -6.254   3.364   3.909  1.00 39.32           H  
ATOM   1659 HE22 GLN A 311      -4.868   3.622   4.387  1.00 39.32           H  
ATOM   1660  N   LEU A 312      -8.224   6.730   0.268  1.00 11.22           N  
ANISOU 1660  N   LEU A 312     1798   1432   1035   -207    442   -192       N  
ATOM   1661  CA  LEU A 312      -8.839   5.893  -0.762  1.00 11.18           C  
ANISOU 1661  CA  LEU A 312     1607   1447   1196   -269    434   -181       C  
ATOM   1662  C   LEU A 312      -7.879   5.534  -1.888  1.00 10.25           C  
ANISOU 1662  C   LEU A 312     1494   1310   1090   -207    373   -173       C  
ATOM   1663  O   LEU A 312      -8.236   4.737  -2.762  1.00 10.81           O  
ANISOU 1663  O   LEU A 312     1568   1322   1218   -242    362   -232       O  
ATOM   1664  CB  LEU A 312     -10.086   6.598  -1.323  1.00 12.42           C  
ANISOU 1664  CB  LEU A 312     1674   1723   1323   -465    744   -314       C  
ATOM   1665  CG  LEU A 312     -11.224   6.791  -0.314  1.00 15.47           C  
ANISOU 1665  CG  LEU A 312     1842   2305   1730   -419    901   -195       C  
ATOM   1666  CD1 LEU A 312     -12.302   7.704  -0.882  1.00 16.68           C  
ANISOU 1666  CD1 LEU A 312     1850   2701   1787     22    946   -313       C  
ATOM   1667  CD2 LEU A 312     -11.821   5.453   0.101  1.00 18.14           C  
ANISOU 1667  CD2 LEU A 312     2261   2555   2075   -719    847     36       C  
ATOM   1668  H   LEU A 312      -8.487   7.548   0.252  1.00 13.48           H  
ATOM   1669  HA  LEU A 312      -9.128   5.059  -0.359  1.00 13.43           H  
ATOM   1670  HB2 LEU A 312      -9.825   7.476  -1.642  1.00 14.92           H  
ATOM   1671  HB3 LEU A 312     -10.433   6.068  -2.058  1.00 14.92           H  
ATOM   1672  HG  LEU A 312     -10.861   7.213   0.481  1.00 18.57           H  
ATOM   1673 HD11 LEU A 312     -12.990   7.835  -0.211  1.00 20.03           H  
ATOM   1674 HD12 LEU A 312     -11.902   8.556  -1.116  1.00 20.03           H  
ATOM   1675 HD13 LEU A 312     -12.684   7.289  -1.671  1.00 20.03           H  
ATOM   1676 HD21 LEU A 312     -12.783   5.547   0.179  1.00 21.77           H  
ATOM   1677 HD22 LEU A 312     -11.606   4.789  -0.573  1.00 21.77           H  
ATOM   1678 HD23 LEU A 312     -11.444   5.190   0.955  1.00 21.77           H  
ATOM   1679  N   LEU A 313      -6.682   6.100  -1.895  1.00  9.86           N  
ANISOU 1679  N   LEU A 313     1529   1241    976   -260    320   -156       N  
ATOM   1680  CA  LEU A 313      -5.749   5.827  -2.985  1.00  9.03           C  
ANISOU 1680  CA  LEU A 313     1428   1192    810   -163    267    -60       C  
ATOM   1681  C   LEU A 313      -5.380   4.351  -3.077  1.00  8.63           C  
ANISOU 1681  C   LEU A 313     1369   1174    734    -63    180    -60       C  
ATOM   1682  O   LEU A 313      -5.255   3.816  -4.182  1.00  8.36           O  
ANISOU 1682  O   LEU A 313     1387   1160    630   -124    162    -91       O  
ATOM   1683  CB  LEU A 313      -4.532   6.723  -2.819  1.00  9.39           C  
ANISOU 1683  CB  LEU A 313     1512   1224    834   -202    259    -33       C  
ATOM   1684  CG  LEU A 313      -3.546   6.749  -3.971  1.00  9.42           C  
ANISOU 1684  CG  LEU A 313     1460   1248    872    -19    264      6       C  
ATOM   1685  CD1 LEU A 313      -4.227   7.137  -5.273  1.00  9.06           C  
ANISOU 1685  CD1 LEU A 313     1396   1263    785     55    319     37       C  
ATOM   1686  CD2 LEU A 313      -2.440   7.707  -3.632  1.00 10.64           C  
ANISOU 1686  CD2 LEU A 313     1476   1499   1067   -297    264   -116       C  
ATOM   1687  H   LEU A 313      -6.386   6.638  -1.293  1.00 11.84           H  
ATOM   1688  HA  LEU A 313      -6.166   6.041  -3.834  1.00 10.84           H  
ATOM   1689  HB2 LEU A 313      -4.844   7.633  -2.692  1.00 11.28           H  
ATOM   1690  HB3 LEU A 313      -4.045   6.427  -2.035  1.00 11.28           H  
ATOM   1691  HG  LEU A 313      -3.174   5.864  -4.108  1.00 11.32           H  
ATOM   1692 HD11 LEU A 313      -3.548   7.330  -5.939  1.00 10.88           H  
ATOM   1693 HD12 LEU A 313      -4.783   6.400  -5.571  1.00 10.88           H  
ATOM   1694 HD13 LEU A 313      -4.774   7.924  -5.121  1.00 10.88           H  
ATOM   1695 HD21 LEU A 313      -1.858   7.802  -4.402  1.00 12.78           H  
ATOM   1696 HD22 LEU A 313      -2.826   8.566  -3.401  1.00 12.78           H  
ATOM   1697 HD23 LEU A 313      -1.938   7.356  -2.879  1.00 12.78           H  
ATOM   1698  N   LYS A 314      -5.213   3.670  -1.940  1.00  9.68           N  
ANISOU 1698  N   LYS A 314     1792   1242    646   -132    125    -14       N  
ATOM   1699  CA  LYS A 314      -4.897   2.248  -1.989  1.00 10.18           C  
ANISOU 1699  CA  LYS A 314     1890   1232    747   -209    -53     74       C  
ATOM   1700  C   LYS A 314      -6.002   1.482  -2.707  1.00  9.44           C  
ANISOU 1700  C   LYS A 314     1708   1215    663   -112     39     85       C  
ATOM   1701  O   LYS A 314      -5.724   0.676  -3.599  1.00  8.97           O  
ANISOU 1701  O   LYS A 314     1567   1139    701    -76    -38     68       O  
ATOM   1702  CB  LYS A 314      -4.643   1.689  -0.591  1.00 12.67           C  
ANISOU 1702  CB  LYS A 314     2502   1377    936   -427   -342    258       C  
ATOM   1703  CG  LYS A 314      -4.207   0.221  -0.636  1.00 14.89           C  
ANISOU 1703  CG  LYS A 314     2831   1574   1253   -404   -612    403       C  
ATOM   1704  CD  LYS A 314      -3.806  -0.354   0.717  1.00 16.75           C  
ANISOU 1704  CD  LYS A 314     2978   1941   1447   -440   -581    547       C  
ATOM   1705  CE  LYS A 314      -3.093  -1.710   0.573  1.00 18.30           C  
ANISOU 1705  CE  LYS A 314     3004   2389   1562   -356   -336    724       C  
ATOM   1706  NZ  LYS A 314      -1.672  -1.573   0.084  1.00 18.92           N  
ANISOU 1706  NZ  LYS A 314     2936   2722   1532   -204   -361    799       N  
ATOM   1707  H   LYS A 314      -5.277   4.001  -1.149  1.00 11.63           H  
ATOM   1708  HA  LYS A 314      -4.071   2.130  -2.484  1.00 12.23           H  
ATOM   1709  HB2 LYS A 314      -3.940   2.203  -0.164  1.00 15.22           H  
ATOM   1710  HB3 LYS A 314      -5.460   1.747  -0.071  1.00 15.22           H  
ATOM   1711  HG2 LYS A 314      -4.943  -0.312  -0.975  1.00 17.88           H  
ATOM   1712  HG3 LYS A 314      -3.441   0.143  -1.226  1.00 17.88           H  
ATOM   1713  HD2 LYS A 314      -3.202   0.262   1.161  1.00 20.11           H  
ATOM   1714  HD3 LYS A 314      -4.601  -0.485   1.258  1.00 20.11           H  
ATOM   1715  HE2 LYS A 314      -3.072  -2.150   1.437  1.00 21.97           H  
ATOM   1716  HE3 LYS A 314      -3.578  -2.255  -0.066  1.00 21.97           H  
ATOM   1717  HZ1 LYS A 314      -1.661  -1.177  -0.712  1.00 22.71           H  
ATOM   1718  HZ2 LYS A 314      -1.200  -1.083   0.657  1.00 22.71           H  
ATOM   1719  HZ3 LYS A 314      -1.297  -2.377   0.013  1.00 22.71           H  
ATOM   1720  N   SER A 315      -7.267   1.727  -2.346  1.00 10.32           N  
ANISOU 1720  N   SER A 315     1942   1223    756   -218    273     -8       N  
ATOM   1721  CA  SER A 315      -8.351   1.014  -3.014  1.00  9.76           C  
ANISOU 1721  CA  SER A 315     1560   1279    870   -250    357    -13       C  
ATOM   1722  C   SER A 315      -8.378   1.308  -4.506  1.00  8.32           C  
ANISOU 1722  C   SER A 315     1089   1168    904   -116    289    -61       C  
ATOM   1723  O   SER A 315      -8.687   0.430  -5.309  1.00  8.26           O  
ANISOU 1723  O   SER A 315     1076   1125    938    -74    179    -19       O  
ATOM   1724  CB  SER A 315      -9.705   1.292  -2.368  1.00 11.98           C  
ANISOU 1724  CB  SER A 315     1809   1632   1110   -261    517   -122       C  
ATOM   1725  OG  SER A 315     -10.169   2.597  -2.537  1.00 14.12           O  
ANISOU 1725  OG  SER A 315     2021   1940   1403   -266    526   -215       O  
ATOM   1726  H   SER A 315      -7.512   2.283  -1.737  1.00 12.40           H  
ATOM   1727  HA  SER A 315      -8.195   0.063  -2.900  1.00 11.72           H  
ATOM   1728  HB2 SER A 315     -10.355   0.688  -2.759  1.00 14.38           H  
ATOM   1729  HB3 SER A 315      -9.625   1.122  -1.416  1.00 14.38           H  
ATOM   1730  HG  SER A 315      -9.618   3.142  -2.213  1.00 16.95           H  
ATOM   1731  N   ALA A 316      -8.028   2.532  -4.905  1.00  7.95           N  
ANISOU 1731  N   ALA A 316     1131   1054    834   -107    240    -57       N  
ATOM   1732  CA  ALA A 316      -7.953   2.840  -6.323  1.00  7.38           C  
ANISOU 1732  CA  ALA A 316     1035    920    850      0    167     -4       C  
ATOM   1733  C   ALA A 316      -6.908   1.967  -7.012  1.00  6.82           C  
ANISOU 1733  C   ALA A 316      974    841    777    -47     43     10       C  
ATOM   1734  O   ALA A 316      -7.183   1.354  -8.052  1.00  7.05           O  
ANISOU 1734  O   ALA A 316      876    992    809     21      7    -62       O  
ATOM   1735  CB  ALA A 316      -7.670   4.325  -6.513  1.00  7.75           C  
ANISOU 1735  CB  ALA A 316     1062   1044    840      9    186    -26       C  
ATOM   1736  H   ALA A 316      -7.834   3.186  -4.382  1.00  9.54           H  
ATOM   1737  HA  ALA A 316      -8.807   2.654  -6.743  1.00  8.87           H  
ATOM   1738  HB1 ALA A 316      -7.639   4.522  -7.463  1.00  9.31           H  
ATOM   1739  HB2 ALA A 316      -8.377   4.838  -6.092  1.00  9.31           H  
ATOM   1740  HB3 ALA A 316      -6.817   4.539  -6.104  1.00  9.31           H  
ATOM   1741  N   TYR A 317      -5.706   1.875  -6.442  1.00  6.80           N  
ANISOU 1741  N   TYR A 317      993    918    672    -58     44    -19       N  
ATOM   1742  CA  TYR A 317      -4.675   1.010  -7.014  1.00  6.34           C  
ANISOU 1742  CA  TYR A 317      868    906    634    -41      1     39       C  
ATOM   1743  C   TYR A 317      -5.046  -0.476  -6.973  1.00  6.59           C  
ANISOU 1743  C   TYR A 317      830    976    699    -93    -34     42       C  
ATOM   1744  O   TYR A 317      -4.584  -1.242  -7.816  1.00  6.60           O  
ANISOU 1744  O   TYR A 317      867    901    741    -51     74    -15       O  
ATOM   1745  CB  TYR A 317      -3.329   1.225  -6.330  1.00  6.77           C  
ANISOU 1745  CB  TYR A 317      956    982    634    -49     20     72       C  
ATOM   1746  CG  TYR A 317      -2.569   2.419  -6.857  1.00  6.40           C  
ANISOU 1746  CG  TYR A 317      879    868    685    -20     20    -10       C  
ATOM   1747  CD1 TYR A 317      -2.054   2.406  -8.143  1.00  6.41           C  
ANISOU 1747  CD1 TYR A 317      943    824    669    -29      9    -15       C  
ATOM   1748  CD2 TYR A 317      -2.356   3.553  -6.087  1.00  6.60           C  
ANISOU 1748  CD2 TYR A 317      908    933    667     28     32    -30       C  
ATOM   1749  CE1 TYR A 317      -1.349   3.483  -8.653  1.00  6.45           C  
ANISOU 1749  CE1 TYR A 317      874    948    628     35      3     18       C  
ATOM   1750  CE2 TYR A 317      -1.641   4.636  -6.589  1.00  6.67           C  
ANISOU 1750  CE2 TYR A 317      946    878    709    -38    -22    -34       C  
ATOM   1751  CZ  TYR A 317      -1.138   4.584  -7.863  1.00  6.35           C  
ANISOU 1751  CZ  TYR A 317      844    903    664     19    -17     38       C  
ATOM   1752  OH  TYR A 317      -0.413   5.620  -8.410  1.00  6.60           O  
ANISOU 1752  OH  TYR A 317      852    921    734      9     11      5       O  
ATOM   1753  H   TYR A 317      -5.465   2.296  -5.732  1.00  8.17           H  
ATOM   1754  HA  TYR A 317      -4.584   1.267  -7.945  1.00  7.61           H  
ATOM   1755  HB2 TYR A 317      -3.478   1.363  -5.382  1.00  8.14           H  
ATOM   1756  HB3 TYR A 317      -2.779   0.438  -6.469  1.00  8.14           H  
ATOM   1757  HD1 TYR A 317      -2.184   1.655  -8.677  1.00  7.70           H  
ATOM   1758  HD2 TYR A 317      -2.696   3.589  -5.222  1.00  7.93           H  
ATOM   1759  HE1 TYR A 317      -1.022   3.460  -9.523  1.00  7.75           H  
ATOM   1760  HE2 TYR A 317      -1.506   5.391  -6.063  1.00  8.01           H  
ATOM   1761  HH  TYR A 317      -0.358   6.254  -7.862  1.00  7.93           H  
ATOM   1762  N   GLU A 318      -5.841  -0.897  -5.996  1.00  6.94           N  
ANISOU 1762  N   GLU A 318      970    943    723    -41     52     57       N  
ATOM   1763  CA  GLU A 318      -6.208  -2.309  -5.898  1.00  7.25           C  
ANISOU 1763  CA  GLU A 318     1013    968    775    -71     92     56       C  
ATOM   1764  C   GLU A 318      -6.916  -2.779  -7.163  1.00  7.30           C  
ANISOU 1764  C   GLU A 318      960   1024    789   -124    165     69       C  
ATOM   1765  O   GLU A 318      -6.824  -3.961  -7.523  1.00  7.68           O  
ANISOU 1765  O   GLU A 318     1187    902    828   -137    112     64       O  
ATOM   1766  CB  GLU A 318      -7.063  -2.536  -4.665  1.00  8.19           C  
ANISOU 1766  CB  GLU A 318     1160   1140    812    -26    166     80       C  
ATOM   1767  CG  GLU A 318      -7.344  -3.998  -4.370  1.00 10.27           C  
ANISOU 1767  CG  GLU A 318     1521   1297   1083   -132    338    175       C  
ATOM   1768  CD  GLU A 318      -6.092  -4.764  -3.962  1.00 11.21           C  
ANISOU 1768  CD  GLU A 318     1694   1279   1285      6    464    321       C  
ATOM   1769  OE1 GLU A 318      -5.319  -4.223  -3.142  1.00 12.52           O  
ANISOU 1769  OE1 GLU A 318     1681   1575   1501    -11    159    420       O  
ATOM   1770  OE2 GLU A 318      -5.880  -5.902  -4.455  1.00 13.49           O  
ANISOU 1770  OE2 GLU A 318     2311   1289   1527    130    796    207       O  
ATOM   1771  H   GLU A 318      -6.179  -0.396  -5.385  1.00  8.34           H  
ATOM   1772  HA  GLU A 318      -5.408  -2.849  -5.795  1.00  8.71           H  
ATOM   1773  HB2 GLU A 318      -6.605  -2.162  -3.896  1.00  9.84           H  
ATOM   1774  HB3 GLU A 318      -7.916  -2.091  -4.792  1.00  9.84           H  
ATOM   1775  HG2 GLU A 318      -7.982  -4.057  -3.642  1.00 12.33           H  
ATOM   1776  HG3 GLU A 318      -7.707  -4.417  -5.165  1.00 12.33           H  
ATOM   1777  N   ASN A 319      -7.596  -1.873  -7.866  1.00  7.00           N  
ANISOU 1777  N   ASN A 319      893    938    827    -72     91     47       N  
ATOM   1778  CA  ASN A 319      -8.225  -2.249  -9.119  1.00  7.31           C  
ANISOU 1778  CA  ASN A 319      803   1085    891   -100     85     13       C  
ATOM   1779  C   ASN A 319      -7.222  -2.783 -10.138  1.00  6.97           C  
ANISOU 1779  C   ASN A 319      858    968    823   -125     54    -14       C  
ATOM   1780  O   ASN A 319      -7.585  -3.577 -11.015  1.00  7.66           O  
ANISOU 1780  O   ASN A 319      914   1132    864   -269     62   -135       O  
ATOM   1781  CB  ASN A 319      -8.950  -1.048  -9.729  1.00  7.65           C  
ANISOU 1781  CB  ASN A 319      741   1294    869    -88     16     45       C  
ATOM   1782  CG  ASN A 319     -10.115  -0.583  -8.898  1.00  8.45           C  
ANISOU 1782  CG  ASN A 319      837   1362   1012    -79     72     18       C  
ATOM   1783  OD1 ASN A 319     -11.173  -1.196  -8.916  1.00  9.82           O  
ANISOU 1783  OD1 ASN A 319      975   1497   1257   -152    157    -60       O  
ATOM   1784  ND2 ASN A 319      -9.943   0.519  -8.190  1.00  8.52           N  
ANISOU 1784  ND2 ASN A 319      900   1332   1004     71     60    -81       N  
ATOM   1785  H   ASN A 319      -7.703  -1.050  -7.641  1.00  8.40           H  
ATOM   1786  HA  ASN A 319      -8.869  -2.948  -8.923  1.00  8.78           H  
ATOM   1787  HB2 ASN A 319      -8.325  -0.310  -9.809  1.00  9.18           H  
ATOM   1788  HB3 ASN A 319      -9.286  -1.294 -10.605  1.00  9.18           H  
ATOM   1789 HD21 ASN A 319     -10.583   0.820  -7.701  1.00 10.23           H  
ATOM   1790 HD22 ASN A 319      -9.191   0.935  -8.218  1.00 10.23           H  
ATOM   1791  N   PHE A 320      -5.965  -2.355 -10.060  1.00  6.17           N  
ANISOU 1791  N   PHE A 320      754    858    732    -79     52    -38       N  
ATOM   1792  CA  PHE A 320      -4.972  -2.816 -11.019  1.00  6.61           C  
ANISOU 1792  CA  PHE A 320      848    922    742    -49     80    -64       C  
ATOM   1793  C   PHE A 320      -4.714  -4.322 -10.876  1.00  6.84           C  
ANISOU 1793  C   PHE A 320      899    884    815   -174     56    -28       C  
ATOM   1794  O   PHE A 320      -4.245  -4.964 -11.823  1.00  7.41           O  
ANISOU 1794  O   PHE A 320     1020    908    889   -180    188   -133       O  
ATOM   1795  CB  PHE A 320      -3.621  -2.120 -10.821  1.00  6.28           C  
ANISOU 1795  CB  PHE A 320      748    921    718    -42     68    -13       C  
ATOM   1796  CG  PHE A 320      -3.540  -0.635 -11.182  1.00  5.88           C  
ANISOU 1796  CG  PHE A 320      672    854    707    -69     36    -61       C  
ATOM   1797  CD1 PHE A 320      -4.641   0.207 -11.259  1.00  6.52           C  
ANISOU 1797  CD1 PHE A 320      623    972    881    -83      2     58       C  
ATOM   1798  CD2 PHE A 320      -2.298  -0.088 -11.400  1.00  6.09           C  
ANISOU 1798  CD2 PHE A 320      709    901    706     13     85    -11       C  
ATOM   1799  CE1 PHE A 320      -4.480   1.566 -11.548  1.00  6.37           C  
ANISOU 1799  CE1 PHE A 320      649    921    849     -5    -96     49       C  
ATOM   1800  CE2 PHE A 320      -2.136   1.261 -11.677  1.00  5.98           C  
ANISOU 1800  CE2 PHE A 320      684    889    701    -81    102     10       C  
ATOM   1801  CZ  PHE A 320      -3.217   2.089 -11.737  1.00  5.88           C  
ANISOU 1801  CZ  PHE A 320      718    894    622    -54    -39     -4       C  
ATOM   1802  H   PHE A 320      -5.667  -1.806  -9.469  1.00  7.41           H  
ATOM   1803  HA  PHE A 320      -5.308  -2.598 -11.902  1.00  7.94           H  
ATOM   1804  HB2 PHE A 320      -3.381  -2.196  -9.884  1.00  7.55           H  
ATOM   1805  HB3 PHE A 320      -2.965  -2.579 -11.369  1.00  7.55           H  
ATOM   1806  HD1 PHE A 320      -5.494  -0.136 -11.117  1.00  7.83           H  
ATOM   1807  HD2 PHE A 320      -1.548  -0.636 -11.361  1.00  7.32           H  
ATOM   1808  HE1 PHE A 320      -5.225   2.119 -11.613  1.00  7.65           H  
ATOM   1809  HE2 PHE A 320      -1.284   1.604 -11.822  1.00  7.19           H  
ATOM   1810  HZ  PHE A 320      -3.104   2.997 -11.904  1.00  7.07           H  
ATOM   1811  N   ASN A 321      -5.007  -4.883  -9.705  1.00  6.93           N  
ANISOU 1811  N   ASN A 321      962    818    854    -85     71     -8       N  
ATOM   1812  CA  ASN A 321      -4.650  -6.266  -9.403  1.00  7.23           C  
ANISOU 1812  CA  ASN A 321      916    875    954    -58     65    -10       C  
ATOM   1813  C   ASN A 321      -5.522  -7.283 -10.104  1.00  7.32           C  
ANISOU 1813  C   ASN A 321      892    915    976   -119    126     11       C  
ATOM   1814  O   ASN A 321      -5.236  -8.482 -10.012  1.00  7.98           O  
ANISOU 1814  O   ASN A 321     1137    863   1030   -108    121    -41       O  
ATOM   1815  CB  ASN A 321      -4.627  -6.475  -7.898  1.00  7.47           C  
ANISOU 1815  CB  ASN A 321      904    956    976   -121     49     68       C  
ATOM   1816  CG  ASN A 321      -3.395  -5.872  -7.294  1.00  8.07           C  
ANISOU 1816  CG  ASN A 321     1008   1039   1019   -206    -11     90       C  
ATOM   1817  OD1 ASN A 321      -2.372  -5.733  -7.970  1.00  9.89           O  
ANISOU 1817  OD1 ASN A 321     1074   1601   1081   -379    -78     58       O  
ATOM   1818  ND2 ASN A 321      -3.484  -5.482  -6.036  1.00  8.64           N  
ANISOU 1818  ND2 ASN A 321     1172   1089   1023   -191     -5     29       N  
ATOM   1819  H   ASN A 321      -5.416  -4.481  -9.064  1.00  8.33           H  
ATOM   1820  HA  ASN A 321      -3.749  -6.435  -9.720  1.00  8.68           H  
ATOM   1821  HB2 ASN A 321      -5.404  -6.051  -7.501  1.00  8.97           H  
ATOM   1822  HB3 ASN A 321      -4.631  -7.425  -7.703  1.00  8.97           H  
ATOM   1823 HD21 ASN A 321      -2.803  -5.129  -5.646  1.00 10.38           H  
ATOM   1824 HD22 ASN A 321      -4.223  -5.579  -5.607  1.00 10.38           H  
ATOM   1825  N   GLN A 322      -6.528  -6.845 -10.830  1.00  7.43           N  
ANISOU 1825  N   GLN A 322      812    951   1060   -156     93    -15       N  
ATOM   1826  CA  GLN A 322      -7.337  -7.709 -11.678  1.00  8.05           C  
ANISOU 1826  CA  GLN A 322      852   1087   1119   -232     84    -76       C  
ATOM   1827  C   GLN A 322      -6.781  -7.823 -13.090  1.00  7.05           C  
ANISOU 1827  C   GLN A 322      724    893   1062   -120      7      2       C  
ATOM   1828  O   GLN A 322      -7.374  -8.538 -13.907  1.00  7.75           O  
ANISOU 1828  O   GLN A 322      780    984   1179   -188     23   -113       O  
ATOM   1829  CB  GLN A 322      -8.787  -7.230 -11.677  1.00 10.43           C  
ANISOU 1829  CB  GLN A 322      888   1688   1386   -190    263   -412       C  
ATOM   1830  CG  GLN A 322      -9.530  -7.640 -10.413  1.00 14.01           C  
ANISOU 1830  CG  GLN A 322     1416   2106   1801   -268    353   -500       C  
ATOM   1831  CD  GLN A 322      -8.880  -7.111  -9.146  1.00 14.81           C  
ANISOU 1831  CD  GLN A 322     1862   1726   2038   -381    512   -207       C  
ATOM   1832  OE1 GLN A 322      -8.237  -7.843  -8.371  1.00 17.41           O  
ANISOU 1832  OE1 GLN A 322     2532   1866   2216    -31    590     18       O  
ATOM   1833  NE2 GLN A 322      -9.036  -5.833  -8.934  1.00 14.64           N  
ANISOU 1833  NE2 GLN A 322     1921   1679   1964   -334    540   -334       N  
ATOM   1834  H   GLN A 322      -6.775  -6.022 -10.854  1.00  8.92           H  
ATOM   1835  HA  GLN A 322      -7.348  -8.608 -11.314  1.00  9.67           H  
ATOM   1836  HB2 GLN A 322      -8.802  -6.262 -11.736  1.00 12.52           H  
ATOM   1837  HB3 GLN A 322      -9.250  -7.616 -12.438  1.00 12.52           H  
ATOM   1838  HG2 GLN A 322     -10.435  -7.293 -10.452  1.00 16.82           H  
ATOM   1839  HG3 GLN A 322      -9.548  -8.608 -10.358  1.00 16.82           H  
ATOM   1840 HE21 GLN A 322      -9.482  -5.356  -9.493  1.00 17.58           H  
ATOM   1841 HE22 GLN A 322      -8.693  -5.468  -8.234  1.00 17.58           H  
ATOM   1842  N   HIS A 323      -5.647  -7.206 -13.386  1.00  6.52           N  
ANISOU 1842  N   HIS A 323      703    852    923   -115     22    -38       N  
ATOM   1843  CA  HIS A 323      -5.072  -7.204 -14.729  1.00  6.55           C  
ANISOU 1843  CA  HIS A 323      712    849    928   -120    -47    -28       C  
ATOM   1844  C   HIS A 323      -3.595  -7.527 -14.640  1.00  6.72           C  
ANISOU 1844  C   HIS A 323      768    893    893   -136    -37    -52       C  
ATOM   1845  O   HIS A 323      -2.878  -6.935 -13.842  1.00  7.71           O  
ANISOU 1845  O   HIS A 323      805   1087   1039     34   -116   -202       O  
ATOM   1846  CB  HIS A 323      -5.288  -5.833 -15.371  1.00  7.28           C  
ANISOU 1846  CB  HIS A 323      754    925   1087   -137    -70    115       C  
ATOM   1847  CG  HIS A 323      -6.728  -5.469 -15.416  1.00  7.80           C  
ANISOU 1847  CG  HIS A 323      737    992   1233    -59    -35    154       C  
ATOM   1848  ND1 HIS A 323      -7.552  -5.903 -16.419  1.00  8.85           N  
ANISOU 1848  ND1 HIS A 323      821   1299   1242    -36    -40    131       N  
ATOM   1849  CD2 HIS A 323      -7.525  -4.848 -14.512  1.00  8.73           C  
ANISOU 1849  CD2 HIS A 323      856    972   1491    -54     88     72       C  
ATOM   1850  CE1 HIS A 323      -8.790  -5.529 -16.151  1.00  9.57           C  
ANISOU 1850  CE1 HIS A 323      939   1266   1432    -15   -127    116       C  
ATOM   1851  NE2 HIS A 323      -8.806  -4.894 -14.996  1.00  9.68           N  
ANISOU 1851  NE2 HIS A 323      909   1168   1599     66     43    162       N  
ATOM   1852  H   HIS A 323      -5.178  -6.769 -12.814  1.00  7.84           H  
ATOM   1853  HA  HIS A 323      -5.484  -7.887 -15.282  1.00  7.87           H  
ATOM   1854  HB2 HIS A 323      -4.820  -5.160 -14.853  1.00  8.74           H  
ATOM   1855  HB3 HIS A 323      -4.949  -5.847 -16.279  1.00  8.74           H  
ATOM   1856  HD1 HIS A 323      -7.303  -6.347 -17.112  1.00 10.63           H  
ATOM   1857  HD2 HIS A 323      -7.253  -4.461 -13.711  1.00 10.49           H  
ATOM   1858  HE1 HIS A 323      -9.530  -5.689 -16.691  1.00 11.49           H  
ATOM   1859  N  AGLU A 324      -3.127  -8.468 -15.460  0.53  6.00           N  
ANISOU 1859  N  AGLU A 324      718    759    802   -181    -75      1       N  
ATOM   1860  N  BGLU A 324      -3.153  -8.444 -15.484  0.47  6.53           N  
ANISOU 1860  N  BGLU A 324      870    765    844   -170    108   -102       N  
ATOM   1861  CA AGLU A 324      -1.752  -8.932 -15.304  0.53  5.89           C  
ANISOU 1861  CA AGLU A 324      663    736    840    -13    -67     21       C  
ATOM   1862  CA BGLU A 324      -1.795  -8.952 -15.392  0.47  7.14           C  
ANISOU 1862  CA BGLU A 324     1080    698    935   -107    171   -135       C  
ATOM   1863  C  AGLU A 324      -0.727  -7.883 -15.728  0.53  5.63           C  
ANISOU 1863  C  AGLU A 324      589    721    829     31     -9    -70       C  
ATOM   1864  C  BGLU A 324      -0.763  -7.879 -15.721  0.47  6.36           C  
ANISOU 1864  C  BGLU A 324      887    642    888    -47     77    -83       C  
ATOM   1865  O  AGLU A 324       0.373  -7.846 -15.157  0.53  5.85           O  
ANISOU 1865  O  AGLU A 324      429    957    838    113   -130    -94       O  
ATOM   1866  O  BGLU A 324       0.295  -7.812 -15.080  0.47  7.34           O  
ANISOU 1866  O  BGLU A 324     1270    580    938      0     57     -6       O  
ATOM   1867  CB AGLU A 324      -1.505 -10.244 -16.060  0.53  7.51           C  
ANISOU 1867  CB AGLU A 324     1193    845    814   -114    139    162       C  
ATOM   1868  CB BGLU A 324      -1.665 -10.110 -16.366  0.47  8.85           C  
ANISOU 1868  CB BGLU A 324     1599    673   1089   -229    431   -151       C  
ATOM   1869  CG AGLU A 324      -1.707 -10.194 -17.577  0.53  7.19           C  
ANISOU 1869  CG AGLU A 324      833   1072    828   -160   -117     27       C  
ATOM   1870  CG BGLU A 324      -0.580 -11.051 -16.033  0.47  9.62           C  
ANISOU 1870  CG BGLU A 324     1410   1005   1240      6    157   -150       C  
ATOM   1871  CD AGLU A 324      -1.136 -11.446 -18.291  0.53  9.59           C  
ANISOU 1871  CD AGLU A 324      975   1514   1155   -224   -196   -124       C  
ATOM   1872  CD BGLU A 324      -0.465 -12.116 -17.078  0.47  8.89           C  
ANISOU 1872  CD BGLU A 324     1241   1006   1132    -13    185     39       C  
ATOM   1873  OE1AGLU A 324       0.102 -11.605 -18.292  0.53 10.20           O  
ANISOU 1873  OE1AGLU A 324     1274   1468   1135   -509   -269    -30       O  
ATOM   1874  OE1BGLU A 324      -0.079 -11.764 -18.212  0.47 10.30           O  
ANISOU 1874  OE1BGLU A 324     1571   1224   1117   -326    366    -28       O  
ATOM   1875  OE2AGLU A 324      -1.916 -12.260 -18.851  0.53 10.49           O  
ANISOU 1875  OE2AGLU A 324     1170   1290   1524    -27   -204    -76       O  
ATOM   1876  OE2BGLU A 324      -0.775 -13.303 -16.787  0.47  9.64           O  
ANISOU 1876  OE2BGLU A 324      961   1534   1167   -129     84    -90       O  
ATOM   1877  H  AGLU A 324      -3.572  -8.842 -16.095  0.53  7.21           H  
ATOM   1878  H  BGLU A 324      -3.617  -8.789 -16.120  0.47  7.84           H  
ATOM   1879  HA AGLU A 324      -1.623  -9.114 -14.360  0.53  7.08           H  
ATOM   1880  HA BGLU A 324      -1.620  -9.253 -14.487  0.47  8.58           H  
ATOM   1881  HB2AGLU A 324      -0.587 -10.516 -15.902  0.53  9.02           H  
ATOM   1882  HB2BGLU A 324      -2.497 -10.607 -16.371  0.47 10.62           H  
ATOM   1883  HB3AGLU A 324      -2.114 -10.913 -15.712  0.53  9.02           H  
ATOM   1884  HB3BGLU A 324      -1.486  -9.754 -17.251  0.47 10.62           H  
ATOM   1885  HG2AGLU A 324      -2.656 -10.144 -17.770  0.53  8.64           H  
ATOM   1886  HG2BGLU A 324       0.262 -10.572 -15.987  0.47 11.55           H  
ATOM   1887  HG3AGLU A 324      -1.254  -9.412 -17.932  0.53  8.64           H  
ATOM   1888  HG3BGLU A 324      -0.769 -11.474 -15.181  0.47 11.55           H  
ATOM   1889  N   VAL A 325      -1.043  -7.071 -16.737  1.00  5.80           N  
ANISOU 1889  N   VAL A 325      560    815    827    -85      1    -14       N  
ATOM   1890  CA  VAL A 325      -0.126  -6.057 -17.257  1.00  5.36           C  
ANISOU 1890  CA  VAL A 325      488    767    782    -76     -6    -42       C  
ATOM   1891  C   VAL A 325      -0.950  -4.820 -17.578  1.00  5.00           C  
ANISOU 1891  C   VAL A 325      422    768    712    -55    -58     14       C  
ATOM   1892  O   VAL A 325      -1.971  -4.914 -18.250  1.00  5.64           O  
ANISOU 1892  O   VAL A 325      453    858    831    -37    -97    -32       O  
ATOM   1893  CB  VAL A 325       0.580  -6.541 -18.537  1.00  6.30           C  
ANISOU 1893  CB  VAL A 325      558    871    967    -10    101      6       C  
ATOM   1894  CG1 VAL A 325       1.490  -5.461 -19.093  1.00  7.61           C  
ANISOU 1894  CG1 VAL A 325      708   1068   1115     15    261     24       C  
ATOM   1895  CG2 VAL A 325       1.377  -7.815 -18.288  1.00  7.74           C  
ANISOU 1895  CG2 VAL A 325      928    917   1098    144     84     17       C  
ATOM   1896  H   VAL A 325      -1.799  -7.088 -17.147  1.00  6.97           H  
ATOM   1897  HA  VAL A 325       0.541  -5.843 -16.587  1.00  6.44           H  
ATOM   1898  HB  VAL A 325      -0.105  -6.739 -19.194  1.00  7.57           H  
ATOM   1899 HG11 VAL A 325       2.046  -5.845 -19.789  1.00  9.14           H  
ATOM   1900 HG12 VAL A 325       0.945  -4.748 -19.462  1.00  9.14           H  
ATOM   1901 HG13 VAL A 325       2.046  -5.116 -18.377  1.00  9.14           H  
ATOM   1902 HG21 VAL A 325       1.812  -8.081 -19.113  1.00  9.30           H  
ATOM   1903 HG22 VAL A 325       2.042  -7.643 -17.603  1.00  9.30           H  
ATOM   1904 HG23 VAL A 325       0.771  -8.513 -17.993  1.00  9.30           H  
ATOM   1905  N   LEU A 326      -0.474  -3.651 -17.136  1.00  4.99           N  
ANISOU 1905  N   LEU A 326      351    785    762    -26    -46     16       N  
ATOM   1906  CA  LEU A 326      -1.164  -2.390 -17.394  1.00  4.87           C  
ANISOU 1906  CA  LEU A 326      325    781    745    -56    -70     48       C  
ATOM   1907  C   LEU A 326      -0.158  -1.311 -17.760  1.00  4.72           C  
ANISOU 1907  C   LEU A 326      318    796    680     -8    -69    -22       C  
ATOM   1908  O   LEU A 326       0.936  -1.277 -17.206  1.00  5.54           O  
ANISOU 1908  O   LEU A 326      465    838    803    -42   -114     87       O  
ATOM   1909  CB  LEU A 326      -1.936  -1.857 -16.165  1.00  5.77           C  
ANISOU 1909  CB  LEU A 326      505    826    862    -52      9     57       C  
ATOM   1910  CG  LEU A 326      -2.797  -2.867 -15.408  1.00  5.70           C  
ANISOU 1910  CG  LEU A 326      515    825    824   -119    -27     13       C  
ATOM   1911  CD1 LEU A 326      -2.005  -3.550 -14.304  1.00  6.84           C  
ANISOU 1911  CD1 LEU A 326      728   1070    800     94     43    -16       C  
ATOM   1912  CD2 LEU A 326      -4.002  -2.176 -14.815  1.00  6.13           C  
ANISOU 1912  CD2 LEU A 326      533    925    873    -47     58     66       C  
ATOM   1913  H   LEU A 326       0.252  -3.565 -16.683  1.00  6.00           H  
ATOM   1914  HA  LEU A 326      -1.779  -2.553 -18.126  1.00  5.86           H  
ATOM   1915  HB2 LEU A 326      -1.289  -1.504 -15.534  1.00  6.94           H  
ATOM   1916  HB3 LEU A 326      -2.526  -1.148 -16.466  1.00  6.94           H  
ATOM   1917  HG  LEU A 326      -3.092  -3.549 -16.032  1.00  6.84           H  
ATOM   1918 HD11 LEU A 326      -2.588  -4.163 -13.830  1.00  8.22           H  
ATOM   1919 HD12 LEU A 326      -1.265  -4.036 -14.700  1.00  8.22           H  
ATOM   1920 HD13 LEU A 326      -1.669  -2.875 -13.693  1.00  8.22           H  
ATOM   1921 HD21 LEU A 326      -4.508  -2.817 -14.292  1.00  7.37           H  
ATOM   1922 HD22 LEU A 326      -3.701  -1.449 -14.247  1.00  7.37           H  
ATOM   1923 HD23 LEU A 326      -4.552  -1.827 -15.534  1.00  7.37           H  
ATOM   1924  N   LEU A 327      -0.564  -0.402 -18.653  1.00  4.76           N  
ANISOU 1924  N   LEU A 327      337    789    681    -39    -49     48       N  
ATOM   1925  CA  LEU A 327       0.072   0.907 -18.854  1.00  4.59           C  
ANISOU 1925  CA  LEU A 327      319    766    660    -47    -41    -31       C  
ATOM   1926  C   LEU A 327      -0.761   1.927 -18.089  1.00  4.64           C  
ANISOU 1926  C   LEU A 327      347    720    696    -18    -15     22       C  
ATOM   1927  O   LEU A 327      -1.982   1.972 -18.287  1.00  5.41           O  
ANISOU 1927  O   LEU A 327      350    898    809     36    -60   -135       O  
ATOM   1928  CB  LEU A 327       0.047   1.249 -20.337  1.00  4.96           C  
ANISOU 1928  CB  LEU A 327      381    791    713    -15      2    -40       C  
ATOM   1929  CG  LEU A 327       0.520   2.667 -20.695  1.00  5.45           C  
ANISOU 1929  CG  LEU A 327      535    839    699      8     60    -23       C  
ATOM   1930  CD1 LEU A 327       1.957   2.951 -20.281  1.00  5.68           C  
ANISOU 1930  CD1 LEU A 327      606    762    792    -91     20     48       C  
ATOM   1931  CD2 LEU A 327       0.331   2.915 -22.185  1.00  6.10           C  
ANISOU 1931  CD2 LEU A 327      706    874    738    -32     29     59       C  
ATOM   1932  H   LEU A 327      -1.234  -0.525 -19.178  1.00  5.72           H  
ATOM   1933  HA  LEU A 327       0.988   0.918 -18.537  1.00  5.52           H  
ATOM   1934  HB2 LEU A 327       0.624   0.625 -20.803  1.00  5.96           H  
ATOM   1935  HB3 LEU A 327      -0.865   1.159 -20.655  1.00  5.96           H  
ATOM   1936  HG  LEU A 327      -0.025   3.290 -20.189  1.00  6.55           H  
ATOM   1937 HD11 LEU A 327       2.201   3.842 -20.579  1.00  6.83           H  
ATOM   1938 HD12 LEU A 327       2.025   2.896 -19.315  1.00  6.83           H  
ATOM   1939 HD13 LEU A 327       2.540   2.294 -20.692  1.00  6.83           H  
ATOM   1940 HD21 LEU A 327       0.606   3.822 -22.392  1.00  7.33           H  
ATOM   1941 HD22 LEU A 327       0.875   2.283 -22.682  1.00  7.33           H  
ATOM   1942 HD23 LEU A 327      -0.605   2.793 -22.409  1.00  7.33           H  
ATOM   1943  N   ALA A 328      -0.140   2.738 -17.229  1.00  4.88           N  
ANISOU 1943  N   ALA A 328      350    835    670    -44    -51    -83       N  
ATOM   1944  CA  ALA A 328      -0.918   3.585 -16.343  1.00  4.80           C  
ANISOU 1944  CA  ALA A 328      350    798    675     41    -28    -48       C  
ATOM   1945  C   ALA A 328      -0.195   4.886 -16.043  1.00  4.57           C  
ANISOU 1945  C   ALA A 328      362    795    580    -48    -26    -29       C  
ATOM   1946  O   ALA A 328       1.046   4.934 -16.028  1.00  5.10           O  
ANISOU 1946  O   ALA A 328      325    829    782    -25      6    -43       O  
ATOM   1947  CB  ALA A 328      -1.176   2.887 -15.014  1.00  5.42           C  
ANISOU 1947  CB  ALA A 328      422    892    746    -37     33      5       C  
ATOM   1948  H   ALA A 328       0.713   2.809 -17.148  1.00  5.87           H  
ATOM   1949  HA  ALA A 328      -1.746   3.799 -16.801  1.00  5.77           H  
ATOM   1950  HB1 ALA A 328      -1.688   3.479 -14.441  1.00  6.52           H  
ATOM   1951  HB2 ALA A 328      -1.675   2.071 -15.177  1.00  6.52           H  
ATOM   1952  HB3 ALA A 328      -0.326   2.677 -14.597  1.00  6.52           H  
ATOM   1953  N   PRO A 329      -0.963   5.940 -15.720  1.00  4.85           N  
ANISOU 1953  N   PRO A 329      403    802    638      1    -19    -55       N  
ATOM   1954  CA  PRO A 329      -0.398   7.096 -15.023  1.00  5.24           C  
ANISOU 1954  CA  PRO A 329      422    865    703    -53    -40    -76       C  
ATOM   1955  C   PRO A 329      -0.359   6.809 -13.528  1.00  5.63           C  
ANISOU 1955  C   PRO A 329      459    967    715    -51    -30    -96       C  
ATOM   1956  O   PRO A 329      -1.039   5.915 -13.033  1.00  6.40           O  
ANISOU 1956  O   PRO A 329      652   1079    699   -121    -18    -12       O  
ATOM   1957  CB  PRO A 329      -1.435   8.177 -15.320  1.00  5.93           C  
ANISOU 1957  CB  PRO A 329      568    956    731     64     24    -49       C  
ATOM   1958  CG  PRO A 329      -2.746   7.405 -15.270  1.00  5.61           C  
ANISOU 1958  CG  PRO A 329      518    952    664     90     -2    -54       C  
ATOM   1959  CD  PRO A 329      -2.427   6.007 -15.794  1.00  5.33           C  
ANISOU 1959  CD  PRO A 329      422    905    698     54      8    -98       C  
ATOM   1960  HA  PRO A 329       0.475   7.353 -15.358  1.00  6.29           H  
ATOM   1961  HB2 PRO A 329      -1.405   8.871 -14.643  1.00  7.13           H  
ATOM   1962  HB3 PRO A 329      -1.282   8.562 -16.197  1.00  7.13           H  
ATOM   1963  HG2 PRO A 329      -3.067   7.364 -14.356  1.00  6.75           H  
ATOM   1964  HG3 PRO A 329      -3.404   7.841 -15.834  1.00  6.75           H  
ATOM   1965  HD2 PRO A 329      -2.832   5.328 -15.232  1.00  6.40           H  
ATOM   1966  HD3 PRO A 329      -2.731   5.905 -16.709  1.00  6.40           H  
ATOM   1967  N   LEU A 330       0.397   7.616 -12.783  1.00  6.26           N  
ANISOU 1967  N   LEU A 330      564   1102    714   -112    -38    -91       N  
ATOM   1968  CA  LEU A 330       0.187   7.658 -11.343  1.00  6.42           C  
ANISOU 1968  CA  LEU A 330      632   1093    715      8    -89   -148       C  
ATOM   1969  C   LEU A 330      -1.217   8.158 -11.067  1.00  6.57           C  
ANISOU 1969  C   LEU A 330      636   1117    742     81    -21     -9       C  
ATOM   1970  O   LEU A 330      -1.692   9.090 -11.705  1.00  9.95           O  
ANISOU 1970  O   LEU A 330      801   1730   1250    326    199    653       O  
ATOM   1971  CB  LEU A 330       1.181   8.595 -10.669  1.00  7.40           C  
ANISOU 1971  CB  LEU A 330      697   1348    768   -100   -111   -252       C  
ATOM   1972  CG  LEU A 330       2.593   8.048 -10.597  1.00  9.53           C  
ANISOU 1972  CG  LEU A 330      753   1936    933    -56   -128   -275       C  
ATOM   1973  CD1 LEU A 330       3.543   9.158 -10.200  1.00 11.94           C  
ANISOU 1973  CD1 LEU A 330     1015   2398   1125   -451   -215   -171       C  
ATOM   1974  CD2 LEU A 330       2.686   6.889  -9.635  1.00  9.80           C  
ANISOU 1974  CD2 LEU A 330      818   1899   1009    274   -276   -218       C  
ATOM   1975  H   LEU A 330       1.018   8.131 -13.081  1.00  7.52           H  
ATOM   1976  HA  LEU A 330       0.314   6.770 -10.974  1.00  7.71           H  
ATOM   1977  HB2 LEU A 330       1.211   9.426 -11.168  1.00  8.89           H  
ATOM   1978  HB3 LEU A 330       0.882   8.763  -9.762  1.00  8.89           H  
ATOM   1979  HG  LEU A 330       2.851   7.711 -11.469  1.00 11.45           H  
ATOM   1980 HD11 LEU A 330       4.439   8.794 -10.125  1.00 14.34           H  
ATOM   1981 HD12 LEU A 330       3.522   9.849 -10.880  1.00 14.34           H  
ATOM   1982 HD13 LEU A 330       3.262   9.523  -9.347  1.00 14.34           H  
ATOM   1983 HD21 LEU A 330       3.619   6.655  -9.513  1.00 11.77           H  
ATOM   1984 HD22 LEU A 330       2.296   7.151  -8.786  1.00 11.77           H  
ATOM   1985 HD23 LEU A 330       2.201   6.134 -10.003  1.00 11.77           H  
ATOM   1986  N   LEU A 331      -1.886   7.554 -10.096  1.00  5.59           N  
ANISOU 1986  N   LEU A 331      675    844    604     -9     -8    -25       N  
ATOM   1987  CA  LEU A 331      -3.223   7.960  -9.716  1.00  5.86           C  
ANISOU 1987  CA  LEU A 331      643    938    644    -17    -10    -86       C  
ATOM   1988  C   LEU A 331      -3.191   9.194  -8.822  1.00  5.81           C  
ANISOU 1988  C   LEU A 331      624    929    656      4     25   -103       C  
ATOM   1989  O   LEU A 331      -2.275   9.402  -8.015  1.00  6.50           O  
ANISOU 1989  O   LEU A 331      733   1034    702     72    -66   -121       O  
ATOM   1990  CB  LEU A 331      -3.962   6.822  -9.028  1.00  6.46           C  
ANISOU 1990  CB  LEU A 331      806    950    698     11     24    -94       C  
ATOM   1991  CG  LEU A 331      -4.177   5.583  -9.895  1.00  6.97           C  
ANISOU 1991  CG  LEU A 331      836    965    846    -30     21   -162       C  
ATOM   1992  CD1 LEU A 331      -4.882   4.532  -9.056  1.00  7.60           C  
ANISOU 1992  CD1 LEU A 331      919    945   1023   -146     36    -88       C  
ATOM   1993  CD2 LEU A 331      -4.945   5.899 -11.146  1.00  8.50           C  
ANISOU 1993  CD2 LEU A 331     1231   1023    974    -90   -120   -205       C  
ATOM   1994  H   LEU A 331      -1.580   6.895  -9.636  1.00  6.72           H  
ATOM   1995  HA  LEU A 331      -3.721   8.193 -10.516  1.00  7.03           H  
ATOM   1996  HB2 LEU A 331      -3.450   6.550  -8.250  1.00  7.76           H  
ATOM   1997  HB3 LEU A 331      -4.835   7.144  -8.755  1.00  7.76           H  
ATOM   1998  HG  LEU A 331      -3.322   5.237 -10.195  1.00  8.37           H  
ATOM   1999 HD11 LEU A 331      -4.998   3.730  -9.588  1.00  9.13           H  
ATOM   2000 HD12 LEU A 331      -4.340   4.336  -8.276  1.00  9.13           H  
ATOM   2001 HD13 LEU A 331      -5.746   4.875  -8.781  1.00  9.13           H  
ATOM   2002 HD21 LEU A 331      -5.201   5.068 -11.577  1.00 10.20           H  
ATOM   2003 HD22 LEU A 331      -5.738   6.406 -10.910  1.00 10.20           H  
ATOM   2004 HD23 LEU A 331      -4.383   6.420 -11.739  1.00 10.20           H  
ATOM   2005  N   SER A 332      -4.246   9.993  -8.952  1.00  6.11           N  
ANISOU 2005  N   SER A 332      720    900    702     42    -31    -98       N  
ATOM   2006  CA  SER A 332      -4.478  11.185  -8.143  1.00  6.63           C  
ANISOU 2006  CA  SER A 332      777    871    870     55     -6   -136       C  
ATOM   2007  C   SER A 332      -3.421  12.258  -8.348  1.00  6.45           C  
ANISOU 2007  C   SER A 332      782    862    807     72      4    -88       C  
ATOM   2008  O   SER A 332      -3.288  13.149  -7.516  1.00  7.51           O  
ANISOU 2008  O   SER A 332     1035    982    838      2    -13   -132       O  
ATOM   2009  CB  SER A 332      -4.724  10.846  -6.670  1.00  7.11           C  
ANISOU 2009  CB  SER A 332      831   1020    851    -45    168   -158       C  
ATOM   2010  OG  SER A 332      -5.904  10.082  -6.532  1.00  7.79           O  
ANISOU 2010  OG  SER A 332      866   1114    980    -68    173   -171       O  
ATOM   2011  H   SER A 332      -4.869   9.858  -9.528  1.00  7.34           H  
ATOM   2012  HA  SER A 332      -5.303  11.597  -8.445  1.00  7.96           H  
ATOM   2013  HB2 SER A 332      -3.972  10.333  -6.333  1.00  8.54           H  
ATOM   2014  HB3 SER A 332      -4.817  11.669  -6.166  1.00  8.54           H  
ATOM   2015  HG  SER A 332      -6.566  10.524  -6.801  1.00  9.36           H  
ATOM   2016  N   ALA A 333      -2.742  12.227  -9.485  1.00  6.91           N  
ANISOU 2016  N   ALA A 333      872    863    888     39     74    -20       N  
ATOM   2017  CA  ALA A 333      -1.863  13.316  -9.916  1.00  7.57           C  
ANISOU 2017  CA  ALA A 333      863    988   1027     13     24    -45       C  
ATOM   2018  C   ALA A 333      -2.650  14.237 -10.850  1.00  7.04           C  
ANISOU 2018  C   ALA A 333      844    926    906    -21    106    -86       C  
ATOM   2019  O   ALA A 333      -3.846  14.418 -10.654  1.00  7.25           O  
ANISOU 2019  O   ALA A 333      863    944    948    -28     21      7       O  
ATOM   2020  CB  ALA A 333      -0.573  12.772 -10.521  1.00  9.27           C  
ANISOU 2020  CB  ALA A 333     1008   1245   1269    123     66    -27       C  
ATOM   2021  H   ALA A 333      -2.770  11.572 -10.042  1.00  8.30           H  
ATOM   2022  HA  ALA A 333      -1.567  13.853  -9.164  1.00  9.10           H  
ATOM   2023  HB1 ALA A 333      -0.005  13.516 -10.776  1.00 11.13           H  
ATOM   2024  HB2 ALA A 333      -0.122  12.222  -9.861  1.00 11.13           H  
ATOM   2025  HB3 ALA A 333      -0.790  12.239 -11.302  1.00 11.13           H  
ATOM   2026  N   GLY A 334      -2.033  14.860 -11.847  1.00  8.20           N  
ANISOU 2026  N   GLY A 334     1130   1141    845     93    220    -42       N  
ATOM   2027  CA  GLY A 334      -2.754  15.824 -12.660  1.00  8.61           C  
ANISOU 2027  CA  GLY A 334     1346   1131    795    117    205     76       C  
ATOM   2028  C   GLY A 334      -3.153  17.021 -11.815  1.00  7.76           C  
ANISOU 2028  C   GLY A 334     1128   1038    783     85    102    -15       C  
ATOM   2029  O   GLY A 334      -2.293  17.651 -11.196  1.00  8.07           O  
ANISOU 2029  O   GLY A 334     1026   1179    860     33     63   -110       O  
ATOM   2030  H   GLY A 334      -1.210  14.742 -12.068  1.00  9.85           H  
ATOM   2031  HA2 GLY A 334      -2.192  16.126 -13.390  1.00 10.35           H  
ATOM   2032  HA3 GLY A 334      -3.554  15.414 -13.025  1.00 10.35           H  
ATOM   2033  N   ILE A 335      -4.446  17.311 -11.755  1.00  6.99           N  
ANISOU 2033  N   ILE A 335     1053    914    688    -31     37     -2       N  
ATOM   2034  CA  ILE A 335      -4.990  18.351 -10.885  1.00  6.79           C  
ANISOU 2034  CA  ILE A 335      926    864    790    -41     -2    -26       C  
ATOM   2035  C   ILE A 335      -5.721  17.749  -9.692  1.00  6.58           C  
ANISOU 2035  C   ILE A 335      835    864    802      0     32    -21       C  
ATOM   2036  O   ILE A 335      -6.435  18.472  -8.982  1.00  7.58           O  
ANISOU 2036  O   ILE A 335      956   1029    896     85    185    -10       O  
ATOM   2037  CB  ILE A 335      -5.834  19.407 -11.629  1.00  7.51           C  
ANISOU 2037  CB  ILE A 335     1093    877    885    -40    -69     -5       C  
ATOM   2038  CG1 ILE A 335      -7.139  18.838 -12.189  1.00  8.08           C  
ANISOU 2038  CG1 ILE A 335      981   1052   1037    -27   -133     41       C  
ATOM   2039  CG2 ILE A 335      -4.985  20.063 -12.713  1.00  7.95           C  
ANISOU 2039  CG2 ILE A 335     1150    959    910   -104    -36     13       C  
ATOM   2040  CD1 ILE A 335      -8.138  19.908 -12.577  1.00  9.06           C  
ANISOU 2040  CD1 ILE A 335     1022   1185   1235      2   -185     46       C  
ATOM   2041  H   ILE A 335      -5.047  16.908 -12.220  1.00  8.39           H  
ATOM   2042  HA  ILE A 335      -4.237  18.852 -10.534  1.00  8.16           H  
ATOM   2043  HB  ILE A 335      -6.104  20.081 -10.986  1.00  9.02           H  
ATOM   2044 HG12 ILE A 335      -6.940  18.314 -12.980  1.00  9.70           H  
ATOM   2045 HG13 ILE A 335      -7.551  18.276 -11.514  1.00  9.70           H  
ATOM   2046 HG21 ILE A 335      -5.507  20.757 -13.145  1.00  9.54           H  
ATOM   2047 HG22 ILE A 335      -4.195  20.450 -12.304  1.00  9.54           H  
ATOM   2048 HG23 ILE A 335      -4.727  19.391 -13.362  1.00  9.54           H  
ATOM   2049 HD11 ILE A 335      -8.953  19.482 -12.887  1.00 10.88           H  
ATOM   2050 HD12 ILE A 335      -8.327  20.459 -11.802  1.00 10.88           H  
ATOM   2051 HD13 ILE A 335      -7.759  20.451 -13.285  1.00 10.88           H  
ATOM   2052  N   PHE A 336      -5.547  16.449  -9.433  1.00  6.57           N  
ANISOU 2052  N   PHE A 336      754    925    816     24    130     16       N  
ATOM   2053  CA  PHE A 336      -6.222  15.819  -8.307  1.00  6.53           C  
ANISOU 2053  CA  PHE A 336      709    928    846     50    167     25       C  
ATOM   2054  C   PHE A 336      -5.554  16.088  -6.959  1.00  6.79           C  
ANISOU 2054  C   PHE A 336      759    948    873     91    188    -51       C  
ATOM   2055  O   PHE A 336      -6.225  15.987  -5.929  1.00  8.27           O  
ANISOU 2055  O   PHE A 336      964   1217    963      8    349   -129       O  
ATOM   2056  CB  PHE A 336      -6.321  14.292  -8.500  1.00  7.02           C  
ANISOU 2056  CB  PHE A 336      950    900    819     33    101     61       C  
ATOM   2057  CG  PHE A 336      -7.399  13.793  -9.444  1.00  7.84           C  
ANISOU 2057  CG  PHE A 336     1027   1000    953    -27    103     74       C  
ATOM   2058  CD1 PHE A 336      -7.604  14.334 -10.702  1.00 10.33           C  
ANISOU 2058  CD1 PHE A 336     1487   1312   1126   -470   -275    248       C  
ATOM   2059  CD2 PHE A 336      -8.142  12.667  -9.086  1.00  7.67           C  
ANISOU 2059  CD2 PHE A 336      930   1014    972    -52    265      0       C  
ATOM   2060  CE1 PHE A 336      -8.550  13.794 -11.546  1.00 11.25           C  
ANISOU 2060  CE1 PHE A 336     1611   1450   1215   -518   -274    248       C  
ATOM   2061  CE2 PHE A 336      -9.073  12.123  -9.944  1.00  8.28           C  
ANISOU 2061  CE2 PHE A 336     1054    982   1109   -173    163      1       C  
ATOM   2062  CZ  PHE A 336      -9.277  12.676 -11.163  1.00 10.34           C  
ANISOU 2062  CZ  PHE A 336     1415   1271   1244   -428   -107     47       C  
ATOM   2063  H   PHE A 336      -5.048  15.920  -9.892  1.00  7.89           H  
ATOM   2064  HA  PHE A 336      -7.120  16.185  -8.282  1.00  7.85           H  
ATOM   2065  HB2 PHE A 336      -5.472  13.977  -8.847  1.00  8.44           H  
ATOM   2066  HB3 PHE A 336      -6.494  13.890  -7.634  1.00  8.44           H  
ATOM   2067  HD1 PHE A 336      -7.101  15.066 -10.978  1.00 12.40           H  
ATOM   2068  HD2 PHE A 336      -8.007  12.276  -8.253  1.00  9.22           H  
ATOM   2069  HE1 PHE A 336      -8.702  14.182 -12.378  1.00 13.51           H  
ATOM   2070  HE2 PHE A 336      -9.561  11.375  -9.686  1.00  9.94           H  
ATOM   2071  HZ  PHE A 336      -9.904  12.307 -11.743  1.00 12.42           H  
ATOM   2072  N   GLY A 337      -4.261  16.395  -6.926  1.00  6.87           N  
ANISOU 2072  N   GLY A 337      758    996    855     45    127   -111       N  
ATOM   2073  CA  GLY A 337      -3.631  16.919  -5.731  1.00  7.90           C  
ANISOU 2073  CA  GLY A 337      953   1099    948     52     79   -222       C  
ATOM   2074  C   GLY A 337      -2.820  15.979  -4.857  1.00  8.72           C  
ANISOU 2074  C   GLY A 337     1098   1286    928    139    -24   -339       C  
ATOM   2075  O   GLY A 337      -2.236  16.446  -3.867  1.00 10.91           O  
ANISOU 2075  O   GLY A 337     1574   1433   1139    363   -284   -455       O  
ATOM   2076  H   GLY A 337      -3.726  16.307  -7.593  1.00  8.25           H  
ATOM   2077  HA2 GLY A 337      -3.032  17.632  -6.002  1.00  9.49           H  
ATOM   2078  HA3 GLY A 337      -4.329  17.289  -5.169  1.00  9.49           H  
ATOM   2079  N   ALA A 338      -2.748  14.690  -5.147  1.00  7.73           N  
ANISOU 2079  N   ALA A 338      899   1187    850    155      2   -229       N  
ATOM   2080  CA  ALA A 338      -1.922  13.829  -4.312  1.00  8.39           C  
ANISOU 2080  CA  ALA A 338     1014   1352    820    208    -74   -170       C  
ATOM   2081  C   ALA A 338      -0.455  14.063  -4.624  1.00  8.74           C  
ANISOU 2081  C   ALA A 338      889   1446    986    116   -100    -65       C  
ATOM   2082  O   ALA A 338      -0.085  14.327  -5.763  1.00 11.56           O  
ANISOU 2082  O   ALA A 338      897   2328   1168    281     55    356       O  
ATOM   2083  CB  ALA A 338      -2.254  12.366  -4.530  1.00  9.20           C  
ANISOU 2083  CB  ALA A 338     1151   1408    935    177    -86    -47       C  
ATOM   2084  H   ALA A 338      -3.152  14.301  -5.799  1.00  9.28           H  
ATOM   2085  HA  ALA A 338      -2.090  14.033  -3.379  1.00 10.07           H  
ATOM   2086  HB1 ALA A 338      -1.683  11.824  -3.962  1.00 11.04           H  
ATOM   2087  HB2 ALA A 338      -3.185  12.216  -4.302  1.00 11.04           H  
ATOM   2088  HB3 ALA A 338      -2.101  12.142  -5.461  1.00 11.04           H  
ATOM   2089  N  AASP A 339       0.387  13.929  -3.615  0.52  9.89           N  
ANISOU 2089  N  AASP A 339     1130   1457   1169    107   -249   -177       N  
ATOM   2090  N  BASP A 339       0.381  13.902  -3.613  0.48  8.23           N  
ANISOU 2090  N  BASP A 339     1010   1079   1036     31   -142   -281       N  
ATOM   2091  CA AASP A 339       1.830  14.027  -3.831  0.52 11.38           C  
ANISOU 2091  CA AASP A 339     1213   1617   1493      6   -393   -193       C  
ATOM   2092  CA BASP A 339       1.815  13.972  -3.834  0.48  8.64           C  
ANISOU 2092  CA BASP A 339     1021    939   1324   -163   -364   -192       C  
ATOM   2093  C  AASP A 339       2.279  12.849  -4.690  0.52  9.35           C  
ANISOU 2093  C  AASP A 339      880   1319   1352    -80   -146     11       C  
ATOM   2094  C  BASP A 339       2.252  12.782  -4.685  0.48  8.26           C  
ANISOU 2094  C  BASP A 339      902   1081   1154    -24   -307     62       C  
ATOM   2095  O  AASP A 339       2.055  11.700  -4.297  0.52  8.87           O  
ANISOU 2095  O  AASP A 339     1055   1130   1185   -244      7   -141       O  
ATOM   2096  O  BASP A 339       1.928  11.639  -4.353  0.48  8.64           O  
ANISOU 2096  O  BASP A 339     1064   1111   1106    140   -334    -47       O  
ATOM   2097  CB AASP A 339       2.515  13.992  -2.470  0.52 15.28           C  
ANISOU 2097  CB AASP A 339     1769   2220   1818     35   -708   -387       C  
ATOM   2098  CB BASP A 339       2.547  13.944  -2.507  0.48  9.92           C  
ANISOU 2098  CB BASP A 339     1175    986   1606    -68   -618   -372       C  
ATOM   2099  CG AASP A 339       3.977  14.374  -2.540  0.52 18.93           C  
ANISOU 2099  CG AASP A 339     2302   2879   2013    -85  -1016   -540       C  
ATOM   2100  CG BASP A 339       4.035  14.048  -2.682  0.48 11.24           C  
ANISOU 2100  CG BASP A 339     1210   1296   1765    -88   -730    -46       C  
ATOM   2101  OD1AASP A 339       4.414  14.855  -3.610  0.52 21.41           O  
ANISOU 2101  OD1AASP A 339     2715   3230   2189   -211   -827   -446       O  
ATOM   2102  OD1BASP A 339       4.493  15.186  -2.859  0.48 11.71           O  
ANISOU 2102  OD1BASP A 339     1381   1127   1941      0   -324    -35       O  
ATOM   2103  OD2AASP A 339       4.679  14.207  -1.516  0.52 20.39           O  
ANISOU 2103  OD2AASP A 339     2529   2981   2237     78  -1170   -628       O  
ATOM   2104  OD2BASP A 339       4.733  13.023  -2.688  0.48 12.21           O  
ANISOU 2104  OD2BASP A 339     1335   1484   1819    -68   -543   -269       O  
ATOM   2105  H  AASP A 339       0.156  13.782  -2.799  0.52 11.87           H  
ATOM   2106  H  BASP A 339       0.148  13.752  -2.798  0.48  9.88           H  
ATOM   2107  HA AASP A 339       2.068  14.849  -4.288  0.52 13.66           H  
ATOM   2108  HA BASP A 339       2.038  14.796  -4.295  0.48 10.38           H  
ATOM   2109  HB2AASP A 339       2.070  14.616  -1.876  0.52 18.35           H  
ATOM   2110  HB2BASP A 339       2.253  14.692  -1.964  0.48 11.91           H  
ATOM   2111  HB3AASP A 339       2.457  13.093  -2.111  0.52 18.35           H  
ATOM   2112  HB3BASP A 339       2.353  13.108  -2.053  0.48 11.91           H  
ATOM   2113  N  APRO A 340       2.906  13.067  -5.853  0.52  9.45           N  
ANISOU 2113  N  APRO A 340      972   1068   1549    -62   -160    130       N  
ATOM   2114  N  BPRO A 340       3.017  12.999  -5.754  0.48  8.38           N  
ANISOU 2114  N  BPRO A 340     1057    921   1205     15    -95    151       N  
ATOM   2115  CA APRO A 340       3.269  11.913  -6.694  0.52  9.31           C  
ANISOU 2115  CA APRO A 340      934   1226   1376   -153   -246    122       C  
ATOM   2116  CA BPRO A 340       3.355  11.877  -6.645  0.48  8.15           C  
ANISOU 2116  CA BPRO A 340     1125    968   1005    -18    -41    183       C  
ATOM   2117  C  APRO A 340       4.134  10.881  -6.005  0.52  7.80           C  
ANISOU 2117  C  APRO A 340      701   1104   1159    -43   -291      9       C  
ATOM   2118  C  BPRO A 340       4.289  10.864  -6.025  0.48  8.38           C  
ANISOU 2118  C  BPRO A 340     1399    913    871    -19    -26    164       C  
ATOM   2119  O  APRO A 340       3.923   9.684  -6.235  0.52  8.63           O  
ANISOU 2119  O  APRO A 340      976   1156   1147   -108   -522    -26       O  
ATOM   2120  O  BPRO A 340       4.204   9.681  -6.375  0.48  8.99           O  
ANISOU 2120  O  BPRO A 340     1779    779    857     12    -78    -18       O  
ATOM   2121  CB APRO A 340       3.951  12.557  -7.906  0.52 11.03           C  
ANISOU 2121  CB APRO A 340     1098   1576   1517     84   -219    373       C  
ATOM   2122  CB BPRO A 340       3.980  12.566  -7.863  0.48  9.75           C  
ANISOU 2122  CB BPRO A 340     1270   1309   1124    165     95    320       C  
ATOM   2123  CG APRO A 340       3.295  13.895  -8.012  0.52 11.73           C  
ANISOU 2123  CG APRO A 340     1162   1550   1744     78   -104    601       C  
ATOM   2124  CG BPRO A 340       4.468  13.883  -7.337  0.48  9.77           C  
ANISOU 2124  CG BPRO A 340     1259   1190   1261     30    105    350       C  
ATOM   2125  CD APRO A 340       3.076  14.338  -6.583  0.52 10.38           C  
ANISOU 2125  CD APRO A 340      905   1259   1779    192     80    291       C  
ATOM   2126  CD BPRO A 340       3.569  14.281  -6.222  0.48 10.30           C  
ANISOU 2126  CD BPRO A 340     1277   1238   1398    153    -67    178       C  
ATOM   2127  HA APRO A 340       2.458  11.470  -6.991  0.52 11.18           H  
ATOM   2128  HA BPRO A 340       2.543  11.422  -6.919  0.48  9.79           H  
ATOM   2129  HB2APRO A 340       4.904  12.644  -7.747  0.52 13.25           H  
ATOM   2130  HB2BPRO A 340       4.714  12.033  -8.206  0.48 11.71           H  
ATOM   2131  HB3APRO A 340       3.795  12.024  -8.701  0.52 13.25           H  
ATOM   2132  HB3BPRO A 340       3.311  12.692  -8.554  0.48 11.71           H  
ATOM   2133  HG2APRO A 340       3.878  14.513  -8.481  0.52 14.08           H  
ATOM   2134  HG2BPRO A 340       5.378  13.783  -7.016  0.48 11.73           H  
ATOM   2135  HG3APRO A 340       2.451  13.813  -8.483  0.52 14.08           H  
ATOM   2136  HG3BPRO A 340       4.438  14.543  -8.047  0.48 11.73           H  
ATOM   2137  HD2APRO A 340       3.847  14.825  -6.251  0.52 12.46           H  
ATOM   2138  HD2BPRO A 340       4.068  14.720  -5.516  0.48 12.37           H  
ATOM   2139  HD3APRO A 340       2.280  14.887  -6.510  0.52 12.46           H  
ATOM   2140  HD3BPRO A 340       2.863  14.865  -6.541  0.48 12.37           H  
ATOM   2141  N  AILE A 341       5.100  11.282  -5.183  0.52  7.75           N  
ANISOU 2141  N  AILE A 341      856    960   1129     -2   -281    -83       N  
ATOM   2142  N  BILE A 341       5.191  11.277  -5.138  0.48  9.00           N  
ANISOU 2142  N  BILE A 341     1397    996   1025   -104   -150     -4       N  
ATOM   2143  CA AILE A 341       5.930  10.283  -4.519  0.52  7.56           C  
ANISOU 2143  CA AILE A 341      911    990    972    152   -293   -120       C  
ATOM   2144  CA BILE A 341       6.004  10.292  -4.437  0.48 10.15           C  
ANISOU 2144  CA BILE A 341     1594   1183   1081    -17   -303    -10       C  
ATOM   2145  C  AILE A 341       5.079   9.397  -3.617  0.52  8.89           C  
ANISOU 2145  C  AILE A 341     1418   1092    869    182   -558   -108       C  
ATOM   2146  C  BILE A 341       5.117   9.402  -3.571  0.48 10.71           C  
ANISOU 2146  C  BILE A 341     1826   1221   1022    -21   -358   -187       C  
ATOM   2147  O  AILE A 341       5.300   8.183  -3.523  0.52  9.34           O  
ANISOU 2147  O  AILE A 341     1550    943   1056     34   -726     85       O  
ATOM   2148  O  BILE A 341       5.334   8.188  -3.477  0.48 11.24           O  
ANISOU 2148  O  BILE A 341     1974   1126   1169   -376   -539   -189       O  
ATOM   2149  CB AILE A 341       7.107  10.947  -3.782  0.52  7.83           C  
ANISOU 2149  CB AILE A 341      841    988   1146    116    -78   -323       C  
ATOM   2150  CB BILE A 341       7.133  10.977  -3.641  0.48 11.91           C  
ANISOU 2150  CB BILE A 341     1577   1575   1373     51   -414    103       C  
ATOM   2151  CG1AILE A 341       8.083   9.896  -3.263  0.52  7.59           C  
ANISOU 2151  CG1AILE A 341      760   1098   1027    153    -59    -20       C  
ATOM   2152  CG1BILE A 341       8.080  11.741  -4.591  0.48 13.82           C  
ANISOU 2152  CG1BILE A 341     1498   2058   1693   -102   -250    433       C  
ATOM   2153  CG2AILE A 341       6.615  11.796  -2.634  0.52  9.58           C  
ANISOU 2153  CG2AILE A 341     1018   1308   1314    -92   -150   -455       C  
ATOM   2154  CG2BILE A 341       7.899   9.942  -2.848  0.48 12.44           C  
ANISOU 2154  CG2BILE A 341     1767   1622   1337    201   -472     32       C  
ATOM   2155  CD1AILE A 341       8.656   8.997  -4.346  0.52  9.88           C  
ANISOU 2155  CD1AILE A 341     1057   1432   1266    119   -335   -118       C  
ATOM   2156  CD1BILE A 341       9.134  12.602  -3.902  0.48 15.42           C  
ANISOU 2156  CD1BILE A 341     1655   2326   1877   -270   -134    539       C  
ATOM   2157  H  AILE A 341       5.290  12.100  -4.998  0.52  9.31           H  
ATOM   2158  H  BILE A 341       5.346  12.097  -4.931  0.48 10.80           H  
ATOM   2159  HA AILE A 341       6.320   9.706  -5.195  0.52  9.08           H  
ATOM   2160  HA BILE A 341       6.438   9.721  -5.090  0.48 12.19           H  
ATOM   2161  HB AILE A 341       7.565  11.516  -4.420  0.52  9.41           H  
ATOM   2162  HB BILE A 341       6.738  11.617  -3.029  0.48 14.30           H  
ATOM   2163 HG12AILE A 341       8.826  10.347  -2.831  0.52  9.12           H  
ATOM   2164 HG12BILE A 341       8.548  11.094  -5.142  0.48 16.59           H  
ATOM   2165 HG13AILE A 341       7.622   9.330  -2.624  0.52  9.12           H  
ATOM   2166 HG13BILE A 341       7.546  12.328  -5.149  0.48 16.59           H  
ATOM   2167 HG21AILE A 341       7.342  12.359  -2.324  0.52 11.51           H  
ATOM   2168 HG21BILE A 341       8.705  10.348  -2.494  0.48 14.94           H  
ATOM   2169 HG22AILE A 341       5.878  12.347  -2.942  0.52 11.51           H  
ATOM   2170 HG22BILE A 341       7.341   9.625  -2.120  0.48 14.94           H  
ATOM   2171 HG23AILE A 341       6.317  11.216  -1.917  0.52 11.51           H  
ATOM   2172 HG23BILE A 341       8.129   9.203  -3.433  0.48 14.94           H  
ATOM   2173 HD11AILE A 341       9.340   8.431  -3.957  0.52 11.87           H  
ATOM   2174 HD11BILE A 341       9.613  13.112  -4.574  0.48 18.51           H  
ATOM   2175 HD12AILE A 341       7.943   8.451  -4.713  0.52 11.87           H  
ATOM   2176 HD12BILE A 341       8.694  13.203  -3.281  0.48 18.51           H  
ATOM   2177 HD13AILE A 341       9.041   9.550  -5.044  0.52 11.87           H  
ATOM   2178 HD13BILE A 341       9.749  12.025  -3.424  0.48 18.51           H  
ATOM   2179  N   HIS A 342       4.106   9.989  -2.924  1.00  9.79           N  
ANISOU 2179  N   HIS A 342     1744   1116    859   -194   -217   -114       N  
ATOM   2180  CA  HIS A 342       3.184   9.182  -2.139  1.00 10.96           C  
ANISOU 2180  CA  HIS A 342     2124   1286    756   -279    -90   -136       C  
ATOM   2181  C   HIS A 342       2.360   8.248  -3.020  1.00 10.72           C  
ANISOU 2181  C   HIS A 342     2192   1194    686   -258   -198    -57       C  
ATOM   2182  O   HIS A 342       2.160   7.079  -2.677  1.00 11.34           O  
ANISOU 2182  O   HIS A 342     2359   1198    749   -387   -211     12       O  
ATOM   2183  CB  HIS A 342       2.273  10.098  -1.345  1.00 12.54           C  
ANISOU 2183  CB  HIS A 342     2407   1528    829   -487     70   -174       C  
ATOM   2184  CG  HIS A 342       1.230   9.360  -0.596  1.00 13.52           C  
ANISOU 2184  CG  HIS A 342     2476   1736    925   -544     33   -148       C  
ATOM   2185  ND1 HIS A 342       1.527   8.508   0.445  1.00 15.40           N  
ANISOU 2185  ND1 HIS A 342     2695   2166    990   -452    -96    133       N  
ATOM   2186  CD2 HIS A 342      -0.104   9.274  -0.793  1.00 13.70           C  
ANISOU 2186  CD2 HIS A 342     2430   1710   1063   -419    160   -214       C  
ATOM   2187  CE1 HIS A 342       0.407   7.964   0.883  1.00 15.12           C  
ANISOU 2187  CE1 HIS A 342     2635   2074   1037   -480     45    115       C  
ATOM   2188  NE2 HIS A 342      -0.597   8.418   0.152  1.00 14.07           N  
ANISOU 2188  NE2 HIS A 342     2366   1886   1094   -499     91   -165       N  
ATOM   2189  H   HIS A 342       3.966  10.837  -2.896  1.00 11.75           H  
ATOM   2190  HA  HIS A 342       3.693   8.631  -1.523  1.00 13.17           H  
ATOM   2191  HB2 HIS A 342       2.805  10.597  -0.706  1.00 15.05           H  
ATOM   2192  HB3 HIS A 342       1.829  10.708  -1.955  1.00 15.05           H  
ATOM   2193  HD2 HIS A 342      -0.594   9.714  -1.449  1.00 16.45           H  
ATOM   2194  HE1 HIS A 342       0.335   7.361   1.587  1.00 18.15           H  
ATOM   2195  HE2 HIS A 342      -1.425   8.210   0.255  1.00 16.89           H  
ATOM   2196  N   SER A 343       1.869   8.743  -4.155  1.00  9.06           N  
ANISOU 2196  N   SER A 343     1652   1039    751   -220    -79    -63       N  
ATOM   2197  CA  SER A 343       1.116   7.885  -5.062  1.00  7.94           C  
ANISOU 2197  CA  SER A 343     1221   1005    792   -158    -63      5       C  
ATOM   2198  C   SER A 343       1.971   6.720  -5.542  1.00  7.04           C  
ANISOU 2198  C   SER A 343     1027    934    713    -87   -223    -29       C  
ATOM   2199  O   SER A 343       1.491   5.586  -5.628  1.00  7.52           O  
ANISOU 2199  O   SER A 343     1074    997    787    -50   -178    -22       O  
ATOM   2200  CB  SER A 343       0.559   8.712  -6.209  1.00  7.38           C  
ANISOU 2200  CB  SER A 343     1000    950    852    -14    -40   -121       C  
ATOM   2201  OG  SER A 343      -0.283   7.890  -6.997  1.00  7.41           O  
ANISOU 2201  OG  SER A 343      951    947    919     71    -54    -18       O  
ATOM   2202  H   SER A 343       1.957   9.557  -4.417  1.00 10.88           H  
ATOM   2203  HA  SER A 343       0.354   7.502  -4.599  1.00  9.54           H  
ATOM   2204  HB2 SER A 343       0.046   9.455  -5.853  1.00  8.86           H  
ATOM   2205  HB3 SER A 343       1.289   9.045  -6.753  1.00  8.86           H  
ATOM   2206  HG  SER A 343      -0.633   8.344  -7.612  1.00  8.91           H  
ATOM   2207  N   LEU A 344       3.239   6.977  -5.842  1.00  7.26           N  
ANISOU 2207  N   LEU A 344     1042    888    827    -96   -302    -54       N  
ATOM   2208  CA  LEU A 344       4.141   5.905  -6.257  1.00  7.49           C  
ANISOU 2208  CA  LEU A 344      941    942    964    -85   -387    -24       C  
ATOM   2209  C   LEU A 344       4.341   4.890  -5.132  1.00  7.85           C  
ANISOU 2209  C   LEU A 344      947    995   1040   -136   -433     46       C  
ATOM   2210  O   LEU A 344       4.368   3.687  -5.367  1.00  8.44           O  
ANISOU 2210  O   LEU A 344     1125    888   1192   -133   -449     65       O  
ATOM   2211  CB  LEU A 344       5.472   6.500  -6.722  1.00  7.73           C  
ANISOU 2211  CB  LEU A 344      905    969   1061    -48   -431     13       C  
ATOM   2212  CG  LEU A 344       6.520   5.469  -7.141  1.00  8.05           C  
ANISOU 2212  CG  LEU A 344      812    998   1248   -101   -410     43       C  
ATOM   2213  CD1 LEU A 344       6.051   4.587  -8.285  1.00  8.52           C  
ANISOU 2213  CD1 LEU A 344      919   1118   1202      0   -279    -63       C  
ATOM   2214  CD2 LEU A 344       7.801   6.186  -7.536  1.00  9.51           C  
ANISOU 2214  CD2 LEU A 344      936   1086   1592   -129   -347      9       C  
ATOM   2215  H   LEU A 344       3.602   7.756  -5.815  1.00  8.72           H  
ATOM   2216  HA  LEU A 344       3.756   5.430  -7.010  1.00  9.00           H  
ATOM   2217  HB2 LEU A 344       5.302   7.073  -7.485  1.00  9.28           H  
ATOM   2218  HB3 LEU A 344       5.848   7.020  -5.994  1.00  9.28           H  
ATOM   2219  HG  LEU A 344       6.682   4.881  -6.387  1.00  9.67           H  
ATOM   2220 HD11 LEU A 344       6.767   3.981  -8.531  1.00 10.24           H  
ATOM   2221 HD12 LEU A 344       5.275   4.081  -7.996  1.00 10.24           H  
ATOM   2222 HD13 LEU A 344       5.817   5.147  -9.041  1.00 10.24           H  
ATOM   2223 HD21 LEU A 344       8.475   5.527  -7.764  1.00 11.42           H  
ATOM   2224 HD22 LEU A 344       7.622   6.754  -8.302  1.00 11.42           H  
ATOM   2225 HD23 LEU A 344       8.105   6.725  -6.789  1.00 11.42           H  
ATOM   2226  N   ARG A 345       4.521   5.364  -3.901  1.00  8.94           N  
ANISOU 2226  N   ARG A 345     1333   1004   1062   -188   -545    135       N  
ATOM   2227  CA  ARG A 345       4.669   4.475  -2.747  1.00 10.13           C  
ANISOU 2227  CA  ARG A 345     1532   1221   1094   -328   -719    268       C  
ATOM   2228  C   ARG A 345       3.457   3.559  -2.608  1.00 10.18           C  
ANISOU 2228  C   ARG A 345     1650   1258    958   -346   -659    244       C  
ATOM   2229  O   ARG A 345       3.591   2.342  -2.425  1.00 10.57           O  
ANISOU 2229  O   ARG A 345     1665   1194   1157   -343   -685    292       O  
ATOM   2230  CB  ARG A 345       4.853   5.334  -1.484  1.00 12.85           C  
ANISOU 2230  CB  ARG A 345     2085   1543   1253   -607   -830    280       C  
ATOM   2231  CG  ARG A 345       4.939   4.575  -0.174  1.00 16.38           C  
ANISOU 2231  CG  ARG A 345     2618   2039   1566   -584  -1045    322       C  
ATOM   2232  CD  ARG A 345       6.335   4.057   0.026  1.00 19.29           C  
ANISOU 2232  CD  ARG A 345     2880   2355   2094   -631   -909    146       C  
ATOM   2233  NE  ARG A 345       6.491   2.707  -0.498  1.00 21.23           N  
ANISOU 2233  NE  ARG A 345     2953   2688   2423   -805   -956   -121       N  
ATOM   2234  CZ  ARG A 345       7.635   2.196  -0.950  1.00 23.99           C  
ANISOU 2234  CZ  ARG A 345     3162   3276   2676   -913  -1008   -319       C  
ATOM   2235  NH1 ARG A 345       8.738   2.932  -0.989  1.00 25.03           N  
ANISOU 2235  NH1 ARG A 345     3044   3718   2750   -848  -1183   -312       N  
ATOM   2236  NH2 ARG A 345       7.668   0.947  -1.389  1.00 25.04           N  
ANISOU 2236  NH2 ARG A 345     3372   3338   2804  -1018   -819   -398       N  
ATOM   2237  H   ARG A 345       4.562   6.200  -3.703  1.00 10.74           H  
ATOM   2238  HA  ARG A 345       5.452   3.914  -2.860  1.00 12.16           H  
ATOM   2239  HB2 ARG A 345       5.676   5.839  -1.578  1.00 15.43           H  
ATOM   2240  HB3 ARG A 345       4.098   5.940  -1.416  1.00 15.43           H  
ATOM   2241  HG2 ARG A 345       4.719   5.167   0.563  1.00 19.66           H  
ATOM   2242  HG3 ARG A 345       4.327   3.824  -0.190  1.00 19.66           H  
ATOM   2243  HD2 ARG A 345       6.961   4.636  -0.436  1.00 23.15           H  
ATOM   2244  HD3 ARG A 345       6.537   4.039   0.974  1.00 23.15           H  
ATOM   2245  HE  ARG A 345       5.794   2.204  -0.517  1.00 25.48           H  
ATOM   2246 HH11 ARG A 345       8.719   3.749  -0.721  1.00 30.05           H  
ATOM   2247 HH12 ARG A 345       9.471   2.592  -1.282  1.00 30.05           H  
ATOM   2248 HH21 ARG A 345       6.953   0.470  -1.382  1.00 30.06           H  
ATOM   2249 HH22 ARG A 345       8.405   0.614  -1.681  1.00 30.06           H  
ATOM   2250  N   VAL A 346       2.260   4.147  -2.682  1.00  9.76           N  
ANISOU 2250  N   VAL A 346     1669   1265    775   -371   -410    196       N  
ATOM   2251  CA  VAL A 346       1.050   3.352  -2.556  1.00  9.80           C  
ANISOU 2251  CA  VAL A 346     1712   1264    748   -258   -272    162       C  
ATOM   2252  C   VAL A 346       0.959   2.361  -3.713  1.00  8.93           C  
ANISOU 2252  C   VAL A 346     1450   1127    815   -177   -349    198       C  
ATOM   2253  O   VAL A 346       0.601   1.191  -3.518  1.00  9.25           O  
ANISOU 2253  O   VAL A 346     1552   1101    861   -298   -208    172       O  
ATOM   2254  CB  VAL A 346      -0.196   4.254  -2.456  1.00 10.23           C  
ANISOU 2254  CB  VAL A 346     1909   1177    803   -256   -138     88       C  
ATOM   2255  CG1 VAL A 346      -1.479   3.416  -2.423  1.00 10.11           C  
ANISOU 2255  CG1 VAL A 346     1743   1242    857   -158   -108    120       C  
ATOM   2256  CG2 VAL A 346      -0.121   5.150  -1.235  1.00 11.65           C  
ANISOU 2256  CG2 VAL A 346     2186   1335    904   -392    -77    -46       C  
ATOM   2257  H   VAL A 346       2.129   4.989  -2.802  1.00 11.72           H  
ATOM   2258  HA  VAL A 346       1.095   2.846  -1.730  1.00 11.77           H  
ATOM   2259  HB  VAL A 346      -0.223   4.818  -3.245  1.00 12.29           H  
ATOM   2260 HG11 VAL A 346      -2.222   3.987  -2.173  1.00 12.14           H  
ATOM   2261 HG12 VAL A 346      -1.633   3.040  -3.303  1.00 12.14           H  
ATOM   2262 HG13 VAL A 346      -1.374   2.705  -1.772  1.00 12.14           H  
ATOM   2263 HG21 VAL A 346      -0.916   5.704  -1.200  1.00 13.98           H  
ATOM   2264 HG22 VAL A 346      -0.068   4.597  -0.440  1.00 13.98           H  
ATOM   2265 HG23 VAL A 346       0.669   5.709  -1.302  1.00 13.98           H  
ATOM   2266  N   CYS A 347       1.301   2.800  -4.925  1.00  8.06           N  
ANISOU 2266  N   CYS A 347     1191   1057    813   -169   -261    136       N  
ATOM   2267  CA  CYS A 347       1.330   1.886  -6.061  1.00  7.31           C  
ANISOU 2267  CA  CYS A 347      999    976    804   -176   -217     14       C  
ATOM   2268  C   CYS A 347       2.235   0.685  -5.782  1.00  7.84           C  
ANISOU 2268  C   CYS A 347     1109    983    886   -193   -358    148       C  
ATOM   2269  O   CYS A 347       1.823  -0.475  -5.920  1.00  8.32           O  
ANISOU 2269  O   CYS A 347     1142   1024    996   -157   -367    159       O  
ATOM   2270  CB  CYS A 347       1.813   2.656  -7.290  1.00  6.98           C  
ANISOU 2270  CB  CYS A 347      901    972    779    -71   -197    -24       C  
ATOM   2271  SG  CYS A 347       1.825   1.669  -8.813  1.00  7.51           S  
ANISOU 2271  SG  CYS A 347      959   1043    851    -32    -84     12       S  
ATOM   2272  H   CYS A 347       1.517   3.611  -5.112  1.00  9.68           H  
ATOM   2273  HA  CYS A 347       0.438   1.545  -6.230  1.00  8.78           H  
ATOM   2274  HB2 CYS A 347       1.226   3.414  -7.434  1.00  8.39           H  
ATOM   2275  HB3 CYS A 347       2.719   2.963  -7.129  1.00  8.39           H  
ATOM   2276  HG  CYS A 347       2.189   2.361  -9.723  1.00  9.02           H  
ATOM   2277  N   VAL A 348       3.480   0.946  -5.390  1.00  8.31           N  
ANISOU 2277  N   VAL A 348     1174    966   1016   -167   -447    196       N  
ATOM   2278  CA  VAL A 348       4.430  -0.135  -5.152  1.00  9.03           C  
ANISOU 2278  CA  VAL A 348     1197   1083   1151   -153   -433    252       C  
ATOM   2279  C   VAL A 348       3.932  -1.077  -4.069  1.00  9.50           C  
ANISOU 2279  C   VAL A 348     1251   1186   1173   -162   -485    235       C  
ATOM   2280  O   VAL A 348       4.144  -2.295  -4.137  1.00 10.33           O  
ANISOU 2280  O   VAL A 348     1376   1120   1428   -133   -447    329       O  
ATOM   2281  CB  VAL A 348       5.801   0.462  -4.799  1.00  9.78           C  
ANISOU 2281  CB  VAL A 348     1184   1210   1324   -190   -434    211       C  
ATOM   2282  CG1 VAL A 348       6.721  -0.568  -4.198  1.00 10.90           C  
ANISOU 2282  CG1 VAL A 348     1158   1400   1581   -115   -393    318       C  
ATOM   2283  CG2 VAL A 348       6.403   1.083  -6.039  1.00  9.95           C  
ANISOU 2283  CG2 VAL A 348     1147   1280   1352   -193   -449    276       C  
ATOM   2284  H   VAL A 348       3.797   1.734  -5.257  1.00  9.98           H  
ATOM   2285  HA  VAL A 348       4.516  -0.659  -5.964  1.00 10.85           H  
ATOM   2286  HB  VAL A 348       5.686   1.149  -4.124  1.00 11.75           H  
ATOM   2287 HG11 VAL A 348       7.633  -0.241  -4.242  1.00 13.08           H  
ATOM   2288 HG12 VAL A 348       6.467  -0.717  -3.274  1.00 13.08           H  
ATOM   2289 HG13 VAL A 348       6.641  -1.394  -4.701  1.00 13.08           H  
ATOM   2290 HG21 VAL A 348       7.277   1.443  -5.819  1.00 11.94           H  
ATOM   2291 HG22 VAL A 348       6.489   0.401  -6.724  1.00 11.94           H  
ATOM   2292 HG23 VAL A 348       5.821   1.794  -6.350  1.00 11.94           H  
ATOM   2293  N   ASP A 349       3.307  -0.521  -3.039  1.00  9.75           N  
ANISOU 2293  N   ASP A 349     1438   1198   1068   -228   -559    349       N  
ATOM   2294  CA  ASP A 349       2.876  -1.305  -1.893  1.00 10.84           C  
ANISOU 2294  CA  ASP A 349     1766   1271   1083   -392   -586    368       C  
ATOM   2295  C   ASP A 349       1.539  -1.994  -2.105  1.00 10.74           C  
ANISOU 2295  C   ASP A 349     1686   1332   1062   -366   -518    366       C  
ATOM   2296  O   ASP A 349       1.135  -2.789  -1.254  1.00 12.51           O  
ANISOU 2296  O   ASP A 349     1912   1668   1172   -643   -577    587       O  
ATOM   2297  CB  ASP A 349       2.808  -0.405  -0.666  1.00 12.94           C  
ANISOU 2297  CB  ASP A 349     2274   1472   1170   -579   -634    378       C  
ATOM   2298  CG  ASP A 349       4.184   0.073  -0.218  1.00 15.40           C  
ANISOU 2298  CG  ASP A 349     2629   1752   1471   -766   -850    414       C  
ATOM   2299  OD1 ASP A 349       5.195  -0.543  -0.620  1.00 17.06           O  
ANISOU 2299  OD1 ASP A 349     2666   2096   1722   -878   -982    390       O  
ATOM   2300  OD2 ASP A 349       4.235   1.053   0.529  1.00 16.74           O  
ANISOU 2300  OD2 ASP A 349     3019   1829   1511   -814   -958    350       O  
ATOM   2301  H   ASP A 349       3.119   0.316  -2.981  1.00 11.71           H  
ATOM   2302  HA  ASP A 349       3.529  -2.002  -1.723  1.00 13.02           H  
ATOM   2303  HB2 ASP A 349       2.271   0.376  -0.875  1.00 15.54           H  
ATOM   2304  HB3 ASP A 349       2.407  -0.897   0.067  1.00 15.54           H  
ATOM   2305  N   THR A 350       0.857  -1.735  -3.208  1.00 10.04           N  
ANISOU 2305  N   THR A 350     1527   1275   1013   -480   -412    360       N  
ATOM   2306  CA  THR A 350      -0.463  -2.279  -3.474  1.00  9.83           C  
ANISOU 2306  CA  THR A 350     1541   1188   1007   -345   -336    322       C  
ATOM   2307  C   THR A 350      -0.502  -3.177  -4.693  1.00  9.38           C  
ANISOU 2307  C   THR A 350     1473   1117    974   -339   -395    308       C  
ATOM   2308  O   THR A 350      -1.176  -4.220  -4.669  1.00 10.27           O  
ANISOU 2308  O   THR A 350     1581   1282   1038   -456   -306    318       O  
ATOM   2309  CB  THR A 350      -1.482  -1.135  -3.647  1.00 10.22           C  
ANISOU 2309  CB  THR A 350     1565   1257   1059   -396   -328    276       C  
ATOM   2310  OG1 THR A 350      -1.442  -0.286  -2.494  1.00 11.05           O  
ANISOU 2310  OG1 THR A 350     1734   1352   1113   -401   -227    236       O  
ATOM   2311  CG2 THR A 350      -2.888  -1.655  -3.822  1.00 10.73           C  
ANISOU 2311  CG2 THR A 350     1584   1251   1241   -282   -369    296       C  
ATOM   2312  H   THR A 350       1.147  -1.229  -3.839  1.00 12.06           H  
ATOM   2313  HA  THR A 350      -0.740  -2.810  -2.710  1.00 11.81           H  
ATOM   2314  HB  THR A 350      -1.252  -0.634  -4.445  1.00 12.27           H  
ATOM   2315  HG1 THR A 350      -0.680   0.060  -2.418  1.00 13.27           H  
ATOM   2316 HG21 THR A 350      -3.524  -0.931  -3.722  1.00 12.88           H  
ATOM   2317 HG22 THR A 350      -2.990  -2.044  -4.705  1.00 12.88           H  
ATOM   2318 HG23 THR A 350      -3.076  -2.335  -3.156  1.00 12.88           H  
ATOM   2319  N   VAL A 351       0.160  -2.792  -5.773  1.00 10.03           N  
ANISOU 2319  N   VAL A 351     1535   1262   1014   -577   -340    292       N  
ATOM   2320  CA  VAL A 351       0.038  -3.514  -7.027  1.00  9.77           C  
ANISOU 2320  CA  VAL A 351     1346   1407    960   -601   -372    309       C  
ATOM   2321  C   VAL A 351       0.878  -4.773  -6.974  1.00  9.55           C  
ANISOU 2321  C   VAL A 351     1168   1485    975   -495   -353    365       C  
ATOM   2322  O   VAL A 351       2.073  -4.738  -6.654  1.00 11.86           O  
ANISOU 2322  O   VAL A 351     1346   2033   1126   -558   -446    382       O  
ATOM   2323  CB  VAL A 351       0.406  -2.620  -8.220  1.00 11.11           C  
ANISOU 2323  CB  VAL A 351     1817   1410    995   -802   -510    319       C  
ATOM   2324  CG1 VAL A 351       0.345  -3.409  -9.520  1.00 13.36           C  
ANISOU 2324  CG1 VAL A 351     2335   1678   1062   -985   -412    421       C  
ATOM   2325  CG2 VAL A 351      -0.529  -1.419  -8.270  1.00 12.13           C  
ANISOU 2325  CG2 VAL A 351     2074   1435   1099   -770   -697    413       C  
ATOM   2326  H   VAL A 351       0.688  -2.114  -5.805  1.00 12.05           H  
ATOM   2327  HA  VAL A 351      -0.884  -3.791  -7.141  1.00 11.73           H  
ATOM   2328  HB  VAL A 351       1.315  -2.300  -8.113  1.00 13.34           H  
ATOM   2329 HG11 VAL A 351       0.491  -2.804 -10.264  1.00 16.04           H  
ATOM   2330 HG12 VAL A 351       1.035  -4.091  -9.509  1.00 16.04           H  
ATOM   2331 HG13 VAL A 351      -0.529  -3.824  -9.598  1.00 16.04           H  
ATOM   2332 HG21 VAL A 351      -0.307  -0.878  -9.045  1.00 14.56           H  
ATOM   2333 HG22 VAL A 351      -1.444  -1.733  -8.338  1.00 14.56           H  
ATOM   2334 HG23 VAL A 351      -0.417  -0.898  -7.460  1.00 14.56           H  
ATOM   2335  N  AARG A 352       0.282  -5.919  -7.360  0.63  8.34           N  
ATOM   2336  N  BARG A 352       0.199  -5.874  -7.208  0.37  8.64           N  
ATOM   2337  CA AARG A 352       0.963  -7.222  -7.346  0.63 10.09           C  
ATOM   2338  CA BARG A 352       0.768  -7.197  -7.251  0.37  9.00           C  
ATOM   2339  C  AARG A 352       1.010  -7.932  -8.698  0.63  8.11           C  
ATOM   2340  C  BARG A 352       1.026  -7.637  -8.678  0.37 10.00           C  
ATOM   2341  O  AARG A 352       1.463  -9.084  -8.783  0.63  9.01           O  
ATOM   2342  O  BARG A 352       1.838  -8.542  -8.896  0.37 12.88           O  
ATOM   2343  CB AARG A 352       0.338  -8.175  -6.339  0.63 10.94           C  
ATOM   2344  CB BARG A 352      -0.171  -8.161  -6.506  0.37  7.65           C  
ATOM   2345  CG AARG A 352       0.548  -7.784  -4.910  0.63 13.46           C  
ATOM   2346  CG BARG A 352      -0.281  -7.775  -5.028  0.37 10.18           C  
ATOM   2347  CD AARG A 352      -0.167  -8.754  -4.000  0.63 13.65           C  
ATOM   2348  CD BARG A 352      -1.139  -8.705  -4.197  0.37 11.54           C  
ATOM   2349  NE AARG A 352      -1.607  -8.823  -4.257  0.63 13.79           N  
ATOM   2350  NE BARG A 352      -2.530  -8.268  -4.187  0.37 22.24           N  
ATOM   2351  CZ AARG A 352      -2.495  -7.977  -3.751  0.63 12.51           C  
ATOM   2352  CZ BARG A 352      -3.578  -9.026  -4.498  0.37 24.48           C  
ATOM   2353  NH1AARG A 352      -2.106  -6.972  -2.975  0.63 22.21           N  
ATOM   2354  NH1BARG A 352      -3.428 -10.300  -4.839  0.37 25.59           N  
ATOM   2355  NH2AARG A 352      -3.785  -8.126  -4.027  0.63 21.35           N  
ATOM   2356  NH2BARG A 352      -4.795  -8.502  -4.451  0.37 23.45           N  
ATOM   2357  H  AARG A 352      -0.531  -5.964  -7.639  0.63 10.01           H  
ATOM   2358  H  BARG A 352      -0.649  -5.881  -7.354  0.37 10.37           H  
ATOM   2359  HA AARG A 352       1.875  -7.030  -7.077  0.63 12.11           H  
ATOM   2360  HA BARG A 352       1.620  -7.244  -6.791  0.37 10.81           H  
ATOM   2361  HB2AARG A 352      -0.619  -8.208  -6.496  0.63 13.13           H  
ATOM   2362  HB2BARG A 352      -1.056  -8.122  -6.902  0.37  9.19           H  
ATOM   2363  HB3AARG A 352       0.725  -9.055  -6.463  0.63 13.13           H  
ATOM   2364  HB3BARG A 352       0.179  -9.064  -6.564  0.37  9.19           H  
ATOM   2365  HG2AARG A 352       1.496  -7.803  -4.702  0.63 16.16           H  
ATOM   2366  HG2BARG A 352       0.609  -7.775  -4.641  0.37 12.22           H  
ATOM   2367  HG3AARG A 352       0.193  -6.895  -4.759  0.63 16.16           H  
ATOM   2368  HG3BARG A 352      -0.669  -6.888  -4.968  0.37 12.22           H  
ATOM   2369  HD2AARG A 352       0.202  -9.641  -4.131  0.63 16.39           H  
ATOM   2370  HD2BARG A 352      -1.101  -9.599  -4.572  0.37 13.85           H  
ATOM   2371  HD3AARG A 352      -0.041  -8.475  -3.079  0.63 16.39           H  
ATOM   2372  HD3BARG A 352      -0.814  -8.714  -3.283  0.37 13.85           H  
ATOM   2373  HE AARG A 352      -1.896  -9.451  -4.768  0.63 16.55           H  
ATOM   2374  HE BARG A 352      -2.685  -7.453  -3.962  0.37 26.69           H  
ATOM   2375 HH11AARG A 352      -1.272  -6.864  -2.796  0.63 26.66           H  
ATOM   2376 HH11BARG A 352      -2.643 -10.649  -4.863  0.37 30.71           H  
ATOM   2377 HH12AARG A 352      -2.689  -6.428  -2.651  0.63 26.66           H  
ATOM   2378 HH12BARG A 352      -4.117 -10.775  -5.037  0.37 30.71           H  
ATOM   2379 HH21AARG A 352      -4.044  -8.771  -4.534  0.63 25.63           H  
ATOM   2380 HH21BARG A 352      -4.900  -7.680  -4.221  0.37 28.15           H  
ATOM   2381 HH22AARG A 352      -4.361  -7.578  -3.699  0.63 25.63           H  
ATOM   2382 HH22BARG A 352      -5.479  -8.984  -4.650  0.37 28.15           H  
ATOM   2383  N  ATHR A 353       0.566  -7.265  -9.751  0.63  7.10           N  
ATOM   2384  N  BTHR A 353       0.371  -7.001  -9.649  0.37  6.33           N  
ATOM   2385  CA ATHR A 353       0.722  -7.718 -11.123  0.63  7.29           C  
ATOM   2386  CA BTHR A 353       0.525  -7.314 -11.067  0.37  5.14           C  
ATOM   2387  C  ATHR A 353       1.897  -6.914 -11.677  0.63  6.57           C  
ATOM   2388  C  BTHR A 353       1.566  -6.360 -11.671  0.37  4.68           C  
ATOM   2389  O  ATHR A 353       2.871  -6.691 -10.932  0.63  7.10           O  
ATOM   2390  O  BTHR A 353       2.044  -5.443 -11.019  0.37  6.29           O  
ATOM   2391  CB ATHR A 353      -0.623  -7.500 -11.813  0.63  7.06           C  
ATOM   2392  CB BTHR A 353      -0.827  -7.175 -11.760  0.37  7.82           C  
ATOM   2393  OG1ATHR A 353      -1.017  -6.125 -11.678  0.63  8.35           O  
ATOM   2394  OG1BTHR A 353      -1.355  -5.884 -11.442  0.37  7.04           O  
ATOM   2395  CG2ATHR A 353      -1.672  -8.411 -11.177  0.63  7.51           C  
ATOM   2396  CG2BTHR A 353      -1.801  -8.262 -11.291  0.37  7.75           C  
ATOM   2397  H  ATHR A 353       0.152  -6.514  -9.695  0.63  8.53           H  
ATOM   2398  H  BTHR A 353      -0.188  -6.363  -9.505  0.37  7.60           H  
ATOM   2399  HA ATHR A 353       0.929  -8.655 -11.260  0.63  8.75           H  
ATOM   2400  HA BTHR A 353       0.838  -8.224 -11.185  0.37  6.17           H  
ATOM   2401  HB ATHR A 353      -0.559  -7.711 -12.757  0.63  8.48           H  
ATOM   2402  HB BTHR A 353      -0.726  -7.274 -12.720  0.37  9.39           H  
ATOM   2403  HG1ATHR A 353      -1.767  -6.004 -12.037  0.63 10.03           H  
ATOM   2404  HG1BTHR A 353      -2.107  -5.784 -11.802  0.37  8.45           H  
ATOM   2405 HG21ATHR A 353      -2.511  -8.336 -11.658  0.63  9.02           H  
ATOM   2406 HG21BTHR A 353      -2.667  -8.134 -11.708  0.37  9.31           H  
ATOM   2407 HG22ATHR A 353      -1.373  -9.333 -11.208  0.63  9.02           H  
ATOM   2408 HG22BTHR A 353      -1.461  -9.138 -11.532  0.37  9.31           H  
ATOM   2409 HG23ATHR A 353      -1.815  -8.157 -10.252  0.63  9.02           H  
ATOM   2410 HG23BTHR A 353      -1.906  -8.220 -10.327  0.37  9.31           H  
ATOM   2411  N   ASN A 354       1.826  -6.450 -12.939  1.00  6.04           N  
ANISOU 2411  N   ASN A 354      640    793    861    -21    -55      5       N  
ATOM   2412  CA  ASN A 354       2.919  -5.687 -13.532  1.00  6.16           C  
ANISOU 2412  CA  ASN A 354      644    783    915    -39    -57     89       C  
ATOM   2413  C   ASN A 354       2.337  -4.403 -14.103  1.00  5.56           C  
ANISOU 2413  C   ASN A 354      467    786    859    -38   -140     74       C  
ATOM   2414  O   ASN A 354       1.537  -4.436 -15.041  1.00  6.79           O  
ANISOU 2414  O   ASN A 354      702    784   1096     -5   -305     17       O  
ATOM   2415  CB  ASN A 354       3.651  -6.434 -14.628  1.00  7.31           C  
ANISOU 2415  CB  ASN A 354      764   1014   1000    170    105    187       C  
ATOM   2416  CG  ASN A 354       4.636  -7.480 -14.092  1.00  7.92           C  
ANISOU 2416  CG  ASN A 354      917   1014   1079     30      1    178       C  
ATOM   2417  OD1 ASN A 354       4.653  -7.854 -12.910  1.00 11.28           O  
ANISOU 2417  OD1 ASN A 354     1484   1418   1384    329    112    345       O  
ATOM   2418  ND2 ASN A 354       5.473  -7.912 -14.939  1.00  7.36           N  
ANISOU 2418  ND2 ASN A 354      812    942   1043    278    261    230       N  
ATOM   2419  H   ASN A 354       1.153  -6.568 -13.462  1.00  7.26           H  
ATOM   2420  HA  ASN A 354       3.565  -5.497 -12.834  1.00  7.41           H  
ATOM   2421  HB2 ASN A 354       3.002  -6.894 -15.183  1.00  8.78           H  
ATOM   2422  HB3 ASN A 354       4.153  -5.798 -15.161  1.00  8.78           H  
ATOM   2423 HD21 ASN A 354       5.459  -7.617 -15.747  1.00  8.84           H  
ATOM   2424 HD22 ASN A 354       6.056  -8.500 -14.707  1.00  8.84           H  
ATOM   2425  N   VAL A 355       2.766  -3.284 -13.546  1.00  5.69           N  
ANISOU 2425  N   VAL A 355      510    848    802    -95   -110     51       N  
ATOM   2426  CA  VAL A 355       2.311  -1.976 -13.990  1.00  5.57           C  
ANISOU 2426  CA  VAL A 355      362    852    903    -46    -42    -35       C  
ATOM   2427  C   VAL A 355       3.484  -1.191 -14.544  1.00  5.16           C  
ANISOU 2427  C   VAL A 355      302    750    907     10   -116    -80       C  
ATOM   2428  O   VAL A 355       4.546  -1.107 -13.921  1.00  5.94           O  
ANISOU 2428  O   VAL A 355      446    906    907    -36   -116    114       O  
ATOM   2429  CB  VAL A 355       1.549  -1.189 -12.906  1.00  7.69           C  
ANISOU 2429  CB  VAL A 355      623   1091   1207   -134    185   -205       C  
ATOM   2430  CG1 VAL A 355       2.369  -0.927 -11.698  1.00  9.46           C  
ANISOU 2430  CG1 VAL A 355      877   1507   1210   -163    167   -351       C  
ATOM   2431  CG2 VAL A 355       1.008   0.115 -13.478  1.00  8.48           C  
ANISOU 2431  CG2 VAL A 355      705    901   1614     63    232   -164       C  
ATOM   2432  H   VAL A 355       3.330  -3.255 -12.897  1.00  6.83           H  
ATOM   2433  HA  VAL A 355       1.689  -2.117 -14.721  1.00  6.69           H  
ATOM   2434  HB  VAL A 355       0.806  -1.742 -12.619  1.00  9.23           H  
ATOM   2435 HG11 VAL A 355       1.822  -0.473 -11.038  1.00 11.36           H  
ATOM   2436 HG12 VAL A 355       2.684  -1.772 -11.342  1.00 11.36           H  
ATOM   2437 HG13 VAL A 355       3.123  -0.369 -11.943  1.00 11.36           H  
ATOM   2438 HG21 VAL A 355       0.420   0.527 -12.824  1.00 10.18           H  
ATOM   2439 HG22 VAL A 355       1.751   0.707 -13.673  1.00 10.18           H  
ATOM   2440 HG23 VAL A 355       0.515  -0.077 -14.291  1.00 10.18           H  
ATOM   2441  N   TYR A 356       3.247  -0.610 -15.705  1.00  5.05           N  
ANISOU 2441  N   TYR A 356      333    726    861    -18    -91      0       N  
ATOM   2442  CA  TYR A 356       4.185   0.236 -16.435  1.00  5.13           C  
ANISOU 2442  CA  TYR A 356      321    767    860    -26    -62    -21       C  
ATOM   2443  C   TYR A 356       3.661   1.660 -16.345  1.00  4.93           C  
ANISOU 2443  C   TYR A 356      316    813    746    -42    -40    -11       C  
ATOM   2444  O   TYR A 356       2.633   1.983 -16.942  1.00  5.39           O  
ANISOU 2444  O   TYR A 356      404    815    827      2   -132    -70       O  
ATOM   2445  CB  TYR A 356       4.263  -0.249 -17.882  1.00  5.16           C  
ANISOU 2445  CB  TYR A 356      399    756    804    -11    -31    -20       C  
ATOM   2446  CG  TYR A 356       4.991  -1.582 -18.003  1.00  5.45           C  
ANISOU 2446  CG  TYR A 356      464    806    802     20      2    -27       C  
ATOM   2447  CD1 TYR A 356       4.329  -2.788 -17.846  1.00  5.91           C  
ANISOU 2447  CD1 TYR A 356      455    889    900    -37      0    -67       C  
ATOM   2448  CD2 TYR A 356       6.344  -1.612 -18.245  1.00  5.69           C  
ANISOU 2448  CD2 TYR A 356      432    866    864    -20    -10    -49       C  
ATOM   2449  CE1 TYR A 356       5.005  -3.990 -17.935  1.00  6.70           C  
ANISOU 2449  CE1 TYR A 356      703    801   1043    -59    -39    -87       C  
ATOM   2450  CE2 TYR A 356       7.033  -2.799 -18.343  1.00  6.08           C  
ANISOU 2450  CE2 TYR A 356      451    912    947     78    -32   -130       C  
ATOM   2451  CZ  TYR A 356       6.356  -3.994 -18.186  1.00  6.78           C  
ANISOU 2451  CZ  TYR A 356      713    870    993    154    -99   -129       C  
ATOM   2452  OH  TYR A 356       7.048  -5.184 -18.287  1.00  8.17           O  
ANISOU 2452  OH  TYR A 356      883    944   1277    238    -82   -196       O  
ATOM   2453  H   TYR A 356       2.499  -0.693 -16.122  1.00  6.07           H  
ATOM   2454  HA  TYR A 356       5.074   0.212 -16.047  1.00  6.16           H  
ATOM   2455  HB2 TYR A 356       3.365  -0.362 -18.229  1.00  6.20           H  
ATOM   2456  HB3 TYR A 356       4.743   0.407 -18.412  1.00  6.20           H  
ATOM   2457  HD1 TYR A 356       3.415  -2.789 -17.678  1.00  7.10           H  
ATOM   2458  HD2 TYR A 356       6.805  -0.811 -18.346  1.00  6.84           H  
ATOM   2459  HE1 TYR A 356       4.548  -4.792 -17.825  1.00  8.05           H  
ATOM   2460  HE2 TYR A 356       7.947  -2.798 -18.513  1.00  7.30           H  
ATOM   2461  HH  TYR A 356       7.868  -5.032 -18.392  1.00  9.81           H  
ATOM   2462  N   LEU A 357       4.342   2.476 -15.540  1.00  5.12           N  
ANISOU 2462  N   LEU A 357      310    827    809    -16   -107    -34       N  
ATOM   2463  CA  LEU A 357       3.939   3.849 -15.277  1.00  4.98           C  
ANISOU 2463  CA  LEU A 357      327    780    784     -4    -83      5       C  
ATOM   2464  C   LEU A 357       4.590   4.802 -16.265  1.00  4.93           C  
ANISOU 2464  C   LEU A 357      264    767    841    -30    -42    -14       C  
ATOM   2465  O   LEU A 357       5.797   4.744 -16.492  1.00  5.99           O  
ANISOU 2465  O   LEU A 357      380    877   1020      2    -26     86       O  
ATOM   2466  CB  LEU A 357       4.343   4.258 -13.864  1.00  5.31           C  
ANISOU 2466  CB  LEU A 357      398    822    797    -31   -108    -57       C  
ATOM   2467  CG  LEU A 357       3.675   3.489 -12.732  1.00  6.32           C  
ANISOU 2467  CG  LEU A 357      610    941    851    -36   -113    -55       C  
ATOM   2468  CD1 LEU A 357       4.358   3.811 -11.422  1.00  7.40           C  
ANISOU 2468  CD1 LEU A 357      792   1162    859     -2   -223     17       C  
ATOM   2469  CD2 LEU A 357       2.201   3.834 -12.641  1.00  6.92           C  
ANISOU 2469  CD2 LEU A 357      635   1160    836    -42    -79      5       C  
ATOM   2470  H   LEU A 357       5.059   2.248 -15.124  1.00  6.15           H  
ATOM   2471  HA  LEU A 357       2.976   3.915 -15.371  1.00  5.98           H  
ATOM   2472  HB2 LEU A 357       5.300   4.130 -13.774  1.00  6.38           H  
ATOM   2473  HB3 LEU A 357       4.122   5.195 -13.746  1.00  6.38           H  
ATOM   2474  HG  LEU A 357       3.752   2.538 -12.907  1.00  7.60           H  
ATOM   2475 HD11 LEU A 357       3.952   3.285 -10.716  1.00  8.89           H  
ATOM   2476 HD12 LEU A 357       5.301   3.594 -11.496  1.00  8.89           H  
ATOM   2477 HD13 LEU A 357       4.250   4.757 -11.234  1.00  8.89           H  
ATOM   2478 HD21 LEU A 357       1.813   3.366 -11.884  1.00  8.32           H  
ATOM   2479 HD22 LEU A 357       2.108   4.792 -12.520  1.00  8.32           H  
ATOM   2480 HD23 LEU A 357       1.761   3.559 -13.460  1.00  8.32           H  
ATOM   2481  N   ALA A 358       3.788   5.721 -16.786  1.00  5.41           N  
ANISOU 2481  N   ALA A 358      354    818    885    -16      2     57       N  
ATOM   2482  CA  ALA A 358       4.256   6.804 -17.636  1.00  5.68           C  
ANISOU 2482  CA  ALA A 358      399    841    917    -28     62     63       C  
ATOM   2483  C   ALA A 358       4.157   8.102 -16.850  1.00  5.36           C  
ANISOU 2483  C   ALA A 358      346    823    866     25     55    123       C  
ATOM   2484  O   ALA A 358       3.075   8.450 -16.364  1.00  6.44           O  
ANISOU 2484  O   ALA A 358      485    879   1084    -30     79    -23       O  
ATOM   2485  CB  ALA A 358       3.419   6.899 -18.900  1.00  6.44           C  
ANISOU 2485  CB  ALA A 358      690    895    864      1    -45     32       C  
ATOM   2486  H   ALA A 358       2.938   5.738 -16.657  1.00  6.50           H  
ATOM   2487  HA  ALA A 358       5.180   6.649 -17.884  1.00  6.82           H  
ATOM   2488  HB1 ALA A 358       3.746   7.635 -19.440  1.00  7.74           H  
ATOM   2489  HB2 ALA A 358       3.497   6.067 -19.393  1.00  7.74           H  
ATOM   2490  HB3 ALA A 358       2.493   7.054 -18.656  1.00  7.74           H  
ATOM   2491  N   VAL A 359       5.272   8.816 -16.747  1.00  5.17           N  
ANISOU 2491  N   VAL A 359      343    812    811      4     33     68       N  
ATOM   2492  CA  VAL A 359       5.351  10.104 -16.080  1.00  5.47           C  
ANISOU 2492  CA  VAL A 359      377    894    807     22    -36     25       C  
ATOM   2493  C   VAL A 359       5.763  11.122 -17.122  1.00  5.38           C  
ANISOU 2493  C   VAL A 359      416    881    746    -34    -51     57       C  
ATOM   2494  O   VAL A 359       6.797  10.956 -17.770  1.00  5.74           O  
ANISOU 2494  O   VAL A 359      483    840    858    -22     48     58       O  
ATOM   2495  CB  VAL A 359       6.334  10.074 -14.911  1.00  6.82           C  
ANISOU 2495  CB  VAL A 359      684   1037    872     -1   -191     65       C  
ATOM   2496  CG1 VAL A 359       6.488  11.456 -14.290  1.00  7.59           C  
ANISOU 2496  CG1 VAL A 359      797   1123    962   -126   -264    -31       C  
ATOM   2497  CG2 VAL A 359       5.863   9.046 -13.866  1.00  8.44           C  
ANISOU 2497  CG2 VAL A 359     1163   1133    912   -139   -241    176       C  
ATOM   2498  H   VAL A 359       6.027   8.561 -17.070  1.00  6.22           H  
ATOM   2499  HA  VAL A 359       4.481  10.355 -15.731  1.00  6.57           H  
ATOM   2500  HB  VAL A 359       7.208   9.807 -15.236  1.00  8.20           H  
ATOM   2501 HG11 VAL A 359       6.967  11.373 -13.450  1.00  9.11           H  
ATOM   2502 HG12 VAL A 359       6.986  12.023 -14.900  1.00  9.11           H  
ATOM   2503 HG13 VAL A 359       5.608  11.832 -14.132  1.00  9.11           H  
ATOM   2504 HG21 VAL A 359       6.463   9.073 -13.104  1.00 10.14           H  
ATOM   2505 HG22 VAL A 359       4.962   9.271 -13.585  1.00 10.14           H  
ATOM   2506 HG23 VAL A 359       5.874   8.162 -14.264  1.00 10.14           H  
ATOM   2507  N   PHE A 360       4.963  12.179 -17.283  1.00  5.99           N  
ANISOU 2507  N   PHE A 360      607    898    770    116    -18     82       N  
ATOM   2508  CA  PHE A 360       5.155  13.098 -18.398  1.00  5.97           C  
ANISOU 2508  CA  PHE A 360      659    795    815     76    -41     31       C  
ATOM   2509  C   PHE A 360       6.356  14.033 -18.227  1.00  6.08           C  
ANISOU 2509  C   PHE A 360      573    806    930    133    -20     65       C  
ATOM   2510  O   PHE A 360       7.183  14.159 -19.146  1.00  6.83           O  
ANISOU 2510  O   PHE A 360      786    818    992     84     68     52       O  
ATOM   2511  CB  PHE A 360       3.878  13.902 -18.602  1.00  6.20           C  
ANISOU 2511  CB  PHE A 360      618    837    903     17    -56     80       C  
ATOM   2512  CG  PHE A 360       3.842  14.643 -19.910  1.00  6.69           C  
ANISOU 2512  CG  PHE A 360      816    815    913    148   -173     11       C  
ATOM   2513  CD1 PHE A 360       4.420  15.887 -20.042  1.00  6.19           C  
ANISOU 2513  CD1 PHE A 360      669    799    884     73    -46    -22       C  
ATOM   2514  CD2 PHE A 360       3.232  14.079 -21.008  1.00  8.31           C  
ANISOU 2514  CD2 PHE A 360     1234    879   1044     38   -336      8       C  
ATOM   2515  CE1 PHE A 360       4.378  16.553 -21.251  1.00  7.17           C  
ANISOU 2515  CE1 PHE A 360      976    835    913     74     -5     47       C  
ATOM   2516  CE2 PHE A 360       3.183  14.730 -22.221  1.00  9.61           C  
ANISOU 2516  CE2 PHE A 360     1702    980    971    137   -320    -82       C  
ATOM   2517  CZ  PHE A 360       3.762  15.977 -22.340  1.00  8.69           C  
ANISOU 2517  CZ  PHE A 360     1433    969    901    237    -93     23       C  
ATOM   2518  H   PHE A 360       4.308  12.382 -16.764  1.00  7.20           H  
ATOM   2519  HA  PHE A 360       5.342  12.567 -19.188  1.00  7.17           H  
ATOM   2520  HB2 PHE A 360       3.120  13.296 -18.583  1.00  7.45           H  
ATOM   2521  HB3 PHE A 360       3.800  14.554 -17.888  1.00  7.45           H  
ATOM   2522  HD1 PHE A 360       4.840  16.281 -19.312  1.00  7.44           H  
ATOM   2523  HD2 PHE A 360       2.844  13.238 -20.929  1.00  9.98           H  
ATOM   2524  HE1 PHE A 360       4.767  17.393 -21.331  1.00  8.61           H  
ATOM   2525  HE2 PHE A 360       2.764  14.334 -22.950  1.00 11.55           H  
ATOM   2526  HZ  PHE A 360       3.736  16.427 -23.154  1.00 10.44           H  
ATOM   2527  N   ASP A 361       6.444  14.730 -17.100  1.00  6.51           N  
ANISOU 2527  N   ASP A 361      594    947    933     80    -89     15       N  
ATOM   2528  CA  ASP A 361       7.436  15.782 -16.947  1.00  6.95           C  
ANISOU 2528  CA  ASP A 361      624   1007   1011     68   -136    -47       C  
ATOM   2529  C   ASP A 361       8.795  15.169 -16.607  1.00  7.18           C  
ANISOU 2529  C   ASP A 361      604   1077   1048     76   -110    -63       C  
ATOM   2530  O   ASP A 361       8.907  14.351 -15.695  1.00  7.35           O  
ANISOU 2530  O   ASP A 361      628   1085   1078     82   -135    -10       O  
ATOM   2531  CB  ASP A 361       7.074  16.747 -15.809  1.00  7.61           C  
ANISOU 2531  CB  ASP A 361      641   1045   1204    105   -195   -166       C  
ATOM   2532  CG  ASP A 361       5.850  17.614 -16.078  1.00  8.54           C  
ANISOU 2532  CG  ASP A 361      794   1157   1296    231   -220   -253       C  
ATOM   2533  OD1 ASP A 361       5.109  17.345 -17.017  1.00  7.91           O  
ANISOU 2533  OD1 ASP A 361      841   1083   1083    265   -162    -63       O  
ATOM   2534  OD2 ASP A 361       5.606  18.518 -15.256  1.00 13.25           O  
ANISOU 2534  OD2 ASP A 361     1294   1856   1885    650   -623   -872       O  
ATOM   2535  H   ASP A 361       5.941  14.613 -16.412  1.00  7.82           H  
ATOM   2536  HA  ASP A 361       7.474  16.272 -17.783  1.00  8.35           H  
ATOM   2537  HB2 ASP A 361       6.894  16.228 -15.009  1.00  9.14           H  
ATOM   2538  HB3 ASP A 361       7.825  17.341 -15.656  1.00  9.14           H  
ATOM   2539  N   LYS A 362       9.833  15.632 -17.291  1.00  7.91           N  
ANISOU 2539  N   LYS A 362      599   1226   1179     42   -100    143       N  
ATOM   2540  CA  LYS A 362      11.183  15.159 -17.016  1.00  9.31           C  
ANISOU 2540  CA  LYS A 362      570   1420   1547     75   -127    236       C  
ATOM   2541  C   LYS A 362      11.581  15.352 -15.555  1.00  9.25           C  
ANISOU 2541  C   LYS A 362      630   1242   1644    -92   -424    252       C  
ATOM   2542  O   LYS A 362      12.159  14.443 -14.944  1.00  9.58           O  
ANISOU 2542  O   LYS A 362      750   1216   1676   -130   -372    240       O  
ATOM   2543  CB  LYS A 362      12.174  15.898 -17.912  1.00 12.99           C  
ANISOU 2543  CB  LYS A 362      692   2205   2037    164    138    429       C  
ATOM   2544  CG  LYS A 362      13.604  15.397 -17.756  1.00 16.85           C  
ANISOU 2544  CG  LYS A 362      869   3036   2497      6    214    519       C  
ATOM   2545  CD  LYS A 362      14.600  16.292 -18.474  1.00 21.74           C  
ANISOU 2545  CD  LYS A 362     1457   3844   2959     37    199    648       C  
ATOM   2546  CE  LYS A 362      16.026  15.736 -18.440  1.00 26.31           C  
ANISOU 2546  CE  LYS A 362     2321   4388   3287     50    249    750       C  
ATOM   2547  NZ  LYS A 362      16.341  14.939 -17.222  1.00 29.12           N  
ANISOU 2547  NZ  LYS A 362     2941   4665   3458    113    235    784       N  
ATOM   2548  H   LYS A 362       9.785  16.219 -17.918  1.00  9.50           H  
ATOM   2549  HA  LYS A 362      11.210  14.209 -17.209  1.00 11.18           H  
ATOM   2550  HB2 LYS A 362      11.913  15.776 -18.838  1.00 15.59           H  
ATOM   2551  HB3 LYS A 362      12.161  16.841 -17.685  1.00 15.59           H  
ATOM   2552  HG2 LYS A 362      13.836  15.380 -16.814  1.00 20.23           H  
ATOM   2553  HG3 LYS A 362      13.672  14.504 -18.130  1.00 20.23           H  
ATOM   2554  HD2 LYS A 362      14.334  16.379 -19.403  1.00 26.10           H  
ATOM   2555  HD3 LYS A 362      14.607  17.163 -18.049  1.00 26.10           H  
ATOM   2556  HE2 LYS A 362      16.154  15.159 -19.209  1.00 31.58           H  
ATOM   2557  HE3 LYS A 362      16.650  16.478 -18.474  1.00 31.58           H  
ATOM   2558  HZ1 LYS A 362      16.152  15.411 -16.492  1.00 34.95           H  
ATOM   2559  HZ2 LYS A 362      15.860  14.190 -17.215  1.00 34.95           H  
ATOM   2560  HZ3 LYS A 362      17.206  14.727 -17.212  1.00 34.95           H  
ATOM   2561  N   ASN A 363      11.330  16.535 -14.981  1.00 10.58           N  
ANISOU 2561  N   ASN A 363     1157   1073   1790   -124   -585    180       N  
ATOM   2562  CA  ASN A 363      11.799  16.772 -13.614  1.00 11.73           C  
ANISOU 2562  CA  ASN A 363     1507   1040   1910   -193   -775     69       C  
ATOM   2563  C   ASN A 363      11.112  15.854 -12.618  1.00 10.40           C  
ANISOU 2563  C   ASN A 363     1221   1123   1609     44   -641   -130       C  
ATOM   2564  O   ASN A 363      11.737  15.404 -11.658  1.00 11.43           O  
ANISOU 2564  O   ASN A 363     1254   1534   1555     32   -563   -101       O  
ATOM   2565  CB  ASN A 363      11.562  18.226 -13.193  1.00 16.32           C  
ANISOU 2565  CB  ASN A 363     2498   1373   2328   -596  -1113    299       C  
ATOM   2566  CG  ASN A 363      12.545  19.180 -13.802  1.00 20.47           C  
ANISOU 2566  CG  ASN A 363     2855   2066   2857   -653  -1364    369       C  
ATOM   2567  OD1 ASN A 363      12.357  19.667 -14.926  1.00 21.58           O  
ANISOU 2567  OD1 ASN A 363     3061   2088   3051   -351  -1312    524       O  
ATOM   2568  ND2 ASN A 363      13.582  19.497 -13.051  1.00 23.43           N  
ANISOU 2568  ND2 ASN A 363     3168   2615   3120   -796  -1286    217       N  
ATOM   2569  H   ASN A 363      10.907  17.188 -15.347  1.00 12.70           H  
ATOM   2570  HA  ASN A 363      12.754  16.599 -13.605  1.00 14.08           H  
ATOM   2571  HB2 ASN A 363      10.673  18.494 -13.473  1.00 19.59           H  
ATOM   2572  HB3 ASN A 363      11.640  18.291 -12.229  1.00 19.59           H  
ATOM   2573 HD21 ASN A 363      14.178  20.040 -13.349  1.00 28.13           H  
ATOM   2574 HD22 ASN A 363      13.662  19.160 -12.264  1.00 28.13           H  
ATOM   2575  N   LEU A 364       9.806  15.617 -12.793  1.00  9.88           N  
ANISOU 2575  N   LEU A 364     1293   1142   1320    218   -463    -45       N  
ATOM   2576  CA  LEU A 364       9.092  14.717 -11.895  1.00  9.09           C  
ANISOU 2576  CA  LEU A 364     1178   1192   1083     60   -147     54       C  
ATOM   2577  C   LEU A 364       9.600  13.304 -12.048  1.00  8.46           C  
ANISOU 2577  C   LEU A 364      909   1329    978     30    -53     80       C  
ATOM   2578  O   LEU A 364       9.815  12.607 -11.056  1.00  9.49           O  
ANISOU 2578  O   LEU A 364     1078   1571    955     16   -131     56       O  
ATOM   2579  CB  LEU A 364       7.587  14.780 -12.123  1.00  9.57           C  
ANISOU 2579  CB  LEU A 364     1193   1322   1122    162     15    -64       C  
ATOM   2580  CG  LEU A 364       6.802  13.843 -11.199  1.00 10.72           C  
ANISOU 2580  CG  LEU A 364     1248   1539   1287     61    202   -167       C  
ATOM   2581  CD1 LEU A 364       7.053  14.138  -9.724  1.00 12.14           C  
ANISOU 2581  CD1 LEU A 364     1504   1850   1258     71    176   -173       C  
ATOM   2582  CD2 LEU A 364       5.314  13.902 -11.484  1.00 11.94           C  
ANISOU 2582  CD2 LEU A 364     1496   1518   1522    119    320    -91       C  
ATOM   2583  H   LEU A 364       9.322  15.961 -13.415  1.00 11.87           H  
ATOM   2584  HA  LEU A 364       9.249  15.010 -10.984  1.00 10.92           H  
ATOM   2585  HB2 LEU A 364       7.282  15.686 -11.961  1.00 11.49           H  
ATOM   2586  HB3 LEU A 364       7.397  14.525 -13.040  1.00 11.49           H  
ATOM   2587  HG  LEU A 364       7.119  12.945 -11.380  1.00 12.88           H  
ATOM   2588 HD11 LEU A 364       6.460  13.589  -9.187  1.00 14.58           H  
ATOM   2589 HD12 LEU A 364       7.977  13.931  -9.513  1.00 14.58           H  
ATOM   2590 HD13 LEU A 364       6.878  15.077  -9.555  1.00 14.58           H  
ATOM   2591 HD21 LEU A 364       4.854  13.290 -10.888  1.00 14.34           H  
ATOM   2592 HD22 LEU A 364       4.999  14.807 -11.335  1.00 14.34           H  
ATOM   2593 HD23 LEU A 364       5.159  13.645 -12.406  1.00 14.34           H  
ATOM   2594  N   TYR A 365       9.772  12.846 -13.289  1.00  7.81           N  
ANISOU 2594  N   TYR A 365      839   1297    831    -64   -132     72       N  
ATOM   2595  CA  TYR A 365      10.317  11.523 -13.458  1.00  7.31           C  
ANISOU 2595  CA  TYR A 365      704   1212    862    -32   -160     60       C  
ATOM   2596  C   TYR A 365      11.647  11.401 -12.712  1.00  7.62           C  
ANISOU 2596  C   TYR A 365      732   1170    994    -56   -129     60       C  
ATOM   2597  O   TYR A 365      11.870  10.450 -11.953  1.00  8.73           O  
ANISOU 2597  O   TYR A 365      839   1418   1060   -171   -245    216       O  
ATOM   2598  CB  TYR A 365      10.486  11.225 -14.942  1.00  7.20           C  
ANISOU 2598  CB  TYR A 365      641   1197    898   -138   -166    108       C  
ATOM   2599  CG  TYR A 365      11.273   9.979 -15.163  1.00  7.95           C  
ANISOU 2599  CG  TYR A 365      709   1218   1094    -48   -193     34       C  
ATOM   2600  CD1 TYR A 365      10.675   8.733 -15.214  1.00  8.26           C  
ANISOU 2600  CD1 TYR A 365      746   1203   1189    -43   -319     99       C  
ATOM   2601  CD2 TYR A 365      12.637  10.033 -15.262  1.00  9.16           C  
ANISOU 2601  CD2 TYR A 365      714   1363   1401    -99    -66   -202       C  
ATOM   2602  CE1 TYR A 365      11.444   7.594 -15.377  1.00  9.94           C  
ANISOU 2602  CE1 TYR A 365     1133   1182   1463    120   -393    -20       C  
ATOM   2603  CE2 TYR A 365      13.387   8.923 -15.403  1.00 10.85           C  
ANISOU 2603  CE2 TYR A 365      798   1584   1740     50   -150   -384       C  
ATOM   2604  CZ  TYR A 365      12.806   7.711 -15.469  1.00 11.29           C  
ANISOU 2604  CZ  TYR A 365      945   1539   1806    380   -372   -349       C  
ATOM   2605  OH  TYR A 365      13.649   6.627 -15.621  1.00 14.08           O  
ANISOU 2605  OH  TYR A 365     1319   1753   2276    483   -526   -526       O  
ATOM   2606  H   TYR A 365       9.585  13.271 -14.013  1.00  9.38           H  
ATOM   2607  HA  TYR A 365       9.704  10.864 -13.095  1.00  8.78           H  
ATOM   2608  HB2 TYR A 365       9.612  11.110 -15.348  1.00  8.65           H  
ATOM   2609  HB3 TYR A 365      10.955  11.961 -15.366  1.00  8.65           H  
ATOM   2610  HD1 TYR A 365       9.751   8.660 -15.138  1.00  9.92           H  
ATOM   2611  HD2 TYR A 365      13.059  10.861 -15.230  1.00 11.00           H  
ATOM   2612  HE1 TYR A 365      11.039   6.758 -15.424  1.00 11.94           H  
ATOM   2613  HE2 TYR A 365      14.313   8.994 -15.455  1.00 13.03           H  
ATOM   2614  HH  TYR A 365      13.203   5.914 -15.624  1.00 16.90           H  
ATOM   2615  N   ASP A 366      12.558  12.352 -12.953  1.00  7.52           N  
ANISOU 2615  N   ASP A 366      703   1155   1001    -93   -130    -15       N  
ATOM   2616  CA  ASP A 366      13.882  12.259 -12.342  1.00  8.17           C  
ANISOU 2616  CA  ASP A 366      639   1219   1247    -44   -115    -88       C  
ATOM   2617  C   ASP A 366      13.779  12.244 -10.809  1.00  8.65           C  
ANISOU 2617  C   ASP A 366      768   1299   1219    -12   -301    -32       C  
ATOM   2618  O   ASP A 366      14.513  11.516 -10.145  1.00  9.74           O  
ANISOU 2618  O   ASP A 366      839   1468   1393     -5   -358    -29       O  
ATOM   2619  CB  ASP A 366      14.754  13.429 -12.803  1.00  9.73           C  
ANISOU 2619  CB  ASP A 366      807   1346   1542   -167    -92    -65       C  
ATOM   2620  CG  ASP A 366      15.187  13.340 -14.266  1.00 11.64           C  
ANISOU 2620  CG  ASP A 366     1073   1506   1845   -211    103     56       C  
ATOM   2621  OD1 ASP A 366      15.029  12.292 -14.924  1.00 12.30           O  
ANISOU 2621  OD1 ASP A 366     1402   1649   1624   -177    333    -30       O  
ATOM   2622  OD2 ASP A 366      15.700  14.366 -14.756  1.00 14.00           O  
ANISOU 2622  OD2 ASP A 366     1364   1743   2214   -375    257    300       O  
ATOM   2623  H   ASP A 366      12.436  13.042 -13.453  1.00  9.04           H  
ATOM   2624  HA  ASP A 366      14.305  11.435 -12.630  1.00  9.82           H  
ATOM   2625  HB2 ASP A 366      14.253  14.253 -12.693  1.00 11.68           H  
ATOM   2626  HB3 ASP A 366      15.556  13.453 -12.259  1.00 11.68           H  
ATOM   2627  N   LYS A 367      12.876  13.048 -10.239  1.00  9.17           N  
ANISOU 2627  N   LYS A 367      909   1483   1092     57   -261    -93       N  
ATOM   2628  CA  LYS A 367      12.652  13.108  -8.792  1.00 10.34           C  
ANISOU 2628  CA  LYS A 367     1163   1683   1084    -70   -452    -43       C  
ATOM   2629  C   LYS A 367      12.033  11.834  -8.235  1.00 11.69           C  
ANISOU 2629  C   LYS A 367     1493   1820   1127   -368   -550    178       C  
ATOM   2630  O   LYS A 367      12.409  11.394  -7.148  1.00 13.75           O  
ANISOU 2630  O   LYS A 367     1811   2195   1218   -509   -653    392       O  
ATOM   2631  CB  LYS A 367      11.766  14.312  -8.472  1.00 11.96           C  
ANISOU 2631  CB  LYS A 367     1535   1856   1155   -117   -199    -60       C  
ATOM   2632  CG  LYS A 367      11.428  14.516  -6.997  1.00 14.75           C  
ANISOU 2632  CG  LYS A 367     1874   2501   1228   -362    -95   -175       C  
ATOM   2633  CD  LYS A 367      12.653  14.795  -6.155  1.00 18.70           C  
ANISOU 2633  CD  LYS A 367     2743   3114   1246   -752     69   -358       C  
ATOM   2634  CE  LYS A 367      13.379  16.042  -6.610  1.00 21.89           C  
ANISOU 2634  CE  LYS A 367     3462   3472   1381  -1142    141   -599       C  
ATOM   2635  NZ  LYS A 367      14.434  16.430  -5.659  1.00 23.09           N  
ANISOU 2635  NZ  LYS A 367     3717   3604   1452  -1264    190   -652       N  
ATOM   2636  H   LYS A 367      12.366  13.583 -10.679  1.00 11.01           H  
ATOM   2637  HA  LYS A 367      13.512  13.214  -8.356  1.00 12.42           H  
ATOM   2638  HB2 LYS A 367      12.220  15.113  -8.776  1.00 14.37           H  
ATOM   2639  HB3 LYS A 367      10.926  14.207  -8.947  1.00 14.37           H  
ATOM   2640  HG2 LYS A 367      10.826  15.271  -6.911  1.00 17.71           H  
ATOM   2641  HG3 LYS A 367      11.005  13.713  -6.655  1.00 17.71           H  
ATOM   2642  HD2 LYS A 367      12.385  14.921  -5.232  1.00 22.44           H  
ATOM   2643  HD3 LYS A 367      13.266  14.046  -6.224  1.00 22.44           H  
ATOM   2644  HE2 LYS A 367      13.791  15.877  -7.473  1.00 26.27           H  
ATOM   2645  HE3 LYS A 367      12.746  16.774  -6.680  1.00 26.27           H  
ATOM   2646  HZ1 LYS A 367      14.866  17.147  -5.960  1.00 27.72           H  
ATOM   2647  HZ2 LYS A 367      14.075  16.620  -4.867  1.00 27.72           H  
ATOM   2648  HZ3 LYS A 367      15.015  15.763  -5.560  1.00 27.72           H  
ATOM   2649  N   LEU A 368      11.025  11.274  -8.911  1.00 10.68           N  
ANISOU 2649  N   LEU A 368     1448   1498   1112   -284   -564    256       N  
ATOM   2650  CA  LEU A 368      10.411  10.038  -8.442  1.00 11.31           C  
ANISOU 2650  CA  LEU A 368     1558   1546   1192   -359   -396    412       C  
ATOM   2651  C   LEU A 368      11.435   8.947  -8.372  1.00 11.90           C  
ANISOU 2651  C   LEU A 368     1330   1850   1343   -620   -586    564       C  
ATOM   2652  O   LEU A 368      11.486   8.184  -7.406  1.00 13.33           O  
ANISOU 2652  O   LEU A 368     1513   2079   1471   -645   -716    692       O  
ATOM   2653  CB  LEU A 368       9.314   9.601  -9.407  1.00 10.20           C  
ANISOU 2653  CB  LEU A 368     1164   1547   1166   -310   -414    361       C  
ATOM   2654  CG  LEU A 368       8.067  10.437  -9.265  1.00 10.66           C  
ANISOU 2654  CG  LEU A 368     1036   1816   1199   -351   -125    188       C  
ATOM   2655  CD1 LEU A 368       7.137  10.086 -10.401  1.00 10.85           C  
ANISOU 2655  CD1 LEU A 368      980   1804   1339   -362   -212    113       C  
ATOM   2656  CD2 LEU A 368       7.412  10.220  -7.911  1.00 12.01           C  
ANISOU 2656  CD2 LEU A 368     1403   1929   1232   -263    159    151       C  
ATOM   2657  H   LEU A 368      10.684  11.590  -9.634  1.00 12.83           H  
ATOM   2658  HA  LEU A 368      10.025  10.196  -7.567  1.00 13.58           H  
ATOM   2659  HB2 LEU A 368       9.637   9.690 -10.317  1.00 12.25           H  
ATOM   2660  HB3 LEU A 368       9.082   8.676  -9.226  1.00 12.25           H  
ATOM   2661  HG  LEU A 368       8.281  11.383  -9.308  1.00 12.80           H  
ATOM   2662 HD11 LEU A 368       6.308  10.577 -10.294  1.00 13.03           H  
ATOM   2663 HD12 LEU A 368       7.559  10.328 -11.241  1.00 13.03           H  
ATOM   2664 HD13 LEU A 368       6.962   9.132 -10.382  1.00 13.03           H  
ATOM   2665 HD21 LEU A 368       6.480  10.482  -7.966  1.00 14.42           H  
ATOM   2666 HD22 LEU A 368       7.479   9.282  -7.675  1.00 14.42           H  
ATOM   2667 HD23 LEU A 368       7.870  10.761  -7.249  1.00 14.42           H  
ATOM   2668  N  AVAL A 369      12.273   8.842  -9.379  0.56  9.99           N  
ANISOU 2668  N  AVAL A 369     1151   1720    924   -581   -435    273       N  
ATOM   2669  N  BVAL A 369      12.249   8.842  -9.424  0.44 13.71           N  
ANISOU 2669  N  BVAL A 369     1472   1966   1772   -769   -736    548       N  
ATOM   2670  CA AVAL A 369      13.276   7.814  -9.291  0.56  8.67           C  
ANISOU 2670  CA AVAL A 369      987   1459    846   -144   -473    258       C  
ATOM   2671  CA BVAL A 369      13.250   7.797  -9.495  0.44 15.22           C  
ANISOU 2671  CA BVAL A 369     1724   1864   2194   -636  -1039    663       C  
ATOM   2672  C  AVAL A 369      14.181   8.103  -8.104  0.56  8.27           C  
ANISOU 2672  C  AVAL A 369      958   1541    642   -428   -200    -92       C  
ATOM   2673  C  BVAL A 369      14.320   8.037  -8.447  0.44 15.66           C  
ANISOU 2673  C  BVAL A 369     2017   1728   2203   -593  -1165    736       C  
ATOM   2674  O  AVAL A 369      14.364   7.249  -7.241  0.56  9.33           O  
ANISOU 2674  O  AVAL A 369     1271   1708    565   -444    -48   -215       O  
ATOM   2675  O  BVAL A 369      14.783   7.091  -7.797  0.44 14.73           O  
ANISOU 2675  O  BVAL A 369     1939   1531   2128   -522  -1113    715       O  
ATOM   2676  CB AVAL A 369      14.010   7.679 -10.625  0.56  8.60           C  
ANISOU 2676  CB AVAL A 369      989   1225   1053   -255   -572    100       C  
ATOM   2677  CB BVAL A 369      13.837   7.716 -10.914  0.44 15.65           C  
ANISOU 2677  CB BVAL A 369     1644   1921   2381   -502  -1060    661       C  
ATOM   2678  CG1AVAL A 369      15.174   6.747 -10.516  0.56  8.67           C  
ANISOU 2678  CG1AVAL A 369      999   1170   1124    -40   -445     -6       C  
ATOM   2679  CG1BVAL A 369      15.068   6.825 -10.896  0.44 17.11           C  
ANISOU 2679  CG1BVAL A 369     1788   2169   2545   -348  -1150    702       C  
ATOM   2680  CG2AVAL A 369      13.020   7.205 -11.736  0.56  8.27           C  
ANISOU 2680  CG2AVAL A 369      752   1169   1221    -41   -529     37       C  
ATOM   2681  CG2BVAL A 369      12.798   7.220 -11.921  0.44 15.62           C  
ANISOU 2681  CG2BVAL A 369     1635   1891   2407   -443  -1076    606       C  
ATOM   2682  H  AVAL A 369      12.281   9.329 -10.087  0.56 12.00           H  
ATOM   2683  H  BVAL A 369      12.238   9.365 -10.106  0.44 16.46           H  
ATOM   2684  HA AVAL A 369      12.867   6.950  -9.127  0.56 10.41           H  
ATOM   2685  HA BVAL A 369      12.831   6.943  -9.306  0.44 18.27           H  
ATOM   2686  HB AVAL A 369      14.362   8.548 -10.873  0.56 10.33           H  
ATOM   2687  HB BVAL A 369      14.100   8.603 -11.206  0.44 18.79           H  
ATOM   2688 HG11AVAL A 369      15.507   6.552 -11.406  0.56 10.41           H  
ATOM   2689 HG11BVAL A 369      15.273   6.551 -11.803  0.44 20.55           H  
ATOM   2690 HG12AVAL A 369      15.870   7.171  -9.989  0.56 10.41           H  
ATOM   2691 HG12BVAL A 369      15.813   7.323 -10.525  0.44 20.55           H  
ATOM   2692 HG13AVAL A 369      14.885   5.928 -10.084  0.56 10.41           H  
ATOM   2693 HG13BVAL A 369      14.886   6.046 -10.348  0.44 20.55           H  
ATOM   2694 HG21AVAL A 369      13.493   7.156 -12.581  0.56  9.93           H  
ATOM   2695 HG21BVAL A 369      13.215   7.143 -12.793  0.44 18.75           H  
ATOM   2696 HG22AVAL A 369      12.675   6.329 -11.499  0.56  9.93           H  
ATOM   2697 HG22BVAL A 369      12.469   6.354 -11.634  0.44 18.75           H  
ATOM   2698 HG23AVAL A 369      12.290   7.841 -11.801  0.56  9.93           H  
ATOM   2699 HG23BVAL A 369      12.066   7.856 -11.958  0.44 18.75           H  
ATOM   2700  N  ASER A 370      14.733   9.322  -8.029  0.56  8.05           N  
ANISOU 2700  N  ASER A 370      874   1455    729   -396   -178   -138       N  
ATOM   2701  N  BSER A 370      14.723   9.303  -8.260  0.44 15.57           N  
ANISOU 2701  N  BSER A 370     1936   1759   2220   -710  -1128    709       N  
ATOM   2702  CA ASER A 370      15.712   9.596  -6.989  0.56  8.14           C  
ANISOU 2702  CA ASER A 370      673   1631    787   -257   -191   -227       C  
ATOM   2703  CA BSER A 370      15.683   9.638  -7.212  0.44 16.17           C  
ANISOU 2703  CA BSER A 370     1988   1905   2252   -611  -1174    686       C  
ATOM   2704  C  ASER A 370      15.087   9.483  -5.606  0.56  7.34           C  
ANISOU 2704  C  ASER A 370      659   1356    774    -70    -49   -205       C  
ATOM   2705  C  BSER A 370      15.102   9.377  -5.821  0.44 15.53           C  
ANISOU 2705  C  BSER A 370     1812   1974   2115   -506  -1098    418       C  
ATOM   2706  O  ASER A 370      15.722   8.949  -4.690  0.56  8.54           O  
ANISOU 2706  O  ASER A 370      841   1536    867    157   -338   -257       O  
ATOM   2707  O  BSER A 370      15.705   8.668  -5.008  0.44 15.04           O  
ANISOU 2707  O  BSER A 370     1576   2022   2116   -275  -1022    446       O  
ATOM   2708  CB ASER A 370      16.369  10.958  -7.233  0.56  9.59           C  
ANISOU 2708  CB ASER A 370      794   1703   1147   -366   -217   -374       C  
ATOM   2709  CB BSER A 370      16.151  11.097  -7.363  0.44 17.09           C  
ANISOU 2709  CB BSER A 370     2161   2000   2331   -828  -1208    738       C  
ATOM   2710  OG ASER A 370      15.447  12.005  -7.115  0.56 12.71           O  
ANISOU 2710  OG ASER A 370     1757   1707   1366   -505   -337     52       O  
ATOM   2711  OG BSER A 370      17.155  11.424  -6.412  0.44 17.31           O  
ANISOU 2711  OG BSER A 370     1993   2065   2520   -663  -1223    697       O  
ATOM   2712  H  ASER A 370      14.559   9.981  -8.553  0.56  9.67           H  
ATOM   2713  H  BSER A 370      14.456   9.976  -8.724  0.44 18.69           H  
ATOM   2714  HA ASER A 370      16.423   8.937  -7.026  0.56  9.77           H  
ATOM   2715  HA BSER A 370      16.464   9.071  -7.314  0.44 19.42           H  
ATOM   2716  HB2ASER A 370      17.073  11.086  -6.580  0.56 11.52           H  
ATOM   2717  HB2BSER A 370      16.513  11.219  -8.254  0.44 20.51           H  
ATOM   2718  HB3ASER A 370      16.741  10.968  -8.129  0.56 11.52           H  
ATOM   2719  HB3BSER A 370      15.391  11.684  -7.230  0.44 20.51           H  
ATOM   2720  HG ASER A 370      15.151  12.040  -6.330  0.56 15.26           H  
ATOM   2721  HG BSER A 370      17.422  12.211  -6.536  0.44 20.79           H  
ATOM   2722  N  ASER A 371      13.867  10.011  -5.413  0.56  7.69           N  
ANISOU 2722  N  ASER A 371      849   1445    629    123   -156   -190       N  
ATOM   2723  N  BSER A 371      13.945   9.970  -5.509  0.44 14.87           N  
ANISOU 2723  N  BSER A 371     1828   1846   1977   -456  -1077    224       N  
ATOM   2724  CA ASER A 371      13.201   9.915  -4.120  0.56  7.98           C  
ANISOU 2724  CA ASER A 371      758   1706    566    239   -170   -155       C  
ATOM   2725  CA BSER A 371      13.395   9.852  -4.160  0.44 14.78           C  
ANISOU 2725  CA BSER A 371     1929   1907   1781   -498  -1024    104       C  
ATOM   2726  C  ASER A 371      12.796   8.484  -3.788  0.56  8.47           C  
ANISOU 2726  C  ASER A 371      832   1791    594    -54   -228    -79       C  
ATOM   2727  C  BSER A 371      13.060   8.404  -3.810  0.44 14.83           C  
ANISOU 2727  C  BSER A 371     2060   1923   1652   -691   -935    139       C  
ATOM   2728  O  ASER A 371      12.914   8.040  -2.636  0.56  9.48           O  
ANISOU 2728  O  ASER A 371     1192   1774    636     86   -370    -71       O  
ATOM   2729  O  BSER A 371      13.333   7.945  -2.691  0.44 15.11           O  
ANISOU 2729  O  BSER A 371     2249   1984   1510   -620   -956    138       O  
ATOM   2730  CB ASER A 371      11.965  10.816  -4.097  0.56  9.14           C  
ANISOU 2730  CB ASER A 371      926   1888    659    235   -184      4       C  
ATOM   2731  CB BSER A 371      12.159  10.732  -4.014  0.44 14.56           C  
ANISOU 2731  CB BSER A 371     1809   2020   1704   -220  -1033     21       C  
ATOM   2732  OG ASER A 371      12.372  12.154  -4.283  0.56 11.48           O  
ANISOU 2732  OG ASER A 371     1282   2143    935    596    -30    148       O  
ATOM   2733  OG BSER A 371      11.102  10.178  -4.755  0.44 13.47           O  
ANISOU 2733  OG BSER A 371     1871   1727   1518      6   -951    135       O  
ATOM   2734  H  ASER A 371      13.413  10.424  -6.015  0.56  9.24           H  
ATOM   2735  H  BSER A 371      13.469  10.437  -6.052  0.44 17.85           H  
ATOM   2736  HA ASER A 371      13.824  10.217  -3.441  0.56  9.58           H  
ATOM   2737  HA BSER A 371      14.065  10.164  -3.531  0.44 17.75           H  
ATOM   2738  HB2ASER A 371      11.364  10.558  -4.813  0.56 10.98           H  
ATOM   2739  HB2BSER A 371      11.906  10.778  -3.078  0.44 17.48           H  
ATOM   2740  HB3ASER A 371      11.518  10.730  -3.241  0.56 10.98           H  
ATOM   2741  HB3BSER A 371      12.355  11.621  -4.348  0.44 17.48           H  
ATOM   2742  HG ASER A 371      11.705  12.664  -4.251  0.56 13.78           H  
ATOM   2743  HG BSER A 371      11.265  10.239  -5.577  0.44 16.17           H  
ATOM   2744  N  APHE A 372      12.284   7.756  -4.775  0.56  9.09           N  
ANISOU 2744  N  APHE A 372      812   2052    592    -98   -150     55       N  
ATOM   2745  N  BPHE A 372      12.458   7.670  -4.750  0.44 14.66           N  
ANISOU 2745  N  BPHE A 372     2116   1813   1643   -847   -875    246       N  
ATOM   2746  CA APHE A 372      11.940   6.364  -4.533  0.56  9.82           C  
ANISOU 2746  CA APHE A 372     1025   2072    633   -441   -166     36       C  
ATOM   2747  CA BPHE A 372      12.103   6.278  -4.486  0.44 14.93           C  
ANISOU 2747  CA BPHE A 372     2005   1932   1737   -722   -947    200       C  
ATOM   2748  C  APHE A 372      13.169   5.586  -4.072  0.56  9.11           C  
ANISOU 2748  C  APHE A 372     1242   1573    647   -493   -230   -121       C  
ATOM   2749  C  BPHE A 372      13.327   5.491  -4.044  0.44 16.21           C  
ANISOU 2749  C  BPHE A 372     1991   2272   1894   -356   -775    224       C  
ATOM   2750  O  APHE A 372      13.088   4.755  -3.158  0.56 10.00           O  
ANISOU 2750  O  APHE A 372     1479   1626    694   -495   -324    -71       O  
ATOM   2751  O  BPHE A 372      13.271   4.696  -3.096  0.44 15.15           O  
ANISOU 2751  O  BPHE A 372     1662   2260   1833   -197   -684    260       O  
ATOM   2752  CB APHE A 372      11.329   5.704  -5.769  0.56 11.23           C  
ANISOU 2752  CB APHE A 372     1274   2246    749   -585   -251    108       C  
ATOM   2753  CB BPHE A 372      11.479   5.624  -5.728  0.44 14.31           C  
ANISOU 2753  CB BPHE A 372     1990   1794   1653   -805   -759      4       C  
ATOM   2754  CG APHE A 372      10.944   4.282  -5.522  0.56 12.82           C  
ANISOU 2754  CG APHE A 372     1440   2360   1070   -592   -502    127       C  
ATOM   2755  CG BPHE A 372      11.046   4.206  -5.491  0.44 16.22           C  
ANISOU 2755  CG BPHE A 372     2414   2047   1700   -956   -823     22       C  
ATOM   2756  CD1APHE A 372       9.794   3.993  -4.830  0.56 14.16           C  
ANISOU 2756  CD1APHE A 372     1621   2463   1295   -710   -596     51       C  
ATOM   2757  CD1BPHE A 372       9.864   3.945  -4.833  0.44 17.39           C  
ANISOU 2757  CD1BPHE A 372     2518   2364   1726  -1091   -799     34       C  
ATOM   2758  CD2APHE A 372      11.764   3.237  -5.918  0.56 14.20           C  
ANISOU 2758  CD2APHE A 372     1477   2619   1300   -600   -551    -54       C  
ATOM   2759  CD2BPHE A 372      11.843   3.140  -5.876  0.44 17.49           C  
ANISOU 2759  CD2BPHE A 372     2722   2200   1724   -832  -1013     53       C  
ATOM   2760  CE1APHE A 372       9.454   2.694  -4.560  0.56 15.13           C  
ANISOU 2760  CE1APHE A 372     1814   2491   1444   -945   -560     11       C  
ATOM   2761  CE1BPHE A 372       9.475   2.650  -4.581  0.44 17.87           C  
ANISOU 2761  CE1BPHE A 372     2552   2441   1795  -1088   -803    -52       C  
ATOM   2762  CE2APHE A 372      11.407   1.912  -5.642  0.56 14.69           C  
ANISOU 2762  CE2APHE A 372     1525   2605   1452   -577   -642   -110       C  
ATOM   2763  CE2BPHE A 372      11.451   1.830  -5.619  0.44 18.51           C  
ANISOU 2763  CE2BPHE A 372     2947   2291   1796   -767   -979    141       C  
ATOM   2764  CZ APHE A 372      10.260   1.658  -4.970  0.56 14.61           C  
ANISOU 2764  CZ APHE A 372     1785   2398   1367   -692   -661      7       C  
ATOM   2765  CZ BPHE A 372      10.269   1.596  -4.978  0.44 18.91           C  
ANISOU 2765  CZ BPHE A 372     2906   2455   1823   -885   -850    120       C  
ATOM   2766  H  APHE A 372      12.129   8.037  -5.573  0.56 10.92           H  
ATOM   2767  H  BPHE A 372      12.248   7.951  -5.536  0.44 17.60           H  
ATOM   2768  HA APHE A 372      11.262   6.339  -3.840  0.56 11.79           H  
ATOM   2769  HA BPHE A 372      11.438   6.259  -3.780  0.44 17.93           H  
ATOM   2770  HB2APHE A 372      10.532   6.193  -6.028  0.56 13.49           H  
ATOM   2771  HB2BPHE A 372      10.698   6.135  -5.993  0.44 17.18           H  
ATOM   2772  HB3APHE A 372      11.977   5.721  -6.491  0.56 13.49           H  
ATOM   2773  HB3BPHE A 372      12.133   5.622  -6.444  0.44 17.18           H  
ATOM   2774  HD1APHE A 372       9.242   4.684  -4.543  0.56 17.00           H  
ATOM   2775  HD1BPHE A 372       9.325   4.650  -4.557  0.44 20.88           H  
ATOM   2776  HD2APHE A 372      12.557   3.418  -6.369  0.56 17.05           H  
ATOM   2777  HD2BPHE A 372      12.649   3.302  -6.310  0.44 21.00           H  
ATOM   2778  HE1APHE A 372       8.670   2.510  -4.094  0.56 18.16           H  
ATOM   2779  HE1BPHE A 372       8.672   2.485  -4.141  0.44 21.45           H  
ATOM   2780  HE2APHE A 372      11.954   1.212  -5.918  0.56 17.64           H  
ATOM   2781  HE2BPHE A 372      11.990   1.120  -5.883  0.44 22.23           H  
ATOM   2782  HZ APHE A 372      10.016   0.780  -4.785  0.56 17.54           H  
ATOM   2783  HZ BPHE A 372       9.999   0.722  -4.808  0.44 22.70           H  
ATOM   2784  N  ALEU A 373      14.325   5.848  -4.701  0.56  8.21           N  
ANISOU 2784  N  ALEU A 373     1036   1373    710   -291   -190   -230       N  
ATOM   2785  N  BLEU A 373      14.452   5.713  -4.720  0.44 18.57           N  
ANISOU 2785  N  BLEU A 373     2256   2582   2218   -152   -390     57       N  
ATOM   2786  CA ALEU A 373      15.544   5.119  -4.371  0.56  8.99           C  
ANISOU 2786  CA ALEU A 373     1208   1209    999   -204    -32   -141       C  
ATOM   2787  CA BLEU A 373      15.689   5.050  -4.340  0.44 21.85           C  
ANISOU 2787  CA BLEU A 373     2782   2991   2527    114   -153    -23       C  
ATOM   2788  C  ALEU A 373      16.065   5.447  -2.970  0.56  8.71           C  
ANISOU 2788  C  ALEU A 373     1022   1165   1123    -33   -151     13       C  
ATOM   2789  C  BLEU A 373      16.120   5.411  -2.922  0.44 21.79           C  
ANISOU 2789  C  BLEU A 373     2722   3015   2542    435    -95     61       C  
ATOM   2790  O  ALEU A 373      16.877   4.696  -2.434  0.56 11.51           O  
ANISOU 2790  O  ALEU A 373     1356   1455   1562    265   -191    249       O  
ATOM   2791  O  BLEU A 373      16.910   4.677  -2.323  0.44 22.09           O  
ANISOU 2791  O  BLEU A 373     2823   3031   2540    621    156     46       O  
ATOM   2792  CB ALEU A 373      16.618   5.352  -5.430  0.56 10.08           C  
ANISOU 2792  CB ALEU A 373     1258   1449   1121    -73     92   -138       C  
ATOM   2793  CB BLEU A 373      16.780   5.392  -5.354  0.44 24.54           C  
ANISOU 2793  CB BLEU A 373     3321   3245   2758      0    -18   -120       C  
ATOM   2794  CG ALEU A 373      16.310   4.709  -6.781  0.56 13.40           C  
ANISOU 2794  CG ALEU A 373     1774   1893   1425   -128    609   -327       C  
ATOM   2795  CG BLEU A 373      17.072   4.388  -6.478  0.44 26.65           C  
ANISOU 2795  CG BLEU A 373     3839   3332   2954   -150     42   -198       C  
ATOM   2796  CD1ALEU A 373      17.302   5.162  -7.830  0.56 15.53           C  
ANISOU 2796  CD1ALEU A 373     1974   2414   1514   -116    504   -499       C  
ATOM   2797  CD1BLEU A 373      15.962   3.359  -6.691  0.44 27.24           C  
ANISOU 2797  CD1BLEU A 373     3988   3344   3016   -148     37   -236       C  
ATOM   2798  CD2ALEU A 373      16.299   3.179  -6.685  0.56 15.67           C  
ANISOU 2798  CD2ALEU A 373     2422   1897   1635   -155    370   -362       C  
ATOM   2799  CD2BLEU A 373      17.340   5.126  -7.783  0.44 27.40           C  
ANISOU 2799  CD2BLEU A 373     4040   3359   3013   -239     78   -225       C  
ATOM   2800  H  ALEU A 373      14.423   6.439  -5.318  0.56  9.86           H  
ATOM   2801  H  BLEU A 373      14.523   6.238  -5.397  0.44 22.29           H  
ATOM   2802  HA ALEU A 373      15.348   4.169  -4.382  0.56 10.80           H  
ATOM   2803  HA BLEU A 373      15.564   4.089  -4.359  0.44 26.22           H  
ATOM   2804  HB2ALEU A 373      16.711   6.307  -5.572  0.56 12.10           H  
ATOM   2805  HB2BLEU A 373      16.530   6.224  -5.785  0.44 29.46           H  
ATOM   2806  HB3ALEU A 373      17.456   4.982  -5.110  0.56 12.10           H  
ATOM   2807  HB3BLEU A 373      17.610   5.508  -4.865  0.44 29.46           H  
ATOM   2808  HG ALEU A 373      15.424   4.993  -7.055  0.56 16.09           H  
ATOM   2809  HG BLEU A 373      17.858   3.887  -6.206  0.44 31.99           H  
ATOM   2810 HD11ALEU A 373      17.079   4.746  -8.677  0.56 18.65           H  
ATOM   2811 HD11BLEU A 373      16.109   2.906  -7.536  0.44 32.69           H  
ATOM   2812 HD12ALEU A 373      17.255   6.127  -7.913  0.56 18.65           H  
ATOM   2813 HD12BLEU A 373      15.983   2.717  -5.964  0.44 32.69           H  
ATOM   2814 HD13ALEU A 373      18.194   4.897  -7.556  0.56 18.65           H  
ATOM   2815 HD13BLEU A 373      15.107   3.816  -6.704  0.44 32.69           H  
ATOM   2816 HD21ALEU A 373      16.304   2.806  -7.580  0.56 18.81           H  
ATOM   2817 HD21BLEU A 373      18.031   5.791  -7.634  0.44 32.89           H  
ATOM   2818 HD22ALEU A 373      17.087   2.887  -6.200  0.56 18.81           H  
ATOM   2819 HD22BLEU A 373      17.634   4.489  -8.452  0.44 32.89           H  
ATOM   2820 HD23ALEU A 373      15.499   2.898  -6.214  0.56 18.81           H  
ATOM   2821 HD23BLEU A 373      16.523   5.560  -8.074  0.44 32.89           H  
ATOM   2822  N  AGLU A 374      15.605   6.532  -2.350  0.56  7.17           N  
ANISOU 2822  N  AGLU A 374      977    941    805     -3   -345    -84       N  
ATOM   2823  N  BGLU A 374      15.612   6.511  -2.363  0.44 21.97           N  
ANISOU 2823  N  BGLU A 374     2740   3037   2569    444   -316    105       N  
ATOM   2824  CA AGLU A 374      15.950   6.814  -0.956  0.56  7.69           C  
ANISOU 2824  CA AGLU A 374     1029   1128    764    -58   -305    -74       C  
ATOM   2825  CA BGLU A 374      15.901   6.830  -0.971  0.44 23.14           C  
ANISOU 2825  CA BGLU A 374     3050   3098   2644    338   -531    141       C  
ATOM   2826  C  AGLU A 374      15.089   6.033   0.031  0.56  7.90           C  
ANISOU 2826  C  AGLU A 374     1085   1120    797     54   -307    -31       C  
ATOM   2827  C  BGLU A 374      15.114   5.955  -0.008  0.44 22.34           C  
ANISOU 2827  C  BGLU A 374     2965   2907   2617    400   -681    142       C  
ATOM   2828  O  AGLU A 374      15.333   6.043   1.244  0.56 10.15           O  
ANISOU 2828  O  AGLU A 374     2125   1000    732   -551   -415    127       O  
ATOM   2829  O  BGLU A 374      15.506   5.822   1.156  0.44 22.35           O  
ANISOU 2829  O  BGLU A 374     3047   2929   2514    450  -1052    310       O  
ATOM   2830  CB AGLU A 374      15.755   8.303  -0.658  0.56  9.99           C  
ANISOU 2830  CB AGLU A 374     1635   1166    995   -265   -306    -89       C  
ATOM   2831  CB BGLU A 374      15.528   8.278  -0.644  0.44 25.39           C  
ANISOU 2831  CB BGLU A 374     3582   3314   2751    151   -553    231       C  
ATOM   2832  CG AGLU A 374      16.654   9.242  -1.437  0.56 11.90           C  
ANISOU 2832  CG AGLU A 374     1884   1524   1112   -651   -658    303       C  
ATOM   2833  CG BGLU A 374      15.847   9.302  -1.707  0.44 27.82           C  
ANISOU 2833  CG BGLU A 374     4170   3515   2886    -14   -473    294       C  
ATOM   2834  CD AGLU A 374      18.101   9.190  -1.032  0.56 14.28           C  
ANISOU 2834  CD AGLU A 374     2039   1974   1411   -982   -774    685       C  
ATOM   2835  CD BGLU A 374      17.312   9.674  -1.754  0.44 29.61           C  
ANISOU 2835  CD BGLU A 374     4658   3675   2916   -139   -390    413       C  
ATOM   2836  OE1AGLU A 374      18.413   8.666   0.058  0.56 13.88           O  
ANISOU 2836  OE1AGLU A 374     1894   1965   1417   -789   -779    695       O  
ATOM   2837  OE1BGLU A 374      18.085   9.170  -0.912  0.44 29.57           O  
ANISOU 2837  OE1BGLU A 374     4721   3705   2808   -339   -515    445       O  
ATOM   2838  OE2AGLU A 374      18.933   9.687  -1.820  0.56 18.65           O  
ANISOU 2838  OE2AGLU A 374     2351   2859   1876  -1002   -608    768       O  
ATOM   2839  OE2BGLU A 374      17.688  10.478  -2.634  0.44 30.66           O  
ANISOU 2839  OE2BGLU A 374     4906   3767   2976     -9   -225    474       O  
ATOM   2840  H  AGLU A 374      15.092   7.120  -2.713  0.56  8.61           H  
ATOM   2841  H  BGLU A 374      15.105   7.078  -2.764  0.44 26.37           H  
ATOM   2842  HA AGLU A 374      16.883   6.582  -0.824  0.56  9.24           H  
ATOM   2843  HA BGLU A 374      16.855   6.710  -0.843  0.44 27.78           H  
ATOM   2844  HB2AGLU A 374      14.838   8.539  -0.867  0.56 12.00           H  
ATOM   2845  HB2BGLU A 374      14.572   8.316  -0.488  0.44 30.48           H  
ATOM   2846  HB3AGLU A 374      15.929   8.451   0.285  0.56 12.00           H  
ATOM   2847  HB3BGLU A 374      16.006   8.540   0.158  0.44 30.48           H  
ATOM   2848  HG2AGLU A 374      16.603   9.011  -2.377  0.56 14.29           H  
ATOM   2849  HG2BGLU A 374      15.603   8.942  -2.574  0.44 33.40           H  
ATOM   2850  HG3AGLU A 374      16.344  10.151  -1.301  0.56 14.29           H  
ATOM   2851  HG3BGLU A 374      15.340  10.109  -1.528  0.44 33.40           H  
ATOM   2852  N  AMET A 375      14.023   5.440  -0.409  0.56  7.03           N  
ANISOU 2852  N  AMET A 375      944   1123    602    -79   -248     -5       N  
ATOM   2853  N  BMET A 375      14.008   5.377  -0.459  0.44 22.45           N  
ANISOU 2853  N  BMET A 375     2970   2801   2757    284   -360   -130       N  
ATOM   2854  CA AMET A 375      13.150   4.733   0.511  0.56  7.96           C  
ANISOU 2854  CA AMET A 375     1059   1176    788   -194   -228    -27       C  
ATOM   2855  CA BMET A 375      13.109   4.663   0.429  0.44 22.75           C  
ANISOU 2855  CA BMET A 375     3064   2710   2871     78   -170   -404       C  
ATOM   2856  C  AMET A 375      13.657   3.314   0.692  0.56  8.81           C  
ANISOU 2856  C  AMET A 375     1167   1241    938     20   -150     35       C  
ATOM   2857  C  BMET A 375      13.570   3.226   0.623  0.44 21.54           C  
ANISOU 2857  C  BMET A 375     2810   2555   2818    -58     39   -676       C  
ATOM   2858  O  AMET A 375      14.438   2.809  -0.108  0.56  9.54           O  
ANISOU 2858  O  AMET A 375     1428   1256    941    154   -217     66       O  
ATOM   2859  O  BMET A 375      14.114   2.589  -0.285  0.44 15.96           O  
ANISOU 2859  O  BMET A 375     1950   1827   2288   -186    362  -1184       O  
ATOM   2860  CB AMET A 375      11.705   4.778   0.026  0.56  8.77           C  
ANISOU 2860  CB AMET A 375     1168   1207    957   -188   -132    -52       C  
ATOM   2861  CB BMET A 375      11.691   4.684  -0.140  0.44 24.39           C  
ANISOU 2861  CB BMET A 375     3381   2811   3073      7   -207   -441       C  
ATOM   2862  CG AMET A 375      11.148   6.211   0.017  0.56 12.37           C  
ANISOU 2862  CG AMET A 375     1780   1467   1454   -228   -227   -223       C  
ATOM   2863  CG BMET A 375      11.175   6.094  -0.411  0.44 26.04           C  
ANISOU 2863  CG BMET A 375     3779   2909   3205    -25   -317   -451       C  
ATOM   2864  SD AMET A 375       9.382   6.313  -0.172  0.56 13.26           S  
ANISOU 2864  SD AMET A 375     1461   1468   2108    -70   -432    134       S  
ATOM   2865  SD BMET A 375       9.454   6.146  -0.945  0.44 28.17           S  
ANISOU 2865  SD BMET A 375     4178   3124   3402    -52   -374   -444       S  
ATOM   2866  CE AMET A 375       9.238   6.023  -1.921  0.56 18.12           C  
ANISOU 2866  CE AMET A 375     2166   2239   2481   -613   -239    -20       C  
ATOM   2867  CE BMET A 375       8.698   6.834   0.525  0.44 27.14           C  
ANISOU 2867  CE BMET A 375     3953   3036   3324   -113   -476   -570       C  
ATOM   2868  H  AMET A 375      13.772   5.425  -1.232  0.56  8.44           H  
ATOM   2869  H  BMET A 375      13.757   5.386  -1.281  0.44 26.94           H  
ATOM   2870  HA AMET A 375      13.146   5.167   1.379  0.56  9.56           H  
ATOM   2871  HA BMET A 375      13.095   5.101   1.294  0.44 27.31           H  
ATOM   2872  HB2AMET A 375      11.660   4.428  -0.877  0.56 10.53           H  
ATOM   2873  HB2BMET A 375      11.682   4.197  -0.979  0.44 29.27           H  
ATOM   2874  HB3AMET A 375      11.153   4.241   0.617  0.56 10.53           H  
ATOM   2875  HB3BMET A 375      11.091   4.263   0.495  0.44 29.27           H  
ATOM   2876  HG2AMET A 375      11.378   6.638   0.857  0.56 14.86           H  
ATOM   2877  HG2BMET A 375      11.248   6.614   0.404  0.44 31.25           H  
ATOM   2878  HG3AMET A 375      11.550   6.695  -0.722  0.56 14.86           H  
ATOM   2879  HG3BMET A 375      11.714   6.495  -1.110  0.44 31.25           H  
ATOM   2880  HE1AMET A 375       8.315   5.811  -2.131  0.56 21.76           H  
ATOM   2881  HE1BMET A 375       7.892   6.335   0.729  0.44 32.58           H  
ATOM   2882  HE2AMET A 375       9.509   6.824  -2.397  0.56 21.76           H  
ATOM   2883  HE2BMET A 375       9.324   6.767   1.263  0.44 32.58           H  
ATOM   2884  HE3AMET A 375       9.812   5.281  -2.167  0.56 21.76           H  
ATOM   2885  HE3BMET A 375       8.478   7.764   0.361  0.44 32.58           H  
ATOM   2886  N  ALYS A 376      13.248   2.703   1.801  0.56  9.14           N  
ANISOU 2886  N  ALYS A 376     1241   1175   1058    -16   -168    184       N  
ATOM   2887  N  BLYS A 376      13.341   2.716   1.830  0.44 24.99           N  
ANISOU 2887  N  BLYS A 376     3336   2999   3159    -16   -145   -323       N  
ATOM   2888  CA ALYS A 376      13.763   1.395   2.170  0.56 10.88           C  
ANISOU 2888  CA ALYS A 376     1475   1441   1217   -320   -302    120       C  
ATOM   2889  CA BLYS A 376      13.809   1.383   2.172  0.44 27.65           C  
ANISOU 2889  CA BLYS A 376     3713   3369   3423     67   -418   -111       C  
ATOM   2890  C  ALYS A 376      13.235   0.354   1.191  0.56 16.13           C  
ANISOU 2890  C  ALYS A 376     2004   2066   2059   -506   -435    256       C  
ATOM   2891  C  BLYS A 376      13.246   0.364   1.194  0.44 29.66           C  
ANISOU 2891  C  BLYS A 376     3947   3656   3666    117   -757    -61       C  
ATOM   2892  O  ALYS A 376      12.043   0.336   0.877  0.56 13.57           O  
ANISOU 2892  O  ALYS A 376     1759   1613   1782   -402   -484    189       O  
ATOM   2893  O  BLYS A 376      12.046   0.361   0.902  0.44 30.90           O  
ANISOU 2893  O  BLYS A 376     4187   3799   3753    103   -913     -9       O  
ATOM   2894  CB ALYS A 376      13.336   1.061   3.598  0.56 10.61           C  
ANISOU 2894  CB ALYS A 376     1468   1478   1086    -72   -297    250       C  
ATOM   2895  CB BLYS A 376      13.383   1.034   3.594  0.44 27.74           C  
ANISOU 2895  CB BLYS A 376     3711   3407   3421     71   -314    -29       C  
ATOM   2896  CG ALYS A 376      14.027  -0.160   4.175  0.56 10.14           C  
ANISOU 2896  CG ALYS A 376     1404   1398   1051   -231   -137    202       C  
ATOM   2897  CG BLYS A 376      14.504   1.132   4.606  0.44 27.25           C  
ANISOU 2897  CG BLYS A 376     3605   3375   3375    -17   -194      1       C  
ATOM   2898  CD ALYS A 376      13.691  -0.368   5.649  0.56 10.81           C  
ANISOU 2898  CD ALYS A 376     1386   1438   1282    -85   -121    255       C  
ATOM   2899  CD BLYS A 376      14.607  -0.128   5.431  0.44 26.91           C  
ANISOU 2899  CD BLYS A 376     3489   3393   3342   -262    -28    -10       C  
ATOM   2900  CE ALYS A 376      12.246  -0.791   5.839  0.56 10.94           C  
ANISOU 2900  CE ALYS A 376     1234   1608   1315   -167   -153    253       C  
ATOM   2901  CE BLYS A 376      13.463  -0.259   6.413  0.44 27.39           C  
ANISOU 2901  CE BLYS A 376     3598   3483   3326   -496    139     -4       C  
ATOM   2902  NZ ALYS A 376      11.919  -1.137   7.253  0.56 10.57           N  
ANISOU 2902  NZ ALYS A 376     1195   1563   1256   -165   -123    308       N  
ATOM   2903  NZ BLYS A 376      12.183  -0.718   5.807  0.44 27.85           N  
ANISOU 2903  NZ BLYS A 376     3698   3570   3313   -693    237     -3       N  
ATOM   2904  H  ALYS A 376      12.674   3.026   2.354  0.56 10.98           H  
ATOM   2905  H  BLYS A 376      12.920   3.120   2.461  0.44 29.99           H  
ATOM   2906  HA ALYS A 376      14.733   1.387   2.136  0.56 13.06           H  
ATOM   2907  HA BLYS A 376      14.778   1.356   2.125  0.44 33.19           H  
ATOM   2908  HB2ALYS A 376      13.544   1.816   4.170  0.56 12.74           H  
ATOM   2909  HB2BLYS A 376      12.682   1.645   3.869  0.44 33.30           H  
ATOM   2910  HB3ALYS A 376      12.381   0.891   3.606  0.56 12.74           H  
ATOM   2911  HB3BLYS A 376      13.053   0.122   3.606  0.44 33.30           H  
ATOM   2912  HG2ALYS A 376      13.742  -0.948   3.686  0.56 12.18           H  
ATOM   2913  HG2BLYS A 376      15.346   1.265   4.143  0.44 32.71           H  
ATOM   2914  HG3ALYS A 376      14.987  -0.050   4.096  0.56 12.18           H  
ATOM   2915  HG3BLYS A 376      14.333   1.877   5.205  0.44 32.71           H  
ATOM   2916  HD2ALYS A 376      14.262  -1.063   6.013  0.56 12.98           H  
ATOM   2917  HD2BLYS A 376      14.590  -0.898   4.842  0.44 32.30           H  
ATOM   2918  HD3ALYS A 376      13.832   0.462   6.130  0.56 12.98           H  
ATOM   2919  HD3BLYS A 376      15.437  -0.113   5.934  0.44 32.30           H  
ATOM   2920  HE2ALYS A 376      11.666  -0.061   5.569  0.56 13.14           H  
ATOM   2921  HE2BLYS A 376      13.711  -0.902   7.095  0.44 32.88           H  
ATOM   2922  HE3ALYS A 376      12.072  -1.573   5.293  0.56 13.14           H  
ATOM   2923  HE3BLYS A 376      13.300   0.608   6.818  0.44 32.88           H  
ATOM   2924  HZ1ALYS A 376      11.060  -1.358   7.321  0.56 12.69           H  
ATOM   2925  HZ1BLYS A 376      12.323  -1.449   5.319  0.44 33.43           H  
ATOM   2926  HZ2ALYS A 376      12.417  -1.825   7.520  0.56 12.69           H  
ATOM   2927  HZ2BLYS A 376      11.593  -0.906   6.446  0.44 33.43           H  
ATOM   2928  HZ3ALYS A 376      12.081  -0.440   7.782  0.56 12.69           H  
ATOM   2929  HZ3BLYS A 376      11.849  -0.081   5.283  0.44 33.43           H  
ATOM   2930  N   SER A 377      14.118  -0.499   0.685  1.00 29.68           N  
ATOM   2931  CA  SER A 377      13.703  -1.498  -0.296  1.00 29.68           C  
ATOM   2932  C   SER A 377      13.176  -2.744   0.396  1.00 29.68           C  
ATOM   2933  O   SER A 377      12.629  -3.628  -0.261  1.00 29.68           O  
ATOM   2934  CB  SER A 377      14.854  -1.857  -1.235  1.00 29.68           C  
ATOM   2935  OG  SER A 377      16.016  -2.206  -0.509  1.00 29.68           O  
ATOM   2936  OXT SER A 377      13.272  -2.885   1.617  1.00 29.89           O  
ATOM   2937  H  ASER A 377      14.953  -0.520   0.890  0.56 35.62           H  
ATOM   2938  HA  SER A 377      12.990  -1.128  -0.840  1.00 35.62           H  
ATOM   2939  HB2 SER A 377      14.589  -2.611  -1.784  1.00 35.62           H  
ATOM   2940  HB3 SER A 377      15.053  -1.091  -1.796  1.00 35.62           H  
ATOM   2941  HG  SER A 377      16.643  -2.386  -1.038  1.00 35.62           H  
TER    2942      SER A 377                                                      
HETATM 2943  O  AHOH A 401      -8.968  17.862   0.488  0.91 39.29           O  
ANISOU 2943  O  AHOH A 401     6787   4575   3565   -348    689  -1213       O  
HETATM 2944  O  BHOH A 402     -12.824  23.773  -5.723  1.00 40.36           O  
ANISOU 2944  O  BHOH A 402     6461   4439   4435    -95    269      9       O  
HETATM 2945  O   HOH A 403     -21.333  11.189 -25.620  1.00 40.08           O  
ANISOU 2945  O   HOH A 403     5399   4908   4920   1528    326   -370       O  
HETATM 2946  O   HOH A 404      13.797  20.022 -16.844  1.00 38.93           O  
ANISOU 2946  O   HOH A 404     5426   4587   4780   1726    548   -218       O  
HETATM 2947  O  AHOH A 405       6.041  14.072  -5.283  0.92 28.03           O  
ANISOU 2947  O  AHOH A 405     3845   2434   4369   -972    486    -33       O  
HETATM 2948  O   HOH A 406     -15.071  16.061  -1.471  1.00 34.89           O  
ANISOU 2948  O   HOH A 406     4525   4374   4356     16   1019   -662       O  
HETATM 2949  O   HOH A 407     -16.144  12.166  -6.875  1.00 14.46           O  
ANISOU 2949  O   HOH A 407     1391   2235   1867    278    526   -424       O  
HETATM 2950  O   HOH A 408      -3.783  10.966 -31.331  1.00 31.39           O  
ANISOU 2950  O   HOH A 408     3776   4503   3646    203    431   -309       O  
HETATM 2951  O  AHOH A 409      -9.662  15.389   1.154  0.50 24.95           O  
ANISOU 2951  O  AHOH A 409     4534   2336   2608    -26   -179    164       O  
HETATM 2952  O  BHOH A 409      -8.333  15.876   0.774  0.50  8.68           O  
ANISOU 2952  O  BHOH A 409     1196   1093   1008    -98    197    -11       O  
HETATM 2953  O   HOH A 410      -2.977  11.177 -12.381  1.00 22.43           O  
ANISOU 2953  O   HOH A 410     3529   1939   3056   1160  -1355   -452       O  
HETATM 2954  O   HOH A 411       2.181   2.481   1.001  1.00 28.06           O  
ANISOU 2954  O   HOH A 411     4783   3362   2518  -1213   -600   -459       O  
HETATM 2955  O   HOH A 412      13.258   2.151  -2.645  1.00 18.08           O  
ANISOU 2955  O   HOH A 412     2996   2694   1180   -826   -354    136       O  
HETATM 2956  O   HOH A 413     -17.994  -1.309 -24.369  1.00 27.48           O  
ANISOU 2956  O   HOH A 413     2778   2648   5015  -1122   -604   -795       O  
HETATM 2957  O   HOH A 414     -23.593  -2.180 -12.936  1.00 38.50           O  
ANISOU 2957  O   HOH A 414     6202   4303   4122   1649   -134    290       O  
HETATM 2958  O   HOH A 415     -20.759  10.104 -18.838  1.00 27.62           O  
ANISOU 2958  O   HOH A 415     2364   5116   3016   -316  -1344     92       O  
HETATM 2959  O   HOH A 416       7.029  -8.196  -6.233  1.00 37.09           O  
ANISOU 2959  O   HOH A 416     5321   4613   4158     36   -606  -1222       O  
HETATM 2960  O   HOH A 417     -15.022  13.480   0.495  1.00 29.79           O  
ANISOU 2960  O   HOH A 417     2578   3002   5738   -679   1759   -620       O  
HETATM 2961  O   HOH A 418       0.254  17.209 -11.446  1.00 31.18           O  
ANISOU 2961  O   HOH A 418     3903   3172   4770   -928    412    712       O  
HETATM 2962  O   HOH A 419     -13.070  15.971 -23.517  1.00 37.69           O  
ANISOU 2962  O   HOH A 419     6043   4398   3878    906   2148   -152       O  
HETATM 2963  O   HOH A 420       7.637  20.077 -14.733  1.00 13.63           O  
ANISOU 2963  O   HOH A 420     1538   1389   2253     81     11   -229       O  
HETATM 2964  O   HOH A 421     -30.603   4.925 -17.533  1.00 11.83           O  
ANISOU 2964  O   HOH A 421      719    959   2816    -12    -44    321       O  
HETATM 2965  O   HOH A 422     -12.210  11.748  -7.961  1.00  9.18           O  
ANISOU 2965  O   HOH A 422      939   1168   1379     41    203     -3       O  
HETATM 2966  O   HOH A 423       6.053  -7.520 -17.470  1.00 11.13           O  
ANISOU 2966  O   HOH A 423     1800   1035   1393     96    350   -130       O  
HETATM 2967  O   HOH A 424     -27.088   4.704 -23.623  1.00 14.64           O  
ANISOU 2967  O   HOH A 424     1116   2200   2246    -58    258    -20       O  
HETATM 2968  O   HOH A 425       2.488 -11.005 -17.355  1.00  9.43           O  
ANISOU 2968  O   HOH A 425      962   1271   1351    -17    -60     80       O  
HETATM 2969  O   HOH A 426     -24.916  -0.520 -11.413  1.00 24.77           O  
ANISOU 2969  O   HOH A 426     2590   2542   4279   -604   -298    631       O  
HETATM 2970  O   HOH A 427     -28.045  -1.918 -15.078  1.00 14.97           O  
ANISOU 2970  O   HOH A 427     1168   1182   3339    200    653    184       O  
HETATM 2971  O   HOH A 428       5.723   1.127   2.704  1.00 28.69           O  
ANISOU 2971  O   HOH A 428     3909   4376   2618   -304  -1825     82       O  
HETATM 2972  O   HOH A 429      -7.505  11.808 -33.581  1.00 43.59           O  
ANISOU 2972  O   HOH A 429     5770   5432   5359   -300   -416   1690       O  
HETATM 2973  O   HOH A 430     -16.110  15.011  -4.038  1.00 29.19           O  
ANISOU 2973  O   HOH A 430     3843   4455   2793   2185    472   -453       O  
HETATM 2974  O   HOH A 431     -25.787   2.027 -10.181  1.00 51.89           O  
ANISOU 2974  O   HOH A 431     5307   6935   7475   -178    148    207       O  
HETATM 2975  O   HOH A 432     -26.568  10.072 -10.940  1.00 12.10           O  
ANISOU 2975  O   HOH A 432      904   1665   2027    102   -188    -25       O  
HETATM 2976  O   HOH A 433     -23.479   2.848 -10.041  1.00 38.17           O  
ANISOU 2976  O   HOH A 433     4304   4156   6044   -603   -874   1329       O  
HETATM 2977  O   HOH A 434       6.462  16.347  -4.387  1.00 38.06           O  
ANISOU 2977  O   HOH A 434     3855   5693   4912    944   -324   -165       O  
HETATM 2978  O   HOH A 435      -1.284   1.448 -31.983  1.00 20.50           O  
ANISOU 2978  O   HOH A 435     2965   2458   2366    317   -692   -820       O  
HETATM 2979  O   HOH A 436       9.686  -5.344 -18.611  1.00 20.45           O  
ANISOU 2979  O   HOH A 436     1383   3626   2760    658   -299  -1384       O  
HETATM 2980  O   HOH A 437       5.963  -3.701  -5.840  1.00 12.35           O  
ANISOU 2980  O   HOH A 437     1548   1898   1246   -517   -250    303       O  
HETATM 2981  O   HOH A 438      -4.583 -12.341 -18.893  1.00 12.09           O  
ANISOU 2981  O   HOH A 438     1531   1657   1406     45    126    -25       O  
HETATM 2982  O   HOH A 439     -20.767  13.521 -23.765  1.00 36.27           O  
ANISOU 2982  O   HOH A 439     4961   2197   6622   1194    -10    628       O  
HETATM 2983  O   HOH A 440       9.035  -3.408 -27.314  1.00 14.24           O  
ANISOU 2983  O   HOH A 440     1484   1828   2099     13     50     -3       O  
HETATM 2984  O   HOH A 441       3.251  19.765 -15.058  1.00 10.08           O  
ANISOU 2984  O   HOH A 441      986   1135   1708    221   -306   -139       O  
HETATM 2985  O  AHOH A 442      -2.140  -8.668 -20.848  0.90 19.02           O  
ANISOU 2985  O  AHOH A 442     1894   2832   2502    552    349   1288       O  
HETATM 2986  O   HOH A 443      -2.651 -14.745 -18.171  1.00 12.65           O  
ANISOU 2986  O   HOH A 443     1470   2126   1210   -866    291    -99       O  
HETATM 2987  O   HOH A 444     -16.001   8.846 -32.544  1.00 43.48           O  
ANISOU 2987  O   HOH A 444     4697   5633   6190  -1746  -2264  -1001       O  
HETATM 2988  O   HOH A 445     -20.978   1.408 -23.061  1.00 16.26           O  
ANISOU 2988  O   HOH A 445     1054   1560   3562   -200    162   -705       O  
HETATM 2989  O   HOH A 446      -9.721  -8.821 -15.182  1.00 16.50           O  
ANISOU 2989  O   HOH A 446     1114   2827   2328   -216   -214  -1119       O  
HETATM 2990  O   HOH A 447      -6.177  -2.708  -1.096  1.00 20.06           O  
ANISOU 2990  O   HOH A 447     3676   2813   1133   -892    133    267       O  
HETATM 2991  O   HOH A 448      15.519  16.720 -13.470  1.00 28.80           O  
ANISOU 2991  O   HOH A 448     3263   1952   5729   -430    794    -85       O  
HETATM 2992  O   HOH A 449     -15.561  14.749 -22.739  1.00 27.91           O  
ANISOU 2992  O   HOH A 449     5011   2133   3460  -1280  -1702    685       O  
HETATM 2993  O   HOH A 450      -3.497  -5.243  -1.441  1.00 26.32           O  
ANISOU 2993  O   HOH A 450     4458   2634   2907    516   -365   -779       O  
HETATM 2994  O   HOH A 451     -12.898  16.239 -16.183  1.00 27.74           O  
ANISOU 2994  O   HOH A 451     4604   2641   3293   -627   1211   -199       O  
HETATM 2995  O   HOH A 452       5.875  -3.789 -30.877  1.00 13.31           O  
ANISOU 2995  O   HOH A 452     2025   1778   1255    -16    481    -48       O  
HETATM 2996  O   HOH A 453     -16.952  -3.946 -17.844  1.00 45.85           O  
ANISOU 2996  O   HOH A 453     6419   4938   6064   -782    672   -413       O  
HETATM 2997  O   HOH A 454      16.995  10.495 -15.373  1.00 13.51           O  
ANISOU 2997  O   HOH A 454     1562   1668   1902    -44   -149   -251       O  
HETATM 2998  O   HOH A 455       9.912  18.998 -15.865  1.00 13.18           O  
ANISOU 2998  O   HOH A 455     1575   1346   2085     86   -598    131       O  
HETATM 2999  O   HOH A 456      16.031  13.262  -4.777  1.00 31.33           O  
ANISOU 2999  O   HOH A 456     5236   3488   3181  -1442   1933  -1092       O  
HETATM 3000  O   HOH A 457      15.920  12.827 -18.859  1.00 34.66           O  
ANISOU 3000  O   HOH A 457     2135   4156   6879    450    266    147       O  
HETATM 3001  O   HOH A 458      10.808   7.923 -23.110  1.00 23.58           O  
ANISOU 3001  O   HOH A 458     3704   2872   2384    852   1476     17       O  
HETATM 3002  O   HOH A 459       6.594  -9.998  -8.191  1.00 36.69           O  
ANISOU 3002  O   HOH A 459     4115   4752   5075  -1875    442    929       O  
HETATM 3003  O   HOH A 460      -2.186  17.443  -8.494  1.00  8.53           O  
ANISOU 3003  O   HOH A 460     1034   1186   1022   -146    106    120       O  
HETATM 3004  O   HOH A 461     -15.316  19.820  -2.689  1.00 39.04           O  
ANISOU 3004  O   HOH A 461     4320   4756   5758   -542    510   1419       O  
HETATM 3005  O   HOH A 462     -20.241   8.332  -6.708  1.00 25.84           O  
ANISOU 3005  O   HOH A 462     4135   2968   2714    500   1058   -734       O  
HETATM 3006  O   HOH A 463      14.168  -2.080 -19.311  1.00 22.94           O  
ANISOU 3006  O   HOH A 463     2549   2049   4117    748  -1465  -1314       O  
HETATM 3007  O   HOH A 464     -16.181  15.183 -25.361  1.00 25.72           O  
ANISOU 3007  O   HOH A 464     4317   2367   3089    950    832   -352       O  
HETATM 3008  O   HOH A 465     -27.481   0.753 -23.863  1.00 24.68           O  
ANISOU 3008  O   HOH A 465     1840   3834   3703  -1083    233  -1245       O  
HETATM 3009  O   HOH A 466      -5.795   9.490 -32.630  1.00 22.63           O  
ANISOU 3009  O   HOH A 466     3743   2837   2019   -828   1200   -131       O  
HETATM 3010  O   HOH A 467     -12.564   7.909   3.515  1.00 39.87           O  
ANISOU 3010  O   HOH A 467     6194   5290   3663    244   -188   2306       O  
HETATM 3011  O   HOH A 468     -18.979  -1.999 -13.961  1.00 28.68           O  
ANISOU 3011  O   HOH A 468     2664   2283   5949   -650  -1350   1402       O  
HETATM 3012  O   HOH A 469     -23.972  -0.826 -21.377  1.00 35.29           O  
ANISOU 3012  O   HOH A 469     3589   3852   5969    302   2334   -911       O  
HETATM 3013  O   HOH A 470      12.590  -8.694 -10.930  1.00 21.04           O  
ANISOU 3013  O   HOH A 470     2152   2617   3223   -736    314   -528       O  
HETATM 3014  O   HOH A 471      -0.077  15.590  -8.181  1.00 10.87           O  
ANISOU 3014  O   HOH A 471     1617   1334   1178    108    156    -38       O  
HETATM 3015  O   HOH A 472       2.742  -4.722  -4.009  1.00 12.01           O  
ANISOU 3015  O   HOH A 472     1793   1503   1265   -211   -272    253       O  
HETATM 3016  O   HOH A 473      13.071  -2.457  -5.273  1.00 31.04           O  
ANISOU 3016  O   HOH A 473     3546   4504   3744    -55  -1533   1730       O  
HETATM 3017  O   HOH A 474      11.131   1.174  -1.560  1.00 25.82           O  
ANISOU 3017  O   HOH A 474     3904   2977   2928   -464  -1766   -162       O  
HETATM 3018  O   HOH A 475      -6.151   9.814 -10.905  1.00  8.59           O  
ANISOU 3018  O   HOH A 475      813   1334   1116   -154   -258    124       O  
HETATM 3019  O  AHOH A 476      -7.462  -6.463 -21.811  0.93 15.29           O  
ANISOU 3019  O  AHOH A 476     1663   1609   2538   -481   -369    324       O  
HETATM 3020  O   HOH A 477       6.350   6.935 -25.901  1.00 20.46           O  
ANISOU 3020  O   HOH A 477     4169   1497   2108   -201   1530     12       O  
HETATM 3021  O   HOH A 478      -3.031   7.270   0.653  1.00 13.28           O  
ANISOU 3021  O   HOH A 478     2073   1475   1499   -144     49    -30       O  
HETATM 3022  O   HOH A 479     -13.232   3.458 -22.735  1.00  7.93           O  
ANISOU 3022  O   HOH A 479      803   1053   1155     -1   -301   -145       O  
HETATM 3023  O   HOH A 480      -8.733   8.917 -11.234  1.00  6.64           O  
ANISOU 3023  O   HOH A 480      594   1030    900    -50     28    -96       O  
HETATM 3024  O   HOH A 481      11.446  -7.448 -15.462  1.00 27.89           O  
ANISOU 3024  O   HOH A 481     4496   1643   4458     91   1559   -473       O  
HETATM 3025  O   HOH A 482      -8.096   2.722   0.231  1.00 16.46           O  
ANISOU 3025  O   HOH A 482     3312   1764   1177   -640    739   -241       O  
HETATM 3026  O   HOH A 483      13.707   4.538 -22.461  1.00 11.25           O  
ANISOU 3026  O   HOH A 483      964   1641   1670   -102    223     68       O  
HETATM 3027  O   HOH A 484       0.017  13.978 -13.446  1.00 13.99           O  
ANISOU 3027  O   HOH A 484     1847   1984   1484    234    442    232       O  
HETATM 3028  O   HOH A 485      -7.904  -7.289  -5.702  1.00 23.91           O  
ANISOU 3028  O   HOH A 485     4118   2748   2218  -1633    272     35       O  
HETATM 3029  O   HOH A 486     -24.913   9.026 -19.512  1.00 12.89           O  
ANISOU 3029  O   HOH A 486     1055   1517   2324    292    140    -72       O  
HETATM 3030  O   HOH A 487      -0.218  -0.857   2.306  1.00 31.92           O  
ANISOU 3030  O   HOH A 487     4494   4328   3305  -1148  -1465   -174       O  
HETATM 3031  O   HOH A 488     -10.620  -1.523  -5.159  1.00 15.88           O  
ANISOU 3031  O   HOH A 488     1633   1831   2570   -588    264    223       O  
HETATM 3032  O   HOH A 489       3.945   7.693   1.477  1.00 34.56           O  
ANISOU 3032  O   HOH A 489     3960   6512   2657     71  -1490    474       O  
HETATM 3033  O   HOH A 490       2.989  17.204  -3.982  1.00 23.56           O  
ANISOU 3033  O   HOH A 490     2117   2175   4662    660  -1358   -929       O  
HETATM 3034  O   HOH A 491      12.069  13.906 -21.310  1.00 35.69           O  
ANISOU 3034  O   HOH A 491     4116   4630   4814    626   1874   2106       O  
HETATM 3035  O   HOH A 492       4.616  -0.060 -32.231  1.00 15.84           O  
ANISOU 3035  O   HOH A 492     2860   1888   1271    392    635     -5       O  
HETATM 3036  O   HOH A 493     -20.796  -3.281 -15.467  1.00 43.40           O  
ANISOU 3036  O   HOH A 493     5777   4650   6063   2088    396   1593       O  
HETATM 3037  O   HOH A 494      14.170   0.387  -7.008  1.00 28.42           O  
ANISOU 3037  O   HOH A 494     3146   3719   3934  -1749  -1060    -31       O  
HETATM 3038  O   HOH A 495       4.407  13.181 -26.994  1.00 21.61           O  
ANISOU 3038  O   HOH A 495     2880   2515   2817    148    851    936       O  
HETATM 3039  O   HOH A 496       2.347  -9.770 -14.950  1.00 14.00           O  
ANISOU 3039  O   HOH A 496     1675   1712   1933    675   -509   -353       O  
HETATM 3040  O   HOH A 497     -13.975  15.091  -7.615  1.00 23.01           O  
ANISOU 3040  O   HOH A 497     2996   2751   2994    576   1118    606       O  
HETATM 3041  O  BHOH A 498      -1.341  -9.896 -19.820  0.91 39.94           O  
ANISOU 3041  O  BHOH A 498     4940   5850   4385    815    -46   -257       O  
HETATM 3042  O   HOH A 499      -1.061  13.140 -23.790  1.00 11.89           O  
ANISOU 3042  O   HOH A 499     1016   1723   1779     54    -65   -260       O  
HETATM 3043  O   HOH A 500     -13.077  -2.818 -13.204  1.00 11.30           O  
ANISOU 3043  O   HOH A 500      943   1472   1879     36   -112   -339       O  
HETATM 3044  O   HOH A 501     -20.779   2.123 -12.031  1.00 15.15           O  
ANISOU 3044  O   HOH A 501     1372   2315   2068    568   -112     14       O  
HETATM 3045  O  AHOH A 502      -1.411 -11.324  -5.436  1.00 43.62           O  
ANISOU 3045  O  AHOH A 502     5954   5608   5011   -938    -82   -714       O  
HETATM 3046  O   HOH A 503      -4.644  13.256 -27.278  1.00 11.32           O  
ANISOU 3046  O   HOH A 503     1190   1704   1408   -272   -187    427       O  
HETATM 3047  O   HOH A 504      16.111  -1.973 -12.007  1.00 31.20           O  
ANISOU 3047  O   HOH A 504     2580   3687   5589   1610   -188   -288       O  
HETATM 3048  O   HOH A 505       8.471  16.160 -20.578  1.00 20.32           O  
ANISOU 3048  O   HOH A 505     2342   1508   3870    178   1438    553       O  
HETATM 3049  O   HOH A 506      10.290  -4.455 -20.939  1.00 16.81           O  
ANISOU 3049  O   HOH A 506     1678   1741   2969   -110   -764   -272       O  
HETATM 3050  O   HOH A 507     -13.255   3.535 -31.332  1.00 16.87           O  
ANISOU 3050  O   HOH A 507     2334   2560   1516    253   -253   -284       O  
HETATM 3051  O   HOH A 508       1.368   9.912 -33.002  1.00 43.94           O  
ANISOU 3051  O   HOH A 508     6457   5278   4958   -739    756    822       O  
HETATM 3052  O   HOH A 509       5.809 -10.367 -11.958  1.00  9.67           O  
ANISOU 3052  O   HOH A 509     1566   1013   1095    228   -258     73       O  
HETATM 3053  O   HOH A 510     -23.635   7.338 -25.488  1.00 14.89           O  
ANISOU 3053  O   HOH A 510      982   2498   2176    300   -384    -75       O  
HETATM 3054  O   HOH A 511     -15.684   5.679  -1.965  1.00 22.66           O  
ANISOU 3054  O   HOH A 511     2228   4010   2371     50   1294     -5       O  
HETATM 3055  O   HOH A 512       0.184  12.669 -27.538  1.00 14.75           O  
ANISOU 3055  O   HOH A 512     1524   2538   1542     96   -412    235       O  
HETATM 3056  O   HOH A 513      -9.130  19.167  -8.877  1.00 15.51           O  
ANISOU 3056  O   HOH A 513     1482   1553   2856   -195    952   -338       O  
HETATM 3057  O   HOH A 514     -11.139  -4.782 -13.476  1.00 11.52           O  
ANISOU 3057  O   HOH A 514     1042   1348   1985    -34    146     98       O  
HETATM 3058  O   HOH A 515     -17.889  -2.130 -17.926  1.00 27.98           O  
ANISOU 3058  O   HOH A 515     2163   4017   4451    112   1582    444       O  
HETATM 3059  O   HOH A 516      -7.559  12.619 -16.135  1.00  6.71           O  
ANISOU 3059  O   HOH A 516      668   1022    860   -106    -46    -84       O  
HETATM 3060  O   HOH A 517      -6.612  -1.329 -30.169  1.00 17.76           O  
ANISOU 3060  O   HOH A 517     1690   2324   2735    534   -528  -1314       O  
HETATM 3061  O   HOH A 518       2.887  -4.096   0.492  1.00 29.15           O  
ANISOU 3061  O   HOH A 518     4167   3912   2998   -226  -1415   1524       O  
HETATM 3062  O   HOH A 519       0.863   9.398 -17.796  1.00  7.57           O  
ANISOU 3062  O   HOH A 519      734   1198    944     18    -12    -13       O  
HETATM 3063  O   HOH A 520       0.274  17.663  -3.604  1.00 13.77           O  
ANISOU 3063  O   HOH A 520     1476   1376   2378     66    -16    353       O  
HETATM 3064  O   HOH A 521     -17.500  12.964 -12.431  1.00 14.63           O  
ANISOU 3064  O   HOH A 521     1086   1737   2735   -101     51   -267       O  
HETATM 3065  O   HOH A 522     -10.333  -4.130 -11.095  1.00 17.18           O  
ANISOU 3065  O   HOH A 522     1634   2098   2795    -45   -436   -592       O  
HETATM 3066  O   HOH A 523      16.143   6.432 -14.354  1.00 13.01           O  
ANISOU 3066  O   HOH A 523     1072   1620   2251    181     60   -291       O  
HETATM 3067  O   HOH A 524      -4.678  -9.603 -27.890  1.00 32.07           O  
ANISOU 3067  O   HOH A 524     2635   5102   4447   -830   -458    641       O  
HETATM 3068  O   HOH A 525      -0.554  12.893  -1.165  1.00 24.26           O  
ANISOU 3068  O   HOH A 525     3382   4598   1239     33     98    154       O  
HETATM 3069  O   HOH A 526     -14.237   2.410  -3.348  1.00 33.52           O  
ANISOU 3069  O   HOH A 526     5903   2684   4150   -752   2291    374       O  
HETATM 3070  O   HOH A 527     -18.044   4.748 -28.795  1.00 13.99           O  
ANISOU 3070  O   HOH A 527     1485   2342   1488   -552   -279   -508       O  
HETATM 3071  O   HOH A 528      -1.240 -11.464 -21.463  1.00 38.48           O  
ANISOU 3071  O   HOH A 528     6285   4225   4110   -804   1013   -518       O  
HETATM 3072  O   HOH A 529       9.046  -5.423 -25.536  1.00 18.22           O  
ANISOU 3072  O   HOH A 529     3483   1428   2010    -68   1044   -201       O  
HETATM 3073  O   HOH A 530     -16.549  -0.173  -9.497  1.00 30.85           O  
ANISOU 3073  O   HOH A 530     4471   3092   4160   -599   2120    708       O  
HETATM 3074  O   HOH A 531      -4.949   0.912 -33.048  1.00 33.77           O  
ANISOU 3074  O   HOH A 531     5373   4215   3241   1242    862   -531       O  
HETATM 3075  O   HOH A 532       5.967  -3.197  -1.173  1.00 37.24           O  
ANISOU 3075  O   HOH A 532     3922   4584   5644    379  -1040   1466       O  
HETATM 3076  O   HOH A 533      14.177  -2.174 -22.090  1.00 20.16           O  
ANISOU 3076  O   HOH A 533     1373   2251   4035    312     82   -889       O  
HETATM 3077  O   HOH A 534      19.102  15.104 -17.801  1.00 40.69           O  
ANISOU 3077  O   HOH A 534     4296   5835   5330    534   1140   1292       O  
HETATM 3078  O   HOH A 535       8.368   3.560 -26.220  1.00 29.92           O  
ANISOU 3078  O   HOH A 535     4740   2956   3671   1150   2147    155       O  
HETATM 3079  O   HOH A 536       1.842   9.738 -14.163  1.00  9.97           O  
ANISOU 3079  O   HOH A 536     1374   1349   1065   -426    286   -194       O  
HETATM 3080  O   HOH A 537       2.050  10.784 -19.795  1.00  6.82           O  
ANISOU 3080  O   HOH A 537      640   1024    927     20      6   -174       O  
HETATM 3081  O   HOH A 538      -1.403  -3.737 -20.767  1.00  7.79           O  
ANISOU 3081  O   HOH A 538      653   1444    864    198     42    -24       O  
HETATM 3082  O   HOH A 539       3.204  -2.904 -30.360  1.00 12.19           O  
ANISOU 3082  O   HOH A 539     1762   1517   1354    -82     44     38       O  
HETATM 3083  O   HOH A 540     -10.969  12.548 -14.843  1.00 18.04           O  
ANISOU 3083  O   HOH A 540     1163   2046   3645    217    433   1194       O  
HETATM 3084  O   HOH A 541       3.360   6.848 -30.595  1.00 24.99           O  
ANISOU 3084  O   HOH A 541     3656   4257   1581    226    836    722       O  
HETATM 3085  O   HOH A 542     -22.907  10.385  -7.833  1.00 45.05           O  
ANISOU 3085  O   HOH A 542     7575   4720   4821    632   -638    391       O  
HETATM 3086  O   HOH A 543      -1.725  16.226  -1.081  1.00 21.17           O  
ANISOU 3086  O   HOH A 543     2901   3767   1375   1156    136   -176       O  
HETATM 3087  O   HOH A 544       1.638  15.622 -25.497  1.00 19.63           O  
ANISOU 3087  O   HOH A 544     3785   1477   2195   -483   -993    194       O  
HETATM 3088  O   HOH A 545      10.581  -6.834  -6.459  1.00 33.74           O  
ANISOU 3088  O   HOH A 545     6009   4045   2766    821  -1470    880       O  
HETATM 3089  O   HOH A 546     -11.262  14.878 -24.979  1.00 13.30           O  
ANISOU 3089  O   HOH A 546     1359   1399   2294    198   -659   -130       O  
HETATM 3090  O   HOH A 547       3.429 -10.423 -10.343  1.00 19.47           O  
ANISOU 3090  O   HOH A 547     1970   2024   3402     -9   -103   -953       O  
HETATM 3091  O   HOH A 548       7.468   0.489 -24.674  1.00 11.95           O  
ANISOU 3091  O   HOH A 548      967   2261   1313    248    216    130       O  
HETATM 3092  O   HOH A 549      14.178  16.340 -10.529  1.00 35.97           O  
ANISOU 3092  O   HOH A 549     3259   4406   6002  -1396  -1152  -1250       O  
HETATM 3093  O   HOH A 550      -9.477  14.625 -16.035  1.00  9.43           O  
ANISOU 3093  O   HOH A 550     1323    994   1264    -31   -195    -75       O  
HETATM 3094  O   HOH A 551     -14.322  -6.775 -24.624  1.00 50.34           O  
ANISOU 3094  O   HOH A 551     5833   5479   7815   -676  -1333  -1524       O  
HETATM 3095  O   HOH A 552      11.633   4.021   3.757  1.00 16.87           O  
ANISOU 3095  O   HOH A 552     2800   1522   2087   -182    210    -60       O  
HETATM 3096  O  AHOH A 553      10.290  13.719  -3.105  0.95 21.87           O  
ANISOU 3096  O  AHOH A 553     4426   2024   1859  -1191   -795    253       O  
HETATM 3097  O   HOH A 554      -4.441   5.245 -33.290  1.00 24.19           O  
ANISOU 3097  O   HOH A 554     2633   3324   3234    437   1318    134       O  
HETATM 3098  O   HOH A 555      12.381   7.157 -19.086  1.00  8.79           O  
ANISOU 3098  O   HOH A 555      454   1184   1700     16    150    127       O  
HETATM 3099  O   HOH A 556      -6.129  15.988 -13.666  1.00  8.73           O  
ANISOU 3099  O   HOH A 556     1154   1140   1021   -104     11    -52       O  
HETATM 3100  O   HOH A 557     -13.069  10.697 -16.451  1.00 10.24           O  
ANISOU 3100  O   HOH A 557      902   1582   1407    342   -151    -35       O  
HETATM 3101  O   HOH A 558       6.423   9.476 -24.902  1.00 10.91           O  
ANISOU 3101  O   HOH A 558     1358   1494   1293     84    402     28       O  
HETATM 3102  O   HOH A 559       2.899  -4.350 -32.785  1.00 26.53           O  
ANISOU 3102  O   HOH A 559     4076   2867   3137   1622   -352    814       O  
HETATM 3103  O   HOH A 560      -9.984  -1.912 -28.436  1.00 11.76           O  
ANISOU 3103  O   HOH A 560     1426   1689   1354   -177   -488   -244       O  
HETATM 3104  O   HOH A 561     -19.644  13.641 -26.417  1.00 25.70           O  
ANISOU 3104  O   HOH A 561     2263   4044   3458   1357    344   1079       O  
HETATM 3105  O   HOH A 562      -3.663  -9.823  -8.001  1.00 20.06           O  
ANISOU 3105  O   HOH A 562     4147   2177   1299   1515    -82     30       O  
HETATM 3106  O   HOH A 563      14.053  11.831 -17.983  1.00 22.13           O  
ANISOU 3106  O   HOH A 563     1401   1660   5347    -63   -121    835       O  
HETATM 3107  O   HOH A 564      -5.220  12.216 -11.957  1.00 11.75           O  
ANISOU 3107  O   HOH A 564     2027   1205   1232   -462   -561    139       O  
HETATM 3108  O   HOH A 565      -3.495   1.953   4.090  1.00 40.42           O  
ANISOU 3108  O   HOH A 565     6808   4590   3961   -253   1175   1014       O  
HETATM 3109  O   HOH A 566      15.267   0.817  -9.496  1.00 22.51           O  
ANISOU 3109  O   HOH A 566     2369   3766   2418  -1100   -762    124       O  
HETATM 3110  O   HOH A 567     -22.487  -2.124 -19.193  1.00 41.45           O  
ANISOU 3110  O   HOH A 567     5626   5021   5100   -376   -148  -1510       O  
HETATM 3111  O   HOH A 568     -16.210  -3.268 -15.462  1.00 23.07           O  
ANISOU 3111  O   HOH A 568     3280   2799   2688  -1654    935   -372       O  
HETATM 3112  O   HOH A 569      -4.104   4.774   0.650  1.00 15.34           O  
ANISOU 3112  O   HOH A 569     3175   1626   1027   -130    241   -118       O  
HETATM 3113  O   HOH A 570     -17.687   8.129  -4.266  1.00 20.71           O  
ANISOU 3113  O   HOH A 570     1900   2697   3272    154   1169   -786       O  
HETATM 3114  O   HOH A 571     -11.623   5.437 -31.890  1.00 28.93           O  
ANISOU 3114  O   HOH A 571     4054   3483   3456    -13   -721   -652       O  
HETATM 3115  O   HOH A 572      -3.638  13.795 -15.911  1.00  8.52           O  
ANISOU 3115  O   HOH A 572      928   1230   1080    -20    -65   -104       O  
HETATM 3116  O   HOH A 573     -17.458   1.970  -8.136  1.00 17.02           O  
ANISOU 3116  O   HOH A 573     1974   1589   2902    131    446     20       O  
HETATM 3117  O   HOH A 574      -2.615   0.880 -29.524  1.00 14.00           O  
ANISOU 3117  O   HOH A 574     1660   2296   1364    517   -167   -509       O  
HETATM 3118  O   HOH A 575      -1.090   8.896 -34.197  1.00 48.26           O  
ANISOU 3118  O   HOH A 575     6565   6150   5620   1334    117     65       O  
HETATM 3119  O   HOH A 576     -18.635  11.729 -30.738  1.00 21.76           O  
ANISOU 3119  O   HOH A 576     2281   3506   2479     82  -1187    224       O  
HETATM 3120  O   HOH A 577     -12.665  -3.458 -26.951  1.00 31.14           O  
ANISOU 3120  O   HOH A 577     4265   3392   4175   -709   1077  -2086       O  
HETATM 3121  O   HOH A 578      -1.135  -4.508  -0.467  1.00 25.47           O  
ANISOU 3121  O   HOH A 578     4218   2584   2875   -485    612   1157       O  
HETATM 3122  O   HOH A 579     -23.268  10.215 -25.638  1.00 30.90           O  
ANISOU 3122  O   HOH A 579     2793   4734   4212   -267   -238    946       O  
HETATM 3123  O   HOH A 580     -13.714  11.084   0.234  1.00 23.90           O  
ANISOU 3123  O   HOH A 580     1686   2827   4568   -378    123   1377       O  
HETATM 3124  O   HOH A 581      11.451  -2.132 -20.121  1.00 13.18           O  
ANISOU 3124  O   HOH A 581     1712   1332   1964    -93   -387   -102       O  
HETATM 3125  O   HOH A 582     -14.727  11.621  -9.236  1.00  9.93           O  
ANISOU 3125  O   HOH A 582     1055   1418   1299     19    225   -274       O  
HETATM 3126  O   HOH A 583     -25.340  13.947 -10.266  1.00 33.57           O  
ANISOU 3126  O   HOH A 583     3524   4080   5152    476   -437   -669       O  
HETATM 3127  O   HOH A 584     -11.215  -5.029 -27.220  1.00 40.26           O  
ANISOU 3127  O   HOH A 584     5567   6153   3575    214  -1691  -1983       O  
HETATM 3128  O   HOH A 585       2.683   1.395 -33.254  1.00 31.87           O  
ANISOU 3128  O   HOH A 585     5023   4124   2960   1629  -1238   -560       O  
HETATM 3129  O   HOH A 586     -14.236  -1.232  -8.666  1.00 32.01           O  
ANISOU 3129  O   HOH A 586     5152   3162   3847  -1839    493    880       O  
HETATM 3130  O   HOH A 587     -10.360  13.919 -31.942  1.00 39.81           O  
ANISOU 3130  O   HOH A 587     5353   4426   5347   -938  -1173     79       O  
HETATM 3131  O   HOH A 588     -12.188  -4.022  -9.322  1.00 29.37           O  
ANISOU 3131  O   HOH A 588     3190   4515   3455  -1098    545   -305       O  
HETATM 3132  O   HOH A 589       6.549   9.752 -29.291  1.00 39.48           O  
ANISOU 3132  O   HOH A 589     6163   4844   3995   -100   1787   -386       O  
HETATM 3133  O   HOH A 590      -3.822  -3.892 -27.744  1.00 19.02           O  
ANISOU 3133  O   HOH A 590     1294   3684   2250    156   -283  -1440       O  
HETATM 3134  O   HOH A 591      15.903  14.394  -8.949  1.00 28.26           O  
ANISOU 3134  O   HOH A 591     2967   4480   3290  -1412    143  -1029       O  
HETATM 3135  O   HOH A 592     -17.100   0.324 -27.224  1.00 37.72           O  
ANISOU 3135  O   HOH A 592     3287   7316   3730   -243   -648  -2388       O  
HETATM 3136  O   HOH A 593     -12.119  14.158  -9.537  1.00 13.29           O  
ANISOU 3136  O   HOH A 593     1844   1527   1677     58    118    163       O  
HETATM 3137  O   HOH A 594     -20.839  13.213 -19.976  1.00 38.62           O  
ANISOU 3137  O   HOH A 594     3404   2359   8912   -202   -465    164       O  
HETATM 3138  O   HOH A 595      -5.336  -5.734 -28.955  1.00 29.09           O  
ANISOU 3138  O   HOH A 595     2765   5129   3157    922  -1380  -1152       O  
HETATM 3139  O   HOH A 596       9.849   5.217 -27.797  1.00 38.66           O  
ANISOU 3139  O   HOH A 596     5158   4934   4597   -331    816    920       O  
HETATM 3140  O   HOH A 597       0.693  -5.834  -2.236  1.00 16.53           O  
ANISOU 3140  O   HOH A 597     2637   1962   1682   -280    131     12       O  
HETATM 3141  O   HOH A 598     -24.818  11.607 -23.293  1.00 37.83           O  
ANISOU 3141  O   HOH A 598     4641   4280   5454   2147   1862   2150       O  
HETATM 3142  O   HOH A 599      11.793   4.072 -24.547  1.00 28.89           O  
ANISOU 3142  O   HOH A 599     6140   2508   2328  -1074   -787   -377       O  
HETATM 3143  O   HOH A 600      14.327  13.408  -2.161  1.00 20.21           O  
ANISOU 3143  O   HOH A 600     4551   1608   1518   -135     24    -98       O  
HETATM 3144  O  AHOH A 601      -0.058  11.579  -7.488  0.77 17.14           O  
ANISOU 3144  O  AHOH A 601     1590   1879   3043    288   -371   -539       O  
HETATM 3145  O   HOH A 602     -14.622  -2.770 -10.204  1.00 40.86           O  
ANISOU 3145  O   HOH A 602     4940   6224   4359    197   1138    443       O  
HETATM 3146  O   HOH A 603     -14.251   0.080 -29.769  1.00 35.49           O  
ANISOU 3146  O   HOH A 603     4779   5278   3428   -736  -1574   -922       O  
HETATM 3147  O   HOH A 604     -24.940  -3.627 -16.599  1.00 38.21           O  
ANISOU 3147  O   HOH A 604     4578   4598   5343   -828   -329   -574       O  
HETATM 3148  O   HOH A 605     -10.479  -3.760  -6.933  1.00 18.62           O  
ANISOU 3148  O   HOH A 605     2740   2156   2179   -294    700    -27       O  
HETATM 3149  O   HOH A 606     -15.985  17.136  -0.265  1.00 36.75           O  
ANISOU 3149  O   HOH A 606     6072   3881   4009   -590   1785  -1099       O  
HETATM 3150  O   HOH A 607       7.762   6.224  -4.315  1.00 41.92           O  
ANISOU 3150  O   HOH A 607     4892   6024   5010    600   -652    774       O  
HETATM 3151  O   HOH A 608      -2.244 -13.124 -21.975  1.00 31.92           O  
ANISOU 3151  O   HOH A 608     3438   5189   3502   -644    451   1491       O  
HETATM 3152  O   HOH A 609     -16.776  12.237  -3.027  1.00 38.35           O  
ANISOU 3152  O   HOH A 609     4178   6331   4062   1049   1778  -1299       O  
HETATM 3153  O   HOH A 610       9.738  -1.402  -2.425  1.00 35.24           O  
ANISOU 3153  O   HOH A 610     4252   4985   4152   1747  -1642   -440       O  
HETATM 3154  O   HOH A 611     -11.893  14.695 -12.223  1.00 19.51           O  
ANISOU 3154  O   HOH A 611     2928   2235   2250  -1224   -511    654       O  
HETATM 3155  O   HOH A 612       3.960  16.531 -13.102  1.00 38.68           O  
ANISOU 3155  O   HOH A 612     7007   4222   3468   1720   1454    526       O  
HETATM 3156  O   HOH A 613      -2.886   8.017   3.342  1.00 29.92           O  
ANISOU 3156  O   HOH A 613     5189   4409   1769     -6   -885   -413       O  
HETATM 3157  O   HOH A 614     -15.562  19.497  -0.260  1.00 34.55           O  
ANISOU 3157  O   HOH A 614     4322   4818   3988   1169   1122    224       O  
HETATM 3158  O   HOH A 615     -24.119  11.934 -16.175  1.00 22.11           O  
ANISOU 3158  O   HOH A 615     2265   2534   3601   -728    105    316       O  
HETATM 3159  O   HOH A 616     -25.647   7.062 -23.541  1.00 16.15           O  
ANISOU 3159  O   HOH A 616     1436   2263   2436    245    -20    -26       O  
HETATM 3160  O   HOH A 617      -0.334   1.529   0.517  1.00 23.60           O  
ANISOU 3160  O   HOH A 617     3545   3305   2115     -8   -328   1172       O  
HETATM 3161  O   HOH A 618      -4.547  17.593 -15.255  1.00  9.31           O  
ANISOU 3161  O   HOH A 618     1196   1192   1148    -39     91    -59       O  
HETATM 3162  O   HOH A 619     -17.564   9.228 -31.245  1.00 30.83           O  
ANISOU 3162  O   HOH A 619     4036   3455   4221    142   -823   -663       O  
HETATM 3163  O   HOH A 620      -2.633 -15.097 -20.808  1.00 21.65           O  
ANISOU 3163  O   HOH A 620     3717   2696   1812   1681    -48     66       O  
HETATM 3164  O   HOH A 621      -2.452  15.700 -20.373  1.00 30.96           O  
ANISOU 3164  O   HOH A 621     2825   2356   6582    412   -823  -1561       O  
HETATM 3165  O   HOH A 622     -11.113  18.998 -10.712  1.00 17.21           O  
ANISOU 3165  O   HOH A 622     1940   2006   2592    148    607   -218       O  
HETATM 3166  O   HOH A 623     -19.162  15.015 -13.083  1.00 41.35           O  
ANISOU 3166  O   HOH A 623     5225   4672   5812   -599   -658   1519       O  
HETATM 3167  O   HOH A 624      10.649  -7.386 -17.245  1.00 36.22           O  
ANISOU 3167  O   HOH A 624     2997   3201   7562    344   -294    862       O  
HETATM 3168  O   HOH A 625       8.634   1.271   2.166  1.00 40.89           O  
ANISOU 3168  O   HOH A 625     5514   5930   4091   -693   -900    550       O  
HETATM 3169  O   HOH A 626      -6.551  13.770 -31.971  1.00 44.42           O  
ANISOU 3169  O   HOH A 626     6335   5704   4838   -332   -401    533       O  
HETATM 3170  O   HOH A 627     -23.886  15.138 -12.789  1.00 48.66           O  
ANISOU 3170  O   HOH A 627     5830   5397   7261   1450   -620    102       O  
HETATM 3171  O   HOH A 628     -24.404   1.344  -5.380  1.00 39.71           O  
ANISOU 3171  O   HOH A 628     4193   5796   5099    387    252   -519       O  
HETATM 3172  O   HOH A 629     -20.236   3.491 -27.757  1.00 21.36           O  
ANISOU 3172  O   HOH A 629     2058   2775   3283   -838    -17   -447       O  
HETATM 3173  O   HOH A 630     -12.296  14.349 -29.810  1.00 34.92           O  
ANISOU 3173  O   HOH A 630     3713   3674   5882     67  -1017    962       O  
HETATM 3174  O   HOH A 631      -4.061  -1.544 -29.344  1.00 17.37           O  
ANISOU 3174  O   HOH A 631     1695   2370   2534    497   -325   -707       O  
HETATM 3175  O   HOH A 632     -26.771   8.665 -17.506  1.00 11.77           O  
ANISOU 3175  O   HOH A 632      777   1413   2281    101    -82   -274       O  
HETATM 3176  O   HOH A 633      -8.622  18.684 -15.937  1.00 14.18           O  
ANISOU 3176  O   HOH A 633     1890   2201   1297   -785    -80    336       O  
HETATM 3177  O   HOH A 634      -1.635  12.465 -14.575  1.00 19.65           O  
ANISOU 3177  O   HOH A 634     2334   3046   2087   1417   -901  -1160       O  
HETATM 3178  O   HOH A 635     -11.309  -9.039 -24.842  1.00 42.54           O  
ANISOU 3178  O   HOH A 635     5771   4441   5951    -15    147   -456       O  
HETATM 3179  O   HOH A 636     -10.410  -5.953  -5.496  1.00 36.50           O  
ANISOU 3179  O   HOH A 636     3820   5162   4887  -1018   -345    492       O  
HETATM 3180  O   HOH A 637      -4.501 -10.134 -25.220  1.00 22.06           O  
ANISOU 3180  O   HOH A 637     3460   1617   3304   -270   -539   -313       O  
HETATM 3181  O   HOH A 638     -16.471  16.084 -13.930  1.00 37.08           O  
ANISOU 3181  O   HOH A 638     5206   4770   4112   1229    588    175       O  
HETATM 3182  O   HOH A 639      12.310   1.929 -26.166  1.00 29.07           O  
ANISOU 3182  O   HOH A 639     1975   5212   3859   -486    293   -455       O  
HETATM 3183  O   HOH A 640     -14.777  15.922 -11.884  1.00 26.80           O  
ANISOU 3183  O   HOH A 640     3208   2961   4014  -1029   -362    657       O  
HETATM 3184  O   HOH A 641      -2.469   3.656 -32.866  1.00 40.36           O  
ANISOU 3184  O   HOH A 641     5504   4841   4989   1696  -1700    -65       O  
HETATM 3185  O   HOH A 642     -12.725  25.869  -5.876  1.00 45.53           O  
ANISOU 3185  O   HOH A 642     5852   5801   5647    790    291   -480       O  
HETATM 3186  O   HOH A 643      -6.750  -1.078 -32.469  1.00 38.87           O  
ANISOU 3186  O   HOH A 643     5584   5087   4098    126   -132   -851       O  
HETATM 3187  O   HOH A 644     -26.118   9.305 -22.015  1.00 18.93           O  
ANISOU 3187  O   HOH A 644     1606   2860   2726    240    -80    -71       O  
HETATM 3188  O   HOH A 645     -23.235  10.941 -18.543  1.00 19.98           O  
ANISOU 3188  O   HOH A 645     1831   2042   3720   -145    282   -510       O  
HETATM 3189  O   HOH A 646       4.334  -6.668  -3.333  1.00 41.22           O  
ANISOU 3189  O   HOH A 646     5941   4423   5296    640   1167   1354       O  
HETATM 3190  O   HOH A 647      13.214  -7.471  -8.517  1.00 37.14           O  
ANISOU 3190  O   HOH A 647     4221   5282   4607    773   -993  -1858       O  
HETATM 3191  O   HOH A 648     -14.684  -4.124 -25.493  1.00 25.79           O  
ANISOU 3191  O   HOH A 648     3355   3411   3034    -20   -157     -1       O  
HETATM 3192  O   HOH A 649     -13.378  -9.121 -24.480  1.00 46.07           O  
ANISOU 3192  O   HOH A 649     5882   4822   6799   -201    132    940       O  
HETATM 3193  O   HOH A 650      13.650  -4.886  -8.505  1.00 39.68           O  
ANISOU 3193  O   HOH A 650     3499   5558   6018   1268   -984  -1195       O  
HETATM 3194  O   HOH A 651       7.334  -4.390  -3.489  1.00 25.20           O  
ANISOU 3194  O   HOH A 651     4100   3358   2118    550  -1428    294       O  
HETATM 3195  O   HOH A 652       4.331  -2.093 -33.606  1.00 58.91           O  
ANISOU 3195  O   HOH A 652     7347   9331   5706   -658   -834   1010       O  
HETATM 3196  O   HOH A 653      11.116   7.118 -27.465  1.00 49.18           O  
ANISOU 3196  O   HOH A 653     6177   6867   5641   -236   -405   -309       O  
HETATM 3197  O   HOH A 654     -27.142   4.673 -26.493  1.00 32.92           O  
ANISOU 3197  O   HOH A 654     3675   5442   3389   -460   -173     94       O  
HETATM 3198  O   HOH A 655     -11.616   1.484 -32.463  1.00 35.15           O  
ANISOU 3198  O   HOH A 655     4991   4604   3760    113   1547   -435       O  
HETATM 3199  O   HOH A 656      -4.636  13.001 -30.000  1.00 25.93           O  
ANISOU 3199  O   HOH A 656     3967   4364   1519  -1296     55     88       O  
HETATM 3200  O   HOH A 657     -16.388  18.187  -4.834  1.00 38.32           O  
ANISOU 3200  O   HOH A 657     4142   5744   4672   -595   -586    274       O  
HETATM 3201  O   HOH A 658      -2.039  13.063 -21.042  1.00 12.33           O  
ANISOU 3201  O   HOH A 658     1217   1658   1810    -99   -150    -68       O  
HETATM 3202  O   HOH A 659      -8.687  -1.860  -1.327  1.00 25.95           O  
ANISOU 3202  O   HOH A 659     4706   2789   2363   1310   1030   1072       O  
HETATM 3203  O   HOH A 660     -21.007  -0.261 -20.765  1.00 25.84           O  
ANISOU 3203  O   HOH A 660     3227   2384   4206   -745  -1398   -123       O  
HETATM 3204  O   HOH A 661     -19.064  15.080 -21.843  1.00 35.17           O  
ANISOU 3204  O   HOH A 661     4358   3404   5599    746   1385    430       O  
HETATM 3205  O   HOH A 662      -3.980   7.734 -34.171  1.00 32.90           O  
ANISOU 3205  O   HOH A 662     3291   5242   3968   -194    669   1444       O  
HETATM 3206  O   HOH A 663     -20.448  -0.232 -25.174  1.00 34.99           O  
ANISOU 3206  O   HOH A 663     4152   4038   5105   -933   -652  -2255       O  
HETATM 3207  O   HOH A 664     -11.920  -7.352 -14.120  1.00 21.63           O  
ANISOU 3207  O   HOH A 664     2813   2037   3368   -843    352   -248       O  
HETATM 3208  O   HOH A 665       1.454  12.545   1.039  1.00 39.88           O  
ANISOU 3208  O   HOH A 665     7917   4652   2584    980   -966  -1025       O  
HETATM 3209  O   HOH A 666       9.751   6.894 -25.132  1.00 39.81           O  
ANISOU 3209  O   HOH A 666     5254   5770   4100    583   -412   -785       O  
HETATM 3210  O   HOH A 667      -5.447  -9.572 -21.029  1.00 44.52           O  
ANISOU 3210  O   HOH A 667     6090   6144   4681   -896   -193    622       O  
HETATM 3211  O   HOH A 668      -8.741  16.542 -14.252  1.00  9.19           O  
ANISOU 3211  O   HOH A 668     1067   1289   1136   -159     32   -196       O  
HETATM 3212  O   HOH A 669      12.910   7.047 -21.727  1.00 13.99           O  
ANISOU 3212  O   HOH A 669     1633   1728   1955    -70    543     -4       O  
HETATM 3213  O   HOH A 670      14.085  -3.774 -16.731  1.00 25.11           O  
ANISOU 3213  O   HOH A 670     3536   2216   3789   -670    312   -596       O  
HETATM 3214  O   HOH A 671     -15.957  13.956 -10.302  1.00 17.35           O  
ANISOU 3214  O   HOH A 671     2100   1822   2668    127    359    -86       O  
HETATM 3215  O  AHOH A 672       0.049  11.235 -15.907  0.51 11.10           O  
ANISOU 3215  O  AHOH A 672      890   1723   1606    -56    -71   -362       O  
HETATM 3216  O  BHOH A 672       0.197  11.857 -16.882  0.49 13.28           O  
ANISOU 3216  O  BHOH A 672      722   1787   2538    126    108   -471       O  
HETATM 3217  O   HOH A 673      14.249   9.240 -18.790  1.00 13.69           O  
ANISOU 3217  O   HOH A 673      863   1563   2775   -286   -252    544       O  
HETATM 3218  O   HOH A 674       2.511   4.851   2.149  1.00 34.15           O  
ANISOU 3218  O   HOH A 674     6407   3716   2851  -1710     28   -560       O  
HETATM 3219  O   HOH A 675      12.383  -4.584  -4.907  1.00 49.36           O  
ANISOU 3219  O   HOH A 675     5869   6073   6811    556  -2024    272       O  
HETATM 3220  O   HOH A 676       1.991  -2.265   2.810  1.00 36.57           O  
ANISOU 3220  O   HOH A 676     4555   4053   5285  -1088    521   1788       O  
HETATM 3221  O   HOH A 677     -22.411  -2.357 -24.437  1.00 34.89           O  
ANISOU 3221  O   HOH A 677     4277   4093   4888   -166    229   -787       O  
HETATM 3222  O   HOH A 678     -10.758  17.149 -12.557  1.00 18.44           O  
ANISOU 3222  O   HOH A 678     2284   1558   3163   -180   1459     24       O  
HETATM 3223  O   HOH A 679      -7.330  -4.097 -29.813  1.00 33.15           O  
ANISOU 3223  O   HOH A 679     3888   3813   4893   1055   -167    -70       O  
HETATM 3224  O   HOH A 680      -5.769  13.427 -14.301  1.00  8.90           O  
ANISOU 3224  O   HOH A 680     1069   1108   1205    -71   -126    -57       O  
HETATM 3225  O   HOH A 681      -1.254  10.291   3.871  1.00 44.75           O  
ANISOU 3225  O   HOH A 681     5139   5598   6266   -160  -1029   -917       O  
HETATM 3226  O   HOH A 682      -8.264  -5.726 -31.257  1.00 46.20           O  
ANISOU 3226  O   HOH A 682     6396   5392   5765    792    466   -570       O  
HETATM 3227  O   HOH A 683      -0.131   5.179   2.820  1.00 36.78           O  
ANISOU 3227  O   HOH A 683     6122   4052   3799   -517    -88   -376       O  
HETATM 3228  O   HOH A 684     -17.990  10.730  -5.339  1.00 28.55           O  
ANISOU 3228  O   HOH A 684     3102   3673   4071    684   2012    390       O  
HETATM 3229  O   HOH A 685     -11.666  15.987 -27.446  1.00 24.99           O  
ANISOU 3229  O   HOH A 685     3341   2956   3197    326   -645    848       O  
HETATM 3230  O   HOH A 686     -16.433   0.255 -29.570  1.00 46.43           O  
ANISOU 3230  O   HOH A 686     5652   5988   6000    405   -392   -443       O  
HETATM 3231  O   HOH A 687      -2.192   3.288   1.813  1.00 24.65           O  
ANISOU 3231  O   HOH A 687     4943   2236   2188   -836  -1371    571       O  
HETATM 3232  O   HOH A 688     -16.715  -2.822 -26.767  1.00 34.98           O  
ANISOU 3232  O   HOH A 688     3309   3610   6372    432  -1890  -1654       O  
HETATM 3233  O   HOH A 689     -10.515  -2.017 -32.609  1.00 42.14           O  
ANISOU 3233  O   HOH A 689     4639   6956   4416    498   -231    250       O  
HETATM 3234  O   HOH A 690     -26.714   2.396 -27.708  1.00 39.48           O  
ANISOU 3234  O   HOH A 690     5420   4510   5072    757   -277   -740       O  
HETATM 3235  O   HOH A 691     -17.682  14.179  -7.987  1.00 32.76           O  
ANISOU 3235  O   HOH A 691     3254   3367   5825    781   -968   -301       O  
HETATM 3236  O   HOH A 692      -0.208  15.844 -23.529  1.00 22.97           O  
ANISOU 3236  O   HOH A 692     3686   1606   3437    -92  -1961   -214       O  
HETATM 3237  O   HOH A 693     -12.341  18.491 -14.402  1.00 36.21           O  
ANISOU 3237  O   HOH A 693     4088   3763   5906    321    619   1725       O  
HETATM 3238  O   HOH A 694     -21.515  12.266 -29.805  1.00 40.03           O  
ANISOU 3238  O   HOH A 694     4037   5118   6056   1815   -656   1218       O  
HETATM 3239  O   HOH A 695     -16.574   0.893  -5.715  1.00 34.01           O  
ANISOU 3239  O   HOH A 695     4067   3657   5198   1262    165    940       O  
HETATM 3240  O   HOH A 696      -2.124  13.488 -26.326  1.00 12.82           O  
ANISOU 3240  O   HOH A 696     1339   1590   1942   -170   -280    104       O  
HETATM 3241  O   HOH A 697     -11.020  -3.150 -30.642  1.00 42.24           O  
ANISOU 3241  O   HOH A 697     5790   4789   5470   -729   -684    941       O  
HETATM 3242  O   HOH A 698      -2.533  14.043  -0.240  1.00 35.49           O  
ANISOU 3242  O   HOH A 698     5138   3438   4907     46  -1347    555       O  
HETATM 3243  O   HOH A 699     -14.772  10.401  -1.888  1.00 28.06           O  
ANISOU 3243  O   HOH A 699     4796   3348   2516     82   1649     65       O  
HETATM 3244  O   HOH A 700      10.103  -8.987  -5.966  1.00 39.97           O  
ANISOU 3244  O   HOH A 700     4851   4218   6118   -625   -736     64       O  
HETATM 3245  O   HOH A 701     -19.738  -2.395 -19.707  1.00 32.40           O  
ANISOU 3245  O   HOH A 701     2413   3818   6078  -1059   -113  -1390       O  
HETATM 3246  O   HOH A 702     -24.541   5.561 -27.369  1.00 27.08           O  
ANISOU 3246  O   HOH A 702     2585   3894   3811   -772  -1194   -193       O  
HETATM 3247  O   HOH A 703     -18.507  15.212  -4.922  1.00 44.83           O  
ANISOU 3247  O   HOH A 703     5868   6025   5141   -607     68    441       O  
HETATM 3248  O   HOH A 704     -18.595   6.483 -30.899  1.00 22.60           O  
ANISOU 3248  O   HOH A 704     2900   3583   2105    -88   -939   -313       O  
HETATM 3249  O   HOH A 705      -4.875  15.851 -26.099  1.00 25.20           O  
ANISOU 3249  O   HOH A 705     4400   1596   3580    -27    715     92       O  
HETATM 3250  O   HOH A 706     -26.366   8.702 -13.228  1.00 13.04           O  
ANISOU 3250  O   HOH A 706     1212   1879   1865     54   -116   -198       O  
HETATM 3251  O   HOH A 707     -26.947  -1.600 -23.371  1.00 37.93           O  
ANISOU 3251  O   HOH A 707     5328   3808   5274  -1422     79    486       O  
HETATM 3252  O   HOH A 708     -16.303   8.207  -1.568  1.00 37.80           O  
ANISOU 3252  O   HOH A 708     5225   5277   3859   2089   1419    683       O  
HETATM 3253  O   HOH A 709      16.768  -3.266 -13.394  1.00 31.87           O  
ANISOU 3253  O   HOH A 709     3470   4076   4562   1735    842   1798       O  
HETATM 3254  O   HOH A 710      13.220  -4.627 -23.071  1.00 30.04           O  
ANISOU 3254  O   HOH A 710     2681   3800   4933    582   -945  -1372       O  
HETATM 3255  O   HOH A 711       1.672  12.351 -33.896  1.00 49.82           O  
ANISOU 3255  O   HOH A 711     7489   6609   4832    550    673    819       O  
HETATM 3256  O   HOH A 712      14.565   0.363  -4.315  1.00 29.61           O  
ANISOU 3256  O   HOH A 712     4562   4473   2216    589  -1082   -342       O  
HETATM 3257  O   HOH A 713     -11.775  -7.369 -27.485  1.00 31.29           O  
ANISOU 3257  O   HOH A 713     2644   6369   2876   1749   -564  -1437       O  
HETATM 3258  O   HOH A 714      -5.672  14.940   2.158  1.00 42.84           O  
ANISOU 3258  O   HOH A 714     3840   6547   5888    956    494    292       O  
HETATM 3259  O   HOH A 715      -6.009  -3.883   1.284  1.00 20.16           O  
ANISOU 3259  O   HOH A 715     2421   3668   1571    470    732    807       O  
HETATM 3260  O   HOH A 716      -2.971  13.248 -33.594  1.00 44.35           O  
ANISOU 3260  O   HOH A 716     6620   5018   5212   -597    383    414       O  
HETATM 3261  O   HOH A 717     -10.478  -2.859  -2.812  1.00 26.46           O  
ANISOU 3261  O   HOH A 717     2531   3971   3551    429   1219   1740       O  
HETATM 3262  O   HOH A 718     -23.846   0.766  -8.007  1.00 50.88           O  
ANISOU 3262  O   HOH A 718     5960   7640   5730    -70   -640    889       O  
HETATM 3263  O  AHOH A 719      -6.863  -9.030 -23.133  0.91 29.12           O  
ANISOU 3263  O  AHOH A 719     4762   1790   4511   -509    582    353       O  
HETATM 3264  O   HOH A 720     -14.797  11.224   2.402  1.00 37.17           O  
ANISOU 3264  O   HOH A 720     3076   6811   4234   1064     53  -1285       O  
HETATM 3265  O   HOH A 721     -18.373  -2.961 -22.442  1.00 39.58           O  
ANISOU 3265  O   HOH A 721     4048   5581   5409  -1423  -2075    189       O  
HETATM 3266  O   HOH A 722     -23.433  15.116 -24.421  1.00 42.95           O  
ANISOU 3266  O   HOH A 722     5317   5544   5458   1124    641   -447       O  
HETATM 3267  O   HOH A 723     -14.449   8.911   2.201  1.00 28.86           O  
ANISOU 3267  O   HOH A 723     3395   3808   3761   -717    584    546       O  
HETATM 3268  O   HOH A 724      12.132  -5.349 -17.518  1.00 30.81           O  
ANISOU 3268  O   HOH A 724     3701   5210   2795    681    363   -725       O  
HETATM 3269  O   HOH A 725      17.072  -4.535 -11.532  1.00 48.26           O  
ANISOU 3269  O   HOH A 725     7230   4794   6313    103    127     90       O  
HETATM 3270  O   HOH A 726       8.774  15.409  -4.849  1.00 39.09           O  
ANISOU 3270  O   HOH A 726     4234   5026   5591     87  -1405  -1075       O  
HETATM 3271  O   HOH A 727      17.214   0.289  -4.154  1.00 37.93           O  
ANISOU 3271  O   HOH A 727     4658   4240   5512    727    147   1381       O  
HETATM 3272  O   HOH A 728     -19.718   1.012 -27.341  1.00 30.12           O  
ANISOU 3272  O   HOH A 728     3810   3927   3705   -785  -1251   -322       O  
HETATM 3273  O   HOH A 729     -10.155  -5.304 -29.924  1.00 43.96           O  
ANISOU 3273  O   HOH A 729     4486   6281   5937   1378    773    420       O  
HETATM 3274  O   HOH A 730       4.191  19.787  -2.657  1.00 40.16           O  
ANISOU 3274  O   HOH A 730     4809   5584   4866   -199  -1196   2149       O  
HETATM 3275  O   HOH A 731       9.978   3.978 -30.866  1.00 43.72           O  
ANISOU 3275  O   HOH A 731     4790   5638   6182   1216   1534   -644       O  
HETATM 3276  O   HOH A 732     -14.339  -7.466 -26.947  1.00 40.74           O  
ANISOU 3276  O   HOH A 732     5760   5096   4622    858   -411  -1024       O  
HETATM 3277  O   HOH A 733      10.102  -5.325  -3.782  1.00 45.20           O  
ANISOU 3277  O   HOH A 733     4948   5524   6703    414   -750   1395       O  
HETATM 3278  O   HOH A 734      -3.571  -2.822 -31.846  1.00 32.58           O  
ANISOU 3278  O   HOH A 734     2817   6169   3392    625    384  -2109       O  
HETATM 3279  O   HOH A 735      -4.645  -2.732   3.492  1.00 27.19           O  
ANISOU 3279  O   HOH A 735     2957   2921   4452   -552   -518   1850       O  
HETATM 3280  O   HOH A 736      -9.089 -10.097 -24.288  1.00 27.43           O  
ANISOU 3280  O   HOH A 736     3410   2666   4345  -1139  -1319    954       O  
HETATM 3281  O   HOH A 737     -21.271  15.814 -11.057  1.00 42.13           O  
ANISOU 3281  O   HOH A 737     6163   3805   6040   -626    335  -1003       O  
HETATM 3282  O   HOH A 738       6.332  11.322 -26.941  1.00 24.36           O  
ANISOU 3282  O   HOH A 738     3310   3046   2898    868   1181   1379       O  
HETATM 3283  O   HOH A 739     -10.787 -11.060 -11.878  1.00 26.37           O  
ANISOU 3283  O   HOH A 739     2876   3156   3987   -855   1513   -976       O  
HETATM 3284  O   HOH A 740       2.124  -7.634  -0.988  1.00 42.10           O  
ANISOU 3284  O   HOH A 740     6907   4782   4308    -44   -482   1614       O  
HETATM 3285  O   HOH A 741     -12.745  -0.861 -31.755  1.00 37.94           O  
ANISOU 3285  O   HOH A 741     7144   4318   2954    -44   -805  -1068       O  
HETATM 3286  O   HOH A 742     -24.311  13.396 -19.997  1.00 45.68           O  
ANISOU 3286  O   HOH A 742     5140   6053   6163   -335    -27    261       O  
HETATM 3287  O   HOH A 743       2.027  16.089  -9.686  1.00 21.22           O  
ANISOU 3287  O   HOH A 743     2340   4035   1689    -68    350   -202       O  
HETATM 3288  O   HOH A 744     -16.790   6.277 -32.836  1.00 21.51           O  
ANISOU 3288  O   HOH A 744     2594   3254   2326   -109  -1177   -407       O  
HETATM 3289  O   HOH A 745       0.318  13.069 -19.600  1.00 13.10           O  
ANISOU 3289  O   HOH A 745     1655   1742   1579    407   -496   -302       O  
HETATM 3290  O   HOH A 746      15.112  14.099 -21.861  1.00 48.74           O  
ANISOU 3290  O   HOH A 746     5816   6925   5777    817    408    692       O  
HETATM 3291  O   HOH A 747     -18.780   7.217  -2.066  1.00 48.91           O  
ANISOU 3291  O   HOH A 747     6976   6040   5568    534    330    786       O  
HETATM 3292  O   HOH A 748      -0.386  -7.921   1.560  1.00 44.22           O  
ANISOU 3292  O   HOH A 748     5311   5714   5776    346    264   -428       O  
HETATM 3293  O   HOH A 749     -20.363  13.081  -7.831  1.00 37.33           O  
ANISOU 3293  O   HOH A 749     4094   4269   5822    905    361  -1727       O  
HETATM 3294  O   HOH A 750      -3.743  14.565   1.391  1.00 34.92           O  
ANISOU 3294  O   HOH A 750     4275   3665   5329    860   -290    541       O  
HETATM 3295  O   HOH A 751      -3.738  17.864 -27.823  1.00 39.70           O  
ANISOU 3295  O   HOH A 751     5000   4046   6039   -745    259    635       O  
HETATM 3296  O   HOH A 752     -12.312  -8.970 -12.349  1.00 37.34           O  
ANISOU 3296  O   HOH A 752     5339   3171   5676  -1654  -1402   1062       O  
HETATM 3297  O   HOH A 753     -18.306   5.163  -1.143  1.00 39.83           O  
ANISOU 3297  O   HOH A 753     5064   4996   5075    -42    342   -664       O  
HETATM 3298  O   HOH A 754     -14.356  -6.628 -15.091  1.00 39.24           O  
ANISOU 3298  O   HOH A 754     4808   5241   4861   -786    139   -838       O  
HETATM 3299  O   HOH A 755     -10.951  -5.484  -2.821  1.00 38.21           O  
ANISOU 3299  O   HOH A 755     5613   4355   4548    -20   1568   1001       O  
HETATM 3300  O   HOH A 756     -15.191   4.876   1.271  1.00 35.72           O  
ANISOU 3300  O   HOH A 756     4039   5072   4461   1004   1094   -446       O  
HETATM 3301  O   HOH A 757      -1.023  17.247 -20.650  1.00 38.39           O  
ANISOU 3301  O   HOH A 757     5944   5310   3331    352    341    747       O  
HETATM 3302  O   HOH A 758       0.374  15.705 -20.798  1.00 18.42           O  
ANISOU 3302  O   HOH A 758     1984   1757   3256    -96   -797   -352       O  
HETATM 3303  O   HOH A 759     -28.872   9.372 -21.565  1.00 19.14           O  
ANISOU 3303  O   HOH A 759     1522   2444   3306   -354    -79    551       O  
HETATM 3304  O   HOH A 760     -13.517  20.307 -14.065  1.00 41.48           O  
ANISOU 3304  O   HOH A 760     5332   4474   5953   -104   -299   -649       O  
HETATM 3305  O   HOH A 761     -19.458   0.580 -29.659  1.00 36.35           O  
ANISOU 3305  O   HOH A 761     5197   5122   3493   -520    924  -1230       O  
HETATM 3306  O   HOH A 762     -21.346   5.615 -31.549  1.00 30.29           O  
ANISOU 3306  O   HOH A 762     4150   4484   2876   -191  -1722   -891       O  
HETATM 3307  O   HOH A 763     -23.041   9.499 -30.625  1.00 40.63           O  
ANISOU 3307  O   HOH A 763     4186   6078   5174    664  -1674   1315       O  
MASTER      306    0    0    9    7    0    0    6 1663    1    0   14          
END                                                                             
HEADER    VIRAL PROTEIN                           13-APR-20   6WJI              
TITLE     2.05 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF C-TERMINAL DIMERIZATION 
TITLE    2 DOMAIN OF NUCLEOCAPSID PHOSPHOPROTEIN FROM SARS-COV-2                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SARS-COV-2 NUCLEOCAPSID PROTEIN;                           
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: C-TERMINAL DIMERIZATION DOMAIN (UNP RESIDUES 257-364);     
COMPND   5 SYNONYM: NUCLEOPROTEIN,NUCLEOCAPSID PROTEIN,PROTEIN N;               
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: MAGIC;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-11A                                   
KEYWDS    STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS     
KEYWDS   2 DISEASES, CSGID, NUCLEOCAPSID PHOSPHOPROTEIN, SARS-COV-2, VIRAL      
KEYWDS   3 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.MINASOV,L.SHUVALOVA,G.WIERSUM,K.J.F.SATCHELL,CENTER FOR STRUCTURAL  
AUTHOR   2 GENOMICS OF INFECTIOUS DISEASES (CSGID)                              
REVDAT   2   06-MAY-20 6WJI    1       COMPND SOURCE DBREF  SEQADV              
REVDAT   1   22-APR-20 6WJI    0                                                
JRNL        AUTH   G.MINASOV,L.SHUVALOVA,G.WIERSUM,K.J.F.SATCHELL               
JRNL        TITL   2.05 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF C-TERMINAL     
JRNL        TITL 2 DIMERIZATION DOMAIN OF NUCLEOCAPSID PHOSPHOPROTEIN FROM      
JRNL        TITL 3 SARS-COV-2                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0258                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 43303                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R-VALUE                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.062                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2192                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.11                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2545                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 129                          
REMARK   3   BIN FREE R VALUE                    : 0.2850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5196                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 9                                       
REMARK   3   SOLVENT ATOMS            : 622                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.65                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.16900                                              
REMARK   3    B22 (A**2) : -0.38600                                             
REMARK   3    B33 (A**2) : -0.78400                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.227         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.181         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.130         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.062         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5354 ; 0.004 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  4844 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7240 ; 1.493 ; 1.668       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11284 ; 0.394 ; 1.587       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   646 ; 2.439 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   300 ;20.429 ;22.200       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   902 ; 7.608 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ; 9.126 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   692 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6058 ; 0.053 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1186 ; 0.048 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1148 ; 0.208 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):   118 ; 0.191 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2642 ; 0.175 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   559 ; 0.132 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2596 ; 0.769 ; 1.161       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2595 ; 0.769 ; 1.161       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3238 ; 1.322 ; 1.733       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3239 ; 1.322 ; 1.733       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2758 ; 0.960 ; 1.297       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2758 ; 0.960 ; 1.297       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4002 ; 1.621 ; 1.896       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4002 ; 1.621 ; 1.896       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 24                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   257        A   263                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.2903   8.2626 -21.6174              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0848 T22:   0.0393                                     
REMARK   3      T33:   0.0614 T12:   0.0109                                     
REMARK   3      T13:  -0.0365 T23:  -0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.7264 L22:   6.8416                                     
REMARK   3      L33:   3.4834 L12:   2.4535                                     
REMARK   3      L13:   6.1927 L23:   0.1379                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1953 S12:  -0.0751 S13:   0.0807                       
REMARK   3      S21:  -0.1626 S22:   0.1163 S23:  -0.1403                       
REMARK   3      S31:  -0.0920 S32:  -0.0665 S33:   0.0791                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   264        A   281                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3561   9.8427 -11.8059              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0358 T22:   0.0171                                     
REMARK   3      T33:   0.0634 T12:   0.0068                                     
REMARK   3      T13:  -0.0294 T23:  -0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5177 L22:   3.1346                                     
REMARK   3      L33:   7.6420 L12:   0.1785                                     
REMARK   3      L13:  -2.3157 L23:  -2.6886                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0102 S12:  -0.0699 S13:   0.2092                       
REMARK   3      S21:   0.0834 S22:  -0.1134 S23:  -0.1054                       
REMARK   3      S31:  -0.4064 S32:   0.0983 S33:   0.1032                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   282        A   323                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0901   0.0499 -17.0260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0258 T22:   0.0342                                     
REMARK   3      T33:   0.0231 T12:   0.0089                                     
REMARK   3      T13:  -0.0026 T23:  -0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2638 L22:   0.9006                                     
REMARK   3      L33:   0.6971 L12:   0.6159                                     
REMARK   3      L13:   0.3278 L23:   0.3482                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0765 S12:   0.0162 S13:   0.0576                       
REMARK   3      S21:  -0.0487 S22:   0.0898 S23:  -0.0858                       
REMARK   3      S31:   0.0127 S32:   0.1163 S33:  -0.0133                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   324        A   364                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.3449  -4.6863 -11.5757              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0232 T22:   0.0425                                     
REMARK   3      T33:   0.0427 T12:   0.0154                                     
REMARK   3      T13:   0.0104 T23:  -0.0194                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9071 L22:   0.2249                                     
REMARK   3      L33:   0.2251 L12:   0.1818                                     
REMARK   3      L13:   0.0915 L23:  -0.1822                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0114 S12:  -0.0897 S13:  -0.0240                       
REMARK   3      S21:  -0.0333 S22:  -0.0249 S23:  -0.0460                       
REMARK   3      S31:   0.0366 S32:   0.0071 S33:   0.0363                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   257        B   264                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.7370 -11.6169 -27.0979              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0558 T22:   0.1024                                     
REMARK   3      T33:   0.1451 T12:   0.0030                                     
REMARK   3      T13:   0.0074 T23:   0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2682 L22:   1.6317                                     
REMARK   3      L33:   5.8233 L12:   3.1206                                     
REMARK   3      L13:   3.5799 L23:   1.8208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1328 S12:   0.4330 S13:  -0.1981                       
REMARK   3      S21:  -0.0901 S22:   0.1062 S23:  -0.3002                       
REMARK   3      S31:  -0.1421 S32:   0.3892 S33:   0.0266                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   265        B   300                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.2559 -14.7106 -28.9637              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0498 T22:   0.0202                                     
REMARK   3      T33:   0.0429 T12:  -0.0177                                     
REMARK   3      T13:  -0.0002 T23:  -0.0196                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8580 L22:   3.4089                                     
REMARK   3      L33:   5.0009 L12:  -0.6843                                     
REMARK   3      L13:  -0.6698 L23:   0.1509                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0409 S12:   0.1566 S13:  -0.1520                       
REMARK   3      S21:  -0.1079 S22:  -0.0276 S23:   0.1394                       
REMARK   3      S31:   0.2837 S32:  -0.1700 S33:  -0.0133                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   301        B   323                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.1545  -1.6159 -19.6155              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0893 T22:   0.0707                                     
REMARK   3      T33:   0.1036 T12:   0.0025                                     
REMARK   3      T13:  -0.0119 T23:  -0.0084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9563 L22:   0.0182                                     
REMARK   3      L33:   3.2311 L12:   0.0719                                     
REMARK   3      L13:   2.1225 L23:   0.1892                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0934 S12:  -0.0022 S13:   0.0289                       
REMARK   3      S21:  -0.0103 S22:  -0.0025 S23:  -0.0098                       
REMARK   3      S31:   0.0934 S32:  -0.0599 S33:  -0.0909                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   324        B   364                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.5867  -6.0713 -19.8922              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0376 T22:   0.0356                                     
REMARK   3      T33:   0.0156 T12:  -0.0109                                     
REMARK   3      T13:   0.0213 T23:  -0.0110                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4468 L22:   1.3317                                     
REMARK   3      L33:   1.2903 L12:  -0.4171                                     
REMARK   3      L13:   0.7343 L23:  -0.5726                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0235 S12:   0.0365 S13:  -0.0065                       
REMARK   3      S21:   0.0946 S22:   0.0053 S23:   0.0743                       
REMARK   3      S31:  -0.0485 S32:  -0.0958 S33:   0.0182                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   257        C   264                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.4770  -6.2964 -51.6339              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0558 T22:   0.0348                                     
REMARK   3      T33:   0.0712 T12:  -0.0132                                     
REMARK   3      T13:  -0.0192 T23:  -0.0117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2198 L22:   6.5865                                     
REMARK   3      L33:   3.3441 L12:  -2.6358                                     
REMARK   3      L13:   4.8646 L23:  -2.2491                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3448 S12:  -0.2570 S13:   0.2881                       
REMARK   3      S21:   0.3192 S22:   0.1671 S23:  -0.2470                       
REMARK   3      S31:  -0.2684 S32:  -0.1618 S33:   0.1777                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   265        C   282                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.7685  -5.0337 -61.7862              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0398 T22:   0.0375                                     
REMARK   3      T33:   0.0729 T12:   0.0036                                     
REMARK   3      T13:  -0.0169 T23:   0.0231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6272 L22:   4.7724                                     
REMARK   3      L33:   6.4912 L12:  -0.6056                                     
REMARK   3      L13:  -1.5794 L23:   4.4424                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0215 S12:   0.1353 S13:   0.3253                       
REMARK   3      S21:  -0.0655 S22:  -0.0136 S23:  -0.0594                       
REMARK   3      S31:  -0.2187 S32:  -0.1370 S33:   0.0351                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   283        C   323                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.4010 -14.5419 -56.0822              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0423 T22:   0.0302                                     
REMARK   3      T33:   0.0163 T12:  -0.0151                                     
REMARK   3      T13:   0.0034 T23:  -0.0058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1204 L22:   0.9567                                     
REMARK   3      L33:   0.8413 L12:  -0.7980                                     
REMARK   3      L13:   0.0426 L23:  -0.0089                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0230 S12:  -0.0505 S13:  -0.0152                       
REMARK   3      S21:  -0.0056 S22:   0.0312 S23:   0.0976                       
REMARK   3      S31:  -0.0644 S32:  -0.0589 S33:  -0.0083                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   324        C   364                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.3686 -19.2144 -61.6937              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0622 T22:   0.0538                                     
REMARK   3      T33:   0.0294 T12:  -0.0149                                     
REMARK   3      T13:   0.0187 T23:  -0.0089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0941 L22:   0.4013                                     
REMARK   3      L33:   0.3567 L12:  -0.4564                                     
REMARK   3      L13:  -0.2083 L23:  -0.1604                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0285 S12:  -0.0212 S13:  -0.0576                       
REMARK   3      S21:  -0.0294 S22:  -0.0329 S23:   0.0003                       
REMARK   3      S31:   0.0745 S32:   0.0248 S33:   0.0614                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   257        D   274                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.7200 -28.7379 -43.6549              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0559 T22:   0.0463                                     
REMARK   3      T33:   0.0401 T12:  -0.0254                                     
REMARK   3      T13:   0.0243 T23:   0.0136                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1122 L22:   1.6039                                     
REMARK   3      L33:   7.7720 L12:  -1.7537                                     
REMARK   3      L13:   4.0277 L23:  -0.8183                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0753 S12:  -0.3133 S13:  -0.1461                       
REMARK   3      S21:   0.1501 S22:   0.0186 S23:   0.0581                       
REMARK   3      S31:   0.0775 S32:  -0.2201 S33:   0.0567                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   275        D   299                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9920 -29.7494 -46.8418              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0248 T22:   0.0108                                     
REMARK   3      T33:   0.0277 T12:   0.0118                                     
REMARK   3      T13:   0.0096 T23:   0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1663 L22:   3.0815                                     
REMARK   3      L33:   7.8787 L12:  -0.4822                                     
REMARK   3      L13:  -1.0107 L23:   3.3428                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0451 S12:  -0.0793 S13:  -0.1602                       
REMARK   3      S21:   0.0841 S22:   0.0060 S23:  -0.0421                       
REMARK   3      S31:   0.1850 S32:   0.1409 S33:   0.0391                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   300        D   340                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.5780 -18.8407 -55.9850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0478 T22:   0.0234                                     
REMARK   3      T33:   0.0222 T12:   0.0136                                     
REMARK   3      T13:   0.0112 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3692 L22:   0.4529                                     
REMARK   3      L33:   1.1516 L12:   0.2189                                     
REMARK   3      L13:   0.6228 L23:   0.5178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0244 S12:   0.0350 S13:   0.0056                       
REMARK   3      S21:   0.0511 S22:  -0.0155 S23:  -0.0260                       
REMARK   3      S31:   0.0049 S32:   0.0552 S33:   0.0398                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   341        D   364                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.4779 -19.7232 -49.1742              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0192 T22:   0.0501                                     
REMARK   3      T33:   0.0081 T12:   0.0021                                     
REMARK   3      T13:  -0.0040 T23:  -0.0038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4539 L22:  11.9459                                     
REMARK   3      L33:   0.6627 L12:   1.0324                                     
REMARK   3      L13:   0.0382 L23:   1.8010                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0320 S12:  -0.0965 S13:   0.0064                       
REMARK   3      S21:   0.0432 S22:   0.0787 S23:  -0.2667                       
REMARK   3      S31:   0.0178 S32:   0.1447 S33:  -0.0467                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   257        E   269                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3833  11.1670 -38.1668              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0577 T22:   0.0647                                     
REMARK   3      T33:   0.0343 T12:   0.0299                                     
REMARK   3      T13:  -0.0186 T23:   0.0190                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3026 L22:   6.1938                                     
REMARK   3      L33:   5.3403 L12:   5.9279                                     
REMARK   3      L13:  -3.7576 L23:  -4.9028                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0773 S12:   0.0390 S13:  -0.1249                       
REMARK   3      S21:  -0.0079 S22:   0.0103 S23:  -0.1265                       
REMARK   3      S31:  -0.0361 S32:   0.0669 S33:   0.0670                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   270        E   281                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.3749  20.2460 -34.9388              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1236 T22:   0.0831                                     
REMARK   3      T33:   0.0177 T12:   0.0070                                     
REMARK   3      T13:   0.0035 T23:  -0.0174                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2062 L22:   5.5240                                     
REMARK   3      L33:   3.9466 L12:  -1.7003                                     
REMARK   3      L13:   2.1110 L23:  -1.6736                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0449 S12:  -0.6093 S13:   0.2024                       
REMARK   3      S21:   0.3928 S22:  -0.1074 S23:  -0.0429                       
REMARK   3      S31:  -0.5126 S32:  -0.2090 S33:   0.1523                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   282        E   323                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.3211  15.1150 -45.9375              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0321 T22:   0.0297                                     
REMARK   3      T33:   0.0270 T12:   0.0186                                     
REMARK   3      T13:  -0.0010 T23:   0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3933 L22:   1.0754                                     
REMARK   3      L33:   2.0512 L12:   0.4469                                     
REMARK   3      L13:  -0.5217 L23:  -1.0514                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0070 S12:  -0.0173 S13:  -0.0690                       
REMARK   3      S21:   0.0326 S22:   0.0492 S23:   0.0590                       
REMARK   3      S31:  -0.0398 S32:  -0.1270 S33:  -0.0562                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   324        E   364                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.9741  19.1099 -47.8171              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0814 T22:   0.0752                                     
REMARK   3      T33:   0.0633 T12:   0.0521                                     
REMARK   3      T13:   0.0100 T23:   0.0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2451 L22:   2.1555                                     
REMARK   3      L33:   1.7998 L12:   1.5753                                     
REMARK   3      L13:   0.5068 L23:   0.5290                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0445 S12:   0.0157 S13:  -0.0295                       
REMARK   3      S21:  -0.0490 S22:   0.0577 S23:   0.0849                       
REMARK   3      S31:  -0.0677 S32:  -0.2559 S33:  -0.0132                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   257        F   274                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.6948  14.9737 -64.1329              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0470 T22:   0.0352                                     
REMARK   3      T33:   0.0198 T12:  -0.0097                                     
REMARK   3      T13:  -0.0159 T23:  -0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7749 L22:   1.8637                                     
REMARK   3      L33:   3.8963 L12:   1.6614                                     
REMARK   3      L13:  -2.7318 L23:  -1.8680                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1174 S12:   0.1133 S13:  -0.1510                       
REMARK   3      S21:  -0.2770 S22:   0.0734 S23:   0.0459                       
REMARK   3      S31:   0.1899 S32:   0.0382 S33:   0.0441                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   275        F   288                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.4754  28.8114 -61.6919              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0778 T22:   0.0788                                     
REMARK   3      T33:   0.0613 T12:  -0.0101                                     
REMARK   3      T13:  -0.0125 T23:   0.0148                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0727 L22:   6.6719                                     
REMARK   3      L33:   1.9670 L12:  -2.2555                                     
REMARK   3      L13:   2.3390 L23:   0.0712                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1495 S12:  -0.1939 S13:   0.1196                       
REMARK   3      S21:  -0.2087 S22:   0.0435 S23:   0.3818                       
REMARK   3      S31:  -0.2317 S32:  -0.2082 S33:   0.1060                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   289        F   340                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.5971  20.4746 -52.8708              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0493 T22:   0.0234                                     
REMARK   3      T33:   0.0359 T12:   0.0061                                     
REMARK   3      T13:  -0.0090 T23:   0.0147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9468 L22:   0.6036                                     
REMARK   3      L33:   1.0239 L12:  -0.0638                                     
REMARK   3      L13:  -0.2579 L23:  -0.0437                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0487 S12:   0.0096 S13:   0.0030                       
REMARK   3      S21:   0.0582 S22:   0.0442 S23:  -0.0802                       
REMARK   3      S31:  -0.0125 S32:   0.0468 S33:   0.0045                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   341        F   364                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0247  28.4180 -52.1573              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0456 T22:   0.0268                                     
REMARK   3      T33:   0.0719 T12:  -0.0065                                     
REMARK   3      T13:  -0.0089 T23:  -0.0319                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0749 L22:   1.9041                                     
REMARK   3      L33:   9.8101 L12:  -2.0211                                     
REMARK   3      L13:   3.8628 L23:  -4.2196                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1881 S12:  -0.1294 S13:   0.1790                       
REMARK   3      S21:   0.0983 S22:   0.0340 S23:  -0.1114                       
REMARK   3      S31:  -0.1777 S32:   0.0138 S33:   0.1541                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR        
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 6WJI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000248437.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-APR-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : DIAMOND(111)                       
REMARK 200  OPTICS                         : BE                                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43336                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.17100                            
REMARK 200  R SYM                      (I) : 0.17100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.63000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2CJR                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20.0 MG/ML PROTEIN IN 0.1 M SODIUM       
REMARK 280  CHLORIDE, 0.01 M TRIS, PH 8.3 AGAINST CLASSICS II SCREEN D8 (0.1    
REMARK 280  M HEPES, PH 7.5, 25% W/V PEG3350), VAPOR DIFFUSION, SITTING DROP,   
REMARK 280  TEMPERATURE 292K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       21.80600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.31650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.15850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.31650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.80600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.15850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   244                                                      
REMARK 465     ASN A   245                                                      
REMARK 465     ALA A   246                                                      
REMARK 465     THR A   247                                                      
REMARK 465     LYS A   248                                                      
REMARK 465     LYS A   249                                                      
REMARK 465     SER A   250                                                      
REMARK 465     ALA A   251                                                      
REMARK 465     ALA A   252                                                      
REMARK 465     GLU A   253                                                      
REMARK 465     ALA A   254                                                      
REMARK 465     SER A   255                                                      
REMARK 465     LYS A   256                                                      
REMARK 465     SER B   244                                                      
REMARK 465     ASN B   245                                                      
REMARK 465     ALA B   246                                                      
REMARK 465     THR B   247                                                      
REMARK 465     LYS B   248                                                      
REMARK 465     LYS B   249                                                      
REMARK 465     SER B   250                                                      
REMARK 465     ALA B   251                                                      
REMARK 465     ALA B   252                                                      
REMARK 465     GLU B   253                                                      
REMARK 465     ALA B   254                                                      
REMARK 465     SER B   255                                                      
REMARK 465     LYS B   256                                                      
REMARK 465     SER C   244                                                      
REMARK 465     ASN C   245                                                      
REMARK 465     ALA C   246                                                      
REMARK 465     THR C   247                                                      
REMARK 465     LYS C   248                                                      
REMARK 465     LYS C   249                                                      
REMARK 465     SER C   250                                                      
REMARK 465     ALA C   251                                                      
REMARK 465     ALA C   252                                                      
REMARK 465     GLU C   253                                                      
REMARK 465     ALA C   254                                                      
REMARK 465     SER C   255                                                      
REMARK 465     LYS C   256                                                      
REMARK 465     SER D   244                                                      
REMARK 465     ASN D   245                                                      
REMARK 465     ALA D   246                                                      
REMARK 465     THR D   247                                                      
REMARK 465     LYS D   248                                                      
REMARK 465     LYS D   249                                                      
REMARK 465     SER D   250                                                      
REMARK 465     ALA D   251                                                      
REMARK 465     ALA D   252                                                      
REMARK 465     GLU D   253                                                      
REMARK 465     ALA D   254                                                      
REMARK 465     SER D   255                                                      
REMARK 465     LYS D   256                                                      
REMARK 465     SER E   244                                                      
REMARK 465     ASN E   245                                                      
REMARK 465     ALA E   246                                                      
REMARK 465     THR E   247                                                      
REMARK 465     LYS E   248                                                      
REMARK 465     LYS E   249                                                      
REMARK 465     SER E   250                                                      
REMARK 465     ALA E   251                                                      
REMARK 465     ALA E   252                                                      
REMARK 465     GLU E   253                                                      
REMARK 465     ALA E   254                                                      
REMARK 465     SER E   255                                                      
REMARK 465     LYS E   256                                                      
REMARK 465     SER F   244                                                      
REMARK 465     ASN F   245                                                      
REMARK 465     ALA F   246                                                      
REMARK 465     THR F   247                                                      
REMARK 465     LYS F   248                                                      
REMARK 465     LYS F   249                                                      
REMARK 465     SER F   250                                                      
REMARK 465     ALA F   251                                                      
REMARK 465     ALA F   252                                                      
REMARK 465     GLU F   253                                                      
REMARK 465     ALA F   254                                                      
REMARK 465     SER F   255                                                      
REMARK 465     LYS F   256                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR B 268       80.09   -155.41                                   
REMARK 500    TYR E 268       79.90   -166.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: IDP51003.402   RELATED DB: TARGETTRACK                   
DBREF  6WJI A  257   364  UNP    P0DTC9   NCAP_SARS2     257    364             
DBREF  6WJI B  257   364  UNP    P0DTC9   NCAP_SARS2     257    364             
DBREF  6WJI C  257   364  UNP    P0DTC9   NCAP_SARS2     257    364             
DBREF  6WJI D  257   364  UNP    P0DTC9   NCAP_SARS2     257    364             
DBREF  6WJI E  257   364  UNP    P0DTC9   NCAP_SARS2     257    364             
DBREF  6WJI F  257   364  UNP    P0DTC9   NCAP_SARS2     257    364             
SEQADV 6WJI SER A  244  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ASN A  245  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA A  246  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI THR A  247  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS A  248  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS A  249  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER A  250  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA A  251  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA A  252  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI GLU A  253  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA A  254  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER A  255  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS A  256  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER B  244  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ASN B  245  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA B  246  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI THR B  247  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS B  248  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS B  249  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER B  250  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA B  251  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA B  252  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI GLU B  253  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA B  254  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER B  255  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS B  256  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER C  244  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ASN C  245  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA C  246  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI THR C  247  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS C  248  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS C  249  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER C  250  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA C  251  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA C  252  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI GLU C  253  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA C  254  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER C  255  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS C  256  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER D  244  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ASN D  245  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA D  246  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI THR D  247  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS D  248  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS D  249  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER D  250  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA D  251  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA D  252  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI GLU D  253  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA D  254  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER D  255  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS D  256  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER E  244  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ASN E  245  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA E  246  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI THR E  247  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS E  248  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS E  249  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER E  250  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA E  251  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA E  252  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI GLU E  253  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA E  254  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER E  255  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS E  256  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER F  244  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ASN F  245  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA F  246  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI THR F  247  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS F  248  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS F  249  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER F  250  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA F  251  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA F  252  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI GLU F  253  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI ALA F  254  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI SER F  255  UNP  P0DTC9              EXPRESSION TAG                 
SEQADV 6WJI LYS F  256  UNP  P0DTC9              EXPRESSION TAG                 
SEQRES   1 A  121  SER ASN ALA THR LYS LYS SER ALA ALA GLU ALA SER LYS          
SEQRES   2 A  121  LYS PRO ARG GLN LYS ARG THR ALA THR LYS ALA TYR ASN          
SEQRES   3 A  121  VAL THR GLN ALA PHE GLY ARG ARG GLY PRO GLU GLN THR          
SEQRES   4 A  121  GLN GLY ASN PHE GLY ASP GLN GLU LEU ILE ARG GLN GLY          
SEQRES   5 A  121  THR ASP TYR LYS HIS TRP PRO GLN ILE ALA GLN PHE ALA          
SEQRES   6 A  121  PRO SER ALA SER ALA PHE PHE GLY MET SER ARG ILE GLY          
SEQRES   7 A  121  MET GLU VAL THR PRO SER GLY THR TRP LEU THR TYR THR          
SEQRES   8 A  121  GLY ALA ILE LYS LEU ASP ASP LYS ASP PRO ASN PHE LYS          
SEQRES   9 A  121  ASP GLN VAL ILE LEU LEU ASN LYS HIS ILE ASP ALA TYR          
SEQRES  10 A  121  LYS THR PHE PRO                                              
SEQRES   1 B  121  SER ASN ALA THR LYS LYS SER ALA ALA GLU ALA SER LYS          
SEQRES   2 B  121  LYS PRO ARG GLN LYS ARG THR ALA THR LYS ALA TYR ASN          
SEQRES   3 B  121  VAL THR GLN ALA PHE GLY ARG ARG GLY PRO GLU GLN THR          
SEQRES   4 B  121  GLN GLY ASN PHE GLY ASP GLN GLU LEU ILE ARG GLN GLY          
SEQRES   5 B  121  THR ASP TYR LYS HIS TRP PRO GLN ILE ALA GLN PHE ALA          
SEQRES   6 B  121  PRO SER ALA SER ALA PHE PHE GLY MET SER ARG ILE GLY          
SEQRES   7 B  121  MET GLU VAL THR PRO SER GLY THR TRP LEU THR TYR THR          
SEQRES   8 B  121  GLY ALA ILE LYS LEU ASP ASP LYS ASP PRO ASN PHE LYS          
SEQRES   9 B  121  ASP GLN VAL ILE LEU LEU ASN LYS HIS ILE ASP ALA TYR          
SEQRES  10 B  121  LYS THR PHE PRO                                              
SEQRES   1 C  121  SER ASN ALA THR LYS LYS SER ALA ALA GLU ALA SER LYS          
SEQRES   2 C  121  LYS PRO ARG GLN LYS ARG THR ALA THR LYS ALA TYR ASN          
SEQRES   3 C  121  VAL THR GLN ALA PHE GLY ARG ARG GLY PRO GLU GLN THR          
SEQRES   4 C  121  GLN GLY ASN PHE GLY ASP GLN GLU LEU ILE ARG GLN GLY          
SEQRES   5 C  121  THR ASP TYR LYS HIS TRP PRO GLN ILE ALA GLN PHE ALA          
SEQRES   6 C  121  PRO SER ALA SER ALA PHE PHE GLY MET SER ARG ILE GLY          
SEQRES   7 C  121  MET GLU VAL THR PRO SER GLY THR TRP LEU THR TYR THR          
SEQRES   8 C  121  GLY ALA ILE LYS LEU ASP ASP LYS ASP PRO ASN PHE LYS          
SEQRES   9 C  121  ASP GLN VAL ILE LEU LEU ASN LYS HIS ILE ASP ALA TYR          
SEQRES  10 C  121  LYS THR PHE PRO                                              
SEQRES   1 D  121  SER ASN ALA THR LYS LYS SER ALA ALA GLU ALA SER LYS          
SEQRES   2 D  121  LYS PRO ARG GLN LYS ARG THR ALA THR LYS ALA TYR ASN          
SEQRES   3 D  121  VAL THR GLN ALA PHE GLY ARG ARG GLY PRO GLU GLN THR          
SEQRES   4 D  121  GLN GLY ASN PHE GLY ASP GLN GLU LEU ILE ARG GLN GLY          
SEQRES   5 D  121  THR ASP TYR LYS HIS TRP PRO GLN ILE ALA GLN PHE ALA          
SEQRES   6 D  121  PRO SER ALA SER ALA PHE PHE GLY MET SER ARG ILE GLY          
SEQRES   7 D  121  MET GLU VAL THR PRO SER GLY THR TRP LEU THR TYR THR          
SEQRES   8 D  121  GLY ALA ILE LYS LEU ASP ASP LYS ASP PRO ASN PHE LYS          
SEQRES   9 D  121  ASP GLN VAL ILE LEU LEU ASN LYS HIS ILE ASP ALA TYR          
SEQRES  10 D  121  LYS THR PHE PRO                                              
SEQRES   1 E  121  SER ASN ALA THR LYS LYS SER ALA ALA GLU ALA SER LYS          
SEQRES   2 E  121  LYS PRO ARG GLN LYS ARG THR ALA THR LYS ALA TYR ASN          
SEQRES   3 E  121  VAL THR GLN ALA PHE GLY ARG ARG GLY PRO GLU GLN THR          
SEQRES   4 E  121  GLN GLY ASN PHE GLY ASP GLN GLU LEU ILE ARG GLN GLY          
SEQRES   5 E  121  THR ASP TYR LYS HIS TRP PRO GLN ILE ALA GLN PHE ALA          
SEQRES   6 E  121  PRO SER ALA SER ALA PHE PHE GLY MET SER ARG ILE GLY          
SEQRES   7 E  121  MET GLU VAL THR PRO SER GLY THR TRP LEU THR TYR THR          
SEQRES   8 E  121  GLY ALA ILE LYS LEU ASP ASP LYS ASP PRO ASN PHE LYS          
SEQRES   9 E  121  ASP GLN VAL ILE LEU LEU ASN LYS HIS ILE ASP ALA TYR          
SEQRES  10 E  121  LYS THR PHE PRO                                              
SEQRES   1 F  121  SER ASN ALA THR LYS LYS SER ALA ALA GLU ALA SER LYS          
SEQRES   2 F  121  LYS PRO ARG GLN LYS ARG THR ALA THR LYS ALA TYR ASN          
SEQRES   3 F  121  VAL THR GLN ALA PHE GLY ARG ARG GLY PRO GLU GLN THR          
SEQRES   4 F  121  GLN GLY ASN PHE GLY ASP GLN GLU LEU ILE ARG GLN GLY          
SEQRES   5 F  121  THR ASP TYR LYS HIS TRP PRO GLN ILE ALA GLN PHE ALA          
SEQRES   6 F  121  PRO SER ALA SER ALA PHE PHE GLY MET SER ARG ILE GLY          
SEQRES   7 F  121  MET GLU VAL THR PRO SER GLY THR TRP LEU THR TYR THR          
SEQRES   8 F  121  GLY ALA ILE LYS LEU ASP ASP LYS ASP PRO ASN PHE LYS          
SEQRES   9 F  121  ASP GLN VAL ILE LEU LEU ASN LYS HIS ILE ASP ALA TYR          
SEQRES  10 F  121  LYS THR PHE PRO                                              
HET     CL  A 401       1                                                       
HET     CL  B 401       2                                                       
HET     CL  C 401       1                                                       
HET     CL  D 401       1                                                       
HET     CL  D 402       2                                                       
HET     CL  E 401       2                                                       
HET     CL  E 402       1                                                       
HET     CL  F 401       2                                                       
HET     CL  F 402       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   7   CL    9(CL 1-)                                                     
FORMUL  16  HOH   *622(H2 O)                                                    
HELIX    1 AA1 PRO A  258  ARG A  262  5                                   5    
HELIX    2 AA2 ASN A  269  GLY A  275  1                                   7    
HELIX    3 AA3 ASP A  288  GLY A  295  1                                   8    
HELIX    4 AA4 THR A  296  TYR A  298  5                                   3    
HELIX    5 AA5 TRP A  301  GLN A  306  1                                   6    
HELIX    6 AA6 SER A  310  SER A  318  1                                   9    
HELIX    7 AA7 ASN A  345  ILE A  357  1                                  13    
HELIX    8 AA8 ASP A  358  PHE A  363  5                                   6    
HELIX    9 AA9 PRO B  258  ARG B  262  5                                   5    
HELIX   10 AB1 ASN B  269  GLY B  275  1                                   7    
HELIX   11 AB2 ASP B  288  GLY B  295  1                                   8    
HELIX   12 AB3 THR B  296  TYR B  298  5                                   3    
HELIX   13 AB4 HIS B  300  GLN B  306  1                                   7    
HELIX   14 AB5 SER B  310  SER B  318  1                                   9    
HELIX   15 AB6 ASN B  345  ILE B  357  1                                  13    
HELIX   16 AB7 ASP B  358  PHE B  363  5                                   6    
HELIX   17 AB8 PRO C  258  ARG C  262  5                                   5    
HELIX   18 AB9 ASN C  269  GLY C  275  1                                   7    
HELIX   19 AC1 ASP C  288  GLY C  295  1                                   8    
HELIX   20 AC2 THR C  296  TYR C  298  5                                   3    
HELIX   21 AC3 HIS C  300  GLN C  306  1                                   7    
HELIX   22 AC4 SER C  310  SER C  318  1                                   9    
HELIX   23 AC5 ASN C  345  ILE C  357  1                                  13    
HELIX   24 AC6 ASP C  358  PHE C  363  5                                   6    
HELIX   25 AC7 PRO D  258  ARG D  262  5                                   5    
HELIX   26 AC8 ASN D  269  GLY D  275  1                                   7    
HELIX   27 AC9 ASP D  288  GLY D  295  1                                   8    
HELIX   28 AD1 THR D  296  TYR D  298  5                                   3    
HELIX   29 AD2 HIS D  300  GLN D  306  1                                   7    
HELIX   30 AD3 SER D  310  SER D  318  1                                   9    
HELIX   31 AD4 ASN D  345  ILE D  357  1                                  13    
HELIX   32 AD5 ASP D  358  PHE D  363  5                                   6    
HELIX   33 AD6 PRO E  258  ARG E  262  5                                   5    
HELIX   34 AD7 ASN E  269  GLY E  275  1                                   7    
HELIX   35 AD8 ASP E  288  GLY E  295  1                                   8    
HELIX   36 AD9 THR E  296  TYR E  298  5                                   3    
HELIX   37 AE1 HIS E  300  GLN E  306  1                                   7    
HELIX   38 AE2 SER E  310  SER E  318  1                                   9    
HELIX   39 AE3 ASN E  345  ILE E  357  1                                  13    
HELIX   40 AE4 ASP E  358  PHE E  363  5                                   6    
HELIX   41 AE5 PRO F  258  ARG F  262  5                                   5    
HELIX   42 AE6 ASN F  269  GLY F  275  1                                   7    
HELIX   43 AE7 ASP F  288  GLY F  295  1                                   8    
HELIX   44 AE8 THR F  296  TYR F  298  5                                   3    
HELIX   45 AE9 HIS F  300  GLN F  306  1                                   7    
HELIX   46 AF1 SER F  310  SER F  318  1                                   9    
HELIX   47 AF2 ASN F  345  ILE F  357  1                                  13    
HELIX   48 AF3 ASP F  358  PHE F  363  5                                   6    
SHEET    1 AA1 4 ARG A 319  THR A 325  0                                        
SHEET    2 AA1 4 GLY A 328  LYS A 338 -1  O  TRP A 330   N  GLU A 323           
SHEET    3 AA1 4 GLY B 328  LYS B 338 -1  O  ILE B 337   N  LEU A 331           
SHEET    4 AA1 4 ARG B 319  THR B 325 -1  N  THR B 325   O  GLY B 328           
SHEET    1 AA2 4 ARG C 319  THR C 325  0                                        
SHEET    2 AA2 4 GLY C 328  LYS C 338 -1  O  TRP C 330   N  GLU C 323           
SHEET    3 AA2 4 GLY D 328  LYS D 338 -1  O  LEU D 331   N  ILE C 337           
SHEET    4 AA2 4 ARG D 319  THR D 325 -1  N  THR D 325   O  GLY D 328           
SHEET    1 AA3 4 ARG E 319  THR E 325  0                                        
SHEET    2 AA3 4 GLY E 328  LYS E 338 -1  O  TRP E 330   N  GLU E 323           
SHEET    3 AA3 4 GLY F 328  LYS F 338 -1  O  LEU F 331   N  ILE E 337           
SHEET    4 AA3 4 ARG F 319  THR F 325 -1  N  GLU F 323   O  TRP F 330           
CRYST1   43.612  122.317  130.633  90.00  90.00  90.00 P 21 21 21   24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022929  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008175  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007655        0.00000                         
ATOM      1  N   LYS A 257      -3.431  13.681 -23.213  1.00 37.87           N  
ANISOU    1  N   LYS A 257     4940   3880   5570    140  -1400   -140       N  
ATOM      2  CA  LYS A 257      -2.944  12.371 -23.737  1.00 36.12           C  
ANISOU    2  CA  LYS A 257     4850   3890   4980      0  -1090     10       C  
ATOM      3  C   LYS A 257      -3.130  11.296 -22.669  1.00 30.48           C  
ANISOU    3  C   LYS A 257     4070   3390   4130    160   -830   -170       C  
ATOM      4  O   LYS A 257      -2.763  11.500 -21.514  1.00 31.14           O  
ANISOU    4  O   LYS A 257     4070   3540   4220    280   -790   -330       O  
ATOM      5  CB  LYS A 257      -1.477  12.474 -24.162  1.00 39.68           C  
ANISOU    5  CB  LYS A 257     5370   4390   5320   -160  -1020    170       C  
ATOM      6  CG  LYS A 257      -0.920  11.232 -24.843  1.00 40.62           C  
ANISOU    6  CG  LYS A 257     5560   4740   5130   -260   -730    200       C  
ATOM      7  CD  LYS A 257       0.470  11.438 -25.395  1.00 45.05           C  
ANISOU    7  CD  LYS A 257     6100   5420   5600   -430   -620    330       C  
ATOM      8  CE  LYS A 257       0.942  10.278 -26.244  1.00 48.41           C  
ANISOU    8  CE  LYS A 257     6540   6110   5740   -500   -340    240       C  
ATOM      9  NZ  LYS A 257       2.289  10.535 -26.806  1.00 52.65           N  
ANISOU    9  NZ  LYS A 257     6970   6860   6170   -680   -180    330       N  
ATOM     10  N   PRO A 258      -3.718  10.126 -23.011  1.00 26.29           N  
ANISOU   10  N   PRO A 258     3570   2950   3470    120   -700   -110       N  
ATOM     11  CA  PRO A 258      -3.934   9.057 -22.033  1.00 23.84           C  
ANISOU   11  CA  PRO A 258     3170   2820   3060    180   -540   -150       C  
ATOM     12  C   PRO A 258      -2.660   8.725 -21.236  1.00 20.81           C  
ANISOU   12  C   PRO A 258     2800   2510   2600    190   -450   -160       C  
ATOM     13  O   PRO A 258      -1.588   8.696 -21.808  1.00 19.26           O  
ANISOU   13  O   PRO A 258     2680   2230   2410    130   -430   -130       O  
ATOM     14  CB  PRO A 258      -4.411   7.882 -22.897  1.00 24.07           C  
ANISOU   14  CB  PRO A 258     3270   2820   3060     80   -540    -40       C  
ATOM     15  CG  PRO A 258      -5.089   8.557 -24.070  1.00 25.59           C  
ANISOU   15  CG  PRO A 258     3540   2870   3310     20   -710     10       C  
ATOM     16  CD  PRO A 258      -4.235   9.776 -24.343  1.00 26.44           C  
ANISOU   16  CD  PRO A 258     3710   2910   3430    -20   -780     20       C  
ATOM     17  N   ARG A 259      -2.831   8.495 -19.935  1.00 19.87           N  
ANISOU   17  N   ARG A 259     2570   2580   2400    230   -400   -200       N  
ATOM     18  CA  ARG A 259      -1.718   8.188 -18.997  1.00 19.18           C  
ANISOU   18  CA  ARG A 259     2490   2560   2240    220   -390   -180       C  
ATOM     19  C   ARG A 259      -0.906   6.988 -19.493  1.00 17.12           C  
ANISOU   19  C   ARG A 259     2270   2150   2080    130   -400    -40       C  
ATOM     20  O   ARG A 259       0.331   7.047 -19.401  1.00 16.92           O  
ANISOU   20  O   ARG A 259     2260   2020   2140    130   -420    -60       O  
ATOM     21  CB  ARG A 259      -2.291   7.938 -17.596  1.00 21.82           C  
ANISOU   21  CB  ARG A 259     2710   3230   2350    200   -350   -170       C  
ATOM     22  CG  ARG A 259      -1.249   7.688 -16.509  1.00 24.05           C  
ANISOU   22  CG  ARG A 259     3020   3610   2510    140   -420   -110       C  
ATOM     23  CD  ARG A 259      -1.893   7.703 -15.132  1.00 27.56           C  
ANISOU   23  CD  ARG A 259     3360   4530   2580     80   -360   -140       C  
ATOM     24  NE  ARG A 259      -0.973   7.538 -14.011  1.00 30.21           N  
ANISOU   24  NE  ARG A 259     3750   5010   2720    -20   -480    -60       N  
ATOM     25  CZ  ARG A 259      -0.774   6.411 -13.323  1.00 32.24           C  
ANISOU   25  CZ  ARG A 259     3990   5420   2840   -270   -590    320       C  
ATOM     26  NH1 ARG A 259      -1.444   5.309 -13.619  1.00 33.20           N  
ANISOU   26  NH1 ARG A 259     4020   5550   3040   -440   -600    640       N  
ATOM     27  NH2 ARG A 259       0.082   6.397 -12.317  1.00 33.26           N  
ANISOU   27  NH2 ARG A 259     4190   5660   2790   -380   -760    390       N  
ATOM     28  N   GLN A 260      -1.572   5.972 -20.048  1.00 15.48           N  
ANISOU   28  N   GLN A 260     2050   1900   1920     70   -410     50       N  
ATOM     29  CA  GLN A 260      -0.852   4.746 -20.483  1.00 15.23           C  
ANISOU   29  CA  GLN A 260     2010   1690   2090     30   -490     80       C  
ATOM     30  C   GLN A 260       0.005   5.000 -21.731  1.00 14.79           C  
ANISOU   30  C   GLN A 260     2010   1530   2080     80   -400   -120       C  
ATOM     31  O   GLN A 260       0.871   4.155 -22.009  1.00 15.20           O  
ANISOU   31  O   GLN A 260     1990   1460   2330    100   -420   -230       O  
ATOM     32  CB  GLN A 260      -1.811   3.576 -20.725  1.00 15.63           C  
ANISOU   32  CB  GLN A 260     2020   1670   2250    -30   -620    200       C  
ATOM     33  CG  GLN A 260      -2.835   3.770 -21.837  1.00 14.86           C  
ANISOU   33  CG  GLN A 260     1990   1550   2110    -20   -600    130       C  
ATOM     34  CD  GLN A 260      -4.056   4.588 -21.482  1.00 14.69           C  
ANISOU   34  CD  GLN A 260     1920   1710   1950    -20   -540    210       C  
ATOM     35  OE1 GLN A 260      -4.124   5.271 -20.466  1.00 14.68           O  
ANISOU   35  OE1 GLN A 260     1840   1910   1830      0   -460    220       O  
ATOM     36  NE2 GLN A 260      -5.062   4.499 -22.335  1.00 14.72           N  
ANISOU   36  NE2 GLN A 260     1950   1640   2010    -40   -610    220       N  
ATOM     37  N   LYS A 261      -0.202   6.116 -22.436  1.00 14.28           N  
ANISOU   37  N   LYS A 261     2030   1540   1860     70   -310   -160       N  
ATOM     38  CA  LYS A 261       0.594   6.377 -23.665  1.00 15.31           C  
ANISOU   38  CA  LYS A 261     2180   1700   1930     20   -200   -270       C  
ATOM     39  C   LYS A 261       1.667   7.436 -23.401  1.00 15.71           C  
ANISOU   39  C   LYS A 261     2190   1780   2010    -10   -160   -220       C  
ATOM     40  O   LYS A 261       2.395   7.759 -24.343  1.00 16.84           O  
ANISOU   40  O   LYS A 261     2300   2030   2070   -110    -40   -230       O  
ATOM     41  CB  LYS A 261      -0.323   6.791 -24.819  1.00 15.86           C  
ANISOU   41  CB  LYS A 261     2380   1840   1810    -70   -220   -230       C  
ATOM     42  CG  LYS A 261      -1.315   5.720 -25.263  1.00 16.22           C  
ANISOU   42  CG  LYS A 261     2470   1830   1870    -50   -310   -290       C  
ATOM     43  CD  LYS A 261      -0.630   4.432 -25.691  1.00 17.71           C  
ANISOU   43  CD  LYS A 261     2590   1990   2150     10   -280   -540       C  
ATOM     44  CE  LYS A 261      -1.590   3.362 -26.164  1.00 18.67           C  
ANISOU   44  CE  LYS A 261     2760   1980   2350     30   -460   -630       C  
ATOM     45  NZ  LYS A 261      -0.871   2.141 -26.604  1.00 21.00           N  
ANISOU   45  NZ  LYS A 261     2950   2190   2840    130   -500   -980       N  
ATOM     46  N   ARG A 262       1.784   7.914 -22.160  1.00 15.18           N  
ANISOU   46  N   ARG A 262     2090   1650   2030     50   -250   -160       N  
ATOM     47  CA  ARG A 262       2.789   8.960 -21.845  1.00 15.95           C  
ANISOU   47  CA  ARG A 262     2140   1700   2220     30   -300   -120       C  
ATOM     48  C   ARG A 262       4.204   8.376 -21.834  1.00 16.61           C  
ANISOU   48  C   ARG A 262     2080   1760   2470     20   -220   -160       C  
ATOM     49  O   ARG A 262       4.368   7.182 -21.541  1.00 16.74           O  
ANISOU   49  O   ARG A 262     2040   1720   2600     80   -220   -250       O  
ATOM     50  CB  ARG A 262       2.482   9.605 -20.492  1.00 16.01           C  
ANISOU   50  CB  ARG A 262     2170   1660   2250    120   -460   -150       C  
ATOM     51  CG  ARG A 262       1.147  10.329 -20.452  1.00 16.10           C  
ANISOU   51  CG  ARG A 262     2220   1700   2200    180   -550   -200       C  
ATOM     52  CD  ARG A 262       0.841  10.862 -19.070  1.00 16.90           C  
ANISOU   52  CD  ARG A 262     2290   1870   2260    310   -660   -370       C  
ATOM     53  NE  ARG A 262      -0.479  11.470 -19.032  1.00 17.98           N  
ANISOU   53  NE  ARG A 262     2380   2050   2400    400   -710   -520       N  
ATOM     54  CZ  ARG A 262      -1.063  11.941 -17.940  1.00 20.05           C  
ANISOU   54  CZ  ARG A 262     2550   2480   2590    550   -750   -780       C  
ATOM     55  NH1 ARG A 262      -2.270  12.470 -18.022  1.00 22.31           N  
ANISOU   55  NH1 ARG A 262     2710   2800   2960    660   -790   -980       N  
ATOM     56  NH2 ARG A 262      -0.453  11.882 -16.771  1.00 21.01           N  
ANISOU   56  NH2 ARG A 262     2670   2760   2550    580   -760   -890       N  
ATOM     57  N   THR A 263       5.174   9.227 -22.165  1.00 17.85           N  
ANISOU   57  N   THR A 263     2150   1920   2710    -70   -200    -90       N  
ATOM     58  CA  THR A 263       6.611   8.880 -22.192  1.00 19.50           C  
ANISOU   58  CA  THR A 263     2150   2120   3150    -80   -110   -130       C  
ATOM     59  C   THR A 263       7.315   9.822 -21.217  1.00 19.46           C  
ANISOU   59  C   THR A 263     2110   1940   3350    -90   -330    -10       C  
ATOM     60  O   THR A 263       7.227  11.026 -21.430  1.00 19.62           O  
ANISOU   60  O   THR A 263     2170   1930   3360   -180   -450    140       O  
ATOM     61  CB  THR A 263       7.175   8.981 -23.612  1.00 22.08           C  
ANISOU   61  CB  THR A 263     2320   2710   3350   -230    150   -140       C  
ATOM     62  OG1 THR A 263       6.408   8.108 -24.440  1.00 22.80           O  
ANISOU   62  OG1 THR A 263     2490   2960   3210   -200    300   -330       O  
ATOM     63  CG2 THR A 263       8.641   8.620 -23.691  1.00 24.57           C  
ANISOU   63  CG2 THR A 263     2320   3080   3930   -230    300   -250       C  
ATOM     64  N   ALA A 264       7.924   9.288 -20.158  1.00 14.75           N  
ANISOU   64  N   ALA A 264     2020   1670   1920    200    -20    130       N  
ATOM     65  CA  ALA A 264       8.630  10.157 -19.192  1.00 15.10           C  
ANISOU   65  CA  ALA A 264     1970   1670   2090    170    -40    170       C  
ATOM     66  C   ALA A 264      10.014  10.507 -19.755  1.00 16.01           C  
ANISOU   66  C   ALA A 264     2050   1790   2250    150     50    310       C  
ATOM     67  O   ALA A 264      10.649   9.631 -20.372  1.00 16.25           O  
ANISOU   67  O   ALA A 264     2090   1860   2230    220    160    380       O  
ATOM     68  CB  ALA A 264       8.722   9.485 -17.850  1.00 14.52           C  
ANISOU   68  CB  ALA A 264     1830   1620   2060    140    -70    120       C  
ATOM     69  N   THR A 265      10.441  11.748 -19.536  1.00 17.84           N  
ANISOU   69  N   THR A 265     2260   1970   2550     60     10    370       N  
ATOM     70  CA  THR A 265      11.749  12.285 -20.006  1.00 19.97           C  
ANISOU   70  CA  THR A 265     2460   2270   2860    -20     80    520       C  
ATOM     71  C   THR A 265      12.235  13.301 -18.973  1.00 21.19           C  
ANISOU   71  C   THR A 265     2580   2380   3080   -240      0    520       C  
ATOM     72  O   THR A 265      11.522  13.486 -17.978  1.00 20.33           O  
ANISOU   72  O   THR A 265     2550   2210   2970   -270    -80    390       O  
ATOM     73  CB  THR A 265      11.611  13.020 -21.349  1.00 21.04           C  
ANISOU   73  CB  THR A 265     2710   2330   2960     30    150    600       C  
ATOM     74  OG1 THR A 265      10.798  14.172 -21.112  1.00 21.75           O  
ANISOU   74  OG1 THR A 265     2940   2270   3060     10     90    540       O  
ATOM     75  CG2 THR A 265      11.007  12.186 -22.458  1.00 20.71           C  
ANISOU   75  CG2 THR A 265     2760   2320   2790    190    210    580       C  
ATOM     76  N   LYS A 266      13.375  13.954 -19.218  1.00 23.72           N  
ANISOU   76  N   LYS A 266     2820   2740   3440   -400     40    670       N  
ATOM     77  CA  LYS A 266      13.870  14.998 -18.284  1.00 26.41           C  
ANISOU   77  CA  LYS A 266     3190   3040   3810   -700    -50    650       C  
ATOM     78  C   LYS A 266      12.827  16.122 -18.165  1.00 26.07           C  
ANISOU   78  C   LYS A 266     3470   2700   3740   -710    -60    520       C  
ATOM     79  O   LYS A 266      12.562  16.567 -17.032  1.00 26.67           O  
ANISOU   79  O   LYS A 266     3670   2670   3790   -850   -130    390       O  
ATOM     80  CB  LYS A 266      15.179  15.612 -18.793  1.00 29.72           C  
ANISOU   80  CB  LYS A 266     3490   3550   4250   -930      0    850       C  
ATOM     81  CG  LYS A 266      16.328  14.637 -18.974  1.00 31.79           C  
ANISOU   81  CG  LYS A 266     3400   4150   4530   -880     50   1060       C  
ATOM     82  CD  LYS A 266      17.607  15.274 -19.477  1.00 35.29           C  
ANISOU   82  CD  LYS A 266     3660   4740   5000  -1110    100   1290       C  
ATOM     83  CE  LYS A 266      18.707  14.260 -19.698  1.00 37.01           C  
ANISOU   83  CE  LYS A 266     3500   5330   5230   -970    200   1560       C  
ATOM     84  NZ  LYS A 266      18.983  13.489 -18.463  1.00 37.38           N  
ANISOU   84  NZ  LYS A 266     3330   5620   5250   -980     90   1570       N  
ATOM     85  N   ALA A 267      12.231  16.518 -19.295  1.00 25.79           N  
ANISOU   85  N   ALA A 267     3570   2530   3700   -530     40    560       N  
ATOM     86  CA  ALA A 267      11.245  17.629 -19.355  1.00 26.69           C  
ANISOU   86  CA  ALA A 267     3980   2380   3780   -450     80    500       C  
ATOM     87  C   ALA A 267       9.909  17.259 -18.699  1.00 25.29           C  
ANISOU   87  C   ALA A 267     3860   2190   3570   -240     40    370       C  
ATOM     88  O   ALA A 267       9.247  18.171 -18.185  1.00 27.11           O  
ANISOU   88  O   ALA A 267     4330   2200   3770   -200     90    310       O  
ATOM     89  CB  ALA A 267      11.040  18.033 -20.794  1.00 27.35           C  
ANISOU   89  CB  ALA A 267     4140   2410   3840   -280    190    630       C  
ATOM     90  N   TYR A 268       9.527  15.981 -18.754  1.00 23.45           N  
ANISOU   90  N   TYR A 268     3430   2160   3320   -110    -20    330       N  
ATOM     91  CA  TYR A 268       8.256  15.452 -18.185  1.00 21.52           C  
ANISOU   91  CA  TYR A 268     3170   1970   3040     60    -60    230       C  
ATOM     92  C   TYR A 268       8.653  14.155 -17.474  1.00 19.61           C  
ANISOU   92  C   TYR A 268     2740   1900   2810    -20   -130    170       C  
ATOM     93  O   TYR A 268       8.588  13.081 -18.088  1.00 18.38           O  
ANISOU   93  O   TYR A 268     2480   1870   2630     60   -130    190       O  
ATOM     94  CB  TYR A 268       7.238  15.364 -19.327  1.00 21.68           C  
ANISOU   94  CB  TYR A 268     3180   2060   2990    280    -40    300       C  
ATOM     95  CG  TYR A 268       5.831  14.955 -18.974  1.00 21.57           C  
ANISOU   95  CG  TYR A 268     3110   2160   2930    430    -90    260       C  
ATOM     96  CD1 TYR A 268       5.063  15.713 -18.106  1.00 22.67           C  
ANISOU   96  CD1 TYR A 268     3350   2200   3070    540    -50    240       C  
ATOM     97  CD2 TYR A 268       5.202  13.919 -19.648  1.00 21.37           C  
ANISOU   97  CD2 TYR A 268     2940   2360   2820    480   -150    260       C  
ATOM     98  CE1 TYR A 268       3.753  15.368 -17.811  1.00 22.81           C  
ANISOU   98  CE1 TYR A 268     3260   2370   3040    710    -70    250       C  
ATOM     99  CE2 TYR A 268       3.885  13.577 -19.385  1.00 21.36           C  
ANISOU   99  CE2 TYR A 268     2840   2510   2760    570   -200    260       C  
ATOM    100  CZ  TYR A 268       3.157  14.301 -18.461  1.00 22.15           C  
ANISOU  100  CZ  TYR A 268     2970   2550   2890    700   -160    270       C  
ATOM    101  OH  TYR A 268       1.859  13.968 -18.194  1.00 22.08           O  
ANISOU  101  OH  TYR A 268     2820   2750   2820    810   -190    300       O  
ATOM    102  N   ASN A 269       9.065  14.285 -16.206  1.00 19.65           N  
ANISOU  102  N   ASN A 269     2750   1880   2840   -160   -180    100       N  
ATOM    103  CA  ASN A 269       9.617  13.162 -15.398  1.00 18.62           C  
ANISOU  103  CA  ASN A 269     2450   1920   2710   -220   -230     90       C  
ATOM    104  C   ASN A 269       8.529  12.173 -14.956  1.00 17.34           C  
ANISOU  104  C   ASN A 269     2250   1810   2520    -70   -250      0       C  
ATOM    105  O   ASN A 269       7.328  12.422 -15.209  1.00 17.40           O  
ANISOU  105  O   ASN A 269     2330   1770   2500     50   -230    -40       O  
ATOM    106  CB  ASN A 269      10.492  13.707 -14.261  1.00 20.01           C  
ANISOU  106  CB  ASN A 269     2630   2100   2870   -460   -310     70       C  
ATOM    107  CG  ASN A 269       9.729  14.476 -13.203  1.00 20.49           C  
ANISOU  107  CG  ASN A 269     2910   1990   2880   -500   -330    -70       C  
ATOM    108  OD1 ASN A 269       8.635  14.087 -12.805  1.00 19.38           O  
ANISOU  108  OD1 ASN A 269     2810   1840   2720   -320   -310   -150       O  
ATOM    109  ND2 ASN A 269      10.332  15.538 -12.701  1.00 22.64           N  
ANISOU  109  ND2 ASN A 269     3350   2140   3100   -760   -350   -100       N  
ATOM    110  N   VAL A 270       8.966  11.078 -14.321  1.00 15.90           N  
ANISOU  110  N   VAL A 270     1950   1760   2340    -90   -260      0       N  
ATOM    111  CA  VAL A 270       8.064   9.981 -13.860  1.00 15.14           C  
ANISOU  111  CA  VAL A 270     1830   1710   2210     10   -250    -60       C  
ATOM    112  C   VAL A 270       7.024  10.524 -12.873  1.00 15.41           C  
ANISOU  112  C   VAL A 270     1940   1690   2230     30   -290   -160       C  
ATOM    113  O   VAL A 270       5.863  10.078 -12.943  1.00 15.28           O  
ANISOU  113  O   VAL A 270     1920   1700   2190    120   -270   -200       O  
ATOM    114  CB  VAL A 270       8.894   8.830 -13.258  1.00 14.80           C  
ANISOU  114  CB  VAL A 270     1680   1780   2170     10   -220    -10       C  
ATOM    115  CG1 VAL A 270       8.021   7.702 -12.732  1.00 14.09           C  
ANISOU  115  CG1 VAL A 270     1610   1690   2040     90   -190    -70       C  
ATOM    116  CG2 VAL A 270       9.906   8.302 -14.263  1.00 15.01           C  
ANISOU  116  CG2 VAL A 270     1650   1850   2200     60   -130    130       C  
ATOM    117  N   THR A 271       7.408  11.470 -12.016  1.00 16.58           N  
ANISOU  117  N   THR A 271     2180   1760   2360    -70   -320   -200       N  
ATOM    118  CA  THR A 271       6.449  12.027 -11.024  1.00 17.81           C  
ANISOU  118  CA  THR A 271     2470   1830   2470    -10   -310   -290       C  
ATOM    119  C   THR A 271       5.356  12.840 -11.725  1.00 18.35           C  
ANISOU  119  C   THR A 271     2640   1800   2540    150   -240   -270       C  
ATOM    120  O   THR A 271       4.184  12.702 -11.336  1.00 18.27           O  
ANISOU  120  O   THR A 271     2610   1830   2500    310   -200   -290       O  
ATOM    121  CB  THR A 271       7.166  12.885  -9.978  1.00 19.43           C  
ANISOU  121  CB  THR A 271     2830   1950   2610   -190   -350   -350       C  
ATOM    122  OG1 THR A 271       8.132  12.058  -9.326  1.00 18.80           O  
ANISOU  122  OG1 THR A 271     2590   2050   2500   -320   -440   -320       O  
ATOM    123  CG2 THR A 271       6.210  13.479  -8.966  1.00 20.56           C  
ANISOU  123  CG2 THR A 271     3180   1960   2670   -110   -300   -450       C  
ATOM    124  N   GLN A 272       5.735  13.624 -12.735  1.00 19.19           N  
ANISOU  124  N   GLN A 272     2810   1810   2670    140   -220   -210       N  
ATOM    125  CA  GLN A 272       4.791  14.497 -13.484  1.00 20.86           C  
ANISOU  125  CA  GLN A 272     3120   1940   2860    340   -130   -150       C  
ATOM    126  C   GLN A 272       3.876  13.656 -14.376  1.00 19.58           C  
ANISOU  126  C   GLN A 272     2750   2000   2690    470   -160    -80       C  
ATOM    127  O   GLN A 272       2.684  13.997 -14.498  1.00 20.55           O  
ANISOU  127  O   GLN A 272     2850   2180   2770    660   -110    -10       O  
ATOM    128  CB  GLN A 272       5.594  15.506 -14.306  1.00 22.83           C  
ANISOU  128  CB  GLN A 272     3520   2030   3130    260    -90    -90       C  
ATOM    129  CG  GLN A 272       6.329  16.524 -13.442  1.00 25.12           C  
ANISOU  129  CG  GLN A 272     4070   2080   3390     70    -60   -160       C  
ATOM    130  CD  GLN A 272       7.334  17.329 -14.224  1.00 26.83           C  
ANISOU  130  CD  GLN A 272     4400   2160   3630   -100    -40   -100       C  
ATOM    131  OE1 GLN A 272       7.971  16.832 -15.149  1.00 26.53           O  
ANISOU  131  OE1 GLN A 272     4170   2270   3640   -150    -80    -10       O  
ATOM    132  NE2 GLN A 272       7.537  18.568 -13.809  1.00 30.37           N  
ANISOU  132  NE2 GLN A 272     5190   2320   4030   -220     50   -140       N  
ATOM    133  N   ALA A 273       4.413  12.576 -14.935  1.00 17.96           N  
ANISOU  133  N   ALA A 273     2420   1910   2500    350   -220    -80       N  
ATOM    134  CA  ALA A 273       3.639  11.710 -15.848  1.00 17.51           C  
ANISOU  134  CA  ALA A 273     2230   2040   2380    390   -250    -40       C  
ATOM    135  C   ALA A 273       2.858  10.628 -15.099  1.00 16.95           C  
ANISOU  135  C   ALA A 273     2050   2100   2290    360   -280   -100       C  
ATOM    136  O   ALA A 273       1.703  10.378 -15.497  1.00 17.67           O  
ANISOU  136  O   ALA A 273     2030   2370   2310    390   -310    -50       O  
ATOM    137  CB  ALA A 273       4.585  11.065 -16.837  1.00 16.29           C  
ANISOU  137  CB  ALA A 273     2080   1900   2220    290   -260    -30       C  
ATOM    138  N   PHE A 274       3.443  10.025 -14.056  1.00 16.50           N  
ANISOU  138  N   PHE A 274     2010   1990   2270    280   -270   -180       N  
ATOM    139  CA  PHE A 274       2.754   8.874 -13.404  1.00 16.23           C  
ANISOU  139  CA  PHE A 274     1900   2060   2210    230   -270   -220       C  
ATOM    140  C   PHE A 274       2.556   9.060 -11.891  1.00 16.82           C  
ANISOU  140  C   PHE A 274     1990   2100   2300    280   -250   -260       C  
ATOM    141  O   PHE A 274       2.172   8.066 -11.216  1.00 17.17           O  
ANISOU  141  O   PHE A 274     1980   2210   2330    240   -230   -290       O  
ATOM    142  CB  PHE A 274       3.544   7.598 -13.730  1.00 15.07           C  
ANISOU  142  CB  PHE A 274     1780   1890   2050    120   -250   -240       C  
ATOM    143  CG  PHE A 274       3.887   7.466 -15.194  1.00 15.19           C  
ANISOU  143  CG  PHE A 274     1850   1910   2020     90   -240   -210       C  
ATOM    144  CD1 PHE A 274       2.890   7.295 -16.145  1.00 15.35           C  
ANISOU  144  CD1 PHE A 274     1850   2050   1940     30   -290   -210       C  
ATOM    145  CD2 PHE A 274       5.206   7.516 -15.628  1.00 14.62           C  
ANISOU  145  CD2 PHE A 274     1830   1750   1980    100   -190   -170       C  
ATOM    146  CE1 PHE A 274       3.200   7.206 -17.493  1.00 15.99           C  
ANISOU  146  CE1 PHE A 274     2010   2130   1940      0   -280   -190       C  
ATOM    147  CE2 PHE A 274       5.516   7.404 -16.976  1.00 14.98           C  
ANISOU  147  CE2 PHE A 274     1950   1780   1960     90   -160   -140       C  
ATOM    148  CZ  PHE A 274       4.512   7.258 -17.908  1.00 15.77           C  
ANISOU  148  CZ  PHE A 274     2070   1970   1950     40   -200   -160       C  
ATOM    149  N   GLY A 275       2.797  10.263 -11.367  1.00 17.44           N  
ANISOU  149  N   GLY A 275     2170   2060   2390    350   -230   -270       N  
ATOM    150  CA  GLY A 275       2.610  10.503  -9.925  1.00 18.56           C  
ANISOU  150  CA  GLY A 275     2390   2160   2500    390   -190   -320       C  
ATOM    151  C   GLY A 275       3.799  10.065  -9.080  1.00 18.86           C  
ANISOU  151  C   GLY A 275     2460   2170   2530    250   -240   -370       C  
ATOM    152  O   GLY A 275       4.713   9.368  -9.599  1.00 17.57           O  
ANISOU  152  O   GLY A 275     2220   2050   2400    160   -270   -340       O  
ATOM    153  N   ARG A 276       3.783  10.482  -7.814  1.00 20.73           N  
ANISOU  153  N   ARG A 276     2820   2360   2700    250   -220   -430       N  
ATOM    154  CA  ARG A 276       4.837  10.159  -6.822  1.00 22.69           C  
ANISOU  154  CA  ARG A 276     3080   2650   2890    110   -290   -460       C  
ATOM    155  C   ARG A 276       4.859   8.650  -6.591  1.00 19.92           C  
ANISOU  155  C   ARG A 276     2570   2440   2560    130   -280   -410       C  
ATOM    156  O   ARG A 276       3.763   8.064  -6.544  1.00 18.53           O  
ANISOU  156  O   ARG A 276     2350   2290   2400    220   -210   -410       O  
ATOM    157  CB  ARG A 276       4.515  10.793  -5.462  1.00 27.16           C  
ANISOU  157  CB  ARG A 276     3840   3140   3340    120   -260   -550       C  
ATOM    158  CG  ARG A 276       4.421  12.310  -5.447  1.00 33.57           C  
ANISOU  158  CG  ARG A 276     4930   3740   4090    100   -210   -620       C  
ATOM    159  CD  ARG A 276       5.742  13.058  -5.458  1.00 39.48           C  
ANISOU  159  CD  ARG A 276     5810   4410   4780   -170   -320   -660       C  
ATOM    160  NE  ARG A 276       6.479  12.922  -4.201  1.00 44.56           N  
ANISOU  160  NE  ARG A 276     6510   5150   5270   -370   -420   -720       N  
ATOM    161  CZ  ARG A 276       7.440  12.030  -3.956  1.00 46.24           C  
ANISOU  161  CZ  ARG A 276     6480   5620   5480   -500   -550   -630       C  
ATOM    162  NH1 ARG A 276       7.814  11.167  -4.888  1.00 48.62           N  
ANISOU  162  NH1 ARG A 276     6500   6050   5920   -430   -560   -500       N  
ATOM    163  NH2 ARG A 276       8.028  12.006  -2.771  1.00 46.23           N  
ANISOU  163  NH2 ARG A 276     6520   5740   5300   -670   -650   -660       N  
ATOM    164  N   ARG A 277       6.048   8.047  -6.481  1.00 18.01           N  
ANISOU  164  N   ARG A 277     2250   2280   2310     60   -330   -340       N  
ATOM    165  CA  ARG A 277       6.120   6.597  -6.171  1.00 17.00           C  
ANISOU  165  CA  ARG A 277     2030   2240   2190    120   -270   -270       C  
ATOM    166  C   ARG A 277       5.543   6.391  -4.768  1.00 17.63           C  
ANISOU  166  C   ARG A 277     2160   2360   2180    160   -250   -300       C  
ATOM    167  O   ARG A 277       5.656   7.330  -3.939  1.00 17.69           O  
ANISOU  167  O   ARG A 277     2260   2360   2090    100   -320   -370       O  
ATOM    168  CB  ARG A 277       7.555   6.069  -6.218  1.00 17.63           C  
ANISOU  168  CB  ARG A 277     2000   2440   2260    110   -290   -130       C  
ATOM    169  CG  ARG A 277       8.085   5.686  -7.594  1.00 17.22           C  
ANISOU  169  CG  ARG A 277     1900   2360   2280    150   -230    -50       C  
ATOM    170  CD  ARG A 277       8.080   6.727  -8.701  1.00 16.70           C  
ANISOU  170  CD  ARG A 277     1860   2220   2270     80   -270   -100       C  
ATOM    171  NE  ARG A 277       6.761   7.010  -9.245  1.00 16.08           N  
ANISOU  171  NE  ARG A 277     1870   2020   2210    100   -250   -200       N  
ATOM    172  CZ  ARG A 277       6.123   6.232 -10.124  1.00 15.15           C  
ANISOU  172  CZ  ARG A 277     1770   1870   2110    130   -180   -210       C  
ATOM    173  NH1 ARG A 277       4.923   6.575 -10.568  1.00 15.01           N  
ANISOU  173  NH1 ARG A 277     1780   1840   2090    130   -190   -270       N  
ATOM    174  NH2 ARG A 277       6.670   5.096 -10.526  1.00 15.37           N  
ANISOU  174  NH2 ARG A 277     1820   1890   2130    170    -80   -140       N  
ATOM    175  N   GLY A 278       4.962   5.218  -4.499  1.00 17.38           N  
ANISOU  175  N   GLY A 278     2100   2350   2150    230   -160   -260       N  
ATOM    176  CA  GLY A 278       4.386   4.962  -3.162  1.00 18.10           C  
ANISOU  176  CA  GLY A 278     2240   2480   2160    280   -120   -280       C  
ATOM    177  C   GLY A 278       3.932   3.519  -2.974  1.00 18.19           C  
ANISOU  177  C   GLY A 278     2240   2490   2190    330     10   -210       C  
ATOM    178  O   GLY A 278       4.022   2.705  -3.898  1.00 18.00           O  
ANISOU  178  O   GLY A 278     2210   2400   2230    310     80   -160       O  
ATOM    179  N   PRO A 279       3.418   3.172  -1.770  1.00 18.99           N  
ANISOU  179  N   PRO A 279     2370   2640   2210    380     70   -190       N  
ATOM    180  CA  PRO A 279       2.987   1.808  -1.462  1.00 19.79           C  
ANISOU  180  CA  PRO A 279     2500   2710   2310    400    220   -110       C  
ATOM    181  C   PRO A 279       1.504   1.465  -1.662  1.00 20.20           C  
ANISOU  181  C   PRO A 279     2530   2740   2410    340    310   -150       C  
ATOM    182  O   PRO A 279       1.147   0.343  -1.382  1.00 20.39           O  
ANISOU  182  O   PRO A 279     2610   2720   2420    310    440    -80       O  
ATOM    183  CB  PRO A 279       3.287   1.746   0.043  1.00 20.56           C  
ANISOU  183  CB  PRO A 279     2630   2910   2270    490    220    -60       C  
ATOM    184  CG  PRO A 279       2.985   3.150   0.548  1.00 21.30           C  
ANISOU  184  CG  PRO A 279     2760   3050   2290    470    120   -180       C  
ATOM    185  CD  PRO A 279       3.227   4.079  -0.629  1.00 20.33           C  
ANISOU  185  CD  PRO A 279     2610   2860   2260    400     30   -250       C  
ATOM    186  N   GLU A 280       0.694   2.406  -2.157  1.00 20.69           N  
ANISOU  186  N   GLU A 280     2520   2840   2500    310    260   -210       N  
ATOM    187  CA  GLU A 280      -0.764   2.136  -2.317  1.00 22.25           C  
ANISOU  187  CA  GLU A 280     2620   3110   2720    240    340   -190       C  
ATOM    188  C   GLU A 280      -1.012   1.214  -3.525  1.00 23.41           C  
ANISOU  188  C   GLU A 280     2760   3220   2920     50    350   -190       C  
ATOM    189  O   GLU A 280      -0.217   1.256  -4.485  1.00 21.74           O  
ANISOU  189  O   GLU A 280     2610   2920   2740     20    290   -220       O  
ATOM    190  CB  GLU A 280      -1.516   3.465  -2.335  1.00 21.79           C  
ANISOU  190  CB  GLU A 280     2480   3140   2660    350    310   -210       C  
ATOM    191  CG  GLU A 280      -1.245   4.296  -1.093  1.00 21.98           C  
ANISOU  191  CG  GLU A 280     2620   3140   2590    510    330   -250       C  
ATOM    192  CD  GLU A 280      -1.638   3.643   0.228  1.00 22.86           C  
ANISOU  192  CD  GLU A 280     2760   3310   2620    560    450   -200       C  
ATOM    193  OE1 GLU A 280      -1.029   3.995   1.260  1.00 21.99           O  
ANISOU  193  OE1 GLU A 280     2800   3170   2390    640    440   -230       O  
ATOM    194  OE2 GLU A 280      -2.563   2.795   0.229  1.00 22.43           O  
ANISOU  194  OE2 GLU A 280     2590   3340   2590    500    540   -120       O  
ATOM    195  N   GLN A 281      -2.095   0.425  -3.448  1.00 28.03           N  
ANISOU  195  N   GLN A 281     3290   3870   3490   -110    430   -150       N  
ATOM    196  CA  GLN A 281      -2.515  -0.605  -4.449  1.00 31.90           C  
ANISOU  196  CA  GLN A 281     3830   4310   3980   -390    460   -160       C  
ATOM    197  C   GLN A 281      -2.371  -0.183  -5.915  1.00 31.40           C  
ANISOU  197  C   GLN A 281     3750   4260   3920   -490    340   -220       C  
ATOM    198  O   GLN A 281      -1.897  -1.037  -6.684  1.00 34.94           O  
ANISOU  198  O   GLN A 281     4400   4540   4340   -640    380   -260       O  
ATOM    199  CB  GLN A 281      -3.952  -1.076  -4.210  1.00 36.42           C  
ANISOU  199  CB  GLN A 281     4250   5070   4520   -600    520    -90       C  
ATOM    200  CG  GLN A 281      -4.089  -2.059  -3.055  1.00 40.32           C  
ANISOU  200  CG  GLN A 281     4860   5480   4990   -630    690    -30       C  
ATOM    201  CD  GLN A 281      -3.355  -3.360  -3.298  1.00 45.83           C  
ANISOU  201  CD  GLN A 281     5890   5870   5650   -760    810    -60       C  
ATOM    202  OE1 GLN A 281      -2.716  -3.569  -4.335  1.00 47.99           O  
ANISOU  202  OE1 GLN A 281     6320   6000   5920   -820    780   -130       O  
ATOM    203  NE2 GLN A 281      -3.449  -4.265  -2.333  1.00 49.38           N  
ANISOU  203  NE2 GLN A 281     6470   6220   6070   -760    990     20       N  
ATOM    204  N   THR A 282      -2.818   1.009  -6.319  1.00 26.97           N  
ANISOU  204  N   THR A 282     3190   3940   3120     50     40   -380       N  
ATOM    205  CA  THR A 282      -2.685   1.372  -7.764  1.00 25.88           C  
ANISOU  205  CA  THR A 282     3080   3660   3090     80     10   -350       C  
ATOM    206  C   THR A 282      -1.703   2.541  -7.934  1.00 26.53           C  
ANISOU  206  C   THR A 282     3140   3700   3240    110    -20   -400       C  
ATOM    207  O   THR A 282      -1.860   3.329  -8.894  1.00 28.33           O  
ANISOU  207  O   THR A 282     3360   3830   3580    120    -40   -410       O  
ATOM    208  CB  THR A 282      -4.059   1.624  -8.396  1.00 25.48           C  
ANISOU  208  CB  THR A 282     3010   3560   3110     80     10   -370       C  
ATOM    209  OG1 THR A 282      -4.691   2.664  -7.658  1.00 24.81           O  
ANISOU  209  OG1 THR A 282     2840   3510   3070     80     30   -500       O  
ATOM    210  CG2 THR A 282      -4.935   0.389  -8.403  1.00 26.13           C  
ANISOU  210  CG2 THR A 282     3120   3670   3140     60     40   -310       C  
ATOM    211  N   GLN A 283      -0.724   2.625  -7.034  1.00 24.54           N  
ANISOU  211  N   GLN A 283     2880   3520   2930    100    -20   -420       N  
ATOM    212  CA  GLN A 283       0.323   3.670  -7.072  1.00 22.41           C  
ANISOU  212  CA  GLN A 283     2580   3220   2720    110    -40   -480       C  
ATOM    213  C   GLN A 283       1.614   3.005  -7.570  1.00 19.43           C  
ANISOU  213  C   GLN A 283     2250   2820   2310    120    -60   -380       C  
ATOM    214  O   GLN A 283       1.882   1.861  -7.148  1.00 18.71           O  
ANISOU  214  O   GLN A 283     2190   2790   2130    120    -60   -320       O  
ATOM    215  CB  GLN A 283       0.473   4.257  -5.669  1.00 24.32           C  
ANISOU  215  CB  GLN A 283     2760   3570   2910    100    -30   -590       C  
ATOM    216  CG  GLN A 283       1.448   5.416  -5.561  1.00 25.45           C  
ANISOU  216  CG  GLN A 283     2860   3690   3120    110    -60   -670       C  
ATOM    217  CD  GLN A 283       1.511   5.947  -4.147  1.00 27.28           C  
ANISOU  217  CD  GLN A 283     3020   4050   3300     90    -40   -800       C  
ATOM    218  OE1 GLN A 283       1.058   5.308  -3.193  1.00 26.06           O  
ANISOU  218  OE1 GLN A 283     2860   4020   3020     60    -10   -810       O  
ATOM    219  NE2 GLN A 283       2.100   7.122  -3.994  1.00 27.97           N  
ANISOU  219  NE2 GLN A 283     3060   4100   3470     90    -60   -910       N  
ATOM    220  N   GLY A 284       2.352   3.671  -8.460  1.00 16.66           N  
ANISOU  220  N   GLY A 284     1910   2380   2040    140    -90   -380       N  
ATOM    221  CA  GLY A 284       3.620   3.120  -8.969  1.00 15.14           C  
ANISOU  221  CA  GLY A 284     1750   2170   1830    140   -100   -310       C  
ATOM    222  C   GLY A 284       4.665   3.078  -7.867  1.00 14.67           C  
ANISOU  222  C   GLY A 284     1660   2200   1710    140   -110   -340       C  
ATOM    223  O   GLY A 284       4.686   4.014  -7.035  1.00 15.18           O  
ANISOU  223  O   GLY A 284     1680   2310   1780    140   -110   -430       O  
ATOM    224  N   ASN A 285       5.493   2.032  -7.845  1.00 13.53           N  
ANISOU  224  N   ASN A 285     1550   2080   1510    160   -120   -270       N  
ATOM    225  CA  ASN A 285       6.545   1.882  -6.801  1.00 13.47           C  
ANISOU  225  CA  ASN A 285     1510   2160   1440    160   -140   -280       C  
ATOM    226  C   ASN A 285       7.918   1.709  -7.448  1.00 12.92           C  
ANISOU  226  C   ASN A 285     1440   2050   1410    180   -160   -240       C  
ATOM    227  O   ASN A 285       8.878   1.435  -6.704  1.00 13.25           O  
ANISOU  227  O   ASN A 285     1460   2160   1410    180   -190   -240       O  
ATOM    228  CB  ASN A 285       6.340   0.625  -5.949  1.00 13.48           C  
ANISOU  228  CB  ASN A 285     1530   2240   1350    150   -150   -210       C  
ATOM    229  CG  ASN A 285       6.528  -0.657  -6.743  1.00 13.06           C  
ANISOU  229  CG  ASN A 285     1530   2120   1310    170   -150   -100       C  
ATOM    230  OD1 ASN A 285       6.298  -0.695  -7.951  1.00 11.97           O  
ANISOU  230  OD1 ASN A 285     1420   1890   1240    180   -140    -90       O  
ATOM    231  ND2 ASN A 285       6.952  -1.718  -6.074  1.00 13.30           N  
ANISOU  231  ND2 ASN A 285     1570   2200   1290    180   -180    -30       N  
ATOM    232  N   PHE A 286       8.017   1.903  -8.763  1.00 12.22           N  
ANISOU  232  N   PHE A 286     1380   1870   1400    180   -140   -230       N  
ATOM    233  CA  PHE A 286       9.316   1.648  -9.438  1.00 12.06           C  
ANISOU  233  CA  PHE A 286     1350   1820   1410    190   -150   -200       C  
ATOM    234  C   PHE A 286      10.068   2.934  -9.792  1.00 12.12           C  
ANISOU  234  C   PHE A 286     1320   1800   1480    170   -150   -260       C  
ATOM    235  O   PHE A 286       9.459   3.867 -10.365  1.00 11.37           O  
ANISOU  235  O   PHE A 286     1230   1650   1440    150   -140   -280       O  
ATOM    236  CB  PHE A 286       9.052   0.827 -10.703  1.00 11.48           C  
ANISOU  236  CB  PHE A 286     1320   1690   1350    190   -130   -140       C  
ATOM    237  CG  PHE A 286      10.274   0.317 -11.424  1.00 11.44           C  
ANISOU  237  CG  PHE A 286     1310   1660   1380    210   -120   -130       C  
ATOM    238  CD1 PHE A 286      10.890   1.073 -12.407  1.00 11.18           C  
ANISOU  238  CD1 PHE A 286     1260   1600   1390    180   -110   -150       C  
ATOM    239  CD2 PHE A 286      10.784  -0.942 -11.141  1.00 11.43           C  
ANISOU  239  CD2 PHE A 286     1310   1670   1360    240   -140    -90       C  
ATOM    240  CE1 PHE A 286      11.998   0.590 -13.082  1.00 11.19           C  
ANISOU  240  CE1 PHE A 286     1240   1600   1410    190    -90   -150       C  
ATOM    241  CE2 PHE A 286      11.891  -1.421 -11.816  1.00 11.51           C  
ANISOU  241  CE2 PHE A 286     1290   1670   1410    250   -130   -100       C  
ATOM    242  CZ  PHE A 286      12.491  -0.659 -12.790  1.00 11.37           C  
ANISOU  242  CZ  PHE A 286     1260   1630   1430    230   -100   -130       C  
ATOM    243  N   GLY A 287      11.367   2.954  -9.462  1.00 12.72           N  
ANISOU  243  N   GLY A 287     1360   1920   1560    180   -170   -280       N  
ATOM    244  CA  GLY A 287      12.245   4.082  -9.820  1.00 13.26           C  
ANISOU  244  CA  GLY A 287     1390   1960   1690    150   -170   -320       C  
ATOM    245  C   GLY A 287      13.007   4.706  -8.666  1.00 14.22           C  
ANISOU  245  C   GLY A 287     1450   2150   1800    150   -200   -400       C  
ATOM    246  O   GLY A 287      12.365   5.088  -7.662  1.00 14.36           O  
ANISOU  246  O   GLY A 287     1460   2210   1790    150   -210   -450       O  
ATOM    247  N   ASP A 288      14.336   4.797  -8.809  1.00 14.89           N  
ANISOU  247  N   ASP A 288     1500   2240   1910    150   -210   -410       N  
ATOM    248  CA  ASP A 288      15.170   5.478  -7.786  1.00 16.03           C  
ANISOU  248  CA  ASP A 288     1580   2450   2060    140   -240   -490       C  
ATOM    249  C   ASP A 288      15.138   6.969  -8.153  1.00 16.67           C  
ANISOU  249  C   ASP A 288     1630   2470   2230    100   -230   -550       C  
ATOM    250  O   ASP A 288      14.451   7.315  -9.133  1.00 16.03           O  
ANISOU  250  O   ASP A 288     1590   2300   2200     80   -200   -510       O  
ATOM    251  CB  ASP A 288      16.581   4.887  -7.687  1.00 16.27           C  
ANISOU  251  CB  ASP A 288     1570   2530   2090    160   -260   -470       C  
ATOM    252  CG  ASP A 288      17.486   5.112  -8.888  1.00 16.23           C  
ANISOU  252  CG  ASP A 288     1540   2470   2150    140   -230   -470       C  
ATOM    253  OD1 ASP A 288      17.065   5.797  -9.843  1.00 15.87           O  
ANISOU  253  OD1 ASP A 288     1520   2350   2160    100   -200   -460       O  
ATOM    254  OD2 ASP A 288      18.619   4.593  -8.856  1.00 16.72           O  
ANISOU  254  OD2 ASP A 288     1560   2560   2220    160   -250   -470       O  
ATOM    255  N   GLN A 289      15.861   7.819  -7.430  1.00 18.67           N  
ANISOU  255  N   GLN A 289     1820   2760   2520     80   -250   -640       N  
ATOM    256  CA  GLN A 289      15.828   9.278  -7.725  1.00 19.96           C  
ANISOU  256  CA  GLN A 289     1950   2840   2790     40   -250   -700       C  
ATOM    257  C   GLN A 289      16.277   9.570  -9.167  1.00 19.37           C  
ANISOU  257  C   GLN A 289     1890   2680   2790      0   -220   -630       C  
ATOM    258  O   GLN A 289      15.601  10.377  -9.833  1.00 19.03           O  
ANISOU  258  O   GLN A 289     1860   2540   2830    -30   -220   -610       O  
ATOM    259  CB  GLN A 289      16.640  10.036  -6.670  1.00 22.60           C  
ANISOU  259  CB  GLN A 289     2210   3230   3140     20   -280   -810       C  
ATOM    260  CG  GLN A 289      15.946  10.089  -5.311  1.00 24.99           C  
ANISOU  260  CG  GLN A 289     2490   3630   3380     30   -290   -900       C  
ATOM    261  CD  GLN A 289      16.787  10.671  -4.199  1.00 28.54           C  
ANISOU  261  CD  GLN A 289     2860   4160   3810     10   -330  -1020       C  
ATOM    262  OE1 GLN A 289      16.415  11.654  -3.552  1.00 30.73           O  
ANISOU  262  OE1 GLN A 289     3100   4440   4140    -10   -330  -1140       O  
ATOM    263  NE2 GLN A 289      17.954  10.083  -3.986  1.00 31.22           N  
ANISOU  263  NE2 GLN A 289     3180   4580   4100     20   -350   -990       N  
ATOM    264  N   GLU A 290      17.324   8.903  -9.653  1.00 19.43           N  
ANISOU  264  N   GLU A 290     1890   2720   2780     10   -210   -590       N  
ATOM    265  CA  GLU A 290      17.862   9.162 -11.020  1.00 19.31           C  
ANISOU  265  CA  GLU A 290     1880   2640   2810    -40   -180   -530       C  
ATOM    266  C   GLU A 290      16.821   8.832 -12.101  1.00 18.04           C  
ANISOU  266  C   GLU A 290     1790   2430   2640    -50   -150   -450       C  
ATOM    267  O   GLU A 290      16.604   9.672 -13.001  1.00 17.65           O  
ANISOU  267  O   GLU A 290     1750   2300   2650   -100   -150   -410       O  
ATOM    268  CB  GLU A 290      19.143   8.350 -11.218  1.00 20.71           C  
ANISOU  268  CB  GLU A 290     2020   2890   2960    -30   -170   -530       C  
ATOM    269  CG  GLU A 290      19.846   8.630 -12.532  1.00 22.14           C  
ANISOU  269  CG  GLU A 290     2190   3040   3180    -90   -130   -490       C  
ATOM    270  CD  GLU A 290      21.137   7.851 -12.748  1.00 23.50           C  
ANISOU  270  CD  GLU A 290     2310   3280   3340    -70   -110   -500       C  
ATOM    271  OE1 GLU A 290      21.353   6.833 -12.053  1.00 23.19           O  
ANISOU  271  OE1 GLU A 290     2260   3290   3250    -10   -130   -520       O  
ATOM    272  OE2 GLU A 290      21.929   8.276 -13.602  1.00 26.01           O  
ANISOU  272  OE2 GLU A 290     2600   3590   3690   -130    -70   -500       O  
ATOM    273  N   LEU A 291      16.198   7.658 -12.017  1.00 16.68           N  
ANISOU  273  N   LEU A 291     1660   2290   2390      0   -150   -410       N  
ATOM    274  CA  LEU A 291      15.191   7.261 -13.033  1.00 16.39           C  
ANISOU  274  CA  LEU A 291     1690   2210   2330    -10   -130   -340       C  
ATOM    275  C   LEU A 291      13.971   8.188 -12.956  1.00 16.14           C  
ANISOU  275  C   LEU A 291     1680   2110   2350    -20   -150   -340       C  
ATOM    276  O   LEU A 291      13.463   8.589 -14.025  1.00 16.31           O  
ANISOU  276  O   LEU A 291     1730   2070   2410    -60   -140   -280       O  
ATOM    277  CB  LEU A 291      14.806   5.800 -12.800  1.00 15.79           C  
ANISOU  277  CB  LEU A 291     1650   2170   2180     50   -120   -310       C  
ATOM    278  CG  LEU A 291      13.712   5.245 -13.713  1.00 15.78           C  
ANISOU  278  CG  LEU A 291     1710   2140   2150     50   -100   -250       C  
ATOM    279  CD1 LEU A 291      14.035   5.480 -15.180  1.00 15.91           C  
ANISOU  279  CD1 LEU A 291     1740   2130   2180    -10    -70   -210       C  
ATOM    280  CD2 LEU A 291      13.511   3.758 -13.448  1.00 15.54           C  
ANISOU  280  CD2 LEU A 291     1710   2140   2060    100    -90   -230       C  
ATOM    281  N   ILE A 292      13.513   8.511 -11.746  1.00 16.24           N  
ANISOU  281  N   ILE A 292     1670   2130   2370     10   -170   -410       N  
ATOM    282  CA  ILE A 292      12.318   9.399 -11.600  1.00 16.59           C  
ANISOU  282  CA  ILE A 292     1710   2110   2480      0   -190   -430       C  
ATOM    283  C   ILE A 292      12.565  10.739 -12.308  1.00 16.85           C  
ANISOU  283  C   ILE A 292     1720   2040   2640    -50   -200   -420       C  
ATOM    284  O   ILE A 292      11.644  11.221 -12.959  1.00 16.62           O  
ANISOU  284  O   ILE A 292     1710   1930   2670    -70   -220   -380       O  
ATOM    285  CB  ILE A 292      11.952   9.597 -10.114  1.00 16.77           C  
ANISOU  285  CB  ILE A 292     1700   2190   2490     30   -200   -540       C  
ATOM    286  CG1 ILE A 292      11.493   8.283  -9.472  1.00 16.15           C  
ANISOU  286  CG1 ILE A 292     1650   2200   2280     70   -190   -520       C  
ATOM    287  CG2 ILE A 292      10.892  10.679  -9.951  1.00 17.13           C  
ANISOU  287  CG2 ILE A 292     1720   2150   2630     20   -220   -590       C  
ATOM    288  CD1 ILE A 292      11.247   8.378  -7.981  1.00 16.48           C  
ANISOU  288  CD1 ILE A 292     1660   2330   2280     90   -200   -620       C  
ATOM    289  N   ARG A 293      13.767  11.305 -12.210  1.00 18.10           N  
ANISOU  289  N   ARG A 293     1830   2210   2840    -80   -210   -450       N  
ATOM    290  CA  ARG A 293      14.006  12.628 -12.847  1.00 19.33           C  
ANISOU  290  CA  ARG A 293     1960   2260   3120   -140   -230   -430       C  
ATOM    291  C   ARG A 293      14.371  12.504 -14.334  1.00 18.79           C  
ANISOU  291  C   ARG A 293     1920   2170   3040   -200   -210   -310       C  
ATOM    292  O   ARG A 293      14.148  13.510 -15.046  1.00 19.79           O  
ANISOU  292  O   ARG A 293     2050   2200   3270   -250   -230   -250       O  
ATOM    293  CB  ARG A 293      15.048  13.422 -12.043  1.00 21.31           C  
ANISOU  293  CB  ARG A 293     2140   2520   3440   -160   -240   -530       C  
ATOM    294  CG  ARG A 293      16.397  12.745 -11.868  1.00 22.55           C  
ANISOU  294  CG  ARG A 293     2270   2780   3520   -160   -220   -550       C  
ATOM    295  CD  ARG A 293      17.269  13.527 -10.901  1.00 25.17           C  
ANISOU  295  CD  ARG A 293     2530   3120   3910   -180   -240   -660       C  
ATOM    296  NE  ARG A 293      18.551  12.880 -10.690  1.00 26.16           N  
ANISOU  296  NE  ARG A 293     2620   3350   3970   -170   -220   -680       N  
ATOM    297  CZ  ARG A 293      19.607  13.039 -11.475  1.00 28.08           C  
ANISOU  297  CZ  ARG A 293     2840   3590   4240   -220   -200   -640       C  
ATOM    298  NH1 ARG A 293      19.533  13.828 -12.533  1.00 29.93           N  
ANISOU  298  NH1 ARG A 293     3080   3730   4560   -290   -190   -570       N  
ATOM    299  NH2 ARG A 293      20.734  12.402 -11.209  1.00 29.36           N  
ANISOU  299  NH2 ARG A 293     2960   3840   4350   -210   -200   -670       N  
ATOM    300  N   GLN A 294      14.771  11.320 -14.821  1.00 17.23           N  
ANISOU  300  N   GLN A 294     1760   2060   2730   -190   -170   -270       N  
ATOM    301  CA  GLN A 294      15.204  11.209 -16.246  1.00 17.05           C  
ANISOU  301  CA  GLN A 294     1760   2040   2680   -250   -140   -170       C  
ATOM    302  C   GLN A 294      14.213  10.435 -17.126  1.00 16.19           C  
ANISOU  302  C   GLN A 294     1710   1940   2500   -250   -130    -90       C  
ATOM    303  O   GLN A 294      14.179  10.722 -18.336  1.00 15.93           O  
ANISOU  303  O   GLN A 294     1700   1890   2460   -320   -120      0       O  
ATOM    304  CB  GLN A 294      16.588  10.562 -16.309  1.00 16.98           C  
ANISOU  304  CB  GLN A 294     1710   2120   2620   -260   -100   -200       C  
ATOM    305  CG  GLN A 294      17.664  11.411 -15.645  1.00 17.68           C  
ANISOU  305  CG  GLN A 294     1730   2200   2780   -290   -110   -270       C  
ATOM    306  CD  GLN A 294      19.017  10.749 -15.630  1.00 18.26           C  
ANISOU  306  CD  GLN A 294     1760   2370   2810   -280    -80   -310       C  
ATOM    307  OE1 GLN A 294      19.145   9.537 -15.787  1.00 18.14           O  
ANISOU  307  OE1 GLN A 294     1760   2420   2710   -240    -50   -310       O  
ATOM    308  NE2 GLN A 294      20.046  11.548 -15.401  1.00 19.02           N  
ANISOU  308  NE2 GLN A 294     1790   2460   2970   -330    -80   -350       N  
ATOM    309  N   GLY A 295      13.447   9.501 -16.566  1.00 15.50           N  
ANISOU  309  N   GLY A 295     1660   1880   2350   -180   -130   -120       N  
ATOM    310  CA  GLY A 295      12.516   8.720 -17.404  1.00 15.25           C  
ANISOU  310  CA  GLY A 295     1680   1860   2250   -180   -110    -60       C  
ATOM    311  C   GLY A 295      13.272   7.999 -18.509  1.00 15.46           C  
ANISOU  311  C   GLY A 295     1720   1950   2210   -220    -70    -20       C  
ATOM    312  O   GLY A 295      14.368   7.486 -18.225  1.00 15.38           O  
ANISOU  312  O   GLY A 295     1670   2000   2170   -200    -40    -70       O  
ATOM    313  N   THR A 296      12.755   8.032 -19.740  1.00 16.35           N  
ANISOU  313  N   THR A 296     1860   2060   2280   -270    -60     60       N  
ATOM    314  CA  THR A 296      13.396   7.338 -20.895  1.00 16.95           C  
ANISOU  314  CA  THR A 296     1940   2220   2270   -320    -10     90       C  
ATOM    315  C   THR A 296      14.772   7.944 -21.237  1.00 18.29           C  
ANISOU  315  C   THR A 296     2060   2430   2460   -390     20     80       C  
ATOM    316  O   THR A 296      15.433   7.375 -22.111  1.00 19.26           O  
ANISOU  316  O   THR A 296     2170   2630   2510   -430     70     80       O  
ATOM    317  CB  THR A 296      12.438   7.282 -22.092  1.00 17.30           C  
ANISOU  317  CB  THR A 296     2040   2270   2270   -370    -20    170       C  
ATOM    318  OG1 THR A 296      12.082   8.600 -22.507  1.00 17.76           O  
ANISOU  318  OG1 THR A 296     2100   2260   2390   -430    -70    260       O  
ATOM    319  CG2 THR A 296      11.177   6.517 -21.765  1.00 16.50           C  
ANISOU  319  CG2 THR A 296     1980   2150   2140   -300    -40    160       C  
ATOM    320  N   ASP A 297      15.188   9.043 -20.589  1.00 19.02           N  
ANISOU  320  N   ASP A 297     2120   2460   2650   -400    -20     70       N  
ATOM    321  CA  ASP A 297      16.538   9.625 -20.840  1.00 20.18           C  
ANISOU  321  CA  ASP A 297     2210   2640   2820   -470     10     70       C  
ATOM    322  C   ASP A 297      17.548   8.907 -19.925  1.00 19.83           C  
ANISOU  322  C   ASP A 297     2120   2650   2770   -400     40    -40       C  
ATOM    323  O   ASP A 297      18.750   9.169 -20.047  1.00 19.10           O  
ANISOU  323  O   ASP A 297     1970   2600   2690   -450     70    -70       O  
ATOM    324  CB  ASP A 297      16.562  11.143 -20.632  1.00 21.40           C  
ANISOU  324  CB  ASP A 297     2340   2700   3090   -520    -40    110       C  
ATOM    325  CG  ASP A 297      15.748  11.933 -21.650  1.00 22.84           C  
ANISOU  325  CG  ASP A 297     2560   2820   3290   -600    -70    240       C  
ATOM    326  OD1 ASP A 297      15.685  11.502 -22.819  1.00 24.43           O  
ANISOU  326  OD1 ASP A 297     2790   3100   3400   -660    -40    310       O  
ATOM    327  OD2 ASP A 297      15.164  12.963 -21.262  1.00 23.54           O  
ANISOU  327  OD2 ASP A 297     2650   2800   3500   -590   -130    270       O  
ATOM    328  N   TYR A 298      17.057   8.063 -19.012  1.00 19.01           N  
ANISOU  328  N   TYR A 298     2030   2540   2650   -310     20   -100       N  
ATOM    329  CA  TYR A 298      17.933   7.289 -18.093  1.00 18.87           C  
ANISOU  329  CA  TYR A 298     1970   2580   2630   -240     30   -190       C  
ATOM    330  C   TYR A 298      18.898   6.478 -18.959  1.00 19.63           C  
ANISOU  330  C   TYR A 298     2030   2750   2670   -260     90   -210       C  
ATOM    331  O   TYR A 298      18.398   5.734 -19.812  1.00 19.10           O  
ANISOU  331  O   TYR A 298     2000   2710   2550   -270    120   -180       O  
ATOM    332  CB  TYR A 298      17.054   6.442 -17.175  1.00 17.93           C  
ANISOU  332  CB  TYR A 298     1890   2450   2480   -150      0   -210       C  
ATOM    333  CG  TYR A 298      17.756   5.576 -16.162  1.00 17.79           C  
ANISOU  333  CG  TYR A 298     1830   2470   2450    -80    -10   -270       C  
ATOM    334  CD1 TYR A 298      18.445   6.137 -15.101  1.00 17.79           C  
ANISOU  334  CD1 TYR A 298     1780   2480   2500    -60    -40   -330       C  
ATOM    335  CD2 TYR A 298      17.607   4.201 -16.181  1.00 17.40           C  
ANISOU  335  CD2 TYR A 298     1800   2450   2360    -20     10   -280       C  
ATOM    336  CE1 TYR A 298      19.040   5.347 -14.132  1.00 18.43           C  
ANISOU  336  CE1 TYR A 298     1830   2610   2560      0    -60   -370       C  
ATOM    337  CE2 TYR A 298      18.192   3.396 -15.217  1.00 17.89           C  
ANISOU  337  CE2 TYR A 298     1830   2540   2430     40    -20   -320       C  
ATOM    338  CZ  TYR A 298      18.909   3.972 -14.185  1.00 18.15           C  
ANISOU  338  CZ  TYR A 298     1810   2590   2490     50    -50   -360       C  
ATOM    339  OH  TYR A 298      19.475   3.192 -13.222  1.00 19.07           O  
ANISOU  339  OH  TYR A 298     1890   2750   2600    120    -90   -380       O  
ATOM    340  N   LYS A 299      20.212   6.610 -18.726  1.00 20.59           N  
ANISOU  340  N   LYS A 299     2080   2920   2830   -270    110   -260       N  
ATOM    341  CA  LYS A 299      21.254   5.928 -19.554  1.00 21.85           C  
ANISOU  341  CA  LYS A 299     2190   3160   2960   -300    170   -300       C  
ATOM    342  C   LYS A 299      21.108   4.399 -19.548  1.00 21.26           C  
ANISOU  342  C   LYS A 299     2120   3110   2850   -220    190   -350       C  
ATOM    343  O   LYS A 299      21.644   3.776 -20.492  1.00 21.88           O  
ANISOU  343  O   LYS A 299     2160   3250   2900   -250    240   -380       O  
ATOM    344  CB  LYS A 299      22.661   6.361 -19.133  1.00 23.72           C  
ANISOU  344  CB  LYS A 299     2330   3430   3250   -320    180   -370       C  
ATOM    345  CG  LYS A 299      22.941   7.851 -19.296  1.00 25.66           C  
ANISOU  345  CG  LYS A 299     2560   3650   3540   -410    170   -320       C  
ATOM    346  CD  LYS A 299      22.645   8.369 -20.689  1.00 27.76           C  
ANISOU  346  CD  LYS A 299     2860   3930   3760   -520    210   -240       C  
ATOM    347  CE  LYS A 299      22.845   9.863 -20.827  1.00 30.04           C  
ANISOU  347  CE  LYS A 299     3130   4160   4120   -620    190   -180       C  
ATOM    348  NZ  LYS A 299      22.450  10.339 -22.175  1.00 31.22           N  
ANISOU  348  NZ  LYS A 299     3320   4330   4220   -730    210    -60       N  
ATOM    349  N   HIS A 300      20.435   3.816 -18.551  1.00 20.01           N  
ANISOU  349  N   HIS A 300     2000   2910   2700   -130    140   -350       N  
ATOM    350  CA  HIS A 300      20.235   2.339 -18.527  1.00 20.09           C  
ANISOU  350  CA  HIS A 300     2010   2920   2690    -60    140   -380       C  
ATOM    351  C   HIS A 300      18.771   2.012 -18.835  1.00 18.50           C  
ANISOU  351  C   HIS A 300     1900   2680   2450    -50    140   -320       C  
ATOM    352  O   HIS A 300      18.334   0.894 -18.522  1.00 18.85           O  
ANISOU  352  O   HIS A 300     1960   2710   2490     10    120   -330       O  
ATOM    353  CB  HIS A 300      20.760   1.740 -17.216  1.00 21.12           C  
ANISOU  353  CB  HIS A 300     2110   3050   2870     30     90   -420       C  
ATOM    354  CG  HIS A 300      22.248   1.785 -17.151  1.00 22.69           C  
ANISOU  354  CG  HIS A 300     2210   3290   3120     30    100   -480       C  
ATOM    355  ND1 HIS A 300      22.930   2.880 -16.671  1.00 24.52           N  
ANISOU  355  ND1 HIS A 300     2400   3540   3380    -10     90   -490       N  
ATOM    356  CD2 HIS A 300      23.178   0.894 -17.557  1.00 24.10           C  
ANISOU  356  CD2 HIS A 300     2320   3510   3330     50    140   -550       C  
ATOM    357  CE1 HIS A 300      24.224   2.661 -16.763  1.00 25.70           C  
ANISOU  357  CE1 HIS A 300     2460   3740   3570    -10    110   -560       C  
ATOM    358  NE2 HIS A 300      24.406   1.441 -17.303  1.00 26.40           N  
ANISOU  358  NE2 HIS A 300     2520   3840   3670     40    140   -600       N  
ATOM    359  N   TRP A 301      18.059   2.941 -19.473  1.00 17.05           N  
ANISOU  359  N   TRP A 301     1760   2480   2230   -120    140   -260       N  
ATOM    360  CA  TRP A 301      16.632   2.710 -19.805  1.00 15.91           C  
ANISOU  360  CA  TRP A 301     1690   2300   2050   -120    130   -210       C  
ATOM    361  C   TRP A 301      16.458   1.472 -20.688  1.00 15.66           C  
ANISOU  361  C   TRP A 301     1670   2310   1970   -120    170   -240       C  
ATOM    362  O   TRP A 301      15.542   0.696 -20.445  1.00 15.26           O  
ANISOU  362  O   TRP A 301     1660   2220   1910    -70    150   -230       O  
ATOM    363  CB  TRP A 301      15.980   3.954 -20.412  1.00 15.62           C  
ANISOU  363  CB  TRP A 301     1690   2240   2000   -200    110   -130       C  
ATOM    364  CG  TRP A 301      14.549   3.698 -20.762  1.00 14.68           C  
ANISOU  364  CG  TRP A 301     1640   2090   1850   -190    100    -80       C  
ATOM    365  CD1 TRP A 301      14.023   3.546 -22.009  1.00 14.71           C  
ANISOU  365  CD1 TRP A 301     1670   2130   1790   -250    120    -40       C  
ATOM    366  CD2 TRP A 301      13.483   3.419 -19.840  1.00 13.90           C  
ANISOU  366  CD2 TRP A 301     1570   1940   1770   -130     60    -80       C  
ATOM    367  NE1 TRP A 301      12.689   3.256 -21.928  1.00 14.06           N  
ANISOU  367  NE1 TRP A 301     1640   2000   1700   -220     90    -10       N  
ATOM    368  CE2 TRP A 301      12.329   3.161 -20.613  1.00 13.69           C  
ANISOU  368  CE2 TRP A 301     1600   1900   1700   -150     50    -30       C  
ATOM    369  CE3 TRP A 301      13.380   3.381 -18.444  1.00 13.30           C  
ANISOU  369  CE3 TRP A 301     1490   1840   1730    -60     20   -110       C  
ATOM    370  CZ2 TRP A 301      11.090   2.884 -20.033  1.00 12.95           C  
ANISOU  370  CZ2 TRP A 301     1540   1770   1610   -100     20    -20       C  
ATOM    371  CZ3 TRP A 301      12.160   3.094 -17.874  1.00 12.88           C  
ANISOU  371  CZ3 TRP A 301     1480   1750   1670    -20      0    -90       C  
ATOM    372  CH2 TRP A 301      11.032   2.847 -18.659  1.00 12.70           C  
ANISOU  372  CH2 TRP A 301     1500   1710   1620    -40      0    -50       C  
ATOM    373  N   PRO A 302      17.282   1.227 -21.737  1.00 16.44           N  
ANISOU  373  N   PRO A 302     1720   2480   2050   -170    230   -280       N  
ATOM    374  CA  PRO A 302      17.110   0.033 -22.570  1.00 16.83           C  
ANISOU  374  CA  PRO A 302     1770   2560   2060   -160    270   -330       C  
ATOM    375  C   PRO A 302      17.112  -1.280 -21.775  1.00 16.64           C  
ANISOU  375  C   PRO A 302     1740   2490   2100    -60    250   -380       C  
ATOM    376  O   PRO A 302      16.317  -2.132 -22.098  1.00 16.89           O  
ANISOU  376  O   PRO A 302     1800   2500   2110    -40    260   -390       O  
ATOM    377  CB  PRO A 302      18.301   0.077 -23.539  1.00 17.82           C  
ANISOU  377  CB  PRO A 302     1830   2780   2160   -230    340   -390       C  
ATOM    378  CG  PRO A 302      18.626   1.550 -23.629  1.00 17.89           C  
ANISOU  378  CG  PRO A 302     1830   2800   2160   -310    330   -330       C  
ATOM    379  CD  PRO A 302      18.360   2.092 -22.237  1.00 17.17           C  
ANISOU  379  CD  PRO A 302     1760   2620   2140   -240    260   -290       C  
ATOM    380  N   GLN A 303      17.989  -1.410 -20.770  1.00 16.73           N  
ANISOU  380  N   GLN A 303     1700   2480   2170      0    220   -410       N  
ATOM    381  CA  GLN A 303      18.031  -2.657 -19.954  1.00 16.78           C  
ANISOU  381  CA  GLN A 303     1690   2440   2250    100    190   -440       C  
ATOM    382  C   GLN A 303      16.777  -2.758 -19.067  1.00 16.25           C  
ANISOU  382  C   GLN A 303     1700   2310   2170    140    140   -360       C  
ATOM    383  O   GLN A 303      16.588  -3.819 -18.462  1.00 17.24           O  
ANISOU  383  O   GLN A 303     1830   2390   2330    200    100   -360       O  
ATOM    384  CB  GLN A 303      19.326  -2.778 -19.146  1.00 17.14           C  
ANISOU  384  CB  GLN A 303     1660   2490   2360    150    170   -480       C  
ATOM    385  CG  GLN A 303      20.555  -3.074 -20.001  1.00 18.14           C  
ANISOU  385  CG  GLN A 303     1690   2670   2530    130    230   -580       C  
ATOM    386  CD  GLN A 303      20.965  -1.907 -20.864  1.00 18.27           C  
ANISOU  386  CD  GLN A 303     1690   2770   2480     30    280   -590       C  
ATOM    387  OE1 GLN A 303      20.941  -0.760 -20.428  1.00 17.51           O  
ANISOU  387  OE1 GLN A 303     1620   2670   2370    -10    260   -530       O  
ATOM    388  NE2 GLN A 303      21.404  -2.204 -22.078  1.00 18.62           N  
ANISOU  388  NE2 GLN A 303     1690   2880   2500    -30    360   -660       N  
ATOM    389  N   ILE A 304      15.973  -1.696 -18.961  1.00 15.65           N  
ANISOU  389  N   ILE A 304     1680   2230   2040    100    120   -300       N  
ATOM    390  CA  ILE A 304      14.708  -1.779 -18.168  1.00 14.78           C  
ANISOU  390  CA  ILE A 304     1630   2070   1920    120     80   -240       C  
ATOM    391  C   ILE A 304      13.576  -2.071 -19.161  1.00 14.52           C  
ANISOU  391  C   ILE A 304     1650   2030   1840     90    100   -220       C  
ATOM    392  O   ILE A 304      12.750  -2.959 -18.881  1.00 13.72           O  
ANISOU  392  O   ILE A 304     1580   1890   1740    130     80   -210       O  
ATOM    393  CB  ILE A 304      14.443  -0.500 -17.348  1.00 14.55           C  
ANISOU  393  CB  ILE A 304     1610   2040   1880    110     40   -210       C  
ATOM    394  CG1 ILE A 304      15.505  -0.298 -16.261  1.00 15.00           C  
ANISOU  394  CG1 ILE A 304     1610   2110   1970    140     10   -230       C  
ATOM    395  CG2 ILE A 304      13.033  -0.523 -16.762  1.00 14.07           C  
ANISOU  395  CG2 ILE A 304     1610   1940   1800    130     10   -160       C  
ATOM    396  CD1 ILE A 304      15.353   0.972 -15.450  1.00 14.90           C  
ANISOU  396  CD1 ILE A 304     1600   2100   1960    130    -20   -220       C  
ATOM    397  N   ALA A 305      13.580  -1.351 -20.288  1.00 14.70           N  
ANISOU  397  N   ALA A 305     1680   2090   1820     20    130   -220       N  
ATOM    398  CA  ALA A 305      12.551  -1.464 -21.350  1.00 14.56           C  
ANISOU  398  CA  ALA A 305     1700   2080   1750    -30    150   -190       C  
ATOM    399  C   ALA A 305      12.527  -2.877 -21.953  1.00 14.72           C  
ANISOU  399  C   ALA A 305     1710   2110   1770    -10    180   -260       C  
ATOM    400  O   ALA A 305      11.450  -3.263 -22.430  1.00 13.77           O  
ANISOU  400  O   ALA A 305     1640   1980   1620    -30    180   -240       O  
ATOM    401  CB  ALA A 305      12.794  -0.414 -22.412  1.00 14.89           C  
ANISOU  401  CB  ALA A 305     1740   2170   1750   -120    170   -160       C  
ATOM    402  N   GLN A 306      13.647  -3.617 -21.918  1.00 15.37           N  
ANISOU  402  N   GLN A 306     1740   2200   1900     20    210   -330       N  
ATOM    403  CA  GLN A 306      13.663  -4.997 -22.487  1.00 16.65           C  
ANISOU  403  CA  GLN A 306     1880   2360   2090     40    240   -410       C  
ATOM    404  C   GLN A 306      12.626  -5.866 -21.758  1.00 16.17           C  
ANISOU  404  C   GLN A 306     1860   2210   2070    100    200   -380       C  
ATOM    405  O   GLN A 306      12.273  -6.928 -22.294  1.00 17.01           O  
ANISOU  405  O   GLN A 306     1970   2300   2200    110    220   -430       O  
ATOM    406  CB  GLN A 306      15.045  -5.658 -22.402  1.00 17.73           C  
ANISOU  406  CB  GLN A 306     1930   2500   2300     90    260   -500       C  
ATOM    407  CG  GLN A 306      15.542  -5.900 -20.980  1.00 18.17           C  
ANISOU  407  CG  GLN A 306     1970   2500   2440    170    200   -470       C  
ATOM    408  CD  GLN A 306      16.902  -6.560 -20.958  1.00 19.96           C  
ANISOU  408  CD  GLN A 306     2100   2730   2760    210    220   -570       C  
ATOM    409  OE1 GLN A 306      17.188  -7.460 -21.746  1.00 22.10           O  
ANISOU  409  OE1 GLN A 306     2320   3000   3070    220    260   -660       O  
ATOM    410  NE2 GLN A 306      17.748  -6.141 -20.027  1.00 19.72           N  
ANISOU  410  NE2 GLN A 306     2030   2700   2770    250    180   -540       N  
ATOM    411  N   PHE A 307      12.153  -5.430 -20.590  1.00 15.60           N  
ANISOU  411  N   PHE A 307     1820   2100   2000    130    150   -300       N  
ATOM    412  CA  PHE A 307      11.142  -6.231 -19.846  1.00 15.50           C  
ANISOU  412  CA  PHE A 307     1850   2020   2020    180    110   -250       C  
ATOM    413  C   PHE A 307       9.738  -5.647 -20.058  1.00 14.66           C  
ANISOU  413  C   PHE A 307     1810   1920   1850    130    100   -200       C  
ATOM    414  O   PHE A 307       8.770  -6.270 -19.586  1.00 14.65           O  
ANISOU  414  O   PHE A 307     1840   1870   1860    160     80   -170       O  
ATOM    415  CB  PHE A 307      11.522  -6.355 -18.370  1.00 15.77           C  
ANISOU  415  CB  PHE A 307     1870   2030   2090    230     60   -210       C  
ATOM    416  CG  PHE A 307      12.850  -7.034 -18.142  1.00 17.14           C  
ANISOU  416  CG  PHE A 307     1980   2190   2350    280     50   -260       C  
ATOM    417  CD1 PHE A 307      12.978  -8.406 -18.305  1.00 17.83           C  
ANISOU  417  CD1 PHE A 307     2040   2220   2510    320     50   -290       C  
ATOM    418  CD2 PHE A 307      13.966  -6.308 -17.759  1.00 17.56           C  
ANISOU  418  CD2 PHE A 307     1990   2280   2400    290     50   -270       C  
ATOM    419  CE1 PHE A 307      14.202  -9.027 -18.108  1.00 19.36           C  
ANISOU  419  CE1 PHE A 307     2170   2390   2800    370     40   -340       C  
ATOM    420  CE2 PHE A 307      15.186  -6.936 -17.548  1.00 18.17           C  
ANISOU  420  CE2 PHE A 307     1990   2350   2560    340     30   -320       C  
ATOM    421  CZ  PHE A 307      15.300  -8.291 -17.719  1.00 19.29           C  
ANISOU  421  CZ  PHE A 307     2110   2430   2790    380     30   -350       C  
ATOM    422  N   ALA A 308       9.619  -4.506 -20.748  1.00 14.46           N  
ANISOU  422  N   ALA A 308     1790   1940   1760     80    110   -180       N  
ATOM    423  CA  ALA A 308       8.273  -3.925 -20.975  1.00 13.81           C  
ANISOU  423  CA  ALA A 308     1760   1850   1640     40     90   -130       C  
ATOM    424  C   ALA A 308       7.581  -4.730 -22.072  1.00 13.52           C  
ANISOU  424  C   ALA A 308     1740   1830   1570     10    120   -160       C  
ATOM    425  O   ALA A 308       8.201  -5.082 -23.070  1.00 13.54           O  
ANISOU  425  O   ALA A 308     1710   1870   1560    -20    160   -210       O  
ATOM    426  CB  ALA A 308       8.369  -2.463 -21.333  1.00 14.01           C  
ANISOU  426  CB  ALA A 308     1780   1910   1630    -10     90    -90       C  
ATOM    427  N   PRO A 309       6.282  -5.067 -21.926  1.00 12.96           N  
ANISOU  427  N   PRO A 309     1700   1720   1500     20     90   -130       N  
ATOM    428  CA  PRO A 309       5.599  -5.855 -22.945  1.00 12.75           C  
ANISOU  428  CA  PRO A 309     1690   1710   1450    -20    110   -160       C  
ATOM    429  C   PRO A 309       5.058  -5.067 -24.140  1.00 12.13           C  
ANISOU  429  C   PRO A 309     1630   1690   1290    -90    110   -140       C  
ATOM    430  O   PRO A 309       4.631  -3.944 -23.979  1.00 11.71           O  
ANISOU  430  O   PRO A 309     1590   1640   1220   -110     80    -70       O  
ATOM    431  CB  PRO A 309       4.399  -6.429 -22.182  1.00 12.63           C  
ANISOU  431  CB  PRO A 309     1700   1630   1460     20     90   -130       C  
ATOM    432  CG  PRO A 309       4.070  -5.353 -21.173  1.00 12.59           C  
ANISOU  432  CG  PRO A 309     1710   1610   1460     30     50    -60       C  
ATOM    433  CD  PRO A 309       5.409  -4.748 -20.782  1.00 12.58           C  
ANISOU  433  CD  PRO A 309     1680   1630   1470     50     60    -70       C  
ATOM    434  N   SER A 310       5.150  -5.670 -25.320  1.00 11.80           N  
ANISOU  434  N   SER A 310     1570   1700   1210   -130    140   -200       N  
ATOM    435  CA  SER A 310       4.544  -5.057 -26.522  1.00 11.62           C  
ANISOU  435  CA  SER A 310     1570   1760   1090   -210    130   -160       C  
ATOM    436  C   SER A 310       3.041  -4.963 -26.234  1.00 10.73           C  
ANISOU  436  C   SER A 310     1490   1600    990   -210     90   -110       C  
ATOM    437  O   SER A 310       2.605  -5.593 -25.247  1.00  9.79           O  
ANISOU  437  O   SER A 310     1380   1400    940   -150     80   -110       O  
ATOM    438  CB  SER A 310       4.787  -5.915 -27.728  1.00 12.30           C  
ANISOU  438  CB  SER A 310     1630   1920   1120   -260    180   -260       C  
ATOM    439  OG  SER A 310       4.163  -7.183 -27.548  1.00 12.04           O  
ANISOU  439  OG  SER A 310     1600   1830   1140   -230    190   -320       O  
ATOM    440  N   ALA A 311       2.287  -4.226 -27.048  1.00 10.55           N  
ANISOU  440  N   ALA A 311     1480   1620    910   -260     50    -50       N  
ATOM    441  CA  ALA A 311       0.826  -4.133 -26.848  1.00 10.39           C  
ANISOU  441  CA  ALA A 311     1480   1560    900   -260      0      0       C  
ATOM    442  C   ALA A 311       0.222  -5.547 -26.943  1.00 10.42           C  
ANISOU  442  C   ALA A 311     1490   1550    920   -240     20    -70       C  
ATOM    443  O   ALA A 311      -0.624  -5.906 -26.100  1.00  9.51           O  
ANISOU  443  O   ALA A 311     1380   1370    860   -200     10    -60       O  
ATOM    444  CB  ALA A 311       0.236  -3.215 -27.886  1.00 10.82           C  
ANISOU  444  CB  ALA A 311     1540   1670    890   -330    -40     70       C  
ATOM    445  N   SER A 312       0.683  -6.324 -27.925  1.00 11.04           N  
ANISOU  445  N   SER A 312     1550   1690    950   -280     60   -160       N  
ATOM    446  CA  SER A 312       0.197  -7.711 -28.154  1.00 11.60           C  
ANISOU  446  CA  SER A 312     1620   1750   1050   -280     90   -250       C  
ATOM    447  C   SER A 312       0.493  -8.582 -26.921  1.00 11.43           C  
ANISOU  447  C   SER A 312     1590   1620   1140   -200    100   -270       C  
ATOM    448  O   SER A 312      -0.426  -9.293 -26.464  1.00 11.72           O  
ANISOU  448  O   SER A 312     1640   1590   1220   -180     90   -280       O  
ATOM    449  CB  SER A 312       0.822  -8.280 -29.415  1.00 12.31           C  
ANISOU  449  CB  SER A 312     1680   1930   1070   -340    130   -350       C  
ATOM    450  OG  SER A 312       0.230  -9.514 -29.785  1.00 12.59           O  
ANISOU  450  OG  SER A 312     1700   1950   1130   -340    150   -440       O  
ATOM    451  N   ALA A 313       1.717  -8.525 -26.387  1.00 11.39           N  
ANISOU  451  N   ALA A 313     1570   1590   1170   -160    130   -290       N  
ATOM    452  CA  ALA A 313       2.057  -9.360 -25.206  1.00 11.22           C  
ANISOU  452  CA  ALA A 313     1540   1470   1250    -90    130   -300       C  
ATOM    453  C   ALA A 313       1.284  -8.873 -23.972  1.00 10.74           C  
ANISOU  453  C   ALA A 313     1510   1360   1220    -50     90   -200       C  
ATOM    454  O   ALA A 313       0.899  -9.712 -23.137  1.00 10.83           O  
ANISOU  454  O   ALA A 313     1520   1300   1290    -20     80   -190       O  
ATOM    455  CB  ALA A 313       3.544  -9.346 -24.975  1.00 11.43           C  
ANISOU  455  CB  ALA A 313     1530   1500   1310    -60    160   -330       C  
ATOM    456  N   PHE A 314       1.075  -7.561 -23.847  1.00 10.32           N  
ANISOU  456  N   PHE A 314     1460   1340   1120    -70     70   -140       N  
ATOM    457  CA  PHE A 314       0.320  -7.036 -22.683  1.00  9.93           C  
ANISOU  457  CA  PHE A 314     1430   1250   1090    -40     30    -70       C  
ATOM    458  C   PHE A 314      -1.067  -7.689 -22.616  1.00 10.01           C  
ANISOU  458  C   PHE A 314     1450   1230   1120    -50     20    -60       C  
ATOM    459  O   PHE A 314      -1.456  -8.120 -21.533  1.00  9.73           O  
ANISOU  459  O   PHE A 314     1420   1150   1130    -20     20    -40       O  
ATOM    460  CB  PHE A 314       0.209  -5.516 -22.759  1.00  9.92           C  
ANISOU  460  CB  PHE A 314     1430   1280   1060    -60     10    -20       C  
ATOM    461  CG  PHE A 314      -0.566  -4.897 -21.631  1.00  9.62           C  
ANISOU  461  CG  PHE A 314     1390   1210   1050    -30    -20     30       C  
ATOM    462  CD1 PHE A 314       0.019  -4.725 -20.385  1.00  9.35           C  
ANISOU  462  CD1 PHE A 314     1350   1160   1050     10    -20     30       C  
ATOM    463  CD2 PHE A 314      -1.875  -4.483 -21.820  1.00  9.73           C  
ANISOU  463  CD2 PHE A 314     1400   1220   1070    -50    -50     50       C  
ATOM    464  CE1 PHE A 314      -0.690  -4.142 -19.352  1.00  9.26           C  
ANISOU  464  CE1 PHE A 314     1330   1140   1060     30    -40     50       C  
ATOM    465  CE2 PHE A 314      -2.582  -3.894 -20.786  1.00  9.55           C  
ANISOU  465  CE2 PHE A 314     1370   1180   1080    -20    -70     70       C  
ATOM    466  CZ  PHE A 314      -1.991  -3.740 -19.550  1.00  9.48           C  
ANISOU  466  CZ  PHE A 314     1350   1160   1090     10    -60     70       C  
ATOM    467  N   PHE A 315      -1.795  -7.737 -23.734  1.00 10.41           N  
ANISOU  467  N   PHE A 315     1500   1320   1130   -100     10    -80       N  
ATOM    468  CA  PHE A 315      -3.147  -8.357 -23.734  1.00 10.80           C  
ANISOU  468  CA  PHE A 315     1560   1350   1200   -110      0    -80       C  
ATOM    469  C   PHE A 315      -3.072  -9.872 -23.916  1.00 11.49           C  
ANISOU  469  C   PHE A 315     1640   1390   1330   -110     30   -150       C  
ATOM    470  O   PHE A 315      -4.099 -10.533 -23.705  1.00 11.48           O  
ANISOU  470  O   PHE A 315     1640   1360   1360   -120     20   -150       O  
ATOM    471  CB  PHE A 315      -4.042  -7.722 -24.799  1.00 11.00           C  
ANISOU  471  CB  PHE A 315     1580   1430   1170   -160    -30    -70       C  
ATOM    472  CG  PHE A 315      -4.532  -6.357 -24.408  1.00 10.69           C  
ANISOU  472  CG  PHE A 315     1540   1390   1130   -150    -70      0       C  
ATOM    473  CD1 PHE A 315      -5.584  -6.235 -23.515  1.00 10.46           C  
ANISOU  473  CD1 PHE A 315     1500   1320   1150   -130    -90     20       C  
ATOM    474  CD2 PHE A 315      -3.944  -5.207 -24.908  1.00 10.79           C  
ANISOU  474  CD2 PHE A 315     1550   1440   1110   -170   -100     40       C  
ATOM    475  CE1 PHE A 315      -6.049  -4.987 -23.140  1.00 10.51           C  
ANISOU  475  CE1 PHE A 315     1490   1330   1180   -120   -130     70       C  
ATOM    476  CE2 PHE A 315      -4.407  -3.959 -24.525  1.00 10.62           C  
ANISOU  476  CE2 PHE A 315     1520   1400   1120   -160   -140    100       C  
ATOM    477  CZ  PHE A 315      -5.458  -3.852 -23.648  1.00 10.51           C  
ANISOU  477  CZ  PHE A 315     1490   1350   1160   -130   -160    110       C  
ATOM    478  N   GLY A 316      -1.902 -10.404 -24.268  1.00 12.07           N  
ANISOU  478  N   GLY A 316     1700   1470   1420   -100     60   -210       N  
ATOM    479  CA  GLY A 316      -1.806 -11.860 -24.475  1.00 12.94           C  
ANISOU  479  CA  GLY A 316     1800   1520   1600   -100     80   -280       C  
ATOM    480  C   GLY A 316      -1.369 -12.606 -23.226  1.00 12.94           C  
ANISOU  480  C   GLY A 316     1800   1430   1690    -40     80   -250       C  
ATOM    481  O   GLY A 316      -1.905 -13.698 -22.989  1.00 12.91           O  
ANISOU  481  O   GLY A 316     1790   1350   1760    -40     80   -260       O  
ATOM    482  N   MET A 317      -0.474 -12.006 -22.437  1.00 13.14           N  
ANISOU  482  N   MET A 317     1820   1460   1710      0     70   -210       N  
ATOM    483  CA  MET A 317       0.106 -12.645 -21.222  1.00 13.85           C  
ANISOU  483  CA  MET A 317     1910   1470   1880     50     60   -160       C  
ATOM    484  C   MET A 317      -0.665 -12.293 -19.947  1.00 13.90           C  
ANISOU  484  C   MET A 317     1930   1470   1880     50     40    -60       C  
ATOM    485  O   MET A 317      -0.796 -13.181 -19.091  1.00 14.30           O  
ANISOU  485  O   MET A 317     1980   1460   1990     70     30    -20       O  
ATOM    486  CB  MET A 317       1.534 -12.143 -20.977  1.00 14.35           C  
ANISOU  486  CB  MET A 317     1950   1560   1950     80     70   -170       C  
ATOM    487  CG  MET A 317       2.503 -12.324 -22.137  1.00 15.16           C  
ANISOU  487  CG  MET A 317     2020   1690   2050     80    100   -270       C  
ATOM    488  SD  MET A 317       4.197 -11.807 -21.692  1.00 15.57           S  
ANISOU  488  SD  MET A 317     2040   1760   2120    120    100   -280       S  
ATOM    489  CE  MET A 317       3.956 -10.126 -21.131  1.00 15.24           C  
ANISOU  489  CE  MET A 317     2020   1790   1980    110     90   -190       C  
ATOM    490  N   SER A 318      -1.171 -11.060 -19.857  1.00 13.28           N  
ANISOU  490  N   SER A 318     1860   1460   1720     40     30    -30       N  
ATOM    491  CA  SER A 318      -1.803 -10.545 -18.614  1.00 12.86           C  
ANISOU  491  CA  SER A 318     1820   1420   1650     40     20     40       C  
ATOM    492  C   SER A 318      -3.205 -11.084 -18.316  1.00 13.46           C  
ANISOU  492  C   SER A 318     1900   1480   1740     10     20     60       C  
ATOM    493  O   SER A 318      -3.897 -11.594 -19.220  1.00 13.13           O  
ANISOU  493  O   SER A 318     1860   1420   1710    -20     20     20       O  
ATOM    494  CB  SER A 318      -1.866  -9.041 -18.672  1.00 12.10           C  
ANISOU  494  CB  SER A 318     1720   1380   1490     40     10     40       C  
ATOM    495  OG  SER A 318      -0.584  -8.482 -18.962  1.00 11.88           O  
ANISOU  495  OG  SER A 318     1680   1380   1450     60     10     20       O  
ATOM    496  N   ARG A 319      -3.576 -10.956 -17.044  1.00 13.60           N  
ANISOU  496  N   ARG A 319     1920   1510   1740     10     10    120       N  
ATOM    497  CA  ARG A 319      -4.943 -11.289 -16.599  1.00 14.15           C  
ANISOU  497  CA  ARG A 319     1980   1580   1810    -20     20    150       C  
ATOM    498  C   ARG A 319      -5.635  -9.932 -16.611  1.00 13.98           C  
ANISOU  498  C   ARG A 319     1950   1620   1740    -30     10    130       C  
ATOM    499  O   ARG A 319      -5.218  -9.040 -15.836  1.00 14.32           O  
ANISOU  499  O   ARG A 319     1980   1710   1750    -10     10    140       O  
ATOM    500  CB  ARG A 319      -4.967 -12.057 -15.278  1.00 14.62           C  
ANISOU  500  CB  ARG A 319     2050   1630   1880    -30     10    220       C  
ATOM    501  CG  ARG A 319      -4.295 -13.416 -15.403  1.00 15.36           C  
ANISOU  501  CG  ARG A 319     2150   1630   2050    -20      0    240       C  
ATOM    502  CD  ARG A 319      -4.727 -14.390 -14.334  1.00 16.12           C  
ANISOU  502  CD  ARG A 319     2250   1700   2180    -50    -10    330       C  
ATOM    503  NE  ARG A 319      -6.166 -14.576 -14.388  1.00 15.98           N  
ANISOU  503  NE  ARG A 319     2230   1690   2150   -100     10    330       N  
ATOM    504  CZ  ARG A 319      -6.803 -15.397 -15.220  1.00 16.14           C  
ANISOU  504  CZ  ARG A 319     2240   1650   2240   -130     20    300       C  
ATOM    505  NH1 ARG A 319      -8.120 -15.479 -15.173  1.00 15.92           N  
ANISOU  505  NH1 ARG A 319     2210   1640   2200   -180     30    300       N  
ATOM    506  NH2 ARG A 319      -6.133 -16.124 -16.098  1.00 16.25           N  
ANISOU  506  NH2 ARG A 319     2260   1580   2330   -110     10    250       N  
ATOM    507  N   ILE A 320      -6.534  -9.765 -17.577  1.00 13.94           N  
ANISOU  507  N   ILE A 320     1940   1620   1740    -50     10     90       N  
ATOM    508  CA  ILE A 320      -7.281  -8.499 -17.808  1.00 13.90           C  
ANISOU  508  CA  ILE A 320     1910   1660   1710    -60      0     70       C  
ATOM    509  C   ILE A 320      -8.653  -8.582 -17.142  1.00 14.79           C  
ANISOU  509  C   ILE A 320     1990   1790   1830    -80      0     80       C  
ATOM    510  O   ILE A 320      -9.297  -9.642 -17.222  1.00 16.21           O  
ANISOU  510  O   ILE A 320     2180   1950   2030   -110     20     90       O  
ATOM    511  CB  ILE A 320      -7.417  -8.233 -19.318  1.00 13.24           C  
ANISOU  511  CB  ILE A 320     1830   1580   1630    -70    -30     50       C  
ATOM    512  CG1 ILE A 320      -6.060  -8.215 -20.030  1.00 13.08           C  
ANISOU  512  CG1 ILE A 320     1830   1550   1590    -60    -20     30       C  
ATOM    513  CG2 ILE A 320      -8.205  -6.960 -19.570  1.00 13.20           C  
ANISOU  513  CG2 ILE A 320     1800   1600   1620    -70    -60     40       C  
ATOM    514  CD1 ILE A 320      -5.124  -7.140 -19.562  1.00 12.79           C  
ANISOU  514  CD1 ILE A 320     1790   1530   1540    -30    -30     50       C  
ATOM    515  N   GLY A 321      -9.054  -7.479 -16.524  1.00 15.33           N  
ANISOU  515  N   GLY A 321     2030   1900   1890    -70      0     70       N  
ATOM    516  CA  GLY A 321     -10.355  -7.342 -15.855  1.00 16.38           C  
ANISOU  516  CA  GLY A 321     2120   2070   2040    -90     10     50       C  
ATOM    517  C   GLY A 321     -10.848  -5.921 -16.044  1.00 17.34           C  
ANISOU  517  C   GLY A 321     2190   2210   2190    -70    -10     10       C  
ATOM    518  O   GLY A 321     -10.071  -5.082 -16.561  1.00 16.46           O  
ANISOU  518  O   GLY A 321     2090   2080   2080    -40    -40     10       O  
ATOM    519  N   MET A 322     -12.096  -5.653 -15.682  1.00 18.18           N  
ANISOU  519  N   MET A 322     2250   2340   2320    -90    -10    -20       N  
ATOM    520  CA  MET A 322     -12.621  -4.280 -15.825  1.00 19.97           C  
ANISOU  520  CA  MET A 322     2420   2570   2600    -60    -40    -70       C  
ATOM    521  C   MET A 322     -13.470  -4.011 -14.585  1.00 20.61           C  
ANISOU  521  C   MET A 322     2430   2710   2690    -70      0   -130       C  
ATOM    522  O   MET A 322     -14.226  -4.909 -14.181  1.00 20.02           O  
ANISOU  522  O   MET A 322     2350   2670   2590   -110     40   -120       O  
ATOM    523  CB  MET A 322     -13.415  -4.124 -17.131  1.00 22.61           C  
ANISOU  523  CB  MET A 322     2740   2870   2980    -60    -90    -70       C  
ATOM    524  CG  MET A 322     -13.847  -2.698 -17.435  1.00 24.28           C  
ANISOU  524  CG  MET A 322     2890   3060   3270    -30   -140    -90       C  
ATOM    525  SD  MET A 322     -14.402  -2.469 -19.157  1.00 27.44           S  
ANISOU  525  SD  MET A 322     3300   3430   3700    -40   -230    -50       S  
ATOM    526  CE  MET A 322     -15.785  -3.603 -19.219  1.00 27.81           C  
ANISOU  526  CE  MET A 322     3310   3500   3750    -80   -210    -80       C  
ATOM    527  N   GLU A 323     -13.244  -2.871 -13.937  1.00 20.93           N  
ANISOU  527  N   GLU A 323     2430   2770   2750    -40      0   -180       N  
ATOM    528  CA  GLU A 323     -14.011  -2.521 -12.716  1.00 21.76           C  
ANISOU  528  CA  GLU A 323     2460   2950   2860    -50     40   -260       C  
ATOM    529  C   GLU A 323     -14.670  -1.162 -12.896  1.00 20.09           C  
ANISOU  529  C   GLU A 323     2160   2710   2760    -10     10   -340       C  
ATOM    530  O   GLU A 323     -14.017  -0.246 -13.422  1.00 18.11           O  
ANISOU  530  O   GLU A 323     1920   2400   2560     30    -40   -340       O  
ATOM    531  CB  GLU A 323     -13.121  -2.375 -11.484  1.00 24.07           C  
ANISOU  531  CB  GLU A 323     2760   3310   3080    -50     80   -280       C  
ATOM    532  CG  GLU A 323     -12.333  -3.608 -11.126  1.00 26.93           C  
ANISOU  532  CG  GLU A 323     3190   3690   3350    -80    110   -190       C  
ATOM    533  CD  GLU A 323     -11.522  -3.420  -9.860  1.00 29.54           C  
ANISOU  533  CD  GLU A 323     3520   4100   3600    -90    140   -200       C  
ATOM    534  OE1 GLU A 323     -10.588  -4.213  -9.635  1.00 33.18           O  
ANISOU  534  OE1 GLU A 323     4040   4570   4000   -100    140   -120       O  
ATOM    535  OE2 GLU A 323     -11.847  -2.486  -9.090  1.00 33.42           O  
ANISOU  535  OE2 GLU A 323     3940   4660   4100    -90    160   -300       O  
ATOM    536  N   VAL A 324     -15.908  -1.053 -12.439  1.00 18.40           N  
ANISOU  536  N   VAL A 324     2020   2580   2390     40    -40   -180       N  
ATOM    537  CA  VAL A 324     -16.651   0.231 -12.505  1.00 18.31           C  
ANISOU  537  CA  VAL A 324     1970   2560   2420     60    -40   -190       C  
ATOM    538  C   VAL A 324     -16.782   0.697 -11.058  1.00 17.87           C  
ANISOU  538  C   VAL A 324     1880   2550   2360     80    -20   -230       C  
ATOM    539  O   VAL A 324     -17.419  -0.028 -10.261  1.00 17.30           O  
ANISOU  539  O   VAL A 324     1790   2530   2260     80    -10   -220       O  
ATOM    540  CB  VAL A 324     -18.020   0.085 -13.196  1.00 19.18           C  
ANISOU  540  CB  VAL A 324     2070   2680   2540     40    -50   -140       C  
ATOM    541  CG1 VAL A 324     -18.759   1.417 -13.235  1.00 19.37           C  
ANISOU  541  CG1 VAL A 324     2050   2690   2620     60    -50   -150       C  
ATOM    542  CG2 VAL A 324     -17.879  -0.489 -14.601  1.00 19.05           C  
ANISOU  542  CG2 VAL A 324     2090   2630   2510     10    -70   -100       C  
ATOM    543  N   THR A 325     -16.134   1.816 -10.737  1.00 17.15           N  
ANISOU  543  N   THR A 325     1770   2440   2300    110    -10   -280       N  
ATOM    544  CA  THR A 325     -16.158   2.396  -9.373  1.00 17.13           C  
ANISOU  544  CA  THR A 325     1730   2480   2300    130     10   -330       C  
ATOM    545  C   THR A 325     -16.607   3.851  -9.478  1.00 16.74           C  
ANISOU  545  C   THR A 325     1640   2400   2320    160     10   -360       C  
ATOM    546  O   THR A 325     -16.843   4.353 -10.571  1.00 16.35           O  
ANISOU  546  O   THR A 325     1600   2300   2310    150      0   -340       O  
ATOM    547  CB  THR A 325     -14.768   2.310  -8.737  1.00 17.29           C  
ANISOU  547  CB  THR A 325     1770   2510   2300    140     20   -370       C  
ATOM    548  OG1 THR A 325     -13.969   3.364  -9.277  1.00 16.45           O  
ANISOU  548  OG1 THR A 325     1660   2350   2240    150     20   -390       O  
ATOM    549  CG2 THR A 325     -14.114   0.959  -8.950  1.00 17.18           C  
ANISOU  549  CG2 THR A 325     1790   2500   2230    120     10   -330       C  
ATOM    550  N   PRO A 326     -16.764   4.577  -8.354  1.00 17.19           N  
ANISOU  550  N   PRO A 326     1660   2490   2380    180     30   -420       N  
ATOM    551  CA  PRO A 326     -17.161   5.986  -8.411  1.00 17.64           C  
ANISOU  551  CA  PRO A 326     1680   2510   2520    210     40   -460       C  
ATOM    552  C   PRO A 326     -16.185   6.889  -9.191  1.00 17.06           C  
ANISOU  552  C   PRO A 326     1620   2370   2500    210     20   -470       C  
ATOM    553  O   PRO A 326     -16.623   7.915  -9.667  1.00 18.06           O  
ANISOU  553  O   PRO A 326     1710   2450   2700    220     20   -470       O  
ATOM    554  CB  PRO A 326     -17.223   6.377  -6.925  1.00 18.15           C  
ANISOU  554  CB  PRO A 326     1700   2630   2570    230     60   -530       C  
ATOM    555  CG  PRO A 326     -17.541   5.065  -6.224  1.00 18.06           C  
ANISOU  555  CG  PRO A 326     1700   2690   2470    220     70   -510       C  
ATOM    556  CD  PRO A 326     -16.696   4.062  -6.977  1.00 17.53           C  
ANISOU  556  CD  PRO A 326     1690   2600   2370    190     50   -450       C  
ATOM    557  N   SER A 327     -14.913   6.491  -9.310  1.00 16.09           N  
ANISOU  557  N   SER A 327     1530   2240   2340    200     20   -470       N  
ATOM    558  CA  SER A 327     -13.890   7.283 -10.047  1.00 15.49           C  
ANISOU  558  CA  SER A 327     1470   2100   2310    200     10   -470       C  
ATOM    559  C   SER A 327     -13.969   7.035 -11.559  1.00 15.23           C  
ANISOU  559  C   SER A 327     1460   2030   2300    180    -20   -400       C  
ATOM    560  O   SER A 327     -13.378   7.829 -12.300  1.00 14.97           O  
ANISOU  560  O   SER A 327     1430   1950   2310    180    -30   -390       O  
ATOM    561  CB  SER A 327     -12.506   7.000  -9.537  1.00 15.15           C  
ANISOU  561  CB  SER A 327     1450   2070   2230    200     10   -500       C  
ATOM    562  OG  SER A 327     -12.213   5.617  -9.593  1.00 14.46           O  
ANISOU  562  OG  SER A 327     1400   2010   2080    180     10   -460       O  
ATOM    563  N   GLY A 328     -14.651   5.968 -11.992  1.00 14.95           N  
ANISOU  563  N   GLY A 328     1450   2020   2220    160    -20   -350       N  
ATOM    564  CA  GLY A 328     -14.781   5.664 -13.433  1.00 14.63           C  
ANISOU  564  CA  GLY A 328     1430   1950   2180    130    -40   -290       C  
ATOM    565  C   GLY A 328     -14.657   4.175 -13.716  1.00 14.32           C  
ANISOU  565  C   GLY A 328     1440   1930   2070    100    -40   -260       C  
ATOM    566  O   GLY A 328     -14.784   3.381 -12.766  1.00 14.21           O  
ANISOU  566  O   GLY A 328     1420   1960   2010    110    -30   -270       O  
ATOM    567  N   THR A 329     -14.436   3.819 -14.985  1.00 13.95           N  
ANISOU  567  N   THR A 329     1420   1870   2020     80    -60   -210       N  
ATOM    568  CA  THR A 329     -14.271   2.406 -15.418  1.00 13.74           C  
ANISOU  568  CA  THR A 329     1440   1850   1930     50    -60   -180       C  
ATOM    569  C   THR A 329     -12.768   2.147 -15.558  1.00 13.23           C  
ANISOU  569  C   THR A 329     1400   1780   1850     50    -50   -200       C  
ATOM    570  O   THR A 329     -12.093   2.939 -16.261  1.00 13.24           O  
ANISOU  570  O   THR A 329     1410   1750   1880     50    -60   -200       O  
ATOM    571  CB  THR A 329     -15.110   2.132 -16.674  1.00 13.99           C  
ANISOU  571  CB  THR A 329     1480   1880   1960     20    -80   -130       C  
ATOM    572  OG1 THR A 329     -16.471   2.408 -16.331  1.00 14.18           O  
ANISOU  572  OG1 THR A 329     1460   1920   2010     30    -80   -120       O  
ATOM    573  CG2 THR A 329     -14.974   0.719 -17.199  1.00 13.76           C  
ANISOU  573  CG2 THR A 329     1490   1860   1880    -10    -80   -110       C  
ATOM    574  N   TRP A 330     -12.274   1.089 -14.912  1.00 12.84           N  
ANISOU  574  N   TRP A 330     1380   1750   1750     50    -40   -210       N  
ATOM    575  CA  TRP A 330     -10.820   0.791 -14.929  1.00 13.07           C  
ANISOU  575  CA  TRP A 330     1430   1770   1770     50    -40   -230       C  
ATOM    576  C   TRP A 330     -10.510  -0.575 -15.536  1.00 13.10           C  
ANISOU  576  C   TRP A 330     1480   1770   1730     30    -40   -200       C  
ATOM    577  O   TRP A 330     -11.235  -1.556 -15.262  1.00 13.35           O  
ANISOU  577  O   TRP A 330     1520   1820   1740     20    -40   -190       O  
ATOM    578  CB  TRP A 330     -10.261   0.870 -13.512  1.00 13.19           C  
ANISOU  578  CB  TRP A 330     1430   1810   1770     80    -20   -260       C  
ATOM    579  CG  TRP A 330     -10.367   2.218 -12.873  1.00 13.38           C  
ANISOU  579  CG  TRP A 330     1420   1830   1840    100    -20   -300       C  
ATOM    580  CD1 TRP A 330     -11.474   2.780 -12.310  1.00 13.56           C  
ANISOU  580  CD1 TRP A 330     1400   1870   1880    110    -20   -320       C  
ATOM    581  CD2 TRP A 330      -9.292   3.153 -12.672  1.00 13.56           C  
ANISOU  581  CD2 TRP A 330     1430   1830   1890    110    -20   -330       C  
ATOM    582  NE1 TRP A 330     -11.168   4.007 -11.788  1.00 13.89           N  
ANISOU  582  NE1 TRP A 330     1420   1900   1960    130    -10   -360       N  
ATOM    583  CE2 TRP A 330      -9.838   4.264 -11.996  1.00 13.66           C  
ANISOU  583  CE2 TRP A 330     1410   1850   1940    130    -10   -370       C  
ATOM    584  CE3 TRP A 330      -7.932   3.161 -13.012  1.00 13.33           C  
ANISOU  584  CE3 TRP A 330     1430   1780   1860    110    -20   -330       C  
ATOM    585  CZ2 TRP A 330      -9.066   5.372 -11.648  1.00 13.87           C  
ANISOU  585  CZ2 TRP A 330     1410   1850   2010    150    -10   -410       C  
ATOM    586  CZ3 TRP A 330      -7.167   4.252 -12.662  1.00 13.66           C  
ANISOU  586  CZ3 TRP A 330     1450   1810   1930    130    -20   -370       C  
ATOM    587  CH2 TRP A 330      -7.732   5.344 -11.995  1.00 13.92           C  
ANISOU  587  CH2 TRP A 330     1440   1840   2010    150    -20   -410       C  
ATOM    588  N   LEU A 331      -9.462  -0.599 -16.351  1.00 13.32           N  
ANISOU  588  N   LEU A 331     1530   1770   1750     30    -40   -200       N  
ATOM    589  CA  LEU A 331      -8.964  -1.835 -16.987  1.00 13.83           C  
ANISOU  589  CA  LEU A 331     1630   1830   1790     10    -30   -190       C  
ATOM    590  C   LEU A 331      -7.856  -2.338 -16.062  1.00 13.28           C  
ANISOU  590  C   LEU A 331     1570   1770   1710     20    -20   -210       C  
ATOM    591  O   LEU A 331      -6.803  -1.665 -15.966  1.00 12.63           O  
ANISOU  591  O   LEU A 331     1490   1680   1640     40    -10   -230       O  
ATOM    592  CB  LEU A 331      -8.435  -1.514 -18.386  1.00 14.83           C  
ANISOU  592  CB  LEU A 331     1780   1940   1920    -10    -40   -180       C  
ATOM    593  CG  LEU A 331      -7.922  -2.705 -19.188  1.00 15.88           C  
ANISOU  593  CG  LEU A 331     1950   2070   2020    -30    -30   -170       C  
ATOM    594  CD1 LEU A 331      -9.055  -3.655 -19.529  1.00 16.67           C  
ANISOU  594  CD1 LEU A 331     2060   2170   2100    -50    -40   -150       C  
ATOM    595  CD2 LEU A 331      -7.244  -2.238 -20.462  1.00 17.16           C  
ANISOU  595  CD2 LEU A 331     2130   2220   2180    -40    -30   -160       C  
ATOM    596  N   THR A 332      -8.110  -3.429 -15.351  1.00 13.19           N  
ANISOU  596  N   THR A 332     1560   1770   1670     20    -10   -200       N  
ATOM    597  CA  THR A 332      -7.086  -3.960 -14.418  1.00 13.05           C  
ANISOU  597  CA  THR A 332     1550   1770   1640     30      0   -210       C  
ATOM    598  C   THR A 332      -6.205  -4.971 -15.144  1.00 12.72           C  
ANISOU  598  C   THR A 332     1540   1700   1590     20      0   -210       C  
ATOM    599  O   THR A 332      -6.694  -5.665 -16.086  1.00 12.76           O  
ANISOU  599  O   THR A 332     1570   1690   1590      0      0   -190       O  
ATOM    600  CB  THR A 332      -7.728  -4.579 -13.177  1.00 13.32           C  
ANISOU  600  CB  THR A 332     1560   1840   1660     30      0   -210       C  
ATOM    601  OG1 THR A 332      -8.566  -5.627 -13.644  1.00 13.77           O  
ANISOU  601  OG1 THR A 332     1630   1890   1710     10    -10   -180       O  
ATOM    602  CG2 THR A 332      -8.527  -3.583 -12.371  1.00 14.05           C  
ANISOU  602  CG2 THR A 332     1620   1960   1760     50      0   -220       C  
ATOM    603  N   TYR A 333      -4.954  -5.051 -14.715  1.00 12.12           N  
ANISOU  603  N   TYR A 333     1470   1620   1520     40     20   -220       N  
ATOM    604  CA  TYR A 333      -4.029  -6.010 -15.350  1.00 12.23           C  
ANISOU  604  CA  TYR A 333     1510   1610   1530     30     30   -210       C  
ATOM    605  C   TYR A 333      -3.043  -6.546 -14.313  1.00 12.39           C  
ANISOU  605  C   TYR A 333     1520   1630   1550     50     40   -210       C  
ATOM    606  O   TYR A 333      -2.633  -5.791 -13.399  1.00 12.07           O  
ANISOU  606  O   TYR A 333     1460   1620   1510     60     40   -220       O  
ATOM    607  CB  TYR A 333      -3.286  -5.345 -16.507  1.00 12.24           C  
ANISOU  607  CB  TYR A 333     1520   1590   1540     30     30   -220       C  
ATOM    608  CG  TYR A 333      -2.389  -4.197 -16.113  1.00 12.45           C  
ANISOU  608  CG  TYR A 333     1530   1620   1580     50     30   -240       C  
ATOM    609  CD1 TYR A 333      -1.082  -4.422 -15.714  1.00 12.66           C  
ANISOU  609  CD1 TYR A 333     1560   1640   1610     70     50   -240       C  
ATOM    610  CD2 TYR A 333      -2.831  -2.886 -16.169  1.00 12.62           C  
ANISOU  610  CD2 TYR A 333     1530   1640   1620     60     20   -240       C  
ATOM    611  CE1 TYR A 333      -0.239  -3.383 -15.363  1.00 12.54           C  
ANISOU  611  CE1 TYR A 333     1530   1630   1610     80     50   -250       C  
ATOM    612  CE2 TYR A 333      -1.996  -1.831 -15.837  1.00 12.79           C  
ANISOU  612  CE2 TYR A 333     1540   1660   1660     70     20   -250       C  
ATOM    613  CZ  TYR A 333      -0.697  -2.079 -15.426  1.00 12.68           C  
ANISOU  613  CZ  TYR A 333     1530   1650   1640     80     40   -260       C  
ATOM    614  OH  TYR A 333       0.124  -1.044 -15.084  1.00 12.65           O  
ANISOU  614  OH  TYR A 333     1510   1640   1660     90     30   -270       O  
ATOM    615  N   THR A 334      -2.689  -7.819 -14.467  1.00 12.80           N  
ANISOU  615  N   THR A 334     1590   1670   1610     40     40   -200       N  
ATOM    616  CA  THR A 334      -1.697  -8.481 -13.583  1.00 13.05           C  
ANISOU  616  CA  THR A 334     1610   1700   1640     50     50   -190       C  
ATOM    617  C   THR A 334      -0.934  -9.524 -14.403  1.00 13.32           C  
ANISOU  617  C   THR A 334     1670   1700   1690     50     60   -190       C  
ATOM    618  O   THR A 334      -1.513 -10.093 -15.369  1.00 12.39           O  
ANISOU  618  O   THR A 334     1580   1560   1570     40     60   -190       O  
ATOM    619  CB  THR A 334      -2.316  -9.219 -12.392  1.00 13.52           C  
ANISOU  619  CB  THR A 334     1650   1790   1700     50     40   -170       C  
ATOM    620  OG1 THR A 334      -3.046 -10.326 -12.921  1.00 14.97           O  
ANISOU  620  OG1 THR A 334     1850   1950   1890     30     30   -150       O  
ATOM    621  CG2 THR A 334      -3.202  -8.352 -11.525  1.00 13.56           C  
ANISOU  621  CG2 THR A 334     1620   1840   1690     50     30   -170       C  
ATOM    622  N   GLY A 335       0.309  -9.787 -14.018  1.00 13.53           N  
ANISOU  622  N   GLY A 335     1690   1720   1730     60     70   -180       N  
ATOM    623  CA  GLY A 335       1.081 -10.808 -14.737  1.00 14.18           C  
ANISOU  623  CA  GLY A 335     1790   1760   1830     70     90   -190       C  
ATOM    624  C   GLY A 335       2.487 -10.917 -14.206  1.00 14.45           C  
ANISOU  624  C   GLY A 335     1820   1790   1890     90    100   -180       C  
ATOM    625  O   GLY A 335       2.818 -10.211 -13.234  1.00 13.69           O  
ANISOU  625  O   GLY A 335     1690   1730   1780     90     90   -170       O  
ATOM    626  N   ALA A 336       3.271 -11.793 -14.826  1.00 15.39           N  
ANISOU  626  N   ALA A 336     1950   1870   2030     90    120   -180       N  
ATOM    627  CA  ALA A 336       4.673 -11.990 -14.415  1.00 15.85           C  
ANISOU  627  CA  ALA A 336     1990   1920   2110    110    130   -170       C  
ATOM    628  C   ALA A 336       5.483 -12.296 -15.670  1.00 16.51           C  
ANISOU  628  C   ALA A 336     2100   1970   2200    120    150   -190       C  
ATOM    629  O   ALA A 336       4.990 -13.034 -16.530  1.00 16.66           O  
ANISOU  629  O   ALA A 336     2140   1960   2230    110    160   -210       O  
ATOM    630  CB  ALA A 336       4.768 -13.083 -13.389  1.00 16.28           C  
ANISOU  630  CB  ALA A 336     2020   1970   2190    110    120   -130       C  
ATOM    631  N   ILE A 337       6.645 -11.663 -15.771  1.00 16.98           N  
ANISOU  631  N   ILE A 337     2150   2040   2260    130    160   -200       N  
ATOM    632  CA  ILE A 337       7.598 -11.815 -16.902  1.00 17.37           C  
ANISOU  632  CA  ILE A 337     2220   2060   2320    150    190   -220       C  
ATOM    633  C   ILE A 337       8.780 -12.620 -16.363  1.00 17.54           C  
ANISOU  633  C   ILE A 337     2220   2060   2380    170    200   -200       C  
ATOM    634  O   ILE A 337       9.387 -12.168 -15.380  1.00 16.58           O  
ANISOU  634  O   ILE A 337     2070   1960   2260    170    200   -170       O  
ATOM    635  CB  ILE A 337       7.959 -10.411 -17.431  1.00 17.17           C  
ANISOU  635  CB  ILE A 337     2190   2060   2270    150    190   -230       C  
ATOM    636  CG1 ILE A 337       6.698  -9.749 -17.995  1.00 17.70           C  
ANISOU  636  CG1 ILE A 337     2270   2150   2310    130    170   -240       C  
ATOM    637  CG2 ILE A 337       9.089 -10.457 -18.453  1.00 17.44           C  
ANISOU  637  CG2 ILE A 337     2230   2090   2310    160    220   -240       C  
ATOM    638  CD1 ILE A 337       6.880  -8.341 -18.487  1.00 17.50           C  
ANISOU  638  CD1 ILE A 337     2240   2140   2260    120    170   -250       C  
ATOM    639  N   LYS A 338       9.067 -13.769 -16.981  1.00 18.22           N  
ANISOU  639  N   LYS A 338     2320   2110   2500    170    220   -210       N  
ATOM    640  CA  LYS A 338      10.161 -14.654 -16.508  1.00 19.44           C  
ANISOU  640  CA  LYS A 338     2450   2240   2700    190    240   -190       C  
ATOM    641  C   LYS A 338      11.515 -14.123 -16.984  1.00 19.23           C  
ANISOU  641  C   LYS A 338     2420   2220   2680    210    260   -200       C  
ATOM    642  O   LYS A 338      11.645 -13.798 -18.182  1.00 18.41           O  
ANISOU  642  O   LYS A 338     2330   2110   2550    210    280   -230       O  
ATOM    643  CB  LYS A 338       9.945 -16.080 -17.025  1.00 21.13           C  
ANISOU  643  CB  LYS A 338     2680   2400   2960    190    250   -210       C  
ATOM    644  CG  LYS A 338      10.837 -17.157 -16.414  1.00 22.83           C  
ANISOU  644  CG  LYS A 338     2860   2570   3230    210    260   -180       C  
ATOM    645  CD  LYS A 338      10.489 -18.548 -16.920  1.00 24.93           C  
ANISOU  645  CD  LYS A 338     3140   2780   3550    210    270   -200       C  
ATOM    646  CE  LYS A 338      11.158 -19.670 -16.158  1.00 26.59           C  
ANISOU  646  CE  LYS A 338     3320   2950   3830    230    270   -160       C  
ATOM    647  NZ  LYS A 338      12.633 -19.574 -16.210  1.00 28.38           N  
ANISOU  647  NZ  LYS A 338     3530   3170   4090    250    300   -150       N  
ATOM    648  N   LEU A 339      12.466 -14.004 -16.060  1.00 19.41           N  
ANISOU  648  N   LEU A 339     2410   2250   2720    220    260   -160       N  
ATOM    649  CA  LEU A 339      13.830 -13.566 -16.433  1.00 20.07           C  
ANISOU  649  CA  LEU A 339     2480   2340   2810    240    280   -160       C  
ATOM    650  C   LEU A 339      14.598 -14.801 -16.906  1.00 20.95           C  
ANISOU  650  C   LEU A 339     2590   2400   2970    260    310   -170       C  
ATOM    651  O   LEU A 339      14.349 -15.906 -16.376  1.00 20.80           O  
ANISOU  651  O   LEU A 339     2560   2350   3000    270    310   -150       O  
ATOM    652  CB  LEU A 339      14.562 -12.889 -15.272  1.00 20.25           C  
ANISOU  652  CB  LEU A 339     2470   2390   2830    250    270   -120       C  
ATOM    653  CG  LEU A 339      14.240 -11.420 -15.016  1.00 20.56           C  
ANISOU  653  CG  LEU A 339     2510   2470   2830    230    250   -120       C  
ATOM    654  CD1 LEU A 339      12.813 -11.226 -14.521  1.00 20.45           C  
ANISOU  654  CD1 LEU A 339     2500   2480   2790    210    220   -130       C  
ATOM    655  CD2 LEU A 339      15.227 -10.845 -14.014  1.00 20.69           C  
ANISOU  655  CD2 LEU A 339     2490   2520   2850    240    240    -90       C  
ATOM    656  N   ASP A 340      15.491 -14.599 -17.870  1.00 21.64           N  
ANISOU  656  N   ASP A 340     2680   2480   3060    280    340   -190       N  
ATOM    657  CA  ASP A 340      16.316 -15.692 -18.436  1.00 22.86           C  
ANISOU  657  CA  ASP A 340     2830   2590   3260    300    370   -210       C  
ATOM    658  C   ASP A 340      17.508 -15.902 -17.503  1.00 23.03           C  
ANISOU  658  C   ASP A 340     2810   2610   3330    320    380   -160       C  
ATOM    659  O   ASP A 340      18.508 -15.186 -17.667  1.00 20.71           O  
ANISOU  659  O   ASP A 340     2500   2340   3020    330    390   -150       O  
ATOM    660  CB  ASP A 340      16.737 -15.327 -19.857  1.00 24.92           C  
ANISOU  660  CB  ASP A 340     3110   2870   3490    310    400   -250       C  
ATOM    661  CG  ASP A 340      17.530 -16.406 -20.560  1.00 26.14           C  
ANISOU  661  CG  ASP A 340     3260   2980   3690    330    440   -280       C  
ATOM    662  OD1 ASP A 340      17.589 -17.533 -20.029  1.00 26.64           O  
ANISOU  662  OD1 ASP A 340     3310   3000   3820    340    450   -270       O  
ATOM    663  OD2 ASP A 340      18.084 -16.100 -21.627  1.00 29.41           O  
ANISOU  663  OD2 ASP A 340     3680   3410   4080    340    470   -320       O  
ATOM    664  N   ASP A 341      17.394 -16.845 -16.562  1.00 24.63           N  
ANISOU  664  N   ASP A 341     2990   2790   3580    330    370   -120       N  
ATOM    665  CA  ASP A 341      18.495 -17.081 -15.588  1.00 27.39           C  
ANISOU  665  CA  ASP A 341     3300   3130   3980    340    370    -60       C  
ATOM    666  C   ASP A 341      19.696 -17.709 -16.304  1.00 26.53           C  
ANISOU  666  C   ASP A 341     3180   2990   3920    370    410    -70       C  
ATOM    667  O   ASP A 341      20.740 -17.817 -15.663  1.00 26.52           O  
ANISOU  667  O   ASP A 341     3140   2990   3950    390    410    -30       O  
ATOM    668  CB  ASP A 341      18.053 -17.923 -14.385  1.00 30.62           C  
ANISOU  668  CB  ASP A 341     3680   3530   4420    330    340    -10       C  
ATOM    669  CG  ASP A 341      17.697 -19.364 -14.706  1.00 33.39           C  
ANISOU  669  CG  ASP A 341     4040   3810   4840    340    350    -30       C  
ATOM    670  OD1 ASP A 341      17.314 -19.639 -15.852  1.00 36.36           O  
ANISOU  670  OD1 ASP A 341     4440   4160   5210    340    370    -90       O  
ATOM    671  OD2 ASP A 341      17.854 -20.207 -13.809  1.00 39.31           O  
ANISOU  671  OD2 ASP A 341     4750   4540   5640    340    340     30       O  
ATOM    672  N   LYS A 342      19.552 -18.089 -17.578  1.00 25.75           N  
ANISOU  672  N   LYS A 342     3100   2860   3820    380    440   -140       N  
ATOM    673  CA  LYS A 342      20.695 -18.681 -18.320  1.00 27.25           C  
ANISOU  673  CA  LYS A 342     3280   3020   4050    410    480   -160       C  
ATOM    674  C   LYS A 342      21.463 -17.574 -19.045  1.00 25.85           C  
ANISOU  674  C   LYS A 342     3110   2890   3830    420    500   -170       C  
ATOM    675  O   LYS A 342      22.586 -17.849 -19.504  1.00 24.97           O  
ANISOU  675  O   LYS A 342     2970   2770   3750    450    530   -180       O  
ATOM    676  CB  LYS A 342      20.228 -19.768 -19.293  1.00 29.69           C  
ANISOU  676  CB  LYS A 342     3610   3280   4390    420    500   -220       C  
ATOM    677  CG  LYS A 342      19.599 -20.991 -18.636  1.00 31.63           C  
ANISOU  677  CG  LYS A 342     3850   3460   4700    420    490   -210       C  
ATOM    678  CD  LYS A 342      20.443 -21.588 -17.518  1.00 34.31           C  
ANISOU  678  CD  LYS A 342     4140   3780   5120    430    480   -130       C  
ATOM    679  CE  LYS A 342      21.874 -21.900 -17.915  1.00 37.45           C  
ANISOU  679  CE  LYS A 342     4510   4150   5570    470    520   -140       C  
ATOM    680  NZ  LYS A 342      21.960 -22.883 -19.024  1.00 40.30           N  
ANISOU  680  NZ  LYS A 342     4880   4450   5980    490    560   -210       N  
ATOM    681  N   ASP A 343      20.883 -16.371 -19.114  1.00 24.30           N  
ANISOU  681  N   ASP A 343     2930   2740   3560    390    470   -170       N  
ATOM    682  CA  ASP A 343      21.525 -15.209 -19.787  1.00 23.69           C  
ANISOU  682  CA  ASP A 343     2850   2710   3430    390    480   -180       C  
ATOM    683  C   ASP A 343      22.747 -14.789 -18.972  1.00 22.96           C  
ANISOU  683  C   ASP A 343     2720   2640   3370    410    480   -120       C  
ATOM    684  O   ASP A 343      22.655 -14.620 -17.759  1.00 21.41           O  
ANISOU  684  O   ASP A 343     2510   2450   3180    400    450    -80       O  
ATOM    685  CB  ASP A 343      20.507 -14.075 -19.956  1.00 24.79           C  
ANISOU  685  CB  ASP A 343     3020   2900   3500    360    460   -190       C  
ATOM    686  CG  ASP A 343      21.016 -12.804 -20.620  1.00 25.66           C  
ANISOU  686  CG  ASP A 343     3130   3050   3570    360    460   -190       C  
ATOM    687  OD1 ASP A 343      22.241 -12.571 -20.620  1.00 26.23           O  
ANISOU  687  OD1 ASP A 343     3170   3140   3660    380    480   -170       O  
ATOM    688  OD2 ASP A 343      20.172 -12.059 -21.144  1.00 26.49           O  
ANISOU  688  OD2 ASP A 343     3260   3180   3620    340    440   -210       O  
ATOM    689  N   PRO A 344      23.941 -14.638 -19.589  1.00 22.28           N  
ANISOU  689  N   PRO A 344     2620   2560   3290    430    510   -120       N  
ATOM    690  CA  PRO A 344      25.126 -14.213 -18.844  1.00 22.20           C  
ANISOU  690  CA  PRO A 344     2560   2570   3300    440    510    -70       C  
ATOM    691  C   PRO A 344      24.921 -12.850 -18.158  1.00 20.67           C  
ANISOU  691  C   PRO A 344     2370   2420   3060    410    470    -30       C  
ATOM    692  O   PRO A 344      25.593 -12.589 -17.180  1.00 20.44           O  
ANISOU  692  O   PRO A 344     2310   2410   3050    410    450     20       O  
ATOM    693  CB  PRO A 344      26.226 -14.121 -19.916  1.00 22.75           C  
ANISOU  693  CB  PRO A 344     2620   2650   3370    460    550    -80       C  
ATOM    694  CG  PRO A 344      25.741 -15.033 -21.028  1.00 23.55           C  
ANISOU  694  CG  PRO A 344     2750   2720   3480    470    590   -150       C  
ATOM    695  CD  PRO A 344      24.231 -14.911 -21.005  1.00 22.93           C  
ANISOU  695  CD  PRO A 344     2710   2640   3360    440    560   -180       C  
ATOM    696  N   ASN A 345      23.972 -12.052 -18.663  1.00 19.75           N  
ANISOU  696  N   ASN A 345     2290   2330   2890    390    450    -70       N  
ATOM    697  CA  ASN A 345      23.666 -10.694 -18.131  1.00 19.93           C  
ANISOU  697  CA  ASN A 345     2310   2390   2870    370    410    -50       C  
ATOM    698  C   ASN A 345      22.574 -10.748 -17.045  1.00 18.54           C  
ANISOU  698  C   ASN A 345     2140   2220   2690    350    380    -40       C  
ATOM    699  O   ASN A 345      22.221  -9.673 -16.528  1.00 18.60           O  
ANISOU  699  O   ASN A 345     2150   2250   2660    330    350    -30       O  
ATOM    700  CB  ASN A 345      23.224  -9.757 -19.264  1.00 20.77           C  
ANISOU  700  CB  ASN A 345     2440   2530   2930    350    420    -80       C  
ATOM    701  CG  ASN A 345      24.228  -9.672 -20.397  1.00 22.28           C  
ANISOU  701  CG  ASN A 345     2620   2730   3110    370    450    -90       C  
ATOM    702  OD1 ASN A 345      25.427  -9.894 -20.207  1.00 23.37           O  
ANISOU  702  OD1 ASN A 345     2730   2870   3280    390    470    -60       O  
ATOM    703  ND2 ASN A 345      23.753  -9.335 -21.583  1.00 23.06           N  
ANISOU  703  ND2 ASN A 345     2740   2850   3170    360    460   -120       N  
ATOM    704  N   PHE A 346      22.079 -11.939 -16.689  1.00 18.17           N  
ANISOU  704  N   PHE A 346     2100   2140   2670    350    380    -40       N  
ATOM    705  CA  PHE A 346      20.994 -12.099 -15.672  1.00 17.30           C  
ANISOU  705  CA  PHE A 346     1990   2030   2550    330    350    -30       C  
ATOM    706  C   PHE A 346      21.308 -11.393 -14.343  1.00 16.95           C  
ANISOU  706  C   PHE A 346     1920   2020   2500    320    320     10       C  
ATOM    707  O   PHE A 346      20.438 -10.660 -13.837  1.00 16.34           O  
ANISOU  707  O   PHE A 346     1850   1970   2390    300    290     10       O  
ATOM    708  CB  PHE A 346      20.711 -13.583 -15.425  1.00 17.44           C  
ANISOU  708  CB  PHE A 346     2010   2000   2620    340    360    -20       C  
ATOM    709  CG  PHE A 346      19.742 -13.871 -14.302  1.00 16.92           C  
ANISOU  709  CG  PHE A 346     1940   1940   2550    320    330      0       C  
ATOM    710  CD1 PHE A 346      18.386 -13.633 -14.451  1.00 17.05           C  
ANISOU  710  CD1 PHE A 346     1980   1970   2530    300    310    -30       C  
ATOM    711  CD2 PHE A 346      20.182 -14.444 -13.120  1.00 17.26           C  
ANISOU  711  CD2 PHE A 346     1940   1990   2630    320    310     50       C  
ATOM    712  CE1 PHE A 346      17.499 -13.911 -13.421  1.00 17.11           C  
ANISOU  712  CE1 PHE A 346     1980   1980   2530    280    280    -10       C  
ATOM    713  CE2 PHE A 346      19.298 -14.731 -12.094  1.00 17.50           C  
ANISOU  713  CE2 PHE A 346     1970   2030   2650    300    280     80       C  
ATOM    714  CZ  PHE A 346      17.954 -14.464 -12.246  1.00 17.50           C  
ANISOU  714  CZ  PHE A 346     2000   2040   2610    290    270     40       C  
ATOM    715  N   LYS A 347      22.491 -11.610 -13.772  1.00 16.93           N  
ANISOU  715  N   LYS A 347     1880   2020   2530    330    320     60       N  
ATOM    716  CA  LYS A 347      22.791 -10.963 -12.467  1.00 17.65           C  
ANISOU  716  CA  LYS A 347     1940   2150   2610    320    290    100       C  
ATOM    717  C   LYS A 347      22.650  -9.443 -12.591  1.00 16.89           C  
ANISOU  717  C   LYS A 347     1860   2090   2470    300    270     80       C  
ATOM    718  O   LYS A 347      22.047  -8.852 -11.684  1.00 15.61           O  
ANISOU  718  O   LYS A 347     1690   1960   2280    280    240     80       O  
ATOM    719  CB  LYS A 347      24.162 -11.409 -11.949  1.00 19.60           C  
ANISOU  719  CB  LYS A 347     2150   2400   2900    330    300    150       C  
ATOM    720  CG  LYS A 347      24.225 -12.878 -11.560  1.00 21.47           C  
ANISOU  720  CG  LYS A 347     2370   2600   3190    340    310    180       C  
ATOM    721  CD  LYS A 347      25.575 -13.340 -11.054  1.00 23.35           C  
ANISOU  721  CD  LYS A 347     2560   2830   3480    360    310    240       C  
ATOM    722  CE  LYS A 347      25.515 -14.764 -10.553  1.00 26.14           C  
ANISOU  722  CE  LYS A 347     2890   3150   3890    370    320    280       C  
ATOM    723  NZ  LYS A 347      26.841 -15.246 -10.101  1.00 29.40           N  
ANISOU  723  NZ  LYS A 347     3250   3560   4360    380    330    340       N  
ATOM    724  N   ASP A 348      23.185  -8.845 -13.661  1.00 17.10           N  
ANISOU  724  N   ASP A 348     1900   2120   2490    310    290     60       N  
ATOM    725  CA  ASP A 348      23.092  -7.374 -13.865  1.00 17.37           C  
ANISOU  725  CA  ASP A 348     1940   2180   2490    290    270     50       C  
ATOM    726  C   ASP A 348      21.622  -6.964 -14.002  1.00 16.80           C  
ANISOU  726  C   ASP A 348     1890   2110   2380    280    250     10       C  
ATOM    727  O   ASP A 348      21.285  -5.862 -13.539  1.00 17.05           O  
ANISOU  727  O   ASP A 348     1920   2160   2390    260    220      0       O  
ATOM    728  CB  ASP A 348      23.925  -6.921 -15.071  1.00 18.31           C  
ANISOU  728  CB  ASP A 348     2050   2290   2610    300    290     40       C  
ATOM    729  CG  ASP A 348      25.419  -7.089 -14.861  1.00 19.39           C  
ANISOU  729  CG  ASP A 348     2160   2430   2780    320    300     80       C  
ATOM    730  OD1 ASP A 348      25.846  -7.062 -13.701  1.00 20.09           O  
ANISOU  730  OD1 ASP A 348     2220   2540   2880    310    280    120       O  
ATOM    731  OD2 ASP A 348      26.136  -7.283 -15.856  1.00 22.83           O  
ANISOU  731  OD2 ASP A 348     2590   2860   3220    340    340     80       O  
ATOM    732  N   GLN A 349      20.797  -7.815 -14.615  1.00 16.70           N  
ANISOU  732  N   GLN A 349     1910   2070   2370    280    270    -20       N  
ATOM    733  CA  GLN A 349      19.351  -7.519 -14.807  1.00 16.65           C  
ANISOU  733  CA  GLN A 349     1930   2060   2330    260    250    -50       C  
ATOM    734  C   GLN A 349      18.687  -7.470 -13.429  1.00 16.60           C  
ANISOU  734  C   GLN A 349     1910   2080   2320    250    220    -40       C  
ATOM    735  O   GLN A 349      17.935  -6.502 -13.172  1.00 15.67           O  
ANISOU  735  O   GLN A 349     1800   1980   2170    230    200    -60       O  
ATOM    736  CB  GLN A 349      18.694  -8.554 -15.722  1.00 17.37           C  
ANISOU  736  CB  GLN A 349     2050   2130   2430    270    280    -80       C  
ATOM    737  CG  GLN A 349      19.217  -8.524 -17.152  1.00 17.74           C  
ANISOU  737  CG  GLN A 349     2110   2160   2470    280    300   -100       C  
ATOM    738  CD  GLN A 349      18.725  -9.684 -17.985  1.00 18.93           C  
ANISOU  738  CD  GLN A 349     2280   2280   2630    290    330   -130       C  
ATOM    739  OE1 GLN A 349      18.094 -10.620 -17.489  1.00 18.62           O  
ANISOU  739  OE1 GLN A 349     2250   2220   2610    290    330   -130       O  
ATOM    740  NE2 GLN A 349      19.023  -9.630 -19.273  1.00 19.32           N  
ANISOU  740  NE2 GLN A 349     2340   2330   2670    290    350   -150       N  
ATOM    741  N   VAL A 350      18.979  -8.467 -12.579  1.00 16.29           N  
ANISOU  741  N   VAL A 350     1850   2040   2300    250    220    -10       N  
ATOM    742  CA  VAL A 350      18.418  -8.508 -11.198  1.00 15.91           C  
ANISOU  742  CA  VAL A 350     1790   2020   2240    240    200     10       C  
ATOM    743  C   VAL A 350      18.881  -7.251 -10.444  1.00 15.73           C  
ANISOU  743  C   VAL A 350     1740   2030   2200    230    170     10       C  
ATOM    744  O   VAL A 350      18.020  -6.580  -9.866  1.00 15.18           O  
ANISOU  744  O   VAL A 350     1680   1990   2100    210    150    -10       O  
ATOM    745  CB  VAL A 350      18.798  -9.806 -10.463  1.00 16.20           C  
ANISOU  745  CB  VAL A 350     1800   2040   2310    240    200     50       C  
ATOM    746  CG1 VAL A 350      18.532  -9.718  -8.966  1.00 16.36           C  
ANISOU  746  CG1 VAL A 350     1790   2110   2310    220    170     80       C  
ATOM    747  CG2 VAL A 350      18.090 -11.006 -11.070  1.00 16.04           C  
ANISOU  747  CG2 VAL A 350     1800   1980   2310    250    220     40       C  
ATOM    748  N   ILE A 351      20.183  -6.941 -10.467  1.00 15.78           N  
ANISOU  748  N   ILE A 351     1730   2040   2220    230    180     30       N  
ATOM    749  CA  ILE A 351      20.712  -5.726  -9.772  1.00 16.18           C  
ANISOU  749  CA  ILE A 351     1760   2130   2260    220    160     40       C  
ATOM    750  C   ILE A 351      19.943  -4.476 -10.239  1.00 16.40           C  
ANISOU  750  C   ILE A 351     1810   2160   2260    210    140    -10       C  
ATOM    751  O   ILE A 351      19.474  -3.700  -9.372  1.00 15.34           O  
ANISOU  751  O   ILE A 351     1660   2060   2110    190    120    -30       O  
ATOM    752  CB  ILE A 351      22.226  -5.572 -10.014  1.00 16.95           C  
ANISOU  752  CB  ILE A 351     1840   2220   2380    230    170     70       C  
ATOM    753  CG1 ILE A 351      23.031  -6.716  -9.381  1.00 17.55           C  
ANISOU  753  CG1 ILE A 351     1880   2300   2480    240    170    120       C  
ATOM    754  CG2 ILE A 351      22.699  -4.215  -9.519  1.00 16.83           C  
ANISOU  754  CG2 ILE A 351     1800   2240   2350    210    140     60       C  
ATOM    755  CD1 ILE A 351      24.509  -6.679  -9.694  1.00 17.97           C  
ANISOU  755  CD1 ILE A 351     1910   2350   2570    250    190    150       C  
ATOM    756  N   LEU A 352      19.829  -4.279 -11.556  1.00 16.76           N  
ANISOU  756  N   LEU A 352     1880   2180   2310    220    160    -30       N  
ATOM    757  CA  LEU A 352      19.135  -3.081 -12.111  1.00 17.51           C  
ANISOU  757  CA  LEU A 352     1990   2270   2400    210    150    -60       C  
ATOM    758  C   LEU A 352      17.671  -3.008 -11.648  1.00 17.22           C  
ANISOU  758  C   LEU A 352     1960   2240   2340    200    130    -90       C  
ATOM    759  O   LEU A 352      17.256  -1.938 -11.149  1.00 17.12           O  
ANISOU  759  O   LEU A 352     1940   2250   2320    180    110   -110       O  
ATOM    760  CB  LEU A 352      19.241  -3.135 -13.635  1.00 18.13           C  
ANISOU  760  CB  LEU A 352     2090   2320   2480    220    170    -70       C  
ATOM    761  CG  LEU A 352      18.536  -2.017 -14.392  1.00 18.89           C  
ANISOU  761  CG  LEU A 352     2190   2420   2570    210    160    -90       C  
ATOM    762  CD1 LEU A 352      19.070  -0.654 -13.983  1.00 19.77           C  
ANISOU  762  CD1 LEU A 352     2280   2540   2690    200    130    -90       C  
ATOM    763  CD2 LEU A 352      18.680  -2.228 -15.890  1.00 19.02           C  
ANISOU  763  CD2 LEU A 352     2230   2420   2580    210    180    -90       C  
ATOM    764  N   LEU A 353      16.909  -4.088 -11.799  1.00 16.83           N  
ANISOU  764  N   LEU A 353     1930   2180   2280    200    140    -90       N  
ATOM    765  CA  LEU A 353      15.485  -4.052 -11.380  1.00 17.03           C  
ANISOU  765  CA  LEU A 353     1970   2220   2290    190    130   -120       C  
ATOM    766  C   LEU A 353      15.365  -3.820  -9.865  1.00 17.02           C  
ANISOU  766  C   LEU A 353     1940   2250   2270    180    110   -110       C  
ATOM    767  O   LEU A 353      14.519  -2.992  -9.476  1.00 15.99           O  
ANISOU  767  O   LEU A 353     1810   2140   2130    170     90   -140       O  
ATOM    768  CB  LEU A 353      14.802  -5.348 -11.826  1.00 17.14           C  
ANISOU  768  CB  LEU A 353     2000   2210   2300    190    150   -110       C  
ATOM    769  CG  LEU A 353      14.652  -5.512 -13.337  1.00 16.75           C  
ANISOU  769  CG  LEU A 353     1980   2130   2260    200    170   -130       C  
ATOM    770  CD1 LEU A 353      14.211  -6.923 -13.695  1.00 16.96           C  
ANISOU  770  CD1 LEU A 353     2020   2130   2290    210    180   -120       C  
ATOM    771  CD2 LEU A 353      13.679  -4.485 -13.901  1.00 16.89           C  
ANISOU  771  CD2 LEU A 353     2010   2150   2260    190    150   -150       C  
ATOM    772  N   ASN A 354      16.196  -4.483  -9.052  1.00 17.43           N  
ANISOU  772  N   ASN A 354     1970   2330   2330    180    110    -80       N  
ATOM    773  CA  ASN A 354      16.110  -4.307  -7.575  1.00 18.60           C  
ANISOU  773  CA  ASN A 354     2090   2520   2460    160     90    -70       C  
ATOM    774  C   ASN A 354      16.487  -2.873  -7.197  1.00 19.13           C  
ANISOU  774  C   ASN A 354     2140   2610   2520    150     70   -100       C  
ATOM    775  O   ASN A 354      15.965  -2.394  -6.181  1.00 20.49           O  
ANISOU  775  O   ASN A 354     2300   2820   2660    140     50   -120       O  
ATOM    776  CB  ASN A 354      16.941  -5.338  -6.804  1.00 18.91           C  
ANISOU  776  CB  ASN A 354     2100   2580   2500    160     90    -20       C  
ATOM    777  CG  ASN A 354      16.309  -6.715  -6.798  1.00 18.99           C  
ANISOU  777  CG  ASN A 354     2120   2580   2520    170    100      0       C  
ATOM    778  OD1 ASN A 354      15.089  -6.843  -6.874  1.00 18.64           O  
ANISOU  778  OD1 ASN A 354     2090   2530   2460    160    100    -20       O  
ATOM    779  ND2 ASN A 354      17.126  -7.747  -6.661  1.00 18.90           N  
ANISOU  779  ND2 ASN A 354     2090   2550   2540    170    110     50       N  
ATOM    780  N   LYS A 355      17.340  -2.217  -7.987  1.00 18.84           N  
ANISOU  780  N   LYS A 355     2110   2550   2500    160     70   -100       N  
ATOM    781  CA  LYS A 355      17.735  -0.818  -7.674  1.00 20.15           C  
ANISOU  781  CA  LYS A 355     2260   2730   2670    150     50   -120       C  
ATOM    782  C   LYS A 355      16.512   0.110  -7.735  1.00 18.22           C  
ANISOU  782  C   LYS A 355     2030   2480   2420    140     40   -170       C  
ATOM    783  O   LYS A 355      16.511   1.112  -7.010  1.00 18.31           O  
ANISOU  783  O   LYS A 355     2020   2510   2430    130     20   -200       O  
ATOM    784  CB  LYS A 355      18.780  -0.301  -8.675  1.00 22.22           C  
ANISOU  784  CB  LYS A 355     2520   2960   2960    160     60   -110       C  
ATOM    785  CG  LYS A 355      19.116   1.176  -8.526  1.00 25.00           C  
ANISOU  785  CG  LYS A 355     2860   3310   3320    150     40   -130       C  
ATOM    786  CD  LYS A 355      20.042   1.763  -9.578  1.00 27.36           C  
ANISOU  786  CD  LYS A 355     3160   3580   3650    150     40   -110       C  
ATOM    787  CE  LYS A 355      21.445   1.208  -9.549  1.00 30.06           C  
ANISOU  787  CE  LYS A 355     3490   3930   4000    160     50    -70       C  
ATOM    788  NZ  LYS A 355      22.312   1.906 -10.528  1.00 31.01           N  
ANISOU  788  NZ  LYS A 355     3600   4030   4150    160     50    -50       N  
ATOM    789  N   HIS A 356      15.499  -0.220  -8.541  1.00 15.91           N  
ANISOU  789  N   HIS A 356     1760   2160   2120    150     50   -180       N  
ATOM    790  CA  HIS A 356      14.335   0.699  -8.689  1.00 15.49           C  
ANISOU  790  CA  HIS A 356     1710   2100   2070    150     40   -230       C  
ATOM    791  C   HIS A 356      13.080   0.227  -7.945  1.00 15.67           C  
ANISOU  791  C   HIS A 356     1740   2150   2070    140     40   -240       C  
ATOM    792  O   HIS A 356      12.231   1.098  -7.646  1.00 16.66           O  
ANISOU  792  O   HIS A 356     1860   2280   2190    140     30   -280       O  
ATOM    793  CB  HIS A 356      14.048   0.920 -10.175  1.00 14.46           C  
ANISOU  793  CB  HIS A 356     1610   1930   1960    150     50   -220       C  
ATOM    794  CG  HIS A 356      15.216   1.488 -10.892  1.00 13.99           C  
ANISOU  794  CG  HIS A 356     1540   1850   1920    160     50   -210       C  
ATOM    795  ND1 HIS A 356      15.576   2.808 -10.765  1.00 13.42           N  
ANISOU  795  ND1 HIS A 356     1450   1770   1870    150     30   -220       N  
ATOM    796  CD2 HIS A 356      16.114   0.919 -11.723  1.00 13.64           C  
ANISOU  796  CD2 HIS A 356     1500   1790   1890    170     70   -170       C  
ATOM    797  CE1 HIS A 356      16.654   3.036 -11.486  1.00 14.10           C  
ANISOU  797  CE1 HIS A 356     1530   1840   1980    150     30   -190       C  
ATOM    798  NE2 HIS A 356      17.000   1.893 -12.093  1.00 13.91           N  
ANISOU  798  NE2 HIS A 356     1520   1820   1940    160     60   -160       N  
ATOM    799  N   ILE A 357      12.936  -1.074  -7.693  1.00 15.76           N  
ANISOU  799  N   ILE A 357     1750   2170   2060    140     50   -220       N  
ATOM    800  CA  ILE A 357      11.724  -1.584  -6.977  1.00 15.96           C  
ANISOU  800  CA  ILE A 357     1770   2230   2060    140     50   -230       C  
ATOM    801  C   ILE A 357      11.706  -1.043  -5.545  1.00 15.74           C  
ANISOU  801  C   ILE A 357     1710   2260   2010    120     30   -250       C  
ATOM    802  O   ILE A 357      12.638  -1.362  -4.794  1.00 15.36           O  
ANISOU  802  O   ILE A 357     1650   2240   1950    120     30   -220       O  
ATOM    803  CB  ILE A 357      11.674  -3.126  -6.997  1.00 16.71           C  
ANISOU  803  CB  ILE A 357     1880   2320   2150    140     60   -180       C  
ATOM    804  CG1 ILE A 357      11.613  -3.667  -8.428  1.00 16.91           C  
ANISOU  804  CG1 ILE A 357     1930   2300   2200    150     80   -170       C  
ATOM    805  CG2 ILE A 357      10.511  -3.639  -6.153  1.00 16.81           C  
ANISOU  805  CG2 ILE A 357     1880   2370   2140    130     60   -190       C  
ATOM    806  CD1 ILE A 357      11.712  -5.171  -8.515  1.00 17.57           C  
ANISOU  806  CD1 ILE A 357     2020   2370   2290    150     90   -140       C  
ATOM    807  N   ASP A 358      10.662  -0.273  -5.198  1.00 15.34           N  
ANISOU  807  N   ASP A 358     1660   2220   1950    120     20   -290       N  
ATOM    808  CA  ASP A 358      10.479   0.305  -3.839  1.00 15.54           C  
ANISOU  808  CA  ASP A 358     1650   2310   1940    110     10   -330       C  
ATOM    809  C   ASP A 358      11.661   1.192  -3.419  1.00 15.59           C  
ANISOU  809  C   ASP A 358     1640   2320   1960    100      0   -340       C  
ATOM    810  O   ASP A 358      11.837   1.381  -2.214  1.00 15.61           O  
ANISOU  810  O   ASP A 358     1620   2380   1930     80    -10   -360       O  
ATOM    811  CB  ASP A 358      10.246  -0.799  -2.802  1.00 16.02           C  
ANISOU  811  CB  ASP A 358     1700   2430   1960     90     10   -300       C  
ATOM    812  CG  ASP A 358       8.880  -1.455  -2.890  1.00 16.24           C  
ANISOU  812  CG  ASP A 358     1730   2460   1980    100     20   -290       C  
ATOM    813  OD1 ASP A 358       7.961  -0.836  -3.457  1.00 15.70           O  
ANISOU  813  OD1 ASP A 358     1680   2370   1920    100     20   -330       O  
ATOM    814  OD2 ASP A 358       8.748  -2.578  -2.386  1.00 17.53           O  
ANISOU  814  OD2 ASP A 358     1890   2650   2120     90     20   -250       O  
ATOM    815  N   ALA A 359      12.408   1.757  -4.366  1.00 15.55           N  
ANISOU  815  N   ALA A 359     1650   2270   1990    110      0   -340       N  
ATOM    816  CA  ALA A 359      13.547   2.630  -3.995  1.00 15.45           C  
ANISOU  816  CA  ALA A 359     1620   2260   1990    100    -20   -350       C  
ATOM    817  C   ALA A 359      13.060   3.893  -3.255  1.00 15.86           C  
ANISOU  817  C   ALA A 359     1650   2330   2040     90    -30   -420       C  
ATOM    818  O   ALA A 359      13.825   4.424  -2.430  1.00 15.33           O  
ANISOU  818  O   ALA A 359     1560   2290   1970     80    -50   -440       O  
ATOM    819  CB  ALA A 359      14.312   2.994  -5.242  1.00 15.58           C  
ANISOU  819  CB  ALA A 359     1650   2220   2050    110    -10   -330       C  
ATOM    820  N   TYR A 360      11.818   4.331  -3.514  1.00 15.72           N  
ANISOU  820  N   TYR A 360     1640   2300   2030    100    -30   -460       N  
ATOM    821  CA  TYR A 360      11.253   5.567  -2.904  1.00 16.44           C  
ANISOU  821  CA  TYR A 360     1710   2400   2140     90    -40   -530       C  
ATOM    822  C   TYR A 360      11.275   5.520  -1.371  1.00 17.31           C  
ANISOU  822  C   TYR A 360     1800   2580   2200     80    -50   -560       C  
ATOM    823  O   TYR A 360      11.261   6.596  -0.744  1.00 16.95           O  
ANISOU  823  O   TYR A 360     1730   2550   2160     70    -60   -620       O  
ATOM    824  CB  TYR A 360       9.798   5.765  -3.332  1.00 16.71           C  
ANISOU  824  CB  TYR A 360     1760   2410   2180    110    -30   -550       C  
ATOM    825  CG  TYR A 360       8.831   4.813  -2.678  1.00 16.58           C  
ANISOU  825  CG  TYR A 360     1740   2450   2120    100    -20   -550       C  
ATOM    826  CD1 TYR A 360       8.232   5.141  -1.475  1.00 17.56           C  
ANISOU  826  CD1 TYR A 360     1840   2630   2210    100    -20   -600       C  
ATOM    827  CD2 TYR A 360       8.519   3.587  -3.243  1.00 16.79           C  
ANISOU  827  CD2 TYR A 360     1790   2470   2130    110    -10   -490       C  
ATOM    828  CE1 TYR A 360       7.345   4.280  -0.849  1.00 17.91           C  
ANISOU  828  CE1 TYR A 360     1870   2730   2200     90    -10   -590       C  
ATOM    829  CE2 TYR A 360       7.637   2.711  -2.629  1.00 16.66           C  
ANISOU  829  CE2 TYR A 360     1760   2500   2070    100      0   -480       C  
ATOM    830  CZ  TYR A 360       7.049   3.059  -1.426  1.00 17.39           C  
ANISOU  830  CZ  TYR A 360     1830   2650   2130    100      0   -530       C  
ATOM    831  OH  TYR A 360       6.170   2.220  -0.808  1.00 17.77           O  
ANISOU  831  OH  TYR A 360     1870   2750   2130     90      0   -520       O  
ATOM    832  N   LYS A 361      11.316   4.322  -0.782  1.00 18.28           N  
ANISOU  832  N   LYS A 361     1910   2760   2270     70    -40   -520       N  
ATOM    833  CA  LYS A 361      11.295   4.188   0.702  1.00 19.40           C  
ANISOU  833  CA  LYS A 361     2020   2990   2360     50    -40   -540       C  
ATOM    834  C   LYS A 361      12.530   4.828   1.354  1.00 19.34           C  
ANISOU  834  C   LYS A 361     2000   3010   2350     30    -60   -560       C  
ATOM    835  O   LYS A 361      12.404   5.230   2.525  1.00 19.41           O  
ANISOU  835  O   LYS A 361     1980   3080   2320     10    -70   -610       O  
ATOM    836  CB  LYS A 361      11.225   2.717   1.130  1.00 20.74           C  
ANISOU  836  CB  LYS A 361     2190   3210   2480     40    -40   -480       C  
ATOM    837  CG  LYS A 361       9.999   1.930   0.686  1.00 21.79           C  
ANISOU  837  CG  LYS A 361     2340   3330   2610     50    -20   -460       C  
ATOM    838  CD  LYS A 361       9.985   0.532   1.282  1.00 24.37           C  
ANISOU  838  CD  LYS A 361     2650   3710   2900     40    -20   -390       C  
ATOM    839  CE  LYS A 361       8.896  -0.376   0.748  1.00 26.28           C  
ANISOU  839  CE  LYS A 361     2910   3930   3140     50      0   -370       C  
ATOM    840  NZ  LYS A 361       7.542   0.175   0.975  1.00 28.91           N  
ANISOU  840  NZ  LYS A 361     3240   4290   3460     60      0   -420       N  
ATOM    841  N   THR A 362      13.654   4.953   0.632  1.00 18.60           N  
ANISOU  841  N   THR A 362     1910   2860   2290     30    -70   -520       N  
ATOM    842  CA  THR A 362      14.914   5.505   1.211  1.00 18.85           C  
ANISOU  842  CA  THR A 362     1920   2920   2320     10    -90   -530       C  
ATOM    843  C   THR A 362      15.049   7.025   1.036  1.00 18.45           C  
ANISOU  843  C   THR A 362     1870   2820   2320     10   -100   -600       C  
ATOM    844  O   THR A 362      16.102   7.556   1.433  1.00 18.50           O  
ANISOU  844  O   THR A 362     1860   2840   2330      0   -120   -600       O  
ATOM    845  CB  THR A 362      16.133   4.822   0.579  1.00 19.09           C  
ANISOU  845  CB  THR A 362     1960   2920   2370     20    -90   -450       C  
ATOM    846  OG1 THR A 362      16.159   5.166  -0.808  1.00 19.48           O  
ANISOU  846  OG1 THR A 362     2040   2890   2480     40    -80   -440       O  
ATOM    847  CG2 THR A 362      16.110   3.320   0.742  1.00 19.60           C  
ANISOU  847  CG2 THR A 362     2030   3020   2400     20    -70   -380       C  
ATOM    848  N   PHE A 363      14.042   7.711   0.493  1.00 17.99           N  
ANISOU  848  N   PHE A 363     1820   2720   2290     30   -100   -640       N  
ATOM    849  CA  PHE A 363      14.163   9.184   0.316  1.00 18.02           C  
ANISOU  849  CA  PHE A 363     1820   2670   2350     30   -120   -700       C  
ATOM    850  C   PHE A 363      12.788   9.837   0.397  1.00 17.68           C  
ANISOU  850  C   PHE A 363     1770   2620   2330     40   -110   -770       C  
ATOM    851  O   PHE A 363      11.775   9.180   0.170  1.00 16.70           O  
ANISOU  851  O   PHE A 363     1660   2500   2180     60    -90   -760       O  
ATOM    852  CB  PHE A 363      14.879   9.519  -0.995  1.00 18.38           C  
ANISOU  852  CB  PHE A 363     1880   2640   2460     40   -120   -660       C  
ATOM    853  CG  PHE A 363      14.306   8.893  -2.245  1.00 17.95           C  
ANISOU  853  CG  PHE A 363     1860   2540   2420     60   -110   -610       C  
ATOM    854  CD1 PHE A 363      13.243   9.478  -2.915  1.00 18.18           C  
ANISOU  854  CD1 PHE A 363     1890   2520   2490     80   -100   -630       C  
ATOM    855  CD2 PHE A 363      14.880   7.753  -2.790  1.00 17.84           C  
ANISOU  855  CD2 PHE A 363     1860   2530   2390     70    -90   -530       C  
ATOM    856  CE1 PHE A 363      12.732   8.910  -4.071  1.00 18.19           C  
ANISOU  856  CE1 PHE A 363     1920   2490   2500     90    -90   -590       C  
ATOM    857  CE2 PHE A 363      14.377   7.190  -3.954  1.00 18.15           C  
ANISOU  857  CE2 PHE A 363     1920   2530   2440     80    -80   -490       C  
ATOM    858  CZ  PHE A 363      13.301   7.769  -4.592  1.00 18.31           C  
ANISOU  858  CZ  PHE A 363     1950   2510   2500    100    -70   -520       C  
ATOM    859  N   PRO A 364      12.714  11.143   0.753  1.00 17.95           N  
ANISOU  859  N   PRO A 364     1790   2630   2400     40   -130   -850       N  
ATOM    860  CA  PRO A 364      11.435  11.845   0.844  1.00 18.36           C  
ANISOU  860  CA  PRO A 364     1830   2670   2480     50   -120   -920       C  
ATOM    861  C   PRO A 364      10.693  11.791  -0.498  1.00 18.12           C  
ANISOU  861  C   PRO A 364     1820   2570   2500     80   -110   -880       C  
ATOM    862  O   PRO A 364      11.275  12.133  -1.529  1.00 18.19           O  
ANISOU  862  O   PRO A 364     1840   2510   2560     80   -120   -840       O  
ATOM    863  CB  PRO A 364      11.806  13.292   1.202  1.00 18.79           C  
ANISOU  863  CB  PRO A 364     1860   2690   2590     40   -140  -1000       C  
ATOM    864  CG  PRO A 364      13.211  13.208   1.768  1.00 19.09           C  
ANISOU  864  CG  PRO A 364     1890   2760   2600     20   -160   -980       C  
ATOM    865  CD  PRO A 364      13.851  12.010   1.097  1.00 18.56           C  
ANISOU  865  CD  PRO A 364     1850   2700   2500     20   -150   -880       C  
ATOM    866  OXT PRO A 364       9.530  11.401  -0.569  1.00 18.45           O  
ANISOU  866  OXT PRO A 364     1870   2620   2520     90    -90   -890       O  
TER     867      PRO A 364                                                      
ATOM    868  N   LYS B 257      12.534 -14.736 -29.589  1.00 40.06           N  
ANISOU  868  N   LYS B 257     3560   5860   5800    240    310   -990       N  
ATOM    869  CA  LYS B 257      11.988 -13.501 -28.945  1.00 36.91           C  
ANISOU  869  CA  LYS B 257     3440   5340   5240     80    280   -610       C  
ATOM    870  C   LYS B 257      11.485 -13.778 -27.535  1.00 31.35           C  
ANISOU  870  C   LYS B 257     2920   4270   4730    210    140   -420       C  
ATOM    871  O   LYS B 257      10.720 -14.719 -27.322  1.00 30.94           O  
ANISOU  871  O   LYS B 257     2930   4000   4830    320     70   -440       O  
ATOM    872  CB  LYS B 257      10.780 -12.944 -29.708  1.00 39.06           C  
ANISOU  872  CB  LYS B 257     3880   5640   5320    -60    330   -480       C  
ATOM    873  CG  LYS B 257      11.058 -12.105 -30.948  1.00 42.56           C  
ANISOU  873  CG  LYS B 257     4240   6480   5450   -340    410   -450       C  
ATOM    874  CD  LYS B 257      11.602 -10.734 -30.619  1.00 44.14           C  
ANISOU  874  CD  LYS B 257     4530   6700   5540   -560    340   -180       C  
ATOM    875  CE  LYS B 257      11.667  -9.818 -31.823  1.00 47.13           C  
ANISOU  875  CE  LYS B 257     4890   7410   5600   -920    350    -10       C  
ATOM    876  NZ  LYS B 257      12.139  -8.463 -31.446  1.00 48.71           N  
ANISOU  876  NZ  LYS B 257     5220   7530   5760  -1160    220    290       N  
ATOM    877  N   PRO B 258      11.915 -12.989 -26.522  1.00 27.20           N  
ANISOU  877  N   PRO B 258     2450   3710   4170    150     80   -240       N  
ATOM    878  CA  PRO B 258      11.379 -13.141 -25.172  1.00 23.67           C  
ANISOU  878  CA  PRO B 258     2140   3040   3800    190    -50    -70       C  
ATOM    879  C   PRO B 258       9.851 -12.974 -25.282  1.00 19.82           C  
ANISOU  879  C   PRO B 258     1840   2460   3230    160    -30      0       C  
ATOM    880  O   PRO B 258       9.392 -12.139 -26.055  1.00 18.02           O  
ANISOU  880  O   PRO B 258     1680   2300   2870     80     40      0       O  
ATOM    881  CB  PRO B 258      12.071 -12.033 -24.371  1.00 24.07           C  
ANISOU  881  CB  PRO B 258     2200   3180   3760     80    -70     40       C  
ATOM    882  CG  PRO B 258      13.365 -11.799 -25.132  1.00 26.89           C  
ANISOU  882  CG  PRO B 258     2360   3770   4080     20      0    -80       C  
ATOM    883  CD  PRO B 258      12.995 -11.992 -26.589  1.00 27.73           C  
ANISOU  883  CD  PRO B 258     2430   4000   4110    -10    110   -210       C  
ATOM    884  N   ARG B 259       9.106 -13.757 -24.506  1.00 17.99           N  
ANISOU  884  N   ARG B 259     1680   2090   3070    200   -120     70       N  
ATOM    885  CA  ARG B 259       7.625 -13.736 -24.552  1.00 16.27           C  
ANISOU  885  CA  ARG B 259     1580   1850   2750    160   -100    100       C  
ATOM    886  C   ARG B 259       7.078 -12.303 -24.510  1.00 14.86           C  
ANISOU  886  C   ARG B 259     1480   1750   2410    100    -60    100       C  
ATOM    887  O   ARG B 259       6.158 -12.024 -25.295  1.00 13.94           O  
ANISOU  887  O   ARG B 259     1420   1650   2230    110    -30     60       O  
ATOM    888  CB  ARG B 259       7.061 -14.576 -23.401  1.00 16.63           C  
ANISOU  888  CB  ARG B 259     1660   1840   2820    100   -220    240       C  
ATOM    889  CG  ARG B 259       5.545 -14.739 -23.401  1.00 16.06           C  
ANISOU  889  CG  ARG B 259     1660   1820   2610     30   -210    240       C  
ATOM    890  CD  ARG B 259       5.150 -15.785 -22.372  1.00 17.59           C  
ANISOU  890  CD  ARG B 259     1870   2000   2810   -110   -350    420       C  
ATOM    891  NE  ARG B 259       3.738 -16.163 -22.337  1.00 17.61           N  
ANISOU  891  NE  ARG B 259     1910   2110   2670   -240   -350    430       N  
ATOM    892  CZ  ARG B 259       2.867 -15.873 -21.368  1.00 18.20           C  
ANISOU  892  CZ  ARG B 259     1950   2480   2490   -420   -360    480       C  
ATOM    893  NH1 ARG B 259       3.242 -15.205 -20.287  1.00 18.68           N  
ANISOU  893  NH1 ARG B 259     1930   2750   2420   -490   -380    510       N  
ATOM    894  NH2 ARG B 259       1.618 -16.298 -21.467  1.00 18.44           N  
ANISOU  894  NH2 ARG B 259     1980   2640   2380   -550   -350    470       N  
ATOM    895  N   GLN B 260       7.657 -11.421 -23.687  1.00 14.33           N  
ANISOU  895  N   GLN B 260     1400   1720   2320     60   -100    130       N  
ATOM    896  CA  GLN B 260       7.098 -10.046 -23.552  1.00 14.00           C  
ANISOU  896  CA  GLN B 260     1430   1670   2220     30   -130     80       C  
ATOM    897  C   GLN B 260       7.285  -9.199 -24.824  1.00 14.15           C  
ANISOU  897  C   GLN B 260     1500   1620   2250      0   -130    110       C  
ATOM    898  O   GLN B 260       6.582  -8.179 -24.930  1.00 14.53           O  
ANISOU  898  O   GLN B 260     1630   1570   2320     10   -220     80       O  
ATOM    899  CB  GLN B 260       7.668  -9.298 -22.335  1.00 14.60           C  
ANISOU  899  CB  GLN B 260     1460   1790   2290    -20   -190     40       C  
ATOM    900  CG  GLN B 260       9.164  -9.003 -22.353  1.00 15.17           C  
ANISOU  900  CG  GLN B 260     1490   1880   2400    -90   -190    100       C  
ATOM    901  CD  GLN B 260      10.069 -10.144 -21.962  1.00 15.44           C  
ANISOU  901  CD  GLN B 260     1410   1990   2470    -80   -190    180       C  
ATOM    902  OE1 GLN B 260       9.668 -11.302 -21.909  1.00 15.42           O  
ANISOU  902  OE1 GLN B 260     1390   1970   2500    -20   -210    230       O  
ATOM    903  NE2 GLN B 260      11.318  -9.808 -21.663  1.00 16.14           N  
ANISOU  903  NE2 GLN B 260     1410   2160   2570   -140   -210    200       N  
ATOM    904  N   LYS B 261       8.163  -9.597 -25.749  1.00 14.31           N  
ANISOU  904  N   LYS B 261     1470   1720   2250    -60    -60    150       N  
ATOM    905  CA  LYS B 261       8.389  -8.800 -26.987  1.00 15.37           C  
ANISOU  905  CA  LYS B 261     1630   1900   2310   -200    -70    240       C  
ATOM    906  C   LYS B 261       7.718  -9.462 -28.194  1.00 15.56           C  
ANISOU  906  C   LYS B 261     1630   2040   2250   -200      0    210       C  
ATOM    907  O   LYS B 261       7.863  -8.924 -29.290  1.00 16.88           O  
ANISOU  907  O   LYS B 261     1790   2330   2290   -370    -20    310       O  
ATOM    908  CB  LYS B 261       9.883  -8.611 -27.257  1.00 16.57           C  
ANISOU  908  CB  LYS B 261     1670   2220   2410   -360    -30    270       C  
ATOM    909  CG  LYS B 261      10.632  -7.804 -26.206  1.00 16.91           C  
ANISOU  909  CG  LYS B 261     1730   2180   2520   -420   -110    300       C  
ATOM    910  CD  LYS B 261      10.096  -6.392 -26.040  1.00 17.68           C  
ANISOU  910  CD  LYS B 261     1990   2040   2680   -490   -280    390       C  
ATOM    911  CE  LYS B 261      10.927  -5.560 -25.087  1.00 18.59           C  
ANISOU  911  CE  LYS B 261     2110   2090   2870   -590   -360    370       C  
ATOM    912  NZ  LYS B 261      10.364  -4.207 -24.897  1.00 20.03           N  
ANISOU  912  NZ  LYS B 261     2450   1960   3200   -630   -570    390       N  
ATOM    913  N   ARG B 262       7.015 -10.579 -28.000  1.00 14.79           N  
ANISOU  913  N   ARG B 262     1510   1920   2190    -60     50    100       N  
ATOM    914  CA  ARG B 262       6.343 -11.237 -29.151  1.00 15.28           C  
ANISOU  914  CA  ARG B 262     1540   2100   2170    -70    120     30       C  
ATOM    915  C   ARG B 262       5.154 -10.401 -29.635  1.00 15.42           C  
ANISOU  915  C   ARG B 262     1660   2090   2100   -100     40    140       C  
ATOM    916  O   ARG B 262       4.536  -9.676 -28.816  1.00 14.54           O  
ANISOU  916  O   ARG B 262     1640   1810   2070    -20    -70    170       O  
ATOM    917  CB  ARG B 262       5.843 -12.628 -28.759  1.00 14.94           C  
ANISOU  917  CB  ARG B 262     1470   1980   2230     50    160   -110       C  
ATOM    918  CG  ARG B 262       6.962 -13.573 -28.363  1.00 15.90           C  
ANISOU  918  CG  ARG B 262     1470   2060   2510    120    170   -210       C  
ATOM    919  CD  ARG B 262       6.476 -14.904 -27.853  1.00 16.15           C  
ANISOU  919  CD  ARG B 262     1510   1920   2710    210    110   -260       C  
ATOM    920  NE  ARG B 262       7.625 -15.687 -27.422  1.00 17.71           N  
ANISOU  920  NE  ARG B 262     1590   2010   3130    300     40   -330       N  
ATOM    921  CZ  ARG B 262       7.550 -16.842 -26.779  1.00 18.93           C  
ANISOU  921  CZ  ARG B 262     1760   1920   3510    370   -110   -310       C  
ATOM    922  NH1 ARG B 262       6.376 -17.368 -26.474  1.00 18.69           N  
ANISOU  922  NH1 ARG B 262     1850   1780   3470    290   -170   -210       N  
ATOM    923  NH2 ARG B 262       8.655 -17.459 -26.419  1.00 21.02           N  
ANISOU  923  NH2 ARG B 262     1900   2060   4020    480   -230   -360       N  
ATOM    924  N   THR B 263       4.868 -10.496 -30.936  1.00 16.57           N  
ANISOU  924  N   THR B 263     1770   2430   2100   -200     70    160       N  
ATOM    925  CA  THR B 263       3.706  -9.793 -31.531  1.00 17.32           C  
ANISOU  925  CA  THR B 263     1940   2510   2130   -220    -50    290       C  
ATOM    926  C   THR B 263       2.848 -10.834 -32.247  1.00 17.11           C  
ANISOU  926  C   THR B 263     1850   2660   1990   -210     50    150       C  
ATOM    927  O   THR B 263       3.337 -11.433 -33.216  1.00 18.18           O  
ANISOU  927  O   THR B 263     1860   3060   1990   -330    170     50       O  
ATOM    928  CB  THR B 263       4.126  -8.681 -32.492  1.00 19.74           C  
ANISOU  928  CB  THR B 263     2280   2910   2310   -460   -180    550       C  
ATOM    929  OG1 THR B 263       4.945  -7.793 -31.740  1.00 20.51           O  
ANISOU  929  OG1 THR B 263     2450   2800   2540   -490   -290    650       O  
ATOM    930  CG2 THR B 263       2.946  -7.943 -33.085  1.00 21.09           C  
ANISOU  930  CG2 THR B 263     2530   3010   2470   -460   -390    730       C  
ATOM    931  N   ALA B 264       1.628 -11.049 -31.764  1.00 16.05           N  
ANISOU  931  N   ALA B 264     1760   2430   1910    -70     20     90       N  
ATOM    932  CA  ALA B 264       0.723 -12.026 -32.401  1.00 16.07           C  
ANISOU  932  CA  ALA B 264     1690   2600   1810    -80    100    -50       C  
ATOM    933  C   ALA B 264       0.186 -11.455 -33.720  1.00 17.67           C  
ANISOU  933  C   ALA B 264     1870   3020   1820   -200     30     80       C  
ATOM    934  O   ALA B 264      -0.100 -10.246 -33.772  1.00 18.38           O  
ANISOU  934  O   ALA B 264     2030   3010   1940   -190   -160    300       O  
ATOM    935  CB  ALA B 264      -0.409 -12.362 -31.462  1.00 15.19           C  
ANISOU  935  CB  ALA B 264     1610   2400   1760     40     80   -130       C  
ATOM    936  N   THR B 265       0.120 -12.309 -34.747  1.00 12.76           N  
ANISOU  936  N   THR B 265     1820   1700   1340    120    350   -120       N  
ATOM    937  CA  THR B 265      -0.426 -12.010 -36.098  1.00 13.69           C  
ANISOU  937  CA  THR B 265     2050   1850   1300    160    360   -100       C  
ATOM    938  C   THR B 265      -1.096 -13.295 -36.594  1.00 14.12           C  
ANISOU  938  C   THR B 265     2190   1910   1270    200    260   -210       C  
ATOM    939  O   THR B 265      -0.993 -14.285 -35.881  1.00 13.47           O  
ANISOU  939  O   THR B 265     2090   1770   1260    190    230   -280       O  
ATOM    940  CB  THR B 265       0.665 -11.559 -37.074  1.00 15.25           C  
ANISOU  940  CB  THR B 265     2260   2120   1410    190    520    -40       C  
ATOM    941  OG1 THR B 265       1.585 -12.648 -37.130  1.00 15.72           O  
ANISOU  941  OG1 THR B 265     2280   2220   1480    250    580   -130       O  
ATOM    942  CG2 THR B 265       1.353 -10.268 -36.673  1.00 15.37           C  
ANISOU  942  CG2 THR B 265     2200   2110   1520    100    630     60       C  
ATOM    943  N   LYS B 266      -1.739 -13.295 -37.762  1.00 15.69           N  
ANISOU  943  N   LYS B 266     2490   2170   1300    240    220   -230       N  
ATOM    944  CA  LYS B 266      -2.365 -14.557 -38.251  1.00 17.00           C  
ANISOU  944  CA  LYS B 266     2750   2330   1390    250    110   -370       C  
ATOM    945  C   LYS B 266      -1.292 -15.646 -38.415  1.00 17.40           C  
ANISOU  945  C   LYS B 266     2860   2330   1420    310    200   -460       C  
ATOM    946  O   LYS B 266      -1.626 -16.812 -38.167  1.00 17.59           O  
ANISOU  946  O   LYS B 266     2950   2260   1480    290    130   -580       O  
ATOM    947  CB  LYS B 266      -3.117 -14.325 -39.565  1.00 19.29           C  
ANISOU  947  CB  LYS B 266     3140   2720   1470    290     30   -380       C  
ATOM    948  CG  LYS B 266      -4.301 -13.377 -39.441  1.00 19.92           C  
ANISOU  948  CG  LYS B 266     3150   2860   1560    270    -90   -300       C  
ATOM    949  CD  LYS B 266      -4.993 -13.002 -40.751  1.00 22.67           C  
ANISOU  949  CD  LYS B 266     3600   3350   1670    350   -190   -280       C  
ATOM    950  CE  LYS B 266      -6.130 -12.027 -40.502  1.00 23.03           C  
ANISOU  950  CE  LYS B 266     3550   3460   1750    380   -300   -180       C  
ATOM    951  NZ  LYS B 266      -6.765 -11.569 -41.755  1.00 25.84           N  
ANISOU  951  NZ  LYS B 266     3990   3960   1860    500   -410   -140       N  
ATOM    952  N   ALA B 267      -0.050 -15.266 -38.744  1.00 17.53           N  
ANISOU  952  N   ALA B 267     2850   2400   1410    390    370   -410       N  
ATOM    953  CA  ALA B 267       1.068 -16.224 -38.962  1.00 18.78           C  
ANISOU  953  CA  ALA B 267     3040   2550   1550    510    490   -490       C  
ATOM    954  C   ALA B 267       1.738 -16.683 -37.649  1.00 17.94           C  
ANISOU  954  C   ALA B 267     2810   2380   1640    520    500   -480       C  
ATOM    955  O   ALA B 267       2.577 -17.584 -37.724  1.00 18.92           O  
ANISOU  955  O   ALA B 267     2950   2480   1760    650    570   -550       O  
ATOM    956  CB  ALA B 267       2.080 -15.597 -39.890  1.00 19.94           C  
ANISOU  956  CB  ALA B 267     3170   2820   1590    580    670   -420       C  
ATOM    957  N   TYR B 268       1.431 -16.042 -36.517  1.00 16.90           N  
ANISOU  957  N   TYR B 268     2550   2220   1650    420    430   -400       N  
ATOM    958  CA  TYR B 268       1.967 -16.375 -35.164  1.00 16.70           C  
ANISOU  958  CA  TYR B 268     2420   2150   1770    430    410   -380       C  
ATOM    959  C   TYR B 268       0.902 -15.837 -34.208  1.00 15.40           C  
ANISOU  959  C   TYR B 268     2230   1930   1690    290    300   -340       C  
ATOM    960  O   TYR B 268       1.068 -14.715 -33.665  1.00 14.88           O  
ANISOU  960  O   TYR B 268     2050   1910   1690    230    310   -260       O  
ATOM    961  CB  TYR B 268       3.385 -15.816 -35.011  1.00 17.66           C  
ANISOU  961  CB  TYR B 268     2360   2400   1950    470    530   -330       C  
ATOM    962  CG  TYR B 268       4.119 -16.160 -33.736  1.00 17.82           C  
ANISOU  962  CG  TYR B 268     2250   2430   2090    520    490   -320       C  
ATOM    963  CD1 TYR B 268       4.488 -17.466 -33.456  1.00 18.94           C  
ANISOU  963  CD1 TYR B 268     2450   2510   2240    680    480   -370       C  
ATOM    964  CD2 TYR B 268       4.564 -15.171 -32.873  1.00 17.40           C  
ANISOU  964  CD2 TYR B 268     2020   2450   2130    420    480   -260       C  
ATOM    965  CE1 TYR B 268       5.191 -17.796 -32.308  1.00 19.31           C  
ANISOU  965  CE1 TYR B 268     2380   2590   2370    770    430   -340       C  
ATOM    966  CE2 TYR B 268       5.288 -15.481 -31.731  1.00 17.80           C  
ANISOU  966  CE2 TYR B 268     1950   2550   2260    480    420   -260       C  
ATOM    967  CZ  TYR B 268       5.603 -16.797 -31.446  1.00 18.72           C  
ANISOU  967  CZ  TYR B 268     2120   2630   2370    660    390   -290       C  
ATOM    968  OH  TYR B 268       6.316 -17.118 -30.329  1.00 19.32           O  
ANISOU  968  OH  TYR B 268     2080   2760   2500    760    320   -270       O  
ATOM    969  N   ASN B 269      -0.174 -16.622 -34.048  1.00 15.44           N  
ANISOU  969  N   ASN B 269     2340   1840   1690    250    200   -390       N  
ATOM    970  CA  ASN B 269      -1.391 -16.203 -33.293  1.00 14.51           C  
ANISOU  970  CA  ASN B 269     2190   1690   1630    130    110   -360       C  
ATOM    971  C   ASN B 269      -1.166 -16.107 -31.775  1.00 13.96           C  
ANISOU  971  C   ASN B 269     2050   1590   1670    110    110   -310       C  
ATOM    972  O   ASN B 269      -0.062 -16.426 -31.281  1.00 13.72           O  
ANISOU  972  O   ASN B 269     1980   1560   1670    190    140   -300       O  
ATOM    973  CB  ASN B 269      -2.604 -17.039 -33.731  1.00 15.21           C  
ANISOU  973  CB  ASN B 269     2380   1720   1680     60     30   -440       C  
ATOM    974  CG  ASN B 269      -2.558 -18.496 -33.321  1.00 15.90           C  
ANISOU  974  CG  ASN B 269     2580   1660   1800     50     20   -510       C  
ATOM    975  OD1 ASN B 269      -2.101 -18.829 -32.232  1.00 15.48           O  
ANISOU  975  OD1 ASN B 269     2520   1530   1830     80     50   -460       O  
ATOM    976  ND2 ASN B 269      -3.092 -19.362 -34.165  1.00 16.93           N  
ANISOU  976  ND2 ASN B 269     2840   1720   1870     10    -30   -620       N  
ATOM    977  N   VAL B 270      -2.199 -15.616 -31.074  1.00 13.38           N  
ANISOU  977  N   VAL B 270     1940   1510   1640     20     60   -270       N  
ATOM    978  CA  VAL B 270      -2.143 -15.413 -29.600  1.00 13.04           C  
ANISOU  978  CA  VAL B 270     1850   1440   1660      0     50   -220       C  
ATOM    979  C   VAL B 270      -1.829 -16.743 -28.900  1.00 13.55           C  
ANISOU  979  C   VAL B 270     2000   1410   1740     40     50   -230       C  
ATOM    980  O   VAL B 270      -1.030 -16.717 -27.962  1.00 13.12           O  
ANISOU  980  O   VAL B 270     1910   1380   1700    100     50   -200       O  
ATOM    981  CB  VAL B 270      -3.442 -14.767 -29.086  1.00 12.69           C  
ANISOU  981  CB  VAL B 270     1770   1410   1640    -90     30   -200       C  
ATOM    982  CG1 VAL B 270      -3.468 -14.675 -27.575  1.00 12.38           C  
ANISOU  982  CG1 VAL B 270     1720   1350   1630   -100     40   -160       C  
ATOM    983  CG2 VAL B 270      -3.671 -13.395 -29.713  1.00 12.70           C  
ANISOU  983  CG2 VAL B 270     1720   1480   1620    -80     40   -170       C  
ATOM    984  N   THR B 271      -2.421 -17.855 -29.353  1.00 14.43           N  
ANISOU  984  N   THR B 271     2220   1420   1840     10     40   -280       N  
ATOM    985  CA  THR B 271      -2.161 -19.177 -28.725  1.00 15.67           C  
ANISOU  985  CA  THR B 271     2510   1430   2010     50     50   -270       C  
ATOM    986  C   THR B 271      -0.701 -19.586 -28.948  1.00 15.98           C  
ANISOU  986  C   THR B 271     2570   1480   2020    240     80   -280       C  
ATOM    987  O   THR B 271      -0.070 -20.088 -27.994  1.00 16.36           O  
ANISOU  987  O   THR B 271     2650   1480   2080    350     70   -230       O  
ATOM    988  CB  THR B 271      -3.116 -20.248 -29.268  1.00 17.29           C  
ANISOU  988  CB  THR B 271     2860   1490   2220    -50     40   -340       C  
ATOM    989  OG1 THR B 271      -4.424 -19.970 -28.774  1.00 17.15           O  
ANISOU  989  OG1 THR B 271     2780   1500   2240   -220     20   -320       O  
ATOM    990  CG2 THR B 271      -2.737 -21.652 -28.854  1.00 18.97           C  
ANISOU  990  CG2 THR B 271     3270   1500   2440     10     70   -340       C  
ATOM    991  N   GLN B 272      -0.199 -19.378 -30.164  1.00 16.14           N  
ANISOU  991  N   GLN B 272     2570   1560   2010    300    110   -340       N  
ATOM    992  CA  GLN B 272       1.196 -19.755 -30.514  1.00 17.24           C  
ANISOU  992  CA  GLN B 272     2690   1740   2120    490    160   -360       C  
ATOM    993  C   GLN B 272       2.186 -18.887 -29.730  1.00 16.54           C  
ANISOU  993  C   GLN B 272     2400   1820   2070    540    150   -290       C  
ATOM    994  O   GLN B 272       3.179 -19.428 -29.221  1.00 17.23           O  
ANISOU  994  O   GLN B 272     2450   1930   2170    710    150   -270       O  
ATOM    995  CB  GLN B 272       1.417 -19.627 -32.027  1.00 17.93           C  
ANISOU  995  CB  GLN B 272     2790   1890   2140    520    220   -440       C  
ATOM    996  CG  GLN B 272       0.760 -20.731 -32.854  1.00 19.10           C  
ANISOU  996  CG  GLN B 272     3160   1870   2230    510    210   -550       C  
ATOM    997  CD  GLN B 272       0.849 -20.503 -34.347  1.00 19.47           C  
ANISOU  997  CD  GLN B 272     3240   2000   2150    540    260   -630       C  
ATOM    998  OE1 GLN B 272       0.533 -19.426 -34.855  1.00 18.83           O  
ANISOU  998  OE1 GLN B 272     3070   2060   2030    460    250   -600       O  
ATOM    999  NE2 GLN B 272       1.216 -21.547 -35.076  1.00 21.03           N  
ANISOU  999  NE2 GLN B 272     3610   2100   2280    660    310   -740       N  
ATOM   1000  N   ALA B 273       1.905 -17.593 -29.621  1.00 15.61           N  
ANISOU 1000  N   ALA B 273     2160   1800   1970    410    140   -260       N  
ATOM   1001  CA  ALA B 273       2.836 -16.673 -28.934  1.00 15.71           C  
ANISOU 1001  CA  ALA B 273     1990   1960   2020    410    130   -230       C  
ATOM   1002  C   ALA B 273       2.612 -16.615 -27.417  1.00 15.17           C  
ANISOU 1002  C   ALA B 273     1920   1870   1970    380     50   -190       C  
ATOM   1003  O   ALA B 273       3.630 -16.505 -26.712  1.00 15.83           O  
ANISOU 1003  O   ALA B 273     1880   2070   2060    450      0   -170       O  
ATOM   1004  CB  ALA B 273       2.691 -15.303 -29.537  1.00 15.55           C  
ANISOU 1004  CB  ALA B 273     1890   2010   2010    280    170   -220       C  
ATOM   1005  N   PHE B 274       1.374 -16.770 -26.921  1.00 13.98           N  
ANISOU 1005  N   PHE B 274     1890   1610   1810    300     20   -170       N  
ATOM   1006  CA  PHE B 274       1.169 -16.586 -25.457  1.00 14.00           C  
ANISOU 1006  CA  PHE B 274     1910   1620   1790    280    -30   -120       C  
ATOM   1007  C   PHE B 274       0.417 -17.732 -24.772  1.00 14.86           C  
ANISOU 1007  C   PHE B 274     2190   1590   1870    300    -30    -70       C  
ATOM   1008  O   PHE B 274       0.020 -17.539 -23.600  1.00 14.25           O  
ANISOU 1008  O   PHE B 274     2140   1520   1750    270    -50    -30       O  
ATOM   1009  CB  PHE B 274       0.444 -15.259 -25.240  1.00 12.88           C  
ANISOU 1009  CB  PHE B 274     1720   1520   1660    140    -30   -130       C  
ATOM   1010  CG  PHE B 274       1.089 -14.115 -25.979  1.00 12.44           C  
ANISOU 1010  CG  PHE B 274     1540   1550   1640     90      0   -170       C  
ATOM   1011  CD1 PHE B 274       2.366 -13.686 -25.643  1.00 13.39           C  
ANISOU 1011  CD1 PHE B 274     1530   1780   1780    100    -30   -190       C  
ATOM   1012  CD2 PHE B 274       0.418 -13.463 -27.001  1.00 11.72           C  
ANISOU 1012  CD2 PHE B 274     1460   1430   1560     20     50   -170       C  
ATOM   1013  CE1 PHE B 274       2.964 -12.643 -26.335  1.00 13.57           C  
ANISOU 1013  CE1 PHE B 274     1440   1870   1850     10     20   -210       C  
ATOM   1014  CE2 PHE B 274       1.008 -12.404 -27.676  1.00 12.07           C  
ANISOU 1014  CE2 PHE B 274     1430   1520   1630    -30    100   -170       C  
ATOM   1015  CZ  PHE B 274       2.278 -11.994 -27.341  1.00 12.87           C  
ANISOU 1015  CZ  PHE B 274     1410   1710   1770    -50     90   -190       C  
ATOM   1016  N   GLY B 275       0.198 -18.855 -25.461  1.00 15.86           N  
ANISOU 1016  N   GLY B 275     2440   1580   2010    340      0    -80       N  
ATOM   1017  CA  GLY B 275      -0.491 -19.997 -24.833  1.00 17.58           C  
ANISOU 1017  CA  GLY B 275     2850   1630   2210    330     30    -30       C  
ATOM   1018  C   GLY B 275      -2.006 -19.851 -24.792  1.00 18.01           C  
ANISOU 1018  C   GLY B 275     2930   1620   2290    120     60    -30       C  
ATOM   1019  O   GLY B 275      -2.526 -18.744 -25.064  1.00 15.82           O  
ANISOU 1019  O   GLY B 275     2520   1460   2030     30     60    -60       O  
ATOM   1020  N   ARG B 276      -2.686 -20.951 -24.459  1.00 20.51           N  
ANISOU 1020  N   ARG B 276     3410   1770   2610     60    110     10       N  
ATOM   1021  CA  ARG B 276      -4.167 -20.989 -24.384  1.00 22.04           C  
ANISOU 1021  CA  ARG B 276     3610   1920   2850   -150    160     10       C  
ATOM   1022  C   ARG B 276      -4.705 -20.014 -23.338  1.00 20.32           C  
ANISOU 1022  C   ARG B 276     3280   1840   2600   -200    180     70       C  
ATOM   1023  O   ARG B 276      -4.036 -19.798 -22.305  1.00 20.14           O  
ANISOU 1023  O   ARG B 276     3290   1860   2510    -90    170    130       O  
ATOM   1024  CB  ARG B 276      -4.679 -22.371 -23.961  1.00 25.88           C  
ANISOU 1024  CB  ARG B 276     4310   2180   3350   -240    230     60       C  
ATOM   1025  CG  ARG B 276      -4.736 -23.438 -25.046  1.00 30.70           C  
ANISOU 1025  CG  ARG B 276     5060   2600   4010   -280    220    -30       C  
ATOM   1026  CD  ARG B 276      -5.724 -23.098 -26.155  1.00 32.99           C  
ANISOU 1026  CD  ARG B 276     5220   2970   4350   -480    190   -150       C  
ATOM   1027  NE  ARG B 276      -6.172 -24.259 -26.929  1.00 37.73           N  
ANISOU 1027  NE  ARG B 276     5990   3360   4990   -620    190   -250       N  
ATOM   1028  CZ  ARG B 276      -5.545 -24.801 -27.973  1.00 40.49           C  
ANISOU 1028  CZ  ARG B 276     6460   3610   5310   -520    150   -360       C  
ATOM   1029  NH1 ARG B 276      -6.071 -25.854 -28.579  1.00 43.22           N  
ANISOU 1029  NH1 ARG B 276     6990   3740   5690   -680    160   -470       N  
ATOM   1030  NH2 ARG B 276      -4.392 -24.313 -28.395  1.00 40.57           N  
ANISOU 1030  NH2 ARG B 276     6430   3720   5260   -290    130   -380       N  
ATOM   1031  N   ARG B 277      -5.874 -19.447 -23.631  1.00 18.96           N  
ANISOU 1031  N   ARG B 277     2980   1740   2480   -350    210     30       N  
ATOM   1032  CA  ARG B 277      -6.575 -18.571 -22.667  1.00 18.08           C  
ANISOU 1032  CA  ARG B 277     2780   1750   2340   -380    260     80       C  
ATOM   1033  C   ARG B 277      -7.099 -19.505 -21.571  1.00 19.46           C  
ANISOU 1033  C   ARG B 277     3090   1820   2490   -450    360    180       C  
ATOM   1034  O   ARG B 277      -7.493 -20.640 -21.908  1.00 20.97           O  
ANISOU 1034  O   ARG B 277     3380   1860   2730   -570    400    190       O  
ATOM   1035  CB  ARG B 277      -7.714 -17.790 -23.328  1.00 17.36           C  
ANISOU 1035  CB  ARG B 277     2500   1780   2310   -480    260     20       C  
ATOM   1036  CG  ARG B 277      -7.333 -16.477 -24.008  1.00 15.71           C  
ANISOU 1036  CG  ARG B 277     2190   1680   2100   -380    200    -30       C  
ATOM   1037  CD  ARG B 277      -6.306 -16.452 -25.123  1.00 14.59           C  
ANISOU 1037  CD  ARG B 277     2070   1520   1950   -310    120    -80       C  
ATOM   1038  NE  ARG B 277      -4.927 -16.652 -24.720  1.00 14.00           N  
ANISOU 1038  NE  ARG B 277     2070   1410   1840   -200    100    -70       N  
ATOM   1039  CZ  ARG B 277      -4.142 -15.705 -24.209  1.00 13.34           C  
ANISOU 1039  CZ  ARG B 277     1950   1390   1720   -130     80    -60       C  
ATOM   1040  NH1 ARG B 277      -4.607 -14.486 -23.985  1.00 12.70           N  
ANISOU 1040  NH1 ARG B 277     1800   1380   1640   -150    100    -70       N  
ATOM   1041  NH2 ARG B 277      -2.897 -15.996 -23.885  1.00 13.52           N  
ANISOU 1041  NH2 ARG B 277     2010   1420   1710    -40     50    -60       N  
ATOM   1042  N   GLY B 278      -7.069 -19.071 -20.317  1.00 19.15           N  
ANISOU 1042  N   GLY B 278     3080   1850   2350   -390    420    250       N  
ATOM   1043  CA  GLY B 278      -7.551 -19.933 -19.226  1.00 20.92           C  
ANISOU 1043  CA  GLY B 278     3450   1980   2520   -450    540    380       C  
ATOM   1044  C   GLY B 278      -7.665 -19.167 -17.916  1.00 21.13           C  
ANISOU 1044  C   GLY B 278     3490   2130   2410   -380    600    430       C  
ATOM   1045  O   GLY B 278      -7.372 -17.971 -17.866  1.00 19.43           O  
ANISOU 1045  O   GLY B 278     3170   2050   2160   -300    540    350       O  
ATOM   1046  N   PRO B 279      -8.061 -19.854 -16.823  1.00 23.02           N  
ANISOU 1046  N   PRO B 279     3880   2310   2550   -410    740    560       N  
ATOM   1047  CA  PRO B 279      -8.236 -19.219 -15.518  1.00 24.12           C  
ANISOU 1047  CA  PRO B 279     4070   2580   2520   -340    820    610       C  
ATOM   1048  C   PRO B 279      -7.046 -19.210 -14.545  1.00 24.84           C  
ANISOU 1048  C   PRO B 279     4340   2690   2410   -140    720    660       C  
ATOM   1049  O   PRO B 279      -7.177 -18.588 -13.519  1.00 25.49           O  
ANISOU 1049  O   PRO B 279     4460   2890   2330    -80    770    670       O  
ATOM   1050  CB  PRO B 279      -9.343 -20.110 -14.937  1.00 26.36           C  
ANISOU 1050  CB  PRO B 279     4430   2780   2800   -500   1030    740       C  
ATOM   1051  CG  PRO B 279      -8.956 -21.503 -15.404  1.00 27.28           C  
ANISOU 1051  CG  PRO B 279     4720   2650   2990   -560   1010    820       C  
ATOM   1052  CD  PRO B 279      -8.404 -21.287 -16.799  1.00 25.26           C  
ANISOU 1052  CD  PRO B 279     4340   2380   2870   -530    840    670       C  
ATOM   1053  N   GLU B 280      -5.923 -19.848 -14.886  1.00 25.51           N  
ANISOU 1053  N   GLU B 280     4520   2680   2500    -30    580    680       N  
ATOM   1054  CA  GLU B 280      -4.774 -19.880 -13.931  1.00 27.28           C  
ANISOU 1054  CA  GLU B 280     4880   2970   2520    190    460    730       C  
ATOM   1055  C   GLU B 280      -4.023 -18.544 -13.955  1.00 25.49           C  
ANISOU 1055  C   GLU B 280     4490   2930   2260    260    310    570       C  
ATOM   1056  O   GLU B 280      -4.029 -17.878 -15.009  1.00 22.35           O  
ANISOU 1056  O   GLU B 280     3910   2560   2030    190    260    450       O  
ATOM   1057  CB  GLU B 280      -3.822 -21.039 -14.244  1.00 28.99           C  
ANISOU 1057  CB  GLU B 280     5230   3030   2750    320    380    810       C  
ATOM   1058  CG  GLU B 280      -4.490 -22.408 -14.227  1.00 32.10           C  
ANISOU 1058  CG  GLU B 280     5850   3180   3180    240    540    960       C  
ATOM   1059  CD  GLU B 280      -5.162 -22.809 -12.921  1.00 35.61           C  
ANISOU 1059  CD  GLU B 280     6510   3580   3440    210    700   1140       C  
ATOM   1060  OE1 GLU B 280      -4.889 -22.173 -11.877  1.00 36.47           O  
ANISOU 1060  OE1 GLU B 280     6650   3870   3340    330    660   1160       O  
ATOM   1061  OE2 GLU B 280      -5.977 -23.755 -12.954  1.00 39.13           O  
ANISOU 1061  OE2 GLU B 280     7090   3820   3950     50    880   1250       O  
ATOM   1062  N   GLN B 281      -3.389 -18.197 -12.825  1.00 27.30           N  
ANISOU 1062  N   GLN B 281     4810   3290   2270    390    220    580       N  
ATOM   1063  CA  GLN B 281      -2.604 -16.939 -12.665  1.00 27.22           C  
ANISOU 1063  CA  GLN B 281     4680   3450   2210    430     60    420       C  
ATOM   1064  C   GLN B 281      -1.439 -16.899 -13.662  1.00 25.85           C  
ANISOU 1064  C   GLN B 281     4340   3300   2180    480   -110    340       C  
ATOM   1065  O   GLN B 281      -0.952 -15.783 -13.937  1.00 26.00           O  
ANISOU 1065  O   GLN B 281     4200   3430   2250    430   -200    190       O  
ATOM   1066  CB  GLN B 281      -2.092 -16.796 -11.229  1.00 30.61           C  
ANISOU 1066  CB  GLN B 281     5260   4020   2350    560    -30    440       C  
ATOM   1067  CG  GLN B 281      -3.209 -16.570 -10.220  1.00 32.84           C  
ANISOU 1067  CG  GLN B 281     5690   4320   2470    520    160    480       C  
ATOM   1068  CD  GLN B 281      -3.973 -15.297 -10.508  1.00 32.64           C  
ANISOU 1068  CD  GLN B 281     5540   4330   2540    400    240    330       C  
ATOM   1069  OE1 GLN B 281      -3.429 -14.322 -11.027  1.00 31.80           O  
ANISOU 1069  OE1 GLN B 281     5290   4270   2530    370    120    160       O  
ATOM   1070  NE2 GLN B 281      -5.248 -15.288 -10.153  1.00 34.15           N  
ANISOU 1070  NE2 GLN B 281     5780   4500   2700    340    470    380       N  
ATOM   1071  N   THR B 282      -1.026 -18.054 -14.194  1.00 25.24           N  
ANISOU 1071  N   THR B 282     4300   3120   2170    560   -120    430       N  
ATOM   1072  CA  THR B 282       0.090 -18.108 -15.185  1.00 24.23           C  
ANISOU 1072  CA  THR B 282     4010   3020   2170    620   -250    370       C  
ATOM   1073  C   THR B 282      -0.448 -17.967 -16.618  1.00 21.50           C  
ANISOU 1073  C   THR B 282     3550   2570   2050    480   -160    300       C  
ATOM   1074  O   THR B 282       0.368 -17.844 -17.540  1.00 21.84           O  
ANISOU 1074  O   THR B 282     3450   2660   2190    520   -230    230       O  
ATOM   1075  CB  THR B 282       0.850 -19.435 -15.100  1.00 25.56           C  
ANISOU 1075  CB  THR B 282     4290   3120   2300    830   -300    490       C  
ATOM   1076  OG1 THR B 282      -0.104 -20.444 -15.439  1.00 25.71           O  
ANISOU 1076  OG1 THR B 282     4490   2900   2380    770   -140    600       O  
ATOM   1077  CG2 THR B 282       1.464 -19.695 -13.741  1.00 27.97           C  
ANISOU 1077  CG2 THR B 282     4720   3540   2360   1020   -420    580       C  
ATOM   1078  N   GLN B 283      -1.770 -17.986 -16.797  1.00 20.01           N  
ANISOU 1078  N   GLN B 283     3410   2280   1910    340    -10    320       N  
ATOM   1079  CA  GLN B 283      -2.370 -17.907 -18.156  1.00 17.95           C  
ANISOU 1079  CA  GLN B 283     3040   1950   1830    210     50    260       C  
ATOM   1080  C   GLN B 283      -3.006 -16.545 -18.438  1.00 15.90           C  
ANISOU 1080  C   GLN B 283     2640   1770   1620    100     80    160       C  
ATOM   1081  O   GLN B 283      -3.451 -15.872 -17.483  1.00 16.03           O  
ANISOU 1081  O   GLN B 283     2690   1860   1550     80    120    160       O  
ATOM   1082  CB  GLN B 283      -3.485 -18.951 -18.277  1.00 18.98           C  
ANISOU 1082  CB  GLN B 283     3300   1910   2000    110    180    340       C  
ATOM   1083  CG  GLN B 283      -3.005 -20.397 -18.229  1.00 20.81           C  
ANISOU 1083  CG  GLN B 283     3720   1970   2220    210    180    440       C  
ATOM   1084  CD  GLN B 283      -4.146 -21.384 -18.132  1.00 22.48           C  
ANISOU 1084  CD  GLN B 283     4080   2000   2460     60    330    530       C  
ATOM   1085  OE1 GLN B 283      -5.136 -21.165 -17.434  1.00 22.83           O  
ANISOU 1085  OE1 GLN B 283     4130   2070   2470    -60    450    580       O  
ATOM   1086  NE2 GLN B 283      -3.986 -22.524 -18.782  1.00 24.19           N  
ANISOU 1086  NE2 GLN B 283     4430   2010   2750     70    350    550       N  
ATOM   1087  N   GLY B 284      -3.012 -16.148 -19.712  1.00 13.73           N  
ANISOU 1087  N   GLY B 284     2250   1490   1480     50     70     90       N  
ATOM   1088  CA  GLY B 284      -3.716 -14.919 -20.109  1.00 12.38           C  
ANISOU 1088  CA  GLY B 284     1970   1370   1360    -30    100     20       C  
ATOM   1089  C   GLY B 284      -5.199 -15.255 -20.193  1.00 12.07           C  
ANISOU 1089  C   GLY B 284     1930   1290   1360   -120    210     60       C  
ATOM   1090  O   GLY B 284      -5.507 -16.451 -20.365  1.00 12.26           O  
ANISOU 1090  O   GLY B 284     2020   1230   1410   -170    250    120       O  
ATOM   1091  N   ASN B 285      -6.096 -14.277 -20.072  1.00 11.51           N  
ANISOU 1091  N   ASN B 285     1790   1280   1300   -150    270     30       N  
ATOM   1092  CA  ASN B 285      -7.546 -14.616 -20.138  1.00 12.02           C  
ANISOU 1092  CA  ASN B 285     1790   1360   1420   -240    380     70       C  
ATOM   1093  C   ASN B 285      -8.259 -13.740 -21.164  1.00 11.29           C  
ANISOU 1093  C   ASN B 285     1550   1330   1410   -240    370     10       C  
ATOM   1094  O   ASN B 285      -9.499 -13.799 -21.229  1.00 12.01           O  
ANISOU 1094  O   ASN B 285     1530   1480   1550   -300    440     30       O  
ATOM   1095  CB  ASN B 285      -8.240 -14.379 -18.796  1.00 13.11           C  
ANISOU 1095  CB  ASN B 285     1970   1550   1460   -230    500    110       C  
ATOM   1096  CG  ASN B 285      -8.234 -12.919 -18.388  1.00 12.90           C  
ANISOU 1096  CG  ASN B 285     1920   1590   1390   -140    510     30       C  
ATOM   1097  OD1 ASN B 285      -7.350 -12.158 -18.791  1.00 11.81           O  
ANISOU 1097  OD1 ASN B 285     1790   1430   1260    -90    410    -30       O  
ATOM   1098  ND2 ASN B 285      -9.215 -12.521 -17.591  1.00 13.86           N  
ANISOU 1098  ND2 ASN B 285     2030   1780   1460   -110    640     40       N  
ATOM   1099  N   PHE B 286      -7.497 -13.001 -21.963  1.00 10.51           N  
ANISOU 1099  N   PHE B 286     1440   1220   1340   -190    280    -40       N  
ATOM   1100  CA  PHE B 286      -8.123 -12.037 -22.900  1.00 10.47           C  
ANISOU 1100  CA  PHE B 286     1330   1260   1390   -160    270    -60       C  
ATOM   1101  C   PHE B 286      -8.124 -12.510 -24.355  1.00 10.34           C  
ANISOU 1101  C   PHE B 286     1260   1250   1420   -190    200    -70       C  
ATOM   1102  O   PHE B 286      -7.067 -12.975 -24.856  1.00  9.85           O  
ANISOU 1102  O   PHE B 286     1260   1130   1350   -200    150    -90       O  
ATOM   1103  CB  PHE B 286      -7.354 -10.716 -22.809  1.00 10.06           C  
ANISOU 1103  CB  PHE B 286     1330   1180   1310    -80    260   -100       C  
ATOM   1104  CG  PHE B 286      -7.964  -9.561 -23.563  1.00 10.05           C  
ANISOU 1104  CG  PHE B 286     1280   1190   1350    -10    270   -110       C  
ATOM   1105  CD1 PHE B 286      -7.657  -9.335 -24.893  1.00  9.63           C  
ANISOU 1105  CD1 PHE B 286     1210   1120   1330      0    210    -90       C  
ATOM   1106  CD2 PHE B 286      -8.824  -8.682 -22.926  1.00 10.84           C  
ANISOU 1106  CD2 PHE B 286     1370   1310   1440     70    350   -110       C  
ATOM   1107  CE1 PHE B 286      -8.210  -8.260 -25.571  1.00 10.20           C  
ANISOU 1107  CE1 PHE B 286     1270   1190   1410     90    220    -70       C  
ATOM   1108  CE2 PHE B 286      -9.375  -7.607 -23.604  1.00 11.37           C  
ANISOU 1108  CE2 PHE B 286     1420   1360   1540    180    360   -100       C  
ATOM   1109  CZ  PHE B 286      -9.067  -7.398 -24.925  1.00 11.05           C  
ANISOU 1109  CZ  PHE B 286     1370   1300   1520    190    290    -70       C  
ATOM   1110  N   GLY B 287      -9.282 -12.353 -25.011  1.00 11.03           N  
ANISOU 1110  N   GLY B 287     1230   1420   1550   -200    190    -70       N  
ATOM   1111  CA  GLY B 287      -9.394 -12.669 -26.442  1.00 11.53           C  
ANISOU 1111  CA  GLY B 287     1250   1510   1620   -220    100   -100       C  
ATOM   1112  C   GLY B 287     -10.457 -13.681 -26.810  1.00 12.89           C  
ANISOU 1112  C   GLY B 287     1320   1740   1840   -350     70   -120       C  
ATOM   1113  O   GLY B 287     -10.461 -14.775 -26.238  1.00 13.25           O  
ANISOU 1113  O   GLY B 287     1410   1720   1900   -460    110   -120       O  
ATOM   1114  N   ASP B 288     -11.325 -13.305 -27.755  1.00 14.23           N  
ANISOU 1114  N   ASP B 288     1360   2040   2010   -320      0   -140       N  
ATOM   1115  CA  ASP B 288     -12.349 -14.241 -28.280  1.00 16.01           C  
ANISOU 1115  CA  ASP B 288     1450   2350   2280   -470    -70   -190       C  
ATOM   1116  C   ASP B 288     -11.609 -15.069 -29.344  1.00 16.43           C  
ANISOU 1116  C   ASP B 288     1640   2320   2280   -530   -160   -260       C  
ATOM   1117  O   ASP B 288     -10.394 -14.810 -29.544  1.00 14.50           O  
ANISOU 1117  O   ASP B 288     1550   1980   1980   -430   -140   -250       O  
ATOM   1118  CB  ASP B 288     -13.599 -13.512 -28.780  1.00 17.47           C  
ANISOU 1118  CB  ASP B 288     1410   2750   2480   -410   -130   -190       C  
ATOM   1119  CG  ASP B 288     -13.405 -12.635 -30.011  1.00 17.39           C  
ANISOU 1119  CG  ASP B 288     1420   2810   2380   -240   -240   -180       C  
ATOM   1120  OD1 ASP B 288     -12.320 -12.679 -30.620  1.00 16.29           O  
ANISOU 1120  OD1 ASP B 288     1460   2550   2170   -210   -270   -190       O  
ATOM   1121  OD2 ASP B 288     -14.357 -11.927 -30.362  1.00 18.87           O  
ANISOU 1121  OD2 ASP B 288     1440   3170   2570   -120   -300   -160       O  
ATOM   1122  N   GLN B 289     -12.288 -15.995 -30.021  1.00 18.84           N  
ANISOU 1122  N   GLN B 289     1890   2660   2600   -680   -240   -350       N  
ATOM   1123  CA  GLN B 289     -11.609 -16.860 -31.027  1.00 20.47           C  
ANISOU 1123  CA  GLN B 289     2270   2770   2740   -730   -320   -440       C  
ATOM   1124  C   GLN B 289     -11.033 -16.033 -32.182  1.00 19.67           C  
ANISOU 1124  C   GLN B 289     2220   2740   2510   -560   -400   -440       C  
ATOM   1125  O   GLN B 289      -9.920 -16.360 -32.617  1.00 18.74           O  
ANISOU 1125  O   GLN B 289     2280   2500   2330   -510   -370   -460       O  
ATOM   1126  CB  GLN B 289     -12.568 -17.945 -31.516  1.00 24.43           C  
ANISOU 1126  CB  GLN B 289     2710   3300   3280   -960   -410   -550       C  
ATOM   1127  CG  GLN B 289     -12.907 -18.925 -30.409  1.00 26.86           C  
ANISOU 1127  CG  GLN B 289     3040   3470   3700  -1160   -300   -540       C  
ATOM   1128  CD  GLN B 289     -13.844 -20.024 -30.825  1.00 31.95           C  
ANISOU 1128  CD  GLN B 289     3630   4110   4410  -1440   -370   -660       C  
ATOM   1129  OE1 GLN B 289     -13.670 -21.177 -30.437  1.00 36.53           O  
ANISOU 1129  OE1 GLN B 289     4380   4460   5040  -1610   -300   -690       O  
ATOM   1130  NE2 GLN B 289     -14.821 -19.681 -31.649  1.00 35.38           N  
ANISOU 1130  NE2 GLN B 289     3830   4780   4830  -1490   -520   -740       N  
ATOM   1131  N   GLU B 290     -11.738 -14.989 -32.618  1.00 20.44           N  
ANISOU 1131  N   GLU B 290     2180   3010   2580   -450   -460   -400       N  
ATOM   1132  CA  GLU B 290     -11.277 -14.143 -33.754  1.00 20.67           C  
ANISOU 1132  CA  GLU B 290     2280   3100   2470   -280   -520   -370       C  
ATOM   1133  C   GLU B 290      -9.974 -13.423 -33.377  1.00 18.39           C  
ANISOU 1133  C   GLU B 290     2130   2680   2170   -170   -390   -280       C  
ATOM   1134  O   GLU B 290      -9.013 -13.470 -34.179  1.00 17.40           O  
ANISOU 1134  O   GLU B 290     2150   2510   1950   -110   -380   -290       O  
ATOM   1135  CB  GLU B 290     -12.397 -13.184 -34.152  1.00 23.28           C  
ANISOU 1135  CB  GLU B 290     2430   3640   2770   -170   -620   -320       C  
ATOM   1136  CG  GLU B 290     -12.046 -12.318 -35.337  1.00 25.06           C  
ANISOU 1136  CG  GLU B 290     2760   3930   2830     20   -680   -260       C  
ATOM   1137  CD  GLU B 290     -13.142 -11.376 -35.796  1.00 28.05           C  
ANISOU 1137  CD  GLU B 290     2990   4510   3160    180   -790   -190       C  
ATOM   1138  OE1 GLU B 290     -14.165 -11.255 -35.082  1.00 29.75           O  
ANISOU 1138  OE1 GLU B 290     2990   4830   3490    170   -800   -190       O  
ATOM   1139  OE2 GLU B 290     -12.975 -10.775 -36.883  1.00 31.28           O  
ANISOU 1139  OE2 GLU B 290     3500   4980   3400    340   -850   -140       O  
ATOM   1140  N   LEU B 291      -9.917 -12.800 -32.199  1.00 16.96           N  
ANISOU 1140  N   LEU B 291     1910   2450   2080   -140   -290   -210       N  
ATOM   1141  CA  LEU B 291      -8.657 -12.106 -31.808  1.00 15.60           C  
ANISOU 1141  CA  LEU B 291     1860   2160   1910    -60   -190   -150       C  
ATOM   1142  C   LEU B 291      -7.534 -13.130 -31.596  1.00 14.77           C  
ANISOU 1142  C   LEU B 291     1850   1940   1820   -130   -140   -200       C  
ATOM   1143  O   LEU B 291      -6.391 -12.828 -31.974  1.00 13.15           O  
ANISOU 1143  O   LEU B 291     1730   1700   1570    -80   -100   -180       O  
ATOM   1144  CB  LEU B 291      -8.872 -11.278 -30.543  1.00 15.27           C  
ANISOU 1144  CB  LEU B 291     1770   2090   1950    -30   -110   -100       C  
ATOM   1145  CG  LEU B 291      -7.593 -10.691 -29.941  1.00 14.45           C  
ANISOU 1145  CG  LEU B 291     1770   1870   1860    -10    -20    -70       C  
ATOM   1146  CD1 LEU B 291      -6.875  -9.793 -30.937  1.00 14.70           C  
ANISOU 1146  CD1 LEU B 291     1880   1870   1830     60      0    -30       C  
ATOM   1147  CD2 LEU B 291      -7.911  -9.927 -28.669  1.00 14.61           C  
ANISOU 1147  CD2 LEU B 291     1770   1850   1930     20     50    -50       C  
ATOM   1148  N   ILE B 292      -7.844 -14.280 -30.993  1.00 15.36           N  
ANISOU 1148  N   ILE B 292     1920   1970   1940   -240   -150   -250       N  
ATOM   1149  CA  ILE B 292      -6.800 -15.322 -30.756  1.00 15.85           C  
ANISOU 1149  CA  ILE B 292     2100   1910   2010   -260   -110   -280       C  
ATOM   1150  C   ILE B 292      -6.192 -15.761 -32.099  1.00 16.57           C  
ANISOU 1150  C   ILE B 292     2290   2000   2010   -220   -140   -350       C  
ATOM   1151  O   ILE B 292      -4.953 -15.841 -32.194  1.00 15.82           O  
ANISOU 1151  O   ILE B 292     2260   1860   1890   -140    -80   -340       O  
ATOM   1152  CB  ILE B 292      -7.393 -16.510 -29.968  1.00 17.06           C  
ANISOU 1152  CB  ILE B 292     2280   1980   2230   -380   -100   -310       C  
ATOM   1153  CG1 ILE B 292      -7.746 -16.091 -28.537  1.00 16.79           C  
ANISOU 1153  CG1 ILE B 292     2180   1950   2250   -400    -30   -230       C  
ATOM   1154  CG2 ILE B 292      -6.447 -17.706 -29.977  1.00 17.42           C  
ANISOU 1154  CG2 ILE B 292     2490   1870   2260   -370    -80   -340       C  
ATOM   1155  CD1 ILE B 292      -8.462 -17.157 -27.727  1.00 18.47           C  
ANISOU 1155  CD1 ILE B 292     2410   2090   2520   -530     10   -220       C  
ATOM   1156  N   ARG B 293      -7.032 -15.965 -33.111  1.00 18.28           N  
ANISOU 1156  N   ARG B 293     2500   2290   2160   -260   -230   -410       N  
ATOM   1157  CA  ARG B 293      -6.554 -16.456 -34.431  1.00 20.36           C  
ANISOU 1157  CA  ARG B 293     2880   2550   2300   -220   -260   -500       C  
ATOM   1158  C   ARG B 293      -5.812 -15.375 -35.234  1.00 19.10           C  
ANISOU 1158  C   ARG B 293     2750   2470   2040    -80   -210   -430       C  
ATOM   1159  O   ARG B 293      -4.882 -15.764 -35.972  1.00 19.03           O  
ANISOU 1159  O   ARG B 293     2850   2440   1940    -10   -160   -470       O  
ATOM   1160  CB  ARG B 293      -7.746 -16.970 -35.249  1.00 23.36           C  
ANISOU 1160  CB  ARG B 293     3250   3010   2620   -320   -400   -600       C  
ATOM   1161  CG  ARG B 293      -7.370 -17.610 -36.578  1.00 26.69           C  
ANISOU 1161  CG  ARG B 293     3830   3430   2880   -290   -450   -720       C  
ATOM   1162  CD  ARG B 293      -8.565 -18.068 -37.401  1.00 30.67           C  
ANISOU 1162  CD  ARG B 293     4310   4040   3300   -410   -620   -850       C  
ATOM   1163  NE  ARG B 293      -9.425 -16.954 -37.799  1.00 33.19           N  
ANISOU 1163  NE  ARG B 293     4470   4580   3560   -350   -730   -780       N  
ATOM   1164  CZ  ARG B 293     -10.501 -16.523 -37.132  1.00 34.70           C  
ANISOU 1164  CZ  ARG B 293     4450   4870   3870   -410   -780   -730       C  
ATOM   1165  NH1 ARG B 293     -10.889 -17.110 -36.009  1.00 35.69           N  
ANISOU 1165  NH1 ARG B 293     4490   4900   4170   -560   -730   -730       N  
ATOM   1166  NH2 ARG B 293     -11.194 -15.499 -37.598  1.00 35.44           N  
ANISOU 1166  NH2 ARG B 293     4420   5160   3890   -300   -870   -650       N  
ATOM   1167  N   GLN B 294      -6.150 -14.089 -35.056  1.00 17.90           N  
ANISOU 1167  N   GLN B 294     2510   2390   1900    -30   -210   -320       N  
ATOM   1168  CA  GLN B 294      -5.551 -13.005 -35.892  1.00 17.90           C  
ANISOU 1168  CA  GLN B 294     2560   2440   1790     70   -150   -230       C  
ATOM   1169  C   GLN B 294      -4.533 -12.111 -35.171  1.00 16.22           C  
ANISOU 1169  C   GLN B 294     2330   2160   1670     90    -20   -140       C  
ATOM   1170  O   GLN B 294      -3.737 -11.473 -35.887  1.00 16.20           O  
ANISOU 1170  O   GLN B 294     2390   2170   1590    140     70    -80       O  
ATOM   1171  CB  GLN B 294      -6.696 -12.155 -36.431  1.00 18.93           C  
ANISOU 1171  CB  GLN B 294     2650   2690   1860    130   -250   -180       C  
ATOM   1172  CG  GLN B 294      -7.702 -12.984 -37.212  1.00 20.92           C  
ANISOU 1172  CG  GLN B 294     2890   3050   2010    100   -410   -290       C  
ATOM   1173  CD  GLN B 294      -8.889 -12.183 -37.677  1.00 22.90           C  
ANISOU 1173  CD  GLN B 294     3050   3450   2200    180   -530   -230       C  
ATOM   1174  OE1 GLN B 294      -8.935 -10.970 -37.536  1.00 24.40           O  
ANISOU 1174  OE1 GLN B 294     3230   3640   2390    300   -480   -100       O  
ATOM   1175  NE2 GLN B 294      -9.872 -12.866 -38.234  1.00 25.43           N  
ANISOU 1175  NE2 GLN B 294     3300   3910   2450    120   -700   -340       N  
ATOM   1176  N   GLY B 295      -4.542 -12.046 -33.838  1.00 14.40           N  
ANISOU 1176  N   GLY B 295     2030   1870   1570     40      0   -130       N  
ATOM   1177  CA  GLY B 295      -3.584 -11.164 -33.139  1.00 13.36           C  
ANISOU 1177  CA  GLY B 295     1880   1690   1510     30     90    -80       C  
ATOM   1178  C   GLY B 295      -3.716  -9.712 -33.591  1.00 13.50           C  
ANISOU 1178  C   GLY B 295     1940   1690   1500     70    140     20       C  
ATOM   1179  O   GLY B 295      -4.861  -9.236 -33.727  1.00 13.81           O  
ANISOU 1179  O   GLY B 295     1980   1760   1510    130     80     50       O  
ATOM   1180  N   THR B 296      -2.589  -9.036 -33.844  1.00 13.30           N  
ANISOU 1180  N   THR B 296     1940   1630   1480     50    250     70       N  
ATOM   1181  CA  THR B 296      -2.598  -7.609 -34.270  1.00 13.94           C  
ANISOU 1181  CA  THR B 296     2110   1650   1530     70    320    180       C  
ATOM   1182  C   THR B 296      -3.263  -7.441 -35.644  1.00 14.98           C  
ANISOU 1182  C   THR B 296     2340   1840   1510    180    300    250       C  
ATOM   1183  O   THR B 296      -3.495  -6.295 -36.030  1.00 16.24           O  
ANISOU 1183  O   THR B 296     2600   1940   1630    240    340    360       O  
ATOM   1184  CB  THR B 296      -1.185  -7.025 -34.241  1.00 14.47           C  
ANISOU 1184  CB  THR B 296     2180   1670   1650    -30    460    210       C  
ATOM   1185  OG1 THR B 296      -0.383  -7.814 -35.114  1.00 14.80           O  
ANISOU 1185  OG1 THR B 296     2190   1810   1620    -20    520    190       O  
ATOM   1186  CG2 THR B 296      -0.585  -7.030 -32.854  1.00 13.82           C  
ANISOU 1186  CG2 THR B 296     1990   1550   1710   -130    450    140       C  
ATOM   1187  N   ASP B 297      -3.538  -8.535 -36.358  1.00 14.99           N  
ANISOU 1187  N   ASP B 297     2340   1950   1400    220    220    180       N  
ATOM   1188  CA  ASP B 297      -4.240  -8.464 -37.667  1.00 16.27           C  
ANISOU 1188  CA  ASP B 297     2590   2210   1380    330    150    220       C  
ATOM   1189  C   ASP B 297      -5.745  -8.320 -37.397  1.00 16.08           C  
ANISOU 1189  C   ASP B 297     2500   2240   1370    400      0    220       C  
ATOM   1190  O   ASP B 297      -6.492  -8.000 -38.330  1.00 17.47           O  
ANISOU 1190  O   ASP B 297     2730   2510   1400    520    -90    270       O  
ATOM   1191  CB  ASP B 297      -3.937  -9.688 -38.538  1.00 17.02           C  
ANISOU 1191  CB  ASP B 297     2720   2400   1340    330    120    120       C  
ATOM   1192  CG  ASP B 297      -2.504  -9.755 -39.034  1.00 17.78           C  
ANISOU 1192  CG  ASP B 297     2870   2490   1390    320    300    140       C  
ATOM   1193  OD1 ASP B 297      -1.897  -8.687 -39.189  1.00 18.72           O  
ANISOU 1193  OD1 ASP B 297     3040   2560   1520    310    440    270       O  
ATOM   1194  OD2 ASP B 297      -1.997 -10.874 -39.235  1.00 18.09           O  
ANISOU 1194  OD2 ASP B 297     2910   2560   1400    320    310     30       O  
ATOM   1195  N   TYR B 298      -6.167  -8.539 -36.152  1.00 14.72           N  
ANISOU 1195  N   TYR B 298     2210   2030   1360    330    -40    160       N  
ATOM   1196  CA  TYR B 298      -7.603  -8.422 -35.780  1.00 15.03           C  
ANISOU 1196  CA  TYR B 298     2140   2150   1430    390   -160    160       C  
ATOM   1197  C   TYR B 298      -8.109  -7.037 -36.182  1.00 16.40           C  
ANISOU 1197  C   TYR B 298     2380   2310   1550    560   -150    300       C  
ATOM   1198  O   TYR B 298      -7.438  -6.032 -35.897  1.00 16.34           O  
ANISOU 1198  O   TYR B 298     2480   2140   1580    570    -20    380       O  
ATOM   1199  CB  TYR B 298      -7.776  -8.737 -34.294  1.00 13.55           C  
ANISOU 1199  CB  TYR B 298     1840   1900   1410    300   -130    100       C  
ATOM   1200  CG  TYR B 298      -9.162  -8.581 -33.727  1.00 14.02           C  
ANISOU 1200  CG  TYR B 298     1750   2050   1530    350   -200     90       C  
ATOM   1201  CD1 TYR B 298     -10.202  -9.392 -34.147  1.00 14.98           C  
ANISOU 1201  CD1 TYR B 298     1740   2330   1620    320   -330     30       C  
ATOM   1202  CD2 TYR B 298      -9.402  -7.724 -32.663  1.00 13.65           C  
ANISOU 1202  CD2 TYR B 298     1690   1930   1570    400   -120    130       C  
ATOM   1203  CE1 TYR B 298     -11.469  -9.283 -33.597  1.00 15.80           C  
ANISOU 1203  CE1 TYR B 298     1660   2550   1790    360   -380     20       C  
ATOM   1204  CE2 TYR B 298     -10.653  -7.619 -32.087  1.00 14.26           C  
ANISOU 1204  CE2 TYR B 298     1610   2100   1710    460   -160    120       C  
ATOM   1205  CZ  TYR B 298     -11.694  -8.397 -32.559  1.00 15.52           C  
ANISOU 1205  CZ  TYR B 298     1600   2450   1850    440   -280     80       C  
ATOM   1206  OH  TYR B 298     -12.933  -8.304 -31.998  1.00 16.43           O  
ANISOU 1206  OH  TYR B 298     1520   2700   2030    490   -300     70       O  
ATOM   1207  N   LYS B 299      -9.273  -7.015 -36.825  1.00 18.01           N  
ANISOU 1207  N   LYS B 299     2520   2670   1660    680   -290    310       N  
ATOM   1208  CA  LYS B 299      -9.926  -5.781 -37.330  1.00 20.09           C  
ANISOU 1208  CA  LYS B 299     2850   2950   1840    910   -320    460       C  
ATOM   1209  C   LYS B 299     -10.039  -4.694 -36.253  1.00 19.58           C  
ANISOU 1209  C   LYS B 299     2800   2710   1920    980   -200    520       C  
ATOM   1210  O   LYS B 299      -9.825  -3.511 -36.595  1.00 20.43           O  
ANISOU 1210  O   LYS B 299     3100   2690   1980   1110   -120    660       O  
ATOM   1211  CB  LYS B 299     -11.327  -6.133 -37.834  1.00 22.23           C  
ANISOU 1211  CB  LYS B 299     2950   3470   2030   1020   -530    430       C  
ATOM   1212  CG  LYS B 299     -12.104  -4.960 -38.390  1.00 24.97           C  
ANISOU 1212  CG  LYS B 299     3340   3870   2280   1310   -580    580       C  
ATOM   1213  CD  LYS B 299     -13.448  -5.332 -38.942  1.00 27.48           C  
ANISOU 1213  CD  LYS B 299     3440   4490   2510   1420   -820    550       C  
ATOM   1214  CE  LYS B 299     -14.154  -4.138 -39.542  1.00 30.37           C  
ANISOU 1214  CE  LYS B 299     3870   4920   2750   1760   -890    720       C  
ATOM   1215  NZ  LYS B 299     -15.453  -4.533 -40.127  1.00 33.38           N  
ANISOU 1215  NZ  LYS B 299     3990   5650   3040   1880  -1150    680       N  
ATOM   1216  N   HIS B 300     -10.364  -5.070 -35.011  1.00 18.21           N  
ANISOU 1216  N   HIS B 300     2480   2540   1900    890   -190    430       N  
ATOM   1217  CA  HIS B 300     -10.535  -4.053 -33.939  1.00 18.38           C  
ANISOU 1217  CA  HIS B 300     2540   2410   2040    970    -80    460       C  
ATOM   1218  C   HIS B 300      -9.302  -3.966 -33.023  1.00 16.57           C  
ANISOU 1218  C   HIS B 300     2410   1980   1910    780     60    410       C  
ATOM   1219  O   HIS B 300      -9.412  -3.315 -31.971  1.00 16.70           O  
ANISOU 1219  O   HIS B 300     2460   1880   2010    810    140    390       O  
ATOM   1220  CB  HIS B 300     -11.825  -4.335 -33.159  1.00 18.93           C  
ANISOU 1220  CB  HIS B 300     2380   2630   2180   1030   -140    400       C  
ATOM   1221  CG  HIS B 300     -13.036  -4.453 -34.025  1.00 21.27           C  
ANISOU 1221  CG  HIS B 300     2510   3170   2400   1200   -300    440       C  
ATOM   1222  ND1 HIS B 300     -13.533  -3.387 -34.755  1.00 23.75           N  
ANISOU 1222  ND1 HIS B 300     2910   3490   2620   1470   -330    570       N  
ATOM   1223  CD2 HIS B 300     -13.893  -5.477 -34.221  1.00 21.99           C  
ANISOU 1223  CD2 HIS B 300     2360   3510   2490   1120   -440    350       C  
ATOM   1224  CE1 HIS B 300     -14.619  -3.763 -35.397  1.00 25.73           C  
ANISOU 1224  CE1 HIS B 300     2950   4020   2800   1580   -510    570       C  
ATOM   1225  NE2 HIS B 300     -14.863  -5.043 -35.087  1.00 24.77           N  
ANISOU 1225  NE2 HIS B 300     2610   4050   2740   1350   -580    420       N  
ATOM   1226  N   TRP B 301      -8.164  -4.537 -33.426  1.00 15.43           N  
ANISOU 1226  N   TRP B 301     1930   2070   1870    100   -240     40       N  
ATOM   1227  CA  TRP B 301      -6.939  -4.511 -32.582  1.00 14.99           C  
ANISOU 1227  CA  TRP B 301     1890   1970   1830    120   -240     20       C  
ATOM   1228  C   TRP B 301      -6.536  -3.097 -32.156  1.00 14.64           C  
ANISOU 1228  C   TRP B 301     1810   1940   1820    120   -170     50       C  
ATOM   1229  O   TRP B 301      -6.242  -2.887 -30.982  1.00 14.54           O  
ANISOU 1229  O   TRP B 301     1800   1890   1830    100   -160     50       O  
ATOM   1230  CB  TRP B 301      -5.762  -5.237 -33.246  1.00 15.27           C  
ANISOU 1230  CB  TRP B 301     1950   2000   1850    190   -290    -50       C  
ATOM   1231  CG  TRP B 301      -4.524  -5.087 -32.420  1.00 15.13           C  
ANISOU 1231  CG  TRP B 301     1930   1970   1850    210   -280    -70       C  
ATOM   1232  CD1 TRP B 301      -3.464  -4.265 -32.664  1.00 15.16           C  
ANISOU 1232  CD1 TRP B 301     1870   2050   1840    240   -220    -70       C  
ATOM   1233  CD2 TRP B 301      -4.296  -5.653 -31.118  1.00 15.12           C  
ANISOU 1233  CD2 TRP B 301     1990   1890   1870    180   -320    -80       C  
ATOM   1234  NE1 TRP B 301      -2.561  -4.335 -31.637  1.00 14.99           N  
ANISOU 1234  NE1 TRP B 301     1870   1990   1840    240   -230    -90       N  
ATOM   1235  CE2 TRP B 301      -3.047  -5.171 -30.671  1.00 14.92           C  
ANISOU 1235  CE2 TRP B 301     1930   1880   1850    210   -290   -100       C  
ATOM   1236  CE3 TRP B 301      -5.012  -6.538 -30.299  1.00 15.30           C  
ANISOU 1236  CE3 TRP B 301     2080   1830   1900    110   -400    -60       C  
ATOM   1237  CZ2 TRP B 301      -2.494  -5.558 -29.452  1.00 14.91           C  
ANISOU 1237  CZ2 TRP B 301     1970   1820   1870    200   -320   -110       C  
ATOM   1238  CZ3 TRP B 301      -4.466  -6.917 -29.094  1.00 15.29           C  
ANISOU 1238  CZ3 TRP B 301     2120   1770   1920     80   -440    -60       C  
ATOM   1239  CH2 TRP B 301      -3.226  -6.429 -28.677  1.00 15.11           C  
ANISOU 1239  CH2 TRP B 301     2070   1760   1910    130   -400    -90       C  
ATOM   1240  N   PRO B 302      -6.467  -2.088 -33.060  1.00 14.63           N  
ANISOU 1240  N   PRO B 302     1760   1980   1810    150   -130     80       N  
ATOM   1241  CA  PRO B 302      -6.067  -0.738 -32.659  1.00 14.43           C  
ANISOU 1241  CA  PRO B 302     1730   1940   1810    140   -100    110       C  
ATOM   1242  C   PRO B 302      -6.945  -0.152 -31.535  1.00 14.37           C  
ANISOU 1242  C   PRO B 302     1730   1900   1830    140   -100    110       C  
ATOM   1243  O   PRO B 302      -6.415   0.624 -30.741  1.00 14.39           O  
ANISOU 1243  O   PRO B 302     1740   1860   1870    140    -90    110       O  
ATOM   1244  CB  PRO B 302      -6.163   0.087 -33.955  1.00 14.84           C  
ANISOU 1244  CB  PRO B 302     1750   2040   1850    140    -90    160       C  
ATOM   1245  CG  PRO B 302      -6.081  -0.941 -35.066  1.00 15.01           C  
ANISOU 1245  CG  PRO B 302     1750   2130   1820    170   -100    130       C  
ATOM   1246  CD  PRO B 302      -6.740  -2.185 -34.504  1.00 14.88           C  
ANISOU 1246  CD  PRO B 302     1770   2080   1810    170   -130     80       C  
ATOM   1247  N   GLN B 303      -8.235  -0.516 -31.482  1.00 14.27           N  
ANISOU 1247  N   GLN B 303     1700   1930   1800    130   -100    110       N  
ATOM   1248  CA  GLN B 303      -9.153  -0.015 -30.417  1.00 14.44           C  
ANISOU 1248  CA  GLN B 303     1700   1980   1810    140   -100     90       C  
ATOM   1249  C   GLN B 303      -8.783  -0.654 -29.072  1.00 14.14           C  
ANISOU 1249  C   GLN B 303     1660   1940   1770    100   -110     70       C  
ATOM   1250  O   GLN B 303      -9.147  -0.084 -28.034  1.00 14.38           O  
ANISOU 1250  O   GLN B 303     1660   2010   1790    120   -110     50       O  
ATOM   1251  CB  GLN B 303     -10.607  -0.340 -30.755  1.00 14.97           C  
ANISOU 1251  CB  GLN B 303     1720   2140   1820    140   -110     90       C  
ATOM   1252  CG  GLN B 303     -11.057   0.258 -32.072  1.00 15.34           C  
ANISOU 1252  CG  GLN B 303     1760   2190   1870    180   -110    110       C  
ATOM   1253  CD  GLN B 303     -12.398  -0.273 -32.508  1.00 15.90           C  
ANISOU 1253  CD  GLN B 303     1790   2370   1880    170   -110    110       C  
ATOM   1254  OE1 GLN B 303     -12.530  -0.811 -33.610  1.00 16.23           O  
ANISOU 1254  OE1 GLN B 303     1840   2410   1910    150   -120    130       O  
ATOM   1255  NE2 GLN B 303     -13.376  -0.205 -31.619  1.00 16.21           N  
ANISOU 1255  NE2 GLN B 303     1770   2520   1870    160   -120     90       N  
ATOM   1256  N   ILE B 304      -8.135  -1.818 -29.107  1.00 13.71           N  
ANISOU 1256  N   ILE B 304     1650   1850   1710     60   -130     80       N  
ATOM   1257  CA  ILE B 304      -7.693  -2.539 -27.879  1.00 13.68           C  
ANISOU 1257  CA  ILE B 304     1660   1820   1710     10   -150     70       C  
ATOM   1258  C   ILE B 304      -6.300  -2.025 -27.505  1.00 13.29           C  
ANISOU 1258  C   ILE B 304     1630   1710   1710     40   -130     50       C  
ATOM   1259  O   ILE B 304      -6.069  -1.752 -26.316  1.00 13.20           O  
ANISOU 1259  O   ILE B 304     1610   1700   1700     30   -130     40       O  
ATOM   1260  CB  ILE B 304      -7.703  -4.064 -28.115  1.00 13.97           C  
ANISOU 1260  CB  ILE B 304     1750   1830   1720    -50   -220     80       C  
ATOM   1261  CG1 ILE B 304      -9.123  -4.572 -28.386  1.00 14.32           C  
ANISOU 1261  CG1 ILE B 304     1780   1950   1710   -120   -260    120       C  
ATOM   1262  CG2 ILE B 304      -7.051  -4.802 -26.951  1.00 14.11           C  
ANISOU 1262  CG2 ILE B 304     1820   1800   1750   -100   -270     90       C  
ATOM   1263  CD1 ILE B 304      -9.186  -6.015 -28.799  1.00 14.83           C  
ANISOU 1263  CD1 ILE B 304     1920   1950   1760   -190   -360    140       C  
ATOM   1264  N   ALA B 305      -5.438  -1.846 -28.510  1.00 13.07           N  
ANISOU 1264  N   ALA B 305     1610   1660   1690     80   -120     50       N  
ATOM   1265  CA  ALA B 305      -4.048  -1.388 -28.279  1.00 12.84           C  
ANISOU 1265  CA  ALA B 305     1590   1600   1690    100   -110     40       C  
ATOM   1266  C   ALA B 305      -4.004   0.012 -27.654  1.00 12.74           C  
ANISOU 1266  C   ALA B 305     1560   1570   1710    100    -90     50       C  
ATOM   1267  O   ALA B 305      -2.990   0.305 -27.000  1.00 12.65           O  
ANISOU 1267  O   ALA B 305     1560   1530   1710     90    -80     50       O  
ATOM   1268  CB  ALA B 305      -3.275  -1.435 -29.575  1.00 13.09           C  
ANISOU 1268  CB  ALA B 305     1600   1680   1700    120   -110     40       C  
ATOM   1269  N   GLN B 306      -5.043   0.843 -27.828  1.00 12.85           N  
ANISOU 1269  N   GLN B 306     1570   1590   1720    120    -90     60       N  
ATOM   1270  CA  GLN B 306      -5.001   2.215 -27.243  1.00 12.98           C  
ANISOU 1270  CA  GLN B 306     1600   1560   1770    150   -110     60       C  
ATOM   1271  C   GLN B 306      -4.919   2.118 -25.714  1.00 12.87           C  
ANISOU 1271  C   GLN B 306     1580   1550   1760    160   -110     20       C  
ATOM   1272  O   GLN B 306      -4.564   3.134 -25.076  1.00 13.12           O  
ANISOU 1272  O   GLN B 306     1630   1530   1830    180   -140      0       O  
ATOM   1273  CB  GLN B 306      -6.210   3.064 -27.661  1.00 13.37           C  
ANISOU 1273  CB  GLN B 306     1640   1620   1820    200   -140     50       C  
ATOM   1274  CG  GLN B 306      -7.546   2.575 -27.110  1.00 13.43           C  
ANISOU 1274  CG  GLN B 306     1600   1720   1780    230   -130     10       C  
ATOM   1275  CD  GLN B 306      -8.721   3.314 -27.706  1.00 13.91           C  
ANISOU 1275  CD  GLN B 306     1650   1820   1820    300   -160    -10       C  
ATOM   1276  OE1 GLN B 306      -8.692   4.527 -27.888  1.00 14.36           O  
ANISOU 1276  OE1 GLN B 306     1740   1800   1910    370   -220    -20       O  
ATOM   1277  NE2 GLN B 306      -9.786   2.583 -28.000  1.00 13.93           N  
ANISOU 1277  NE2 GLN B 306     1600   1930   1760    290   -140    -10       N  
ATOM   1278  N   PHE B 307      -5.219   0.945 -25.150  1.00 12.59           N  
ANISOU 1278  N   PHE B 307     1520   1570   1700    120    -90      0       N  
ATOM   1279  CA  PHE B 307      -5.177   0.799 -23.673  1.00 12.65           C  
ANISOU 1279  CA  PHE B 307     1510   1610   1690    110   -100    -20       C  
ATOM   1280  C   PHE B 307      -3.861   0.161 -23.217  1.00 12.46           C  
ANISOU 1280  C   PHE B 307     1520   1530   1690     80    -90    -20       C  
ATOM   1281  O   PHE B 307      -3.591   0.210 -22.001  1.00 12.60           O  
ANISOU 1281  O   PHE B 307     1520   1560   1710     70    -90    -40       O  
ATOM   1282  CB  PHE B 307      -6.406   0.032 -23.183  1.00 12.80           C  
ANISOU 1282  CB  PHE B 307     1480   1740   1640     80   -100    -20       C  
ATOM   1283  CG  PHE B 307      -7.692   0.728 -23.528  1.00 13.20           C  
ANISOU 1283  CG  PHE B 307     1480   1880   1660    130   -100    -50       C  
ATOM   1284  CD1 PHE B 307      -8.054   1.891 -22.870  1.00 13.69           C  
ANISOU 1284  CD1 PHE B 307     1500   1990   1710    220   -120   -110       C  
ATOM   1285  CD2 PHE B 307      -8.538   0.223 -24.498  1.00 13.22           C  
ANISOU 1285  CD2 PHE B 307     1470   1930   1620    110   -110    -20       C  
ATOM   1286  CE1 PHE B 307      -9.229   2.548 -23.192  1.00 14.35           C  
ANISOU 1286  CE1 PHE B 307     1540   2160   1750    310   -140   -150       C  
ATOM   1287  CE2 PHE B 307      -9.719   0.877 -24.811  1.00 13.77           C  
ANISOU 1287  CE2 PHE B 307     1480   2100   1650    170   -110    -40       C  
ATOM   1288  CZ  PHE B 307     -10.061   2.034 -24.156  1.00 14.31           C  
ANISOU 1288  CZ  PHE B 307     1510   2210   1710    280   -130   -120       C  
ATOM   1289  N   ALA B 308      -3.067  -0.373 -24.150  1.00 12.50           N  
ANISOU 1289  N   ALA B 308     1550   1500   1700     70    -90      0       N  
ATOM   1290  CA  ALA B 308      -1.777  -1.015 -23.791  1.00 12.38           C  
ANISOU 1290  CA  ALA B 308     1550   1450   1690     60   -100    -20       C  
ATOM   1291  C   ALA B 308      -0.793   0.067 -23.373  1.00 12.40           C  
ANISOU 1291  C   ALA B 308     1550   1430   1730     70    -80    -20       C  
ATOM   1292  O   ALA B 308      -0.704   1.104 -24.019  1.00 12.87           O  
ANISOU 1292  O   ALA B 308     1610   1480   1800     70    -80      0       O  
ATOM   1293  CB  ALA B 308      -1.247  -1.820 -24.949  1.00 12.50           C  
ANISOU 1293  CB  ALA B 308     1580   1480   1690     80   -120    -20       C  
ATOM   1294  N   PRO B 309      -0.014  -0.138 -22.295  1.00 12.23           N  
ANISOU 1294  N   PRO B 309     1530   1400   1710     60    -80    -40       N  
ATOM   1295  CA  PRO B 309       0.918   0.883 -21.840  1.00 12.44           C  
ANISOU 1295  CA  PRO B 309     1560   1400   1770     50    -80    -40       C  
ATOM   1296  C   PRO B 309       2.232   0.975 -22.614  1.00 12.69           C  
ANISOU 1296  C   PRO B 309     1570   1470   1780     40    -70    -20       C  
ATOM   1297  O   PRO B 309       2.711  -0.017 -23.149  1.00 12.66           O  
ANISOU 1297  O   PRO B 309     1560   1510   1740     60    -70    -40       O  
ATOM   1298  CB  PRO B 309       1.260   0.435 -20.410  1.00 12.22           C  
ANISOU 1298  CB  PRO B 309     1530   1370   1740     50    -80    -70       C  
ATOM   1299  CG  PRO B 309       1.143  -1.081 -20.471  1.00 12.08           C  
ANISOU 1299  CG  PRO B 309     1530   1360   1690     40   -100    -80       C  
ATOM   1300  CD  PRO B 309       0.014  -1.341 -21.448  1.00 12.16           C  
ANISOU 1300  CD  PRO B 309     1540   1390   1690     40   -110    -60       C  
ATOM   1301  N   SER B 310       2.758   2.192 -22.683  1.00 13.14           N  
ANISOU 1301  N   SER B 310     1630   1510   1860      0    -80     10       N  
ATOM   1302  CA  SER B 310       4.089   2.381 -23.301  1.00 13.59           C  
ANISOU 1302  CA  SER B 310     1650   1640   1870    -40    -80     40       C  
ATOM   1303  C   SER B 310       5.092   1.754 -22.321  1.00 13.26           C  
ANISOU 1303  C   SER B 310     1590   1630   1820    -30    -70      0       C  
ATOM   1304  O   SER B 310       4.690   1.459 -21.171  1.00 12.65           O  
ANISOU 1304  O   SER B 310     1540   1490   1780      0    -70    -40       O  
ATOM   1305  CB  SER B 310       4.382   3.838 -23.500  1.00 14.34           C  
ANISOU 1305  CB  SER B 310     1760   1700   1990   -120   -120    120       C  
ATOM   1306  OG  SER B 310       4.464   4.496 -22.237  1.00 14.45           O  
ANISOU 1306  OG  SER B 310     1820   1620   2050   -120   -140     90       O  
ATOM   1307  N   ALA B 311       6.342   1.572 -22.738  1.00 13.67           N  
ANISOU 1307  N   ALA B 311     1580   1800   1810    -40    -60      0       N  
ATOM   1308  CA  ALA B 311       7.368   0.997 -21.838  1.00 13.51           C  
ANISOU 1308  CA  ALA B 311     1540   1820   1770    -20    -50    -60       C  
ATOM   1309  C   ALA B 311       7.521   1.901 -20.610  1.00 13.35           C  
ANISOU 1309  C   ALA B 311     1560   1710   1810    -70    -60    -40       C  
ATOM   1310  O   ALA B 311       7.651   1.360 -19.484  1.00 13.14           O  
ANISOU 1310  O   ALA B 311     1550   1640   1800    -30    -60    -90       O  
ATOM   1311  CB  ALA B 311       8.675   0.854 -22.579  1.00 14.36           C  
ANISOU 1311  CB  ALA B 311     1560   2110   1790    -20    -50    -60       C  
ATOM   1312  N   SER B 312       7.496   3.221 -20.827  1.00 13.58           N  
ANISOU 1312  N   SER B 312     1600   1700   1860   -150    -80     30       N  
ATOM   1313  CA  SER B 312       7.634   4.223 -19.736  1.00 13.63           C  
ANISOU 1313  CA  SER B 312     1650   1610   1920   -180   -120     40       C  
ATOM   1314  C   SER B 312       6.431   4.126 -18.784  1.00 13.05           C  
ANISOU 1314  C   SER B 312     1630   1430   1900   -110   -120    -20       C  
ATOM   1315  O   SER B 312       6.661   4.084 -17.559  1.00 12.89           O  
ANISOU 1315  O   SER B 312     1620   1380   1900    -90   -120    -60       O  
ATOM   1316  CB  SER B 312       7.795   5.621 -20.303  1.00 14.55           C  
ANISOU 1316  CB  SER B 312     1800   1680   2040   -290   -180    130       C  
ATOM   1317  OG  SER B 312       8.019   6.574 -19.276  1.00 14.82           O  
ANISOU 1317  OG  SER B 312     1890   1610   2130   -320   -240    130       O  
ATOM   1318  N   ALA B 313       5.208   4.062 -19.322  1.00 12.73           N  
ANISOU 1318  N   ALA B 313     1610   1350   1880    -70   -120    -20       N  
ATOM   1319  CA  ALA B 313       3.997   3.962 -18.472  1.00 12.45           C  
ANISOU 1319  CA  ALA B 313     1590   1280   1860      0   -130    -70       C  
ATOM   1320  C   ALA B 313       3.951   2.593 -17.784  1.00 11.90           C  
ANISOU 1320  C   ALA B 313     1490   1260   1770     20    -90   -110       C  
ATOM   1321  O   ALA B 313       3.491   2.515 -16.634  1.00 11.87           O  
ANISOU 1321  O   ALA B 313     1480   1260   1770     40    -90   -150       O  
ATOM   1322  CB  ALA B 313       2.753   4.209 -19.290  1.00 12.53           C  
ANISOU 1322  CB  ALA B 313     1610   1270   1880     30   -140    -60       C  
ATOM   1323  N   PHE B 314       4.422   1.548 -18.460  1.00 11.76           N  
ANISOU 1323  N   PHE B 314     1460   1290   1720     20    -70   -100       N  
ATOM   1324  CA  PHE B 314       4.405   0.212 -17.832  1.00 11.47           C  
ANISOU 1324  CA  PHE B 314     1430   1260   1660     30    -70   -130       C  
ATOM   1325  C   PHE B 314       5.199   0.267 -16.521  1.00 11.60           C  
ANISOU 1325  C   PHE B 314     1440   1280   1680     30    -70   -150       C  
ATOM   1326  O   PHE B 314       4.695  -0.226 -15.502  1.00 11.48           O  
ANISOU 1326  O   PHE B 314     1440   1260   1660     20    -80   -170       O  
ATOM   1327  CB  PHE B 314       4.953  -0.850 -18.786  1.00 11.51           C  
ANISOU 1327  CB  PHE B 314     1440   1300   1630     60    -90   -140       C  
ATOM   1328  CG  PHE B 314       5.020  -2.222 -18.172  1.00 11.46           C  
ANISOU 1328  CG  PHE B 314     1470   1270   1610     80   -140   -170       C  
ATOM   1329  CD1 PHE B 314       3.886  -3.016 -18.086  1.00 11.44           C  
ANISOU 1329  CD1 PHE B 314     1510   1240   1600     50   -180   -150       C  
ATOM   1330  CD2 PHE B 314       6.214  -2.712 -17.666  1.00 11.62           C  
ANISOU 1330  CD2 PHE B 314     1490   1310   1610    110   -160   -210       C  
ATOM   1331  CE1 PHE B 314       3.948  -4.273 -17.509  1.00 11.71           C  
ANISOU 1331  CE1 PHE B 314     1600   1230   1620     50   -250   -150       C  
ATOM   1332  CE2 PHE B 314       6.275  -3.973 -17.093  1.00 11.82           C  
ANISOU 1332  CE2 PHE B 314     1580   1290   1630    130   -230   -230       C  
ATOM   1333  CZ  PHE B 314       5.141  -4.747 -17.011  1.00 11.94           C  
ANISOU 1333  CZ  PHE B 314     1650   1250   1640     90   -290   -200       C  
ATOM   1334  N   PHE B 315       6.388   0.869 -16.549  1.00 11.89           N  
ANISOU 1334  N   PHE B 315     1460   1330   1720     10    -70   -150       N  
ATOM   1335  CA  PHE B 315       7.239   0.946 -15.329  1.00 12.14           C  
ANISOU 1335  CA  PHE B 315     1490   1360   1760     10    -60   -180       C  
ATOM   1336  C   PHE B 315       6.897   2.170 -14.475  1.00 12.42           C  
ANISOU 1336  C   PHE B 315     1530   1350   1830    -10    -70   -190       C  
ATOM   1337  O   PHE B 315       7.413   2.244 -13.348  1.00 12.47           O  
ANISOU 1337  O   PHE B 315     1530   1360   1840    -10    -70   -220       O  
ATOM   1338  CB  PHE B 315       8.726   0.902 -15.684  1.00 12.46           C  
ANISOU 1338  CB  PHE B 315     1500   1470   1770      0    -60   -180       C  
ATOM   1339  CG  PHE B 315       9.213  -0.473 -16.062  1.00 12.52           C  
ANISOU 1339  CG  PHE B 315     1500   1530   1730     60    -80   -220       C  
ATOM   1340  CD1 PHE B 315       9.594  -1.371 -15.076  1.00 12.56           C  
ANISOU 1340  CD1 PHE B 315     1530   1520   1730     90   -100   -260       C  
ATOM   1341  CD2 PHE B 315       9.284  -0.874 -17.385  1.00 12.80           C  
ANISOU 1341  CD2 PHE B 315     1510   1630   1720     90    -80   -230       C  
ATOM   1342  CE1 PHE B 315      10.038  -2.642 -15.408  1.00 12.90           C  
ANISOU 1342  CE1 PHE B 315     1590   1580   1730    170   -160   -310       C  
ATOM   1343  CE2 PHE B 315       9.719  -2.150 -17.714  1.00 13.15           C  
ANISOU 1343  CE2 PHE B 315     1560   1710   1720    170   -130   -290       C  
ATOM   1344  CZ  PHE B 315      10.107  -3.024 -16.727  1.00 13.23           C  
ANISOU 1344  CZ  PHE B 315     1610   1680   1730    220   -180   -330       C  
ATOM   1345  N   GLY B 316       6.044   3.069 -14.974  1.00 12.83           N  
ANISOU 1345  N   GLY B 316     1600   1360   1910      0    -90   -170       N  
ATOM   1346  CA  GLY B 316       5.678   4.261 -14.189  1.00 13.47           C  
ANISOU 1346  CA  GLY B 316     1700   1390   2020     20   -130   -210       C  
ATOM   1347  C   GLY B 316       4.383   4.075 -13.422  1.00 13.81           C  
ANISOU 1347  C   GLY B 316     1720   1470   2050     80   -130   -260       C  
ATOM   1348  O   GLY B 316       4.303   4.597 -12.294  1.00 14.22           O  
ANISOU 1348  O   GLY B 316     1760   1540   2100    120   -160   -320       O  
ATOM   1349  N   MET B 317       3.421   3.333 -13.991  1.00 14.01           N  
ANISOU 1349  N   MET B 317     1730   1550   2040     90   -110   -240       N  
ATOM   1350  CA  MET B 317       2.078   3.113 -13.376  1.00 14.53           C  
ANISOU 1350  CA  MET B 317     1750   1700   2060    130   -110   -280       C  
ATOM   1351  C   MET B 317       1.969   1.795 -12.593  1.00 14.55           C  
ANISOU 1351  C   MET B 317     1720   1800   2010     80    -90   -260       C  
ATOM   1352  O   MET B 317       1.177   1.742 -11.626  1.00 14.86           O  
ANISOU 1352  O   MET B 317     1700   1950   2000     90    -90   -280       O  
ATOM   1353  CB  MET B 317       1.015   3.025 -14.478  1.00 14.80           C  
ANISOU 1353  CB  MET B 317     1780   1750   2080    140   -110   -260       C  
ATOM   1354  CG  MET B 317       1.001   4.181 -15.467  1.00 15.27           C  
ANISOU 1354  CG  MET B 317     1890   1720   2190    170   -150   -250       C  
ATOM   1355  SD  MET B 317      -0.376   4.027 -16.654  1.00 15.98           S  
ANISOU 1355  SD  MET B 317     1970   1850   2260    200   -150   -230       S  
ATOM   1356  CE  MET B 317      -0.127   2.378 -17.302  1.00 15.34           C  
ANISOU 1356  CE  MET B 317     1880   1800   2150    110   -100   -170       C  
ATOM   1357  N   SER B 318       2.724   0.772 -12.986  1.00 14.29           N  
ANISOU 1357  N   SER B 318     1720   1720   1990     30    -80   -210       N  
ATOM   1358  CA  SER B 318       2.581  -0.575 -12.377  1.00 14.49           C  
ANISOU 1358  CA  SER B 318     1750   1790   1970    -30   -100   -180       C  
ATOM   1359  C   SER B 318       3.253  -0.740 -11.013  1.00 14.64           C  
ANISOU 1359  C   SER B 318     1750   1840   1970    -50   -100   -190       C  
ATOM   1360  O   SER B 318       4.145   0.058 -10.663  1.00 14.85           O  
ANISOU 1360  O   SER B 318     1780   1830   2040    -10    -90   -230       O  
ATOM   1361  CB  SER B 318       3.140  -1.612 -13.335  1.00 14.36           C  
ANISOU 1361  CB  SER B 318     1790   1700   1960    -50   -130   -150       C  
ATOM   1362  OG  SER B 318       2.507  -1.520 -14.613  1.00 14.46           O  
ANISOU 1362  OG  SER B 318     1810   1700   1980    -40   -120   -130       O  
ATOM   1363  N   ARG B 319       2.741  -1.702 -10.240  1.00 14.97           N  
ANISOU 1363  N   ARG B 319     1780   1950   1950   -120   -140   -150       N  
ATOM   1364  CA  ARG B 319       3.391  -2.094  -8.969  1.00 15.11           C  
ANISOU 1364  CA  ARG B 319     1790   2000   1950   -160   -150   -150       C  
ATOM   1365  C   ARG B 319       4.305  -3.231  -9.420  1.00 14.84           C  
ANISOU 1365  C   ARG B 319     1850   1840   1940   -170   -210   -120       C  
ATOM   1366  O   ARG B 319       3.773  -4.262  -9.920  1.00 15.27           O  
ANISOU 1366  O   ARG B 319     1960   1870   1970   -230   -270    -60       O  
ATOM   1367  CB  ARG B 319       2.420  -2.481  -7.850  1.00 15.96           C  
ANISOU 1367  CB  ARG B 319     1830   2270   1960   -240   -170   -110       C  
ATOM   1368  CG  ARG B 319       1.571  -1.318  -7.360  1.00 16.48           C  
ANISOU 1368  CG  ARG B 319     1790   2480   1990   -180   -130   -170       C  
ATOM   1369  CD  ARG B 319       1.009  -1.539  -5.973  1.00 17.25           C  
ANISOU 1369  CD  ARG B 319     1790   2790   1970   -240   -140   -160       C  
ATOM   1370  NE  ARG B 319       2.091  -1.758  -5.024  1.00 17.24           N  
ANISOU 1370  NE  ARG B 319     1810   2750   1990   -260   -150   -160       N  
ATOM   1371  CZ  ARG B 319       2.867  -0.803  -4.505  1.00 17.07           C  
ANISOU 1371  CZ  ARG B 319     1780   2700   2010   -160   -120   -250       C  
ATOM   1372  NH1 ARG B 319       2.715   0.465  -4.856  1.00 17.25           N  
ANISOU 1372  NH1 ARG B 319     1780   2700   2080    -40    -90   -340       N  
ATOM   1373  NH2 ARG B 319       3.816  -1.128  -3.648  1.00 16.82           N  
ANISOU 1373  NH2 ARG B 319     1760   2640   1990   -190   -130   -240       N  
ATOM   1374  N   ILE B 320       5.612  -2.989  -9.385  1.00 14.35           N  
ANISOU 1374  N   ILE B 320     1810   1720   1920   -120   -190   -160       N  
ATOM   1375  CA  ILE B 320       6.615  -3.983  -9.861  1.00 14.58           C  
ANISOU 1375  CA  ILE B 320     1910   1660   1960    -90   -250   -170       C  
ATOM   1376  C   ILE B 320       7.161  -4.760  -8.661  1.00 15.17           C  
ANISOU 1376  C   ILE B 320     2020   1730   2010   -120   -310   -150       C  
ATOM   1377  O   ILE B 320       7.314  -4.162  -7.568  1.00 15.10           O  
ANISOU 1377  O   ILE B 320     1960   1780   2000   -140   -270   -160       O  
ATOM   1378  CB  ILE B 320       7.738  -3.282 -10.657  1.00 14.20           C  
ANISOU 1378  CB  ILE B 320     1850   1600   1950    -10   -210   -220       C  
ATOM   1379  CG1 ILE B 320       7.198  -2.443 -11.823  1.00 14.14           C  
ANISOU 1379  CG1 ILE B 320     1810   1600   1960     10   -160   -220       C  
ATOM   1380  CG2 ILE B 320       8.776  -4.286 -11.127  1.00 14.50           C  
ANISOU 1380  CG2 ILE B 320     1930   1600   1970     50   -270   -260       C  
ATOM   1381  CD1 ILE B 320       6.458  -3.228 -12.889  1.00 14.11           C  
ANISOU 1381  CD1 ILE B 320     1850   1570   1940     10   -200   -200       C  
ATOM   1382  N   GLY B 321       7.432  -6.046  -8.876  1.00 16.10           N  
ANISOU 1382  N   GLY B 321     2230   1770   2120   -120   -430   -140       N  
ATOM   1383  CA  GLY B 321       7.985  -6.938  -7.845  1.00 17.06           C  
ANISOU 1383  CA  GLY B 321     2410   1850   2220   -150   -520   -120       C  
ATOM   1384  C   GLY B 321       8.954  -7.929  -8.459  1.00 18.07           C  
ANISOU 1384  C   GLY B 321     2640   1870   2360    -50   -630   -170       C  
ATOM   1385  O   GLY B 321       8.897  -8.129  -9.691  1.00 17.92           O  
ANISOU 1385  O   GLY B 321     2640   1810   2350     20   -650   -210       O  
ATOM   1386  N   MET B 322       9.810  -8.511  -7.626  1.00 19.36           N  
ANISOU 1386  N   MET B 322     2850   1990   2510    -30   -710   -190       N  
ATOM   1387  CA  MET B 322      10.826  -9.515  -8.027  1.00 21.68           C  
ANISOU 1387  CA  MET B 322     3240   2190   2810    100   -850   -270       C  
ATOM   1388  C   MET B 322      10.534 -10.771  -7.200  1.00 23.36           C  
ANISOU 1388  C   MET B 322     3590   2280   3000     20  -1040   -190       C  
ATOM   1389  O   MET B 322      10.544 -10.655  -5.971  1.00 23.10           O  
ANISOU 1389  O   MET B 322     3540   2290   2950    -70  -1030   -130       O  
ATOM   1390  CB  MET B 322      12.233  -8.998  -7.701  1.00 22.68           C  
ANISOU 1390  CB  MET B 322     3300   2390   2930    210   -780   -360       C  
ATOM   1391  CG  MET B 322      13.367  -9.940  -8.081  1.00 25.08           C  
ANISOU 1391  CG  MET B 322     3670   2650   3210    380   -920   -470       C  
ATOM   1392  SD  MET B 322      13.771  -9.940  -9.846  1.00 27.70           S  
ANISOU 1392  SD  MET B 322     3960   3040   3520    540   -910   -580       S  
ATOM   1393  CE  MET B 322      14.584  -8.352  -9.997  1.00 26.95           C  
ANISOU 1393  CE  MET B 322     3670   3160   3400    540   -690   -610       C  
ATOM   1394  N   GLU B 323      10.222 -11.902  -7.835  1.00 25.39           N  
ANISOU 1394  N   GLU B 323     3990   2400   3260     30  -1220   -180       N  
ATOM   1395  CA  GLU B 323       9.936 -13.133  -7.053  1.00 27.71           C  
ANISOU 1395  CA  GLU B 323     4450   2550   3530    -70  -1450    -90       C  
ATOM   1396  C   GLU B 323      10.857 -14.266  -7.495  1.00 28.47           C  
ANISOU 1396  C   GLU B 323     4700   2480   3640    100  -1670   -200       C  
ATOM   1397  O   GLU B 323      10.945 -14.523  -8.703  1.00 28.91           O  
ANISOU 1397  O   GLU B 323     4790   2490   3700    240  -1720   -290       O  
ATOM   1398  CB  GLU B 323       8.497 -13.618  -7.223  1.00 29.99           C  
ANISOU 1398  CB  GLU B 323     4800   2790   3800   -260  -1530     50       C  
ATOM   1399  CG  GLU B 323       7.450 -12.656  -6.708  1.00 31.38           C  
ANISOU 1399  CG  GLU B 323     4820   3160   3950   -430  -1350    150       C  
ATOM   1400  CD  GLU B 323       6.029 -13.200  -6.784  1.00 34.37           C  
ANISOU 1400  CD  GLU B 323     5240   3540   4280   -640  -1440    300       C  
ATOM   1401  OE1 GLU B 323       5.846 -14.337  -7.288  1.00 36.65           O  
ANISOU 1401  OE1 GLU B 323     5700   3650   4570   -660  -1660    340       O  
ATOM   1402  OE2 GLU B 323       5.106 -12.497  -6.321  1.00 37.13           O  
ANISOU 1402  OE2 GLU B 323     5450   4080   4580   -770  -1310    380       O  
ATOM   1403  N   VAL B 324      11.487 -14.924  -6.526  1.00 21.04           N  
ANISOU 1403  N   VAL B 324     2900   2300   2800   -170   -680    380       N  
ATOM   1404  CA  VAL B 324      12.379 -16.079  -6.806  1.00 21.21           C  
ANISOU 1404  CA  VAL B 324     2840   2320   2900   -120   -690    410       C  
ATOM   1405  C   VAL B 324      11.620 -17.317  -6.319  1.00 21.12           C  
ANISOU 1405  C   VAL B 324     2910   2260   2860    -90   -670    410       C  
ATOM   1406  O   VAL B 324      11.397 -17.436  -5.099  1.00 21.14           O  
ANISOU 1406  O   VAL B 324     3000   2230   2800   -120   -720    430       O  
ATOM   1407  CB  VAL B 324      13.760 -15.906  -6.152  1.00 22.23           C  
ANISOU 1407  CB  VAL B 324     2930   2440   3080   -130   -810    480       C  
ATOM   1408  CG1 VAL B 324      14.630 -17.133  -6.362  1.00 23.12           C  
ANISOU 1408  CG1 VAL B 324     2960   2550   3270    -60   -820    510       C  
ATOM   1409  CG2 VAL B 324      14.457 -14.654  -6.675  1.00 22.27           C  
ANISOU 1409  CG2 VAL B 324     2840   2490   3130   -170   -840    500       C  
ATOM   1410  N   THR B 325      11.212 -18.174  -7.261  1.00 20.77           N  
ANISOU 1410  N   THR B 325     2830   2210   2850    -50   -590    380       N  
ATOM   1411  CA  THR B 325      10.418 -19.393  -6.959  1.00 20.89           C  
ANISOU 1411  CA  THR B 325     2910   2170   2860    -30   -570    370       C  
ATOM   1412  C   THR B 325      11.130 -20.620  -7.516  1.00 21.45           C  
ANISOU 1412  C   THR B 325     2920   2210   3020     40   -580    380       C  
ATOM   1413  O   THR B 325      12.130 -20.503  -8.221  1.00 20.58           O  
ANISOU 1413  O   THR B 325     2720   2140   2970     80   -580    370       O  
ATOM   1414  CB  THR B 325       9.023 -19.294  -7.597  1.00 20.29           C  
ANISOU 1414  CB  THR B 325     2870   2100   2740    -50   -480    320       C  
ATOM   1415  OG1 THR B 325       9.173 -19.429  -9.010  1.00 19.81           O  
ANISOU 1415  OG1 THR B 325     2730   2060   2730    -10   -430    270       O  
ATOM   1416  CG2 THR B 325       8.301 -18.004  -7.273  1.00 19.55           C  
ANISOU 1416  CG2 THR B 325     2820   2050   2560   -100   -460    310       C  
ATOM   1417  N   PRO B 326      10.656 -21.842  -7.196  1.00 22.68           N  
ANISOU 1417  N   PRO B 326     3130   2290   3190     50   -590    390       N  
ATOM   1418  CA  PRO B 326      11.262 -23.054  -7.744  1.00 24.22           C  
ANISOU 1418  CA  PRO B 326     3290   2440   3480    130   -610    380       C  
ATOM   1419  C   PRO B 326      11.279 -23.035  -9.283  1.00 25.07           C  
ANISOU 1419  C   PRO B 326     3320   2580   3620    190   -540    300       C  
ATOM   1420  O   PRO B 326      12.158 -23.627  -9.841  1.00 26.95           O  
ANISOU 1420  O   PRO B 326     3500   2820   3920    270   -550    290       O  
ATOM   1421  CB  PRO B 326      10.358 -24.177  -7.208  1.00 24.10           C  
ANISOU 1421  CB  PRO B 326     3360   2330   3460    110   -620    400       C  
ATOM   1422  CG  PRO B 326       9.763 -23.603  -5.943  1.00 23.55           C  
ANISOU 1422  CG  PRO B 326     3360   2280   3300     30   -640    460       C  
ATOM   1423  CD  PRO B 326       9.572 -22.131  -6.244  1.00 22.77           C  
ANISOU 1423  CD  PRO B 326     3240   2270   3140      0   -590    420       C  
ATOM   1424  N   SER B 327      10.339 -22.315  -9.915  1.00 25.81           N  
ANISOU 1424  N   SER B 327     3430   2720   3660    150   -470    250       N  
ATOM   1425  CA  SER B 327      10.248 -22.244 -11.401  1.00 26.55           C  
ANISOU 1425  CA  SER B 327     3470   2860   3760    210   -400    180       C  
ATOM   1426  C   SER B 327      11.130 -21.127 -11.982  1.00 26.89           C  
ANISOU 1426  C   SER B 327     3410   3000   3800    220   -370    190       C  
ATOM   1427  O   SER B 327      11.065 -20.930 -13.212  1.00 28.71           O  
ANISOU 1427  O   SER B 327     3600   3290   4030    260   -310    140       O  
ATOM   1428  CB  SER B 327       8.824 -22.064 -11.841  1.00 26.38           C  
ANISOU 1428  CB  SER B 327     3500   2830   3700    160   -340    130       C  
ATOM   1429  OG  SER B 327       8.300 -20.833 -11.366  1.00 26.26           O  
ANISOU 1429  OG  SER B 327     3500   2860   3620     80   -320    160       O  
ATOM   1430  N   GLY B 328      11.882 -20.399 -11.147  1.00 25.38           N  
ANISOU 1430  N   GLY B 328     3200   2840   3610    180   -420    250       N  
ATOM   1431  CA  GLY B 328      12.773 -19.336 -11.657  1.00 24.67           C  
ANISOU 1431  CA  GLY B 328     3000   2840   3530    180   -410    280       C  
ATOM   1432  C   GLY B 328      12.558 -17.980 -10.997  1.00 22.83           C  
ANISOU 1432  C   GLY B 328     2800   2620   3260     80   -440    320       C  
ATOM   1433  O   GLY B 328      11.985 -17.927  -9.882  1.00 21.16           O  
ANISOU 1433  O   GLY B 328     2680   2360   3000     30   -480    330       O  
ATOM   1434  N   THR B 329      13.027 -16.925 -11.673  1.00 21.50           N  
ANISOU 1434  N   THR B 329     2550   2520   3100     70   -420    340       N  
ATOM   1435  CA  THR B 329      12.921 -15.522 -11.194  1.00 20.56           C  
ANISOU 1435  CA  THR B 329     2450   2410   2950    -20   -460    360       C  
ATOM   1436  C   THR B 329      11.881 -14.799 -12.050  1.00 19.46           C  
ANISOU 1436  C   THR B 329     2330   2300   2760    -40   -380    320       C  
ATOM   1437  O   THR B 329      12.023 -14.839 -13.290  1.00 19.27           O  
ANISOU 1437  O   THR B 329     2230   2340   2750      0   -310    310       O  
ATOM   1438  CB  THR B 329      14.283 -14.825 -11.236  1.00 20.98           C  
ANISOU 1438  CB  THR B 329     2390   2520   3070    -40   -520    440       C  
ATOM   1439  OG1 THR B 329      15.183 -15.658 -10.505  1.00 22.12           O  
ANISOU 1439  OG1 THR B 329     2510   2630   3260    -10   -590    480       O  
ATOM   1440  CG2 THR B 329      14.247 -13.426 -10.660  1.00 20.53           C  
ANISOU 1440  CG2 THR B 329     2360   2440   2990   -130   -590    470       C  
ATOM   1441  N   TRP B 330      10.925 -14.120 -11.407  1.00 18.46           N  
ANISOU 1441  N   TRP B 330     2300   2140   2570   -100   -400    300       N  
ATOM   1442  CA  TRP B 330       9.832 -13.435 -12.146  1.00 17.73           C  
ANISOU 1442  CA  TRP B 330     2230   2070   2430   -120   -330    250       C  
ATOM   1443  C   TRP B 330       9.705 -11.951 -11.792  1.00 17.49           C  
ANISOU 1443  C   TRP B 330     2230   2030   2380   -180   -370    270       C  
ATOM   1444  O   TRP B 330       9.829 -11.596 -10.608  1.00 17.89           O  
ANISOU 1444  O   TRP B 330     2350   2040   2410   -210   -450    280       O  
ATOM   1445  CB  TRP B 330       8.515 -14.143 -11.836  1.00 17.25           C  
ANISOU 1445  CB  TRP B 330     2270   1970   2320   -110   -290    200       C  
ATOM   1446  CG  TRP B 330       8.525 -15.596 -12.182  1.00 17.98           C  
ANISOU 1446  CG  TRP B 330     2350   2040   2440    -50   -260    180       C  
ATOM   1447  CD1 TRP B 330       9.056 -16.619 -11.447  1.00 18.54           C  
ANISOU 1447  CD1 TRP B 330     2430   2070   2540    -30   -310    200       C  
ATOM   1448  CD2 TRP B 330       7.944 -16.194 -13.348  1.00 17.93           C  
ANISOU 1448  CD2 TRP B 330     2320   2050   2440    -10   -190    130       C  
ATOM   1449  NE1 TRP B 330       8.866 -17.810 -12.090  1.00 19.05           N  
ANISOU 1449  NE1 TRP B 330     2490   2110   2640     30   -280    170       N  
ATOM   1450  CE2 TRP B 330       8.181 -17.582 -13.256  1.00 18.84           C  
ANISOU 1450  CE2 TRP B 330     2440   2120   2590     40   -210    120       C  
ATOM   1451  CE3 TRP B 330       7.260 -15.689 -14.461  1.00 18.37           C  
ANISOU 1451  CE3 TRP B 330     2360   2150   2470    -10   -130     90       C  
ATOM   1452  CZ2 TRP B 330       7.754 -18.469 -14.242  1.00 19.16           C  
ANISOU 1452  CZ2 TRP B 330     2480   2150   2640     90   -170     60       C  
ATOM   1453  CZ3 TRP B 330       6.831 -16.568 -15.430  1.00 18.37           C  
ANISOU 1453  CZ3 TRP B 330     2350   2150   2470     40    -90     30       C  
ATOM   1454  CH2 TRP B 330       7.079 -17.938 -15.318  1.00 18.99           C  
ANISOU 1454  CH2 TRP B 330     2440   2180   2590     90   -110     20       C  
ATOM   1455  N   LEU B 331       9.464 -11.132 -12.813  1.00 16.97           N  
ANISOU 1455  N   LEU B 331     2120   2010   2320   -190   -330    270       N  
ATOM   1456  CA  LEU B 331       9.214  -9.683 -12.642  1.00 17.21           C  
ANISOU 1456  CA  LEU B 331     2180   2020   2340   -250   -370    280       C  
ATOM   1457  C   LEU B 331       7.691  -9.556 -12.608  1.00 16.09           C  
ANISOU 1457  C   LEU B 331     2130   1860   2120   -240   -310    210       C  
ATOM   1458  O   LEU B 331       7.083  -9.683 -13.680  1.00 16.56           O  
ANISOU 1458  O   LEU B 331     2160   1960   2170   -220   -240    190       O  
ATOM   1459  CB  LEU B 331       9.812  -8.895 -13.812  1.00 17.87           C  
ANISOU 1459  CB  LEU B 331     2160   2160   2470   -260   -350    330       C  
ATOM   1460  CG  LEU B 331       9.654  -7.376 -13.733  1.00 18.56           C  
ANISOU 1460  CG  LEU B 331     2270   2220   2560   -330   -410    350       C  
ATOM   1461  CD1 LEU B 331      10.358  -6.825 -12.505  1.00 19.61           C  
ANISOU 1461  CD1 LEU B 331     2440   2280   2720   -380   -540    380       C  
ATOM   1462  CD2 LEU B 331      10.211  -6.709 -14.979  1.00 19.27           C  
ANISOU 1462  CD2 LEU B 331     2240   2370   2700   -340   -380    420       C  
ATOM   1463  N   THR B 332       7.104  -9.396 -11.425  1.00 15.36           N  
ANISOU 1463  N   THR B 332     2140   1720   1980   -250   -350    180       N  
ATOM   1464  CA  THR B 332       5.625  -9.297 -11.320  1.00 14.87           C  
ANISOU 1464  CA  THR B 332     2150   1650   1850   -240   -290    130       C  
ATOM   1465  C   THR B 332       5.149  -7.877 -11.629  1.00 14.66           C  
ANISOU 1465  C   THR B 332     2150   1610   1810   -260   -300    110       C  
ATOM   1466  O   THR B 332       5.918  -6.918 -11.399  1.00 15.27           O  
ANISOU 1466  O   THR B 332     2220   1670   1920   -290   -380    140       O  
ATOM   1467  CB  THR B 332       5.141  -9.693  -9.925  1.00 14.79           C  
ANISOU 1467  CB  THR B 332     2240   1610   1770   -230   -310    110       C  
ATOM   1468  OG1 THR B 332       5.710  -8.762  -9.001  1.00 15.22           O  
ANISOU 1468  OG1 THR B 332     2350   1620   1810   -260   -410    120       O  
ATOM   1469  CG2 THR B 332       5.506 -11.117  -9.578  1.00 15.34           C  
ANISOU 1469  CG2 THR B 332     2300   1670   1860   -220   -310    130       C  
ATOM   1470  N   TYR B 333       3.911  -7.758 -12.102  1.00 13.81           N  
ANISOU 1470  N   TYR B 333     2060   1520   1670   -240   -230     80       N  
ATOM   1471  CA  TYR B 333       3.350  -6.420 -12.411  1.00 13.56           C  
ANISOU 1471  CA  TYR B 333     2050   1480   1630   -250   -240     60       C  
ATOM   1472  C   TYR B 333       1.833  -6.439 -12.219  1.00 12.96           C  
ANISOU 1472  C   TYR B 333     2030   1410   1490   -220   -170     10       C  
ATOM   1473  O   TYR B 333       1.199  -7.452 -12.547  1.00 12.09           O  
ANISOU 1473  O   TYR B 333     1890   1330   1370   -200   -100      0       O  
ATOM   1474  CB  TYR B 333       3.714  -5.981 -13.831  1.00 13.26           C  
ANISOU 1474  CB  TYR B 333     1920   1480   1640   -270   -220     90       C  
ATOM   1475  CG  TYR B 333       3.155  -6.836 -14.941  1.00 12.63           C  
ANISOU 1475  CG  TYR B 333     1780   1460   1560   -240   -130     80       C  
ATOM   1476  CD1 TYR B 333       1.892  -6.592 -15.468  1.00 12.41           C  
ANISOU 1476  CD1 TYR B 333     1770   1440   1500   -220    -70     50       C  
ATOM   1477  CD2 TYR B 333       3.901  -7.861 -15.501  1.00 12.59           C  
ANISOU 1477  CD2 TYR B 333     1710   1490   1580   -220   -100    100       C  
ATOM   1478  CE1 TYR B 333       1.380  -7.358 -16.503  1.00 12.08           C  
ANISOU 1478  CE1 TYR B 333     1680   1450   1460   -200    -10     30       C  
ATOM   1479  CE2 TYR B 333       3.405  -8.635 -16.538  1.00 12.29           C  
ANISOU 1479  CE2 TYR B 333     1640   1500   1540   -190    -40     70       C  
ATOM   1480  CZ  TYR B 333       2.139  -8.383 -17.039  1.00 12.05           C  
ANISOU 1480  CZ  TYR B 333     1630   1480   1470   -180     10     40       C  
ATOM   1481  OH  TYR B 333       1.645  -9.141 -18.057  1.00 12.00           O  
ANISOU 1481  OH  TYR B 333     1590   1510   1460   -160     60     10       O  
ATOM   1482  N   THR B 334       1.303  -5.349 -11.658  1.00 13.53           N  
ANISOU 1482  N   THR B 334     2170   1450   1520   -210   -200    -20       N  
ATOM   1483  CA  THR B 334      -0.156  -5.167 -11.439  1.00 13.46           C  
ANISOU 1483  CA  THR B 334     2200   1450   1460   -170   -140    -60       C  
ATOM   1484  C   THR B 334      -0.473  -3.687 -11.632  1.00 12.98           C  
ANISOU 1484  C   THR B 334     2180   1360   1400   -160   -170    -80       C  
ATOM   1485  O   THR B 334       0.451  -2.858 -11.447  1.00 13.39           O  
ANISOU 1485  O   THR B 334     2250   1360   1480   -190   -270    -70       O  
ATOM   1486  CB  THR B 334      -0.627  -5.529 -10.023  1.00 14.34           C  
ANISOU 1486  CB  THR B 334     2400   1560   1490   -140   -130    -80       C  
ATOM   1487  OG1 THR B 334      -0.066  -4.563  -9.136  1.00 15.82           O  
ANISOU 1487  OG1 THR B 334     2670   1700   1650   -130   -220   -100       O  
ATOM   1488  CG2 THR B 334      -0.234  -6.919  -9.579  1.00 14.75           C  
ANISOU 1488  CG2 THR B 334     2430   1630   1540   -150   -110    -50       C  
ATOM   1489  N   GLY B 335      -1.718  -3.371 -11.969  1.00 12.11           N  
ANISOU 1489  N   GLY B 335     2070   1270   1270   -120   -110   -110       N  
ATOM   1490  CA  GLY B 335      -2.103  -1.959 -12.124  1.00 12.35           C  
ANISOU 1490  CA  GLY B 335     2140   1260   1300   -100   -150   -130       C  
ATOM   1491  C   GLY B 335      -3.503  -1.797 -12.680  1.00 11.99           C  
ANISOU 1491  C   GLY B 335     2060   1250   1240    -60    -70   -150       C  
ATOM   1492  O   GLY B 335      -4.185  -2.821 -12.924  1.00 11.25           O  
ANISOU 1492  O   GLY B 335     1920   1210   1140    -50     10   -140       O  
ATOM   1493  N   ALA B 336      -3.913  -0.544 -12.857  1.00 12.32           N  
ANISOU 1493  N   ALA B 336     2140   1250   1290    -30   -110   -170       N  
ATOM   1494  CA  ALA B 336      -5.244  -0.220 -13.408  1.00 12.41           C  
ANISOU 1494  CA  ALA B 336     2120   1290   1300     20    -50   -190       C  
ATOM   1495  C   ALA B 336      -5.119   0.990 -14.340  1.00 12.53           C  
ANISOU 1495  C   ALA B 336     2130   1260   1370      0   -110   -170       C  
ATOM   1496  O   ALA B 336      -4.389   1.939 -14.004  1.00 12.45           O  
ANISOU 1496  O   ALA B 336     2180   1170   1380    -10   -200   -180       O  
ATOM   1497  CB  ALA B 336      -6.215   0.023 -12.289  1.00 13.05           C  
ANISOU 1497  CB  ALA B 336     2270   1380   1310    100    -10   -240       C  
ATOM   1498  N   ILE B 337      -5.785   0.907 -15.491  1.00 12.60           N  
ANISOU 1498  N   ILE B 337     2060   1310   1410      0    -60   -150       N  
ATOM   1499  CA  ILE B 337      -5.797   1.967 -16.537  1.00 13.29           C  
ANISOU 1499  CA  ILE B 337     2130   1370   1550    -10   -100   -120       C  
ATOM   1500  C   ILE B 337      -7.233   2.479 -16.653  1.00 14.07           C  
ANISOU 1500  C   ILE B 337     2230   1480   1640     60    -70   -150       C  
ATOM   1501  O   ILE B 337      -8.146   1.688 -16.987  1.00 12.92           O  
ANISOU 1501  O   ILE B 337     2030   1410   1470     80     10   -150       O  
ATOM   1502  CB  ILE B 337      -5.221   1.410 -17.849  1.00 12.83           C  
ANISOU 1502  CB  ILE B 337     1980   1370   1530    -70    -90    -50       C  
ATOM   1503  CG1 ILE B 337      -3.755   1.017 -17.642  1.00 13.01           C  
ANISOU 1503  CG1 ILE B 337     1990   1380   1570   -130   -130    -20       C  
ATOM   1504  CG2 ILE B 337      -5.388   2.397 -18.991  1.00 13.11           C  
ANISOU 1504  CG2 ILE B 337     1980   1390   1600    -80   -120    -10       C  
ATOM   1505  CD1 ILE B 337      -3.151   0.261 -18.790  1.00 12.87           C  
ANISOU 1505  CD1 ILE B 337     1890   1440   1570   -170    -90     30       C  
ATOM   1506  N   LYS B 338      -7.406   3.763 -16.370  1.00 15.69           N  
ANISOU 1506  N   LYS B 338     2500   1600   1860    100   -130   -170       N  
ATOM   1507  CA  LYS B 338      -8.745   4.383 -16.373  1.00 17.28           C  
ANISOU 1507  CA  LYS B 338     2710   1810   2050    190   -100   -210       C  
ATOM   1508  C   LYS B 338      -9.228   4.685 -17.794  1.00 16.88           C  
ANISOU 1508  C   LYS B 338     2580   1780   2050    170   -100   -150       C  
ATOM   1509  O   LYS B 338      -8.455   5.275 -18.567  1.00 16.24           O  
ANISOU 1509  O   LYS B 338     2500   1660   2020    120   -160   -100       O  
ATOM   1510  CB  LYS B 338      -8.661   5.705 -15.607  1.00 19.61           C  
ANISOU 1510  CB  LYS B 338     3120   1990   2340    250   -190   -250       C  
ATOM   1511  CG  LYS B 338      -9.997   6.349 -15.282  1.00 21.94           C  
ANISOU 1511  CG  LYS B 338     3440   2280   2610    370   -150   -310       C  
ATOM   1512  CD  LYS B 338      -9.869   7.742 -14.722  1.00 24.69           C  
ANISOU 1512  CD  LYS B 338     3900   2500   2970    430   -260   -360       C  
ATOM   1513  CE  LYS B 338     -11.202   8.327 -14.322  1.00 27.43           C  
ANISOU 1513  CE  LYS B 338     4280   2850   3290    570   -220   -430       C  
ATOM   1514  NZ  LYS B 338     -12.178   8.298 -15.441  1.00 28.60           N  
ANISOU 1514  NZ  LYS B 338     4320   3060   3480    580   -160   -380       N  
ATOM   1515  N   LEU B 339     -10.435   4.229 -18.136  1.00 17.24           N  
ANISOU 1515  N   LEU B 339     2570   1900   2080    210    -20   -160       N  
ATOM   1516  CA  LEU B 339     -11.034   4.610 -19.439  1.00 16.95           C  
ANISOU 1516  CA  LEU B 339     2470   1890   2080    210    -30   -120       C  
ATOM   1517  C   LEU B 339     -11.532   6.050 -19.275  1.00 18.57           C  
ANISOU 1517  C   LEU B 339     2730   2010   2320    280    -90   -130       C  
ATOM   1518  O   LEU B 339     -11.766   6.467 -18.119  1.00 18.68           O  
ANISOU 1518  O   LEU B 339     2820   1980   2300    360    -90   -200       O  
ATOM   1519  CB  LEU B 339     -12.191   3.684 -19.826  1.00 16.80           C  
ANISOU 1519  CB  LEU B 339     2360   1970   2050    220     50   -110       C  
ATOM   1520  CG  LEU B 339     -11.835   2.365 -20.513  1.00 15.91           C  
ANISOU 1520  CG  LEU B 339     2180   1930   1930    150     80    -90       C  
ATOM   1521  CD1 LEU B 339     -11.072   1.430 -19.596  1.00 15.99           C  
ANISOU 1521  CD1 LEU B 339     2220   1940   1910    120    110   -110       C  
ATOM   1522  CD2 LEU B 339     -13.100   1.688 -21.022  1.00 16.15           C  
ANISOU 1522  CD2 LEU B 339     2130   2040   1970    160    130    -80       C  
ATOM   1523  N   ASP B 340     -11.683   6.778 -20.380  1.00 19.98           N  
ANISOU 1523  N   ASP B 340     2880   2170   2540    270   -130    -80       N  
ATOM   1524  CA  ASP B 340     -12.154   8.189 -20.352  1.00 22.07           C  
ANISOU 1524  CA  ASP B 340     3200   2340   2850    340   -200    -90       C  
ATOM   1525  C   ASP B 340     -13.674   8.187 -20.579  1.00 23.74           C  
ANISOU 1525  C   ASP B 340     3350   2610   3060    430   -150   -110       C  
ATOM   1526  O   ASP B 340     -14.089   7.863 -21.706  1.00 22.30           O  
ANISOU 1526  O   ASP B 340     3080   2500   2890    390   -130    -60       O  
ATOM   1527  CB  ASP B 340     -11.371   8.994 -21.394  1.00 22.57           C  
ANISOU 1527  CB  ASP B 340     3260   2340   2970    270   -290    -10       C  
ATOM   1528  CG  ASP B 340     -11.669  10.483 -21.462  1.00 24.03           C  
ANISOU 1528  CG  ASP B 340     3500   2410   3220    320   -390      0       C  
ATOM   1529  OD1 ASP B 340     -12.634  10.940 -20.802  1.00 24.12           O  
ANISOU 1529  OD1 ASP B 340     3550   2390   3220    440   -380    -70       O  
ATOM   1530  OD2 ASP B 340     -10.916  11.181 -22.175  1.00 24.49           O  
ANISOU 1530  OD2 ASP B 340     3570   2400   3330    250   -470     80       O  
ATOM   1531  N   ASP B 341     -14.462   8.521 -19.544  1.00 25.83           N  
ANISOU 1531  N   ASP B 341     3650   2860   3300    540   -120   -180       N  
ATOM   1532  CA  ASP B 341     -15.949   8.537 -19.663  1.00 28.31           C  
ANISOU 1532  CA  ASP B 341     3900   3240   3620    630    -60   -190       C  
ATOM   1533  C   ASP B 341     -16.394   9.539 -20.732  1.00 27.79           C  
ANISOU 1533  C   ASP B 341     3810   3130   3620    650   -120   -150       C  
ATOM   1534  O   ASP B 341     -17.473   9.312 -21.325  1.00 29.45           O  
ANISOU 1534  O   ASP B 341     3930   3410   3850    680    -80   -120       O  
ATOM   1535  CB  ASP B 341     -16.653   8.884 -18.344  1.00 31.47           C  
ANISOU 1535  CB  ASP B 341     4350   3630   3980    770    -10   -270       C  
ATOM   1536  CG  ASP B 341     -16.639   7.781 -17.298  1.00 34.67           C  
ANISOU 1536  CG  ASP B 341     4750   4120   4310    770     80   -310       C  
ATOM   1537  OD1 ASP B 341     -16.078   6.701 -17.579  1.00 36.78           O  
ANISOU 1537  OD1 ASP B 341     4970   4440   4560    660    110   -270       O  
ATOM   1538  OD2 ASP B 341     -17.220   7.999 -16.216  1.00 38.94           O  
ANISOU 1538  OD2 ASP B 341     5330   4670   4790    880    130   -370       O  
ATOM   1539  N   LYS B 342     -15.596  10.584 -20.968  1.00 27.18           N  
ANISOU 1539  N   LYS B 342     3810   2930   3580    630   -230   -130       N  
ATOM   1540  CA  LYS B 342     -15.947  11.639 -21.960  1.00 27.85           C  
ANISOU 1540  CA  LYS B 342     3890   2950   3740    650   -310    -70       C  
ATOM   1541  C   LYS B 342     -15.570  11.218 -23.385  1.00 24.77           C  
ANISOU 1541  C   LYS B 342     3420   2630   3360    530   -320     30       C  
ATOM   1542  O   LYS B 342     -16.017  11.896 -24.322  1.00 25.65           O  
ANISOU 1542  O   LYS B 342     3510   2720   3520    550   -370     90       O  
ATOM   1543  CB  LYS B 342     -15.300  12.970 -21.569  1.00 30.36           C  
ANISOU 1543  CB  LYS B 342     4330   3100   4100    670   -430    -90       C  
ATOM   1544  CG  LYS B 342     -15.799  13.525 -20.242  1.00 33.43           C  
ANISOU 1544  CG  LYS B 342     4810   3420   4470    810   -430   -200       C  
ATOM   1545  CD  LYS B 342     -15.288  14.908 -19.918  1.00 36.51           C  
ANISOU 1545  CD  LYS B 342     5330   3630   4920    850   -570   -230       C  
ATOM   1546  CE  LYS B 342     -15.846  15.433 -18.613  1.00 39.30           C  
ANISOU 1546  CE  LYS B 342     5780   3920   5230   1010   -570   -360       C  
ATOM   1547  NZ  LYS B 342     -15.391  16.819 -18.345  1.00 42.94           N  
ANISOU 1547  NZ  LYS B 342     6380   4180   5760   1050   -720   -390       N  
ATOM   1548  N   ASP B 343     -14.778  10.157 -23.550  1.00 21.61           N  
ANISOU 1548  N   ASP B 343     2990   2300   2920    440   -280     50       N  
ATOM   1549  CA  ASP B 343     -14.413   9.707 -24.917  1.00 19.65           C  
ANISOU 1549  CA  ASP B 343     2680   2120   2670    340   -280    140       C  
ATOM   1550  C   ASP B 343     -15.717   9.294 -25.598  1.00 18.54           C  
ANISOU 1550  C   ASP B 343     2450   2070   2520    380   -250    140       C  
ATOM   1551  O   ASP B 343     -16.476   8.511 -25.035  1.00 18.05           O  
ANISOU 1551  O   ASP B 343     2350   2080   2440    420   -170     90       O  
ATOM   1552  CB  ASP B 343     -13.345   8.611 -24.843  1.00 18.62           C  
ANISOU 1552  CB  ASP B 343     2530   2050   2490    250   -240    140       C  
ATOM   1553  CG  ASP B 343     -12.904   8.040 -26.176  1.00 18.42           C  
ANISOU 1553  CG  ASP B 343     2450   2110   2440    180   -240    220       C  
ATOM   1554  OD1 ASP B 343     -13.709   8.076 -27.126  1.00 18.99           O  
ANISOU 1554  OD1 ASP B 343     2470   2240   2510    190   -240    250       O  
ATOM   1555  OD2 ASP B 343     -11.740   7.581 -26.257  1.00 18.39           O  
ANISOU 1555  OD2 ASP B 343     2450   2130   2420    100   -230    240       O  
ATOM   1556  N   PRO B 344     -16.034   9.806 -26.810  1.00 18.03           N  
ANISOU 1556  N   PRO B 344     2350   2020   2480    370   -300    220       N  
ATOM   1557  CA  PRO B 344     -17.293   9.464 -27.479  1.00 17.93           C  
ANISOU 1557  CA  PRO B 344     2250   2090   2470    410   -280    230       C  
ATOM   1558  C   PRO B 344     -17.444   7.976 -27.829  1.00 16.75           C  
ANISOU 1558  C   PRO B 344     2030   2060   2270    360   -210    210       C  
ATOM   1559  O   PRO B 344     -18.552   7.569 -28.084  1.00 17.18           O  
ANISOU 1559  O   PRO B 344     2020   2180   2330    390   -200    200       O  
ATOM   1560  CB  PRO B 344     -17.291  10.337 -28.748  1.00 18.58           C  
ANISOU 1560  CB  PRO B 344     2330   2160   2570    400   -360    320       C  
ATOM   1561  CG  PRO B 344     -15.833  10.671 -28.979  1.00 18.59           C  
ANISOU 1561  CG  PRO B 344     2390   2110   2570    310   -400    380       C  
ATOM   1562  CD  PRO B 344     -15.215  10.741 -27.597  1.00 18.54           C  
ANISOU 1562  CD  PRO B 344     2450   2020   2570    320   -380    310       C  
ATOM   1563  N   ASN B 345     -16.338   7.223 -27.837  1.00 15.64           N  
ANISOU 1563  N   ASN B 345     1910   1950   2080    280   -190    210       N  
ATOM   1564  CA  ASN B 345     -16.346   5.763 -28.143  1.00 15.02           C  
ANISOU 1564  CA  ASN B 345     1790   1970   1950    230   -140    190       C  
ATOM   1565  C   ASN B 345     -16.339   4.946 -26.842  1.00 14.54           C  
ANISOU 1565  C   ASN B 345     1730   1910   1890    240    -70    120       C  
ATOM   1566  O   ASN B 345     -16.199   3.711 -26.934  1.00 14.11           O  
ANISOU 1566  O   ASN B 345     1650   1910   1800    190    -40    100       O  
ATOM   1567  CB  ASN B 345     -15.166   5.375 -29.042  1.00 14.66           C  
ANISOU 1567  CB  ASN B 345     1750   1960   1860    150   -150    230       C  
ATOM   1568  CG  ASN B 345     -15.336   5.860 -30.467  1.00 15.43           C  
ANISOU 1568  CG  ASN B 345     1830   2100   1940    150   -210    300       C  
ATOM   1569  OD1 ASN B 345     -16.397   5.655 -31.062  1.00 15.62           O  
ANISOU 1569  OD1 ASN B 345     1800   2170   1960    170   -220    300       O  
ATOM   1570  ND2 ASN B 345     -14.288   6.443 -31.038  1.00 15.39           N  
ANISOU 1570  ND2 ASN B 345     1850   2080   1920    110   -230    370       N  
ATOM   1571  N   PHE B 346     -16.517   5.605 -25.690  1.00 14.68           N  
ANISOU 1571  N   PHE B 346     1790   1860   1930    300    -60     80       N  
ATOM   1572  CA  PHE B 346     -16.506   4.919 -24.371  1.00 14.57           C  
ANISOU 1572  CA  PHE B 346     1790   1850   1900    310     10     20       C  
ATOM   1573  C   PHE B 346     -17.436   3.699 -24.371  1.00 14.67           C  
ANISOU 1573  C   PHE B 346     1720   1950   1900    300     60     10       C  
ATOM   1574  O   PHE B 346     -16.999   2.635 -23.925  1.00 13.40           O  
ANISOU 1574  O   PHE B 346     1560   1810   1720    260    100    -10       O  
ATOM   1575  CB  PHE B 346     -16.894   5.878 -23.241  1.00 15.07           C  
ANISOU 1575  CB  PHE B 346     1910   1850   1970    410     10    -20       C  
ATOM   1576  CG  PHE B 346     -16.934   5.225 -21.882  1.00 15.00           C  
ANISOU 1576  CG  PHE B 346     1920   1850   1930    440     80    -70       C  
ATOM   1577  CD1 PHE B 346     -15.770   5.017 -21.161  1.00 14.73           C  
ANISOU 1577  CD1 PHE B 346     1960   1780   1860    400     80   -100       C  
ATOM   1578  CD2 PHE B 346     -18.129   4.789 -21.332  1.00 15.41           C  
ANISOU 1578  CD2 PHE B 346     1900   1970   1980    500    150    -90       C  
ATOM   1579  CE1 PHE B 346     -15.800   4.398 -19.916  1.00 14.81           C  
ANISOU 1579  CE1 PHE B 346     1990   1810   1830    420    140   -140       C  
ATOM   1580  CE2 PHE B 346     -18.159   4.178 -20.086  1.00 15.57           C  
ANISOU 1580  CE2 PHE B 346     1940   2020   1960    520    230   -120       C  
ATOM   1581  CZ  PHE B 346     -16.996   3.987 -19.376  1.00 15.06           C  
ANISOU 1581  CZ  PHE B 346     1960   1910   1850    480    220   -150       C  
ATOM   1582  N   LYS B 347     -18.670   3.857 -24.862  1.00 15.83           N  
ANISOU 1582  N   LYS B 347     1790   2140   2080    340     60     30       N  
ATOM   1583  CA  LYS B 347     -19.666   2.746 -24.872  1.00 16.82           C  
ANISOU 1583  CA  LYS B 347     1820   2340   2220    330    100     30       C  
ATOM   1584  C   LYS B 347     -19.165   1.624 -25.790  1.00 15.91           C  
ANISOU 1584  C   LYS B 347     1690   2260   2090    230     70     40       C  
ATOM   1585  O   LYS B 347     -19.324   0.449 -25.396  1.00 15.48           O  
ANISOU 1585  O   LYS B 347     1610   2240   2030    190    100     30       O  
ATOM   1586  CB  LYS B 347     -21.057   3.301 -25.200  1.00 18.85           C  
ANISOU 1586  CB  LYS B 347     2000   2630   2530    390     80     60       C  
ATOM   1587  CG  LYS B 347     -21.618   4.211 -24.105  1.00 20.83           C  
ANISOU 1587  CG  LYS B 347     2260   2860   2800    510    130     40       C  
ATOM   1588  CD  LYS B 347     -22.787   5.079 -24.504  1.00 22.98           C  
ANISOU 1588  CD  LYS B 347     2470   3140   3120    590    100     60       C  
ATOM   1589  CE  LYS B 347     -24.011   4.309 -24.927  1.00 25.02           C  
ANISOU 1589  CE  LYS B 347     2590   3490   3420    580    120    100       C  
ATOM   1590  NZ  LYS B 347     -25.101   5.224 -25.345  1.00 26.96           N  
ANISOU 1590  NZ  LYS B 347     2770   3750   3730    670     90    130       N  
ATOM   1591  N   ASP B 348     -18.522   1.960 -26.915  1.00 15.36           N  
ANISOU 1591  N   ASP B 348     1650   2190   2000    200     10     60       N  
ATOM   1592  CA  ASP B 348     -18.005   0.895 -27.822  1.00 15.09           C  
ANISOU 1592  CA  ASP B 348     1620   2190   1920    130    -10     60       C  
ATOM   1593  C   ASP B 348     -16.787   0.223 -27.184  1.00 14.13           C  
ANISOU 1593  C   ASP B 348     1550   2050   1770     90     30     30       C  
ATOM   1594  O   ASP B 348     -16.646  -1.000 -27.355  1.00 13.55           O  
ANISOU 1594  O   ASP B 348     1460   2000   1680     50     30     10       O  
ATOM   1595  CB  ASP B 348     -17.677   1.421 -29.223  1.00 15.81           C  
ANISOU 1595  CB  ASP B 348     1720   2300   1980    120    -70    100       C  
ATOM   1596  CG  ASP B 348     -18.910   1.719 -30.062  1.00 17.17           C  
ANISOU 1596  CG  ASP B 348     1830   2510   2180    140   -130    130       C  
ATOM   1597  OD1 ASP B 348     -20.006   1.343 -29.632  1.00 17.35           O  
ANISOU 1597  OD1 ASP B 348     1790   2550   2250    160   -110    110       O  
ATOM   1598  OD2 ASP B 348     -18.755   2.314 -31.150  1.00 19.31           O  
ANISOU 1598  OD2 ASP B 348     2120   2800   2420    150   -180    170       O  
ATOM   1599  N   GLN B 349     -15.941   0.995 -26.492  1.00 13.75           N  
ANISOU 1599  N   GLN B 349     1560   1950   1710    110     40     30       N  
ATOM   1600  CA  GLN B 349     -14.726   0.430 -25.838  1.00 13.16           C  
ANISOU 1600  CA  GLN B 349     1540   1850   1610     70     70     10       C  
ATOM   1601  C   GLN B 349     -15.154  -0.588 -24.771  1.00 13.20           C  
ANISOU 1601  C   GLN B 349     1530   1860   1630     70    120    -20       C  
ATOM   1602  O   GLN B 349     -14.543  -1.677 -24.713  1.00 13.39           O  
ANISOU 1602  O   GLN B 349     1560   1900   1630     30    130    -40       O  
ATOM   1603  CB  GLN B 349     -13.887   1.574 -25.272  1.00 13.25           C  
ANISOU 1603  CB  GLN B 349     1610   1790   1630     90     50     20       C  
ATOM   1604  CG  GLN B 349     -13.343   2.494 -26.360  1.00 13.49           C  
ANISOU 1604  CG  GLN B 349     1660   1820   1650     80      0     80       C  
ATOM   1605  CD  GLN B 349     -12.851   3.820 -25.835  1.00 13.76           C  
ANISOU 1605  CD  GLN B 349     1750   1760   1720    100    -40    100       C  
ATOM   1606  OE1 GLN B 349     -12.952   4.114 -24.644  1.00 14.12           O  
ANISOU 1606  OE1 GLN B 349     1830   1750   1780    130    -30     60       O  
ATOM   1607  NE2 GLN B 349     -12.344   4.650 -26.737  1.00 13.71           N  
ANISOU 1607  NE2 GLN B 349     1750   1740   1720     80    -90    170       N  
ATOM   1608  N   VAL B 350     -16.171  -0.252 -23.975  1.00 13.09           N  
ANISOU 1608  N   VAL B 350     1490   1850   1640    120    150    -30       N  
ATOM   1609  CA  VAL B 350     -16.666  -1.179 -22.914  1.00 13.32           C  
ANISOU 1609  CA  VAL B 350     1490   1900   1670    120    210    -40       C  
ATOM   1610  C   VAL B 350     -17.175  -2.473 -23.571  1.00 13.18           C  
ANISOU 1610  C   VAL B 350     1400   1930   1680     60    190    -30       C  
ATOM   1611  O   VAL B 350     -16.816  -3.562 -23.076  1.00 12.77           O  
ANISOU 1611  O   VAL B 350     1360   1870   1620     20    220    -40       O  
ATOM   1612  CB  VAL B 350     -17.741  -0.505 -22.040  1.00 14.02           C  
ANISOU 1612  CB  VAL B 350     1550   2000   1780    200    250    -40       C  
ATOM   1613  CG1 VAL B 350     -18.462  -1.503 -21.143  1.00 14.39           C  
ANISOU 1613  CG1 VAL B 350     1540   2090   1830    190    320    -30       C  
ATOM   1614  CG2 VAL B 350     -17.141   0.627 -21.214  1.00 14.10           C  
ANISOU 1614  CG2 VAL B 350     1650   1950   1760    260    250    -60       C  
ATOM   1615  N   ILE B 351     -17.976  -2.355 -24.635  1.00 13.63           N  
ANISOU 1615  N   ILE B 351     1410   2020   1760     60    150    -20       N  
ATOM   1616  CA  ILE B 351     -18.519  -3.543 -25.359  1.00 14.11           C  
ANISOU 1616  CA  ILE B 351     1410   2110   1850      0    120    -20       C  
ATOM   1617  C   ILE B 351     -17.352  -4.368 -25.919  1.00 13.55           C  
ANISOU 1617  C   ILE B 351     1400   2020   1730    -50     90    -50       C  
ATOM   1618  O   ILE B 351     -17.332  -5.584 -25.701  1.00 13.55           O  
ANISOU 1618  O   ILE B 351     1390   2010   1750    -90     80    -60       O  
ATOM   1619  CB  ILE B 351     -19.514  -3.096 -26.448  1.00 15.07           C  
ANISOU 1619  CB  ILE B 351     1470   2260   1990     10     60     10       C  
ATOM   1620  CG1 ILE B 351     -20.756  -2.460 -25.816  1.00 16.06           C  
ANISOU 1620  CG1 ILE B 351     1520   2410   2170     70     90     40       C  
ATOM   1621  CG2 ILE B 351     -19.897  -4.253 -27.367  1.00 15.49           C  
ANISOU 1621  CG2 ILE B 351     1490   2340   2060    -50    -10      0       C  
ATOM   1622  CD1 ILE B 351     -21.733  -1.880 -26.818  1.00 16.79           C  
ANISOU 1622  CD1 ILE B 351     1550   2530   2290     90     30     70       C  
ATOM   1623  N   LEU B 352     -16.400  -3.717 -26.583  1.00 13.50           N  
ANISOU 1623  N   LEU B 352     1440   2010   1680    -30     70    -50       N  
ATOM   1624  CA  LEU B 352     -15.244  -4.431 -27.175  1.00 13.44           C  
ANISOU 1624  CA  LEU B 352     1480   2000   1620    -60     50    -80       C  
ATOM   1625  C   LEU B 352     -14.472  -5.181 -26.074  1.00 13.41           C  
ANISOU 1625  C   LEU B 352     1510   1960   1620    -80     90   -100       C  
ATOM   1626  O   LEU B 352     -14.251  -6.397 -26.233  1.00 12.68           O  
ANISOU 1626  O   LEU B 352     1420   1860   1530   -110     80   -130       O  
ATOM   1627  CB  LEU B 352     -14.361  -3.416 -27.910  1.00 13.55           C  
ANISOU 1627  CB  LEU B 352     1530   2020   1590    -40     40    -60       C  
ATOM   1628  CG  LEU B 352     -13.127  -3.999 -28.598  1.00 13.37           C  
ANISOU 1628  CG  LEU B 352     1550   2020   1510    -60     30    -70       C  
ATOM   1629  CD1 LEU B 352     -13.516  -5.090 -29.582  1.00 13.98           C  
ANISOU 1629  CD1 LEU B 352     1620   2130   1560    -70    -10   -110       C  
ATOM   1630  CD2 LEU B 352     -12.345  -2.911 -29.297  1.00 13.81           C  
ANISOU 1630  CD2 LEU B 352     1620   2100   1530    -40     20    -30       C  
ATOM   1631  N   LEU B 353     -14.109  -4.495 -24.986  1.00 13.63           N  
ANISOU 1631  N   LEU B 353     1570   1960   1650    -60    130    -90       N  
ATOM   1632  CA  LEU B 353     -13.345  -5.159 -23.894  1.00 14.13           C  
ANISOU 1632  CA  LEU B 353     1660   1990   1710    -80    170   -100       C  
ATOM   1633  C   LEU B 353     -14.169  -6.321 -23.306  1.00 14.71           C  
ANISOU 1633  C   LEU B 353     1700   2060   1820   -110    180   -100       C  
ATOM   1634  O   LEU B 353     -13.583  -7.402 -23.115  1.00 14.97           O  
ANISOU 1634  O   LEU B 353     1750   2080   1860   -140    180   -110       O  
ATOM   1635  CB  LEU B 353     -12.951  -4.112 -22.845  1.00 14.16           C  
ANISOU 1635  CB  LEU B 353     1710   1960   1710    -50    190    -90       C  
ATOM   1636  CG  LEU B 353     -11.910  -3.090 -23.309  1.00 13.81           C  
ANISOU 1636  CG  LEU B 353     1710   1900   1640    -40    170    -80       C  
ATOM   1637  CD1 LEU B 353     -11.784  -1.955 -22.314  1.00 14.02           C  
ANISOU 1637  CD1 LEU B 353     1780   1880   1670      0    170    -70       C  
ATOM   1638  CD2 LEU B 353     -10.554  -3.745 -23.540  1.00 13.35           C  
ANISOU 1638  CD2 LEU B 353     1670   1840   1560    -70    160    -80       C  
ATOM   1639  N   ASN B 354     -15.463  -6.117 -23.043  1.00 15.91           N  
ANISOU 1639  N   ASN B 354     1790   2240   2010    -90    200    -70       N  
ATOM   1640  CA  ASN B 354     -16.347  -7.191 -22.502  1.00 17.11           C  
ANISOU 1640  CA  ASN B 354     1890   2400   2210   -130    210    -50       C  
ATOM   1641  C   ASN B 354     -16.385  -8.405 -23.440  1.00 18.75           C  
ANISOU 1641  C   ASN B 354     2080   2600   2440   -190    150    -70       C  
ATOM   1642  O   ASN B 354     -16.582  -9.531 -22.948  1.00 19.10           O  
ANISOU 1642  O   ASN B 354     2110   2620   2530   -230    140    -60       O  
ATOM   1643  CB  ASN B 354     -17.796  -6.730 -22.314  1.00 17.86           C  
ANISOU 1643  CB  ASN B 354     1900   2540   2340   -110    230    -10       C  
ATOM   1644  CG  ASN B 354     -18.015  -5.913 -21.060  1.00 18.27           C  
ANISOU 1644  CG  ASN B 354     1960   2610   2370    -40    310     10       C  
ATOM   1645  OD1 ASN B 354     -17.154  -5.879 -20.188  1.00 17.53           O  
ANISOU 1645  OD1 ASN B 354     1940   2490   2240    -30    340    -10       O  
ATOM   1646  ND2 ASN B 354     -19.188  -5.302 -20.942  1.00 18.31           N  
ANISOU 1646  ND2 ASN B 354     1900   2660   2400      0    340     40       N  
ATOM   1647  N   LYS B 355     -16.222  -8.172 -24.743  1.00 20.22           N  
ANISOU 1647  N   LYS B 355     2280   2790   2610   -180     90   -100       N  
ATOM   1648  CA  LYS B 355     -16.274  -9.264 -25.746  1.00 20.35           C  
ANISOU 1648  CA  LYS B 355     2300   2800   2640   -220     20   -140       C  
ATOM   1649  C   LYS B 355     -15.017 -10.146 -25.666  1.00 18.65           C  
ANISOU 1649  C   LYS B 355     2150   2540   2390   -230     10   -180       C  
ATOM   1650  O   LYS B 355     -15.113 -11.313 -26.086  1.00 17.93           O  
ANISOU 1650  O   LYS B 355     2070   2420   2330   -260    -50   -210       O  
ATOM   1651  CB  LYS B 355     -16.434  -8.642 -27.136  1.00 22.64           C  
ANISOU 1651  CB  LYS B 355     2590   3120   2890   -190    -40   -150       C  
ATOM   1652  CG  LYS B 355     -16.661  -9.629 -28.270  1.00 25.80           C  
ANISOU 1652  CG  LYS B 355     3000   3520   3290   -220   -130   -200       C  
ATOM   1653  CD  LYS B 355     -16.907  -8.962 -29.608  1.00 27.71           C  
ANISOU 1653  CD  LYS B 355     3240   3810   3480   -190   -180   -210       C  
ATOM   1654  CE  LYS B 355     -17.235  -9.962 -30.697  1.00 29.76           C  
ANISOU 1654  CE  LYS B 355     3520   4060   3730   -210   -280   -270       C  
ATOM   1655  NZ  LYS B 355     -17.467  -9.305 -32.006  1.00 31.38           N  
ANISOU 1655  NZ  LYS B 355     3730   4320   3870   -180   -330   -270       N  
ATOM   1656  N   HIS B 356     -13.910  -9.647 -25.093  1.00 16.76           N  
ANISOU 1656  N   HIS B 356     1960   2300   2110   -200     60   -180       N  
ATOM   1657  CA  HIS B 356     -12.648 -10.446 -25.067  1.00 16.07           C  
ANISOU 1657  CA  HIS B 356     1930   2180   2000   -200     60   -210       C  
ATOM   1658  C   HIS B 356     -12.247 -10.911 -23.659  1.00 14.94           C  
ANISOU 1658  C   HIS B 356     1800   2000   1880   -210    100   -190       C  
ATOM   1659  O   HIS B 356     -11.528 -11.927 -23.567  1.00 14.50           O  
ANISOU 1659  O   HIS B 356     1780   1900   1830   -220     80   -210       O  
ATOM   1660  CB  HIS B 356     -11.515  -9.653 -25.739  1.00 15.78           C  
ANISOU 1660  CB  HIS B 356     1920   2170   1900   -150     70   -220       C  
ATOM   1661  CG  HIS B 356     -11.789  -9.346 -27.170  1.00 16.27           C  
ANISOU 1661  CG  HIS B 356     1980   2280   1920   -130     30   -240       C  
ATOM   1662  ND1 HIS B 356     -11.548 -10.260 -28.175  1.00 17.07           N  
ANISOU 1662  ND1 HIS B 356     2100   2390   1990   -120    -20   -290       N  
ATOM   1663  CD2 HIS B 356     -12.300  -8.246 -27.771  1.00 16.52           C  
ANISOU 1663  CD2 HIS B 356     1990   2360   1930   -120     20   -210       C  
ATOM   1664  CE1 HIS B 356     -11.898  -9.733 -29.336  1.00 17.39           C  
ANISOU 1664  CE1 HIS B 356     2140   2480   1990   -100    -50   -300       C  
ATOM   1665  NE2 HIS B 356     -12.363  -8.501 -29.114  1.00 16.71           N  
ANISOU 1665  NE2 HIS B 356     2020   2420   1910   -100    -30   -240       N  
ATOM   1666  N   ILE B 357     -12.688 -10.219 -22.611  1.00 14.53           N  
ANISOU 1666  N   ILE B 357     1730   1950   1840   -210    150   -150       N  
ATOM   1667  CA  ILE B 357     -12.316 -10.615 -21.219  1.00 14.50           C  
ANISOU 1667  CA  ILE B 357     1750   1920   1840   -220    190   -120       C  
ATOM   1668  C   ILE B 357     -13.026 -11.928 -20.852  1.00 14.65           C  
ANISOU 1668  C   ILE B 357     1740   1910   1920   -270    170   -100       C  
ATOM   1669  O   ILE B 357     -14.282 -11.935 -20.787  1.00 14.78           O  
ANISOU 1669  O   ILE B 357     1690   1950   1970   -290    180    -60       O  
ATOM   1670  CB  ILE B 357     -12.602  -9.475 -20.219  1.00 14.53           C  
ANISOU 1670  CB  ILE B 357     1750   1950   1820   -190    240    -90       C  
ATOM   1671  CG1 ILE B 357     -11.724  -8.256 -20.527  1.00 14.30           C  
ANISOU 1671  CG1 ILE B 357     1770   1920   1740   -150    240   -110       C  
ATOM   1672  CG2 ILE B 357     -12.404  -9.960 -18.792  1.00 14.87           C  
ANISOU 1672  CG2 ILE B 357     1820   1980   1850   -200    280    -60       C  
ATOM   1673  CD1 ILE B 357     -11.990  -7.049 -19.664  1.00 14.05           C  
ANISOU 1673  CD1 ILE B 357     1750   1900   1690   -110    280    -90       C  
ATOM   1674  N   ASP B 358     -12.230 -12.986 -20.634  1.00 14.16           N  
ANISOU 1674  N   ASP B 358     1710   1800   1870   -290    150   -110       N  
ATOM   1675  CA  ASP B 358     -12.715 -14.347 -20.269  1.00 14.80           C  
ANISOU 1675  CA  ASP B 358     1780   1830   2010   -340    110    -80       C  
ATOM   1676  C   ASP B 358     -13.626 -14.920 -21.359  1.00 14.99           C  
ANISOU 1676  C   ASP B 358     1760   1840   2090   -380     40   -100       C  
ATOM   1677  O   ASP B 358     -14.479 -15.769 -21.018  1.00 15.11           O  
ANISOU 1677  O   ASP B 358     1740   1830   2180   -440     20    -50       O  
ATOM   1678  CB  ASP B 358     -13.464 -14.347 -18.936  1.00 15.54           C  
ANISOU 1678  CB  ASP B 358     1830   1950   2120   -370    170      0       C  
ATOM   1679  CG  ASP B 358     -12.600 -14.093 -17.716  1.00 15.87           C  
ANISOU 1679  CG  ASP B 358     1930   1990   2110   -340    220     20       C  
ATOM   1680  OD1 ASP B 358     -11.371 -14.350 -17.779  1.00 15.45           O  
ANISOU 1680  OD1 ASP B 358     1930   1900   2040   -330    200    -20       O  
ATOM   1681  OD2 ASP B 358     -13.163 -13.636 -16.718  1.00 16.87           O  
ANISOU 1681  OD2 ASP B 358     2030   2160   2220   -330    290     70       O  
ATOM   1682  N   ALA B 359     -13.450 -14.486 -22.609  1.00 14.75           N  
ANISOU 1682  N   ALA B 359     1750   1830   2030   -350     10   -160       N  
ATOM   1683  CA  ALA B 359     -14.297 -14.994 -23.714  1.00 15.71           C  
ANISOU 1683  CA  ALA B 359     1840   1940   2190   -370    -80   -190       C  
ATOM   1684  C   ALA B 359     -14.108 -16.509 -23.875  1.00 16.39           C  
ANISOU 1684  C   ALA B 359     1960   1940   2330   -410   -160   -220       C  
ATOM   1685  O   ALA B 359     -15.074 -17.173 -24.306  1.00 17.74           O  
ANISOU 1685  O   ALA B 359     2100   2070   2570   -460   -240   -220       O  
ATOM   1686  CB  ALA B 359     -13.970 -14.265 -24.992  1.00 15.48           C  
ANISOU 1686  CB  ALA B 359     1830   1960   2090   -320   -100   -250       C  
ATOM   1687  N   TYR B 360     -12.934 -17.036 -23.500  1.00 16.49           N  
ANISOU 1687  N   TYR B 360     2030   1910   2320   -380   -150   -250       N  
ATOM   1688  CA  TYR B 360     -12.639 -18.489 -23.642  1.00 18.15           C  
ANISOU 1688  CA  TYR B 360     2290   2020   2590   -400   -230   -290       C  
ATOM   1689  C   TYR B 360     -13.670 -19.343 -22.894  1.00 19.90           C  
ANISOU 1689  C   TYR B 360     2460   2180   2920   -490   -270   -210       C  
ATOM   1690  O   TYR B 360     -13.939 -20.471 -23.333  1.00 21.20           O  
ANISOU 1690  O   TYR B 360     2650   2260   3150   -530   -370   -240       O  
ATOM   1691  CB  TYR B 360     -11.251 -18.844 -23.097  1.00 17.47           C  
ANISOU 1691  CB  TYR B 360     2260   1900   2470   -360   -200   -300       C  
ATOM   1692  CG  TYR B 360     -11.157 -18.786 -21.596  1.00 17.20           C  
ANISOU 1692  CG  TYR B 360     2210   1870   2460   -390   -140   -220       C  
ATOM   1693  CD1 TYR B 360     -11.503 -19.883 -20.821  1.00 18.14           C  
ANISOU 1693  CD1 TYR B 360     2330   1910   2660   -450   -170   -160       C  
ATOM   1694  CD2 TYR B 360     -10.764 -17.629 -20.946  1.00 16.49           C  
ANISOU 1694  CD2 TYR B 360     2110   1850   2310   -360    -50   -180       C  
ATOM   1695  CE1 TYR B 360     -11.443 -19.838 -19.437  1.00 18.10           C  
ANISOU 1695  CE1 TYR B 360     2310   1910   2660   -480   -110    -70       C  
ATOM   1696  CE2 TYR B 360     -10.686 -17.569 -19.565  1.00 16.49           C  
ANISOU 1696  CE2 TYR B 360     2110   1850   2310   -380     10   -110       C  
ATOM   1697  CZ  TYR B 360     -11.026 -18.677 -18.808  1.00 17.50           C  
ANISOU 1697  CZ  TYR B 360     2230   1920   2500   -440    -20    -50       C  
ATOM   1698  OH  TYR B 360     -10.955 -18.615 -17.449  1.00 18.09           O  
ANISOU 1698  OH  TYR B 360     2310   2000   2560   -450     30     30       O  
ATOM   1699  N   LYS B 361     -14.232 -18.820 -21.802  1.00 21.30           N  
ANISOU 1699  N   LYS B 361     2580   2410   3100   -530   -190   -110       N  
ATOM   1700  CA  LYS B 361     -15.215 -19.591 -20.989  1.00 23.19           C  
ANISOU 1700  CA  LYS B 361     2760   2610   3440   -620   -210    -10       C  
ATOM   1701  C   LYS B 361     -16.397 -20.070 -21.839  1.00 24.84           C  
ANISOU 1701  C   LYS B 361     2910   2790   3740   -680   -310    -10       C  
ATOM   1702  O   LYS B 361     -17.014 -21.079 -21.453  1.00 25.21           O  
ANISOU 1702  O   LYS B 361     2920   2770   3890   -760   -370     60       O  
ATOM   1703  CB  LYS B 361     -15.706 -18.757 -19.804  1.00 23.46           C  
ANISOU 1703  CB  LYS B 361     2730   2730   3450   -620    -90     90       C  
ATOM   1704  CG  LYS B 361     -14.677 -18.539 -18.707  1.00 23.60           C  
ANISOU 1704  CG  LYS B 361     2800   2760   3400   -580    -10    110       C  
ATOM   1705  CD  LYS B 361     -15.231 -17.771 -17.544  1.00 24.83           C  
ANISOU 1705  CD  LYS B 361     2910   3000   3520   -570    100    190       C  
ATOM   1706  CE  LYS B 361     -14.224 -17.571 -16.434  1.00 25.77           C  
ANISOU 1706  CE  LYS B 361     3090   3130   3570   -530    160    210       C  
ATOM   1707  NZ  LYS B 361     -14.803 -16.764 -15.334  1.00 26.84           N  
ANISOU 1707  NZ  LYS B 361     3190   3360   3650   -510    260    280       N  
ATOM   1708  N   THR B 362     -16.670 -19.405 -22.964  1.00 26.18           N  
ANISOU 1708  N   THR B 362     3080   3000   3870   -640   -330    -70       N  
ATOM   1709  CA  THR B 362     -17.816 -19.789 -23.832  1.00 28.42           C  
ANISOU 1709  CA  THR B 362     3310   3260   4230   -700   -440    -80       C  
ATOM   1710  C   THR B 362     -17.362 -20.507 -25.107  1.00 29.46           C  
ANISOU 1710  C   THR B 362     3530   3310   4350   -680   -570   -200       C  
ATOM   1711  O   THR B 362     -18.256 -20.857 -25.901  1.00 31.05           O  
ANISOU 1711  O   THR B 362     3700   3480   4610   -720   -680   -220       O  
ATOM   1712  CB  THR B 362     -18.623 -18.560 -24.266  1.00 28.57           C  
ANISOU 1712  CB  THR B 362     3260   3390   4210   -680   -400    -60       C  
ATOM   1713  OG1 THR B 362     -17.767 -17.746 -25.067  1.00 28.47           O  
ANISOU 1713  OG1 THR B 362     3310   3420   4090   -590   -380   -150       O  
ATOM   1714  CG2 THR B 362     -19.163 -17.765 -23.101  1.00 28.86           C  
ANISOU 1714  CG2 THR B 362     3210   3510   4250   -680   -280     50       C  
ATOM   1715  N   PHE B 363     -16.058 -20.728 -25.314  1.00 29.74           N  
ANISOU 1715  N   PHE B 363     3670   3320   4310   -600   -560   -290       N  
ATOM   1716  CA  PHE B 363     -15.673 -21.408 -26.580  1.00 31.43           C  
ANISOU 1716  CA  PHE B 363     3970   3470   4500   -560   -680   -410       C  
ATOM   1717  C   PHE B 363     -16.338 -22.780 -26.646  1.00 34.60           C  
ANISOU 1717  C   PHE B 363     4380   3740   5030   -650   -830   -410       C  
ATOM   1718  O   PHE B 363     -16.340 -23.519 -25.664  1.00 34.58           O  
ANISOU 1718  O   PHE B 363     4360   3660   5120   -710   -830   -340       O  
ATOM   1719  CB  PHE B 363     -14.158 -21.532 -26.779  1.00 30.15           C  
ANISOU 1719  CB  PHE B 363     3900   3300   4250   -460   -650   -500       C  
ATOM   1720  CG  PHE B 363     -13.395 -20.233 -26.786  1.00 27.49           C  
ANISOU 1720  CG  PHE B 363     3560   3090   3800   -390   -520   -500       C  
ATOM   1721  CD1 PHE B 363     -13.984 -19.059 -27.236  1.00 26.53           C  
ANISOU 1721  CD1 PHE B 363     3390   3070   3630   -380   -480   -480       C  
ATOM   1722  CD2 PHE B 363     -12.029 -20.226 -26.545  1.00 26.48           C  
ANISOU 1722  CD2 PHE B 363     3490   2970   3610   -320   -460   -530       C  
ATOM   1723  CE1 PHE B 363     -13.265 -17.873 -27.270  1.00 25.77           C  
ANISOU 1723  CE1 PHE B 363     3290   3060   3430   -320   -380   -470       C  
ATOM   1724  CE2 PHE B 363     -11.299 -19.049 -26.619  1.00 25.35           C  
ANISOU 1724  CE2 PHE B 363     3330   2930   3370   -250   -360   -520       C  
ATOM   1725  CZ  PHE B 363     -11.919 -17.870 -26.973  1.00 24.94           C  
ANISOU 1725  CZ  PHE B 363     3230   2970   3280   -260   -320   -490       C  
ATOM   1726  N   PRO B 364     -16.938 -23.150 -27.802  1.00 39.37           N  
ANISOU 1726  N   PRO B 364     5010   4300   5650   -660   -970   -490       N  
ATOM   1727  CA  PRO B 364     -17.596 -24.448 -27.955  1.00 42.12           C  
ANISOU 1727  CA  PRO B 364     5370   4500   6130   -740  -1140   -490       C  
ATOM   1728  C   PRO B 364     -16.635 -25.623 -27.723  1.00 44.70           C  
ANISOU 1728  C   PRO B 364     5800   4700   6490   -720  -1190   -550       C  
ATOM   1729  O   PRO B 364     -15.411 -25.464 -27.685  1.00 44.41           O  
ANISOU 1729  O   PRO B 364     5830   4690   6350   -610  -1110   -610       O  
ATOM   1730  CB  PRO B 364     -18.094 -24.467 -29.409  1.00 42.92           C  
ANISOU 1730  CB  PRO B 364     5510   4600   6200   -720  -1270   -600       C  
ATOM   1731  CG  PRO B 364     -18.131 -23.009 -29.825  1.00 42.31           C  
ANISOU 1731  CG  PRO B 364     5390   4680   6000   -660  -1160   -590       C  
ATOM   1732  CD  PRO B 364     -17.045 -22.325 -29.017  1.00 40.92           C  
ANISOU 1732  CD  PRO B 364     5220   4580   5740   -590   -980   -560       C  
ATOM   1733  OXT PRO B 364     -17.086 -26.757 -27.571  1.00 48.23           O  
ANISOU 1733  OXT PRO B 364     6260   5000   7060   -800  -1330   -530       O  
TER    1734      PRO B 364                                                      
ATOM   1735  N   LYS C 257       3.261  -1.258 -49.323  1.00 42.67           N  
ANISOU 1735  N   LYS C 257     5600   4140   6470     10  -1730   -400       N  
ATOM   1736  CA  LYS C 257       2.416  -2.491 -49.183  1.00 39.97           C  
ANISOU 1736  CA  LYS C 257     5310   4140   5740     80  -1310   -450       C  
ATOM   1737  C   LYS C 257       2.782  -3.500 -50.269  1.00 33.45           C  
ANISOU 1737  C   LYS C 257     4290   3460   4960   -140   -990   -220       C  
ATOM   1738  O   LYS C 257       2.503  -3.264 -51.439  1.00 32.60           O  
ANISOU 1738  O   LYS C 257     4080   3390   4920   -260   -860    -80       O  
ATOM   1739  CB  LYS C 257       0.929  -2.145 -49.317  1.00 42.94           C  
ANISOU 1739  CB  LYS C 257     5760   4660   5900    230  -1190   -550       C  
ATOM   1740  CG  LYS C 257      -0.029  -3.332 -49.233  1.00 42.95           C  
ANISOU 1740  CG  LYS C 257     5740   4970   5600    280   -810   -510       C  
ATOM   1741  CD  LYS C 257      -0.146  -3.963 -47.863  1.00 44.45           C  
ANISOU 1741  CD  LYS C 257     6050   5340   5500    480   -770   -600       C  
ATOM   1742  CE  LYS C 257      -0.819  -3.050 -46.860  1.00 47.61           C  
ANISOU 1742  CE  LYS C 257     6620   5800   5670    840   -920   -850       C  
ATOM   1743  NZ  LYS C 257      -0.978  -3.703 -45.541  1.00 50.26           N  
ANISOU 1743  NZ  LYS C 257     7070   6400   5630   1080   -820   -880       N  
ATOM   1744  N   PRO C 258       3.427  -4.643 -49.936  1.00 29.95           N  
ANISOU 1744  N   PRO C 258     3810   3090   4470   -160   -870   -180       N  
ATOM   1745  CA  PRO C 258       3.761  -5.650 -50.943  1.00 25.75           C  
ANISOU 1745  CA  PRO C 258     3130   2690   3970   -290   -600    -40       C  
ATOM   1746  C   PRO C 258       2.510  -6.028 -51.751  1.00 22.12           C  
ANISOU 1746  C   PRO C 258     2690   2390   3310   -280   -380    -40       C  
ATOM   1747  O   PRO C 258       1.455  -6.232 -51.164  1.00 20.40           O  
ANISOU 1747  O   PRO C 258     2580   2250   2920   -180   -350   -120       O  
ATOM   1748  CB  PRO C 258       4.291  -6.827 -50.119  1.00 26.22           C  
ANISOU 1748  CB  PRO C 258     3210   2770   3980   -250   -600    -80       C  
ATOM   1749  CG  PRO C 258       4.835  -6.173 -48.861  1.00 29.15           C  
ANISOU 1749  CG  PRO C 258     3690   2970   4410   -170   -920   -170       C  
ATOM   1750  CD  PRO C 258       3.906  -5.008 -48.595  1.00 30.27           C  
ANISOU 1750  CD  PRO C 258     3980   3080   4440    -50  -1050   -300       C  
ATOM   1751  N   ARG C 259       2.666  -6.104 -53.071  1.00 20.07           N  
ANISOU 1751  N   ARG C 259     2330   2200   3090   -360   -230     70       N  
ATOM   1752  CA  ARG C 259       1.566  -6.428 -54.019  1.00 18.57           C  
ANISOU 1752  CA  ARG C 259     2190   2120   2750   -360    -90     70       C  
ATOM   1753  C   ARG C 259       0.771  -7.664 -53.558  1.00 15.81           C  
ANISOU 1753  C   ARG C 259     1900   1830   2280   -300    -40    -10       C  
ATOM   1754  O   ARG C 259      -0.466  -7.623 -53.651  1.00 14.63           O  
ANISOU 1754  O   ARG C 259     1790   1700   2060   -280    -30    -10       O  
ATOM   1755  CB  ARG C 259       2.176  -6.597 -55.416  1.00 20.50           C  
ANISOU 1755  CB  ARG C 259     2340   2470   2970   -390     50    180       C  
ATOM   1756  CG  ARG C 259       1.182  -6.851 -56.540  1.00 21.70           C  
ANISOU 1756  CG  ARG C 259     2580   2710   2950   -360    120    170       C  
ATOM   1757  CD  ARG C 259       1.871  -6.781 -57.893  1.00 24.42           C  
ANISOU 1757  CD  ARG C 259     2870   3230   3180   -340    270    300       C  
ATOM   1758  NE  ARG C 259       0.954  -6.963 -59.012  1.00 27.05           N  
ANISOU 1758  NE  ARG C 259     3340   3640   3300   -280    280    260       N  
ATOM   1759  CZ  ARG C 259       0.776  -8.090 -59.713  1.00 28.50           C  
ANISOU 1759  CZ  ARG C 259     3630   3900   3300   -130    300    110       C  
ATOM   1760  NH1 ARG C 259       1.478  -9.179 -59.444  1.00 31.56           N  
ANISOU 1760  NH1 ARG C 259     3980   4310   3700    -20    340    -20       N  
ATOM   1761  NH2 ARG C 259      -0.093  -8.113 -60.710  1.00 28.72           N  
ANISOU 1761  NH2 ARG C 259     3810   3950   3150    -80    240     80       N  
ATOM   1762  N   GLN C 260       1.438  -8.694 -53.030  1.00 14.23           N  
ANISOU 1762  N   GLN C 260     1670   1620   2110   -280    -50    -30       N  
ATOM   1763  CA  GLN C 260       0.716  -9.934 -52.624  1.00 13.23           C  
ANISOU 1763  CA  GLN C 260     1560   1510   1950   -270    -60    -30       C  
ATOM   1764  C   GLN C 260      -0.186  -9.721 -51.394  1.00 13.03           C  
ANISOU 1764  C   GLN C 260     1570   1550   1830   -220    -70     30       C  
ATOM   1765  O   GLN C 260      -1.047 -10.595 -51.165  1.00 13.10           O  
ANISOU 1765  O   GLN C 260     1530   1600   1840   -240    -60    140       O  
ATOM   1766  CB  GLN C 260       1.662 -11.114 -52.373  1.00 13.54           C  
ANISOU 1766  CB  GLN C 260     1560   1500   2080   -260   -110    -50       C  
ATOM   1767  CG  GLN C 260       2.666 -10.950 -51.237  1.00 13.48           C  
ANISOU 1767  CG  GLN C 260     1540   1450   2130   -260   -190    -40       C  
ATOM   1768  CD  GLN C 260       3.896 -10.141 -51.563  1.00 14.15           C  
ANISOU 1768  CD  GLN C 260     1550   1490   2340   -270   -200    -50       C  
ATOM   1769  OE1 GLN C 260       3.930  -9.368 -52.520  1.00 14.05           O  
ANISOU 1769  OE1 GLN C 260     1490   1520   2330   -290   -110    -20       O  
ATOM   1770  NE2 GLN C 260       4.926 -10.315 -50.746  1.00 13.96           N  
ANISOU 1770  NE2 GLN C 260     1490   1370   2440   -280   -320    -50       N  
ATOM   1771  N   LYS C 261      -0.038  -8.615 -50.654  1.00 13.31           N  
ANISOU 1771  N   LYS C 261     1670   1600   1800   -150   -110    -30       N  
ATOM   1772  CA  LYS C 261      -0.894  -8.388 -49.454  1.00 14.47           C  
ANISOU 1772  CA  LYS C 261     1860   1880   1760    -10    -90    -10       C  
ATOM   1773  C   LYS C 261      -1.940  -7.306 -49.749  1.00 15.13           C  
ANISOU 1773  C   LYS C 261     1950   2000   1790     80    -50    -70       C  
ATOM   1774  O   LYS C 261      -2.694  -6.955 -48.832  1.00 16.90           O  
ANISOU 1774  O   LYS C 261     2200   2380   1840    270    -10    -90       O  
ATOM   1775  CB  LYS C 261      -0.046  -8.012 -48.237  1.00 15.52           C  
ANISOU 1775  CB  LYS C 261     2110   2000   1790    110   -230   -100       C  
ATOM   1776  CG  LYS C 261       0.941  -9.086 -47.790  1.00 15.68           C  
ANISOU 1776  CG  LYS C 261     2120   1970   1870     30   -290    -40       C  
ATOM   1777  CD  LYS C 261       0.288 -10.414 -47.409  1.00 15.99           C  
ANISOU 1777  CD  LYS C 261     2090   2140   1850    -10   -200    170       C  
ATOM   1778  CE  LYS C 261       1.297 -11.451 -46.960  1.00 16.10           C  
ANISOU 1778  CE  LYS C 261     2090   2050   1970    -90   -330    230       C  
ATOM   1779  NZ  LYS C 261       0.654 -12.748 -46.658  1.00 16.91           N  
ANISOU 1779  NZ  LYS C 261     2100   2230   2090   -160   -300    490       N  
ATOM   1780  N   ARG C 262      -1.995  -6.820 -50.988  1.00 14.03           N  
ANISOU 1780  N   ARG C 262     1790   1750   1790    -20    -70    -90       N  
ATOM   1781  CA  ARG C 262      -2.986  -5.771 -51.326  1.00 14.87           C  
ANISOU 1781  CA  ARG C 262     1890   1850   1910     50    -90   -130       C  
ATOM   1782  C   ARG C 262      -4.407  -6.343 -51.309  1.00 14.81           C  
ANISOU 1782  C   ARG C 262     1780   1980   1870     90     40    -20       C  
ATOM   1783  O   ARG C 262      -4.587  -7.559 -51.557  1.00 14.32           O  
ANISOU 1783  O   ARG C 262     1640   1940   1860    -20    100    130       O  
ATOM   1784  CB  ARG C 262      -2.648  -5.133 -52.674  1.00 14.24           C  
ANISOU 1784  CB  ARG C 262     1810   1630   1970    -90   -170   -120       C  
ATOM   1785  CG  ARG C 262      -1.333  -4.376 -52.647  1.00 14.91           C  
ANISOU 1785  CG  ARG C 262     1920   1580   2170   -140   -320   -140       C  
ATOM   1786  CD  ARG C 262      -0.968  -3.826 -53.996  1.00 14.94           C  
ANISOU 1786  CD  ARG C 262     1870   1510   2290   -290   -350    -10       C  
ATOM   1787  NE  ARG C 262       0.351  -3.221 -53.955  1.00 15.94           N  
ANISOU 1787  NE  ARG C 262     1940   1520   2600   -370   -480     80       N  
ATOM   1788  CZ  ARG C 262       0.991  -2.758 -55.016  1.00 16.98           C  
ANISOU 1788  CZ  ARG C 262     1960   1640   2850   -510   -480    290       C  
ATOM   1789  NH1 ARG C 262       2.195  -2.235 -54.882  1.00 18.67           N  
ANISOU 1789  NH1 ARG C 262     2050   1740   3300   -590   -610    440       N  
ATOM   1790  NH2 ARG C 262       0.433  -2.832 -56.211  1.00 16.96           N  
ANISOU 1790  NH2 ARG C 262     1960   1740   2740   -560   -350    390       N  
ATOM   1791  N   THR C 263      -5.352  -5.460 -50.988  1.00 15.88           N  
ANISOU 1791  N   THR C 263     1890   2180   1960    250     50    -80       N  
ATOM   1792  CA  THR C 263      -6.808  -5.729 -50.929  1.00 16.75           C  
ANISOU 1792  CA  THR C 263     1830   2440   2100    320    180     60       C  
ATOM   1793  C   THR C 263      -7.490  -4.758 -51.894  1.00 16.29           C  
ANISOU 1793  C   THR C 263     1760   2240   2190    310     70    -10       C  
ATOM   1794  O   THR C 263      -7.474  -3.547 -51.615  1.00 17.22           O  
ANISOU 1794  O   THR C 263     1950   2310   2280    470    -30   -200       O  
ATOM   1795  CB  THR C 263      -7.352  -5.586 -49.501  1.00 19.47           C  
ANISOU 1795  CB  THR C 263     2110   3080   2210    610    340     70       C  
ATOM   1796  OG1 THR C 263      -6.655  -6.519 -48.682  1.00 20.03           O  
ANISOU 1796  OG1 THR C 263     2220   3270   2130    590    410    180       O  
ATOM   1797  CG2 THR C 263      -8.841  -5.844 -49.394  1.00 21.50           C  
ANISOU 1797  CG2 THR C 263     2110   3540   2520    700    530    290       C  
ATOM   1798  N   ALA C 264      -8.013  -5.261 -53.010  1.00 15.18           N  
ANISOU 1798  N   ALA C 264     1550   1990   2230    130     30    110       N  
ATOM   1799  CA  ALA C 264      -8.699  -4.377 -53.976  1.00 15.47           C  
ANISOU 1799  CA  ALA C 264     1590   1870   2410    100   -100     70       C  
ATOM   1800  C   ALA C 264     -10.073  -3.989 -53.415  1.00 17.74           C  
ANISOU 1800  C   ALA C 264     1690   2280   2770    300    -30    110       C  
ATOM   1801  O   ALA C 264     -10.719  -4.850 -52.776  1.00 18.56           O  
ANISOU 1801  O   ALA C 264     1590   2570   2890    340    140    300       O  
ATOM   1802  CB  ALA C 264      -8.832  -5.059 -55.312  1.00 14.44           C  
ANISOU 1802  CB  ALA C 264     1500   1600   2390   -100   -210    180       C  
ATOM   1803  N   THR C 265     -10.469  -2.732 -53.639  1.00 16.29           N  
ANISOU 1803  N   THR C 265     2020   1880   2290     10     70   -540       N  
ATOM   1804  CA  THR C 265     -11.786  -2.173 -53.225  1.00 18.21           C  
ANISOU 1804  CA  THR C 265     2120   2200   2590     10    160   -750       C  
ATOM   1805  C   THR C 265     -12.224  -1.179 -54.312  1.00 18.89           C  
ANISOU 1805  C   THR C 265     2020   2310   2840    190     20   -740       C  
ATOM   1806  O   THR C 265     -11.444  -0.992 -55.267  1.00 17.59           O  
ANISOU 1806  O   THR C 265     1900   2080   2700    260    -80   -560       O  
ATOM   1807  CB  THR C 265     -11.712  -1.450 -51.875  1.00 19.05           C  
ANISOU 1807  CB  THR C 265     2300   2250   2690      0    190   -850       C  
ATOM   1808  OG1 THR C 265     -10.845  -0.337 -52.075  1.00 18.97           O  
ANISOU 1808  OG1 THR C 265     2280   2130   2800    110     40   -760       O  
ATOM   1809  CG2 THR C 265     -11.213  -2.312 -50.736  1.00 19.45           C  
ANISOU 1809  CG2 THR C 265     2620   2260   2520   -120    280   -840       C  
ATOM   1810  N   LYS C 266     -13.394  -0.545 -54.165  1.00 20.94           N  
ANISOU 1810  N   LYS C 266     2110   2660   3190    280     40   -950       N  
ATOM   1811  CA  LYS C 266     -13.838   0.439 -55.188  1.00 22.55           C  
ANISOU 1811  CA  LYS C 266     2200   2860   3500    540   -130   -940       C  
ATOM   1812  C   LYS C 266     -12.806   1.568 -55.307  1.00 21.91           C  
ANISOU 1812  C   LYS C 266     2320   2530   3480    640   -220   -750       C  
ATOM   1813  O   LYS C 266     -12.504   1.963 -56.438  1.00 21.91           O  
ANISOU 1813  O   LYS C 266     2400   2440   3480    780   -320   -580       O  
ATOM   1814  CB  LYS C 266     -15.159   1.111 -54.811  1.00 25.72           C  
ANISOU 1814  CB  LYS C 266     2390   3390   3990    690   -140  -1240       C  
ATOM   1815  CG  LYS C 266     -16.339   0.194 -54.542  1.00 27.90           C  
ANISOU 1815  CG  LYS C 266     2410   3940   4250    550     10  -1550       C  
ATOM   1816  CD  LYS C 266     -17.582   0.961 -54.113  1.00 31.19           C  
ANISOU 1816  CD  LYS C 266     2570   4500   4780    700      0  -1910       C  
ATOM   1817  CE  LYS C 266     -18.717   0.057 -53.684  1.00 33.38           C  
ANISOU 1817  CE  LYS C 266     2570   5060   5060    470    230  -2310       C  
ATOM   1818  NZ  LYS C 266     -19.051  -0.919 -54.746  1.00 33.67           N  
ANISOU 1818  NZ  LYS C 266     2450   5290   5050    420    210  -2370       N  
ATOM   1819  N   ALA C 267     -12.273   2.030 -54.169  1.00 21.47           N  
ANISOU 1819  N   ALA C 267     2350   2360   3450    550   -150   -780       N  
ATOM   1820  CA  ALA C 267     -11.304   3.154 -54.122  1.00 21.72           C  
ANISOU 1820  CA  ALA C 267     2530   2150   3570    580   -180   -680       C  
ATOM   1821  C   ALA C 267      -9.921   2.744 -54.642  1.00 20.14           C  
ANISOU 1821  C   ALA C 267     2440   1880   3320    450   -180   -490       C  
ATOM   1822  O   ALA C 267      -9.174   3.633 -55.065  1.00 20.63           O  
ANISOU 1822  O   ALA C 267     2630   1750   3460    460   -180   -410       O  
ATOM   1823  CB  ALA C 267     -11.226   3.687 -52.709  1.00 22.39           C  
ANISOU 1823  CB  ALA C 267     2630   2190   3690    510   -120   -840       C  
ATOM   1824  N   TYR C 268      -9.596   1.452 -54.593  1.00 18.76           N  
ANISOU 1824  N   TYR C 268     2240   1850   3040    340   -170   -460       N  
ATOM   1825  CA  TYR C 268      -8.289   0.917 -55.059  1.00 17.41           C  
ANISOU 1825  CA  TYR C 268     2130   1660   2830    240   -190   -330       C  
ATOM   1826  C   TYR C 268      -8.646  -0.403 -55.745  1.00 16.10           C  
ANISOU 1826  C   TYR C 268     1930   1630   2560    230   -190   -270       C  
ATOM   1827  O   TYR C 268      -8.491  -1.470 -55.137  1.00 15.40           O  
ANISOU 1827  O   TYR C 268     1870   1620   2350    150   -160   -300       O  
ATOM   1828  CB  TYR C 268      -7.336   0.863 -53.861  1.00 17.69           C  
ANISOU 1828  CB  TYR C 268     2190   1700   2830    150   -190   -430       C  
ATOM   1829  CG  TYR C 268      -5.920   0.430 -54.146  1.00 17.32           C  
ANISOU 1829  CG  TYR C 268     2140   1670   2770     90   -230   -400       C  
ATOM   1830  CD1 TYR C 268      -5.061   1.241 -54.872  1.00 18.15           C  
ANISOU 1830  CD1 TYR C 268     2230   1660   3000     30   -200   -390       C  
ATOM   1831  CD2 TYR C 268      -5.392  -0.713 -53.571  1.00 17.12           C  
ANISOU 1831  CD2 TYR C 268     2150   1760   2600    100   -290   -430       C  
ATOM   1832  CE1 TYR C 268      -3.744   0.873 -55.111  1.00 18.38           C  
ANISOU 1832  CE1 TYR C 268     2190   1750   3050    -50   -210   -440       C  
ATOM   1833  CE2 TYR C 268      -4.074  -1.088 -53.785  1.00 17.36           C  
ANISOU 1833  CE2 TYR C 268     2130   1840   2630     90   -360   -460       C  
ATOM   1834  CZ  TYR C 268      -3.244  -0.293 -54.559  1.00 18.01           C  
ANISOU 1834  CZ  TYR C 268     2100   1870   2870      0   -320   -500       C  
ATOM   1835  OH  TYR C 268      -1.939  -0.655 -54.781  1.00 18.73           O  
ANISOU 1835  OH  TYR C 268     2080   2050   2980    -20   -370   -600       O  
ATOM   1836  N   ASN C 269      -9.144  -0.288 -56.983  1.00 16.09           N  
ANISOU 1836  N   ASN C 269     1900   1650   2570    320   -220   -190       N  
ATOM   1837  CA  ASN C 269      -9.692  -1.435 -57.758  1.00 15.51           C  
ANISOU 1837  CA  ASN C 269     1760   1730   2410    300   -220   -170       C  
ATOM   1838  C   ASN C 269      -8.611  -2.437 -58.176  1.00 14.37           C  
ANISOU 1838  C   ASN C 269     1670   1590   2200    200   -200    -70       C  
ATOM   1839  O   ASN C 269      -7.426  -2.229 -57.868  1.00 13.59           O  
ANISOU 1839  O   ASN C 269     1630   1410   2120    150   -210    -30       O  
ATOM   1840  CB  ASN C 269     -10.582  -0.934 -58.900  1.00 16.53           C  
ANISOU 1840  CB  ASN C 269     1830   1910   2540    480   -300   -160       C  
ATOM   1841  CG  ASN C 269      -9.849  -0.148 -59.964  1.00 16.75           C  
ANISOU 1841  CG  ASN C 269     2020   1780   2570    570   -350     20       C  
ATOM   1842  OD1 ASN C 269      -8.719  -0.471 -60.322  1.00 15.61           O  
ANISOU 1842  OD1 ASN C 269     1950   1570   2410    440   -290    130       O  
ATOM   1843  ND2 ASN C 269     -10.515   0.848 -60.519  1.00 18.51           N  
ANISOU 1843  ND2 ASN C 269     2310   1930   2790    800   -430     40       N  
ATOM   1844  N   VAL C 270      -9.049  -3.518 -58.822  1.00 14.41           N  
ANISOU 1844  N   VAL C 270     1630   1720   2120    160   -180    -70       N  
ATOM   1845  CA  VAL C 270      -8.142  -4.620 -59.254  1.00 13.91           C  
ANISOU 1845  CA  VAL C 270     1630   1660   1990     80   -150     10       C  
ATOM   1846  C   VAL C 270      -7.061  -4.086 -60.202  1.00 13.98           C  
ANISOU 1846  C   VAL C 270     1660   1610   2050    100   -200    130       C  
ATOM   1847  O   VAL C 270      -5.898  -4.539 -60.085  1.00 13.99           O  
ANISOU 1847  O   VAL C 270     1680   1580   2050     50   -190    140       O  
ATOM   1848  CB  VAL C 270      -8.958  -5.757 -59.889  1.00 14.08           C  
ANISOU 1848  CB  VAL C 270     1600   1810   1940     30    -90    -50       C  
ATOM   1849  CG1 VAL C 270      -8.067  -6.845 -60.469  1.00 13.43           C  
ANISOU 1849  CG1 VAL C 270     1590   1720   1800    -30    -70     30       C  
ATOM   1850  CG2 VAL C 270      -9.949  -6.342 -58.895  1.00 14.77           C  
ANISOU 1850  CG2 VAL C 270     1690   1940   1980    -70     30   -210       C  
ATOM   1851  N   THR C 271      -7.424  -3.173 -61.104  1.00 14.50           N  
ANISOU 1851  N   THR C 271     1740   1640   2130    190   -220    190       N  
ATOM   1852  CA  THR C 271      -6.438  -2.615 -62.066  1.00 15.26           C  
ANISOU 1852  CA  THR C 271     1930   1630   2240    160   -190    310       C  
ATOM   1853  C   THR C 271      -5.367  -1.826 -61.309  1.00 15.74           C  
ANISOU 1853  C   THR C 271     2010   1560   2410     70   -140    260       C  
ATOM   1854  O   THR C 271      -4.177  -2.020 -61.610  1.00 15.76           O  
ANISOU 1854  O   THR C 271     2000   1550   2440    -50    -80    240       O  
ATOM   1855  CB  THR C 271      -7.104  -1.715 -63.117  1.00 17.05           C  
ANISOU 1855  CB  THR C 271     2270   1800   2410    300   -230    400       C  
ATOM   1856  OG1 THR C 271      -8.049  -2.478 -63.874  1.00 17.21           O  
ANISOU 1856  OG1 THR C 271     2220   2010   2320    390   -310    380       O  
ATOM   1857  CG2 THR C 271      -6.100  -1.088 -64.062  1.00 18.32           C  
ANISOU 1857  CG2 THR C 271     2620   1800   2540    230   -130    530       C  
ATOM   1858  N   GLN C 272      -5.795  -0.987 -60.363  1.00 15.88           N  
ANISOU 1858  N   GLN C 272     2040   1500   2490    110   -160    200       N  
ATOM   1859  CA  GLN C 272      -4.892  -0.131 -59.553  1.00 16.86           C  
ANISOU 1859  CA  GLN C 272     2180   1500   2730     20   -110    110       C  
ATOM   1860  C   GLN C 272      -3.951  -0.982 -58.694  1.00 16.04           C  
ANISOU 1860  C   GLN C 272     1950   1530   2620    -40   -150    -20       C  
ATOM   1861  O   GLN C 272      -2.739  -0.717 -58.709  1.00 16.57           O  
ANISOU 1861  O   GLN C 272     1950   1580   2760   -150   -100   -130       O  
ATOM   1862  CB  GLN C 272      -5.735   0.816 -58.689  1.00 17.85           C  
ANISOU 1862  CB  GLN C 272     2340   1540   2900    110   -130     50       C  
ATOM   1863  CG  GLN C 272      -6.511   1.840 -59.508  1.00 19.67           C  
ANISOU 1863  CG  GLN C 272     2730   1610   3130    240   -120    150       C  
ATOM   1864  CD  GLN C 272      -7.464   2.681 -58.689  1.00 20.73           C  
ANISOU 1864  CD  GLN C 272     2870   1680   3330    380   -160     70       C  
ATOM   1865  OE1 GLN C 272      -8.263   2.178 -57.902  1.00 19.87           O  
ANISOU 1865  OE1 GLN C 272     2620   1730   3200    430   -210    -40       O  
ATOM   1866  NE2 GLN C 272      -7.438   3.981 -58.931  1.00 23.27           N  
ANISOU 1866  NE2 GLN C 272     3400   1740   3700    440   -100    110       N  
ATOM   1867  N   ALA C 273      -4.485  -2.002 -58.023  1.00 15.18           N  
ANISOU 1867  N   ALA C 273     1820   1530   2410     20   -220    -40       N  
ATOM   1868  CA  ALA C 273      -3.662  -2.843 -57.125  1.00 15.00           C  
ANISOU 1868  CA  ALA C 273     1780   1600   2330     50   -290   -150       C  
ATOM   1869  C   ALA C 273      -2.888  -3.938 -57.864  1.00 14.73           C  
ANISOU 1869  C   ALA C 273     1710   1640   2250     60   -310   -120       C  
ATOM   1870  O   ALA C 273      -1.749  -4.224 -57.416  1.00 14.99           O  
ANISOU 1870  O   ALA C 273     1680   1740   2280    100   -390   -260       O  
ATOM   1871  CB  ALA C 273      -4.561  -3.475 -56.087  1.00 14.70           C  
ANISOU 1871  CB  ALA C 273     1850   1580   2160    110   -310   -160       C  
ATOM   1872  N   PHE C 274      -3.450  -4.511 -58.944  1.00 14.19           N  
ANISOU 1872  N   PHE C 274     1670   1580   2140     40   -260      0       N  
ATOM   1873  CA  PHE C 274      -2.769  -5.670 -59.592  1.00 14.61           C  
ANISOU 1873  CA  PHE C 274     1710   1700   2140     50   -270      0       C  
ATOM   1874  C   PHE C 274      -2.520  -5.495 -61.101  1.00 15.33           C  
ANISOU 1874  C   PHE C 274     1750   1800   2280    -40   -190     70       C  
ATOM   1875  O   PHE C 274      -2.034  -6.465 -61.713  1.00 15.17           O  
ANISOU 1875  O   PHE C 274     1700   1850   2220    -30   -180     60       O  
ATOM   1876  CB  PHE C 274      -3.585  -6.936 -59.297  1.00 13.75           C  
ANISOU 1876  CB  PHE C 274     1730   1600   1890    100   -260     50       C  
ATOM   1877  CG  PHE C 274      -3.946  -7.082 -57.839  1.00 13.84           C  
ANISOU 1877  CG  PHE C 274     1880   1570   1810    160   -290      0       C  
ATOM   1878  CD1 PHE C 274      -2.959  -7.256 -56.879  1.00 14.54           C  
ANISOU 1878  CD1 PHE C 274     2030   1660   1840    290   -410    -90       C  
ATOM   1879  CD2 PHE C 274      -5.272  -7.088 -57.431  1.00 13.68           C  
ANISOU 1879  CD2 PHE C 274     1940   1520   1740    100   -200     10       C  
ATOM   1880  CE1 PHE C 274      -3.290  -7.375 -55.538  1.00 15.27           C  
ANISOU 1880  CE1 PHE C 274     2310   1710   1790    360   -430   -120       C  
ATOM   1881  CE2 PHE C 274      -5.600  -7.232 -56.088  1.00 14.43           C  
ANISOU 1881  CE2 PHE C 274     2200   1560   1720    130   -180    -40       C  
ATOM   1882  CZ  PHE C 274      -4.610  -7.368 -55.144  1.00 15.18           C  
ANISOU 1882  CZ  PHE C 274     2410   1640   1720    260   -300    -90       C  
ATOM   1883  N   GLY C 275      -2.804  -4.321 -61.675  1.00 16.65           N  
ANISOU 1883  N   GLY C 275     1940   1890   2500   -100   -120    140       N  
ATOM   1884  CA  GLY C 275      -2.554  -4.096 -63.114  1.00 17.89           C  
ANISOU 1884  CA  GLY C 275     2140   2030   2630   -170    -20    220       C  
ATOM   1885  C   GLY C 275      -3.717  -4.531 -63.997  1.00 18.14           C  
ANISOU 1885  C   GLY C 275     2240   2110   2540   -100    -40    340       C  
ATOM   1886  O   GLY C 275      -4.605  -5.266 -63.507  1.00 16.55           O  
ANISOU 1886  O   GLY C 275     2000   1980   2300    -30   -110    320       O  
ATOM   1887  N   ARG C 276      -3.704  -4.073 -65.256  1.00 20.10           N  
ANISOU 1887  N   ARG C 276     2600   2320   2720   -120     20    440       N  
ATOM   1888  CA  ARG C 276      -4.751  -4.400 -66.262  1.00 21.11           C  
ANISOU 1888  CA  ARG C 276     2780   2530   2700    -20    -40    520       C  
ATOM   1889  C   ARG C 276      -4.806  -5.907 -66.505  1.00 18.09           C  
ANISOU 1889  C   ARG C 276     2280   2320   2280    -50    -50    450       C  
ATOM   1890  O   ARG C 276      -3.729  -6.530 -66.544  1.00 16.29           O  
ANISOU 1890  O   ARG C 276     2000   2100   2090   -150     20    400       O  
ATOM   1891  CB  ARG C 276      -4.432  -3.781 -67.630  1.00 25.92           C  
ANISOU 1891  CB  ARG C 276     3600   3060   3190    -30     50    640       C  
ATOM   1892  CG  ARG C 276      -4.435  -2.263 -67.692  1.00 30.56           C  
ANISOU 1892  CG  ARG C 276     4430   3420   3760     10    110    750       C  
ATOM   1893  CD  ARG C 276      -5.818  -1.676 -67.493  1.00 35.29           C  
ANISOU 1893  CD  ARG C 276     5100   4010   4300    270    -60    790       C  
ATOM   1894  NE  ARG C 276      -6.784  -2.134 -68.488  1.00 39.23           N  
ANISOU 1894  NE  ARG C 276     5620   4680   4610    460   -200    810       N  
ATOM   1895  CZ  ARG C 276      -6.988  -1.576 -69.684  1.00 42.73           C  
ANISOU 1895  CZ  ARG C 276     6350   5060   4830    610   -220    950       C  
ATOM   1896  NH1 ARG C 276      -7.901  -2.084 -70.497  1.00 42.54           N  
ANISOU 1896  NH1 ARG C 276     6280   5260   4620    820   -400    920       N  
ATOM   1897  NH2 ARG C 276      -6.281  -0.525 -70.069  1.00 44.64           N  
ANISOU 1897  NH2 ARG C 276     6960   5000   5000    560    -60   1100       N  
ATOM   1898  N   ARG C 277      -6.014  -6.467 -66.647  1.00 16.39           N  
ANISOU 1898  N   ARG C 277     2010   2230   1990     20   -120    410       N  
ATOM   1899  CA  ARG C 277      -6.106  -7.908 -66.979  1.00 15.40           C  
ANISOU 1899  CA  ARG C 277     1800   2230   1820    -40    -90    330       C  
ATOM   1900  C   ARG C 277      -5.505  -8.090 -68.380  1.00 16.37           C  
ANISOU 1900  C   ARG C 277     1970   2400   1850    -80    -50    380       C  
ATOM   1901  O   ARG C 277      -5.535  -7.112 -69.167  1.00 16.64           O  
ANISOU 1901  O   ARG C 277     2130   2400   1790    -20    -60    490       O  
ATOM   1902  CB  ARG C 277      -7.550  -8.424 -66.960  1.00 15.75           C  
ANISOU 1902  CB  ARG C 277     1750   2420   1820    -10   -130    200       C  
ATOM   1903  CG  ARG C 277      -8.123  -8.816 -65.603  1.00 15.18           C  
ANISOU 1903  CG  ARG C 277     1640   2320   1810    -70    -90     90       C  
ATOM   1904  CD  ARG C 277      -8.168  -7.795 -64.473  1.00 14.75           C  
ANISOU 1904  CD  ARG C 277     1610   2160   1840    -10   -120    120       C  
ATOM   1905  NE  ARG C 277      -6.859  -7.519 -63.897  1.00 13.90           N  
ANISOU 1905  NE  ARG C 277     1590   1900   1790    -20   -110    210       N  
ATOM   1906  CZ  ARG C 277      -6.221  -8.332 -63.048  1.00 13.40           C  
ANISOU 1906  CZ  ARG C 277     1590   1770   1730    -70    -70    180       C  
ATOM   1907  NH1 ARG C 277      -5.035  -7.993 -62.571  1.00 13.21           N  
ANISOU 1907  NH1 ARG C 277     1590   1670   1760    -40   -110    200       N  
ATOM   1908  NH2 ARG C 277      -6.751  -9.497 -62.705  1.00 13.44           N  
ANISOU 1908  NH2 ARG C 277     1650   1780   1670   -130     10    100       N  
ATOM   1909  N   GLY C 278      -4.976  -9.279 -68.685  1.00 16.10           N  
ANISOU 1909  N   GLY C 278     1890   2410   1810   -170     20    310       N  
ATOM   1910  CA  GLY C 278      -4.396  -9.509 -70.023  1.00 17.66           C  
ANISOU 1910  CA  GLY C 278     2130   2670   1910   -220     90    330       C  
ATOM   1911  C   GLY C 278      -3.941 -10.952 -70.209  1.00 17.80           C  
ANISOU 1911  C   GLY C 278     2080   2740   1950   -290    150    220       C  
ATOM   1912  O   GLY C 278      -4.030 -11.740 -69.274  1.00 16.10           O  
ANISOU 1912  O   GLY C 278     1840   2470   1800   -280    150    150       O  
ATOM   1913  N   PRO C 279      -3.434 -11.314 -71.415  1.00 19.49           N  
ANISOU 1913  N   PRO C 279     2300   3030   2080   -350    230    200       N  
ATOM   1914  CA  PRO C 279      -2.995 -12.679 -71.718  1.00 20.08           C  
ANISOU 1914  CA  PRO C 279     2320   3140   2170   -400    300     80       C  
ATOM   1915  C   PRO C 279      -1.509 -13.017 -71.518  1.00 21.12           C  
ANISOU 1915  C   PRO C 279     2400   3210   2420   -420    370      0       C  
ATOM   1916  O   PRO C 279      -1.150 -14.151 -71.768  1.00 20.93           O  
ANISOU 1916  O   PRO C 279     2350   3200   2400   -420    410   -110       O  
ATOM   1917  CB  PRO C 279      -3.287 -12.736 -73.226  1.00 21.38           C  
ANISOU 1917  CB  PRO C 279     2520   3450   2160   -450    330     80       C  
ATOM   1918  CG  PRO C 279      -2.923 -11.348 -73.721  1.00 22.19           C  
ANISOU 1918  CG  PRO C 279     2740   3510   2180   -440    350    220       C  
ATOM   1919  CD  PRO C 279      -3.266 -10.419 -72.568  1.00 21.49           C  
ANISOU 1919  CD  PRO C 279     2670   3310   2190   -370    270    300       C  
ATOM   1920  N   GLU C 280      -0.696 -12.057 -71.064  1.00 22.81           N  
ANISOU 1920  N   GLU C 280     2580   3360   2720   -430    370     20       N  
ATOM   1921  CA  GLU C 280       0.759 -12.323 -70.903  1.00 24.69           C  
ANISOU 1921  CA  GLU C 280     2690   3610   3080   -430    430   -140       C  
ATOM   1922  C   GLU C 280       1.013 -13.230 -69.691  1.00 26.34           C  
ANISOU 1922  C   GLU C 280     2870   3760   3380   -250    300   -230       C  
ATOM   1923  O   GLU C 280       0.172 -13.274 -68.772  1.00 24.48           O  
ANISOU 1923  O   GLU C 280     2750   3440   3120   -180    210   -140       O  
ATOM   1924  CB  GLU C 280       1.546 -11.015 -70.854  1.00 25.49           C  
ANISOU 1924  CB  GLU C 280     2740   3690   3260   -540    510   -160       C  
ATOM   1925  CG  GLU C 280       1.330 -10.150 -72.082  1.00 26.29           C  
ANISOU 1925  CG  GLU C 280     2990   3780   3220   -700    670    -40       C  
ATOM   1926  CD  GLU C 280       1.639 -10.822 -73.412  1.00 27.69           C  
ANISOU 1926  CD  GLU C 280     3180   4060   3280   -790    800   -100       C  
ATOM   1927  OE1 GLU C 280       2.502 -11.730 -73.446  1.00 27.21           O  
ANISOU 1927  OE1 GLU C 280     2940   4080   3320   -790    840   -300       O  
ATOM   1928  OE2 GLU C 280       0.971 -10.476 -74.405  1.00 28.15           O  
ANISOU 1928  OE2 GLU C 280     3430   4120   3130   -830    850     50       O  
ATOM   1929  N   GLN C 281       2.166 -13.898 -69.731  1.00 30.20           N  
ANISOU 1929  N   GLN C 281     3240   4290   3940   -170    300   -420       N  
ATOM   1930  CA  GLN C 281       2.692 -14.900 -68.764  1.00 35.20           C  
ANISOU 1930  CA  GLN C 281     3900   4860   4620     80    170   -540       C  
ATOM   1931  C   GLN C 281       2.403 -14.559 -67.292  1.00 35.11           C  
ANISOU 1931  C   GLN C 281     3990   4750   4600    220     20   -480       C  
ATOM   1932  O   GLN C 281       1.750 -15.385 -66.621  1.00 40.37           O  
ANISOU 1932  O   GLN C 281     4890   5270   5170    340    -30   -400       O  
ATOM   1933  CB  GLN C 281       4.199 -15.039 -68.996  1.00 40.58           C  
ANISOU 1933  CB  GLN C 281     4330   5670   5420    150    160   -820       C  
ATOM   1934  CG  GLN C 281       4.870 -16.137 -68.183  1.00 46.17           C  
ANISOU 1934  CG  GLN C 281     5060   6340   6140    500    -20   -980       C  
ATOM   1935  CD  GLN C 281       4.399 -17.522 -68.553  1.00 49.43           C  
ANISOU 1935  CD  GLN C 281     5710   6610   6460    600     20   -930       C  
ATOM   1936  OE1 GLN C 281       3.521 -17.702 -69.397  1.00 52.57           O  
ANISOU 1936  OE1 GLN C 281     6210   6980   6790    380    170   -800       O  
ATOM   1937  NE2 GLN C 281       4.993 -18.522 -67.920  1.00 52.47           N  
ANISOU 1937  NE2 GLN C 281     6210   6900   6820    940   -130  -1060       N  
ATOM   1938  N   THR C 282       2.883 -13.421 -66.790  1.00 32.79           N  
ANISOU 1938  N   THR C 282     3550   4520   4390    190    -30   -530       N  
ATOM   1939  CA  THR C 282       2.691 -13.100 -65.345  1.00 30.56           C  
ANISOU 1939  CA  THR C 282     3350   4160   4100    340   -180   -500       C  
ATOM   1940  C   THR C 282       1.659 -11.986 -65.144  1.00 26.54           C  
ANISOU 1940  C   THR C 282     2910   3600   3570    170   -130   -320       C  
ATOM   1941  O   THR C 282       1.679 -11.353 -64.069  1.00 26.27           O  
ANISOU 1941  O   THR C 282     2880   3540   3560    240   -220   -330       O  
ATOM   1942  CB  THR C 282       4.051 -12.777 -64.717  1.00 32.99           C  
ANISOU 1942  CB  THR C 282     3430   4600   4510    490   -310   -770       C  
ATOM   1943  OG1 THR C 282       4.622 -11.704 -65.471  1.00 32.47           O  
ANISOU 1943  OG1 THR C 282     3110   4650   4580    230   -160   -880       O  
ATOM   1944  CG2 THR C 282       4.981 -13.971 -64.721  1.00 34.79           C  
ANISOU 1944  CG2 THR C 282     3610   4880   4730    770   -430   -980       C  
ATOM   1945  N   GLN C 283       0.775 -11.807 -66.127  1.00 21.39           N  
ANISOU 1945  N   GLN C 283     2890   2910   2330   -140    200    230       N  
ATOM   1946  CA  GLN C 283      -0.297 -10.787 -66.103  1.00 20.40           C  
ANISOU 1946  CA  GLN C 283     2790   2730   2230   -130    190    270       C  
ATOM   1947  C   GLN C 283      -1.592 -11.450 -65.612  1.00 18.34           C  
ANISOU 1947  C   GLN C 283     2540   2460   1960   -120    130    190       C  
ATOM   1948  O   GLN C 283      -1.858 -12.602 -66.037  1.00 18.49           O  
ANISOU 1948  O   GLN C 283     2560   2540   1920    -90    100    140       O  
ATOM   1949  CB  GLN C 283      -0.439 -10.223 -67.515  1.00 21.56           C  
ANISOU 1949  CB  GLN C 283     2940   2940   2310    -80    220    360       C  
ATOM   1950  CG  GLN C 283      -1.443  -9.094 -67.644  1.00 22.69           C  
ANISOU 1950  CG  GLN C 283     3100   3040   2490    -60    210    420       C  
ATOM   1951  CD  GLN C 283      -1.467  -8.527 -69.045  1.00 23.71           C  
ANISOU 1951  CD  GLN C 283     3230   3230   2540      0    250    540       C  
ATOM   1952  OE1 GLN C 283      -0.999  -9.142 -70.002  1.00 24.03           O  
ANISOU 1952  OE1 GLN C 283     3270   3380   2480     50    270    550       O  
ATOM   1953  NE2 GLN C 283      -2.062  -7.356 -69.185  1.00 24.66           N  
ANISOU 1953  NE2 GLN C 283     3360   3300   2710     20    260    620       N  
ATOM   1954  N   GLY C 284      -2.343 -10.773 -64.740  1.00 15.75           N  
ANISOU 1954  N   GLY C 284     2220   2060   1690   -140    110    190       N  
ATOM   1955  CA  GLY C 284      -3.619 -11.317 -64.232  1.00 14.55           C  
ANISOU 1955  CA  GLY C 284     2080   1910   1540   -130     70    130       C  
ATOM   1956  C   GLY C 284      -4.651 -11.393 -65.346  1.00 14.45           C  
ANISOU 1956  C   GLY C 284     2070   1950   1470    -70     40    140       C  
ATOM   1957  O   GLY C 284      -4.621 -10.515 -66.226  1.00 14.84           O  
ANISOU 1957  O   GLY C 284     2130   2020   1490    -40     60    210       O  
ATOM   1958  N   ASN C 285      -5.534 -12.394 -65.312  1.00 13.70           N  
ANISOU 1958  N   ASN C 285     1970   1880   1360    -60      0     70       N  
ATOM   1959  CA  ASN C 285      -6.566 -12.561 -66.372  1.00 13.63           C  
ANISOU 1959  CA  ASN C 285     1960   1930   1290      0    -40     60       C  
ATOM   1960  C   ASN C 285      -7.952 -12.757 -65.757  1.00 13.21           C  
ANISOU 1960  C   ASN C 285     1880   1850   1280    -10    -80     20       C  
ATOM   1961  O   ASN C 285      -8.900 -12.994 -66.535  1.00 13.80           O  
ANISOU 1961  O   ASN C 285     1940   1970   1330     40   -120      0       O  
ATOM   1962  CB  ASN C 285      -6.314 -13.802 -67.233  1.00 13.57           C  
ANISOU 1962  CB  ASN C 285     1940   2000   1220     30    -70      0       C  
ATOM   1963  CG  ASN C 285      -6.507 -15.105 -66.479  1.00 13.08           C  
ANISOU 1963  CG  ASN C 285     1850   1900   1220    -10   -100    -80       C  
ATOM   1964  OD1 ASN C 285      -6.358 -15.162 -65.263  1.00 12.22           O  
ANISOU 1964  OD1 ASN C 285     1740   1730   1170    -60    -80    -80       O  
ATOM   1965  ND2 ASN C 285      -6.833 -16.169 -67.199  1.00 13.24           N  
ANISOU 1965  ND2 ASN C 285     1860   1960   1210     20   -140   -160       N  
ATOM   1966  N   PHE C 286      -8.075 -12.609 -64.436  1.00 12.55           N  
ANISOU 1966  N   PHE C 286     1800   1700   1270    -50    -70     10       N  
ATOM   1967  CA  PHE C 286      -9.373 -12.888 -63.763  1.00 12.17           C  
ANISOU 1967  CA  PHE C 286     1720   1640   1270    -50    -90    -20       C  
ATOM   1968  C   PHE C 286     -10.140 -11.623 -63.382  1.00 12.41           C  
ANISOU 1968  C   PHE C 286     1760   1640   1320    -30    -90     10       C  
ATOM   1969  O   PHE C 286      -9.573 -10.731 -62.739  1.00 11.89           O  
ANISOU 1969  O   PHE C 286     1710   1520   1280    -50    -50     40       O  
ATOM   1970  CB  PHE C 286      -9.113 -13.724 -62.509  1.00 11.52           C  
ANISOU 1970  CB  PHE C 286     1620   1520   1230    -90    -80    -50       C  
ATOM   1971  CG  PHE C 286     -10.334 -14.228 -61.783  1.00 11.28           C  
ANISOU 1971  CG  PHE C 286     1560   1480   1250   -100    -90    -80       C  
ATOM   1972  CD1 PHE C 286     -10.890 -15.455 -62.109  1.00 11.47           C  
ANISOU 1972  CD1 PHE C 286     1540   1510   1310   -110   -130   -120       C  
ATOM   1973  CD2 PHE C 286     -10.913 -13.492 -60.763  1.00 11.05           C  
ANISOU 1973  CD2 PHE C 286     1520   1420   1250   -100    -70    -60       C  
ATOM   1974  CE1 PHE C 286     -11.998 -15.935 -61.431  1.00 11.46           C  
ANISOU 1974  CE1 PHE C 286     1490   1500   1370   -120   -130   -130       C  
ATOM   1975  CE2 PHE C 286     -12.026 -13.970 -60.091  1.00 11.13           C  
ANISOU 1975  CE2 PHE C 286     1490   1430   1310   -100    -80    -70       C  
ATOM   1976  CZ  PHE C 286     -12.561 -15.193 -60.420  1.00 11.50           C  
ANISOU 1976  CZ  PHE C 286     1490   1490   1390   -110   -100   -100       C  
ATOM   1977  N   GLY C 287     -11.421 -11.579 -63.773  1.00 13.09           N  
ANISOU 1977  N   GLY C 287     1820   1750   1410      0   -120     10       N  
ATOM   1978  CA  GLY C 287     -12.296 -10.455 -63.404  1.00 13.45           C  
ANISOU 1978  CA  GLY C 287     1860   1770   1480     30   -120     40       C  
ATOM   1979  C   GLY C 287     -13.042  -9.814 -64.559  1.00 14.27           C  
ANISOU 1979  C   GLY C 287     1960   1910   1550     90   -150     70       C  
ATOM   1980  O   GLY C 287     -12.394  -9.418 -65.557  1.00 14.22           O  
ANISOU 1980  O   GLY C 287     1980   1930   1490    120   -140    120       O  
ATOM   1981  N   ASP C 288     -14.369  -9.721 -64.422  1.00 14.50           N  
ANISOU 1981  N   ASP C 288     1950   1950   1600    120   -180     50       N  
ATOM   1982  CA  ASP C 288     -15.187  -9.020 -65.442  1.00 15.54           C  
ANISOU 1982  CA  ASP C 288     2080   2130   1700    190   -210     90       C  
ATOM   1983  C   ASP C 288     -15.149  -7.539 -65.029  1.00 16.20           C  
ANISOU 1983  C   ASP C 288     2190   2140   1820    220   -170    160       C  
ATOM   1984  O   ASP C 288     -14.462  -7.225 -64.034  1.00 14.62           O  
ANISOU 1984  O   ASP C 288     2020   1870   1660    180   -130    150       O  
ATOM   1985  CB  ASP C 288     -16.595  -9.615 -65.576  1.00 15.81           C  
ANISOU 1985  CB  ASP C 288     2050   2210   1750    220   -260     40       C  
ATOM   1986  CG  ASP C 288     -17.494  -9.459 -64.361  1.00 15.62           C  
ANISOU 1986  CG  ASP C 288     1990   2150   1800    200   -250     20       C  
ATOM   1987  OD1 ASP C 288     -17.099  -8.756 -63.409  1.00 14.68           O  
ANISOU 1987  OD1 ASP C 288     1900   1970   1710    190   -200     50       O  
ATOM   1988  OD2 ASP C 288     -18.595 -10.047 -64.383  1.00 16.55           O  
ANISOU 1988  OD2 ASP C 288     2040   2300   1950    210   -290    -20       O  
ATOM   1989  N   GLN C 289     -15.881  -6.677 -65.735  1.00 18.04           N  
ANISOU 1989  N   GLN C 289     2430   2390   2030    290   -190    210       N  
ATOM   1990  CA  GLN C 289     -15.882  -5.213 -65.460  1.00 18.94           C  
ANISOU 1990  CA  GLN C 289     2570   2430   2200    320   -160    270       C  
ATOM   1991  C   GLN C 289     -16.368  -4.923 -64.035  1.00 18.76           C  
ANISOU 1991  C   GLN C 289     2530   2340   2250    300   -140    220       C  
ATOM   1992  O   GLN C 289     -15.767  -4.049 -63.376  1.00 18.59           O  
ANISOU 1992  O   GLN C 289     2540   2230   2290    290   -110    240       O  
ATOM   1993  CB  GLN C 289     -16.726  -4.499 -66.521  1.00 20.98           C  
ANISOU 1993  CB  GLN C 289     2820   2730   2420    410   -190    340       C  
ATOM   1994  CG  GLN C 289     -16.042  -4.376 -67.880  1.00 22.21           C  
ANISOU 1994  CG  GLN C 289     3000   2940   2490    450   -180    420       C  
ATOM   1995  CD  GLN C 289     -17.006  -4.044 -68.995  1.00 24.30           C  
ANISOU 1995  CD  GLN C 289     3250   3290   2690    550   -230    470       C  
ATOM   1996  OE1 GLN C 289     -16.868  -3.042 -69.705  1.00 25.37           O  
ANISOU 1996  OE1 GLN C 289     3410   3420   2810    610   -210    580       O  
ATOM   1997  NE2 GLN C 289     -18.025  -4.878 -69.140  1.00 25.01           N  
ANISOU 1997  NE2 GLN C 289     3290   3470   2750    570   -290    390       N  
ATOM   1998  N   GLU C 290     -17.376  -5.658 -63.563  1.00 18.43           N  
ANISOU 1998  N   GLU C 290     2440   2350   2220    300   -170    160       N  
ATOM   1999  CA  GLU C 290     -17.940  -5.409 -62.209  1.00 18.48           C  
ANISOU 1999  CA  GLU C 290     2420   2310   2280    300   -150    120       C  
ATOM   2000  C   GLU C 290     -16.894  -5.724 -61.122  1.00 17.27           C  
ANISOU 2000  C   GLU C 290     2290   2120   2150    230   -110     80       C  
ATOM   2001  O   GLU C 290     -16.709  -4.873 -60.231  1.00 16.62           O  
ANISOU 2001  O   GLU C 290     2230   1980   2110    240    -80     70       O  
ATOM   2002  CB  GLU C 290     -19.230  -6.213 -62.026  1.00 19.00           C  
ANISOU 2002  CB  GLU C 290     2420   2450   2350    310   -170     80       C  
ATOM   2003  CG  GLU C 290     -19.967  -5.882 -60.743  1.00 19.69           C  
ANISOU 2003  CG  GLU C 290     2470   2520   2490    330   -150     50       C  
ATOM   2004  CD  GLU C 290     -21.258  -6.652 -60.515  1.00 20.41           C  
ANISOU 2004  CD  GLU C 290     2480   2680   2600    330   -160     30       C  
ATOM   2005  OE1 GLU C 290     -21.543  -7.602 -61.280  1.00 19.94           O  
ANISOU 2005  OE1 GLU C 290     2380   2670   2530    310   -200     20       O  
ATOM   2006  OE2 GLU C 290     -21.981  -6.289 -59.569  1.00 21.84           O  
ANISOU 2006  OE2 GLU C 290     2620   2860   2820    370   -130     10       O  
ATOM   2007  N   LEU C 291     -16.230  -6.884 -61.195  1.00 16.14           N  
ANISOU 2007  N   LEU C 291     2150   2010   1970    180   -110     60       N  
ATOM   2008  CA  LEU C 291     -15.212  -7.272 -60.174  1.00 15.54           C  
ANISOU 2008  CA  LEU C 291     2090   1900   1910    120    -80     30       C  
ATOM   2009  C   LEU C 291     -13.987  -6.348 -60.252  1.00 15.57           C  
ANISOU 2009  C   LEU C 291     2150   1840   1920    110    -60     60       C  
ATOM   2010  O   LEU C 291     -13.490  -5.927 -59.179  1.00 15.48           O  
ANISOU 2010  O   LEU C 291     2150   1790   1940    100    -40     20       O  
ATOM   2011  CB  LEU C 291     -14.817  -8.738 -60.373  1.00 15.33           C  
ANISOU 2011  CB  LEU C 291     2050   1920   1850     80    -80     10       C  
ATOM   2012  CG  LEU C 291     -13.720  -9.258 -59.442  1.00 15.09           C  
ANISOU 2012  CG  LEU C 291     2030   1880   1820     30    -50    -10       C  
ATOM   2013  CD1 LEU C 291     -14.052  -8.973 -57.988  1.00 15.51           C  
ANISOU 2013  CD1 LEU C 291     2070   1920   1900     40    -30    -30       C  
ATOM   2014  CD2 LEU C 291     -13.495 -10.746 -59.651  1.00 15.00           C  
ANISOU 2014  CD2 LEU C 291     2000   1900   1800    -10    -60    -20       C  
ATOM   2015  N   ILE C 292     -13.523  -6.037 -61.464  1.00 15.63           N  
ANISOU 2015  N   ILE C 292     2180   1850   1910    120    -60    110       N  
ATOM   2016  CA  ILE C 292     -12.344  -5.138 -61.640  1.00 15.76           C  
ANISOU 2016  CA  ILE C 292     2230   1790   1960    100    -40    150       C  
ATOM   2017  C   ILE C 292     -12.570  -3.801 -60.915  1.00 16.65           C  
ANISOU 2017  C   ILE C 292     2360   1820   2150    130    -30    140       C  
ATOM   2018  O   ILE C 292     -11.657  -3.380 -60.170  1.00 16.17           O  
ANISOU 2018  O   ILE C 292     2310   1690   2140     90    -10    110       O  
ATOM   2019  CB  ILE C 292     -12.035  -4.937 -63.139  1.00 15.99           C  
ANISOU 2019  CB  ILE C 292     2280   1850   1950    120    -40    230       C  
ATOM   2020  CG1 ILE C 292     -11.498  -6.228 -63.763  1.00 15.23           C  
ANISOU 2020  CG1 ILE C 292     2170   1830   1780    100    -40    220       C  
ATOM   2021  CG2 ILE C 292     -11.063  -3.775 -63.337  1.00 16.67           C  
ANISOU 2021  CG2 ILE C 292     2390   1850   2090    110      0    300       C  
ATOM   2022  CD1 ILE C 292     -11.328  -6.173 -65.259  1.00 15.73           C  
ANISOU 2022  CD1 ILE C 292     2250   1960   1770    140    -50    290       C  
ATOM   2023  N   ARG C 293     -13.742  -3.176 -61.080  1.00 17.75           N  
ANISOU 2023  N   ARG C 293     2490   1950   2310    190    -40    160       N  
ATOM   2024  CA  ARG C 293     -13.965  -1.855 -60.429  1.00 19.32           C  
ANISOU 2024  CA  ARG C 293     2700   2050   2590    220    -30    150       C  
ATOM   2025  C   ARG C 293     -14.385  -1.979 -58.957  1.00 18.61           C  
ANISOU 2025  C   ARG C 293     2590   1970   2510    230    -30     50       C  
ATOM   2026  O   ARG C 293     -14.320  -0.943 -58.269  1.00 19.87           O  
ANISOU 2026  O   ARG C 293     2760   2050   2740    250    -30     10       O  
ATOM   2027  CB  ARG C 293     -14.979  -1.014 -61.217  1.00 20.88           C  
ANISOU 2027  CB  ARG C 293     2890   2230   2810    300    -50    210       C  
ATOM   2028  CG  ARG C 293     -16.363  -1.624 -61.373  1.00 21.65           C  
ANISOU 2028  CG  ARG C 293     2950   2430   2850    340    -70    200       C  
ATOM   2029  CD  ARG C 293     -17.280  -0.731 -62.202  1.00 23.27           C  
ANISOU 2029  CD  ARG C 293     3150   2620   3070    430    -90    260       C  
ATOM   2030  NE  ARG C 293     -18.523  -1.425 -62.498  1.00 23.65           N  
ANISOU 2030  NE  ARG C 293     3150   2770   3070    460   -120    250       N  
ATOM   2031  CZ  ARG C 293     -19.594  -1.430 -61.715  1.00 24.59           C  
ANISOU 2031  CZ  ARG C 293     3230   2910   3210    500   -130    200       C  
ATOM   2032  NH1 ARG C 293     -20.668  -2.112 -62.075  1.00 24.56           N  
ANISOU 2032  NH1 ARG C 293     3170   3000   3160    520   -160    190       N  
ATOM   2033  NH2 ARG C 293     -19.592  -0.760 -60.574  1.00 25.64           N  
ANISOU 2033  NH2 ARG C 293     3370   2980   3400    510   -110    150       N  
ATOM   2034  N   GLN C 294     -14.724  -3.173 -58.461  1.00 17.53           N  
ANISOU 2034  N   GLN C 294     2430   1920   2320    210    -30     10       N  
ATOM   2035  CA  GLN C 294     -15.188  -3.271 -57.045  1.00 16.91           C  
ANISOU 2035  CA  GLN C 294     2320   1870   2240    230    -30    -70       C  
ATOM   2036  C   GLN C 294     -14.222  -4.068 -56.162  1.00 16.21           C  
ANISOU 2036  C   GLN C 294     2240   1810   2110    180    -10   -110       C  
ATOM   2037  O   GLN C 294     -14.228  -3.832 -54.939  1.00 15.93           O  
ANISOU 2037  O   GLN C 294     2200   1780   2080    200      0   -180       O  
ATOM   2038  CB  GLN C 294     -16.583  -3.894 -57.005  1.00 16.76           C  
ANISOU 2038  CB  GLN C 294     2250   1930   2190    270    -30    -60       C  
ATOM   2039  CG  GLN C 294     -17.630  -3.022 -57.683  1.00 17.62           C  
ANISOU 2039  CG  GLN C 294     2350   2020   2330    330    -40    -30       C  
ATOM   2040  CD  GLN C 294     -18.990  -3.670 -57.708  1.00 17.97           C  
ANISOU 2040  CD  GLN C 294     2330   2140   2350    360    -50    -30       C  
ATOM   2041  OE1 GLN C 294     -19.125  -4.874 -57.503  1.00 18.01           O  
ANISOU 2041  OE1 GLN C 294     2300   2220   2330    320    -50    -30       O  
ATOM   2042  NE2 GLN C 294     -20.009  -2.871 -57.989  1.00 18.51           N  
ANISOU 2042  NE2 GLN C 294     2380   2210   2440    430    -60    -10       N  
ATOM   2043  N   GLY C 295     -13.427  -4.962 -56.743  1.00 15.36           N  
ANISOU 2043  N   GLY C 295     2140   1720   1980    120    -10    -80       N  
ATOM   2044  CA  GLY C 295     -12.525  -5.774 -55.912  1.00 14.93           C  
ANISOU 2044  CA  GLY C 295     2080   1700   1890     80      0   -120       C  
ATOM   2045  C   GLY C 295     -13.299  -6.509 -54.826  1.00 15.07           C  
ANISOU 2045  C   GLY C 295     2060   1790   1870    100     20   -150       C  
ATOM   2046  O   GLY C 295     -14.363  -7.101 -55.144  1.00 14.64           O  
ANISOU 2046  O   GLY C 295     1970   1780   1810    120     20   -120       O  
ATOM   2047  N   THR C 296     -12.828  -6.412 -53.578  1.00 15.21           N  
ANISOU 2047  N   THR C 296     2080   1820   1870    120     30   -200       N  
ATOM   2048  CA  THR C 296     -13.467  -7.115 -52.437  1.00 15.32           C  
ANISOU 2048  CA  THR C 296     2060   1920   1840    150     50   -210       C  
ATOM   2049  C   THR C 296     -14.819  -6.483 -52.085  1.00 15.90           C  
ANISOU 2049  C   THR C 296     2110   2010   1920    220     60   -230       C  
ATOM   2050  O   THR C 296     -15.467  -7.026 -51.183  1.00 15.43           O  
ANISOU 2050  O   THR C 296     2010   2030   1820    250    100   -220       O  
ATOM   2051  CB  THR C 296     -12.518  -7.205 -51.236  1.00 15.59           C  
ANISOU 2051  CB  THR C 296     2100   1990   1830    160     60   -270       C  
ATOM   2052  OG1 THR C 296     -12.230  -5.889 -50.770  1.00 16.05           O  
ANISOU 2052  OG1 THR C 296     2180   2000   1910    190     40   -350       O  
ATOM   2053  CG2 THR C 296     -11.233  -7.937 -51.572  1.00 14.72           C  
ANISOU 2053  CG2 THR C 296     2010   1870   1710     90     50   -250       C  
ATOM   2054  N   ASP C 297     -15.223  -5.399 -52.761  1.00 16.41           N  
ANISOU 2054  N   ASP C 297     2190   2010   2030    240     40   -230       N  
ATOM   2055  CA  ASP C 297     -16.557  -4.793 -52.493  1.00 17.91           C  
ANISOU 2055  CA  ASP C 297     2350   2220   2240    320     50   -240       C  
ATOM   2056  C   ASP C 297     -17.599  -5.527 -53.340  1.00 17.73           C  
ANISOU 2056  C   ASP C 297     2280   2240   2220    310     50   -170       C  
ATOM   2057  O   ASP C 297     -18.786  -5.251 -53.160  1.00 18.49           O  
ANISOU 2057  O   ASP C 297     2330   2370   2330    360     60   -170       O  
ATOM   2058  CB  ASP C 297     -16.595  -3.283 -52.748  1.00 19.43           C  
ANISOU 2058  CB  ASP C 297     2570   2320   2490    360     30   -280       C  
ATOM   2059  CG  ASP C 297     -15.826  -2.465 -51.726  1.00 20.36           C  
ANISOU 2059  CG  ASP C 297     2720   2400   2620    380     20   -370       C  
ATOM   2060  OD1 ASP C 297     -15.766  -2.896 -50.553  1.00 21.37           O  
ANISOU 2060  OD1 ASP C 297     2830   2610   2680    410     40   -420       O  
ATOM   2061  OD2 ASP C 297     -15.256  -1.431 -52.119  1.00 21.77           O  
ANISOU 2061  OD2 ASP C 297     2930   2470   2870    370    -10   -400       O  
ATOM   2062  N   TYR C 298     -17.146  -6.413 -54.236  1.00 17.24           N  
ANISOU 2062  N   TYR C 298     2220   2170   2160    240     40   -130       N  
ATOM   2063  CA  TYR C 298     -18.028  -7.225 -55.117  1.00 16.83           C  
ANISOU 2063  CA  TYR C 298     2120   2160   2120    230     30    -80       C  
ATOM   2064  C   TYR C 298     -18.981  -8.018 -54.209  1.00 17.06           C  
ANISOU 2064  C   TYR C 298     2080   2260   2150    240     60    -70       C  
ATOM   2065  O   TYR C 298     -18.494  -8.741 -53.316  1.00 16.04           O  
ANISOU 2065  O   TYR C 298     1940   2160   1990    220    100    -70       O  
ATOM   2066  CB  TYR C 298     -17.130  -8.058 -56.035  1.00 16.24           C  
ANISOU 2066  CB  TYR C 298     2070   2070   2030    160     10    -60       C  
ATOM   2067  CG  TYR C 298     -17.808  -8.943 -57.048  1.00 16.63           C  
ANISOU 2067  CG  TYR C 298     2070   2150   2100    140    -20    -40       C  
ATOM   2068  CD1 TYR C 298     -18.412  -8.405 -58.173  1.00 17.12           C  
ANISOU 2068  CD1 TYR C 298     2130   2210   2170    170    -60    -20       C  
ATOM   2069  CD2 TYR C 298     -17.738 -10.322 -56.949  1.00 16.49           C  
ANISOU 2069  CD2 TYR C 298     2020   2160   2090     90    -20    -30       C  
ATOM   2070  CE1 TYR C 298     -19.003  -9.212 -59.131  1.00 17.87           C  
ANISOU 2070  CE1 TYR C 298     2180   2340   2270    160   -100    -20       C  
ATOM   2071  CE2 TYR C 298     -18.324 -11.146 -57.898  1.00 17.32           C  
ANISOU 2071  CE2 TYR C 298     2080   2280   2220     70    -50    -30       C  
ATOM   2072  CZ  TYR C 298     -18.959 -10.589 -58.997  1.00 17.93           C  
ANISOU 2072  CZ  TYR C 298     2150   2370   2290    110   -100    -30       C  
ATOM   2073  OH  TYR C 298     -19.527 -11.388 -59.946  1.00 18.50           O  
ANISOU 2073  OH  TYR C 298     2170   2470   2380     90   -150    -50       O  
ATOM   2074  N   LYS C 299     -20.292  -7.884 -54.433  1.00 18.01           N  
ANISOU 2074  N   LYS C 299     2140   2410   2290    280     60    -60       N  
ATOM   2075  CA  LYS C 299     -21.327  -8.548 -53.583  1.00 18.95           C  
ANISOU 2075  CA  LYS C 299     2170   2600   2420    300    100    -40       C  
ATOM   2076  C   LYS C 299     -21.183 -10.074 -53.570  1.00 18.65           C  
ANISOU 2076  C   LYS C 299     2090   2580   2410    230    120      0       C  
ATOM   2077  O   LYS C 299     -21.663 -10.684 -52.588  1.00 19.18           O  
ANISOU 2077  O   LYS C 299     2100   2700   2480    230    170     30       O  
ATOM   2078  CB  LYS C 299     -22.738  -8.134 -54.017  1.00 20.82           C  
ANISOU 2078  CB  LYS C 299     2350   2860   2700    340     90    -30       C  
ATOM   2079  CG  LYS C 299     -23.052  -6.656 -53.829  1.00 22.45           C  
ANISOU 2079  CG  LYS C 299     2580   3050   2900    430     90    -60       C  
ATOM   2080  CD  LYS C 299     -22.814  -6.200 -52.404  1.00 24.26           C  
ANISOU 2080  CD  LYS C 299     2830   3300   3090    480    140   -100       C  
ATOM   2081  CE  LYS C 299     -22.995  -4.715 -52.191  1.00 25.65           C  
ANISOU 2081  CE  LYS C 299     3040   3440   3270    560    120   -160       C  
ATOM   2082  NZ  LYS C 299     -22.559  -4.330 -50.826  1.00 27.29           N  
ANISOU 2082  NZ  LYS C 299     3270   3670   3420    610    160   -220       N  
ATOM   2083  N   HIS C 300     -20.574 -10.671 -54.598  1.00 17.74           N  
ANISOU 2083  N   HIS C 300     2000   2430   2310    170     80      0       N  
ATOM   2084  CA  HIS C 300     -20.402 -12.150 -54.609  1.00 17.75           C  
ANISOU 2084  CA  HIS C 300     1960   2430   2350    100     80     30       C  
ATOM   2085  C   HIS C 300     -18.939 -12.513 -54.342  1.00 16.49           C  
ANISOU 2085  C   HIS C 300     1870   2250   2150     70     90     20       C  
ATOM   2086  O   HIS C 300     -18.555 -13.657 -54.634  1.00 16.01           O  
ANISOU 2086  O   HIS C 300     1800   2170   2120     10     90     40       O  
ATOM   2087  CB  HIS C 300     -20.967 -12.753 -55.901  1.00 18.38           C  
ANISOU 2087  CB  HIS C 300     2000   2500   2480     70     30     20       C  
ATOM   2088  CG  HIS C 300     -22.451 -12.674 -55.935  1.00 19.57           C  
ANISOU 2088  CG  HIS C 300     2060   2690   2690    100     20     30       C  
ATOM   2089  ND1 HIS C 300     -23.117 -11.597 -56.476  1.00 20.70           N  
ANISOU 2089  ND1 HIS C 300     2200   2840   2820    150    -10     10       N  
ATOM   2090  CD2 HIS C 300     -23.393 -13.509 -55.448  1.00 20.43           C  
ANISOU 2090  CD2 HIS C 300     2070   2820   2870     80     50     60       C  
ATOM   2091  CE1 HIS C 300     -24.412 -11.780 -56.337  1.00 21.38           C  
ANISOU 2091  CE1 HIS C 300     2190   2970   2960    170      0     20       C  
ATOM   2092  NE2 HIS C 300     -24.611 -12.948 -55.711  1.00 21.40           N  
ANISOU 2092  NE2 HIS C 300     2130   2980   3020    120     40     60       N  
ATOM   2093  N   TRP C 301     -18.177 -11.581 -53.766  1.00 16.21           N  
ANISOU 2093  N   TRP C 301     1900   2210   2050    100    110      0       N  
ATOM   2094  CA  TRP C 301     -16.744 -11.820 -53.451  1.00 15.41           C  
ANISOU 2094  CA  TRP C 301     1860   2090   1910     70    110    -10       C  
ATOM   2095  C   TRP C 301     -16.564 -13.037 -52.541  1.00 15.67           C  
ANISOU 2095  C   TRP C 301     1860   2150   1940     50    150     30       C  
ATOM   2096  O   TRP C 301     -15.644 -13.824 -52.766  1.00 16.78           O  
ANISOU 2096  O   TRP C 301     2020   2270   2090     10    150     40       O  
ATOM   2097  CB  TRP C 301     -16.074 -10.572 -52.864  1.00 15.29           C  
ANISOU 2097  CB  TRP C 301     1900   2060   1850    110    110    -60       C  
ATOM   2098  CG  TRP C 301     -14.662 -10.862 -52.466  1.00 14.88           C  
ANISOU 2098  CG  TRP C 301     1890   2000   1760     80    110    -70       C  
ATOM   2099  CD1 TRP C 301     -14.179 -11.055 -51.205  1.00 14.96           C  
ANISOU 2099  CD1 TRP C 301     1900   2060   1730    110    140    -80       C  
ATOM   2100  CD2 TRP C 301     -13.573 -11.149 -53.359  1.00 14.11           C  
ANISOU 2100  CD2 TRP C 301     1830   1860   1670     30     80    -70       C  
ATOM   2101  NE1 TRP C 301     -12.846 -11.365 -51.252  1.00 14.34           N  
ANISOU 2101  NE1 TRP C 301     1860   1960   1630     70    130    -90       N  
ATOM   2102  CE2 TRP C 301     -12.447 -11.435 -52.558  1.00 13.87           C  
ANISOU 2102  CE2 TRP C 301     1820   1850   1600     20    100    -90       C  
ATOM   2103  CE3 TRP C 301     -13.434 -11.166 -54.749  1.00 14.00           C  
ANISOU 2103  CE3 TRP C 301     1830   1810   1680      0     50    -60       C  
ATOM   2104  CZ2 TRP C 301     -11.200 -11.731 -53.104  1.00 13.55           C  
ANISOU 2104  CZ2 TRP C 301     1810   1780   1560    -20     80    -90       C  
ATOM   2105  CZ3 TRP C 301     -12.204 -11.471 -55.292  1.00 13.73           C  
ANISOU 2105  CZ3 TRP C 301     1830   1750   1640    -40     40    -70       C  
ATOM   2106  CH2 TRP C 301     -11.103 -11.745 -54.477  1.00 13.67           C  
ANISOU 2106  CH2 TRP C 301     1840   1750   1600    -50     50    -80       C  
ATOM   2107  N   PRO C 302     -17.383 -13.256 -51.484  1.00 16.14           N  
ANISOU 2107  N   PRO C 302     1860   2270   2000     90    210     70       N  
ATOM   2108  CA  PRO C 302     -17.199 -14.430 -50.630  1.00 16.30           C  
ANISOU 2108  CA  PRO C 302     1840   2320   2020     80    260    130       C  
ATOM   2109  C   PRO C 302     -17.231 -15.751 -51.419  1.00 16.10           C  
ANISOU 2109  C   PRO C 302     1780   2250   2090     10    240    170       C  
ATOM   2110  O   PRO C 302     -16.447 -16.617 -51.084  1.00 16.28           O  
ANISOU 2110  O   PRO C 302     1820   2260   2110    -20    260    200       O  
ATOM   2111  CB  PRO C 302     -18.356 -14.345 -49.616  1.00 17.23           C  
ANISOU 2111  CB  PRO C 302     1890   2520   2140    130    320    180       C  
ATOM   2112  CG  PRO C 302     -18.722 -12.870 -49.605  1.00 17.41           C  
ANISOU 2112  CG  PRO C 302     1940   2560   2120    190    300    110       C  
ATOM   2113  CD  PRO C 302     -18.508 -12.419 -51.035  1.00 16.87           C  
ANISOU 2113  CD  PRO C 302     1920   2410   2090    150    230     60       C  
ATOM   2114  N   GLN C 303     -18.086 -15.861 -52.451  1.00 16.06           N  
ANISOU 2114  N   GLN C 303     1740   2210   2160    -20    200    150       N  
ATOM   2115  CA  GLN C 303     -18.177 -17.112 -53.259  1.00 16.23           C  
ANISOU 2115  CA  GLN C 303     1720   2180   2270    -90    180    160       C  
ATOM   2116  C   GLN C 303     -16.927 -17.274 -54.129  1.00 15.48           C  
ANISOU 2116  C   GLN C 303     1700   2040   2150   -120    130    110       C  
ATOM   2117  O   GLN C 303     -16.724 -18.377 -54.664  1.00 16.04           O  
ANISOU 2117  O   GLN C 303     1750   2060   2290   -160    100    110       O  
ATOM   2118  CB  GLN C 303     -19.483 -17.187 -54.052  1.00 17.12           C  
ANISOU 2118  CB  GLN C 303     1760   2280   2470   -100    140    140       C  
ATOM   2119  CG  GLN C 303     -20.700 -17.497 -53.180  1.00 18.16           C  
ANISOU 2119  CG  GLN C 303     1790   2450   2660    -90    200    210       C  
ATOM   2120  CD  GLN C 303     -21.048 -16.401 -52.203  1.00 18.69           C  
ANISOU 2120  CD  GLN C 303     1870   2590   2650    -10    250    230       C  
ATOM   2121  OE1 GLN C 303     -21.305 -16.654 -51.022  1.00 19.79           O  
ANISOU 2121  OE1 GLN C 303     1960   2780   2770     10    330    300       O  
ATOM   2122  NE2 GLN C 303     -21.033 -15.168 -52.681  1.00 17.89           N  
ANISOU 2122  NE2 GLN C 303     1820   2500   2480     30    210    170       N  
ATOM   2123  N   ILE C 304     -16.132 -16.217 -54.282  1.00 14.68           N  
ANISOU 2123  N   ILE C 304     1670   1940   1960    -90    110     70       N  
ATOM   2124  CA  ILE C 304     -14.856 -16.338 -55.041  1.00 13.98           C  
ANISOU 2124  CA  ILE C 304     1640   1820   1840   -110     70     40       C  
ATOM   2125  C   ILE C 304     -13.754 -16.639 -54.016  1.00 13.65           C  
ANISOU 2125  C   ILE C 304     1630   1790   1760   -110    110     60       C  
ATOM   2126  O   ILE C 304     -12.954 -17.535 -54.270  1.00 13.46           O  
ANISOU 2126  O   ILE C 304     1620   1740   1750   -140    100     60       O  
ATOM   2127  CB  ILE C 304     -14.540 -15.069 -55.866  1.00 13.97           C  
ANISOU 2127  CB  ILE C 304     1700   1820   1790    -90     40    -10       C  
ATOM   2128  CG1 ILE C 304     -15.608 -14.801 -56.933  1.00 14.40           C  
ANISOU 2128  CG1 ILE C 304     1720   1870   1870    -80    -10    -20       C  
ATOM   2129  CG2 ILE C 304     -13.150 -15.168 -56.489  1.00 13.54           C  
ANISOU 2129  CG2 ILE C 304     1700   1740   1700   -110     20    -30       C  
ATOM   2130  CD1 ILE C 304     -15.420 -13.498 -57.678  1.00 14.50           C  
ANISOU 2130  CD1 ILE C 304     1790   1890   1840    -50    -30    -40       C  
ATOM   2131  N   ALA C 305     -13.749 -15.913 -52.892  1.00 14.02           N  
ANISOU 2131  N   ALA C 305     1690   1880   1750    -70    150     70       N  
ATOM   2132  CA  ALA C 305     -12.717 -16.044 -51.830  1.00 14.15           C  
ANISOU 2132  CA  ALA C 305     1730   1930   1710    -50    170     80       C  
ATOM   2133  C   ALA C 305     -12.649 -17.473 -51.279  1.00 14.20           C  
ANISOU 2133  C   ALA C 305     1700   1940   1760    -60    210    150       C  
ATOM   2134  O   ALA C 305     -11.543 -17.861 -50.828  1.00 14.46           O  
ANISOU 2134  O   ALA C 305     1760   1980   1750    -60    220    160       O  
ATOM   2135  CB  ALA C 305     -12.981 -15.045 -50.718  1.00 14.52           C  
ANISOU 2135  CB  ALA C 305     1780   2040   1690     10    200     70       C  
ATOM   2136  N   GLN C 306     -13.762 -18.214 -51.299  1.00 14.39           N  
ANISOU 2136  N   GLN C 306     1660   1950   1860    -80    230    200       N  
ATOM   2137  CA  GLN C 306     -13.764 -19.611 -50.778  1.00 15.24           C  
ANISOU 2137  CA  GLN C 306     1720   2040   2030   -100    280    280       C  
ATOM   2138  C   GLN C 306     -12.743 -20.464 -51.548  1.00 14.86           C  
ANISOU 2138  C   GLN C 306     1700   1930   2020   -140    240    260       C  
ATOM   2139  O   GLN C 306     -12.376 -21.539 -51.032  1.00 15.21           O  
ANISOU 2139  O   GLN C 306     1720   1950   2100   -140    270    330       O  
ATOM   2140  CB  GLN C 306     -15.155 -20.245 -50.858  1.00 16.13           C  
ANISOU 2140  CB  GLN C 306     1740   2130   2250   -120    300    340       C  
ATOM   2141  CG  GLN C 306     -15.710 -20.365 -52.272  1.00 16.36           C  
ANISOU 2141  CG  GLN C 306     1750   2100   2370   -170    240    270       C  
ATOM   2142  CD  GLN C 306     -17.057 -21.051 -52.302  1.00 17.44           C  
ANISOU 2142  CD  GLN C 306     1790   2210   2630   -200    250    320       C  
ATOM   2143  OE1 GLN C 306     -17.335 -21.942 -51.507  1.00 18.25           O  
ANISOU 2143  OE1 GLN C 306     1830   2300   2800   -200    310    410       O  
ATOM   2144  NE2 GLN C 306     -17.887 -20.684 -53.265  1.00 17.26           N  
ANISOU 2144  NE2 GLN C 306     1740   2170   2650   -210    200    260       N  
ATOM   2145  N   PHE C 307     -12.279 -19.993 -52.711  1.00 14.03           N  
ANISOU 2145  N   PHE C 307     1640   1790   1900   -160    180    180       N  
ATOM   2146  CA  PHE C 307     -11.295 -20.788 -53.494  1.00 14.19           C  
ANISOU 2146  CA  PHE C 307     1680   1760   1950   -190    150    150       C  
ATOM   2147  C   PHE C 307      -9.881 -20.241 -53.290  1.00 13.82           C  
ANISOU 2147  C   PHE C 307     1700   1750   1810   -170    140    120       C  
ATOM   2148  O   PHE C 307      -8.938 -20.921 -53.712  1.00 14.31           O  
ANISOU 2148  O   PHE C 307     1780   1780   1880   -180    130    110       O  
ATOM   2149  CB  PHE C 307     -11.709 -20.861 -54.961  1.00 14.31           C  
ANISOU 2149  CB  PHE C 307     1690   1740   2010   -220     90     80       C  
ATOM   2150  CG  PHE C 307     -13.031 -21.556 -55.155  1.00 14.64           C  
ANISOU 2150  CG  PHE C 307     1660   1740   2160   -240     80    100       C  
ATOM   2151  CD1 PHE C 307     -13.125 -22.930 -55.020  1.00 15.09           C  
ANISOU 2151  CD1 PHE C 307     1670   1740   2330   -270     90    130       C  
ATOM   2152  CD2 PHE C 307     -14.173 -20.841 -55.474  1.00 14.79           C  
ANISOU 2152  CD2 PHE C 307     1650   1780   2190   -240     70     80       C  
ATOM   2153  CE1 PHE C 307     -14.344 -23.571 -55.170  1.00 16.01           C  
ANISOU 2153  CE1 PHE C 307     1700   1810   2570   -300     90    140       C  
ATOM   2154  CE2 PHE C 307     -15.387 -21.487 -55.642  1.00 15.32           C  
ANISOU 2154  CE2 PHE C 307     1630   1820   2370   -260     60     90       C  
ATOM   2155  CZ  PHE C 307     -15.473 -22.848 -55.481  1.00 16.16           C  
ANISOU 2155  CZ  PHE C 307     1680   1860   2600   -300     70    120       C  
ATOM   2156  N   ALA C 308      -9.736 -19.077 -52.649  1.00 13.45           N  
ANISOU 2156  N   ALA C 308     1680   1750   1680   -140    150    110       N  
ATOM   2157  CA  ALA C 308      -8.375 -18.541 -52.417  1.00 13.22           C  
ANISOU 2157  CA  ALA C 308     1700   1750   1580   -130    140     80       C  
ATOM   2158  C   ALA C 308      -7.717 -19.384 -51.326  1.00 13.47           C  
ANISOU 2158  C   ALA C 308     1720   1810   1590   -100    170    130       C  
ATOM   2159  O   ALA C 308      -8.354 -19.737 -50.336  1.00 13.57           O  
ANISOU 2159  O   ALA C 308     1700   1860   1600    -70    210    190       O  
ATOM   2160  CB  ALA C 308      -8.429 -17.076 -52.052  1.00 13.35           C  
ANISOU 2160  CB  ALA C 308     1740   1800   1540   -100    130     40       C  
ATOM   2161  N   PRO C 309      -6.425 -19.746 -51.466  1.00 12.99           N  
ANISOU 2161  N   PRO C 309     1680   1740   1510   -110    160    120       N  
ATOM   2162  CA  PRO C 309      -5.763 -20.564 -50.458  1.00 12.81           C  
ANISOU 2162  CA  PRO C 309     1650   1750   1470    -80    180    170       C  
ATOM   2163  C   PRO C 309      -5.207 -19.833 -49.230  1.00 13.03           C  
ANISOU 2163  C   PRO C 309     1680   1870   1400    -20    190    160       C  
ATOM   2164  O   PRO C 309      -4.777 -18.688 -49.343  1.00 12.82           O  
ANISOU 2164  O   PRO C 309     1680   1860   1330    -30    160     90       O  
ATOM   2165  CB  PRO C 309      -4.559 -21.120 -51.232  1.00 12.79           C  
ANISOU 2165  CB  PRO C 309     1660   1710   1490   -100    160    140       C  
ATOM   2166  CG  PRO C 309      -4.206 -20.017 -52.200  1.00 12.50           C  
ANISOU 2166  CG  PRO C 309     1660   1670   1430   -130    120     70       C  
ATOM   2167  CD  PRO C 309      -5.543 -19.424 -52.605  1.00 12.66           C  
ANISOU 2167  CD  PRO C 309     1670   1670   1470   -140    120     60       C  
ATOM   2168  N   SER C 310      -5.246 -20.515 -48.082  1.00 12.98           N  
ANISOU 2168  N   SER C 310     1650   1920   1360     30    230    240       N  
ATOM   2169  CA  SER C 310      -4.645 -19.970 -46.844  1.00 13.07           C  
ANISOU 2169  CA  SER C 310     1670   2030   1260     90    230    230       C  
ATOM   2170  C   SER C 310      -3.139 -19.862 -47.119  1.00 12.58           C  
ANISOU 2170  C   SER C 310     1630   1970   1180     80    180    170       C  
ATOM   2171  O   SER C 310      -2.688 -20.451 -48.120  1.00 11.62           O  
ANISOU 2171  O   SER C 310     1520   1780   1130     30    170    170       O  
ATOM   2172  CB  SER C 310      -4.898 -20.891 -45.686  1.00 13.54           C  
ANISOU 2172  CB  SER C 310     1700   2160   1290    150    280    340       C  
ATOM   2173  OG  SER C 310      -4.204 -22.110 -45.905  1.00 13.37           O  
ANISOU 2173  OG  SER C 310     1670   2090   1320    140    290    400       O  
ATOM   2174  N   ALA C 311      -2.380 -19.161 -46.279  1.00 13.15           N  
ANISOU 2174  N   ALA C 311     1710   2120   1170    120    150    110       N  
ATOM   2175  CA  ALA C 311      -0.922 -19.087 -46.538  1.00 12.85           C  
ANISOU 2175  CA  ALA C 311     1670   2090   1120    110    110     60       C  
ATOM   2176  C   ALA C 311      -0.333 -20.502 -46.461  1.00 12.91           C  
ANISOU 2176  C   ALA C 311     1670   2090   1150    130    130    140       C  
ATOM   2177  O   ALA C 311       0.542 -20.832 -47.288  1.00 12.84           O  
ANISOU 2177  O   ALA C 311     1660   2030   1180     90    110    120       O  
ATOM   2178  CB  ALA C 311      -0.263 -18.154 -45.554  1.00 13.30           C  
ANISOU 2178  CB  ALA C 311     1730   2240   1090    160     70    -20       C  
ATOM   2179  N   SER C 312      -0.821 -21.308 -45.514  1.00 13.18           N  
ANISOU 2179  N   SER C 312     1680   2170   1150    190    170    240       N  
ATOM   2180  CA  SER C 312      -0.341 -22.701 -45.316  1.00 13.42           C  
ANISOU 2180  CA  SER C 312     1700   2200   1210    210    200    340       C  
ATOM   2181  C   SER C 312      -0.604 -23.528 -46.585  1.00 12.88           C  
ANISOU 2181  C   SER C 312     1630   1990   1270    140    210    360       C  
ATOM   2182  O   SER C 312       0.321 -24.221 -47.039  1.00 12.49           O  
ANISOU 2182  O   SER C 312     1580   1910   1260    140    190    360       O  
ATOM   2183  CB  SER C 312      -0.997 -23.319 -44.089  1.00 14.30           C  
ANISOU 2183  CB  SER C 312     1780   2380   1270    290    260    460       C  
ATOM   2184  OG  SER C 312      -0.435 -24.588 -43.779  1.00 14.63           O  
ANISOU 2184  OG  SER C 312     1810   2410   1340    330    280    560       O  
ATOM   2185  N   ALA C 313      -1.814 -23.423 -47.147  1.00 12.74           N  
ANISOU 2185  N   ALA C 313     1610   1910   1310    100    230    360       N  
ATOM   2186  CA  ALA C 313      -2.187 -24.182 -48.368  1.00 12.74           C  
ANISOU 2186  CA  ALA C 313     1610   1790   1440     40    230    360       C  
ATOM   2187  C   ALA C 313      -1.406 -23.654 -49.574  1.00 12.18           C  
ANISOU 2187  C   ALA C 313     1570   1690   1370      0    180    260       C  
ATOM   2188  O   ALA C 313      -1.021 -24.463 -50.423  1.00 12.03           O  
ANISOU 2188  O   ALA C 313     1550   1600   1420    -30    170    250       O  
ATOM   2189  CB  ALA C 313      -3.678 -24.096 -48.604  1.00 12.70           C  
ANISOU 2189  CB  ALA C 313     1590   1750   1490     10    250    380       C  
ATOM   2190  N   PHE C 314      -1.207 -22.336 -49.656  1.00 12.14           N  
ANISOU 2190  N   PHE C 314     1580   1730   1300    -10    150    180       N  
ATOM   2191  CA  PHE C 314      -0.451 -21.774 -50.802  1.00 11.91           C  
ANISOU 2191  CA  PHE C 314     1570   1670   1280    -60    120    100       C  
ATOM   2192  C   PHE C 314       0.934 -22.426 -50.864  1.00 12.42           C  
ANISOU 2192  C   PHE C 314     1630   1750   1340    -40    100    100       C  
ATOM   2193  O   PHE C 314       1.370 -22.794 -51.967  1.00 12.67           O  
ANISOU 2193  O   PHE C 314     1670   1730   1410    -60     90     70       O  
ATOM   2194  CB  PHE C 314      -0.342 -20.252 -50.703  1.00 11.73           C  
ANISOU 2194  CB  PHE C 314     1560   1690   1210    -70     90     40       C  
ATOM   2195  CG  PHE C 314       0.455 -19.631 -51.820  1.00 11.34           C  
ANISOU 2195  CG  PHE C 314     1530   1610   1170   -110     70    -20       C  
ATOM   2196  CD1 PHE C 314      -0.127 -19.378 -53.054  1.00 10.94           C  
ANISOU 2196  CD1 PHE C 314     1490   1510   1160   -140     70    -30       C  
ATOM   2197  CD2 PHE C 314       1.793 -19.314 -51.642  1.00 11.29           C  
ANISOU 2197  CD2 PHE C 314     1510   1640   1140   -100     50    -50       C  
ATOM   2198  CE1 PHE C 314       0.614 -18.817 -54.084  1.00 10.87           C  
ANISOU 2198  CE1 PHE C 314     1490   1490   1150   -170     50    -70       C  
ATOM   2199  CE2 PHE C 314       2.532 -18.751 -52.670  1.00 11.22           C  
ANISOU 2199  CE2 PHE C 314     1500   1610   1150   -140     40    -90       C  
ATOM   2200  CZ  PHE C 314       1.939 -18.494 -53.886  1.00 11.11           C  
ANISOU 2200  CZ  PHE C 314     1510   1550   1170   -170     50    -90       C  
ATOM   2201  N   PHE C 315       1.611 -22.533 -49.716  1.00 12.69           N  
ANISOU 2201  N   PHE C 315     1650   1850   1320     10    100    130       N  
ATOM   2202  CA  PHE C 315       2.961 -23.147 -49.690  1.00 12.82           C  
ANISOU 2202  CA  PHE C 315     1650   1890   1330     30     90    130       C  
ATOM   2203  C   PHE C 315       2.881 -24.671 -49.604  1.00 13.07           C  
ANISOU 2203  C   PHE C 315     1670   1870   1420     60    120    210       C  
ATOM   2204  O   PHE C 315       3.911 -25.297 -49.884  1.00 13.27           O  
ANISOU 2204  O   PHE C 315     1690   1890   1460     80    110    200       O  
ATOM   2205  CB  PHE C 315       3.818 -22.536 -48.580  1.00 12.99           C  
ANISOU 2205  CB  PHE C 315     1660   2010   1270     80     70    100       C  
ATOM   2206  CG  PHE C 315       4.382 -21.199 -48.970  1.00 12.73           C  
ANISOU 2206  CG  PHE C 315     1620   1990   1220     40     30     10       C  
ATOM   2207  CD1 PHE C 315       5.520 -21.133 -49.757  1.00 12.61           C  
ANISOU 2207  CD1 PHE C 315     1590   1970   1230     10     10    -30       C  
ATOM   2208  CD2 PHE C 315       3.774 -20.019 -48.580  1.00 12.92           C  
ANISOU 2208  CD2 PHE C 315     1660   2040   1210     30     20    -40       C  
ATOM   2209  CE1 PHE C 315       6.036 -19.912 -50.151  1.00 12.54           C  
ANISOU 2209  CE1 PHE C 315     1580   1960   1230    -30    -10   -100       C  
ATOM   2210  CE2 PHE C 315       4.292 -18.797 -48.978  1.00 12.62           C  
ANISOU 2210  CE2 PHE C 315     1620   1990   1190    -20    -10   -120       C  
ATOM   2211  CZ  PHE C 315       5.428 -18.749 -49.752  1.00 12.49           C  
ANISOU 2211  CZ  PHE C 315     1580   1960   1210    -50    -30   -140       C  
ATOM   2212  N   GLY C 316       1.713 -25.234 -49.288  1.00 13.26           N  
ANISOU 2212  N   GLY C 316     1690   1860   1490     70    150    280       N  
ATOM   2213  CA  GLY C 316       1.598 -26.699 -49.178  1.00 13.96           C  
ANISOU 2213  CA  GLY C 316     1770   1880   1660     90    180    360       C  
ATOM   2214  C   GLY C 316       1.220 -27.371 -50.485  1.00 13.95           C  
ANISOU 2214  C   GLY C 316     1770   1760   1770     40    170    320       C  
ATOM   2215  O   GLY C 316       1.797 -28.422 -50.784  1.00 14.05           O  
ANISOU 2215  O   GLY C 316     1770   1720   1850     60    170    340       O  
ATOM   2216  N   MET C 317       0.305 -26.773 -51.251  1.00 14.04           N  
ANISOU 2216  N   MET C 317     1790   1740   1800    -10    160    270       N  
ATOM   2217  CA  MET C 317      -0.187 -27.378 -52.521  1.00 14.68           C  
ANISOU 2217  CA  MET C 317     1870   1730   1980    -50    140    220       C  
ATOM   2218  C   MET C 317       0.639 -26.960 -53.745  1.00 14.59           C  
ANISOU 2218  C   MET C 317     1880   1730   1940    -60    110    120       C  
ATOM   2219  O   MET C 317       0.794 -27.800 -54.665  1.00 15.89           O  
ANISOU 2219  O   MET C 317     2040   1830   2170    -60     90     80       O  
ATOM   2220  CB  MET C 317      -1.615 -26.901 -52.801  1.00 14.52           C  
ANISOU 2220  CB  MET C 317     1840   1680   1990    -90    140    210       C  
ATOM   2221  CG  MET C 317      -2.583 -27.089 -51.652  1.00 15.25           C  
ANISOU 2221  CG  MET C 317     1910   1780   2110    -80    190    310       C  
ATOM   2222  SD  MET C 317      -4.225 -26.459 -52.072  1.00 15.71           S  
ANISOU 2222  SD  MET C 317     1950   1820   2200   -120    190    290       S  
ATOM   2223  CE  MET C 317      -3.842 -24.764 -52.509  1.00 14.65           C  
ANISOU 2223  CE  MET C 317     1860   1770   1940   -130    150    200       C  
ATOM   2224  N   SER C 318       1.160 -25.732 -53.741  1.00 13.90           N  
ANISOU 2224  N   SER C 318     1810   1720   1760    -70    100     80       N  
ATOM   2225  CA  SER C 318       1.838 -25.158 -54.932  1.00 13.80           C  
ANISOU 2225  CA  SER C 318     1810   1720   1710    -80     70     10       C  
ATOM   2226  C   SER C 318       3.239 -25.691 -55.222  1.00 14.30           C  
ANISOU 2226  C   SER C 318     1860   1800   1770    -60     70    -10       C  
ATOM   2227  O   SER C 318       3.922 -26.229 -54.318  1.00 14.14           O  
ANISOU 2227  O   SER C 318     1830   1800   1740    -20     80     30       O  
ATOM   2228  CB  SER C 318       1.914 -23.659 -54.792  1.00 13.32           C  
ANISOU 2228  CB  SER C 318     1760   1720   1580   -110     70    -10       C  
ATOM   2229  OG  SER C 318       0.624 -23.104 -54.578  1.00 13.28           O  
ANISOU 2229  OG  SER C 318     1760   1700   1580   -120     70      0       O  
ATOM   2230  N   ARG C 319       3.616 -25.550 -56.491  1.00 14.25           N  
ANISOU 2230  N   ARG C 319     1870   1800   1750    -60     60    -80       N  
ATOM   2231  CA  ARG C 319       4.995 -25.862 -56.908  1.00 14.79           C  
ANISOU 2231  CA  ARG C 319     1920   1900   1800    -30     60   -100       C  
ATOM   2232  C   ARG C 319       5.654 -24.490 -56.862  1.00 14.67           C  
ANISOU 2232  C   ARG C 319     1900   1960   1720    -60     60   -110       C  
ATOM   2233  O   ARG C 319       5.232 -23.592 -57.628  1.00 14.20           O  
ANISOU 2233  O   ARG C 319     1860   1910   1630    -90     60   -130       O  
ATOM   2234  CB  ARG C 319       5.073 -26.633 -58.225  1.00 15.16           C  
ANISOU 2234  CB  ARG C 319     1970   1920   1880    -10     50   -160       C  
ATOM   2235  CG  ARG C 319       4.462 -28.022 -58.100  1.00 15.73           C  
ANISOU 2235  CG  ARG C 319     2040   1890   2040     10     40   -160       C  
ATOM   2236  CD  ARG C 319       4.829 -28.947 -59.227  1.00 15.96           C  
ANISOU 2236  CD  ARG C 319     2060   1890   2110     40     20   -240       C  
ATOM   2237  NE  ARG C 319       6.271 -29.122 -59.287  1.00 15.79           N  
ANISOU 2237  NE  ARG C 319     2030   1920   2050     80     30   -250       N  
ATOM   2238  CZ  ARG C 319       6.975 -29.978 -58.550  1.00 15.70           C  
ANISOU 2238  CZ  ARG C 319     2000   1890   2080    120     40   -210       C  
ATOM   2239  NH1 ARG C 319       8.288 -30.042 -58.694  1.00 15.77           N  
ANISOU 2239  NH1 ARG C 319     1990   1950   2050    160     50   -230       N  
ATOM   2240  NH2 ARG C 319       6.378 -30.756 -57.666  1.00 15.77           N  
ANISOU 2240  NH2 ARG C 319     2000   1810   2170    130     40   -160       N  
ATOM   2241  N   ILE C 320       6.566 -24.331 -55.910  1.00 14.63           N  
ANISOU 2241  N   ILE C 320     1870   2000   1690    -40     60    -80       N  
ATOM   2242  CA  ILE C 320       7.259 -23.041 -55.658  1.00 14.36           C  
ANISOU 2242  CA  ILE C 320     1820   2020   1610    -70     60    -90       C  
ATOM   2243  C   ILE C 320       8.651 -23.057 -56.277  1.00 15.28           C  
ANISOU 2243  C   ILE C 320     1900   2180   1720    -60     70   -110       C  
ATOM   2244  O   ILE C 320       9.369 -24.073 -56.141  1.00 15.32           O  
ANISOU 2244  O   ILE C 320     1890   2190   1740    -10     70   -110       O  
ATOM   2245  CB  ILE C 320       7.354 -22.780 -54.141  1.00 14.29           C  
ANISOU 2245  CB  ILE C 320     1800   2050   1580    -60     50    -70       C  
ATOM   2246  CG1 ILE C 320       5.987 -22.816 -53.457  1.00 13.94           C  
ANISOU 2246  CG1 ILE C 320     1780   1970   1540    -50     50    -40       C  
ATOM   2247  CG2 ILE C 320       8.089 -21.479 -53.866  1.00 14.40           C  
ANISOU 2247  CG2 ILE C 320     1790   2110   1570    -80     30   -100       C  
ATOM   2248  CD1 ILE C 320       5.028 -21.767 -53.942  1.00 13.77           C  
ANISOU 2248  CD1 ILE C 320     1790   1930   1520   -100     50    -60       C  
ATOM   2249  N   GLY C 321       9.025 -21.922 -56.855  1.00 15.55           N  
ANISOU 2249  N   GLY C 321     1920   2240   1740   -100     80   -130       N  
ATOM   2250  CA  GLY C 321      10.349 -21.751 -57.462  1.00 16.91           C  
ANISOU 2250  CA  GLY C 321     2050   2460   1910   -100    100   -140       C  
ATOM   2251  C   GLY C 321      10.843 -20.349 -57.195  1.00 17.99           C  
ANISOU 2251  C   GLY C 321     2150   2620   2060   -150     90   -140       C  
ATOM   2252  O   GLY C 321      10.056 -19.529 -56.696  1.00 17.58           O  
ANISOU 2252  O   GLY C 321     2130   2540   2010   -180     80   -140       O  
ATOM   2253  N   MET C 322      12.123 -20.111 -57.431  1.00 19.35           N  
ANISOU 2253  N   MET C 322     2270   2840   2250   -150    110   -140       N  
ATOM   2254  CA  MET C 322      12.661 -18.752 -57.245  1.00 21.32           C  
ANISOU 2254  CA  MET C 322     2470   3090   2540   -210    100   -140       C  
ATOM   2255  C   MET C 322      13.490 -18.475 -58.494  1.00 22.55           C  
ANISOU 2255  C   MET C 322     2590   3280   2700   -220    160   -110       C  
ATOM   2256  O   MET C 322      14.303 -19.350 -58.879  1.00 22.54           O  
ANISOU 2256  O   MET C 322     2550   3320   2690   -180    170   -110       O  
ATOM   2257  CB  MET C 322      13.482 -18.616 -55.960  1.00 22.97           C  
ANISOU 2257  CB  MET C 322     2630   3340   2760   -210     60   -170       C  
ATOM   2258  CG  MET C 322      13.907 -17.196 -55.703  1.00 24.37           C  
ANISOU 2258  CG  MET C 322     2760   3500   3000   -270     50   -200       C  
ATOM   2259  SD  MET C 322      14.428 -16.933 -54.006  1.00 25.63           S  
ANISOU 2259  SD  MET C 322     2870   3700   3170   -260    -30   -270       S  
ATOM   2260  CE  MET C 322      15.736 -18.147 -53.873  1.00 25.76           C  
ANISOU 2260  CE  MET C 322     2830   3800   3160   -210    -30   -260       C  
ATOM   2261  N   GLU C 323      13.243 -17.322 -59.109  1.00 22.65           N  
ANISOU 2261  N   GLU C 323     2600   3260   2750   -270    180    -80       N  
ATOM   2262  CA  GLU C 323      13.917 -16.946 -60.371  1.00 23.38           C  
ANISOU 2262  CA  GLU C 323     2650   3390   2840   -280    240    -30       C  
ATOM   2263  C   GLU C 323      14.596 -15.583 -60.192  1.00 21.79           C  
ANISOU 2263  C   GLU C 323     2380   3160   2740   -350    250    -10       C  
ATOM   2264  O   GLU C 323      13.965 -14.674 -59.651  1.00 21.03           O  
ANISOU 2264  O   GLU C 323     2300   3000   2680   -400    230    -20       O  
ATOM   2265  CB  GLU C 323      12.823 -16.996 -61.441  1.00 25.16           C  
ANISOU 2265  CB  GLU C 323     2940   3600   3010   -260    270      0       C  
ATOM   2266  CG  GLU C 323      13.294 -16.864 -62.869  1.00 29.30           C  
ANISOU 2266  CG  GLU C 323     3440   4190   3500   -240    340     60       C  
ATOM   2267  CD  GLU C 323      12.167 -17.082 -63.867  1.00 30.60           C  
ANISOU 2267  CD  GLU C 323     3670   4360   3590   -190    350     70       C  
ATOM   2268  OE1 GLU C 323      11.103 -17.577 -63.451  1.00 31.79           O  
ANISOU 2268  OE1 GLU C 323     3880   4470   3730   -180    300     20       O  
ATOM   2269  OE2 GLU C 323      12.352 -16.751 -65.052  1.00 39.15           O  
ANISOU 2269  OE2 GLU C 323     4740   5490   4640   -170    400    120       O  
ATOM   2270  N   VAL C 324      15.863 -15.483 -60.585  1.00 21.88           N  
ANISOU 2270  N   VAL C 324     2190   3160   2960     50    180    520       N  
ATOM   2271  CA  VAL C 324      16.626 -14.205 -60.494  1.00 21.64           C  
ANISOU 2271  CA  VAL C 324     2080   3120   3030     10    150    520       C  
ATOM   2272  C   VAL C 324      16.743 -13.664 -61.923  1.00 21.01           C  
ANISOU 2272  C   VAL C 324     2000   2980   3000     10    190    570       C  
ATOM   2273  O   VAL C 324      17.394 -14.325 -62.743  1.00 21.37           O  
ANISOU 2273  O   VAL C 324     2050   3030   3040     60    240    650       O  
ATOM   2274  CB  VAL C 324      18.002 -14.411 -59.832  1.00 22.07           C  
ANISOU 2274  CB  VAL C 324     2060   3220   3100     20    130    540       C  
ATOM   2275  CG1 VAL C 324      18.839 -13.140 -59.845  1.00 22.63           C  
ANISOU 2275  CG1 VAL C 324     2040   3280   3280    -20    100    540       C  
ATOM   2276  CG2 VAL C 324      17.863 -14.942 -58.414  1.00 21.84           C  
ANISOU 2276  CG2 VAL C 324     2030   3260   3000     20     90    490       C  
ATOM   2277  N   THR C 325      16.116 -12.518 -62.197  1.00 19.92           N  
ANISOU 2277  N   THR C 325     1850   2800   2920    -20    180    540       N  
ATOM   2278  CA  THR C 325      16.132 -11.920 -63.555  1.00 19.42           C  
ANISOU 2278  CA  THR C 325     1780   2680   2910    -10    220    600       C  
ATOM   2279  C   THR C 325      16.550 -10.455 -63.468  1.00 19.19           C  
ANISOU 2279  C   THR C 325     1670   2610   3010    -60    200    590       C  
ATOM   2280  O   THR C 325      16.756  -9.931 -62.377  1.00 18.99           O  
ANISOU 2280  O   THR C 325     1600   2600   3020   -100    140    530       O  
ATOM   2281  CB  THR C 325      14.743 -12.030 -64.194  1.00 18.96           C  
ANISOU 2281  CB  THR C 325     1800   2600   2800      0    240    570       C  
ATOM   2282  OG1 THR C 325      13.908 -11.045 -63.591  1.00 18.95           O  
ANISOU 2282  OG1 THR C 325     1790   2570   2840    -50    200    500       O  
ATOM   2283  CG2 THR C 325      14.146 -13.412 -64.054  1.00 18.80           C  
ANISOU 2283  CG2 THR C 325     1860   2610   2680     30    260    560       C  
ATOM   2284  N   PRO C 326      16.689  -9.750 -64.614  1.00 18.86           N  
ANISOU 2284  N   PRO C 326     1600   2530   3030    -50    240    650       N  
ATOM   2285  CA  PRO C 326      17.063  -8.335 -64.608  1.00 19.04           C  
ANISOU 2285  CA  PRO C 326     1540   2500   3190    -90    220    650       C  
ATOM   2286  C   PRO C 326      16.036  -7.467 -63.863  1.00 18.46           C  
ANISOU 2286  C   PRO C 326     1480   2400   3140   -140    180    550       C  
ATOM   2287  O   PRO C 326      16.391  -6.401 -63.424  1.00 18.69           O  
ANISOU 2287  O   PRO C 326     1440   2390   3280   -190    150    520       O  
ATOM   2288  CB  PRO C 326      17.114  -7.967 -66.103  1.00 19.29           C  
ANISOU 2288  CB  PRO C 326     1570   2500   3260    -60    290    740       C  
ATOM   2289  CG  PRO C 326      17.351  -9.297 -66.799  1.00 19.21           C  
ANISOU 2289  CG  PRO C 326     1620   2540   3140     10    340    800       C  
ATOM   2290  CD  PRO C 326      16.541 -10.281 -65.978  1.00 18.72           C  
ANISOU 2290  CD  PRO C 326     1630   2510   2970     10    310    720       C  
ATOM   2291  N   SER C 327      14.794  -7.948 -63.739  1.00 17.55           N  
ANISOU 2291  N   SER C 327     1450   2290   2930   -130    170    500       N  
ATOM   2292  CA  SER C 327      13.748  -7.169 -63.026  1.00 17.35           C  
ANISOU 2292  CA  SER C 327     1430   2240   2920   -170    130    410       C  
ATOM   2293  C   SER C 327      13.836  -7.412 -61.514  1.00 17.44           C  
ANISOU 2293  C   SER C 327     1430   2290   2900   -200     70    330       C  
ATOM   2294  O   SER C 327      13.205  -6.646 -60.773  1.00 17.65           O  
ANISOU 2294  O   SER C 327     1450   2300   2960   -240     30    250       O  
ATOM   2295  CB  SER C 327      12.366  -7.480 -63.555  1.00 16.80           C  
ANISOU 2295  CB  SER C 327     1440   2160   2780   -150    160    400       C  
ATOM   2296  OG  SER C 327      12.045  -8.862 -63.415  1.00 16.07           O  
ANISOU 2296  OG  SER C 327     1420   2120   2570   -120    160    400       O  
ATOM   2297  N   GLY C 328      14.561  -8.453 -61.075  1.00 17.23           N  
ANISOU 2297  N   GLY C 328     1410   2330   2810   -180     60    340       N  
ATOM   2298  CA  GLY C 328      14.684  -8.734 -59.630  1.00 17.21           C  
ANISOU 2298  CA  GLY C 328     1390   2380   2770   -190      0    270       C  
ATOM   2299  C   GLY C 328      14.589 -10.216 -59.293  1.00 16.73           C  
ANISOU 2299  C   GLY C 328     1390   2380   2590   -150     10    290       C  
ATOM   2300  O   GLY C 328      14.857 -11.060 -60.180  1.00 16.27           O  
ANISOU 2300  O   GLY C 328     1360   2330   2490   -110     70    360       O  
ATOM   2301  N   THR C 329      14.243 -10.523 -58.038  1.00 16.59           N  
ANISOU 2301  N   THR C 329     1380   2420   2510   -150    -30    220       N  
ATOM   2302  CA  THR C 329      14.117 -11.929 -57.568  1.00 16.21           C  
ANISOU 2302  CA  THR C 329     1380   2430   2350   -110    -20    240       C  
ATOM   2303  C   THR C 329      12.625 -12.219 -57.465  1.00 15.70           C  
ANISOU 2303  C   THR C 329     1390   2350   2220   -100    -10    200       C  
ATOM   2304  O   THR C 329      11.933 -11.455 -56.758  1.00 15.59           O  
ANISOU 2304  O   THR C 329     1370   2340   2220   -130    -50    130       O  
ATOM   2305  CB  THR C 329      14.888 -12.157 -56.262  1.00 16.82           C  
ANISOU 2305  CB  THR C 329     1400   2580   2400   -100    -70    210       C  
ATOM   2306  OG1 THR C 329      16.259 -11.824 -56.501  1.00 17.56           O  
ANISOU 2306  OG1 THR C 329     1420   2680   2570   -110    -70    250       O  
ATOM   2307  CG2 THR C 329      14.790 -13.578 -55.748  1.00 16.53           C  
ANISOU 2307  CG2 THR C 329     1410   2610   2260    -50    -50    230       C  
ATOM   2308  N   TRP C 330      12.167 -13.268 -58.151  1.00 15.19           N  
ANISOU 2308  N   TRP C 330     1390   2280   2100    -70     40    250       N  
ATOM   2309  CA  TRP C 330      10.725 -13.614 -58.175  1.00 15.04           C  
ANISOU 2309  CA  TRP C 330     1440   2240   2030    -70     50    220       C  
ATOM   2310  C   TRP C 330      10.460 -14.992 -57.580  1.00 15.13           C  
ANISOU 2310  C   TRP C 330     1500   2300   1950    -30     70    230       C  
ATOM   2311  O   TRP C 330      11.248 -15.919 -57.840  1.00 15.92           O  
ANISOU 2311  O   TRP C 330     1600   2420   2030      0    100    290       O  
ATOM   2312  CB  TRP C 330      10.206 -13.566 -59.618  1.00 14.71           C  
ANISOU 2312  CB  TRP C 330     1440   2140   2000    -60    100    250       C  
ATOM   2313  CG  TRP C 330      10.295 -12.217 -60.250  1.00 14.89           C  
ANISOU 2313  CG  TRP C 330     1430   2120   2110    -90     90    250       C  
ATOM   2314  CD1 TRP C 330      11.408 -11.627 -60.773  1.00 15.34           C  
ANISOU 2314  CD1 TRP C 330     1430   2160   2240   -100    100    300       C  
ATOM   2315  CD2 TRP C 330       9.211 -11.297 -60.461  1.00 14.63           C  
ANISOU 2315  CD2 TRP C 330     1410   2050   2100   -120     80    210       C  
ATOM   2316  NE1 TRP C 330      11.096 -10.395 -61.279  1.00 15.33           N  
ANISOU 2316  NE1 TRP C 330     1400   2110   2310   -120    100    290       N  
ATOM   2317  CE2 TRP C 330       9.756 -10.166 -61.107  1.00 15.04           C  
ANISOU 2317  CE2 TRP C 330     1410   2060   2250   -140     90    230       C  
ATOM   2318  CE3 TRP C 330       7.842 -11.317 -60.171  1.00 14.34           C  
ANISOU 2318  CE3 TRP C 330     1420   2000   2020   -130     80    160       C  
ATOM   2319  CZ2 TRP C 330       8.974  -9.066 -61.459  1.00 14.96           C  
ANISOU 2319  CZ2 TRP C 330     1400   2000   2290   -160     90    210       C  
ATOM   2320  CZ3 TRP C 330       7.069 -10.232 -60.525  1.00 14.24           C  
ANISOU 2320  CZ3 TRP C 330     1410   1950   2060   -150     70    140       C  
ATOM   2321  CH2 TRP C 330       7.632  -9.123 -61.157  1.00 14.54           C  
ANISOU 2321  CH2 TRP C 330     1400   1940   2190   -170     80    160       C  
ATOM   2322  N   LEU C 331       9.371 -15.086 -56.818  1.00 15.10           N  
ANISOU 2322  N   LEU C 331     1530   2310   1900    -40     50    180       N  
ATOM   2323  CA  LEU C 331       8.905 -16.357 -56.225  1.00 15.20           C  
ANISOU 2323  CA  LEU C 331     1580   2350   1840      0     70    200       C  
ATOM   2324  C   LEU C 331       7.786 -16.825 -57.159  1.00 14.45           C  
ANISOU 2324  C   LEU C 331     1550   2200   1730      0    110    200       C  
ATOM   2325  O   LEU C 331       6.760 -16.125 -57.247  1.00 14.24           O  
ANISOU 2325  O   LEU C 331     1540   2150   1720    -30    100    160       O  
ATOM   2326  CB  LEU C 331       8.406 -16.115 -54.799  1.00 15.88           C  
ANISOU 2326  CB  LEU C 331     1650   2490   1890      0     30    140       C  
ATOM   2327  CG  LEU C 331       8.022 -17.366 -54.018  1.00 16.24           C  
ANISOU 2327  CG  LEU C 331     1720   2580   1860     40     50    160       C  
ATOM   2328  CD1 LEU C 331       9.246 -18.241 -53.797  1.00 17.14           C  
ANISOU 2328  CD1 LEU C 331     1810   2740   1960     70     70    220       C  
ATOM   2329  CD2 LEU C 331       7.394 -17.004 -52.681  1.00 16.75           C  
ANISOU 2329  CD2 LEU C 331     1780   2700   1890     40     10    110       C  
ATOM   2330  N   THR C 332       8.008 -17.922 -57.871  1.00 14.01           N  
ANISOU 2330  N   THR C 332     1530   2130   1660     30    160    260       N  
ATOM   2331  CA  THR C 332       7.016 -18.434 -58.845  1.00 13.33           C  
ANISOU 2331  CA  THR C 332     1500   2000   1560     30    190    260       C  
ATOM   2332  C   THR C 332       6.121 -19.470 -58.169  1.00 13.23           C  
ANISOU 2332  C   THR C 332     1530   1990   1500     50    210    250       C  
ATOM   2333  O   THR C 332       6.590 -20.148 -57.231  1.00 13.00           O  
ANISOU 2333  O   THR C 332     1490   2010   1450     70    210    270       O  
ATOM   2334  CB  THR C 332       7.710 -19.040 -60.070  1.00 13.28           C  
ANISOU 2334  CB  THR C 332     1510   1970   1560     60    240    310       C  
ATOM   2335  OG1 THR C 332       8.489 -20.146 -59.616  1.00 13.12           O  
ANISOU 2335  OG1 THR C 332     1490   1980   1520     90    260    350       O  
ATOM   2336  CG2 THR C 332       8.580 -18.051 -60.818  1.00 13.49           C  
ANISOU 2336  CG2 THR C 332     1500   1990   1640     50    230    330       C  
ATOM   2337  N   TYR C 333       4.883 -19.587 -58.647  1.00 13.01           N  
ANISOU 2337  N   TYR C 333     1550   1930   1470     30    220    220       N  
ATOM   2338  CA  TYR C 333       3.951 -20.573 -58.055  1.00 13.09           C  
ANISOU 2338  CA  TYR C 333     1590   1930   1450     40    230    220       C  
ATOM   2339  C   TYR C 333       2.984 -21.091 -59.119  1.00 13.14           C  
ANISOU 2339  C   TYR C 333     1650   1890   1460     40    260    210       C  
ATOM   2340  O   TYR C 333       2.576 -20.320 -60.011  1.00 12.95           O  
ANISOU 2340  O   TYR C 333     1630   1840   1450     20    250    180       O  
ATOM   2341  CB  TYR C 333       3.202 -19.946 -56.878  1.00 13.11           C  
ANISOU 2341  CB  TYR C 333     1580   1970   1440     30    200    180       C  
ATOM   2342  CG  TYR C 333       2.306 -18.789 -57.235  1.00 12.84           C  
ANISOU 2342  CG  TYR C 333     1550   1910   1420    -10    170    130       C  
ATOM   2343  CD1 TYR C 333       0.995 -18.997 -57.622  1.00 12.55           C  
ANISOU 2343  CD1 TYR C 333     1550   1840   1380    -20    180    110       C  
ATOM   2344  CD2 TYR C 333       2.761 -17.485 -57.169  1.00 13.05           C  
ANISOU 2344  CD2 TYR C 333     1540   1940   1480    -30    140    110       C  
ATOM   2345  CE1 TYR C 333       0.159 -17.942 -57.949  1.00 12.46           C  
ANISOU 2345  CE1 TYR C 333     1540   1810   1390    -50    160     70       C  
ATOM   2346  CE2 TYR C 333       1.939 -16.417 -57.490  1.00 12.90           C  
ANISOU 2346  CE2 TYR C 333     1520   1900   1480    -60    120     70       C  
ATOM   2347  CZ  TYR C 333       0.633 -16.645 -57.881  1.00 12.49           C  
ANISOU 2347  CZ  TYR C 333     1510   1820   1420    -70    130     50       C  
ATOM   2348  OH  TYR C 333      -0.171 -15.592 -58.205  1.00 12.27           O  
ANISOU 2348  OH  TYR C 333     1480   1770   1410    -90    110     20       O  
ATOM   2349  N   THR C 334       2.681 -22.386 -59.039  1.00 13.77           N  
ANISOU 2349  N   THR C 334     1760   1950   1530     60    300    230       N  
ATOM   2350  CA  THR C 334       1.713 -23.065 -59.936  1.00 14.04           C  
ANISOU 2350  CA  THR C 334     1830   1930   1570     60    320    210       C  
ATOM   2351  C   THR C 334       0.979 -24.085 -59.073  1.00 14.37           C  
ANISOU 2351  C   THR C 334     1890   1970   1610     60    340    210       C  
ATOM   2352  O   THR C 334       1.609 -24.644 -58.145  1.00 14.52           O  
ANISOU 2352  O   THR C 334     1890   2010   1620     90    360    250       O  
ATOM   2353  CB  THR C 334       2.350 -23.770 -61.145  1.00 14.54           C  
ANISOU 2353  CB  THR C 334     1920   1970   1640     80    350    230       C  
ATOM   2354  OG1 THR C 334       3.173 -24.848 -60.698  1.00 16.09           O  
ANISOU 2354  OG1 THR C 334     2110   2170   1830    110    390    270       O  
ATOM   2355  CG2 THR C 334       3.182 -22.860 -62.017  1.00 14.66           C  
ANISOU 2355  CG2 THR C 334     1920   1990   1660     80    340    240       C  
ATOM   2356  N   GLY C 335      -0.299 -24.310 -59.355  1.00 14.24           N  
ANISOU 2356  N   GLY C 335     1900   1910   1600     40    340    180       N  
ATOM   2357  CA  GLY C 335      -1.056 -25.295 -58.577  1.00 14.32           C  
ANISOU 2357  CA  GLY C 335     1920   1910   1620     50    370    190       C  
ATOM   2358  C   GLY C 335      -2.450 -25.466 -59.125  1.00 14.51           C  
ANISOU 2358  C   GLY C 335     1970   1890   1660     20    370    150       C  
ATOM   2359  O   GLY C 335      -2.792 -24.806 -60.133  1.00 14.01           O  
ANISOU 2359  O   GLY C 335     1920   1810   1600      0    350    110       O  
ATOM   2360  N   ALA C 336      -3.230 -26.324 -58.481  1.00 14.84           N  
ANISOU 2360  N   ALA C 336     2010   1910   1720     30    390    170       N  
ATOM   2361  CA  ALA C 336      -4.608 -26.567 -58.942  1.00 15.46           C  
ANISOU 2361  CA  ALA C 336     2110   1940   1830      0    390    130       C  
ATOM   2362  C   ALA C 336      -5.460 -26.865 -57.716  1.00 15.87           C  
ANISOU 2362  C   ALA C 336     2140   2000   1890      0    400    150       C  
ATOM   2363  O   ALA C 336      -4.983 -27.561 -56.832  1.00 16.04           O  
ANISOU 2363  O   ALA C 336     2150   2030   1910     30    430    200       O  
ATOM   2364  CB  ALA C 336      -4.629 -27.694 -59.947  1.00 15.58           C  
ANISOU 2364  CB  ALA C 336     2150   1890   1880      0    420    110       C  
ATOM   2365  N   ILE C 337      -6.660 -26.303 -57.682  1.00 16.63           N  
ANISOU 2365  N   ILE C 337     2240   2090   1990    -30    380    120       N  
ATOM   2366  CA  ILE C 337      -7.610 -26.482 -56.551  1.00 17.77           C  
ANISOU 2366  CA  ILE C 337     2370   2250   2140    -30    390    140       C  
ATOM   2367  C   ILE C 337      -8.804 -27.253 -57.108  1.00 18.45           C  
ANISOU 2367  C   ILE C 337     2460   2270   2280    -50    410    120       C  
ATOM   2368  O   ILE C 337      -9.370 -26.804 -58.098  1.00 18.00           O  
ANISOU 2368  O   ILE C 337     2420   2190   2220    -80    380     70       O  
ATOM   2369  CB  ILE C 337      -7.953 -25.101 -55.960  1.00 17.61           C  
ANISOU 2369  CB  ILE C 337     2330   2280   2080    -40    350    120       C  
ATOM   2370  CG1 ILE C 337      -6.680 -24.449 -55.408  1.00 18.27           C  
ANISOU 2370  CG1 ILE C 337     2400   2430   2120    -10    330    140       C  
ATOM   2371  CG2 ILE C 337      -9.052 -25.183 -54.907  1.00 18.20           C  
ANISOU 2371  CG2 ILE C 337     2390   2370   2150    -30    360    140       C  
ATOM   2372  CD1 ILE C 337      -6.846 -23.025 -54.944  1.00 18.37           C  
ANISOU 2372  CD1 ILE C 337     2390   2490   2100    -20    290    110       C  
ATOM   2373  N   LYS C 338      -9.119 -28.397 -56.508  1.00 20.65           N  
ANISOU 2373  N   LYS C 338     2730   2520   2600    -40    450    160       N  
ATOM   2374  CA  LYS C 338     -10.236 -29.250 -56.984  1.00 22.47           C  
ANISOU 2374  CA  LYS C 338     2970   2680   2900    -70    470    140       C  
ATOM   2375  C   LYS C 338     -11.571 -28.754 -56.420  1.00 22.45           C  
ANISOU 2375  C   LYS C 338     2940   2690   2900    -90    460    140       C  
ATOM   2376  O   LYS C 338     -11.682 -28.604 -55.184  1.00 22.57           O  
ANISOU 2376  O   LYS C 338     2940   2740   2890    -60    470    190       O  
ATOM   2377  CB  LYS C 338      -9.971 -30.699 -56.566  1.00 25.11           C  
ANISOU 2377  CB  LYS C 338     3290   2960   3290    -40    530    190       C  
ATOM   2378  CG  LYS C 338     -11.050 -31.712 -56.930  1.00 27.52           C  
ANISOU 2378  CG  LYS C 338     3590   3180   3680    -70    560    170       C  
ATOM   2379  CD  LYS C 338     -10.648 -33.133 -56.585  1.00 29.84           C  
ANISOU 2379  CD  LYS C 338     3880   3420   4040    -40    620    230       C  
ATOM   2380  CE  LYS C 338     -11.756 -34.145 -56.783  1.00 33.08           C  
ANISOU 2380  CE  LYS C 338     4270   3740   4560    -70    650    220       C  
ATOM   2381  NZ  LYS C 338     -12.238 -34.161 -58.182  1.00 35.46           N  
ANISOU 2381  NZ  LYS C 338     4600   3990   4880   -120    610    120       N  
ATOM   2382  N   LEU C 339     -12.524 -28.449 -57.300  1.00 21.85           N  
ANISOU 2382  N   LEU C 339     2880   2580   2840   -130    430     80       N  
ATOM   2383  CA  LEU C 339     -13.869 -28.050 -56.817  1.00 22.69           C  
ANISOU 2383  CA  LEU C 339     2960   2700   2960   -140    420     80       C  
ATOM   2384  C   LEU C 339     -14.617 -29.335 -56.451  1.00 23.37           C  
ANISOU 2384  C   LEU C 339     3030   2720   3130   -150    470    110       C  
ATOM   2385  O   LEU C 339     -14.301 -30.387 -57.033  1.00 22.93           O  
ANISOU 2385  O   LEU C 339     2980   2610   3120   -150    490    100       O  
ATOM   2386  CB  LEU C 339     -14.635 -27.257 -57.878  1.00 22.61           C  
ANISOU 2386  CB  LEU C 339     2960   2690   2940   -180    370     10       C  
ATOM   2387  CG  LEU C 339     -14.171 -25.825 -58.115  1.00 22.90           C  
ANISOU 2387  CG  LEU C 339     3010   2780   2900   -180    330    -10       C  
ATOM   2388  CD1 LEU C 339     -12.790 -25.787 -58.741  1.00 23.33           C  
ANISOU 2388  CD1 LEU C 339     3090   2840   2930   -160    330    -20       C  
ATOM   2389  CD2 LEU C 339     -15.178 -25.095 -58.988  1.00 22.70           C  
ANISOU 2389  CD2 LEU C 339     2990   2760   2880   -210    300    -70       C  
ATOM   2390  N   ASP C 340     -15.556 -29.243 -55.510  1.00 24.17           N  
ANISOU 2390  N   ASP C 340     3100   2840   3240   -150    480    150       N  
ATOM   2391  CA  ASP C 340     -16.344 -30.419 -55.067  1.00 25.47           C  
ANISOU 2391  CA  ASP C 340     3240   2940   3490   -150    530    190       C  
ATOM   2392  C   ASP C 340     -17.575 -30.539 -55.975  1.00 26.51           C  
ANISOU 2392  C   ASP C 340     3370   3020   3680   -200    510    130       C  
ATOM   2393  O   ASP C 340     -18.582 -29.852 -55.693  1.00 24.17           O  
ANISOU 2393  O   ASP C 340     3050   2760   3370   -220    490    130       O  
ATOM   2394  CB  ASP C 340     -16.717 -30.263 -53.594  1.00 27.23           C  
ANISOU 2394  CB  ASP C 340     3430   3220   3700   -110    560    270       C  
ATOM   2395  CG  ASP C 340     -17.531 -31.416 -53.047  1.00 28.77           C  
ANISOU 2395  CG  ASP C 340     3590   3350   3990   -110    620    330       C  
ATOM   2396  OD1 ASP C 340     -17.607 -32.461 -53.732  1.00 28.50           O  
ANISOU 2396  OD1 ASP C 340     3560   3230   4040   -140    640    310       O  
ATOM   2397  OD2 ASP C 340     -18.104 -31.244 -51.954  1.00 32.04           O  
ANISOU 2397  OD2 ASP C 340     3980   3810   4390    -80    640    390       O  
ATOM   2398  N   ASP C 341     -17.508 -31.413 -56.987  1.00 27.73           N  
ANISOU 2398  N   ASP C 341     3530   3110   3900   -230    510     80       N  
ATOM   2399  CA  ASP C 341     -18.629 -31.562 -57.957  1.00 31.19           C  
ANISOU 2399  CA  ASP C 341     3960   3500   4390   -280    480     10       C  
ATOM   2400  C   ASP C 341     -19.835 -32.239 -57.295  1.00 31.17           C  
ANISOU 2400  C   ASP C 341     3910   3450   4480   -290    520     50       C  
ATOM   2401  O   ASP C 341     -20.867 -32.357 -57.980  1.00 31.94           O  
ANISOU 2401  O   ASP C 341     3990   3510   4630   -340    490      0       O  
ATOM   2402  CB  ASP C 341     -18.165 -32.231 -59.258  1.00 33.80           C  
ANISOU 2402  CB  ASP C 341     4310   3770   4750   -290    470    -60       C  
ATOM   2403  CG  ASP C 341     -17.635 -33.648 -59.125  1.00 36.20           C  
ANISOU 2403  CG  ASP C 341     4610   4000   5140   -280    520    -40       C  
ATOM   2404  OD1 ASP C 341     -18.037 -34.349 -58.171  1.00 36.38           O  
ANISOU 2404  OD1 ASP C 341     4600   3990   5230   -280    570     30       O  
ATOM   2405  OD2 ASP C 341     -16.807 -34.034 -59.978  1.00 40.66           O  
ANISOU 2405  OD2 ASP C 341     5210   4540   5700   -280    520    -80       O  
ATOM   2406  N   LYS C 342     -19.714 -32.631 -56.020  1.00 31.94           N  
ANISOU 2406  N   LYS C 342     3990   3550   4600   -260    570    150       N  
ATOM   2407  CA  LYS C 342     -20.836 -33.270 -55.278  1.00 34.29           C  
ANISOU 2407  CA  LYS C 342     4240   3810   4980   -270    610    200       C  
ATOM   2408  C   LYS C 342     -21.586 -32.199 -54.473  1.00 31.63           C  
ANISOU 2408  C   LYS C 342     3880   3550   4580   -250    600    240       C  
ATOM   2409  O   LYS C 342     -22.677 -32.505 -53.954  1.00 32.29           O  
ANISOU 2409  O   LYS C 342     3920   3610   4730   -260    620    280       O  
ATOM   2410  CB  LYS C 342     -20.341 -34.391 -54.358  1.00 38.29           C  
ANISOU 2410  CB  LYS C 342     4720   4280   5550   -230    690    300       C  
ATOM   2411  CG  LYS C 342     -19.663 -35.559 -55.069  1.00 43.21           C  
ANISOU 2411  CG  LYS C 342     5360   4810   6250   -240    710    270       C  
ATOM   2412  CD  LYS C 342     -19.342 -36.736 -54.159  1.00 47.82           C  
ANISOU 2412  CD  LYS C 342     5910   5350   6910   -200    800    370       C  
ATOM   2413  CE  LYS C 342     -20.578 -37.394 -53.574  1.00 51.14           C  
ANISOU 2413  CE  LYS C 342     6270   5710   7450   -210    840    430       C  
ATOM   2414  NZ  LYS C 342     -20.232 -38.559 -52.726  1.00 53.06           N  
ANISOU 2414  NZ  LYS C 342     6480   5900   7780   -170    930    530       N  
ATOM   2415  N   ASP C 343     -21.008 -31.001 -54.361  1.00 28.78           N  
ANISOU 2415  N   ASP C 343     3550   3280   4110   -230    560    220       N  
ATOM   2416  CA  ASP C 343     -21.657 -29.881 -53.630  1.00 27.36           C  
ANISOU 2416  CA  ASP C 343     3360   3170   3860   -220    540    240       C  
ATOM   2417  C   ASP C 343     -22.809 -29.372 -54.497  1.00 25.32           C  
ANISOU 2417  C   ASP C 343     3100   2900   3620   -270    500    180       C  
ATOM   2418  O   ASP C 343     -22.612 -29.104 -55.682  1.00 23.46           O  
ANISOU 2418  O   ASP C 343     2890   2650   3380   -300    450    100       O  
ATOM   2419  CB  ASP C 343     -20.633 -28.791 -53.292  1.00 28.18           C  
ANISOU 2419  CB  ASP C 343     3500   3360   3850   -180    510    240       C  
ATOM   2420  CG  ASP C 343     -21.203 -27.579 -52.570  1.00 29.62           C  
ANISOU 2420  CG  ASP C 343     3670   3620   3970   -160    490    250       C  
ATOM   2421  OD1 ASP C 343     -22.435 -27.529 -52.382  1.00 29.61           O  
ANISOU 2421  OD1 ASP C 343     3640   3610   4000   -180    500    260       O  
ATOM   2422  OD2 ASP C 343     -20.406 -26.685 -52.208  1.00 31.85           O  
ANISOU 2422  OD2 ASP C 343     3970   3970   4160   -140    470    240       O  
ATOM   2423  N   PRO C 344     -24.048 -29.245 -53.956  1.00 23.82           N  
ANISOU 2423  N   PRO C 344     2870   2720   3460   -270    510    210       N  
ATOM   2424  CA  PRO C 344     -25.184 -28.761 -54.746  1.00 22.85           C  
ANISOU 2424  CA  PRO C 344     2730   2590   3360   -320    470    160       C  
ATOM   2425  C   PRO C 344     -24.937 -27.375 -55.371  1.00 21.45           C  
ANISOU 2425  C   PRO C 344     2590   2470   3080   -320    410     90       C  
ATOM   2426  O   PRO C 344     -25.576 -27.056 -56.358  1.00 20.63           O  
ANISOU 2426  O   PRO C 344     2490   2360   2990   -360    370     30       O  
ATOM   2427  CB  PRO C 344     -26.332 -28.672 -53.728  1.00 23.48           C  
ANISOU 2427  CB  PRO C 344     2770   2690   3470   -310    500    220       C  
ATOM   2428  CG  PRO C 344     -25.940 -29.631 -52.622  1.00 24.23           C  
ANISOU 2428  CG  PRO C 344     2840   2760   3600   -270    570    320       C  
ATOM   2429  CD  PRO C 344     -24.427 -29.568 -52.571  1.00 24.30           C  
ANISOU 2429  CD  PRO C 344     2890   2800   3540   -230    560    310       C  
ATOM   2430  N   ASN C 345     -24.019 -26.607 -54.774  1.00 19.84           N  
ANISOU 2430  N   ASN C 345     2420   2330   2790   -280    410    110       N  
ATOM   2431  CA  ASN C 345     -23.651 -25.237 -55.221  1.00 19.53           C  
ANISOU 2431  CA  ASN C 345     2410   2350   2670   -280    360     70       C  
ATOM   2432  C   ASN C 345     -22.620 -25.289 -56.366  1.00 18.73           C  
ANISOU 2432  C   ASN C 345     2340   2230   2550   -290    330     10       C  
ATOM   2433  O   ASN C 345     -22.387 -24.239 -56.984  1.00 17.61           O  
ANISOU 2433  O   ASN C 345     2220   2120   2350   -300    290    -30       O  
ATOM   2434  CB  ASN C 345     -23.084 -24.423 -54.050  1.00 19.82           C  
ANISOU 2434  CB  ASN C 345     2450   2450   2630   -230    360    110       C  
ATOM   2435  CG  ASN C 345     -24.052 -24.251 -52.894  1.00 20.08           C  
ANISOU 2435  CG  ASN C 345     2450   2510   2660   -210    390    160       C  
ATOM   2436  OD1 ASN C 345     -25.248 -24.492 -53.025  1.00 21.35           O  
ANISOU 2436  OD1 ASN C 345     2590   2650   2870   -230    400    170       O  
ATOM   2437  ND2 ASN C 345     -23.551 -23.816 -51.754  1.00 20.05           N  
ANISOU 2437  ND2 ASN C 345     2450   2570   2600   -160    400    200       N  
ATOM   2438  N   PHE C 346     -22.048 -26.466 -56.647  1.00 18.85           N  
ANISOU 2438  N   PHE C 346     2360   2190   2620   -300    350     10       N  
ATOM   2439  CA  PHE C 346     -21.008 -26.645 -57.699  1.00 19.01           C  
ANISOU 2439  CA  PHE C 346     2410   2190   2620   -300    340    -40       C  
ATOM   2440  C   PHE C 346     -21.354 -25.928 -59.012  1.00 19.48           C  
ANISOU 2440  C   PHE C 346     2480   2270   2650   -330    280   -110       C  
ATOM   2441  O   PHE C 346     -20.512 -25.130 -59.480  1.00 18.32           O  
ANISOU 2441  O   PHE C 346     2360   2160   2440   -310    260   -130       O  
ATOM   2442  CB  PHE C 346     -20.756 -28.132 -57.950  1.00 19.83           C  
ANISOU 2442  CB  PHE C 346     2510   2220   2800   -310    370    -40       C  
ATOM   2443  CG  PHE C 346     -19.798 -28.432 -59.076  1.00 19.96           C  
ANISOU 2443  CG  PHE C 346     2560   2220   2810   -310    350    -90       C  
ATOM   2444  CD1 PHE C 346     -18.431 -28.272 -58.906  1.00 19.71           C  
ANISOU 2444  CD1 PHE C 346     2550   2210   2730   -280    360    -70       C  
ATOM   2445  CD2 PHE C 346     -20.259 -28.930 -60.286  1.00 20.64           C  
ANISOU 2445  CD2 PHE C 346     2640   2260   2940   -350    330   -160       C  
ATOM   2446  CE1 PHE C 346     -17.550 -28.557 -59.938  1.00 19.55           C  
ANISOU 2446  CE1 PHE C 346     2560   2170   2700   -280    350   -110       C  
ATOM   2447  CE2 PHE C 346     -19.377 -29.226 -61.316  1.00 20.79           C  
ANISOU 2447  CE2 PHE C 346     2690   2270   2940   -340    320   -210       C  
ATOM   2448  CZ  PHE C 346     -18.024 -29.034 -61.140  1.00 20.41           C  
ANISOU 2448  CZ  PHE C 346     2670   2240   2840   -310    330   -180       C  
ATOM   2449  N   LYS C 347     -22.527 -26.185 -59.596  1.00 20.76           N  
ANISOU 2449  N   LYS C 347     2620   2400   2860   -360    270   -150       N  
ATOM   2450  CA  LYS C 347     -22.874 -25.525 -60.887  1.00 22.52           C  
ANISOU 2450  CA  LYS C 347     2850   2650   3050   -380    220   -210       C  
ATOM   2451  C   LYS C 347     -22.746 -23.996 -60.787  1.00 20.75           C  
ANISOU 2451  C   LYS C 347     2640   2490   2750   -360    200   -200       C  
ATOM   2452  O   LYS C 347     -22.178 -23.409 -61.721  1.00 19.28           O  
ANISOU 2452  O   LYS C 347     2480   2330   2510   -360    170   -240       O  
ATOM   2453  CB  LYS C 347     -24.256 -25.960 -61.385  1.00 25.44           C  
ANISOU 2453  CB  LYS C 347     3190   2990   3480   -420    210   -250       C  
ATOM   2454  CG  LYS C 347     -24.298 -27.402 -61.876  1.00 29.94           C  
ANISOU 2454  CG  LYS C 347     3750   3490   4130   -440    220   -280       C  
ATOM   2455  CD  LYS C 347     -25.620 -27.831 -62.471  1.00 32.60           C  
ANISOU 2455  CD  LYS C 347     4050   3800   4540   -480    190   -330       C  
ATOM   2456  CE  LYS C 347     -25.561 -29.237 -63.026  1.00 35.98           C  
ANISOU 2456  CE  LYS C 347     4470   4150   5050   -510    200   -380       C  
ATOM   2457  NZ  LYS C 347     -26.834 -29.617 -63.684  1.00 39.80           N  
ANISOU 2457  NZ  LYS C 347     4910   4610   5600   -550    170   -440       N  
ATOM   2458  N   ASP C 348     -23.238 -23.377 -59.711  1.00 19.78           N  
ANISOU 2458  N   ASP C 348     2500   2400   2610   -350    210   -160       N  
ATOM   2459  CA  ASP C 348     -23.133 -21.898 -59.583  1.00 20.02           C  
ANISOU 2459  CA  ASP C 348     2550   2490   2580   -330    190   -160       C  
ATOM   2460  C   ASP C 348     -21.672 -21.474 -59.398  1.00 18.29           C  
ANISOU 2460  C   ASP C 348     2350   2280   2310   -310    190   -150       C  
ATOM   2461  O   ASP C 348     -21.343 -20.375 -59.876  1.00 17.75           O  
ANISOU 2461  O   ASP C 348     2300   2250   2200   -300    170   -170       O  
ATOM   2462  CB  ASP C 348     -24.082 -21.374 -58.506  1.00 21.04           C  
ANISOU 2462  CB  ASP C 348     2650   2640   2700   -330    200   -120       C  
ATOM   2463  CG  ASP C 348     -25.525 -21.607 -58.912  1.00 21.86           C  
ANISOU 2463  CG  ASP C 348     2720   2730   2850   -360    190   -130       C  
ATOM   2464  OD1 ASP C 348     -25.725 -22.056 -60.053  1.00 23.54           O  
ANISOU 2464  OD1 ASP C 348     2930   2920   3080   -380    170   -180       O  
ATOM   2465  OD2 ASP C 348     -26.425 -21.362 -58.092  1.00 23.20           O  
ANISOU 2465  OD2 ASP C 348     2870   2910   3030   -350    200   -100       O  
ATOM   2466  N   GLN C 349     -20.850 -22.303 -58.744  1.00 17.48           N  
ANISOU 2466  N   GLN C 349     2260   2160   2220   -290    220   -120       N  
ATOM   2467  CA  GLN C 349     -19.408 -21.999 -58.532  1.00 17.02           C  
ANISOU 2467  CA  GLN C 349     2220   2120   2120   -270    220   -110       C  
ATOM   2468  C   GLN C 349     -18.707 -21.932 -59.895  1.00 17.20           C  
ANISOU 2468  C   GLN C 349     2260   2140   2130   -270    200   -150       C  
ATOM   2469  O   GLN C 349     -17.943 -20.972 -60.107  1.00 16.20           O  
ANISOU 2469  O   GLN C 349     2150   2040   1970   -260    190   -150       O  
ATOM   2470  CB  GLN C 349     -18.770 -23.044 -57.612  1.00 16.75           C  
ANISOU 2470  CB  GLN C 349     2180   2070   2110   -240    260    -60       C  
ATOM   2471  CG  GLN C 349     -19.359 -23.045 -56.209  1.00 16.56           C  
ANISOU 2471  CG  GLN C 349     2130   2070   2090   -230    280    -10       C  
ATOM   2472  CD  GLN C 349     -18.870 -24.172 -55.333  1.00 16.94           C  
ANISOU 2472  CD  GLN C 349     2170   2100   2160   -200    330     40       C  
ATOM   2473  OE1 GLN C 349     -18.182 -25.094 -55.775  1.00 17.15           O  
ANISOU 2473  OE1 GLN C 349     2210   2090   2220   -200    340     40       O  
ATOM   2474  NE2 GLN C 349     -19.245 -24.115 -54.066  1.00 17.05           N  
ANISOU 2474  NE2 GLN C 349     2170   2150   2160   -170    350     90       N  
ATOM   2475  N   VAL C 350     -18.960 -22.917 -60.770  1.00 18.03           N  
ANISOU 2475  N   VAL C 350     2370   2200   2280   -290    200   -180       N  
ATOM   2476  CA  VAL C 350     -18.357 -22.964 -62.134  1.00 18.86           C  
ANISOU 2476  CA  VAL C 350     2500   2300   2360   -290    190   -220       C  
ATOM   2477  C   VAL C 350     -18.824 -21.721 -62.906  1.00 19.08           C  
ANISOU 2477  C   VAL C 350     2520   2380   2350   -290    150   -250       C  
ATOM   2478  O   VAL C 350     -17.967 -21.043 -63.510  1.00 17.85           O  
ANISOU 2478  O   VAL C 350     2380   2240   2160   -270    140   -250       O  
ATOM   2479  CB  VAL C 350     -18.729 -24.264 -62.875  1.00 19.89           C  
ANISOU 2479  CB  VAL C 350     2630   2390   2550   -310    190   -260       C  
ATOM   2480  CG1 VAL C 350     -18.166 -24.283 -64.290  1.00 20.30           C  
ANISOU 2480  CG1 VAL C 350     2700   2450   2570   -300    170   -310       C  
ATOM   2481  CG2 VAL C 350     -18.290 -25.505 -62.113  1.00 20.05           C  
ANISOU 2481  CG2 VAL C 350     2640   2360   2620   -300    230   -230       C  
ATOM   2482  N   ILE C 351     -20.130 -21.427 -62.864  1.00 19.97           N  
ANISOU 2482  N   ILE C 351     2610   2500   2480   -310    140   -250       N  
ATOM   2483  CA  ILE C 351     -20.685 -20.228 -63.563  1.00 20.62           C  
ANISOU 2483  CA  ILE C 351     2690   2620   2520   -310    110   -270       C  
ATOM   2484  C   ILE C 351     -19.975 -18.966 -63.053  1.00 19.81           C  
ANISOU 2484  C   ILE C 351     2600   2550   2390   -290    110   -240       C  
ATOM   2485  O   ILE C 351     -19.527 -18.167 -63.899  1.00 19.26           O  
ANISOU 2485  O   ILE C 351     2530   2500   2280   -270    100   -250       O  
ATOM   2486  CB  ILE C 351     -22.212 -20.142 -63.382  1.00 21.32           C  
ANISOU 2486  CB  ILE C 351     2750   2710   2640   -330    100   -280       C  
ATOM   2487  CG1 ILE C 351     -22.906 -21.342 -64.033  1.00 23.06           C  
ANISOU 2487  CG1 ILE C 351     2960   2900   2900   -360     90   -320       C  
ATOM   2488  CG2 ILE C 351     -22.743 -18.820 -63.920  1.00 21.19           C  
ANISOU 2488  CG2 ILE C 351     2730   2740   2580   -320     80   -280       C  
ATOM   2489  CD1 ILE C 351     -24.400 -21.396 -63.811  1.00 24.14           C  
ANISOU 2489  CD1 ILE C 351     3060   3040   3070   -380     90   -320       C  
ATOM   2490  N   LEU C 352     -19.872 -18.801 -61.731  1.00 19.40           N  
ANISOU 2490  N   LEU C 352     2540   2490   2340   -280    130   -210       N  
ATOM   2491  CA  LEU C 352     -19.213 -17.597 -61.152  1.00 19.98           C  
ANISOU 2491  CA  LEU C 352     2620   2590   2380   -260    130   -190       C  
ATOM   2492  C   LEU C 352     -17.749 -17.519 -61.609  1.00 19.52           C  
ANISOU 2492  C   LEU C 352     2570   2530   2310   -250    130   -190       C  
ATOM   2493  O   LEU C 352     -17.342 -16.457 -62.092  1.00 19.76           O  
ANISOU 2493  O   LEU C 352     2600   2580   2320   -240    120   -190       O  
ATOM   2494  CB  LEU C 352     -19.319 -17.624 -59.619  1.00 20.54           C  
ANISOU 2494  CB  LEU C 352     2680   2670   2460   -260    140   -160       C  
ATOM   2495  CG  LEU C 352     -18.582 -16.499 -58.879  1.00 21.77           C  
ANISOU 2495  CG  LEU C 352     2830   2850   2590   -240    140   -150       C  
ATOM   2496  CD1 LEU C 352     -19.044 -15.125 -59.341  1.00 21.38           C  
ANISOU 2496  CD1 LEU C 352     2780   2820   2530   -240    120   -170       C  
ATOM   2497  CD2 LEU C 352     -18.749 -16.629 -57.372  1.00 22.28           C  
ANISOU 2497  CD2 LEU C 352     2890   2930   2640   -220    150   -130       C  
ATOM   2498  N   LEU C 353     -16.991 -18.603 -61.479  1.00 18.90           N  
ANISOU 2498  N   LEU C 353     2500   2430   2240   -240    140   -180       N  
ATOM   2499  CA  LEU C 353     -15.558 -18.554 -61.877  1.00 18.94           C  
ANISOU 2499  CA  LEU C 353     2520   2440   2230   -230    150   -180       C  
ATOM   2500  C   LEU C 353     -15.403 -18.282 -63.381  1.00 19.21           C  
ANISOU 2500  C   LEU C 353     2560   2480   2250   -220    130   -200       C  
ATOM   2501  O   LEU C 353     -14.582 -17.393 -63.736  1.00 18.46           O  
ANISOU 2501  O   LEU C 353     2470   2400   2140   -210    130   -190       O  
ATOM   2502  CB  LEU C 353     -14.898 -19.866 -61.448  1.00 19.30           C  
ANISOU 2502  CB  LEU C 353     2580   2460   2300   -220    170   -160       C  
ATOM   2503  CG  LEU C 353     -14.817 -20.071 -59.935  1.00 18.97           C  
ANISOU 2503  CG  LEU C 353     2520   2430   2260   -210    180   -130       C  
ATOM   2504  CD1 LEU C 353     -14.353 -21.483 -59.602  1.00 19.33           C  
ANISOU 2504  CD1 LEU C 353     2570   2450   2330   -200    210   -110       C  
ATOM   2505  CD2 LEU C 353     -13.903 -19.035 -59.299  1.00 18.34           C  
ANISOU 2505  CD2 LEU C 353     2440   2380   2150   -200    170   -120       C  
ATOM   2506  N   ASN C 354     -16.167 -18.984 -64.226  1.00 19.07           N  
ANISOU 2506  N   ASN C 354     2550   2450   2240   -230    130   -230       N  
ATOM   2507  CA  ASN C 354     -16.077 -18.805 -65.702  1.00 20.13           C  
ANISOU 2507  CA  ASN C 354     2690   2610   2350   -220    120   -250       C  
ATOM   2508  C   ASN C 354     -16.492 -17.383 -66.111  1.00 19.70           C  
ANISOU 2508  C   ASN C 354     2620   2590   2280   -210    100   -240       C  
ATOM   2509  O   ASN C 354     -16.026 -16.919 -67.172  1.00 18.86           O  
ANISOU 2509  O   ASN C 354     2520   2500   2150   -190    100   -240       O  
ATOM   2510  CB  ASN C 354     -16.883 -19.865 -66.462  1.00 21.20           C  
ANISOU 2510  CB  ASN C 354     2830   2730   2500   -230    110   -290       C  
ATOM   2511  CG  ASN C 354     -16.235 -21.235 -66.444  1.00 22.36           C  
ANISOU 2511  CG  ASN C 354     2990   2840   2670   -230    130   -310       C  
ATOM   2512  OD1 ASN C 354     -15.043 -21.369 -66.163  1.00 22.07           O  
ANISOU 2512  OD1 ASN C 354     2970   2790   2630   -210    140   -280       O  
ATOM   2513  ND2 ASN C 354     -16.999 -22.256 -66.797  1.00 23.19           N  
ANISOU 2513  ND2 ASN C 354     3090   2910   2800   -250    120   -350       N  
ATOM   2514  N   LYS C 355     -17.323 -16.719 -65.310  1.00 19.15           N  
ANISOU 2514  N   LYS C 355     2540   2520   2220   -230    100   -230       N  
ATOM   2515  CA  LYS C 355     -17.756 -15.335 -65.639  1.00 19.77           C  
ANISOU 2515  CA  LYS C 355     2600   2630   2280   -220     90   -220       C  
ATOM   2516  C   LYS C 355     -16.556 -14.379 -65.559  1.00 17.99           C  
ANISOU 2516  C   LYS C 355     2380   2400   2060   -200    100   -190       C  
ATOM   2517  O   LYS C 355     -16.559 -13.364 -66.287  1.00 17.92           O  
ANISOU 2517  O   LYS C 355     2360   2410   2040   -190    100   -180       O  
ATOM   2518  CB  LYS C 355     -18.815 -14.850 -64.642  1.00 22.15           C  
ANISOU 2518  CB  LYS C 355     2890   2930   2600   -240     90   -220       C  
ATOM   2519  CG  LYS C 355     -19.352 -13.454 -64.910  1.00 24.87           C  
ANISOU 2519  CG  LYS C 355     3220   3300   2940   -230     80   -210       C  
ATOM   2520  CD  LYS C 355     -20.180 -12.877 -63.779  1.00 27.04           C  
ANISOU 2520  CD  LYS C 355     3480   3570   3220   -240     80   -200       C  
ATOM   2521  CE  LYS C 355     -21.429 -13.658 -63.447  1.00 29.94           C  
ANISOU 2521  CE  LYS C 355     3840   3930   3600   -260     80   -210       C  
ATOM   2522  NZ  LYS C 355     -22.195 -12.985 -62.368  1.00 32.09           N  
ANISOU 2522  NZ  LYS C 355     4100   4210   3880   -260     80   -200       N  
ATOM   2523  N   HIS C 356     -15.561 -14.704 -64.727  1.00 15.79           N  
ANISOU 2523  N   HIS C 356     2100   2110   1790   -200    110   -180       N  
ATOM   2524  CA  HIS C 356     -14.395 -13.798 -64.533  1.00 14.84           C  
ANISOU 2524  CA  HIS C 356     1980   1980   1680   -190    110   -160       C  
ATOM   2525  C   HIS C 356     -13.129 -14.271 -65.260  1.00 14.47           C  
ANISOU 2525  C   HIS C 356     1940   1940   1620   -170    120   -150       C  
ATOM   2526  O   HIS C 356     -12.254 -13.413 -65.507  1.00 14.53           O  
ANISOU 2526  O   HIS C 356     1930   1950   1640   -160    130   -120       O  
ATOM   2527  CB  HIS C 356     -14.161 -13.611 -63.036  1.00 14.61           C  
ANISOU 2527  CB  HIS C 356     1940   1950   1660   -200    110   -160       C  
ATOM   2528  CG  HIS C 356     -15.337 -13.026 -62.329  1.00 14.22           C  
ANISOU 2528  CG  HIS C 356     1880   1900   1620   -210    100   -170       C  
ATOM   2529  ND1 HIS C 356     -15.631 -11.680 -62.384  1.00 13.90           N  
ANISOU 2529  ND1 HIS C 356     1830   1870   1590   -210    100   -170       N  
ATOM   2530  CD2 HIS C 356     -16.267 -13.590 -61.528  1.00 14.08           C  
ANISOU 2530  CD2 HIS C 356     1870   1890   1600   -220    100   -180       C  
ATOM   2531  CE1 HIS C 356     -16.712 -11.445 -61.665  1.00 14.38           C  
ANISOU 2531  CE1 HIS C 356     1880   1930   1650   -220     90   -180       C  
ATOM   2532  NE2 HIS C 356     -17.120 -12.605 -61.125  1.00 13.84           N  
ANISOU 2532  NE2 HIS C 356     1830   1870   1570   -220    100   -180       N  
ATOM   2533  N   ILE C 357     -13.009 -15.563 -65.566  1.00 14.10           N  
ANISOU 2533  N   ILE C 357     1910   1880   1570   -170    130   -160       N  
ATOM   2534  CA  ILE C 357     -11.796 -16.079 -66.273  1.00 14.11           C  
ANISOU 2534  CA  ILE C 357     1920   1880   1560   -150    140   -150       C  
ATOM   2535  C   ILE C 357     -11.757 -15.537 -67.714  1.00 14.00           C  
ANISOU 2535  C   ILE C 357     1900   1890   1520   -120    140   -140       C  
ATOM   2536  O   ILE C 357     -12.676 -15.861 -68.506  1.00 13.22           O  
ANISOU 2536  O   ILE C 357     1810   1810   1400   -120    130   -170       O  
ATOM   2537  CB  ILE C 357     -11.761 -17.618 -66.243  1.00 14.64           C  
ANISOU 2537  CB  ILE C 357     2010   1930   1630   -150    150   -170       C  
ATOM   2538  CG1 ILE C 357     -11.694 -18.156 -64.808  1.00 15.01           C  
ANISOU 2538  CG1 ILE C 357     2050   1960   1690   -170    160   -160       C  
ATOM   2539  CG2 ILE C 357     -10.613 -18.147 -67.090  1.00 14.84           C  
ANISOU 2539  CG2 ILE C 357     2040   1960   1640   -120    160   -160       C  
ATOM   2540  CD1 ILE C 357     -11.775 -19.666 -64.714  1.00 15.03           C  
ANISOU 2540  CD1 ILE C 357     2070   1930   1710   -170    170   -170       C  
ATOM   2541  N   ASP C 358     -10.724 -14.748 -68.031  1.00 13.72           N  
ANISOU 2541  N   ASP C 358     1850   1860   1500   -100    150   -100       N  
ATOM   2542  CA  ASP C 358     -10.514 -14.169 -69.387  1.00 14.05           C  
ANISOU 2542  CA  ASP C 358     1890   1930   1520    -70    160    -80       C  
ATOM   2543  C   ASP C 358     -11.689 -13.298 -69.836  1.00 13.71           C  
ANISOU 2543  C   ASP C 358     1830   1910   1470    -70    150    -90       C  
ATOM   2544  O   ASP C 358     -11.871 -13.175 -71.058  1.00 13.64           O  
ANISOU 2544  O   ASP C 358     1820   1940   1420    -40    160    -80       O  
ATOM   2545  CB  ASP C 358     -10.293 -15.272 -70.423  1.00 14.98           C  
ANISOU 2545  CB  ASP C 358     2020   2070   1600    -40    170   -100       C  
ATOM   2546  CG  ASP C 358      -8.961 -15.979 -70.288  1.00 15.70           C  
ANISOU 2546  CG  ASP C 358     2130   2150   1690    -30    190    -80       C  
ATOM   2547  OD1 ASP C 358      -8.009 -15.351 -69.795  1.00 15.76           O  
ANISOU 2547  OD1 ASP C 358     2120   2140   1730    -30    200    -50       O  
ATOM   2548  OD2 ASP C 358      -8.896 -17.146 -70.674  1.00 18.34           O  
ANISOU 2548  OD2 ASP C 358     2480   2480   2010    -20    190   -110       O  
ATOM   2549  N   ALA C 359     -12.435 -12.707 -68.904  1.00 13.41           N  
ANISOU 2549  N   ALA C 359     1780   1860   1450   -100    140    -90       N  
ATOM   2550  CA  ALA C 359     -13.572 -11.841 -69.295  1.00 14.17           C  
ANISOU 2550  CA  ALA C 359     1860   1980   1540   -100    140    -90       C  
ATOM   2551  C   ALA C 359     -13.069 -10.584 -70.019  1.00 14.69           C  
ANISOU 2551  C   ALA C 359     1900   2050   1620    -70    160    -40       C  
ATOM   2552  O   ALA C 359     -13.794 -10.100 -70.905  1.00 14.69           O  
ANISOU 2552  O   ALA C 359     1890   2090   1600    -40    160    -30       O  
ATOM   2553  CB  ALA C 359     -14.373 -11.454 -68.078  1.00 14.01           C  
ANISOU 2553  CB  ALA C 359     1840   1940   1550   -130    130   -110       C  
ATOM   2554  N   TYR C 360     -11.863 -10.108 -69.678  1.00 15.48           N  
ANISOU 2554  N   TYR C 360     1990   2130   1760    -60    170    -10       N  
ATOM   2555  CA  TYR C 360     -11.282  -8.862 -70.260  1.00 16.26           C  
ANISOU 2555  CA  TYR C 360     2060   2230   1890    -40    200     40       C  
ATOM   2556  C   TYR C 360     -11.245  -8.901 -71.796  1.00 17.10           C  
ANISOU 2556  C   TYR C 360     2160   2380   1960     10    210     70       C  
ATOM   2557  O   TYR C 360     -11.193  -7.820 -72.435  1.00 16.42           O  
ANISOU 2557  O   TYR C 360     2050   2300   1890     40    240    130       O  
ATOM   2558  CB  TYR C 360      -9.851  -8.646 -69.768  1.00 17.06           C  
ANISOU 2558  CB  TYR C 360     2150   2300   2040    -50    210     60       C  
ATOM   2559  CG  TYR C 360      -8.846  -9.557 -70.424  1.00 17.45           C  
ANISOU 2559  CG  TYR C 360     2210   2360   2060    -20    220     80       C  
ATOM   2560  CD1 TYR C 360      -8.581 -10.819 -69.916  1.00 17.93           C  
ANISOU 2560  CD1 TYR C 360     2300   2420   2100    -30    200     50       C  
ATOM   2561  CD2 TYR C 360      -8.182  -9.167 -71.574  1.00 18.03           C  
ANISOU 2561  CD2 TYR C 360     2260   2460   2130     20    250    130       C  
ATOM   2562  CE1 TYR C 360      -7.669 -11.668 -70.524  1.00 18.08           C  
ANISOU 2562  CE1 TYR C 360     2330   2450   2090    -10    220     60       C  
ATOM   2563  CE2 TYR C 360      -7.270 -10.005 -72.199  1.00 18.70           C  
ANISOU 2563  CE2 TYR C 360     2360   2560   2190     50    260    150       C  
ATOM   2564  CZ  TYR C 360      -7.013 -11.261 -71.673  1.00 18.67           C  
ANISOU 2564  CZ  TYR C 360     2390   2550   2160     40    240    110       C  
ATOM   2565  OH  TYR C 360      -6.123 -12.103 -72.279  1.00 18.79           O  
ANISOU 2565  OH  TYR C 360     2410   2580   2150     70    260    120       O  
ATOM   2566  N   LYS C 361     -11.256 -10.096 -72.386  1.00 17.97           N  
ANISOU 2566  N   LYS C 361     2300   2520   2010     30    210     50       N  
ATOM   2567  CA  LYS C 361     -11.195 -10.213 -73.868  1.00 19.14           C  
ANISOU 2567  CA  LYS C 361     2440   2720   2110     80    220     70       C  
ATOM   2568  C   LYS C 361     -12.444  -9.604 -74.527  1.00 18.28           C  
ANISOU 2568  C   LYS C 361     2320   2660   1970    100    220     80       C  
ATOM   2569  O   LYS C 361     -12.323  -9.173 -75.690  1.00 17.64           O  
ANISOU 2569  O   LYS C 361     2220   2630   1860    150    240    120       O  
ATOM   2570  CB  LYS C 361     -11.006 -11.680 -74.261  1.00 21.46           C  
ANISOU 2570  CB  LYS C 361     2770   3040   2350     90    210     30       C  
ATOM   2571  CG  LYS C 361      -9.691 -12.290 -73.795  1.00 23.01           C  
ANISOU 2571  CG  LYS C 361     2980   3200   2570     80    220     30       C  
ATOM   2572  CD  LYS C 361      -9.559 -13.767 -74.042  1.00 25.88           C  
ANISOU 2572  CD  LYS C 361     3370   3570   2890     90    210    -20       C  
ATOM   2573  CE  LYS C 361      -9.541 -14.129 -75.507  1.00 29.34           C  
ANISOU 2573  CE  LYS C 361     3820   4060   3270    150    220    -20       C  
ATOM   2574  NZ  LYS C 361      -9.314 -15.584 -75.682  1.00 33.25           N  
ANISOU 2574  NZ  LYS C 361     4340   4560   3740    150    210    -70       N  
ATOM   2575  N   THR C 362     -13.571  -9.516 -73.805  1.00 17.22           N  
ANISOU 2575  N   THR C 362     2190   2510   1850     60    190     40       N  
ATOM   2576  CA  THR C 362     -14.850  -8.990 -74.373  1.00 17.37           C  
ANISOU 2576  CA  THR C 362     2190   2570   1840     80    190     40       C  
ATOM   2577  C   THR C 362     -15.021  -7.470 -74.192  1.00 16.85           C  
ANISOU 2577  C   THR C 362     2090   2490   1820     80    210    100       C  
ATOM   2578  O   THR C 362     -16.104  -6.980 -74.572  1.00 16.93           O  
ANISOU 2578  O   THR C 362     2090   2530   1810    100    210    100       O  
ATOM   2579  CB  THR C 362     -16.051  -9.713 -73.747  1.00 17.47           C  
ANISOU 2579  CB  THR C 362     2220   2580   1840     40    150    -20       C  
ATOM   2580  OG1 THR C 362     -16.138  -9.327 -72.376  1.00 17.22           O  
ANISOU 2580  OG1 THR C 362     2190   2490   1860    -10    150    -30       O  
ATOM   2581  CG2 THR C 362     -15.953 -11.219 -73.859  1.00 17.54           C  
ANISOU 2581  CG2 THR C 362     2260   2590   1810     30    130    -80       C  
ATOM   2582  N   PHE C 363     -14.019  -6.745 -73.673  1.00 16.27           N  
ANISOU 2582  N   PHE C 363     2000   2370   1810     80    230    140       N  
ATOM   2583  CA  PHE C 363     -14.142  -5.269 -73.492  1.00 16.37           C  
ANISOU 2583  CA  PHE C 363     1980   2350   1890     80    260    190       C  
ATOM   2584  C   PHE C 363     -12.775  -4.588 -73.548  1.00 15.90           C  
ANISOU 2584  C   PHE C 363     1900   2250   1890     90    290    240       C  
ATOM   2585  O   PHE C 363     -11.740  -5.236 -73.391  1.00 14.98           O  
ANISOU 2585  O   PHE C 363     1790   2120   1770     90    290    230       O  
ATOM   2586  CB  PHE C 363     -14.867  -4.928 -72.185  1.00 16.92           C  
ANISOU 2586  CB  PHE C 363     2060   2380   2000     30    240    150       C  
ATOM   2587  CG  PHE C 363     -14.313  -5.586 -70.946  1.00 17.02           C  
ANISOU 2587  CG  PHE C 363     2090   2340   2030    -20    220    100       C  
ATOM   2588  CD1 PHE C 363     -13.237  -5.043 -70.264  1.00 17.30           C  
ANISOU 2588  CD1 PHE C 363     2110   2330   2130    -30    230    110       C  
ATOM   2589  CD2 PHE C 363     -14.895  -6.741 -70.447  1.00 17.39           C  
ANISOU 2589  CD2 PHE C 363     2170   2400   2030    -40    190     40       C  
ATOM   2590  CE1 PHE C 363     -12.742  -5.652 -69.122  1.00 17.15           C  
ANISOU 2590  CE1 PHE C 363     2110   2280   2120    -70    210     70       C  
ATOM   2591  CE2 PHE C 363     -14.407  -7.343 -69.298  1.00 17.24           C  
ANISOU 2591  CE2 PHE C 363     2170   2350   2030    -80    170     10       C  
ATOM   2592  CZ  PHE C 363     -13.331  -6.796 -68.639  1.00 17.28           C  
ANISOU 2592  CZ  PHE C 363     2160   2310   2090    -90    180     20       C  
ATOM   2593  N   PRO C 364     -12.723  -3.258 -73.815  1.00 15.84           N  
ANISOU 2593  N   PRO C 364     1850   2230   1940    110    330    300       N  
ATOM   2594  CA  PRO C 364     -11.453  -2.539 -73.874  1.00 15.88           C  
ANISOU 2594  CA  PRO C 364     1820   2190   2020    120    360    360       C  
ATOM   2595  C   PRO C 364     -10.724  -2.621 -72.525  1.00 15.64           C  
ANISOU 2595  C   PRO C 364     1800   2090   2050     60    340    310       C  
ATOM   2596  O   PRO C 364     -11.308  -2.319 -71.468  1.00 15.16           O  
ANISOU 2596  O   PRO C 364     1750   1990   2020     20    310    260       O  
ATOM   2597  CB  PRO C 364     -11.832  -1.092 -74.214  1.00 16.25           C  
ANISOU 2597  CB  PRO C 364     1830   2220   2130    150    400    420       C  
ATOM   2598  CG  PRO C 364     -13.220  -1.195 -74.813  1.00 16.32           C  
ANISOU 2598  CG  PRO C 364     1850   2290   2070    170    390    420       C  
ATOM   2599  CD  PRO C 364     -13.864  -2.384 -74.129  1.00 15.92           C  
ANISOU 2599  CD  PRO C 364     1840   2250   1950    130    340    330       C  
ATOM   2600  OXT PRO C 364      -9.560  -3.003 -72.500  1.00 14.88           O  
ANISOU 2600  OXT PRO C 364     1700   1980   1970     60    340    320       O  
TER    2601      PRO C 364                                                      
ATOM   2602  N   LYS D 257     -11.869 -29.574 -43.642  1.00 41.77           N  
ANISOU 2602  N   LYS D 257     4460   6530   4880   -560    450    380       N  
ATOM   2603  CA  LYS D 257     -12.072 -28.352 -44.484  1.00 40.08           C  
ANISOU 2603  CA  LYS D 257     4290   6290   4640   -310    420    140       C  
ATOM   2604  C   LYS D 257     -11.534 -28.562 -45.894  1.00 34.62           C  
ANISOU 2604  C   LYS D 257     3780   5230   4150   -380    340     70       C  
ATOM   2605  O   LYS D 257     -10.646 -29.387 -46.103  1.00 34.52           O  
ANISOU 2605  O   LYS D 257     3900   4950   4270   -510    310    120       O  
ATOM   2606  CB  LYS D 257     -11.312 -27.143 -43.929  1.00 43.29           C  
ANISOU 2606  CB  LYS D 257     4860   6630   4960    -20    390    -20       C  
ATOM   2607  CG  LYS D 257     -11.769 -26.613 -42.580  1.00 47.81           C  
ANISOU 2607  CG  LYS D 257     5300   7580   5280    200    430    -40       C  
ATOM   2608  CD  LYS D 257     -11.015 -25.364 -42.186  1.00 49.52           C  
ANISOU 2608  CD  LYS D 257     5740   7630   5440    480    320   -250       C  
ATOM   2609  CE  LYS D 257     -11.477 -24.771 -40.874  1.00 54.30           C  
ANISOU 2609  CE  LYS D 257     6250   8630   5750    800    310   -350       C  
ATOM   2610  NZ  LYS D 257     -10.740 -23.523 -40.568  1.00 55.28           N  
ANISOU 2610  NZ  LYS D 257     6660   8490   5860   1070    120   -580       N  
ATOM   2611  N   PRO D 258     -12.043 -27.810 -46.902  1.00 30.86           N  
ANISOU 2611  N   PRO D 258     3290   4760   3670   -250    300    -70       N  
ATOM   2612  CA  PRO D 258     -11.526 -27.912 -48.264  1.00 26.82           C  
ANISOU 2612  CA  PRO D 258     2930   3980   3290   -270    230   -140       C  
ATOM   2613  C   PRO D 258     -10.002 -27.703 -48.197  1.00 22.52           C  
ANISOU 2613  C   PRO D 258     2580   3180   2800   -240    230   -140       C  
ATOM   2614  O   PRO D 258      -9.547 -26.851 -47.455  1.00 20.39           O  
ANISOU 2614  O   PRO D 258     2370   2920   2460   -130    230   -160       O  
ATOM   2615  CB  PRO D 258     -12.270 -26.826 -49.059  1.00 27.83           C  
ANISOU 2615  CB  PRO D 258     3030   4210   3340    -80    190   -270       C  
ATOM   2616  CG  PRO D 258     -12.961 -25.965 -48.006  1.00 30.03           C  
ANISOU 2616  CG  PRO D 258     3200   4760   3440    120    210   -320       C  
ATOM   2617  CD  PRO D 258     -13.154 -26.852 -46.795  1.00 31.11           C  
ANISOU 2617  CD  PRO D 258     3180   5110   3530    -30    300   -170       C  
ATOM   2618  N   ARG D 259      -9.265 -28.486 -48.977  1.00 19.51           N  
ANISOU 2618  N   ARG D 259     2280   2620   2510   -310    190   -130       N  
ATOM   2619  CA  ARG D 259      -7.778 -28.477 -48.994  1.00 17.83           C  
ANISOU 2619  CA  ARG D 259     2190   2270   2320   -280    190   -110       C  
ATOM   2620  C   ARG D 259      -7.200 -27.054 -49.048  1.00 15.82           C  
ANISOU 2620  C   ARG D 259     1980   2010   2020   -190    180   -120       C  
ATOM   2621  O   ARG D 259      -6.256 -26.787 -48.284  1.00 14.56           O  
ANISOU 2621  O   ARG D 259     1870   1810   1850   -200    170    -70       O  
ATOM   2622  CB  ARG D 259      -7.314 -29.345 -50.170  1.00 18.61           C  
ANISOU 2622  CB  ARG D 259     2330   2280   2460   -270    140   -150       C  
ATOM   2623  CG  ARG D 259      -5.811 -29.566 -50.269  1.00 19.04           C  
ANISOU 2623  CG  ARG D 259     2450   2300   2490   -200    140   -130       C  
ATOM   2624  CD  ARG D 259      -5.548 -30.608 -51.340  1.00 20.33           C  
ANISOU 2624  CD  ARG D 259     2660   2420   2650   -100     60   -220       C  
ATOM   2625  NE  ARG D 259      -4.156 -31.014 -51.480  1.00 21.31           N  
ANISOU 2625  NE  ARG D 259     2800   2600   2700     40     50   -220       N  
ATOM   2626  CZ  ARG D 259      -3.315 -30.595 -52.423  1.00 21.84           C  
ANISOU 2626  CZ  ARG D 259     2790   2870   2640    170     80   -230       C  
ATOM   2627  NH1 ARG D 259      -3.711 -29.745 -53.354  1.00 22.54           N  
ANISOU 2627  NH1 ARG D 259     2820   3070   2670    170    100   -210       N  
ATOM   2628  NH2 ARG D 259      -2.076 -31.051 -52.442  1.00 22.45           N  
ANISOU 2628  NH2 ARG D 259     2840   3070   2620    320     70   -230       N  
ATOM   2629  N   GLN D 260      -7.764 -26.167 -49.875  1.00 14.94           N  
ANISOU 2629  N   GLN D 260     1880   1920   1880   -120    130   -160       N  
ATOM   2630  CA  GLN D 260      -7.194 -24.799 -50.010  1.00 14.39           C  
ANISOU 2630  CA  GLN D 260     1920   1770   1780    -80     50   -130       C  
ATOM   2631  C   GLN D 260      -7.353 -23.982 -48.716  1.00 14.81           C  
ANISOU 2631  C   GLN D 260     2040   1780   1800      0    -20   -180       C  
ATOM   2632  O   GLN D 260      -6.647 -22.964 -48.605  1.00 14.40           O  
ANISOU 2632  O   GLN D 260     2120   1590   1760    -10   -150   -140       O  
ATOM   2633  CB  GLN D 260      -7.766 -24.034 -51.215  1.00 14.75           C  
ANISOU 2633  CB  GLN D 260     2000   1810   1800    -10    -20   -140       C  
ATOM   2634  CG  GLN D 260      -9.261 -23.709 -51.184  1.00 15.48           C  
ANISOU 2634  CG  GLN D 260     2050   1990   1840    130    -50   -270       C  
ATOM   2635  CD  GLN D 260     -10.201 -24.844 -51.521  1.00 15.36           C  
ANISOU 2635  CD  GLN D 260     1870   2130   1830    100     30   -320       C  
ATOM   2636  OE1 GLN D 260      -9.818 -26.008 -51.593  1.00 14.54           O  
ANISOU 2636  OE1 GLN D 260     1720   2020   1780    -20     90   -290       O  
ATOM   2637  NE2 GLN D 260     -11.458 -24.498 -51.766  1.00 16.59           N  
ANISOU 2637  NE2 GLN D 260     1950   2430   1920    220      0   -410       N  
ATOM   2638  N   LYS D 261      -8.208 -24.398 -47.773  1.00 14.57           N  
ANISOU 2638  N   LYS D 261     1920   1900   1710     70     40   -250       N  
ATOM   2639  CA  LYS D 261      -8.382 -23.604 -46.519  1.00 15.88           C  
ANISOU 2639  CA  LYS D 261     2150   2110   1780    230    -30   -330       C  
ATOM   2640  C   LYS D 261      -7.712 -24.283 -45.316  1.00 16.05           C  
ANISOU 2640  C   LYS D 261     2130   2180   1790    160     40   -270       C  
ATOM   2641  O   LYS D 261      -7.807 -23.729 -44.203  1.00 16.68           O  
ANISOU 2641  O   LYS D 261     2250   2330   1750    320    -20   -360       O  
ATOM   2642  CB  LYS D 261      -9.869 -23.382 -46.220  1.00 16.99           C  
ANISOU 2642  CB  LYS D 261     2170   2510   1780    430    -20   -440       C  
ATOM   2643  CG  LYS D 261     -10.615 -22.539 -47.244  1.00 17.46           C  
ANISOU 2643  CG  LYS D 261     2280   2540   1820    580   -120   -530       C  
ATOM   2644  CD  LYS D 261     -10.031 -21.151 -47.412  1.00 18.14           C  
ANISOU 2644  CD  LYS D 261     2650   2320   1920    690   -350   -590       C  
ATOM   2645  CE  LYS D 261     -10.869 -20.268 -48.314  1.00 19.18           C  
ANISOU 2645  CE  LYS D 261     2870   2410   2010    880   -490   -670       C  
ATOM   2646  NZ  LYS D 261     -10.293 -18.911 -48.434  1.00 20.44           N  
ANISOU 2646  NZ  LYS D 261     3360   2200   2210    950   -790   -690       N  
ATOM   2647  N   ARG D 262      -7.022 -25.402 -45.533  1.00 15.42           N  
ANISOU 2647  N   ARG D 262     2010   2060   1790    -10    130   -160       N  
ATOM   2648  CA  ARG D 262      -6.388 -26.118 -44.397  1.00 15.93           C  
ANISOU 2648  CA  ARG D 262     2050   2160   1840    -60    180    -90       C  
ATOM   2649  C   ARG D 262      -5.189 -25.329 -43.874  1.00 16.08           C  
ANISOU 2649  C   ARG D 262     2190   2060   1860    -40     70   -110       C  
ATOM   2650  O   ARG D 262      -4.574 -24.558 -44.655  1.00 15.85           O  
ANISOU 2650  O   ARG D 262     2240   1880   1890    -80    -30   -110       O  
ATOM   2651  CB  ARG D 262      -5.976 -27.529 -44.818  1.00 15.33           C  
ANISOU 2651  CB  ARG D 262     1940   2030   1850   -210    250     10       C  
ATOM   2652  CG  ARG D 262      -7.149 -28.392 -45.248  1.00 16.36           C  
ANISOU 2652  CG  ARG D 262     1980   2240   2000   -290    290     50       C  
ATOM   2653  CD  ARG D 262      -6.691 -29.721 -45.800  1.00 16.58           C  
ANISOU 2653  CD  ARG D 262     2060   2110   2130   -400    260    110       C  
ATOM   2654  NE  ARG D 262      -7.803 -30.537 -46.261  1.00 17.79           N  
ANISOU 2654  NE  ARG D 262     2150   2280   2330   -530    230    140       N  
ATOM   2655  CZ  ARG D 262      -7.667 -31.717 -46.854  1.00 18.80           C  
ANISOU 2655  CZ  ARG D 262     2370   2220   2560   -610    130    160       C  
ATOM   2656  NH1 ARG D 262      -6.464 -32.222 -47.068  1.00 17.97           N  
ANISOU 2656  NH1 ARG D 262     2400   1950   2480   -520     80    120       N  
ATOM   2657  NH2 ARG D 262      -8.735 -32.390 -47.239  1.00 20.83           N  
ANISOU 2657  NH2 ARG D 262     2570   2470   2870   -770     60    200       N  
ATOM   2658  N   THR D 263      -4.908 -25.522 -42.586  1.00 16.62           N  
ANISOU 2658  N   THR D 263     2260   2210   1850     10     80   -110       N  
ATOM   2659  CA  THR D 263      -3.775 -24.886 -41.878  1.00 17.31           C  
ANISOU 2659  CA  THR D 263     2440   2210   1930     30    -40   -140       C  
ATOM   2660  C   THR D 263      -2.913 -26.014 -41.312  1.00 17.04           C  
ANISOU 2660  C   THR D 263     2350   2220   1900    -50     40    -30       C  
ATOM   2661  O   THR D 263      -3.426 -26.777 -40.464  1.00 17.38           O  
ANISOU 2661  O   THR D 263     2340   2420   1850    -10    140     20       O  
ATOM   2662  CB  THR D 263      -4.270 -23.936 -40.779  1.00 19.43           C  
ANISOU 2662  CB  THR D 263     2790   2550   2050    250   -170   -300       C  
ATOM   2663  OG1 THR D 263      -5.074 -22.925 -41.382  1.00 21.11           O  
ANISOU 2663  OG1 THR D 263     3080   2690   2250    370   -280   -410       O  
ATOM   2664  CG2 THR D 263      -3.146 -23.276 -40.009  1.00 20.66           C  
ANISOU 2664  CG2 THR D 263     3070   2580   2210    260   -350   -350       C  
ATOM   2665  N   ALA D 264      -1.677 -26.154 -41.795  1.00 16.34           N  
ANISOU 2665  N   ALA D 264     2270   2050   1890   -150     10     40       N  
ATOM   2666  CA  ALA D 264      -0.806 -27.219 -41.249  1.00 16.13           C  
ANISOU 2666  CA  ALA D 264     2200   2080   1850   -160     60    110       C  
ATOM   2667  C   ALA D 264      -0.220 -26.746 -39.911  1.00 16.74           C  
ANISOU 2667  C   ALA D 264     2320   2200   1840   -100    -30     80       C  
ATOM   2668  O   ALA D 264       0.103 -25.555 -39.794  1.00 17.00           O  
ANISOU 2668  O   ALA D 264     2410   2170   1880   -110   -180      0       O  
ATOM   2669  CB  ALA D 264       0.271 -27.590 -42.244  1.00 15.53           C  
ANISOU 2669  CB  ALA D 264     2070   2000   1830   -220     60    180       C  
ATOM   2670  N   THR D 265      -0.140 -27.656 -38.933  1.00 17.36           N  
ANISOU 2670  N   THR D 265     2380   2380   1840    -40     40    130       N  
ATOM   2671  CA  THR D 265       0.425 -27.388 -37.580  1.00 18.19           C  
ANISOU 2671  CA  THR D 265     2510   2580   1820     60    -40     90       C  
ATOM   2672  C   THR D 265       1.113 -28.669 -37.081  1.00 18.37           C  
ANISOU 2672  C   THR D 265     2510   2650   1810     70     20    220       C  
ATOM   2673  O   THR D 265       1.082 -29.673 -37.809  1.00 17.59           O  
ANISOU 2673  O   THR D 265     2410   2480   1790     20     90    310       O  
ATOM   2674  CB  THR D 265      -0.655 -26.969 -36.574  1.00 19.45           C  
ANISOU 2674  CB  THR D 265     2680   2890   1820    210    -30     20       C  
ATOM   2675  OG1 THR D 265      -1.493 -28.099 -36.341  1.00 19.91           O  
ANISOU 2675  OG1 THR D 265     2660   3090   1810    190    130    170       O  
ATOM   2676  CG2 THR D 265      -1.477 -25.784 -37.030  1.00 19.98           C  
ANISOU 2676  CG2 THR D 265     2800   2910   1890    280   -120   -130       C  
ATOM   2677  N   LYS D 266       1.688 -28.651 -35.879  1.00 19.67           N  
ANISOU 2677  N   LYS D 266     2690   2930   1860    170    -30    210       N  
ATOM   2678  CA  LYS D 266       2.346 -29.881 -35.357  1.00 20.47           C  
ANISOU 2678  CA  LYS D 266     2800   3070   1910    210      0    340       C  
ATOM   2679  C   LYS D 266       1.303 -31.003 -35.218  1.00 20.78           C  
ANISOU 2679  C   LYS D 266     2870   3100   1930    170    110    500       C  
ATOM   2680  O   LYS D 266       1.679 -32.164 -35.413  1.00 21.22           O  
ANISOU 2680  O   LYS D 266     2990   3040   2030    170    100    620       O  
ATOM   2681  CB  LYS D 266       3.063 -29.595 -34.034  1.00 22.19           C  
ANISOU 2681  CB  LYS D 266     3020   3430   1980    330    -90    300       C  
ATOM   2682  CG  LYS D 266       4.253 -28.651 -34.149  1.00 22.81           C  
ANISOU 2682  CG  LYS D 266     3060   3500   2110    300   -250    180       C  
ATOM   2683  CD  LYS D 266       5.013 -28.432 -32.861  1.00 24.72           C  
ANISOU 2683  CD  LYS D 266     3300   3880   2210    420   -370    120       C  
ATOM   2684  CE  LYS D 266       6.212 -27.526 -33.048  1.00 25.60           C  
ANISOU 2684  CE  LYS D 266     3350   3980   2390    310   -570     40       C  
ATOM   2685  NZ  LYS D 266       6.968 -27.355 -31.787  1.00 27.65           N  
ANISOU 2685  NZ  LYS D 266     3610   4380   2510    430   -720    -30       N  
ATOM   2686  N   ALA D 267       0.037 -30.653 -34.964  1.00 20.85           N  
ANISOU 2686  N   ALA D 267     2830   3230   1860    150    180    520       N  
ATOM   2687  CA  ALA D 267      -1.066 -31.637 -34.804  1.00 22.36           C  
ANISOU 2687  CA  ALA D 267     3000   3480   2020     40    270    740       C  
ATOM   2688  C   ALA D 267      -1.611 -32.125 -36.160  1.00 21.78           C  
ANISOU 2688  C   ALA D 267     2940   3190   2140   -110    280    760       C  
ATOM   2689  O   ALA D 267      -2.266 -33.177 -36.188  1.00 23.80           O  
ANISOU 2689  O   ALA D 267     3220   3400   2420   -270    280    960       O  
ATOM   2690  CB  ALA D 267      -2.175 -31.006 -33.993  1.00 23.61           C  
ANISOU 2690  CB  ALA D 267     3030   3980   1970    110    340    740       C  
ATOM   2691  N   TYR D 268      -1.374 -31.377 -37.238  1.00 20.55           N  
ANISOU 2691  N   TYR D 268     2790   2930   2100   -100    250    580       N  
ATOM   2692  CA  TYR D 268      -1.876 -31.725 -38.595  1.00 19.53           C  
ANISOU 2692  CA  TYR D 268     2670   2630   2120   -200    250    570       C  
ATOM   2693  C   TYR D 268      -0.848 -31.164 -39.575  1.00 17.89           C  
ANISOU 2693  C   TYR D 268     2480   2320   1990   -140    210    420       C  
ATOM   2694  O   TYR D 268      -1.078 -30.088 -40.148  1.00 17.43           O  
ANISOU 2694  O   TYR D 268     2380   2290   1960   -140    210    310       O  
ATOM   2695  CB  TYR D 268      -3.303 -31.182 -38.720  1.00 19.81           C  
ANISOU 2695  CB  TYR D 268     2600   2820   2110   -260    320    560       C  
ATOM   2696  CG  TYR D 268      -3.997 -31.435 -40.030  1.00 19.28           C  
ANISOU 2696  CG  TYR D 268     2520   2620   2180   -370    320    540       C  
ATOM   2697  CD1 TYR D 268      -4.286 -32.726 -40.443  1.00 20.50           C  
ANISOU 2697  CD1 TYR D 268     2740   2610   2430   -510    260    670       C  
ATOM   2698  CD2 TYR D 268      -4.492 -30.387 -40.790  1.00 18.63           C  
ANISOU 2698  CD2 TYR D 268     2380   2580   2110   -320    330    400       C  
ATOM   2699  CE1 TYR D 268      -4.957 -32.975 -41.630  1.00 20.30           C  
ANISOU 2699  CE1 TYR D 268     2720   2480   2520   -600    220    630       C  
ATOM   2700  CE2 TYR D 268      -5.180 -30.619 -41.971  1.00 18.25           C  
ANISOU 2700  CE2 TYR D 268     2320   2450   2160   -400    320    370       C  
ATOM   2701  CZ  TYR D 268      -5.412 -31.916 -42.391  1.00 18.88           C  
ANISOU 2701  CZ  TYR D 268     2450   2390   2340   -540    270    480       C  
ATOM   2702  OH  TYR D 268      -6.087 -32.153 -43.550  1.00 19.68           O  
ANISOU 2702  OH  TYR D 268     2540   2410   2530   -610    220    430       O  
ATOM   2703  N   ASN D 269       0.242 -31.915 -39.757  1.00 18.20           N  
ANISOU 2703  N   ASN D 269     2570   2290   2050    -70    150    430       N  
ATOM   2704  CA  ASN D 269       1.426 -31.478 -40.550  1.00 17.42           C  
ANISOU 2704  CA  ASN D 269     2420   2230   1970      0    110    340       C  
ATOM   2705  C   ASN D 269       1.142 -31.311 -42.051  1.00 16.53           C  
ANISOU 2705  C   ASN D 269     2270   2080   1930    -20    130    280       C  
ATOM   2706  O   ASN D 269       0.029 -31.637 -42.532  1.00 15.86           O  
ANISOU 2706  O   ASN D 269     2230   1890   1900    -80    140    280       O  
ATOM   2707  CB  ASN D 269       2.637 -32.373 -40.255  1.00 18.67           C  
ANISOU 2707  CB  ASN D 269     2600   2410   2070    150     50    360       C  
ATOM   2708  CG  ASN D 269       2.521 -33.780 -40.786  1.00 19.71           C  
ANISOU 2708  CG  ASN D 269     2880   2370   2240    250    -20    370       C  
ATOM   2709  OD1 ASN D 269       1.982 -34.001 -41.866  1.00 19.67           O  
ANISOU 2709  OD1 ASN D 269     2900   2270   2300    240    -30    310       O  
ATOM   2710  ND2 ASN D 269       3.091 -34.727 -40.064  1.00 21.30           N  
ANISOU 2710  ND2 ASN D 269     3190   2510   2390    380   -100    420       N  
ATOM   2711  N   VAL D 270       2.148 -30.771 -42.747  1.00 15.66           N  
ANISOU 2711  N   VAL D 270     2050   2110   1790     10    110    250       N  
ATOM   2712  CA  VAL D 270       2.081 -30.490 -44.209  1.00 15.26           C  
ANISOU 2712  CA  VAL D 270     1930   2110   1750     10    120    220       C  
ATOM   2713  C   VAL D 270       1.730 -31.764 -44.982  1.00 15.38           C  
ANISOU 2713  C   VAL D 270     2040   2030   1780    150    100    150       C  
ATOM   2714  O   VAL D 270       0.894 -31.673 -45.888  1.00 14.67           O  
ANISOU 2714  O   VAL D 270     1960   1880   1730    110    110    110       O  
ATOM   2715  CB  VAL D 270       3.404 -29.868 -44.697  1.00 15.82           C  
ANISOU 2715  CB  VAL D 270     1820   2450   1740     10    110    270       C  
ATOM   2716  CG1 VAL D 270       3.445 -29.727 -46.211  1.00 16.34           C  
ANISOU 2716  CG1 VAL D 270     1780   2660   1760     40    130    270       C  
ATOM   2717  CG2 VAL D 270       3.658 -28.527 -44.024  1.00 15.80           C  
ANISOU 2717  CG2 VAL D 270     1780   2460   1770   -180     50    330       C  
ATOM   2718  N   THR D 271       2.355 -32.893 -44.642  1.00 16.84           N  
ANISOU 2718  N   THR D 271     2300   2180   1920    320     30    130       N  
ATOM   2719  CA  THR D 271       2.092 -34.180 -45.346  1.00 18.31           C  
ANISOU 2719  CA  THR D 271     2650   2190   2120    490    -90     30       C  
ATOM   2720  C   THR D 271       0.630 -34.587 -45.143  1.00 18.23           C  
ANISOU 2720  C   THR D 271     2790   1890   2250    290   -120     80       C  
ATOM   2721  O   THR D 271      -0.014 -34.977 -46.126  1.00 18.54           O  
ANISOU 2721  O   THR D 271     2890   1820   2330    310   -190      0       O  
ATOM   2722  CB  THR D 271       3.056 -35.269 -44.860  1.00 20.14           C  
ANISOU 2722  CB  THR D 271     2990   2380   2280    740   -210      0       C  
ATOM   2723  OG1 THR D 271       4.367 -34.785 -45.129  1.00 20.55           O  
ANISOU 2723  OG1 THR D 271     2820   2810   2170    910   -160    -30       O  
ATOM   2724  CG2 THR D 271       2.852 -36.612 -45.526  1.00 22.33           C  
ANISOU 2724  CG2 THR D 271     3510   2410   2570    960   -420   -130       C  
ATOM   2725  N   GLN D 272       0.134 -34.484 -43.910  1.00 18.38           N  
ANISOU 2725  N   GLN D 272     2830   1850   2300    120    -80    220       N  
ATOM   2726  CA  GLN D 272      -1.269 -34.863 -43.596  1.00 19.24           C  
ANISOU 2726  CA  GLN D 272     3000   1810   2500   -100   -100    320       C  
ATOM   2727  C   GLN D 272      -2.238 -33.910 -44.299  1.00 18.04           C  
ANISOU 2727  C   GLN D 272     2720   1760   2380   -220    -10    280       C  
ATOM   2728  O   GLN D 272      -3.220 -34.393 -44.884  1.00 18.66           O  
ANISOU 2728  O   GLN D 272     2830   1720   2530   -320    -70    280       O  
ATOM   2729  CB  GLN D 272      -1.490 -34.828 -42.083  1.00 20.48           C  
ANISOU 2729  CB  GLN D 272     3140   2030   2610   -220    -50    500       C  
ATOM   2730  CG  GLN D 272      -0.823 -35.971 -41.331  1.00 22.70           C  
ANISOU 2730  CG  GLN D 272     3590   2150   2880   -150   -180    600       C  
ATOM   2731  CD  GLN D 272      -0.833 -35.753 -39.836  1.00 23.88           C  
ANISOU 2731  CD  GLN D 272     3690   2450   2930   -220   -100    770       C  
ATOM   2732  OE1 GLN D 272      -0.470 -34.685 -39.347  1.00 22.66           O  
ANISOU 2732  OE1 GLN D 272     3400   2530   2680   -160     20    710       O  
ATOM   2733  NE2 GLN D 272      -1.164 -36.797 -39.091  1.00 26.26           N  
ANISOU 2733  NE2 GLN D 272     4130   2610   3240   -340   -200    980       N  
ATOM   2734  N   ALA D 273      -1.940 -32.611 -44.277  1.00 16.65           N  
ANISOU 2734  N   ALA D 273     2410   1770   2140   -190    110    240       N  
ATOM   2735  CA  ALA D 273      -2.841 -31.608 -44.886  1.00 16.07           C  
ANISOU 2735  CA  ALA D 273     2240   1780   2080   -260    170    190       C  
ATOM   2736  C   ALA D 273      -2.667 -31.489 -46.404  1.00 15.75           C  
ANISOU 2736  C   ALA D 273     2190   1740   2060   -180    140     90       C  
ATOM   2737  O   ALA D 273      -3.693 -31.335 -47.080  1.00 15.26           O  
ANISOU 2737  O   ALA D 273     2100   1660   2030   -240    140     50       O  
ATOM   2738  CB  ALA D 273      -2.593 -30.263 -44.249  1.00 15.40           C  
ANISOU 2738  CB  ALA D 273     2090   1820   1940   -250    220    180       C  
ATOM   2739  N   PHE D 274      -1.446 -31.614 -46.933  1.00 16.25           N  
ANISOU 2739  N   PHE D 274     2240   1880   2060    -40    120     50       N  
ATOM   2740  CA  PHE D 274      -1.306 -31.348 -48.388  1.00 16.52           C  
ANISOU 2740  CA  PHE D 274     2210   2020   2050     50    110    -20       C  
ATOM   2741  C   PHE D 274      -0.564 -32.442 -49.161  1.00 18.76           C  
ANISOU 2741  C   PHE D 274     2530   2340   2250    290     30   -120       C  
ATOM   2742  O   PHE D 274      -0.233 -32.172 -50.333  1.00 19.25           O  
ANISOU 2742  O   PHE D 274     2500   2610   2210    410     40   -170       O  
ATOM   2743  CB  PHE D 274      -0.601 -29.999 -48.558  1.00 15.60           C  
ANISOU 2743  CB  PHE D 274     1960   2100   1870      0    170     60       C  
ATOM   2744  CG  PHE D 274      -1.226 -28.886 -47.757  1.00 14.00           C  
ANISOU 2744  CG  PHE D 274     1770   1820   1720   -160    190    110       C  
ATOM   2745  CD1 PHE D 274      -2.481 -28.392 -48.085  1.00 13.08           C  
ANISOU 2745  CD1 PHE D 274     1680   1640   1650   -210    190     70       C  
ATOM   2746  CD2 PHE D 274      -0.544 -28.303 -46.698  1.00 13.78           C  
ANISOU 2746  CD2 PHE D 274     1740   1810   1690   -220    170    170       C  
ATOM   2747  CE1 PHE D 274      -3.051 -27.362 -47.354  1.00 12.74           C  
ANISOU 2747  CE1 PHE D 274     1670   1550   1620   -260    170     80       C  
ATOM   2748  CE2 PHE D 274      -1.114 -27.270 -45.968  1.00 13.14           C  
ANISOU 2748  CE2 PHE D 274     1710   1650   1630   -290    130    160       C  
ATOM   2749  CZ  PHE D 274      -2.367 -26.803 -46.296  1.00 12.97           C  
ANISOU 2749  CZ  PHE D 274     1730   1570   1630   -280    130    110       C  
ATOM   2750  N   GLY D 275      -0.345 -33.618 -48.571  1.00 20.67           N  
ANISOU 2750  N   GLY D 275     2380   2760   2710   -610    480   -570       N  
ATOM   2751  CA  GLY D 275       0.355 -34.697 -49.297  1.00 21.37           C  
ANISOU 2751  CA  GLY D 275     2650   2650   2810   -650    520   -510       C  
ATOM   2752  C   GLY D 275       1.868 -34.581 -49.202  1.00 20.57           C  
ANISOU 2752  C   GLY D 275     2720   2370   2730   -450    450   -290       C  
ATOM   2753  O   GLY D 275       2.383 -33.482 -48.915  1.00 17.88           O  
ANISOU 2753  O   GLY D 275     2320   2080   2390   -290    350   -200       O  
ATOM   2754  N   ARG D 276       2.576 -35.675 -49.479  1.00 23.03           N  
ANISOU 2754  N   ARG D 276     3240   2480   3030   -450    510   -230       N  
ATOM   2755  CA  ARG D 276       4.052 -35.613 -49.370  1.00 23.69           C  
ANISOU 2755  CA  ARG D 276     3430   2460   3110   -230    430    -70       C  
ATOM   2756  C   ARG D 276       4.626 -34.755 -50.504  1.00 21.25           C  
ANISOU 2756  C   ARG D 276     2960   2270   2840   -100    320    -80       C  
ATOM   2757  O   ARG D 276       4.016 -34.686 -51.608  1.00 20.29           O  
ANISOU 2757  O   ARG D 276     2760   2220   2730   -150    300   -180       O  
ATOM   2758  CB  ARG D 276       4.686 -37.010 -49.394  1.00 28.77           C  
ANISOU 2758  CB  ARG D 276     4360   2880   3700   -190    510    -20       C  
ATOM   2759  CG  ARG D 276       4.567 -37.736 -50.725  1.00 33.06           C  
ANISOU 2759  CG  ARG D 276     4930   3370   4260   -240    540   -110       C  
ATOM   2760  CD  ARG D 276       5.250 -39.096 -50.718  1.00 39.29           C  
ANISOU 2760  CD  ARG D 276     6050   3900   4980   -150    610    -70       C  
ATOM   2761  NE  ARG D 276       5.162 -39.753 -52.021  1.00 42.10           N  
ANISOU 2761  NE  ARG D 276     6440   4210   5350   -200    640   -160       N  
ATOM   2762  CZ  ARG D 276       4.137 -40.496 -52.437  1.00 46.93           C  
ANISOU 2762  CZ  ARG D 276     7150   4740   5940   -470    770   -300       C  
ATOM   2763  NH1 ARG D 276       4.169 -41.045 -53.641  1.00 48.87           N  
ANISOU 2763  NH1 ARG D 276     7410   4960   6190   -490    780   -390       N  
ATOM   2764  NH2 ARG D 276       3.083 -40.685 -51.658  1.00 49.63           N  
ANISOU 2764  NH2 ARG D 276     7550   5070   6240   -750    900   -370       N  
ATOM   2765  N   ARG D 277       5.742 -34.093 -50.213  1.00 18.62           N  
ANISOU 2765  N   ARG D 277     2600   1970   2510     40    260     10       N  
ATOM   2766  CA  ARG D 277       6.477 -33.290 -51.213  1.00 17.14           C  
ANISOU 2766  CA  ARG D 277     2320   1860   2330    110    200      0       C  
ATOM   2767  C   ARG D 277       6.961 -34.280 -52.280  1.00 18.05           C  
ANISOU 2767  C   ARG D 277     2500   1910   2450    150    230    -40       C  
ATOM   2768  O   ARG D 277       7.288 -35.420 -51.908  1.00 18.05           O  
ANISOU 2768  O   ARG D 277     2620   1800   2440    200    270    -10       O  
ATOM   2769  CB  ARG D 277       7.639 -32.537 -50.559  1.00 16.69           C  
ANISOU 2769  CB  ARG D 277     2210   1870   2260    180    170     50       C  
ATOM   2770  CG  ARG D 277       7.276 -31.255 -49.811  1.00 15.28           C  
ANISOU 2770  CG  ARG D 277     1990   1750   2060    140    140     70       C  
ATOM   2771  CD  ARG D 277       6.270 -31.277 -48.673  1.00 14.95           C  
ANISOU 2771  CD  ARG D 277     1970   1700   2010    100    140     90       C  
ATOM   2772  NE  ARG D 277       4.883 -31.500 -49.057  1.00 14.83           N  
ANISOU 2772  NE  ARG D 277     1930   1690   2010     30    170     20       N  
ATOM   2773  CZ  ARG D 277       4.072 -30.577 -49.576  1.00 14.75           C  
ANISOU 2773  CZ  ARG D 277     1860   1770   1970     50    120    -50       C  
ATOM   2774  NH1 ARG D 277       4.510 -29.351 -49.817  1.00 14.30           N  
ANISOU 2774  NH1 ARG D 277     1840   1720   1870    120     70    -30       N  
ATOM   2775  NH2 ARG D 277       2.820 -30.894 -49.879  1.00 15.23           N  
ANISOU 2775  NH2 ARG D 277     1850   1910   2030      0    130   -170       N  
ATOM   2776  N   GLY D 278       6.945 -33.888 -53.555  1.00 18.09           N  
ANISOU 2776  N   GLY D 278     2470   1960   2450    140    220    -90       N  
ATOM   2777  CA  GLY D 278       7.396 -34.805 -54.619  1.00 18.94           C  
ANISOU 2777  CA  GLY D 278     2630   2010   2550    170    250   -130       C  
ATOM   2778  C   GLY D 278       7.706 -34.073 -55.920  1.00 18.81           C  
ANISOU 2778  C   GLY D 278     2590   2060   2500    170    250   -170       C  
ATOM   2779  O   GLY D 278       7.504 -32.861 -56.033  1.00 17.90           O  
ANISOU 2779  O   GLY D 278     2470   2000   2330    160    220   -160       O  
ATOM   2780  N   PRO D 279       8.204 -34.805 -56.940  1.00 19.19           N  
ANISOU 2780  N   PRO D 279     2680   2080   2530    210    280   -220       N  
ATOM   2781  CA  PRO D 279       8.558 -34.202 -58.224  1.00 19.57           C  
ANISOU 2781  CA  PRO D 279     2750   2170   2510    200    310   -260       C  
ATOM   2782  C   PRO D 279       7.431 -34.103 -59.262  1.00 19.87           C  
ANISOU 2782  C   PRO D 279     2860   2200   2490    180    260   -320       C  
ATOM   2783  O   PRO D 279       7.679 -33.528 -60.314  1.00 20.42           O  
ANISOU 2783  O   PRO D 279     3020   2280   2460    190    270   -340       O  
ATOM   2784  CB  PRO D 279       9.629 -35.179 -58.723  1.00 19.44           C  
ANISOU 2784  CB  PRO D 279     2730   2150   2510    260    370   -310       C  
ATOM   2785  CG  PRO D 279       9.135 -36.529 -58.235  1.00 20.30           C  
ANISOU 2785  CG  PRO D 279     2910   2130   2670    300    360   -310       C  
ATOM   2786  CD  PRO D 279       8.493 -36.250 -56.893  1.00 19.84           C  
ANISOU 2786  CD  PRO D 279     2840   2060   2640    260    320   -240       C  
ATOM   2787  N   GLU D 280       6.241 -34.626 -58.953  1.00 19.74           N  
ANISOU 2787  N   GLU D 280     2810   2190   2500    140    210   -370       N  
ATOM   2788  CA  GLU D 280       5.135 -34.595 -59.952  1.00 21.44           C  
ANISOU 2788  CA  GLU D 280     3030   2470   2640    150    130   -490       C  
ATOM   2789  C   GLU D 280       4.442 -33.226 -59.943  1.00 20.94           C  
ANISOU 2789  C   GLU D 280     2970   2500   2480    240     30   -490       C  
ATOM   2790  O   GLU D 280       4.439 -32.562 -58.892  1.00 19.98           O  
ANISOU 2790  O   GLU D 280     2820   2390   2390    250     20   -420       O  
ATOM   2791  CB  GLU D 280       4.194 -35.779 -59.728  1.00 22.78           C  
ANISOU 2791  CB  GLU D 280     3140   2650   2860     30    150   -610       C  
ATOM   2792  CG  GLU D 280       4.905 -37.106 -59.954  1.00 24.95           C  
ANISOU 2792  CG  GLU D 280     3530   2770   3180    -20    260   -610       C  
ATOM   2793  CD  GLU D 280       4.066 -38.372 -59.886  1.00 26.86           C  
ANISOU 2793  CD  GLU D 280     3820   2950   3440   -190    320   -740       C  
ATOM   2794  OE1 GLU D 280       4.669 -39.473 -59.881  1.00 28.08           O  
ANISOU 2794  OE1 GLU D 280     4140   2920   3610   -210    420   -720       O  
ATOM   2795  OE2 GLU D 280       2.828 -38.266 -59.867  1.00 28.29           O  
ANISOU 2795  OE2 GLU D 280     3870   3280   3600   -310    290   -890       O  
ATOM   2796  N   GLN D 281       3.877 -32.841 -61.093  1.00 22.31           N  
ANISOU 2796  N   GLN D 281     3220   2740   2510    350    -60   -580       N  
ATOM   2797  CA  GLN D 281       3.172 -31.541 -61.278  1.00 24.26           C  
ANISOU 2797  CA  GLN D 281     3560   3060   2600    530   -190   -600       C  
ATOM   2798  C   GLN D 281       2.087 -31.337 -60.210  1.00 23.26           C  
ANISOU 2798  C   GLN D 281     3230   3080   2520    560   -270   -680       C  
ATOM   2799  O   GLN D 281       1.950 -30.201 -59.726  1.00 23.61           O  
ANISOU 2799  O   GLN D 281     3360   3120   2490    680   -320   -620       O  
ATOM   2800  CB  GLN D 281       2.527 -31.481 -62.668  1.00 27.61           C  
ANISOU 2800  CB  GLN D 281     4080   3570   2850    690   -310   -730       C  
ATOM   2801  CG  GLN D 281       1.784 -30.178 -62.954  1.00 30.41           C  
ANISOU 2801  CG  GLN D 281     4590   3990   2980    980   -480   -760       C  
ATOM   2802  CD  GLN D 281       2.708 -28.988 -63.018  1.00 32.06           C  
ANISOU 2802  CD  GLN D 281     5160   3960   3050   1020   -400   -580       C  
ATOM   2803  OE1 GLN D 281       3.869 -29.098 -63.416  1.00 33.67           O  
ANISOU 2803  OE1 GLN D 281     5510   4010   3270    870   -240   -480       O  
ATOM   2804  NE2 GLN D 281       2.186 -27.826 -62.658  1.00 34.44           N  
ANISOU 2804  NE2 GLN D 281     5620   4250   3210   1230   -500   -560       N  
ATOM   2805  N   THR D 282       1.340 -32.391 -59.877  1.00 22.66           N  
ANISOU 2805  N   THR D 282     2930   3130   2550    420   -250   -820       N  
ATOM   2806  CA  THR D 282       0.235 -32.313 -58.882  1.00 22.78           C  
ANISOU 2806  CA  THR D 282     2730   3330   2600    390   -290   -950       C  
ATOM   2807  C   THR D 282       0.740 -32.265 -57.438  1.00 20.62           C  
ANISOU 2807  C   THR D 282     2450   2940   2450    260   -180   -790       C  
ATOM   2808  O   THR D 282      -0.090 -32.002 -56.558  1.00 21.11           O  
ANISOU 2808  O   THR D 282     2360   3140   2520    250   -200   -880       O  
ATOM   2809  CB  THR D 282      -0.665 -33.548 -58.978  1.00 24.45           C  
ANISOU 2809  CB  THR D 282     2730   3700   2860    180   -250  -1180       C  
ATOM   2810  OG1 THR D 282       0.183 -34.655 -58.661  1.00 23.57           O  
ANISOU 2810  OG1 THR D 282     2730   3350   2870    -40    -70  -1060       O  
ATOM   2811  CG2 THR D 282      -1.312 -33.715 -60.334  1.00 25.97           C  
ANISOU 2811  CG2 THR D 282     2860   4070   2930    280   -370  -1390       C  
ATOM   2812  N   GLN D 283       2.031 -32.508 -57.199  1.00 18.18           N  
ANISOU 2812  N   GLN D 283     2280   2420   2210    200    -80   -610       N  
ATOM   2813  CA  GLN D 283       2.547 -32.518 -55.804  1.00 17.02           C  
ANISOU 2813  CA  GLN D 283     2130   2180   2150    110     10   -480       C  
ATOM   2814  C   GLN D 283       3.211 -31.199 -55.408  1.00 15.58           C  
ANISOU 2814  C   GLN D 283     2040   1950   1930    220    -20   -350       C  
ATOM   2815  O   GLN D 283       3.777 -30.518 -56.286  1.00 16.15           O  
ANISOU 2815  O   GLN D 283     2250   1970   1910    310    -40   -310       O  
ATOM   2816  CB  GLN D 283       3.605 -33.611 -55.636  1.00 16.92           C  
ANISOU 2816  CB  GLN D 283     2210   2010   2220     20    120   -390       C  
ATOM   2817  CG  GLN D 283       3.070 -35.029 -55.758  1.00 18.15           C  
ANISOU 2817  CG  GLN D 283     2370   2120   2400   -130    200   -500       C  
ATOM   2818  CD  GLN D 283       4.191 -36.040 -55.725  1.00 18.48           C  
ANISOU 2818  CD  GLN D 283     2570   1970   2480   -120    280   -400       C  
ATOM   2819  OE1 GLN D 283       5.153 -35.963 -56.495  1.00 17.28           O  
ANISOU 2819  OE1 GLN D 283     2460   1790   2320    -20    270   -360       O  
ATOM   2820  NE2 GLN D 283       4.039 -37.040 -54.870  1.00 19.33           N  
ANISOU 2820  NE2 GLN D 283     2800   1950   2600   -230    380   -400       N  
ATOM   2821  N   GLY D 284       3.127 -30.862 -54.118  1.00 14.45           N  
ANISOU 2821  N   GLY D 284     1850   1820   1820    190    -10   -300       N  
ATOM   2822  CA  GLY D 284       3.821 -29.673 -53.592  1.00 13.26           C  
ANISOU 2822  CA  GLY D 284     1790   1610   1630    250    -10   -200       C  
ATOM   2823  C   GLY D 284       5.308 -29.997 -53.506  1.00 12.38           C  
ANISOU 2823  C   GLY D 284     1730   1410   1570    170     70   -100       C  
ATOM   2824  O   GLY D 284       5.638 -31.199 -53.365  1.00 12.25           O  
ANISOU 2824  O   GLY D 284     1660   1370   1630    130    110   -100       O  
ATOM   2825  N   ASN D 285       6.187 -29.000 -53.593  1.00 11.92           N  
ANISOU 2825  N   ASN D 285     1770   1310   1450    170    100    -60       N  
ATOM   2826  CA  ASN D 285       7.647 -29.288 -53.548  1.00 11.51           C  
ANISOU 2826  CA  ASN D 285     1680   1260   1430     90    180    -40       C  
ATOM   2827  C   ASN D 285       8.318 -28.424 -52.483  1.00 11.23           C  
ANISOU 2827  C   ASN D 285     1620   1260   1380     30    200    -10       C  
ATOM   2828  O   ASN D 285       9.558 -28.451 -52.408  1.00 11.45           O  
ANISOU 2828  O   ASN D 285     1580   1360   1420    -40    260    -50       O  
ATOM   2829  CB  ASN D 285       8.331 -28.965 -54.880  1.00 11.97           C  
ANISOU 2829  CB  ASN D 285     1850   1290   1410     50    250    -70       C  
ATOM   2830  CG  ASN D 285       8.337 -27.481 -55.199  1.00 12.79           C  
ANISOU 2830  CG  ASN D 285     2170   1320   1370      0    280    -60       C  
ATOM   2831  OD1 ASN D 285       7.438 -26.738 -54.791  1.00 12.97           O  
ANISOU 2831  OD1 ASN D 285     2300   1300   1330     90    210    -30       O  
ATOM   2832  ND2 ASN D 285       9.350 -27.030 -55.922  1.00 13.29           N  
ANISOU 2832  ND2 ASN D 285     2350   1360   1350   -130    410    -90       N  
ATOM   2833  N   PHE D 286       7.527 -27.734 -51.665  1.00 11.07           N  
ANISOU 2833  N   PHE D 286     1640   1220   1340     50    160     10       N  
ATOM   2834  CA  PHE D 286       8.111 -26.784 -50.686  1.00 11.32           C  
ANISOU 2834  CA  PHE D 286     1690   1270   1340    -20    180     20       C  
ATOM   2835  C   PHE D 286       8.071 -27.294 -49.243  1.00 11.07           C  
ANISOU 2835  C   PHE D 286     1520   1310   1380     10    140     50       C  
ATOM   2836  O   PHE D 286       7.006 -27.756 -48.783  1.00 10.96           O  
ANISOU 2836  O   PHE D 286     1490   1280   1390     70    100     70       O  
ATOM   2837  CB  PHE D 286       7.350 -25.460 -50.781  1.00 11.40           C  
ANISOU 2837  CB  PHE D 286     1910   1190   1240     10    170     30       C  
ATOM   2838  CG  PHE D 286       7.953 -24.312 -50.012  1.00 11.60           C  
ANISOU 2838  CG  PHE D 286     2030   1180   1190   -100    220     20       C  
ATOM   2839  CD1 PHE D 286       7.648 -24.110 -48.677  1.00 11.02           C  
ANISOU 2839  CD1 PHE D 286     1890   1150   1150    -80    180     40       C  
ATOM   2840  CD2 PHE D 286       8.798 -23.410 -50.642  1.00 12.71           C  
ANISOU 2840  CD2 PHE D 286     2380   1240   1210   -260    340    -10       C  
ATOM   2841  CE1 PHE D 286       8.185 -23.036 -47.987  1.00 11.84           C  
ANISOU 2841  CE1 PHE D 286     2090   1230   1180   -200    230     10       C  
ATOM   2842  CE2 PHE D 286       9.337 -22.339 -49.952  1.00 13.52           C  
ANISOU 2842  CE2 PHE D 286     2600   1300   1240   -420    420    -50       C  
ATOM   2843  CZ  PHE D 286       9.032 -22.155 -48.624  1.00 13.26           C  
ANISOU 2843  CZ  PHE D 286     2470   1320   1250   -380    360    -40       C  
ATOM   2844  N   GLY D 287       9.205 -27.135 -48.549  1.00 11.86           N  
ANISOU 2844  N   GLY D 287     1540   1500   1470    -50    160     30       N  
ATOM   2845  CA  GLY D 287       9.337 -27.508 -47.128  1.00 12.01           C  
ANISOU 2845  CA  GLY D 287     1470   1580   1510      0    110     50       C  
ATOM   2846  C   GLY D 287      10.442 -28.507 -46.823  1.00 12.70           C  
ANISOU 2846  C   GLY D 287     1430   1790   1610    100     70     10       C  
ATOM   2847  O   GLY D 287      10.476 -29.583 -47.449  1.00 12.78           O  
ANISOU 2847  O   GLY D 287     1440   1760   1650    190     70     20       O  
ATOM   2848  N   ASP D 288      11.331 -28.149 -45.891  1.00 14.07           N  
ANISOU 2848  N   ASP D 288     1490   2110   1740    100     40    -50       N  
ATOM   2849  CA  ASP D 288      12.380 -29.097 -45.433  1.00 15.35           C  
ANISOU 2849  CA  ASP D 288     1530   2430   1870    280    -40   -120       C  
ATOM   2850  C   ASP D 288      11.675 -30.010 -44.408  1.00 15.53           C  
ANISOU 2850  C   ASP D 288     1710   2330   1870    450   -100     10       C  
ATOM   2851  O   ASP D 288      10.450 -29.825 -44.200  1.00 13.54           O  
ANISOU 2851  O   ASP D 288     1590   1910   1640    360    -60    100       O  
ATOM   2852  CB  ASP D 288      13.635 -28.378 -44.917  1.00 17.05           C  
ANISOU 2852  CB  ASP D 288     1530   2920   2030    220    -60   -290       C  
ATOM   2853  CG  ASP D 288      13.470 -27.591 -43.627  1.00 17.45           C  
ANISOU 2853  CG  ASP D 288     1590   3010   2030    170   -100   -290       C  
ATOM   2854  OD1 ASP D 288      12.363 -27.633 -43.037  1.00 16.76           O  
ANISOU 2854  OD1 ASP D 288     1690   2730   1940    200   -120   -140       O  
ATOM   2855  OD2 ASP D 288      14.463 -26.945 -43.210  1.00 19.00           O  
ANISOU 2855  OD2 ASP D 288     1600   3450   2170     80   -110   -460       O  
ATOM   2856  N   GLN D 289      12.388 -30.932 -43.760  1.00 17.96           N  
ANISOU 2856  N   GLN D 289     2020   2710   2090    700   -200    -10       N  
ATOM   2857  CA  GLN D 289      11.704 -31.846 -42.797  1.00 19.45           C  
ANISOU 2857  CA  GLN D 289     2480   2710   2210    840   -230    120       C  
ATOM   2858  C   GLN D 289      11.144 -31.061 -41.601  1.00 19.18           C  
ANISOU 2858  C   GLN D 289     2490   2670   2130    740   -230    160       C  
ATOM   2859  O   GLN D 289      10.059 -31.427 -41.109  1.00 18.66           O  
ANISOU 2859  O   GLN D 289     2640   2410   2040    690   -160    270       O  
ATOM   2860  CB  GLN D 289      12.648 -32.984 -42.407  1.00 22.30           C  
ANISOU 2860  CB  GLN D 289     2930   3110   2440   1190   -340     90       C  
ATOM   2861  CG  GLN D 289      12.965 -33.887 -43.592  1.00 23.78           C  
ANISOU 2861  CG  GLN D 289     3130   3240   2660   1290   -320     60       C  
ATOM   2862  CD  GLN D 289      13.896 -35.035 -43.288  1.00 28.09           C  
ANISOU 2862  CD  GLN D 289     3800   3820   3050   1700   -440     10       C  
ATOM   2863  OE1 GLN D 289      14.734 -34.974 -42.392  1.00 30.89           O  
ANISOU 2863  OE1 GLN D 289     4080   4380   3270   1960   -590    -70       O  
ATOM   2864  NE2 GLN D 289      13.787 -36.090 -44.081  1.00 31.04           N  
ANISOU 2864  NE2 GLN D 289     4370   4010   3420   1810   -400     40       N  
ATOM   2865  N   GLU D 290      11.808 -29.982 -41.195  1.00 19.46           N  
ANISOU 2865  N   GLU D 290     2330   2910   2150    680   -280     60       N  
ATOM   2866  CA  GLU D 290      11.328 -29.207 -40.021  1.00 19.49           C  
ANISOU 2866  CA  GLU D 290     2390   2920   2100    610   -280    100       C  
ATOM   2867  C   GLU D 290       9.995 -28.527 -40.363  1.00 17.35           C  
ANISOU 2867  C   GLU D 290     2190   2480   1920    390   -170    160       C  
ATOM   2868  O   GLU D 290       9.038 -28.665 -39.572  1.00 16.79           O  
ANISOU 2868  O   GLU D 290     2270   2300   1810    370   -130    240       O  
ATOM   2869  CB  GLU D 290      12.420 -28.225 -39.590  1.00 21.45           C  
ANISOU 2869  CB  GLU D 290     2410   3440   2300    570   -350    -70       C  
ATOM   2870  CG  GLU D 290      12.122 -27.507 -38.296  1.00 22.26           C  
ANISOU 2870  CG  GLU D 290     2570   3560   2330    520   -380    -60       C  
ATOM   2871  CD  GLU D 290      13.223 -26.569 -37.833  1.00 24.62           C  
ANISOU 2871  CD  GLU D 290     2640   4150   2570    450   -440   -250       C  
ATOM   2872  OE1 GLU D 290      14.187 -26.340 -38.604  1.00 26.28           O  
ANISOU 2872  OE1 GLU D 290     2630   4550   2800    370   -430   -420       O  
ATOM   2873  OE2 GLU D 290      13.121 -26.079 -36.698  1.00 26.54           O  
ANISOU 2873  OE2 GLU D 290     2930   4430   2720    450   -490   -260       O  
ATOM   2874  N   LEU D 291       9.916 -27.847 -41.507  1.00 15.88           N  
ANISOU 2874  N   LEU D 291     1920   2290   1820    250   -110    120       N  
ATOM   2875  CA  LEU D 291       8.652 -27.156 -41.870  1.00 14.93           C  
ANISOU 2875  CA  LEU D 291     1880   2050   1740    130    -30    160       C  
ATOM   2876  C   LEU D 291       7.522 -28.170 -42.075  1.00 14.83           C  
ANISOU 2876  C   LEU D 291     1960   1920   1760    150     10    220       C  
ATOM   2877  O   LEU D 291       6.396 -27.884 -41.607  1.00 14.26           O  
ANISOU 2877  O   LEU D 291     1930   1810   1680    100     50    230       O  
ATOM   2878  CB  LEU D 291       8.856 -26.316 -43.132  1.00 14.71           C  
ANISOU 2878  CB  LEU D 291     1830   2020   1750     20     10    100       C  
ATOM   2879  CG  LEU D 291       7.599 -25.631 -43.671  1.00 14.43           C  
ANISOU 2879  CG  LEU D 291     1900   1870   1710      0     40    120       C  
ATOM   2880  CD1 LEU D 291       6.943 -24.764 -42.606  1.00 14.67           C  
ANISOU 2880  CD1 LEU D 291     1990   1890   1690      0     40    120       C  
ATOM   2881  CD2 LEU D 291       7.929 -24.796 -44.897  1.00 14.79           C  
ANISOU 2881  CD2 LEU D 291     2020   1860   1730    -70     90     70       C  
ATOM   2882  N   ILE D 292       7.813 -29.282 -42.760  1.00 15.34           N  
ANISOU 2882  N   ILE D 292     2040   1940   1850    210     20    240       N  
ATOM   2883  CA  ILE D 292       6.809 -30.349 -43.060  1.00 16.20           C  
ANISOU 2883  CA  ILE D 292     2260   1920   1980    180     90    260       C  
ATOM   2884  C   ILE D 292       6.179 -30.871 -41.759  1.00 17.64           C  
ANISOU 2884  C   ILE D 292     2600   2030   2080    160    150    310       C  
ATOM   2885  O   ILE D 292       4.943 -31.021 -41.713  1.00 18.03           O  
ANISOU 2885  O   ILE D 292     2670   2050   2140     20    250    280       O  
ATOM   2886  CB  ILE D 292       7.467 -31.472 -43.889  1.00 17.01           C  
ANISOU 2886  CB  ILE D 292     2410   1960   2090    260     90    270       C  
ATOM   2887  CG1 ILE D 292       7.818 -30.973 -45.295  1.00 16.34           C  
ANISOU 2887  CG1 ILE D 292     2190   1940   2080    230     80    210       C  
ATOM   2888  CG2 ILE D 292       6.574 -32.708 -43.942  1.00 18.35           C  
ANISOU 2888  CG2 ILE D 292     2760   1970   2240    200    190    290       C  
ATOM   2889  CD1 ILE D 292       8.612 -31.950 -46.140  1.00 17.42           C  
ANISOU 2889  CD1 ILE D 292     2340   2050   2230    330     70    190       C  
ATOM   2890  N   ARG D 293       7.000 -31.092 -40.735  1.00 18.31           N  
ANISOU 2890  N   ARG D 293     2780   2110   2060    290     90    360       N  
ATOM   2891  CA  ARG D 293       6.538 -31.627 -39.430  1.00 20.23           C  
ANISOU 2891  CA  ARG D 293     3250   2250   2180    280    150    420       C  
ATOM   2892  C   ARG D 293       5.835 -30.553 -38.587  1.00 18.95           C  
ANISOU 2892  C   ARG D 293     3020   2180   2010    170    180    400       C  
ATOM   2893  O   ARG D 293       5.002 -30.941 -37.735  1.00 19.50           O  
ANISOU 2893  O   ARG D 293     3250   2170   1990     80    290    420       O  
ATOM   2894  CB  ARG D 293       7.758 -32.170 -38.670  1.00 23.50           C  
ANISOU 2894  CB  ARG D 293     3820   2660   2450    540     30    470       C  
ATOM   2895  CG  ARG D 293       7.463 -32.673 -37.265  1.00 27.03           C  
ANISOU 2895  CG  ARG D 293     4580   2980   2700    590     70    550       C  
ATOM   2896  CD  ARG D 293       8.658 -33.280 -36.540  1.00 30.95           C  
ANISOU 2896  CD  ARG D 293     5270   3480   3010    930    -80    580       C  
ATOM   2897  NE  ARG D 293       9.762 -32.358 -36.280  1.00 32.37           N  
ANISOU 2897  NE  ARG D 293     5150   3950   3190   1090   -270    490       N  
ATOM   2898  CZ  ARG D 293      10.853 -32.213 -37.036  1.00 33.22           C  
ANISOU 2898  CZ  ARG D 293     4990   4260   3360   1220   -390    380       C  
ATOM   2899  NH1 ARG D 293      11.784 -31.342 -36.680  1.00 33.71           N  
ANISOU 2899  NH1 ARG D 293     4780   4620   3410   1280   -530    250       N  
ATOM   2900  NH2 ARG D 293      11.021 -32.934 -38.131  1.00 34.04           N  
ANISOU 2900  NH2 ARG D 293     5100   4290   3540   1270   -370    370       N  
ATOM   2901  N   GLN D 294       6.081 -29.267 -38.853  1.00 17.06           N  
ANISOU 2901  N   GLN D 294     2570   2080   1840    170    100    340       N  
ATOM   2902  CA  GLN D 294       5.510 -28.211 -37.976  1.00 17.20           C  
ANISOU 2902  CA  GLN D 294     2560   2160   1820    110    120    320       C  
ATOM   2903  C   GLN D 294       4.484 -27.296 -38.658  1.00 15.93           C  
ANISOU 2903  C   GLN D 294     2270   2050   1740     20    160    240       C  
ATOM   2904  O   GLN D 294       3.661 -26.720 -37.910  1.00 15.05           O  
ANISOU 2904  O   GLN D 294     2150   1980   1590    -10    200    200       O  
ATOM   2905  CB  GLN D 294       6.679 -27.409 -37.413  1.00 17.87           C  
ANISOU 2905  CB  GLN D 294     2590   2350   1860    180      0    300       C  
ATOM   2906  CG  GLN D 294       7.625 -28.271 -36.588  1.00 19.81           C  
ANISOU 2906  CG  GLN D 294     2940   2610   1980    340    -80    340       C  
ATOM   2907  CD  GLN D 294       8.819 -27.502 -36.088  1.00 20.82           C  
ANISOU 2907  CD  GLN D 294     2940   2920   2050    410   -210    260       C  
ATOM   2908  OE1 GLN D 294       9.095 -26.388 -36.527  1.00 20.86           O  
ANISOU 2908  OE1 GLN D 294     2790   3010   2120    300   -210    170       O  
ATOM   2909  NE2 GLN D 294       9.558 -28.113 -35.179  1.00 22.89           N  
ANISOU 2909  NE2 GLN D 294     3290   3240   2160    610   -310    270       N  
ATOM   2910  N   GLY D 295       4.524 -27.139 -39.985  1.00 14.91           N  
ANISOU 2910  N   GLY D 295     2050   1920   1690     30    130    200       N  
ATOM   2911  CA  GLY D 295       3.552 -26.243 -40.646  1.00 14.23           C  
ANISOU 2911  CA  GLY D 295     1900   1880   1630     40    130    120       C  
ATOM   2912  C   GLY D 295       3.641 -24.819 -40.104  1.00 14.15           C  
ANISOU 2912  C   GLY D 295     1930   1890   1560     80     90     90       C  
ATOM   2913  O   GLY D 295       4.776 -24.320 -39.951  1.00 13.63           O  
ANISOU 2913  O   GLY D 295     1910   1800   1470     60     50    120       O  
ATOM   2914  N   THR D 296       2.495 -24.209 -39.767  1.00 14.04           N  
ANISOU 2914  N   THR D 296     1890   1930   1510    130    110     20       N  
ATOM   2915  CA  THR D 296       2.454 -22.808 -39.264  1.00 14.29           C  
ANISOU 2915  CA  THR D 296     2020   1950   1460    200     80    -20       C  
ATOM   2916  C   THR D 296       3.132 -22.678 -37.892  1.00 14.62           C  
ANISOU 2916  C   THR D 296     2110   1990   1460    120     90     30       C  
ATOM   2917  O   THR D 296       3.239 -21.531 -37.413  1.00 15.15           O  
ANISOU 2917  O   THR D 296     2280   2030   1450    150     70      0       O  
ATOM   2918  CB  THR D 296       1.019 -22.265 -39.265  1.00 15.11           C  
ANISOU 2918  CB  THR D 296     2060   2150   1520    330     80   -140       C  
ATOM   2919  OG1 THR D 296       0.204 -23.069 -38.416  1.00 15.33           O  
ANISOU 2919  OG1 THR D 296     1950   2310   1560    250    170   -200       O  
ATOM   2920  CG2 THR D 296       0.416 -22.246 -40.652  1.00 15.68           C  
ANISOU 2920  CG2 THR D 296     2090   2260   1600    460     20   -220       C  
ATOM   2921  N   ASP D 297       3.543 -23.791 -37.274  1.00 14.73           N  
ANISOU 2921  N   ASP D 297     2100   2020   1480     60    110    100       N  
ATOM   2922  CA  ASP D 297       4.255 -23.739 -35.966  1.00 15.51           C  
ANISOU 2922  CA  ASP D 297     2270   2130   1490     40    100    130       C  
ATOM   2923  C   ASP D 297       5.759 -23.571 -36.227  1.00 15.76           C  
ANISOU 2923  C   ASP D 297     2280   2180   1520     30     10    140       C  
ATOM   2924  O   ASP D 297       6.510 -23.400 -35.240  1.00 16.62           O  
ANISOU 2924  O   ASP D 297     2410   2350   1550     40    -40    130       O  
ATOM   2925  CB  ASP D 297       3.981 -24.981 -35.110  1.00 16.57           C  
ANISOU 2925  CB  ASP D 297     2470   2260   1570     20    160    190       C  
ATOM   2926  CG  ASP D 297       2.574 -25.039 -34.546  1.00 17.34           C  
ANISOU 2926  CG  ASP D 297     2560   2390   1640    -40    280    130       C  
ATOM   2927  OD1 ASP D 297       2.135 -24.016 -33.957  1.00 17.72           O  
ANISOU 2927  OD1 ASP D 297     2600   2490   1640    -20    290     70       O  
ATOM   2928  OD2 ASP D 297       1.911 -26.073 -34.740  1.00 17.24           O  
ANISOU 2928  OD2 ASP D 297     2560   2360   1630   -130    390    130       O  
ATOM   2929  N   TYR D 298       6.177 -23.641 -37.498  1.00 15.18           N  
ANISOU 2929  N   TYR D 298     2160   2080   1530     20      0    130       N  
ATOM   2930  CA  TYR D 298       7.611 -23.488 -37.884  1.00 15.47           C  
ANISOU 2930  CA  TYR D 298     2130   2190   1560    -30    -50     90       C  
ATOM   2931  C   TYR D 298       8.133 -22.155 -37.335  1.00 16.00           C  
ANISOU 2931  C   TYR D 298     2240   2290   1550   -130    -40      0       C  
ATOM   2932  O   TYR D 298       7.411 -21.158 -37.445  1.00 15.50           O  
ANISOU 2932  O   TYR D 298     2310   2120   1460   -160      0    -20       O  
ATOM   2933  CB  TYR D 298       7.754 -23.628 -39.404  1.00 14.52           C  
ANISOU 2933  CB  TYR D 298     1980   2020   1520    -60    -20     80       C  
ATOM   2934  CG  TYR D 298       9.155 -23.517 -39.953  1.00 15.04           C  
ANISOU 2934  CG  TYR D 298     1950   2180   1580   -140    -20      0       C  
ATOM   2935  CD1 TYR D 298      10.092 -24.501 -39.699  1.00 15.85           C  
ANISOU 2935  CD1 TYR D 298     1910   2420   1680    -50    -90    -30       C  
ATOM   2936  CD2 TYR D 298       9.519 -22.485 -40.803  1.00 15.14           C  
ANISOU 2936  CD2 TYR D 298     2040   2140   1570   -290     50    -70       C  
ATOM   2937  CE1 TYR D 298      11.379 -24.424 -40.208  1.00 16.86           C  
ANISOU 2937  CE1 TYR D 298     1890   2720   1810   -120   -100   -160       C  
ATOM   2938  CE2 TYR D 298      10.800 -22.397 -41.327  1.00 16.34           C  
ANISOU 2938  CE2 TYR D 298     2080   2420   1720   -430     90   -190       C  
ATOM   2939  CZ  TYR D 298      11.735 -23.372 -41.034  1.00 16.99           C  
ANISOU 2939  CZ  TYR D 298     1930   2710   1820   -340     10   -250       C  
ATOM   2940  OH  TYR D 298      12.998 -23.313 -41.549  1.00 17.87           O  
ANISOU 2940  OH  TYR D 298     1860   3020   1910   -470     50   -420       O  
ATOM   2941  N   LYS D 299       9.345 -22.159 -36.764  1.00 17.63           N  
ANISOU 2941  N   LYS D 299     2340   2650   1710   -180   -100    -90       N  
ATOM   2942  CA  LYS D 299       9.973 -20.953 -36.148  1.00 19.55           C  
ANISOU 2942  CA  LYS D 299     2610   2960   1860   -330    -90   -220       C  
ATOM   2943  C   LYS D 299       9.985 -19.757 -37.112  1.00 19.17           C  
ANISOU 2943  C   LYS D 299     2710   2770   1800   -530     30   -280       C  
ATOM   2944  O   LYS D 299       9.789 -18.633 -36.620  1.00 19.81           O  
ANISOU 2944  O   LYS D 299     2960   2760   1800   -630     80   -330       O  
ATOM   2945  CB  LYS D 299      11.395 -21.274 -35.680  1.00 22.14           C  
ANISOU 2945  CB  LYS D 299     2720   3560   2130   -350   -170   -360       C  
ATOM   2946  CG  LYS D 299      12.307 -21.837 -36.760  1.00 24.05           C  
ANISOU 2946  CG  LYS D 299     2780   3930   2430   -380   -170   -430       C  
ATOM   2947  CD  LYS D 299      13.701 -22.190 -36.289  1.00 27.14           C  
ANISOU 2947  CD  LYS D 299     2890   4670   2750   -340   -280   -630       C  
ATOM   2948  CE  LYS D 299      14.512 -22.858 -37.384  1.00 29.03           C  
ANISOU 2948  CE  LYS D 299     2930   5050   3050   -310   -270   -720       C  
ATOM   2949  NZ  LYS D 299      15.891 -23.174 -36.938  1.00 33.01           N  
ANISOU 2949  NZ  LYS D 299     3100   5970   3470   -230   -400   -970       N  
ATOM   2950  N   HIS D 300      10.195 -19.979 -38.415  1.00 19.30           N  
ANISOU 2950  N   HIS D 300     2710   2660   1960    310   -380    290       N  
ATOM   2951  CA  HIS D 300      10.232 -18.844 -39.379  1.00 18.81           C  
ANISOU 2951  CA  HIS D 300     2590   2590   1960    300   -340    230       C  
ATOM   2952  C   HIS D 300       8.985 -18.845 -40.269  1.00 17.17           C  
ANISOU 2952  C   HIS D 300     2400   2340   1780    270   -280    250       C  
ATOM   2953  O   HIS D 300       9.067 -18.315 -41.401  1.00 16.52           O  
ANISOU 2953  O   HIS D 300     2290   2240   1750    260   -260    220       O  
ATOM   2954  CB  HIS D 300      11.523 -18.847 -40.209  1.00 19.38           C  
ANISOU 2954  CB  HIS D 300     2610   2660   2090    330   -360    200       C  
ATOM   2955  CG  HIS D 300      12.759 -18.758 -39.385  1.00 21.06           C  
ANISOU 2955  CG  HIS D 300     2800   2920   2280    360   -420    180       C  
ATOM   2956  ND1 HIS D 300      13.635 -19.817 -39.252  1.00 23.33           N  
ANISOU 2956  ND1 HIS D 300     3090   3210   2570    420   -480    190       N  
ATOM   2957  CD2 HIS D 300      13.234 -17.772 -38.596  1.00 22.60           C  
ANISOU 2957  CD2 HIS D 300     2960   3170   2460    350   -430    130       C  
ATOM   2958  CE1 HIS D 300      14.628 -19.469 -38.457  1.00 23.48           C  
ANISOU 2958  CE1 HIS D 300     3070   3280   2570    440   -520    160       C  
ATOM   2959  NE2 HIS D 300      14.402 -18.223 -38.036  1.00 24.05           N  
ANISOU 2959  NE2 HIS D 300     3120   3390   2630    400   -490    130       N  
ATOM   2960  N   TRP D 301       7.874 -19.403 -39.785  1.00 16.46           N  
ANISOU 2960  N   TRP D 301     2360   2250   1640    240   -270    290       N  
ATOM   2961  CA  TRP D 301       6.640 -19.395 -40.615  1.00 15.68           C  
ANISOU 2961  CA  TRP D 301     2270   2120   1560    210   -210    290       C  
ATOM   2962  C   TRP D 301       6.247 -17.967 -41.031  1.00 15.27           C  
ANISOU 2962  C   TRP D 301     2180   2080   1540    190   -180    230       C  
ATOM   2963  O   TRP D 301       5.888 -17.752 -42.185  1.00 14.94           O  
ANISOU 2963  O   TRP D 301     2130   2000   1550    190   -150    220       O  
ATOM   2964  CB  TRP D 301       5.482 -20.129 -39.937  1.00 15.50           C  
ANISOU 2964  CB  TRP D 301     2300   2100   1480    180   -200    330       C  
ATOM   2965  CG  TRP D 301       4.269 -20.046 -40.801  1.00 14.92           C  
ANISOU 2965  CG  TRP D 301     2230   2000   1430    150   -140    330       C  
ATOM   2966  CD1 TRP D 301       3.156 -19.285 -40.594  1.00 14.69           C  
ANISOU 2966  CD1 TRP D 301     2190   2010   1380    120   -100    290       C  
ATOM   2967  CD2 TRP D 301       4.133 -20.607 -42.118  1.00 14.19           C  
ANISOU 2967  CD2 TRP D 301     2140   1850   1400    160   -130    340       C  
ATOM   2968  NE1 TRP D 301       2.306 -19.393 -41.660  1.00 14.01           N  
ANISOU 2968  NE1 TRP D 301     2100   1890   1340    110    -70    290       N  
ATOM   2969  CE2 TRP D 301       2.876 -20.201 -42.609  1.00 13.77           C  
ANISOU 2969  CE2 TRP D 301     2080   1800   1350    130    -80    320       C  
ATOM   2970  CE3 TRP D 301       4.930 -21.439 -42.912  1.00 14.04           C  
ANISOU 2970  CE3 TRP D 301     2120   1780   1430    200   -160    360       C  
ATOM   2971  CZ2 TRP D 301       2.401 -20.601 -43.858  1.00 13.24           C  
ANISOU 2971  CZ2 TRP D 301     2010   1680   1330    140    -60    320       C  
ATOM   2972  CZ3 TRP D 301       4.456 -21.839 -44.143  1.00 13.64           C  
ANISOU 2972  CZ3 TRP D 301     2070   1690   1420    200   -130    360       C  
ATOM   2973  CH2 TRP D 301       3.212 -21.419 -44.609  1.00 13.19           C  
ANISOU 2973  CH2 TRP D 301     2010   1630   1370    170    -80    340       C  
ATOM   2974  N   PRO D 302       6.242 -16.941 -40.143  1.00 15.77           N  
ANISOU 2974  N   PRO D 302     2220   2190   1580    180   -190    180       N  
ATOM   2975  CA  PRO D 302       5.875 -15.586 -40.563  1.00 15.72           C  
ANISOU 2975  CA  PRO D 302     2190   2170   1620    170   -170    130       C  
ATOM   2976  C   PRO D 302       6.732 -15.084 -41.739  1.00 15.93           C  
ANISOU 2976  C   PRO D 302     2180   2160   1710    170   -170    120       C  
ATOM   2977  O   PRO D 302       6.180 -14.426 -42.609  1.00 15.41           O  
ANISOU 2977  O   PRO D 302     2110   2060   1690    160   -150    110       O  
ATOM   2978  CB  PRO D 302       6.106 -14.724 -39.311  1.00 16.20           C  
ANISOU 2978  CB  PRO D 302     2220   2290   1640    160   -190     70       C  
ATOM   2979  CG  PRO D 302       5.958 -15.704 -38.160  1.00 16.47           C  
ANISOU 2979  CG  PRO D 302     2290   2380   1590    160   -200    110       C  
ATOM   2980  CD  PRO D 302       6.489 -17.022 -38.694  1.00 16.43           C  
ANISOU 2980  CD  PRO D 302     2320   2330   1590    180   -210    180       C  
ATOM   2981  N   GLN D 303       8.034 -15.403 -41.740  1.00 16.29           N  
ANISOU 2981  N   GLN D 303     2210   2210   1770    190   -200    130       N  
ATOM   2982  CA  GLN D 303       8.944 -14.977 -42.841  1.00 16.95           C  
ANISOU 2982  CA  GLN D 303     2250   2280   1910    180   -210    120       C  
ATOM   2983  C   GLN D 303       8.557 -15.674 -44.162  1.00 16.02           C  
ANISOU 2983  C   GLN D 303     2150   2130   1810    190   -180    150       C  
ATOM   2984  O   GLN D 303       8.947 -15.170 -45.237  1.00 16.27           O  
ANISOU 2984  O   GLN D 303     2150   2150   1890    170   -170    150       O  
ATOM   2985  CB  GLN D 303      10.411 -15.216 -42.465  1.00 18.46           C  
ANISOU 2985  CB  GLN D 303     2410   2510   2090    210   -240    110       C  
ATOM   2986  CG  GLN D 303      10.930 -14.288 -41.369  1.00 20.32           C  
ANISOU 2986  CG  GLN D 303     2630   2780   2310    200   -270     60       C  
ATOM   2987  CD  GLN D 303      10.346 -14.524 -39.994  1.00 22.49           C  
ANISOU 2987  CD  GLN D 303     2930   3090   2520    210   -290     60       C  
ATOM   2988  OE1 GLN D 303       9.861 -15.602 -39.671  1.00 24.72           O  
ANISOU 2988  OE1 GLN D 303     3260   3370   2760    230   -280    110       O  
ATOM   2989  NE2 GLN D 303      10.436 -13.515 -39.140  1.00 24.93           N  
ANISOU 2989  NE2 GLN D 303     3220   3430   2820    200   -300     10       N  
ATOM   2990  N   ILE D 304       7.832 -16.790 -44.097  1.00 15.05           N  
ANISOU 2990  N   ILE D 304     2060   1990   1670    200   -160    190       N  
ATOM   2991  CA  ILE D 304       7.384 -17.504 -45.332  1.00 14.37           C  
ANISOU 2991  CA  ILE D 304     1980   1870   1610    210   -140    210       C  
ATOM   2992  C   ILE D 304       6.008 -16.963 -45.726  1.00 13.58           C  
ANISOU 2992  C   ILE D 304     1900   1750   1520    180   -100    210       C  
ATOM   2993  O   ILE D 304       5.822 -16.625 -46.914  1.00 13.17           O  
ANISOU 2993  O   ILE D 304     1830   1680   1500    170    -80    210       O  
ATOM   2994  CB  ILE D 304       7.359 -19.032 -45.112  1.00 14.72           C  
ANISOU 2994  CB  ILE D 304     2060   1900   1630    240   -150    240       C  
ATOM   2995  CG1 ILE D 304       8.775 -19.583 -44.902  1.00 15.15           C  
ANISOU 2995  CG1 ILE D 304     2090   1970   1690    280   -200    240       C  
ATOM   2996  CG2 ILE D 304       6.639 -19.729 -46.261  1.00 14.09           C  
ANISOU 2996  CG2 ILE D 304     1990   1780   1580    240   -120    260       C  
ATOM   2997  CD1 ILE D 304       8.828 -21.039 -44.504  1.00 15.85           C  
ANISOU 2997  CD1 ILE D 304     2220   2030   1770    320   -240    270       C  
ATOM   2998  N   ALA D 305       5.098 -16.877 -44.752  1.00 13.33           N  
ANISOU 2998  N   ALA D 305     1890   1720   1450    170   -100    200       N  
ATOM   2999  CA  ALA D 305       3.714 -16.392 -44.965  1.00 13.17           C  
ANISOU 2999  CA  ALA D 305     1880   1690   1430    150    -70    190       C  
ATOM   3000  C   ALA D 305       3.702 -14.976 -45.558  1.00 13.29           C  
ANISOU 3000  C   ALA D 305     1870   1690   1490    140    -70    150       C  
ATOM   3001  O   ALA D 305       2.696 -14.641 -46.212  1.00 13.08           O  
ANISOU 3001  O   ALA D 305     1850   1640   1480    130    -50    140       O  
ATOM   3002  CB  ALA D 305       2.951 -16.443 -43.668  1.00 13.36           C  
ANISOU 3002  CB  ALA D 305     1920   1760   1400    140    -60    170       C  
ATOM   3003  N   GLN D 306       4.773 -14.187 -45.375  1.00 13.47           N  
ANISOU 3003  N   GLN D 306     1870   1720   1530    130   -100    130       N  
ATOM   3004  CA  GLN D 306       4.762 -12.806 -45.933  1.00 13.56           C  
ANISOU 3004  CA  GLN D 306     1860   1700   1590    110   -110    110       C  
ATOM   3005  C   GLN D 306       4.666 -12.849 -47.464  1.00 13.29           C  
ANISOU 3005  C   GLN D 306     1830   1630   1590    100   -100    140       C  
ATOM   3006  O   GLN D 306       4.265 -11.831 -48.052  1.00 13.46           O  
ANISOU 3006  O   GLN D 306     1850   1620   1650     80   -110    140       O  
ATOM   3007  CB  GLN D 306       5.999 -12.007 -45.506  1.00 13.92           C  
ANISOU 3007  CB  GLN D 306     1880   1750   1650    100   -150     90       C  
ATOM   3008  CG  GLN D 306       7.319 -12.570 -46.008  1.00 13.84           C  
ANISOU 3008  CG  GLN D 306     1850   1770   1640     90   -150    120       C  
ATOM   3009  CD  GLN D 306       8.484 -11.785 -45.452  1.00 14.39           C  
ANISOU 3009  CD  GLN D 306     1890   1860   1720     80   -180     90       C  
ATOM   3010  OE1 GLN D 306       8.404 -10.572 -45.263  1.00 14.77           O  
ANISOU 3010  OE1 GLN D 306     1930   1880   1800     50   -210     60       O  
ATOM   3011  NE2 GLN D 306       9.586 -12.471 -45.202  1.00 13.95           N  
ANISOU 3011  NE2 GLN D 306     1810   1850   1650     90   -190     90       N  
ATOM   3012  N   PHE D 307       5.001 -13.983 -48.082  1.00 13.21           N  
ANISOU 3012  N   PHE D 307     1820   1640   1570    110    -80    180       N  
ATOM   3013  CA  PHE D 307       4.955 -14.083 -49.566  1.00 13.13           C  
ANISOU 3013  CA  PHE D 307     1800   1620   1580     90    -60    200       C  
ATOM   3014  C   PHE D 307       3.625 -14.687 -50.034  1.00 12.78           C  
ANISOU 3014  C   PHE D 307     1780   1550   1530    110    -30    210       C  
ATOM   3015  O   PHE D 307       3.344 -14.614 -51.233  1.00 12.96           O  
ANISOU 3015  O   PHE D 307     1790   1570   1560     90    -20    230       O  
ATOM   3016  CB  PHE D 307       6.168 -14.860 -50.080  1.00 13.12           C  
ANISOU 3016  CB  PHE D 307     1760   1650   1570    100    -60    210       C  
ATOM   3017  CG  PHE D 307       7.470 -14.223 -49.680  1.00 13.80           C  
ANISOU 3017  CG  PHE D 307     1820   1770   1660     80    -80    200       C  
ATOM   3018  CD1 PHE D 307       7.852 -13.008 -50.225  1.00 14.24           C  
ANISOU 3018  CD1 PHE D 307     1860   1820   1740     30    -90    210       C  
ATOM   3019  CD2 PHE D 307       8.316 -14.834 -48.772  1.00 14.02           C  
ANISOU 3019  CD2 PHE D 307     1830   1830   1670    110   -100    180       C  
ATOM   3020  CE1 PHE D 307       9.039 -12.404 -49.844  1.00 14.75           C  
ANISOU 3020  CE1 PHE D 307     1890   1910   1810     10   -120    190       C  
ATOM   3021  CE2 PHE D 307       9.509 -14.234 -48.406  1.00 14.69           C  
ANISOU 3021  CE2 PHE D 307     1880   1940   1760     90   -130    170       C  
ATOM   3022  CZ  PHE D 307       9.865 -13.018 -48.940  1.00 14.80           C  
ANISOU 3022  CZ  PHE D 307     1870   1950   1790     40   -130    170       C  
ATOM   3023  N   ALA D 308       2.840 -15.260 -49.120  1.00 12.84           N  
ANISOU 3023  N   ALA D 308     1810   1560   1510    120    -20    200       N  
ATOM   3024  CA  ALA D 308       1.536 -15.852 -49.498  1.00 12.26           C  
ANISOU 3024  CA  ALA D 308     1750   1480   1430    130      0    200       C  
ATOM   3025  C   ALA D 308       0.578 -14.729 -49.875  1.00 12.16           C  
ANISOU 3025  C   ALA D 308     1730   1450   1440    120      0    180       C  
ATOM   3026  O   ALA D 308       0.514 -13.701 -49.208  1.00 12.42           O  
ANISOU 3026  O   ALA D 308     1760   1470   1480    120    -20    150       O  
ATOM   3027  CB  ALA D 308       0.979 -16.691 -48.370  1.00 12.50           C  
ANISOU 3027  CB  ALA D 308     1800   1530   1420    130     10    200       C  
ATOM   3028  N   PRO D 309      -0.209 -14.891 -50.954  1.00 11.82           N  
ANISOU 3028  N   PRO D 309     1690   1390   1410    120     20    190       N  
ATOM   3029  CA  PRO D 309      -1.131 -13.843 -51.375  1.00 11.81           C  
ANISOU 3029  CA  PRO D 309     1690   1360   1430    120      0    160       C  
ATOM   3030  C   PRO D 309      -2.470 -13.771 -50.630  1.00 11.83           C  
ANISOU 3030  C   PRO D 309     1690   1380   1420    140     10    120       C  
ATOM   3031  O   PRO D 309      -2.981 -14.803 -50.215  1.00 11.77           O  
ANISOU 3031  O   PRO D 309     1690   1400   1380    130     40    110       O  
ATOM   3032  CB  PRO D 309      -1.417 -14.234 -52.833  1.00 11.58           C  
ANISOU 3032  CB  PRO D 309     1660   1330   1410    120     10    190       C  
ATOM   3033  CG  PRO D 309      -1.351 -15.743 -52.809  1.00 11.65           C  
ANISOU 3033  CG  PRO D 309     1670   1360   1390    120     50    200       C  
ATOM   3034  CD  PRO D 309      -0.234 -16.064 -51.838  1.00 11.67           C  
ANISOU 3034  CD  PRO D 309     1670   1380   1380    120     40    210       C  
ATOM   3035  N   SER D 310      -2.963 -12.543 -50.440  1.00 11.88           N  
ANISOU 3035  N   SER D 310     1690   1360   1460    150    -30     70       N  
ATOM   3036  CA  SER D 310      -4.304 -12.329 -49.847  1.00 12.15           C  
ANISOU 3036  CA  SER D 310     1710   1420   1480    170    -20     10       C  
ATOM   3037  C   SER D 310      -5.296 -12.942 -50.844  1.00 11.75           C  
ANISOU 3037  C   SER D 310     1660   1370   1430    170      0     20       C  
ATOM   3038  O   SER D 310      -4.861 -13.226 -51.966  1.00 10.68           O  
ANISOU 3038  O   SER D 310     1540   1210   1310    160      0     70       O  
ATOM   3039  CB  SER D 310      -4.588 -10.865 -49.672  1.00 12.61           C  
ANISOU 3039  CB  SER D 310     1760   1440   1590    190    -80    -40       C  
ATOM   3040  OG  SER D 310      -4.614 -10.211 -50.945  1.00 12.83           O  
ANISOU 3040  OG  SER D 310     1810   1400   1660    190   -110    -10       O  
ATOM   3041  N   ALA D 311      -6.567 -13.116 -50.479  1.00 12.07           N  
ANISOU 3041  N   ALA D 311     1680   1450   1460    180     20    -40       N  
ATOM   3042  CA  ALA D 311      -7.524 -13.681 -51.461  1.00 11.95           C  
ANISOU 3042  CA  ALA D 311     1660   1440   1440    180     40    -40       C  
ATOM   3043  C   ALA D 311      -7.617 -12.743 -52.676  1.00 12.03           C  
ANISOU 3043  C   ALA D 311     1670   1390   1500    210    -10    -20       C  
ATOM   3044  O   ALA D 311      -7.621 -13.247 -53.817  1.00 12.30           O  
ANISOU 3044  O   ALA D 311     1720   1420   1540    200     10     20       O  
ATOM   3045  CB  ALA D 311      -8.874 -13.886 -50.817  1.00 12.50           C  
ANISOU 3045  CB  ALA D 311     1700   1570   1480    190     60   -110       C  
ATOM   3046  N   SER D 312      -7.664 -11.431 -52.429  1.00 12.16           N  
ANISOU 3046  N   SER D 312     1690   1370   1560    230    -60    -60       N  
ATOM   3047  CA  SER D 312      -7.762 -10.393 -53.494  1.00 12.70           C  
ANISOU 3047  CA  SER D 312     1770   1380   1680    250   -120    -40       C  
ATOM   3048  C   SER D 312      -6.560 -10.479 -54.451  1.00 12.34           C  
ANISOU 3048  C   SER D 312     1750   1300   1630    210   -120     50       C  
ATOM   3049  O   SER D 312      -6.776 -10.447 -55.678  1.00 12.13           O  
ANISOU 3049  O   SER D 312     1740   1260   1610    210   -140     90       O  
ATOM   3050  CB  SER D 312      -7.878  -9.012 -52.884  1.00 13.33           C  
ANISOU 3050  CB  SER D 312     1850   1410   1810    280   -190   -100       C  
ATOM   3051  OG  SER D 312      -8.051  -8.022 -53.887  1.00 13.72           O  
ANISOU 3051  OG  SER D 312     1920   1380   1910    290   -260    -80       O  
ATOM   3052  N   ALA D 313      -5.346 -10.563 -53.900  1.00 12.21           N  
ANISOU 3052  N   ALA D 313     1750   1290   1610    180   -110     80       N  
ATOM   3053  CA  ALA D 313      -4.103 -10.655 -54.702  1.00 12.16           C  
ANISOU 3053  CA  ALA D 313     1750   1270   1590    140   -110    150       C  
ATOM   3054  C   ALA D 313      -4.038 -11.999 -55.429  1.00 11.73           C  
ANISOU 3054  C   ALA D 313     1690   1270   1500    130    -60    180       C  
ATOM   3055  O   ALA D 313      -3.502 -12.043 -56.555  1.00 11.85           O  
ANISOU 3055  O   ALA D 313     1710   1290   1510    110    -60    230       O  
ATOM   3056  CB  ALA D 313      -2.902 -10.479 -53.808  1.00 12.30           C  
ANISOU 3056  CB  ALA D 313     1770   1290   1610    120   -110    160       C  
ATOM   3057  N   PHE D 314      -4.538 -13.062 -54.798  1.00 11.56           N  
ANISOU 3057  N   PHE D 314     1660   1280   1450    150    -10    150       N  
ATOM   3058  CA  PHE D 314      -4.496 -14.390 -55.454  1.00 11.53           C  
ANISOU 3058  CA  PHE D 314     1650   1310   1420    140     30    170       C  
ATOM   3059  C   PHE D 314      -5.302 -14.332 -56.758  1.00 11.67           C  
ANISOU 3059  C   PHE D 314     1660   1330   1440    140     30    180       C  
ATOM   3060  O   PHE D 314      -4.802 -14.804 -57.783  1.00 12.01           O  
ANISOU 3060  O   PHE D 314     1700   1390   1470    130     40    210       O  
ATOM   3061  CB  PHE D 314      -4.989 -15.485 -54.506  1.00 11.17           C  
ANISOU 3061  CB  PHE D 314     1600   1290   1350    140     70    150       C  
ATOM   3062  CG  PHE D 314      -5.098 -16.841 -55.154  1.00 10.94           C  
ANISOU 3062  CG  PHE D 314     1570   1280   1310    140    100    160       C  
ATOM   3063  CD1 PHE D 314      -3.970 -17.632 -55.341  1.00 10.79           C  
ANISOU 3063  CD1 PHE D 314     1550   1270   1280    130    110    190       C  
ATOM   3064  CD2 PHE D 314      -6.330 -17.336 -55.564  1.00 10.81           C  
ANISOU 3064  CD2 PHE D 314     1540   1280   1290    140    120    130       C  
ATOM   3065  CE1 PHE D 314      -4.070 -18.878 -55.938  1.00 10.62           C  
ANISOU 3065  CE1 PHE D 314     1520   1250   1250    130    130    190       C  
ATOM   3066  CE2 PHE D 314      -6.425 -18.582 -56.166  1.00 10.56           C  
ANISOU 3066  CE2 PHE D 314     1510   1260   1250    130    150    140       C  
ATOM   3067  CZ  PHE D 314      -5.295 -19.351 -56.348  1.00 10.60           C  
ANISOU 3067  CZ  PHE D 314     1520   1260   1250    130    150    170       C  
ATOM   3068  N   PHE D 315      -6.499 -13.748 -56.712  1.00 12.17           N  
ANISOU 3068  N   PHE D 315     1720   1380   1520    170     10    140       N  
ATOM   3069  CA  PHE D 315      -7.351 -13.656 -57.930  1.00 12.58           C  
ANISOU 3069  CA  PHE D 315     1770   1440   1580    180    -10    140       C  
ATOM   3070  C   PHE D 315      -6.988 -12.435 -58.776  1.00 12.97           C  
ANISOU 3070  C   PHE D 315     1830   1450   1650    170    -60    190       C  
ATOM   3071  O   PHE D 315      -7.465 -12.358 -59.926  1.00 13.42           O  
ANISOU 3071  O   PHE D 315     1890   1510   1700    170    -80    210       O  
ATOM   3072  CB  PHE D 315      -8.837 -13.646 -57.574  1.00 12.66           C  
ANISOU 3072  CB  PHE D 315     1760   1460   1590    210    -10     70       C  
ATOM   3073  CG  PHE D 315      -9.366 -15.015 -57.239  1.00 12.56           C  
ANISOU 3073  CG  PHE D 315     1730   1490   1550    200     50     50       C  
ATOM   3074  CD1 PHE D 315      -9.700 -15.893 -58.260  1.00 12.25           C  
ANISOU 3074  CD1 PHE D 315     1680   1480   1500    190     80     60       C  
ATOM   3075  CD2 PHE D 315      -9.526 -15.429 -55.927  1.00 12.26           C  
ANISOU 3075  CD2 PHE D 315     1680   1470   1500    190     80     20       C  
ATOM   3076  CE1 PHE D 315     -10.181 -17.160 -57.974  1.00 12.13           C  
ANISOU 3076  CE1 PHE D 315     1650   1490   1470    180    120     30       C  
ATOM   3077  CE2 PHE D 315      -9.999 -16.699 -55.646  1.00 12.25           C  
ANISOU 3077  CE2 PHE D 315     1670   1510   1470    170    130      0       C  
ATOM   3078  CZ  PHE D 315     -10.337 -17.555 -56.669  1.00 12.14           C  
ANISOU 3078  CZ  PHE D 315     1650   1500   1450    160    150     10       C  
ATOM   3079  N   GLY D 316      -6.154 -11.541 -58.247  1.00 13.24           N  
ANISOU 3079  N   GLY D 316     1880   1440   1700    160   -100    210       N  
ATOM   3080  CA  GLY D 316      -5.782 -10.342 -59.018  1.00 13.80           C  
ANISOU 3080  CA  GLY D 316     1980   1470   1800    140   -160    260       C  
ATOM   3081  C   GLY D 316      -4.455 -10.501 -59.733  1.00 13.98           C  
ANISOU 3081  C   GLY D 316     2000   1520   1790     80   -140    330       C  
ATOM   3082  O   GLY D 316      -4.342  -9.965 -60.826  1.00 14.38           O  
ANISOU 3082  O   GLY D 316     2070   1560   1830     50   -180    390       O  
ATOM   3083  N   MET D 317      -3.514 -11.265 -59.166  1.00 14.02           N  
ANISOU 3083  N   MET D 317     1990   1560   1780     60   -100    330       N  
ATOM   3084  CA  MET D 317      -2.157 -11.422 -59.767  1.00 14.17           C  
ANISOU 3084  CA  MET D 317     2000   1620   1770     10    -80    380       C  
ATOM   3085  C   MET D 317      -2.029 -12.689 -60.622  1.00 14.08           C  
ANISOU 3085  C   MET D 317     1960   1680   1710     10    -30    380       C  
ATOM   3086  O   MET D 317      -1.350 -12.625 -61.639  1.00 14.21           O  
ANISOU 3086  O   MET D 317     1960   1750   1700    -30    -30    420       O  
ATOM   3087  CB  MET D 317      -1.084 -11.539 -58.678  1.00 14.40           C  
ANISOU 3087  CB  MET D 317     2020   1650   1800      0    -70    360       C  
ATOM   3088  CG  MET D 317      -1.025 -10.391 -57.696  1.00 15.17           C  
ANISOU 3088  CG  MET D 317     2140   1690   1940      0   -120    350       C  
ATOM   3089  SD  MET D 317       0.306 -10.611 -56.458  1.00 16.10           S  
ANISOU 3089  SD  MET D 317     2240   1830   2050    -10   -100    330       S  
ATOM   3090  CE  MET D 317      -0.040 -12.271 -55.878  1.00 15.72           C  
ANISOU 3090  CE  MET D 317     2170   1830   1970     40    -40    290       C  
ATOM   3091  N   SER D 318      -2.673 -13.783 -60.216  1.00 13.71           N  
ANISOU 3091  N   SER D 318     1900   1650   1660     50     10    330       N  
ATOM   3092  CA  SER D 318      -2.546 -15.109 -60.875  1.00 13.24           C  
ANISOU 3092  CA  SER D 318     1810   1650   1570     60     50    310       C  
ATOM   3093  C   SER D 318      -3.258 -15.238 -62.224  1.00 13.56           C  
ANISOU 3093  C   SER D 318     1840   1720   1590     60     50    320       C  
ATOM   3094  O   SER D 318      -4.221 -14.496 -62.497  1.00 13.68           O  
ANISOU 3094  O   SER D 318     1870   1710   1620     70     20    330       O  
ATOM   3095  CB  SER D 318      -3.122 -16.174 -59.964  1.00 12.94           C  
ANISOU 3095  CB  SER D 318     1770   1600   1540    100     80    270       C  
ATOM   3096  OG  SER D 318      -2.616 -16.070 -58.646  1.00 12.53           O  
ANISOU 3096  OG  SER D 318     1740   1520   1510    100     70    260       O  
ATOM   3097  N   ARG D 319      -2.772 -16.194 -63.020  1.00 13.81           N  
ANISOU 3097  N   ARG D 319     1840   1820   1590     50     80    310       N  
ATOM   3098  CA  ARG D 319      -3.425 -16.593 -64.287  1.00 13.66           C  
ANISOU 3098  CA  ARG D 319     1800   1840   1550     60     90    300       C  
ATOM   3099  C   ARG D 319      -4.339 -17.735 -63.843  1.00 13.45           C  
ANISOU 3099  C   ARG D 319     1770   1800   1540    100    120    240       C  
ATOM   3100  O   ARG D 319      -3.821 -18.753 -63.338  1.00 13.89           O  
ANISOU 3100  O   ARG D 319     1820   1860   1600    110    140    220       O  
ATOM   3101  CB  ARG D 319      -2.450 -16.962 -65.405  1.00 13.98           C  
ANISOU 3101  CB  ARG D 319     1800   1980   1540     30    110    310       C  
ATOM   3102  CG  ARG D 319      -1.599 -15.787 -65.861  1.00 14.63           C  
ANISOU 3102  CG  ARG D 319     1880   2080   1590    -30     80    380       C  
ATOM   3103  CD  ARG D 319      -1.064 -15.959 -67.264  1.00 15.29           C  
ANISOU 3103  CD  ARG D 319     1920   2280   1610    -70    100    390       C  
ATOM   3104  NE  ARG D 319      -2.147 -16.178 -68.210  1.00 15.15           N  
ANISOU 3104  NE  ARG D 319     1900   2280   1570    -50    100    380       N  
ATOM   3105  CZ  ARG D 319      -2.930 -15.231 -68.730  1.00 15.59           C  
ANISOU 3105  CZ  ARG D 319     1990   2320   1610    -70     50    440       C  
ATOM   3106  NH1 ARG D 319      -2.776 -13.962 -68.392  1.00 15.65           N  
ANISOU 3106  NH1 ARG D 319     2040   2260   1640   -110     10    500       N  
ATOM   3107  NH2 ARG D 319      -3.883 -15.566 -69.585  1.00 15.62           N  
ANISOU 3107  NH2 ARG D 319     1990   2350   1600    -50     50    420       N  
ATOM   3108  N   ILE D 320      -5.646 -17.513 -63.911  1.00 13.52           N  
ANISOU 3108  N   ILE D 320     1790   1780   1560    120    110    230       N  
ATOM   3109  CA  ILE D 320      -6.632 -18.526 -63.440  1.00 13.74           C  
ANISOU 3109  CA  ILE D 320     1820   1800   1610    140    130    180       C  
ATOM   3110  C   ILE D 320      -7.213 -19.269 -64.641  1.00 14.35           C  
ANISOU 3110  C   ILE D 320     1870   1920   1660    150    140    150       C  
ATOM   3111  O   ILE D 320      -7.456 -18.637 -65.687  1.00 14.45           O  
ANISOU 3111  O   ILE D 320     1870   1970   1650    140    120    170       O  
ATOM   3112  CB  ILE D 320      -7.736 -17.859 -62.596  1.00 13.35           C  
ANISOU 3112  CB  ILE D 320     1790   1700   1580    150    110    160       C  
ATOM   3113  CG1 ILE D 320      -7.163 -17.056 -61.423  1.00 13.06           C  
ANISOU 3113  CG1 ILE D 320     1780   1630   1560    150    100    180       C  
ATOM   3114  CG2 ILE D 320      -8.755 -18.887 -62.124  1.00 13.11           C  
ANISOU 3114  CG2 ILE D 320     1750   1670   1560    160    140    110       C  
ATOM   3115  CD1 ILE D 320      -6.422 -17.878 -60.408  1.00 12.99           C  
ANISOU 3115  CD1 ILE D 320     1770   1610   1550    140    120    170       C  
ATOM   3116  N   GLY D 321      -7.419 -20.571 -64.473  1.00 15.32           N  
ANISOU 3116  N   GLY D 321     1980   2040   1800    160    170    100       N  
ATOM   3117  CA  GLY D 321      -8.005 -21.421 -65.520  1.00 16.60           C  
ANISOU 3117  CA  GLY D 321     2110   2250   1950    160    190     60       C  
ATOM   3118  C   GLY D 321      -8.930 -22.441 -64.895  1.00 18.38           C  
ANISOU 3118  C   GLY D 321     2340   2440   2200    170    210     10       C  
ATOM   3119  O   GLY D 321      -8.844 -22.648 -63.660  1.00 16.31           O  
ANISOU 3119  O   GLY D 321     2110   2130   1970    160    210     20       O  
ATOM   3120  N   MET D 322      -9.810 -23.036 -65.696  1.00 20.87           N  
ANISOU 3120  N   MET D 322     2630   2780   2520    170    210    -30       N  
ATOM   3121  CA  MET D 322     -10.703 -24.064 -65.122  1.00 25.48           C  
ANISOU 3121  CA  MET D 322     3220   3330   3130    160    230    -70       C  
ATOM   3122  C   MET D 322     -10.618 -25.292 -66.031  1.00 25.86           C  
ANISOU 3122  C   MET D 322     3240   3400   3190    170    240   -120       C  
ATOM   3123  O   MET D 322     -11.022 -25.184 -67.205  1.00 24.29           O  
ANISOU 3123  O   MET D 322     3010   3250   2960    180    240   -150       O  
ATOM   3124  CB  MET D 322     -12.137 -23.548 -64.999  1.00 28.93           C  
ANISOU 3124  CB  MET D 322     3650   3780   3570    160    230    -90       C  
ATOM   3125  CG  MET D 322     -12.947 -24.348 -64.015  1.00 34.72           C  
ANISOU 3125  CG  MET D 322     4390   4480   4320    130    260   -120       C  
ATOM   3126  SD  MET D 322     -14.491 -23.527 -63.600  1.00 45.01           S  
ANISOU 3126  SD  MET D 322     5670   5810   5620    130    260   -150       S  
ATOM   3127  CE  MET D 322     -15.010 -24.541 -62.220  1.00 47.33           C  
ANISOU 3127  CE  MET D 322     5980   6080   5920     70    290   -170       C  
ATOM   3128  N   GLU D 323     -10.040 -26.383 -65.522  1.00 27.22           N  
ANISOU 3128  N   GLU D 323     3430   3520   3390    170    240   -130       N  
ATOM   3129  CA  GLU D 323      -9.905 -27.615 -66.341  1.00 29.74           C  
ANISOU 3129  CA  GLU D 323     3720   3850   3730    180    240   -190       C  
ATOM   3130  C   GLU D 323     -10.945 -28.659 -65.931  1.00 28.83           C  
ANISOU 3130  C   GLU D 323     3620   3680   3660    150    250   -230       C  
ATOM   3131  O   GLU D 323     -10.981 -29.048 -64.752  1.00 26.39           O  
ANISOU 3131  O   GLU D 323     3350   3300   3370    120    250   -200       O  
ATOM   3132  CB  GLU D 323      -8.499 -28.201 -66.234  1.00 32.44           C  
ANISOU 3132  CB  GLU D 323     4070   4170   4090    200    230   -200       C  
ATOM   3133  CG  GLU D 323      -7.433 -27.283 -66.791  1.00 36.06           C  
ANISOU 3133  CG  GLU D 323     4500   4700   4510    220    220   -170       C  
ATOM   3134  CD  GLU D 323      -6.048 -27.901 -66.852  1.00 39.96           C  
ANISOU 3134  CD  GLU D 323     4970   5190   5010    240    210   -200       C  
ATOM   3135  OE1 GLU D 323      -5.934 -29.119 -66.581  1.00 42.88           O  
ANISOU 3135  OE1 GLU D 323     5350   5500   5430    260    190   -240       O  
ATOM   3136  OE2 GLU D 323      -5.088 -27.164 -67.168  1.00 43.00           O  
ANISOU 3136  OE2 GLU D 323     5340   5640   5360    250    210   -180       O  
ATOM   3137  N   VAL D 324     -11.747 -29.081 -66.907  1.00 29.53           N  
ANISOU 3137  N   VAL D 324     3670   3800   3740    150    250   -280       N  
ATOM   3138  CA  VAL D 324     -12.791 -30.126 -66.731  1.00 31.47           C  
ANISOU 3138  CA  VAL D 324     3920   4010   4030    120    260   -330       C  
ATOM   3139  C   VAL D 324     -12.186 -31.436 -67.241  1.00 32.81           C  
ANISOU 3139  C   VAL D 324     4080   4140   4240    130    240   -380       C  
ATOM   3140  O   VAL D 324     -12.012 -31.565 -68.469  1.00 36.43           O  
ANISOU 3140  O   VAL D 324     4490   4660   4690    170    230   -440       O  
ATOM   3141  CB  VAL D 324     -14.079 -29.759 -67.492  1.00 31.14           C  
ANISOU 3141  CB  VAL D 324     3840   4030   3960    110    270   -370       C  
ATOM   3142  CG1 VAL D 324     -15.100 -30.883 -67.464  1.00 32.91           C  
ANISOU 3142  CG1 VAL D 324     4060   4220   4220     70    280   -420       C  
ATOM   3143  CG2 VAL D 324     -14.684 -28.466 -66.971  1.00 30.64           C  
ANISOU 3143  CG2 VAL D 324     3780   4000   3860    100    280   -330       C  
ATOM   3144  N   THR D 325     -11.844 -32.345 -66.331  1.00 31.91           N  
ANISOU 3144  N   THR D 325     4020   3930   4180    120    220   -360       N  
ATOM   3145  CA  THR D 325     -11.249 -33.650 -66.719  1.00 32.45           C  
ANISOU 3145  CA  THR D 325     4080   3940   4310    140    190   -420       C  
ATOM   3146  C   THR D 325     -12.224 -34.755 -66.330  1.00 34.00           C  
ANISOU 3146  C   THR D 325     4310   4050   4550     80    180   -440       C  
ATOM   3147  O   THR D 325     -13.147 -34.516 -65.554  1.00 34.01           O  
ANISOU 3147  O   THR D 325     4330   4050   4540     20    200   -390       O  
ATOM   3148  CB  THR D 325      -9.901 -33.881 -66.025  1.00 30.99           C  
ANISOU 3148  CB  THR D 325     3930   3700   4140    170    150   -380       C  
ATOM   3149  OG1 THR D 325     -10.159 -34.152 -64.649  1.00 30.65           O  
ANISOU 3149  OG1 THR D 325     3960   3570   4120    120    150   -310       O  
ATOM   3150  CG2 THR D 325      -8.948 -32.716 -66.171  1.00 30.93           C  
ANISOU 3150  CG2 THR D 325     3900   3770   4080    210    170   -350       C  
ATOM   3151  N   PRO D 326     -12.078 -35.989 -66.865  1.00 36.93           N  
ANISOU 3151  N   PRO D 326     4680   4370   4990    100    140   -510       N  
ATOM   3152  CA  PRO D 326     -12.968 -37.087 -66.486  1.00 36.82           C  
ANISOU 3152  CA  PRO D 326     4700   4260   5030     40    120   -520       C  
ATOM   3153  C   PRO D 326     -12.938 -37.352 -64.968  1.00 36.66           C  
ANISOU 3153  C   PRO D 326     4760   4140   5030    -20    110   -420       C  
ATOM   3154  O   PRO D 326     -13.936 -37.807 -64.447  1.00 35.94           O  
ANISOU 3154  O   PRO D 326     4690   4020   4950   -110    120   -400       O  
ATOM   3155  CB  PRO D 326     -12.428 -38.296 -67.265  1.00 37.53           C  
ANISOU 3155  CB  PRO D 326     4770   4290   5200     80     70   -610       C  
ATOM   3156  CG  PRO D 326     -11.643 -37.689 -68.418  1.00 37.68           C  
ANISOU 3156  CG  PRO D 326     4720   4430   5170    160     80   -670       C  
ATOM   3157  CD  PRO D 326     -11.096 -36.378 -67.890  1.00 36.97           C  
ANISOU 3157  CD  PRO D 326     4640   4400   5010    170    110   -580       C  
ATOM   3158  N   SER D 327     -11.829 -37.005 -64.297  1.00 35.77           N  
ANISOU 3158  N   SER D 327     4670   4010   4900     10    100   -360       N  
ATOM   3159  CA  SER D 327     -11.681 -37.237 -62.832  1.00 35.37           C  
ANISOU 3159  CA  SER D 327     4700   3880   4860    -40     80   -270       C  
ATOM   3160  C   SER D 327     -12.101 -36.013 -61.996  1.00 33.92           C  
ANISOU 3160  C   SER D 327     4520   3770   4600    -80    130   -200       C  
ATOM   3161  O   SER D 327     -11.906 -36.069 -60.766  1.00 36.83           O  
ANISOU 3161  O   SER D 327     4950   4090   4960   -120    120   -120       O  
ATOM   3162  CB  SER D 327     -10.269 -37.633 -62.501  1.00 35.91           C  
ANISOU 3162  CB  SER D 327     4800   3870   4970     20     20   -250       C  
ATOM   3163  OG  SER D 327      -9.378 -36.561 -62.762  1.00 36.20           O  
ANISOU 3163  OG  SER D 327     4800   4000   4950     80     40   -250       O  
ATOM   3164  N   GLY D 328     -12.623 -34.941 -62.604  1.00 30.90           N  
ANISOU 3164  N   GLY D 328     4080   3500   4160    -60    180   -220       N  
ATOM   3165  CA  GLY D 328     -13.044 -33.776 -61.792  1.00 27.77           C  
ANISOU 3165  CA  GLY D 328     3690   3160   3700    -90    220   -170       C  
ATOM   3166  C   GLY D 328     -12.776 -32.426 -62.447  1.00 25.34           C  
ANISOU 3166  C   GLY D 328     3330   2950   3350    -30    240   -190       C  
ATOM   3167  O   GLY D 328     -12.154 -32.381 -63.532  1.00 23.50           O  
ANISOU 3167  O   GLY D 328     3060   2750   3120     20    230   -230       O  
ATOM   3168  N   THR D 329     -13.247 -31.358 -61.795  1.00 22.81           N  
ANISOU 3168  N   THR D 329     3000   2680   2980    -50    270   -150       N  
ATOM   3169  CA  THR D 329     -13.077 -29.961 -62.273  1.00 21.70           C  
ANISOU 3169  CA  THR D 329     2830   2620   2800      0    280   -160       C  
ATOM   3170  C   THR D 329     -12.040 -29.268 -61.376  1.00 20.38           C  
ANISOU 3170  C   THR D 329     2690   2440   2610     10    270   -100       C  
ATOM   3171  O   THR D 329     -12.248 -29.244 -60.142  1.00 19.08           O  
ANISOU 3171  O   THR D 329     2560   2250   2440    -30    280    -60       O  
ATOM   3172  CB  THR D 329     -14.428 -29.236 -62.315  1.00 21.72           C  
ANISOU 3172  CB  THR D 329     2790   2690   2770    -30    310   -180       C  
ATOM   3173  OG1 THR D 329     -15.307 -29.967 -63.173  1.00 22.54           O  
ANISOU 3173  OG1 THR D 329     2870   2800   2890    -40    310   -240       O  
ATOM   3174  CG2 THR D 329     -14.309 -27.811 -62.806  1.00 21.48           C  
ANISOU 3174  CG2 THR D 329     2740   2720   2710     20    310   -180       C  
ATOM   3175  N   TRP D 330     -11.000 -28.689 -61.987  1.00 19.37           N  
ANISOU 3175  N   TRP D 330     2550   2330   2480     70    260    -90       N  
ATOM   3176  CA  TRP D 330      -9.903 -28.031 -61.234  1.00 19.45           C  
ANISOU 3176  CA  TRP D 330     2580   2330   2480     80    240    -40       C  
ATOM   3177  C   TRP D 330      -9.754 -26.550 -61.582  1.00 18.62           C  
ANISOU 3177  C   TRP D 330     2450   2280   2340    110    250    -30       C  
ATOM   3178  O   TRP D 330      -9.831 -26.197 -62.775  1.00 18.29           O  
ANISOU 3178  O   TRP D 330     2380   2290   2280    130    250    -60       O  
ATOM   3179  CB  TRP D 330      -8.582 -28.753 -61.528  1.00 20.81           C  
ANISOU 3179  CB  TRP D 330     2760   2470   2680    120    220    -50       C  
ATOM   3180  CG  TRP D 330      -8.562 -30.197 -61.130  1.00 22.34           C  
ANISOU 3180  CG  TRP D 330     2990   2590   2910    100    190    -50       C  
ATOM   3181  CD1 TRP D 330      -9.089 -31.250 -61.823  1.00 23.20           C  
ANISOU 3181  CD1 TRP D 330     3090   2670   3060    100    190   -100       C  
ATOM   3182  CD2 TRP D 330      -7.939 -30.754 -59.962  1.00 22.72           C  
ANISOU 3182  CD2 TRP D 330     3090   2560   2980     90    170    -10       C  
ATOM   3183  NE1 TRP D 330      -8.867 -32.418 -61.149  1.00 24.32           N  
ANISOU 3183  NE1 TRP D 330     3280   2720   3250     80    150    -90       N  
ATOM   3184  CE2 TRP D 330      -8.162 -32.147 -60.005  1.00 24.15           C  
ANISOU 3184  CE2 TRP D 330     3300   2670   3210     80    140    -20       C  
ATOM   3185  CE3 TRP D 330      -7.237 -30.213 -58.878  1.00 22.67           C  
ANISOU 3185  CE3 TRP D 330     3110   2550   2950     90    160     50       C  
ATOM   3186  CZ2 TRP D 330      -7.699 -33.004 -59.006  1.00 25.29           C  
ANISOU 3186  CZ2 TRP D 330     3500   2720   3380     60    100     20       C  
ATOM   3187  CZ3 TRP D 330      -6.772 -31.062 -57.897  1.00 24.26           C  
ANISOU 3187  CZ3 TRP D 330     3370   2680   3170     80    120     90       C  
ATOM   3188  CH2 TRP D 330      -7.004 -32.438 -57.959  1.00 24.99           C  
ANISOU 3188  CH2 TRP D 330     3490   2690   3320     70     90     80       C  
ATOM   3189  N   LEU D 331      -9.526 -25.734 -60.552  1.00 17.89           N  
ANISOU 3189  N   LEU D 331     2380   2190   2230    100    250     10       N  
ATOM   3190  CA  LEU D 331      -9.254 -24.283 -60.696  1.00 17.49           C  
ANISOU 3190  CA  LEU D 331     2320   2170   2150    120    240     30       C  
ATOM   3191  C   LEU D 331      -7.727 -24.182 -60.750  1.00 16.26           C  
ANISOU 3191  C   LEU D 331     2170   2010   2000    140    220     50       C  
ATOM   3192  O   LEU D 331      -7.090 -24.438 -59.712  1.00 16.08           O  
ANISOU 3192  O   LEU D 331     2180   1950   1980    130    220     80       O  
ATOM   3193  CB  LEU D 331      -9.815 -23.523 -59.491  1.00 18.69           C  
ANISOU 3193  CB  LEU D 331     2490   2320   2290    100    240     40       C  
ATOM   3194  CG  LEU D 331      -9.681 -22.003 -59.557  1.00 19.23           C  
ANISOU 3194  CG  LEU D 331     2550   2410   2350    120    220     50       C  
ATOM   3195  CD1 LEU D 331     -10.538 -21.450 -60.685  1.00 20.07           C  
ANISOU 3195  CD1 LEU D 331     2620   2540   2460    140    220     20       C  
ATOM   3196  CD2 LEU D 331     -10.081 -21.358 -58.235  1.00 20.12           C  
ANISOU 3196  CD2 LEU D 331     2670   2520   2460    110    220     40       C  
ATOM   3197  N   THR D 332      -7.158 -23.902 -61.917  1.00 15.50           N  
ANISOU 3197  N   THR D 332     2050   1950   1890    160    220     50       N  
ATOM   3198  CA  THR D 332      -5.676 -23.834 -62.012  1.00 14.97           C  
ANISOU 3198  CA  THR D 332     1970   1890   1820    170    200     60       C  
ATOM   3199  C   THR D 332      -5.218 -22.412 -61.717  1.00 14.28           C  
ANISOU 3199  C   THR D 332     1890   1820   1720    160    190    110       C  
ATOM   3200  O   THR D 332      -5.992 -21.467 -61.969  1.00 14.05           O  
ANISOU 3200  O   THR D 332     1860   1800   1680    150    190    110       O  
ATOM   3201  CB  THR D 332      -5.164 -24.295 -63.379  1.00 14.96           C  
ANISOU 3201  CB  THR D 332     1930   1950   1810    190    200     30       C  
ATOM   3202  OG1 THR D 332      -5.681 -23.381 -64.344  1.00 14.88           O  
ANISOU 3202  OG1 THR D 332     1890   1990   1770    180    210     40       O  
ATOM   3203  CG2 THR D 332      -5.565 -25.719 -63.702  1.00 15.12           C  
ANISOU 3203  CG2 THR D 332     1940   1950   1860    200    210    -20       C  
ATOM   3204  N   TYR D 333      -3.996 -22.285 -61.208  1.00 13.63           N  
ANISOU 3204  N   TYR D 333     1810   1730   1640    170    180    120       N  
ATOM   3205  CA  TYR D 333      -3.456 -20.948 -60.885  1.00 13.09           C  
ANISOU 3205  CA  TYR D 333     1750   1670   1560    150    170    160       C  
ATOM   3206  C   TYR D 333      -1.949 -20.956 -61.099  1.00 13.03           C  
ANISOU 3206  C   TYR D 333     1710   1700   1540    150    160    170       C  
ATOM   3207  O   TYR D 333      -1.286 -21.987 -60.824  1.00 13.26           O  
ANISOU 3207  O   TYR D 333     1730   1720   1580    170    160    150       O  
ATOM   3208  CB  TYR D 333      -3.802 -20.545 -59.452  1.00 12.76           C  
ANISOU 3208  CB  TYR D 333     1740   1580   1530    150    160    180       C  
ATOM   3209  CG  TYR D 333      -3.213 -21.420 -58.373  1.00 12.52           C  
ANISOU 3209  CG  TYR D 333     1730   1530   1500    150    160    180       C  
ATOM   3210  CD1 TYR D 333      -1.952 -21.167 -57.859  1.00 12.62           C  
ANISOU 3210  CD1 TYR D 333     1740   1540   1520    160    140    190       C  
ATOM   3211  CD2 TYR D 333      -3.932 -22.472 -57.832  1.00 12.39           C  
ANISOU 3211  CD2 TYR D 333     1730   1480   1500    150    170    160       C  
ATOM   3212  CE1 TYR D 333      -1.407 -21.951 -56.854  1.00 12.57           C  
ANISOU 3212  CE1 TYR D 333     1750   1510   1520    170    130    200       C  
ATOM   3213  CE2 TYR D 333      -3.408 -23.262 -56.820  1.00 12.72           C  
ANISOU 3213  CE2 TYR D 333     1800   1490   1540    160    160    180       C  
ATOM   3214  CZ  TYR D 333      -2.140 -23.000 -56.329  1.00 13.02           C  
ANISOU 3214  CZ  TYR D 333     1840   1530   1580    170    140    190       C  
ATOM   3215  OH  TYR D 333      -1.616 -23.778 -55.334  1.00 13.45           O  
ANISOU 3215  OH  TYR D 333     1920   1550   1640    180    120    210       O  
ATOM   3216  N   THR D 334      -1.442 -19.830 -61.584  1.00 13.19           N  
ANISOU 3216  N   THR D 334     1720   1750   1540    130    150    200       N  
ATOM   3217  CA  THR D 334       0.010 -19.666 -61.823  1.00 13.73           C  
ANISOU 3217  CA  THR D 334     1760   1870   1590    110    150    210       C  
ATOM   3218  C   THR D 334       0.343 -18.186 -61.633  1.00 13.10           C  
ANISOU 3218  C   THR D 334     1690   1780   1500     70    130    260       C  
ATOM   3219  O   THR D 334      -0.558 -17.342 -61.828  1.00 12.32           O  
ANISOU 3219  O   THR D 334     1620   1660   1410     60    110    280       O  
ATOM   3220  CB  THR D 334       0.414 -20.176 -63.210  1.00 14.64           C  
ANISOU 3220  CB  THR D 334     1820   2070   1670    110    160    180       C  
ATOM   3221  OG1 THR D 334       1.837 -20.151 -63.300  1.00 17.27           O  
ANISOU 3221  OG1 THR D 334     2110   2460   1990    100    160    170       O  
ATOM   3222  CG2 THR D 334      -0.164 -19.352 -64.333  1.00 14.81           C  
ANISOU 3222  CG2 THR D 334     1840   2130   1660     70    160    210       C  
ATOM   3223  N   GLY D 335       1.580 -17.892 -61.245  1.00 12.65           N  
ANISOU 3223  N   GLY D 335     1620   1750   1440     60    120    270       N  
ATOM   3224  CA  GLY D 335       1.964 -16.487 -61.059  1.00 12.63           C  
ANISOU 3224  CA  GLY D 335     1630   1730   1440     10    100    310       C  
ATOM   3225  C   GLY D 335       3.364 -16.362 -60.512  1.00 12.96           C  
ANISOU 3225  C   GLY D 335     1640   1800   1480      0     90    310       C  
ATOM   3226  O   GLY D 335       4.022 -17.405 -60.280  1.00 12.46           O  
ANISOU 3226  O   GLY D 335     1550   1770   1410     30    100    270       O  
ATOM   3227  N   ALA D 336       3.799 -15.120 -60.339  1.00 13.21           N  
ANISOU 3227  N   ALA D 336     1680   1820   1510    -50     70    350       N  
ATOM   3228  CA  ALA D 336       5.136 -14.816 -59.796  1.00 13.61           C  
ANISOU 3228  CA  ALA D 336     1700   1900   1560    -80     60    340       C  
ATOM   3229  C   ALA D 336       5.013 -13.599 -58.880  1.00 13.88           C  
ANISOU 3229  C   ALA D 336     1780   1860   1630   -100     30    370       C  
ATOM   3230  O   ALA D 336       4.310 -12.637 -59.252  1.00 13.92           O  
ANISOU 3230  O   ALA D 336     1820   1820   1640   -130      0    410       O  
ATOM   3231  CB  ALA D 336       6.114 -14.588 -60.919  1.00 14.28           C  
ANISOU 3231  CB  ALA D 336     1740   2090   1600   -140     70    360       C  
ATOM   3232  N   ILE D 337       5.636 -13.688 -57.707  1.00 14.21           N  
ANISOU 3232  N   ILE D 337     1820   1890   1690    -80     20    340       N  
ATOM   3233  CA  ILE D 337       5.656 -12.623 -56.666  1.00 14.51           C  
ANISOU 3233  CA  ILE D 337     1890   1870   1760    -90    -20    350       C  
ATOM   3234  C   ILE D 337       7.091 -12.106 -56.534  1.00 15.09           C  
ANISOU 3234  C   ILE D 337     1920   1990   1820   -140    -30    350       C  
ATOM   3235  O   ILE D 337       7.989 -12.889 -56.167  1.00 14.16           O  
ANISOU 3235  O   ILE D 337     1770   1920   1690   -120    -20    320       O  
ATOM   3236  CB  ILE D 337       5.089 -13.196 -55.356  1.00 14.44           C  
ANISOU 3236  CB  ILE D 337     1900   1820   1760    -30    -20    310       C  
ATOM   3237  CG1 ILE D 337       3.626 -13.602 -55.557  1.00 14.44           C  
ANISOU 3237  CG1 ILE D 337     1940   1790   1770      0    -10    310       C  
ATOM   3238  CG2 ILE D 337       5.260 -12.214 -54.206  1.00 14.74           C  
ANISOU 3238  CG2 ILE D 337     1960   1820   1820    -40    -50    300       C  
ATOM   3239  CD1 ILE D 337       3.008 -14.292 -54.363  1.00 14.58           C  
ANISOU 3239  CD1 ILE D 337     1970   1780   1780     50      0    280       C  
ATOM   3240  N   LYS D 338       7.278 -10.820 -56.812  1.00 16.72           N  
ANISOU 3240  N   LYS D 338     2140   2170   2050   -210    -60    390       N  
ATOM   3241  CA  LYS D 338       8.615 -10.185 -56.767  1.00 18.78           C  
ANISOU 3241  CA  LYS D 338     2360   2470   2300   -280    -70    400       C  
ATOM   3242  C   LYS D 338       9.040  -9.928 -55.319  1.00 18.70           C  
ANISOU 3242  C   LYS D 338     2360   2420   2320   -250    -90    360       C  
ATOM   3243  O   LYS D 338       8.230  -9.369 -54.568  1.00 17.98           O  
ANISOU 3243  O   LYS D 338     2310   2250   2270   -220   -120    350       O  
ATOM   3244  CB  LYS D 338       8.547  -8.857 -57.528  1.00 20.51           C  
ANISOU 3244  CB  LYS D 338     2610   2650   2530   -360   -100    470       C  
ATOM   3245  CG  LYS D 338       9.867  -8.124 -57.712  1.00 22.61           C  
ANISOU 3245  CG  LYS D 338     2840   2970   2790   -460   -110    490       C  
ATOM   3246  CD  LYS D 338       9.677  -6.786 -58.385  1.00 24.25           C  
ANISOU 3246  CD  LYS D 338     3090   3110   3010   -550   -160    570       C  
ATOM   3247  CE  LYS D 338      10.973  -6.063 -58.642  1.00 26.74           C  
ANISOU 3247  CE  LYS D 338     3360   3480   3310   -670   -160    600       C  
ATOM   3248  NZ  LYS D 338      11.750  -5.866 -57.397  1.00 28.11           N  
ANISOU 3248  NZ  LYS D 338     3520   3650   3520   -650   -180    550       N  
ATOM   3249  N   LEU D 339      10.244 -10.358 -54.937  1.00 19.93           N  
ANISOU 3249  N   LEU D 339     2460   2650   2460   -250    -80    330       N  
ATOM   3250  CA  LEU D 339      10.722 -10.044 -53.566  1.00 21.20           C  
ANISOU 3250  CA  LEU D 339     2620   2790   2640   -230   -110    290       C  
ATOM   3251  C   LEU D 339      11.215  -8.593 -53.604  1.00 22.01           C  
ANISOU 3251  C   LEU D 339     2730   2860   2770   -320   -150    320       C  
ATOM   3252  O   LEU D 339      11.544  -8.113 -54.707  1.00 22.81           O  
ANISOU 3252  O   LEU D 339     2820   2990   2860   -400   -140    360       O  
ATOM   3253  CB  LEU D 339      11.874 -10.957 -53.130  1.00 22.63           C  
ANISOU 3253  CB  LEU D 339     2740   3050   2800   -200   -100    250       C  
ATOM   3254  CG  LEU D 339      11.731 -12.465 -53.346  1.00 23.38           C  
ANISOU 3254  CG  LEU D 339     2830   3190   2870   -130    -70    220       C  
ATOM   3255  CD1 LEU D 339      12.799 -13.192 -52.536  1.00 24.16           C  
ANISOU 3255  CD1 LEU D 339     2880   3340   2960    -80    -80    170       C  
ATOM   3256  CD2 LEU D 339      10.363 -12.973 -52.959  1.00 23.83           C  
ANISOU 3256  CD2 LEU D 339     2940   3170   2930    -70    -70    230       C  
ATOM   3257  N   ASP D 340      11.301  -7.934 -52.451  1.00 22.86           N  
ANISOU 3257  N   ASP D 340     2850   2920   2920   -310   -180    290       N  
ATOM   3258  CA  ASP D 340      11.782  -6.531 -52.381  1.00 24.61           C  
ANISOU 3258  CA  ASP D 340     3080   3090   3180   -390   -230    300       C  
ATOM   3259  C   ASP D 340      13.281  -6.556 -52.050  1.00 26.16           C  
ANISOU 3259  C   ASP D 340     3210   3370   3360   -430   -220    270       C  
ATOM   3260  O   ASP D 340      13.611  -6.757 -50.879  1.00 24.12           O  
ANISOU 3260  O   ASP D 340     2940   3120   3100   -380   -240    220       O  
ATOM   3261  CB  ASP D 340      10.946  -5.752 -51.365  1.00 25.17           C  
ANISOU 3261  CB  ASP D 340     3200   3060   3300   -360   -270    270       C  
ATOM   3262  CG  ASP D 340      11.315  -4.285 -51.226  1.00 26.35           C  
ANISOU 3262  CG  ASP D 340     3370   3140   3500   -430   -330    280       C  
ATOM   3263  OD1 ASP D 340      12.316  -3.858 -51.842  1.00 25.44           O  
ANISOU 3263  OD1 ASP D 340     3220   3060   3380   -520   -330    320       O  
ATOM   3264  OD2 ASP D 340      10.588  -3.582 -50.497  1.00 28.41           O  
ANISOU 3264  OD2 ASP D 340     3670   3320   3810   -400   -380    240       O  
ATOM   3265  N   ASP D 341      14.155  -6.327 -53.041  1.00 28.74           N  
ANISOU 3265  N   ASP D 341     4210   3060   3650   -390   -280      0       N  
ATOM   3266  CA  ASP D 341      15.623  -6.380 -52.771  1.00 31.91           C  
ANISOU 3266  CA  ASP D 341     4530   3570   4020   -440     20    -50       C  
ATOM   3267  C   ASP D 341      16.069  -5.136 -51.982  1.00 32.43           C  
ANISOU 3267  C   ASP D 341     4410   3660   4250   -460     80   -120       C  
ATOM   3268  O   ASP D 341      17.257  -5.085 -51.616  1.00 34.71           O  
ANISOU 3268  O   ASP D 341     4560   3990   4630   -490    260   -190       O  
ATOM   3269  CB  ASP D 341      16.429  -6.731 -54.032  1.00 35.49           C  
ANISOU 3269  CB  ASP D 341     5320   3880   4290   -530    230    -10       C  
ATOM   3270  CG  ASP D 341      16.217  -5.837 -55.240  1.00 38.34           C  
ANISOU 3270  CG  ASP D 341     6140   3970   4460   -620    200     80       C  
ATOM   3271  OD1 ASP D 341      15.860  -4.658 -55.050  1.00 39.27           O  
ANISOU 3271  OD1 ASP D 341     6240   4020   4670   -610     80     90       O  
ATOM   3272  OD2 ASP D 341      16.379  -6.353 -56.370  1.00 41.79           O  
ANISOU 3272  OD2 ASP D 341     7000   4240   4640   -690    300    130       O  
ATOM   3273  N   LYS D 342      15.155  -4.189 -51.731  1.00 32.69           N  
ANISOU 3273  N   LYS D 342     4410   3620   4380   -430    -90   -110       N  
ATOM   3274  CA  LYS D 342      15.447  -2.990 -50.896  1.00 32.90           C  
ANISOU 3274  CA  LYS D 342     4260   3670   4570   -450    -40   -190       C  
ATOM   3275  C   LYS D 342      15.247  -3.370 -49.424  1.00 30.14           C  
ANISOU 3275  C   LYS D 342     3670   3480   4300   -390    -50   -290       C  
ATOM   3276  O   LYS D 342      15.853  -2.714 -48.558  1.00 30.17           O  
ANISOU 3276  O   LYS D 342     3560   3520   4380   -410      0   -380       O  
ATOM   3277  CB  LYS D 342      14.520  -1.806 -51.204  1.00 36.65           C  
ANISOU 3277  CB  LYS D 342     4810   3960   5160   -450   -210   -160       C  
ATOM   3278  CG  LYS D 342      14.852  -0.930 -52.409  1.00 40.35           C  
ANISOU 3278  CG  LYS D 342     5590   4210   5520   -520   -210    -60       C  
ATOM   3279  CD  LYS D 342      16.132  -0.123 -52.222  1.00 43.63           C  
ANISOU 3279  CD  LYS D 342     5960   4640   5980   -600     60   -120       C  
ATOM   3280  CE  LYS D 342      16.271   1.057 -53.167  1.00 46.51           C  
ANISOU 3280  CE  LYS D 342     6630   4740   6300   -690     90    -40       C  
ATOM   3281  NZ  LYS D 342      16.202   0.660 -54.593  1.00 49.73           N  
ANISOU 3281  NZ  LYS D 342     7550   4930   6410   -750     90     90       N  
ATOM   3282  N   ASP D 343      14.394  -4.371 -49.168  1.00 26.80           N  
ANISOU 3282  N   ASP D 343     3220   3100   3860   -340   -110   -280       N  
ATOM   3283  CA  ASP D 343      14.069  -4.863 -47.800  1.00 25.31           C  
ANISOU 3283  CA  ASP D 343     2930   3010   3680   -300    -60   -370       C  
ATOM   3284  C   ASP D 343      15.357  -5.327 -47.126  1.00 25.06           C  
ANISOU 3284  C   ASP D 343     2890   3090   3540   -310    -30   -410       C  
ATOM   3285  O   ASP D 343      16.114  -6.100 -47.706  1.00 24.65           O  
ANISOU 3285  O   ASP D 343     2850   3080   3440   -310    -20   -370       O  
ATOM   3286  CB  ASP D 343      13.006  -5.969 -47.874  1.00 25.06           C  
ANISOU 3286  CB  ASP D 343     2890   2960   3670   -260    -80   -340       C  
ATOM   3287  CG  ASP D 343      12.593  -6.598 -46.550  1.00 24.72           C  
ANISOU 3287  CG  ASP D 343     2830   2950   3610   -250     50   -420       C  
ATOM   3288  OD1 ASP D 343      13.331  -6.441 -45.562  1.00 24.94           O  
ANISOU 3288  OD1 ASP D 343     2930   3040   3500   -270    100   -480       O  
ATOM   3289  OD2 ASP D 343      11.517  -7.245 -46.523  1.00 25.02           O  
ANISOU 3289  OD2 ASP D 343     2820   2910   3770   -230    100   -440       O  
ATOM   3290  N   PRO D 344      15.665  -4.841 -45.900  1.00 25.77           N  
ANISOU 3290  N   PRO D 344     2980   3190   3620   -320    -40   -510       N  
ATOM   3291  CA  PRO D 344      16.875  -5.256 -45.185  1.00 25.55           C  
ANISOU 3291  CA  PRO D 344     2960   3210   3540   -320   -130   -560       C  
ATOM   3292  C   PRO D 344      16.971  -6.770 -44.935  1.00 23.70           C  
ANISOU 3292  C   PRO D 344     2790   3030   3180   -270   -190   -530       C  
ATOM   3293  O   PRO D 344      18.056  -7.246 -44.705  1.00 24.37           O  
ANISOU 3293  O   PRO D 344     2840   3110   3310   -260   -320   -550       O  
ATOM   3294  CB  PRO D 344      16.756  -4.553 -43.821  1.00 26.93           C  
ANISOU 3294  CB  PRO D 344     3250   3330   3650   -340   -170   -670       C  
ATOM   3295  CG  PRO D 344      15.839  -3.376 -44.071  1.00 27.26           C  
ANISOU 3295  CG  PRO D 344     3240   3310   3810   -370    -40   -690       C  
ATOM   3296  CD  PRO D 344      14.887  -3.837 -45.154  1.00 26.73           C  
ANISOU 3296  CD  PRO D 344     3110   3240   3810   -340     20   -590       C  
ATOM   3297  N   ASN D 345      15.834  -7.468 -44.998  1.00 22.03           N  
ANISOU 3297  N   ASN D 345     2650   2830   2880   -260    -90   -480       N  
ATOM   3298  CA  ASN D 345      15.735  -8.933 -44.753  1.00 21.42           C  
ANISOU 3298  CA  ASN D 345     2660   2800   2680   -220   -110   -440       C  
ATOM   3299  C   ASN D 345      15.818  -9.728 -46.063  1.00 19.24           C  
ANISOU 3299  C   ASN D 345     2290   2560   2460   -200   -100   -350       C  
ATOM   3300  O   ASN D 345      15.654 -10.967 -46.001  1.00 17.42           O  
ANISOU 3300  O   ASN D 345     2100   2360   2150   -170   -100   -310       O  
ATOM   3301  CB  ASN D 345      14.407  -9.276 -44.075  1.00 21.73           C  
ANISOU 3301  CB  ASN D 345     2830   2780   2640   -230     50   -460       C  
ATOM   3302  CG  ASN D 345      14.250  -8.638 -42.715  1.00 24.07           C  
ANISOU 3302  CG  ASN D 345     3340   2990   2820   -280    120   -560       C  
ATOM   3303  OD1 ASN D 345      15.218  -8.499 -41.974  1.00 26.45           O  
ANISOU 3303  OD1 ASN D 345     3800   3270   2980   -280    -50   -590       O  
ATOM   3304  ND2 ASN D 345      13.022  -8.306 -42.354  1.00 25.37           N  
ANISOU 3304  ND2 ASN D 345     3540   3040   3060   -320    380   -620       N  
ATOM   3305  N   PHE D 346      16.071  -9.051 -47.189  1.00 18.25           N  
ANISOU 3305  N   PHE D 346     2090   2410   2430   -220    -60   -320       N  
ATOM   3306  CA  PHE D 346      16.133  -9.720 -48.515  1.00 17.77           C  
ANISOU 3306  CA  PHE D 346     2060   2330   2360   -230    -20   -250       C  
ATOM   3307  C   PHE D 346      17.107 -10.906 -48.516  1.00 17.15           C  
ANISOU 3307  C   PHE D 346     1940   2290   2280   -210    -10   -260       C  
ATOM   3308  O   PHE D 346      16.695 -11.991 -48.941  1.00 15.93           O  
ANISOU 3308  O   PHE D 346     1840   2160   2060   -180      0   -210       O  
ATOM   3309  CB  PHE D 346      16.530  -8.738 -49.621  1.00 18.47           C  
ANISOU 3309  CB  PHE D 346     2200   2320   2490   -290     50   -230       C  
ATOM   3310  CG  PHE D 346      16.713  -9.411 -50.956  1.00 18.44           C  
ANISOU 3310  CG  PHE D 346     2360   2250   2390   -320    140   -170       C  
ATOM   3311  CD1 PHE D 346      15.614  -9.774 -51.721  1.00 18.59           C  
ANISOU 3311  CD1 PHE D 346     2560   2200   2300   -310     30    -90       C  
ATOM   3312  CD2 PHE D 346      17.978  -9.711 -51.435  1.00 19.22           C  
ANISOU 3312  CD2 PHE D 346     2440   2300   2560   -370    330   -210       C  
ATOM   3313  CE1 PHE D 346      15.780 -10.411 -52.941  1.00 19.12           C  
ANISOU 3313  CE1 PHE D 346     2870   2170   2220   -350     90    -50       C  
ATOM   3314  CE2 PHE D 346      18.140 -10.357 -52.650  1.00 19.76           C  
ANISOU 3314  CE2 PHE D 346     2730   2260   2510   -420    490   -170       C  
ATOM   3315  CZ  PHE D 346      17.044 -10.694 -53.406  1.00 19.96           C  
ANISOU 3315  CZ  PHE D 346     3020   2240   2320   -410    360    -80       C  
ATOM   3316  N   LYS D 347      18.341 -10.707 -48.049  1.00 17.88           N  
ANISOU 3316  N   LYS D 347     1910   2360   2520   -210    -40   -330       N  
ATOM   3317  CA  LYS D 347      19.340 -11.808 -48.071  1.00 19.12           C  
ANISOU 3317  CA  LYS D 347     1960   2490   2810   -190    -70   -360       C  
ATOM   3318  C   LYS D 347      18.870 -12.982 -47.202  1.00 18.60           C  
ANISOU 3318  C   LYS D 347     1980   2490   2600   -120   -220   -330       C  
ATOM   3319  O   LYS D 347      19.141 -14.129 -47.596  1.00 17.73           O  
ANISOU 3319  O   LYS D 347     1840   2370   2530    -90   -200   -310       O  
ATOM   3320  CB  LYS D 347      20.731 -11.313 -47.661  1.00 21.97           C  
ANISOU 3320  CB  LYS D 347     2110   2740   3490   -200   -140   -470       C  
ATOM   3321  CG  LYS D 347      21.386 -10.360 -48.650  1.00 23.78           C  
ANISOU 3321  CG  LYS D 347     2250   2860   3930   -280    110   -520       C  
ATOM   3322  CD  LYS D 347      22.776  -9.925 -48.249  1.00 27.14           C  
ANISOU 3322  CD  LYS D 347     2380   3120   4810   -290     50   -670       C  
ATOM   3323  CE  LYS D 347      23.403  -8.991 -49.260  1.00 29.16           C  
ANISOU 3323  CE  LYS D 347     2560   3220   5300   -400    410   -720       C  
ATOM   3324  NZ  LYS D 347      24.769  -8.585 -48.859  1.00 33.00           N  
ANISOU 3324  NZ  LYS D 347     2690   3500   6350   -420    360   -900       N  
ATOM   3325  N   ASP D 348      18.197 -12.710 -46.081  1.00 18.46           N  
ANISOU 3325  N   ASP D 348     2100   2500   2420   -110   -330   -330       N  
ATOM   3326  CA  ASP D 348      17.705 -13.804 -45.193  1.00 19.10           C  
ANISOU 3326  CA  ASP D 348     2360   2580   2310    -70   -410   -290       C  
ATOM   3327  C   ASP D 348      16.512 -14.507 -45.852  1.00 17.16           C  
ANISOU 3327  C   ASP D 348     2150   2390   1990    -70   -230   -220       C  
ATOM   3328  O   ASP D 348      16.350 -15.719 -45.633  1.00 18.14           O  
ANISOU 3328  O   ASP D 348     2340   2510   2040    -40   -250   -180       O  
ATOM   3329  CB  ASP D 348      17.315 -13.277 -43.808  1.00 21.03           C  
ANISOU 3329  CB  ASP D 348     2850   2770   2370    -90   -480   -330       C  
ATOM   3330  CG  ASP D 348      18.479 -12.823 -42.948  1.00 22.99           C  
ANISOU 3330  CG  ASP D 348     3150   2920   2660    -80   -770   -400       C  
ATOM   3331  OD1 ASP D 348      19.619 -13.236 -43.224  1.00 23.44           O  
ANISOU 3331  OD1 ASP D 348     3020   2930   2950    -40   -960   -430       O  
ATOM   3332  OD2 ASP D 348      18.228 -12.059 -42.008  1.00 26.17           O  
ANISOU 3332  OD2 ASP D 348     3780   3260   2900   -120   -810   -460       O  
ATOM   3333  N   GLN D 349      15.708 -13.760 -46.610  1.00 16.01           N  
ANISOU 3333  N   GLN D 349     1950   2240   1880   -100   -120   -210       N  
ATOM   3334  CA  GLN D 349      14.522 -14.306 -47.321  1.00 15.29           C  
ANISOU 3334  CA  GLN D 349     1870   2140   1810    -90    -40   -170       C  
ATOM   3335  C   GLN D 349      15.017 -15.276 -48.402  1.00 14.28           C  
ANISOU 3335  C   GLN D 349     1720   2030   1680    -80    -50   -120       C  
ATOM   3336  O   GLN D 349      14.413 -16.354 -48.567  1.00 13.61           O  
ANISOU 3336  O   GLN D 349     1660   1940   1570    -50    -40    -90       O  
ATOM   3337  CB  GLN D 349      13.690 -13.159 -47.903  1.00 16.03           C  
ANISOU 3337  CB  GLN D 349     1920   2160   2010   -120    -30   -170       C  
ATOM   3338  CG  GLN D 349      13.024 -12.284 -46.848  1.00 17.46           C  
ANISOU 3338  CG  GLN D 349     2100   2290   2250   -140     40   -240       C  
ATOM   3339  CD  GLN D 349      12.472 -10.998 -47.417  1.00 19.20           C  
ANISOU 3339  CD  GLN D 349     2240   2420   2630   -160     10   -260       C  
ATOM   3340  OE1 GLN D 349      12.611 -10.706 -48.607  1.00 20.79           O  
ANISOU 3340  OE1 GLN D 349     2460   2590   2850   -160   -100   -200       O  
ATOM   3341  NE2 GLN D 349      11.860 -10.198 -46.557  1.00 19.79           N  
ANISOU 3341  NE2 GLN D 349     2280   2420   2810   -180    110   -340       N  
ATOM   3342  N   VAL D 350      16.110 -14.921 -49.080  1.00 13.87           N  
ANISOU 3342  N   VAL D 350     1630   1960   1670   -100    -20   -140       N  
ATOM   3343  CA  VAL D 350      16.672 -15.799 -50.147  1.00 13.30           C  
ANISOU 3343  CA  VAL D 350     1580   1860   1610   -110     60   -120       C  
ATOM   3344  C   VAL D 350      17.156 -17.104 -49.500  1.00 13.19           C  
ANISOU 3344  C   VAL D 350     1490   1880   1640    -60     10   -130       C  
ATOM   3345  O   VAL D 350      16.830 -18.172 -50.035  1.00 12.00           O  
ANISOU 3345  O   VAL D 350     1390   1720   1450    -40     40   -100       O  
ATOM   3346  CB  VAL D 350      17.788 -15.089 -50.938  1.00 14.37           C  
ANISOU 3346  CB  VAL D 350     1700   1900   1850   -180    220   -170       C  
ATOM   3347  CG1 VAL D 350      18.596 -16.057 -51.784  1.00 15.22           C  
ANISOU 3347  CG1 VAL D 350     1820   1930   2030   -200    390   -200       C  
ATOM   3348  CG2 VAL D 350      17.232 -13.954 -51.789  1.00 14.86           C  
ANISOU 3348  CG2 VAL D 350     1950   1890   1810   -240    250   -130       C  
ATOM   3349  N   ILE D 351      17.873 -17.013 -48.377  1.00 14.31           N  
ANISOU 3349  N   ILE D 351     1560   2020   1860    -30   -120   -170       N  
ATOM   3350  CA  ILE D 351      18.393 -18.229 -47.679  1.00 15.66           C  
ANISOU 3350  CA  ILE D 351     1700   2160   2090     30   -260   -170       C  
ATOM   3351  C   ILE D 351      17.221 -19.094 -47.197  1.00 15.09           C  
ANISOU 3351  C   ILE D 351     1800   2130   1800     50   -260   -100       C  
ATOM   3352  O   ILE D 351      17.286 -20.315 -47.377  1.00 15.19           O  
ANISOU 3352  O   ILE D 351     1810   2130   1830     90   -270    -70       O  
ATOM   3353  CB  ILE D 351      19.337 -17.820 -46.531  1.00 17.76           C  
ANISOU 3353  CB  ILE D 351     1930   2350   2460     60   -500   -230       C  
ATOM   3354  CG1 ILE D 351      20.593 -17.142 -47.088  1.00 19.43           C  
ANISOU 3354  CG1 ILE D 351     1890   2470   3030     30   -470   -330       C  
ATOM   3355  CG2 ILE D 351      19.690 -19.014 -45.659  1.00 19.22           C  
ANISOU 3355  CG2 ILE D 351     2200   2460   2640    120   -750   -210       C  
ATOM   3356  CD1 ILE D 351      21.497 -16.541 -46.037  1.00 21.56           C  
ANISOU 3356  CD1 ILE D 351     2090   2620   3490     60   -780   -410       C  
ATOM   3357  N   LEU D 352      16.180 -18.474 -46.641  1.00 14.96           N  
ANISOU 3357  N   LEU D 352     1910   2130   1650     30   -210    -90       N  
ATOM   3358  CA  LEU D 352      15.008 -19.229 -46.124  1.00 15.59           C  
ANISOU 3358  CA  LEU D 352     2120   2190   1610     30   -120    -50       C  
ATOM   3359  C   LEU D 352      14.308 -19.982 -47.266  1.00 14.64           C  
ANISOU 3359  C   LEU D 352     1910   2080   1570     40    -40    -20       C  
ATOM   3360  O   LEU D 352      14.030 -21.189 -47.103  1.00 14.10           O  
ANISOU 3360  O   LEU D 352     1890   1990   1480     60    -20     10       O  
ATOM   3361  CB  LEU D 352      14.057 -18.244 -45.429  1.00 16.22           C  
ANISOU 3361  CB  LEU D 352     2290   2220   1650    -20      0    -90       C  
ATOM   3362  CG  LEU D 352      12.779 -18.842 -44.839  1.00 17.20           C  
ANISOU 3362  CG  LEU D 352     2530   2250   1750    -40    210    -90       C  
ATOM   3363  CD1 LEU D 352      13.096 -19.953 -43.847  1.00 18.74           C  
ANISOU 3363  CD1 LEU D 352     3000   2380   1740    -40    190    -50       C  
ATOM   3364  CD2 LEU D 352      11.942 -17.763 -44.170  1.00 18.27           C  
ANISOU 3364  CD2 LEU D 352     2720   2290   1930   -100    390   -170       C  
ATOM   3365  N   LEU D 353      14.052 -19.306 -48.386  1.00 14.07           N  
ANISOU 3365  N   LEU D 353     1770   2010   1570     10    -30    -30       N  
ATOM   3366  CA  LEU D 353      13.344 -19.959 -49.520  1.00 14.18           C  
ANISOU 3366  CA  LEU D 353     1780   1980   1630     20    -30    -10       C  
ATOM   3367  C   LEU D 353      14.212 -21.066 -50.134  1.00 14.53           C  
ANISOU 3367  C   LEU D 353     1840   2040   1640     30    -20      0       C  
ATOM   3368  O   LEU D 353      13.652 -22.125 -50.449  1.00 13.58           O  
ANISOU 3368  O   LEU D 353     1730   1890   1540     50    -20     20       O  
ATOM   3369  CB  LEU D 353      12.942 -18.891 -50.540  1.00 14.39           C  
ANISOU 3369  CB  LEU D 353     1840   1940   1690    -20   -100    -10       C  
ATOM   3370  CG  LEU D 353      11.909 -17.880 -50.039  1.00 14.48           C  
ANISOU 3370  CG  LEU D 353     1780   1880   1840    -30   -120    -40       C  
ATOM   3371  CD1 LEU D 353      11.766 -16.720 -51.007  1.00 14.83           C  
ANISOU 3371  CD1 LEU D 353     1890   1840   1900    -50   -250    -40       C  
ATOM   3372  CD2 LEU D 353      10.564 -18.551 -49.785  1.00 15.14           C  
ANISOU 3372  CD2 LEU D 353     1770   1860   2120    -10   -110    -70       C  
ATOM   3373  N   ASN D 354      15.524 -20.848 -50.251  1.00 15.68           N  
ANISOU 3373  N   ASN D 354     1940   2200   1820     30     10    -20       N  
ATOM   3374  CA  ASN D 354      16.443 -21.867 -50.832  1.00 17.33           C  
ANISOU 3374  CA  ASN D 354     2110   2370   2100     30     80    -50       C  
ATOM   3375  C   ASN D 354      16.475 -23.118 -49.949  1.00 17.55           C  
ANISOU 3375  C   ASN D 354     2100   2410   2160    100      0    -20       C  
ATOM   3376  O   ASN D 354      16.740 -24.225 -50.472  1.00 17.46           O  
ANISOU 3376  O   ASN D 354     2070   2360   2200    110     40    -30       O  
ATOM   3377  CB  ASN D 354      17.873 -21.335 -50.988  1.00 19.04           C  
ANISOU 3377  CB  ASN D 354     2210   2530   2490     10    170   -120       C  
ATOM   3378  CG  ASN D 354      18.043 -20.368 -52.138  1.00 20.16           C  
ANISOU 3378  CG  ASN D 354     2470   2600   2590    -80    350   -150       C  
ATOM   3379  OD1 ASN D 354      17.287 -20.413 -53.105  1.00 20.50           O  
ANISOU 3379  OD1 ASN D 354     2740   2600   2450   -120    390   -110       O  
ATOM   3380  ND2 ASN D 354      19.071 -19.537 -52.073  1.00 21.73           N  
ANISOU 3380  ND2 ASN D 354     2550   2740   2970   -110    450   -220       N  
ATOM   3381  N   LYS D 355      16.203 -22.938 -48.661  1.00 18.05           N  
ANISOU 3381  N   LYS D 355     2210   2490   2160    120   -110     10       N  
ATOM   3382  CA  LYS D 355      16.237 -24.055 -47.684  1.00 19.28           C  
ANISOU 3382  CA  LYS D 355     2440   2610   2280    170   -210     50       C  
ATOM   3383  C   LYS D 355      14.997 -24.947 -47.829  1.00 17.17           C  
ANISOU 3383  C   LYS D 355     2250   2330   1940    160   -100     90       C  
ATOM   3384  O   LYS D 355      15.104 -26.146 -47.489  1.00 18.24           O  
ANISOU 3384  O   LYS D 355     2430   2420   2080    200   -140    120       O  
ATOM   3385  CB  LYS D 355      16.330 -23.439 -46.284  1.00 22.42           C  
ANISOU 3385  CB  LYS D 355     3000   2970   2550    170   -330     50       C  
ATOM   3386  CG  LYS D 355      16.469 -24.399 -45.114  1.00 26.97           C  
ANISOU 3386  CG  LYS D 355     3810   3440   3000    200   -480    110       C  
ATOM   3387  CD  LYS D 355      16.664 -23.669 -43.791  1.00 30.60           C  
ANISOU 3387  CD  LYS D 355     4550   3810   3270    180   -640    100       C  
ATOM   3388  CE  LYS D 355      17.894 -22.780 -43.796  1.00 33.58           C  
ANISOU 3388  CE  LYS D 355     4770   4170   3820    200   -880     40       C  
ATOM   3389  NZ  LYS D 355      18.069 -22.053 -42.518  1.00 38.08           N  
ANISOU 3389  NZ  LYS D 355     5660   4620   4180    180  -1090     20       N  
ATOM   3390  N   HIS D 356      13.901 -24.420 -48.385  1.00 14.73           N  
ANISOU 3390  N   HIS D 356     1920   2030   1640    130    -10     70       N  
ATOM   3391  CA  HIS D 356      12.640 -25.213 -48.459  1.00 14.34           C  
ANISOU 3391  CA  HIS D 356     1880   1920   1650    120     80     80       C  
ATOM   3392  C   HIS D 356      12.244 -25.651 -49.874  1.00 14.07           C  
ANISOU 3392  C   HIS D 356     1780   1860   1700    120     30     70       C  
ATOM   3393  O   HIS D 356      11.545 -26.684 -49.977  1.00 15.25           O  
ANISOU 3393  O   HIS D 356     1920   1940   1940    130     60     70       O  
ATOM   3394  CB  HIS D 356      11.510 -24.425 -47.789  1.00 14.43           C  
ANISOU 3394  CB  HIS D 356     1900   1860   1730     80    190     50       C  
ATOM   3395  CG  HIS D 356      11.758 -24.202 -46.335  1.00 15.22           C  
ANISOU 3395  CG  HIS D 356     2190   1930   1670     60    280     70       C  
ATOM   3396  ND1 HIS D 356      11.602 -25.211 -45.400  1.00 15.93           N  
ANISOU 3396  ND1 HIS D 356     2480   1920   1650     50    380    100       N  
ATOM   3397  CD2 HIS D 356      12.140 -23.103 -45.650  1.00 15.51           C  
ANISOU 3397  CD2 HIS D 356     2320   1980   1590     40    260     40       C  
ATOM   3398  CE1 HIS D 356      11.891 -24.742 -44.207  1.00 17.43           C  
ANISOU 3398  CE1 HIS D 356     2940   2050   1630     20    410    110       C  
ATOM   3399  NE2 HIS D 356      12.223 -23.449 -44.331  1.00 16.74           N  
ANISOU 3399  NE2 HIS D 356     2780   2040   1550     10    330     60       N  
ATOM   3400  N   ILE D 357      12.632 -24.903 -50.907  1.00 13.31           N  
ANISOU 3400  N   ILE D 357     1710   1770   1570    100    -20     50       N  
ATOM   3401  CA  ILE D 357      12.262 -25.262 -52.306  1.00 13.53           C  
ANISOU 3401  CA  ILE D 357     1830   1720   1590     80   -100     30       C  
ATOM   3402  C   ILE D 357      12.986 -26.544 -52.728  1.00 13.41           C  
ANISOU 3402  C   ILE D 357     1850   1700   1540     90    -30     20       C  
ATOM   3403  O   ILE D 357      14.235 -26.533 -52.779  1.00 13.76           O  
ANISOU 3403  O   ILE D 357     1880   1780   1560     90     70     10       O  
ATOM   3404  CB  ILE D 357      12.566 -24.086 -53.258  1.00 14.17           C  
ANISOU 3404  CB  ILE D 357     2060   1760   1570     30   -150     20       C  
ATOM   3405  CG1 ILE D 357      11.732 -22.853 -52.891  1.00 14.46           C  
ANISOU 3405  CG1 ILE D 357     2040   1760   1690     30   -250     20       C  
ATOM   3406  CG2 ILE D 357      12.352 -24.507 -54.702  1.00 15.37           C  
ANISOU 3406  CG2 ILE D 357     2470   1770   1600      0   -240      0       C  
ATOM   3407  CD1 ILE D 357      12.030 -21.625 -53.713  1.00 14.77           C  
ANISOU 3407  CD1 ILE D 357     2250   1740   1620    -20   -310     20       C  
ATOM   3408  N   ASP D 358      12.217 -27.592 -53.041  1.00 13.32           N  
ANISOU 3408  N   ASP D 358     1850   1620   1590    110    -90     20       N  
ATOM   3409  CA  ASP D 358      12.759 -28.904 -53.492  1.00 14.03           C  
ANISOU 3409  CA  ASP D 358     1970   1690   1670    120    -20     10       C  
ATOM   3410  C   ASP D 358      13.669 -29.532 -52.428  1.00 13.78           C  
ANISOU 3410  C   ASP D 358     1810   1730   1700    170     70     30       C  
ATOM   3411  O   ASP D 358      14.529 -30.356 -52.819  1.00 14.13           O  
ANISOU 3411  O   ASP D 358     1840   1740   1790    180    150      0       O  
ATOM   3412  CB  ASP D 358      13.491 -28.775 -54.835  1.00 15.15           C  
ANISOU 3412  CB  ASP D 358     2330   1760   1670     60     60    -50       C  
ATOM   3413  CG  ASP D 358      12.576 -28.476 -56.006  1.00 16.48           C  
ANISOU 3413  CG  ASP D 358     2770   1780   1710     20   -130    -60       C  
ATOM   3414  OD1 ASP D 358      11.401 -28.903 -55.955  1.00 16.47           O  
ANISOU 3414  OD1 ASP D 358     2720   1710   1830     50   -330    -60       O  
ATOM   3415  OD2 ASP D 358      13.035 -27.796 -56.951  1.00 18.32           O  
ANISOU 3415  OD2 ASP D 358     3300   1920   1750    -50    -70    -90       O  
ATOM   3416  N   ALA D 359      13.474 -29.195 -51.147  1.00 13.24           N  
ANISOU 3416  N   ALA D 359     1680   1700   1640    190     50     80       N  
ATOM   3417  CA  ALA D 359      14.317 -29.772 -50.073  1.00 14.10           C  
ANISOU 3417  CA  ALA D 359     1770   1810   1770    230     30    120       C  
ATOM   3418  C   ALA D 359      14.122 -31.297 -50.002  1.00 14.87           C  
ANISOU 3418  C   ALA D 359     1880   1850   1930    270     40    140       C  
ATOM   3419  O   ALA D 359      15.116 -31.993 -49.704  1.00 15.66           O  
ANISOU 3419  O   ALA D 359     1940   1900   2100    310    -20    150       O  
ATOM   3420  CB  ALA D 359      13.988 -29.125 -48.750  1.00 14.28           C  
ANISOU 3420  CB  ALA D 359     1880   1840   1700    230      0    160       C  
ATOM   3421  N   TYR D 360      12.911 -31.786 -50.316  1.00 14.60           N  
ANISOU 3421  N   TYR D 360     1860   1770   1920    250     90    140       N  
ATOM   3422  CA  TYR D 360      12.563 -33.236 -50.254  1.00 15.74           C  
ANISOU 3422  CA  TYR D 360     2000   1830   2140    270    120    160       C  
ATOM   3423  C   TYR D 360      13.530 -34.085 -51.094  1.00 16.61           C  
ANISOU 3423  C   TYR D 360     2070   1930   2310    300    110    120       C  
ATOM   3424  O   TYR D 360      13.609 -35.306 -50.847  1.00 16.88           O  
ANISOU 3424  O   TYR D 360     2100   1900   2420    330    110    150       O  
ATOM   3425  CB  TYR D 360      11.155 -33.501 -50.792  1.00 15.70           C  
ANISOU 3425  CB  TYR D 360     1960   1740   2260    240    150    120       C  
ATOM   3426  CG  TYR D 360      11.085 -33.411 -52.291  1.00 15.52           C  
ANISOU 3426  CG  TYR D 360     1950   1700   2250    220     50     50       C  
ATOM   3427  CD1 TYR D 360      10.887 -32.202 -52.930  1.00 15.60           C  
ANISOU 3427  CD1 TYR D 360     2000   1720   2200    190    -50     10       C  
ATOM   3428  CD2 TYR D 360      11.279 -34.536 -53.078  1.00 16.36           C  
ANISOU 3428  CD2 TYR D 360     2080   1750   2380    230     40     10       C  
ATOM   3429  CE1 TYR D 360      10.862 -32.113 -54.312  1.00 16.34           C  
ANISOU 3429  CE1 TYR D 360     2260   1740   2210    160   -170    -40       C  
ATOM   3430  CE2 TYR D 360      11.255 -34.467 -54.460  1.00 17.05           C  
ANISOU 3430  CE2 TYR D 360     2320   1780   2390    200    -50    -60       C  
ATOM   3431  CZ  TYR D 360      11.045 -33.249 -55.081  1.00 17.01           C  
ANISOU 3431  CZ  TYR D 360     2440   1750   2270    160   -160    -80       C  
ATOM   3432  OH  TYR D 360      11.030 -33.173 -56.442  1.00 18.09           O  
ANISOU 3432  OH  TYR D 360     2850   1770   2250    110   -260   -140       O  
ATOM   3433  N   LYS D 361      14.208 -33.474 -52.072  1.00 17.70           N  
ANISOU 3433  N   LYS D 361     2200   2090   2430    270    130     50       N  
ATOM   3434  CA  LYS D 361      15.160 -34.212 -52.951  1.00 20.13           C  
ANISOU 3434  CA  LYS D 361     2480   2330   2840    270    230    -20       C  
ATOM   3435  C   LYS D 361      16.329 -34.787 -52.145  1.00 21.22           C  
ANISOU 3435  C   LYS D 361     2470   2420   3180    340    190    -10       C  
ATOM   3436  O   LYS D 361      16.942 -35.745 -52.621  1.00 21.71           O  
ANISOU 3436  O   LYS D 361     2450   2380   3410    350    270    -70       O  
ATOM   3437  CB  LYS D 361      15.718 -33.315 -54.061  1.00 20.88           C  
ANISOU 3437  CB  LYS D 361     2670   2400   2860    200    360   -110       C  
ATOM   3438  CG  LYS D 361      14.743 -32.947 -55.170  1.00 21.47           C  
ANISOU 3438  CG  LYS D 361     2990   2440   2730    140    330   -130       C  
ATOM   3439  CD  LYS D 361      15.416 -32.186 -56.294  1.00 23.55           C  
ANISOU 3439  CD  LYS D 361     3480   2610   2860     50    510   -210       C  
ATOM   3440  CE  LYS D 361      14.515 -31.956 -57.490  1.00 25.05           C  
ANISOU 3440  CE  LYS D 361     4050   2680   2790    -20    400   -230       C  
ATOM   3441  NZ  LYS D 361      15.219 -31.224 -58.571  1.00 27.84           N  
ANISOU 3441  NZ  LYS D 361     4750   2900   2930   -130    620   -300       N  
ATOM   3442  N   THR D 362      16.620 -34.218 -50.976  1.00 23.04           N  
ANISOU 3442  N   THR D 362     2670   2680   3400    370     40     50       N  
ATOM   3443  CA  THR D 362      17.756 -34.695 -50.147  1.00 27.04           C  
ANISOU 3443  CA  THR D 362     3070   3070   4130    440   -140     60       C  
ATOM   3444  C   THR D 362      17.266 -35.502 -48.940  1.00 28.81           C  
ANISOU 3444  C   THR D 362     3470   3240   4240    490   -320    190       C  
ATOM   3445  O   THR D 362      18.131 -35.929 -48.162  1.00 32.15           O  
ANISOU 3445  O   THR D 362     3890   3520   4810    550   -560    210       O  
ATOM   3446  CB  THR D 362      18.593 -33.517 -49.631  1.00 28.13           C  
ANISOU 3446  CB  THR D 362     3140   3210   4350    450   -260     40       C  
ATOM   3447  OG1 THR D 362      17.744 -32.734 -48.792  1.00 28.94           O  
ANISOU 3447  OG1 THR D 362     3440   3400   4150    430   -340    120       O  
ATOM   3448  CG2 THR D 362      19.175 -32.657 -50.732  1.00 28.05           C  
ANISOU 3448  CG2 THR D 362     2990   3210   4470    390    -40    -90       C  
ATOM   3449  N   PHE D 363      15.954 -35.706 -48.768  1.00 29.45           N  
ANISOU 3449  N   PHE D 363     3720   3370   4100    450   -200    250       N  
ATOM   3450  CA  PHE D 363      15.537 -36.465 -47.558  1.00 31.80           C  
ANISOU 3450  CA  PHE D 363     4260   3550   4280    470   -290    360       C  
ATOM   3451  C   PHE D 363      16.039 -37.902 -47.651  1.00 35.89           C  
ANISOU 3451  C   PHE D 363     4730   3930   4980    530   -370    380       C  
ATOM   3452  O   PHE D 363      15.845 -38.564 -48.669  1.00 35.62           O  
ANISOU 3452  O   PHE D 363     4530   3920   5080    520   -230    310       O  
ATOM   3453  CB  PHE D 363      14.023 -36.495 -47.322  1.00 29.90           C  
ANISOU 3453  CB  PHE D 363     4160   3310   3880    400    -60    390       C  
ATOM   3454  CG  PHE D 363      13.323 -35.163 -47.223  1.00 27.86           C  
ANISOU 3454  CG  PHE D 363     3930   3140   3520    340     60    370       C  
ATOM   3455  CD1 PHE D 363      13.968 -34.046 -46.718  1.00 27.76           C  
ANISOU 3455  CD1 PHE D 363     3970   3170   3400    340    -60    370       C  
ATOM   3456  CD2 PHE D 363      11.954 -35.086 -47.433  1.00 27.26           C  
ANISOU 3456  CD2 PHE D 363     3820   3040   3500    280    270    330       C  
ATOM   3457  CE1 PHE D 363      13.296 -32.838 -46.590  1.00 26.83           C  
ANISOU 3457  CE1 PHE D 363     3870   3120   3200    280     60    340       C  
ATOM   3458  CE2 PHE D 363      11.272 -33.891 -47.264  1.00 26.43           C  
ANISOU 3458  CE2 PHE D 363     3700   2960   3370    220    380    300       C  
ATOM   3459  CZ  PHE D 363      11.947 -32.764 -46.849  1.00 26.03           C  
ANISOU 3459  CZ  PHE D 363     3720   2990   3180    230    280    300       C  
ATOM   3460  N   PRO D 364      16.728 -38.413 -46.606  1.00 41.95           N  
ANISOU 3460  N   PRO D 364     5660   4530   5750    580   -650    460       N  
ATOM   3461  CA  PRO D 364      17.208 -39.796 -46.608  1.00 46.22           C  
ANISOU 3461  CA  PRO D 364     6160   4900   6500    650   -790    480       C  
ATOM   3462  C   PRO D 364      16.102 -40.793 -47.000  1.00 48.07           C  
ANISOU 3462  C   PRO D 364     6450   5150   6670    610   -520    500       C  
ATOM   3463  O   PRO D 364      16.369 -41.946 -47.352  1.00 51.63           O  
ANISOU 3463  O   PRO D 364     6790   5500   7330    650   -540    490       O  
ATOM   3464  CB  PRO D 364      17.665 -40.005 -45.155  1.00 48.70           C  
ANISOU 3464  CB  PRO D 364     6850   4980   6670    700  -1160    610       C  
ATOM   3465  CG  PRO D 364      18.095 -38.622 -44.701  1.00 47.95           C  
ANISOU 3465  CG  PRO D 364     6810   4930   6480    680  -1320    590       C  
ATOM   3466  CD  PRO D 364      17.149 -37.670 -45.406  1.00 44.28           C  
ANISOU 3466  CD  PRO D 364     6220   4730   5870    590   -920    520       C  
ATOM   3467  OXT PRO D 364      14.908 -40.475 -46.980  1.00 49.75           O  
ANISOU 3467  OXT PRO D 364     6770   5440   6700    530   -270    520       O  
TER    3468      PRO D 364                                                      
ATOM   3469  N   LYS E 257       3.257  12.359 -36.227  1.00 36.57           N  
ANISOU 3469  N   LYS E 257     3940   5350   4610   -200   -610   1310       N  
ATOM   3470  CA  LYS E 257       3.050  12.446 -37.713  1.00 34.96           C  
ANISOU 3470  CA  LYS E 257     3810   4960   4510     30   -390   1050       C  
ATOM   3471  C   LYS E 257       2.428  13.794 -38.083  1.00 29.94           C  
ANISOU 3471  C   LYS E 257     3460   4300   3620    -80   -440    770       C  
ATOM   3472  O   LYS E 257       1.530  14.285 -37.396  1.00 27.50           O  
ANISOU 3472  O   LYS E 257     3350   3950   3140   -170   -480    630       O  
ATOM   3473  CB  LYS E 257       2.176  11.286 -38.201  1.00 36.27           C  
ANISOU 3473  CB  LYS E 257     4010   4930   4840    250   -190    880       C  
ATOM   3474  CG  LYS E 257       1.949  11.235 -39.708  1.00 37.67           C  
ANISOU 3474  CG  LYS E 257     4300   4970   5040    330     30    640       C  
ATOM   3475  CD  LYS E 257       1.219   9.992 -40.183  1.00 39.25           C  
ANISOU 3475  CD  LYS E 257     4590   4980   5350    420    270    490       C  
ATOM   3476  CE  LYS E 257       1.984   8.714 -39.918  1.00 42.72           C  
ANISOU 3476  CE  LYS E 257     4810   5260   6160    580    510    700       C  
ATOM   3477  NZ  LYS E 257       1.242   7.520 -40.387  1.00 44.16           N  
ANISOU 3477  NZ  LYS E 257     5160   5200   6420    610    800    500       N  
ATOM   3478  N   PRO E 258       2.886  14.439 -39.182  1.00 26.94           N  
ANISOU 3478  N   PRO E 258     3090   3910   3240    -60   -390    710       N  
ATOM   3479  CA  PRO E 258       2.332  15.725 -39.598  1.00 24.37           C  
ANISOU 3479  CA  PRO E 258     2980   3530   2740   -140   -420    530       C  
ATOM   3480  C   PRO E 258       0.805  15.607 -39.707  1.00 20.85           C  
ANISOU 3480  C   PRO E 258     2670   2960   2300    -30   -350    360       C  
ATOM   3481  O   PRO E 258       0.313  14.655 -40.274  1.00 18.47           O  
ANISOU 3481  O   PRO E 258     2310   2630   2080     80   -270    320       O  
ATOM   3482  CB  PRO E 258       3.022  16.020 -40.937  1.00 24.86           C  
ANISOU 3482  CB  PRO E 258     2970   3630   2850   -110   -360    530       C  
ATOM   3483  CG  PRO E 258       4.315  15.224 -40.865  1.00 27.67           C  
ANISOU 3483  CG  PRO E 258     3070   4070   3370    -70   -310    760       C  
ATOM   3484  CD  PRO E 258       3.962  13.979 -40.076  1.00 28.23           C  
ANISOU 3484  CD  PRO E 258     3040   4090   3590     40   -260    840       C  
ATOM   3485  N   ARG E 259       0.114  16.607 -39.168  1.00 19.57           N  
ANISOU 3485  N   ARG E 259     2680   2700   2060    -90   -330    300       N  
ATOM   3486  CA  ARG E 259      -1.368  16.658 -39.111  1.00 18.38           C  
ANISOU 3486  CA  ARG E 259     2590   2420   1980     20   -240    230       C  
ATOM   3487  C   ARG E 259      -2.008  16.366 -40.482  1.00 16.62           C  
ANISOU 3487  C   ARG E 259     2260   2230   1830    110   -250    270       C  
ATOM   3488  O   ARG E 259      -3.001  15.619 -40.492  1.00 15.17           O  
ANISOU 3488  O   ARG E 259     2030   2050   1680    170   -240    280       O  
ATOM   3489  CB  ARG E 259      -1.771  18.005 -38.505  1.00 20.32           C  
ANISOU 3489  CB  ARG E 259     3030   2480   2210    -60   -100    180       C  
ATOM   3490  CG  ARG E 259      -3.268  18.224 -38.347  1.00 22.24           C  
ANISOU 3490  CG  ARG E 259     3290   2540   2630    100     80    190       C  
ATOM   3491  CD  ARG E 259      -3.522  19.449 -37.488  1.00 25.45           C  
ANISOU 3491  CD  ARG E 259     3940   2660   3060     10    360    100       C  
ATOM   3492  NE  ARG E 259      -4.929  19.820 -37.398  1.00 28.55           N  
ANISOU 3492  NE  ARG E 259     4300   2810   3740    210    630    180       N  
ATOM   3493  CZ  ARG E 259      -5.543  20.714 -38.185  1.00 30.99           C  
ANISOU 3493  CZ  ARG E 259     4480   2940   4350    380    780    390       C  
ATOM   3494  NH1 ARG E 259      -4.874  21.346 -39.140  1.00 31.33           N  
ANISOU 3494  NH1 ARG E 259     4470   3030   4400    340    650    490       N  
ATOM   3495  NH2 ARG E 259      -6.830  20.977 -38.004  1.00 31.90           N  
ANISOU 3495  NH2 ARG E 259     4480   2840   4800    580   1060    560       N  
ATOM   3496  N   GLN E 260      -1.458  16.890 -41.585  1.00 15.82           N  
ANISOU 3496  N   GLN E 260     2120   2190   1700     50   -290    310       N  
ATOM   3497  CA  GLN E 260      -2.088  16.670 -42.918  1.00 15.68           C  
ANISOU 3497  CA  GLN E 260     2030   2270   1660      0   -320    390       C  
ATOM   3498  C   GLN E 260      -1.963  15.203 -43.365  1.00 15.06           C  
ANISOU 3498  C   GLN E 260     1950   2260   1510    -60   -270    280       C  
ATOM   3499  O   GLN E 260      -2.719  14.819 -44.261  1.00 14.74           O  
ANISOU 3499  O   GLN E 260     1920   2320   1370   -210   -290    310       O  
ATOM   3500  CB  GLN E 260      -1.537  17.607 -44.005  1.00 16.28           C  
ANISOU 3500  CB  GLN E 260     2080   2410   1690   -120   -380    470       C  
ATOM   3501  CG  GLN E 260      -0.078  17.410 -44.402  1.00 16.40           C  
ANISOU 3501  CG  GLN E 260     2110   2500   1620   -190   -350    370       C  
ATOM   3502  CD  GLN E 260       0.951  17.969 -43.448  1.00 16.55           C  
ANISOU 3502  CD  GLN E 260     2150   2470   1670   -160   -360    360       C  
ATOM   3503  OE1 GLN E 260       0.657  18.326 -42.307  1.00 16.77           O  
ANISOU 3503  OE1 GLN E 260     2260   2390   1720   -130   -360    360       O  
ATOM   3504  NE2 GLN E 260       2.182  18.059 -43.929  1.00 16.29           N  
ANISOU 3504  NE2 GLN E 260     2070   2520   1600   -230   -360    380       N  
ATOM   3505  N   LYS E 261      -1.067  14.414 -42.761  1.00 14.62           N  
ANISOU 3505  N   LYS E 261     1890   2160   1510     10   -180    200       N  
ATOM   3506  CA  LYS E 261      -0.919  12.987 -43.167  1.00 15.59           C  
ANISOU 3506  CA  LYS E 261     2030   2240   1650    -10    -10    100       C  
ATOM   3507  C   LYS E 261      -1.628  12.047 -42.178  1.00 15.44           C  
ANISOU 3507  C   LYS E 261     2010   2150   1700     90      0     90       C  
ATOM   3508  O   LYS E 261      -1.534  10.826 -42.379  1.00 16.14           O  
ANISOU 3508  O   LYS E 261     2140   2140   1850     80    190     10       O  
ATOM   3509  CB  LYS E 261       0.560  12.599 -43.264  1.00 16.26           C  
ANISOU 3509  CB  LYS E 261     2040   2270   1870     50    160    110       C  
ATOM   3510  CG  LYS E 261       1.356  13.354 -44.317  1.00 16.70           C  
ANISOU 3510  CG  LYS E 261     2100   2400   1850    -60    190    100       C  
ATOM   3511  CD  LYS E 261       0.824  13.189 -45.729  1.00 17.52           C  
ANISOU 3511  CD  LYS E 261     2360   2560   1740   -310    290    -40       C  
ATOM   3512  CE  LYS E 261       1.698  13.890 -46.749  1.00 18.40           C  
ANISOU 3512  CE  LYS E 261     2470   2750   1760   -450    340    -50       C  
ATOM   3513  NZ  LYS E 261       1.175  13.753 -48.122  1.00 19.94           N  
ANISOU 3513  NZ  LYS E 261     2850   3050   1670   -820    420   -160       N  
ATOM   3514  N   ARG E 262      -2.318  12.583 -41.168  1.00 15.01           N  
ANISOU 3514  N   ARG E 262     1950   2100   1650    150   -130    150       N  
ATOM   3515  CA  ARG E 262      -3.002  11.708 -40.173  1.00 15.14           C  
ANISOU 3515  CA  ARG E 262     1960   2070   1720    220   -130    150       C  
ATOM   3516  C   ARG E 262      -4.229  11.031 -40.780  1.00 15.07           C  
ANISOU 3516  C   ARG E 262     2000   2090   1640    140   -110    120       C  
ATOM   3517  O   ARG E 262      -4.800  11.559 -41.754  1.00 15.60           O  
ANISOU 3517  O   ARG E 262     2080   2250   1600     10   -170    170       O  
ATOM   3518  CB  ARG E 262      -3.431  12.500 -38.937  1.00 15.44           C  
ANISOU 3518  CB  ARG E 262     2020   2100   1750    260   -200    200       C  
ATOM   3519  CG  ARG E 262      -2.266  13.065 -38.145  1.00 16.20           C  
ANISOU 3519  CG  ARG E 262     2110   2220   1820    200   -250    250       C  
ATOM   3520  CD  ARG E 262      -2.721  13.980 -37.031  1.00 17.55           C  
ANISOU 3520  CD  ARG E 262     2420   2350   1900    110   -240    210       C  
ATOM   3521  NE  ARG E 262      -1.564  14.603 -36.412  1.00 19.04           N  
ANISOU 3521  NE  ARG E 262     2660   2610   1960    -90   -300    260       N  
ATOM   3522  CZ  ARG E 262      -1.609  15.542 -35.477  1.00 20.95           C  
ANISOU 3522  CZ  ARG E 262     3120   2800   2040   -300   -240    190       C  
ATOM   3523  NH1 ARG E 262      -0.482  16.042 -35.010  1.00 23.33           N  
ANISOU 3523  NH1 ARG E 262     3470   3220   2170   -580   -340    270       N  
ATOM   3524  NH2 ARG E 262      -2.762  16.000 -35.026  1.00 21.89           N  
ANISOU 3524  NH2 ARG E 262     3400   2740   2170   -280    -50     60       N  
ATOM   3525  N   THR E 263      -4.593   9.892 -40.192  1.00 15.30           N  
ANISOU 3525  N   THR E 263     2050   2060   1710    170    -60     90       N  
ATOM   3526  CA  THR E 263      -5.765   9.072 -40.586  1.00 15.92           C  
ANISOU 3526  CA  THR E 263     2190   2170   1690     30    -50     70       C  
ATOM   3527  C   THR E 263      -6.626   8.862 -39.333  1.00 14.74           C  
ANISOU 3527  C   THR E 263     1980   2020   1600    140   -120    140       C  
ATOM   3528  O   THR E 263      -6.184   8.122 -38.425  1.00 14.59           O  
ANISOU 3528  O   THR E 263     1950   1910   1680    240    -80    120       O  
ATOM   3529  CB  THR E 263      -5.314   7.746 -41.216  1.00 17.93           C  
ANISOU 3529  CB  THR E 263     2580   2290   1940    -80    190    -80       C  
ATOM   3530  OG1 THR E 263      -4.454   8.064 -42.309  1.00 20.13           O  
ANISOU 3530  OG1 THR E 263     2930   2550   2170   -190    320   -170       O  
ATOM   3531  CG2 THR E 263      -6.459   6.886 -41.703  1.00 19.59           C  
ANISOU 3531  CG2 THR E 263     2940   2540   1970   -350    210   -130       C  
ATOM   3532  N   ALA E 264      -7.785   9.519 -39.271  1.00 14.04           N  
ANISOU 3532  N   ALA E 264     1830   2030   1480    130   -220    260       N  
ATOM   3533  CA  ALA E 264      -8.686   9.366 -38.110  1.00 13.43           C  
ANISOU 3533  CA  ALA E 264     1700   1940   1460    230   -220    320       C  
ATOM   3534  C   ALA E 264      -9.358   7.989 -38.156  1.00 13.55           C  
ANISOU 3534  C   ALA E 264     1750   1990   1410    110   -230    310       C  
ATOM   3535  O   ALA E 264      -9.779   7.575 -39.245  1.00 14.61           O  
ANISOU 3535  O   ALA E 264     1930   2210   1410   -110   -260    330       O  
ATOM   3536  CB  ALA E 264      -9.712  10.476 -38.095  1.00 14.18           C  
ANISOU 3536  CB  ALA E 264     1670   2070   1650    290   -220    510       C  
ATOM   3537  N   THR E 265      -9.439   7.324 -36.999  1.00 12.91           N  
ANISOU 3537  N   THR E 265     1680   1850   1380    190   -210    280       N  
ATOM   3538  CA  THR E 265     -10.085   5.993 -36.844  1.00 13.29           C  
ANISOU 3538  CA  THR E 265     1780   1890   1380     90   -210    270       C  
ATOM   3539  C   THR E 265     -10.742   5.924 -35.465  1.00 12.88           C  
ANISOU 3539  C   THR E 265     1660   1860   1370    190   -240    330       C  
ATOM   3540  O   THR E 265     -10.624   6.898 -34.706  1.00 13.09           O  
ANISOU 3540  O   THR E 265     1660   1880   1440    280   -210    340       O  
ATOM   3541  CB  THR E 265      -9.086   4.830 -36.898  1.00 13.54           C  
ANISOU 3541  CB  THR E 265     1910   1740   1490     90    -80    160       C  
ATOM   3542  OG1 THR E 265      -8.255   4.985 -35.746  1.00 13.03           O  
ANISOU 3542  OG1 THR E 265     1750   1640   1560    250   -100    230       O  
ATOM   3543  CG2 THR E 265      -8.263   4.779 -38.166  1.00 14.40           C  
ANISOU 3543  CG2 THR E 265     2120   1760   1580    -10     70     50       C  
ATOM   3544  N   LYS E 266     -11.351   4.786 -35.142  1.00 13.31           N  
ANISOU 3544  N   LYS E 266     1740   1920   1400    110   -250    350       N  
ATOM   3545  CA  LYS E 266     -11.985   4.590 -33.816  1.00 13.27           C  
ANISOU 3545  CA  LYS E 266     1680   1950   1410    160   -270    410       C  
ATOM   3546  C   LYS E 266     -10.922   4.682 -32.715  1.00 13.02           C  
ANISOU 3546  C   LYS E 266     1670   1870   1420    210   -270    390       C  
ATOM   3547  O   LYS E 266     -11.289   5.040 -31.588  1.00 13.77           O  
ANISOU 3547  O   LYS E 266     1760   2020   1450    180   -260    400       O  
ATOM   3548  CB  LYS E 266     -12.707   3.241 -33.776  1.00 14.03           C  
ANISOU 3548  CB  LYS E 266     1820   2060   1460     30   -300    440       C  
ATOM   3549  CG  LYS E 266     -13.963   3.175 -34.636  1.00 15.23           C  
ANISOU 3549  CG  LYS E 266     1930   2360   1490   -140   -360    540       C  
ATOM   3550  CD  LYS E 266     -14.645   1.840 -34.615  1.00 16.54           C  
ANISOU 3550  CD  LYS E 266     2180   2540   1560   -330   -390    560       C  
ATOM   3551  CE  LYS E 266     -15.939   1.858 -35.390  1.00 18.33           C  
ANISOU 3551  CE  LYS E 266     2330   3010   1630   -590   -500    750       C  
ATOM   3552  NZ  LYS E 266     -16.536   0.510 -35.436  1.00 20.12           N  
ANISOU 3552  NZ  LYS E 266     2690   3250   1700   -870   -530    740       N  
ATOM   3553  N   ALA E 267      -9.657   4.400 -33.039  1.00 12.98           N  
ANISOU 3553  N   ALA E 267     1660   1770   1500    240   -260    390       N  
ATOM   3554  CA  ALA E 267      -8.570   4.434 -32.025  1.00 13.87           C  
ANISOU 3554  CA  ALA E 267     1710   1910   1650    220   -320    510       C  
ATOM   3555  C   ALA E 267      -7.850   5.792 -32.028  1.00 13.81           C  
ANISOU 3555  C   ALA E 267     1720   1950   1570    190   -330    470       C  
ATOM   3556  O   ALA E 267      -6.893   5.950 -31.261  1.00 14.50           O  
ANISOU 3556  O   ALA E 267     1760   2120   1630     80   -420    600       O  
ATOM   3557  CB  ALA E 267      -7.608   3.301 -32.297  1.00 14.79           C  
ANISOU 3557  CB  ALA E 267     1730   1880   2000    280   -270    640       C  
ATOM   3558  N   TYR E 268      -8.294   6.724 -32.875  1.00 13.71           N  
ANISOU 3558  N   TYR E 268     1770   1910   1520    250   -260    340       N  
ATOM   3559  CA  TYR E 268      -7.696   8.081 -33.009  1.00 14.06           C  
ANISOU 3559  CA  TYR E 268     1870   1960   1510    230   -240    290       C  
ATOM   3560  C   TYR E 268      -8.710   8.890 -33.811  1.00 13.88           C  
ANISOU 3560  C   TYR E 268     1850   1900   1520    310   -140    240       C  
ATOM   3561  O   TYR E 268      -8.525   9.076 -35.038  1.00 14.04           O  
ANISOU 3561  O   TYR E 268     1840   1910   1580    350   -160    250       O  
ATOM   3562  CB  TYR E 268      -6.307   7.964 -33.636  1.00 14.54           C  
ANISOU 3562  CB  TYR E 268     1860   2010   1660    240   -280    350       C  
ATOM   3563  CG  TYR E 268      -5.529   9.248 -33.741  1.00 14.85           C  
ANISOU 3563  CG  TYR E 268     1950   2070   1620    180   -280    330       C  
ATOM   3564  CD1 TYR E 268      -5.179   9.957 -32.604  1.00 16.40           C  
ANISOU 3564  CD1 TYR E 268     2240   2340   1650    -30   -310    340       C  
ATOM   3565  CD2 TYR E 268      -5.001   9.666 -34.950  1.00 14.77           C  
ANISOU 3565  CD2 TYR E 268     1910   2020   1670    250   -260    300       C  
ATOM   3566  CE1 TYR E 268      -4.428  11.119 -32.681  1.00 16.74           C  
ANISOU 3566  CE1 TYR E 268     2370   2390   1590   -150   -310    310       C  
ATOM   3567  CE2 TYR E 268      -4.225  10.810 -35.044  1.00 15.06           C  
ANISOU 3567  CE2 TYR E 268     1990   2080   1650    180   -270    290       C  
ATOM   3568  CZ  TYR E 268      -3.944  11.542 -33.904  1.00 15.98           C  
ANISOU 3568  CZ  TYR E 268     2220   2250   1600    -20   -300    290       C  
ATOM   3569  OH  TYR E 268      -3.177  12.664 -33.985  1.00 16.30           O  
ANISOU 3569  OH  TYR E 268     2350   2300   1550   -150   -300    280       O  
ATOM   3570  N   ASN E 269      -9.742   9.350 -33.097  1.00 14.42           N  
ANISOU 3570  N   ASN E 269     1950   1940   1590    320    -20    240       N  
ATOM   3571  CA  ASN E 269     -10.930  10.029 -33.674  1.00 14.95           C  
ANISOU 3571  CA  ASN E 269     1920   1970   1790    430    100    340       C  
ATOM   3572  C   ASN E 269     -10.587  11.374 -34.321  1.00 15.64           C  
ANISOU 3572  C   ASN E 269     2010   1950   1970    500    200    360       C  
ATOM   3573  O   ASN E 269      -9.472  11.924 -34.105  1.00 15.70           O  
ANISOU 3573  O   ASN E 269     2160   1910   1900    420    210    230       O  
ATOM   3574  CB  ASN E 269     -12.068  10.098 -32.646  1.00 16.15           C  
ANISOU 3574  CB  ASN E 269     2070   2070   1990    460    290    360       C  
ATOM   3575  CG  ASN E 269     -11.827  11.074 -31.518  1.00 17.46           C  
ANISOU 3575  CG  ASN E 269     2450   2070   2110    390    570    200       C  
ATOM   3576  OD1 ASN E 269     -11.489  12.222 -31.763  1.00 18.16           O  
ANISOU 3576  OD1 ASN E 269     2610   2010   2280    410    740    150       O  
ATOM   3577  ND2 ASN E 269     -12.074  10.648 -30.290  1.00 18.34           N  
ANISOU 3577  ND2 ASN E 269     2680   2210   2080    240    660    100       N  
ATOM   3578  N   VAL E 270     -11.552  11.871 -35.098  1.00 14.30           N  
ANISOU 3578  N   VAL E 270     1660   1830   1950   -210   -150    690       N  
ATOM   3579  CA  VAL E 270     -11.399  13.146 -35.851  1.00 13.13           C  
ANISOU 3579  CA  VAL E 270     1620   1690   1680   -130    -90    500       C  
ATOM   3580  C   VAL E 270     -11.015  14.290 -34.904  1.00 13.12           C  
ANISOU 3580  C   VAL E 270     1680   1840   1470   -170    -40    480       C  
ATOM   3581  O   VAL E 270     -10.126  15.077 -35.275  1.00 13.13           O  
ANISOU 3581  O   VAL E 270     1740   1800   1450   -160    -50    410       O  
ATOM   3582  CB  VAL E 270     -12.690  13.435 -36.636  1.00 12.91           C  
ANISOU 3582  CB  VAL E 270     1600   1630   1680    -70    -70    390       C  
ATOM   3583  CG1 VAL E 270     -12.671  14.809 -37.276  1.00 12.13           C  
ANISOU 3583  CG1 VAL E 270     1610   1540   1460     10    -20    240       C  
ATOM   3584  CG2 VAL E 270     -12.940  12.353 -37.677  1.00 13.32           C  
ANISOU 3584  CG2 VAL E 270     1630   1500   1930    -20   -200    350       C  
ATOM   3585  N   THR E 271     -11.647  14.366 -33.729  1.00 13.75           N  
ANISOU 3585  N   THR E 271     1740   2080   1410   -210      0    550       N  
ATOM   3586  CA  THR E 271     -11.371  15.455 -32.753  1.00 14.49           C  
ANISOU 3586  CA  THR E 271     1940   2300   1260   -210     10    460       C  
ATOM   3587  C   THR E 271      -9.918  15.403 -32.282  1.00 14.91           C  
ANISOU 3587  C   THR E 271     2010   2350   1300   -290   -120    520       C  
ATOM   3588  O   THR E 271      -9.285  16.472 -32.217  1.00 15.40           O  
ANISOU 3588  O   THR E 271     2170   2370   1310   -300   -190    400       O  
ATOM   3589  CB  THR E 271     -12.329  15.382 -31.559  1.00 16.04           C  
ANISOU 3589  CB  THR E 271     2110   2730   1250   -190    110    530       C  
ATOM   3590  OG1 THR E 271     -13.653  15.494 -32.085  1.00 15.42           O  
ANISOU 3590  OG1 THR E 271     1950   2660   1250   -120    220    500       O  
ATOM   3591  CG2 THR E 271     -12.072  16.461 -30.528  1.00 17.61           C  
ANISOU 3591  CG2 THR E 271     2470   3070   1150   -140     90    390       C  
ATOM   3592  N   GLN E 272      -9.429  14.209 -31.953  1.00 15.35           N  
ANISOU 3592  N   GLN E 272     1970   2410   1450   -350   -180    720       N  
ATOM   3593  CA  GLN E 272      -8.036  14.032 -31.464  1.00 16.32           C  
ANISOU 3593  CA  GLN E 272     2070   2540   1590   -410   -330    810       C  
ATOM   3594  C   GLN E 272      -7.035  14.312 -32.590  1.00 15.09           C  
ANISOU 3594  C   GLN E 272     1860   2220   1650   -390   -350    760       C  
ATOM   3595  O   GLN E 272      -6.029  14.957 -32.324  1.00 15.63           O  
ANISOU 3595  O   GLN E 272     1920   2290   1720   -450   -450    750       O  
ATOM   3596  CB  GLN E 272      -7.886  12.619 -30.898  1.00 17.58           C  
ANISOU 3596  CB  GLN E 272     2130   2720   1830   -450   -390   1070       C  
ATOM   3597  CG  GLN E 272      -8.817  12.360 -29.726  1.00 19.53           C  
ANISOU 3597  CG  GLN E 272     2400   3180   1840   -470   -330   1210       C  
ATOM   3598  CD  GLN E 272      -8.485  13.251 -28.557  1.00 21.61           C  
ANISOU 3598  CD  GLN E 272     2800   3660   1760   -480   -400   1140       C  
ATOM   3599  OE1 GLN E 272      -7.321  13.426 -28.211  1.00 22.76           O  
ANISOU 3599  OE1 GLN E 272     2960   3790   1890   -520   -590   1140       O  
ATOM   3600  NE2 GLN E 272      -9.512  13.779 -27.908  1.00 23.25           N  
ANISOU 3600  NE2 GLN E 272     3090   4070   1680   -410   -270   1070       N  
ATOM   3601  N   ALA E 273      -7.342  13.884 -33.809  1.00 14.15           N  
ANISOU 3601  N   ALA E 273     1710   1980   1690   -310   -260    720       N  
ATOM   3602  CA  ALA E 273      -6.418  14.076 -34.951  1.00 13.95           C  
ANISOU 3602  CA  ALA E 273     1630   1860   1810   -240   -220    700       C  
ATOM   3603  C   ALA E 273      -6.528  15.464 -35.584  1.00 13.66           C  
ANISOU 3603  C   ALA E 273     1670   1800   1710   -240   -150    580       C  
ATOM   3604  O   ALA E 273      -5.476  15.968 -36.055  1.00 14.17           O  
ANISOU 3604  O   ALA E 273     1660   1840   1880   -260   -140    640       O  
ATOM   3605  CB  ALA E 273      -6.703  13.026 -35.998  1.00 13.59           C  
ANISOU 3605  CB  ALA E 273     1560   1710   1890   -110   -160    680       C  
ATOM   3606  N   PHE E 274      -7.716  16.084 -35.586  1.00 13.41           N  
ANISOU 3606  N   PHE E 274     1760   1780   1560   -220   -110    450       N  
ATOM   3607  CA  PHE E 274      -7.833  17.383 -36.310  1.00 13.26           C  
ANISOU 3607  CA  PHE E 274     1820   1690   1530   -200    -70    360       C  
ATOM   3608  C   PHE E 274      -8.508  18.492 -35.492  1.00 13.87           C  
ANISOU 3608  C   PHE E 274     2020   1770   1480   -230   -120    230       C  
ATOM   3609  O   PHE E 274      -8.823  19.540 -36.074  1.00 14.18           O  
ANISOU 3609  O   PHE E 274     2140   1710   1530   -200   -100    160       O  
ATOM   3610  CB  PHE E 274      -8.603  17.143 -37.611  1.00 12.16           C  
ANISOU 3610  CB  PHE E 274     1720   1510   1400    -70     30    310       C  
ATOM   3611  CG  PHE E 274      -8.044  16.007 -38.426  1.00 11.98           C  
ANISOU 3611  CG  PHE E 274     1620   1470   1460     20     70    370       C  
ATOM   3612  CD1 PHE E 274      -6.773  16.093 -38.971  1.00 12.72           C  
ANISOU 3612  CD1 PHE E 274     1630   1580   1620     50    130    470       C  
ATOM   3613  CD2 PHE E 274      -8.805  14.881 -38.697  1.00 11.78           C  
ANISOU 3613  CD2 PHE E 274     1600   1410   1460    100     40    320       C  
ATOM   3614  CE1 PHE E 274      -6.253  15.047 -39.712  1.00 13.34           C  
ANISOU 3614  CE1 PHE E 274     1650   1660   1750    190    180    490       C  
ATOM   3615  CE2 PHE E 274      -8.288  13.843 -39.456  1.00 12.31           C  
ANISOU 3615  CE2 PHE E 274     1640   1430   1610    220     40    320       C  
ATOM   3616  CZ  PHE E 274      -7.011  13.925 -39.953  1.00 13.15           C  
ANISOU 3616  CZ  PHE E 274     1680   1580   1740    290    130    390       C  
ATOM   3617  N   GLY E 275      -8.725  18.286 -34.199  1.00 14.95           N  
ANISOU 3617  N   GLY E 275     2190   2020   1480   -270   -180    210       N  
ATOM   3618  CA  GLY E 275      -9.366  19.347 -33.401  1.00 16.48           C  
ANISOU 3618  CA  GLY E 275     2520   2240   1500   -240   -210     30       C  
ATOM   3619  C   GLY E 275     -10.878  19.268 -33.478  1.00 16.71           C  
ANISOU 3619  C   GLY E 275     2570   2340   1440   -110    -70    -40       C  
ATOM   3620  O   GLY E 275     -11.409  18.681 -34.453  1.00 15.07           O  
ANISOU 3620  O   GLY E 275     2270   2100   1350    -70     10     30       O  
ATOM   3621  N   ARG E 276     -11.543  19.867 -32.492  1.00 18.98           N  
ANISOU 3621  N   ARG E 276     2950   2740   1530    -30    -60   -170       N  
ATOM   3622  CA  ARG E 276     -13.023  19.864 -32.393  1.00 20.14           C  
ANISOU 3622  CA  ARG E 276     3060   3010   1590    120    100   -220       C  
ATOM   3623  C   ARG E 276     -13.640  20.627 -33.574  1.00 19.03           C  
ANISOU 3623  C   ARG E 276     2930   2690   1610    210    130   -320       C  
ATOM   3624  O   ARG E 276     -13.028  21.612 -34.039  1.00 18.56           O  
ANISOU 3624  O   ARG E 276     2990   2430   1630    190     20   -400       O  
ATOM   3625  CB  ARG E 276     -13.409  20.487 -31.046  1.00 24.23           C  
ANISOU 3625  CB  ARG E 276     3690   3700   1810    240    130   -380       C  
ATOM   3626  CG  ARG E 276     -14.906  20.589 -30.788  1.00 27.20           C  
ANISOU 3626  CG  ARG E 276     3990   4260   2090    430    340   -420       C  
ATOM   3627  CD  ARG E 276     -15.217  21.184 -29.422  1.00 31.81           C  
ANISOU 3627  CD  ARG E 276     4720   5070   2310    600    400   -590       C  
ATOM   3628  NE  ARG E 276     -16.650  21.386 -29.219  1.00 34.86           N  
ANISOU 3628  NE  ARG E 276     4990   5650   2610    830    640   -630       N  
ATOM   3629  CZ  ARG E 276     -17.205  21.852 -28.100  1.00 39.50           C  
ANISOU 3629  CZ  ARG E 276     5660   6500   2850   1060    780   -770       C  
ATOM   3630  NH1 ARG E 276     -18.518  22.000 -28.021  1.00 41.80           N  
ANISOU 3630  NH1 ARG E 276     5790   6980   3110   1280   1030   -770       N  
ATOM   3631  NH2 ARG E 276     -16.452  22.165 -27.059  1.00 42.07           N  
ANISOU 3631  NH2 ARG E 276     6230   6910   2840   1100    670   -930       N  
ATOM   3632  N   ARG E 277     -14.779  20.145 -34.083  1.00 18.36           N  
ANISOU 3632  N   ARG E 277     2710   2660   1600    280    230   -260       N  
ATOM   3633  CA  ARG E 277     -15.497  20.859 -35.168  1.00 17.90           C  
ANISOU 3633  CA  ARG E 277     2660   2470   1670    390    230   -340       C  
ATOM   3634  C   ARG E 277     -15.987  22.194 -34.586  1.00 19.82           C  
ANISOU 3634  C   ARG E 277     3030   2680   1820    560    240   -540       C  
ATOM   3635  O   ARG E 277     -16.362  22.208 -33.392  1.00 21.17           O  
ANISOU 3635  O   ARG E 277     3200   3050   1800    640    330   -610       O  
ATOM   3636  CB  ARG E 277     -16.702  20.071 -35.702  1.00 18.03           C  
ANISOU 3636  CB  ARG E 277     2490   2560   1800    440    280   -240       C  
ATOM   3637  CG  ARG E 277     -16.444  19.021 -36.780  1.00 16.45           C  
ANISOU 3637  CG  ARG E 277     2230   2270   1750    340    200   -130       C  
ATOM   3638  CD  ARG E 277     -15.550  17.827 -36.495  1.00 15.89           C  
ANISOU 3638  CD  ARG E 277     2120   2220   1700    200    170      0       C  
ATOM   3639  NE  ARG E 277     -14.139  18.156 -36.379  1.00 15.44           N  
ANISOU 3639  NE  ARG E 277     2190   2100   1580    140    130    -10       N  
ATOM   3640  CZ  ARG E 277     -13.317  18.377 -37.404  1.00 14.74           C  
ANISOU 3640  CZ  ARG E 277     2170   1890   1550    140     90    -10       C  
ATOM   3641  NH1 ARG E 277     -12.046  18.658 -37.171  1.00 15.07           N  
ANISOU 3641  NH1 ARG E 277     2260   1900   1570     70     60     20       N  
ATOM   3642  NH2 ARG E 277     -13.761  18.334 -38.651  1.00 14.29           N  
ANISOU 3642  NH2 ARG E 277     2130   1750   1550    220     60    -40       N  
ATOM   3643  N   GLY E 278     -15.998  23.264 -35.385  1.00 19.67           N  
ANISOU 3643  N   GLY E 278     3120   2440   1920    620    160   -630       N  
ATOM   3644  CA  GLY E 278     -16.465  24.569 -34.878  1.00 22.12           C  
ANISOU 3644  CA  GLY E 278     3560   2660   2190    810    140   -850       C  
ATOM   3645  C   GLY E 278     -16.662  25.593 -35.995  1.00 22.67           C  
ANISOU 3645  C   GLY E 278     3700   2450   2450    880     40   -870       C  
ATOM   3646  O   GLY E 278     -16.440  25.294 -37.170  1.00 20.79           O  
ANISOU 3646  O   GLY E 278     3420   2140   2330    800      0   -700       O  
ATOM   3647  N   PRO E 279     -17.090  26.830 -35.643  1.00 25.29           N  
ANISOU 3647  N   PRO E 279     4170   2630   2810   1070    -20  -1080       N  
ATOM   3648  CA  PRO E 279     -17.324  27.892 -36.625  1.00 26.48           C  
ANISOU 3648  CA  PRO E 279     4400   2480   3180   1150   -130  -1070       C  
ATOM   3649  C   PRO E 279     -16.122  28.758 -37.047  1.00 27.51           C  
ANISOU 3649  C   PRO E 279     4700   2280   3470    990   -330  -1010       C  
ATOM   3650  O   PRO E 279     -16.232  29.420 -38.054  1.00 27.45           O  
ANISOU 3650  O   PRO E 279     4730   2060   3640   1010   -410   -890       O  
ATOM   3651  CB  PRO E 279     -18.333  28.779 -35.881  1.00 29.55           C  
ANISOU 3651  CB  PRO E 279     4840   2840   3540   1460   -110  -1340       C  
ATOM   3652  CG  PRO E 279     -17.905  28.678 -34.427  1.00 30.85           C  
ANISOU 3652  CG  PRO E 279     5110   3150   3460   1470    -70  -1550       C  
ATOM   3653  CD  PRO E 279     -17.411  27.252 -34.271  1.00 28.07           C  
ANISOU 3653  CD  PRO E 279     4610   3080   2970   1240     30  -1340       C  
ATOM   3654  N   GLU E 280     -15.016  28.739 -36.297  1.00 28.66           N  
ANISOU 3654  N   GLU E 280     4930   2390   3570    820   -420  -1060       N  
ATOM   3655  CA  GLU E 280     -13.841  29.578 -36.669  1.00 30.58           C  
ANISOU 3655  CA  GLU E 280     5280   2300   4040    620   -620   -960       C  
ATOM   3656  C   GLU E 280     -13.252  29.079 -37.994  1.00 28.64           C  
ANISOU 3656  C   GLU E 280     4910   2090   3890    460   -550   -590       C  
ATOM   3657  O   GLU E 280     -13.395  27.887 -38.293  1.00 26.34           O  
ANISOU 3657  O   GLU E 280     4480   2080   3450    450   -390   -490       O  
ATOM   3658  CB  GLU E 280     -12.805  29.590 -35.545  1.00 32.25           C  
ANISOU 3658  CB  GLU E 280     5570   2490   4190    470   -770  -1090       C  
ATOM   3659  CG  GLU E 280     -13.345  30.175 -34.256  1.00 35.90           C  
ANISOU 3659  CG  GLU E 280     6220   2930   4490    680   -850  -1480       C  
ATOM   3660  CD  GLU E 280     -12.342  30.349 -33.125  1.00 38.44           C  
ANISOU 3660  CD  GLU E 280     6680   3190   4740    550  -1080  -1660       C  
ATOM   3661  OE1 GLU E 280     -11.167  29.969 -33.293  1.00 37.72           O  
ANISOU 3661  OE1 GLU E 280     6490   3080   4760    260  -1180  -1440       O  
ATOM   3662  OE2 GLU E 280     -12.741  30.888 -32.079  1.00 42.23           O  
ANISOU 3662  OE2 GLU E 280     7360   3650   5040    750  -1180  -2020       O  
ATOM   3663  N   GLN E 281     -12.617  29.975 -38.756  1.00 31.05           N  
ANISOU 3663  N   GLN E 281     5260   2110   4430    350   -670   -400       N  
ATOM   3664  CA  GLN E 281     -12.018  29.619 -40.075  1.00 30.54           C  
ANISOU 3664  CA  GLN E 281     5090   2110   4410    230   -580    -30       C  
ATOM   3665  C   GLN E 281     -10.872  28.613 -39.913  1.00 27.92           C  
ANISOU 3665  C   GLN E 281     4610   1980   4010     40   -490    100       C  
ATOM   3666  O   GLN E 281     -10.604  27.883 -40.877  1.00 25.39           O  
ANISOU 3666  O   GLN E 281     4190   1850   3610     40   -340    320       O  
ATOM   3667  CB  GLN E 281     -11.514  30.868 -40.797  1.00 34.81           C  
ANISOU 3667  CB  GLN E 281     5690   2300   5240    140   -710    210       C  
ATOM   3668  CG  GLN E 281     -12.631  31.784 -41.273  1.00 38.41           C  
ANISOU 3668  CG  GLN E 281     6270   2550   5780    350   -790    170       C  
ATOM   3669  CD  GLN E 281     -13.496  31.126 -42.323  1.00 38.61           C  
ANISOU 3669  CD  GLN E 281     6240   2830   5610    520   -630    280       C  
ATOM   3670  OE1 GLN E 281     -13.057  30.243 -43.063  1.00 39.12           O  
ANISOU 3670  OE1 GLN E 281     6210   3150   5510    460   -480    480       O  
ATOM   3671  NE2 GLN E 281     -14.738  31.570 -42.412  1.00 40.59           N  
ANISOU 3671  NE2 GLN E 281     6550   3000   5870    750   -680    140       N  
ATOM   3672  N   THR E 282     -10.225  28.583 -38.748  1.00 22.69           N  
ANISOU 3672  N   THR E 282     4170   2190   2260     70    480   -270       N  
ATOM   3673  CA  THR E 282      -9.088  27.648 -38.527  1.00 21.85           C  
ANISOU 3673  CA  THR E 282     3970   2210   2130    -60    350   -260       C  
ATOM   3674  C   THR E 282      -9.627  26.266 -38.128  1.00 21.11           C  
ANISOU 3674  C   THR E 282     3740   2230   2050      0    330   -210       C  
ATOM   3675  O   THR E 282      -8.839  25.312 -38.125  1.00 20.80           O  
ANISOU 3675  O   THR E 282     3590   2290   2020    -70    230   -180       O  
ATOM   3676  CB  THR E 282      -8.119  28.212 -37.477  1.00 22.41           C  
ANISOU 3676  CB  THR E 282     4180   2260   2070   -220    330   -330       C  
ATOM   3677  OG1 THR E 282      -8.823  28.328 -36.241  1.00 23.46           O  
ANISOU 3677  OG1 THR E 282     4420   2370   2120   -200    410   -380       O  
ATOM   3678  CG2 THR E 282      -7.539  29.558 -37.864  1.00 22.84           C  
ANISOU 3678  CG2 THR E 282     4390   2190   2110   -300    350   -370       C  
ATOM   3679  N   GLN E 283     -10.932  26.162 -37.854  1.00 21.18           N  
ANISOU 3679  N   GLN E 283     3740   2230   2080    120    420   -200       N  
ATOM   3680  CA  GLN E 283     -11.534  24.870 -37.422  1.00 20.47           C  
ANISOU 3680  CA  GLN E 283     3520   2250   2010    160    400   -150       C  
ATOM   3681  C   GLN E 283     -12.250  24.152 -38.568  1.00 18.99           C  
ANISOU 3681  C   GLN E 283     3180   2110   1930    250    380    -80       C  
ATOM   3682  O   GLN E 283     -12.775  24.836 -39.464  1.00 19.21           O  
ANISOU 3682  O   GLN E 283     3210   2080   2010    330    430    -70       O  
ATOM   3683  CB  GLN E 283     -12.578  25.117 -36.333  1.00 21.78           C  
ANISOU 3683  CB  GLN E 283     3760   2400   2110    230    510   -180       C  
ATOM   3684  CG  GLN E 283     -12.008  25.676 -35.039  1.00 23.17           C  
ANISOU 3684  CG  GLN E 283     4100   2550   2160    120    530   -250       C  
ATOM   3685  CD  GLN E 283     -13.109  25.994 -34.057  1.00 24.49           C  
ANISOU 3685  CD  GLN E 283     4350   2690   2260    210    660   -280       C  
ATOM   3686  OE1 GLN E 283     -14.072  26.698 -34.374  1.00 24.65           O  
ANISOU 3686  OE1 GLN E 283     4410   2630   2320    340    770   -280       O  
ATOM   3687  NE2 GLN E 283     -12.951  25.505 -32.840  1.00 24.90           N  
ANISOU 3687  NE2 GLN E 283     4430   2820   2220    130    650   -300       N  
ATOM   3688  N   GLY E 284     -12.260  22.815 -38.520  1.00 17.16           N  
ANISOU 3688  N   GLY E 284     2820   1970   1730    240    320    -40       N  
ATOM   3689  CA  GLY E 284     -12.998  22.020 -39.516  1.00 15.99           C  
ANISOU 3689  CA  GLY E 284     2540   1860   1670    310    300     20       C  
ATOM   3690  C   GLY E 284     -14.468  22.024 -39.125  1.00 16.20           C  
ANISOU 3690  C   GLY E 284     2540   1910   1700    410    380     60       C  
ATOM   3691  O   GLY E 284     -14.735  22.187 -37.928  1.00 16.33           O  
ANISOU 3691  O   GLY E 284     2620   1930   1650    410    440     40       O  
ATOM   3692  N   ASN E 285     -15.392  21.848 -40.073  1.00 15.95           N  
ANISOU 3692  N   ASN E 285     2420   1900   1740    480    390    120       N  
ATOM   3693  CA  ASN E 285     -16.842  21.880 -39.720  1.00 16.53           C  
ANISOU 3693  CA  ASN E 285     2440   2010   1820    570    470    180       C  
ATOM   3694  C   ASN E 285     -17.552  20.627 -40.240  1.00 15.76           C  
ANISOU 3694  C   ASN E 285     2200   2010   1780    570    420    250       C  
ATOM   3695  O   ASN E 285     -18.793  20.574 -40.147  1.00 16.12           O  
ANISOU 3695  O   ASN E 285     2170   2110   1840    640    470    320       O  
ATOM   3696  CB  ASN E 285     -17.544  23.076 -40.365  1.00 17.08           C  
ANISOU 3696  CB  ASN E 285     2540   2030   1920    680    550    210       C  
ATOM   3697  CG  ASN E 285     -17.571  22.990 -41.880  1.00 16.69           C  
ANISOU 3697  CG  ASN E 285     2400   2010   1930    680    490    250       C  
ATOM   3698  OD1 ASN E 285     -16.718  22.340 -42.489  1.00 16.00           O  
ANISOU 3698  OD1 ASN E 285     2290   1940   1860    590    400    230       O  
ATOM   3699  ND2 ASN E 285     -18.544  23.638 -42.502  1.00 17.47           N  
ANISOU 3699  ND2 ASN E 285     2460   2110   2070    780    550    330       N  
ATOM   3700  N   PHE E 286     -16.790  19.639 -40.701  1.00 14.53           N  
ANISOU 3700  N   PHE E 286     2000   1880   1640    480    330    240       N  
ATOM   3701  CA  PHE E 286     -17.401  18.442 -41.329  1.00 14.24           C  
ANISOU 3701  CA  PHE E 286     1840   1910   1660    460    270    290       C  
ATOM   3702  C   PHE E 286     -17.390  17.201 -40.425  1.00 14.39           C  
ANISOU 3702  C   PHE E 286     1830   1970   1670    400    250    310       C  
ATOM   3703  O   PHE E 286     -16.331  16.839 -39.824  1.00 13.30           O  
ANISOU 3703  O   PHE E 286     1740   1810   1510    350    220    270       O  
ATOM   3704  CB  PHE E 286     -16.649  18.159 -42.636  1.00 13.70           C  
ANISOU 3704  CB  PHE E 286     1760   1830   1620    410    200    270       C  
ATOM   3705  CG  PHE E 286     -17.253  17.095 -43.514  1.00 13.45           C  
ANISOU 3705  CG  PHE E 286     1630   1850   1630    370    150    310       C  
ATOM   3706  CD1 PHE E 286     -16.919  15.760 -43.344  1.00 13.06           C  
ANISOU 3706  CD1 PHE E 286     1560   1810   1590    300    100    300       C  
ATOM   3707  CD2 PHE E 286     -18.132  17.433 -44.530  1.00 13.45           C  
ANISOU 3707  CD2 PHE E 286     1570   1900   1640    390    150    360       C  
ATOM   3708  CE1 PHE E 286     -17.470  14.786 -44.160  1.00 13.00           C  
ANISOU 3708  CE1 PHE E 286     1490   1830   1610    240     60    330       C  
ATOM   3709  CE2 PHE E 286     -18.675  16.455 -45.350  1.00 13.58           C  
ANISOU 3709  CE2 PHE E 286     1510   1970   1680    330     90    400       C  
ATOM   3710  CZ  PHE E 286     -18.354  15.134 -45.156  1.00 13.21           C  
ANISOU 3710  CZ  PHE E 286     1460   1910   1640    250     50    370       C  
ATOM   3711  N   GLY E 287     -18.563  16.558 -40.349  1.00 14.83           N  
ANISOU 3711  N   GLY E 287     1790   2090   1750    420    260    380       N  
ATOM   3712  CA  GLY E 287     -18.714  15.304 -39.591  1.00 15.17           C  
ANISOU 3712  CA  GLY E 287     1790   2170   1790    360    230    410       C  
ATOM   3713  C   GLY E 287     -19.776  15.348 -38.513  1.00 16.10           C  
ANISOU 3713  C   GLY E 287     1880   2360   1880    410    300    460       C  
ATOM   3714  O   GLY E 287     -19.773  16.299 -37.717  1.00 16.83           O  
ANISOU 3714  O   GLY E 287     2040   2430   1920    470    370    440       O  
ATOM   3715  N   ASP E 288     -20.676  14.361 -38.532  1.00 16.85           N  
ANISOU 3715  N   ASP E 288     1880   2520   2010    370    280    540       N  
ATOM   3716  CA  ASP E 288     -21.715  14.213 -37.484  1.00 18.29           C  
ANISOU 3716  CA  ASP E 288     2010   2780   2160    410    340    610       C  
ATOM   3717  C   ASP E 288     -21.013  13.459 -36.349  1.00 18.35           C  
ANISOU 3717  C   ASP E 288     2060   2770   2140    360    330    590       C  
ATOM   3718  O   ASP E 288     -19.821  13.120 -36.535  1.00 16.05           O  
ANISOU 3718  O   ASP E 288     1820   2420   1860    310    270    540       O  
ATOM   3719  CB  ASP E 288     -22.988  13.527 -37.997  1.00 19.26           C  
ANISOU 3719  CB  ASP E 288     2000   2990   2330    380    320    710       C  
ATOM   3720  CG  ASP E 288     -22.831  12.077 -38.423  1.00 19.22           C  
ANISOU 3720  CG  ASP E 288     1960   2980   2370    260    230    730       C  
ATOM   3721  OD1 ASP E 288     -21.741  11.502 -38.207  1.00 19.14           O  
ANISOU 3721  OD1 ASP E 288     2020   2900   2360    210    200    670       O  
ATOM   3722  OD2 ASP E 288     -23.808  11.534 -38.979  1.00 20.40           O  
ANISOU 3722  OD2 ASP E 288     2010   3200   2540    210    200    800       O  
ATOM   3723  N   GLN E 289     -21.712  13.159 -35.253  1.00 19.77           N  
ANISOU 3723  N   GLN E 289     2200   3020   2290    370    380    650       N  
ATOM   3724  CA  GLN E 289     -21.037  12.490 -34.106  1.00 21.00           C  
ANISOU 3724  CA  GLN E 289     2400   3170   2410    320    370    650       C  
ATOM   3725  C   GLN E 289     -20.480  11.123 -34.504  1.00 19.81           C  
ANISOU 3725  C   GLN E 289     2220   2990   2320    230    270    670       C  
ATOM   3726  O   GLN E 289     -19.430  10.741 -33.951  1.00 19.03           O  
ANISOU 3726  O   GLN E 289     2170   2860   2200    190    240    650       O  
ATOM   3727  CB  GLN E 289     -21.983  12.378 -32.910  1.00 23.61           C  
ANISOU 3727  CB  GLN E 289     2690   3590   2690    350    440    720       C  
ATOM   3728  CG  GLN E 289     -22.384  13.735 -32.352  1.00 26.36           C  
ANISOU 3728  CG  GLN E 289     3100   3950   2960    460    550    690       C  
ATOM   3729  CD  GLN E 289     -23.173  13.660 -31.068  1.00 30.05           C  
ANISOU 3729  CD  GLN E 289     3550   4510   3360    490    640    750       C  
ATOM   3730  OE1 GLN E 289     -23.871  14.602 -30.700  1.00 35.22           O  
ANISOU 3730  OE1 GLN E 289     4230   5190   3970    590    750    750       O  
ATOM   3731  NE2 GLN E 289     -23.092  12.531 -30.380  1.00 31.57           N  
ANISOU 3731  NE2 GLN E 289     3700   4750   3550    420    600    800       N  
ATOM   3732  N   GLU E 290     -21.138  10.446 -35.445  1.00 19.74           N  
ANISOU 3732  N   GLU E 290     2140   2990   2380    190    240    710       N  
ATOM   3733  CA  GLU E 290     -20.725   9.084 -35.870  1.00 19.96           C  
ANISOU 3733  CA  GLU E 290     2150   2960   2470    100    160    720       C  
ATOM   3734  C   GLU E 290     -19.388   9.152 -36.625  1.00 18.09           C  
ANISOU 3734  C   GLU E 290     1990   2630   2250     90    120    640       C  
ATOM   3735  O   GLU E 290     -18.472   8.373 -36.260  1.00 17.13           O  
ANISOU 3735  O   GLU E 290     1900   2460   2150     60    100    640       O  
ATOM   3736  CB  GLU E 290     -21.868   8.455 -36.671  1.00 21.80           C  
ANISOU 3736  CB  GLU E 290     2300   3230   2750     40    140    780       C  
ATOM   3737  CG  GLU E 290     -21.674   6.988 -36.965  1.00 23.37           C  
ANISOU 3737  CG  GLU E 290     2500   3370   3000    -60     80    800       C  
ATOM   3738  CD  GLU E 290     -22.844   6.330 -37.681  1.00 25.16           C  
ANISOU 3738  CD  GLU E 290     2660   3640   3260   -150     50    860       C  
ATOM   3739  OE1 GLU E 290     -23.758   7.055 -38.141  1.00 26.23           O  
ANISOU 3739  OE1 GLU E 290     2720   3870   3380   -130     60    890       O  
ATOM   3740  OE2 GLU E 290     -22.842   5.090 -37.769  1.00 27.24           O  
ANISOU 3740  OE2 GLU E 290     2930   3850   3570   -250     20    880       O  
ATOM   3741  N   LEU E 291     -19.266  10.046 -37.615  1.00 16.88           N  
ANISOU 3741  N   LEU E 291     1860   2460   2100    120    120    580       N  
ATOM   3742  CA  LEU E 291     -17.987  10.152 -38.376  1.00 15.62           C  
ANISOU 3742  CA  LEU E 291     1760   2220   1960    110     80    510       C  
ATOM   3743  C   LEU E 291     -16.877  10.665 -37.454  1.00 15.09           C  
ANISOU 3743  C   LEU E 291     1750   2140   1840    140    100    480       C  
ATOM   3744  O   LEU E 291     -15.758  10.140 -37.536  1.00 15.00           O  
ANISOU 3744  O   LEU E 291     1760   2080   1860    120     60    470       O  
ATOM   3745  CB  LEU E 291     -18.147  11.089 -39.578  1.00 15.19           C  
ANISOU 3745  CB  LEU E 291     1710   2160   1900    140     80    470       C  
ATOM   3746  CG  LEU E 291     -16.848  11.402 -40.325  1.00 14.33           C  
ANISOU 3746  CG  LEU E 291     1660   1980   1800    140     60    400       C  
ATOM   3747  CD1 LEU E 291     -16.188  10.136 -40.854  1.00 14.43           C  
ANISOU 3747  CD1 LEU E 291     1680   1930   1870     90     20    390       C  
ATOM   3748  CD2 LEU E 291     -17.089  12.376 -41.453  1.00 14.28           C  
ANISOU 3748  CD2 LEU E 291     1650   1980   1790    170     60    370       C  
ATOM   3749  N   ILE E 292     -17.174  11.663 -36.623  1.00 15.08           N  
ANISOU 3749  N   ILE E 292     1770   2180   1780    190    140    480       N  
ATOM   3750  CA  ILE E 292     -16.137  12.227 -35.704  1.00 15.20           C  
ANISOU 3750  CA  ILE E 292     1860   2190   1730    180    150    440       C  
ATOM   3751  C   ILE E 292     -15.495  11.120 -34.857  1.00 15.33           C  
ANISOU 3751  C   ILE E 292     1860   2220   1740    140    120    500       C  
ATOM   3752  O   ILE E 292     -14.245  11.096 -34.765  1.00 15.11           O  
ANISOU 3752  O   ILE E 292     1860   2180   1710    110     80    480       O  
ATOM   3753  CB  ILE E 292     -16.739  13.330 -34.812  1.00 15.88           C  
ANISOU 3753  CB  ILE E 292     1990   2320   1730    230    220    430       C  
ATOM   3754  CG1 ILE E 292     -17.098  14.576 -35.627  1.00 15.82           C  
ANISOU 3754  CG1 ILE E 292     2010   2280   1720    290    260    380       C  
ATOM   3755  CG2 ILE E 292     -15.790  13.677 -33.674  1.00 16.30           C  
ANISOU 3755  CG2 ILE E 292     2120   2390   1690    200    220    400       C  
ATOM   3756  CD1 ILE E 292     -17.808  15.648 -34.823  1.00 16.88           C  
ANISOU 3756  CD1 ILE E 292     2200   2430   1780    350    360    370       C  
ATOM   3757  N   ARG E 293     -16.305  10.221 -34.289  1.00 15.44           N  
ANISOU 3757  N   ARG E 293     1820   2280   1770    120    130    570       N  
ATOM   3758  CA  ARG E 293     -15.730   9.175 -33.402  1.00 15.79           C  
ANISOU 3758  CA  ARG E 293     1840   2330   1820     90    100    640       C  
ATOM   3759  C   ARG E 293     -15.190   7.974 -34.197  1.00 15.47           C  
ANISOU 3759  C   ARG E 293     1780   2220   1880     60     60    660       C  
ATOM   3760  O   ARG E 293     -14.286   7.297 -33.664  1.00 15.52           O  
ANISOU 3760  O   ARG E 293     1780   2210   1900     50     40    710       O  
ATOM   3761  CB  ARG E 293     -16.767   8.764 -32.349  1.00 16.69           C  
ANISOU 3761  CB  ARG E 293     1920   2520   1900     80    140    710       C  
ATOM   3762  CG  ARG E 293     -17.996   8.041 -32.880  1.00 17.02           C  
ANISOU 3762  CG  ARG E 293     1900   2560   2010     70    150    750       C  
ATOM   3763  CD  ARG E 293     -18.978   7.785 -31.750  1.00 18.12           C  
ANISOU 3763  CD  ARG E 293     1990   2790   2100     60    190    830       C  
ATOM   3764  NE  ARG E 293     -20.096   6.947 -32.151  1.00 18.70           N  
ANISOU 3764  NE  ARG E 293     1990   2870   2240     30    190    900       N  
ATOM   3765  CZ  ARG E 293     -20.115   5.614 -32.083  1.00 19.24           C  
ANISOU 3765  CZ  ARG E 293     2030   2910   2370    -40    150    970       C  
ATOM   3766  NH1 ARG E 293     -19.070   4.941 -31.631  1.00 19.10           N  
ANISOU 3766  NH1 ARG E 293     2040   2840   2370    -50    130    990       N  
ATOM   3767  NH2 ARG E 293     -21.187   4.951 -32.479  1.00 19.79           N  
ANISOU 3767  NH2 ARG E 293     2040   2990   2490    -90    150   1020       N  
ATOM   3768  N   GLN E 294     -15.647   7.757 -35.434  1.00 15.05           N  
ANISOU 3768  N   GLN E 294     1720   2110   1890     60     50    630       N  
ATOM   3769  CA  GLN E 294     -15.195   6.565 -36.204  1.00 15.14           C  
ANISOU 3769  CA  GLN E 294     1730   2030   1990     30     30    640       C  
ATOM   3770  C   GLN E 294     -14.138   6.893 -37.267  1.00 14.51           C  
ANISOU 3770  C   GLN E 294     1690   1890   1930     50     10    570       C  
ATOM   3771  O   GLN E 294     -13.397   5.968 -37.624  1.00 14.51           O  
ANISOU 3771  O   GLN E 294     1700   1820   1990     50     10    590       O  
ATOM   3772  CB  GLN E 294     -16.417   5.875 -36.804  1.00 15.48           C  
ANISOU 3772  CB  GLN E 294     1750   2060   2080    -20     30    650       C  
ATOM   3773  CG  GLN E 294     -17.372   5.375 -35.731  1.00 16.47           C  
ANISOU 3773  CG  GLN E 294     1820   2250   2190    -50     40    740       C  
ATOM   3774  CD  GLN E 294     -18.603   4.701 -36.277  1.00 17.37           C  
ANISOU 3774  CD  GLN E 294     1900   2360   2340   -110     30    770       C  
ATOM   3775  OE1 GLN E 294     -18.921   4.797 -37.459  1.00 17.91           O  
ANISOU 3775  OE1 GLN E 294     1980   2400   2430   -140     20    720       O  
ATOM   3776  NE2 GLN E 294     -19.324   4.023 -35.399  1.00 17.89           N  
ANISOU 3776  NE2 GLN E 294     1920   2470   2410   -150     50    860       N  
ATOM   3777  N   GLY E 295     -14.057   8.131 -37.760  1.00 14.31           N  
ANISOU 3777  N   GLY E 295     1680   1890   1870     70     10    510       N  
ATOM   3778  CA  GLY E 295     -13.053   8.443 -38.799  1.00 14.12           C  
ANISOU 3778  CA  GLY E 295     1690   1810   1860     90      0    450       C  
ATOM   3779  C   GLY E 295     -13.188   7.536 -40.026  1.00 14.60           C  
ANISOU 3779  C   GLY E 295     1760   1800   1990     70      0    430       C  
ATOM   3780  O   GLY E 295     -14.329   7.349 -40.504  1.00 14.82           O  
ANISOU 3780  O   GLY E 295     1780   1830   2020     30      0    420       O  
ATOM   3781  N   THR E 296     -12.073   6.978 -40.517  1.00 14.67           N  
ANISOU 3781  N   THR E 296     1790   1740   2040     80      0    420       N  
ATOM   3782  CA  THR E 296     -12.093   6.092 -41.721  1.00 15.10           C  
ANISOU 3782  CA  THR E 296     1880   1710   2150     60     10    380       C  
ATOM   3783  C   THR E 296     -12.809   4.763 -41.431  1.00 15.82           C  
ANISOU 3783  C   THR E 296     1980   1740   2290     20     20    420       C  
ATOM   3784  O   THR E 296     -12.978   3.985 -42.390  1.00 16.75           O  
ANISOU 3784  O   THR E 296     2150   1780   2440    -20     30    380       O  
ATOM   3785  CB  THR E 296     -10.683   5.886 -42.289  1.00 15.02           C  
ANISOU 3785  CB  THR E 296     1900   1640   2170    110     30    370       C  
ATOM   3786  OG1 THR E 296      -9.875   5.306 -41.271  1.00 15.22           O  
ANISOU 3786  OG1 THR E 296     1900   1660   2230    140     50    450       O  
ATOM   3787  CG2 THR E 296     -10.056   7.185 -42.747  1.00 14.76           C  
ANISOU 3787  CG2 THR E 296     1860   1660   2090    130     20    320       C  
ATOM   3788  N   ASP E 297     -13.197   4.506 -40.176  1.00 15.87           N  
ANISOU 3788  N   ASP E 297     1950   1790   2290     10     20    500       N  
ATOM   3789  CA  ASP E 297     -13.954   3.269 -39.836  1.00 16.87           C  
ANISOU 3789  CA  ASP E 297     2080   1870   2460    -50     30    550       C  
ATOM   3790  C   ASP E 297     -15.447   3.534 -40.069  1.00 17.08           C  
ANISOU 3790  C   ASP E 297     2080   1960   2450   -110      0    540       C  
ATOM   3791  O   ASP E 297     -16.246   2.598 -39.915  1.00 17.63           O  
ANISOU 3791  O   ASP E 297     2150   2000   2550   -180      0    580       O  
ATOM   3792  CB  ASP E 297     -13.686   2.810 -38.400  1.00 16.98           C  
ANISOU 3792  CB  ASP E 297     2060   1910   2480    -20     30    650       C  
ATOM   3793  CG  ASP E 297     -12.277   2.285 -38.187  1.00 17.04           C  
ANISOU 3793  CG  ASP E 297     2080   1860   2540     40     50    700       C  
ATOM   3794  OD1 ASP E 297     -11.787   1.581 -39.081  1.00 17.28           O  
ANISOU 3794  OD1 ASP E 297     2160   1770   2630     50     80    670       O  
ATOM   3795  OD2 ASP E 297     -11.669   2.622 -37.151  1.00 16.61           O  
ANISOU 3795  OD2 ASP E 297     1980   1880   2450     70     40    760       O  
ATOM   3796  N   TYR E 298     -15.806   4.774 -40.400  1.00 16.89           N  
ANISOU 3796  N   TYR E 298     2030   2020   2370    -90    -10    500       N  
ATOM   3797  CA  TYR E 298     -17.227   5.134 -40.659  1.00 17.58           C  
ANISOU 3797  CA  TYR E 298     2070   2180   2430   -140    -20    510       C  
ATOM   3798  C   TYR E 298     -17.752   4.287 -41.829  1.00 18.77           C  
ANISOU 3798  C   TYR E 298     2250   2280   2610   -230    -50    480       C  
ATOM   3799  O   TYR E 298     -17.054   4.166 -42.853  1.00 17.79           O  
ANISOU 3799  O   TYR E 298     2190   2080   2490   -240    -50    410       O  
ATOM   3800  CB  TYR E 298     -17.326   6.644 -40.878  1.00 16.56           C  
ANISOU 3800  CB  TYR E 298     1920   2130   2240    -80    -20    480       C  
ATOM   3801  CG  TYR E 298     -18.701   7.176 -41.184  1.00 16.87           C  
ANISOU 3801  CG  TYR E 298     1890   2260   2260   -100    -30    510       C  
ATOM   3802  CD1 TYR E 298     -19.715   7.136 -40.240  1.00 17.36           C  
ANISOU 3802  CD1 TYR E 298     1890   2400   2300   -100    -10    590       C  
ATOM   3803  CD2 TYR E 298     -18.956   7.812 -42.388  1.00 16.52           C  
ANISOU 3803  CD2 TYR E 298     1840   2240   2190   -110    -50    470       C  
ATOM   3804  CE1 TYR E 298     -20.971   7.654 -40.513  1.00 17.87           C  
ANISOU 3804  CE1 TYR E 298     1880   2570   2350   -110    -10    630       C  
ATOM   3805  CE2 TYR E 298     -20.201   8.339 -42.675  1.00 17.04           C  
ANISOU 3805  CE2 TYR E 298     1830   2410   2240   -120    -50    520       C  
ATOM   3806  CZ  TYR E 298     -21.207   8.274 -41.731  1.00 17.71           C  
ANISOU 3806  CZ  TYR E 298     1840   2570   2310   -110    -30    600       C  
ATOM   3807  OH  TYR E 298     -22.425   8.801 -42.029  1.00 18.17           O  
ANISOU 3807  OH  TYR E 298     1810   2740   2350   -110    -30    670       O  
ATOM   3808  N   LYS E 299     -18.956   3.725 -41.675  1.00 21.39           N  
ANISOU 3808  N   LYS E 299     2540   2650   2940   -320    -60    540       N  
ATOM   3809  CA  LYS E 299     -19.569   2.828 -42.704  1.00 23.65           C  
ANISOU 3809  CA  LYS E 299     2860   2890   3240   -440    -90    510       C  
ATOM   3810  C   LYS E 299     -19.585   3.484 -44.091  1.00 22.44           C  
ANISOU 3810  C   LYS E 299     2730   2760   3040   -460   -120    440       C  
ATOM   3811  O   LYS E 299     -19.331   2.761 -45.072  1.00 23.12           O  
ANISOU 3811  O   LYS E 299     2900   2750   3130   -540   -130    370       O  
ATOM   3812  CB  LYS E 299     -20.965   2.372 -42.263  1.00 26.63           C  
ANISOU 3812  CB  LYS E 299     3160   3350   3610   -540   -120    600       C  
ATOM   3813  CG  LYS E 299     -21.950   3.473 -41.892  1.00 28.83           C  
ANISOU 3813  CG  LYS E 299     3320   3790   3840   -500   -120    670       C  
ATOM   3814  CD  LYS E 299     -23.238   2.924 -41.286  1.00 31.53           C  
ANISOU 3814  CD  LYS E 299     3580   4220   4180   -580   -140    780       C  
ATOM   3815  CE  LYS E 299     -24.166   3.982 -40.722  1.00 32.86           C  
ANISOU 3815  CE  LYS E 299     3620   4550   4310   -510   -110    860       C  
ATOM   3816  NZ  LYS E 299     -24.653   4.924 -41.757  1.00 33.47           N  
ANISOU 3816  NZ  LYS E 299     3650   4720   4350   -500   -140    850       N  
ATOM   3817  N   HIS E 300     -19.856   4.786 -44.176  1.00 21.07           N  
ANISOU 3817  N   HIS E 300     2480   2690   2830   -400   -120    450       N  
ATOM   3818  CA  HIS E 300     -19.881   5.451 -45.506  1.00 21.22           C  
ANISOU 3818  CA  HIS E 300     2510   2750   2810   -410   -150    390       C  
ATOM   3819  C   HIS E 300     -18.630   6.306 -45.730  1.00 18.45           C  
ANISOU 3819  C   HIS E 300     2200   2350   2450   -300   -120    330       C  
ATOM   3820  O   HIS E 300     -18.717   7.284 -46.499  1.00 17.80           O  
ANISOU 3820  O   HIS E 300     2100   2330   2330   -280   -130    310       O  
ATOM   3821  CB  HIS E 300     -21.184   6.226 -45.692  1.00 22.40           C  
ANISOU 3821  CB  HIS E 300     2550   3050   2910   -430   -180    470       C  
ATOM   3822  CG  HIS E 300     -22.365   5.323 -45.736  1.00 24.97           C  
ANISOU 3822  CG  HIS E 300     2830   3420   3240   -560   -220    530       C  
ATOM   3823  ND1 HIS E 300     -23.234   5.193 -44.681  1.00 27.11           N  
ANISOU 3823  ND1 HIS E 300     3010   3770   3520   -560   -210    630       N  
ATOM   3824  CD2 HIS E 300     -22.776   4.450 -46.680  1.00 27.38           C  
ANISOU 3824  CD2 HIS E 300     3170   3710   3520   -720   -270    510       C  
ATOM   3825  CE1 HIS E 300     -24.167   4.311 -44.990  1.00 28.80           C  
ANISOU 3825  CE1 HIS E 300     3200   4020   3730   -710   -250    680       C  
ATOM   3826  NE2 HIS E 300     -23.904   3.840 -46.212  1.00 29.07           N  
ANISOU 3826  NE2 HIS E 300     3310   3990   3740   -820   -290    600       N  
ATOM   3827  N   TRP E 301     -17.506   5.936 -45.113  1.00 16.88           N  
ANISOU 3827  N   TRP E 301     2060   2060   2290   -250    -90    310       N  
ATOM   3828  CA  TRP E 301     -16.255   6.715 -45.315  1.00 15.30           C  
ANISOU 3828  CA  TRP E 301     1890   1840   2090   -160    -70    260       C  
ATOM   3829  C   TRP E 301     -15.831   6.705 -46.786  1.00 14.90           C  
ANISOU 3829  C   TRP E 301     1900   1750   2020   -190    -70    190       C  
ATOM   3830  O   TRP E 301     -15.578   7.765 -47.341  1.00 14.12           O  
ANISOU 3830  O   TRP E 301     1780   1690   1880   -150    -80    160       O  
ATOM   3831  CB  TRP E 301     -15.110   6.264 -44.406  1.00 14.59           C  
ANISOU 3831  CB  TRP E 301     1830   1680   2030   -100    -40    270       C  
ATOM   3832  CG  TRP E 301     -13.857   6.974 -44.805  1.00 14.10           C  
ANISOU 3832  CG  TRP E 301     1790   1600   1970    -40    -20    230       C  
ATOM   3833  CD1 TRP E 301     -12.811   6.459 -45.509  1.00 14.04           C  
ANISOU 3833  CD1 TRP E 301     1840   1510   1980    -20      0    190       C  
ATOM   3834  CD2 TRP E 301     -13.605   8.387 -44.693  1.00 13.04           C  
ANISOU 3834  CD2 TRP E 301     1630   1530   1790     20    -30    220       C  
ATOM   3835  NE1 TRP E 301     -11.890   7.438 -45.767  1.00 13.63           N  
ANISOU 3835  NE1 TRP E 301     1780   1490   1910     40     10    170       N  
ATOM   3836  CE2 TRP E 301     -12.350   8.631 -45.284  1.00 12.89           C  
ANISOU 3836  CE2 TRP E 301     1650   1480   1780     50    -10    190       C  
ATOM   3837  CE3 TRP E 301     -14.294   9.455 -44.114  1.00 12.82           C  
ANISOU 3837  CE3 TRP E 301     1570   1580   1720     40    -30    250       C  
ATOM   3838  CZ2 TRP E 301     -11.776   9.901 -45.320  1.00 12.36           C  
ANISOU 3838  CZ2 TRP E 301     1570   1450   1670     90    -20    170       C  
ATOM   3839  CZ3 TRP E 301     -13.727  10.709 -44.146  1.00 12.34           C  
ANISOU 3839  CZ3 TRP E 301     1520   1540   1630     90    -20    230       C  
ATOM   3840  CH2 TRP E 301     -12.487  10.926 -44.741  1.00 12.28           C  
ANISOU 3840  CH2 TRP E 301     1540   1500   1630    110    -20    190       C  
ATOM   3841  N   PRO E 302     -15.767   5.547 -47.489  1.00 15.69           N  
ANISOU 3841  N   PRO E 302     2070   1760   2130   -260    -70    140       N  
ATOM   3842  CA  PRO E 302     -15.343   5.540 -48.890  1.00 15.92           C  
ANISOU 3842  CA  PRO E 302     2160   1760   2130   -290    -70     70       C  
ATOM   3843  C   PRO E 302     -16.192   6.498 -49.742  1.00 16.12           C  
ANISOU 3843  C   PRO E 302     2130   1900   2090   -330   -110     70       C  
ATOM   3844  O   PRO E 302     -15.640   7.127 -50.638  1.00 15.35           O  
ANISOU 3844  O   PRO E 302     2060   1820   1960   -310   -110     20       O  
ATOM   3845  CB  PRO E 302     -15.523   4.081 -49.346  1.00 17.19           C  
ANISOU 3845  CB  PRO E 302     2420   1810   2300   -390    -50     20       C  
ATOM   3846  CG  PRO E 302     -15.516   3.278 -48.057  1.00 17.51           C  
ANISOU 3846  CG  PRO E 302     2450   1790   2410   -370    -30     90       C  
ATOM   3847  CD  PRO E 302     -16.109   4.201 -47.005  1.00 16.72           C  
ANISOU 3847  CD  PRO E 302     2230   1820   2300   -330    -60    170       C  
ATOM   3848  N   GLN E 303     -17.492   6.603 -49.434  1.00 16.73           N  
ANISOU 3848  N   GLN E 303     2140   2070   2150   -390   -160    130       N  
ATOM   3849  CA  GLN E 303     -18.402   7.505 -50.191  1.00 17.76           C  
ANISOU 3849  CA  GLN E 303     2200   2330   2220   -420   -200    170       C  
ATOM   3850  C   GLN E 303     -17.995   8.970 -49.969  1.00 16.86           C  
ANISOU 3850  C   GLN E 303     2040   2270   2100   -290   -180    190       C  
ATOM   3851  O   GLN E 303     -18.308   9.804 -50.826  1.00 17.62           O  
ANISOU 3851  O   GLN E 303     2100   2440   2160   -290   -200    200       O  
ATOM   3852  CB  GLN E 303     -19.868   7.276 -49.818  1.00 19.40           C  
ANISOU 3852  CB  GLN E 303     2310   2640   2420   -500   -240    260       C  
ATOM   3853  CG  GLN E 303     -20.436   5.929 -50.259  1.00 21.38           C  
ANISOU 3853  CG  GLN E 303     2610   2860   2650   -660   -280    240       C  
ATOM   3854  CD  GLN E 303     -20.043   4.733 -49.418  1.00 23.06           C  
ANISOU 3854  CD  GLN E 303     2900   2940   2930   -680   -240    220       C  
ATOM   3855  OE1 GLN E 303     -19.000   4.688 -48.762  1.00 24.29           O  
ANISOU 3855  OE1 GLN E 303     3090   3000   3130   -570   -190    190       O  
ATOM   3856  NE2 GLN E 303     -20.896   3.724 -49.442  1.00 24.47           N  
ANISOU 3856  NE2 GLN E 303     3080   3120   3100   -820   -270    240       N  
ATOM   3857  N   ILE E 304     -17.324   9.271 -48.858  1.00 16.08           N  
ANISOU 3857  N   ILE E 304     1940   2120   2040   -200   -140    200       N  
ATOM   3858  CA  ILE E 304     -16.861  10.664 -48.586  1.00 15.10           C  
ANISOU 3858  CA  ILE E 304     1800   2030   1910    -90   -120    210       C  
ATOM   3859  C   ILE E 304     -15.474  10.849 -49.218  1.00 14.14           C  
ANISOU 3859  C   ILE E 304     1740   1840   1790    -60   -100    140       C  
ATOM   3860  O   ILE E 304     -15.265  11.872 -49.891  1.00 13.36           O  
ANISOU 3860  O   ILE E 304     1640   1770   1670    -30   -100    130       O  
ATOM   3861  CB  ILE E 304     -16.873  10.965 -47.073  1.00 14.88           C  
ANISOU 3861  CB  ILE E 304     1750   2000   1910    -30    -90    250       C  
ATOM   3862  CG1 ILE E 304     -18.309  10.929 -46.533  1.00 15.88           C  
ANISOU 3862  CG1 ILE E 304     1800   2210   2030    -40    -90    330       C  
ATOM   3863  CG2 ILE E 304     -16.191  12.298 -46.780  1.00 14.60           C  
ANISOU 3863  CG2 ILE E 304     1730   1960   1860     60    -60    240       C  
ATOM   3864  CD1 ILE E 304     -18.433  11.157 -45.052  1.00 16.16           C  
ANISOU 3864  CD1 ILE E 304     1810   2250   2070     20    -50    360       C  
ATOM   3865  N   ALA E 305     -14.590   9.864 -49.045  1.00 13.98           N  
ANISOU 3865  N   ALA E 305     1780   1730   1800    -70    -80    100       N  
ATOM   3866  CA  ALA E 305     -13.201   9.910 -49.567  1.00 13.53           C  
ANISOU 3866  CA  ALA E 305     1770   1620   1750    -40    -60     50       C  
ATOM   3867  C   ALA E 305     -13.158  10.032 -51.099  1.00 13.76           C  
ANISOU 3867  C   ALA E 305     1830   1660   1740    -80    -70      0       C  
ATOM   3868  O   ALA E 305     -12.118  10.485 -51.613  1.00 13.08           O  
ANISOU 3868  O   ALA E 305     1770   1560   1640    -40    -40    -30       O  
ATOM   3869  CB  ALA E 305     -12.456   8.687 -49.103  1.00 13.85           C  
ANISOU 3869  CB  ALA E 305     1860   1570   1840    -30    -20     40       C  
ATOM   3870  N   GLN E 306     -14.231   9.654 -51.802  1.00 14.50           N  
ANISOU 3870  N   GLN E 306     1920   1790   1790   -160   -100      0       N  
ATOM   3871  CA  GLN E 306     -14.224   9.742 -53.288  1.00 14.98           C  
ANISOU 3871  CA  GLN E 306     2020   1880   1790   -220   -110    -50       C  
ATOM   3872  C   GLN E 306     -14.129  11.212 -53.721  1.00 14.66           C  
ANISOU 3872  C   GLN E 306     1930   1920   1720   -170   -130    -20       C  
ATOM   3873  O   GLN E 306     -13.785  11.442 -54.879  1.00 14.96           O  
ANISOU 3873  O   GLN E 306     2000   1980   1710   -190   -130    -50       O  
ATOM   3874  CB  GLN E 306     -15.456   9.076 -53.906  1.00 15.79           C  
ANISOU 3874  CB  GLN E 306     2120   2030   1850   -350   -160    -50       C  
ATOM   3875  CG  GLN E 306     -16.762   9.782 -53.585  1.00 15.88           C  
ANISOU 3875  CG  GLN E 306     2030   2160   1850   -360   -210     50       C  
ATOM   3876  CD  GLN E 306     -17.951   9.057 -54.156  1.00 17.03           C  
ANISOU 3876  CD  GLN E 306     2160   2370   1940   -500   -260     60       C  
ATOM   3877  OE1 GLN E 306     -17.912   8.544 -55.274  1.00 18.10           O  
ANISOU 3877  OE1 GLN E 306     2360   2500   2010   -600   -280      0       O  
ATOM   3878  NE2 GLN E 306     -19.036   9.047 -53.400  1.00 17.21           N  
ANISOU 3878  NE2 GLN E 306     2090   2460   1980   -520   -290    150       N  
ATOM   3879  N   PHE E 307     -14.387  12.160 -52.812  1.00 14.33           N  
ANISOU 3879  N   PHE E 307     1830   1910   1710   -100   -130     40       N  
ATOM   3880  CA  PHE E 307     -14.318  13.603 -53.165  1.00 14.06           C  
ANISOU 3880  CA  PHE E 307     1760   1930   1650    -40   -130     80       C  
ATOM   3881  C   PHE E 307     -12.994  14.203 -52.685  1.00 13.58           C  
ANISOU 3881  C   PHE E 307     1740   1810   1620     30    -90     60       C  
ATOM   3882  O   PHE E 307     -12.711  15.366 -53.038  1.00 13.62           O  
ANISOU 3882  O   PHE E 307     1730   1830   1610     70    -90     70       O  
ATOM   3883  CB  PHE E 307     -15.519  14.357 -52.594  1.00 14.33           C  
ANISOU 3883  CB  PHE E 307     1720   2030   1690    -10   -140    160       C  
ATOM   3884  CG  PHE E 307     -16.843  13.838 -53.091  1.00 15.41           C  
ANISOU 3884  CG  PHE E 307     1810   2250   1800    -90   -180    200       C  
ATOM   3885  CD1 PHE E 307     -17.286  14.144 -54.368  1.00 16.20           C  
ANISOU 3885  CD1 PHE E 307     1880   2430   1840   -140   -220    230       C  
ATOM   3886  CD2 PHE E 307     -17.660  13.069 -52.278  1.00 15.96           C  
ANISOU 3886  CD2 PHE E 307     1840   2330   1890   -120   -190    230       C  
ATOM   3887  CE1 PHE E 307     -18.503  13.668 -54.829  1.00 17.25           C  
ANISOU 3887  CE1 PHE E 307     1950   2660   1940   -230   -270    280       C  
ATOM   3888  CE2 PHE E 307     -18.879  12.599 -52.741  1.00 16.81           C  
ANISOU 3888  CE2 PHE E 307     1890   2530   1970   -210   -240    290       C  
ATOM   3889  CZ  PHE E 307     -19.292  12.888 -54.018  1.00 17.29           C  
ANISOU 3889  CZ  PHE E 307     1920   2680   1970   -270   -280    310       C  
ATOM   3890  N   ALA E 308     -12.221  13.451 -51.900  1.00 13.15           N  
ANISOU 3890  N   ALA E 308     1710   1690   1600     40    -70     30       N  
ATOM   3891  CA  ALA E 308     -10.922  13.967 -51.412  1.00 13.09           C  
ANISOU 3891  CA  ALA E 308     1720   1640   1610     90    -50     20       C  
ATOM   3892  C   ALA E 308      -9.961  14.002 -52.591  1.00 13.27           C  
ANISOU 3892  C   ALA E 308     1770   1660   1610     90    -30    -10       C  
ATOM   3893  O   ALA E 308      -9.961  13.087 -53.408  1.00 13.97           O  
ANISOU 3893  O   ALA E 308     1880   1730   1690     60    -20    -50       O  
ATOM   3894  CB  ALA E 308     -10.381  13.106 -50.295  1.00 12.82           C  
ANISOU 3894  CB  ALA E 308     1690   1560   1620    110    -30     30       C  
ATOM   3895  N   PRO E 309      -9.112  15.041 -52.714  1.00 12.96           N  
ANISOU 3895  N   PRO E 309     1720   1630   1570    120    -30      0       N  
ATOM   3896  CA  PRO E 309      -8.188  15.131 -53.837  1.00 13.05           C  
ANISOU 3896  CA  PRO E 309     1750   1650   1560    120    -10    -20       C  
ATOM   3897  C   PRO E 309      -6.853  14.392 -53.703  1.00 12.83           C  
ANISOU 3897  C   PRO E 309     1730   1590   1560    140     30    -30       C  
ATOM   3898  O   PRO E 309      -6.328  14.283 -52.610  1.00 12.92           O  
ANISOU 3898  O   PRO E 309     1720   1580   1600    170     30      0       O  
ATOM   3899  CB  PRO E 309      -7.881  16.636 -53.885  1.00 13.05           C  
ANISOU 3899  CB  PRO E 309     1740   1680   1540    130    -20     10       C  
ATOM   3900  CG  PRO E 309      -7.941  17.064 -52.439  1.00 12.84           C  
ANISOU 3900  CG  PRO E 309     1710   1630   1540    150    -30     40       C  
ATOM   3901  CD  PRO E 309      -9.034  16.212 -51.826  1.00 12.92           C  
ANISOU 3901  CD  PRO E 309     1710   1630   1570    150    -30     40       C  
ATOM   3902  N   SER E 310      -6.364  13.873 -54.829  1.00 12.92           N  
ANISOU 3902  N   SER E 310     1770   1600   1550    140     70    -70       N  
ATOM   3903  CA  SER E 310      -5.030  13.232 -54.853  1.00 12.99           C  
ANISOU 3903  CA  SER E 310     1780   1570   1580    190    120    -60       C  
ATOM   3904  C   SER E 310      -4.026  14.346 -54.533  1.00 12.28           C  
ANISOU 3904  C   SER E 310     1640   1530   1500    210    110    -10       C  
ATOM   3905  O   SER E 310      -4.439  15.518 -54.555  1.00 11.52           O  
ANISOU 3905  O   SER E 310     1530   1470   1380    180     70     10       O  
ATOM   3906  CB  SER E 310      -4.742  12.635 -56.200  1.00 13.56           C  
ANISOU 3906  CB  SER E 310     1900   1640   1620    190    170   -110       C  
ATOM   3907  OG  SER E 310      -4.661  13.662 -57.182  1.00 13.42           O  
ANISOU 3907  OG  SER E 310     1870   1680   1540    170    160   -110       O  
ATOM   3908  N   ALA E 311      -2.765  14.016 -54.277  1.00 12.54           N  
ANISOU 3908  N   ALA E 311     1640   1570   1560    250    150     30       N  
ATOM   3909  CA  ALA E 311      -1.778  15.084 -53.986  1.00 12.44           C  
ANISOU 3909  CA  ALA E 311     1570   1610   1550    240    130     90       C  
ATOM   3910  C   ALA E 311      -1.626  15.985 -55.221  1.00 12.26           C  
ANISOU 3910  C   ALA E 311     1560   1630   1480    220    130     80       C  
ATOM   3911  O   ALA E 311      -1.495  17.226 -55.059  1.00 12.32           O  
ANISOU 3911  O   ALA E 311     1550   1660   1470    180     90    110       O  
ATOM   3912  CB  ALA E 311      -0.463  14.472 -53.572  1.00 12.97           C  
ANISOU 3912  CB  ALA E 311     1580   1690   1650    280    160    150       C  
ATOM   3913  N   SER E 312      -1.635  15.379 -56.406  1.00 12.26           N  
ANISOU 3913  N   SER E 312     1590   1620   1450    240    180     40       N  
ATOM   3914  CA  SER E 312      -1.507  16.124 -57.687  1.00 12.41           C  
ANISOU 3914  CA  SER E 312     1610   1690   1410    220    180     30       C  
ATOM   3915  C   SER E 312      -2.702  17.074 -57.845  1.00 12.01           C  
ANISOU 3915  C   SER E 312     1590   1650   1330    170    120     20       C  
ATOM   3916  O   SER E 312      -2.477  18.255 -58.163  1.00 11.84           O  
ANISOU 3916  O   SER E 312     1550   1660   1290    150    100     60       O  
ATOM   3917  CB  SER E 312      -1.403  15.155 -58.841  1.00 13.15           C  
ANISOU 3917  CB  SER E 312     1750   1770   1470    240    250    -20       C  
ATOM   3918  OG  SER E 312      -1.225  15.830 -60.072  1.00 13.59           O  
ANISOU 3918  OG  SER E 312     1810   1890   1460    220    260    -20       O  
ATOM   3919  N   ALA E 313      -3.914  16.579 -57.569  1.00 11.48           N  
ANISOU 3919  N   ALA E 313     1550   1550   1260    150    100    -10       N  
ATOM   3920  CA  ALA E 313      -5.159  17.372 -57.704  1.00 11.21           C  
ANISOU 3920  CA  ALA E 313     1520   1540   1200    120     50      0       C  
ATOM   3921  C   ALA E 313      -5.206  18.487 -56.653  1.00 10.87           C  
ANISOU 3921  C   ALA E 313     1460   1480   1190    130     20     40       C  
ATOM   3922  O   ALA E 313      -5.660  19.593 -56.979  1.00 10.21           O  
ANISOU 3922  O   ALA E 313     1380   1410   1090    120      0     80       O  
ATOM   3923  CB  ALA E 313      -6.358  16.461 -57.597  1.00 11.33           C  
ANISOU 3923  CB  ALA E 313     1560   1530   1210    100     30    -40       C  
ATOM   3924  N   PHE E 314      -4.728  18.206 -55.442  1.00 11.32           N  
ANISOU 3924  N   PHE E 314     1510   1500   1290    140     20     50       N  
ATOM   3925  CA  PHE E 314      -4.730  19.232 -54.371  1.00 11.43           C  
ANISOU 3925  CA  PHE E 314     1530   1500   1320    130    -10     80       C  
ATOM   3926  C   PHE E 314      -3.894  20.436 -54.822  1.00 11.77           C  
ANISOU 3926  C   PHE E 314     1570   1560   1340    110    -10    120       C  
ATOM   3927  O   PHE E 314      -4.362  21.587 -54.695  1.00 11.76           O  
ANISOU 3927  O   PHE E 314     1600   1530   1330    100    -20    140       O  
ATOM   3928  CB  PHE E 314      -4.230  18.616 -53.067  1.00 11.46           C  
ANISOU 3928  CB  PHE E 314     1520   1480   1350    130    -10     90       C  
ATOM   3929  CG  PHE E 314      -4.101  19.593 -51.932  1.00 11.27           C  
ANISOU 3929  CG  PHE E 314     1510   1440   1330    110    -30    110       C  
ATOM   3930  CD1 PHE E 314      -5.193  19.913 -51.148  1.00 11.11           C  
ANISOU 3930  CD1 PHE E 314     1530   1390   1300    110    -40    100       C  
ATOM   3931  CD2 PHE E 314      -2.874  20.165 -51.631  1.00 11.76           C  
ANISOU 3931  CD2 PHE E 314     1560   1520   1380     70    -40    140       C  
ATOM   3932  CE1 PHE E 314      -5.067  20.795 -50.085  1.00 11.28           C  
ANISOU 3932  CE1 PHE E 314     1590   1390   1310     80    -50    100       C  
ATOM   3933  CE2 PHE E 314      -2.752  21.051 -50.572  1.00 12.10           C  
ANISOU 3933  CE2 PHE E 314     1650   1550   1400     20    -70    150       C  
ATOM   3934  CZ  PHE E 314      -3.850  21.366 -49.802  1.00 11.75           C  
ANISOU 3934  CZ  PHE E 314     1650   1460   1350     30    -60    120       C  
ATOM   3935  N   PHE E 315      -2.699  20.178 -55.356  1.00 12.13           N  
ANISOU 3935  N   PHE E 315     1590   1640   1390    100     10    130       N  
ATOM   3936  CA  PHE E 315      -1.826  21.289 -55.824  1.00 12.80           C  
ANISOU 3936  CA  PHE E 315     1660   1750   1450     70     10    180       C  
ATOM   3937  C   PHE E 315      -2.196  21.735 -57.236  1.00 12.92           C  
ANISOU 3937  C   PHE E 315     1690   1790   1430     70     20    180       C  
ATOM   3938  O   PHE E 315      -1.748  22.822 -57.616  1.00 13.32           O  
ANISOU 3938  O   PHE E 315     1740   1850   1470     40     10    220       O  
ATOM   3939  CB  PHE E 315      -0.351  20.903 -55.733  1.00 13.31           C  
ANISOU 3939  CB  PHE E 315     1670   1860   1530     60     20    210       C  
ATOM   3940  CG  PHE E 315       0.166  20.938 -54.322  1.00 13.63           C  
ANISOU 3940  CG  PHE E 315     1700   1890   1590     30    -10    240       C  
ATOM   3941  CD1 PHE E 315       0.496  22.149 -53.738  1.00 14.48           C  
ANISOU 3941  CD1 PHE E 315     1830   1990   1680    -40    -40    270       C  
ATOM   3942  CD2 PHE E 315       0.298  19.784 -53.572  1.00 13.73           C  
ANISOU 3942  CD2 PHE E 315     1680   1910   1630     60      0    240       C  
ATOM   3943  CE1 PHE E 315       0.954  22.204 -52.430  1.00 14.88           C  
ANISOU 3943  CE1 PHE E 315     1870   2050   1730    -90    -80    290       C  
ATOM   3944  CE2 PHE E 315       0.765  19.841 -52.271  1.00 14.23           C  
ANISOU 3944  CE2 PHE E 315     1720   1980   1700     30    -30    270       C  
ATOM   3945  CZ  PHE E 315       1.093  21.049 -51.704  1.00 14.50           C  
ANISOU 3945  CZ  PHE E 315     1780   2020   1710    -60    -70    300       C  
ATOM   3946  N   GLY E 316      -3.021  20.956 -57.946  1.00 13.29           N  
ANISOU 3946  N   GLY E 316     1740   1850   1460    100     30    140       N  
ATOM   3947  CA  GLY E 316      -3.404  21.292 -59.332  1.00 13.67           C  
ANISOU 3947  CA  GLY E 316     1800   1940   1450     90     30    150       C  
ATOM   3948  C   GLY E 316      -4.718  22.047 -59.438  1.00 13.87           C  
ANISOU 3948  C   GLY E 316     1840   1960   1470     90      0    180       C  
ATOM   3949  O   GLY E 316      -4.814  22.890 -60.340  1.00 14.33           O  
ANISOU 3949  O   GLY E 316     1890   2050   1500     80      0    220       O  
ATOM   3950  N   MET E 317      -5.688  21.774 -58.554  1.00 14.06           N  
ANISOU 3950  N   MET E 317     1870   1950   1520    100    -20    160       N  
ATOM   3951  CA  MET E 317      -7.027  22.430 -58.605  1.00 14.50           C  
ANISOU 3951  CA  MET E 317     1920   2010   1580    120    -40    200       C  
ATOM   3952  C   MET E 317      -7.147  23.608 -57.636  1.00 14.63           C  
ANISOU 3952  C   MET E 317     1970   1950   1630    140    -30    230       C  
ATOM   3953  O   MET E 317      -7.900  24.542 -57.949  1.00 15.37           O  
ANISOU 3953  O   MET E 317     2070   2040   1730    170    -30    290       O  
ATOM   3954  CB  MET E 317      -8.141  21.468 -58.178  1.00 14.51           C  
ANISOU 3954  CB  MET E 317     1910   2020   1580    130    -50    170       C  
ATOM   3955  CG  MET E 317      -8.233  20.184 -58.966  1.00 15.04           C  
ANISOU 3955  CG  MET E 317     1980   2130   1610     90    -50    120       C  
ATOM   3956  SD  MET E 317      -9.600  19.161 -58.353  1.00 15.08           S  
ANISOU 3956  SD  MET E 317     1970   2140   1620     70    -80    100       S  
ATOM   3957  CE  MET E 317      -9.191  18.996 -56.617  1.00 15.02           C  
ANISOU 3957  CE  MET E 317     1970   2050   1690    110    -60     90       C  
ATOM   3958  N   SER E 318      -6.448  23.545 -56.506  1.00 14.28           N  
ANISOU 3958  N   SER E 318     1950   1860   1620    130    -20    210       N  
ATOM   3959  CA  SER E 318      -6.609  24.551 -55.434  1.00 14.12           C  
ANISOU 3959  CA  SER E 318     1980   1760   1620    140    -10    220       C  
ATOM   3960  C   SER E 318      -5.892  25.879 -55.683  1.00 14.70           C  
ANISOU 3960  C   SER E 318     2100   1790   1690    110      0    260       C  
ATOM   3961  O   SER E 318      -4.961  25.938 -56.503  1.00 13.65           O  
ANISOU 3961  O   SER E 318     1940   1700   1540     80    -10    270       O  
ATOM   3962  CB  SER E 318      -6.102  23.960 -54.136  1.00 14.20           C  
ANISOU 3962  CB  SER E 318     2000   1750   1650    120    -20    180       C  
ATOM   3963  OG  SER E 318      -6.713  22.705 -53.856  1.00 13.70           O  
ANISOU 3963  OG  SER E 318     1900   1710   1590    140    -20    150       O  
ATOM   3964  N   ARG E 319      -6.378  26.911 -54.988  1.00 14.98           N  
ANISOU 3964  N   ARG E 319     2200   1740   1740    130     20    270       N  
ATOM   3965  CA  ARG E 319      -5.713  28.233 -54.965  1.00 15.93           C  
ANISOU 3965  CA  ARG E 319     2400   1790   1870     90     30    290       C  
ATOM   3966  C   ARG E 319      -4.827  28.128 -53.732  1.00 15.31           C  
ANISOU 3966  C   ARG E 319     2360   1680   1780     20     20    250       C  
ATOM   3967  O   ARG E 319      -5.384  27.983 -52.630  1.00 15.41           O  
ANISOU 3967  O   ARG E 319     2410   1650   1790     40     40    210       O  
ATOM   3968  CB  ARG E 319      -6.659  29.430 -54.879  1.00 17.04           C  
ANISOU 3968  CB  ARG E 319     2610   1840   2030    150     80    330       C  
ATOM   3969  CG  ARG E 319      -7.558  29.560 -56.092  1.00 17.96           C  
ANISOU 3969  CG  ARG E 319     2660   2010   2150    220     90    410       C  
ATOM   3970  CD  ARG E 319      -8.059  30.972 -56.235  1.00 19.27           C  
ANISOU 3970  CD  ARG E 319     2900   2070   2350    270    140    470       C  
ATOM   3971  NE  ARG E 319      -6.933  31.896 -56.304  1.00 20.02           N  
ANISOU 3971  NE  ARG E 319     3070   2090   2440    190    140    480       N  
ATOM   3972  CZ  ARG E 319      -6.185  32.107 -57.390  1.00 20.31           C  
ANISOU 3972  CZ  ARG E 319     3070   2180   2460    140    110    520       C  
ATOM   3973  NH1 ARG E 319      -5.194  32.984 -57.345  1.00 20.54           N  
ANISOU 3973  NH1 ARG E 319     3170   2140   2490     60    120    530       N  
ATOM   3974  NH2 ARG E 319      -6.419  31.439 -58.510  1.00 19.63           N  
ANISOU 3974  NH2 ARG E 319     2890   2220   2350    160     90    560       N  
ATOM   3975  N   ILE E 320      -3.521  28.084 -53.952  1.00 15.26           N  
ANISOU 3975  N   ILE E 320     2330   1710   1760    -60    -10    260       N  
ATOM   3976  CA  ILE E 320      -2.514  27.910 -52.874  1.00 15.34           C  
ANISOU 3976  CA  ILE E 320     2350   1730   1750   -140    -40    230       C  
ATOM   3977  C   ILE E 320      -1.919  29.266 -52.490  1.00 16.68           C  
ANISOU 3977  C   ILE E 320     2620   1820   1900   -230    -40    240       C  
ATOM   3978  O   ILE E 320      -1.599  30.066 -53.381  1.00 16.86           O  
ANISOU 3978  O   ILE E 320     2660   1820   1920   -260    -30    290       O  
ATOM   3979  CB  ILE E 320      -1.425  26.913 -53.322  1.00 14.72           C  
ANISOU 3979  CB  ILE E 320     2170   1760   1670   -160    -60    250       C  
ATOM   3980  CG1 ILE E 320      -2.009  25.548 -53.704  1.00 14.09           C  
ANISOU 3980  CG1 ILE E 320     2010   1740   1600    -80    -50    230       C  
ATOM   3981  CG2 ILE E 320      -0.348  26.779 -52.256  1.00 15.24           C  
ANISOU 3981  CG2 ILE E 320     2220   1860   1710   -250   -100    260       C  
ATOM   3982  CD1 ILE E 320      -2.677  24.814 -52.573  1.00 13.30           C  
ANISOU 3982  CD1 ILE E 320     1920   1620   1510    -50    -50    190       C  
ATOM   3983  N   GLY E 321      -1.784  29.485 -51.185  1.00 17.64           N  
ANISOU 3983  N   GLY E 321     2820   1890   1990   -290    -40    200       N  
ATOM   3984  CA  GLY E 321      -1.196  30.712 -50.636  1.00 19.08           C  
ANISOU 3984  CA  GLY E 321     3120   1990   2140   -410    -50    190       C  
ATOM   3985  C   GLY E 321      -0.371  30.383 -49.409  1.00 20.78           C  
ANISOU 3985  C   GLY E 321     3340   2250   2310   -520   -100    170       C  
ATOM   3986  O   GLY E 321      -0.371  29.205 -48.972  1.00 19.38           O  
ANISOU 3986  O   GLY E 321     3070   2160   2130   -490   -120    160       O  
ATOM   3987  N   MET E 322       0.327  31.374 -48.876  1.00 23.68           N  
ANISOU 3987  N   MET E 322     3810   2560   2630   -660   -120    160       N  
ATOM   3988  CA  MET E 322       1.131  31.128 -47.665  1.00 26.04           C  
ANISOU 3988  CA  MET E 322     4120   2920   2860   -800   -170    150       C  
ATOM   3989  C   MET E 322       0.948  32.344 -46.765  1.00 26.70           C  
ANISOU 3989  C   MET E 322     4400   2860   2880   -900   -150     80       C  
ATOM   3990  O   MET E 322       1.087  33.471 -47.270  1.00 26.74           O  
ANISOU 3990  O   MET E 322     4510   2760   2890   -950   -130     90       O  
ATOM   3991  CB  MET E 322       2.597  30.905 -48.029  1.00 29.79           C  
ANISOU 3991  CB  MET E 322     4470   3530   3320   -910   -240    230       C  
ATOM   3992  CG  MET E 322       3.426  30.388 -46.874  1.00 33.62           C  
ANISOU 3992  CG  MET E 322     4910   4120   3740  -1030   -310    250       C  
ATOM   3993  SD  MET E 322       4.975  29.679 -47.473  1.00 37.57           S  
ANISOU 3993  SD  MET E 322     5200   4820   4260  -1080   -380    380       S  
ATOM   3994  CE  MET E 322       4.314  28.386 -48.516  1.00 36.28           C  
ANISOU 3994  CE  MET E 322     4910   4690   4190   -850   -320    390       C  
ATOM   3995  N   GLU E 323       0.548  32.120 -45.515  1.00 26.40           N  
ANISOU 3995  N   GLU E 323     4440   2800   2790   -920   -140     20       N  
ATOM   3996  CA  GLU E 323       0.350  33.265 -44.596  1.00 28.16           C  
ANISOU 3996  CA  GLU E 323     4880   2880   2940  -1020   -100    -60       C  
ATOM   3997  C   GLU E 323       0.920  32.935 -43.215  1.00 27.46           C  
ANISOU 3997  C   GLU E 323     4820   2870   2750  -1170   -160    -90       C  
ATOM   3998  O   GLU E 323       0.884  31.755 -42.800  1.00 26.15           O  
ANISOU 3998  O   GLU E 323     4520   2830   2580  -1120   -200    -70       O  
ATOM   3999  CB  GLU E 323      -1.134  33.629 -44.500  1.00 29.65           C  
ANISOU 3999  CB  GLU E 323     5180   2920   3160   -860     10   -120       C  
ATOM   4000  CG  GLU E 323      -2.005  32.509 -43.967  1.00 30.67           C  
ANISOU 4000  CG  GLU E 323     5230   3120   3300   -730     30   -140       C  
ATOM   4001  CD  GLU E 323      -3.479  32.851 -43.812  1.00 33.22           C  
ANISOU 4001  CD  GLU E 323     5650   3320   3660   -570    140   -180       C  
ATOM   4002  OE1 GLU E 323      -4.231  32.000 -43.272  1.00 34.48           O  
ANISOU 4002  OE1 GLU E 323     5750   3530   3820   -480    160   -200       O  
ATOM   4003  OE2 GLU E 323      -3.875  33.965 -44.222  1.00 36.89           O  
ANISOU 4003  OE2 GLU E 323     6240   3630   4150   -540    220   -190       O  
ATOM   4004  N   VAL E 324       1.457  33.958 -42.559  1.00 26.55           N  
ANISOU 4004  N   VAL E 324     3900   2700   3480   -380     90   -310       N  
ATOM   4005  CA  VAL E 324       2.008  33.831 -41.185  1.00 26.28           C  
ANISOU 4005  CA  VAL E 324     3810   2750   3430   -400     30   -390       C  
ATOM   4006  C   VAL E 324       0.960  34.459 -40.266  1.00 26.23           C  
ANISOU 4006  C   VAL E 324     3910   2680   3380   -340     10   -440       C  
ATOM   4007  O   VAL E 324       0.656  35.642 -40.465  1.00 27.30           O  
ANISOU 4007  O   VAL E 324     4150   2670   3550   -370     40   -470       O  
ATOM   4008  CB  VAL E 324       3.383  34.507 -41.065  1.00 27.02           C  
ANISOU 4008  CB  VAL E 324     3860   2850   3560   -550     10   -450       C  
ATOM   4009  CG1 VAL E 324       3.862  34.555 -39.623  1.00 27.62           C  
ANISOU 4009  CG1 VAL E 324     3900   3000   3600   -590    -70   -520       C  
ATOM   4010  CG2 VAL E 324       4.404  33.829 -41.966  1.00 26.80           C  
ANISOU 4010  CG2 VAL E 324     3700   2900   3590   -610     50   -420       C  
ATOM   4011  N   THR E 325       0.380  33.665 -39.367  1.00 25.32           N  
ANISOU 4011  N   THR E 325     3760   2660   3200   -260    -20   -440       N  
ATOM   4012  CA  THR E 325      -0.666  34.147 -38.426  1.00 25.55           C  
ANISOU 4012  CA  THR E 325     3870   2670   3170   -220    -10   -520       C  
ATOM   4013  C   THR E 325      -0.149  33.938 -37.008  1.00 26.45           C  
ANISOU 4013  C   THR E 325     3950   2920   3190   -290    -80   -580       C  
ATOM   4014  O   THR E 325       0.966  33.449 -36.829  1.00 26.61           O  
ANISOU 4014  O   THR E 325     3880   3020   3210   -360   -140   -550       O  
ATOM   4015  CB  THR E 325      -1.986  33.397 -38.656  1.00 24.35           C  
ANISOU 4015  CB  THR E 325     3720   2530   3000    -80     10   -460       C  
ATOM   4016  OG1 THR E 325      -1.793  32.052 -38.220  1.00 23.85           O  
ANISOU 4016  OG1 THR E 325     3570   2610   2880    -70    -40   -390       O  
ATOM   4017  CG2 THR E 325      -2.447  33.429 -40.099  1.00 23.74           C  
ANISOU 4017  CG2 THR E 325     3670   2360   2990    -30     50   -370       C  
ATOM   4018  N   PRO E 326      -0.899  34.351 -35.961  1.00 27.18           N  
ANISOU 4018  N   PRO E 326     4100   3040   3190   -290    -60   -690       N  
ATOM   4019  CA  PRO E 326      -0.463  34.137 -34.579  1.00 28.47           C  
ANISOU 4019  CA  PRO E 326     4230   3360   3220   -380   -130   -750       C  
ATOM   4020  C   PRO E 326      -0.140  32.669 -34.235  1.00 28.14           C  
ANISOU 4020  C   PRO E 326     4100   3480   3120   -380   -220   -610       C  
ATOM   4021  O   PRO E 326       0.770  32.450 -33.451  1.00 29.06           O  
ANISOU 4021  O   PRO E 326     4160   3700   3170   -480   -320   -600       O  
ATOM   4022  CB  PRO E 326      -1.657  34.654 -33.757  1.00 29.05           C  
ANISOU 4022  CB  PRO E 326     4380   3450   3210   -360    -60   -880       C  
ATOM   4023  CG  PRO E 326      -2.283  35.713 -34.643  1.00 28.94           C  
ANISOU 4023  CG  PRO E 326     4440   3210   3350   -280     30   -940       C  
ATOM   4024  CD  PRO E 326      -2.128  35.163 -36.046  1.00 27.47           C  
ANISOU 4024  CD  PRO E 326     4220   2960   3260   -210     20   -770       C  
ATOM   4025  N   SER E 327      -0.848  31.715 -34.854  1.00 26.92           N  
ANISOU 4025  N   SER E 327     3920   3310   3000   -270   -200   -500       N  
ATOM   4026  CA  SER E 327      -0.635  30.263 -34.589  1.00 26.65           C  
ANISOU 4026  CA  SER E 327     3800   3390   2940   -250   -300   -360       C  
ATOM   4027  C   SER E 327       0.619  29.722 -35.306  1.00 26.02           C  
ANISOU 4027  C   SER E 327     3600   3280   3000   -260   -360   -280       C  
ATOM   4028  O   SER E 327       1.122  28.687 -34.850  1.00 26.59           O  
ANISOU 4028  O   SER E 327     3590   3440   3080   -260   -470   -180       O  
ATOM   4029  CB  SER E 327      -1.875  29.454 -34.925  1.00 25.74           C  
ANISOU 4029  CB  SER E 327     3690   3270   2820   -150   -250   -280       C  
ATOM   4030  OG  SER E 327      -2.261  29.622 -36.283  1.00 24.78           O  
ANISOU 4030  OG  SER E 327     3580   3020   2810    -50   -160   -270       O  
ATOM   4031  N   GLY E 328       1.097  30.368 -36.382  1.00 25.47           N  
ANISOU 4031  N   GLY E 328     3530   3110   3040   -250   -290   -320       N  
ATOM   4032  CA  GLY E 328       2.318  29.897 -37.083  1.00 25.16           C  
ANISOU 4032  CA  GLY E 328     3360   3060   3130   -270   -330   -290       C  
ATOM   4033  C   GLY E 328       2.315  30.190 -38.579  1.00 23.84           C  
ANISOU 4033  C   GLY E 328     3200   2790   3060   -240   -220   -300       C  
ATOM   4034  O   GLY E 328       1.563  31.085 -39.006  1.00 23.23           O  
ANISOU 4034  O   GLY E 328     3240   2630   2950   -230   -140   -330       O  
ATOM   4035  N   THR E 329       3.174  29.493 -39.338  1.00 23.49           N  
ANISOU 4035  N   THR E 329     3030   2760   3130   -240   -220   -280       N  
ATOM   4036  CA  THR E 329       3.264  29.655 -40.816  1.00 22.75           C  
ANISOU 4036  CA  THR E 329     2930   2610   3100   -240   -110   -290       C  
ATOM   4037  C   THR E 329       2.343  28.610 -41.442  1.00 21.32           C  
ANISOU 4037  C   THR E 329     2750   2420   2930   -130    -70   -230       C  
ATOM   4038  O   THR E 329       2.516  27.418 -41.114  1.00 21.20           O  
ANISOU 4038  O   THR E 329     2630   2440   2980    -70   -140   -200       O  
ATOM   4039  CB  THR E 329       4.693  29.498 -41.337  1.00 23.86           C  
ANISOU 4039  CB  THR E 329     2920   2790   3350   -320   -100   -340       C  
ATOM   4040  OG1 THR E 329       5.501  30.440 -40.643  1.00 25.52           O  
ANISOU 4040  OG1 THR E 329     3130   3020   3550   -430   -140   -390       O  
ATOM   4041  CG2 THR E 329       4.799  29.720 -42.831  1.00 23.90           C  
ANISOU 4041  CG2 THR E 329     2930   2770   3390   -370     30   -360       C  
ATOM   4042  N   TRP E 330       1.476  29.031 -42.364  1.00 20.30           N  
ANISOU 4042  N   TRP E 330     2720   2230   2760   -120     10   -220       N  
ATOM   4043  CA  TRP E 330       0.480  28.096 -42.952  1.00 19.38           C  
ANISOU 4043  CA  TRP E 330     2610   2110   2640    -20     40   -170       C  
ATOM   4044  C   TRP E 330       0.436  28.131 -44.477  1.00 19.03           C  
ANISOU 4044  C   TRP E 330     2570   2050   2610    -50    140   -170       C  
ATOM   4045  O   TRP E 330       0.569  29.232 -45.063  1.00 19.47           O  
ANISOU 4045  O   TRP E 330     2710   2060   2630   -140    190   -180       O  
ATOM   4046  CB  TRP E 330      -0.915  28.464 -42.427  1.00 19.06           C  
ANISOU 4046  CB  TRP E 330     2690   2040   2510     40     30   -130       C  
ATOM   4047  CG  TRP E 330      -1.054  28.379 -40.942  1.00 19.52           C  
ANISOU 4047  CG  TRP E 330     2750   2140   2520     60    -40   -140       C  
ATOM   4048  CD1 TRP E 330      -0.670  29.310 -40.022  1.00 20.67           C  
ANISOU 4048  CD1 TRP E 330     2940   2290   2620    -10    -70   -190       C  
ATOM   4049  CD2 TRP E 330      -1.659  27.307 -40.205  1.00 19.65           C  
ANISOU 4049  CD2 TRP E 330     2740   2220   2510    110   -100    -80       C  
ATOM   4050  NE1 TRP E 330      -0.964  28.876 -38.759  1.00 21.06           N  
ANISOU 4050  NE1 TRP E 330     2980   2420   2590      0   -140   -180       N  
ATOM   4051  CE2 TRP E 330      -1.573  27.650 -38.839  1.00 20.51           C  
ANISOU 4051  CE2 TRP E 330     2870   2390   2530     70   -160   -100       C  
ATOM   4052  CE3 TRP E 330      -2.240  26.086 -40.566  1.00 19.08           C  
ANISOU 4052  CE3 TRP E 330     2630   2150   2470    180   -100    -20       C  
ATOM   4053  CZ2 TRP E 330      -2.062  26.815 -37.835  1.00 20.85           C  
ANISOU 4053  CZ2 TRP E 330     2910   2510   2500     80   -230    -40       C  
ATOM   4054  CZ3 TRP E 330      -2.723  25.262 -39.573  1.00 19.39           C  
ANISOU 4054  CZ3 TRP E 330     2650   2250   2460    200   -170     50       C  
ATOM   4055  CH2 TRP E 330      -2.639  25.627 -38.226  1.00 20.44           C  
ANISOU 4055  CH2 TRP E 330     2820   2450   2490    150   -230     40       C  
ATOM   4056  N   LEU E 331       0.237  26.951 -45.065  1.00 18.21           N  
ANISOU 4056  N   LEU E 331     2390   1970   2550      0    160   -170       N  
ATOM   4057  CA  LEU E 331       0.024  26.786 -46.522  1.00 18.12           C  
ANISOU 4057  CA  LEU E 331     2390   1970   2520    -40    260   -190       C  
ATOM   4058  C   LEU E 331      -1.501  26.767 -46.670  1.00 16.92           C  
ANISOU 4058  C   LEU E 331     2350   1790   2290     30    250   -110       C  
ATOM   4059  O   LEU E 331      -2.114  25.773 -46.241  1.00 16.41           O  
ANISOU 4059  O   LEU E 331     2250   1730   2250    120    210    -90       O  
ATOM   4060  CB  LEU E 331       0.674  25.489 -47.022  1.00 18.51           C  
ANISOU 4060  CB  LEU E 331     2280   2070   2680    -20    290   -260       C  
ATOM   4061  CG  LEU E 331       0.431  25.138 -48.494  1.00 18.94           C  
ANISOU 4061  CG  LEU E 331     2340   2160   2700    -80    400   -310       C  
ATOM   4062  CD1 LEU E 331       1.272  23.952 -48.927  1.00 19.72           C  
ANISOU 4062  CD1 LEU E 331     2250   2300   2930    -70    450   -430       C  
ATOM   4063  CD2 LEU E 331      -1.041  24.850 -48.770  1.00 18.32           C  
ANISOU 4063  CD2 LEU E 331     2360   2070   2540    -10    380   -230       C  
ATOM   4064  N   THR E 332      -2.085  27.852 -47.181  1.00 16.80           N  
ANISOU 4064  N   THR E 332     2460   1730   2200      0    260    -60       N  
ATOM   4065  CA  THR E 332      -3.558  27.971 -47.343  1.00 16.06           C  
ANISOU 4065  CA  THR E 332     2450   1600   2050     70    240     10       C  
ATOM   4066  C   THR E 332      -4.009  27.334 -48.658  1.00 15.92           C  
ANISOU 4066  C   THR E 332     2430   1630   1990     50    290     20       C  
ATOM   4067  O   THR E 332      -3.221  27.347 -49.638  1.00 16.31           O  
ANISOU 4067  O   THR E 332     2450   1730   2020    -70    350    -10       O  
ATOM   4068  CB  THR E 332      -3.976  29.442 -47.323  1.00 16.78           C  
ANISOU 4068  CB  THR E 332     2670   1600   2110     50    220     50       C  
ATOM   4069  OG1 THR E 332      -3.361  30.038 -48.466  1.00 17.39           O  
ANISOU 4069  OG1 THR E 332     2780   1670   2150    -80    260     80       O  
ATOM   4070  CG2 THR E 332      -3.567  30.155 -46.050  1.00 17.01           C  
ANISOU 4070  CG2 THR E 332     2710   1580   2170     60    180     10       C  
ATOM   4071  N   TYR E 333      -5.249  26.840 -48.684  1.00 15.25           N  
ANISOU 4071  N   TYR E 333     2360   1550   1880    130    260     70       N  
ATOM   4072  CA  TYR E 333      -5.802  26.193 -49.898  1.00 15.30           C  
ANISOU 4072  CA  TYR E 333     2370   1610   1840    100    290     80       C  
ATOM   4073  C   TYR E 333      -7.317  26.418 -49.968  1.00 15.22           C  
ANISOU 4073  C   TYR E 333     2420   1570   1790    170    240    160       C  
ATOM   4074  O   TYR E 333      -7.987  26.372 -48.928  1.00 15.02           O  
ANISOU 4074  O   TYR E 333     2390   1520   1800    270    200    170       O  
ATOM   4075  CB  TYR E 333      -5.465  24.699 -49.911  1.00 15.07           C  
ANISOU 4075  CB  TYR E 333     2220   1630   1870    120    330      0       C  
ATOM   4076  CG  TYR E 333      -6.055  23.893 -48.779  1.00 14.27           C  
ANISOU 4076  CG  TYR E 333     2080   1510   1830    230    270     10       C  
ATOM   4077  CD1 TYR E 333      -7.319  23.338 -48.881  1.00 13.90           C  
ANISOU 4077  CD1 TYR E 333     2050   1470   1760    290    250     50       C  
ATOM   4078  CD2 TYR E 333      -5.349  23.680 -47.608  1.00 14.28           C  
ANISOU 4078  CD2 TYR E 333     2030   1490   1910    270    230      0       C  
ATOM   4079  CE1 TYR E 333      -7.873  22.597 -47.848  1.00 13.50           C  
ANISOU 4079  CE1 TYR E 333     1970   1410   1750    360    210     80       C  
ATOM   4080  CE2 TYR E 333      -5.885  22.941 -46.564  1.00 14.08           C  
ANISOU 4080  CE2 TYR E 333     1980   1460   1920    340    180     30       C  
ATOM   4081  CZ  TYR E 333      -7.153  22.400 -46.681  1.00 13.55           C  
ANISOU 4081  CZ  TYR E 333     1930   1400   1820    380    170     70       C  
ATOM   4082  OH  TYR E 333      -7.683  21.680 -45.654  1.00 13.58           O  
ANISOU 4082  OH  TYR E 333     1910   1410   1840    430    120    120       O  
ATOM   4083  N   THR E 334      -7.828  26.680 -51.173  1.00 15.89           N  
ANISOU 4083  N   THR E 334     2560   1680   1800    110    230    220       N  
ATOM   4084  CA  THR E 334      -9.285  26.870 -51.400  1.00 16.02           C  
ANISOU 4084  CA  THR E 334     2610   1680   1790    180    170    310       C  
ATOM   4085  C   THR E 334      -9.621  26.267 -52.766  1.00 16.09           C  
ANISOU 4085  C   THR E 334     2620   1790   1700     90    180    330       C  
ATOM   4086  O   THR E 334      -8.714  26.172 -53.623  1.00 16.59           O  
ANISOU 4086  O   THR E 334     2690   1910   1700    -50    240    290       O  
ATOM   4087  CB  THR E 334      -9.734  28.339 -51.340  1.00 17.08           C  
ANISOU 4087  CB  THR E 334     2840   1710   1940    200     90    400       C  
ATOM   4088  OG1 THR E 334      -9.188  29.029 -52.457  1.00 18.51           O  
ANISOU 4088  OG1 THR E 334     3090   1890   2050     60     90    470       O  
ATOM   4089  CG2 THR E 334      -9.318  29.048 -50.073  1.00 17.47           C  
ANISOU 4089  CG2 THR E 334     2890   1670   2070    260     90    350       C  
ATOM   4090  N   GLY E 335     -10.875  25.876 -52.957  1.00 15.54           N  
ANISOU 4090  N   GLY E 335     2540   1740   1620    140    130    370       N  
ATOM   4091  CA  GLY E 335     -11.276  25.293 -54.245  1.00 16.04           C  
ANISOU 4091  CA  GLY E 335     2610   1910   1580     50    130    380       C  
ATOM   4092  C   GLY E 335     -12.695  24.764 -54.218  1.00 15.77           C  
ANISOU 4092  C   GLY E 335     2540   1900   1550    130     70    420       C  
ATOM   4093  O   GLY E 335     -13.392  24.906 -53.174  1.00 15.00           O  
ANISOU 4093  O   GLY E 335     2410   1740   1550    260     30    430       O  
ATOM   4094  N   ALA E 336     -13.105  24.183 -55.339  1.00 16.50           N  
ANISOU 4094  N   ALA E 336     2630   2090   1540     30     60    420       N  
ATOM   4095  CA  ALA E 336     -14.456  23.610 -55.485  1.00 16.57           C  
ANISOU 4095  CA  ALA E 336     2600   2150   1550     80      0    450       C  
ATOM   4096  C   ALA E 336     -14.358  22.382 -56.384  1.00 16.90           C  
ANISOU 4096  C   ALA E 336     2610   2310   1510    -40     60    350       C  
ATOM   4097  O   ALA E 336     -13.723  22.481 -57.447  1.00 17.78           O  
ANISOU 4097  O   ALA E 336     2760   2500   1500   -190     90    330       O  
ATOM   4098  CB  ALA E 336     -15.398  24.642 -56.053  1.00 17.76           C  
ANISOU 4098  CB  ALA E 336     2800   2290   1660     80   -130    600       C  
ATOM   4099  N   ILE E 337     -14.959  21.282 -55.937  1.00 16.31           N  
ANISOU 4099  N   ILE E 337     2460   2240   1500     20     70    280       N  
ATOM   4100  CA  ILE E 337     -14.993  19.977 -56.654  1.00 16.81           C  
ANISOU 4100  CA  ILE E 337     2480   2390   1530    -80    130    160       C  
ATOM   4101  C   ILE E 337     -16.417  19.779 -57.176  1.00 17.62           C  
ANISOU 4101  C   ILE E 337     2560   2570   1570    -90     40    230       C  
ATOM   4102  O   ILE E 337     -17.369  19.853 -56.369  1.00 16.83           O  
ANISOU 4102  O   ILE E 337     2420   2430   1550     20    -20    290       O  
ATOM   4103  CB  ILE E 337     -14.544  18.853 -55.703  1.00 15.98           C  
ANISOU 4103  CB  ILE E 337     2300   2200   1570    -10    200     50       C  
ATOM   4104  CG1 ILE E 337     -13.109  19.106 -55.224  1.00 15.72           C  
ANISOU 4104  CG1 ILE E 337     2260   2100   1610     10    270    -10       C  
ATOM   4105  CG2 ILE E 337     -14.709  17.489 -56.362  1.00 16.46           C  
ANISOU 4105  CG2 ILE E 337     2310   2310   1640    -90    250    -80       C  
ATOM   4106  CD1 ILE E 337     -12.629  18.173 -54.149  1.00 15.08           C  
ANISOU 4106  CD1 ILE E 337     2110   1930   1690     90    300    -70       C  
ATOM   4107  N   LYS E 338     -16.557  19.537 -58.473  1.00 19.38           N  
ANISOU 4107  N   LYS E 338     2810   2910   1640   -250     30    200       N  
ATOM   4108  CA  LYS E 338     -17.919  19.365 -59.042  1.00 20.91           C  
ANISOU 4108  CA  LYS E 338     2990   3190   1770   -280    -80    270       C  
ATOM   4109  C   LYS E 338     -18.397  17.924 -58.836  1.00 20.73           C  
ANISOU 4109  C   LYS E 338     2880   3180   1810   -280    -30    140       C  
ATOM   4110  O   LYS E 338     -17.600  17.001 -59.035  1.00 20.46           O  
ANISOU 4110  O   LYS E 338     2830   3140   1800   -350     80    -20       O  
ATOM   4111  CB  LYS E 338     -17.906  19.711 -60.532  1.00 23.14           C  
ANISOU 4111  CB  LYS E 338     3340   3620   1830   -470   -120    310       C  
ATOM   4112  CG  LYS E 338     -19.274  19.869 -61.192  1.00 24.96           C  
ANISOU 4112  CG  LYS E 338     3560   3950   1970   -510   -280    430       C  
ATOM   4113  CD  LYS E 338     -19.155  20.194 -62.663  1.00 27.46           C  
ANISOU 4113  CD  LYS E 338     3960   4430   2050   -730   -330    480       C  
ATOM   4114  CE  LYS E 338     -20.467  20.533 -63.338  1.00 29.65           C  
ANISOU 4114  CE  LYS E 338     4220   4800   2230   -770   -530    650       C  
ATOM   4115  NZ  LYS E 338     -21.444  19.419 -63.300  1.00 30.04           N  
ANISOU 4115  NZ  LYS E 338     4180   4920   2320   -770   -540    550       N  
ATOM   4116  N   LEU E 339     -19.631  17.761 -58.358  1.00 21.09           N  
ANISOU 4116  N   LEU E 339     2870   3230   1920   -200   -110    210       N  
ATOM   4117  CA  LEU E 339     -20.224  16.408 -58.225  1.00 21.57           C  
ANISOU 4117  CA  LEU E 339     2850   3300   2040   -230    -80    110       C  
ATOM   4118  C   LEU E 339     -20.756  16.021 -59.607  1.00 23.69           C  
ANISOU 4118  C   LEU E 339     3130   3720   2150   -400   -120     70       C  
ATOM   4119  O   LEU E 339     -21.273  16.914 -60.311  1.00 24.38           O  
ANISOU 4119  O   LEU E 339     3250   3900   2110   -440   -240    190       O  
ATOM   4120  CB  LEU E 339     -21.370  16.385 -57.205  1.00 20.96           C  
ANISOU 4120  CB  LEU E 339     2700   3190   2070   -110   -140    190       C  
ATOM   4121  CG  LEU E 339     -20.993  16.353 -55.725  1.00 19.83           C  
ANISOU 4121  CG  LEU E 339     2530   2930   2070     20    -80    190       C  
ATOM   4122  CD1 LEU E 339     -20.234  17.597 -55.302  1.00 19.20           C  
ANISOU 4122  CD1 LEU E 339     2510   2780   2000    100    -80    250       C  
ATOM   4123  CD2 LEU E 339     -22.241  16.179 -54.869  1.00 20.02           C  
ANISOU 4123  CD2 LEU E 339     2470   2970   2170     90   -120    240       C  
ATOM   4124  N   ASP E 340     -20.617  14.753 -59.988  1.00 25.18           N  
ANISOU 4124  N   ASP E 340     3290   3930   2350   -500    -50   -100       N  
ATOM   4125  CA  ASP E 340     -21.141  14.295 -61.298  1.00 27.71           C  
ANISOU 4125  CA  ASP E 340     3620   4410   2500   -680    -80   -170       C  
ATOM   4126  C   ASP E 340     -22.625  13.986 -61.089  1.00 28.98           C  
ANISOU 4126  C   ASP E 340     3700   4610   2700   -660   -190   -100       C  
ATOM   4127  O   ASP E 340     -22.916  12.948 -60.480  1.00 28.40           O  
ANISOU 4127  O   ASP E 340     3570   4460   2760   -640   -140   -180       O  
ATOM   4128  CB  ASP E 340     -20.353  13.084 -61.799  1.00 28.69           C  
ANISOU 4128  CB  ASP E 340     3740   4520   2640   -800     60   -420       C  
ATOM   4129  CG  ASP E 340     -20.761  12.587 -63.174  1.00 30.93           C  
ANISOU 4129  CG  ASP E 340     4040   4980   2730  -1020     50   -530       C  
ATOM   4130  OD1 ASP E 340     -21.602  13.251 -63.834  1.00 31.39           O  
ANISOU 4130  OD1 ASP E 340     4120   5190   2620  -1090    -90   -390       O  
ATOM   4131  OD2 ASP E 340     -20.233  11.538 -63.573  1.00 32.73           O  
ANISOU 4131  OD2 ASP E 340     4250   5190   3000  -1120    170   -760       O  
ATOM   4132  N   ASP E 341     -23.522  14.870 -61.541  1.00 31.12           N  
ANISOU 4132  N   ASP E 341     3970   4990   2870   -670   -340     70       N  
ATOM   4133  CA  ASP E 341     -24.976  14.618 -61.345  1.00 33.09           C  
ANISOU 4133  CA  ASP E 341     4110   5300   3160   -640   -450    130       C  
ATOM   4134  C   ASP E 341     -25.429  13.454 -62.242  1.00 33.51           C  
ANISOU 4134  C   ASP E 341     4140   5460   3130   -830   -440    -10       C  
ATOM   4135  O   ASP E 341     -26.592  13.026 -62.094  1.00 33.47           O  
ANISOU 4135  O   ASP E 341     4040   5510   3170   -840   -520     10       O  
ATOM   4136  CB  ASP E 341     -25.818  15.897 -61.491  1.00 35.87           C  
ANISOU 4136  CB  ASP E 341     4440   5700   3490   -570   -620    340       C  
ATOM   4137  CG  ASP E 341     -25.752  16.601 -62.836  1.00 39.26           C  
ANISOU 4137  CG  ASP E 341     4950   6270   3700   -710   -740    440       C  
ATOM   4138  OD1 ASP E 341     -24.887  16.238 -63.657  1.00 41.88           O  
ANISOU 4138  OD1 ASP E 341     5370   6670   3880   -870   -660    330       O  
ATOM   4139  OD2 ASP E 341     -26.589  17.505 -63.055  1.00 42.17           O  
ANISOU 4139  OD2 ASP E 341     5280   6680   4060   -660   -920    620       O  
ATOM   4140  N   LYS E 342     -24.551  12.943 -63.115  1.00 33.48           N  
ANISOU 4140  N   LYS E 342     4210   5500   3000   -990   -350   -170       N  
ATOM   4141  CA  LYS E 342     -24.953  11.787 -63.967  1.00 34.74           C  
ANISOU 4141  CA  LYS E 342     4350   5770   3080  -1180   -330   -340       C  
ATOM   4142  C   LYS E 342     -24.561  10.487 -63.250  1.00 32.86           C  
ANISOU 4142  C   LYS E 342     4070   5360   3050  -1150   -190   -530       C  
ATOM   4143  O   LYS E 342     -24.947   9.407 -63.730  1.00 34.49           O  
ANISOU 4143  O   LYS E 342     4250   5600   3250  -1280   -170   -690       O  
ATOM   4144  CB  LYS E 342     -24.398  11.897 -65.389  1.00 37.01           C  
ANISOU 4144  CB  LYS E 342     4720   6230   3110  -1400   -310   -430       C  
ATOM   4145  CG  LYS E 342     -24.889  13.129 -66.141  1.00 38.77           C  
ANISOU 4145  CG  LYS E 342     4990   6620   3130  -1460   -490   -210       C  
ATOM   4146  CD  LYS E 342     -24.642  13.101 -67.628  1.00 41.65           C  
ANISOU 4146  CD  LYS E 342     5430   7200   3190  -1730   -510   -290       C  
ATOM   4147  CE  LYS E 342     -25.430  12.006 -68.319  1.00 43.58           C  
ANISOU 4147  CE  LYS E 342     5630   7580   3350  -1910   -530   -440       C  
ATOM   4148  NZ  LYS E 342     -25.248  12.052 -69.786  1.00 46.39           N  
ANISOU 4148  NZ  LYS E 342     6070   8190   3370  -2200   -550   -510       N  
ATOM   4149  N   ASP E 343     -23.835  10.598 -62.135  1.00 29.72           N  
ANISOU 4149  N   ASP E 343     3680   4780   2830   -980   -110   -500       N  
ATOM   4150  CA  ASP E 343     -23.440   9.407 -61.337  1.00 28.37           C  
ANISOU 4150  CA  ASP E 343     3480   4420   2880   -940    -10   -630       C  
ATOM   4151  C   ASP E 343     -24.726   8.858 -60.714  1.00 27.85           C  
ANISOU 4151  C   ASP E 343     3330   4350   2910   -920    -80   -560       C  
ATOM   4152  O   ASP E 343     -25.502   9.620 -60.141  1.00 26.97           O  
ANISOU 4152  O   ASP E 343     3180   4280   2790   -820   -170   -380       O  
ATOM   4153  CB  ASP E 343     -22.355   9.800 -60.324  1.00 26.66           C  
ANISOU 4153  CB  ASP E 343     3280   4040   2800   -770     60   -590       C  
ATOM   4154  CG  ASP E 343     -21.839   8.681 -59.434  1.00 26.19           C  
ANISOU 4154  CG  ASP E 343     3200   3780   2980   -720    140   -680       C  
ATOM   4155  OD1 ASP E 343     -22.512   7.637 -59.331  1.00 26.75           O  
ANISOU 4155  OD1 ASP E 343     3220   3800   3140   -780    120   -740       O  
ATOM   4156  OD2 ASP E 343     -20.747   8.859 -58.868  1.00 25.42           O  
ANISOU 4156  OD2 ASP E 343     3120   3560   2980   -620    190   -690       O  
ATOM   4157  N   PRO E 344     -25.046   7.548 -60.850  1.00 28.19           N  
ANISOU 4157  N   PRO E 344     3340   4340   3040  -1030    -50   -710       N  
ATOM   4158  CA  PRO E 344     -26.275   7.007 -60.263  1.00 28.14           C  
ANISOU 4158  CA  PRO E 344     3250   4330   3120  -1040   -110   -640       C  
ATOM   4159  C   PRO E 344     -26.333   7.217 -58.739  1.00 26.16           C  
ANISOU 4159  C   PRO E 344     2970   3950   3020   -880   -100   -490       C  
ATOM   4160  O   PRO E 344     -27.421   7.225 -58.184  1.00 25.88           O  
ANISOU 4160  O   PRO E 344     2860   3970   3010   -870   -160   -380       O  
ATOM   4161  CB  PRO E 344     -26.234   5.509 -60.604  1.00 29.54           C  
ANISOU 4161  CB  PRO E 344     3420   4410   3400  -1180    -50   -850       C  
ATOM   4162  CG  PRO E 344     -25.277   5.414 -61.779  1.00 30.71           C  
ANISOU 4162  CG  PRO E 344     3630   4600   3440  -1280     20  -1050       C  
ATOM   4163  CD  PRO E 344     -24.279   6.535 -61.591  1.00 29.31           C  
ANISOU 4163  CD  PRO E 344     3510   4420   3210  -1150     50   -960       C  
ATOM   4164  N   ASN E 345     -25.166   7.425 -58.123  1.00 24.49           N  
ANISOU 4164  N   ASN E 345     2810   3600   2890   -760    -30   -480       N  
ATOM   4165  CA  ASN E 345     -25.046   7.634 -56.656  1.00 23.13           C  
ANISOU 4165  CA  ASN E 345     2630   3320   2840   -630    -30   -340       C  
ATOM   4166  C   ASN E 345     -25.195   9.120 -56.302  1.00 21.66           C  
ANISOU 4166  C   ASN E 345     2440   3230   2560   -500    -70   -190       C  
ATOM   4167  O   ASN E 345     -25.208   9.430 -55.099  1.00 20.46           O  
ANISOU 4167  O   ASN E 345     2280   3020   2480   -400    -60    -90       O  
ATOM   4168  CB  ASN E 345     -23.685   7.150 -56.141  1.00 22.89           C  
ANISOU 4168  CB  ASN E 345     2650   3090   2960   -570     50   -400       C  
ATOM   4169  CG  ASN E 345     -23.455   5.667 -56.343  1.00 24.24           C  
ANISOU 4169  CG  ASN E 345     2820   3110   3290   -670     80   -550       C  
ATOM   4170  OD1 ASN E 345     -24.402   4.899 -56.453  1.00 25.21           O  
ANISOU 4170  OD1 ASN E 345     2900   3240   3440   -770     50   -570       O  
ATOM   4171  ND2 ASN E 345     -22.196   5.255 -56.364  1.00 24.77           N  
ANISOU 4171  ND2 ASN E 345     2910   3020   3480   -630    140   -660       N  
ATOM   4172  N   PHE E 346     -25.344   9.999 -57.297  1.00 21.63           N  
ANISOU 4172  N   PHE E 346     2450   3360   2400   -520   -120   -180       N  
ATOM   4173  CA  PHE E 346     -25.426  11.456 -57.010  1.00 20.75           C  
ANISOU 4173  CA  PHE E 346     2350   3300   2240   -400   -170    -40       C  
ATOM   4174  C   PHE E 346     -26.404  11.789 -55.875  1.00 20.31           C  
ANISOU 4174  C   PHE E 346     2200   3260   2250   -300   -200     70       C  
ATOM   4175  O   PHE E 346     -25.993  12.499 -54.951  1.00 18.78           O  
ANISOU 4175  O   PHE E 346     2020   3010   2100   -180   -170    130       O  
ATOM   4176  CB  PHE E 346     -25.830  12.263 -58.246  1.00 21.68           C  
ANISOU 4176  CB  PHE E 346     2470   3570   2190   -450   -270      0       C  
ATOM   4177  CG  PHE E 346     -25.998  13.734 -57.961  1.00 21.20           C  
ANISOU 4177  CG  PHE E 346     2410   3530   2110   -320   -340    150       C  
ATOM   4178  CD1 PHE E 346     -24.892  14.566 -57.859  1.00 20.41           C  
ANISOU 4178  CD1 PHE E 346     2400   3360   1990   -250   -300    180       C  
ATOM   4179  CD2 PHE E 346     -27.255  14.287 -57.780  1.00 21.78           C  
ANISOU 4179  CD2 PHE E 346     2380   3690   2210   -260   -440    250       C  
ATOM   4180  CE1 PHE E 346     -25.044  15.921 -57.601  1.00 20.26           C  
ANISOU 4180  CE1 PHE E 346     2380   3340   1980   -140   -370    310       C  
ATOM   4181  CE2 PHE E 346     -27.406  15.643 -57.522  1.00 21.81           C  
ANISOU 4181  CE2 PHE E 346     2370   3680   2230   -130   -510    370       C  
ATOM   4182  CZ  PHE E 346     -26.302  16.458 -57.435  1.00 20.96           C  
ANISOU 4182  CZ  PHE E 346     2370   3490   2110    -70   -480    400       C  
ATOM   4183  N   LYS E 347     -27.643  11.305 -55.945  1.00 21.51           N  
ANISOU 4183  N   LYS E 347     2250   3510   2410   -360   -240     80       N  
ATOM   4184  CA  LYS E 347     -28.646  11.668 -54.899  1.00 22.08           C  
ANISOU 4184  CA  LYS E 347     2210   3620   2550   -280   -260    160       C  
ATOM   4185  C   LYS E 347     -28.184  11.196 -53.510  1.00 21.32           C  
ANISOU 4185  C   LYS E 347     2140   3410   2550   -250   -160    170       C  
ATOM   4186  O   LYS E 347     -28.423  11.954 -52.545  1.00 20.53           O  
ANISOU 4186  O   LYS E 347     2000   3330   2470   -140   -140    230       O  
ATOM   4187  CB  LYS E 347     -30.050  11.206 -55.308  1.00 23.74           C  
ANISOU 4187  CB  LYS E 347     2300   3970   2750   -380   -320    150       C  
ATOM   4188  CG  LYS E 347     -30.614  11.967 -56.506  1.00 25.01           C  
ANISOU 4188  CG  LYS E 347     2420   4260   2820   -390   -450    190       C  
ATOM   4189  CD  LYS E 347     -32.006  11.559 -56.947  1.00 26.85           C  
ANISOU 4189  CD  LYS E 347     2510   4640   3050   -480   -540    190       C  
ATOM   4190  CE  LYS E 347     -32.475  12.363 -58.142  1.00 28.32           C  
ANISOU 4190  CE  LYS E 347     2670   4960   3130   -490   -700    250       C  
ATOM   4191  NZ  LYS E 347     -33.862  12.024 -58.546  1.00 30.40           N  
ANISOU 4191  NZ  LYS E 347     2770   5380   3400   -580   -810    260       N  
ATOM   4192  N   ASP E 348     -27.528  10.031 -53.412  1.00 21.53           N  
ANISOU 4192  N   ASP E 348     2230   3320   2630   -330   -110    110       N  
ATOM   4193  CA  ASP E 348     -27.029   9.518 -52.103  1.00 21.47           C  
ANISOU 4193  CA  ASP E 348     2250   3190   2710   -320    -50    150       C  
ATOM   4194  C   ASP E 348     -25.843  10.367 -51.619  1.00 20.22           C  
ANISOU 4194  C   ASP E 348     2170   2960   2550   -190    -20    180       C  
ATOM   4195  O   ASP E 348     -25.733  10.572 -50.399  1.00 20.01           O  
ANISOU 4195  O   ASP E 348     2140   2910   2550   -140     10    250       O  
ATOM   4196  CB  ASP E 348     -26.663   8.039 -52.197  1.00 22.49           C  
ANISOU 4196  CB  ASP E 348     2420   3190   2940   -430    -30     90       C  
ATOM   4197  CG  ASP E 348     -27.871   7.143 -52.420  1.00 24.40           C  
ANISOU 4197  CG  ASP E 348     2580   3490   3200   -570    -50     70       C  
ATOM   4198  OD1 ASP E 348     -28.998   7.572 -52.075  1.00 25.24           O  
ANISOU 4198  OD1 ASP E 348     2590   3750   3260   -570    -70    130       O  
ATOM   4199  OD2 ASP E 348     -27.683   6.037 -52.955  1.00 25.80           O  
ANISOU 4199  OD2 ASP E 348     2790   3570   3450   -680    -50    -20       O  
ATOM   4200  N   GLN E 349     -24.993  10.829 -52.541  1.00 19.58           N  
ANISOU 4200  N   GLN E 349     2160   2850   2430   -160    -30    130       N  
ATOM   4201  CA  GLN E 349     -23.822  11.678 -52.195  1.00 18.43           C  
ANISOU 4201  CA  GLN E 349     2080   2640   2280    -60      0    150       C  
ATOM   4202  C   GLN E 349     -24.334  12.985 -51.586  1.00 17.59           C  
ANISOU 4202  C   GLN E 349     1940   2610   2130     50    -20    230       C  
ATOM   4203  O   GLN E 349     -23.753  13.449 -50.596  1.00 16.62           O  
ANISOU 4203  O   GLN E 349     1850   2440   2030    120     10    260       O  
ATOM   4204  CB  GLN E 349     -22.983  11.911 -53.453  1.00 18.60           C  
ANISOU 4204  CB  GLN E 349     2160   2660   2250    -80      0     70       C  
ATOM   4205  CG  GLN E 349     -22.410  10.619 -54.027  1.00 19.54           C  
ANISOU 4205  CG  GLN E 349     2300   2690   2430   -180     40    -60       C  
ATOM   4206  CD  GLN E 349     -21.851  10.772 -55.424  1.00 20.33           C  
ANISOU 4206  CD  GLN E 349     2440   2840   2450   -250     50   -170       C  
ATOM   4207  OE1 GLN E 349     -21.945  11.828 -56.046  1.00 20.39           O  
ANISOU 4207  OE1 GLN E 349     2470   2950   2320   -240     20   -130       O  
ATOM   4208  NE2 GLN E 349     -21.273   9.697 -55.939  1.00 21.28           N  
ANISOU 4208  NE2 GLN E 349     2560   2880   2640   -330    110   -320       N  
ATOM   4209  N   VAL E 350     -25.395  13.547 -52.164  1.00 18.08           N  
ANISOU 4209  N   VAL E 350     1930   2790   2140     50    -70    250       N  
ATOM   4210  CA  VAL E 350     -25.974  14.817 -51.633  1.00 18.07           C  
ANISOU 4210  CA  VAL E 350     1880   2840   2140    170   -100    310       C  
ATOM   4211  C   VAL E 350     -26.464  14.581 -50.200  1.00 18.01           C  
ANISOU 4211  C   VAL E 350     1810   2860   2180    190    -30    320       C  
ATOM   4212  O   VAL E 350     -26.107  15.382 -49.323  1.00 17.64           O  
ANISOU 4212  O   VAL E 350     1780   2780   2140    270      0    330       O  
ATOM   4213  CB  VAL E 350     -27.101  15.354 -52.530  1.00 19.17           C  
ANISOU 4213  CB  VAL E 350     1930   3100   2260    180   -190    330       C  
ATOM   4214  CG1 VAL E 350     -27.929  16.415 -51.817  1.00 19.70           C  
ANISOU 4214  CG1 VAL E 350     1890   3210   2390    300   -210    360       C  
ATOM   4215  CG2 VAL E 350     -26.558  15.863 -53.855  1.00 19.38           C  
ANISOU 4215  CG2 VAL E 350     2040   3120   2210    160   -260    350       C  
ATOM   4216  N   ILE E 351     -27.257  13.532 -49.987  1.00 18.54           N  
ANISOU 4216  N   ILE E 351     1810   2970   2270     90    -20    310       N  
ATOM   4217  CA  ILE E 351     -27.788  13.199 -48.632  1.00 19.26           C  
ANISOU 4217  CA  ILE E 351     1830   3110   2370     60     50    330       C  
ATOM   4218  C   ILE E 351     -26.626  12.990 -47.656  1.00 18.47           C  
ANISOU 4218  C   ILE E 351     1840   2900   2270     60     90    360       C  
ATOM   4219  O   ILE E 351     -26.688  13.537 -46.546  1.00 18.37           O  
ANISOU 4219  O   ILE E 351     1810   2940   2230     90    140    370       O  
ATOM   4220  CB  ILE E 351     -28.696  11.958 -48.706  1.00 20.53           C  
ANISOU 4220  CB  ILE E 351     1930   3320   2550    -90     50    330       C  
ATOM   4221  CG1 ILE E 351     -29.931  12.248 -49.566  1.00 21.72           C  
ANISOU 4221  CG1 ILE E 351     1950   3600   2700    -90    -10    300       C  
ATOM   4222  CG2 ILE E 351     -29.069  11.484 -47.307  1.00 21.30           C  
ANISOU 4222  CG2 ILE E 351     1990   3460   2640   -160    120    370       C  
ATOM   4223  CD1 ILE E 351     -30.826  11.056 -49.811  1.00 22.92           C  
ANISOU 4223  CD1 ILE E 351     2030   3820   2870   -240    -20    290       C  
ATOM   4224  N   LEU E 352     -25.594  12.262 -48.083  1.00 18.02           N  
ANISOU 4224  N   LEU E 352     1880   2720   2250     20     80    360       N  
ATOM   4225  CA  LEU E 352     -24.431  11.969 -47.205  1.00 17.75           C  
ANISOU 4225  CA  LEU E 352     1930   2570   2240     20     90    400       C  
ATOM   4226  C   LEU E 352     -23.705  13.268 -46.826  1.00 17.03           C  
ANISOU 4226  C   LEU E 352     1880   2480   2110    140    110    390       C  
ATOM   4227  O   LEU E 352     -23.465  13.470 -45.619  1.00 16.95           O  
ANISOU 4227  O   LEU E 352     1890   2480   2070    140    140    430       O  
ATOM   4228  CB  LEU E 352     -23.509  10.995 -47.946  1.00 18.10           C  
ANISOU 4228  CB  LEU E 352     2040   2470   2360    -20     70    360       C  
ATOM   4229  CG  LEU E 352     -22.246  10.570 -47.201  1.00 18.08           C  
ANISOU 4229  CG  LEU E 352     2110   2330   2430    -10     60    400       C  
ATOM   4230  CD1 LEU E 352     -22.592   9.962 -45.850  1.00 19.01           C  
ANISOU 4230  CD1 LEU E 352     2220   2460   2540    -90     50    510       C  
ATOM   4231  CD2 LEU E 352     -21.436   9.598 -48.037  1.00 18.26           C  
ANISOU 4231  CD2 LEU E 352     2160   2210   2570    -40     40    330       C  
ATOM   4232  N   LEU E 353     -23.378  14.116 -47.808  1.00 16.59           N  
ANISOU 4232  N   LEU E 353     1850   2410   2040    210     90    350       N  
ATOM   4233  CA  LEU E 353     -22.661  15.391 -47.517  1.00 16.25           C  
ANISOU 4233  CA  LEU E 353     1850   2350   1980    320    100    350       C  
ATOM   4234  C   LEU E 353     -23.536  16.277 -46.613  1.00 16.89           C  
ANISOU 4234  C   LEU E 353     1870   2520   2030    370    130    350       C  
ATOM   4235  O   LEU E 353     -22.994  16.793 -45.628  1.00 16.44           O  
ANISOU 4235  O   LEU E 353     1840   2450   1950    400    160    350       O  
ATOM   4236  CB  LEU E 353     -22.258  16.069 -48.834  1.00 16.13           C  
ANISOU 4236  CB  LEU E 353     1880   2310   1950    350     60    320       C  
ATOM   4237  CG  LEU E 353     -21.177  15.333 -49.637  1.00 15.87           C  
ANISOU 4237  CG  LEU E 353     1910   2190   1930    300     60    290       C  
ATOM   4238  CD1 LEU E 353     -21.042  15.896 -51.042  1.00 15.98           C  
ANISOU 4238  CD1 LEU E 353     1950   2230   1890    280     30    260       C  
ATOM   4239  CD2 LEU E 353     -19.833  15.372 -48.919  1.00 15.17           C  
ANISOU 4239  CD2 LEU E 353     1870   2010   1880    320     80    280       C  
ATOM   4240  N   ASN E 354     -24.845  16.378 -46.884  1.00 18.08           N  
ANISOU 4240  N   ASN E 354     1910   2770   2190    380    120    330       N  
ATOM   4241  CA  ASN E 354     -25.758  17.193 -46.031  1.00 19.27           C  
ANISOU 4241  CA  ASN E 354     1960   3020   2350    430    160    300       C  
ATOM   4242  C   ASN E 354     -25.742  16.694 -44.577  1.00 20.01           C  
ANISOU 4242  C   ASN E 354     2050   3170   2390    360    240    300       C  
ATOM   4243  O   ASN E 354     -25.944  17.528 -43.679  1.00 20.93           O  
ANISOU 4243  O   ASN E 354     2130   3340   2480    400    300    240       O  
ATOM   4244  CB  ASN E 354     -27.208  17.185 -46.527  1.00 20.35           C  
ANISOU 4244  CB  ASN E 354     1950   3260   2520    440    140    280       C  
ATOM   4245  CG  ASN E 354     -27.437  18.011 -47.773  1.00 20.73           C  
ANISOU 4245  CG  ASN E 354     1980   3280   2610    530     40    290       C  
ATOM   4246  OD1 ASN E 354     -26.585  18.806 -48.159  1.00 20.65           O  
ANISOU 4246  OD1 ASN E 354     2070   3170   2610    590     10    310       O  
ATOM   4247  ND2 ASN E 354     -28.603  17.863 -48.383  1.00 21.57           N  
ANISOU 4247  ND2 ASN E 354     1970   3470   2760    520    -10    290       N  
ATOM   4248  N   LYS E 355     -25.549  15.391 -44.348  1.00 20.35           N  
ANISOU 4248  N   LYS E 355     2130   3190   2410    230    240    360       N  
ATOM   4249  CA  LYS E 355     -25.537  14.853 -42.956  1.00 21.15           C  
ANISOU 4249  CA  LYS E 355     2240   3350   2440    130    300    400       C  
ATOM   4250  C   LYS E 355     -24.289  15.282 -42.178  1.00 19.77           C  
ANISOU 4250  C   LYS E 355     2170   3120   2220    150    300    420       C  
ATOM   4251  O   LYS E 355     -24.357  15.256 -40.926  1.00 20.63           O  
ANISOU 4251  O   LYS E 355     2280   3310   2240     70    350    430       O  
ATOM   4252  CB  LYS E 355     -25.483  13.321 -42.895  1.00 22.65           C  
ANISOU 4252  CB  LYS E 355     2470   3500   2640    -20    260    490       C  
ATOM   4253  CG  LYS E 355     -26.764  12.551 -43.171  1.00 24.91           C  
ANISOU 4253  CG  LYS E 355     2650   3870   2940   -120    280    490       C  
ATOM   4254  CD  LYS E 355     -26.584  11.061 -42.886  1.00 26.31           C  
ANISOU 4254  CD  LYS E 355     2890   3980   3140   -280    240    590       C  
ATOM   4255  CE  LYS E 355     -27.874  10.263 -42.878  1.00 28.25           C  
ANISOU 4255  CE  LYS E 355     3030   4320   3380   -410    270    600       C  
ATOM   4256  NZ  LYS E 355     -28.569  10.297 -44.186  1.00 28.68           N  
ANISOU 4256  NZ  LYS E 355     3010   4390   3500   -370    240    520       N  
ATOM   4257  N   HIS E 356     -23.207  15.651 -42.869  1.00 17.65           N  
ANISOU 4257  N   HIS E 356     1980   2720   2000    230    250    410       N  
ATOM   4258  CA  HIS E 356     -21.941  15.974 -42.158  1.00 16.92           C  
ANISOU 4258  CA  HIS E 356     1980   2560   1880    240    230    430       C  
ATOM   4259  C   HIS E 356     -21.562  17.456 -42.187  1.00 16.37           C  
ANISOU 4259  C   HIS E 356     1930   2480   1810    360    250    360       C  
ATOM   4260  O   HIS E 356     -20.827  17.854 -41.278  1.00 16.26           O  
ANISOU 4260  O   HIS E 356     1960   2470   1740    350    270    350       O  
ATOM   4261  CB  HIS E 356     -20.809  15.091 -42.704  1.00 15.91           C  
ANISOU 4261  CB  HIS E 356     1930   2290   1830    220    160    490       C  
ATOM   4262  CG  HIS E 356     -21.069  13.645 -42.465  1.00 16.38           C  
ANISOU 4262  CG  HIS E 356     1980   2330   1920    110    130    570       C  
ATOM   4263  ND1 HIS E 356     -20.924  13.077 -41.218  1.00 16.86           N  
ANISOU 4263  ND1 HIS E 356     2070   2410   1920      0    110    670       N  
ATOM   4264  CD2 HIS E 356     -21.480  12.657 -43.290  1.00 16.48           C  
ANISOU 4264  CD2 HIS E 356     1970   2290   2010     60    110    580       C  
ATOM   4265  CE1 HIS E 356     -21.243  11.802 -41.286  1.00 17.68           C  
ANISOU 4265  CE1 HIS E 356     2170   2470   2080    -90     80    750       C  
ATOM   4266  NE2 HIS E 356     -21.595  11.521 -42.542  1.00 17.14           N  
ANISOU 4266  NE2 HIS E 356     2060   2350   2100    -60     80    680       N  
ATOM   4267  N   ILE E 357     -22.012  18.230 -43.180  1.00 16.22           N  
ANISOU 4267  N   ILE E 357     1870   2450   1840    450    250    300       N  
ATOM   4268  CA  ILE E 357     -21.620  19.673 -43.231  1.00 15.99           C  
ANISOU 4268  CA  ILE E 357     1870   2370   1830    560    250    240       C  
ATOM   4269  C   ILE E 357     -22.279  20.431 -42.075  1.00 16.91           C  
ANISOU 4269  C   ILE E 357     1920   2580   1920    580    330    160       C  
ATOM   4270  O   ILE E 357     -23.514  20.443 -42.017  1.00 17.25           O  
ANISOU 4270  O   ILE E 357     1860   2720   1980    590    360    110       O  
ATOM   4271  CB  ILE E 357     -21.935  20.279 -44.613  1.00 15.93           C  
ANISOU 4271  CB  ILE E 357     1850   2310   1900    640    200    240       C  
ATOM   4272  CG1 ILE E 357     -21.081  19.611 -45.698  1.00 15.25           C  
ANISOU 4272  CG1 ILE E 357     1830   2150   1810    600    150    290       C  
ATOM   4273  CG2 ILE E 357     -21.742  21.789 -44.600  1.00 16.25           C  
ANISOU 4273  CG2 ILE E 357     1900   2290   1980    740    190    190       C  
ATOM   4274  CD1 ILE E 357     -21.415  20.031 -47.112  1.00 15.43           C  
ANISOU 4274  CD1 ILE E 357     1850   2150   1860    630     90    310       C  
ATOM   4275  N   ASP E 358     -21.457  20.994 -41.171  1.00 17.09           N  
ANISOU 4275  N   ASP E 358     2010   2600   1890    570    350    120       N  
ATOM   4276  CA  ASP E 358     -21.944  21.787 -40.001  1.00 18.78           C  
ANISOU 4276  CA  ASP E 358     2170   2910   2060    570    440      0       C  
ATOM   4277  C   ASP E 358     -22.874  20.958 -39.099  1.00 19.92           C  
ANISOU 4277  C   ASP E 358     2240   3220   2100    460    510      0       C  
ATOM   4278  O   ASP E 358     -23.761  21.568 -38.444  1.00 20.86           O  
ANISOU 4278  O   ASP E 358     2260   3450   2210    470    610   -130       O  
ATOM   4279  CB  ASP E 358     -22.658  23.069 -40.450  1.00 19.56           C  
ANISOU 4279  CB  ASP E 358     2200   2960   2270    710    460   -110       C  
ATOM   4280  CG  ASP E 358     -21.750  24.152 -41.008  1.00 19.42           C  
ANISOU 4280  CG  ASP E 358     2260   2780   2330    810    400   -120       C  
ATOM   4281  OD1 ASP E 358     -20.537  24.123 -40.716  1.00 18.41           O  
ANISOU 4281  OD1 ASP E 358     2240   2610   2150    760    390    -80       O  
ATOM   4282  OD2 ASP E 358     -22.274  25.035 -41.717  1.00 20.64           O  
ANISOU 4282  OD2 ASP E 358     2370   2860   2610    920    370   -150       O  
ATOM   4283  N   ALA E 359     -22.674  19.640 -39.037  1.00 19.76           N  
ANISOU 4283  N   ALA E 359     2260   3220   2030    340    480    120       N  
ATOM   4284  CA  ALA E 359     -23.533  18.781 -38.185  1.00 21.44           C  
ANISOU 4284  CA  ALA E 359     2410   3600   2140    200    540    150       C  
ATOM   4285  C   ALA E 359     -23.296  19.096 -36.701  1.00 23.07           C  
ANISOU 4285  C   ALA E 359     2640   3930   2180     90    610    100       C  
ATOM   4286  O   ALA E 359     -24.236  18.906 -35.903  1.00 24.35           O  
ANISOU 4286  O   ALA E 359     2730   4280   2250    -10    700     50       O  
ATOM   4287  CB  ALA E 359     -23.263  17.327 -38.483  1.00 20.94           C  
ANISOU 4287  CB  ALA E 359     2400   3480   2080    100    460    310       C  
ATOM   4288  N   TYR E 360     -22.111  19.618 -36.358  1.00 23.31           N  
ANISOU 4288  N   TYR E 360     2770   3900   2190    110    570    100       N  
ATOM   4289  CA  TYR E 360     -21.754  19.918 -34.942  1.00 25.59           C  
ANISOU 4289  CA  TYR E 360     3100   4320   2300    -10    620     50       C  
ATOM   4290  C   TYR E 360     -22.674  20.977 -34.310  1.00 27.74           C  
ANISOU 4290  C   TYR E 360     3280   4730   2530     10    770   -170       C  
ATOM   4291  O   TYR E 360     -22.712  21.060 -33.083  1.00 28.85           O  
ANISOU 4291  O   TYR E 360     3430   5040   2490   -130    840   -230       O  
ATOM   4292  CB  TYR E 360     -20.317  20.438 -34.832  1.00 24.90           C  
ANISOU 4292  CB  TYR E 360     3130   4120   2210     20    540     70       C  
ATOM   4293  CG  TYR E 360     -20.152  21.857 -35.307  1.00 24.57           C  
ANISOU 4293  CG  TYR E 360     3070   3980   2280    180    570    -80       C  
ATOM   4294  CD1 TYR E 360     -19.866  22.148 -36.630  1.00 23.38           C  
ANISOU 4294  CD1 TYR E 360     2930   3650   2300    330    510    -60       C  
ATOM   4295  CD2 TYR E 360     -20.320  22.916 -34.431  1.00 26.30           C  
ANISOU 4295  CD2 TYR E 360     3270   4290   2430    170    670   -270       C  
ATOM   4296  CE1 TYR E 360     -19.742  23.454 -37.070  1.00 23.45           C  
ANISOU 4296  CE1 TYR E 360     2940   3560   2410    460    530   -180       C  
ATOM   4297  CE2 TYR E 360     -20.196  24.229 -34.852  1.00 26.31           C  
ANISOU 4297  CE2 TYR E 360     3260   4170   2560    320    690   -410       C  
ATOM   4298  CZ  TYR E 360     -19.908  24.499 -36.177  1.00 25.05           C  
ANISOU 4298  CZ  TYR E 360     3120   3820   2580    460    610   -350       C  
ATOM   4299  OH  TYR E 360     -19.792  25.791 -36.597  1.00 25.61           O  
ANISOU 4299  OH  TYR E 360     3190   3760   2780    590    620   -460       O  
ATOM   4300  N  ALYS E 361     -23.385  21.749 -35.140  0.50 28.41           N  
ANISOU 4300  N  ALYS E 361     3260   4750   2780    180    800   -290       N  
ATOM   4301  N  BLYS E 361     -23.385  21.758 -35.133  0.50 28.42           N  
ANISOU 4301  N  BLYS E 361     3270   4750   2780    180    800   -290       N  
ATOM   4302  CA ALYS E 361     -24.298  22.827 -34.664  0.50 30.69           C  
ANISOU 4302  CA ALYS E 361     3430   5130   3100    240    940   -520       C  
ATOM   4303  CA BLYS E 361     -24.279  22.834 -34.618  0.50 30.73           C  
ANISOU 4303  CA BLYS E 361     3440   5140   3100    230    940   -530       C  
ATOM   4304  C  ALYS E 361     -25.506  22.243 -33.925  0.50 33.05           C  
ANISOU 4304  C  ALYS E 361     3600   5660   3290    100   1070   -580       C  
ATOM   4305  C  BLYS E 361     -25.505  22.241 -33.913  0.50 33.07           C  
ANISOU 4305  C  BLYS E 361     3610   5670   3290    100   1070   -580       C  
ATOM   4306  O  ALYS E 361     -26.131  22.993 -33.155  0.50 34.85           O  
ANISOU 4306  O  ALYS E 361     3730   6020   3490     90   1210   -800       O  
ATOM   4307  O  BLYS E 361     -26.147  22.988 -33.154  0.50 34.87           O  
ANISOU 4307  O  BLYS E 361     3730   6030   3490     90   1210   -800       O  
ATOM   4308  CB ALYS E 361     -24.789  23.668 -35.848  0.50 30.44           C  
ANISOU 4308  CB ALYS E 361     3310   4940   3320    450    910   -590       C  
ATOM   4309  CB BLYS E 361     -24.706  23.777 -35.749  0.50 30.53           C  
ANISOU 4309  CB BLYS E 361     3330   4950   3320    450    920   -610       C  
ATOM   4310  CG ALYS E 361     -23.707  24.423 -36.608  0.50 29.12           C  
ANISOU 4310  CG ALYS E 361     3260   4550   3260    580    800   -550       C  
ATOM   4311  CG BLYS E 361     -23.571  24.553 -36.408  0.50 29.28           C  
ANISOU 4311  CG BLYS E 361     3290   4570   3260    570    810   -570       C  
ATOM   4312  CD ALYS E 361     -24.219  25.126 -37.850  0.50 29.08           C  
ANISOU 4312  CD ALYS E 361     3190   4390   3470    760    740   -560       C  
ATOM   4313  CD BLYS E 361     -24.029  25.509 -37.490  0.50 29.49           C  
ANISOU 4313  CD BLYS E 361     3250   4440   3520    760    770   -620       C  
ATOM   4314  CE ALYS E 361     -25.282  26.166 -37.575  0.50 31.05           C  
ANISOU 4314  CE ALYS E 361     3280   4660   3860    880    830   -770       C  
ATOM   4315  CE BLYS E 361     -22.883  26.249 -38.149  0.50 28.44           C  
ANISOU 4315  CE BLYS E 361     3250   4100   3460    840    670   -570       C  
ATOM   4316  NZ ALYS E 361     -25.768  26.783 -38.832  0.50 31.14           N  
ANISOU 4316  NZ ALYS E 361     3230   4500   4100   1050    730   -740       N  
ATOM   4317  NZ BLYS E 361     -22.120  27.058 -37.169  0.50 29.28           N  
ANISOU 4317  NZ BLYS E 361     3420   4200   3510    810    720   -700       N  
ATOM   4318  N   THR E 362     -25.817  20.961 -34.140  1.00 33.53           N  
ANISOU 4318  N   THR E 362     3670   5770   3300    -10   1020   -410       N  
ATOM   4319  CA  THR E 362     -27.001  20.351 -33.471  1.00 36.84           C  
ANISOU 4319  CA  THR E 362     3960   6420   3610   -170   1140   -450       C  
ATOM   4320  C   THR E 362     -26.589  19.297 -32.437  1.00 38.78           C  
ANISOU 4320  C   THR E 362     4320   6810   3610   -430   1130   -300       C  
ATOM   4321  O   THR E 362     -27.506  18.682 -31.868  1.00 40.53           O  
ANISOU 4321  O   THR E 362     4460   7230   3710   -600   1230   -300       O  
ATOM   4322  CB  THR E 362     -27.978  19.769 -34.499  1.00 37.06           C  
ANISOU 4322  CB  THR E 362     3880   6420   3780   -110   1110   -400       C  
ATOM   4323  OG1 THR E 362     -27.311  18.730 -35.212  1.00 36.71           O  
ANISOU 4323  OG1 THR E 362     3950   6230   3760   -140    960   -170       O  
ATOM   4324  CG2 THR E 362     -28.491  20.814 -35.465  1.00 37.13           C  
ANISOU 4324  CG2 THR E 362     3770   6310   4030    130   1100   -540       C  
ATOM   4325  N   PHE E 363     -25.291  19.110 -32.168  1.00 39.51           N  
ANISOU 4325  N   PHE E 363     4580   6810   3620   -470   1020   -160       N  
ATOM   4326  CA  PHE E 363     -24.941  18.078 -31.156  1.00 42.30           C  
ANISOU 4326  CA  PHE E 363     5030   7290   3750   -730    980     20       C  
ATOM   4327  C   PHE E 363     -25.497  18.506 -29.799  1.00 46.91           C  
ANISOU 4327  C   PHE E 363     5560   8170   4100   -910   1150   -140       C  
ATOM   4328  O   PHE E 363     -25.452  19.688 -29.462  1.00 47.77           O  
ANISOU 4328  O   PHE E 363     5630   8320   4200   -840   1250   -370       O  
ATOM   4329  CB  PHE E 363     -23.435  17.830 -31.009  1.00 41.17           C  
ANISOU 4329  CB  PHE E 363     5050   7010   3580   -750    820    190       C  
ATOM   4330  CG  PHE E 363     -22.671  17.496 -32.266  1.00 38.45           C  
ANISOU 4330  CG  PHE E 363     4760   6390   3460   -580    670    310       C  
ATOM   4331  CD1 PHE E 363     -23.250  16.754 -33.286  1.00 37.54           C  
ANISOU 4331  CD1 PHE E 363     4590   6180   3490   -520    630    380       C  
ATOM   4332  CD2 PHE E 363     -21.307  17.745 -32.334  1.00 37.60           C  
ANISOU 4332  CD2 PHE E 363     4760   6140   3380   -520    550    370       C  
ATOM   4333  CE1 PHE E 363     -22.521  16.417 -34.418  1.00 35.93           C  
ANISOU 4333  CE1 PHE E 363     4440   5740   3470   -390    510    470       C  
ATOM   4334  CE2 PHE E 363     -20.569  17.374 -33.449  1.00 35.58           C  
ANISOU 4334  CE2 PHE E 363     4540   5660   3320   -380    430    470       C  
ATOM   4335  CZ  PHE E 363     -21.178  16.712 -34.491  1.00 34.75           C  
ANISOU 4335  CZ  PHE E 363     4380   5460   3360   -320    410    510       C  
ATOM   4336  N   PRO E 364     -26.058  17.574 -28.990  1.00 51.03           N  
ANISOU 4336  N   PRO E 364     6080   8890   4410  -1180   1200    -30       N  
ATOM   4337  CA  PRO E 364     -26.584  17.918 -27.670  1.00 54.89           C  
ANISOU 4337  CA  PRO E 364     6520   9700   4640  -1390   1370   -190       C  
ATOM   4338  C   PRO E 364     -25.440  18.300 -26.717  1.00 57.19           C  
ANISOU 4338  C   PRO E 364     6960  10040   4720  -1500   1310   -170       C  
ATOM   4339  O   PRO E 364     -25.679  18.655 -25.562  1.00 60.77           O  
ANISOU 4339  O   PRO E 364     7400  10770   4920  -1700   1450   -300       O  
ATOM   4340  CB  PRO E 364     -27.293  16.643 -27.177  1.00 56.54           C  
ANISOU 4340  CB  PRO E 364     6730  10080   4670  -1670   1390    -10       C  
ATOM   4341  CG  PRO E 364     -27.415  15.761 -28.410  1.00 54.23           C  
ANISOU 4341  CG  PRO E 364     6430   9550   4620  -1550   1250    180       C  
ATOM   4342  CD  PRO E 364     -26.253  16.150 -29.304  1.00 51.36           C  
ANISOU 4342  CD  PRO E 364     6160   8880   4470  -1290   1090    230       C  
ATOM   4343  OXT PRO E 364     -24.259  18.255 -27.091  1.00 56.22           O  
ANISOU 4343  OXT PRO E 364     6960   9710   4690  -1400   1140    -20       O  
TER    4344      PRO E 364                                                      
ATOM   4345  N   LYS F 257     -12.062  10.076 -65.612  1.00 33.71           N  
ANISOU 4345  N   LYS F 257     4390   4260   4160   -920   -420   -330       N  
ATOM   4346  CA  LYS F 257     -11.791   9.990 -64.142  1.00 31.73           C  
ANISOU 4346  CA  LYS F 257     4100   3860   4090   -720   -360   -190       C  
ATOM   4347  C   LYS F 257     -12.053  11.343 -63.481  1.00 27.17           C  
ANISOU 4347  C   LYS F 257     3410   3430   3490   -570   -430    -20       C  
ATOM   4348  O   LYS F 257     -11.591  12.376 -63.961  1.00 26.21           O  
ANISOU 4348  O   LYS F 257     3290   3390   3280   -500   -460    -10       O  
ATOM   4349  CB  LYS F 257     -10.364   9.500 -63.883  1.00 33.30           C  
ANISOU 4349  CB  LYS F 257     4390   3870   4400   -590   -200   -250       C  
ATOM   4350  CG  LYS F 257      -9.932   9.564 -62.425  1.00 33.99           C  
ANISOU 4350  CG  LYS F 257     4390   3930   4600   -400   -160    -60       C  
ATOM   4351  CD  LYS F 257      -8.628   8.862 -62.114  1.00 36.74           C  
ANISOU 4351  CD  LYS F 257     4760   4130   5070   -280      0    -30       C  
ATOM   4352  CE  LYS F 257      -8.720   7.356 -62.244  1.00 40.06           C  
ANISOU 4352  CE  LYS F 257     5230   4270   5720   -340    160    -60       C  
ATOM   4353  NZ  LYS F 257      -7.460   6.691 -61.836  1.00 41.71           N  
ANISOU 4353  NZ  LYS F 257     5420   4330   6110   -160    340     60       N  
ATOM   4354  N   PRO F 258     -12.798  11.381 -62.351  1.00 24.66           N  
ANISOU 4354  N   PRO F 258     2980   3140   3250   -510   -440    100       N  
ATOM   4355  CA  PRO F 258     -13.091  12.640 -61.671  1.00 22.16           C  
ANISOU 4355  CA  PRO F 258     2570   2920   2930   -380   -460    210       C  
ATOM   4356  C   PRO F 258     -11.818  13.474 -61.486  1.00 19.43           C  
ANISOU 4356  C   PRO F 258     2270   2550   2560   -260   -390    150       C  
ATOM   4357  O   PRO F 258     -10.785  12.924 -61.123  1.00 17.69           O  
ANISOU 4357  O   PRO F 258     2110   2260   2350   -220   -330    110       O  
ATOM   4358  CB  PRO F 258     -13.683  12.207 -60.324  1.00 23.05           C  
ANISOU 4358  CB  PRO F 258     2580   3060   3120   -340   -420    300       C  
ATOM   4359  CG  PRO F 258     -14.295  10.850 -60.621  1.00 25.35           C  
ANISOU 4359  CG  PRO F 258     2880   3280   3470   -490   -440    300       C  
ATOM   4360  CD  PRO F 258     -13.380  10.222 -61.657  1.00 25.42           C  
ANISOU 4360  CD  PRO F 258     3040   3150   3460   -570   -410    150       C  
ATOM   4361  N   ARG F 259     -11.949  14.780 -61.719  1.00 18.49           N  
ANISOU 4361  N   ARG F 259     2110   2470   2450   -200   -400    180       N  
ATOM   4362  CA  ARG F 259     -10.835  15.758 -61.632  1.00 17.18           C  
ANISOU 4362  CA  ARG F 259     1990   2260   2280   -130   -330    120       C  
ATOM   4363  C   ARG F 259     -10.090  15.625 -60.301  1.00 15.24           C  
ANISOU 4363  C   ARG F 259     1730   2040   2020    -90   -250     50       C  
ATOM   4364  O   ARG F 259      -8.861  15.665 -60.343  1.00 14.94           O  
ANISOU 4364  O   ARG F 259     1740   2000   1940    -80   -230    -10       O  
ATOM   4365  CB  ARG F 259     -11.399  17.171 -61.811  1.00 18.36           C  
ANISOU 4365  CB  ARG F 259     2060   2390   2520    -60   -290    190       C  
ATOM   4366  CG  ARG F 259     -10.365  18.287 -61.913  1.00 18.69           C  
ANISOU 4366  CG  ARG F 259     2140   2340   2610    -20   -200    130       C  
ATOM   4367  CD  ARG F 259     -11.082  19.579 -62.266  1.00 20.46           C  
ANISOU 4367  CD  ARG F 259     2280   2480   3010     50   -130    260       C  
ATOM   4368  NE  ARG F 259     -10.202  20.703 -62.558  1.00 21.73           N  
ANISOU 4368  NE  ARG F 259     2470   2510   3280     70    -30    240       N  
ATOM   4369  CZ  ARG F 259      -9.978  21.760 -61.778  1.00 22.78           C  
ANISOU 4369  CZ  ARG F 259     2590   2480   3580    100    150    120       C  
ATOM   4370  NH1 ARG F 259     -10.595  21.898 -60.615  1.00 23.90           N  
ANISOU 4370  NH1 ARG F 259     2700   2600   3780    120    260    -10       N  
ATOM   4371  NH2 ARG F 259      -9.151  22.706 -62.192  1.00 22.92           N  
ANISOU 4371  NH2 ARG F 259     2640   2360   3710     80    240    100       N  
ATOM   4372  N   GLN F 260     -10.795  15.397 -59.184  1.00 14.14           N  
ANISOU 4372  N   GLN F 260     1510   1970   1890    -80   -230     80       N  
ATOM   4373  CA  GLN F 260     -10.096  15.344 -57.867  1.00 13.71           C  
ANISOU 4373  CA  GLN F 260     1400   2050   1760    -70   -160     30       C  
ATOM   4374  C   GLN F 260      -9.202  14.105 -57.718  1.00 13.30           C  
ANISOU 4374  C   GLN F 260     1350   2030   1670    -70   -180    120       C  
ATOM   4375  O   GLN F 260      -8.348  14.135 -56.824  1.00 13.25           O  
ANISOU 4375  O   GLN F 260     1270   2200   1570    -70   -140    130       O  
ATOM   4376  CB  GLN F 260     -11.063  15.436 -56.680  1.00 14.54           C  
ANISOU 4376  CB  GLN F 260     1390   2290   1850    -70   -110     50       C  
ATOM   4377  CG  GLN F 260     -12.067  14.293 -56.535  1.00 14.49           C  
ANISOU 4377  CG  GLN F 260     1320   2300   1890    -70   -170    210       C  
ATOM   4378  CD  GLN F 260     -13.273  14.365 -57.442  1.00 14.41           C  
ANISOU 4378  CD  GLN F 260     1310   2190   1980    -80   -220    270       C  
ATOM   4379  OE1 GLN F 260     -13.310  15.115 -58.415  1.00 14.14           O  
ANISOU 4379  OE1 GLN F 260     1320   2070   1980    -70   -240    240       O  
ATOM   4380  NE2 GLN F 260     -14.286  13.580 -57.108  1.00 14.28           N  
ANISOU 4380  NE2 GLN F 260     1210   2220   1990   -110   -250    390       N  
ATOM   4381  N   LYS F 261      -9.354  13.079 -58.559  1.00 13.39           N  
ANISOU 4381  N   LYS F 261     1430   1900   1760    -80   -210    180       N  
ATOM   4382  CA  LYS F 261      -8.511  11.857 -58.418  1.00 14.01           C  
ANISOU 4382  CA  LYS F 261     1500   1930   1890    -50   -160    280       C  
ATOM   4383  C   LYS F 261      -7.471  11.763 -59.539  1.00 13.74           C  
ANISOU 4383  C   LYS F 261     1580   1770   1870    -30   -130    200       C  
ATOM   4384  O   LYS F 261      -6.735  10.766 -59.563  1.00 14.96           O  
ANISOU 4384  O   LYS F 261     1730   1840   2120     20    -50    290       O  
ATOM   4385  CB  LYS F 261      -9.390  10.605 -58.407  1.00 15.20           C  
ANISOU 4385  CB  LYS F 261     1640   1960   2180    -80   -150    380       C  
ATOM   4386  CG  LYS F 261     -10.394  10.539 -57.265  1.00 15.70           C  
ANISOU 4386  CG  LYS F 261     1570   2170   2230    -90   -170    500       C  
ATOM   4387  CD  LYS F 261      -9.745  10.525 -55.905  1.00 16.22           C  
ANISOU 4387  CD  LYS F 261     1480   2480   2210    -30   -120    650       C  
ATOM   4388  CE  LYS F 261     -10.748  10.366 -54.788  1.00 17.28           C  
ANISOU 4388  CE  LYS F 261     1460   2800   2300    -50   -130    770       C  
ATOM   4389  NZ  LYS F 261     -10.085  10.299 -53.468  1.00 18.55           N  
ANISOU 4389  NZ  LYS F 261     1440   3290   2310    -20    -90    940       N  
ATOM   4390  N   ARG F 262      -7.387  12.771 -60.406  1.00 12.97           N  
ANISOU 4390  N   ARG F 262     1550   1670   1710    -60   -180     80       N  
ATOM   4391  CA  ARG F 262      -6.401  12.734 -61.517  1.00 13.20           C  
ANISOU 4391  CA  ARG F 262     1670   1620   1720    -60   -140     10       C  
ATOM   4392  C   ARG F 262      -4.977  12.887 -60.989  1.00 13.62           C  
ANISOU 4392  C   ARG F 262     1670   1770   1740     20    -80     70       C  
ATOM   4393  O   ARG F 262      -4.785  13.505 -59.909  1.00 13.43           O  
ANISOU 4393  O   ARG F 262     1540   1920   1650     10   -100    100       O  
ATOM   4394  CB  ARG F 262      -6.695  13.829 -62.536  1.00 13.00           C  
ANISOU 4394  CB  ARG F 262     1700   1620   1620   -110   -200    -60       C  
ATOM   4395  CG  ARG F 262      -7.978  13.598 -63.314  1.00 13.46           C  
ANISOU 4395  CG  ARG F 262     1780   1660   1670   -200   -270    -70       C  
ATOM   4396  CD  ARG F 262      -8.303  14.784 -64.183  1.00 13.77           C  
ANISOU 4396  CD  ARG F 262     1800   1780   1650   -230   -330    -40       C  
ATOM   4397  NE  ARG F 262      -9.597  14.606 -64.811  1.00 14.97           N  
ANISOU 4397  NE  ARG F 262     1910   2010   1760   -320   -420     10       N  
ATOM   4398  CZ  ARG F 262     -10.206  15.515 -65.551  1.00 15.91           C  
ANISOU 4398  CZ  ARG F 262     1950   2250   1840   -340   -480    130       C  
ATOM   4399  NH1 ARG F 262      -9.646  16.693 -65.752  1.00 15.58           N  
ANISOU 4399  NH1 ARG F 262     1890   2190   1840   -260   -450    210       N  
ATOM   4400  NH2 ARG F 262     -11.385  15.247 -66.077  1.00 17.82           N  
ANISOU 4400  NH2 ARG F 262     2110   2630   2020   -450   -570    210       N  
ATOM   4401  N   THR F 263      -4.029  12.333 -61.747  1.00 14.35           N  
ANISOU 4401  N   THR F 263     1810   1780   1860     60    -10     60       N  
ATOM   4402  CA  THR F 263      -2.582  12.379 -61.429  1.00 15.23           C  
ANISOU 4402  CA  THR F 263     1830   2000   1950    130     60    150       C  
ATOM   4403  C   THR F 263      -1.844  12.999 -62.613  1.00 14.57           C  
ANISOU 4403  C   THR F 263     1830   1900   1800    120     70     50       C  
ATOM   4404  O   THR F 263      -1.795  12.355 -63.669  1.00 14.69           O  
ANISOU 4404  O   THR F 263     1950   1780   1860    120    150    -30       O  
ATOM   4405  CB  THR F 263      -2.036  10.982 -61.117  1.00 17.51           C  
ANISOU 4405  CB  THR F 263     2050   2210   2400    250    190    320       C  
ATOM   4406  OG1 THR F 263      -2.724  10.503 -59.961  1.00 19.23           O  
ANISOU 4406  OG1 THR F 263     2160   2480   2660    260    170    470       O  
ATOM   4407  CG2 THR F 263      -0.544  10.969 -60.865  1.00 18.82           C  
ANISOU 4407  CG2 THR F 263     2080   2520   2550    350    270    480       C  
ATOM   4408  N   ALA F 264      -1.329  14.216 -62.443  1.00 14.29           N  
ANISOU 4408  N   ALA F 264     1750   2010   1670     70     20     30       N  
ATOM   4409  CA  ALA F 264      -0.582  14.863 -63.545  1.00 14.10           C  
ANISOU 4409  CA  ALA F 264     1780   1990   1590     50     40    -20       C  
ATOM   4410  C   ALA F 264       0.778  14.173 -63.710  1.00 15.22           C  
ANISOU 4410  C   ALA F 264     1860   2170   1750    140    150     70       C  
ATOM   4411  O   ALA F 264       1.401  13.822 -62.662  1.00 15.76           O  
ANISOU 4411  O   ALA F 264     1770   2380   1840    200    170    220       O  
ATOM   4412  CB  ALA F 264      -0.421  16.333 -63.267  1.00 14.00           C  
ANISOU 4412  CB  ALA F 264     1720   2060   1540    -40    -20    -50       C  
ATOM   4413  N   THR F 265       1.187  13.951 -64.967  1.00 15.46           N  
ANISOU 4413  N   THR F 265     1970   2140   1770    170    220     10       N  
ATOM   4414  CA  THR F 265       2.495  13.327 -65.324  1.00 16.99           C  
ANISOU 4414  CA  THR F 265     2110   2350   2000    280    370     80       C  
ATOM   4415  C   THR F 265       3.058  14.061 -66.543  1.00 17.40           C  
ANISOU 4415  C   THR F 265     2210   2470   1930    230    390     10       C  
ATOM   4416  O   THR F 265       2.371  14.969 -67.049  1.00 16.73           O  
ANISOU 4416  O   THR F 265     2190   2400   1760    110    280    -60       O  
ATOM   4417  CB  THR F 265       2.368  11.837 -65.661  1.00 18.33           C  
ANISOU 4417  CB  THR F 265     2340   2300   2320    380    550     40       C  
ATOM   4418  OG1 THR F 265       1.598  11.746 -66.859  1.00 18.46           O  
ANISOU 4418  OG1 THR F 265     2530   2220   2260    270    560   -190       O  
ATOM   4419  CG2 THR F 265       1.740  11.028 -64.544  1.00 18.49           C  
ANISOU 4419  CG2 THR F 265     2300   2230   2490    430    560    150       C  
ATOM   4420  N   LYS F 266       4.238  13.666 -67.015  1.00 18.95           N  
ANISOU 4420  N   LYS F 266     2350   2710   2140    320    530     60       N  
ATOM   4421  CA  LYS F 266       4.813  14.344 -68.203  1.00 20.27           C  
ANISOU 4421  CA  LYS F 266     2550   2980   2180    270    560     20       C  
ATOM   4422  C   LYS F 266       3.936  14.053 -69.436  1.00 20.97           C  
ANISOU 4422  C   LYS F 266     2800   3000   2170    190    580   -180       C  
ATOM   4423  O   LYS F 266       3.950  14.884 -70.363  1.00 21.15           O  
ANISOU 4423  O   LYS F 266     2840   3160   2030    100    520   -190       O  
ATOM   4424  CB  LYS F 266       6.272  13.921 -68.407  1.00 22.73           C  
ANISOU 4424  CB  LYS F 266     2740   3370   2530    410    730    120       C  
ATOM   4425  CG  LYS F 266       6.493  12.433 -68.620  1.00 25.39           C  
ANISOU 4425  CG  LYS F 266     3110   3520   3020    570    980     80       C  
ATOM   4426  CD  LYS F 266       7.945  12.038 -68.808  1.00 28.10           C  
ANISOU 4426  CD  LYS F 266     3300   3940   3440    740   1190    230       C  
ATOM   4427  CE  LYS F 266       8.091  10.550 -69.051  1.00 31.13           C  
ANISOU 4427  CE  LYS F 266     3720   4050   4060    920   1500    160       C  
ATOM   4428  NZ  LYS F 266       9.500  10.158 -69.279  1.00 34.28           N  
ANISOU 4428  NZ  LYS F 266     3950   4500   4570   1120   1740    330       N  
ATOM   4429  N   ALA F 267       3.154  12.962 -69.419  1.00 21.31           N  
ANISOU 4429  N   ALA F 267     2940   2870   2290    190    650   -320       N  
ATOM   4430  CA  ALA F 267       2.306  12.599 -70.586  1.00 22.31           C  
ANISOU 4430  CA  ALA F 267     3210   3000   2270     50    670   -550       C  
ATOM   4431  C   ALA F 267       0.895  13.193 -70.462  1.00 20.90           C  
ANISOU 4431  C   ALA F 267     3060   2870   2020    -90    450   -540       C  
ATOM   4432  O   ALA F 267       0.193  13.249 -71.490  1.00 22.21           O  
ANISOU 4432  O   ALA F 267     3280   3170   2000   -240    410   -650       O  
ATOM   4433  CB  ALA F 267       2.258  11.098 -70.738  1.00 24.26           C  
ANISOU 4433  CB  ALA F 267     3550   3010   2660     90    900   -750       C  
ATOM   4434  N   TYR F 268       0.499  13.582 -69.247  1.00 18.84           N  
ANISOU 4434  N   TYR F 268     2730   2540   1880    -40    330   -400       N  
ATOM   4435  CA  TYR F 268      -0.829  14.180 -68.933  1.00 17.30           C  
ANISOU 4435  CA  TYR F 268     2530   2370   1670   -130    160   -360       C  
ATOM   4436  C   TYR F 268      -0.521  15.249 -67.882  1.00 15.23           C  
ANISOU 4436  C   TYR F 268     2170   2120   1490    -70     80   -200       C  
ATOM   4437  O   TYR F 268      -0.704  15.011 -66.682  1.00 13.98           O  
ANISOU 4437  O   TYR F 268     1970   1900   1440    -30     70   -170       O  
ATOM   4438  CB  TYR F 268      -1.798  13.065 -68.521  1.00 17.38           C  
ANISOU 4438  CB  TYR F 268     2600   2240   1770   -160    180   -460       C  
ATOM   4439  CG  TYR F 268      -3.207  13.499 -68.204  1.00 16.79           C  
ANISOU 4439  CG  TYR F 268     2500   2200   1690   -250     20   -410       C  
ATOM   4440  CD1 TYR F 268      -4.039  14.000 -69.193  1.00 17.59           C  
ANISOU 4440  CD1 TYR F 268     2590   2470   1620   -380    -80   -400       C  
ATOM   4441  CD2 TYR F 268      -3.753  13.297 -66.946  1.00 16.13           C  
ANISOU 4441  CD2 TYR F 268     2370   2010   1740   -190    -20   -340       C  
ATOM   4442  CE1 TYR F 268      -5.349  14.365 -68.920  1.00 17.51           C  
ANISOU 4442  CE1 TYR F 268     2520   2510   1630   -440   -210   -310       C  
ATOM   4443  CE2 TYR F 268      -5.066  13.641 -66.662  1.00 15.60           C  
ANISOU 4443  CE2 TYR F 268     2270   1980   1680   -260   -140   -290       C  
ATOM   4444  CZ  TYR F 268      -5.868  14.182 -67.651  1.00 16.13           C  
ANISOU 4444  CZ  TYR F 268     2320   2200   1620   -370   -230   -270       C  
ATOM   4445  OH  TYR F 268      -7.162  14.536 -67.373  1.00 15.66           O  
ANISOU 4445  OH  TYR F 268     2180   2190   1580   -410   -330   -170       O  
ATOM   4446  N   ASN F 269      -0.049  16.397 -68.367  1.00 15.46           N  
ANISOU 4446  N   ASN F 269     2160   2250   1470   -100     50   -120       N  
ATOM   4447  CA  ASN F 269       0.469  17.499 -67.510  1.00 14.71           C  
ANISOU 4447  CA  ASN F 269     1980   2150   1460   -100     30    -30       C  
ATOM   4448  C   ASN F 269      -0.634  18.231 -66.733  1.00 14.10           C  
ANISOU 4448  C   ASN F 269     1880   2000   1480   -130    -40    -20       C  
ATOM   4449  O   ASN F 269      -1.838  17.973 -66.957  1.00 14.63           O  
ANISOU 4449  O   ASN F 269     1980   2030   1550   -140   -100    -20       O  
ATOM   4450  CB  ASN F 269       1.359  18.422 -68.346  1.00 15.33           C  
ANISOU 4450  CB  ASN F 269     2020   2320   1490   -130     50     50       C  
ATOM   4451  CG  ASN F 269       0.603  19.246 -69.361  1.00 15.78           C  
ANISOU 4451  CG  ASN F 269     2070   2410   1510   -190      0    160       C  
ATOM   4452  OD1 ASN F 269      -0.515  19.684 -69.101  1.00 15.34           O  
ANISOU 4452  OD1 ASN F 269     2010   2280   1540   -200    -60    200       O  
ATOM   4453  ND2 ASN F 269       1.236  19.514 -70.491  1.00 16.78           N  
ANISOU 4453  ND2 ASN F 269     2180   2680   1530   -210     40    240       N  
ATOM   4454  N   VAL F 270      -0.196  19.131 -65.851  1.00 13.34           N  
ANISOU 4454  N   VAL F 270     1720   1880   1460   -170    -30    -20       N  
ATOM   4455  CA  VAL F 270      -1.096  19.927 -64.967  1.00 13.39           C  
ANISOU 4455  CA  VAL F 270     1710   1790   1590   -200    -30    -60       C  
ATOM   4456  C   VAL F 270      -2.145  20.673 -65.799  1.00 13.79           C  
ANISOU 4456  C   VAL F 270     1770   1740   1730   -190    -50     50       C  
ATOM   4457  O   VAL F 270      -3.322  20.672 -65.387  1.00 14.10           O  
ANISOU 4457  O   VAL F 270     1790   1720   1840   -160    -60     60       O  
ATOM   4458  CB  VAL F 270      -0.255  20.878 -64.106  1.00 13.97           C  
ANISOU 4458  CB  VAL F 270     1720   1870   1720   -300     30   -140       C  
ATOM   4459  CG1 VAL F 270      -1.118  21.833 -63.295  1.00 14.82           C  
ANISOU 4459  CG1 VAL F 270     1820   1840   1970   -360     90   -240       C  
ATOM   4460  CG2 VAL F 270       0.691  20.090 -63.216  1.00 13.82           C  
ANISOU 4460  CG2 VAL F 270     1630   2050   1570   -320     20   -180       C  
ATOM   4461  N   THR F 271      -1.735  21.270 -66.921  1.00 13.95           N  
ANISOU 4461  N   THR F 271     1770   1780   1750   -200    -30    180       N  
ATOM   4462  CA  THR F 271      -2.687  22.015 -67.786  1.00 15.38           C  
ANISOU 4462  CA  THR F 271     1890   1930   2020   -180    -50    390       C  
ATOM   4463  C   THR F 271      -3.739  21.050 -68.348  1.00 15.25           C  
ANISOU 4463  C   THR F 271     1890   2060   1850   -170   -150    420       C  
ATOM   4464  O   THR F 271      -4.914  21.429 -68.386  1.00 16.14           O  
ANISOU 4464  O   THR F 271     1930   2150   2050   -140   -170    560       O  
ATOM   4465  CB  THR F 271      -1.946  22.746 -68.911  1.00 16.34           C  
ANISOU 4465  CB  THR F 271     1970   2110   2130   -200    -20    570       C  
ATOM   4466  OG1 THR F 271      -1.039  23.651 -68.278  1.00 16.76           O  
ANISOU 4466  OG1 THR F 271     2010   2010   2350   -250     90    510       O  
ATOM   4467  CG2 THR F 271      -2.872  23.486 -69.849  1.00 18.26           C  
ANISOU 4467  CG2 THR F 271     2100   2390   2450   -170    -30    880       C  
ATOM   4468  N   GLN F 272      -3.317  19.856 -68.761  1.00 14.75           N  
ANISOU 4468  N   GLN F 272     1900   2130   1580   -200   -180    300       N  
ATOM   4469  CA  GLN F 272      -4.253  18.860 -69.346  1.00 15.67           C  
ANISOU 4469  CA  GLN F 272     2030   2380   1540   -260   -260    270       C  
ATOM   4470  C   GLN F 272      -5.168  18.298 -68.256  1.00 14.75           C  
ANISOU 4470  C   GLN F 272     1930   2160   1520   -240   -290    190       C  
ATOM   4471  O   GLN F 272      -6.371  18.185 -68.495  1.00 15.94           O  
ANISOU 4471  O   GLN F 272     2030   2380   1650   -280   -360    260       O  
ATOM   4472  CB  GLN F 272      -3.463  17.742 -70.036  1.00 16.08           C  
ANISOU 4472  CB  GLN F 272     2170   2540   1400   -310   -220    100       C  
ATOM   4473  CG  GLN F 272      -2.792  18.163 -71.338  1.00 17.77           C  
ANISOU 4473  CG  GLN F 272     2360   2950   1450   -360   -200    190       C  
ATOM   4474  CD  GLN F 272      -1.878  17.096 -71.900  1.00 18.48           C  
ANISOU 4474  CD  GLN F 272     2540   3100   1380   -390   -100    -20       C  
ATOM   4475  OE1 GLN F 272      -0.980  16.593 -71.221  1.00 17.29           O  
ANISOU 4475  OE1 GLN F 272     2440   2800   1330   -300      0   -130       O  
ATOM   4476  NE2 GLN F 272      -2.049  16.797 -73.181  1.00 20.49           N  
ANISOU 4476  NE2 GLN F 272     2790   3620   1380   -520   -100    -70       N  
ATOM   4477  N   ALA F 273      -4.618  18.027 -67.078  1.00 13.82           N  
ANISOU 4477  N   ALA F 273     1850   1910   1490   -180   -230     70       N  
ATOM   4478  CA  ALA F 273      -5.415  17.423 -65.986  1.00 13.41           C  
ANISOU 4478  CA  ALA F 273     1790   1790   1510   -160   -250     10       C  
ATOM   4479  C   ALA F 273      -6.224  18.454 -65.195  1.00 13.40           C  
ANISOU 4479  C   ALA F 273     1710   1720   1660   -130   -240     80       C  
ATOM   4480  O   ALA F 273      -7.395  18.119 -64.844  1.00 12.97           O  
ANISOU 4480  O   ALA F 273     1620   1670   1630   -120   -280    110       O  
ATOM   4481  CB  ALA F 273      -4.488  16.678 -65.055  1.00 12.66           C  
ANISOU 4481  CB  ALA F 273     1720   1660   1430   -130   -190    -80       C  
ATOM   4482  N   PHE F 274      -5.677  19.658 -64.971  1.00 13.33           N  
ANISOU 4482  N   PHE F 274     1680   1630   1760   -110   -160     90       N  
ATOM   4483  CA  PHE F 274      -6.404  20.615 -64.091  1.00 14.18           C  
ANISOU 4483  CA  PHE F 274     1730   1610   2050    -80    -80     90       C  
ATOM   4484  C   PHE F 274      -6.613  22.001 -64.711  1.00 15.65           C  
ANISOU 4484  C   PHE F 274     1850   1670   2430    -40     10    250       C  
ATOM   4485  O   PHE F 274      -7.031  22.916 -63.960  1.00 16.06           O  
ANISOU 4485  O   PHE F 274     1860   1540   2700    -10    150    200       O  
ATOM   4486  CB  PHE F 274      -5.646  20.712 -62.769  1.00 13.57           C  
ANISOU 4486  CB  PHE F 274     1660   1530   1960   -120      0   -110       C  
ATOM   4487  CG  PHE F 274      -5.255  19.370 -62.207  1.00 12.36           C  
ANISOU 4487  CG  PHE F 274     1520   1530   1650   -130    -70   -170       C  
ATOM   4488  CD1 PHE F 274      -6.215  18.494 -61.722  1.00 12.16           C  
ANISOU 4488  CD1 PHE F 274     1480   1540   1600   -110   -110   -140       C  
ATOM   4489  CD2 PHE F 274      -3.922  18.990 -62.139  1.00 11.99           C  
ANISOU 4489  CD2 PHE F 274     1480   1580   1500   -160    -70   -200       C  
ATOM   4490  CE1 PHE F 274      -5.850  17.262 -61.200  1.00 11.46           C  
ANISOU 4490  CE1 PHE F 274     1390   1550   1420   -100   -140   -140       C  
ATOM   4491  CE2 PHE F 274      -3.560  17.762 -61.608  1.00 11.46           C  
ANISOU 4491  CE2 PHE F 274     1390   1620   1340   -140   -100   -180       C  
ATOM   4492  CZ  PHE F 274      -4.524  16.899 -61.143  1.00 11.29           C  
ANISOU 4492  CZ  PHE F 274     1360   1600   1330   -100   -130   -140       C  
ATOM   4493  N   GLY F 275      -6.372  22.145 -66.015  1.00 19.17           N  
ANISOU 4493  N   GLY F 275     2500   2080   2700   -150   -860    120       N  
ATOM   4494  CA  GLY F 275      -6.571  23.428 -66.715  1.00 19.95           C  
ANISOU 4494  CA  GLY F 275     2760   2170   2650    -80   -900     80       C  
ATOM   4495  C   GLY F 275      -5.428  24.406 -66.498  1.00 19.47           C  
ANISOU 4495  C   GLY F 275     2820   2230   2350   -100   -660    120       C  
ATOM   4496  O   GLY F 275      -4.579  24.152 -65.617  1.00 17.43           O  
ANISOU 4496  O   GLY F 275     2480   2070   2070   -160   -470    160       O  
ATOM   4497  N   ARG F 276      -5.411  25.483 -67.292  1.00 21.70           N  
ANISOU 4497  N   ARG F 276     3290   2480   2480    -40   -700    120       N  
ATOM   4498  CA  ARG F 276      -4.374  26.550 -67.198  1.00 22.50           C  
ANISOU 4498  CA  ARG F 276     3490   2640   2420    -70   -500    190       C  
ATOM   4499  C   ARG F 276      -4.367  27.208 -65.818  1.00 20.23           C  
ANISOU 4499  C   ARG F 276     3010   2420   2260   -140   -380    210       C  
ATOM   4500  O   ARG F 276      -5.452  27.363 -65.235  1.00 19.40           O  
ANISOU 4500  O   ARG F 276     2750   2300   2320   -120   -450    180       O  
ATOM   4501  CB  ARG F 276      -4.649  27.700 -68.178  1.00 26.54           C  
ANISOU 4501  CB  ARG F 276     4220   3060   2800    -10   -600    220       C  
ATOM   4502  CG  ARG F 276      -4.091  27.557 -69.585  1.00 31.47           C  
ANISOU 4502  CG  ARG F 276     5140   3670   3150     70   -600    250       C  
ATOM   4503  CD  ARG F 276      -2.569  27.544 -69.562  1.00 35.84           C  
ANISOU 4503  CD  ARG F 276     5720   4330   3570     20   -300    340       C  
ATOM   4504  NE  ARG F 276      -1.975  27.903 -70.847  1.00 41.95           N  
ANISOU 4504  NE  ARG F 276     6780   5100   4060    100   -200    430       N  
ATOM   4505  CZ  ARG F 276      -1.519  29.122 -71.171  1.00 46.13           C  
ANISOU 4505  CZ  ARG F 276     7420   5590   4520     60    -70    600       C  
ATOM   4506  NH1 ARG F 276      -1.014  29.341 -72.376  1.00 50.52           N  
ANISOU 4506  NH1 ARG F 276     8260   6160   4780    140     50    730       N  
ATOM   4507  NH2 ARG F 276      -1.556  30.116 -70.298  1.00 44.41           N  
ANISOU 4507  NH2 ARG F 276     7030   5320   4520    -60    -70    650       N  
ATOM   4508  N   ARG F 277      -3.175  27.563 -65.325  1.00 19.13           N  
ANISOU 4508  N   ARG F 277     2860   2340   2070   -190   -210    240       N  
ATOM   4509  CA  ARG F 277      -3.066  28.311 -64.047  1.00 18.15           C  
ANISOU 4509  CA  ARG F 277     2620   2250   2030   -210   -150    230       C  
ATOM   4510  C   ARG F 277      -3.666  29.698 -64.299  1.00 18.86           C  
ANISOU 4510  C   ARG F 277     2760   2250   2150   -160   -260    230       C  
ATOM   4511  O   ARG F 277      -3.633  30.148 -65.477  1.00 20.62           O  
ANISOU 4511  O   ARG F 277     3150   2390   2300   -160   -320    280       O  
ATOM   4512  CB  ARG F 277      -1.615  28.466 -63.579  1.00 17.85           C  
ANISOU 4512  CB  ARG F 277     2570   2230   1980   -260    -30    250       C  
ATOM   4513  CG  ARG F 277      -1.027  27.305 -62.782  1.00 17.04           C  
ANISOU 4513  CG  ARG F 277     2380   2210   1890   -280     40    230       C  
ATOM   4514  CD  ARG F 277      -0.996  25.920 -63.394  1.00 16.48           C  
ANISOU 4514  CD  ARG F 277     2320   2160   1780   -290     40    220       C  
ATOM   4515  NE  ARG F 277      -2.303  25.299 -63.497  1.00 16.51           N  
ANISOU 4515  NE  ARG F 277     2280   2150   1840   -260    -60    220       N  
ATOM   4516  CZ  ARG F 277      -2.947  24.704 -62.488  1.00 16.30           C  
ANISOU 4516  CZ  ARG F 277     2120   2160   1910   -270    -60    240       C  
ATOM   4517  NH1 ARG F 277      -2.423  24.674 -61.274  1.00 16.06           N  
ANISOU 4517  NH1 ARG F 277     2040   2200   1870   -280     30    260       N  
ATOM   4518  NH2 ARG F 277      -4.131  24.156 -62.693  1.00 16.72           N  
ANISOU 4518  NH2 ARG F 277     2090   2180   2090   -270   -150    260       N  
ATOM   4519  N   GLY F 278      -4.207  30.340 -63.263  1.00 18.05           N  
ANISOU 4519  N   GLY F 278     2550   2170   2140   -110   -280    170       N  
ATOM   4520  CA  GLY F 278      -4.809  31.675 -63.429  1.00 18.77           C  
ANISOU 4520  CA  GLY F 278     2680   2150   2300    -50   -420    130       C  
ATOM   4521  C   GLY F 278      -5.235  32.282 -62.096  1.00 19.05           C  
ANISOU 4521  C   GLY F 278     2590   2240   2410     50   -420     30       C  
ATOM   4522  O   GLY F 278      -5.111  31.651 -61.049  1.00 19.00           O  
ANISOU 4522  O   GLY F 278     2490   2360   2370     80   -290      0       O  
ATOM   4523  N   PRO F 279      -5.778  33.517 -62.107  1.00 19.98           N  
ANISOU 4523  N   PRO F 279     2720   2260   2610    130   -570    -40       N  
ATOM   4524  CA  PRO F 279      -6.173  34.201 -60.876  1.00 20.84           C  
ANISOU 4524  CA  PRO F 279     2740   2420   2760    280   -580   -180       C  
ATOM   4525  C   PRO F 279      -7.600  34.012 -60.345  1.00 21.91           C  
ANISOU 4525  C   PRO F 279     2700   2660   2970    420   -540   -270       C  
ATOM   4526  O   PRO F 279      -7.846  34.444 -59.232  1.00 22.23           O  
ANISOU 4526  O   PRO F 279     2680   2780   2980    580   -490   -380       O  
ATOM   4527  CB  PRO F 279      -6.035  35.672 -61.309  1.00 22.01           C  
ANISOU 4527  CB  PRO F 279     3000   2360   3000    310   -810   -210       C  
ATOM   4528  CG  PRO F 279      -6.471  35.672 -62.763  1.00 22.42           C  
ANISOU 4528  CG  PRO F 279     3150   2300   3070    230   -910   -110       C  
ATOM   4529  CD  PRO F 279      -5.997  34.337 -63.310  1.00 21.11           C  
ANISOU 4529  CD  PRO F 279     3010   2230   2780    110   -740     10       C  
ATOM   4530  N   GLU F 280      -8.484  33.368 -61.111  1.00 22.76           N  
ANISOU 4530  N   GLU F 280     2730   2750   3170    380   -560   -210       N  
ATOM   4531  CA  GLU F 280      -9.901  33.231 -60.665  1.00 25.23           C  
ANISOU 4531  CA  GLU F 280     2810   3130   3640    500   -510   -280       C  
ATOM   4532  C   GLU F 280      -9.977  32.339 -59.421  1.00 26.36           C  
ANISOU 4532  C   GLU F 280     2800   3490   3720    530   -230   -240       C  
ATOM   4533  O   GLU F 280      -9.130  31.453 -59.272  1.00 24.91           O  
ANISOU 4533  O   GLU F 280     2690   3370   3410    420   -120   -140       O  
ATOM   4534  CB  GLU F 280     -10.778  32.815 -61.845  1.00 25.50           C  
ANISOU 4534  CB  GLU F 280     2790   3040   3860    440   -680   -240       C  
ATOM   4535  CG  GLU F 280     -10.684  33.807 -62.998  1.00 25.68           C  
ANISOU 4535  CG  GLU F 280     3030   2850   3880    440   -970   -270       C  
ATOM   4536  CD  GLU F 280     -11.044  35.251 -62.659  1.00 27.21           C  
ANISOU 4536  CD  GLU F 280     3220   2960   4150    580  -1110   -400       C  
ATOM   4537  OE1 GLU F 280     -11.768  35.469 -61.664  1.00 27.95           O  
ANISOU 4537  OE1 GLU F 280     3100   3170   4350    730  -1010   -520       O  
ATOM   4538  OE2 GLU F 280     -10.571  36.162 -63.374  1.00 27.15           O  
ANISOU 4538  OE2 GLU F 280     3440   2780   4100    560  -1310   -380       O  
ATOM   4539  N   GLN F 281     -10.983  32.597 -58.581  1.00 30.31           N  
ANISOU 4539  N   GLN F 281     3100   4100   4310    700   -100   -310       N  
ATOM   4540  CA  GLN F 281     -11.206  31.924 -57.264  1.00 33.26           C  
ANISOU 4540  CA  GLN F 281     3350   4710   4580    790    220   -250       C  
ATOM   4541  C   GLN F 281     -11.247  30.390 -57.333  1.00 33.13           C  
ANISOU 4541  C   GLN F 281     3220   4740   4630    610    380    -40       C  
ATOM   4542  O   GLN F 281     -10.729  29.771 -56.372  1.00 34.50           O  
ANISOU 4542  O   GLN F 281     3440   5060   4610    630    590     50       O  
ATOM   4543  CB  GLN F 281     -12.444  32.516 -56.577  1.00 36.71           C  
ANISOU 4543  CB  GLN F 281     3560   5250   5140   1010    350   -350       C  
ATOM   4544  CG  GLN F 281     -12.211  33.928 -56.048  1.00 38.21           C  
ANISOU 4544  CG  GLN F 281     3900   5440   5180   1240    230   -580       C  
ATOM   4545  CD  GLN F 281     -11.148  33.965 -54.972  1.00 38.49           C  
ANISOU 4545  CD  GLN F 281     4160   5590   4870   1340    330   -620       C  
ATOM   4546  OE1 GLN F 281     -10.719  32.933 -54.459  1.00 38.65           O  
ANISOU 4546  OE1 GLN F 281     4210   5730   4740   1260    530   -460       O  
ATOM   4547  NE2 GLN F 281     -10.724  35.161 -54.597  1.00 39.19           N  
ANISOU 4547  NE2 GLN F 281     4420   5610   4860   1520    130   -830       N  
ATOM   4548  N   THR F 282     -11.822  29.781 -58.372  1.00 32.44           N  
ANISOU 4548  N   THR F 282     3000   4520   4810    480    250     30       N  
ATOM   4549  CA  THR F 282     -11.856  28.287 -58.393  1.00 31.44           C  
ANISOU 4549  CA  THR F 282     2760   4400   4780    320    350    220       C  
ATOM   4550  C   THR F 282     -10.889  27.755 -59.464  1.00 28.68           C  
ANISOU 4550  C   THR F 282     2630   3910   4360    170    140    230       C  
ATOM   4551  O   THR F 282     -11.060  26.592 -59.900  1.00 27.92           O  
ANISOU 4551  O   THR F 282     2450   3740   4420     50     90    340       O  
ATOM   4552  CB  THR F 282     -13.306  27.802 -58.526  1.00 34.62           C  
ANISOU 4552  CB  THR F 282     2800   4760   5590    310    390    300       C  
ATOM   4553  OG1 THR F 282     -13.838  28.299 -59.752  1.00 34.92           O  
ANISOU 4553  OG1 THR F 282     2830   4590   5850    310     60    180       O  
ATOM   4554  CG2 THR F 282     -14.179  28.263 -57.377  1.00 37.06           C  
ANISOU 4554  CG2 THR F 282     2880   5250   5950    490    700    310       C  
ATOM   4555  N   GLN F 283      -9.875  28.563 -59.806  1.00 26.31           N  
ANISOU 4555  N   GLN F 283     2590   3570   3830    180     20    140       N  
ATOM   4556  CA  GLN F 283      -8.839  28.238 -60.827  1.00 23.89           C  
ANISOU 4556  CA  GLN F 283     2500   3160   3410     70   -120    150       C  
ATOM   4557  C   GLN F 283      -7.501  27.984 -60.114  1.00 20.90           C  
ANISOU 4557  C   GLN F 283     2250   2870   2810     40     10    180       C  
ATOM   4558  O   GLN F 283      -7.206  28.710 -59.138  1.00 20.58           O  
ANISOU 4558  O   GLN F 283     2250   2910   2660    130     90    120       O  
ATOM   4559  CB  GLN F 283      -8.754  29.411 -61.807  1.00 25.25           C  
ANISOU 4559  CB  GLN F 283     2840   3200   3550    110   -330     60       C  
ATOM   4560  CG  GLN F 283      -7.759  29.221 -62.940  1.00 25.15           C  
ANISOU 4560  CG  GLN F 283     3060   3100   3400     20   -430     90       C  
ATOM   4561  CD  GLN F 283      -7.789  30.374 -63.918  1.00 26.74           C  
ANISOU 4561  CD  GLN F 283     3440   3160   3560     60   -610     60       C  
ATOM   4562  OE1 GLN F 283      -8.134  31.513 -63.582  1.00 25.86           O  
ANISOU 4562  OE1 GLN F 283     3310   3010   3500    130   -660      0       O  
ATOM   4563  NE2 GLN F 283      -7.390  30.086 -65.149  1.00 29.05           N  
ANISOU 4563  NE2 GLN F 283     3930   3370   3740     20   -710    100       N  
ATOM   4564  N   GLY F 284      -6.729  26.999 -60.576  1.00 17.92           N  
ANISOU 4564  N   GLY F 284     1950   2470   2390    -70    -10    230       N  
ATOM   4565  CA  GLY F 284      -5.433  26.674 -59.949  1.00 16.11           C  
ANISOU 4565  CA  GLY F 284     1820   2290   2010   -100     80    250       C  
ATOM   4566  C   GLY F 284      -4.409  27.767 -60.197  1.00 14.86           C  
ANISOU 4566  C   GLY F 284     1810   2090   1750    -90     20    170       C  
ATOM   4567  O   GLY F 284      -4.394  28.312 -61.313  1.00 14.41           O  
ANISOU 4567  O   GLY F 284     1840   1930   1710   -110    -80    160       O  
ATOM   4568  N   ASN F 285      -3.580  28.071 -59.198  1.00 14.18           N  
ANISOU 4568  N   ASN F 285     1770   2040   1580    -50     70    130       N  
ATOM   4569  CA  ASN F 285      -2.559  29.142 -59.347  1.00 13.97           C  
ANISOU 4569  CA  ASN F 285     1840   1930   1550    -50    -10     70       C  
ATOM   4570  C   ASN F 285      -1.174  28.588 -59.023  1.00 13.09           C  
ANISOU 4570  C   ASN F 285     1750   1800   1420   -100     10     80       C  
ATOM   4571  O   ASN F 285      -0.214  29.366 -59.088  1.00 13.22           O  
ANISOU 4571  O   ASN F 285     1800   1720   1500   -120    -60     40       O  
ATOM   4572  CB  ASN F 285      -2.797  30.316 -58.389  1.00 15.05           C  
ANISOU 4572  CB  ASN F 285     1990   2060   1670     90    -70    -40       C  
ATOM   4573  CG  ASN F 285      -2.566  29.955 -56.934  1.00 15.95           C  
ANISOU 4573  CG  ASN F 285     2120   2280   1660    210    -20    -80       C  
ATOM   4574  OD1 ASN F 285      -2.711  28.801 -56.542  1.00 15.56           O  
ANISOU 4574  OD1 ASN F 285     2040   2330   1540    180    100      0       O  
ATOM   4575  ND2 ASN F 285      -2.217  30.940 -56.113  1.00 17.12           N  
ANISOU 4575  ND2 ASN F 285     2350   2390   1770    350   -140   -220       N  
ATOM   4576  N   PHE F 286      -1.081  27.283 -58.767  1.00 12.30           N  
ANISOU 4576  N   PHE F 286     1620   1770   1280   -130     70    120       N  
ATOM   4577  CA  PHE F 286       0.202  26.686 -58.320  1.00 11.82           C  
ANISOU 4577  CA  PHE F 286     1580   1680   1230   -160     60    110       C  
ATOM   4578  C   PHE F 286       0.958  25.965 -59.432  1.00 11.34           C  
ANISOU 4578  C   PHE F 286     1510   1580   1230   -260     80    140       C  
ATOM   4579  O   PHE F 286       0.363  25.118 -60.129  1.00 11.66           O  
ANISOU 4579  O   PHE F 286     1540   1640   1250   -290    100    180       O  
ATOM   4580  CB  PHE F 286      -0.080  25.688 -57.197  1.00 11.74           C  
ANISOU 4580  CB  PHE F 286     1580   1760   1120   -120    100    140       C  
ATOM   4581  CG  PHE F 286       1.144  25.173 -56.486  1.00 11.66           C  
ANISOU 4581  CG  PHE F 286     1610   1710   1110   -100     30    110       C  
ATOM   4582  CD1 PHE F 286       1.666  25.863 -55.402  1.00 12.48           C  
ANISOU 4582  CD1 PHE F 286     1800   1790   1150     10    -70     10       C  
ATOM   4583  CD2 PHE F 286       1.763  24.000 -56.882  1.00 10.95           C  
ANISOU 4583  CD2 PHE F 286     1490   1590   1080   -190     10    140       C  
ATOM   4584  CE1 PHE F 286       2.779  25.392 -54.730  1.00 12.74           C  
ANISOU 4584  CE1 PHE F 286     1880   1750   1200     40   -200    -40       C  
ATOM   4585  CE2 PHE F 286       2.883  23.536 -56.211  1.00 11.28           C  
ANISOU 4585  CE2 PHE F 286     1570   1570   1150   -160    -80     90       C  
ATOM   4586  CZ  PHE F 286       3.382  24.227 -55.136  1.00 12.24           C  
ANISOU 4586  CZ  PHE F 286     1770   1660   1220    -60   -200      0       C  
ATOM   4587  N   GLY F 287       2.243  26.297 -59.560  1.00 11.73           N  
ANISOU 4587  N   GLY F 287     1540   1550   1360   -290     70    100       N  
ATOM   4588  CA  GLY F 287       3.129  25.623 -60.523  1.00 11.84           C  
ANISOU 4588  CA  GLY F 287     1520   1550   1430   -350    140    110       C  
ATOM   4589  C   GLY F 287       3.858  26.544 -61.473  1.00 12.67           C  
ANISOU 4589  C   GLY F 287     1610   1590   1620   -400    220    160       C  
ATOM   4590  O   GLY F 287       3.212  27.407 -62.098  1.00 12.81           O  
ANISOU 4590  O   GLY F 287     1690   1590   1590   -410    230    210       O  
ATOM   4591  N   ASP F 288       5.177  26.374 -61.557  1.00 13.71           N  
ANISOU 4591  N   ASP F 288     1640   1670   1900   -440    270    140       N  
ATOM   4592  CA  ASP F 288       5.962  27.143 -62.550  1.00 15.45           C  
ANISOU 4592  CA  ASP F 288     1810   1830   2230   -490    420    230       C  
ATOM   4593  C   ASP F 288       5.901  26.309 -63.836  1.00 16.30           C  
ANISOU 4593  C   ASP F 288     1990   2040   2160   -460    590    270       C  
ATOM   4594  O   ASP F 288       5.264  25.239 -63.813  1.00 14.64           O  
ANISOU 4594  O   ASP F 288     1850   1900   1820   -410    520    200       O  
ATOM   4595  CB  ASP F 288       7.385  27.438 -62.071  1.00 16.80           C  
ANISOU 4595  CB  ASP F 288     1790   1890   2710   -540    410    210       C  
ATOM   4596  CG  ASP F 288       8.275  26.223 -61.862  1.00 17.01           C  
ANISOU 4596  CG  ASP F 288     1700   1940   2820   -520    430    120       C  
ATOM   4597  OD1 ASP F 288       7.865  25.099 -62.225  1.00 15.97           O  
ANISOU 4597  OD1 ASP F 288     1650   1920   2500   -460    470     80       O  
ATOM   4598  OD2 ASP F 288       9.388  26.418 -61.345  1.00 18.48           O  
ANISOU 4598  OD2 ASP F 288     1710   2010   3300   -540    370     70       O  
ATOM   4599  N   GLN F 289       6.584  26.737 -64.893  1.00 18.29           N  
ANISOU 4599  N   GLN F 289     1860   2710   2380   -320    190    520       N  
ATOM   4600  CA  GLN F 289       6.555  25.999 -66.188  1.00 19.42           C  
ANISOU 4600  CA  GLN F 289     1960   2980   2430   -300    230    520       C  
ATOM   4601  C   GLN F 289       7.041  24.556 -66.009  1.00 18.49           C  
ANISOU 4601  C   GLN F 289     1830   2910   2290   -260    240    410       C  
ATOM   4602  O   GLN F 289       6.427  23.656 -66.596  1.00 17.97           O  
ANISOU 4602  O   GLN F 289     1780   2900   2150   -230    250    360       O  
ATOM   4603  CB  GLN F 289       7.388  26.768 -67.216  1.00 21.79           C  
ANISOU 4603  CB  GLN F 289     2200   3370   2720   -350    280    610       C  
ATOM   4604  CG  GLN F 289       6.691  28.034 -67.704  1.00 23.58           C  
ANISOU 4604  CG  GLN F 289     2440   3570   2950   -380    300    740       C  
ATOM   4605  CD  GLN F 289       7.618  29.048 -68.325  1.00 26.23           C  
ANISOU 4605  CD  GLN F 289     2710   3930   3320   -440    340    840       C  
ATOM   4606  OE1 GLN F 289       7.470  29.428 -69.486  1.00 29.55           O  
ANISOU 4606  OE1 GLN F 289     3100   4450   3680   -450    380    940       O  
ATOM   4607  NE2 GLN F 289       8.605  29.481 -67.557  1.00 27.69           N  
ANISOU 4607  NE2 GLN F 289     2870   4040   3610   -480    330    830       N  
ATOM   4608  N   GLU F 290       8.082  24.348 -65.208  1.00 18.11           N  
ANISOU 4608  N   GLU F 290     1750   2820   2300   -260    220    370       N  
ATOM   4609  CA  GLU F 290       8.635  22.980 -65.033  1.00 18.22           C  
ANISOU 4609  CA  GLU F 290     1750   2870   2310   -220    220    270       C  
ATOM   4610  C   GLU F 290       7.587  22.056 -64.382  1.00 16.75           C  
ANISOU 4610  C   GLU F 290     1630   2620   2120   -170    190    210       C  
ATOM   4611  O   GLU F 290       7.294  20.996 -64.975  1.00 16.31           O  
ANISOU 4611  O   GLU F 290     1570   2610   2010   -130    220    150       O  
ATOM   4612  CB  GLU F 290       9.944  23.057 -64.246  1.00 19.11           C  
ANISOU 4612  CB  GLU F 290     1810   2960   2500   -220    210    260       C  
ATOM   4613  CG  GLU F 290      10.691  21.744 -64.196  1.00 20.33           C  
ANISOU 4613  CG  GLU F 290     1920   3150   2650   -170    220    180       C  
ATOM   4614  CD  GLU F 290      11.999  21.804 -63.424  1.00 21.62           C  
ANISOU 4614  CD  GLU F 290     2020   3310   2880   -170    200    180       C  
ATOM   4615  OE1 GLU F 290      12.248  22.824 -62.751  1.00 23.06           O  
ANISOU 4615  OE1 GLU F 290     2200   3450   3110   -220    160    220       O  
ATOM   4616  OE2 GLU F 290      12.777  20.836 -63.510  1.00 23.76           O  
ANISOU 4616  OE2 GLU F 290     2240   3630   3160   -120    220    130       O  
ATOM   4617  N   LEU F 291       7.033  22.433 -63.228  1.00 15.52           N  
ANISOU 4617  N   LEU F 291     1530   2360   2000   -170    140    220       N  
ATOM   4618  CA  LEU F 291       6.017  21.575 -62.552  1.00 14.84           C  
ANISOU 4618  CA  LEU F 291     1510   2220   1910   -120    120    170       C  
ATOM   4619  C   LEU F 291       4.797  21.371 -63.464  1.00 14.65           C  
ANISOU 4619  C   LEU F 291     1510   2230   1820   -120    140    170       C  
ATOM   4620  O   LEU F 291       4.288  20.226 -63.521  1.00 14.07           O  
ANISOU 4620  O   LEU F 291     1460   2160   1730    -90    140    110       O  
ATOM   4621  CB  LEU F 291       5.601  22.195 -61.215  1.00 14.31           C  
ANISOU 4621  CB  LEU F 291     1490   2060   1890   -130     70    180       C  
ATOM   4622  CG  LEU F 291       4.492  21.442 -60.477  1.00 13.59           C  
ANISOU 4622  CG  LEU F 291     1460   1910   1790    -90     40    150       C  
ATOM   4623  CD1 LEU F 291       4.841  19.965 -60.321  1.00 13.76           C  
ANISOU 4623  CD1 LEU F 291     1470   1940   1820    -40     50     90       C  
ATOM   4624  CD2 LEU F 291       4.216  22.076 -59.127  1.00 13.25           C  
ANISOU 4624  CD2 LEU F 291     1460   1800   1780    -90      0    160       C  
ATOM   4625  N   ILE F 292       4.347  22.430 -64.148  1.00 15.16           N  
ANISOU 4625  N   ILE F 292     1580   2330   1850   -160    150    240       N  
ATOM   4626  CA  ILE F 292       3.176  22.318 -65.074  1.00 15.39           C  
ANISOU 4626  CA  ILE F 292     1620   2420   1810   -150    160    250       C  
ATOM   4627  C   ILE F 292       3.452  21.243 -66.130  1.00 16.13           C  
ANISOU 4627  C   ILE F 292     1680   2610   1840   -140    200    180       C  
ATOM   4628  O   ILE F 292       2.551  20.429 -66.403  1.00 16.26           O  
ANISOU 4628  O   ILE F 292     1710   2650   1810   -130    200    130       O  
ATOM   4629  CB  ILE F 292       2.866  23.677 -65.728  1.00 15.95           C  
ANISOU 4629  CB  ILE F 292     1680   2520   1860   -190    170    360       C  
ATOM   4630  CG1 ILE F 292       2.319  24.673 -64.703  1.00 15.42           C  
ANISOU 4630  CG1 ILE F 292     1670   2330   1860   -190    140    410       C  
ATOM   4631  CG2 ILE F 292       1.900  23.506 -66.900  1.00 16.25           C  
ANISOU 4631  CG2 ILE F 292     1720   2660   1800   -180    190    370       C  
ATOM   4632  CD1 ILE F 292       2.154  26.076 -65.247  1.00 16.18           C  
ANISOU 4632  CD1 ILE F 292     1750   2430   1960   -220    150    520       C  
ATOM   4633  N   ARG F 293       4.666  21.226 -66.675  1.00 17.05           N  
ANISOU 4633  N   ARG F 293     1730   2800   1950   -150    240    180       N  
ATOM   4634  CA  ARG F 293       5.043  20.259 -67.738  1.00 18.09           C  
ANISOU 4634  CA  ARG F 293     1820   3040   2020   -130    290    110       C  
ATOM   4635  C   ARG F 293       5.271  18.841 -67.189  1.00 17.91           C  
ANISOU 4635  C   ARG F 293     1810   2960   2040    -90    280      0       C  
ATOM   4636  O   ARG F 293       4.851  17.886 -67.870  1.00 18.27           O  
ANISOU 4636  O   ARG F 293     1850   3050   2040    -70    310    -90       O  
ATOM   4637  CB  ARG F 293       6.314  20.777 -68.424  1.00 19.32           C  
ANISOU 4637  CB  ARG F 293     1900   3280   2160   -150    330    150       C  
ATOM   4638  CG  ARG F 293       6.827  19.912 -69.564  1.00 20.66           C  
ANISOU 4638  CG  ARG F 293     2010   3580   2260   -140    380     80       C  
ATOM   4639  CD  ARG F 293       8.070  20.468 -70.248  1.00 21.76           C  
ANISOU 4639  CD  ARG F 293     2070   3820   2380   -160    430    130       C  
ATOM   4640  NE  ARG F 293       9.206  20.638 -69.342  1.00 22.33           N  
ANISOU 4640  NE  ARG F 293     2110   3820   2550   -160    420    140       N  
ATOM   4641  CZ  ARG F 293       9.609  21.795 -68.805  1.00 22.55           C  
ANISOU 4641  CZ  ARG F 293     2130   3790   2640   -200    400    240       C  
ATOM   4642  NH1 ARG F 293       8.989  22.929 -69.089  1.00 22.86           N  
ANISOU 4642  NH1 ARG F 293     2200   3830   2660   -240    390    340       N  
ATOM   4643  NH2 ARG F 293      10.648  21.815 -67.988  1.00 22.79           N  
ANISOU 4643  NH2 ARG F 293     2130   3770   2750   -200    380    230       N  
ATOM   4644  N   GLN F 294       5.829  18.706 -65.985  1.00 17.55           N  
ANISOU 4644  N   GLN F 294     1770   2810   2080    -70    260      0       N  
ATOM   4645  CA  GLN F 294       6.212  17.371 -65.434  1.00 17.97           C  
ANISOU 4645  CA  GLN F 294     1830   2810   2190    -20    260    -90       C  
ATOM   4646  C   GLN F 294       5.192  16.753 -64.466  1.00 16.82           C  
ANISOU 4646  C   GLN F 294     1750   2560   2080      0    220   -110       C  
ATOM   4647  O   GLN F 294       5.186  15.514 -64.374  1.00 16.62           O  
ANISOU 4647  O   GLN F 294     1730   2500   2090     40    240   -190       O  
ATOM   4648  CB  GLN F 294       7.555  17.509 -64.714  1.00 19.26           C  
ANISOU 4648  CB  GLN F 294     1950   2950   2420      0    250    -70       C  
ATOM   4649  CG  GLN F 294       8.721  17.880 -65.630  1.00 21.08           C  
ANISOU 4649  CG  GLN F 294     2090   3290   2630    -20    290    -60       C  
ATOM   4650  CD  GLN F 294       9.087  16.771 -66.588  1.00 23.17           C  
ANISOU 4650  CD  GLN F 294     2320   3630   2860     20    350   -150       C  
ATOM   4651  OE1 GLN F 294       8.694  15.620 -66.415  1.00 24.78           O  
ANISOU 4651  OE1 GLN F 294     2550   3780   3090     60    350   -230       O  
ATOM   4652  NE2 GLN F 294       9.889  17.098 -67.591  1.00 25.06           N  
ANISOU 4652  NE2 GLN F 294     2480   3980   3050      0    400   -140       N  
ATOM   4653  N   GLY F 295       4.380  17.552 -63.770  1.00 15.53           N  
ANISOU 4653  N   GLY F 295     1640   2340   1920    -20    180    -50       N  
ATOM   4654  CA  GLY F 295       3.422  16.986 -62.801  1.00 14.77           C  
ANISOU 4654  CA  GLY F 295     1600   2160   1860      0    150    -70       C  
ATOM   4655  C   GLY F 295       4.150  16.186 -61.728  1.00 14.50           C  
ANISOU 4655  C   GLY F 295     1570   2050   1890     50    140    -90       C  
ATOM   4656  O   GLY F 295       5.226  16.649 -61.285  1.00 14.35           O  
ANISOU 4656  O   GLY F 295     1510   2040   1900     50    130    -60       O  
ATOM   4657  N   THR F 296       3.624  15.006 -61.373  1.00 14.34           N  
ANISOU 4657  N   THR F 296     1570   1970   1910     80    140   -130       N  
ATOM   4658  CA  THR F 296       4.236  14.130 -60.336  1.00 14.63           C  
ANISOU 4658  CA  THR F 296     1610   1930   2020    130    130   -130       C  
ATOM   4659  C   THR F 296       5.630  13.660 -60.789  1.00 15.46           C  
ANISOU 4659  C   THR F 296     1650   2070   2150    160    160   -170       C  
ATOM   4660  O   THR F 296       6.354  13.101 -59.951  1.00 15.53           O  
ANISOU 4660  O   THR F 296     1640   2040   2220    210    150   -150       O  
ATOM   4661  CB  THR F 296       3.302  12.966 -59.965  1.00 14.65           C  
ANISOU 4661  CB  THR F 296     1660   1850   2060    150    140   -170       C  
ATOM   4662  OG1 THR F 296       2.980  12.231 -61.143  1.00 15.27           O  
ANISOU 4662  OG1 THR F 296     1720   1950   2130    140    190   -250       O  
ATOM   4663  CG2 THR F 296       2.021  13.428 -59.306  1.00 14.06           C  
ANISOU 4663  CG2 THR F 296     1640   1740   1960    120    110   -130       C  
ATOM   4664  N   ASP F 297       5.998  13.885 -62.054  1.00 16.06           N  
ANISOU 4664  N   ASP F 297     1680   2230   2190    140    200   -200       N  
ATOM   4665  CA  ASP F 297       7.353  13.487 -62.528  1.00 17.16           C  
ANISOU 4665  CA  ASP F 297     1750   2420   2350    180    240   -240       C  
ATOM   4666  C   ASP F 297       8.348  14.592 -62.146  1.00 17.08           C  
ANISOU 4666  C   ASP F 297     1700   2460   2340    160    210   -170       C  
ATOM   4667  O   ASP F 297       9.551  14.398 -62.372  1.00 17.63           O  
ANISOU 4667  O   ASP F 297     1700   2570   2430    180    230   -180       O  
ATOM   4668  CB  ASP F 297       7.352  13.170 -64.028  1.00 18.03           C  
ANISOU 4668  CB  ASP F 297     1830   2620   2410    160    300   -310       C  
ATOM   4669  CG  ASP F 297       6.556  11.921 -64.394  1.00 18.60           C  
ANISOU 4669  CG  ASP F 297     1930   2640   2500    180    320   -410       C  
ATOM   4670  OD1 ASP F 297       6.637  10.941 -63.642  1.00 19.10           O  
ANISOU 4670  OD1 ASP F 297     2010   2600   2650    230    320   -430       O  
ATOM   4671  OD2 ASP F 297       5.821  11.957 -65.400  1.00 18.85           O  
ANISOU 4671  OD2 ASP F 297     1970   2730   2460    150    350   -460       O  
ATOM   4672  N   TYR F 298       7.856  15.711 -61.592  1.00 16.77           N  
ANISOU 4672  N   TYR F 298     1690   2410   2270    110    170   -100       N  
ATOM   4673  CA  TYR F 298       8.733  16.842 -61.167  1.00 16.61           C  
ANISOU 4673  CA  TYR F 298     1630   2420   2260     80    140    -40       C  
ATOM   4674  C   TYR F 298       9.776  16.271 -60.204  1.00 16.83           C  
ANISOU 4674  C   TYR F 298     1620   2420   2350    130    120    -40       C  
ATOM   4675  O   TYR F 298       9.383  15.565 -59.252  1.00 16.36           O  
ANISOU 4675  O   TYR F 298     1600   2300   2320    180     90    -40       O  
ATOM   4676  CB  TYR F 298       7.865  17.971 -60.609  1.00 16.20           C  
ANISOU 4676  CB  TYR F 298     1640   2330   2190     30    100     10       C  
ATOM   4677  CG  TYR F 298       8.576  19.205 -60.119  1.00 16.64           C  
ANISOU 4677  CG  TYR F 298     1660   2390   2270    -10     70     60       C  
ATOM   4678  CD1 TYR F 298       9.229  20.059 -60.994  1.00 17.50           C  
ANISOU 4678  CD1 TYR F 298     1720   2570   2360    -50     90     90       C  
ATOM   4679  CD2 TYR F 298       8.483  19.593 -58.793  1.00 16.83           C  
ANISOU 4679  CD2 TYR F 298     1710   2360   2320    -10     10     70       C  
ATOM   4680  CE1 TYR F 298       9.846  21.220 -60.545  1.00 18.20           C  
ANISOU 4680  CE1 TYR F 298     1780   2650   2490   -100     70    130       C  
ATOM   4681  CE2 TYR F 298       9.092  20.749 -58.326  1.00 17.15           C  
ANISOU 4681  CE2 TYR F 298     1730   2410   2380    -50    -20    100       C  
ATOM   4682  CZ  TYR F 298       9.769  21.571 -59.207  1.00 17.84           C  
ANISOU 4682  CZ  TYR F 298     1760   2540   2470   -110     10    130       C  
ATOM   4683  OH  TYR F 298      10.352  22.716 -58.750  1.00 18.68           O  
ANISOU 4683  OH  TYR F 298     1840   2640   2620   -160    -20    150       O  
ATOM   4684  N  ALYS F 299      11.061  16.591 -60.425  0.50 17.50           N  
ANISOU 4684  N  ALYS F 299     1620   2570   2450    130    120    -30       N  
ATOM   4685  N  BLYS F 299      11.053  16.599 -60.442  0.50 17.45           N  
ANISOU 4685  N  BLYS F 299     1620   2570   2440    130    120    -40       N  
ATOM   4686  CA ALYS F 299      12.159  16.023 -59.587  0.50 18.18           C  
ANISOU 4686  CA ALYS F 299     1650   2660   2590    180    100    -30       C  
ATOM   4687  CA BLYS F 299      12.197  16.099 -59.626  0.50 18.10           C  
ANISOU 4687  CA BLYS F 299     1640   2660   2580    180    100    -30       C  
ATOM   4688  C  ALYS F 299      11.949  16.347 -58.101  0.50 17.80           C  
ANISOU 4688  C  ALYS F 299     1640   2560   2560    190     30     10       C  
ATOM   4689  C  BLYS F 299      12.004  16.388 -58.130  0.50 17.76           C  
ANISOU 4689  C  BLYS F 299     1630   2560   2550    180     30     10       C  
ATOM   4690  O  ALYS F 299      12.377  15.521 -57.277  0.50 18.11           O  
ANISOU 4690  O  ALYS F 299     1660   2580   2630    250     10     10       O  
ATOM   4691  O  BLYS F 299      12.498  15.577 -57.328  0.50 18.05           O  
ANISOU 4691  O  BLYS F 299     1650   2590   2630    250     10     10       O  
ATOM   4692  CB ALYS F 299      13.544  16.520 -60.014  0.50 19.08           C  
ANISOU 4692  CB ALYS F 299     1670   2870   2720    170    120    -20       C  
ATOM   4693  CB BLYS F 299      13.513  16.710 -60.116  0.50 18.92           C  
ANISOU 4693  CB BLYS F 299     1650   2850   2690    150    120    -20       C  
ATOM   4694  CG ALYS F 299      13.919  17.914 -59.533  0.50 19.16           C  
ANISOU 4694  CG ALYS F 299     1650   2900   2730     90     70     20       C  
ATOM   4695  CG BLYS F 299      13.898  16.374 -61.551  0.50 19.58           C  
ANISOU 4695  CG BLYS F 299     1680   3010   2750    160    190    -60       C  
ATOM   4696  CD ALYS F 299      13.036  19.012 -60.049  0.50 18.79           C  
ANISOU 4696  CD ALYS F 299     1660   2840   2640     20     80     50       C  
ATOM   4697  CD BLYS F 299      14.046  14.899 -61.821  0.50 20.07           C  
ANISOU 4697  CD BLYS F 299     1730   3050   2840    240    230   -120       C  
ATOM   4698  CE ALYS F 299      13.175  19.182 -61.540  0.50 19.21           C  
ANISOU 4698  CE ALYS F 299     1680   2960   2660    -10    150     50       C  
ATOM   4699  CE BLYS F 299      14.503  14.615 -63.237  0.50 20.88           C  
ANISOU 4699  CE BLYS F 299     1770   3240   2920    250    310   -180       C  
ATOM   4700  NZ ALYS F 299      14.553  19.570 -61.913  0.50 20.09           N  
ANISOU 4700  NZ ALYS F 299     1680   3160   2790    -30    170     60       N  
ATOM   4701  NZ BLYS F 299      14.621  13.162 -63.492  0.50 21.44           N  
ANISOU 4701  NZ BLYS F 299     1840   3280   3030    330    350   -250       N  
ATOM   4702  N   HIS F 300      11.345  17.498 -57.769  1.00 17.27           N  
ANISOU 4702  N   HIS F 300     1620   2480   2460    120      0     30       N  
ATOM   4703  CA  HIS F 300      11.118  17.852 -56.336  1.00 17.27           C  
ANISOU 4703  CA  HIS F 300     1650   2450   2470    120    -70     60       C  
ATOM   4704  C   HIS F 300       9.649  17.671 -55.949  1.00 16.09           C  
ANISOU 4704  C   HIS F 300     1590   2230   2290    130    -80     60       C  
ATOM   4705  O   HIS F 300       9.217  18.310 -54.975  1.00 15.43           O  
ANISOU 4705  O   HIS F 300     1550   2120   2190    110   -120     80       O  
ATOM   4706  CB  HIS F 300      11.637  19.255 -56.015  1.00 18.24           C  
ANISOU 4706  CB  HIS F 300     1740   2600   2590     50   -100     70       C  
ATOM   4707  CG  HIS F 300      13.123  19.311 -55.941  1.00 19.74           C  
ANISOU 4707  CG  HIS F 300     1830   2860   2810     50   -110     70       C  
ATOM   4708  ND1 HIS F 300      13.906  19.568 -57.048  1.00 21.17           N  
ANISOU 4708  ND1 HIS F 300     1940   3100   3000     20    -70     70       N  
ATOM   4709  CD2 HIS F 300      13.966  19.119 -54.904  1.00 20.52           C  
ANISOU 4709  CD2 HIS F 300     1870   3000   2930     80   -160     70       C  
ATOM   4710  CE1 HIS F 300      15.173  19.535 -56.700  1.00 21.79           C  
ANISOU 4710  CE1 HIS F 300     1930   3240   3110     30    -90     70       C  
ATOM   4711  NE2 HIS F 300      15.238  19.269 -55.385  1.00 22.13           N  
ANISOU 4711  NE2 HIS F 300     1980   3280   3160     70   -150     70       N  
ATOM   4712  N   TRP F 301       8.920  16.824 -56.675  1.00 15.47           N  
ANISOU 4712  N   TRP F 301     1550   2120   2210    150    -30     40       N  
ATOM   4713  CA  TRP F 301       7.495  16.578 -56.339  1.00 14.73           C  
ANISOU 4713  CA  TRP F 301     1540   1960   2090    150    -40     40       C  
ATOM   4714  C   TRP F 301       7.349  16.101 -54.891  1.00 14.68           C  
ANISOU 4714  C   TRP F 301     1560   1920   2100    200    -80     70       C  
ATOM   4715  O   TRP F 301       6.446  16.555 -54.190  1.00 13.64           O  
ANISOU 4715  O   TRP F 301     1480   1760   1940    180   -100     90       O  
ATOM   4716  CB  TRP F 301       6.837  15.611 -57.328  1.00 14.47           C  
ANISOU 4716  CB  TRP F 301     1530   1910   2060    170     20      0       C  
ATOM   4717  CG  TRP F 301       5.423  15.331 -56.942  1.00 13.77           C  
ANISOU 4717  CG  TRP F 301     1510   1760   1960    170     10     10       C  
ATOM   4718  CD1 TRP F 301       4.930  14.185 -56.390  1.00 13.71           C  
ANISOU 4718  CD1 TRP F 301     1530   1690   1980    210     20     10       C  
ATOM   4719  CD2 TRP F 301       4.341  16.280 -56.941  1.00 13.15           C  
ANISOU 4719  CD2 TRP F 301     1480   1680   1840    120      0     30       C  
ATOM   4720  NE1 TRP F 301       3.602  14.334 -56.109  1.00 13.25           N  
ANISOU 4720  NE1 TRP F 301     1530   1600   1900    190     10     20       N  
ATOM   4721  CE2 TRP F 301       3.207  15.605 -56.440  1.00 12.80           C  
ANISOU 4721  CE2 TRP F 301     1490   1580   1800    140      0     30       C  
ATOM   4722  CE3 TRP F 301       4.210  17.615 -57.348  1.00 12.84           C  
ANISOU 4722  CE3 TRP F 301     1440   1670   1770     70    -10     50       C  
ATOM   4723  CZ2 TRP F 301       1.965  16.228 -56.327  1.00 12.28           C  
ANISOU 4723  CZ2 TRP F 301     1470   1500   1700    110    -10     40       C  
ATOM   4724  CZ3 TRP F 301       2.982  18.229 -57.242  1.00 12.29           C  
ANISOU 4724  CZ3 TRP F 301     1420   1580   1670     50    -20     60       C  
ATOM   4725  CH2 TRP F 301       1.876  17.542 -56.735  1.00 12.14           C  
ANISOU 4725  CH2 TRP F 301     1450   1520   1650     60    -20     60       C  
ATOM   4726  N   PRO F 302       8.201  15.172 -54.387  1.00 15.35           N  
ANISOU 4726  N   PRO F 302     1600   2010   2220    260    -80     80       N  
ATOM   4727  CA  PRO F 302       8.085  14.708 -53.003  1.00 15.53           C  
ANISOU 4727  CA  PRO F 302     1640   2010   2250    310   -130    120       C  
ATOM   4728  C   PRO F 302       8.120  15.833 -51.956  1.00 15.38           C  
ANISOU 4728  C   PRO F 302     1630   2040   2180    270   -190    140       C  
ATOM   4729  O   PRO F 302       7.400  15.721 -51.000  1.00 15.71           O  
ANISOU 4729  O   PRO F 302     1710   2060   2200    290   -210    170       O  
ATOM   4730  CB  PRO F 302       9.281  13.756 -52.828  1.00 16.47           C  
ANISOU 4730  CB  PRO F 302     1690   2150   2420    380   -120    140       C  
ATOM   4731  CG  PRO F 302       9.569  13.267 -54.232  1.00 16.59           C  
ANISOU 4731  CG  PRO F 302     1680   2160   2470    380    -60     90       C  
ATOM   4732  CD  PRO F 302       9.257  14.459 -55.120  1.00 16.09           C  
ANISOU 4732  CD  PRO F 302     1630   2130   2360    300    -50     60       C  
ATOM   4733  N   GLN F 303       8.932  16.880 -52.151  1.00 15.65           N  
ANISOU 4733  N   GLN F 303     1610   2120   2210    220   -210    120       N  
ATOM   4734  CA  GLN F 303       8.978  17.977 -51.141  1.00 15.55           C  
ANISOU 4734  CA  GLN F 303     1600   2140   2160    190   -260    120       C  
ATOM   4735  C   GLN F 303       7.708  18.836 -51.236  1.00 14.67           C  
ANISOU 4735  C   GLN F 303     1570   1980   2020    140   -250    110       C  
ATOM   4736  O   GLN F 303       7.505  19.655 -50.334  1.00 14.90           O  
ANISOU 4736  O   GLN F 303     1610   2020   2020    110   -300     90       O  
ATOM   4737  CB  GLN F 303      10.285  18.764 -51.229  1.00 16.53           C  
ANISOU 4737  CB  GLN F 303     1650   2330   2300    150   -290    100       C  
ATOM   4738  CG  GLN F 303      11.487  17.972 -50.719  1.00 17.65           C  
ANISOU 4738  CG  GLN F 303     1710   2530   2460    210   -310    120       C  
ATOM   4739  CD  GLN F 303      11.839  16.812 -51.620  1.00 18.13           C  
ANISOU 4739  CD  GLN F 303     1740   2580   2570    260   -260    130       C  
ATOM   4740  OE1 GLN F 303      11.887  16.952 -52.840  1.00 18.26           O  
ANISOU 4740  OE1 GLN F 303     1750   2590   2600    240   -210    110       O  
ATOM   4741  NE2 GLN F 303      12.153  15.672 -51.021  1.00 18.73           N  
ANISOU 4741  NE2 GLN F 303     1800   2660   2660    350   -270    170       N  
ATOM   4742  N   ILE F 304       6.897  18.657 -52.284  1.00 14.00           N  
ANISOU 4742  N   ILE F 304     1520   1860   1940    130   -210    100       N  
ATOM   4743  CA  ILE F 304       5.605  19.390 -52.425  1.00 13.46           C  
ANISOU 4743  CA  ILE F 304     1520   1750   1850     90   -200    100       C  
ATOM   4744  C   ILE F 304       4.499  18.484 -51.870  1.00 13.21           C  
ANISOU 4744  C   ILE F 304     1540   1680   1800    130   -190    120       C  
ATOM   4745  O   ILE F 304       3.716  18.952 -51.022  1.00 12.87           O  
ANISOU 4745  O   ILE F 304     1540   1620   1730    130   -210    120       O  
ATOM   4746  CB  ILE F 304       5.332  19.796 -53.886  1.00 13.39           C  
ANISOU 4746  CB  ILE F 304     1510   1730   1850     50   -150     90       C  
ATOM   4747  CG1 ILE F 304       6.339  20.842 -54.369  1.00 13.86           C  
ANISOU 4747  CG1 ILE F 304     1510   1820   1930      0   -150     90       C  
ATOM   4748  CG2 ILE F 304       3.900  20.284 -54.047  1.00 13.03           C  
ANISOU 4748  CG2 ILE F 304     1520   1650   1780     30   -140    100       C  
ATOM   4749  CD1 ILE F 304       6.231  21.153 -55.826  1.00 14.09           C  
ANISOU 4749  CD1 ILE F 304     1530   1860   1960    -30   -110    100       C  
ATOM   4750  N   ALA F 305       4.460  17.228 -52.327  1.00 13.09           N  
ANISOU 4750  N   ALA F 305     1520   1640   1810    170   -160    120       N  
ATOM   4751  CA  ALA F 305       3.439  16.249 -51.881  1.00 12.99           C  
ANISOU 4751  CA  ALA F 305     1550   1590   1790    200   -140    140       C  
ATOM   4752  C   ALA F 305       3.423  16.095 -50.349  1.00 13.12           C  
ANISOU 4752  C   ALA F 305     1580   1620   1790    240   -180    180       C  
ATOM   4753  O   ALA F 305       2.335  15.812 -49.829  1.00 13.00           O  
ANISOU 4753  O   ALA F 305     1610   1570   1750    240   -170    200       O  
ATOM   4754  CB  ALA F 305       3.679  14.922 -52.551  1.00 13.44           C  
ANISOU 4754  CB  ALA F 305     1590   1610   1900    240   -100    140       C  
ATOM   4755  N   GLN F 306       4.556  16.288 -49.658  1.00 13.29           N  
ANISOU 4755  N   GLN F 306     1560   1690   1800    260   -220    190       N  
ATOM   4756  CA  GLN F 306       4.589  16.133 -48.173  1.00 13.94           C  
ANISOU 4756  CA  GLN F 306     1640   1810   1840    290   -260    230       C  
ATOM   4757  C   GLN F 306       3.551  17.051 -47.503  1.00 13.76           C  
ANISOU 4757  C   GLN F 306     1670   1800   1760    260   -280    210       C  
ATOM   4758  O   GLN F 306       3.201  16.784 -46.329  1.00 14.49           O  
ANISOU 4758  O   GLN F 306     1780   1920   1810    290   -300    250       O  
ATOM   4759  CB  GLN F 306       5.979  16.427 -47.593  1.00 14.60           C  
ANISOU 4759  CB  GLN F 306     1660   1970   1920    300   -310    230       C  
ATOM   4760  CG  GLN F 306       6.458  17.857 -47.810  1.00 14.56           C  
ANISOU 4760  CG  GLN F 306     1630   2000   1900    240   -340    170       C  
ATOM   4761  CD  GLN F 306       7.806  18.114 -47.182  1.00 15.40           C  
ANISOU 4761  CD  GLN F 306     1660   2190   2000    240   -390    160       C  
ATOM   4762  OE1 GLN F 306       8.093  17.644 -46.085  1.00 15.95           O  
ANISOU 4762  OE1 GLN F 306     1710   2320   2030    290   -430    200       O  
ATOM   4763  NE2 GLN F 306       8.636  18.893 -47.863  1.00 15.55           N  
ANISOU 4763  NE2 GLN F 306     1630   2230   2050    190   -400    120       N  
ATOM   4764  N   PHE F 307       3.070  18.079 -48.206  1.00 13.11           N  
ANISOU 4764  N   PHE F 307     1610   1690   1680    200   -270    170       N  
ATOM   4765  CA  PHE F 307       2.076  18.998 -47.598  1.00 13.13           C  
ANISOU 4765  CA  PHE F 307     1650   1690   1640    180   -280    150       C  
ATOM   4766  C   PHE F 307       0.663  18.643 -48.060  1.00 12.56           C  
ANISOU 4766  C   PHE F 307     1630   1570   1570    180   -240    160       C  
ATOM   4767  O   PHE F 307      -0.271  19.246 -47.513  1.00 12.70           O  
ANISOU 4767  O   PHE F 307     1690   1590   1550    170   -240    150       O  
ATOM   4768  CB  PHE F 307       2.399  20.454 -47.925  1.00 13.47           C  
ANISOU 4768  CB  PHE F 307     1690   1730   1700    130   -290    100       C  
ATOM   4769  CG  PHE F 307       3.754  20.889 -47.440  1.00 14.39           C  
ANISOU 4769  CG  PHE F 307     1750   1910   1810    110   -340     70       C  
ATOM   4770  CD1 PHE F 307       3.981  21.098 -46.092  1.00 15.10           C  
ANISOU 4770  CD1 PHE F 307     1830   2060   1850    130   -390     50       C  
ATOM   4771  CD2 PHE F 307       4.792  21.100 -48.330  1.00 14.84           C  
ANISOU 4771  CD2 PHE F 307     1760   1960   1920     90   -330     60       C  
ATOM   4772  CE1 PHE F 307       5.231  21.498 -45.643  1.00 16.15           C  
ANISOU 4772  CE1 PHE F 307     1900   2250   1980    110   -430     20       C  
ATOM   4773  CE2 PHE F 307       6.037  21.508 -47.879  1.00 15.67           C  
ANISOU 4773  CE2 PHE F 307     1800   2130   2030     70   -380     40       C  
ATOM   4774  CZ  PHE F 307       6.255  21.696 -46.536  1.00 16.23           C  
ANISOU 4774  CZ  PHE F 307     1860   2260   2050     80   -430     20       C  
ATOM   4775  N   ALA F 308       0.517  17.728 -49.027  1.00 12.19           N  
ANISOU 4775  N   ALA F 308     1580   1480   1570    190   -200    180       N  
ATOM   4776  CA  ALA F 308      -0.836  17.347 -49.500  1.00 11.72           C  
ANISOU 4776  CA  ALA F 308     1560   1380   1510    180   -160    180       C  
ATOM   4777  C   ALA F 308      -1.529  16.535 -48.412  1.00 11.94           C  
ANISOU 4777  C   ALA F 308     1610   1410   1510    210   -160    230       C  
ATOM   4778  O   ALA F 308      -0.907  15.690 -47.771  1.00 12.35           O  
ANISOU 4778  O   ALA F 308     1650   1470   1570    250   -160    270       O  
ATOM   4779  CB  ALA F 308      -0.767  16.570 -50.787  1.00 11.72           C  
ANISOU 4779  CB  ALA F 308     1550   1350   1550    170   -120    170       C  
ATOM   4780  N   PRO F 309      -2.832  16.773 -48.157  1.00 11.48           N  
ANISOU 4780  N   PRO F 309     1590   1340   1430    200   -140    230       N  
ATOM   4781  CA  PRO F 309      -3.538  16.022 -47.129  1.00 11.58           C  
ANISOU 4781  CA  PRO F 309     1620   1360   1420    230   -130    280       C  
ATOM   4782  C   PRO F 309      -4.112  14.656 -47.518  1.00 11.66           C  
ANISOU 4782  C   PRO F 309     1640   1310   1480    230    -90    320       C  
ATOM   4783  O   PRO F 309      -4.494  14.440 -48.667  1.00 11.22           O  
ANISOU 4783  O   PRO F 309     1580   1220   1460    200    -60    280       O  
ATOM   4784  CB  PRO F 309      -4.735  16.924 -46.808  1.00 11.36           C  
ANISOU 4784  CB  PRO F 309     1620   1350   1350    210   -130    270       C  
ATOM   4785  CG  PRO F 309      -5.013  17.657 -48.101  1.00 11.15           C  
ANISOU 4785  CG  PRO F 309     1590   1300   1350    170   -110    220       C  
ATOM   4786  CD  PRO F 309      -3.666  17.808 -48.783  1.00 11.02           C  
ANISOU 4786  CD  PRO F 309     1550   1280   1360    170   -130    200       C  
ATOM   4787  N   SER F 310      -4.122  13.751 -46.544  1.00 12.04           N  
ANISOU 4787  N   SER F 310     1690   1360   1530    270    -80    380       N  
ATOM   4788  CA  SER F 310      -4.773  12.437 -46.743  1.00 12.19           C  
ANISOU 4788  CA  SER F 310     1720   1310   1610    270    -40    420       C  
ATOM   4789  C   SER F 310      -6.267  12.739 -46.894  1.00 11.75           C  
ANISOU 4789  C   SER F 310     1680   1250   1530    230    -10    410       C  
ATOM   4790  O   SER F 310      -6.658  13.873 -46.571  1.00 11.02           O  
ANISOU 4790  O   SER F 310     1600   1220   1370    220    -30    390       O  
ATOM   4791  CB  SER F 310      -4.542  11.565 -45.560  1.00 12.94           C  
ANISOU 4791  CB  SER F 310     1810   1410   1700    310    -40    510       C  
ATOM   4792  OG  SER F 310      -5.137  12.175 -44.421  1.00 13.21           O  
ANISOU 4792  OG  SER F 310     1860   1520   1650    320    -50    550       O  
ATOM   4793  N   ALA F 311      -7.078  11.779 -47.328  1.00 12.08           N  
ANISOU 4793  N   ALA F 311     1730   1240   1630    210     30    420       N  
ATOM   4794  CA  ALA F 311      -8.529  12.059 -47.449  1.00 12.07           C  
ANISOU 4794  CA  ALA F 311     1730   1250   1610    170     50    410       C  
ATOM   4795  C   ALA F 311      -9.121  12.365 -46.060  1.00 12.28           C  
ANISOU 4795  C   ALA F 311     1770   1330   1570    190     50    470       C  
ATOM   4796  O   ALA F 311      -9.978  13.252 -45.966  1.00 11.81           O  
ANISOU 4796  O   ALA F 311     1720   1320   1460    180     50    440       O  
ATOM   4797  CB  ALA F 311      -9.217  10.883 -48.095  1.00 12.54           C  
ANISOU 4797  CB  ALA F 311     1790   1230   1740    130     90    400       C  
ATOM   4798  N   SER F 312      -8.670  11.649 -45.022  1.00 12.99           N  
ANISOU 4798  N   SER F 312     1860   1420   1650    230     50    550       N  
ATOM   4799  CA  SER F 312      -9.183  11.846 -43.640  1.00 13.27           C  
ANISOU 4799  CA  SER F 312     1900   1530   1610    250     50    610       C  
ATOM   4800  C   SER F 312      -8.863  13.277 -43.180  1.00 12.98           C  
ANISOU 4800  C   SER F 312     1870   1580   1480    270     10    560       C  
ATOM   4801  O   SER F 312      -9.771  13.933 -42.607  1.00 12.64           O  
ANISOU 4801  O   SER F 312     1830   1590   1380    270     20    550       O  
ATOM   4802  CB  SER F 312      -8.610  10.805 -42.703  1.00 14.22           C  
ANISOU 4802  CB  SER F 312     2020   1640   1740    300     60    720       C  
ATOM   4803  OG  SER F 312      -9.191  10.887 -41.402  1.00 14.70           O  
ANISOU 4803  OG  SER F 312     2080   1780   1720    320     70    790       O  
ATOM   4804  N   ALA F 313      -7.636  13.738 -43.458  1.00 12.57           N  
ANISOU 4804  N   ALA F 313     1810   1530   1430    280    -30    520       N  
ATOM   4805  CA  ALA F 313      -7.186  15.097 -43.077  1.00 12.71           C  
ANISOU 4805  CA  ALA F 313     1830   1620   1380    290    -70    460       C  
ATOM   4806  C   ALA F 313      -7.940  16.134 -43.917  1.00 12.38           C  
ANISOU 4806  C   ALA F 313     1800   1560   1350    250    -70    380       C  
ATOM   4807  O   ALA F 313      -8.331  17.177 -43.360  1.00 12.35           O  
ANISOU 4807  O   ALA F 313     1800   1600   1280    260    -80    350       O  
ATOM   4808  CB  ALA F 313      -5.689  15.224 -43.251  1.00 12.78           C  
ANISOU 4808  CB  ALA F 313     1820   1630   1400    300   -120    440       C  
ATOM   4809  N   PHE F 314      -8.137  15.860 -45.210  1.00 11.82           N  
ANISOU 4809  N   PHE F 314     1720   1430   1340    220    -50    360       N  
ATOM   4810  CA  PHE F 314      -8.881  16.820 -46.062  1.00 11.61           C  
ANISOU 4810  CA  PHE F 314     1700   1390   1320    190    -40    310       C  
ATOM   4811  C   PHE F 314     -10.280  17.065 -45.460  1.00 11.73           C  
ANISOU 4811  C   PHE F 314     1720   1440   1300    200    -20    320       C  
ATOM   4812  O   PHE F 314     -10.675  18.242 -45.283  1.00 11.66           O  
ANISOU 4812  O   PHE F 314     1720   1460   1250    200    -20    280       O  
ATOM   4813  CB  PHE F 314      -8.930  16.310 -47.501  1.00 11.46           C  
ANISOU 4813  CB  PHE F 314     1670   1320   1360    160    -20    290       C  
ATOM   4814  CG  PHE F 314      -9.662  17.221 -48.450  1.00 11.12           C  
ANISOU 4814  CG  PHE F 314     1620   1290   1320    140    -20    250       C  
ATOM   4815  CD1 PHE F 314      -9.027  18.326 -48.995  1.00 11.04           C  
ANISOU 4815  CD1 PHE F 314     1610   1280   1310    130    -40    220       C  
ATOM   4816  CD2 PHE F 314     -10.980  16.972 -48.797  1.00 11.15           C  
ANISOU 4816  CD2 PHE F 314     1620   1290   1320    120     10    260       C  
ATOM   4817  CE1 PHE F 314      -9.697  19.160 -49.874  1.00 11.13           C  
ANISOU 4817  CE1 PHE F 314     1610   1300   1320    120    -40    200       C  
ATOM   4818  CE2 PHE F 314     -11.647  17.803 -49.680  1.00 11.30           C  
ANISOU 4818  CE2 PHE F 314     1620   1330   1340    100     10    240       C  
ATOM   4819  CZ  PHE F 314     -11.004  18.896 -50.218  1.00 11.06           C  
ANISOU 4819  CZ  PHE F 314     1600   1300   1310    110    -20    210       C  
ATOM   4820  N   PHE F 315     -11.006  16.000 -45.111  1.00 11.95           N  
ANISOU 4820  N   PHE F 315     1750   1460   1330    190     20    380       N  
ATOM   4821  CA  PHE F 315     -12.360  16.201 -44.529  1.00 12.29           C  
ANISOU 4821  CA  PHE F 315     1790   1550   1340    190     50    390       C  
ATOM   4822  C   PHE F 315     -12.298  16.563 -43.041  1.00 12.74           C  
ANISOU 4822  C   PHE F 315     1850   1680   1310    230     40    420       C  
ATOM   4823  O   PHE F 315     -13.308  17.066 -42.515  1.00 12.57           O  
ANISOU 4823  O   PHE F 315     1830   1700   1250    240     60    410       O  
ATOM   4824  CB  PHE F 315     -13.259  15.002 -44.832  1.00 12.71           C  
ANISOU 4824  CB  PHE F 315     1830   1570   1440    160     90    440       C  
ATOM   4825  CG  PHE F 315     -13.766  15.041 -46.247  1.00 12.37           C  
ANISOU 4825  CG  PHE F 315     1770   1490   1450    120    100    390       C  
ATOM   4826  CD1 PHE F 315     -14.833  15.863 -46.572  1.00 12.36           C  
ANISOU 4826  CD1 PHE F 315     1750   1520   1420    110    100    370       C  
ATOM   4827  CD2 PHE F 315     -13.148  14.323 -47.255  1.00 12.41           C  
ANISOU 4827  CD2 PHE F 315     1770   1440   1510    100     90    380       C  
ATOM   4828  CE1 PHE F 315     -15.285  15.946 -47.877  1.00 12.29           C  
ANISOU 4828  CE1 PHE F 315     1720   1500   1450     80    100    330       C  
ATOM   4829  CE2 PHE F 315     -13.611  14.395 -48.559  1.00 12.22           C  
ANISOU 4829  CE2 PHE F 315     1720   1400   1520     60    100    330       C  
ATOM   4830  CZ  PHE F 315     -14.674  15.209 -48.865  1.00 12.21           C  
ANISOU 4830  CZ  PHE F 315     1700   1450   1490     50    100    310       C  
ATOM   4831  N   GLY F 316     -11.150  16.375 -42.394  1.00 13.38           N  
ANISOU 4831  N   GLY F 316     1940   1780   1370    260     10    430       N  
ATOM   4832  CA  GLY F 316     -11.062  16.689 -40.958  1.00 14.23           C  
ANISOU 4832  CA  GLY F 316     2050   1980   1380    300      0    450       C  
ATOM   4833  C   GLY F 316     -10.583  18.102 -40.682  1.00 14.64           C  
ANISOU 4833  C   GLY F 316     2110   2070   1390    310    -40    360       C  
ATOM   4834  O   GLY F 316     -11.047  18.679 -39.685  1.00 15.03           O  
ANISOU 4834  O   GLY F 316     2160   2190   1360    330    -30    330       O  
ATOM   4835  N   MET F 317      -9.739  18.664 -41.556  1.00 14.71           N  
ANISOU 4835  N   MET F 317     2120   2030   1450    290    -70    300       N  
ATOM   4836  CA  MET F 317      -9.158  20.019 -41.328  1.00 15.31           C  
ANISOU 4836  CA  MET F 317     2200   2120   1500    290   -100    210       C  
ATOM   4837  C   MET F 317      -9.911  21.128 -42.071  1.00 15.01           C  
ANISOU 4837  C   MET F 317     2170   2040   1500    280    -90    150       C  
ATOM   4838  O   MET F 317      -9.905  22.269 -41.574  1.00 14.93           O  
ANISOU 4838  O   MET F 317     2160   2040   1460    290   -100     80       O  
ATOM   4839  CB  MET F 317      -7.717  20.079 -41.849  1.00 15.79           C  
ANISOU 4839  CB  MET F 317     2250   2150   1600    280   -150    190       C  
ATOM   4840  CG  MET F 317      -6.768  19.090 -41.225  1.00 16.84           C  
ANISOU 4840  CG  MET F 317     2360   2330   1710    300   -170    250       C  
ATOM   4841  SD  MET F 317      -5.096  19.273 -41.909  1.00 18.21           S  
ANISOU 4841  SD  MET F 317     2510   2470   1930    280   -210    220       S  
ATOM   4842  CE  MET F 317      -5.419  19.066 -43.659  1.00 18.05           C  
ANISOU 4842  CE  MET F 317     2500   2350   2010    250   -180    220       C  
ATOM   4843  N   SER F 318     -10.546  20.794 -43.192  1.00 14.47           N  
ANISOU 4843  N   SER F 318     2100   1910   1490    260    -60    180       N  
ATOM   4844  CA  SER F 318     -11.172  21.814 -44.069  1.00 14.21           C  
ANISOU 4844  CA  SER F 318     2060   1840   1500    250    -50    140       C  
ATOM   4845  C   SER F 318     -12.563  22.288 -43.643  1.00 15.02           C  
ANISOU 4845  C   SER F 318     2160   1970   1570    270    -20    130       C  
ATOM   4846  O   SER F 318     -13.231  21.635 -42.818  1.00 14.42           O  
ANISOU 4846  O   SER F 318     2080   1940   1450    290     10    170       O  
ATOM   4847  CB  SER F 318     -11.242  21.264 -45.469  1.00 13.50           C  
ANISOU 4847  CB  SER F 318     1960   1700   1470    220    -40    180       C  
ATOM   4848  OG  SER F 318      -9.957  20.843 -45.916  1.00 13.11           O  
ANISOU 4848  OG  SER F 318     1910   1630   1450    200    -70    180       O  
ATOM   4849  N   ARG F 319     -12.937  23.440 -44.206  1.00 15.11           N  
ANISOU 4849  N   ARG F 319     2180   1940   1620    280    -20    100       N  
ATOM   4850  CA  ARG F 319     -14.297  23.986 -44.029  1.00 15.77           C  
ANISOU 4850  CA  ARG F 319     2250   2040   1700    310     20     90       C  
ATOM   4851  C   ARG F 319     -14.983  23.564 -45.321  1.00 15.14           C  
ANISOU 4851  C   ARG F 319     2150   1940   1660    280     30    140       C  
ATOM   4852  O   ARG F 319     -14.539  23.982 -46.409  1.00 15.55           O  
ANISOU 4852  O   ARG F 319     2200   1940   1760    270     20    140       O  
ATOM   4853  CB  ARG F 319     -14.302  25.477 -43.694  1.00 16.49           C  
ANISOU 4853  CB  ARG F 319     2350   2110   1800    330     10     10       C  
ATOM   4854  CG  ARG F 319     -13.624  25.770 -42.365  1.00 17.29           C  
ANISOU 4854  CG  ARG F 319     2470   2250   1850    350      0    -50       C  
ATOM   4855  CD  ARG F 319     -13.980  27.138 -41.833  1.00 18.28           C  
ANISOU 4855  CD  ARG F 319     2610   2360   1980    380     10   -140       C  
ATOM   4856  NE  ARG F 319     -15.417  27.243 -41.631  1.00 18.16           N  
ANISOU 4856  NE  ARG F 319     2580   2370   1950    420     50   -130       N  
ATOM   4857  CZ  ARG F 319     -16.079  26.770 -40.575  1.00 19.07           C  
ANISOU 4857  CZ  ARG F 319     2680   2580   1980    450     80   -130       C  
ATOM   4858  NH1 ARG F 319     -15.440  26.125 -39.609  1.00 19.20           N  
ANISOU 4858  NH1 ARG F 319     2700   2670   1920    440     60   -130       N  
ATOM   4859  NH2 ARG F 319     -17.388  26.930 -40.494  1.00 19.05           N  
ANISOU 4859  NH2 ARG F 319     2660   2610   1970    480    130   -120       N  
ATOM   4860  N   ILE F 320     -15.922  22.641 -45.193  1.00 15.26           N  
ANISOU 4860  N   ILE F 320     2140   2000   1660    280     60    180       N  
ATOM   4861  CA  ILE F 320     -16.612  22.080 -46.380  1.00 15.33           C  
ANISOU 4861  CA  ILE F 320     2120   2000   1700    250     70    220       C  
ATOM   4862  C   ILE F 320     -17.957  22.774 -46.561  1.00 15.87           C  
ANISOU 4862  C   ILE F 320     2160   2090   1770    280    100    220       C  
ATOM   4863  O   ILE F 320     -18.604  23.110 -45.556  1.00 15.94           O  
ANISOU 4863  O   ILE F 320     2170   2140   1750    310    120    200       O  
ATOM   4864  CB  ILE F 320     -16.780  20.558 -46.219  1.00 15.18           C  
ANISOU 4864  CB  ILE F 320     2090   2000   1680    220     90    260       C  
ATOM   4865  CG1 ILE F 320     -15.457  19.866 -45.877  1.00 14.80           C  
ANISOU 4865  CG1 ILE F 320     2070   1920   1630    210     70    270       C  
ATOM   4866  CG2 ILE F 320     -17.422  19.965 -47.468  1.00 14.95           C  
ANISOU 4866  CG2 ILE F 320     2030   1960   1680    180    100    280       C  
ATOM   4867  CD1 ILE F 320     -14.420  19.955 -46.976  1.00 14.39           C  
ANISOU 4867  CD1 ILE F 320     2030   1820   1620    180     40    250       C  
ATOM   4868  N   GLY F 321     -18.344  22.956 -47.817  1.00 16.72           N  
ANISOU 4868  N   GLY F 321     2240   2190   1920    260     90    230       N  
ATOM   4869  CA  GLY F 321     -19.635  23.569 -48.158  1.00 17.59           C  
ANISOU 4869  CA  GLY F 321     2310   2340   2030    290    110    250       C  
ATOM   4870  C   GLY F 321     -20.173  22.928 -49.409  1.00 18.34           C  
ANISOU 4870  C   GLY F 321     2370   2460   2140    250    100    280       C  
ATOM   4871  O   GLY F 321     -19.380  22.277 -50.116  1.00 17.96           O  
ANISOU 4871  O   GLY F 321     2330   2390   2100    210     80    280       O  
ATOM   4872  N   MET F 322     -21.483  23.020 -49.632  1.00 19.87           N  
ANISOU 4872  N   MET F 322     2510   2710   2330    270    120    300       N  
ATOM   4873  CA  MET F 322     -22.034  22.452 -50.882  1.00 21.21           C  
ANISOU 4873  CA  MET F 322     2630   2930   2510    220    110    320       C  
ATOM   4874  C   MET F 322     -22.802  23.599 -51.539  1.00 21.25           C  
ANISOU 4874  C   MET F 322     2590   2960   2520    270    110    350       C  
ATOM   4875  O   MET F 322     -23.590  24.268 -50.834  1.00 20.55           O  
ANISOU 4875  O   MET F 322     2490   2890   2430    330    130    350       O  
ATOM   4876  CB  MET F 322     -22.936  21.241 -50.642  1.00 23.50           C  
ANISOU 4876  CB  MET F 322     2880   3270   2790    180    130    330       C  
ATOM   4877  CG  MET F 322     -22.988  20.327 -51.854  1.00 25.42           C  
ANISOU 4877  CG  MET F 322     3090   3530   3040    110    120    320       C  
ATOM   4878  SD  MET F 322     -24.025  18.867 -51.634  1.00 28.68           S  
ANISOU 4878  SD  MET F 322     3450   3990   3460     40    150    320       S  
ATOM   4879  CE  MET F 322     -25.641  19.642 -51.641  1.00 29.49           C  
ANISOU 4879  CE  MET F 322     3470   4190   3550     80    160    350       C  
ATOM   4880  N   GLU F 323     -22.545  23.837 -52.823  1.00 21.03           N  
ANISOU 4880  N   GLU F 323     2550   2950   2500    260     80    370       N  
ATOM   4881  CA  GLU F 323     -23.197  24.966 -53.534  1.00 22.13           C  
ANISOU 4881  CA  GLU F 323     2640   3120   2650    320     70    410       C  
ATOM   4882  C   GLU F 323     -23.858  24.454 -54.817  1.00 20.40           C  
ANISOU 4882  C   GLU F 323     2350   2990   2400    280     50    440       C  
ATOM   4883  O   GLU F 323     -23.187  23.758 -55.591  1.00 19.98           O  
ANISOU 4883  O   GLU F 323     2310   2950   2330    220     30    420       O  
ATOM   4884  CB  GLU F 323     -22.109  26.017 -53.748  1.00 23.87           C  
ANISOU 4884  CB  GLU F 323     2910   3250   2900    340     60    420       C  
ATOM   4885  CG  GLU F 323     -22.592  27.328 -54.311  1.00 27.62           C  
ANISOU 4885  CG  GLU F 323     3360   3730   3410    410     60    480       C  
ATOM   4886  CD  GLU F 323     -21.520  28.399 -54.247  1.00 30.02           C  
ANISOU 4886  CD  GLU F 323     3720   3930   3760    430     50    480       C  
ATOM   4887  OE1 GLU F 323     -21.687  29.440 -54.921  1.00 33.54           O  
ANISOU 4887  OE1 GLU F 323     4140   4350   4240    480     50    540       O  
ATOM   4888  OE2 GLU F 323     -20.532  28.196 -53.495  1.00 31.06           O  
ANISOU 4888  OE2 GLU F 323     3910   3990   3900    410     50    430       O  
ATOM   4889  N   VAL F 324     -25.145  24.757 -54.992  1.00 19.81           N  
ANISOU 4889  N   VAL F 324     2210   3000   2320    310     60    470       N  
ATOM   4890  CA  VAL F 324     -25.917  24.341 -56.199  1.00 19.51           C  
ANISOU 4890  CA  VAL F 324     2090   3080   2240    280     30    490       C  
ATOM   4891  C   VAL F 324     -26.083  25.595 -57.062  1.00 19.45           C  
ANISOU 4891  C   VAL F 324     2050   3100   2240    350     10    560       C  
ATOM   4892  O   VAL F 324     -26.752  26.532 -56.610  1.00 19.04           O  
ANISOU 4892  O   VAL F 324     1980   3030   2220    430     30    600       O  
ATOM   4893  CB  VAL F 324     -27.264  23.688 -55.824  1.00 20.13           C  
ANISOU 4893  CB  VAL F 324     2100   3240   2310    260     50    480       C  
ATOM   4894  CG1 VAL F 324     -28.070  23.299 -57.056  1.00 20.50           C  
ANISOU 4894  CG1 VAL F 324     2050   3420   2320    230     20    490       C  
ATOM   4895  CG2 VAL F 324     -27.065  22.477 -54.916  1.00 19.71           C  
ANISOU 4895  CG2 VAL F 324     2080   3140   2270    200     70    420       C  
ATOM   4896  N   THR F 325     -25.444  25.611 -58.236  1.00 19.39           N  
ANISOU 4896  N   THR F 325     2040   3120   2200    320    -20    590       N  
ATOM   4897  CA  THR F 325     -25.484  26.767 -59.167  1.00 19.71           C  
ANISOU 4897  CA  THR F 325     2050   3190   2240    380    -30    680       C  
ATOM   4898  C   THR F 325     -25.936  26.307 -60.549  1.00 20.03           C  
ANISOU 4898  C   THR F 325     2010   3390   2210    350    -70    700       C  
ATOM   4899  O   THR F 325     -26.173  25.118 -60.766  1.00 20.97           O  
ANISOU 4899  O   THR F 325     2100   3580   2280    270    -80    630       O  
ATOM   4900  CB  THR F 325     -24.087  27.384 -59.282  1.00 19.92           C  
ANISOU 4900  CB  THR F 325     2160   3110   2300    390    -30    690       C  
ATOM   4901  OG1 THR F 325     -23.293  26.489 -60.062  1.00 19.70           O  
ANISOU 4901  OG1 THR F 325     2140   3130   2220    310    -50    660       O  
ATOM   4902  CG2 THR F 325     -23.453  27.642 -57.932  1.00 19.61           C  
ANISOU 4902  CG2 THR F 325     2200   2930   2320    400      0    640       C  
ATOM   4903  N   PRO F 326     -26.073  27.220 -61.534  1.00 20.04           N  
ANISOU 4903  N   PRO F 326     1970   3450   2190    400    -90    800       N  
ATOM   4904  CA  PRO F 326     -26.475  26.819 -62.883  1.00 20.49           C  
ANISOU 4904  CA  PRO F 326     1950   3680   2160    370   -130    820       C  
ATOM   4905  C   PRO F 326     -25.470  25.858 -63.544  1.00 19.70           C  
ANISOU 4905  C   PRO F 326     1880   3610   2000    280   -140    750       C  
ATOM   4906  O   PRO F 326     -25.847  25.202 -64.478  1.00 20.27           O  
ANISOU 4906  O   PRO F 326     1880   3820   2000    230   -170    720       O  
ATOM   4907  CB  PRO F 326     -26.583  28.151 -63.640  1.00 21.17           C  
ANISOU 4907  CB  PRO F 326     2000   3800   2240    450   -140    960       C  
ATOM   4908  CG  PRO F 326     -26.795  29.181 -62.547  1.00 21.16           C  
ANISOU 4908  CG  PRO F 326     2040   3650   2350    540   -100   1000       C  
ATOM   4909  CD  PRO F 326     -25.952  28.677 -61.394  1.00 20.30           C  
ANISOU 4909  CD  PRO F 326     2030   3400   2290    490    -80    890       C  
ATOM   4910  N   SER F 327     -24.239  25.769 -63.026  1.00 18.96           N  
ANISOU 4910  N   SER F 327     1870   3380   1950    260   -120    710       N  
ATOM   4911  CA  SER F 327     -23.226  24.857 -63.621  1.00 18.61           C  
ANISOU 4911  CA  SER F 327     1850   3350   1860    180   -120    640       C  
ATOM   4912  C   SER F 327     -23.268  23.470 -62.957  1.00 18.35           C  
ANISOU 4912  C   SER F 327     1840   3280   1850    110   -110    520       C  
ATOM   4913  O   SER F 327     -22.588  22.575 -63.463  1.00 17.79           O  
ANISOU 4913  O   SER F 327     1780   3230   1750     40   -120    450       O  
ATOM   4914  CB  SER F 327     -21.847  25.468 -63.568  1.00 18.24           C  
ANISOU 4914  CB  SER F 327     1880   3200   1850    190   -110    670       C  
ATOM   4915  OG  SER F 327     -21.481  25.813 -62.241  1.00 17.32           O  
ANISOU 4915  OG  SER F 327     1840   2920   1820    220    -80    650       O  
ATOM   4916  N   GLY F 328     -24.028  23.303 -61.867  1.00 18.89           N  
ANISOU 4916  N   GLY F 328     1910   3300   1960    120   -100    500       N  
ATOM   4917  CA  GLY F 328     -24.131  21.993 -61.183  1.00 18.78           C  
ANISOU 4917  CA  GLY F 328     1910   3250   1970     50    -80    410       C  
ATOM   4918  C   GLY F 328     -23.977  22.090 -59.672  1.00 18.14           C  
ANISOU 4918  C   GLY F 328     1900   3040   1960     80    -50    400       C  
ATOM   4919  O   GLY F 328     -24.155  23.205 -59.120  1.00 18.31           O  
ANISOU 4919  O   GLY F 328     1930   3020   2010    150    -40    460       O  
ATOM   4920  N   THR F 329     -23.691  20.951 -59.027  1.00 18.14           N  
ANISOU 4920  N   THR F 329     1930   2980   1980     20    -30    330       N  
ATOM   4921  CA  THR F 329     -23.500  20.883 -57.553  1.00 17.70           C  
ANISOU 4921  CA  THR F 329     1930   2820   1980     40      0    330       C  
ATOM   4922  C   THR F 329     -21.996  20.846 -57.289  1.00 17.10           C  
ANISOU 4922  C   THR F 329     1930   2640   1920     40      0    310       C  
ATOM   4923  O   THR F 329     -21.307  20.006 -57.914  1.00 17.62           O  
ANISOU 4923  O   THR F 329     2010   2710   1980    -10      0    260       O  
ATOM   4924  CB  THR F 329     -24.255  19.703 -56.937  1.00 18.41           C  
ANISOU 4924  CB  THR F 329     2000   2910   2090    -10     20    290       C  
ATOM   4925  OG1 THR F 329     -25.622  19.820 -57.327  1.00 18.84           O  
ANISOU 4925  OG1 THR F 329     1960   3080   2120    -10     20    310       O  
ATOM   4926  CG2 THR F 329     -24.162  19.661 -55.426  1.00 18.33           C  
ANISOU 4926  CG2 THR F 329     2040   2820   2110     10     60    300       C  
ATOM   4927  N   TRP F 330     -21.531  21.714 -56.390  1.00 16.50           N  
ANISOU 4927  N   TRP F 330     1910   2490   1870     90     10    340       N  
ATOM   4928  CA  TRP F 330     -20.089  21.844 -56.069  1.00 16.25           C  
ANISOU 4928  CA  TRP F 330     1950   2370   1860    100     10    320       C  
ATOM   4929  C   TRP F 330     -19.806  21.652 -54.579  1.00 15.91           C  
ANISOU 4929  C   TRP F 330     1950   2250   1840    110     30    310       C  
ATOM   4930  O   TRP F 330     -20.595  22.137 -53.745  1.00 15.84           O  
ANISOU 4930  O   TRP F 330     1940   2250   1830    150     50    320       O  
ATOM   4931  CB  TRP F 330     -19.607  23.229 -56.506  1.00 16.19           C  
ANISOU 4931  CB  TRP F 330     1950   2340   1860    140      0    370       C  
ATOM   4932  CG  TRP F 330     -19.750  23.495 -57.970  1.00 16.48           C  
ANISOU 4932  CG  TRP F 330     1940   2460   1860    140    -20    400       C  
ATOM   4933  CD1 TRP F 330     -20.874  23.908 -58.626  1.00 17.14           C  
ANISOU 4933  CD1 TRP F 330     1960   2630   1920    160    -30    450       C  
ATOM   4934  CD2 TRP F 330     -18.711  23.412 -58.961  1.00 16.25           C  
ANISOU 4934  CD2 TRP F 330     1920   2440   1810    110    -30    400       C  
ATOM   4935  NE1 TRP F 330     -20.610  24.065 -59.961  1.00 17.35           N  
ANISOU 4935  NE1 TRP F 330     1950   2740   1900    150    -50    480       N  
ATOM   4936  CE2 TRP F 330     -19.292  23.773 -60.196  1.00 16.53           C  
ANISOU 4936  CE2 TRP F 330     1890   2590   1800    110    -50    450       C  
ATOM   4937  CE3 TRP F 330     -17.353  23.068 -58.925  1.00 15.81           C  
ANISOU 4937  CE3 TRP F 330     1910   2330   1770     80    -30    370       C  
ATOM   4938  CZ2 TRP F 330     -18.561  23.795 -61.382  1.00 16.65           C  
ANISOU 4938  CZ2 TRP F 330     1890   2660   1780     90    -60    460       C  
ATOM   4939  CZ3 TRP F 330     -16.631  23.085 -60.100  1.00 15.84           C  
ANISOU 4939  CZ3 TRP F 330     1890   2380   1740     60    -40    380       C  
ATOM   4940  CH2 TRP F 330     -17.231  23.447 -61.307  1.00 16.49           C  
ANISOU 4940  CH2 TRP F 330     1920   2580   1770     60    -50    420       C  
ATOM   4941  N   LEU F 331     -18.722  20.941 -54.283  1.00 15.42           N  
ANISOU 4941  N   LEU F 331     1930   2140   1790     80     30    280       N  
ATOM   4942  CA  LEU F 331     -18.257  20.735 -52.894  1.00 15.47           C  
ANISOU 4942  CA  LEU F 331     1980   2080   1810    100     50    270       C  
ATOM   4943  C   LEU F 331     -17.155  21.778 -52.706  1.00 14.87           C  
ANISOU 4943  C   LEU F 331     1950   1960   1740    130     30    270       C  
ATOM   4944  O   LEU F 331     -16.107  21.653 -53.384  1.00 14.50           O  
ANISOU 4944  O   LEU F 331     1910   1890   1700    110     10    260       O  
ATOM   4945  CB  LEU F 331     -17.742  19.301 -52.731  1.00 16.66           C  
ANISOU 4945  CB  LEU F 331     2150   2210   1970     50     50    250       C  
ATOM   4946  CG  LEU F 331     -17.380  18.876 -51.308  1.00 17.43           C  
ANISOU 4946  CG  LEU F 331     2280   2270   2080     70     70    260       C  
ATOM   4947  CD1 LEU F 331     -18.598  18.941 -50.400  1.00 18.41           C  
ANISOU 4947  CD1 LEU F 331     2390   2420   2180     90     90    280       C  
ATOM   4948  CD2 LEU F 331     -16.797  17.471 -51.290  1.00 18.01           C  
ANISOU 4948  CD2 LEU F 331     2360   2300   2180     30     80    250       C  
ATOM   4949  N   THR F 332     -17.416  22.815 -51.913  1.00 14.62           N  
ANISOU 4949  N   THR F 332     1930   1910   1710    180     30    270       N  
ATOM   4950  CA  THR F 332     -16.405  23.884 -51.693  1.00 14.72           C  
ANISOU 4950  CA  THR F 332     1980   1870   1750    200     20    260       C  
ATOM   4951  C   THR F 332     -15.492  23.474 -50.534  1.00 14.46           C  
ANISOU 4951  C   THR F 332     1980   1800   1710    200     20    230       C  
ATOM   4952  O   THR F 332     -15.971  22.772 -49.615  1.00 14.00           O  
ANISOU 4952  O   THR F 332     1930   1770   1620    200     30    230       O  
ATOM   4953  CB  THR F 332     -17.058  25.246 -51.415  1.00 15.34           C  
ANISOU 4953  CB  THR F 332     2050   1930   1850    260     30    270       C  
ATOM   4954  OG1 THR F 332     -17.806  25.144 -50.203  1.00 15.68           O  
ANISOU 4954  OG1 THR F 332     2100   1990   1870    280     50    250       O  
ATOM   4955  CG2 THR F 332     -17.953  25.719 -52.541  1.00 15.85           C  
ANISOU 4955  CG2 THR F 332     2070   2030   1920    270     30    320       C  
ATOM   4956  N   TYR F 333     -14.232  23.908 -50.579  1.00 14.25           N  
ANISOU 4956  N   TYR F 333     1980   1730   1700    190      0    210       N  
ATOM   4957  CA  TYR F 333     -13.287  23.571 -49.493  1.00 14.13           C  
ANISOU 4957  CA  TYR F 333     1990   1700   1670    190    -20    190       C  
ATOM   4958  C   TYR F 333     -12.297  24.716 -49.292  1.00 14.45           C  
ANISOU 4958  C   TYR F 333     2050   1700   1740    200    -40    150       C  
ATOM   4959  O   TYR F 333     -11.899  25.353 -50.284  1.00 14.41           O  
ANISOU 4959  O   TYR F 333     2040   1670   1770    180    -40    170       O  
ATOM   4960  CB  TYR F 333     -12.555  22.257 -49.782  1.00 13.73           C  
ANISOU 4960  CB  TYR F 333     1940   1660   1620    160    -20    190       C  
ATOM   4961  CG  TYR F 333     -11.637  22.268 -50.978  1.00 13.22           C  
ANISOU 4961  CG  TYR F 333     1870   1580   1580    130    -30    200       C  
ATOM   4962  CD1 TYR F 333     -10.323  22.691 -50.866  1.00 13.22           C  
ANISOU 4962  CD1 TYR F 333     1880   1550   1590    130    -60    180       C  
ATOM   4963  CD2 TYR F 333     -12.061  21.800 -52.211  1.00 13.19           C  
ANISOU 4963  CD2 TYR F 333     1840   1600   1580    110    -20    210       C  
ATOM   4964  CE1 TYR F 333      -9.462  22.679 -51.954  1.00 12.86           C  
ANISOU 4964  CE1 TYR F 333     1810   1500   1570    100    -60    180       C  
ATOM   4965  CE2 TYR F 333     -11.215  21.783 -53.308  1.00 13.01           C  
ANISOU 4965  CE2 TYR F 333     1800   1570   1570     80    -30    210       C  
ATOM   4966  CZ  TYR F 333      -9.909  22.222 -53.179  1.00 12.92           C  
ANISOU 4966  CZ  TYR F 333     1800   1530   1570     80    -50    200       C  
ATOM   4967  OH  TYR F 333      -9.079  22.208 -54.261  1.00 12.82           O  
ANISOU 4967  OH  TYR F 333     1770   1530   1570     60    -50    200       O  
ATOM   4968  N   THR F 334     -11.979  24.990 -48.027  1.00 14.79           N  
ANISOU 4968  N   THR F 334     2120   1740   1760    210    -40    110       N  
ATOM   4969  CA  THR F 334     -10.972  26.013 -47.646  1.00 15.38           C  
ANISOU 4969  CA  THR F 334     2210   1780   1860    210    -70     70       C  
ATOM   4970  C   THR F 334     -10.243  25.461 -46.418  1.00 14.94           C  
ANISOU 4970  C   THR F 334     2160   1760   1750    210    -90     30       C  
ATOM   4971  O   THR F 334     -10.876  24.728 -45.639  1.00 14.58           O  
ANISOU 4971  O   THR F 334     2120   1770   1650    230    -70     50       O  
ATOM   4972  CB  THR F 334     -11.558  27.397 -47.325  1.00 16.68           C  
ANISOU 4972  CB  THR F 334     2380   1900   2050    240    -50     30       C  
ATOM   4973  OG1 THR F 334     -12.253  27.313 -46.081  1.00 18.59           O  
ANISOU 4973  OG1 THR F 334     2630   2190   2240    270    -40    -10       O  
ATOM   4974  CG2 THR F 334     -12.462  27.951 -48.407  1.00 16.85           C  
ANISOU 4974  CG2 THR F 334     2390   1900   2120    250    -30     70       C  
ATOM   4975  N   GLY F 335      -8.968  25.785 -46.253  1.00 14.82           N  
ANISOU 4975  N   GLY F 335     2140   1730   1750    190   -120      0       N  
ATOM   4976  CA  GLY F 335      -8.258  25.280 -45.067  1.00 15.39           C  
ANISOU 4976  CA  GLY F 335     2220   1860   1770    200   -140    -30       C  
ATOM   4977  C   GLY F 335      -6.825  25.751 -45.032  1.00 15.85           C  
ANISOU 4977  C   GLY F 335     2270   1900   1850    170   -180    -70       C  
ATOM   4978  O   GLY F 335      -6.444  26.565 -45.897  1.00 15.68           O  
ANISOU 4978  O   GLY F 335     2240   1820   1900    140   -180    -70       O  
ATOM   4979  N   ALA F 336      -6.065  25.267 -44.051  1.00 15.91           N  
ANISOU 4979  N   ALA F 336     2260   1970   1810    170   -210    -80       N  
ATOM   4980  CA  ALA F 336      -4.648  25.661 -43.953  1.00 16.65           C  
ANISOU 4980  CA  ALA F 336     2340   2070   1920    140   -250   -120       C  
ATOM   4981  C   ALA F 336      -3.859  24.481 -43.388  1.00 17.06           C  
ANISOU 4981  C   ALA F 336     2360   2200   1920    160   -280    -90       C  
ATOM   4982  O   ALA F 336      -4.414  23.731 -42.557  1.00 17.50           O  
ANISOU 4982  O   ALA F 336     2430   2310   1910    190   -270    -50       O  
ATOM   4983  CB  ALA F 336      -4.508  26.903 -43.103  1.00 17.47           C  
ANISOU 4983  CB  ALA F 336     2440   2170   2020    130   -270   -220       C  
ATOM   4984  N   ILE F 337      -2.648  24.291 -43.898  1.00 16.82           N  
ANISOU 4984  N   ILE F 337     2300   2160   1920    130   -300    -80       N  
ATOM   4985  CA  ILE F 337      -1.732  23.214 -43.428  1.00 17.36           C  
ANISOU 4985  CA  ILE F 337     2340   2300   1960    150   -330    -40       C  
ATOM   4986  C   ILE F 337      -0.529  23.911 -42.790  1.00 18.44           C  
ANISOU 4986  C   ILE F 337     2440   2480   2080    130   -380   -100       C  
ATOM   4987  O   ILE F 337       0.140  24.708 -43.482  1.00 17.29           O  
ANISOU 4987  O   ILE F 337     2280   2290   2000     90   -390   -140       O  
ATOM   4988  CB  ILE F 337      -1.376  22.273 -44.588  1.00 17.09           C  
ANISOU 4988  CB  ILE F 337     2290   2220   1980    150   -310     30       C  
ATOM   4989  CG1 ILE F 337      -2.656  21.595 -45.093  1.00 16.73           C  
ANISOU 4989  CG1 ILE F 337     2280   2140   1940    170   -260     80       C  
ATOM   4990  CG2 ILE F 337      -0.312  21.266 -44.163  1.00 17.68           C  
ANISOU 4990  CG2 ILE F 337     2330   2350   2030    180   -330     70       C  
ATOM   4991  CD1 ILE F 337      -2.494  20.775 -46.343  1.00 16.61           C  
ANISOU 4991  CD1 ILE F 337     2250   2080   1970    160   -230    110       C  
ATOM   4992  N   LYS F 338      -0.288  23.617 -41.512  1.00 19.35           N  
ANISOU 4992  N   LYS F 338     2540   2700   2110    160   -410   -110       N  
ATOM   4993  CA  LYS F 338       0.803  24.265 -40.754  1.00 21.59           C  
ANISOU 4993  CA  LYS F 338     2790   3050   2370    130   -470   -190       C  
ATOM   4994  C   LYS F 338       2.171  23.714 -41.165  1.00 21.75           C  
ANISOU 4994  C   LYS F 338     2750   3100   2420    130   -500   -150       C  
ATOM   4995  O   LYS F 338       2.291  22.487 -41.293  1.00 21.20           O  
ANISOU 4995  O   LYS F 338     2670   3040   2340    170   -490    -60       O  
ATOM   4996  CB  LYS F 338       0.582  23.994 -39.265  1.00 23.36           C  
ANISOU 4996  CB  LYS F 338     3010   3400   2470    170   -500   -200       C  
ATOM   4997  CG  LYS F 338       1.408  24.835 -38.308  1.00 25.33           C  
ANISOU 4997  CG  LYS F 338     3220   3740   2670    150   -560   -300       C  
ATOM   4998  CD  LYS F 338       1.107  24.512 -36.857  1.00 27.18           C  
ANISOU 4998  CD  LYS F 338     3450   4110   2760    190   -580   -310       C  
ATOM   4999  CE  LYS F 338       1.661  25.540 -35.898  1.00 29.06           C  
ANISOU 4999  CE  LYS F 338     3660   4440   2940    160   -630   -450       C  
ATOM   5000  NZ  LYS F 338       3.124  25.698 -36.061  1.00 30.80           N  
ANISOU 5000  NZ  LYS F 338     3810   4700   3190    120   -690   -480       N  
ATOM   5001  N   LEU F 339       3.137  24.606 -41.401  1.00 22.67           N  
ANISOU 5001  N   LEU F 339     2830   3210   2580     70   -530   -220       N  
ATOM   5002  CA  LEU F 339       4.537  24.199 -41.698  1.00 24.42           C  
ANISOU 5002  CA  LEU F 339     2980   3470   2830     60   -560   -200       C  
ATOM   5003  C   LEU F 339       5.287  24.182 -40.364  1.00 25.95           C  
ANISOU 5003  C   LEU F 339     3130   3800   2930     80   -630   -240       C  
ATOM   5004  O   LEU F 339       4.906  24.956 -39.461  1.00 26.15           O  
ANISOU 5004  O   LEU F 339     3170   3870   2900     60   -650   -320       O  
ATOM   5005  CB  LEU F 339       5.223  25.150 -42.686  1.00 25.22           C  
ANISOU 5005  CB  LEU F 339     3060   3500   3030    -10   -560   -240       C  
ATOM   5006  CG  LEU F 339       4.921  24.935 -44.170  1.00 25.45           C  
ANISOU 5006  CG  LEU F 339     3110   3430   3140    -10   -500   -180       C  
ATOM   5007  CD1 LEU F 339       3.438  25.033 -44.482  1.00 25.11           C  
ANISOU 5007  CD1 LEU F 339     3140   3310   3090      0   -450   -170       C  
ATOM   5008  CD2 LEU F 339       5.711  25.927 -45.009  1.00 27.13           C  
ANISOU 5008  CD2 LEU F 339     3280   3590   3440    -90   -500   -220       C  
ATOM   5009  N   ASP F 340       6.284  23.309 -40.237  1.00 27.53           N  
ANISOU 5009  N   ASP F 340     3260   4080   3120    110   -660   -180       N  
ATOM   5010  CA  ASP F 340       7.070  23.228 -38.981  1.00 29.73           C  
ANISOU 5010  CA  ASP F 340     3480   4510   3300    120   -730   -200       C  
ATOM   5011  C   ASP F 340       8.210  24.246 -39.086  1.00 31.33           C  
ANISOU 5011  C   ASP F 340     3620   4740   3550     50   -780   -300       C  
ATOM   5012  O   ASP F 340       9.251  23.913 -39.693  1.00 30.36           O  
ANISOU 5012  O   ASP F 340     3430   4620   3480     40   -790   -270       O  
ATOM   5013  CB  ASP F 340       7.553  21.800 -38.736  1.00 30.44           C  
ANISOU 5013  CB  ASP F 340     3530   4670   3360    200   -740    -80       C  
ATOM   5014  CG  ASP F 340       8.220  21.623 -37.385  1.00 32.46           C  
ANISOU 5014  CG  ASP F 340     3730   5100   3500    230   -820    -80       C  
ATOM   5015  OD1 ASP F 340       8.491  22.652 -36.720  1.00 33.23           O  
ANISOU 5015  OD1 ASP F 340     3800   5270   3550    180   -870   -200       O  
ATOM   5016  OD2 ASP F 340       8.426  20.461 -36.995  1.00 34.31           O  
ANISOU 5016  OD2 ASP F 340     3940   5400   3700    310   -820     30       O  
ATOM   5017  N   ASP F 341       8.011  25.439 -38.514  1.00 32.51           N  
ANISOU 5017  N   ASP F 341     3730   5320   3300   1140    -30   -300       N  
ATOM   5018  CA  ASP F 341       9.033  26.522 -38.581  1.00 34.26           C  
ANISOU 5018  CA  ASP F 341     4230   5230   3560   1150   -200   -530       C  
ATOM   5019  C   ASP F 341      10.274  26.142 -37.763  1.00 35.69           C  
ANISOU 5019  C   ASP F 341     4420   5360   3780   1060   -250   -560       C  
ATOM   5020  O   ASP F 341      11.272  26.882 -37.868  1.00 38.32           O  
ANISOU 5020  O   ASP F 341     4940   5460   4160    940   -430   -670       O  
ATOM   5021  CB  ASP F 341       8.432  27.884 -38.216  1.00 36.86           C  
ANISOU 5021  CB  ASP F 341     4800   5550   3660   1510   -320   -700       C  
ATOM   5022  CG  ASP F 341       7.736  27.940 -36.868  1.00 39.71           C  
ANISOU 5022  CG  ASP F 341     5130   6260   3690   1940   -290   -690       C  
ATOM   5023  OD1 ASP F 341       8.021  27.075 -36.019  1.00 41.39           O  
ANISOU 5023  OD1 ASP F 341     5170   6670   3890   1910   -210   -590       O  
ATOM   5024  OD2 ASP F 341       6.885  28.834 -36.694  1.00 44.44           O  
ANISOU 5024  OD2 ASP F 341     5890   6970   4020   2360   -330   -780       O  
ATOM   5025  N   LYS F 342      10.235  25.037 -37.005  1.00 36.80           N  
ANISOU 5025  N   LYS F 342     4370   5720   3890   1070   -140   -420       N  
ATOM   5026  CA  LYS F 342      11.440  24.628 -36.231  1.00 39.05           C  
ANISOU 5026  CA  LYS F 342     4650   5990   4200    990   -180   -430       C  
ATOM   5027  C   LYS F 342      12.208  23.553 -37.017  1.00 37.25           C  
ANISOU 5027  C   LYS F 342     4330   5660   4160    740   -100   -310       C  
ATOM   5028  O   LYS F 342      13.301  23.172 -36.567  1.00 36.27           O  
ANISOU 5028  O   LYS F 342     4180   5550   4050    690   -110   -290       O  
ATOM   5029  CB  LYS F 342      11.098  24.162 -34.811  1.00 43.46           C  
ANISOU 5029  CB  LYS F 342     5110   6840   4560   1210   -120   -370       C  
ATOM   5030  CG  LYS F 342      10.485  25.223 -33.906  1.00 48.44           C  
ANISOU 5030  CG  LYS F 342     5880   7610   4910   1600   -220   -510       C  
ATOM   5031  CD  LYS F 342      10.441  24.838 -32.429  1.00 53.55           C  
ANISOU 5031  CD  LYS F 342     6440   8570   5340   1840   -180   -460       C  
ATOM   5032  CE  LYS F 342       9.713  23.540 -32.140  1.00 55.71           C  
ANISOU 5032  CE  LYS F 342     6350   9210   5600   1800     10   -150       C  
ATOM   5033  NZ  LYS F 342       8.297  23.584 -32.578  1.00 57.80           N  
ANISOU 5033  NZ  LYS F 342     6450   9750   5760   1910    110     20       N  
ATOM   5034  N   ASP F 343      11.654  23.091 -38.144  1.00 35.91           N  
ANISOU 5034  N   ASP F 343     4140   5420   4090    630    -30   -230       N  
ATOM   5035  CA  ASP F 343      12.319  22.073 -39.007  1.00 34.34           C  
ANISOU 5035  CA  ASP F 343     3950   5100   4010    500     20   -150       C  
ATOM   5036  C   ASP F 343      13.450  22.776 -39.765  1.00 33.35           C  
ANISOU 5036  C   ASP F 343     3860   4870   3950    430    -30   -210       C  
ATOM   5037  O   ASP F 343      13.215  23.805 -40.396  1.00 32.10           O  
ANISOU 5037  O   ASP F 343     3750   4620   3830    380    -90   -280       O  
ATOM   5038  CB  ASP F 343      11.285  21.410 -39.926  1.00 35.10           C  
ANISOU 5038  CB  ASP F 343     4070   5120   4150    410     50    -50       C  
ATOM   5039  CG  ASP F 343      11.829  20.370 -40.890  1.00 35.62           C  
ANISOU 5039  CG  ASP F 343     4270   5000   4270    350     50      0       C  
ATOM   5040  OD1 ASP F 343      13.065  20.309 -41.068  1.00 34.55           O  
ANISOU 5040  OD1 ASP F 343     4160   4850   4130    430     70    -30       O  
ATOM   5041  OD2 ASP F 343      11.004  19.618 -41.455  1.00 37.18           O  
ANISOU 5041  OD2 ASP F 343     4570   5090   4470    250      0    100       O  
ATOM   5042  N   PRO F 344      14.711  22.272 -39.726  1.00 33.06           N  
ANISOU 5042  N   PRO F 344     3770   4890   3900    440    -10   -130       N  
ATOM   5043  CA  PRO F 344      15.823  22.929 -40.422  1.00 32.49           C  
ANISOU 5043  CA  PRO F 344     3630   4860   3860    350    -60    -80       C  
ATOM   5044  C   PRO F 344      15.607  23.085 -41.936  1.00 29.97           C  
ANISOU 5044  C   PRO F 344     3340   4450   3590    320    -30    -60       C  
ATOM   5045  O   PRO F 344      16.285  23.892 -42.529  1.00 29.59           O  
ANISOU 5045  O   PRO F 344     3220   4460   3570    220   -100     10       O  
ATOM   5046  CB  PRO F 344      17.025  22.008 -40.148  1.00 34.82           C  
ANISOU 5046  CB  PRO F 344     3820   5340   4070    450     10     60       C  
ATOM   5047  CG  PRO F 344      16.640  21.263 -38.884  1.00 35.07           C  
ANISOU 5047  CG  PRO F 344     3880   5390   4060    540     40     20       C  
ATOM   5048  CD  PRO F 344      15.146  21.059 -39.014  1.00 33.93           C  
ANISOU 5048  CD  PRO F 344     3850   5090   3950    530     60    -50       C  
ATOM   5049  N   ASN F 345      14.665  22.323 -42.501  1.00 28.93           N  
ANISOU 5049  N   ASN F 345     3320   4190   3480    380     50   -100       N  
ATOM   5050  CA  ASN F 345      14.346  22.371 -43.954  1.00 28.89           C  
ANISOU 5050  CA  ASN F 345     3390   4090   3500    380     70   -100       C  
ATOM   5051  C   ASN F 345      13.307  23.466 -44.236  1.00 26.59           C  
ANISOU 5051  C   ASN F 345     3120   3700   3290    260     10   -180       C  
ATOM   5052  O   ASN F 345      13.075  23.744 -45.417  1.00 24.49           O  
ANISOU 5052  O   ASN F 345     2880   3360   3060    230     10   -180       O  
ATOM   5053  CB  ASN F 345      13.798  21.027 -44.445  1.00 30.04           C  
ANISOU 5053  CB  ASN F 345     3720   4090   3600    470    100    -90       C  
ATOM   5054  CG  ASN F 345      14.756  19.878 -44.222  1.00 33.32           C  
ANISOU 5054  CG  ASN F 345     4210   4560   3890    680    140    -20       C  
ATOM   5055  OD1 ASN F 345      15.960  20.082 -44.080  1.00 37.44           O  
ANISOU 5055  OD1 ASN F 345     4580   5300   4350    780    190     50       O  
ATOM   5056  ND2 ASN F 345      14.230  18.666 -44.203  1.00 34.13           N  
ANISOU 5056  ND2 ASN F 345     4560   4460   3940    720     80    -10       N  
ATOM   5057  N   PHE F 346      12.715  24.048 -43.185  1.00 26.45           N  
ANISOU 5057  N   PHE F 346     3100   3690   3260    250    -50   -250       N  
ATOM   5058  CA  PHE F 346      11.660  25.101 -43.292  1.00 25.80           C  
ANISOU 5058  CA  PHE F 346     3080   3550   3180    260   -110   -340       C  
ATOM   5059  C   PHE F 346      12.009  26.191 -44.317  1.00 26.18           C  
ANISOU 5059  C   PHE F 346     3170   3480   3290    160   -200   -360       C  
ATOM   5060  O   PHE F 346      11.194  26.418 -45.226  1.00 25.06           O  
ANISOU 5060  O   PHE F 346     3060   3280   3180    150   -170   -370       O  
ATOM   5061  CB  PHE F 346      11.393  25.714 -41.915  1.00 25.96           C  
ANISOU 5061  CB  PHE F 346     3140   3640   3090    380   -180   -420       C  
ATOM   5062  CG  PHE F 346      10.411  26.858 -41.906  1.00 26.50           C  
ANISOU 5062  CG  PHE F 346     3330   3670   3070    520   -260   -530       C  
ATOM   5063  CD1 PHE F 346       9.048  26.625 -42.035  1.00 26.37           C  
ANISOU 5063  CD1 PHE F 346     3240   3800   2980    640   -160   -480       C  
ATOM   5064  CD2 PHE F 346      10.842  28.162 -41.712  1.00 26.71           C  
ANISOU 5064  CD2 PHE F 346     3570   3530   3060    540   -470   -640       C  
ATOM   5065  CE1 PHE F 346       8.147  27.677 -42.015  1.00 27.62           C  
ANISOU 5065  CE1 PHE F 346     3500   3990   3010    860   -210   -550       C  
ATOM   5066  CE2 PHE F 346       9.938  29.210 -41.683  1.00 28.03           C  
ANISOU 5066  CE2 PHE F 346     3940   3620   3090    750   -570   -760       C  
ATOM   5067  CZ  PHE F 346       8.593  28.967 -41.834  1.00 28.48           C  
ANISOU 5067  CZ  PHE F 346     3890   3880   3050    950   -410   -720       C  
ATOM   5068  N   LYS F 347      13.156  26.861 -44.167  1.00 28.37           N  
ANISOU 5068  N   LYS F 347     3440   3760   3580     50   -330   -320       N  
ATOM   5069  CA  LYS F 347      13.553  27.943 -45.116  1.00 30.29           C  
ANISOU 5069  CA  LYS F 347     3710   3910   3890   -120   -470   -260       C  
ATOM   5070  C   LYS F 347      13.365  27.488 -46.566  1.00 27.09           C  
ANISOU 5070  C   LYS F 347     3220   3540   3530   -120   -320   -190       C  
ATOM   5071  O   LYS F 347      12.732  28.236 -47.330  1.00 24.89           O  
ANISOU 5071  O   LYS F 347     3010   3140   3300   -160   -370   -220       O  
ATOM   5072  CB  LYS F 347      15.023  28.343 -44.942  1.00 34.90           C  
ANISOU 5072  CB  LYS F 347     4190   4600   4470   -320   -630    -80       C  
ATOM   5073  CG  LYS F 347      15.401  28.962 -43.603  1.00 39.69           C  
ANISOU 5073  CG  LYS F 347     4940   5120   5010   -390   -860   -130       C  
ATOM   5074  CD  LYS F 347      16.899  29.229 -43.484  1.00 42.79           C  
ANISOU 5074  CD  LYS F 347     5170   5680   5400   -660  -1050    130       C  
ATOM   5075  CE  LYS F 347      17.312  29.802 -42.147  1.00 45.98           C  
ANISOU 5075  CE  LYS F 347     5770   5980   5730   -770  -1340     90       C  
ATOM   5076  NZ  LYS F 347      16.670  31.113 -41.890  1.00 49.20           N  
ANISOU 5076  NZ  LYS F 347     6600   5990   6100   -800  -1670    -90       N  
ATOM   5077  N   ASP F 348      13.929  26.325 -46.920  1.00 26.16           N  
ANISOU 5077  N   ASP F 348     2990   3570   3380    -30   -170   -100       N  
ATOM   5078  CA  ASP F 348      13.864  25.758 -48.300  1.00 25.97           C  
ANISOU 5078  CA  ASP F 348     2940   3590   3340     60    -60    -40       C  
ATOM   5079  C   ASP F 348      12.425  25.382 -48.677  1.00 23.39           C  
ANISOU 5079  C   ASP F 348     2770   3080   3040     90    -10   -170       C  
ATOM   5080  O   ASP F 348      12.098  25.468 -49.883  1.00 21.35           O  
ANISOU 5080  O   ASP F 348     2540   2780   2790    100     10   -160       O  
ATOM   5081  CB  ASP F 348      14.789  24.545 -48.445  1.00 27.39           C  
ANISOU 5081  CB  ASP F 348     3070   3940   3390    250     60     50       C  
ATOM   5082  CG  ASP F 348      16.265  24.862 -48.247  1.00 31.35           C  
ANISOU 5082  CG  ASP F 348     3330   4750   3820    230     30    270       C  
ATOM   5083  OD1 ASP F 348      16.597  26.063 -48.109  1.00 32.96           O  
ANISOU 5083  OD1 ASP F 348     3430   4990   4100    -20   -120    370       O  
ATOM   5084  OD2 ASP F 348      17.081  23.900 -48.226  1.00 34.54           O  
ANISOU 5084  OD2 ASP F 348     3680   5370   4070    470    140    370       O  
ATOM   5085  N   GLN F 349      11.618  24.961 -47.695  1.00 21.21           N  
ANISOU 5085  N   GLN F 349     2550   2760   2750    110    -10   -240       N  
ATOM   5086  CA  GLN F 349      10.203  24.573 -47.949  1.00 20.56           C  
ANISOU 5086  CA  GLN F 349     2530   2600   2670     90      0   -260       C  
ATOM   5087  C   GLN F 349       9.423  25.829 -48.344  1.00 20.35           C  
ANISOU 5087  C   GLN F 349     2500   2560   2680     60    -40   -310       C  
ATOM   5088  O   GLN F 349       8.612  25.753 -49.297  1.00 18.86           O  
ANISOU 5088  O   GLN F 349     2330   2330   2500     20    -20   -290       O  
ATOM   5089  CB  GLN F 349       9.586  23.893 -46.725  1.00 20.56           C  
ANISOU 5089  CB  GLN F 349     2520   2680   2620    100      0   -230       C  
ATOM   5090  CG  GLN F 349      10.205  22.543 -46.402  1.00 21.29           C  
ANISOU 5090  CG  GLN F 349     2680   2740   2670    130     10   -170       C  
ATOM   5091  CD  GLN F 349       9.694  21.984 -45.098  1.00 21.99           C  
ANISOU 5091  CD  GLN F 349     2720   2930   2710    110    -10   -100       C  
ATOM   5092  OE1 GLN F 349       8.909  22.616 -44.397  1.00 22.16           O  
ANISOU 5092  OE1 GLN F 349     2610   3100   2700    130      0    -80       O  
ATOM   5093  NE2 GLN F 349      10.158  20.794 -44.757  1.00 22.04           N  
ANISOU 5093  NE2 GLN F 349     2820   2870   2680    130    -30    -30       N  
ATOM   5094  N   VAL F 350       9.677  26.938 -47.641  1.00 20.85           N  
ANISOU 5094  N   VAL F 350     2570   2620   2730     90   -110   -370       N  
ATOM   5095  CA  VAL F 350       8.999  28.233 -47.940  1.00 21.93           C  
ANISOU 5095  CA  VAL F 350     2790   2680   2860    120   -190   -430       C  
ATOM   5096  C   VAL F 350       9.438  28.682 -49.343  1.00 22.01           C  
ANISOU 5096  C   VAL F 350     2800   2600   2970    -10   -220   -380       C  
ATOM   5097  O   VAL F 350       8.563  29.099 -50.122  1.00 21.75           O  
ANISOU 5097  O   VAL F 350     2790   2530   2940     10   -200   -400       O  
ATOM   5098  CB  VAL F 350       9.294  29.296 -46.863  1.00 23.34           C  
ANISOU 5098  CB  VAL F 350     3110   2780   2970    210   -360   -530       C  
ATOM   5099  CG1 VAL F 350       8.857  30.691 -47.292  1.00 24.68           C  
ANISOU 5099  CG1 VAL F 350     3480   2780   3110    260   -510   -600       C  
ATOM   5100  CG2 VAL F 350       8.665  28.926 -45.527  1.00 23.84           C  
ANISOU 5100  CG2 VAL F 350     3170   3000   2890    420   -310   -570       C  
ATOM   5101  N   ILE F 351      10.730  28.551 -49.661  1.00 22.32           N  
ANISOU 5101  N   ILE F 351     2760   2680   3040   -110   -240   -290       N  
ATOM   5102  CA  ILE F 351      11.251  28.958 -51.004  1.00 23.96           C  
ANISOU 5102  CA  ILE F 351     2900   2910   3300   -210   -250   -170       C  
ATOM   5103  C   ILE F 351      10.636  28.069 -52.097  1.00 22.63           C  
ANISOU 5103  C   ILE F 351     2720   2770   3110   -120   -110   -180       C  
ATOM   5104  O   ILE F 351      10.253  28.617 -53.144  1.00 22.24           O  
ANISOU 5104  O   ILE F 351     2680   2680   3090   -150   -110   -160       O  
ATOM   5105  CB  ILE F 351      12.789  28.921 -51.056  1.00 25.39           C  
ANISOU 5105  CB  ILE F 351     2920   3270   3460   -300   -290     20       C  
ATOM   5106  CG1 ILE F 351      13.421  29.921 -50.086  1.00 27.62           C  
ANISOU 5106  CG1 ILE F 351     3240   3490   3760   -480   -530     70       C  
ATOM   5107  CG2 ILE F 351      13.268  29.162 -52.484  1.00 26.72           C  
ANISOU 5107  CG2 ILE F 351     2940   3580   3620   -340   -260    200       C  
ATOM   5108  CD1 ILE F 351      14.934  29.832 -50.000  1.00 29.86           C  
ANISOU 5108  CD1 ILE F 351     3300   4040   4010   -620   -590    330       C  
ATOM   5109  N   LEU F 352      10.574  26.751 -51.880  1.00 22.35           N  
ANISOU 5109  N   LEU F 352     2720   2760   3010    -20    -20   -200       N  
ATOM   5110  CA  LEU F 352       9.994  25.841 -52.911  1.00 23.07           C  
ANISOU 5110  CA  LEU F 352     2920   2800   3050     50     30   -210       C  
ATOM   5111  C   LEU F 352       8.525  26.194 -53.182  1.00 21.10           C  
ANISOU 5111  C   LEU F 352     2710   2470   2850    -40      0   -250       C  
ATOM   5112  O   LEU F 352       8.158  26.299 -54.358  1.00 21.46           O  
ANISOU 5112  O   LEU F 352     2790   2480   2890    -50      0   -240       O  
ATOM   5113  CB  LEU F 352      10.120  24.384 -52.459  1.00 24.36           C  
ANISOU 5113  CB  LEU F 352     3220   2910   3120    140     30   -230       C  
ATOM   5114  CG  LEU F 352       9.430  23.364 -53.366  1.00 25.88           C  
ANISOU 5114  CG  LEU F 352     3650   2950   3240    170    -30   -240       C  
ATOM   5115  CD1 LEU F 352       9.964  23.438 -54.792  1.00 26.90           C  
ANISOU 5115  CD1 LEU F 352     3830   3110   3280    340     10   -240       C  
ATOM   5116  CD2 LEU F 352       9.574  21.957 -52.810  1.00 26.92           C  
ANISOU 5116  CD2 LEU F 352     4000   2960   3270    240   -100   -240       C  
ATOM   5117  N   LEU F 353       7.717  26.359 -52.139  1.00 20.30           N  
ANISOU 5117  N   LEU F 353     2570   2390   2750    -70    -20   -270       N  
ATOM   5118  CA  LEU F 353       6.276  26.681 -52.325  1.00 20.22           C  
ANISOU 5118  CA  LEU F 353     2530   2430   2720   -100    -30   -240       C  
ATOM   5119  C   LEU F 353       6.101  28.060 -52.991  1.00 20.12           C  
ANISOU 5119  C   LEU F 353     2510   2390   2740    -70    -40   -280       C  
ATOM   5120  O   LEU F 353       5.277  28.156 -53.918  1.00 19.75           O  
ANISOU 5120  O   LEU F 353     2450   2360   2690   -110    -30   -240       O  
ATOM   5121  CB  LEU F 353       5.598  26.605 -50.954  1.00 21.09           C  
ANISOU 5121  CB  LEU F 353     2560   2690   2760    -50    -30   -200       C  
ATOM   5122  CG  LEU F 353       5.542  25.208 -50.333  1.00 20.95           C  
ANISOU 5122  CG  LEU F 353     2550   2710   2700   -140    -50   -100       C  
ATOM   5123  CD1 LEU F 353       5.171  25.265 -48.861  1.00 21.69           C  
ANISOU 5123  CD1 LEU F 353     2510   3020   2710    -40    -30    -40       C  
ATOM   5124  CD2 LEU F 353       4.574  24.311 -51.090  1.00 21.90           C  
ANISOU 5124  CD2 LEU F 353     2700   2820   2800   -330   -140     50       C  
ATOM   5125  N   ASN F 354       6.858  29.079 -52.564  1.00 20.07           N  
ANISOU 5125  N   ASN F 354     2540   2320   2760    -30   -100   -340       N  
ATOM   5126  CA  ASN F 354       6.742  30.446 -53.152  1.00 21.24           C  
ANISOU 5126  CA  ASN F 354     2750   2380   2940    -30   -180   -360       C  
ATOM   5127  C   ASN F 354       7.147  30.424 -54.626  1.00 20.27           C  
ANISOU 5127  C   ASN F 354     2580   2240   2890   -130   -150   -280       C  
ATOM   5128  O   ASN F 354       6.644  31.263 -55.385  1.00 19.99           O  
ANISOU 5128  O   ASN F 354     2570   2150   2870   -140   -190   -270       O  
ATOM   5129  CB  ASN F 354       7.563  31.493 -52.392  1.00 22.65           C  
ANISOU 5129  CB  ASN F 354     3060   2420   3120    -30   -350   -400       C  
ATOM   5130  CG  ASN F 354       6.936  31.897 -51.079  1.00 23.99           C  
ANISOU 5130  CG  ASN F 354     3370   2580   3160    180   -410   -510       C  
ATOM   5131  OD1 ASN F 354       5.717  31.837 -50.928  1.00 24.68           O  
ANISOU 5131  OD1 ASN F 354     3430   2810   3140    380   -320   -530       O  
ATOM   5132  ND2 ASN F 354       7.753  32.356 -50.144  1.00 26.20           N  
ANISOU 5132  ND2 ASN F 354     3790   2740   3420    170   -570   -560       N  
ATOM   5133  N   LYS F 355       8.020  29.493 -54.997  1.00 19.80           N  
ANISOU 5133  N   LYS F 355     2460   2240   2820   -160    -90   -230       N  
ATOM   5134  CA  LYS F 355       8.494  29.352 -56.397  1.00 19.88           C  
ANISOU 5134  CA  LYS F 355     2410   2320   2830   -170    -50   -140       C  
ATOM   5135  C   LYS F 355       7.323  28.995 -57.328  1.00 17.36           C  
ANISOU 5135  C   LYS F 355     2150   1960   2480   -150    -10   -180       C  
ATOM   5136  O   LYS F 355       7.321  29.474 -58.471  1.00 17.47           O  
ANISOU 5136  O   LYS F 355     2140   2000   2500   -160    -10   -130       O  
ATOM   5137  CB  LYS F 355       9.565  28.257 -56.431  1.00 22.55           C  
ANISOU 5137  CB  LYS F 355     2720   2770   3070    -70     10    -90       C  
ATOM   5138  CG  LYS F 355      10.193  27.959 -57.780  1.00 25.21           C  
ANISOU 5138  CG  LYS F 355     3010   3260   3310     60     80     10       C  
ATOM   5139  CD  LYS F 355      11.272  26.895 -57.695  1.00 27.67           C  
ANISOU 5139  CD  LYS F 355     3320   3740   3450    290    140     70       C  
ATOM   5140  CE  LYS F 355      12.010  26.715 -59.003  1.00 31.19           C  
ANISOU 5140  CE  LYS F 355     3690   4450   3720    530    220    200       C  
ATOM   5141  NZ  LYS F 355      13.095  25.709 -58.896  1.00 34.23           N  
ANISOU 5141  NZ  LYS F 355     4080   5060   3870    870    290    270       N  
ATOM   5142  N   HIS F 356       6.350  28.221 -56.837  1.00 14.49           N  
ANISOU 5142  N   HIS F 356     1850   1570   2080   -160    -10   -220       N  
ATOM   5143  CA  HIS F 356       5.212  27.762 -57.677  1.00 13.67           C  
ANISOU 5143  CA  HIS F 356     1800   1460   1930   -220    -40   -200       C  
ATOM   5144  C   HIS F 356       3.941  28.592 -57.465  1.00 13.44           C  
ANISOU 5144  C   HIS F 356     1680   1510   1910   -240    -40   -160       C  
ATOM   5145  O   HIS F 356       3.112  28.617 -58.386  1.00 13.75           O  
ANISOU 5145  O   HIS F 356     1710   1590   1930   -290    -50   -110       O  
ATOM   5146  CB  HIS F 356       4.972  26.270 -57.435  1.00 13.78           C  
ANISOU 5146  CB  HIS F 356     1960   1400   1870   -270   -110   -180       C  
ATOM   5147  CG  HIS F 356       6.148  25.430 -57.803  1.00 13.91           C  
ANISOU 5147  CG  HIS F 356     2140   1340   1810   -130   -110   -230       C  
ATOM   5148  ND1 HIS F 356       6.426  25.085 -59.110  1.00 14.42           N  
ANISOU 5148  ND1 HIS F 356     2360   1350   1770    -10   -130   -250       N  
ATOM   5149  CD2 HIS F 356       7.112  24.863 -57.049  1.00 13.90           C  
ANISOU 5149  CD2 HIS F 356     2180   1330   1770    -20    -90   -250       C  
ATOM   5150  CE1 HIS F 356       7.517  24.343 -59.143  1.00 15.43           C  
ANISOU 5150  CE1 HIS F 356     2620   1480   1770    220   -120   -280       C  
ATOM   5151  NE2 HIS F 356       7.958  24.196 -57.897  1.00 14.79           N  
ANISOU 5151  NE2 HIS F 356     2460   1420   1740    200    -90   -270       N  
ATOM   5152  N   ILE F 357       3.772  29.226 -56.307  1.00 13.52           N  
ANISOU 5152  N   ILE F 357     1640   1590   1910   -150    -30   -180       N  
ATOM   5153  CA  ILE F 357       2.549  30.048 -56.075  1.00 14.41           C  
ANISOU 5153  CA  ILE F 357     1680   1850   1950    -40    -20   -140       C  
ATOM   5154  C   ILE F 357       2.551  31.271 -57.007  1.00 14.83           C  
ANISOU 5154  C   ILE F 357     1790   1810   2040     20    -40   -180       C  
ATOM   5155  O   ILE F 357       3.513  32.076 -56.932  1.00 14.56           O  
ANISOU 5155  O   ILE F 357     1860   1600   2070     30   -100   -250       O  
ATOM   5156  CB  ILE F 357       2.459  30.456 -54.597  1.00 15.12           C  
ANISOU 5156  CB  ILE F 357     1770   2030   1950    150    -20   -180       C  
ATOM   5157  CG1 ILE F 357       2.339  29.224 -53.696  1.00 15.22           C  
ANISOU 5157  CG1 ILE F 357     1680   2180   1910     70      0    -90       C  
ATOM   5158  CG2 ILE F 357       1.306  31.424 -54.388  1.00 16.78           C  
ANISOU 5158  CG2 ILE F 357     1950   2430   2000    410      0   -140       C  
ATOM   5159  CD1 ILE F 357       2.482  29.519 -52.216  1.00 16.22           C  
ANISOU 5159  CD1 ILE F 357     1810   2410   1940    280      0   -140       C  
ATOM   5160  N   ASP F 358       1.515  31.389 -57.850  1.00 15.17           N  
ANISOU 5160  N   ASP F 358     1760   1970   2040     10    -10   -100       N  
ATOM   5161  CA  ASP F 358       1.328  32.529 -58.796  1.00 15.75           C  
ANISOU 5161  CA  ASP F 358     1880   1980   2130     80    -30   -110       C  
ATOM   5162  C   ASP F 358       2.518  32.670 -59.761  1.00 15.05           C  
ANISOU 5162  C   ASP F 358     1850   1700   2170    -60    -60   -130       C  
ATOM   5163  O   ASP F 358       2.724  33.782 -60.288  1.00 15.57           O  
ANISOU 5163  O   ASP F 358     1980   1670   2280    -40   -120   -130       O  
ATOM   5164  CB  ASP F 358       1.069  33.836 -58.034  1.00 17.22           C  
ANISOU 5164  CB  ASP F 358     2200   2120   2220    350    -80   -180       C  
ATOM   5165  CG  ASP F 358      -0.284  33.898 -57.346  1.00 18.92           C  
ANISOU 5165  CG  ASP F 358     2300   2660   2220    620    -20   -100       C  
ATOM   5166  OD1 ASP F 358      -1.204  33.164 -57.770  1.00 18.61           O  
ANISOU 5166  OD1 ASP F 358     2040   2900   2130    520     60     70       O  
ATOM   5167  OD2 ASP F 358      -0.414  34.691 -56.402  1.00 21.14           O  
ANISOU 5167  OD2 ASP F 358     2740   2940   2360    940    -60   -180       O  
ATOM   5168  N   ALA F 359       3.257  31.590 -60.001  1.00 14.17           N  
ANISOU 5168  N   ALA F 359     1720   1580   2090   -170    -30   -130       N  
ATOM   5169  CA  ALA F 359       4.395  31.647 -60.946  1.00 14.63           C  
ANISOU 5169  CA  ALA F 359     1770   1600   2190   -220    -30    -90       C  
ATOM   5170  C   ALA F 359       3.887  31.957 -62.364  1.00 14.87           C  
ANISOU 5170  C   ALA F 359     1770   1670   2210   -230    -10    -40       C  
ATOM   5171  O   ALA F 359       4.643  32.584 -63.137  1.00 15.02           O  
ANISOU 5171  O   ALA F 359     1740   1710   2260   -250    -20     40       O  
ATOM   5172  CB  ALA F 359       5.154  30.342 -60.923  1.00 14.12           C  
ANISOU 5172  CB  ALA F 359     1730   1560   2070   -200      0   -100       C  
ATOM   5173  N   TYR F 360       2.652  31.545 -62.677  1.00 15.16           N  
ANISOU 5173  N   TYR F 360     1810   1770   2190   -240      0    -40       N  
ATOM   5174  CA  TYR F 360       2.050  31.733 -64.026  1.00 15.56           C  
ANISOU 5174  CA  TYR F 360     1840   1870   2210   -260      0     10       C  
ATOM   5175  C   TYR F 360       2.015  33.216 -64.429  1.00 16.53           C  
ANISOU 5175  C   TYR F 360     1920   1970   2390   -220      0     50       C  
ATOM   5176  O   TYR F 360       1.927  33.518 -65.636  1.00 16.04           O  
ANISOU 5176  O   TYR F 360     1820   1950   2320   -230     10    110       O  
ATOM   5177  CB  TYR F 360       0.616  31.190 -64.068  1.00 15.83           C  
ANISOU 5177  CB  TYR F 360     1840   2010   2160   -340    -30     70       C  
ATOM   5178  CG  TYR F 360      -0.374  32.083 -63.374  1.00 16.16           C  
ANISOU 5178  CG  TYR F 360     1770   2190   2180   -250      0    120       C  
ATOM   5179  CD1 TYR F 360      -1.029  33.085 -64.069  1.00 16.67           C  
ANISOU 5179  CD1 TYR F 360     1780   2330   2220   -160     20    170       C  
ATOM   5180  CD2 TYR F 360      -0.612  31.973 -62.014  1.00 16.38           C  
ANISOU 5180  CD2 TYR F 360     1760   2300   2160   -180     10    130       C  
ATOM   5181  CE1 TYR F 360      -1.917  33.942 -63.435  1.00 17.73           C  
ANISOU 5181  CE1 TYR F 360     1860   2620   2260     40     50    220       C  
ATOM   5182  CE2 TYR F 360      -1.497  32.819 -61.366  1.00 17.24           C  
ANISOU 5182  CE2 TYR F 360     1790   2600   2160     30     40    180       C  
ATOM   5183  CZ  TYR F 360      -2.146  33.812 -62.076  1.00 17.89           C  
ANISOU 5183  CZ  TYR F 360     1850   2750   2200    170     60    220       C  
ATOM   5184  OH  TYR F 360      -3.007  34.653 -61.437  1.00 19.31           O  
ANISOU 5184  OH  TYR F 360     2000   3130   2200    490    100    270       O  
ATOM   5185  N   LYS F 361       2.075  34.127 -63.455  1.00 17.55           N  
ANISOU 5185  N   LYS F 361     2100   2020   2550   -150    -50     30       N  
ATOM   5186  CA  LYS F 361       2.005  35.579 -63.777  1.00 18.55           C  
ANISOU 5186  CA  LYS F 361     2300   2040   2710   -110   -130     60       C  
ATOM   5187  C   LYS F 361       3.213  36.061 -64.595  1.00 18.66           C  
ANISOU 5187  C   LYS F 361     2280   1990   2820   -250   -200    180       C  
ATOM   5188  O   LYS F 361       3.032  37.055 -65.328  1.00 19.12           O  
ANISOU 5188  O   LYS F 361     2370   1990   2900   -270   -270    270       O  
ATOM   5189  CB  LYS F 361       1.895  36.413 -62.497  1.00 20.27           C  
ANISOU 5189  CB  LYS F 361     2700   2110   2890     40   -240    -10       C  
ATOM   5190  CG  LYS F 361       0.606  36.225 -61.712  1.00 21.23           C  
ANISOU 5190  CG  LYS F 361     2810   2400   2860    280   -170    -60       C  
ATOM   5191  CD  LYS F 361       0.519  37.118 -60.493  1.00 23.87           C  
ANISOU 5191  CD  LYS F 361     3390   2600   3080    540   -290   -160       C  
ATOM   5192  CE  LYS F 361      -0.783  36.955 -59.740  1.00 26.16           C  
ANISOU 5192  CE  LYS F 361     3600   3200   3140    870   -180   -150       C  
ATOM   5193  NZ  LYS F 361      -0.822  37.823 -58.538  1.00 29.31           N  
ANISOU 5193  NZ  LYS F 361     4300   3470   3360   1240   -300   -280       N  
ATOM   5194  N   THR F 362       4.352  35.361 -64.530  1.00 17.69           N  
ANISOU 5194  N   THR F 362     2070   1940   2710   -340   -170    230       N  
ATOM   5195  CA  THR F 362       5.604  35.787 -65.223  1.00 19.13           C  
ANISOU 5195  CA  THR F 362     2120   2220   2930   -470   -230    440       C  
ATOM   5196  C   THR F 362       5.735  35.214 -66.644  1.00 18.94           C  
ANISOU 5196  C   THR F 362     1940   2440   2820   -400   -100    530       C  
ATOM   5197  O   THR F 362       6.760  35.506 -67.284  1.00 18.90           O  
ANISOU 5197  O   THR F 362     1760   2630   2790   -460   -120    770       O  
ATOM   5198  CB  THR F 362       6.827  35.374 -64.395  1.00 19.89           C  
ANISOU 5198  CB  THR F 362     2160   2370   3030   -540   -270    510       C  
ATOM   5199  OG1 THR F 362       6.822  33.948 -64.298  1.00 18.81           O  
ANISOU 5199  OG1 THR F 362     1990   2360   2800   -380   -110    390       O  
ATOM   5200  CG2 THR F 362       6.833  35.975 -63.007  1.00 20.39           C  
ANISOU 5200  CG2 THR F 362     2410   2190   3150   -600   -440    420       C  
ATOM   5201  N   PHE F 363       4.753  34.448 -67.131  1.00 17.85           N  
ANISOU 5201  N   PHE F 363     1860   2320   2600   -280      0    390       N  
ATOM   5202  CA  PHE F 363       4.863  33.883 -68.503  1.00 19.12           C  
ANISOU 5202  CA  PHE F 363     1950   2670   2640   -170     80    450       C  
ATOM   5203  C   PHE F 363       3.485  33.783 -69.150  1.00 18.58           C  
ANISOU 5203  C   PHE F 363     1970   2560   2540   -150     90    350       C  
ATOM   5204  O   PHE F 363       2.466  33.765 -68.458  1.00 17.41           O  
ANISOU 5204  O   PHE F 363     1890   2290   2430   -200     60    260       O  
ATOM   5205  CB  PHE F 363       5.581  32.527 -68.495  1.00 20.17           C  
ANISOU 5205  CB  PHE F 363     2140   2920   2610     10    140    390       C  
ATOM   5206  CG  PHE F 363       4.982  31.464 -67.605  1.00 20.06           C  
ANISOU 5206  CG  PHE F 363     2330   2720   2580     10    110    190       C  
ATOM   5207  CD1 PHE F 363       3.875  30.732 -68.012  1.00 20.27           C  
ANISOU 5207  CD1 PHE F 363     2530   2650   2530      0     60     80       C  
ATOM   5208  CD2 PHE F 363       5.563  31.154 -66.384  1.00 19.75           C  
ANISOU 5208  CD2 PHE F 363     2300   2630   2580    -10    100    160       C  
ATOM   5209  CE1 PHE F 363       3.331  29.749 -67.198  1.00 20.29           C  
ANISOU 5209  CE1 PHE F 363     2690   2500   2510    -70    -20    -20       C  
ATOM   5210  CE2 PHE F 363       5.023  30.163 -65.574  1.00 20.32           C  
ANISOU 5210  CE2 PHE F 363     2540   2560   2630    -20     60     20       C  
ATOM   5211  CZ  PHE F 363       3.907  29.461 -65.983  1.00 20.11           C  
ANISOU 5211  CZ  PHE F 363     2670   2440   2530    -70    -10    -40       C  
ATOM   5212  N   PRO F 364       3.418  33.733 -70.502  1.00 19.49           N  
ANISOU 5212  N   PRO F 364     2040   2810   2550    -80    120    420       N  
ATOM   5213  CA  PRO F 364       2.141  33.629 -71.210  1.00 19.65           C  
ANISOU 5213  CA  PRO F 364     2130   2810   2530    -90    110    360       C  
ATOM   5214  C   PRO F 364       1.356  32.394 -70.745  1.00 19.73           C  
ANISOU 5214  C   PRO F 364     2320   2720   2460   -130     40    220       C  
ATOM   5215  O   PRO F 364       1.944  31.324 -70.617  1.00 20.24           O  
ANISOU 5215  O   PRO F 364     2530   2740   2420    -50     10    140       O  
ATOM   5216  CB  PRO F 364       2.533  33.508 -72.696  1.00 20.54           C  
ANISOU 5216  CB  PRO F 364     2200   3110   2490     50    140    440       C  
ATOM   5217  CG  PRO F 364       3.929  34.103 -72.770  1.00 21.66           C  
ANISOU 5217  CG  PRO F 364     2140   3440   2650    100    190    630       C  
ATOM   5218  CD  PRO F 364       4.564  33.806 -71.425  1.00 20.99           C  
ANISOU 5218  CD  PRO F 364     2090   3250   2640     50    170    590       C  
ATOM   5219  OXT PRO F 364       0.158  32.455 -70.491  1.00 19.34           O  
ANISOU 5219  OXT PRO F 364     2260   2650   2430   -250      0    220       O  
TER    5220      PRO F 364                                                      
HETATM 5221 CL    CL A 401      11.022   2.902 -24.620  1.00 35.16          CL  
HETATM 5222 CL  A CL B 401       0.286  -2.915 -31.587  0.50 28.37          CL  
HETATM 5223 CL  B CL B 401       0.769  -1.071 -31.170  0.50 30.52          CL  
HETATM 5224 CL    CL C 401     -11.116 -11.914 -48.449  1.00 41.19          CL  
HETATM 5225 CL    CL D 401      -0.571 -18.528 -41.481  0.50 19.95          CL  
HETATM 5226 CL  A CL D 402      -7.379 -27.271 -40.945  0.50 23.78          CL  
HETATM 5227 CL  B CL D 402      -8.757 -28.217 -40.992  0.50 28.43          CL  
HETATM 5228 CL  A CL E 401      -8.916   7.026 -46.936  0.50 18.70          CL  
HETATM 5229 CL  B CL E 401      -8.596   6.878 -48.453  0.50 26.60          CL  
HETATM 5230 CL    CL E 402      -1.946   8.830 -38.006  1.00 39.06          CL  
HETATM 5231 CL  A CL F 401       1.799  11.936 -55.074  0.60 23.45          CL  
HETATM 5232 CL  B CL F 401       1.626  11.395 -52.864  0.40 24.03          CL  
HETATM 5233 CL    CL F 402      -5.257  10.403 -63.875  0.60 29.02          CL  
HETATM 5234  O   HOH A 501      17.864 -11.954 -21.217  1.00 26.98           O  
HETATM 5235  O   HOH A 502      21.079   8.292 -16.444  1.00 24.22           O  
HETATM 5236  O   HOH A 503      27.354 -10.694 -18.993  1.00 24.04           O  
HETATM 5237  O   HOH A 504      19.493   3.655  -6.745  1.00 20.66           O  
HETATM 5238  O   HOH A 505      21.718   2.113 -13.349  1.00 26.56           O  
HETATM 5239  O   HOH A 506       6.707  -4.013  -2.609  1.00 29.38           O  
HETATM 5240  O   HOH A 507     -11.967   9.819 -11.606  1.00 31.27           O  
HETATM 5241  O   HOH A 508      10.466   4.614   4.041  1.00 25.71           O  
HETATM 5242  O   HOH A 509     -19.939  -0.357 -10.214  1.00 23.92           O  
HETATM 5243  O   HOH A 510       7.216   5.825 -25.256  1.00 27.70           O  
HETATM 5244  O   HOH A 511      15.012  -0.448  -4.519  1.00 29.04           O  
HETATM 5245  O   HOH A 512      -6.636  -8.147 -13.901  1.00 16.71           O  
HETATM 5246  O   HOH A 513       2.236  14.188 -10.587  1.00 28.57           O  
HETATM 5247  O   HOH A 514     -10.423  -6.514 -12.105  1.00 39.58           O  
HETATM 5248  O   HOH A 515       5.875  -0.143  -2.111  1.00 13.07           O  
HETATM 5249  O   HOH A 516     -10.910 -10.487 -15.390  1.00 21.73           O  
HETATM 5250  O   HOH A 517     -19.050   8.572 -10.300  1.00 36.91           O  
HETATM 5251  O   HOH A 518      20.280  -3.408  -6.919  1.00 32.78           O  
HETATM 5252  O  AHOH A 519       1.804   6.647  -9.065  0.50 10.40           O  
HETATM 5253  O  BHOH A 519      -0.041   7.495  -8.602  0.50 18.17           O  
HETATM 5254  O   HOH A 520       7.664   8.983  -3.477  1.00 13.50           O  
HETATM 5255  O   HOH A 521      -4.273   4.624  -9.340  1.00 24.57           O  
HETATM 5256  O   HOH A 522      -0.253   3.982 -10.853  1.00 14.20           O  
HETATM 5257  O   HOH A 523      14.287  12.308  -8.648  1.00 17.87           O  
HETATM 5258  O   HOH A 524      13.217  15.904 -14.504  1.00 25.55           O  
HETATM 5259  O   HOH A 525      20.074   4.641 -11.042  1.00 17.31           O  
HETATM 5260  O   HOH A 526       4.306   9.440 -25.295  1.00 30.78           O  
HETATM 5261  O   HOH A 527      -7.230 -12.865 -12.680  1.00 26.02           O  
HETATM 5262  O   HOH A 528      22.588   1.434 -21.276  1.00 30.84           O  
HETATM 5263  O   HOH A 529      -0.387   9.895 -12.924  1.00 27.08           O  
HETATM 5264  O   HOH A 530       8.102   9.871  -7.810  1.00 30.10           O  
HETATM 5265  O   HOH A 531      -0.589  -1.630  -1.852  1.00 34.94           O  
HETATM 5266  O   HOH A 532      13.735   0.317  -0.657  1.00 25.61           O  
HETATM 5267  O   HOH A 533      -4.488 -12.333 -21.764  1.00 10.44           O  
HETATM 5268  O   HOH A 534     -17.959   4.878 -12.949  1.00 21.49           O  
HETATM 5269  O   HOH A 535      13.770 -17.604 -14.382  1.00 26.88           O  
HETATM 5270  O   HOH A 536     -17.479   4.825 -15.733  1.00 19.61           O  
HETATM 5271  O   HOH A 537       0.770  12.646 -13.183  1.00 38.25           O  
HETATM 5272  O   HOH A 538      16.097 -11.932 -18.726  1.00 17.43           O  
HETATM 5273  O   HOH A 539       9.887  14.068  -8.952  1.00 30.07           O  
HETATM 5274  O   HOH A 540      -5.884   6.120 -18.608  1.00 15.92           O  
HETATM 5275  O   HOH A 541      -3.632   0.800  -1.263  1.00 19.43           O  
HETATM 5276  O   HOH A 542      13.724  13.144  -2.046  1.00 38.30           O  
HETATM 5277  O   HOH A 543      -5.051 -11.476 -26.057  1.00 12.16           O  
HETATM 5278  O   HOH A 544      -2.444  -9.391 -30.236  1.00 11.93           O  
HETATM 5279  O   HOH A 545       0.889  15.670 -16.308  1.00 40.70           O  
HETATM 5280  O   HOH A 546      19.787  -7.229  -6.345  1.00 25.93           O  
HETATM 5281  O   HOH A 547       7.790 -14.623 -19.240  1.00 21.68           O  
HETATM 5282  O   HOH A 548      15.386  -2.582 -24.627  1.00 21.44           O  
HETATM 5283  O   HOH A 549       1.757 -10.796 -10.772  1.00 31.88           O  
HETATM 5284  O   HOH A 550      24.364 -13.477 -14.891  1.00 25.67           O  
HETATM 5285  O   HOH A 551      -5.242   8.882 -18.619  1.00 20.68           O  
HETATM 5286  O   HOH A 552       5.366  -1.368   0.214  1.00 28.29           O  
HETATM 5287  O   HOH A 553      13.387  -8.322 -24.420  1.00 21.91           O  
HETATM 5288  O   HOH A 554      14.072  -3.703  -4.289  1.00 31.92           O  
HETATM 5289  O   HOH A 555      -0.999 -14.114 -16.462  1.00 17.56           O  
HETATM 5290  O   HOH A 556       3.697  -2.480 -28.723  1.00 23.01           O  
HETATM 5291  O   HOH A 557      10.538   3.660  -6.074  1.00 10.18           O  
HETATM 5292  O   HOH A 558      15.690  -9.508 -22.972  1.00 29.05           O  
HETATM 5293  O   HOH A 559       9.968 -13.735 -20.464  1.00 18.99           O  
HETATM 5294  O   HOH A 560       9.356   8.685  -1.365  1.00 18.89           O  
HETATM 5295  O   HOH A 561      25.162 -10.234 -15.176  1.00 29.83           O  
HETATM 5296  O   HOH A 562      -2.809 -10.282 -27.717  1.00 15.12           O  
HETATM 5297  O   HOH A 563      22.978  -3.547 -13.473  1.00 16.63           O  
HETATM 5298  O   HOH A 564      24.000  -9.346 -24.453  1.00 24.30           O  
HETATM 5299  O   HOH A 565      23.919   3.758  -9.016  1.00 39.96           O  
HETATM 5300  O   HOH A 566      17.685   7.202  -5.285  1.00 17.88           O  
HETATM 5301  O   HOH A 567       5.186  -1.648 -22.318  1.00 13.74           O  
HETATM 5302  O  AHOH A 568       1.462  12.056  -7.125  0.50 18.02           O  
HETATM 5303  O  BHOH A 568       1.834  13.811  -7.992  0.50 18.82           O  
HETATM 5304  O   HOH A 569       1.083   7.461  -1.253  1.00 31.99           O  
HETATM 5305  O   HOH A 570       2.035  -5.211 -30.239  1.00 18.12           O  
HETATM 5306  O   HOH A 571     -17.139  -3.095 -10.760  1.00 44.26           O  
HETATM 5307  O   HOH A 572      20.546  -6.957 -19.855  1.00 22.65           O  
HETATM 5308  O   HOH A 573      22.242 -10.158  -9.075  1.00 10.10           O  
HETATM 5309  O   HOH A 574      13.935  15.524 -21.971  1.00 42.46           O  
HETATM 5310  O   HOH A 575      13.001 -11.945 -20.034  1.00 34.76           O  
HETATM 5311  O   HOH A 576      23.304   7.125 -15.955  1.00 31.79           O  
HETATM 5312  O   HOH A 577      23.088   5.070 -13.756  1.00 33.04           O  
HETATM 5313  O   HOH A 578      19.407   7.291  -7.789  1.00 28.96           O  
HETATM 5314  O   HOH A 579      19.982  -4.402 -23.585  1.00 34.53           O  
HETATM 5315  O   HOH A 580       1.611 -13.843 -16.377  1.00 30.70           O  
HETATM 5316  O   HOH A 581      -2.417  11.415 -14.471  1.00 32.69           O  
HETATM 5317  O   HOH A 582       8.801  16.553 -10.220  1.00 34.71           O  
HETATM 5318  O   HOH A 583      -2.346   2.266 -29.349  1.00 21.63           O  
HETATM 5319  O   HOH A 584       5.207  14.064  -1.547  1.00 42.85           O  
HETATM 5320  O   HOH A 585       4.039  12.087 -23.107  1.00 16.75           O  
HETATM 5321  O   HOH A 586      18.837  -2.927  -4.718  1.00 33.92           O  
HETATM 5322  O   HOH A 587      25.252  -3.960 -12.724  1.00 26.33           O  
HETATM 5323  O   HOH A 588      -2.741  14.139 -15.162  1.00 42.93           O  
HETATM 5324  O  AHOH A 589      12.530  14.330 -10.100  0.50 10.48           O  
HETATM 5325  O  BHOH A 589      13.362  16.367 -10.813  0.50 12.18           O  
HETATM 5326  O   HOH A 590      22.125  -1.425 -12.154  1.00 17.59           O  
HETATM 5327  O   HOH A 591      13.080  11.825  -6.427  1.00 35.42           O  
HETATM 5328  O   HOH A 592      -5.084   9.685 -16.024  1.00 28.28           O  
HETATM 5329  O   HOH A 593      16.097   0.150  -1.829  1.00 25.12           O  
HETATM 5330  O   HOH A 594      24.802 -10.749  -8.612  1.00 29.27           O  
HETATM 5331  O   HOH A 595       5.811   4.155 -26.823  1.00 28.29           O  
HETATM 5332  O   HOH A 596     -15.615  -5.338  -9.475  1.00 36.25           O  
HETATM 5333  O  AHOH A 597       6.061  -3.478 -29.940  0.50 13.92           O  
HETATM 5334  O  BHOH A 597       7.443  -3.907 -28.436  0.50  8.50           O  
HETATM 5335  O   HOH A 598       2.130  13.500 -23.004  1.00 30.91           O  
HETATM 5336  O   HOH A 599      13.791   0.222   2.150  1.00 26.13           O  
HETATM 5337  O   HOH B 501     -13.905   5.971 -16.739  1.00 17.83           O  
HETATM 5338  O   HOH B 502       3.584 -12.499 -35.698  1.00 20.41           O  
HETATM 5339  O   HOH B 503      15.791 -18.045 -10.917  1.00 39.32           O  
HETATM 5340  O   HOH B 504       4.067 -19.259 -36.544  1.00 14.36           O  
HETATM 5341  O   HOH B 505     -16.960 -12.828 -26.935  1.00 20.44           O  
HETATM 5342  O   HOH B 506       9.113   4.130 -13.339  1.00 12.61           O  
HETATM 5343  O   HOH B 507     -15.706  -1.228 -31.859  1.00 33.89           O  
HETATM 5344  O   HOH B 508     -14.423 -10.385 -32.416  1.00 24.91           O  
HETATM 5345  O   HOH B 509     -10.476 -16.415 -16.174  1.00 16.85           O  
HETATM 5346  O   HOH B 510     -10.760  -9.164 -37.861  1.00 23.18           O  
HETATM 5347  O   HOH B 511      -3.706 -17.869 -36.939  1.00 13.47           O  
HETATM 5348  O   HOH B 512      -9.230 -18.863 -32.501  1.00 22.00           O  
HETATM 5349  O   HOH B 513     -19.516  -6.931 -25.262  1.00 20.26           O  
HETATM 5350  O   HOH B 514     -15.116 -11.903 -16.906  1.00 26.61           O  
HETATM 5351  O   HOH B 515       1.050 -22.442 -27.687  1.00 33.84           O  
HETATM 5352  O   HOH B 516     -12.422   7.654 -29.376  1.00 15.85           O  
HETATM 5353  O   HOH B 517       5.216 -13.932 -19.103  1.00 30.61           O  
HETATM 5354  O   HOH B 518       3.955  -6.592  -8.695  1.00 12.10           O  
HETATM 5355  O   HOH B 519      -8.925   9.835 -23.274  1.00 34.79           O  
HETATM 5356  O   HOH B 520     -17.433  -2.191 -29.607  1.00 15.08           O  
HETATM 5357  O   HOH B 521      -4.140  -3.728 -36.380  1.00 32.03           O  
HETATM 5358  O   HOH B 522      -1.771 -18.122 -21.698  1.00 12.41           O  
HETATM 5359  O   HOH B 523       4.598  -5.162 -31.343  1.00 24.64           O  
HETATM 5360  O   HOH B 524      10.306   6.060 -17.967  1.00 10.08           O  
HETATM 5361  O   HOH B 525      -4.183   2.082 -31.065  1.00 11.70           O  
HETATM 5362  O   HOH B 526       6.739 -19.721 -29.816  1.00 28.07           O  
HETATM 5363  O   HOH B 527       3.487 -18.285 -23.985  1.00 22.27           O  
HETATM 5364  O   HOH B 528       0.364 -15.619 -19.175  1.00 19.12           O  
HETATM 5365  O   HOH B 529       5.678  -9.658  -6.453  1.00 27.14           O  
HETATM 5366  O   HOH B 530       5.837   2.135 -11.022  1.00 12.22           O  
HETATM 5367  O   HOH B 531     -11.212   5.445 -23.048  1.00 23.82           O  
HETATM 5368  O   HOH B 532      10.409 -15.483 -22.851  1.00 22.21           O  
HETATM 5369  O   HOH B 533      -4.661   5.733 -25.889  1.00 16.14           O  
HETATM 5370  O   HOH B 534      -9.664   7.417 -24.496  1.00 28.91           O  
HETATM 5371  O   HOH B 535      -8.819 -21.597 -24.106  1.00 27.84           O  
HETATM 5372  O   HOH B 536       7.125  -5.172  -5.028  1.00 21.02           O  
HETATM 5373  O   HOH B 537     -16.077 -12.227 -22.841  1.00 16.52           O  
HETATM 5374  O   HOH B 538       2.091  -2.549 -24.026  1.00 16.52           O  
HETATM 5375  O   HOH B 539      -0.054 -12.456 -40.380  1.00 25.20           O  
HETATM 5376  O   HOH B 540      -3.405 -20.196 -10.659  1.00 28.78           O  
HETATM 5377  O   HOH B 541       7.226 -21.716  -8.983  1.00 40.09           O  
HETATM 5378  O   HOH B 542       3.526 -22.120 -29.721  1.00 28.67           O  
HETATM 5379  O   HOH B 543      -5.545 -21.095 -31.059  1.00 24.89           O  
HETATM 5380  O   HOH B 544     -10.178   9.527 -27.490  1.00 18.67           O  
HETATM 5381  O   HOH B 545       6.812   1.963 -25.463  1.00 21.40           O  
HETATM 5382  O   HOH B 546     -16.100   2.860 -31.868  1.00 15.85           O  
HETATM 5383  O   HOH B 547      -9.972  -1.001 -34.781  1.00 23.07           O  
HETATM 5384  O   HOH B 548      -3.434   3.490 -11.850  1.00 17.31           O  
HETATM 5385  O   HOH B 549       6.773 -11.807 -32.558  1.00 19.13           O  
HETATM 5386  O   HOH B 550      10.175  -7.149  -5.175  1.00 34.98           O  
HETATM 5387  O   HOH B 551     -10.499 -15.323 -23.393  1.00 10.06           O  
HETATM 5388  O   HOH B 552     -14.125   2.025 -30.042  1.00 23.61           O  
HETATM 5389  O   HOH B 553     -19.756   6.468 -25.762  1.00 25.93           O  
HETATM 5390  O   HOH B 554     -16.011 -14.577 -16.707  1.00 32.27           O  
HETATM 5391  O   HOH B 555     -21.614   0.155 -23.721  1.00 16.05           O  
HETATM 5392  O   HOH B 556     -19.325   4.380 -28.202  1.00 25.75           O  
HETATM 5393  O   HOH B 557      -5.353   5.713 -15.978  1.00 15.77           O  
HETATM 5394  O   HOH B 558      -0.277 -19.319 -37.610  1.00 18.92           O  
HETATM 5395  O   HOH B 559      -2.058   1.355 -11.711  1.00 14.67           O  
HETATM 5396  O   HOH B 560     -21.009 -21.646 -25.494  1.00 47.69           O  
HETATM 5397  O   HOH B 561      -7.485 -23.271 -20.692  1.00 32.26           O  
HETATM 5398  O   HOH B 562       8.232   4.331 -23.403  1.00 22.09           O  
HETATM 5399  O   HOH B 563     -15.153 -16.407 -29.657  1.00 25.53           O  
HETATM 5400  O   HOH B 564       3.537 -19.920 -26.356  1.00 20.64           O  
HETATM 5401  O   HOH B 565       8.945   5.036 -15.975  1.00 16.53           O  
HETATM 5402  O   HOH B 566      10.407 -14.296  -3.853  1.00 30.49           O  
HETATM 5403  O   HOH B 567      -1.407 -12.953 -13.144  1.00 39.79           O  
HETATM 5404  O   HOH B 568       4.227  -4.036  -3.016  1.00 38.47           O  
HETATM 5405  O   HOH B 569       8.228 -20.034 -24.894  1.00 35.59           O  
HETATM 5406  O   HOH B 570       3.149 -12.130 -39.691  1.00 23.31           O  
HETATM 5407  O   HOH B 571     -12.485  -1.714 -37.086  1.00 30.78           O  
HETATM 5408  O   HOH B 572      -7.253   6.266 -25.816  1.00 23.85           O  
HETATM 5409  O   HOH B 573     -14.798 -14.997 -31.888  1.00 27.88           O  
HETATM 5410  O   HOH B 574      -6.106 -19.474 -33.221  1.00 27.72           O  
HETATM 5411  O  AHOH B 575      -7.561 -20.495 -26.122  0.50 10.60           O  
HETATM 5412  O  BHOH B 575      -8.377 -21.098 -27.732  0.50  8.43           O  
HETATM 5413  O   HOH B 576     -22.038   3.808 -29.190  1.00 32.79           O  
HETATM 5414  O   HOH B 577     -21.231  -5.651 -23.425  1.00 25.27           O  
HETATM 5415  O   HOH B 578       2.867  -0.646 -26.332  1.00 20.95           O  
HETATM 5416  O   HOH B 579      -5.003 -24.433 -21.297  1.00 40.03           O  
HETATM 5417  O   HOH B 580      -2.145 -19.827 -39.688  1.00 45.79           O  
HETATM 5418  O   HOH B 581      11.109  -5.687 -29.707  1.00 30.48           O  
HETATM 5419  O   HOH B 582       6.950  -0.910 -25.046  1.00 32.95           O  
HETATM 5420  O   HOH B 583      14.553 -24.679  -7.582  1.00 31.81           O  
HETATM 5421  O   HOH B 584     -17.378  -4.970 -29.720  1.00 30.34           O  
HETATM 5422  O   HOH B 585       8.585 -21.410 -15.703  1.00 35.66           O  
HETATM 5423  O   HOH B 586      -0.064 -19.919 -20.530  1.00 21.49           O  
HETATM 5424  O   HOH B 587       5.222 -21.081 -13.407  1.00 33.72           O  
HETATM 5425  O   HOH B 588       6.128 -13.301 -34.963  1.00 31.14           O  
HETATM 5426  O   HOH B 589      -1.148 -16.075 -42.409  1.00 30.59           O  
HETATM 5427  O   HOH B 590       1.843  -9.063  -8.482  1.00 44.38           O  
HETATM 5428  O   HOH B 591       4.649 -19.344 -11.784  1.00 28.14           O  
HETATM 5429  O   HOH B 592     -19.451  -6.546 -29.937  1.00 33.62           O  
HETATM 5430  O   HOH B 593      -9.731 -20.599 -29.939  1.00 30.45           O  
HETATM 5431  O   HOH B 594      -7.395   8.693 -20.867  1.00 26.56           O  
HETATM 5432  O   HOH B 595      -1.210 -23.510 -31.145  1.00 29.91           O  
HETATM 5433  O   HOH B 596       4.620 -16.665 -12.168  1.00 45.47           O  
HETATM 5434  O   HOH B 597       8.653 -13.663 -32.281  1.00 33.82           O  
HETATM 5435  O   HOH C 501       0.617  -4.832 -59.971  1.00 22.84           O  
HETATM 5436  O   HOH C 502       3.408 -13.704 -72.347  1.00 15.93           O  
HETATM 5437  O   HOH C 503      -3.544 -17.415 -44.992  1.00 29.14           O  
HETATM 5438  O   HOH C 504      -0.563   0.895 -56.118  1.00 27.30           O  
HETATM 5439  O   HOH C 505       0.333 -10.649 -62.122  1.00 14.93           O  
HETATM 5440  O   HOH C 506     -13.241   1.218 -58.931  1.00 20.35           O  
HETATM 5441  O   HOH C 507       7.158  -9.307 -51.287  1.00 23.52           O  
HETATM 5442  O   HOH C 508      10.652 -20.439 -60.906  1.00 24.81           O  
HETATM 5443  O   HOH C 509     -14.068  -4.085 -49.082  1.00 35.90           O  
HETATM 5444  O   HOH C 510      18.712  -5.868 -62.529  1.00 27.54           O  
HETATM 5445  O   HOH C 511     -20.308  -3.477 -54.187  1.00 32.67           O  
HETATM 5446  O   HOH C 512     -10.457   3.484 -57.719  1.00 26.06           O  
HETATM 5447  O   HOH C 513      -0.487  -8.368 -74.157  1.00 27.83           O  
HETATM 5448  O   HOH C 514       1.375 -28.619 -57.041  1.00 25.10           O  
HETATM 5449  O   HOH C 515      10.559 -30.737 -57.667  1.00 21.89           O  
HETATM 5450  O   HOH C 516      -6.066 -14.526 -71.293  1.00 10.68           O  
HETATM 5451  O   HOH C 517     -13.256 -20.652 -67.894  1.00 29.06           O  
HETATM 5452  O   HOH C 518     -13.639 -14.143 -72.689  1.00 19.13           O  
HETATM 5453  O   HOH C 519      -2.685 -15.913 -72.916  1.00 32.80           O  
HETATM 5454  O   HOH C 520     -14.237 -31.900 -59.156  1.00 27.75           O  
HETATM 5455  O   HOH C 521     -18.246 -12.147 -67.869  1.00 27.82           O  
HETATM 5456  O   HOH C 522      -4.418  -5.246 -47.847  1.00 26.05           O  
HETATM 5457  O   HOH C 523     -21.261  -6.204 -56.756  1.00 16.56           O  
HETATM 5458  O   HOH C 524     -20.014 -18.036 -66.475  1.00 30.46           O  
HETATM 5459  O   HOH C 525      -7.563  -5.553 -69.781  1.00 13.33           O  
HETATM 5460  O   HOH C 526      -1.664 -24.918 -62.514  1.00 25.99           O  
HETATM 5461  O   HOH C 527     -16.117 -32.601 -62.098  1.00 31.86           O  
HETATM 5462  O   HOH C 528     -18.084  -3.242 -49.306  1.00 41.75           O  
HETATM 5463  O   HOH C 529     -14.054 -18.077 -69.026  1.00 27.92           O  
HETATM 5464  O   HOH C 530      -7.334  -8.989 -47.952  1.00 22.19           O  
HETATM 5465  O   HOH C 531      18.010  -9.332 -60.102  1.00 18.05           O  
HETATM 5466  O   HOH C 532     -13.644 -22.958 -49.163  1.00 30.34           O  
HETATM 5467  O   HOH C 533       2.194 -24.537 -43.319  1.00  8.61           O  
HETATM 5468  O   HOH C 534     -23.179 -31.123 -57.336  1.00 28.93           O  
HETATM 5469  O   HOH C 535      17.376  -9.611 -57.517  1.00 18.43           O  
HETATM 5470  O   HOH C 536       6.878 -22.333 -59.333  1.00 14.89           O  
HETATM 5471  O   HOH C 537     -15.076  -8.336 -48.873  1.00 28.69           O  
HETATM 5472  O   HOH C 538     -14.193  -2.252 -64.611  1.00 20.49           O  
HETATM 5473  O   HOH C 539     -13.892  -9.234 -77.890  1.00 31.37           O  
HETATM 5474  O   HOH C 540     -22.881 -18.158 -59.716  1.00 33.50           O  
HETATM 5475  O   HOH C 541     -22.591  -3.921 -58.400  1.00 27.09           O  
HETATM 5476  O   HOH C 542     -10.072 -28.379 -53.013  1.00 12.79           O  
HETATM 5477  O   HOH C 543       4.602 -27.113 -51.845  1.00  8.60           O  
HETATM 5478  O   HOH C 544     -17.650  -7.804 -76.658  1.00 29.37           O  
HETATM 5479  O   HOH C 545     -22.340 -12.991 -51.304  1.00 20.76           O  
HETATM 5480  O   HOH C 546     -15.525 -17.086 -48.562  1.00 29.32           O  
HETATM 5481  O   HOH C 547     -17.790  -7.274 -67.861  1.00 18.71           O  
HETATM 5482  O   HOH C 548     -20.337  -9.828 -62.296  1.00 18.39           O  
HETATM 5483  O   HOH C 549     -18.293  -7.651 -72.395  1.00 33.17           O  
HETATM 5484  O   HOH C 550      -9.938  -0.548 -64.300  1.00 23.39           O  
HETATM 5485  O   HOH C 551     -20.490 -21.528 -53.332  1.00 16.15           O  
HETATM 5486  O   HOH C 552     -15.159 -14.731 -68.766  1.00 24.06           O  
HETATM 5487  O   HOH C 553     -16.125 -26.673 -54.738  1.00 28.26           O  
HETATM 5488  O   HOH C 554     -15.880 -24.113 -50.626  1.00 24.09           O  
HETATM 5489  O   HOH C 555      -2.338 -17.387 -49.255  1.00 11.75           O  
HETATM 5490  O   HOH C 556       5.074  -5.623 -54.350  1.00 16.91           O  
HETATM 5491  O   HOH C 557     -24.414 -28.071 -58.819  1.00 22.64           O  
HETATM 5492  O   HOH C 558       5.220 -25.925 -62.269  1.00 33.36           O  
HETATM 5493  O   HOH C 559       2.617 -25.249 -45.813  1.00 14.80           O  
HETATM 5494  O   HOH C 560     -20.232 -18.768 -49.528  1.00 28.42           O  
HETATM 5495  O   HOH C 561       4.784 -26.280 -47.407  1.00 12.20           O  
HETATM 5496  O   HOH C 562      -7.975  -4.683 -65.719  1.00 16.81           O  
HETATM 5497  O   HOH C 563     -24.027 -24.070 -48.997  1.00 20.38           O  
HETATM 5498  O   HOH C 564     -10.665 -10.900 -67.221  1.00  8.92           O  
HETATM 5499  O   HOH C 565     -22.101 -24.638 -64.262  1.00 20.22           O  
HETATM 5500  O   HOH C 566     -13.864  -1.314 -70.790  1.00 27.58           O  
HETATM 5501  O   HOH C 567      -5.409 -16.235 -50.629  1.00 14.62           O  
HETATM 5502  O   HOH C 568      -9.448  -5.680 -71.554  1.00 18.09           O  
HETATM 5503  O   HOH C 569     -10.683  -2.642 -68.702  1.00 33.88           O  
HETATM 5504  O   HOH C 570       7.372 -27.128 -61.011  1.00 23.70           O  
HETATM 5505  O   HOH C 571     -29.133 -21.926 -57.375  1.00 23.24           O  
HETATM 5506  O   HOH C 572       1.622 -27.122 -59.911  1.00 26.93           O  
HETATM 5507  O   HOH C 573     -25.234 -24.601 -58.054  1.00 29.39           O  
HETATM 5508  O   HOH C 574      -7.857 -29.358 -54.093  1.00 23.69           O  
HETATM 5509  O   HOH C 575      -2.132 -20.354 -43.101  1.00 18.64           O  
HETATM 5510  O   HOH C 576     -13.753   1.664 -51.671  1.00 28.32           O  
HETATM 5511  O   HOH C 577     -15.723 -24.922 -66.917  1.00 14.53           O  
HETATM 5512  O   HOH C 578     -22.860  -9.983 -60.097  1.00 31.31           O  
HETATM 5513  O   HOH C 579     -19.751  -5.190 -50.283  1.00 36.66           O  
HETATM 5514  O   HOH C 580       1.874 -13.232 -61.750  1.00 31.06           O  
HETATM 5515  O   HOH C 581      -1.341  -2.249 -65.599  1.00 32.29           O  
HETATM 5516  O   HOH C 582     -19.508  -7.164 -65.085  1.00 22.65           O  
HETATM 5517  O   HOH C 583     -13.159   1.685 -61.793  1.00 43.93           O  
HETATM 5518  O   HOH C 584      19.464 -11.047 -64.430  1.00 37.15           O  
HETATM 5519  O   HOH C 585     -19.917 -21.285 -67.154  1.00 23.98           O  
HETATM 5520  O   HOH C 586      -4.102  -2.680 -50.029  1.00 17.07           O  
HETATM 5521  O   HOH C 587      -7.058   4.580 -52.843  1.00 39.69           O  
HETATM 5522  O   HOH C 588     -14.583   4.012 -53.038  1.00 21.36           O  
HETATM 5523  O   HOH C 589       2.752  -3.572 -58.390  1.00 37.66           O  
HETATM 5524  O   HOH C 590     -12.168   1.699 -49.871  1.00 30.25           O  
HETATM 5525  O   HOH C 591     -22.322 -16.138 -61.402  1.00 33.31           O  
HETATM 5526  O   HOH C 592      -8.489   2.162 -62.929  1.00 31.90           O  
HETATM 5527  O   HOH C 593       8.556 -25.021 -59.368  1.00 26.83           O  
HETATM 5528  O   HOH C 594      -6.764 -16.045 -48.298  1.00 30.32           O  
HETATM 5529  O   HOH C 595     -19.192 -16.798 -68.714  1.00 31.49           O  
HETATM 5530  O   HOH C 596     -12.427  -0.407 -63.305  1.00 26.63           O  
HETATM 5531  O   HOH C 597       2.935  -0.875 -58.162  1.00 39.97           O  
HETATM 5532  O  AHOH C 598     -13.428 -22.574 -69.562  0.50 12.73           O  
HETATM 5533  O  BHOH C 598     -14.563 -21.548 -70.459  0.50 10.82           O  
HETATM 5534  O   HOH C 599     -25.457 -28.023 -49.638  1.00 29.55           O  
HETATM 5535  O   HOH C 600     -12.745 -16.519 -73.301  1.00 38.27           O  
HETATM 5536  O   HOH C 601       7.557 -15.623 -66.309  1.00 34.78           O  
HETATM 5537  O   HOH C 602     -21.590 -23.314 -66.484  1.00 21.68           O  
HETATM 5538  O   HOH C 603     -13.868   1.084 -72.349  1.00 33.15           O  
HETATM 5539  O   HOH C 604     -16.288 -13.999 -71.180  1.00 27.42           O  
HETATM 5540  O   HOH C 605     -13.626 -14.346 -75.173  1.00 24.80           O  
HETATM 5541  O   HOH C 606     -17.285   2.940 -56.954  1.00 39.23           O  
HETATM 5542  O   HOH C 607      -6.690 -18.258 -43.939  1.00 44.81           O  
HETATM 5543  O   HOH C 608      -2.561  -1.041 -49.862  1.00 36.83           O  
HETATM 5544  O   HOH D 501      10.682 -24.734 -36.124  1.00 14.48           O  
HETATM 5545  O   HOH D 502     -12.104 -33.179 -70.256  1.00 26.23           O  
HETATM 5546  O   HOH D 503      10.730 -35.054 -39.382  1.00 31.08           O  
HETATM 5547  O   HOH D 504     -17.482 -30.049 -64.412  1.00 38.13           O  
HETATM 5548  O   HOH D 505      14.002  -5.402 -58.440  1.00 39.21           O  
HETATM 5549  O  AHOH D 506      11.573 -26.871 -58.797  0.50  8.15           O  
HETATM 5550  O  BHOH D 506      10.940 -24.999 -58.294  0.50  3.55           O  
HETATM 5551  O   HOH D 507      17.039 -27.645 -46.843  1.00 22.92           O  
HETATM 5552  O   HOH D 508       5.820  -8.547 -54.520  1.00 13.28           O  
HETATM 5553  O   HOH D 509      14.468 -25.381 -41.162  1.00 18.18           O  
HETATM 5554  O   HOH D 510      -4.431 -20.496 -41.956  1.00 27.82           O  
HETATM 5555  O   HOH D 511       0.493 -34.491 -36.943  1.00 27.11           O  
HETATM 5556  O   HOH D 512      16.976 -27.176 -43.855  1.00 30.10           O  
HETATM 5557  O   HOH D 513       4.096 -33.328 -37.157  1.00 32.14           O  
HETATM 5558  O   HOH D 514      -0.415 -24.245 -33.387  1.00 27.18           O  
HETATM 5559  O   HOH D 515      -6.617 -34.660 -44.155  1.00 31.91           O  
HETATM 5560  O   HOH D 516      -0.455 -30.211 -54.642  1.00 10.50           O  
HETATM 5561  O   HOH D 517      15.275 -26.380 -56.835  1.00 23.18           O  
HETATM 5562  O   HOH D 518      10.486  -8.274 -44.291  1.00 34.81           O  
HETATM 5563  O   HOH D 519      16.040 -25.398 -54.381  1.00 22.47           O  
HETATM 5564  O   HOH D 520      -3.411 -33.207 -50.127  1.00 16.64           O  
HETATM 5565  O   HOH D 521      19.506 -21.789 -47.728  1.00 22.93           O  
HETATM 5566  O   HOH D 522      -1.662 -21.355 -37.488  1.00 19.27           O  
HETATM 5567  O   HOH D 523      -5.813 -24.436 -66.834  1.00 37.61           O  
HETATM 5568  O   HOH D 524       3.886 -13.027 -42.244  1.00 16.56           O  
HETATM 5569  O   HOH D 525      17.316 -17.095 -43.505  1.00 23.41           O  
HETATM 5570  O   HOH D 526      12.837 -34.881 -57.530  1.00 28.36           O  
HETATM 5571  O   HOH D 527      -8.839  -9.600 -57.226  1.00 17.26           O  
HETATM 5572  O   HOH D 528      -9.313 -10.369 -59.800  1.00 13.17           O  
HETATM 5573  O   HOH D 529       6.579 -19.172 -35.786  1.00 27.04           O  
HETATM 5574  O   HOH D 530      10.643  -9.355 -50.229  1.00 19.24           O  
HETATM 5575  O   HOH D 531      -3.968 -21.177 -64.561  1.00 15.24           O  
HETATM 5576  O   HOH D 532      20.814 -19.960 -50.024  1.00 33.26           O  
HETATM 5577  O   HOH D 533      -6.962 -19.755 -68.121  1.00 25.64           O  
HETATM 5578  O   HOH D 534      13.684  -8.304 -56.382  1.00 20.49           O  
HETATM 5579  O   HOH D 535       9.216 -33.932 -41.771  1.00 24.06           O  
HETATM 5580  O   HOH D 536      -6.079 -12.484 -62.277  1.00 11.68           O  
HETATM 5581  O   HOH D 537      -3.984 -34.811 -37.561  1.00 32.75           O  
HETATM 5582  O   HOH D 538      10.272 -32.765 -60.778  1.00 27.73           O  
HETATM 5583  O   HOH D 539       9.406  -7.313 -48.273  1.00 31.15           O  
HETATM 5584  O   HOH D 540       6.034 -34.263 -47.246  1.00 30.31           O  
HETATM 5585  O   HOH D 541      11.694 -11.431 -43.777  1.00 18.55           O  
HETATM 5586  O   HOH D 542       3.412 -37.243 -41.127  1.00 38.72           O  
HETATM 5587  O   HOH D 543     -13.850 -30.609 -45.251  1.00 35.82           O  
HETATM 5588  O   HOH D 544      18.694 -21.471 -55.239  1.00 25.69           O  
HETATM 5589  O   HOH D 545       2.253 -36.478 -52.769  1.00 38.24           O  
HETATM 5590  O   HOH D 546      16.795 -19.733 -43.389  1.00 33.75           O  
HETATM 5591  O   HOH D 547      15.517 -11.940 -41.354  1.00 35.48           O  
HETATM 5592  O   HOH D 548     -13.193 -26.171 -53.174  1.00 40.42           O  
HETATM 5593  O   HOH D 549      19.300  -8.223 -47.009  1.00 23.15           O  
HETATM 5594  O   HOH D 550     -10.530 -30.152 -50.836  1.00 26.91           O  
HETATM 5595  O   HOH D 551       5.796 -21.181 -33.686  1.00 32.96           O  
HETATM 5596  O   HOH D 552      16.106 -26.952 -50.635  1.00 15.87           O  
HETATM 5597  O   HOH D 553       1.600 -32.958 -52.309  1.00 17.61           O  
HETATM 5598  O   HOH D 554       3.896 -22.527 -32.342  1.00 28.43           O  
HETATM 5599  O   HOH D 555       0.984 -37.930 -50.035  1.00 33.44           O  
HETATM 5600  O   HOH D 556      10.562 -30.009 -50.288  1.00 10.42           O  
HETATM 5601  O   HOH D 557     -10.469  -8.496 -55.266  1.00  8.79           O  
HETATM 5602  O   HOH D 558      -7.084 -13.007 -47.697  1.00 22.49           O  
HETATM 5603  O   HOH D 559      16.455 -36.870 -55.183  1.00 37.06           O  
HETATM 5604  O   HOH D 560      14.617 -29.884 -41.673  1.00 27.22           O  
HETATM 5605  O   HOH D 561       7.247  -8.779 -47.166  1.00 18.42           O  
HETATM 5606  O   HOH D 562      -2.691 -34.471 -33.674  1.00 34.40           O  
HETATM 5607  O   HOH D 563       5.122  -8.974 -57.208  1.00 12.28           O  
HETATM 5608  O   HOH D 564      -0.420 -35.518 -55.990  1.00 35.79           O  
HETATM 5609  O   HOH D 565       3.159 -10.960 -61.306  1.00 18.59           O  
HETATM 5610  O   HOH D 566      -8.549 -20.988 -43.632  1.00 24.72           O  
HETATM 5611  O   HOH D 567      21.566 -14.536 -49.127  1.00 17.33           O  
HETATM 5612  O   HOH D 568     -10.367 -21.538 -68.112  1.00 23.34           O  
HETATM 5613  O   HOH D 569       4.067 -34.506 -63.457  1.00 22.06           O  
HETATM 5614  O   HOH D 570      -8.264 -10.343 -49.780  1.00  9.26           O  
HETATM 5615  O   HOH D 571       4.514  -9.115 -46.978  1.00 20.86           O  
HETATM 5616  O   HOH D 572       9.029 -36.254 -49.664  1.00 26.26           O  
HETATM 5617  O   HOH D 573     -13.672 -25.020 -68.593  1.00 33.78           O  
HETATM 5618  O   HOH D 574      18.762 -10.218 -44.512  1.00 44.06           O  
HETATM 5619  O   HOH D 575     -12.757 -17.378 -47.610  1.00 30.38           O  
HETATM 5620  O   HOH D 576      11.478 -37.385 -50.342  1.00 36.45           O  
HETATM 5621  O   HOH D 577      19.627 -17.916 -54.576  1.00 26.97           O  
HETATM 5622  O   HOH D 578       1.906 -12.892 -43.857  1.00 13.68           O  
HETATM 5623  O   HOH D 579      15.364 -31.441 -44.269  1.00 24.20           O  
HETATM 5624  O   HOH D 580      10.749 -10.443 -41.382  1.00 31.43           O  
HETATM 5625  O   HOH D 581       7.508 -16.805 -35.030  1.00 35.45           O  
HETATM 5626  O   HOH D 582      12.282 -10.713 -39.250  1.00 45.19           O  
HETATM 5627  O   HOH D 583      12.034 -30.970 -59.849  1.00 32.30           O  
HETATM 5628  O   HOH D 584      -2.880 -15.445 -46.803  1.00 25.48           O  
HETATM 5629  O   HOH D 585      -7.130 -34.339 -49.960  1.00 38.83           O  
HETATM 5630  O   HOH D 586      -2.478 -34.678 -52.009  1.00 27.20           O  
HETATM 5631  O   HOH D 587       6.692 -34.764 -41.002  1.00 37.35           O  
HETATM 5632  O   HOH D 588      21.344 -10.003 -43.837  1.00 28.46           O  
HETATM 5633  O   HOH D 589      -0.187 -34.401 -53.394  1.00 30.39           O  
HETATM 5634  O   HOH D 590       8.000 -35.639 -47.320  1.00 37.78           O  
HETATM 5635  O   HOH D 591      -5.264 -15.922 -73.330  1.00 26.57           O  
HETATM 5636  O   HOH D 592      13.760 -12.910 -42.973  1.00 26.63           O  
HETATM 5637  O   HOH D 593     -11.213 -20.948 -43.788  1.00 35.55           O  
HETATM 5638  O   HOH D 594      -7.657 -32.111 -53.599  1.00 32.14           O  
HETATM 5639  O   HOH D 595      23.306 -13.699 -46.873  1.00 34.68           O  
HETATM 5640  O   HOH D 596       7.095  -6.166 -51.949  1.00 29.42           O  
HETATM 5641  O   HOH D 597      10.766 -24.389 -33.042  1.00 35.00           O  
HETATM 5642  O   HOH D 598       9.497 -35.253 -44.174  1.00 29.18           O  
HETATM 5643  O   HOH D 599       7.193 -36.245 -38.189  1.00 42.26           O  
HETATM 5644  O   HOH E 501     -20.343   3.616 -38.996  1.00 21.01           O  
HETATM 5645  O   HOH E 502      -0.990   9.630 -44.533  1.00 22.86           O  
HETATM 5646  O   HOH E 503      -6.519  33.009 -54.070  1.00 34.64           O  
HETATM 5647  O   HOH E 504      -4.931  29.705 -50.829  1.00 17.04           O  
HETATM 5648  O   HOH E 505     -26.288  14.880 -39.320  1.00 39.84           O  
HETATM 5649  O   HOH E 506       7.267  32.191 -41.267  1.00 33.03           O  
HETATM 5650  O   HOH E 507     -23.897   9.132 -39.935  1.00 16.01           O  
HETATM 5651  O   HOH E 508     -26.230  12.408 -38.714  1.00 27.19           O  
HETATM 5652  O   HOH E 509     -19.573  26.228 -39.144  1.00 23.44           O  
HETATM 5653  O   HOH E 510     -23.943   7.802 -43.899  1.00 38.55           O  
HETATM 5654  O   HOH E 511     -27.662  10.848 -60.990  1.00 32.89           O  
HETATM 5655  O   HOH E 512     -28.923  14.368 -45.428  1.00 19.86           O  
HETATM 5656  O   HOH E 513     -25.251  21.751 -43.506  1.00 25.40           O  
HETATM 5657  O   HOH E 514      -5.908  23.530 -40.207  1.00 38.08           O  
HETATM 5658  O   HOH E 515      -3.211  14.305 -31.901  1.00 33.19           O  
HETATM 5659  O   HOH E 516     -15.077  16.721 -59.823  1.00 19.78           O  
HETATM 5660  O   HOH E 517      -5.606   4.711 -35.765  1.00 27.82           O  
HETATM 5661  O   HOH E 518     -25.149  18.480 -41.261  1.00 18.59           O  
HETATM 5662  O   HOH E 519     -19.783  18.942 -38.077  1.00 12.58           O  
HETATM 5663  O   HOH E 520     -24.375  24.326 -43.202  1.00 33.71           O  
HETATM 5664  O   HOH E 521      -9.980   6.223 -29.584  1.00 15.95           O  
HETATM 5665  O   HOH E 522      -3.429  32.710 -48.409  1.00 30.67           O  
HETATM 5666  O   HOH E 523     -20.217  12.836 -58.167  1.00 24.50           O  
HETATM 5667  O   HOH E 524       0.038  22.247 -59.522  1.00  9.64           O  
HETATM 5668  O   HOH E 525     -19.929   7.117 -57.007  1.00 34.80           O  
HETATM 5669  O   HOH E 526     -15.232  17.435 -33.038  1.00 25.50           O  
HETATM 5670  O   HOH E 527      -9.644   1.552 -35.761  1.00 23.27           O  
HETATM 5671  O   HOH E 528     -30.769  13.247 -52.725  1.00 22.91           O  
HETATM 5672  O   HOH E 529     -30.360  16.059 -47.443  1.00 20.89           O  
HETATM 5673  O   HOH E 530       4.282  27.315 -38.218  1.00 22.43           O  
HETATM 5674  O   HOH E 531      -9.268  26.617 -56.913  1.00 26.62           O  
HETATM 5675  O   HOH E 532      -3.169  25.120 -58.340  1.00 11.13           O  
HETATM 5676  O   HOH E 533     -13.031  24.216 -59.388  1.00 26.21           O  
HETATM 5677  O   HOH E 534      -4.464   6.109 -37.910  1.00 24.10           O  
HETATM 5678  O   HOH E 535       1.541  34.472 -31.831  1.00 33.09           O  
HETATM 5679  O   HOH E 536     -13.951   9.980 -57.150  1.00 15.60           O  
HETATM 5680  O   HOH E 537     -23.137  18.841 -60.699  1.00 30.07           O  
HETATM 5681  O   HOH E 538      -2.318  32.616 -52.814  1.00 16.99           O  
HETATM 5682  O   HOH E 539     -20.994   7.243 -53.911  1.00 17.70           O  
HETATM 5683  O   HOH E 540     -13.194   3.108 -44.952  1.00 33.19           O  
HETATM 5684  O   HOH E 541     -17.963  20.851 -31.667  1.00 31.69           O  
HETATM 5685  O   HOH E 542     -20.807  11.091 -30.015  1.00 25.17           O  
HETATM 5686  O   HOH E 543     -18.947   2.070 -47.957  1.00 37.22           O  
HETATM 5687  O   HOH E 544     -28.132   8.249 -55.414  1.00 38.61           O  
HETATM 5688  O  AHOH E 545     -26.382   8.574 -48.626  0.50  4.01           O  
HETATM 5689  O  BHOH E 545     -28.634   7.967 -48.974  0.50 15.54           O  
HETATM 5690  O  AHOH E 546       3.654  33.087 -36.354  0.60 16.45           O  
HETATM 5691  O  BHOH E 546       3.408  32.379 -34.538  0.40 11.27           O  
HETATM 5692  O   HOH E 547     -15.543   2.202 -44.064  1.00 32.12           O  
HETATM 5693  O   HOH E 548      -1.892   8.037 -41.283  1.00 23.23           O  
HETATM 5694  O   HOH E 549      -4.598  34.362 -55.029  1.00 32.71           O  
HETATM 5695  O   HOH E 550      -5.456  19.158 -34.768  1.00 40.56           O  
HETATM 5696  O   HOH E 551     -13.248   6.190 -51.680  1.00 18.28           O  
HETATM 5697  O   HOH E 552     -14.770  -0.840 -37.099  1.00 31.40           O  
HETATM 5698  O   HOH E 553     -14.421  29.086 -45.193  1.00 32.20           O  
HETATM 5699  O   HOH E 554     -18.841  11.900 -31.487  1.00 18.90           O  
HETATM 5700  O   HOH E 555      -2.234  11.343 -53.693  1.00 20.10           O  
HETATM 5701  O   HOH E 556     -10.859  22.988 -32.941  1.00 28.33           O  
HETATM 5702  O   HOH E 557     -12.107   3.417 -29.460  1.00 12.19           O  
HETATM 5703  O   HOH E 558     -30.513  12.302 -44.384  1.00 32.43           O  
HETATM 5704  O   HOH E 559       1.213  17.236 -60.116  1.00  8.94           O  
HETATM 5705  O   HOH E 560      -0.378  19.437 -59.628  1.00 14.34           O  
HETATM 5706  O   HOH E 561      -8.399  17.706 -29.824  1.00 33.48           O  
HETATM 5707  O   HOH E 562     -14.479  19.426 -60.405  1.00 18.97           O  
HETATM 5708  O   HOH E 563     -16.558   9.481 -57.596  1.00 25.66           O  
HETATM 5709  O   HOH E 564       1.325  18.957 -38.087  1.00 19.68           O  
HETATM 5710  O   HOH E 565     -15.015  14.129 -29.978  1.00 34.45           O  
HETATM 5711  O   HOH E 566     -28.709   9.779 -58.139  1.00 27.75           O  
HETATM 5712  O   HOH E 567     -10.687  21.735 -36.079  1.00 18.07           O  
HETATM 5713  O   HOH E 568     -19.916   0.031 -44.360  1.00 48.01           O  
HETATM 5714  O   HOH E 569     -24.029  20.155 -64.346  1.00 41.06           O  
HETATM 5715  O   HOH E 570       3.609  12.750 -49.320  1.00 27.60           O  
HETATM 5716  O   HOH E 571      -1.035  12.539 -56.694  1.00 18.17           O  
HETATM 5717  O   HOH E 572       1.133  38.027 -42.079  1.00 29.09           O  
HETATM 5718  O   HOH E 573       0.975  33.329 -50.954  1.00 22.93           O  
HETATM 5719  O   HOH E 574     -24.599  13.569 -34.948  1.00 24.32           O  
HETATM 5720  O   HOH E 575     -11.112  24.617 -57.466  1.00 15.80           O  
HETATM 5721  O   HOH E 576      -9.750  20.841 -30.365  1.00 26.47           O  
HETATM 5722  O   HOH E 577     -12.400  13.036 -28.375  1.00 26.42           O  
HETATM 5723  O   HOH E 578     -22.654   8.625 -32.626  1.00 36.58           O  
HETATM 5724  O   HOH E 579     -28.744  19.565 -50.968  1.00 31.97           O  
HETATM 5725  O   HOH E 580     -20.598  28.512 -39.452  1.00 28.83           O  
HETATM 5726  O   HOH E 581     -15.725  30.345 -31.342  1.00 35.29           O  
HETATM 5727  O   HOH E 582       1.159  36.508 -44.347  1.00 28.97           O  
HETATM 5728  O   HOH E 583      -9.106   9.046 -30.042  1.00 14.72           O  
HETATM 5729  O   HOH E 584     -24.232  11.048 -35.897  1.00 33.82           O  
HETATM 5730  O   HOH E 585     -24.785  20.999 -46.775  1.00 28.24           O  
HETATM 5731  O   HOH E 586     -17.162   0.636 -46.005  1.00 31.44           O  
HETATM 5732  O   HOH E 587     -13.205  32.914 -37.597  1.00 23.42           O  
HETATM 5733  O   HOH E 588      -9.040  14.320 -24.695  1.00 39.12           O  
HETATM 5734  O   HOH E 589      -6.763  21.681 -34.284  1.00 29.04           O  
HETATM 5735  O   HOH E 590     -19.640   4.859 -53.948  1.00 27.80           O  
HETATM 5736  O   HOH E 591      -1.737  17.325 -31.901  1.00 28.46           O  
HETATM 5737  O   HOH E 592     -31.790  10.434 -45.901  1.00 38.41           O  
HETATM 5738  O   HOH E 593      -1.812  22.292 -37.206  1.00 33.02           O  
HETATM 5739  O   HOH E 594      -3.172  20.061 -34.096  1.00 30.23           O  
HETATM 5740  O   HOH E 595      -8.904  23.069 -34.757  1.00 20.54           O  
HETATM 5741  O   HOH E 596      -2.764  12.014 -51.071  1.00 34.29           O  
HETATM 5742  O   HOH E 597     -23.988   6.956 -48.472  1.00 34.60           O  
HETATM 5743  O   HOH E 598     -23.302   7.358 -52.396  1.00 30.68           O  
HETATM 5744  O   HOH E 599      -6.230   9.864 -55.117  1.00 30.25           O  
HETATM 5745  O   HOH E 600      -7.332  30.835 -48.600  1.00 32.56           O  
HETATM 5746  O   HOH E 601     -32.309  10.820 -52.340  1.00 26.79           O  
HETATM 5747  O   HOH E 602      -6.770   9.435 -29.012  1.00 39.62           O  
HETATM 5748  O   HOH E 603     -11.940   5.129 -49.552  1.00 34.70           O  
HETATM 5749  O   HOH E 604      -8.795   4.317 -45.902  1.00 44.13           O  
HETATM 5750  O   HOH E 605       4.616  12.556 -45.398  1.00 48.58           O  
HETATM 5751  O   HOH E 606      -3.525   9.603 -55.301  1.00 34.61           O  
HETATM 5752  O   HOH E 607     -17.609  13.654 -30.118  1.00 21.59           O  
HETATM 5753  O   HOH E 608      -1.410  24.516 -34.503  1.00 32.42           O  
HETATM 5754  O   HOH E 609       3.797  11.027 -42.790  1.00 32.61           O  
HETATM 5755  O   HOH E 610      -1.694   7.668 -35.314  1.00 40.92           O  
HETATM 5756  O   HOH F 501      -9.574  24.771 -60.236  1.00 19.63           O  
HETATM 5757  O   HOH F 502     -24.085  29.899 -55.085  1.00 39.89           O  
HETATM 5758  O   HOH F 503       8.384  28.874 -65.184  1.00 16.33           O  
HETATM 5759  O   HOH F 504      -3.179  34.375 -58.700  1.00 14.16           O  
HETATM 5760  O   HOH F 505     -12.831  34.563 -59.590  1.00 26.02           O  
HETATM 5761  O   HOH F 506       8.993  30.616 -59.945  1.00 20.86           O  
HETATM 5762  O   HOH F 507      -2.088  10.192 -64.937  1.00 29.93           O  
HETATM 5763  O   HOH F 508     -20.230  24.979 -45.045  1.00 21.78           O  
HETATM 5764  O   HOH F 509      -8.234  15.816 -69.275  1.00 28.84           O  
HETATM 5765  O   HOH F 510      -8.953  35.840 -65.306  1.00 30.65           O  
HETATM 5766  O   HOH F 511      13.915  25.557 -51.679  1.00 34.82           O  
HETATM 5767  O   HOH F 512      -9.609  20.646 -65.060  1.00 22.59           O  
HETATM 5768  O   HOH F 513      -1.316  25.612 -66.621  1.00 28.18           O  
HETATM 5769  O   HOH F 514      -1.694  30.123 -67.185  1.00 13.44           O  
HETATM 5770  O   HOH F 515     -26.714  20.161 -59.651  1.00 27.56           O  
HETATM 5771  O   HOH F 516       6.464  17.005 -44.148  1.00 27.92           O  
HETATM 5772  O   HOH F 517       7.115  21.885 -42.630  1.00 20.69           O  
HETATM 5773  O   HOH F 518      10.762  31.024 -54.055  1.00 24.49           O  
HETATM 5774  O   HOH F 519       4.570  35.602 -59.869  1.00 21.26           O  
HETATM 5775  O   HOH F 520      -6.673  21.987 -70.261  1.00 31.26           O  
HETATM 5776  O   HOH F 521      -2.204  10.273 -57.389  1.00 21.01           O  
HETATM 5777  O   HOH F 522     -16.621  14.113 -58.207  1.00 26.03           O  
HETATM 5778  O   HOH F 523     -21.215  22.584 -65.721  1.00 35.47           O  
HETATM 5779  O   HOH F 524       5.413   9.446 -66.122  1.00 34.27           O  
HETATM 5780  O   HOH F 525      13.558  25.964 -38.907  1.00 37.40           O  
HETATM 5781  O   HOH F 526      10.456  28.808 -60.960  1.00 24.72           O  
HETATM 5782  O   HOH F 527      11.095  24.323 -60.896  1.00 22.01           O  
HETATM 5783  O   HOH F 528      -7.702  27.352 -66.637  1.00 25.39           O  
HETATM 5784  O   HOH F 529     -11.824  10.574 -41.376  1.00  8.94           O  
HETATM 5785  O   HOH F 530       0.908  20.349 -40.507  1.00 16.01           O  
HETATM 5786  O   HOH F 531      -7.829   8.900 -53.148  1.00 37.58           O  
HETATM 5787  O   HOH F 532      -4.017  15.108 -51.213  1.00 12.90           O  
HETATM 5788  O   HOH F 533     -13.454  26.020 -61.100  1.00 23.84           O  
HETATM 5789  O   HOH F 534     -27.288  22.691 -60.599  1.00 35.25           O  
HETATM 5790  O   HOH F 535     -19.702  27.004 -49.838  1.00 24.85           O  
HETATM 5791  O   HOH F 536      12.690  30.797 -46.524  1.00 21.83           O  
HETATM 5792  O   HOH F 537       6.338  13.604 -49.733  1.00 21.91           O  
HETATM 5793  O   HOH F 538      15.801  21.535 -48.256  1.00 26.76           O  
HETATM 5794  O   HOH F 539     -13.794  19.424 -41.314  1.00  8.22           O  
HETATM 5795  O   HOH F 540       5.035  24.282 -68.816  1.00 13.21           O  
HETATM 5796  O   HOH F 541       8.812  19.117 -39.970  1.00 47.13           O  
HETATM 5797  O   HOH F 542       4.096  18.045 -70.461  1.00 23.04           O  
HETATM 5798  O   HOH F 543       4.507  15.142 -44.623  1.00 17.44           O  
HETATM 5799  O   HOH F 544      14.765  16.123 -43.439  1.00 28.17           O  
HETATM 5800  O  AHOH F 545      -7.710  28.952 -46.092  0.50  4.76           O  
HETATM 5801  O  BHOH F 545      -7.715  28.945 -44.590  0.50 19.36           O  
HETATM 5802  O   HOH F 546       0.751  12.659 -74.077  1.00 22.45           O  
HETATM 5803  O   HOH F 547      -8.553  22.837 -39.289  1.00 13.77           O  
HETATM 5804  O   HOH F 548       1.483  29.316 -61.230  1.00  9.59           O  
HETATM 5805  O   HOH F 549       6.013  32.305 -57.991  1.00 25.00           O  
HETATM 5806  O   HOH F 550     -10.656  11.484 -67.504  1.00 36.41           O  
HETATM 5807  O   HOH F 551      -5.737   9.553 -48.216  1.00 14.74           O  
HETATM 5808  O   HOH F 552      11.208  19.511 -47.095  1.00 21.11           O  
HETATM 5809  O   HOH F 553      -8.672  19.451 -67.645  1.00 30.86           O  
HETATM 5810  O   HOH F 554      -4.919   9.302 -61.129  1.00 27.01           O  
HETATM 5811  O   HOH F 555     -14.415  15.695 -62.561  1.00 20.41           O  
HETATM 5812  O   HOH F 556      15.092  26.318 -41.950  1.00 31.81           O  
HETATM 5813  O   HOH F 557     -14.260  15.083 -40.839  1.00 10.98           O  
HETATM 5814  O   HOH F 558      13.349  15.380 -54.678  1.00 23.90           O  
HETATM 5815  O   HOH F 559     -16.145  25.644 -47.952  1.00 15.31           O  
HETATM 5816  O   HOH F 560      -7.545  25.872 -69.037  1.00 26.30           O  
HETATM 5817  O   HOH F 561     -12.153  13.227 -41.332  1.00 13.38           O  
HETATM 5818  O   HOH F 562       0.159  32.196 -67.347  1.00 21.72           O  
HETATM 5819  O   HOH F 563      -6.974  13.850 -49.814  1.00 16.49           O  
HETATM 5820  O   HOH F 564      10.469  32.777 -50.660  1.00 24.31           O  
HETATM 5821  O   HOH F 565      -6.916  25.664 -63.431  1.00 19.94           O  
HETATM 5822  O   HOH F 566     -13.396  11.113 -67.851  1.00 35.93           O  
HETATM 5823  O   HOH F 567      -2.341  13.762 -72.585  1.00 31.84           O  
HETATM 5824  O   HOH F 568      -7.396   9.146 -45.282  1.00 14.24           O  
HETATM 5825  O   HOH F 569      -7.791  24.133 -42.113  1.00 27.93           O  
HETATM 5826  O   HOH F 570     -16.525  28.337 -43.998  1.00 25.82           O  
HETATM 5827  O   HOH F 571     -23.572  23.391 -47.745  1.00 19.83           O  
HETATM 5828  O   HOH F 572       4.633  33.610 -54.819  1.00 30.32           O  
HETATM 5829  O   HOH F 573      15.904  25.057 -45.117  1.00 33.83           O  
HETATM 5830  O   HOH F 574       6.644  23.359 -70.755  1.00 26.16           O  
HETATM 5831  O   HOH F 575      11.319  15.421 -64.464  1.00 49.52           O  
HETATM 5832  O   HOH F 576      -1.592  21.480 -39.961  1.00 14.91           O  
HETATM 5833  O   HOH F 577       7.107  33.566 -47.534  1.00 35.78           O  
HETATM 5834  O   HOH F 578      -4.271  18.129 -74.591  1.00 43.35           O  
HETATM 5835  O   HOH F 579      -6.492  36.751 -57.917  1.00 31.96           O  
HETATM 5836  O   HOH F 580     -11.359   7.674 -52.806  1.00 25.45           O  
HETATM 5837  O  AHOH F 581      18.066  28.240 -46.671  0.50 19.48           O  
HETATM 5838  O  BHOH F 581      17.434  29.836 -47.028  0.50 15.13           O  
HETATM 5839  O   HOH F 582      -0.349  14.967 -74.833  1.00 29.55           O  
HETATM 5840  O   HOH F 583       0.970  23.428 -70.491  1.00 29.62           O  
HETATM 5841  O   HOH F 584     -26.763  25.727 -52.638  1.00 35.10           O  
HETATM 5842  O   HOH F 585      11.188  18.086 -63.067  1.00 23.07           O  
HETATM 5843  O   HOH F 586      -4.991   5.085 -61.128  1.00 33.50           O  
HETATM 5844  O   HOH F 587       9.987  26.574 -64.397  1.00 26.10           O  
HETATM 5845  O   HOH F 588     -11.681  19.142 -65.734  1.00 36.71           O  
HETATM 5846  O   HOH F 589       7.139  34.287 -54.472  1.00 30.30           O  
HETATM 5847  O   HOH F 590      -3.821  36.744 -58.107  1.00 32.33           O  
HETATM 5848  O   HOH F 591     -22.194  26.660 -49.175  1.00 33.91           O  
HETATM 5849  O   HOH F 592      11.774  22.191 -50.328  1.00 34.87           O  
HETATM 5850  O   HOH F 593       3.228  22.192 -70.080  1.00 29.38           O  
HETATM 5851  O   HOH F 594      -0.346  27.902 -67.112  1.00 26.71           O  
HETATM 5852  O   HOH F 595      -9.312  25.630 -64.445  1.00 33.10           O  
HETATM 5853  O   HOH F 596       3.658  13.614 -73.946  1.00 31.91           O  
HETATM 5854  O   HOH F 597      -9.240   7.169 -51.296  1.00 30.57           O  
HETATM 5855  O   HOH F 598     -15.523  28.190 -49.202  1.00 41.52           O  
HETATM 5856  O   HOH F 599      -1.803  10.476 -46.892  1.00 31.32           O  
HETATM 5857  O   HOH F 600     -13.855  18.306 -64.732  1.00 36.80           O  
HETATM 5858  O   HOH F 601       6.908  34.349 -59.567  1.00 21.90           O  
HETATM 5859  O   HOH F 602      -0.027   8.885 -72.056  1.00 23.74           O  
HETATM 5860  O   HOH F 603      -7.443  10.592 -65.376  1.00 34.99           O  
HETATM 5861  O   HOH F 604      11.419  31.347 -44.407  1.00 36.54           O  
HETATM 5862  O   HOH F 605       9.441  34.214 -46.365  1.00 34.93           O  
HETATM 5863  O  AHOH F 606       5.006  30.983 -74.188  0.50  6.95           O  
HETATM 5864  O  BHOH F 606       4.339  30.594 -72.474  0.50 14.92           O  
HETATM 5865  O   HOH F 607      -5.935   2.597 -63.659  1.00 38.22           O  
HETATM 5866  O   HOH F 608     -14.923  20.413 -62.906  1.00 29.47           O  
HETATM 5867  O   HOH F 609      -3.480   8.636 -47.411  1.00 26.46           O  
MASTER      804    0    9   48   12    0    0    6 5827    6    0   60          
END                                                                             
HEADER    VIRAL PROTEIN                           19-APR-20   6WLC              
TITLE     CRYSTAL STRUCTURE OF NSP15 ENDORIBONUCLEASE FROM SARS COV-2 IN THE    
TITLE    2 COMPLEX WITH URIDINE-5'-MONOPHOSPHATE                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: URIDYLATE-SPECIFIC ENDORIBONUCLEASE;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NSP15 ENDORIBNUCLEASE;                                      
COMPND   5 EC: 3.1.-.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 GENE: REP, 1A-1B;                                                    
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: GOLD;                                     
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMCSG53                                   
KEYWDS    SARS CORONA VIRUS 2, ENDORIBONUCLEASE, COVID-19, STRUCTURAL GENOMICS, 
KEYWDS   2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID, VIRAL  
KEYWDS   3 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.KIM,N.MALTSEVA,R.JEDRZEJCZAK,M.ENDRES,C.CHANG,A.GODZIK,K.MICHALSKA, 
AUTHOR   2 A.JOACHIMIAK,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES   
AUTHOR   3 (CSGID)                                                              
REVDAT   3   10-JUN-20 6WLC    1       COMPND SOURCE REMARK DBREF               
REVDAT   3 2                   1       SEQADV SEQRES HELIX  SHEET               
REVDAT   3 3                   1       SITE   ATOM                              
REVDAT   2   06-MAY-20 6WLC    1       COMPND SOURCE DBREF  SEQADV              
REVDAT   1   29-APR-20 6WLC    0                                                
JRNL        AUTH   Y.KIM,N.MALTSEVA,R.JEDRZEJCZAK,M.ENDRES,A.GODZIK,            
JRNL        AUTH 2 K.MICHALSKA,A.JOACHIMIAK,                                    
JRNL        AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES        
JRNL        AUTH 4 (CSGID)                                                      
JRNL        TITL   CRYSTAL STRUCTURE OF NSP15 ENDORIBONUCLEASE FROM SARS COV-2  
JRNL        TITL 2 IN THE COMPLEX WITH URIDINE-5'-MONOPHOSPHATE                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.17.1_3660                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.63                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 129762                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.940                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6406                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 40.6300 -  5.6500    1.00     4244   204  0.1544 0.1847        
REMARK   3     2  5.6400 -  4.4800    1.00     4150   224  0.1334 0.1599        
REMARK   3     3  4.4800 -  3.9200    1.00     4156   216  0.1334 0.1510        
REMARK   3     4  3.9200 -  3.5600    1.00     4144   223  0.1550 0.1732        
REMARK   3     5  3.5600 -  3.3000    1.00     4077   256  0.1686 0.1945        
REMARK   3     6  3.3000 -  3.1100    1.00     4136   248  0.1773 0.2097        
REMARK   3     7  3.1100 -  2.9500    1.00     4137   204  0.1824 0.2043        
REMARK   3     8  2.9500 -  2.8200    1.00     4107   237  0.1910 0.2204        
REMARK   3     9  2.8200 -  2.7200    1.00     4130   216  0.1821 0.2067        
REMARK   3    10  2.7200 -  2.6200    1.00     4145   196  0.1809 0.1856        
REMARK   3    11  2.6200 -  2.5400    1.00     4132   193  0.1797 0.2092        
REMARK   3    12  2.5400 -  2.4700    1.00     4166   194  0.1787 0.1981        
REMARK   3    13  2.4700 -  2.4000    1.00     4150   198  0.1777 0.2204        
REMARK   3    14  2.4000 -  2.3400    1.00     4115   193  0.1769 0.1858        
REMARK   3    15  2.3400 -  2.2900    1.00     4086   224  0.1745 0.2142        
REMARK   3    16  2.2900 -  2.2400    1.00     4143   209  0.1810 0.2025        
REMARK   3    17  2.2400 -  2.2000    1.00     4148   193  0.1869 0.2160        
REMARK   3    18  2.2000 -  2.1600    1.00     4127   192  0.1910 0.2372        
REMARK   3    19  2.1600 -  2.1200    1.00     4145   192  0.2006 0.2209        
REMARK   3    20  2.1200 -  2.0800    1.00     4077   255  0.2078 0.2345        
REMARK   3    21  2.0800 -  2.0500    1.00     4114   200  0.2077 0.2559        
REMARK   3    22  2.0500 -  2.0200    1.00     4130   207  0.2133 0.2283        
REMARK   3    23  2.0200 -  1.9900    1.00     4136   186  0.2218 0.2502        
REMARK   3    24  1.9900 -  1.9600    1.00     4072   243  0.2340 0.2769        
REMARK   3    25  1.9600 -  1.9300    1.00     4129   227  0.2542 0.2886        
REMARK   3    26  1.9300 -  1.9100    1.00     4084   242  0.2666 0.3022        
REMARK   3    27  1.9100 -  1.8800    1.00     4028   231  0.2845 0.3090        
REMARK   3    28  1.8800 -  1.8600    0.99     4116   193  0.3082 0.3190        
REMARK   3    29  1.8600 -  1.8400    0.97     3954   239  0.3348 0.3427        
REMARK   3    30  1.8400 -  1.8200    0.94     3878   171  0.3524 0.3684        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.233            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.770           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.46                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           5946                                  
REMARK   3   ANGLE     :  0.762           8068                                  
REMARK   3   CHIRALITY :  0.057            917                                  
REMARK   3   PLANARITY :  0.005           1038                                  
REMARK   3   DIHEDRAL  : 19.102           2202                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 197 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  60.6565 -23.4994 -14.5239              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2680 T22:   0.2532                                     
REMARK   3      T33:   0.4518 T12:   0.0237                                     
REMARK   3      T13:   0.0121 T23:   0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2443 L22:   1.6673                                     
REMARK   3      L33:   1.1331 L12:   0.6311                                     
REMARK   3      L13:  -0.5173 L23:  -0.6836                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0875 S12:  -0.0088 S13:   0.3807                       
REMARK   3      S21:   0.0640 S22:   0.0664 S23:   0.2953                       
REMARK   3      S31:  -0.1897 S32:  -0.1489 S33:  -0.1569                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 198 THROUGH 225 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  79.3562 -24.2578 -43.9860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5200 T22:   0.2282                                     
REMARK   3      T33:   0.3525 T12:  -0.0055                                     
REMARK   3      T13:  -0.0492 T23:  -0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4635 L22:   4.9275                                     
REMARK   3      L33:   6.7516 L12:   0.1418                                     
REMARK   3      L13:  -0.6752 L23:  -0.1552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2419 S12:   0.6921 S13:  -0.6218                       
REMARK   3      S21:  -0.7841 S22:   0.1189 S23:   0.1936                       
REMARK   3      S31:   1.1396 S32:  -0.0388 S33:   0.1612                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 226 THROUGH 309 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  87.0133 -24.4001 -33.3291              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3961 T22:   0.2537                                     
REMARK   3      T33:   0.3999 T12:  -0.0056                                     
REMARK   3      T13:   0.0389 T23:   0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4783 L22:   1.9214                                     
REMARK   3      L33:   1.4309 L12:  -1.1973                                     
REMARK   3      L13:  -0.1535 L23:  -0.1467                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0322 S12:   0.0911 S13:  -0.0066                       
REMARK   3      S21:  -0.2804 S22:   0.0199 S23:  -0.0549                       
REMARK   3      S31:   0.1349 S32:   0.0682 S33:   0.0141                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 310 THROUGH 347 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  89.1195 -10.1401 -29.9023              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3600 T22:   0.2766                                     
REMARK   3      T33:   0.5178 T12:   0.0177                                     
REMARK   3      T13:   0.0123 T23:   0.0237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2991 L22:   3.1567                                     
REMARK   3      L33:   2.6738 L12:   1.4659                                     
REMARK   3      L13:  -2.0420 L23:  -0.5843                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1039 S12:  -0.1447 S13:   0.6285                       
REMARK   3      S21:  -0.0370 S22:   0.0716 S23:  -0.4015                       
REMARK   3      S31:   0.1212 S32:   0.2783 S33:  -0.1412                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 38 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  91.3470 -30.9709   7.7388              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2429 T22:   0.2988                                     
REMARK   3      T33:   0.3299 T12:   0.0238                                     
REMARK   3      T13:  -0.0119 T23:  -0.0354                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6851 L22:   4.1834                                     
REMARK   3      L33:   5.3026 L12:   1.4750                                     
REMARK   3      L13:   0.7913 L23:   2.1765                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0644 S12:   0.1015 S13:  -0.1060                       
REMARK   3      S21:   0.0197 S22:   0.1959 S23:  -0.3951                       
REMARK   3      S31:  -0.1734 S32:   0.3588 S33:  -0.1575                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 39 THROUGH 183 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  75.2287 -16.1678  15.7649              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2782 T22:   0.2345                                     
REMARK   3      T33:   0.3555 T12:  -0.0094                                     
REMARK   3      T13:  -0.0230 T23:  -0.0272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9910 L22:   1.7041                                     
REMARK   3      L33:   1.2029 L12:  -0.4786                                     
REMARK   3      L13:  -0.4289 L23:   0.6955                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0109 S12:  -0.0311 S13:   0.2012                       
REMARK   3      S21:   0.0613 S22:   0.0506 S23:  -0.0019                       
REMARK   3      S31:  -0.0898 S32:   0.0665 S33:  -0.0434                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 184 THROUGH 203 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  63.6053 -15.3790  27.1295              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4406 T22:   0.2994                                     
REMARK   3      T33:   0.4647 T12:   0.0051                                     
REMARK   3      T13:  -0.0123 T23:  -0.0771                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7002 L22:   7.6063                                     
REMARK   3      L33:   4.4337 L12:   1.2574                                     
REMARK   3      L13:  -0.8609 L23:  -6.2095                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2347 S12:  -0.2413 S13:   0.2167                       
REMARK   3      S21:   0.1330 S22:   0.0945 S23:   0.4931                       
REMARK   3      S31:  -0.0088 S32:   0.0726 S33:  -0.2332                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 204 THROUGH 236 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  56.1311 -28.0222  46.0494              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8541 T22:   0.5493                                     
REMARK   3      T33:   0.4170 T12:  -0.0563                                     
REMARK   3      T13:   0.1570 T23:  -0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5874 L22:   3.9222                                     
REMARK   3      L33:   3.7258 L12:   1.0542                                     
REMARK   3      L13:   0.7431 L23:   0.7462                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2400 S12:  -1.0418 S13:   0.0599                       
REMARK   3      S21:   1.4317 S22:  -0.2297 S23:   0.4963                       
REMARK   3      S31:   0.0991 S32:  -0.2396 S33:   0.0100                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 237 THROUGH 309 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  56.6054 -34.2534  32.0287              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4147 T22:   0.3342                                     
REMARK   3      T33:   0.3399 T12:  -0.0289                                     
REMARK   3      T13:   0.0643 T23:  -0.0194                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2398 L22:   4.6747                                     
REMARK   3      L33:   2.1821 L12:   1.2770                                     
REMARK   3      L13:  -0.5422 L23:  -0.3145                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0347 S12:  -0.1786 S13:  -0.0429                       
REMARK   3      S21:   0.3791 S22:  -0.0333 S23:   0.0099                       
REMARK   3      S31:   0.0969 S32:  -0.0112 S33:  -0.0087                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 310 THROUGH 347 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  46.0691 -22.0532  30.3950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4160 T22:   0.4592                                     
REMARK   3      T33:   0.6476 T12:  -0.0233                                     
REMARK   3      T13:   0.0811 T23:  -0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7480 L22:   5.2307                                     
REMARK   3      L33:   2.4340 L12:   3.3837                                     
REMARK   3      L13:  -1.3269 L23:  -1.7364                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0981 S12:   0.3501 S13:   0.7513                       
REMARK   3      S21:   0.1546 S22:   0.4292 S23:   1.2301                       
REMARK   3      S31:   0.1514 S32:  -0.6421 S33:  -0.3095                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6WLC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000248566.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-APR-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 X 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 130237                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.14700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.87900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: HKL-3000, MOLREP                                      
REMARK 200 STARTING MODEL: PDBID 6W01                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16 %(W/V) PEG400, 100 MM TRIS PH 8.5,    
REMARK 280  200 MM SODIUM ACETATE, VAPOR DIFFUSION, SITTING DROP,               
REMARK 280  TEMPERATURE 289K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       56.15200            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       56.15200            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       56.15200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 33130 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 83110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000       75.47850            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000     -130.73260            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000      150.95700            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     GLY A   -13                                                      
REMARK 465     VAL A   -12                                                      
REMARK 465     ASP A   -11                                                      
REMARK 465     LEU A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     THR A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     ASN A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     TYR A    -4                                                      
REMARK 465     PHE A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     MET B   -22                                                      
REMARK 465     HIS B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     SER B   -14                                                      
REMARK 465     GLY B   -13                                                      
REMARK 465     VAL B   -12                                                      
REMARK 465     ASP B   -11                                                      
REMARK 465     LEU B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     THR B    -8                                                      
REMARK 465     GLU B    -7                                                      
REMARK 465     ASN B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     TYR B    -4                                                      
REMARK 465     PHE B    -3                                                      
REMARK 465     GLN B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A   0    CG   OD1  ND2                                       
REMARK 470     ASN B   0    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    MET A   1     -138.81     63.57                                   
REMARK 500    SER A   2      141.93   -170.70                                   
REMARK 500    SER A   2      113.89   -170.94                                   
REMARK 500    ASN A  29     -114.38     51.67                                   
REMARK 500    ASN A  29       52.96     34.41                                   
REMARK 500    LEU A 249       66.95     65.75                                   
REMARK 500    MET B   1     -137.53     65.15                                   
REMARK 500    ASN B  29     -118.89     48.34                                   
REMARK 500    LEU B 249       64.13     68.35                                   
REMARK 500    ASP B 297       78.32   -104.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue U5P A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue U5P B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 411                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6VWW   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN, APP FORM                                           
REMARK 900 RELATED ID: 6W01   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH CITRATE                              
DBREF  6WLC A    2   347  UNP    P0DTD1   R1AB_SARS2    6453   6798             
DBREF  6WLC B    2   347  UNP    P0DTD1   R1AB_SARS2    6453   6798             
SEQADV 6WLC MET A  -22  UNP  P0DTD1              INITIATING METHIONINE          
SEQADV 6WLC HIS A  -21  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS A  -20  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS A  -19  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS A  -18  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS A  -17  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS A  -16  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC SER A  -15  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC SER A  -14  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLY A  -13  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC VAL A  -12  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC ASP A  -11  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC LEU A  -10  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLY A   -9  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC THR A   -8  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLU A   -7  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC ASN A   -6  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC LEU A   -5  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC TYR A   -4  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC PHE A   -3  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLN A   -2  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC SER A   -1  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC ASN A    0  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC MET A    1  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC MET B  -22  UNP  P0DTD1              INITIATING METHIONINE          
SEQADV 6WLC HIS B  -21  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS B  -20  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS B  -19  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS B  -18  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS B  -17  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS B  -16  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC SER B  -15  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC SER B  -14  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLY B  -13  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC VAL B  -12  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC ASP B  -11  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC LEU B  -10  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLY B   -9  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC THR B   -8  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLU B   -7  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC ASN B   -6  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC LEU B   -5  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC TYR B   -4  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC PHE B   -3  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLN B   -2  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC SER B   -1  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC ASN B    0  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC MET B    1  UNP  P0DTD1              EXPRESSION TAG                 
SEQRES   1 A  370  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  370  GLY THR GLU ASN LEU TYR PHE GLN SER ASN MET SER LEU          
SEQRES   3 A  370  GLU ASN VAL ALA PHE ASN VAL VAL ASN LYS GLY HIS PHE          
SEQRES   4 A  370  ASP GLY GLN GLN GLY GLU VAL PRO VAL SER ILE ILE ASN          
SEQRES   5 A  370  ASN THR VAL TYR THR LYS VAL ASP GLY VAL ASP VAL GLU          
SEQRES   6 A  370  LEU PHE GLU ASN LYS THR THR LEU PRO VAL ASN VAL ALA          
SEQRES   7 A  370  PHE GLU LEU TRP ALA LYS ARG ASN ILE LYS PRO VAL PRO          
SEQRES   8 A  370  GLU VAL LYS ILE LEU ASN ASN LEU GLY VAL ASP ILE ALA          
SEQRES   9 A  370  ALA ASN THR VAL ILE TRP ASP TYR LYS ARG ASP ALA PRO          
SEQRES  10 A  370  ALA HIS ILE SER THR ILE GLY VAL CYS SER MET THR ASP          
SEQRES  11 A  370  ILE ALA LYS LYS PRO THR GLU THR ILE CYS ALA PRO LEU          
SEQRES  12 A  370  THR VAL PHE PHE ASP GLY ARG VAL ASP GLY GLN VAL ASP          
SEQRES  13 A  370  LEU PHE ARG ASN ALA ARG ASN GLY VAL LEU ILE THR GLU          
SEQRES  14 A  370  GLY SER VAL LYS GLY LEU GLN PRO SER VAL GLY PRO LYS          
SEQRES  15 A  370  GLN ALA SER LEU ASN GLY VAL THR LEU ILE GLY GLU ALA          
SEQRES  16 A  370  VAL LYS THR GLN PHE ASN TYR TYR LYS LYS VAL ASP GLY          
SEQRES  17 A  370  VAL VAL GLN GLN LEU PRO GLU THR TYR PHE THR GLN SER          
SEQRES  18 A  370  ARG ASN LEU GLN GLU PHE LYS PRO ARG SER GLN MET GLU          
SEQRES  19 A  370  ILE ASP PHE LEU GLU LEU ALA MET ASP GLU PHE ILE GLU          
SEQRES  20 A  370  ARG TYR LYS LEU GLU GLY TYR ALA PHE GLU HIS ILE VAL          
SEQRES  21 A  370  TYR GLY ASP PHE SER HIS SER GLN LEU GLY GLY LEU HIS          
SEQRES  22 A  370  LEU LEU ILE GLY LEU ALA LYS ARG PHE LYS GLU SER PRO          
SEQRES  23 A  370  PHE GLU LEU GLU ASP PHE ILE PRO MET ASP SER THR VAL          
SEQRES  24 A  370  LYS ASN TYR PHE ILE THR ASP ALA GLN THR GLY SER SER          
SEQRES  25 A  370  LYS CYS VAL CYS SER VAL ILE ASP LEU LEU LEU ASP ASP          
SEQRES  26 A  370  PHE VAL GLU ILE ILE LYS SER GLN ASP LEU SER VAL VAL          
SEQRES  27 A  370  SER LYS VAL VAL LYS VAL THR ILE ASP TYR THR GLU ILE          
SEQRES  28 A  370  SER PHE MET LEU TRP CYS LYS ASP GLY HIS VAL GLU THR          
SEQRES  29 A  370  PHE TYR PRO LYS LEU GLN                                      
SEQRES   1 B  370  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  370  GLY THR GLU ASN LEU TYR PHE GLN SER ASN MET SER LEU          
SEQRES   3 B  370  GLU ASN VAL ALA PHE ASN VAL VAL ASN LYS GLY HIS PHE          
SEQRES   4 B  370  ASP GLY GLN GLN GLY GLU VAL PRO VAL SER ILE ILE ASN          
SEQRES   5 B  370  ASN THR VAL TYR THR LYS VAL ASP GLY VAL ASP VAL GLU          
SEQRES   6 B  370  LEU PHE GLU ASN LYS THR THR LEU PRO VAL ASN VAL ALA          
SEQRES   7 B  370  PHE GLU LEU TRP ALA LYS ARG ASN ILE LYS PRO VAL PRO          
SEQRES   8 B  370  GLU VAL LYS ILE LEU ASN ASN LEU GLY VAL ASP ILE ALA          
SEQRES   9 B  370  ALA ASN THR VAL ILE TRP ASP TYR LYS ARG ASP ALA PRO          
SEQRES  10 B  370  ALA HIS ILE SER THR ILE GLY VAL CYS SER MET THR ASP          
SEQRES  11 B  370  ILE ALA LYS LYS PRO THR GLU THR ILE CYS ALA PRO LEU          
SEQRES  12 B  370  THR VAL PHE PHE ASP GLY ARG VAL ASP GLY GLN VAL ASP          
SEQRES  13 B  370  LEU PHE ARG ASN ALA ARG ASN GLY VAL LEU ILE THR GLU          
SEQRES  14 B  370  GLY SER VAL LYS GLY LEU GLN PRO SER VAL GLY PRO LYS          
SEQRES  15 B  370  GLN ALA SER LEU ASN GLY VAL THR LEU ILE GLY GLU ALA          
SEQRES  16 B  370  VAL LYS THR GLN PHE ASN TYR TYR LYS LYS VAL ASP GLY          
SEQRES  17 B  370  VAL VAL GLN GLN LEU PRO GLU THR TYR PHE THR GLN SER          
SEQRES  18 B  370  ARG ASN LEU GLN GLU PHE LYS PRO ARG SER GLN MET GLU          
SEQRES  19 B  370  ILE ASP PHE LEU GLU LEU ALA MET ASP GLU PHE ILE GLU          
SEQRES  20 B  370  ARG TYR LYS LEU GLU GLY TYR ALA PHE GLU HIS ILE VAL          
SEQRES  21 B  370  TYR GLY ASP PHE SER HIS SER GLN LEU GLY GLY LEU HIS          
SEQRES  22 B  370  LEU LEU ILE GLY LEU ALA LYS ARG PHE LYS GLU SER PRO          
SEQRES  23 B  370  PHE GLU LEU GLU ASP PHE ILE PRO MET ASP SER THR VAL          
SEQRES  24 B  370  LYS ASN TYR PHE ILE THR ASP ALA GLN THR GLY SER SER          
SEQRES  25 B  370  LYS CYS VAL CYS SER VAL ILE ASP LEU LEU LEU ASP ASP          
SEQRES  26 B  370  PHE VAL GLU ILE ILE LYS SER GLN ASP LEU SER VAL VAL          
SEQRES  27 B  370  SER LYS VAL VAL LYS VAL THR ILE ASP TYR THR GLU ILE          
SEQRES  28 B  370  SER PHE MET LEU TRP CYS LYS ASP GLY HIS VAL GLU THR          
SEQRES  29 B  370  PHE TYR PRO LYS LEU GLN                                      
HET    U5P  A 401      21                                                       
HET    TRS  A 402       8                                                       
HET    EDO  A 403       4                                                       
HET    ACT  A 404       4                                                       
HET    EDO  A 405       4                                                       
HET    EDO  A 406       4                                                       
HET    EDO  A 407       4                                                       
HET    EDO  A 408       4                                                       
HET    EDO  A 409       4                                                       
HET    SO4  A 410       5                                                       
HET    U5P  B 401      21                                                       
HET    TRS  B 402       8                                                       
HET    EDO  B 403       4                                                       
HET    EDO  B 404       4                                                       
HET    ACT  B 405       4                                                       
HET    EDO  B 406       4                                                       
HET    ACT  B 407       4                                                       
HET    ACT  B 408       4                                                       
HET    FMT  B 409       3                                                       
HET    FMT  B 410       3                                                       
HET    EDO  B 411       4                                                       
HETNAM     U5P URIDINE-5'-MONOPHOSPHATE                                         
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     ACT ACETATE ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     FMT FORMIC ACID                                                      
HETSYN     TRS TRIS BUFFER                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  U5P    2(C9 H13 N2 O9 P)                                            
FORMUL   4  TRS    2(C4 H12 N O3 1+)                                            
FORMUL   5  EDO    10(C2 H6 O2)                                                 
FORMUL   6  ACT    4(C2 H3 O2 1-)                                               
FORMUL  12  SO4    O4 S 2-                                                      
FORMUL  21  FMT    2(C H2 O2)                                                   
FORMUL  24  HOH   *486(H2 O)                                                    
HELIX    1 AA1 SER A    2  GLY A   14  1                                  13    
HELIX    2 AA2 PRO A   51  LYS A   61  1                                  11    
HELIX    3 AA3 GLU A   69  LEU A   76  1                                   8    
HELIX    4 AA4 GLU A  114  ALA A  118  5                                   5    
HELIX    5 AA5 GLY A  130  ALA A  138  1                                   9    
HELIX    6 AA6 SER A  208  LEU A  217  1                                  10    
HELIX    7 AA7 ALA A  218  TYR A  226  1                                   9    
HELIX    8 AA8 ALA A  232  VAL A  237  1                                   6    
HELIX    9 AA9 LEU A  251  SER A  262  1                                  12    
HELIX   10 AB1 LEU A  299  LYS A  308  1                                  10    
HELIX   11 AB2 SER B    2  GLY B   14  1                                  13    
HELIX   12 AB3 PRO B   51  LYS B   61  1                                  11    
HELIX   13 AB4 GLU B   69  LEU B   76  1                                   8    
HELIX   14 AB5 GLU B  114  ALA B  118  5                                   5    
HELIX   15 AB6 GLY B  130  ALA B  138  1                                   9    
HELIX   16 AB7 SER B  208  LEU B  217  1                                  10    
HELIX   17 AB8 ALA B  218  TYR B  226  1                                   9    
HELIX   18 AB9 ALA B  232  VAL B  237  1                                   6    
HELIX   19 AC1 LEU B  251  SER B  262  1                                  12    
HELIX   20 AC2 LEU B  299  SER B  309  1                                  11    
SHEET    1 AA1 3 VAL A  25  ILE A  28  0                                        
SHEET    2 AA1 3 THR A  31  VAL A  36 -1  O  TYR A  33   N  SER A  26           
SHEET    3 AA1 3 VAL A  39  GLU A  45 -1  O  VAL A  39   N  VAL A  36           
SHEET    1 AA2 5 ILE A  80  ALA A  81  0                                        
SHEET    2 AA2 5 VAL A 122  ASP A 125  1  O  PHE A 123   N  ILE A  80           
SHEET    3 AA2 5 GLY A 141  THR A 145  1  O  VAL A 142   N  PHE A 124           
SHEET    4 AA2 5 ASN A 178  VAL A 183 -1  O  ASN A 178   N  THR A 145           
SHEET    5 AA2 5 SER A 155  VAL A 156 -1  N  SER A 155   O  TYR A 179           
SHEET    1 AA3 5 ILE A  80  ALA A  81  0                                        
SHEET    2 AA3 5 VAL A 122  ASP A 125  1  O  PHE A 123   N  ILE A  80           
SHEET    3 AA3 5 GLY A 141  THR A 145  1  O  VAL A 142   N  PHE A 124           
SHEET    4 AA3 5 ASN A 178  VAL A 183 -1  O  ASN A 178   N  THR A 145           
SHEET    5 AA3 5 VAL A 186  VAL A 187 -1  O  VAL A 186   N  VAL A 183           
SHEET    1 AA4 2 TRP A  87  ASP A  88  0                                        
SHEET    2 AA4 2 ALA A  93  PRO A  94 -1  O  ALA A  93   N  ASP A  88           
SHEET    1 AA5 2 THR A  99  ILE A 100  0                                        
SHEET    2 AA5 2 ASP A 107  ALA A 109  1  O  ILE A 108   N  THR A  99           
SHEET    1 AA6 2 ALA A 161  LEU A 163  0                                        
SHEET    2 AA6 2 VAL A 166  LEU A 168 -1  O  VAL A 166   N  LEU A 163           
SHEET    1 AA7 3 PHE A 264  GLU A 267  0                                        
SHEET    2 AA7 3 LYS A 277  ASP A 283 -1  O  THR A 282   N  GLU A 265           
SHEET    3 AA7 3 SER A 289  VAL A 295 -1  O  VAL A 295   N  LYS A 277           
SHEET    1 AA8 3 SER A 316  ILE A 323  0                                        
SHEET    2 AA8 3 THR A 326  LYS A 335 -1  O  PHE A 330   N  VAL A 319           
SHEET    3 AA8 3 HIS A 338  PRO A 344 -1  O  GLU A 340   N  TRP A 333           
SHEET    1 AA9 3 VAL B  25  ILE B  28  0                                        
SHEET    2 AA9 3 THR B  31  VAL B  36 -1  O  TYR B  33   N  SER B  26           
SHEET    3 AA9 3 VAL B  39  GLU B  45 -1  O  VAL B  39   N  VAL B  36           
SHEET    1 AB1 5 ILE B  80  ALA B  81  0                                        
SHEET    2 AB1 5 VAL B 122  ASP B 125  1  O  PHE B 123   N  ILE B  80           
SHEET    3 AB1 5 GLY B 141  THR B 145  1  O  VAL B 142   N  PHE B 124           
SHEET    4 AB1 5 ASN B 178  VAL B 183 -1  O  ASN B 178   N  THR B 145           
SHEET    5 AB1 5 SER B 155  VAL B 156 -1  N  SER B 155   O  TYR B 179           
SHEET    1 AB2 5 ILE B  80  ALA B  81  0                                        
SHEET    2 AB2 5 VAL B 122  ASP B 125  1  O  PHE B 123   N  ILE B  80           
SHEET    3 AB2 5 GLY B 141  THR B 145  1  O  VAL B 142   N  PHE B 124           
SHEET    4 AB2 5 ASN B 178  VAL B 183 -1  O  ASN B 178   N  THR B 145           
SHEET    5 AB2 5 VAL B 186  VAL B 187 -1  O  VAL B 186   N  VAL B 183           
SHEET    1 AB3 2 TRP B  87  ASP B  88  0                                        
SHEET    2 AB3 2 ALA B  93  PRO B  94 -1  O  ALA B  93   N  ASP B  88           
SHEET    1 AB4 2 THR B  99  ILE B 100  0                                        
SHEET    2 AB4 2 ASP B 107  ALA B 109  1  O  ILE B 108   N  THR B  99           
SHEET    1 AB5 2 ALA B 161  LEU B 163  0                                        
SHEET    2 AB5 2 VAL B 166  LEU B 168 -1  O  VAL B 166   N  LEU B 163           
SHEET    1 AB6 3 PHE B 264  GLU B 267  0                                        
SHEET    2 AB6 3 LYS B 277  ASP B 283 -1  O  THR B 282   N  GLU B 265           
SHEET    3 AB6 3 SER B 289  VAL B 295 -1  O  VAL B 295   N  LYS B 277           
SHEET    1 AB7 3 SER B 316  ILE B 323  0                                        
SHEET    2 AB7 3 THR B 326  LYS B 335 -1  O  PHE B 330   N  VAL B 319           
SHEET    3 AB7 3 HIS B 338  PRO B 344 -1  O  GLU B 340   N  TRP B 333           
SITE     1 AC1 10 HIS A 250  LYS A 290  VAL A 292  CYS A 293                    
SITE     2 AC1 10 SER A 294  TYR A 343  LEU A 346  HOH A 540                    
SITE     3 AC1 10 HOH A 646  HOH A 655                                          
SITE     1 AC2  5 PHE A  44  GLU A  45  ASP A  92  HOH A 509                    
SITE     2 AC2  5 HOH A 661                                                     
SITE     1 AC3  9 ASN A   0  ASN A  53  GLU A  57  CYS A 103                    
SITE     2 AC3  9 SER A 104  MET A 105  GLU B   4  PRO B  24                    
SITE     3 AC3  9 VAL B  25                                                     
SITE     1 AC4  2 GLU A 340  HOH A 646                                          
SITE     1 AC5  3 ASN A 200  LEU A 201  TYR A 279                               
SITE     1 AC6  5 ASN A  74  VAL A  78  ASP A  79  HOH A 511                    
SITE     2 AC6  5 HOH A 533                                                     
SITE     1 AC7  6 LEU A 312  SER A 313  VAL A 314  LYS A 335                    
SITE     2 AC7  6 ASP A 336  GLY A 337                                          
SITE     1 AC8  5 GLU A  69  VAL A  70  TYR A  89  LYS A  90                    
SITE     2 AC8  5 ASP A 273                                                     
SITE     1 AC9  4 ASN A  75  LEU A  76  LYS A 181  TYR A 325                    
SITE     1 AD1  7 GLU A 229  GLY A 230  TYR A 231  GLY A 337                    
SITE     2 AD1  7 HIS A 338  HOH A 513  HOH A 688                               
SITE     1 AD2  9 HIS B 250  LYS B 290  VAL B 292  CYS B 293                    
SITE     2 AD2  9 SER B 294  TYR B 343  LEU B 346  HOH B 592                    
SITE     3 AD2  9 HOH B 660                                                     
SITE     1 AD3  7 PHE B  44  GLU B  45  TRP B  59  ASP B  92                    
SITE     2 AD3  7 FMT B 410  EDO B 411  HOH B 543                               
SITE     1 AD4  8 LYS A 320  VAL A 321  THR A 322  GLU A 327                    
SITE     2 AD4  8 VAL B 149  LYS B 150  GLY B 151  HOH B 692                    
SITE     1 AD5  4 SER B 155  VAL B 156  GLU B 192  THR B 193                    
SITE     1 AD6  7 LEU B 312  SER B 313  VAL B 314  VAL B 315                    
SITE     2 AD6  7 LYS B 335  ASP B 336  GLY B 337                               
SITE     1 AD7  5 GLU B 192  LYS B 320  THR B 322  GLU B 327                    
SITE     2 AD7  5 HOH B 681                                                     
SITE     1 AD8  4 GLU B 146  LYS B 174  GLN B 176  ASN B 178                    
SITE     1 AD9  7 GLU A 192  GLY B 126  THR B 145  GLY B 147                    
SITE     2 AD9  7 SER B 148  VAL B 149  HOH B 571                               
SITE     1 AE1  2 GLU B  42  HOH B 643                                          
SITE     1 AE2  5 ASP B  92  TRS B 402  EDO B 411  HOH B 513                    
SITE     2 AE2  5 HOH B 537                                                     
SITE     1 AE3  3 GLU B  45  TRS B 402  FMT B 410                               
CRYST1  150.957  150.957  112.304  90.00  90.00 120.00 P 63         12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006624  0.003825  0.000000        0.00000                         
SCALE2      0.000000  0.007649  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008904        0.00000                         
ATOM      1  N  AASN A   0      46.055 -31.384  -2.121  0.56 74.44           N  
ANISOU    1  N  AASN A   0     8134   9188  10962    308   1181    100       N  
ATOM      2  N  BASN A   0      54.569 -29.955   2.502  0.44 35.82           N  
ANISOU    2  N  BASN A   0     4303   4313   4995    -96   1093   -589       N  
ATOM      3  CA AASN A   0      47.039 -31.759  -1.112  0.56 67.29           C  
ANISOU    3  CA AASN A   0     7396   8303   9868    245   1204    -12       C  
ATOM      4  CA BASN A   0      53.212 -30.170   2.033  0.44 52.71           C  
ANISOU    4  CA BASN A   0     6315   6433   7280    -18   1156   -519       C  
ATOM      5  C  AASN A   0      48.291 -32.360  -1.756  0.56 67.28           C  
ANISOU    5  C  AASN A   0     7482   8338   9744    185   1024    -23       C  
ATOM      6  C  BASN A   0      53.191 -30.887   0.686  0.44 54.29           C  
ANISOU    6  C  BASN A   0     6406   6659   7564     15   1009   -410       C  
ATOM      7  O  AASN A   0      48.238 -33.389  -2.432  0.56 67.38           O  
ANISOU    7  O  AASN A   0     7454   8405   9742    143    897     47       O  
ATOM      8  O  BASN A   0      54.212 -31.399   0.232  0.44 64.76           O  
ANISOU    8  O  BASN A   0     7762   8021   8824    -22    872   -390       O  
ATOM      9  CB AASN A   0      46.429 -32.729  -0.114  0.56 70.09           C  
ANISOU    9  CB AASN A   0     7747   8717  10166    199   1280     -6       C  
ATOM     10  CB BASN A   0      52.469 -28.846   1.944  0.44 58.28           C  
ANISOU   10  CB BASN A   0     6992   7032   8121     56   1305   -560       C  
ATOM     11  N  AMET A   1      49.421 -31.700  -1.533  0.56 68.09           N  
ANISOU   11  N  AMET A   1     7705   8404   9761    178   1021   -112       N  
ATOM     12  N  BMET A   1      52.023 -30.895   0.054  0.44 56.96           N  
ANISOU   12  N  BMET A   1     6617   6975   8048     80   1042   -338       N  
ATOM     13  CA AMET A   1      50.680 -32.088  -2.148  0.56 62.19           C  
ANISOU   13  CA AMET A   1     7033   7680   8916    133    869   -122       C  
ATOM     14  CA BMET A   1      51.748 -31.651  -1.184  0.44 60.59           C  
ANISOU   14  CA BMET A   1     6973   7465   8584     97    912   -231       C  
ATOM     15  C  AMET A   1      51.289 -33.284  -1.414  0.56 56.82           C  
ANISOU   15  C  AMET A   1     6437   7070   8082     56    826   -142       C  
ATOM     16  C  BMET A   1      51.897 -33.140  -0.849  0.44 56.63           C  
ANISOU   16  C  BMET A   1     6490   7047   7979     32    843   -195       C  
ATOM     17  O  AMET A   1      51.129 -33.431  -0.199  0.56 52.07           O  
ANISOU   17  O  AMET A   1     5888   6489   7408     29    925   -188       O  
ATOM     18  O  BMET A   1      51.445 -33.568   0.224  0.44 56.40           O  
ANISOU   18  O  BMET A   1     6484   7051   7894      5    931   -212       O  
ATOM     19  CB AMET A   1      51.634 -30.891  -2.138  0.56 65.08           C  
ANISOU   19  CB AMET A   1     7485   7981   9262    150    887   -202       C  
ATOM     20  CB BMET A   1      52.607 -31.158  -2.333  0.44 61.53           C  
ANISOU   20  CB BMET A   1     7099   7551   8730    113    799   -220       C  
ATOM     21  CG AMET A   1      50.954 -29.565  -2.520  0.56 69.81           C  
ANISOU   21  CG AMET A   1     8015   8491  10017    234    979   -194       C  
ATOM     22  CG BMET A   1      51.850 -30.291  -3.332  0.44 60.57           C  
ANISOU   22  CG BMET A   1     6871   7368   8775    189    812   -163       C  
ATOM     23  SD AMET A   1      49.676 -29.003  -1.359  0.56 77.52           S  
ANISOU   23  SD AMET A   1     8954   9423  11075    283   1207   -226       S  
ATOM     24  SD BMET A   1      51.835 -30.959  -5.011  0.44 47.05           S  
ANISOU   24  SD BMET A   1     5077   5689   7112    186    636    -50       S  
ATOM     25  CE AMET A   1      48.431 -28.358  -2.475  0.56 74.36           C  
ANISOU   25  CE AMET A   1     8367   8971  10917    386   1223   -101       C  
ATOM     26  CE BMET A   1      51.275 -32.652  -4.721  0.44 47.37           C  
ANISOU   26  CE BMET A   1     5086   5818   7093    126    593      0       C  
ATOM     27  N  ASER A   2      51.995 -34.142  -2.161  0.56 53.15           N  
ANISOU   27  N  ASER A   2     5987   6638   7569     20    684   -102       N  
ATOM     28  N  BSER A   2      52.508 -33.944  -1.723  0.44 50.90           N  
ANISOU   28  N  BSER A   2     5760   6351   7228      8    699   -145       N  
ATOM     29  CA ASER A   2      52.458 -35.411  -1.604  0.56 44.26           C  
ANISOU   29  CA ASER A   2     4919   5571   6327    -44    639    -94       C  
ATOM     30  CA BSER A   2      52.481 -35.395  -1.563  0.44 44.76           C  
ANISOU   30  CA BSER A   2     4986   5635   6387    -44    641    -96       C  
ATOM     31  C  ASER A   2      53.423 -36.103  -2.562  0.56 39.48           C  
ANISOU   31  C  ASER A   2     4340   4976   5687    -67    497    -61       C  
ATOM     32  C  BSER A   2      53.418 -36.102  -2.538  0.44 39.67           C  
ANISOU   32  C  BSER A   2     4364   4999   5709    -67    499    -62       C  
ATOM     33  O  ASER A   2      53.215 -36.079  -3.778  0.56 38.20           O  
ANISOU   33  O  ASER A   2     4121   4793   5599    -49    428    -16       O  
ATOM     34  O  BSER A   2      53.199 -36.076  -3.754  0.44 38.82           O  
ANISOU   34  O  BSER A   2     4200   4873   5679    -48    431    -17       O  
ATOM     35  CB ASER A   2      51.264 -36.327  -1.310  0.56 47.20           C  
ANISOU   35  CB ASER A   2     5218   5980   6734    -60    679    -34       C  
ATOM     36  CB BSER A   2      51.052 -35.918  -1.745  0.44 46.86           C  
ANISOU   36  CB BSER A   2     5139   5917   6748    -35    676    -25       C  
ATOM     37  OG ASER A   2      51.162 -37.403  -2.232  0.56 39.65           O  
ANISOU   37  OG ASER A   2     4222   5045   5798    -89    568     38       O  
ATOM     38  OG BSER A   2      51.008 -37.334  -1.717  0.44 37.98           O  
ANISOU   38  OG BSER A   2     4019   4840   5573    -90    616     24       O  
ATOM     39  N   LEU A   3      54.462 -36.740  -2.004  1.00 37.05           N  
ANISOU   39  N   LEU A   3     4116   4697   5264   -110    458    -78       N  
ATOM     40  CA  LEU A   3      55.374 -37.537  -2.825  1.00 35.67           C  
ANISOU   40  CA  LEU A   3     3965   4525   5063   -127    346    -42       C  
ATOM     41  C   LEU A   3      54.622 -38.550  -3.680  1.00 33.26           C  
ANISOU   41  C   LEU A   3     3603   4222   4813   -140    300     26       C  
ATOM     42  O   LEU A   3      54.862 -38.670  -4.887  1.00 33.34           O  
ANISOU   42  O   LEU A   3     3601   4208   4858   -136    225     50       O  
ATOM     43  CB  LEU A   3      56.382 -38.270  -1.929  1.00 34.34           C  
ANISOU   43  CB  LEU A   3     3873   4394   4779   -169    323    -44       C  
ATOM     44  CG  LEU A   3      57.263 -39.309  -2.638  1.00 37.94           C  
ANISOU   44  CG  LEU A   3     4349   4846   5219   -182    231      5       C  
ATOM     45  CD1 LEU A   3      58.127 -38.620  -3.695  1.00 36.85           C  
ANISOU   45  CD1 LEU A   3     4216   4670   5114   -154    175    -12       C  
ATOM     46  CD2 LEU A   3      58.130 -40.084  -1.638  1.00 40.22           C  
ANISOU   46  CD2 LEU A   3     4695   5175   5412   -217    215     27       C  
ATOM     47  N   GLU A   4      53.709 -39.297  -3.058  1.00 31.64           N  
ANISOU   47  N   GLU A   4     3368   4046   4608   -166    345     56       N  
ATOM     48  CA  GLU A   4      52.988 -40.342  -3.775  1.00 35.93           C  
ANISOU   48  CA  GLU A   4     3864   4592   5195   -197    300    119       C  
ATOM     49  C   GLU A   4      52.071 -39.767  -4.847  1.00 35.48           C  
ANISOU   49  C   GLU A   4     3716   4520   5246   -178    276    148       C  
ATOM     50  O   GLU A   4      51.850 -40.420  -5.873  1.00 34.06           O  
ANISOU   50  O   GLU A   4     3518   4334   5090   -212    199    190       O  
ATOM     51  CB  GLU A   4      52.193 -41.193  -2.783  1.00 36.43           C  
ANISOU   51  CB  GLU A   4     3912   4691   5240   -233    362    148       C  
ATOM     52  CG  GLU A   4      53.080 -42.141  -1.959  1.00 42.78           C  
ANISOU   52  CG  GLU A   4     4803   5512   5939   -266    354    153       C  
ATOM     53  CD  GLU A   4      53.818 -41.472  -0.783  1.00 47.35           C  
ANISOU   53  CD  GLU A   4     5446   6116   6429   -256    404    102       C  
ATOM     54  OE1 GLU A   4      53.762 -40.234  -0.624  1.00 41.75           O  
ANISOU   54  OE1 GLU A   4     4731   5397   5734   -224    450     48       O  
ATOM     55  OE2 GLU A   4      54.452 -42.208   0.002  1.00 47.42           O  
ANISOU   55  OE2 GLU A   4     5517   6151   6351   -288    396    122       O  
ATOM     56  N   ASN A   5      51.526 -38.558  -4.630  1.00 31.68           N  
ANISOU   56  N   ASN A   5     3180   4028   4829   -128    342    130       N  
ATOM     57  CA  ASN A   5      50.717 -37.919  -5.662  1.00 32.74           C  
ANISOU   57  CA  ASN A   5     3217   4147   5075   -102    312    176       C  
ATOM     58  C   ASN A   5      51.575 -37.422  -6.823  1.00 32.06           C  
ANISOU   58  C   ASN A   5     3167   4030   4985    -88    224    169       C  
ATOM     59  O   ASN A   5      51.153 -37.491  -7.985  1.00 34.23           O  
ANISOU   59  O   ASN A   5     3392   4306   5309   -104    146    224       O  
ATOM     60  CB  ASN A   5      49.913 -36.764  -5.069  1.00 35.95           C  
ANISOU   60  CB  ASN A   5     3552   4537   5568    -41    424    167       C  
ATOM     61  CG  ASN A   5      49.142 -35.994  -6.131  1.00 44.92           C  
ANISOU   61  CG  ASN A   5     4577   5654   6834     -3    391    231       C  
ATOM     62  OD1 ASN A   5      49.483 -34.849  -6.459  1.00 37.20           O  
ANISOU   62  OD1 ASN A   5     3604   4633   5898     52    404    211       O  
ATOM     63  ND2 ASN A   5      48.124 -36.636  -6.706  1.00 37.28           N  
ANISOU   63  ND2 ASN A   5     3511   4721   5932    -38    340    317       N  
ATOM     64  N   VAL A   6      52.766 -36.882  -6.534  1.00 34.26           N  
ANISOU   64  N   VAL A   6     3530   4286   5203    -66    234    106       N  
ATOM     65  CA  VAL A   6      53.684 -36.525  -7.613  1.00 35.44           C  
ANISOU   65  CA  VAL A   6     3719   4406   5340    -59    156    101       C  
ATOM     66  C   VAL A   6      53.999 -37.752  -8.463  1.00 34.18           C  
ANISOU   66  C   VAL A   6     3595   4257   5136   -113     68    134       C  
ATOM     67  O   VAL A   6      53.968 -37.700  -9.701  1.00 34.59           O  
ANISOU   67  O   VAL A   6     3637   4296   5208   -126     -2    165       O  
ATOM     68  CB  VAL A   6      54.970 -35.882  -7.052  1.00 35.31           C  
ANISOU   68  CB  VAL A   6     3784   4370   5264    -40    181     32       C  
ATOM     69  CG1 VAL A   6      55.959 -35.624  -8.176  1.00 36.35           C  
ANISOU   69  CG1 VAL A   6     3953   4473   5384    -36    106     34       C  
ATOM     70  CG2 VAL A   6      54.636 -34.569  -6.334  1.00 35.98           C  
ANISOU   70  CG2 VAL A   6     3849   4427   5393      5    274    -11       C  
ATOM     71  N   ALA A   7      54.303 -38.883  -7.809  1.00 34.28           N  
ANISOU   71  N   ALA A   7     3655   4287   5083   -150     77    127       N  
ATOM     72  CA  ALA A   7      54.602 -40.101  -8.558  1.00 30.11           C  
ANISOU   72  CA  ALA A   7     3171   3750   4518   -200     15    152       C  
ATOM     73  C   ALA A   7      53.401 -40.556  -9.373  1.00 29.42           C  
ANISOU   73  C   ALA A   7     3023   3674   4479   -247    -30    204       C  
ATOM     74  O   ALA A   7      53.549 -41.029 -10.506  1.00 35.45           O  
ANISOU   74  O   ALA A   7     3821   4423   5227   -289    -97    220       O  
ATOM     75  CB  ALA A   7      55.050 -41.208  -7.601  1.00 31.60           C  
ANISOU   75  CB  ALA A   7     3413   3948   4645   -224     43    148       C  
ATOM     76  N   PHE A   8      52.200 -40.429  -8.816  1.00 30.40           N  
ANISOU   76  N   PHE A   8     3061   3830   4662   -248      9    234       N  
ATOM     77  CA  PHE A   8      51.019 -40.826  -9.571  1.00 32.43           C  
ANISOU   77  CA  PHE A   8     3243   4108   4973   -301    -43    298       C  
ATOM     78  C   PHE A   8      50.912 -40.032 -10.869  1.00 38.79           C  
ANISOU   78  C   PHE A   8     4016   4906   5814   -296   -118    327       C  
ATOM     79  O   PHE A   8      50.595 -40.588 -11.932  1.00 35.11           O  
ANISOU   79  O   PHE A   8     3556   4448   5336   -366   -204    364       O  
ATOM     80  CB  PHE A   8      49.763 -40.634  -8.711  1.00 34.65           C  
ANISOU   80  CB  PHE A   8     3413   4423   5330   -289     24    333       C  
ATOM     81  CG  PHE A   8      48.489 -40.856  -9.462  1.00 35.87           C  
ANISOU   81  CG  PHE A   8     3460   4607   5560   -341    -35    414       C  
ATOM     82  CD1 PHE A   8      47.889 -39.817 -10.158  1.00 36.73           C  
ANISOU   82  CD1 PHE A   8     3473   4725   5759   -308    -67    466       C  
ATOM     83  CD2 PHE A   8      47.879 -42.104  -9.473  1.00 38.42           C  
ANISOU   83  CD2 PHE A   8     3775   4950   5871   -429    -62    447       C  
ATOM     84  CE1 PHE A   8      46.715 -40.019 -10.858  1.00 42.41           C  
ANISOU   84  CE1 PHE A   8     4080   5483   6550   -363   -137    557       C  
ATOM     85  CE2 PHE A   8      46.706 -42.306 -10.170  1.00 41.07           C  
ANISOU   85  CE2 PHE A   8     4007   5322   6276   -492   -129    527       C  
ATOM     86  CZ  PHE A   8      46.125 -41.263 -10.867  1.00 47.02           C  
ANISOU   86  CZ  PHE A   8     4656   6095   7116   -460   -172    586       C  
ATOM     87  N   ASN A   9      51.149 -38.720 -10.799  1.00 33.97           N  
ANISOU   87  N   ASN A   9     3379   4280   5246   -220    -88    314       N  
ATOM     88  CA  ASN A   9      51.067 -37.901 -12.002  1.00 35.31           C  
ANISOU   88  CA  ASN A   9     3519   4443   5454   -210   -156    354       C  
ATOM     89  C   ASN A   9      52.138 -38.283 -13.015  1.00 35.87           C  
ANISOU   89  C   ASN A   9     3701   4491   5438   -248   -224    328       C  
ATOM     90  O   ASN A   9      51.866 -38.333 -14.222  1.00 40.21           O  
ANISOU   90  O   ASN A   9     4248   5050   5980   -296   -310    374       O  
ATOM     91  CB  ASN A   9      51.183 -36.417 -11.639  1.00 35.31           C  
ANISOU   91  CB  ASN A   9     3478   4415   5522   -118    -94    341       C  
ATOM     92  CG  ASN A   9      49.862 -35.832 -11.191  1.00 40.20           C  
ANISOU   92  CG  ASN A   9     3962   5049   6263    -79    -40    398       C  
ATOM     93  OD1 ASN A   9      49.196 -35.122 -11.945  1.00 40.87           O  
ANISOU   93  OD1 ASN A   9     3957   5135   6436    -59    -80    473       O  
ATOM     94  ND2 ASN A   9      49.464 -36.143  -9.956  1.00 37.62           N  
ANISOU   94  ND2 ASN A   9     3617   4733   5945    -69     54    370       N  
ATOM     95  N   VAL A  10      53.364 -38.534 -12.552  1.00 34.05           N  
ANISOU   95  N   VAL A  10     3567   4232   5140   -229   -186    261       N  
ATOM     96  CA  VAL A  10      54.431 -38.903 -13.480  1.00 32.57           C  
ANISOU   96  CA  VAL A  10     3480   4016   4880   -255   -228    238       C  
ATOM     97  C   VAL A  10      54.057 -40.185 -14.219  1.00 36.45           C  
ANISOU   97  C   VAL A  10     4014   4512   5326   -347   -283    257       C  
ATOM     98  O   VAL A  10      54.163 -40.267 -15.447  1.00 36.10           O  
ANISOU   98  O   VAL A  10     4012   4458   5244   -395   -345    272       O  
ATOM     99  CB  VAL A  10      55.769 -39.041 -12.733  1.00 37.31           C  
ANISOU   99  CB  VAL A  10     4156   4589   5432   -218   -174    177       C  
ATOM    100  CG1 VAL A  10      56.812 -39.704 -13.642  1.00 35.48           C  
ANISOU  100  CG1 VAL A  10     4022   4322   5136   -247   -200    160       C  
ATOM    101  CG2 VAL A  10      56.263 -37.650 -12.267  1.00 35.51           C  
ANISOU  101  CG2 VAL A  10     3905   4350   5236   -147   -135    151       C  
ATOM    102  N   VAL A  11      53.565 -41.186 -13.481  1.00 35.38           N  
ANISOU  102  N   VAL A  11     3870   4387   5187   -382   -257    259       N  
ATOM    103  CA  VAL A  11      53.239 -42.485 -14.074  1.00 35.23           C  
ANISOU  103  CA  VAL A  11     3902   4359   5124   -478   -298    269       C  
ATOM    104  C   VAL A  11      52.069 -42.377 -15.045  1.00 41.77           C  
ANISOU  104  C   VAL A  11     4669   5225   5975   -552   -385    329       C  
ATOM    105  O   VAL A  11      52.033 -43.069 -16.071  1.00 47.42           O  
ANISOU  105  O   VAL A  11     5455   5929   6633   -643   -444    330       O  
ATOM    106  CB  VAL A  11      52.947 -43.508 -12.956  1.00 40.46           C  
ANISOU  106  CB  VAL A  11     4562   5022   5788   -496   -244    265       C  
ATOM    107  CG1 VAL A  11      52.262 -44.745 -13.511  1.00 48.74           C  
ANISOU  107  CG1 VAL A  11     5641   6064   6815   -607   -286    285       C  
ATOM    108  CG2 VAL A  11      54.232 -43.887 -12.252  1.00 41.39           C  
ANISOU  108  CG2 VAL A  11     4761   5101   5865   -447   -182    220       C  
ATOM    109  N   ASN A  12      51.084 -41.533 -14.739  1.00 38.94           N  
ANISOU  109  N   ASN A  12     4180   4912   5703   -520   -393    384       N  
ATOM    110  CA  ASN A  12      49.855 -41.519 -15.519  1.00 39.62           C  
ANISOU  110  CA  ASN A  12     4180   5046   5827   -594   -483    464       C  
ATOM    111  C   ASN A  12      49.788 -40.388 -16.534  1.00 46.98           C  
ANISOU  111  C   ASN A  12     5075   5994   6781   -575   -551    513       C  
ATOM    112  O   ASN A  12      49.037 -40.494 -17.511  1.00 43.68           O  
ANISOU  112  O   ASN A  12     4622   5617   6359   -660   -654    581       O  
ATOM    113  CB  ASN A  12      48.643 -41.427 -14.589  1.00 45.49           C  
ANISOU  113  CB  ASN A  12     4780   5832   6672   -578   -447    518       C  
ATOM    114  CG  ASN A  12      48.374 -42.732 -13.869  1.00 52.04           C  
ANISOU  114  CG  ASN A  12     5637   6659   7478   -638   -411    498       C  
ATOM    115  OD1 ASN A  12      47.753 -43.632 -14.426  1.00 53.82           O  
ANISOU  115  OD1 ASN A  12     5867   6901   7683   -750   -478    529       O  
ATOM    116  ND2 ASN A  12      48.858 -42.848 -12.633  1.00 40.04           N  
ANISOU  116  ND2 ASN A  12     4141   5118   5954   -573   -307    449       N  
ATOM    117  N   LYS A  13      50.545 -39.317 -16.335  1.00 41.06           N  
ANISOU  117  N   LYS A  13     4332   5216   6052   -474   -503    487       N  
ATOM    118  CA  LYS A  13      50.421 -38.149 -17.188  1.00 39.29           C  
ANISOU  118  CA  LYS A  13     4060   5001   5866   -444   -557    545       C  
ATOM    119  C   LYS A  13      51.743 -37.717 -17.803  1.00 40.51           C  
ANISOU  119  C   LYS A  13     4332   5112   5950   -418   -552    493       C  
ATOM    120  O   LYS A  13      51.748 -36.795 -18.634  1.00 41.21           O  
ANISOU  120  O   LYS A  13     4399   5203   6055   -402   -600    544       O  
ATOM    121  CB  LYS A  13      49.808 -36.983 -16.397  1.00 38.31           C  
ANISOU  121  CB  LYS A  13     3802   4880   5875   -341   -495    586       C  
ATOM    122  CG  LYS A  13      48.319 -37.176 -16.067  1.00 49.13           C  
ANISOU  122  CG  LYS A  13     5024   6301   7344   -364   -510    671       C  
ATOM    123  CD  LYS A  13      47.475 -37.185 -17.338  1.00 58.14           C  
ANISOU  123  CD  LYS A  13     6098   7496   8498   -448   -648    783       C  
ATOM    124  CE  LYS A  13      46.000 -36.962 -17.037  1.00 62.77           C  
ANISOU  124  CE  LYS A  13     6495   8132   9223   -441   -660    896       C  
ATOM    125  NZ  LYS A  13      45.133 -37.009 -18.263  1.00 62.27           N  
ANISOU  125  NZ  LYS A  13     6353   8135   9172   -537   -814   1023       N  
ATOM    126  N   GLY A  14      52.859 -38.355 -17.427  1.00 37.15           N  
ANISOU  126  N   GLY A  14     4018   4644   5451   -411   -493    405       N  
ATOM    127  CA  GLY A  14      54.166 -38.032 -17.951  1.00 35.38           C  
ANISOU  127  CA  GLY A  14     3897   4378   5167   -386   -476    358       C  
ATOM    128  C   GLY A  14      54.880 -36.905 -17.231  1.00 41.44           C  
ANISOU  128  C   GLY A  14     4641   5117   5986   -281   -407    328       C  
ATOM    129  O   GLY A  14      56.073 -36.680 -17.490  1.00 41.41           O  
ANISOU  129  O   GLY A  14     4716   5078   5940   -258   -382    286       O  
ATOM    130  N   HIS A  15      54.196 -36.205 -16.332  1.00 38.36           N  
ANISOU  130  N   HIS A  15     4151   4738   5687   -223   -367    347       N  
ATOM    131  CA  HIS A  15      54.724 -35.054 -15.602  1.00 36.08           C  
ANISOU  131  CA  HIS A  15     3843   4416   5449   -135   -296    314       C  
ATOM    132  C   HIS A  15      53.656 -34.666 -14.583  1.00 38.43           C  
ANISOU  132  C   HIS A  15     4034   4728   5839    -93   -242    333       C  
ATOM    133  O   HIS A  15      52.595 -35.291 -14.516  1.00 37.53           O  
ANISOU  133  O   HIS A  15     3856   4652   5751   -130   -264    379       O  
ATOM    134  CB  HIS A  15      55.048 -33.890 -16.543  1.00 38.02           C  
ANISOU  134  CB  HIS A  15     4087   4637   5720   -105   -327    347       C  
ATOM    135  CG  HIS A  15      53.833 -33.230 -17.114  1.00 36.89           C  
ANISOU  135  CG  HIS A  15     3838   4515   5663    -99   -377    446       C  
ATOM    136  ND1 HIS A  15      53.581 -31.883 -16.966  1.00 39.72           N  
ANISOU  136  ND1 HIS A  15     4127   4841   6125    -22   -340    479       N  
ATOM    137  CD2 HIS A  15      52.776 -33.738 -17.795  1.00 42.06           C  
ANISOU  137  CD2 HIS A  15     4437   5220   6325   -162   -460    527       C  
ATOM    138  CE1 HIS A  15      52.430 -31.584 -17.544  1.00 42.54           C  
ANISOU  138  CE1 HIS A  15     4380   5226   6557    -27   -398    586       C  
ATOM    139  NE2 HIS A  15      51.921 -32.691 -18.054  1.00 42.40           N  
ANISOU  139  NE2 HIS A  15     4365   5266   6479   -116   -479    619       N  
ATOM    140  N   PHE A  16      53.928 -33.629 -13.792  1.00 36.03           N  
ANISOU  140  N   PHE A  16     3715   4390   5586    -20   -162    297       N  
ATOM    141  CA  PHE A  16      52.928 -33.188 -12.825  1.00 37.17           C  
ANISOU  141  CA  PHE A  16     3767   4535   5819     24    -86    308       C  
ATOM    142  C   PHE A  16      51.824 -32.427 -13.542  1.00 37.55           C  
ANISOU  142  C   PHE A  16     3700   4585   5983     52   -117    408       C  
ATOM    143  O   PHE A  16      52.083 -31.395 -14.174  1.00 41.26           O  
ANISOU  143  O   PHE A  16     4164   5018   6497     91   -131    435       O  
ATOM    144  CB  PHE A  16      53.508 -32.313 -11.715  1.00 35.36           C  
ANISOU  144  CB  PHE A  16     3571   4262   5603     83     20    230       C  
ATOM    145  CG  PHE A  16      52.504 -32.042 -10.624  1.00 35.74           C  
ANISOU  145  CG  PHE A  16     3547   4310   5725    120    120    227       C  
ATOM    146  CD1 PHE A  16      52.185 -33.038  -9.709  1.00 40.08           C  
ANISOU  146  CD1 PHE A  16     4102   4900   6228     86    156    204       C  
ATOM    147  CD2 PHE A  16      51.824 -30.830 -10.556  1.00 40.38           C  
ANISOU  147  CD2 PHE A  16     4057   4851   6435    190    187    256       C  
ATOM    148  CE1 PHE A  16      51.231 -32.816  -8.714  1.00 44.95           C  
ANISOU  148  CE1 PHE A  16     4653   5517   6909    117    261    203       C  
ATOM    149  CE2 PHE A  16      50.875 -30.596  -9.568  1.00 44.71           C  
ANISOU  149  CE2 PHE A  16     4538   5392   7059    228    300    253       C  
ATOM    150  CZ  PHE A  16      50.573 -31.594  -8.645  1.00 45.87           C  
ANISOU  150  CZ  PHE A  16     4695   5585   7149    189    338    225       C  
ATOM    151  N   ASP A  17      50.585 -32.915 -13.395  1.00 39.28           N  
ANISOU  151  N   ASP A  17     3818   4846   6260     32   -126    473       N  
ATOM    152  CA  ASP A  17      49.420 -32.365 -14.079  1.00 41.36           C  
ANISOU  152  CA  ASP A  17     3947   5126   6642     50   -170    593       C  
ATOM    153  C   ASP A  17      48.285 -32.037 -13.110  1.00 45.55           C  
ANISOU  153  C   ASP A  17     4352   5654   7300    107    -67    625       C  
ATOM    154  O   ASP A  17      47.150 -31.828 -13.548  1.00 44.23           O  
ANISOU  154  O   ASP A  17     4045   5514   7245    114   -103    741       O  
ATOM    155  CB  ASP A  17      48.947 -33.363 -15.150  1.00 51.58           C  
ANISOU  155  CB  ASP A  17     5226   6486   7885    -54   -309    667       C  
ATOM    156  CG  ASP A  17      47.928 -32.773 -16.117  1.00 71.53           C  
ANISOU  156  CG  ASP A  17     7622   9042  10513    -54   -395    809       C  
ATOM    157  OD1 ASP A  17      47.975 -31.553 -16.381  1.00 73.93           O  
ANISOU  157  OD1 ASP A  17     7886   9304  10902     23   -374    852       O  
ATOM    158  OD2 ASP A  17      47.068 -33.542 -16.602  1.00 70.87           O  
ANISOU  158  OD2 ASP A  17     7474   9024  10429   -137   -486    886       O  
ATOM    159  N   GLY A  18      48.544 -32.018 -11.802  1.00 41.97           N  
ANISOU  159  N   GLY A  18     3942   5174   6832    142     60    531       N  
ATOM    160  CA  GLY A  18      47.502 -31.676 -10.851  1.00 45.44           C  
ANISOU  160  CA  GLY A  18     4275   5604   7387    197    182    552       C  
ATOM    161  C   GLY A  18      46.403 -32.705 -10.677  1.00 45.67           C  
ANISOU  161  C   GLY A  18     4207   5700   7443    144    161    617       C  
ATOM    162  O   GLY A  18      45.335 -32.368 -10.164  1.00 51.48           O  
ANISOU  162  O   GLY A  18     4818   6434   8307    192    249    671       O  
ATOM    163  N   GLN A  19      46.625 -33.957 -11.077  1.00 38.89           N  
ANISOU  163  N   GLN A  19     3404   4896   6477     46     58    614       N  
ATOM    164  CA  GLN A  19      45.594 -34.983 -10.961  1.00 40.38           C  
ANISOU  164  CA  GLN A  19     3507   5147   6690    -21     30    677       C  
ATOM    165  C   GLN A  19      45.630 -35.612  -9.572  1.00 44.78           C  
ANISOU  165  C   GLN A  19     4110   5706   7200    -24    148    601       C  
ATOM    166  O   GLN A  19      46.685 -35.694  -8.938  1.00 41.22           O  
ANISOU  166  O   GLN A  19     3791   5228   6644    -16    196    496       O  
ATOM    167  CB  GLN A  19      45.791 -36.062 -12.029  1.00 48.50           C  
ANISOU  167  CB  GLN A  19     4588   6220   7622   -136   -126    704       C  
ATOM    168  CG  GLN A  19      45.763 -35.527 -13.451  1.00 59.32           C  
ANISOU  168  CG  GLN A  19     5928   7599   9011   -153   -253    783       C  
ATOM    169  CD  GLN A  19      44.427 -34.895 -13.798  1.00 70.72           C  
ANISOU  169  CD  GLN A  19     7179   9073  10617   -126   -277    925       C  
ATOM    170  OE1 GLN A  19      43.371 -35.418 -13.440  1.00 76.04           O  
ANISOU  170  OE1 GLN A  19     7738   9792  11361   -158   -267    987       O  
ATOM    171  NE2 GLN A  19      44.467 -33.761 -14.488  1.00 72.74           N  
ANISOU  171  NE2 GLN A  19     7391   9304  10942    -65   -307    986       N  
ATOM    172  N   GLN A  20      44.464 -36.056  -9.105  1.00 41.03           N  
ANISOU  172  N   GLN A  20     3518   5269   6804    -41    192    662       N  
ATOM    173  CA  GLN A  20      44.369 -36.755  -7.827  1.00 40.25           C  
ANISOU  173  CA  GLN A  20     3455   5180   6657    -57    300    606       C  
ATOM    174  C   GLN A  20      44.754 -38.220  -7.991  1.00 44.24           C  
ANISOU  174  C   GLN A  20     4048   5719   7040   -165    212    588       C  
ATOM    175  O   GLN A  20      44.413 -38.855  -8.990  1.00 46.20           O  
ANISOU  175  O   GLN A  20     4265   6000   7289   -243     86    652       O  
ATOM    176  CB  GLN A  20      42.953 -36.665  -7.264  1.00 45.46           C  
ANISOU  176  CB  GLN A  20     3951   5864   7459    -33    395    685       C  
ATOM    177  CG  GLN A  20      42.520 -35.260  -6.884  1.00 64.28           C  
ANISOU  177  CG  GLN A  20     6249   8196   9978     86    526    696       C  
ATOM    178  CD  GLN A  20      41.058 -35.189  -6.483  1.00 88.22           C  
ANISOU  178  CD  GLN A  20     9095  11250  13173    114    620    795       C  
ATOM    179  OE1 GLN A  20      40.288 -34.414  -7.048  1.00103.20           O  
ANISOU  179  OE1 GLN A  20    10840  13139  15232    171    615    899       O  
ATOM    180  NE2 GLN A  20      40.671 -35.996  -5.498  1.00 89.57           N  
ANISOU  180  NE2 GLN A  20     9271  11451  13312     76    708    772       N  
ATOM    181  N   GLY A  21      45.438 -38.761  -6.995  1.00 40.90           N  
ANISOU  181  N   GLY A  21     3739   5288   6513   -174    280    506       N  
ATOM    182  CA  GLY A  21      45.796 -40.169  -6.999  1.00 38.00           C  
ANISOU  182  CA  GLY A  21     3455   4939   6044   -265    221    493       C  
ATOM    183  C   GLY A  21      47.096 -40.391  -6.259  1.00 39.31           C  
ANISOU  183  C   GLY A  21     3774   5080   6083   -252    260    400       C  
ATOM    184  O   GLY A  21      47.810 -39.458  -5.912  1.00 36.49           O  
ANISOU  184  O   GLY A  21     3465   4695   5704   -187    308    341       O  
ATOM    185  N   GLU A  22      47.400 -41.662  -6.006  1.00 36.68           N  
ANISOU  185  N   GLU A  22     3512   4755   5670   -319    237    393       N  
ATOM    186  CA  GLU A  22      48.668 -41.997  -5.351  1.00 35.20           C  
ANISOU  186  CA  GLU A  22     3458   4549   5367   -311    258    327       C  
ATOM    187  C   GLU A  22      49.160 -43.342  -5.867  1.00 40.52           C  
ANISOU  187  C   GLU A  22     4209   5208   5978   -383    180    338       C  
ATOM    188  O   GLU A  22      48.358 -44.200  -6.234  1.00 37.49           O  
ANISOU  188  O   GLU A  22     3784   4835   5625   -452    146    388       O  
ATOM    189  CB  GLU A  22      48.514 -42.065  -3.818  1.00 41.34           C  
ANISOU  189  CB  GLU A  22     4251   5348   6109   -297    378    305       C  
ATOM    190  CG  GLU A  22      48.437 -40.729  -3.097  1.00 58.07           C  
ANISOU  190  CG  GLU A  22     6351   7462   8251   -225    480    260       C  
ATOM    191  CD  GLU A  22      47.011 -40.298  -2.805  1.00 77.21           C  
ANISOU  191  CD  GLU A  22     8645   9901  10790   -203    571    303       C  
ATOM    192  OE1 GLU A  22      46.111 -41.165  -2.822  1.00 80.80           O  
ANISOU  192  OE1 GLU A  22     9030  10384  11287   -253    566    366       O  
ATOM    193  OE2 GLU A  22      46.793 -39.092  -2.552  1.00 79.04           O  
ANISOU  193  OE2 GLU A  22     8841  10110  11079   -135    653    275       O  
ATOM    194  N   VAL A  23      50.479 -43.521  -5.875  1.00 34.68           N  
ANISOU  194  N   VAL A  23     3578   4440   5158   -369    158    295       N  
ATOM    195  CA  VAL A  23      51.083 -44.830  -6.127  1.00 32.35           C  
ANISOU  195  CA  VAL A  23     3369   4117   4807   -422    118    302       C  
ATOM    196  C   VAL A  23      52.117 -45.104  -5.044  1.00 39.10           C  
ANISOU  196  C   VAL A  23     4302   4970   5585   -395    164    279       C  
ATOM    197  O   VAL A  23      52.623 -44.172  -4.398  1.00 36.35           O  
ANISOU  197  O   VAL A  23     3963   4638   5210   -342    200    243       O  
ATOM    198  CB  VAL A  23      51.725 -44.908  -7.536  1.00 31.21           C  
ANISOU  198  CB  VAL A  23     3276   3932   4652   -437     32    290       C  
ATOM    199  CG1 VAL A  23      50.662 -44.772  -8.625  1.00 38.36           C  
ANISOU  199  CG1 VAL A  23     4109   4850   5616   -487    -31    326       C  
ATOM    200  CG2 VAL A  23      52.818 -43.875  -7.702  1.00 34.52           C  
ANISOU  200  CG2 VAL A  23     3730   4337   5047   -368     28    246       C  
ATOM    201  N   PRO A  24      52.456 -46.378  -4.817  1.00 39.87           N  
ANISOU  201  N   PRO A  24     4459   5044   5645   -435    160    304       N  
ATOM    202  CA  PRO A  24      53.468 -46.688  -3.803  1.00 34.60           C  
ANISOU  202  CA  PRO A  24     3858   4380   4908   -411    190    304       C  
ATOM    203  C   PRO A  24      54.845 -46.315  -4.311  1.00 34.62           C  
ANISOU  203  C   PRO A  24     3916   4354   4883   -368    149    276       C  
ATOM    204  O   PRO A  24      55.178 -46.568  -5.472  1.00 36.67           O  
ANISOU  204  O   PRO A  24     4201   4566   5165   -376    103    270       O  
ATOM    205  CB  PRO A  24      53.344 -48.207  -3.615  1.00 39.10           C  
ANISOU  205  CB  PRO A  24     4467   4920   5470   -465    197    355       C  
ATOM    206  CG  PRO A  24      52.028 -48.594  -4.302  1.00 41.67           C  
ANISOU  206  CG  PRO A  24     4735   5240   5858   -527    183    373       C  
ATOM    207  CD  PRO A  24      51.884 -47.605  -5.407  1.00 36.88           C  
ANISOU  207  CD  PRO A  24     4089   4634   5289   -509    132    341       C  
ATOM    208  N   VAL A  25      55.644 -45.713  -3.432  1.00 35.17           N  
ANISOU  208  N   VAL A  25     4008   4454   4902   -332    167    260       N  
ATOM    209  CA  VAL A  25      56.951 -45.166  -3.802  1.00 30.88           C  
ANISOU  209  CA  VAL A  25     3499   3893   4339   -292    130    235       C  
ATOM    210  C   VAL A  25      58.014 -45.696  -2.851  1.00 30.56           C  
ANISOU  210  C   VAL A  25     3505   3869   4239   -287    130    271       C  
ATOM    211  O   VAL A  25      57.785 -45.778  -1.640  1.00 34.85           O  
ANISOU  211  O   VAL A  25     4052   4461   4730   -305    164    288       O  
ATOM    212  CB  VAL A  25      56.925 -43.620  -3.765  1.00 35.73           C  
ANISOU  212  CB  VAL A  25     4085   4533   4959   -259    139    179       C  
ATOM    213  CG1 VAL A  25      58.325 -43.053  -3.925  1.00 34.69           C  
ANISOU  213  CG1 VAL A  25     3988   4392   4801   -228    104    159       C  
ATOM    214  CG2 VAL A  25      55.983 -43.081  -4.837  1.00 33.99           C  
ANISOU  214  CG2 VAL A  25     3810   4294   4811   -256    126    165       C  
ATOM    215  N   SER A  26      59.199 -46.017  -3.399  1.00 30.96           N  
ANISOU  215  N   SER A  26     3586   3881   4296   -264     93    288       N  
ATOM    216  CA  SER A  26      60.388 -46.346  -2.624  1.00 31.97           C  
ANISOU  216  CA  SER A  26     3739   4027   4383   -250     78    336       C  
ATOM    217  C   SER A  26      61.473 -45.336  -2.956  1.00 29.18           C  
ANISOU  217  C   SER A  26     3381   3680   4027   -217     43    304       C  
ATOM    218  O   SER A  26      61.684 -45.009  -4.125  1.00 32.32           O  
ANISOU  218  O   SER A  26     3777   4032   4472   -196     30    274       O  
ATOM    219  CB  SER A  26      60.930 -47.754  -2.940  1.00 34.28           C  
ANISOU  219  CB  SER A  26     4060   4258   4708   -244     78    405       C  
ATOM    220  OG  SER A  26      60.037 -48.747  -2.520  1.00 47.86           O  
ANISOU  220  OG  SER A  26     5789   5969   6428   -281    110    442       O  
ATOM    221  N   ILE A  27      62.185 -44.870  -1.939  1.00 29.19           N  
ANISOU  221  N   ILE A  27     3384   3738   3967   -223     25    316       N  
ATOM    222  CA  ILE A  27      63.363 -44.026  -2.145  1.00 27.93           C  
ANISOU  222  CA  ILE A  27     3218   3588   3806   -204    -15    301       C  
ATOM    223  C   ILE A  27      64.587 -44.772  -1.634  1.00 29.42           C  
ANISOU  223  C   ILE A  27     3404   3792   3983   -198    -52    392       C  
ATOM    224  O   ILE A  27      64.637 -45.159  -0.458  1.00 32.90           O  
ANISOU  224  O   ILE A  27     3854   4289   4359   -229    -62    443       O  
ATOM    225  CB  ILE A  27      63.218 -42.671  -1.440  1.00 34.16           C  
ANISOU  225  CB  ILE A  27     4011   4432   4537   -228    -12    234       C  
ATOM    226  CG1 ILE A  27      62.035 -41.893  -2.064  1.00 38.05           C  
ANISOU  226  CG1 ILE A  27     4490   4897   5070   -218     31    159       C  
ATOM    227  CG2 ILE A  27      64.515 -41.885  -1.518  1.00 34.40           C  
ANISOU  227  CG2 ILE A  27     4035   4475   4560   -224    -61    227       C  
ATOM    228  CD1 ILE A  27      61.817 -40.559  -1.451  1.00 47.16           C  
ANISOU  228  CD1 ILE A  27     5653   6080   6185   -233     57     87       C  
ATOM    229  N  AILE A  28      65.575 -44.991  -2.481  0.46 33.10           N  
ANISOU  229  N  AILE A  28     3855   4210   4512   -158    -69    422       N  
ATOM    230  N  BILE A  28      65.577 -44.939  -2.531  0.54 31.28           N  
ANISOU  230  N  BILE A  28     3624   3978   4283   -157    -69    418       N  
ATOM    231  CA AILE A  28      66.759 -45.657  -1.951  0.46 28.88           C  
ANISOU  231  CA AILE A  28     3299   3691   3983   -145   -103    524       C  
ATOM    232  CA BILE A  28      66.863 -45.597  -2.275  0.54 30.52           C  
ANISOU  232  CA BILE A  28     3504   3882   4210   -135    -99    516       C  
ATOM    233  C  AILE A  28      67.975 -44.951  -2.520  0.46 28.97           C  
ANISOU  233  C  AILE A  28     3276   3698   4035   -119   -135    524       C  
ATOM    234  C  BILE A  28      67.903 -45.014  -3.231  0.54 29.44           C  
ANISOU  234  C  BILE A  28     3341   3713   4133    -98   -113    503       C  
ATOM    235  O  AILE A  28      68.089 -44.790  -3.739  0.46 32.39           O  
ANISOU  235  O  AILE A  28     3711   4064   4531    -85   -108    485       O  
ATOM    236  O  BILE A  28      67.582 -44.649  -4.364  0.54 29.21           O  
ANISOU  236  O  BILE A  28     3326   3628   4143    -80    -84    438       O  
ATOM    237  CB AILE A  28      66.764 -47.176  -2.226  0.46 32.42           C  
ANISOU  237  CB AILE A  28     3755   4070   4491   -115    -68    604       C  
ATOM    238  CB BILE A  28      66.826 -47.134  -2.483  0.54 33.61           C  
ANISOU  238  CB BILE A  28     3906   4207   4657   -107    -64    596       C  
ATOM    239  CG1AILE A  28      67.996 -47.846  -1.617  0.46 38.04           C  
ANISOU  239  CG1AILE A  28     4431   4798   5226    -92   -100    731       C  
ATOM    240  CG1BILE A  28      65.506 -47.758  -2.055  0.54 29.25           C  
ANISOU  240  CG1BILE A  28     3388   3655   4072   -142    -29    585       C  
ATOM    241  CG2AILE A  28      66.662 -47.476  -3.683  0.46 37.29           C  
ANISOU  241  CG2AILE A  28     4392   4588   5188    -80    -22    564       C  
ATOM    242  CG2BILE A  28      68.000 -47.807  -1.762  0.54 37.83           C  
ANISOU  242  CG2BILE A  28     4405   4763   5206    -88    -97    723       C  
ATOM    243  CD1AILE A  28      67.843 -49.349  -1.473  0.46 44.40           C  
ANISOU  243  CD1AILE A  28     5251   5543   6077    -71    -61    822       C  
ATOM    244  CD1BILE A  28      65.396 -49.237  -2.429  0.54 33.29           C  
ANISOU  244  CD1BILE A  28     3922   4080   4648   -122     16    649       C  
ATOM    245  N  AASN A  29      68.851 -44.489  -1.630  0.46 30.28           N  
ANISOU  245  N  AASN A  29     3412   3938   4154   -147   -195    566       N  
ATOM    246  N  BASN A  29      69.174 -45.005  -2.790  0.54 32.41           N  
ANISOU  246  N  BASN A  29     3673   4124   4519    -90   -158    580       N  
ATOM    247  CA AASN A  29      69.893 -43.529  -1.972  0.46 37.38           C  
ANISOU  247  CA AASN A  29     4276   4852   5074   -145   -234    553       C  
ATOM    248  CA BASN A  29      70.347 -44.521  -3.532  0.54 34.96           C  
ANISOU  248  CA BASN A  29     3954   4424   4905    -58   -171    593       C  
ATOM    249  C  AASN A  29      69.266 -42.340  -2.686  0.46 34.84           C  
ANISOU  249  C  AASN A  29     3981   4506   4750   -152   -208    429       C  
ATOM    250  C  BASN A  29      70.097 -43.332  -4.449  0.54 35.29           C  
ANISOU  250  C  BASN A  29     4012   4444   4952    -60   -158    485       C  
ATOM    251  O  AASN A  29      68.445 -41.626  -2.098  0.46 33.60           O  
ANISOU  251  O  AASN A  29     3857   4385   4523   -194   -202    357       O  
ATOM    252  O  BASN A  29      70.450 -43.393  -5.639  0.54 27.33           O  
ANISOU  252  O  BASN A  29     3003   3366   4013    -19   -121    474       O  
ATOM    253  CB AASN A  29      70.980 -44.203  -2.807  0.46 36.03           C  
ANISOU  253  CB AASN A  29     4057   4621   5011    -82   -223    633       C  
ATOM    254  CB BASN A  29      70.971 -45.613  -4.412  0.54 44.63           C  
ANISOU  254  CB BASN A  29     5165   5558   6235      9   -119    661       C  
ATOM    255  CG AASN A  29      71.639 -45.344  -2.064  0.46 37.76           C  
ANISOU  255  CG AASN A  29     4237   4860   5251    -67   -246    773       C  
ATOM    256  CG BASN A  29      70.548 -46.994  -4.029  0.54 44.35           C  
ANISOU  256  CG BASN A  29     5150   5487   6214     23    -86    729       C  
ATOM    257  OD1AASN A  29      71.903 -45.237  -0.866  0.46 44.72           O  
ANISOU  257  OD1AASN A  29     5101   5831   6058   -117   -314    829       O  
ATOM    258  OD1BASN A  29      71.044 -47.550  -3.054  0.54 38.90           O  
ANISOU  258  OD1BASN A  29     4424   4839   5518     22   -121    835       O  
ATOM    259  ND2AASN A  29      71.890 -46.453  -2.761  0.46 38.42           N  
ANISOU  259  ND2AASN A  29     4312   4854   5433      0   -188    834       N  
ATOM    260  ND2BASN A  29      69.649 -47.579  -4.813  0.54 50.53           N  
ANISOU  260  ND2BASN A  29     5992   6190   7016     30    -22    676       N  
ATOM    261  N  AASN A  30      69.599 -42.152  -3.961  0.46 34.86           N  
ANISOU  261  N  AASN A  30     3973   4442   4830   -108   -183    407       N  
ATOM    262  N  BASN A  30      69.515 -42.254  -3.916  0.54 33.57           N  
ANISOU  262  N  BASN A  30     3812   4278   4664   -108   -181    409       N  
ATOM    263  CA AASN A  30      69.211 -40.963  -4.709  0.46 37.80           C  
ANISOU  263  CA AASN A  30     4362   4792   5210   -111   -169    311       C  
ATOM    264  CA BASN A  30      69.242 -41.034  -4.675  0.54 37.62           C  
ANISOU  264  CA BASN A  30     4338   4769   5186   -110   -170    316       C  
ATOM    265  C  AASN A  30      68.267 -41.280  -5.866  0.46 34.91           C  
ANISOU  265  C  AASN A  30     4026   4354   4883    -81   -118    269       C  
ATOM    266  C  BASN A  30      68.272 -41.280  -5.830  0.54 35.06           C  
ANISOU  266  C  BASN A  30     4045   4375   4901    -81   -118    270       C  
ATOM    267  O  AASN A  30      68.219 -40.545  -6.851  0.46 34.95           O  
ANISOU  267  O  AASN A  30     4037   4323   4918    -68   -106    221       O  
ATOM    268  O  BASN A  30      68.215 -40.495  -6.777  0.54 35.09           O  
ANISOU  268  O  BASN A  30     4054   4345   4933    -70   -108    220       O  
ATOM    269  CB AASN A  30      70.451 -40.233  -5.223  0.46 43.54           C  
ANISOU  269  CB AASN A  30     5052   5513   5979   -102   -193    320       C  
ATOM    270  CB BASN A  30      70.542 -40.404  -5.201  0.54 41.78           C  
ANISOU  270  CB BASN A  30     4825   5289   5760    -98   -194    334       C  
ATOM    271  CG AASN A  30      70.541 -38.809  -4.706  0.46 38.89           C  
ANISOU  271  CG AASN A  30     4468   4967   5342   -152   -226    255       C  
ATOM    272  CG BASN A  30      70.751 -38.974  -4.710  0.54 39.95           C  
ANISOU  272  CG BASN A  30     4593   5102   5483   -148   -230    274       C  
ATOM    273  OD1AASN A  30      69.622 -38.316  -4.055  0.46 35.83           O  
ANISOU  273  OD1AASN A  30     4117   4603   4893   -187   -216    194       O  
ATOM    274  OD1BASN A  30      69.838 -38.336  -4.190  0.54 34.47           O  
ANISOU  274  OD1BASN A  30     3937   4427   4732   -182   -220    203       O  
ATOM    275  ND2AASN A  30      71.637 -38.143  -5.007  0.46 37.35           N  
ANISOU  275  ND2AASN A  30     4237   4774   5179   -159   -254    268       N  
ATOM    276  ND2BASN A  30      71.956 -38.468  -4.890  0.54 43.30           N  
ANISOU  276  ND2BASN A  30     4975   5537   5940   -156   -264    303       N  
ATOM    277  N   THR A  31      67.494 -42.359  -5.765  1.00 32.82           N  
ANISOU  277  N   THR A  31     3782   4071   4616    -79    -91    292       N  
ATOM    278  CA  THR A  31      66.610 -42.768  -6.847  1.00 33.17           C  
ANISOU  278  CA  THR A  31     3858   4054   4691    -69    -54    260       C  
ATOM    279  C   THR A  31      65.201 -42.970  -6.304  1.00 35.83           C  
ANISOU  279  C   THR A  31     4207   4414   4992   -100    -42    236       C  
ATOM    280  O   THR A  31      65.024 -43.446  -5.178  1.00 32.38           O  
ANISOU  280  O   THR A  31     3767   4018   4516   -119    -44    270       O  
ATOM    281  CB  THR A  31      67.131 -44.065  -7.499  1.00 40.06           C  
ANISOU  281  CB  THR A  31     4749   4858   5612    -40    -21    314       C  
ATOM    282  OG1 THR A  31      68.464 -43.838  -7.981  1.00 42.33           O  
ANISOU  282  OG1 THR A  31     5015   5125   5944     -5    -18    342       O  
ATOM    283  CG2 THR A  31      66.233 -44.515  -8.662  1.00 40.00           C  
ANISOU  283  CG2 THR A  31     4791   4787   5620    -51     13    274       C  
ATOM    284  N   VAL A  32      64.200 -42.602  -7.103  1.00 31.59           N  
ANISOU  284  N   VAL A  32     3678   3854   4470   -108    -31    187       N  
ATOM    285  CA  VAL A  32      62.799 -42.801  -6.753  1.00 28.00           C  
ANISOU  285  CA  VAL A  32     3219   3418   4003   -136    -15    172       C  
ATOM    286  C   VAL A  32      62.258 -43.961  -7.580  1.00 31.42           C  
ANISOU  286  C   VAL A  32     3679   3797   4461   -152     -3    191       C  
ATOM    287  O   VAL A  32      62.404 -43.977  -8.812  1.00 31.84           O  
ANISOU  287  O   VAL A  32     3756   3803   4538   -150     -7    176       O  
ATOM    288  CB  VAL A  32      61.976 -41.526  -7.005  1.00 31.89           C  
ANISOU  288  CB  VAL A  32     3685   3925   4506   -136    -15    117       C  
ATOM    289  CG1 VAL A  32      60.514 -41.764  -6.635  1.00 30.56           C  
ANISOU  289  CG1 VAL A  32     3494   3776   4341   -161      9    115       C  
ATOM    290  CG2 VAL A  32      62.542 -40.358  -6.210  1.00 32.62           C  
ANISOU  290  CG2 VAL A  32     3768   4054   4572   -129    -17     86       C  
ATOM    291  N   TYR A  33      61.617 -44.921  -6.911  1.00 30.16           N  
ANISOU  291  N   TYR A  33     3524   3645   4290   -178     16    223       N  
ATOM    292  CA  TYR A  33      60.992 -46.061  -7.566  1.00 28.62           C  
ANISOU  292  CA  TYR A  33     3361   3398   4115   -210     30    237       C  
ATOM    293  C   TYR A  33      59.505 -46.072  -7.264  1.00 32.49           C  
ANISOU  293  C   TYR A  33     3819   3921   4604   -254     33    229       C  
ATOM    294  O   TYR A  33      59.056 -45.552  -6.238  1.00 35.09           O  
ANISOU  294  O   TYR A  33     4111   4308   4914   -252     46    228       O  
ATOM    295  CB  TYR A  33      61.580 -47.398  -7.081  1.00 30.45           C  
ANISOU  295  CB  TYR A  33     3626   3592   4352   -206     57    297       C  
ATOM    296  CG  TYR A  33      63.053 -47.534  -7.302  1.00 34.06           C  
ANISOU  296  CG  TYR A  33     4097   4013   4829   -158     63    325       C  
ATOM    297  CD1 TYR A  33      63.947 -47.013  -6.390  1.00 37.96           C  
ANISOU  297  CD1 TYR A  33     4556   4562   5306   -127     42    356       C  
ATOM    298  CD2 TYR A  33      63.554 -48.202  -8.414  1.00 33.23           C  
ANISOU  298  CD2 TYR A  33     4042   3821   4763   -147     94    323       C  
ATOM    299  CE1 TYR A  33      65.279 -47.131  -6.582  1.00 32.58           C  
ANISOU  299  CE1 TYR A  33     3868   3854   4657    -84     43    396       C  
ATOM    300  CE2 TYR A  33      64.918 -48.323  -8.615  1.00 39.02           C  
ANISOU  300  CE2 TYR A  33     4776   4518   5530    -94    114    357       C  
ATOM    301  CZ  TYR A  33      65.772 -47.779  -7.690  1.00 44.82           C  
ANISOU  301  CZ  TYR A  33     5455   5314   6259    -61     84    399       C  
ATOM    302  OH  TYR A  33      67.130 -47.870  -7.843  1.00 48.53           O  
ANISOU  302  OH  TYR A  33     5906   5759   6776    -10     98    447       O  
ATOM    303  N   THR A  34      58.751 -46.719  -8.146  1.00 30.24           N  
ANISOU  303  N   THR A  34     3554   3598   4339   -299     27    227       N  
ATOM    304  CA  THR A  34      57.364 -47.041  -7.854  1.00 27.87           C  
ANISOU  304  CA  THR A  34     3217   3323   4050   -350     31    239       C  
ATOM    305  C   THR A  34      57.121 -48.521  -8.111  1.00 32.45           C  
ANISOU  305  C   THR A  34     3849   3844   4635   -404     46    265       C  
ATOM    306  O   THR A  34      57.784 -49.148  -8.939  1.00 35.21           O  
ANISOU  306  O   THR A  34     4268   4124   4987   -410     50    258       O  
ATOM    307  CB  THR A  34      56.403 -46.181  -8.678  1.00 31.90           C  
ANISOU  307  CB  THR A  34     3677   3857   4586   -371     -5    216       C  
ATOM    308  OG1 THR A  34      55.072 -46.367  -8.182  1.00 35.81           O  
ANISOU  308  OG1 THR A  34     4112   4390   5104   -412      6    240       O  
ATOM    309  CG2 THR A  34      56.440 -46.577 -10.146  1.00 32.94           C  
ANISOU  309  CG2 THR A  34     3861   3938   4718   -414    -42    204       C  
ATOM    310  N   LYS A  35      56.172 -49.082  -7.378  1.00 32.69           N  
ANISOU  310  N   LYS A  35     3852   3899   4672   -445     65    295       N  
ATOM    311  CA  LYS A  35      55.895 -50.509  -7.454  1.00 34.07           C  
ANISOU  311  CA  LYS A  35     4076   4014   4856   -502     86    324       C  
ATOM    312  C   LYS A  35      54.829 -50.728  -8.516  1.00 45.75           C  
ANISOU  312  C   LYS A  35     5553   5478   6354   -586     50    306       C  
ATOM    313  O   LYS A  35      53.744 -50.140  -8.436  1.00 40.08           O  
ANISOU  313  O   LYS A  35     4753   4822   5655   -612     26    311       O  
ATOM    314  CB  LYS A  35      55.444 -51.050  -6.098  1.00 41.44           C  
ANISOU  314  CB  LYS A  35     4983   4980   5783   -512    127    374       C  
ATOM    315  CG  LYS A  35      55.131 -52.555  -6.099  1.00 49.52           C  
ANISOU  315  CG  LYS A  35     6058   5933   6824   -574    155    412       C  
ATOM    316  CD  LYS A  35      54.650 -53.046  -4.736  1.00 59.58           C  
ANISOU  316  CD  LYS A  35     7305   7245   8089   -587    197    470       C  
ATOM    317  CE  LYS A  35      55.809 -53.359  -3.818  1.00 64.86           C  
ANISOU  317  CE  LYS A  35     8008   7907   8730   -526    222    520       C  
ATOM    318  NZ  LYS A  35      55.353 -54.051  -2.580  1.00 73.53           N  
ANISOU  318  NZ  LYS A  35     9097   9030   9810   -552    262    588       N  
ATOM    319  N   VAL A  36      55.153 -51.538  -9.525  1.00 41.58           N  
ANISOU  319  N   VAL A  36     5112   4866   5820   -630     47    287       N  
ATOM    320  CA  VAL A  36      54.237 -51.880 -10.612  1.00 41.62           C  
ANISOU  320  CA  VAL A  36     5137   4853   5824   -733      3    268       C  
ATOM    321  C   VAL A  36      54.134 -53.399 -10.647  1.00 52.45           C  
ANISOU  321  C   VAL A  36     6594   6135   7200   -805     42    277       C  
ATOM    322  O   VAL A  36      55.103 -54.086 -11.001  1.00 38.86           O  
ANISOU  322  O   VAL A  36     4973   4320   5472   -787     89    260       O  
ATOM    323  CB  VAL A  36      54.707 -51.326 -11.964  1.00 42.96           C  
ANISOU  323  CB  VAL A  36     5357   5001   5965   -739    -37    221       C  
ATOM    324  CG1 VAL A  36      53.716 -51.670 -13.054  1.00 49.33           C  
ANISOU  324  CG1 VAL A  36     6188   5803   6754   -863    -97    208       C  
ATOM    325  CG2 VAL A  36      54.924 -49.812 -11.887  1.00 40.91           C  
ANISOU  325  CG2 VAL A  36     5019   4817   5710   -660    -67    216       C  
ATOM    326  N   ASP A  37      52.971 -53.922 -10.255  1.00 44.80           N  
ANISOU  326  N   ASP A  37     5582   5189   6252   -884     34    308       N  
ATOM    327  CA  ASP A  37      52.694 -55.358 -10.260  1.00 52.44           C  
ANISOU  327  CA  ASP A  37     6626   6071   7230   -969     70    320       C  
ATOM    328  C   ASP A  37      53.786 -56.147  -9.542  1.00 54.65           C  
ANISOU  328  C   ASP A  37     6973   6270   7522   -897    153    345       C  
ATOM    329  O   ASP A  37      54.331 -57.127 -10.056  1.00 53.08           O  
ANISOU  329  O   ASP A  37     6887   5955   7328   -921    199    327       O  
ATOM    330  CB  ASP A  37      52.487 -55.865 -11.686  1.00 68.47           C  
ANISOU  330  CB  ASP A  37     8753   8032   9231  -1079     36    267       C  
ATOM    331  CG  ASP A  37      51.228 -55.302 -12.322  1.00 83.31           C  
ANISOU  331  CG  ASP A  37    10554   9996  11103  -1176    -60    269       C  
ATOM    332  OD1 ASP A  37      51.339 -54.545 -13.310  1.00 89.21           O  
ANISOU  332  OD1 ASP A  37    11309  10771  11816  -1184   -119    237       O  
ATOM    333  OD2 ASP A  37      50.126 -55.598 -11.812  1.00 89.73           O  
ANISOU  333  OD2 ASP A  37    11289  10852  11951  -1243    -76    313       O  
ATOM    334  N   GLY A  38      54.107 -55.706  -8.333  1.00 47.52           N  
ANISOU  334  N   GLY A  38     6002   5429   6624   -809    174    390       N  
ATOM    335  CA  GLY A  38      55.000 -56.439  -7.471  1.00 43.94           C  
ANISOU  335  CA  GLY A  38     5588   4923   6185   -747    238    442       C  
ATOM    336  C   GLY A  38      56.486 -56.176  -7.656  1.00 41.56           C  
ANISOU  336  C   GLY A  38     5325   4584   5883   -647    258    437       C  
ATOM    337  O   GLY A  38      57.283 -56.727  -6.890  1.00 52.12           O  
ANISOU  337  O   GLY A  38     6677   5886   7239   -588    302    498       O  
ATOM    338  N   VAL A  39      56.896 -55.371  -8.643  1.00 40.17           N  
ANISOU  338  N   VAL A  39     5159   4413   5689   -627    227    377       N  
ATOM    339  CA  VAL A  39      58.312 -55.048  -8.815  1.00 40.15           C  
ANISOU  339  CA  VAL A  39     5179   4382   5694   -532    249    377       C  
ATOM    340  C   VAL A  39      58.498 -53.538  -8.872  1.00 39.61           C  
ANISOU  340  C   VAL A  39     5039   4413   5596   -485    194    347       C  
ATOM    341  O   VAL A  39      57.593 -52.784  -9.237  1.00 38.84           O  
ANISOU  341  O   VAL A  39     4900   4379   5480   -528    143    311       O  
ATOM    342  CB  VAL A  39      58.940 -55.696 -10.073  1.00 46.41           C  
ANISOU  342  CB  VAL A  39     6082   5050   6502   -546    295    333       C  
ATOM    343  CG1 VAL A  39      58.843 -57.220  -9.992  1.00 53.11           C  
ANISOU  343  CG1 VAL A  39     7014   5777   7390   -589    367    360       C  
ATOM    344  CG2 VAL A  39      58.306 -55.156 -11.343  1.00 43.20           C  
ANISOU  344  CG2 VAL A  39     5704   4657   6053   -622    246    255       C  
ATOM    345  N   ASP A  40      59.719 -53.113  -8.538  1.00 34.30           N  
ANISOU  345  N   ASP A  40     4352   3750   4931   -397    204    369       N  
ATOM    346  CA  ASP A  40      60.081 -51.699  -8.494  1.00 33.76           C  
ANISOU  346  CA  ASP A  40     4224   3764   4839   -350    160    344       C  
ATOM    347  C   ASP A  40      60.579 -51.221  -9.849  1.00 33.14           C  
ANISOU  347  C   ASP A  40     4185   3645   4760   -342    154    288       C  
ATOM    348  O   ASP A  40      61.404 -51.877 -10.486  1.00 35.78           O  
ANISOU  348  O   ASP A  40     4588   3890   5119   -324    203    287       O  
ATOM    349  CB  ASP A  40      61.152 -51.473  -7.430  1.00 34.09           C  
ANISOU  349  CB  ASP A  40     4228   3843   4883   -276    165    400       C  
ATOM    350  CG  ASP A  40      60.631 -51.766  -6.026  1.00 47.53           C  
ANISOU  350  CG  ASP A  40     5893   5604   6562   -290    165    455       C  
ATOM    351  OD1 ASP A  40      59.428 -51.496  -5.781  1.00 46.17           O  
ANISOU  351  OD1 ASP A  40     5692   5481   6368   -340    153    431       O  
ATOM    352  OD2 ASP A  40      61.408 -52.264  -5.183  1.00 48.49           O  
ANISOU  352  OD2 ASP A  40     6011   5724   6688   -254    179    528       O  
ATOM    353  N   VAL A  41      60.073 -50.071 -10.279  1.00 30.41           N  
ANISOU  353  N   VAL A  41     3800   3363   4392   -355    103    246       N  
ATOM    354  CA  VAL A  41      60.438 -49.445 -11.543  1.00 29.08           C  
ANISOU  354  CA  VAL A  41     3663   3173   4212   -354     88    199       C  
ATOM    355  C   VAL A  41      60.989 -48.067 -11.216  1.00 29.83           C  
ANISOU  355  C   VAL A  41     3693   3336   4305   -292     59    194       C  
ATOM    356  O   VAL A  41      60.354 -47.304 -10.480  1.00 32.99           O  
ANISOU  356  O   VAL A  41     4024   3811   4699   -288     29    197       O  
ATOM    357  CB  VAL A  41      59.224 -49.346 -12.490  1.00 32.02           C  
ANISOU  357  CB  VAL A  41     4051   3555   4560   -442     42    165       C  
ATOM    358  CG1 VAL A  41      59.629 -48.702 -13.816  1.00 34.67           C  
ANISOU  358  CG1 VAL A  41     4430   3873   4871   -447     24    125       C  
ATOM    359  CG2 VAL A  41      58.589 -50.746 -12.696  1.00 36.71           C  
ANISOU  359  CG2 VAL A  41     4711   4084   5153   -524     66    167       C  
ATOM    360  N   GLU A  42      62.166 -47.750 -11.754  1.00 30.50           N  
ANISOU  360  N   GLU A  42     3802   3389   4399   -245     78    186       N  
ATOM    361  CA  GLU A  42      62.783 -46.454 -11.501  1.00 30.63           C  
ANISOU  361  CA  GLU A  42     3763   3461   4416   -194     52    180       C  
ATOM    362  C   GLU A  42      62.038 -45.331 -12.212  1.00 37.97           C  
ANISOU  362  C   GLU A  42     4670   4426   5329   -218      6    142       C  
ATOM    363  O   GLU A  42      61.815 -45.381 -13.425  1.00 36.03           O  
ANISOU  363  O   GLU A  42     4474   4148   5070   -254     -2    118       O  
ATOM    364  CB  GLU A  42      64.253 -46.476 -11.946  1.00 31.55           C  
ANISOU  364  CB  GLU A  42     3902   3529   4556   -142     89    191       C  
ATOM    365  CG  GLU A  42      64.892 -45.095 -11.975  1.00 33.54           C  
ANISOU  365  CG  GLU A  42     4107   3827   4809   -106     60    178       C  
ATOM    366  CD  GLU A  42      66.359 -45.138 -12.389  1.00 49.18           C  
ANISOU  366  CD  GLU A  42     6097   5766   6825    -57    100    199       C  
ATOM    367  OE1 GLU A  42      67.050 -46.129 -12.065  1.00 42.11           O  
ANISOU  367  OE1 GLU A  42     5208   4827   5963    -29    144    246       O  
ATOM    368  OE2 GLU A  42      66.811 -44.187 -13.054  1.00 49.98           O  
ANISOU  368  OE2 GLU A  42     6192   5872   6927    -45     92    176       O  
ATOM    369  N   LEU A  43      61.678 -44.296 -11.456  1.00 32.05           N  
ANISOU  369  N   LEU A  43     3852   3743   4581   -199    -21    138       N  
ATOM    370  CA  LEU A  43      61.025 -43.125 -12.026  1.00 31.45           C  
ANISOU  370  CA  LEU A  43     3743   3698   4511   -206    -58    115       C  
ATOM    371  C   LEU A  43      61.953 -41.928 -12.172  1.00 33.65           C  
ANISOU  371  C   LEU A  43     4006   3983   4798   -160    -62     99       C  
ATOM    372  O   LEU A  43      61.717 -41.071 -13.038  1.00 35.97           O  
ANISOU  372  O   LEU A  43     4294   4276   5098   -162    -87     87       O  
ATOM    373  CB  LEU A  43      59.843 -42.704 -11.153  1.00 33.96           C  
ANISOU  373  CB  LEU A  43     3993   4070   4840   -216    -67    120       C  
ATOM    374  CG  LEU A  43      58.669 -43.645 -11.051  1.00 39.85           C  
ANISOU  374  CG  LEU A  43     4732   4821   5588   -270    -70    140       C  
ATOM    375  CD1 LEU A  43      57.579 -42.930 -10.285  1.00 42.03           C  
ANISOU  375  CD1 LEU A  43     4926   5152   5890   -266    -66    145       C  
ATOM    376  CD2 LEU A  43      58.223 -44.066 -12.451  1.00 40.35           C  
ANISOU  376  CD2 LEU A  43     4835   4852   5644   -328   -105    139       C  
ATOM    377  N   PHE A  44      62.978 -41.819 -11.328  1.00 29.06           N  
ANISOU  377  N   PHE A  44     3413   3411   4216   -124    -45    107       N  
ATOM    378  CA  PHE A  44      63.790 -40.603 -11.318  1.00 28.96           C  
ANISOU  378  CA  PHE A  44     3379   3410   4214    -92    -53     91       C  
ATOM    379  C   PHE A  44      65.085 -40.872 -10.577  1.00 32.01           C  
ANISOU  379  C   PHE A  44     3760   3803   4600    -68    -42    116       C  
ATOM    380  O   PHE A  44      65.056 -41.426  -9.477  1.00 36.00           O  
ANISOU  380  O   PHE A  44     4253   4338   5088    -74    -39    139       O  
ATOM    381  CB  PHE A  44      63.018 -39.459 -10.644  1.00 30.85           C  
ANISOU  381  CB  PHE A  44     3572   3692   4458    -91    -64     65       C  
ATOM    382  CG  PHE A  44      63.835 -38.195 -10.444  1.00 33.23           C  
ANISOU  382  CG  PHE A  44     3859   3999   4768    -68    -67     42       C  
ATOM    383  CD1 PHE A  44      63.966 -37.270 -11.473  1.00 32.87           C  
ANISOU  383  CD1 PHE A  44     3814   3926   4748    -57    -77     30       C  
ATOM    384  CD2 PHE A  44      64.423 -37.911  -9.214  1.00 32.22           C  
ANISOU  384  CD2 PHE A  44     3720   3906   4618    -70    -63     34       C  
ATOM    385  CE1 PHE A  44      64.698 -36.094 -11.287  1.00 32.10           C  
ANISOU  385  CE1 PHE A  44     3706   3826   4664    -44    -77      9       C  
ATOM    386  CE2 PHE A  44      65.153 -36.743  -9.020  1.00 30.41           C  
ANISOU  386  CE2 PHE A  44     3482   3679   4392    -66    -69      8       C  
ATOM    387  CZ  PHE A  44      65.299 -35.837 -10.059  1.00 28.01           C  
ANISOU  387  CZ  PHE A  44     3179   3339   4126    -51    -73     -6       C  
ATOM    388  N   GLU A  45      66.213 -40.482 -11.172  1.00 29.57           N  
ANISOU  388  N   GLU A  45     3455   3471   4311    -46    -37    120       N  
ATOM    389  CA  GLU A  45      67.514 -40.555 -10.522  1.00 30.08           C  
ANISOU  389  CA  GLU A  45     3492   3549   4388    -25    -36    156       C  
ATOM    390  C   GLU A  45      67.999 -39.130 -10.276  1.00 32.82           C  
ANISOU  390  C   GLU A  45     3809   3927   4736    -27    -63    130       C  
ATOM    391  O   GLU A  45      68.120 -38.346 -11.221  1.00 35.36           O  
ANISOU  391  O   GLU A  45     4138   4221   5076    -21    -59    106       O  
ATOM    392  CB  GLU A  45      68.540 -41.312 -11.368  1.00 36.55           C  
ANISOU  392  CB  GLU A  45     4331   4312   5246      4      3    192       C  
ATOM    393  CG  GLU A  45      69.887 -41.362 -10.658  1.00 41.41           C  
ANISOU  393  CG  GLU A  45     4894   4948   5890     28     -3    249       C  
ATOM    394  CD  GLU A  45      71.012 -41.975 -11.487  1.00 51.19           C  
ANISOU  394  CD  GLU A  45     6135   6127   7190     68     52    292       C  
ATOM    395  OE1 GLU A  45      70.874 -42.094 -12.726  1.00 50.13           O  
ANISOU  395  OE1 GLU A  45     6054   5932   7060     73     99    261       O  
ATOM    396  OE2 GLU A  45      72.041 -42.328 -10.876  1.00 57.83           O  
ANISOU  396  OE2 GLU A  45     6921   6981   8070     93     51    363       O  
ATOM    397  N   ASN A  46      68.264 -38.802  -9.015  1.00 30.51           N  
ANISOU  397  N   ASN A  46     3488   3688   4417    -44    -88    135       N  
ATOM    398  CA  ASN A  46      68.632 -37.438  -8.630  1.00 30.03           C  
ANISOU  398  CA  ASN A  46     3411   3652   4348    -62   -111     98       C  
ATOM    399  C   ASN A  46      70.090 -37.166  -8.982  1.00 33.81           C  
ANISOU  399  C   ASN A  46     3860   4123   4862    -54   -123    132       C  
ATOM    400  O   ASN A  46      70.995 -37.821  -8.455  1.00 34.00           O  
ANISOU  400  O   ASN A  46     3853   4173   4892    -53   -139    193       O  
ATOM    401  CB  ASN A  46      68.415 -37.254  -7.132  1.00 32.93           C  
ANISOU  401  CB  ASN A  46     3774   4080   4657   -100   -131     87       C  
ATOM    402  CG  ASN A  46      68.706 -35.848  -6.672  1.00 34.91           C  
ANISOU  402  CG  ASN A  46     4027   4348   4891   -134   -145     34       C  
ATOM    403  OD1 ASN A  46      68.678 -34.899  -7.465  1.00 31.95           O  
ANISOU  403  OD1 ASN A  46     3655   3932   4553   -122   -132     -2       O  
ATOM    404  ND2 ASN A  46      69.011 -35.704  -5.380  1.00 30.81           N  
ANISOU  404  ND2 ASN A  46     3511   3886   4308   -182   -171     32       N  
ATOM    405  N   LYS A  47      70.315 -36.205  -9.873  1.00 32.80           N  
ANISOU  405  N   LYS A  47     3735   3962   4764    -48   -114    103       N  
ATOM    406  CA  LYS A  47      71.644 -35.725 -10.237  1.00 34.39           C  
ANISOU  406  CA  LYS A  47     3904   4156   5005    -48   -121    130       C  
ATOM    407  C   LYS A  47      71.918 -34.323  -9.699  1.00 36.55           C  
ANISOU  407  C   LYS A  47     4168   4451   5268    -90   -150     88       C  
ATOM    408  O   LYS A  47      72.974 -33.750  -9.988  1.00 36.87           O  
ANISOU  408  O   LYS A  47     4179   4487   5344   -101   -159    105       O  
ATOM    409  CB  LYS A  47      71.814 -35.742 -11.765  1.00 38.08           C  
ANISOU  409  CB  LYS A  47     4393   4563   5514    -15    -78    134       C  
ATOM    410  CG  LYS A  47      71.712 -37.149 -12.390  1.00 41.35           C  
ANISOU  410  CG  LYS A  47     4833   4942   5937     17    -36    168       C  
ATOM    411  CD  LYS A  47      72.564 -38.167 -11.628  1.00 46.62           C  
ANISOU  411  CD  LYS A  47     5458   5628   6626     33    -35    236       C  
ATOM    412  CE  LYS A  47      74.055 -37.813 -11.597  1.00 65.98           C  
ANISOU  412  CE  LYS A  47     7845   8092   9133     40    -38    289       C  
ATOM    413  NZ  LYS A  47      74.856 -38.491 -12.651  1.00 68.52           N  
ANISOU  413  NZ  LYS A  47     8165   8352   9516     87     36    332       N  
ATOM    414  N   THR A  48      70.992 -33.768  -8.917  1.00 33.58           N  
ANISOU  414  N   THR A  48     3818   4092   4848   -117   -156     31       N  
ATOM    415  CA  THR A  48      71.122 -32.445  -8.332  1.00 31.31           C  
ANISOU  415  CA  THR A  48     3541   3809   4545   -163   -168    -24       C  
ATOM    416  C   THR A  48      71.795 -32.523  -6.964  1.00 34.77           C  
ANISOU  416  C   THR A  48     3969   4317   4927   -225   -215    -14       C  
ATOM    417  O   THR A  48      72.042 -33.600  -6.419  1.00 34.57           O  
ANISOU  417  O   THR A  48     3922   4337   4875   -225   -240     44       O  
ATOM    418  CB  THR A  48      69.747 -31.792  -8.188  1.00 31.35           C  
ANISOU  418  CB  THR A  48     3584   3787   4539   -157   -132    -91       C  
ATOM    419  OG1 THR A  48      69.127 -32.245  -6.973  1.00 31.51           O  
ANISOU  419  OG1 THR A  48     3622   3855   4496   -182   -130   -109       O  
ATOM    420  CG2 THR A  48      68.853 -32.138  -9.377  1.00 30.28           C  
ANISOU  420  CG2 THR A  48     3451   3609   4443   -102   -104    -77       C  
ATOM    421  N   THR A  49      72.057 -31.359  -6.377  1.00 31.45           N  
ANISOU  421  N   THR A  49     3568   3900   4480   -286   -229    -68       N  
ATOM    422  CA  THR A  49      72.540 -31.277  -5.004  1.00 33.47           C  
ANISOU  422  CA  THR A  49     3834   4226   4657   -368   -278    -74       C  
ATOM    423  C   THR A  49      71.409 -31.064  -3.988  1.00 35.21           C  
ANISOU  423  C   THR A  49     4120   4459   4798   -397   -244   -147       C  
ATOM    424  O   THR A  49      71.685 -30.819  -2.805  1.00 37.04           O  
ANISOU  424  O   THR A  49     4385   4745   4943   -481   -276   -171       O  
ATOM    425  CB  THR A  49      73.581 -30.163  -4.883  1.00 37.45           C  
ANISOU  425  CB  THR A  49     4331   4731   5168   -439   -314    -95       C  
ATOM    426  OG1 THR A  49      72.975 -28.918  -5.249  1.00 37.51           O  
ANISOU  426  OG1 THR A  49     4390   4663   5200   -440   -259   -184       O  
ATOM    427  CG2 THR A  49      74.755 -30.434  -5.829  1.00 34.67           C  
ANISOU  427  CG2 THR A  49     3901   4372   4898   -410   -340    -11       C  
ATOM    428  N   LEU A  50      70.153 -31.164  -4.418  1.00 31.94           N  
ANISOU  428  N   LEU A  50     3725   3999   4410   -337   -180   -178       N  
ATOM    429  CA  LEU A  50      68.963 -31.117  -3.573  1.00 32.29           C  
ANISOU  429  CA  LEU A  50     3818   4049   4400   -346   -128   -235       C  
ATOM    430  C   LEU A  50      68.611 -32.510  -3.050  1.00 33.22           C  
ANISOU  430  C   LEU A  50     3924   4226   4472   -336   -141   -176       C  
ATOM    431  O   LEU A  50      69.075 -33.524  -3.592  1.00 34.05           O  
ANISOU  431  O   LEU A  50     3984   4343   4611   -300   -176    -96       O  
ATOM    432  CB  LEU A  50      67.781 -30.573  -4.372  1.00 31.72           C  
ANISOU  432  CB  LEU A  50     3750   3902   4400   -282    -55   -275       C  
ATOM    433  CG  LEU A  50      67.845 -29.125  -4.848  1.00 43.93           C  
ANISOU  433  CG  LEU A  50     5316   5375   6002   -282    -22   -333       C  
ATOM    434  CD1 LEU A  50      66.687 -28.858  -5.793  1.00 41.40           C  
ANISOU  434  CD1 LEU A  50     4975   4989   5766   -205     33   -333       C  
ATOM    435  CD2 LEU A  50      67.800 -28.179  -3.673  1.00 48.53           C  
ANISOU  435  CD2 LEU A  50     5966   5952   6522   -353     16   -422       C  
ATOM    436  N   PRO A  51      67.784 -32.596  -1.998  1.00 31.39           N  
ANISOU  436  N   PRO A  51     3737   4023   4167   -366   -104   -215       N  
ATOM    437  CA  PRO A  51      67.271 -33.911  -1.568  1.00 32.88           C  
ANISOU  437  CA  PRO A  51     3916   4256   4322   -351   -104   -158       C  
ATOM    438  C   PRO A  51      66.492 -34.586  -2.685  1.00 32.06           C  
ANISOU  438  C   PRO A  51     3773   4105   4304   -271    -76   -125       C  
ATOM    439  O   PRO A  51      65.776 -33.928  -3.441  1.00 32.23           O  
ANISOU  439  O   PRO A  51     3788   4068   4389   -232    -32   -165       O  
ATOM    440  CB  PRO A  51      66.361 -33.573  -0.377  1.00 33.27           C  
ANISOU  440  CB  PRO A  51     4025   4328   4286   -396    -42   -224       C  
ATOM    441  CG  PRO A  51      66.920 -32.237   0.137  1.00 32.33           C  
ANISOU  441  CG  PRO A  51     3961   4202   4121   -465    -40   -306       C  
ATOM    442  CD  PRO A  51      67.362 -31.510  -1.092  1.00 33.87           C  
ANISOU  442  CD  PRO A  51     4120   4329   4422   -422    -51   -313       C  
ATOM    443  N   VAL A  52      66.627 -35.919  -2.771  1.00 29.41           N  
ANISOU  443  N   VAL A  52     3412   3792   3970   -252   -103    -46       N  
ATOM    444  CA  VAL A  52      66.059 -36.677  -3.887  1.00 32.20           C  
ANISOU  444  CA  VAL A  52     3739   4099   4395   -194    -86    -14       C  
ATOM    445  C   VAL A  52      64.555 -36.422  -4.044  1.00 31.11           C  
ANISOU  445  C   VAL A  52     3605   3936   4279   -175    -27    -58       C  
ATOM    446  O   VAL A  52      64.055 -36.257  -5.166  1.00 31.05           O  
ANISOU  446  O   VAL A  52     3577   3880   4339   -138    -16    -61       O  
ATOM    447  CB  VAL A  52      66.365 -38.184  -3.704  1.00 30.20           C  
ANISOU  447  CB  VAL A  52     3475   3868   4132   -187   -109     71       C  
ATOM    448  CG1 VAL A  52      65.898 -38.668  -2.331  1.00 30.47           C  
ANISOU  448  CG1 VAL A  52     3531   3961   4084   -229   -100     84       C  
ATOM    449  CG2 VAL A  52      65.709 -39.013  -4.812  1.00 32.66           C  
ANISOU  449  CG2 VAL A  52     3778   4126   4506   -145    -85     92       C  
ATOM    450  N   ASN A  53      63.800 -36.389  -2.939  1.00 30.50           N  
ANISOU  450  N   ASN A  53     3548   3892   4148   -203     14    -84       N  
ATOM    451  CA  ASN A  53      62.355 -36.221  -3.098  1.00 30.98           C  
ANISOU  451  CA  ASN A  53     3593   3929   4248   -180     77   -111       C  
ATOM    452  C   ASN A  53      61.993 -34.806  -3.527  1.00 34.79           C  
ANISOU  452  C   ASN A  53     4070   4363   4785   -156    116   -172       C  
ATOM    453  O   ASN A  53      60.950 -34.602  -4.167  1.00 33.57           O  
ANISOU  453  O   ASN A  53     3878   4175   4703   -119    148   -170       O  
ATOM    454  CB  ASN A  53      61.610 -36.564  -1.813  1.00 33.10           C  
ANISOU  454  CB  ASN A  53     3884   4243   4451   -212    129   -121       C  
ATOM    455  CG  ASN A  53      62.010 -35.662  -0.659  1.00 33.66           C  
ANISOU  455  CG  ASN A  53     4011   4341   4438   -261    156   -184       C  
ATOM    456  OD1 ASN A  53      63.201 -35.502  -0.364  1.00 32.98           O  
ANISOU  456  OD1 ASN A  53     3950   4281   4299   -298     97   -179       O  
ATOM    457  ND2 ASN A  53      61.014 -35.073   0.006  1.00 34.10           N  
ANISOU  457  ND2 ASN A  53     4085   4389   4481   -266    248   -241       N  
ATOM    458  N   VAL A  54      62.835 -33.827  -3.195  1.00 30.78           N  
ANISOU  458  N   VAL A  54     3596   3849   4251   -181    110   -218       N  
ATOM    459  CA  VAL A  54      62.589 -32.446  -3.618  1.00 33.28           C  
ANISOU  459  CA  VAL A  54     3913   4104   4627   -159    152   -274       C  
ATOM    460  C   VAL A  54      62.924 -32.275  -5.092  1.00 34.11           C  
ANISOU  460  C   VAL A  54     3982   4166   4813   -117    107   -238       C  
ATOM    461  O   VAL A  54      62.145 -31.694  -5.861  1.00 33.01           O  
ANISOU  461  O   VAL A  54     3812   3979   4753    -74    135   -237       O  
ATOM    462  CB  VAL A  54      63.408 -31.475  -2.745  1.00 33.63           C  
ANISOU  462  CB  VAL A  54     4019   4150   4610   -215    162   -342       C  
ATOM    463  CG1 VAL A  54      63.222 -30.023  -3.218  1.00 30.68           C  
ANISOU  463  CG1 VAL A  54     3652   3695   4309   -191    213   -399       C  
ATOM    464  CG2 VAL A  54      63.027 -31.622  -1.279  1.00 32.79           C  
ANISOU  464  CG2 VAL A  54     3965   4089   4404   -268    213   -383       C  
ATOM    465  N   ALA A  55      64.093 -32.783  -5.505  1.00 31.81           N  
ANISOU  465  N   ALA A  55     3691   3891   4503   -130     40   -199       N  
ATOM    466  CA  ALA A  55      64.466 -32.744  -6.913  1.00 34.26           C  
ANISOU  466  CA  ALA A  55     3979   4164   4876    -97      7   -164       C  
ATOM    467  C   ALA A  55      63.427 -33.443  -7.778  1.00 32.47           C  
ANISOU  467  C   ALA A  55     3723   3924   4689    -64      8   -124       C  
ATOM    468  O   ALA A  55      63.108 -32.973  -8.878  1.00 32.24           O  
ANISOU  468  O   ALA A  55     3676   3856   4716    -37      2   -111       O  
ATOM    469  CB  ALA A  55      65.845 -33.383  -7.114  1.00 31.37           C  
ANISOU  469  CB  ALA A  55     3614   3820   4487   -112    -47   -122       C  
ATOM    470  N   PHE A  56      62.894 -34.576  -7.295  1.00 28.23           N  
ANISOU  470  N   PHE A  56     3182   3424   4121    -74     11    -99       N  
ATOM    471  CA  PHE A  56      61.865 -35.307  -8.032  1.00 30.92           C  
ANISOU  471  CA  PHE A  56     3497   3757   4494    -61      7    -63       C  
ATOM    472  C   PHE A  56      60.642 -34.440  -8.282  1.00 28.59           C  
ANISOU  472  C   PHE A  56     3163   3441   4261    -37     39    -73       C  
ATOM    473  O   PHE A  56      60.107 -34.412  -9.395  1.00 30.56           O  
ANISOU  473  O   PHE A  56     3385   3670   4556    -24     13    -39       O  
ATOM    474  CB  PHE A  56      61.468 -36.554  -7.241  1.00 29.89           C  
ANISOU  474  CB  PHE A  56     3370   3665   4321    -84     15    -39       C  
ATOM    475  CG  PHE A  56      60.351 -37.356  -7.856  1.00 31.85           C  
ANISOU  475  CG  PHE A  56     3594   3910   4599    -88     11     -4       C  
ATOM    476  CD1 PHE A  56      60.448 -37.849  -9.152  1.00 31.51           C  
ANISOU  476  CD1 PHE A  56     3559   3839   4575    -91    -29     24       C  
ATOM    477  CD2 PHE A  56      59.233 -37.682  -7.099  1.00 32.02           C  
ANISOU  477  CD2 PHE A  56     3588   3957   4621    -99     48      0       C  
ATOM    478  CE1 PHE A  56      59.429 -38.641  -9.703  1.00 33.42           C  
ANISOU  478  CE1 PHE A  56     3785   4080   4833   -115    -42     55       C  
ATOM    479  CE2 PHE A  56      58.206 -38.472  -7.633  1.00 35.08           C  
ANISOU  479  CE2 PHE A  56     3945   4345   5037   -116     37     38       C  
ATOM    480  CZ  PHE A  56      58.302 -38.955  -8.928  1.00 33.72           C  
ANISOU  480  CZ  PHE A  56     3784   4147   4880   -129    -14     65       C  
ATOM    481  N   GLU A  57      60.191 -33.719  -7.257  1.00 31.60           N  
ANISOU  481  N   GLU A  57     3540   3824   4643    -34     99   -116       N  
ATOM    482  CA  GLU A  57      59.007 -32.878  -7.409  1.00 33.63           C  
ANISOU  482  CA  GLU A  57     3748   4052   4978      1    148   -118       C  
ATOM    483  C   GLU A  57      59.255 -31.703  -8.357  1.00 33.09           C  
ANISOU  483  C   GLU A  57     3670   3928   4974     32    137   -116       C  
ATOM    484  O   GLU A  57      58.391 -31.362  -9.179  1.00 31.21           O  
ANISOU  484  O   GLU A  57     3377   3669   4814     63    131    -72       O  
ATOM    485  CB  GLU A  57      58.560 -32.384  -6.037  1.00 33.85           C  
ANISOU  485  CB  GLU A  57     3790   4084   4988     -2    238   -173       C  
ATOM    486  CG  GLU A  57      57.290 -31.549  -6.084  1.00 37.79           C  
ANISOU  486  CG  GLU A  57     4229   4544   5586     44    314   -169       C  
ATOM    487  CD  GLU A  57      56.710 -31.291  -4.706  1.00 52.76           C  
ANISOU  487  CD  GLU A  57     6143   6444   7460     39    424   -223       C  
ATOM    488  OE1 GLU A  57      56.906 -32.140  -3.812  1.00 59.37           O  
ANISOU  488  OE1 GLU A  57     7019   7334   8204     -6    427   -237       O  
ATOM    489  OE2 GLU A  57      56.064 -30.236  -4.521  1.00 53.55           O  
ANISOU  489  OE2 GLU A  57     6221   6488   7636     80    515   -250       O  
ATOM    490  N   LEU A  58      60.419 -31.059  -8.254  1.00 32.41           N  
ANISOU  490  N   LEU A  58     3632   3821   4861     21    131   -156       N  
ATOM    491  CA  LEU A  58      60.716 -29.953  -9.159  1.00 33.15           C  
ANISOU  491  CA  LEU A  58     3721   3859   5017     48    123   -151       C  
ATOM    492  C   LEU A  58      60.815 -30.434 -10.601  1.00 33.46           C  
ANISOU  492  C   LEU A  58     3743   3900   5071     53     52    -84       C  
ATOM    493  O   LEU A  58      60.306 -29.779 -11.520  1.00 32.41           O  
ANISOU  493  O   LEU A  58     3577   3733   5004     81     42    -44       O  
ATOM    494  CB  LEU A  58      62.008 -29.263  -8.731  1.00 31.87           C  
ANISOU  494  CB  LEU A  58     3613   3677   4818     20    126   -204       C  
ATOM    495  CG  LEU A  58      61.960 -28.619  -7.340  1.00 38.09           C  
ANISOU  495  CG  LEU A  58     4439   4456   5576     -3    198   -282       C  
ATOM    496  CD1 LEU A  58      63.299 -27.957  -7.015  1.00 42.32           C  
ANISOU  496  CD1 LEU A  58     5029   4980   6071    -50    181   -330       C  
ATOM    497  CD2 LEU A  58      60.839 -27.624  -7.269  1.00 40.84           C  
ANISOU  497  CD2 LEU A  58     4764   4742   6012     43    283   -300       C  
ATOM    498  N   TRP A  59      61.460 -31.580 -10.817  1.00 29.35           N  
ANISOU  498  N   TRP A  59     3248   3416   4488     24      6    -68       N  
ATOM    499  CA  TRP A  59      61.520 -32.156 -12.154  1.00 30.47           C  
ANISOU  499  CA  TRP A  59     3393   3556   4627     18    -48    -16       C  
ATOM    500  C   TRP A  59      60.120 -32.433 -12.693  1.00 32.96           C  
ANISOU  500  C   TRP A  59     3661   3884   4980     21    -66     32       C  
ATOM    501  O   TRP A  59      59.804 -32.099 -13.844  1.00 31.92           O  
ANISOU  501  O   TRP A  59     3516   3738   4876     24   -104     78       O  
ATOM    502  CB  TRP A  59      62.357 -33.442 -12.129  1.00 29.96           C  
ANISOU  502  CB  TRP A  59     3368   3518   4498    -10    -69    -13       C  
ATOM    503  CG  TRP A  59      62.290 -34.176 -13.415  1.00 33.71           C  
ANISOU  503  CG  TRP A  59     3863   3985   4959    -26   -106     27       C  
ATOM    504  CD1 TRP A  59      62.870 -33.812 -14.606  1.00 39.29           C  
ANISOU  504  CD1 TRP A  59     4597   4665   5667    -26   -125     45       C  
ATOM    505  CD2 TRP A  59      61.587 -35.394 -13.663  1.00 33.50           C  
ANISOU  505  CD2 TRP A  59     3844   3978   4908    -55   -124     51       C  
ATOM    506  NE1 TRP A  59      62.566 -34.739 -15.573  1.00 38.81           N  
ANISOU  506  NE1 TRP A  59     4569   4606   5574    -57   -151     72       N  
ATOM    507  CE2 TRP A  59      61.785 -35.719 -15.021  1.00 39.39           C  
ANISOU  507  CE2 TRP A  59     4630   4704   5632    -77   -154     74       C  
ATOM    508  CE3 TRP A  59      60.810 -36.242 -12.868  1.00 37.04           C  
ANISOU  508  CE3 TRP A  59     4274   4454   5346    -71   -114     53       C  
ATOM    509  CZ2 TRP A  59      61.250 -36.865 -15.599  1.00 49.01           C  
ANISOU  509  CZ2 TRP A  59     5879   5927   6816   -122   -175     92       C  
ATOM    510  CZ3 TRP A  59      60.276 -37.388 -13.449  1.00 44.36           C  
ANISOU  510  CZ3 TRP A  59     5219   5384   6249   -111   -138     78       C  
ATOM    511  CH2 TRP A  59      60.496 -37.684 -14.802  1.00 52.12           C  
ANISOU  511  CH2 TRP A  59     6251   6345   7209   -140   -170     94       C  
ATOM    512  N   ALA A  60      59.256 -33.044 -11.874  1.00 32.28           N  
ANISOU  512  N   ALA A  60     3545   3828   4892     14    -43     30       N  
ATOM    513  CA  ALA A  60      57.913 -33.344 -12.359  1.00 29.99           C  
ANISOU  513  CA  ALA A  60     3195   3555   4644      8    -66     85       C  
ATOM    514  C   ALA A  60      57.138 -32.069 -12.681  1.00 30.75           C  
ANISOU  514  C   ALA A  60     3226   3623   4835     52    -50    117       C  
ATOM    515  O   ALA A  60      56.250 -32.089 -13.539  1.00 33.16           O  
ANISOU  515  O   ALA A  60     3476   3940   5182     46    -98    187       O  
ATOM    516  CB  ALA A  60      57.129 -34.182 -11.340  1.00 30.77           C  
ANISOU  516  CB  ALA A  60     3267   3691   4733     -8    -33     80       C  
ATOM    517  N   LYS A  61      57.456 -30.959 -12.014  1.00 32.05           N  
ANISOU  517  N   LYS A  61     3396   3747   5035     92     14     73       N  
ATOM    518  CA  LYS A  61      56.749 -29.699 -12.226  1.00 32.91           C  
ANISOU  518  CA  LYS A  61     3444   3810   5250    144     50    103       C  
ATOM    519  C   LYS A  61      57.468 -28.790 -13.226  1.00 32.91           C  
ANISOU  519  C   LYS A  61     3469   3764   5270    158     17    123       C  
ATOM    520  O   LYS A  61      57.147 -27.596 -13.320  1.00 34.57           O  
ANISOU  520  O   LYS A  61     3645   3918   5571    207     58    141       O  
ATOM    521  CB  LYS A  61      56.533 -28.994 -10.885  1.00 37.83           C  
ANISOU  521  CB  LYS A  61     4066   4400   5908    177    161     38       C  
ATOM    522  CG  LYS A  61      55.518 -29.731  -9.990  1.00 36.56           C  
ANISOU  522  CG  LYS A  61     3861   4280   5750    172    208     38       C  
ATOM    523  CD  LYS A  61      55.392 -29.105  -8.608  1.00 38.51           C  
ANISOU  523  CD  LYS A  61     4131   4497   6005    192    331    -39       C  
ATOM    524  CE  LYS A  61      54.269 -29.805  -7.800  1.00 36.67           C  
ANISOU  524  CE  LYS A  61     3845   4304   5784    190    388    -26       C  
ATOM    525  NZ  LYS A  61      54.141 -29.245  -6.412  1.00 39.75           N  
ANISOU  525  NZ  LYS A  61     4275   4666   6164    201    522   -110       N  
ATOM    526  N   ARG A  62      58.405 -29.341 -13.997  1.00 32.82           N  
ANISOU  526  N   ARG A  62     3516   3770   5183    119    -46    126       N  
ATOM    527  CA  ARG A  62      59.163 -28.546 -14.959  1.00 34.94           C  
ANISOU  527  CA  ARG A  62     3815   4000   5462    126    -72    146       C  
ATOM    528  C   ARG A  62      58.234 -27.931 -16.002  1.00 37.63           C  
ANISOU  528  C   ARG A  62     4094   4327   5876    149   -112    241       C  
ATOM    529  O   ARG A  62      57.160 -28.458 -16.302  1.00 32.79           O  
ANISOU  529  O   ARG A  62     3423   3755   5282    138   -153    303       O  
ATOM    530  CB  ARG A  62      60.225 -29.404 -15.653  1.00 33.38           C  
ANISOU  530  CB  ARG A  62     3687   3827   5170     79   -121    138       C  
ATOM    531  CG  ARG A  62      59.667 -30.515 -16.566  1.00 36.01           C  
ANISOU  531  CG  ARG A  62     4022   4204   5454     36   -188    191       C  
ATOM    532  CD  ARG A  62      60.731 -31.580 -16.862  1.00 36.41           C  
ANISOU  532  CD  ARG A  62     4151   4268   5414     -5   -200    160       C  
ATOM    533  NE  ARG A  62      60.223 -32.639 -17.736  1.00 39.86           N  
ANISOU  533  NE  ARG A  62     4612   4735   5797    -57   -252    196       N  
ATOM    534  CZ  ARG A  62      59.470 -33.663 -17.330  1.00 45.76           C  
ANISOU  534  CZ  ARG A  62     5344   5515   6527    -86   -263    196       C  
ATOM    535  NH1 ARG A  62      59.126 -33.780 -16.055  1.00 35.11           N  
ANISOU  535  NH1 ARG A  62     3954   4178   5208    -62   -222    167       N  
ATOM    536  NH2 ARG A  62      59.057 -34.579 -18.195  1.00 49.76           N  
ANISOU  536  NH2 ARG A  62     5885   6042   6980   -148   -312    223       N  
ATOM    537  N   ASN A  63      58.651 -26.789 -16.551  1.00 31.70           N  
ANISOU  537  N   ASN A  63     3352   3521   5172    176   -104    263       N  
ATOM    538  CA  ASN A  63      57.893 -26.159 -17.627  1.00 33.02           C  
ANISOU  538  CA  ASN A  63     3462   3676   5407    196   -152    372       C  
ATOM    539  C   ASN A  63      58.028 -26.989 -18.902  1.00 32.37           C  
ANISOU  539  C   ASN A  63     3416   3649   5233    133   -252    427       C  
ATOM    540  O   ASN A  63      59.149 -27.310 -19.319  1.00 34.95           O  
ANISOU  540  O   ASN A  63     3827   3976   5475     98   -261    388       O  
ATOM    541  CB  ASN A  63      58.408 -24.733 -17.855  1.00 32.97           C  
ANISOU  541  CB  ASN A  63     3467   3586   5472    239   -111    380       C  
ATOM    542  CG  ASN A  63      57.458 -23.893 -18.670  1.00 39.07           C  
ANISOU  542  CG  ASN A  63     4162   4333   6349    280   -140    503       C  
ATOM    543  OD1 ASN A  63      57.000 -24.316 -19.724  1.00 39.45           O  
ANISOU  543  OD1 ASN A  63     4188   4435   6366    248   -234    597       O  
ATOM    544  ND2 ASN A  63      57.159 -22.682 -18.186  1.00 41.42           N  
ANISOU  544  ND2 ASN A  63     4420   4545   6772    350    -58    508       N  
ATOM    545  N   ILE A  64      56.894 -27.359 -19.511  1.00 31.02           N  
ANISOU  545  N   ILE A  64     3182   3526   5077    112   -322    517       N  
ATOM    546  CA  ILE A  64      56.908 -28.207 -20.705  1.00 32.85           C  
ANISOU  546  CA  ILE A  64     3462   3814   5206     33   -418    564       C  
ATOM    547  C   ILE A  64      56.445 -27.435 -21.945  1.00 38.00           C  
ANISOU  547  C   ILE A  64     4082   4470   5888     27   -493    687       C  
ATOM    548  O   ILE A  64      56.031 -28.032 -22.933  1.00 37.72           O  
ANISOU  548  O   ILE A  64     4061   4491   5779    -46   -587    751       O  
ATOM    549  CB  ILE A  64      56.070 -29.488 -20.505  1.00 34.40           C  
ANISOU  549  CB  ILE A  64     3633   4075   5361    -22   -460    566       C  
ATOM    550  CG1 ILE A  64      54.618 -29.123 -20.184  1.00 42.62           C  
ANISOU  550  CG1 ILE A  64     4538   5136   6520     12   -474    650       C  
ATOM    551  CG2 ILE A  64      56.698 -30.393 -19.431  1.00 33.24           C  
ANISOU  551  CG2 ILE A  64     3539   3928   5163    -27   -394    453       C  
ATOM    552  CD1 ILE A  64      53.618 -30.145 -20.653  1.00 45.56           C  
ANISOU  552  CD1 ILE A  64     4871   5583   6855    -68   -565    712       C  
ATOM    553  N   LYS A  65      56.483 -26.127 -21.896  1.00 36.08           N  
ANISOU  553  N   LYS A  65     3797   4165   5747     97   -454    725       N  
ATOM    554  CA  LYS A  65      56.331 -25.293 -23.071  1.00 34.53           C  
ANISOU  554  CA  LYS A  65     3587   3959   5574     97   -516    842       C  
ATOM    555  C   LYS A  65      57.704 -24.825 -23.536  1.00 34.51           C  
ANISOU  555  C   LYS A  65     3690   3910   5512     90   -484    798       C  
ATOM    556  O   LYS A  65      58.694 -24.973 -22.813  1.00 36.82           O  
ANISOU  556  O   LYS A  65     4042   4170   5778     99   -408    683       O  
ATOM    557  CB  LYS A  65      55.446 -24.085 -22.745  1.00 37.56           C  
ANISOU  557  CB  LYS A  65     3850   4290   6133    187   -483    929       C  
ATOM    558  CG  LYS A  65      54.013 -24.452 -22.371  1.00 50.59           C  
ANISOU  558  CG  LYS A  65     5372   5987   7863    201   -512    998       C  
ATOM    559  CD  LYS A  65      53.364 -23.362 -21.533  1.00 74.25           C  
ANISOU  559  CD  LYS A  65     8261   8903  11045    312   -413   1026       C  
ATOM    560  CE  LYS A  65      53.951 -23.333 -20.124  1.00 86.71           C  
ANISOU  560  CE  LYS A  65     9889  10423  12632    351   -276    866       C  
ATOM    561  NZ  LYS A  65      53.339 -22.277 -19.265  1.00 94.07           N  
ANISOU  561  NZ  LYS A  65    10740  11267  13736    453   -157    874       N  
ATOM    562  N   PRO A  66      57.830 -24.282 -24.746  1.00 38.02           N  
ANISOU  562  N   PRO A  66     4158   4354   5932     67   -542    893       N  
ATOM    563  CA  PRO A  66      59.129 -23.707 -25.127  1.00 37.72           C  
ANISOU  563  CA  PRO A  66     4210   4264   5859     67   -496    856       C  
ATOM    564  C   PRO A  66      59.469 -22.572 -24.178  1.00 35.16           C  
ANISOU  564  C   PRO A  66     3851   3844   5664    151   -396    812       C  
ATOM    565  O   PRO A  66      58.627 -21.713 -23.894  1.00 39.61           O  
ANISOU  565  O   PRO A  66     4325   4364   6360    216   -380    878       O  
ATOM    566  CB  PRO A  66      58.898 -23.205 -26.560  1.00 37.96           C  
ANISOU  566  CB  PRO A  66     4253   4313   5857     32   -581    994       C  
ATOM    567  CG  PRO A  66      57.712 -24.005 -27.053  1.00 40.00           C  
ANISOU  567  CG  PRO A  66     4467   4663   6069    -26   -691   1075       C  
ATOM    568  CD  PRO A  66      56.849 -24.199 -25.848  1.00 38.59           C  
ANISOU  568  CD  PRO A  66     4182   4482   5998     29   -658   1044       C  
ATOM    569  N   VAL A  67      60.702 -22.581 -23.674  1.00 36.24           N  
ANISOU  569  N   VAL A  67     4058   3945   5766    146   -325    702       N  
ATOM    570  CA  VAL A  67      61.160 -21.531 -22.760  1.00 36.80           C  
ANISOU  570  CA  VAL A  67     4117   3925   5940    202   -232    643       C  
ATOM    571  C   VAL A  67      62.541 -21.071 -23.210  1.00 34.23           C  
ANISOU  571  C   VAL A  67     3869   3560   5576    176   -203    615       C  
ATOM    572  O   VAL A  67      63.249 -21.792 -23.931  1.00 33.80           O  
ANISOU  572  O   VAL A  67     3879   3553   5410    121   -233    610       O  
ATOM    573  CB  VAL A  67      61.192 -22.020 -21.291  1.00 32.38           C  
ANISOU  573  CB  VAL A  67     3547   3368   5388    215   -171    523       C  
ATOM    574  CG1 VAL A  67      59.762 -22.215 -20.726  1.00 34.84           C  
ANISOU  574  CG1 VAL A  67     3769   3700   5770    254   -173    555       C  
ATOM    575  CG2 VAL A  67      62.010 -23.311 -21.178  1.00 31.86           C  
ANISOU  575  CG2 VAL A  67     3544   3367   5193    156   -186    446       C  
ATOM    576  N   PRO A  68      62.955 -19.871 -22.798  1.00 32.46           N  
ANISOU  576  N   PRO A  68     3643   3244   5448    212   -136    597       N  
ATOM    577  CA  PRO A  68      64.311 -19.413 -23.123  1.00 37.53           C  
ANISOU  577  CA  PRO A  68     4350   3847   6063    181   -104    567       C  
ATOM    578  C   PRO A  68      65.364 -20.401 -22.642  1.00 34.57           C  
ANISOU  578  C   PRO A  68     4021   3522   5592    134    -89    464       C  
ATOM    579  O   PRO A  68      65.227 -21.027 -21.584  1.00 36.65           O  
ANISOU  579  O   PRO A  68     4269   3813   5842    136    -74    385       O  
ATOM    580  CB  PRO A  68      64.418 -18.078 -22.380  1.00 37.51           C  
ANISOU  580  CB  PRO A  68     4333   3733   6187    222    -26    537       C  
ATOM    581  CG  PRO A  68      62.995 -17.579 -22.316  1.00 36.20           C  
ANISOU  581  CG  PRO A  68     4092   3534   6128    288    -27    614       C  
ATOM    582  CD  PRO A  68      62.182 -18.841 -22.087  1.00 35.11           C  
ANISOU  582  CD  PRO A  68     3918   3497   5926    280    -80    607       C  
ATOM    583  N   GLU A  69      66.413 -20.556 -23.444  1.00 33.12           N  
ANISOU  583  N   GLU A  69     3891   3350   5343     93    -91    476       N  
ATOM    584  CA  GLU A  69      67.543 -21.352 -22.985  1.00 37.23           C  
ANISOU  584  CA  GLU A  69     4442   3904   5801     57    -64    392       C  
ATOM    585  C   GLU A  69      68.127 -20.736 -21.718  1.00 38.47           C  
ANISOU  585  C   GLU A  69     4582   4014   6022     60    -13    308       C  
ATOM    586  O   GLU A  69      68.106 -19.514 -21.527  1.00 37.25           O  
ANISOU  586  O   GLU A  69     4420   3781   5953     76     19    313       O  
ATOM    587  CB  GLU A  69      68.602 -21.457 -24.081  1.00 41.34           C  
ANISOU  587  CB  GLU A  69     5016   4431   6262     20    -54    426       C  
ATOM    588  CG  GLU A  69      68.152 -22.313 -25.254  1.00 42.48           C  
ANISOU  588  CG  GLU A  69     5202   4632   6306     -5    -98    485       C  
ATOM    589  CD  GLU A  69      69.263 -22.608 -26.232  1.00 45.34           C  
ANISOU  589  CD  GLU A  69     5629   5002   6596    -45    -64    500       C  
ATOM    590  OE1 GLU A  69      69.514 -21.745 -27.107  1.00 41.62           O  
ANISOU  590  OE1 GLU A  69     5183   4497   6134    -56    -57    567       O  
ATOM    591  OE2 GLU A  69      69.882 -23.708 -26.135  1.00 42.10           O  
ANISOU  591  OE2 GLU A  69     5246   4627   6123    -64    -37    448       O  
ATOM    592  N   VAL A  70      68.663 -21.603 -20.853  1.00 34.89           N  
ANISOU  592  N   VAL A  70     4127   3607   5523     40     -7    233       N  
ATOM    593  CA  VAL A  70      69.160 -21.163 -19.547  1.00 32.48           C  
ANISOU  593  CA  VAL A  70     3811   3275   5254     25     27    151       C  
ATOM    594  C   VAL A  70      70.260 -20.125 -19.702  1.00 31.43           C  
ANISOU  594  C   VAL A  70     3693   3083   5167     -6     58    147       C  
ATOM    595  O   VAL A  70      70.356 -19.186 -18.900  1.00 35.35           O  
ANISOU  595  O   VAL A  70     4192   3519   5720    -19     90     97       O  
ATOM    596  CB  VAL A  70      69.631 -22.384 -18.722  1.00 32.70           C  
ANISOU  596  CB  VAL A  70     3833   3377   5216      2     15     95       C  
ATOM    597  CG1 VAL A  70      70.447 -21.956 -17.505  1.00 36.15           C  
ANISOU  597  CG1 VAL A  70     4265   3802   5668    -37     34     22       C  
ATOM    598  CG2 VAL A  70      68.424 -23.221 -18.280  1.00 35.02           C  
ANISOU  598  CG2 VAL A  70     4110   3714   5481     29     -6     86       C  
ATOM    599  N   LYS A  71      71.103 -20.257 -20.732  1.00 34.14           N  
ANISOU  599  N   LYS A  71     4052   3436   5484    -26     58    197       N  
ATOM    600  CA  LYS A  71      72.164 -19.264 -20.907  1.00 35.97           C  
ANISOU  600  CA  LYS A  71     4291   3611   5765    -61     90    201       C  
ATOM    601  C   LYS A  71      71.586 -17.865 -21.121  1.00 36.67           C  
ANISOU  601  C   LYS A  71     4391   3602   5940    -42    113    229       C  
ATOM    602  O   LYS A  71      72.173 -16.870 -20.663  1.00 34.60           O  
ANISOU  602  O   LYS A  71     4135   3272   5738    -74    146    195       O  
ATOM    603  CB  LYS A  71      73.083 -19.657 -22.072  1.00 33.15           C  
ANISOU  603  CB  LYS A  71     3949   3279   5368    -80     99    260       C  
ATOM    604  CG  LYS A  71      72.394 -19.742 -23.440  1.00 35.03           C  
ANISOU  604  CG  LYS A  71     4221   3520   5570    -55     86    344       C  
ATOM    605  CD  LYS A  71      73.368 -20.113 -24.575  1.00 37.90           C  
ANISOU  605  CD  LYS A  71     4615   3902   5881    -82    115    392       C  
ATOM    606  CE  LYS A  71      72.601 -20.593 -25.805  1.00 39.06           C  
ANISOU  606  CE  LYS A  71     4812   4079   5950    -74     91    459       C  
ATOM    607  NZ  LYS A  71      73.474 -21.085 -26.921  1.00 39.39           N  
ANISOU  607  NZ  LYS A  71     4904   4141   5920   -103    135    494       N  
ATOM    608  N   ILE A  72      70.441 -17.761 -21.799  1.00 33.95           N  
ANISOU  608  N   ILE A  72     4045   3246   5606      8     94    296       N  
ATOM    609  CA  ILE A  72      69.826 -16.447 -21.983  1.00 32.51           C  
ANISOU  609  CA  ILE A  72     3863   2965   5524     39    121    339       C  
ATOM    610  C   ILE A  72      69.341 -15.904 -20.647  1.00 36.12           C  
ANISOU  610  C   ILE A  72     4310   3365   6049     54    162    254       C  
ATOM    611  O   ILE A  72      69.568 -14.735 -20.309  1.00 37.69           O  
ANISOU  611  O   ILE A  72     4528   3462   6331     44    215    230       O  
ATOM    612  CB  ILE A  72      68.666 -16.515 -22.996  1.00 35.86           C  
ANISOU  612  CB  ILE A  72     4273   3402   5949     88     80    449       C  
ATOM    613  CG1 ILE A  72      69.163 -16.847 -24.399  1.00 40.41           C  
ANISOU  613  CG1 ILE A  72     4883   4022   6451     60     49    534       C  
ATOM    614  CG2 ILE A  72      67.907 -15.193 -23.013  1.00 40.82           C  
ANISOU  614  CG2 ILE A  72     4884   3922   6705    137    112    502       C  
ATOM    615  CD1 ILE A  72      70.000 -15.778 -25.027  1.00 43.17           C  
ANISOU  615  CD1 ILE A  72     5259   4298   6847     38     87    579       C  
ATOM    616  N   LEU A  73      68.628 -16.734 -19.884  1.00 34.73           N  
ANISOU  616  N   LEU A  73     4112   3246   5836     73    148    208       N  
ATOM    617  CA  LEU A  73      68.130 -16.296 -18.587  1.00 33.43           C  
ANISOU  617  CA  LEU A  73     3950   3033   5721     84    199    121       C  
ATOM    618  C   LEU A  73      69.282 -15.909 -17.669  1.00 36.55           C  
ANISOU  618  C   LEU A  73     4382   3403   6102      9    228     22       C  
ATOM    619  O   LEU A  73      69.211 -14.888 -16.973  1.00 35.21           O  
ANISOU  619  O   LEU A  73     4242   3137   5998     -2    291    -38       O  
ATOM    620  CB  LEU A  73      67.272 -17.402 -17.949  1.00 34.36           C  
ANISOU  620  CB  LEU A  73     4038   3232   5785    107    177     93       C  
ATOM    621  CG  LEU A  73      66.077 -17.867 -18.779  1.00 35.79           C  
ANISOU  621  CG  LEU A  73     4175   3450   5976    165    136    191       C  
ATOM    622  CD1 LEU A  73      65.492 -19.137 -18.174  1.00 42.57           C  
ANISOU  622  CD1 LEU A  73     5010   4400   6765    167    107    158       C  
ATOM    623  CD2 LEU A  73      65.017 -16.754 -18.830  1.00 40.60           C  
ANISOU  623  CD2 LEU A  73     4753   3961   6713    232    184    241       C  
ATOM    624  N   ASN A  74      70.350 -16.719 -17.644  1.00 33.54           N  
ANISOU  624  N   ASN A  74     4000   3105   5640    -45    186      4       N  
ATOM    625  CA  ASN A  74      71.512 -16.369 -16.833  1.00 34.50           C  
ANISOU  625  CA  ASN A  74     4142   3216   5748   -128    195    -71       C  
ATOM    626  C   ASN A  74      72.100 -15.029 -17.263  1.00 35.61           C  
ANISOU  626  C   ASN A  74     4309   3250   5969   -159    234    -58       C  
ATOM    627  O   ASN A  74      72.456 -14.197 -16.423  1.00 36.46           O  
ANISOU  627  O   ASN A  74     4453   3292   6108   -216    271   -135       O  
ATOM    628  CB  ASN A  74      72.596 -17.442 -16.941  1.00 35.95           C  
ANISOU  628  CB  ASN A  74     4300   3505   5855   -170    144    -59       C  
ATOM    629  CG  ASN A  74      72.230 -18.732 -16.230  1.00 41.63           C  
ANISOU  629  CG  ASN A  74     5001   4320   6497   -158    110    -88       C  
ATOM    630  OD1 ASN A  74      71.289 -18.780 -15.441  1.00 39.37           O  
ANISOU  630  OD1 ASN A  74     4725   4029   6205   -137    125   -135       O  
ATOM    631  ND2 ASN A  74      73.014 -19.777 -16.481  1.00 36.78           N  
ANISOU  631  ND2 ASN A  74     4359   3788   5830   -173     74    -58       N  
ATOM    632  N   ASN A  75      72.284 -14.839 -18.572  1.00 34.62           N  
ANISOU  632  N   ASN A  75     4174   3110   5869   -134    227     40       N  
ATOM    633  CA  ASN A  75      72.883 -13.595 -19.066  1.00 33.88           C  
ANISOU  633  CA  ASN A  75     4104   2915   5853   -165    265     66       C  
ATOM    634  C   ASN A  75      72.025 -12.379 -18.731  1.00 36.93           C  
ANISOU  634  C   ASN A  75     4523   3169   6342   -132    330     46       C  
ATOM    635  O   ASN A  75      72.550 -11.265 -18.588  1.00 38.41           O  
ANISOU  635  O   ASN A  75     4746   3252   6597   -179    377     21       O  
ATOM    636  CB  ASN A  75      73.079 -13.675 -20.579  1.00 39.50           C  
ANISOU  636  CB  ASN A  75     4805   3640   6562   -138    249    185       C  
ATOM    637  CG  ASN A  75      74.174 -14.662 -20.986  1.00 34.94           C  
ANISOU  637  CG  ASN A  75     4206   3164   5906   -178    217    203       C  
ATOM    638  OD1 ASN A  75      74.887 -15.206 -20.145  1.00 35.69           O  
ANISOU  638  OD1 ASN A  75     4282   3316   5964   -226    201    138       O  
ATOM    639  ND2 ASN A  75      74.323 -14.863 -22.285  1.00 34.66           N  
ANISOU  639  ND2 ASN A  75     4174   3148   5846   -159    214    296       N  
ATOM    640  N   LEU A  76      70.711 -12.557 -18.649  1.00 38.49           N  
ANISOU  640  N   LEU A  76     4704   3359   6560    -51    340     65       N  
ATOM    641  CA  LEU A  76      69.833 -11.452 -18.289  1.00 43.57           C  
ANISOU  641  CA  LEU A  76     5369   3870   7317     -5    418     51       C  
ATOM    642  C   LEU A  76      69.695 -11.277 -16.783  1.00 43.74           C  
ANISOU  642  C   LEU A  76     5431   3857   7332    -41    474    -89       C  
ATOM    643  O   LEU A  76      68.921 -10.416 -16.349  1.00 47.18           O  
ANISOU  643  O   LEU A  76     5890   4174   7861      0    561   -118       O  
ATOM    644  CB  LEU A  76      68.448 -11.640 -18.913  1.00 37.78           C  
ANISOU  644  CB  LEU A  76     4586   3140   6630    101    410    152       C  
ATOM    645  CG  LEU A  76      68.368 -11.473 -20.431  1.00 44.85           C  
ANISOU  645  CG  LEU A  76     5456   4038   7546    136    366    303       C  
ATOM    646  CD1 LEU A  76      67.041 -12.029 -20.945  1.00 44.62           C  
ANISOU  646  CD1 LEU A  76     5368   4063   7524    217    323    399       C  
ATOM    647  CD2 LEU A  76      68.536 -10.009 -20.842  1.00 45.91           C  
ANISOU  647  CD2 LEU A  76     5618   4021   7804    144    430    351       C  
ATOM    648  N   GLY A  77      70.419 -12.065 -15.986  1.00 39.90           N  
ANISOU  648  N   GLY A  77     4953   3468   6738   -117    432   -172       N  
ATOM    649  CA  GLY A  77      70.395 -11.908 -14.545  1.00 43.39           C  
ANISOU  649  CA  GLY A  77     5447   3889   7149   -173    476   -305       C  
ATOM    650  C   GLY A  77      69.170 -12.466 -13.843  1.00 39.96           C  
ANISOU  650  C   GLY A  77     5002   3484   6698   -110    507   -338       C  
ATOM    651  O   GLY A  77      68.880 -12.042 -12.722  1.00 43.25           O  
ANISOU  651  O   GLY A  77     5476   3844   7114   -139    579   -445       O  
ATOM    652  N   VAL A  78      68.444 -13.400 -14.464  1.00 40.20           N  
ANISOU  652  N   VAL A  78     4965   3598   6710    -32    458   -252       N  
ATOM    653  CA  VAL A  78      67.259 -13.976 -13.831  1.00 37.47           C  
ANISOU  653  CA  VAL A  78     4597   3286   6355     26    485   -273       C  
ATOM    654  C   VAL A  78      67.674 -14.804 -12.622  1.00 40.75           C  
ANISOU  654  C   VAL A  78     5042   3794   6648    -48    463   -374       C  
ATOM    655  O   VAL A  78      68.565 -15.654 -12.713  1.00 39.22           O  
ANISOU  655  O   VAL A  78     4833   3705   6363   -100    378   -365       O  
ATOM    656  CB  VAL A  78      66.465 -14.825 -14.835  1.00 34.17           C  
ANISOU  656  CB  VAL A  78     4100   2943   5938    105    423   -153       C  
ATOM    657  CG1 VAL A  78      65.394 -15.629 -14.109  1.00 35.82           C  
ANISOU  657  CG1 VAL A  78     4278   3211   6121    145    437   -177       C  
ATOM    658  CG2 VAL A  78      65.826 -13.934 -15.912  1.00 37.89           C  
ANISOU  658  CG2 VAL A  78     4540   3322   6536    181    446    -41       C  
ATOM    659  N   ASP A  79      67.019 -14.566 -11.485  1.00 40.07           N  
ANISOU  659  N   ASP A  79     4996   3668   6560    -50    544   -465       N  
ATOM    660  CA  ASP A  79      67.271 -15.292 -10.240  1.00 37.58           C  
ANISOU  660  CA  ASP A  79     4719   3439   6123   -122    530   -559       C  
ATOM    661  C   ASP A  79      66.262 -16.400  -9.960  1.00 41.41           C  
ANISOU  661  C   ASP A  79     5154   4010   6569    -62    521   -535       C  
ATOM    662  O   ASP A  79      66.583 -17.349  -9.229  1.00 37.74           O  
ANISOU  662  O   ASP A  79     4698   3651   5991   -115    473   -571       O  
ATOM    663  CB  ASP A  79      67.225 -14.317  -9.056  1.00 41.29           C  
ANISOU  663  CB  ASP A  79     5287   3808   6593   -181    637   -691       C  
ATOM    664  CG  ASP A  79      68.301 -13.264  -9.139  1.00 48.31           C  
ANISOU  664  CG  ASP A  79     6237   4613   7504   -268    643   -733       C  
ATOM    665  OD1 ASP A  79      69.476 -13.651  -9.292  1.00 53.75           O  
ANISOU  665  OD1 ASP A  79     6914   5384   8124   -348    543   -718       O  
ATOM    666  OD2 ASP A  79      67.970 -12.055  -9.077  1.00 49.02           O  
ANISOU  666  OD2 ASP A  79     6382   4551   7692   -255    751   -775       O  
ATOM    667  N   ILE A  80      65.042 -16.278 -10.465  1.00 38.67           N  
ANISOU  667  N   ILE A  80     4754   3621   6319     40    567   -470       N  
ATOM    668  CA  ILE A  80      63.939 -17.122 -10.025  1.00 37.60           C  
ANISOU  668  CA  ILE A  80     4575   3546   6166     91    585   -460       C  
ATOM    669  C   ILE A  80      62.810 -16.961 -11.024  1.00 41.55           C  
ANISOU  669  C   ILE A  80     4989   4009   6789    199    596   -344       C  
ATOM    670  O   ILE A  80      62.738 -15.952 -11.734  1.00 39.10           O  
ANISOU  670  O   ILE A  80     4670   3599   6588    240    627   -296       O  
ATOM    671  CB  ILE A  80      63.515 -16.709  -8.584  1.00 36.07           C  
ANISOU  671  CB  ILE A  80     4453   3301   5952     63    704   -583       C  
ATOM    672  CG1 ILE A  80      62.649 -17.786  -7.911  1.00 41.24           C  
ANISOU  672  CG1 ILE A  80     5075   4046   6549     85    713   -587       C  
ATOM    673  CG2 ILE A  80      62.795 -15.333  -8.582  1.00 35.61           C  
ANISOU  673  CG2 ILE A  80     4414   3077   6040    126    844   -601       C  
ATOM    674  CD1 ILE A  80      62.530 -17.581  -6.387  1.00 37.95           C  
ANISOU  674  CD1 ILE A  80     4750   3609   6058     26    816   -719       C  
ATOM    675  N   ALA A  81      61.918 -17.943 -11.076  1.00 38.48           N  
ANISOU  675  N   ALA A  81     4532   3702   6385    241    567   -292       N  
ATOM    676  CA  ALA A  81      60.793 -17.937 -11.999  1.00 42.02           C  
ANISOU  676  CA  ALA A  81     4885   4140   6940    330    556   -170       C  
ATOM    677  C   ALA A  81      59.480 -17.790 -11.237  1.00 43.38           C  
ANISOU  677  C   ALA A  81     5015   4275   7193    393    665   -181       C  
ATOM    678  O   ALA A  81      59.330 -18.321 -10.131  1.00 39.01           O  
ANISOU  678  O   ALA A  81     4493   3762   6566    362    710   -266       O  
ATOM    679  CB  ALA A  81      60.765 -19.223 -12.829  1.00 40.89           C  
ANISOU  679  CB  ALA A  81     4689   4123   6723    320    428    -85       C  
ATOM    680  N   ALA A  82      58.528 -17.075 -11.835  1.00 39.32           N  
ANISOU  680  N   ALA A  82     4425   3684   6832    483    709    -86       N  
ATOM    681  CA  ALA A  82      57.202 -16.899 -11.248  1.00 42.36           C  
ANISOU  681  CA  ALA A  82     4745   4027   7324    558    821    -72       C  
ATOM    682  C   ALA A  82      56.343 -18.126 -11.543  1.00 39.62           C  
ANISOU  682  C   ALA A  82     4297   3806   6953    573    739     15       C  
ATOM    683  O   ALA A  82      55.891 -18.320 -12.677  1.00 45.15           O  
ANISOU  683  O   ALA A  82     4909   4544   7704    605    644    151       O  
ATOM    684  CB  ALA A  82      56.538 -15.638 -11.795  1.00 44.49           C  
ANISOU  684  CB  ALA A  82     4957   4161   7787    655    901     14       C  
ATOM    685  N   ASN A  83      56.136 -18.965 -10.529  1.00 40.62           N  
ANISOU  685  N   ASN A  83     4442   3998   6992    539    770    -61       N  
ATOM    686  CA  ASN A  83      55.115 -20.018 -10.573  1.00 43.28           C  
ANISOU  686  CA  ASN A  83     4680   4432   7331    557    730     11       C  
ATOM    687  C   ASN A  83      55.387 -21.077 -11.642  1.00 43.03           C  
ANISOU  687  C   ASN A  83     4617   4515   7216    513    556     95       C  
ATOM    688  O   ASN A  83      54.464 -21.625 -12.253  1.00 43.20           O  
ANISOU  688  O   ASN A  83     4536   4594   7284    535    495    205       O  
ATOM    689  CB  ASN A  83      53.740 -19.388 -10.751  1.00 45.75           C  
ANISOU  689  CB  ASN A  83     4871   4679   7833    660    814    110       C  
ATOM    690  CG  ASN A  83      53.478 -18.344  -9.697  1.00 49.18           C  
ANISOU  690  CG  ASN A  83     5349   4984   8354    707   1010     18       C  
ATOM    691  OD1 ASN A  83      53.834 -17.177  -9.858  1.00 60.43           O  
ANISOU  691  OD1 ASN A  83     6816   6286   9858    737   1075      0       O  
ATOM    692  ND2 ASN A  83      52.900 -18.770  -8.581  1.00 53.08           N  
ANISOU  692  ND2 ASN A  83     5847   5497   8825    705   1112    -50       N  
ATOM    693  N   THR A  84      56.662 -21.389 -11.851  1.00 37.63           N  
ANISOU  693  N   THR A  84     4023   3865   6409    443    482     43       N  
ATOM    694  CA  THR A  84      57.067 -22.458 -12.757  1.00 37.89           C  
ANISOU  694  CA  THR A  84     4053   3998   6348    394    341     98       C  
ATOM    695  C   THR A  84      58.469 -22.885 -12.347  1.00 35.35           C  
ANISOU  695  C   THR A  84     3835   3707   5891    321    313      2       C  
ATOM    696  O   THR A  84      59.118 -22.224 -11.533  1.00 40.86           O  
ANISOU  696  O   THR A  84     4601   4351   6575    303    383    -91       O  
ATOM    697  CB  THR A  84      57.010 -22.005 -14.230  1.00 44.74           C  
ANISOU  697  CB  THR A  84     4879   4848   7273    416    261    217       C  
ATOM    698  OG1 THR A  84      57.223 -23.123 -15.103  1.00 44.97           O  
ANISOU  698  OG1 THR A  84     4910   4974   7204    363    137    267       O  
ATOM    699  CG2 THR A  84      58.065 -20.926 -14.527  1.00 42.31           C  
ANISOU  699  CG2 THR A  84     4640   4457   6979    413    282    186       C  
ATOM    700  N   VAL A  85      58.925 -24.009 -12.909  1.00 34.93           N  
ANISOU  700  N   VAL A  85     3793   3738   5742    274    213     28       N  
ATOM    701  CA  VAL A  85      60.301 -24.480 -12.761  1.00 31.75           C  
ANISOU  701  CA  VAL A  85     3468   3367   5229    214    175    -31       C  
ATOM    702  C   VAL A  85      60.927 -24.511 -14.147  1.00 35.58           C  
ANISOU  702  C   VAL A  85     3962   3858   5699    202     95     34       C  
ATOM    703  O   VAL A  85      60.432 -25.210 -15.038  1.00 34.91           O  
ANISOU  703  O   VAL A  85     3846   3820   5600    198     30    107       O  
ATOM    704  CB  VAL A  85      60.386 -25.882 -12.124  1.00 36.59           C  
ANISOU  704  CB  VAL A  85     4094   4066   5742    172    147    -60       C  
ATOM    705  CG1 VAL A  85      61.841 -26.364 -12.084  1.00 33.24           C  
ANISOU  705  CG1 VAL A  85     3732   3672   5224    120    104    -97       C  
ATOM    706  CG2 VAL A  85      59.784 -25.895 -10.735  1.00 38.74           C  
ANISOU  706  CG2 VAL A  85     4366   4340   6012    176    229   -122       C  
ATOM    707  N   ILE A  86      62.022 -23.783 -14.330  1.00 33.46           N  
ANISOU  707  N   ILE A  86     3742   3545   5427    185    103      6       N  
ATOM    708  CA  ILE A  86      62.823 -23.925 -15.536  1.00 29.72           C  
ANISOU  708  CA  ILE A  86     3290   3083   4920    163     41     56       C  
ATOM    709  C   ILE A  86      63.825 -25.045 -15.269  1.00 33.05           C  
ANISOU  709  C   ILE A  86     3751   3568   5239    114     10     16       C  
ATOM    710  O   ILE A  86      64.762 -24.870 -14.483  1.00 35.03           O  
ANISOU  710  O   ILE A  86     4032   3813   5463     84     33    -48       O  
ATOM    711  CB  ILE A  86      63.540 -22.620 -15.911  1.00 33.39           C  
ANISOU  711  CB  ILE A  86     3781   3467   5439    167     68     56       C  
ATOM    712  CG1 ILE A  86      62.531 -21.480 -16.058  1.00 33.78           C  
ANISOU  712  CG1 ILE A  86     3789   3438   5609    226    113    100       C  
ATOM    713  CG2 ILE A  86      64.292 -22.806 -17.209  1.00 32.35           C  
ANISOU  713  CG2 ILE A  86     3671   3351   5269    145     12    115       C  
ATOM    714  CD1 ILE A  86      61.478 -21.759 -17.099  1.00 38.40           C  
ANISOU  714  CD1 ILE A  86     4313   4052   6224    258     56    215       C  
ATOM    715  N   TRP A  87      63.626 -26.201 -15.901  1.00 30.36           N  
ANISOU  715  N   TRP A  87     3408   3285   4844    100    -41     56       N  
ATOM    716  CA  TRP A  87      64.556 -27.310 -15.714  1.00 28.47           C  
ANISOU  716  CA  TRP A  87     3201   3092   4523     64    -58     30       C  
ATOM    717  C   TRP A  87      65.773 -27.122 -16.613  1.00 32.20           C  
ANISOU  717  C   TRP A  87     3708   3548   4979     47    -68     48       C  
ATOM    718  O   TRP A  87      65.636 -26.890 -17.818  1.00 33.48           O  
ANISOU  718  O   TRP A  87     3880   3694   5145     50    -89    103       O  
ATOM    719  CB  TRP A  87      63.882 -28.649 -16.013  1.00 31.16           C  
ANISOU  719  CB  TRP A  87     3538   3486   4816     53    -93     58       C  
ATOM    720  CG  TRP A  87      64.725 -29.833 -15.560  1.00 32.94           C  
ANISOU  720  CG  TRP A  87     3792   3749   4976     27    -94     30       C  
ATOM    721  CD1 TRP A  87      65.485 -30.653 -16.355  1.00 35.71           C  
ANISOU  721  CD1 TRP A  87     4179   4106   5281      9   -106     49       C  
ATOM    722  CD2 TRP A  87      64.907 -30.301 -14.210  1.00 30.04           C  
ANISOU  722  CD2 TRP A  87     3418   3410   4585     19    -75    -14       C  
ATOM    723  NE1 TRP A  87      66.117 -31.606 -15.587  1.00 32.88           N  
ANISOU  723  NE1 TRP A  87     3829   3775   4890     -1    -95     27       N  
ATOM    724  CE2 TRP A  87      65.770 -31.425 -14.271  1.00 35.59           C  
ANISOU  724  CE2 TRP A  87     4146   4138   5241      1    -84     -7       C  
ATOM    725  CE3 TRP A  87      64.395 -29.905 -12.964  1.00 32.37           C  
ANISOU  725  CE3 TRP A  87     3695   3711   4893     23    -45    -56       C  
ATOM    726  CZ2 TRP A  87      66.154 -32.145 -13.133  1.00 33.44           C  
ANISOU  726  CZ2 TRP A  87     3870   3900   4936    -11    -78    -26       C  
ATOM    727  CZ3 TRP A  87      64.771 -30.627 -11.827  1.00 32.65           C  
ANISOU  727  CZ3 TRP A  87     3741   3788   4879      0    -39    -85       C  
ATOM    728  CH2 TRP A  87      65.651 -31.733 -11.923  1.00 31.04           C  
ANISOU  728  CH2 TRP A  87     3551   3612   4630    -16    -62    -63       C  
ATOM    729  N   ASP A  88      66.965 -27.228 -16.026  1.00 32.20           N  
ANISOU  729  N   ASP A  88     3722   3555   4958     25    -54      9       N  
ATOM    730  CA  ASP A  88      68.221 -27.015 -16.755  1.00 31.37           C  
ANISOU  730  CA  ASP A  88     3636   3433   4849      8    -51     28       C  
ATOM    731  C   ASP A  88      68.695 -28.379 -17.246  1.00 35.07           C  
ANISOU  731  C   ASP A  88     4123   3940   5262      0    -59     49       C  
ATOM    732  O   ASP A  88      69.290 -29.152 -16.494  1.00 33.58           O  
ANISOU  732  O   ASP A  88     3925   3783   5052    -10    -55     31       O  
ATOM    733  CB  ASP A  88      69.247 -26.351 -15.841  1.00 32.91           C  
ANISOU  733  CB  ASP A  88     3824   3617   5064    -18    -35    -16       C  
ATOM    734  CG  ASP A  88      70.563 -26.048 -16.543  1.00 36.37           C  
ANISOU  734  CG  ASP A  88     4267   4038   5515    -37    -27      9       C  
ATOM    735  OD1 ASP A  88      70.861 -26.608 -17.619  1.00 37.79           O  
ANISOU  735  OD1 ASP A  88     4461   4222   5675    -28    -23     54       O  
ATOM    736  OD2 ASP A  88      71.310 -25.226 -15.995  1.00 38.81           O  
ANISOU  736  OD2 ASP A  88     4567   4326   5852    -67    -19    -18       O  
ATOM    737  N   TYR A  89      68.422 -28.685 -18.512  1.00 31.48           N  
ANISOU  737  N   TYR A  89     3699   3479   4784      0    -67     91       N  
ATOM    738  CA  TYR A  89      68.731 -30.018 -19.016  1.00 34.93           C  
ANISOU  738  CA  TYR A  89     4171   3937   5166    -11    -58    102       C  
ATOM    739  C   TYR A  89      70.242 -30.232 -19.212  1.00 39.85           C  
ANISOU  739  C   TYR A  89     4800   4549   5793    -14    -17    106       C  
ATOM    740  O   TYR A  89      70.694 -31.379 -19.251  1.00 38.21           O  
ANISOU  740  O   TYR A  89     4608   4350   5560    -13      8    108       O  
ATOM    741  CB  TYR A  89      67.970 -30.260 -20.323  1.00 33.19           C  
ANISOU  741  CB  TYR A  89     3996   3713   4902    -27    -79    140       C  
ATOM    742  CG  TYR A  89      66.494 -30.604 -20.145  1.00 33.95           C  
ANISOU  742  CG  TYR A  89     4076   3836   4988    -32   -124    148       C  
ATOM    743  CD1 TYR A  89      65.520 -29.605 -20.037  1.00 35.32           C  
ANISOU  743  CD1 TYR A  89     4206   4004   5211    -16   -153    172       C  
ATOM    744  CD2 TYR A  89      66.074 -31.929 -20.113  1.00 34.66           C  
ANISOU  744  CD2 TYR A  89     4191   3952   5028    -54   -131    138       C  
ATOM    745  CE1 TYR A  89      64.165 -29.928 -19.884  1.00 34.86           C  
ANISOU  745  CE1 TYR A  89     4115   3973   5156    -19   -192    191       C  
ATOM    746  CE2 TYR A  89      64.739 -32.254 -19.955  1.00 40.28           C  
ANISOU  746  CE2 TYR A  89     4880   4691   5735    -68   -174    151       C  
ATOM    747  CZ  TYR A  89      63.789 -31.259 -19.847  1.00 37.86           C  
ANISOU  747  CZ  TYR A  89     4516   4386   5481    -50   -206    181       C  
ATOM    748  OH  TYR A  89      62.465 -31.621 -19.705  1.00 40.36           O  
ANISOU  748  OH  TYR A  89     4796   4735   5806    -62   -246    206       O  
ATOM    749  N   LYS A  90      71.035 -29.165 -19.330  1.00 37.29           N  
ANISOU  749  N   LYS A  90     4458   4199   5510    -17     -3    113       N  
ATOM    750  CA  LYS A  90      72.487 -29.351 -19.403  1.00 37.17           C  
ANISOU  750  CA  LYS A  90     4428   4180   5515    -20     37    126       C  
ATOM    751  C   LYS A  90      73.058 -29.819 -18.067  1.00 40.39           C  
ANISOU  751  C   LYS A  90     4783   4622   5940    -22     26    109       C  
ATOM    752  O   LYS A  90      74.052 -30.543 -18.042  1.00 41.43           O  
ANISOU  752  O   LYS A  90     4893   4764   6085    -16     55    133       O  
ATOM    753  CB  LYS A  90      73.176 -28.051 -19.825  1.00 47.80           C  
ANISOU  753  CB  LYS A  90     5764   5492   6906    -33     51    141       C  
ATOM    754  CG  LYS A  90      72.663 -27.440 -21.120  1.00 57.99           C  
ANISOU  754  CG  LYS A  90     7104   6750   8180    -35     56    173       C  
ATOM    755  CD  LYS A  90      73.151 -28.202 -22.327  1.00 60.50           C  
ANISOU  755  CD  LYS A  90     7475   7063   8450    -39    104    202       C  
ATOM    756  CE  LYS A  90      72.881 -27.425 -23.605  1.00 59.64           C  
ANISOU  756  CE  LYS A  90     7416   6926   8317    -54    108    244       C  
ATOM    757  NZ  LYS A  90      71.424 -27.165 -23.812  1.00 53.00           N  
ANISOU  757  NZ  LYS A  90     6594   6093   7451    -56     44    257       N  
ATOM    758  N   ARG A  91      72.476 -29.378 -16.954  1.00 34.42           N  
ANISOU  758  N   ARG A  91     4006   3885   5188    -32    -12     73       N  
ATOM    759  CA  ARG A  91      72.920 -29.758 -15.619  1.00 35.74           C  
ANISOU  759  CA  ARG A  91     4133   4094   5352    -48    -33     59       C  
ATOM    760  C   ARG A  91      72.061 -30.862 -14.997  1.00 36.93           C  
ANISOU  760  C   ARG A  91     4293   4279   5462    -35    -47     50       C  
ATOM    761  O   ARG A  91      72.418 -31.364 -13.926  1.00 38.27           O  
ANISOU  761  O   ARG A  91     4434   4489   5619    -48    -66     51       O  
ATOM    762  CB  ARG A  91      72.930 -28.519 -14.693  1.00 33.52           C  
ANISOU  762  CB  ARG A  91     3838   3811   5088    -84    -56     17       C  
ATOM    763  CG  ARG A  91      74.076 -27.480 -14.966  1.00 34.31           C  
ANISOU  763  CG  ARG A  91     3917   3884   5234   -116    -50     27       C  
ATOM    764  CD  ARG A  91      73.807 -26.118 -14.239  1.00 37.68           C  
ANISOU  764  CD  ARG A  91     4358   4282   5676   -155    -60    -30       C  
ATOM    765  NE  ARG A  91      73.612 -26.359 -12.818  1.00 40.28           N  
ANISOU  765  NE  ARG A  91     4685   4658   5963   -189    -88    -72       N  
ATOM    766  CZ  ARG A  91      72.464 -26.246 -12.169  1.00 37.84           C  
ANISOU  766  CZ  ARG A  91     4407   4344   5627   -180    -80   -121       C  
ATOM    767  NH1 ARG A  91      72.430 -26.564 -10.886  1.00 39.00           N  
ANISOU  767  NH1 ARG A  91     4557   4540   5722   -218   -101   -154       N  
ATOM    768  NH2 ARG A  91      71.365 -25.795 -12.778  1.00 39.67           N  
ANISOU  768  NH2 ARG A  91     4663   4526   5885   -137    -49   -130       N  
ATOM    769  N  AASP A  92      70.962 -31.245 -15.645  0.53 34.90           N  
ANISOU  769  N  AASP A  92     4071   4007   5180    -18    -42     48       N  
ATOM    770  N  BASP A  92      70.974 -31.278 -15.655  0.47 34.45           N  
ANISOU  770  N  BASP A  92     4015   3952   5124    -18    -42     49       N  
ATOM    771  CA AASP A  92      69.989 -32.180 -15.080  0.53 30.01           C  
ANISOU  771  CA AASP A  92     3459   3415   4527    -13    -55     38       C  
ATOM    772  CA BASP A  92      69.980 -32.197 -15.078  0.47 30.29           C  
ANISOU  772  CA BASP A  92     3495   3451   4562    -13    -55     38       C  
ATOM    773  C  AASP A  92      69.561 -31.735 -13.684  0.53 33.38           C  
ANISOU  773  C  AASP A  92     3863   3872   4949    -28    -74      2       C  
ATOM    774  C  BASP A  92      69.557 -31.737 -13.682  0.47 33.24           C  
ANISOU  774  C  BASP A  92     3845   3855   4931    -28    -74      2       C  
ATOM    775  O  AASP A  92      69.568 -32.508 -12.723  0.53 33.60           O  
ANISOU  775  O  AASP A  92     3880   3938   4950    -36    -83      2       O  
ATOM    776  O  BASP A  92      69.556 -32.507 -12.717  0.47 33.63           O  
ANISOU  776  O  BASP A  92     3883   3942   4952    -36    -83      1       O  
ATOM    777  CB AASP A  92      70.552 -33.605 -15.058  0.53 33.52           C  
ANISOU  777  CB AASP A  92     3908   3871   4957     -4    -36     67       C  
ATOM    778  CB BASP A  92      70.503 -33.642 -15.042  0.47 32.94           C  
ANISOU  778  CB BASP A  92     3835   3798   4882     -4    -37     67       C  
ATOM    779  CG AASP A  92      69.475 -34.639 -14.923  0.53 33.91           C  
ANISOU  779  CG AASP A  92     3982   3931   4973     -4    -41     64       C  
ATOM    780  CG BASP A  92      70.666 -34.251 -16.429  0.47 40.09           C  
ANISOU  780  CG BASP A  92     4789   4666   5779      5      0     88       C  
ATOM    781  OD1AASP A  92      68.286 -34.264 -15.006  0.53 34.58           O  
ANISOU  781  OD1AASP A  92     4074   4019   5047    -11    -60     45       O  
ATOM    782  OD1BASP A  92      69.823 -33.985 -17.313  0.47 50.34           O  
ANISOU  782  OD1BASP A  92     6125   5947   7054     -5     -7     81       O  
ATOM    783  OD2AASP A  92      69.807 -35.825 -14.737  0.53 39.34           O  
ANISOU  783  OD2AASP A  92     4675   4619   5652      4    -22     86       O  
ATOM    784  OD2BASP A  92      71.638 -35.010 -16.635  0.47 57.84           O  
ANISOU  784  OD2BASP A  92     7036   6899   8042     20     41    115       O  
ATOM    785  N   ALA A  93      69.185 -30.461 -13.575  1.00 31.07           N  
ANISOU  785  N   ALA A  93     3569   3556   4680    -33    -72    -29       N  
ATOM    786  CA  ALA A  93      68.892 -29.864 -12.282  1.00 27.72           C  
ANISOU  786  CA  ALA A  93     3138   3146   4247    -54    -72    -76       C  
ATOM    787  C   ALA A  93      68.037 -28.619 -12.499  1.00 30.76           C  
ANISOU  787  C   ALA A  93     3530   3481   4675    -40    -49   -104       C  
ATOM    788  O   ALA A  93      67.959 -28.106 -13.619  1.00 32.00           O  
ANISOU  788  O   ALA A  93     3690   3598   4869    -20    -46    -75       O  
ATOM    789  CB  ALA A  93      70.192 -29.510 -11.533  1.00 30.50           C  
ANISOU  789  CB  ALA A  93     3480   3519   4592    -96    -88    -88       C  
ATOM    790  N   PRO A  94      67.373 -28.123 -11.461  1.00 32.23           N  
ANISOU  790  N   PRO A  94     3722   3665   4858    -48    -24   -153       N  
ATOM    791  CA  PRO A  94      66.641 -26.855 -11.621  1.00 33.63           C  
ANISOU  791  CA  PRO A  94     3902   3779   5096    -27     15   -175       C  
ATOM    792  C   PRO A  94      67.611 -25.749 -11.996  1.00 32.11           C  
ANISOU  792  C   PRO A  94     3725   3536   4939    -47     19   -185       C  
ATOM    793  O   PRO A  94      68.743 -25.705 -11.507  1.00 32.69           O  
ANISOU  793  O   PRO A  94     3809   3630   4983    -95      1   -206       O  
ATOM    794  CB  PRO A  94      66.027 -26.603 -10.238  1.00 32.63           C  
ANISOU  794  CB  PRO A  94     3791   3657   4949    -42     58   -240       C  
ATOM    795  CG  PRO A  94      66.091 -27.923  -9.520  1.00 36.45           C  
ANISOU  795  CG  PRO A  94     4273   4219   5358    -63     32   -233       C  
ATOM    796  CD  PRO A  94      67.311 -28.626 -10.075  1.00 32.02           C  
ANISOU  796  CD  PRO A  94     3704   3689   4775    -79    -22   -188       C  
ATOM    797  N   ALA A  95      67.161 -24.849 -12.875  1.00 31.49           N  
ANISOU  797  N   ALA A  95     3642   3393   4928    -13     39   -161       N  
ATOM    798  CA  ALA A  95      67.993 -23.706 -13.242  1.00 36.33           C  
ANISOU  798  CA  ALA A  95     4273   3947   5585    -33     51   -168       C  
ATOM    799  C   ALA A  95      68.148 -22.710 -12.100  1.00 40.98           C  
ANISOU  799  C   ALA A  95     4895   4492   6185    -72     95   -249       C  
ATOM    800  O   ALA A  95      69.143 -21.973 -12.067  1.00 34.82           O  
ANISOU  800  O   ALA A  95     4134   3680   5415   -119     95   -271       O  
ATOM    801  CB  ALA A  95      67.406 -23.003 -14.472  1.00 37.04           C  
ANISOU  801  CB  ALA A  95     4352   3977   5746     14     61   -108       C  
ATOM    802  N   HIS A  96      67.203 -22.687 -11.159  1.00 34.09           N  
ANISOU  802  N   HIS A  96     4033   3616   5304    -61    139   -298       N  
ATOM    803  CA  HIS A  96      67.193 -21.731 -10.061  1.00 41.08           C  
ANISOU  803  CA  HIS A  96     4969   4448   6191   -101    200   -388       C  
ATOM    804  C   HIS A  96      67.049 -22.461  -8.728  1.00 41.82           C  
ANISOU  804  C   HIS A  96     5086   4612   6192   -143    203   -444       C  
ATOM    805  O   HIS A  96      66.351 -23.471  -8.636  1.00 40.92           O  
ANISOU  805  O   HIS A  96     4941   4554   6050   -110    192   -413       O  
ATOM    806  CB  HIS A  96      66.047 -20.721 -10.280  1.00 35.31           C  
ANISOU  806  CB  HIS A  96     4237   3617   5562    -37    284   -392       C  
ATOM    807  CG  HIS A  96      66.110 -20.059 -11.625  1.00 37.35           C  
ANISOU  807  CG  HIS A  96     4469   3813   5908      6    273   -317       C  
ATOM    808  ND1 HIS A  96      65.172 -20.279 -12.614  1.00 37.11           N  
ANISOU  808  ND1 HIS A  96     4383   3781   5935     79    258   -227       N  
ATOM    809  CD2 HIS A  96      67.037 -19.229 -12.162  1.00 32.77           C  
ANISOU  809  CD2 HIS A  96     3910   3178   5361    -24    266   -310       C  
ATOM    810  CE1 HIS A  96      65.506 -19.589 -13.692  1.00 41.56           C  
ANISOU  810  CE1 HIS A  96     4942   4293   6557     95    244   -167       C  
ATOM    811  NE2 HIS A  96      66.636 -18.948 -13.446  1.00 35.53           N  
ANISOU  811  NE2 HIS A  96     4224   3494   5783     36    254   -217       N  
ATOM    812  N  AILE A  97      67.695 -21.918  -7.690  0.54 45.08           N  
ANISOU  812  N  AILE A  97     5558   5017   6552   -225    218   -524       N  
ATOM    813  N  BILE A  97      67.693 -21.923  -7.690  0.46 45.34           N  
ANISOU  813  N  BILE A  97     5591   5050   6584   -225    218   -524       N  
ATOM    814  CA AILE A  97      67.750 -22.615  -6.407  0.54 53.35           C  
ANISOU  814  CA AILE A  97     6637   6143   7489   -284    207   -569       C  
ATOM    815  CA BILE A  97      67.744 -22.643  -6.419  0.46 53.24           C  
ANISOU  815  CA BILE A  97     6622   6131   7475   -283    206   -567       C  
ATOM    816  C  AILE A  97      66.403 -22.585  -5.691  0.54 49.89           C  
ANISOU  816  C  AILE A  97     6223   5683   7051   -248    298   -616       C  
ATOM    817  C  BILE A  97      66.417 -22.574  -5.664  0.46 49.75           C  
ANISOU  817  C  BILE A  97     6206   5664   7030   -251    299   -618       C  
ATOM    818  O  AILE A  97      66.038 -23.545  -5.000  0.54 46.87           O  
ANISOU  818  O  AILE A  97     5838   5376   6595   -257    289   -613       O  
ATOM    819  O  BILE A  97      66.080 -23.499  -4.917  0.46 47.06           O  
ANISOU  819  O  BILE A  97     5868   5400   6613   -264    291   -620       O  
ATOM    820  CB AILE A  97      68.869 -22.022  -5.526  0.54 59.86           C  
ANISOU  820  CB AILE A  97     7524   6977   8244   -402    183   -637       C  
ATOM    821  CB BILE A  97      68.903 -22.122  -5.550  0.46 60.19           C  
ANISOU  821  CB BILE A  97     7561   7027   8283   -401    176   -630       C  
ATOM    822  CG1AILE A  97      68.949 -22.757  -4.184  0.54 59.38           C  
ANISOU  822  CG1AILE A  97     7500   7009   8053   -474    160   -672       C  
ATOM    823  CG1BILE A  97      69.284 -20.692  -5.941  0.46 62.38           C  
ANISOU  823  CG1BILE A  97     7875   7195   8633   -425    217   -673       C  
ATOM    824  CG2AILE A  97      68.665 -20.527  -5.316  0.54 62.72           C  
ANISOU  824  CG2AILE A  97     7957   7218   8655   -427    273   -724       C  
ATOM    825  CG2BILE A  97      70.110 -23.055  -5.658  0.46 63.70           C  
ANISOU  825  CG2BILE A  97     7957   7572   8675   -443     64   -562       C  
ATOM    826  CD1AILE A  97      69.138 -24.261  -4.313  0.54 61.75           C  
ANISOU  826  CD1AILE A  97     7734   7416   8313   -447     80   -582       C  
ATOM    827  CD1BILE A  97      68.737 -19.628  -5.002  0.46 63.20           C  
ANISOU  827  CD1BILE A  97     8073   7212   8727   -466    323   -789       C  
ATOM    828  N   SER A  98      65.644 -21.507  -5.840  1.00 38.83           N  
ANISOU  828  N   SER A  98     4841   4174   5739   -205    395   -652       N  
ATOM    829  CA  SER A  98      64.399 -21.317  -5.104  1.00 37.40           C  
ANISOU  829  CA  SER A  98     4681   3956   5574   -169    507   -701       C  
ATOM    830  C   SER A  98      63.217 -21.248  -6.060  1.00 35.56           C  
ANISOU  830  C   SER A  98     4365   3674   5470    -53    546   -624       C  
ATOM    831  O   SER A  98      63.373 -21.154  -7.282  1.00 38.99           O  
ANISOU  831  O   SER A  98     4746   4092   5977     -9    491   -545       O  
ATOM    832  CB  SER A  98      64.468 -20.042  -4.255  1.00 43.19           C  
ANISOU  832  CB  SER A  98     5515   4590   6305   -223    614   -818       C  
ATOM    833  OG  SER A  98      65.405 -20.204  -3.210  1.00 43.19           O  
ANISOU  833  OG  SER A  98     5594   4653   6163   -347    573   -889       O  
ATOM    834  N   THR A  99      62.011 -21.289  -5.492  1.00 35.59           N  
ANISOU  834  N   THR A  99     4359   3660   5505     -8    642   -643       N  
ATOM    835  CA  THR A  99      60.808 -21.261  -6.305  1.00 35.63           C  
ANISOU  835  CA  THR A  99     4269   3630   5638     97    673   -558       C  
ATOM    836  C   THR A  99      59.797 -20.292  -5.709  1.00 41.38           C  
ANISOU  836  C   THR A  99     5010   4250   6460    148    834   -608       C  
ATOM    837  O   THR A  99      59.920 -19.829  -4.569  1.00 41.11           O  
ANISOU  837  O   THR A  99     5071   4179   6370     97    931   -720       O  
ATOM    838  CB  THR A  99      60.182 -22.664  -6.450  1.00 40.91           C  
ANISOU  838  CB  THR A  99     4866   4406   6272    118    612   -486       C  
ATOM    839  OG1 THR A  99      59.980 -23.237  -5.154  1.00 40.82           O  
ANISOU  839  OG1 THR A  99     4900   4448   6163     73    660   -552       O  
ATOM    840  CG2 THR A  99      61.071 -23.580  -7.290  1.00 41.64           C  
ANISOU  840  CG2 THR A  99     4938   4580   6304     89    469   -422       C  
ATOM    841  N   ILE A 100      58.794 -19.976  -6.520  1.00 41.31           N  
ANISOU  841  N   ILE A 100     4908   4191   6598    247    866   -518       N  
ATOM    842  CA  ILE A 100      57.658 -19.165  -6.113  1.00 39.97           C  
ANISOU  842  CA  ILE A 100     4715   3918   6554    322   1025   -532       C  
ATOM    843  C   ILE A 100      56.413 -19.966  -6.452  1.00 45.83           C  
ANISOU  843  C   ILE A 100     5329   4721   7364    393   1013   -426       C  
ATOM    844  O   ILE A 100      56.105 -20.159  -7.633  1.00 44.73           O  
ANISOU  844  O   ILE A 100     5093   4605   7299    440    920   -303       O  
ATOM    845  CB  ILE A 100      57.627 -17.804  -6.814  1.00 42.70           C  
ANISOU  845  CB  ILE A 100     5052   4123   7049    382   1082   -504       C  
ATOM    846  CG1 ILE A 100      58.895 -17.005  -6.499  1.00 40.86           C  
ANISOU  846  CG1 ILE A 100     4947   3826   6750    298   1090   -610       C  
ATOM    847  CG2 ILE A 100      56.343 -17.048  -6.423  1.00 40.74           C  
ANISOU  847  CG2 ILE A 100     4760   3761   6957    478   1260   -499       C  
ATOM    848  CD1 ILE A 100      59.035 -15.730  -7.333  1.00 43.56           C  
ANISOU  848  CD1 ILE A 100     5285   4033   7234    347   1124   -570       C  
ATOM    849  N   GLY A 101      55.700 -20.431  -5.427  1.00 43.21           N  
ANISOU  849  N   GLY A 101     4999   4418   6999    391   1103   -470       N  
ATOM    850  CA  GLY A 101      54.427 -21.109  -5.643  1.00 43.50           C  
ANISOU  850  CA  GLY A 101     4908   4504   7116    454   1110   -371       C  
ATOM    851  C   GLY A 101      54.520 -22.446  -6.356  1.00 49.80           C  
ANISOU  851  C   GLY A 101     5644   5434   7844    422    941   -283       C  
ATOM    852  O   GLY A 101      53.595 -22.814  -7.087  1.00 51.62           O  
ANISOU  852  O   GLY A 101     5752   5695   8168    473    899   -167       O  
ATOM    853  N   VAL A 102      55.601 -23.194  -6.158  1.00 38.97           N  
ANISOU  853  N   VAL A 102     4352   4139   6314    336    844   -332       N  
ATOM    854  CA  VAL A 102      55.806 -24.482  -6.823  1.00 40.67           C  
ANISOU  854  CA  VAL A 102     4528   4465   6461    303    697   -260       C  
ATOM    855  C   VAL A 102      55.851 -25.635  -5.826  1.00 48.60           C  
ANISOU  855  C   VAL A 102     5569   5557   7338    244    695   -302       C  
ATOM    856  O   VAL A 102      55.214 -26.667  -6.032  1.00 49.15           O  
ANISOU  856  O   VAL A 102     5573   5696   7405    244    649   -237       O  
ATOM    857  CB  VAL A 102      57.084 -24.472  -7.693  1.00 47.28           C  
ANISOU  857  CB  VAL A 102     5410   5312   7242    265    577   -250       C  
ATOM    858  CG1 VAL A 102      57.295 -25.857  -8.310  1.00 41.66           C  
ANISOU  858  CG1 VAL A 102     4673   4701   6455    229    449   -188       C  
ATOM    859  CG2 VAL A 102      56.994 -23.404  -8.778  1.00 46.00           C  
ANISOU  859  CG2 VAL A 102     5208   5068   7201    320    570   -190       C  
ATOM    860  N   CYS A 103      56.631 -25.493  -4.757  1.00 42.31           N  
ANISOU  860  N   CYS A 103     4881   4763   6432    184    737   -406       N  
ATOM    861  CA  CYS A 103      57.038 -26.640  -3.955  1.00 49.14           C  
ANISOU  861  CA  CYS A 103     5792   5722   7155    114    696   -431       C  
ATOM    862  C   CYS A 103      57.320 -26.167  -2.539  1.00 50.28           C  
ANISOU  862  C   CYS A 103     6044   5851   7209     61    798   -545       C  
ATOM    863  O   CYS A 103      58.009 -25.162  -2.352  1.00 45.75           O  
ANISOU  863  O   CYS A 103     5544   5216   6624     36    827   -616       O  
ATOM    864  CB  CYS A 103      58.277 -27.304  -4.567  1.00 44.70           C  
ANISOU  864  CB  CYS A 103     5254   5215   6514     68    552   -403       C  
ATOM    865  SG  CYS A 103      59.197 -28.397  -3.452  1.00 49.92           S  
ANISOU  865  SG  CYS A 103     5992   5973   7002    -24    502   -439       S  
ATOM    866  N   SER A 104      56.795 -26.884  -1.545  1.00 43.14           N  
ANISOU  866  N   SER A 104     5156   5003   6233     34    851   -562       N  
ATOM    867  CA  SER A 104      56.854 -26.369  -0.181  1.00 44.34           C  
ANISOU  867  CA  SER A 104     5416   5135   6295    -19    970   -673       C  
ATOM    868  C   SER A 104      58.278 -26.332   0.358  1.00 48.28           C  
ANISOU  868  C   SER A 104     6026   5673   6644   -121    892   -734       C  
ATOM    869  O   SER A 104      58.611 -25.441   1.150  1.00 49.52           O  
ANISOU  869  O   SER A 104     6288   5784   6744   -175    972   -838       O  
ATOM    870  CB  SER A 104      55.953 -27.197   0.736  1.00 61.19           C  
ANISOU  870  CB  SER A 104     7542   7328   8380    -29   1045   -667       C  
ATOM    871  OG  SER A 104      54.624 -27.183   0.253  1.00 73.16           O  
ANISOU  871  OG  SER A 104     8941   8809  10047     62   1118   -603       O  
ATOM    872  N   MET A 105      59.138 -27.267  -0.065  1.00 39.46           N  
ANISOU  872  N   MET A 105     4888   4637   5468   -154    741   -671       N  
ATOM    873  CA  MET A 105      60.509 -27.261   0.433  1.00 44.95           C  
ANISOU  873  CA  MET A 105     5666   5378   6036   -250    659   -708       C  
ATOM    874  C   MET A 105      61.345 -26.128  -0.163  1.00 48.40           C  
ANISOU  874  C   MET A 105     6128   5742   6521   -258    634   -745       C  
ATOM    875  O   MET A 105      62.266 -25.647   0.501  1.00 50.27           O  
ANISOU  875  O   MET A 105     6452   5986   6662   -349    616   -812       O  
ATOM    876  CB  MET A 105      61.178 -28.617   0.168  1.00 44.67           C  
ANISOU  876  CB  MET A 105     5589   5440   5942   -270    520   -618       C  
ATOM    877  CG  MET A 105      60.965 -29.656   1.292  1.00 46.76           C  
ANISOU  877  CG  MET A 105     5887   5794   6086   -322    525   -606       C  
ATOM    878  SD  MET A 105      61.723 -29.134   2.853  1.00 51.71           S  
ANISOU  878  SD  MET A 105     6654   6460   6532   -453    547   -703       S  
ATOM    879  CE  MET A 105      63.351 -28.714   2.232  1.00 61.19           C  
ANISOU  879  CE  MET A 105     7854   7665   7731   -497    409   -688       C  
ATOM    880  N   THR A 106      61.074 -25.703  -1.407  1.00 40.64           N  
ANISOU  880  N   THR A 106     5070   4694   5679   -176    625   -696       N  
ATOM    881  CA  THR A 106      61.922 -24.704  -2.061  1.00 38.90           C  
ANISOU  881  CA  THR A 106     4868   4407   5506   -184    595   -716       C  
ATOM    882  C   THR A 106      61.283 -23.324  -2.215  1.00 40.64           C  
ANISOU  882  C   THR A 106     5104   4497   5838   -136    720   -769       C  
ATOM    883  O   THR A 106      61.997 -22.370  -2.565  1.00 39.20           O  
ANISOU  883  O   THR A 106     4958   4247   5688   -157    713   -801       O  
ATOM    884  CB  THR A 106      62.366 -25.175  -3.455  1.00 35.86           C  
ANISOU  884  CB  THR A 106     4400   4040   5185   -140    480   -616       C  
ATOM    885  OG1 THR A 106      61.221 -25.393  -4.281  1.00 39.99           O  
ANISOU  885  OG1 THR A 106     4837   4540   5817    -48    504   -547       O  
ATOM    886  CG2 THR A 106      63.183 -26.472  -3.370  1.00 41.70           C  
ANISOU  886  CG2 THR A 106     5127   4888   5828   -185    365   -563       C  
ATOM    887  N   ASP A 107      59.976 -23.192  -1.994  1.00 38.51           N  
ANISOU  887  N   ASP A 107     4804   4186   5642    -68    838   -771       N  
ATOM    888  CA  ASP A 107      59.304 -21.906  -2.158  1.00 42.63           C  
ANISOU  888  CA  ASP A 107     5329   4573   6296     -5    971   -806       C  
ATOM    889  C   ASP A 107      59.855 -20.879  -1.179  1.00 42.22           C  
ANISOU  889  C   ASP A 107     5415   4448   6176    -85   1064   -943       C  
ATOM    890  O   ASP A 107      60.024 -21.163   0.008  1.00 41.77           O  
ANISOU  890  O   ASP A 107     5450   4441   5981   -170   1099  -1022       O  
ATOM    891  CB  ASP A 107      57.800 -22.054  -1.919  1.00 45.36           C  
ANISOU  891  CB  ASP A 107     5608   4897   6731     78   1093   -779       C  
ATOM    892  CG  ASP A 107      57.033 -22.484  -3.151  1.00 47.43           C  
ANISOU  892  CG  ASP A 107     5723   5174   7124    173   1031   -642       C  
ATOM    893  OD1 ASP A 107      57.640 -22.759  -4.209  1.00 45.97           O  
ANISOU  893  OD1 ASP A 107     5497   5020   6948    174    895   -571       O  
ATOM    894  OD2 ASP A 107      55.793 -22.561  -3.047  1.00 48.54           O  
ANISOU  894  OD2 ASP A 107     5788   5298   7358    242   1121   -603       O  
ATOM    895  N   ILE A 108      60.113 -19.666  -1.669  1.00 40.61           N  
ANISOU  895  N   ILE A 108     5236   4125   6069    -66   1108   -970       N  
ATOM    896  CA  ILE A 108      60.287 -18.538  -0.767  1.00 41.09           C  
ANISOU  896  CA  ILE A 108     5431   4081   6102   -127   1242  -1107       C  
ATOM    897  C   ILE A 108      59.037 -17.682  -0.693  1.00 42.70           C  
ANISOU  897  C   ILE A 108     5621   4146   6459    -24   1438  -1128       C  
ATOM    898  O   ILE A 108      58.977 -16.765   0.143  1.00 45.06           O  
ANISOU  898  O   ILE A 108     6041   4339   6743    -65   1589  -1253       O  
ATOM    899  CB  ILE A 108      61.491 -17.659  -1.171  1.00 48.64           C  
ANISOU  899  CB  ILE A 108     6447   4977   7056   -194   1182  -1143       C  
ATOM    900  CG1 ILE A 108      61.213 -16.963  -2.506  1.00 48.40           C  
ANISOU  900  CG1 ILE A 108     6327   4847   7217    -84   1186  -1054       C  
ATOM    901  CG2 ILE A 108      62.765 -18.494  -1.240  1.00 44.30           C  
ANISOU  901  CG2 ILE A 108     5896   4564   6371   -290    996  -1111       C  
ATOM    902  CD1 ILE A 108      62.364 -16.135  -3.002  1.00 52.06           C  
ANISOU  902  CD1 ILE A 108     6838   5252   7690   -144   1128  -1074       C  
ATOM    903  N   ALA A 109      58.048 -17.939  -1.545  1.00 45.20           N  
ANISOU  903  N   ALA A 109     5793   4455   6925    103   1442  -1006       N  
ATOM    904  CA  ALA A 109      56.812 -17.167  -1.591  1.00 43.70           C  
ANISOU  904  CA  ALA A 109     5554   4137   6914    218   1621   -992       C  
ATOM    905  C   ALA A 109      55.820 -17.948  -2.434  1.00 49.54           C  
ANISOU  905  C   ALA A 109     6117   4942   7764    325   1562   -836       C  
ATOM    906  O   ALA A 109      56.206 -18.816  -3.217  1.00 45.72           O  
ANISOU  906  O   ALA A 109     5564   4568   7239    312   1386   -745       O  
ATOM    907  CB  ALA A 109      57.035 -15.770  -2.183  1.00 46.29           C  
ANISOU  907  CB  ALA A 109     5906   4302   7381    259   1685  -1003       C  
ATOM    908  N   LYS A 110      54.539 -17.629  -2.269  1.00 45.30           N  
ANISOU  908  N   LYS A 110     5508   4334   7371    425   1716   -805       N  
ATOM    909  CA  LYS A 110      53.526 -18.228  -3.127  1.00 51.26           C  
ANISOU  909  CA  LYS A 110     6082   5142   8254    523   1660   -644       C  
ATOM    910  C   LYS A 110      53.246 -17.398  -4.371  1.00 51.03           C  
ANISOU  910  C   LYS A 110     5951   5022   8416    621   1638   -527       C  
ATOM    911  O   LYS A 110      52.898 -17.961  -5.414  1.00 46.30           O  
ANISOU  911  O   LYS A 110     5221   4496   7874    661   1504   -384       O  
ATOM    912  CB  LYS A 110      52.228 -18.444  -2.341  1.00 58.84           C  
ANISOU  912  CB  LYS A 110     6985   6091   9280    581   1824   -643       C  
ATOM    913  CG  LYS A 110      52.416 -19.274  -1.084  1.00 66.90           C  
ANISOU  913  CG  LYS A 110     8108   7204  10108    484   1856   -749       C  
ATOM    914  CD  LYS A 110      51.090 -19.799  -0.559  1.00 80.98           C  
ANISOU  914  CD  LYS A 110     9797   9014  11956    543   1976   -707       C  
ATOM    915  CE  LYS A 110      50.027 -18.708  -0.525  1.00 87.56           C  
ANISOU  915  CE  LYS A 110    10565   9693  13009    665   2189   -688       C  
ATOM    916  NZ  LYS A 110      50.439 -17.519   0.277  1.00 90.40           N  
ANISOU  916  NZ  LYS A 110    11094   9905  13349    642   2371   -847       N  
ATOM    917  N   LYS A 111      53.412 -16.082  -4.295  1.00 44.63           N  
ANISOU  917  N   LYS A 111     5204   4052   7700    651   1762   -583       N  
ATOM    918  CA  LYS A 111      53.192 -15.176  -5.409  1.00 51.17           C  
ANISOU  918  CA  LYS A 111     5949   4778   8715    744   1754   -470       C  
ATOM    919  C   LYS A 111      54.385 -14.243  -5.548  1.00 53.88           C  
ANISOU  919  C   LYS A 111     6423   5028   9021    684   1745   -554       C  
ATOM    920  O   LYS A 111      55.024 -13.897  -4.548  1.00 49.79           O  
ANISOU  920  O   LYS A 111     6061   4465   8393    598   1830   -715       O  
ATOM    921  CB  LYS A 111      51.915 -14.341  -5.209  1.00 52.30           C  
ANISOU  921  CB  LYS A 111     6011   4782   9081    875   1960   -426       C  
ATOM    922  CG  LYS A 111      50.637 -15.167  -5.084  1.00 53.47           C  
ANISOU  922  CG  LYS A 111     6006   5012   9296    940   1985   -329       C  
ATOM    923  CD  LYS A 111      49.436 -14.271  -4.792  1.00 58.04           C  
ANISOU  923  CD  LYS A 111     6504   5442  10108   1074   2213   -289       C  
ATOM    924  CE  LYS A 111      48.171 -15.087  -4.564  1.00 60.79           C  
ANISOU  924  CE  LYS A 111     6696   5874  10527   1131   2250   -196       C  
ATOM    925  NZ  LYS A 111      47.025 -14.194  -4.190  1.00 68.46           N  
ANISOU  925  NZ  LYS A 111     7591   6700  11721   1257   2486   -157       N  
ATOM    926  N   PRO A 112      54.708 -13.811  -6.772  1.00 49.82           N  
ANISOU  926  N   PRO A 112     5853   4486   8592    718   1641   -445       N  
ATOM    927  CA  PRO A 112      55.865 -12.918  -6.955  1.00 49.42           C  
ANISOU  927  CA  PRO A 112     5920   4346   8513    657   1630   -515       C  
ATOM    928  C   PRO A 112      55.640 -11.511  -6.431  1.00 62.95           C  
ANISOU  928  C   PRO A 112     7712   5849  10356    698   1843   -596       C  
ATOM    929  O   PRO A 112      56.577 -10.705  -6.436  1.00 56.63           O  
ANISOU  929  O   PRO A 112     7025   4959   9533    635   1855   -673       O  
ATOM    930  CB  PRO A 112      56.081 -12.928  -8.478  1.00 50.93           C  
ANISOU  930  CB  PRO A 112     6011   4570   8768    695   1469   -352       C  
ATOM    931  CG  PRO A 112      54.762 -13.316  -9.054  1.00 58.85           C  
ANISOU  931  CG  PRO A 112     6843   5612   9904    806   1456   -193       C  
ATOM    932  CD  PRO A 112      54.121 -14.235  -8.056  1.00 58.77           C  
ANISOU  932  CD  PRO A 112     6820   5688   9822    793   1508   -251       C  
ATOM    933  N   THR A 113      54.435 -11.197  -5.964  1.00 55.29           N  
ANISOU  933  N   THR A 113     6687   4794   9527    800   2020   -583       N  
ATOM    934  CA  THR A 113      54.148  -9.904  -5.367  1.00 67.02           C  
ANISOU  934  CA  THR A 113     8258   6065  11142    844   2255   -672       C  
ATOM    935  C   THR A 113      54.583  -9.814  -3.910  1.00 63.42           C  
ANISOU  935  C   THR A 113     7993   5578  10526    730   2387   -894       C  
ATOM    936  O   THR A 113      54.514  -8.730  -3.333  1.00 60.74           O  
ANISOU  936  O   THR A 113     7763   5062  10252    734   2580   -998       O  
ATOM    937  CB  THR A 113      52.650  -9.607  -5.477  1.00 64.71           C  
ANISOU  937  CB  THR A 113     7817   5694  11078   1006   2402   -554       C  
ATOM    938  OG1 THR A 113      51.901 -10.753  -5.042  1.00 63.89           O  
ANISOU  938  OG1 THR A 113     7627   5730  10919   1018   2386   -530       O  
ATOM    939  CG2 THR A 113      52.287  -9.288  -6.921  1.00 60.85           C  
ANISOU  939  CG2 THR A 113     7164   5205  10751   1102   2283   -332       C  
ATOM    940  N   GLU A 114      55.028 -10.912  -3.302  1.00 60.72           N  
ANISOU  940  N   GLU A 114     7699   5407   9965    621   2282   -962       N  
ATOM    941  CA  GLU A 114      55.464 -10.842  -1.915  1.00 59.42           C  
ANISOU  941  CA  GLU A 114     7722   5227   9629    498   2390  -1163       C  
ATOM    942  C   GLU A 114      56.784 -10.070  -1.814  1.00 58.33           C  
ANISOU  942  C   GLU A 114     7745   5019   9399    370   2355  -1279       C  
ATOM    943  O   GLU A 114      57.571  -9.996  -2.765  1.00 62.02           O  
ANISOU  943  O   GLU A 114     8174   5516   9875    350   2194  -1204       O  
ATOM    944  CB  GLU A 114      55.568 -12.250  -1.315  1.00 55.23           C  
ANISOU  944  CB  GLU A 114     7188   4903   8895    417   2278  -1182       C  
ATOM    945  CG  GLU A 114      54.197 -12.925  -1.137  1.00 59.14           C  
ANISOU  945  CG  GLU A 114     7550   5445   9473    525   2358  -1100       C  
ATOM    946  CD  GLU A 114      54.281 -14.402  -0.769  1.00 67.90           C  
ANISOU  946  CD  GLU A 114     8632   6762  10403    456   2221  -1084       C  
ATOM    947  OE1 GLU A 114      53.729 -15.243  -1.516  1.00 67.77           O  
ANISOU  947  OE1 GLU A 114     8453   6849  10446    524   2107   -935       O  
ATOM    948  OE2 GLU A 114      54.899 -14.728   0.267  1.00 66.58           O  
ANISOU  948  OE2 GLU A 114     8610   6654  10033    328   2225  -1216       O  
ATOM    949  N  ATHR A 115      57.015  -9.491  -0.632  0.40 57.84           N  
ANISOU  949  N  ATHR A 115     7868   4864   9245    274   2514  -1466       N  
ATOM    950  N  BTHR A 115      57.009  -9.477  -0.636  0.60 57.86           N  
ANISOU  950  N  BTHR A 115     7871   4865   9250    276   2516  -1466       N  
ATOM    951  CA ATHR A 115      58.121  -8.554  -0.452  0.40 58.52           C  
ANISOU  951  CA ATHR A 115     8117   4848   9271    151   2520  -1588       C  
ATOM    952  CA BTHR A 115      58.127  -8.552  -0.457  0.60 58.37           C  
ANISOU  952  CA BTHR A 115     8098   4829   9252    150   2519  -1587       C  
ATOM    953  C  ATHR A 115      59.479  -9.216  -0.638  0.40 58.48           C  
ANISOU  953  C  ATHR A 115     8136   5011   9073      5   2272  -1588       C  
ATOM    954  C  BTHR A 115      59.473  -9.228  -0.678  0.60 58.62           C  
ANISOU  954  C  BTHR A 115     8148   5030   9095      9   2268  -1582       C  
ATOM    955  O  ATHR A 115      60.427  -8.562  -1.086  0.40 58.47           O  
ANISOU  955  O  ATHR A 115     8186   4953   9079    -62   2205  -1603       O  
ATOM    956  O  BTHR A 115      60.400  -8.606  -1.209  0.60 57.72           O  
ANISOU  956  O  BTHR A 115     8071   4864   8995    -49   2193  -1584       O  
ATOM    957  CB ATHR A 115      58.046  -7.920   0.934  0.40 60.33           C  
ANISOU  957  CB ATHR A 115     8546   4979   9400     54   2722  -1783       C  
ATOM    958  CB BTHR A 115      58.068  -7.931   0.939  0.60 60.49           C  
ANISOU  958  CB BTHR A 115     8567   5000   9416     51   2719  -1785       C  
ATOM    959  OG1ATHR A 115      58.345  -8.912   1.925  0.40 62.38           O  
ANISOU  959  OG1ATHR A 115     8886   5392   9423    -70   2668  -1879       O  
ATOM    960  OG1BTHR A 115      56.824  -7.238   1.099  0.60 63.72           O  
ANISOU  960  OG1BTHR A 115     8924   5310   9977    177   2909  -1731       O  
ATOM    961  CG2ATHR A 115      56.655  -7.374   1.184  0.40 63.21           C  
ANISOU  961  CG2ATHR A 115     8848   5257   9911    189   2922  -1727       C  
ATOM    962  CG2BTHR A 115      59.214  -6.949   1.150  0.60 54.80           C  
ANISOU  962  CG2BTHR A 115     8007   4206   8610    -99   2695  -1892       C  
ATOM    963  N   ILE A 116      59.602 -10.500  -0.293  1.00 57.97           N  
ANISOU  963  N   ILE A 116     8033   5147   8845    -45   2140  -1565       N  
ATOM    964  CA  ILE A 116      60.883 -11.184  -0.430  1.00 52.97           C  
ANISOU  964  CA  ILE A 116     7412   4673   8042   -174   1914  -1554       C  
ATOM    965  C   ILE A 116      61.317 -11.263  -1.887  1.00 50.55           C  
ANISOU  965  C   ILE A 116     6970   4396   7841   -109   1754  -1400       C  
ATOM    966  O   ILE A 116      62.511 -11.392  -2.171  1.00 53.56           O  
ANISOU  966  O   ILE A 116     7371   4846   8132   -209   1602  -1396       O  
ATOM    967  CB  ILE A 116      60.804 -12.582   0.220  1.00 60.16           C  
ANISOU  967  CB  ILE A 116     8298   5780   8779   -220   1822  -1545       C  
ATOM    968  CG1 ILE A 116      62.202 -13.131   0.513  1.00 65.47           C  
ANISOU  968  CG1 ILE A 116     9029   6594   9252   -384   1633  -1575       C  
ATOM    969  CG2 ILE A 116      60.024 -13.543  -0.658  1.00 48.28           C  
ANISOU  969  CG2 ILE A 116     6604   4371   7369    -81   1741  -1376       C  
ATOM    970  CD1 ILE A 116      62.195 -14.567   1.025  1.00 71.26           C  
ANISOU  970  CD1 ILE A 116     9722   7522   9830   -420   1524  -1537       C  
ATOM    971  N   CYS A 117      60.371 -11.169  -2.829  1.00 48.58           N  
ANISOU  971  N   CYS A 117     6582   4095   7781     53   1787  -1267       N  
ATOM    972  CA  CYS A 117      60.679 -11.251  -4.253  1.00 47.42           C  
ANISOU  972  CA  CYS A 117     6314   3979   7727    114   1642  -1113       C  
ATOM    973  C   CYS A 117      61.085  -9.920  -4.867  1.00 50.82           C  
ANISOU  973  C   CYS A 117     6783   4238   8288    126   1695  -1111       C  
ATOM    974  O   CYS A 117      61.645  -9.914  -5.970  1.00 52.10           O  
ANISOU  974  O   CYS A 117     6878   4429   8489    138   1566  -1005       O  
ATOM    975  CB  CYS A 117      59.476 -11.779  -5.034  1.00 58.66           C  
ANISOU  975  CB  CYS A 117     7567   5438   9283    269   1632   -956       C  
ATOM    976  SG  CYS A 117      58.935 -13.416  -4.560  1.00 58.40           S  
ANISOU  976  SG  CYS A 117     7464   5605   9123    266   1555   -926       S  
ATOM    977  N   ALA A 118      60.782  -8.799  -4.209  1.00 51.42           N  
ANISOU  977  N   ALA A 118     6969   4132   8438    124   1892  -1222       N  
ATOM    978  CA  ALA A 118      61.064  -7.487  -4.792  1.00 57.24           C  
ANISOU  978  CA  ALA A 118     7743   4684   9322    146   1962  -1214       C  
ATOM    979  C   ALA A 118      62.511  -7.326  -5.250  1.00 57.86           C  
ANISOU  979  C   ALA A 118     7868   4801   9315     21   1810  -1222       C  
ATOM    980  O   ALA A 118      62.720  -6.905  -6.399  1.00 54.15           O  
ANISOU  980  O   ALA A 118     7326   4286   8963     78   1752  -1103       O  
ATOM    981  CB  ALA A 118      60.652  -6.386  -3.801  1.00 57.13           C  
ANISOU  981  CB  ALA A 118     7876   4465   9367    133   2209  -1368       C  
ATOM    982  N   PRO A 119      63.539  -7.651  -4.451  1.00 55.84           N  
ANISOU  982  N   PRO A 119     7719   4635   8863   -148   1735  -1343       N  
ATOM    983  CA  PRO A 119      64.918  -7.484  -4.941  1.00 54.13           C  
ANISOU  983  CA  PRO A 119     7523   4457   8586   -262   1591  -1332       C  
ATOM    984  C   PRO A 119      65.369  -8.530  -5.962  1.00 55.08           C  
ANISOU  984  C   PRO A 119     7501   4754   8671   -232   1387  -1180       C  
ATOM    985  O   PRO A 119      66.402  -8.318  -6.610  1.00 48.54           O  
ANISOU  985  O   PRO A 119     6664   3940   7837   -293   1285  -1141       O  
ATOM    986  CB  PRO A 119      65.760  -7.569  -3.660  1.00 59.75           C  
ANISOU  986  CB  PRO A 119     8382   5220   9099   -454   1576  -1500       C  
ATOM    987  CG  PRO A 119      64.948  -8.350  -2.726  1.00 63.40           C  
ANISOU  987  CG  PRO A 119     8858   5763   9470   -434   1632  -1551       C  
ATOM    988  CD  PRO A 119      63.519  -7.993  -3.016  1.00 63.08           C  
ANISOU  988  CD  PRO A 119     8756   5600   9613   -255   1797  -1499       C  
ATOM    989  N   LEU A 120      64.649  -9.636  -6.137  1.00 46.57           N  
ANISOU  989  N   LEU A 120     6317   3804   7572   -145   1333  -1097       N  
ATOM    990  CA  LEU A 120      65.083 -10.661  -7.076  1.00 47.86           C  
ANISOU  990  CA  LEU A 120     6365   4126   7693   -125   1154   -967       C  
ATOM    991  C   LEU A 120      64.597 -10.339  -8.483  1.00 47.14           C  
ANISOU  991  C   LEU A 120     6168   3980   7764      2   1139   -812       C  
ATOM    992  O   LEU A 120      63.524  -9.757  -8.675  1.00 49.35           O  
ANISOU  992  O   LEU A 120     6415   4146   8189    114   1254   -772       O  
ATOM    993  CB  LEU A 120      64.559 -12.038  -6.656  1.00 45.11           C  
ANISOU  993  CB  LEU A 120     5959   3938   7243   -103   1097   -946       C  
ATOM    994  CG  LEU A 120      64.886 -12.496  -5.234  1.00 50.18           C  
ANISOU  994  CG  LEU A 120     6698   4654   7716   -221   1106  -1079       C  
ATOM    995  CD1 LEU A 120      64.124 -13.774  -4.906  1.00 46.64           C  
ANISOU  995  CD1 LEU A 120     6183   4337   7202   -172   1076  -1040       C  
ATOM    996  CD2 LEU A 120      66.380 -12.711  -5.074  1.00 51.46           C  
ANISOU  996  CD2 LEU A 120     6902   4902   7748   -365    974  -1110       C  
ATOM    997  N   THR A 121      65.394 -10.730  -9.474  1.00 40.38           N  
ANISOU  997  N   THR A 121     5255   3207   6882    -16    999   -719       N  
ATOM    998  CA  THR A 121      64.995 -10.601 -10.872  1.00 43.97           C  
ANISOU  998  CA  THR A 121     5612   3641   7454     89    959   -561       C  
ATOM    999  C   THR A 121      64.142 -11.814 -11.230  1.00 46.18           C  
ANISOU  999  C   THR A 121     5787   4053   7707    167    890   -468       C  
ATOM   1000  O   THR A 121      64.656 -12.920 -11.431  1.00 47.23           O  
ANISOU 1000  O   THR A 121     5889   4332   7723    126    769   -443       O  
ATOM   1001  CB  THR A 121      66.217 -10.464 -11.775  1.00 44.40           C  
ANISOU 1001  CB  THR A 121     5665   3721   7486     29    857   -507       C  
ATOM   1002  OG1 THR A 121      66.848  -9.198 -11.526  1.00 47.15           O  
ANISOU 1002  OG1 THR A 121     6102   3922   7888    -36    934   -580       O  
ATOM   1003  CG2 THR A 121      65.809 -10.531 -13.250  1.00 41.23           C  
ANISOU 1003  CG2 THR A 121     5167   3329   7168    125    799   -337       C  
ATOM   1004  N   VAL A 122      62.825 -11.596 -11.295  1.00 41.66           N  
ANISOU 1004  N   VAL A 122     5156   3421   7252    278    972   -414       N  
ATOM   1005  CA  VAL A 122      61.845 -12.660 -11.480  1.00 38.99           C  
ANISOU 1005  CA  VAL A 122     4718   3193   6901    346    924   -334       C  
ATOM   1006  C   VAL A 122      61.548 -12.815 -12.966  1.00 45.08           C  
ANISOU 1006  C   VAL A 122     5391   4000   7739    413    826   -162       C  
ATOM   1007  O   VAL A 122      61.317 -11.822 -13.670  1.00 44.60           O  
ANISOU 1007  O   VAL A 122     5308   3826   7811    471    864    -82       O  
ATOM   1008  CB  VAL A 122      60.553 -12.355 -10.698  1.00 40.95           C  
ANISOU 1008  CB  VAL A 122     4946   3366   7247    426   1070   -362       C  
ATOM   1009  CG1 VAL A 122      59.485 -13.395 -11.016  1.00 36.30           C  
ANISOU 1009  CG1 VAL A 122     4236   2888   6668    495   1015   -259       C  
ATOM   1010  CG2 VAL A 122      60.827 -12.295  -9.191  1.00 40.62           C  
ANISOU 1010  CG2 VAL A 122     5020   3303   7110    346   1170   -540       C  
ATOM   1011  N   PHE A 123      61.531 -14.063 -13.437  1.00 38.53           N  
ANISOU 1011  N   PHE A 123     4506   3321   6813    400    702   -103       N  
ATOM   1012  CA  PHE A 123      61.159 -14.376 -14.810  1.00 36.29           C  
ANISOU 1012  CA  PHE A 123     4138   3089   6561    447    602     54       C  
ATOM   1013  C   PHE A 123      59.646 -14.524 -14.910  1.00 40.57           C  
ANISOU 1013  C   PHE A 123     4575   3634   7205    541    627    147       C  
ATOM   1014  O   PHE A 123      59.064 -15.382 -14.238  1.00 41.62           O  
ANISOU 1014  O   PHE A 123     4680   3842   7292    542    633    111       O  
ATOM   1015  CB  PHE A 123      61.841 -15.662 -15.274  1.00 36.70           C  
ANISOU 1015  CB  PHE A 123     4192   3292   6461    382    470     67       C  
ATOM   1016  CG  PHE A 123      61.363 -16.143 -16.613  1.00 41.43           C  
ANISOU 1016  CG  PHE A 123     4720   3957   7066    414    367    214       C  
ATOM   1017  CD1 PHE A 123      61.718 -15.465 -17.777  1.00 45.89           C  
ANISOU 1017  CD1 PHE A 123     5286   4478   7672    421    331    310       C  
ATOM   1018  CD2 PHE A 123      60.536 -17.256 -16.714  1.00 43.02           C  
ANISOU 1018  CD2 PHE A 123     4860   4264   7224    426    308    260       C  
ATOM   1019  CE1 PHE A 123      61.275 -15.904 -19.022  1.00 45.73           C  
ANISOU 1019  CE1 PHE A 123     5213   4526   7637    435    232    447       C  
ATOM   1020  CE2 PHE A 123      60.088 -17.698 -17.955  1.00 48.34           C  
ANISOU 1020  CE2 PHE A 123     5479   5001   7888    435    206    392       C  
ATOM   1021  CZ  PHE A 123      60.469 -17.022 -19.113  1.00 47.54           C  
ANISOU 1021  CZ  PHE A 123     5387   4863   7815    437    166    484       C  
ATOM   1022  N   PHE A 124      59.028 -13.705 -15.760  1.00 42.20           N  
ANISOU 1022  N   PHE A 124     4717   3762   7554    617    639    276       N  
ATOM   1023  CA  PHE A 124      57.597 -13.723 -16.041  1.00 44.80           C  
ANISOU 1023  CA  PHE A 124     4923   4091   8007    711    649    401       C  
ATOM   1024  C   PHE A 124      57.343 -14.173 -17.477  1.00 52.38           C  
ANISOU 1024  C   PHE A 124     5808   5143   8950    713    497    570       C  
ATOM   1025  O   PHE A 124      58.097 -13.828 -18.391  1.00 43.22           O  
ANISOU 1025  O   PHE A 124     4687   3973   7760    682    434    620       O  
ATOM   1026  CB  PHE A 124      56.975 -12.336 -15.848  1.00 42.03           C  
ANISOU 1026  CB  PHE A 124     4545   3566   7858    806    792    436       C  
ATOM   1027  CG  PHE A 124      57.129 -11.775 -14.464  1.00 46.68           C  
ANISOU 1027  CG  PHE A 124     5222   4044   8469    800    962    267       C  
ATOM   1028  CD1 PHE A 124      56.201 -12.083 -13.474  1.00 50.71           C  
ANISOU 1028  CD1 PHE A 124     5696   4556   9016    842   1063    217       C  
ATOM   1029  CD2 PHE A 124      58.174 -10.901 -14.159  1.00 42.41           C  
ANISOU 1029  CD2 PHE A 124     4804   3395   7915    748   1026    160       C  
ATOM   1030  CE1 PHE A 124      56.314 -11.554 -12.198  1.00 45.73           C  
ANISOU 1030  CE1 PHE A 124     5162   3822   8392    829   1230     56       C  
ATOM   1031  CE2 PHE A 124      58.295 -10.358 -12.881  1.00 46.52           C  
ANISOU 1031  CE2 PHE A 124     5420   3811   8444    727   1183     -2       C  
ATOM   1032  CZ  PHE A 124      57.356 -10.691 -11.896  1.00 46.65           C  
ANISOU 1032  CZ  PHE A 124     5411   3830   8483    767   1288    -57       C  
ATOM   1033  N   ASP A 125      56.256 -14.908 -17.685  1.00 49.73           N  
ANISOU 1033  N   ASP A 125     5367   4896   8633    743    441    661       N  
ATOM   1034  CA  ASP A 125      55.942 -15.498 -18.985  1.00 44.56           C  
ANISOU 1034  CA  ASP A 125     4650   4347   7934    722    284    812       C  
ATOM   1035  C   ASP A 125      54.607 -14.927 -19.463  1.00 50.84           C  
ANISOU 1035  C   ASP A 125     5302   5107   8908    815    285    989       C  
ATOM   1036  O   ASP A 125      53.542 -15.312 -18.966  1.00 48.82           O  
ANISOU 1036  O   ASP A 125     4948   4882   8719    856    312   1017       O  
ATOM   1037  CB  ASP A 125      55.917 -17.029 -18.867  1.00 46.21           C  
ANISOU 1037  CB  ASP A 125     4863   4707   7986    649    194    768       C  
ATOM   1038  CG  ASP A 125      55.640 -17.731 -20.189  1.00 49.38           C  
ANISOU 1038  CG  ASP A 125     5226   5222   8316    604     33    902       C  
ATOM   1039  OD1 ASP A 125      55.373 -17.065 -21.207  1.00 50.41           O  
ANISOU 1039  OD1 ASP A 125     5312   5328   8512    630    -20   1046       O  
ATOM   1040  OD2 ASP A 125      55.691 -18.974 -20.205  1.00 50.30           O  
ANISOU 1040  OD2 ASP A 125     5361   5449   8301    537    -40    866       O  
ATOM   1041  N   GLY A 126      54.663 -14.017 -20.436  1.00 50.65           N  
ANISOU 1041  N   GLY A 126     5258   5021   8965    847    255   1119       N  
ATOM   1042  CA  GLY A 126      53.465 -13.367 -20.945  1.00 51.17           C  
ANISOU 1042  CA  GLY A 126     5180   5046   9217    941    251   1311       C  
ATOM   1043  C   GLY A 126      52.438 -14.310 -21.543  1.00 50.38           C  
ANISOU 1043  C   GLY A 126     4958   5092   9093    921    111   1449       C  
ATOM   1044  O   GLY A 126      51.298 -13.890 -21.769  1.00 57.70           O  
ANISOU 1044  O   GLY A 126     5737   5998  10187   1001    111   1610       O  
ATOM   1045  N   ARG A 127      52.804 -15.566 -21.808  1.00 44.14           N  
ANISOU 1045  N   ARG A 127     4221   4444   8106    815     -6   1395       N  
ATOM   1046  CA  ARG A 127      51.828 -16.539 -22.283  1.00 49.54           C  
ANISOU 1046  CA  ARG A 127     4802   5267   8755    778   -135   1505       C  
ATOM   1047  C   ARG A 127      50.878 -16.984 -21.177  1.00 54.37           C  
ANISOU 1047  C   ARG A 127     5320   5888   9449    822    -53   1462       C  
ATOM   1048  O   ARG A 127      49.794 -17.491 -21.476  1.00 65.17           O  
ANISOU 1048  O   ARG A 127     6557   7342  10861    820   -134   1588       O  
ATOM   1049  CB  ARG A 127      52.546 -17.755 -22.889  1.00 44.61           C  
ANISOU 1049  CB  ARG A 127     4282   4773   7895    646   -266   1447       C  
ATOM   1050  CG  ARG A 127      53.347 -17.398 -24.141  1.00 55.23           C  
ANISOU 1050  CG  ARG A 127     5709   6124   9152    595   -355   1515       C  
ATOM   1051  CD  ARG A 127      54.298 -18.509 -24.541  1.00 53.03           C  
ANISOU 1051  CD  ARG A 127     5562   5940   8646    477   -429   1414       C  
ATOM   1052  NE  ARG A 127      55.195 -18.877 -23.449  1.00 48.59           N  
ANISOU 1052  NE  ARG A 127     5092   5345   8024    468   -324   1214       N  
ATOM   1053  CZ  ARG A 127      56.187 -19.751 -23.572  1.00 47.05           C  
ANISOU 1053  CZ  ARG A 127     5012   5206   7659    386   -351   1107       C  
ATOM   1054  NH1 ARG A 127      56.414 -20.332 -24.747  1.00 41.57           N  
ANISOU 1054  NH1 ARG A 127     4368   4592   6833    304   -464   1168       N  
ATOM   1055  NH2 ARG A 127      56.951 -20.037 -22.530  1.00 44.74           N  
ANISOU 1055  NH2 ARG A 127     4786   4887   7328    382   -263    946       N  
ATOM   1056  N   VAL A 128      51.261 -16.801 -19.916  1.00 54.97           N  
ANISOU 1056  N   VAL A 128     5460   5883   9542    855    105   1292       N  
ATOM   1057  CA  VAL A 128      50.433 -17.157 -18.769  1.00 54.23           C  
ANISOU 1057  CA  VAL A 128     5297   5789   9520    897    209   1236       C  
ATOM   1058  C   VAL A 128      49.602 -15.938 -18.382  1.00 58.56           C  
ANISOU 1058  C   VAL A 128     5738   6199  10313   1031    355   1314       C  
ATOM   1059  O   VAL A 128      50.125 -14.817 -18.303  1.00 52.00           O  
ANISOU 1059  O   VAL A 128     4968   5231   9559   1082    453   1284       O  
ATOM   1060  CB  VAL A 128      51.311 -17.637 -17.598  1.00 51.26           C  
ANISOU 1060  CB  VAL A 128     5059   5404   9013    850    301   1012       C  
ATOM   1061  CG1 VAL A 128      50.479 -17.925 -16.360  1.00 52.62           C  
ANISOU 1061  CG1 VAL A 128     5173   5568   9253    892    427    950       C  
ATOM   1062  CG2 VAL A 128      52.142 -18.862 -18.004  1.00 54.41           C  
ANISOU 1062  CG2 VAL A 128     5554   5929   9189    729    166    948       C  
ATOM   1063  N   ASP A 129      48.300 -16.148 -18.159  1.00 56.54           N  
ANISOU 1063  N   ASP A 129     5320   5973  10190   1087    376   1420       N  
ATOM   1064  CA  ASP A 129      47.420 -15.039 -17.815  1.00 60.06           C  
ANISOU 1064  CA  ASP A 129     5645   6285  10891   1226    526   1511       C  
ATOM   1065  C   ASP A 129      47.918 -14.324 -16.567  1.00 51.54           C  
ANISOU 1065  C   ASP A 129     4682   5052   9849   1276    752   1320       C  
ATOM   1066  O   ASP A 129      48.313 -14.955 -15.585  1.00 54.46           O  
ANISOU 1066  O   ASP A 129     5151   5450  10091   1221    814   1140       O  
ATOM   1067  CB  ASP A 129      45.987 -15.527 -17.581  1.00 70.84           C  
ANISOU 1067  CB  ASP A 129     6826   7720  12370   1263    531   1626       C  
ATOM   1068  CG  ASP A 129      45.239 -15.795 -18.871  1.00 87.70           C  
ANISOU 1068  CG  ASP A 129     8835   9980  14508   1218    329   1848       C  
ATOM   1069  OD1 ASP A 129      44.956 -16.978 -19.162  1.00 96.10           O  
ANISOU 1069  OD1 ASP A 129     9842  11189  15480   1140    184   1887       O  
ATOM   1070  OD2 ASP A 129      44.937 -14.823 -19.595  1.00 98.49           O  
ANISOU 1070  OD2 ASP A 129    10163  11298  15962   1251    315   1981       O  
ATOM   1071  N   GLY A 130      47.900 -12.994 -16.613  1.00 53.64           N  
ANISOU 1071  N   GLY A 130     4955   5164  10262   1356    868   1354       N  
ATOM   1072  CA  GLY A 130      48.243 -12.177 -15.476  1.00 57.85           C  
ANISOU 1072  CA  GLY A 130     5604   5542  10833   1391   1090   1181       C  
ATOM   1073  C   GLY A 130      49.715 -11.836 -15.341  1.00 51.96           C  
ANISOU 1073  C   GLY A 130     5042   4717   9985   1341   1108   1026       C  
ATOM   1074  O   GLY A 130      50.049 -10.883 -14.627  1.00 55.48           O  
ANISOU 1074  O   GLY A 130     5589   5012  10480   1365   1280    909       O  
ATOM   1075  N   GLN A 131      50.606 -12.569 -16.010  1.00 51.95           N  
ANISOU 1075  N   GLN A 131     5115   4842   9783   1229    927   1008       N  
ATOM   1076  CA  GLN A 131      52.028 -12.367 -15.745  1.00 44.42           C  
ANISOU 1076  CA  GLN A 131     4347   3850   8682   1145    939    839       C  
ATOM   1077  C   GLN A 131      52.561 -11.082 -16.371  1.00 51.25           C  
ANISOU 1077  C   GLN A 131     5254   4572   9645   1180    971    891       C  
ATOM   1078  O   GLN A 131      53.487 -10.479 -15.815  1.00 53.47           O  
ANISOU 1078  O   GLN A 131     5675   4752   9888   1144   1065    743       O  
ATOM   1079  CB  GLN A 131      52.840 -13.590 -16.194  1.00 42.82           C  
ANISOU 1079  CB  GLN A 131     4206   3818   8244   1020    757    799       C  
ATOM   1080  CG  GLN A 131      52.496 -14.855 -15.381  1.00 47.50           C  
ANISOU 1080  CG  GLN A 131     4790   4534   8726    974    747    714       C  
ATOM   1081  CD  GLN A 131      53.715 -15.654 -14.906  1.00 65.51           C  
ANISOU 1081  CD  GLN A 131     7214   6889  10786    859    700    548       C  
ATOM   1082  OE1 GLN A 131      54.807 -15.569 -15.476  1.00 61.60           O  
ANISOU 1082  OE1 GLN A 131     6806   6404  10197    799    624    525       O  
ATOM   1083  NE2 GLN A 131      53.521 -16.440 -13.852  1.00 68.30           N  
ANISOU 1083  NE2 GLN A 131     7588   7299  11065    830    749    443       N  
ATOM   1084  N   VAL A 132      51.990 -10.615 -17.489  1.00 48.78           N  
ANISOU 1084  N   VAL A 132     4825   4246   9463   1245    897   1102       N  
ATOM   1085  CA  VAL A 132      52.427  -9.316 -18.004  1.00 50.48           C  
ANISOU 1085  CA  VAL A 132     5079   4306   9794   1289    950   1158       C  
ATOM   1086  C   VAL A 132      52.187  -8.238 -16.957  1.00 57.54           C  
ANISOU 1086  C   VAL A 132     6029   5044  10790   1334   1175   1046       C  
ATOM   1087  O   VAL A 132      53.067  -7.413 -16.681  1.00 53.74           O  
ANISOU 1087  O   VAL A 132     5680   4439  10301   1306   1263    935       O  
ATOM   1088  CB  VAL A 132      51.742  -8.978 -19.343  1.00 51.94           C  
ANISOU 1088  CB  VAL A 132     5139   4545  10050   1320    825   1404       C  
ATOM   1089  CG1 VAL A 132      51.987  -7.517 -19.712  1.00 56.00           C  
ANISOU 1089  CG1 VAL A 132     5697   4921  10660   1350    906   1448       C  
ATOM   1090  CG2 VAL A 132      52.283  -9.865 -20.440  1.00 53.72           C  
ANISOU 1090  CG2 VAL A 132     5369   4914  10127   1241    608   1486       C  
ATOM   1091  N   ASP A 133      51.010  -8.255 -16.324  1.00 53.12           N  
ANISOU 1091  N   ASP A 133     5377   4489  10316   1392   1275   1065       N  
ATOM   1092  CA  ASP A 133      50.701  -7.239 -15.321  1.00 57.76           C  
ANISOU 1092  CA  ASP A 133     6022   4930  10996   1431   1498    961       C  
ATOM   1093  C   ASP A 133      51.517  -7.424 -14.047  1.00 54.20           C  
ANISOU 1093  C   ASP A 133     5737   4420  10437   1371   1618    708       C  
ATOM   1094  O   ASP A 133      51.845  -6.437 -13.380  1.00 57.81           O  
ANISOU 1094  O   ASP A 133     6309   4736  10919   1362   1777    589       O  
ATOM   1095  CB  ASP A 133      49.210  -7.251 -15.004  1.00 69.79           C  
ANISOU 1095  CB  ASP A 133     7400   6475  12643   1507   1576   1059       C  
ATOM   1096  CG  ASP A 133      48.368  -6.825 -16.186  1.00 85.37           C  
ANISOU 1096  CG  ASP A 133     9215   8482  14740   1561   1481   1309       C  
ATOM   1097  OD1 ASP A 133      47.575  -7.649 -16.683  1.00 96.22           O  
ANISOU 1097  OD1 ASP A 133    10447   9995  16119   1567   1353   1448       O  
ATOM   1098  OD2 ASP A 133      48.524  -5.671 -16.637  1.00 91.76           O  
ANISOU 1098  OD2 ASP A 133    10046   9183  15638   1590   1527   1368       O  
ATOM   1099  N   LEU A 134      51.846  -8.666 -13.686  1.00 49.89           N  
ANISOU 1099  N   LEU A 134     5208   3982   9766   1322   1545    625       N  
ATOM   1100  CA  LEU A 134      52.773  -8.881 -12.579  1.00 56.28           C  
ANISOU 1100  CA  LEU A 134     6183   4748  10452   1246   1632    390       C  
ATOM   1101  C   LEU A 134      54.127  -8.245 -12.873  1.00 56.05           C  
ANISOU 1101  C   LEU A 134     6299   4650  10349   1165   1598    313       C  
ATOM   1102  O   LEU A 134      54.744  -7.637 -11.991  1.00 56.44           O  
ANISOU 1102  O   LEU A 134     6494   4583  10366   1115   1730    140       O  
ATOM   1103  CB  LEU A 134      52.929 -10.376 -12.304  1.00 55.49           C  
ANISOU 1103  CB  LEU A 134     6082   4854  10147   1156   1500    336       C  
ATOM   1104  CG  LEU A 134      51.654 -11.039 -11.767  1.00 57.64           C  
ANISOU 1104  CG  LEU A 134     6233   5187  10482   1219   1558    377       C  
ATOM   1105  CD1 LEU A 134      51.887 -12.528 -11.511  1.00 61.34           C  
ANISOU 1105  CD1 LEU A 134     6714   5854  10737   1119   1424    321       C  
ATOM   1106  CD2 LEU A 134      51.182 -10.318 -10.509  1.00 59.50           C  
ANISOU 1106  CD2 LEU A 134     6522   5266  10817   1274   1817    253       C  
ATOM   1107  N   PHE A 135      54.597  -8.364 -14.114  1.00 51.30           N  
ANISOU 1107  N   PHE A 135     5660   4119   9713   1141   1423    441       N  
ATOM   1108  CA  PHE A 135      55.839  -7.704 -14.507  1.00 55.30           C  
ANISOU 1108  CA  PHE A 135     6286   4560  10167   1070   1393    392       C  
ATOM   1109  C   PHE A 135      55.724  -6.182 -14.411  1.00 57.16           C  
ANISOU 1109  C   PHE A 135     6561   4586  10570   1127   1555    396       C  
ATOM   1110  O   PHE A 135      56.675  -5.506 -13.998  1.00 57.04           O  
ANISOU 1110  O   PHE A 135     6689   4470  10513   1054   1623    261       O  
ATOM   1111  CB  PHE A 135      56.225  -8.127 -15.924  1.00 50.22           C  
ANISOU 1111  CB  PHE A 135     5586   4036   9458   1041   1187    547       C  
ATOM   1112  CG  PHE A 135      57.421  -7.396 -16.474  1.00 53.21           C  
ANISOU 1112  CG  PHE A 135     6066   4344   9807    979   1159    530       C  
ATOM   1113  CD1 PHE A 135      58.706  -7.764 -16.106  1.00 52.76           C  
ANISOU 1113  CD1 PHE A 135     6134   4344   9569    850   1114    378       C  
ATOM   1114  CD2 PHE A 135      57.260  -6.349 -17.366  1.00 51.42           C  
ANISOU 1114  CD2 PHE A 135     5801   3996   9740   1048   1176    678       C  
ATOM   1115  CE1 PHE A 135      59.806  -7.087 -16.615  1.00 46.18           C  
ANISOU 1115  CE1 PHE A 135     5382   3448   8718    790   1092    369       C  
ATOM   1116  CE2 PHE A 135      58.351  -5.681 -17.876  1.00 49.91           C  
ANISOU 1116  CE2 PHE A 135     5701   3738   9523    987   1156    667       C  
ATOM   1117  CZ  PHE A 135      59.624  -6.057 -17.498  1.00 46.37           C  
ANISOU 1117  CZ  PHE A 135     5374   3349   8896    856   1115    509       C  
ATOM   1118  N   ARG A 136      54.572  -5.622 -14.796  1.00 52.08           N  
ANISOU 1118  N   ARG A 136     5797   3924  10066   1224   1596    548       N  
ATOM   1119  CA  ARG A 136      54.408  -4.171 -14.735  1.00 54.70           C  
ANISOU 1119  CA  ARG A 136     6164   4105  10514   1257   1735    558       C  
ATOM   1120  C   ARG A 136      54.497  -3.651 -13.305  1.00 60.09           C  
ANISOU 1120  C   ARG A 136     6979   4675  11180   1224   1938    348       C  
ATOM   1121  O   ARG A 136      54.842  -2.482 -13.091  1.00 60.35           O  
ANISOU 1121  O   ARG A 136     7105   4568  11259   1208   2052    289       O  
ATOM   1122  CB  ARG A 136      53.068  -3.755 -15.351  1.00 64.31           C  
ANISOU 1122  CB  ARG A 136     7212   5329  11893   1368   1744    767       C  
ATOM   1123  CG  ARG A 136      52.906  -4.035 -16.844  1.00 63.62           C  
ANISOU 1123  CG  ARG A 136     7002   5345  11826   1392   1547    993       C  
ATOM   1124  CD  ARG A 136      51.550  -3.506 -17.321  1.00 69.07           C  
ANISOU 1124  CD  ARG A 136     7529   6031  12682   1490   1573   1192       C  
ATOM   1125  NE  ARG A 136      51.397  -3.507 -18.776  1.00 62.77           N  
ANISOU 1125  NE  ARG A 136     6628   5315  11907   1503   1396   1415       N  
ATOM   1126  CZ  ARG A 136      51.970  -2.623 -19.589  1.00 70.28           C  
ANISOU 1126  CZ  ARG A 136     7618   6197  12886   1495   1369   1488       C  
ATOM   1127  NH1 ARG A 136      52.756  -1.667 -19.100  1.00 69.45           N  
ANISOU 1127  NH1 ARG A 136     7651   5939  12796   1474   1502   1354       N  
ATOM   1128  NH2 ARG A 136      51.770  -2.702 -20.898  1.00 75.61           N  
ANISOU 1128  NH2 ARG A 136     8202   6961  13566   1500   1204   1695       N  
ATOM   1129  N   ASN A 137      54.160  -4.486 -12.320  1.00 61.77           N  
ANISOU 1129  N   ASN A 137     7203   4946  11321   1210   1988    236       N  
ATOM   1130  CA  ASN A 137      54.188  -4.092 -10.916  1.00 66.26           C  
ANISOU 1130  CA  ASN A 137     7903   5424  11847   1168   2178     35       C  
ATOM   1131  C   ASN A 137      55.472  -4.492 -10.204  1.00 64.45           C  
ANISOU 1131  C   ASN A 137     7847   5204  11437   1032   2158   -174       C  
ATOM   1132  O   ASN A 137      55.767  -3.941  -9.138  1.00 71.83           O  
ANISOU 1132  O   ASN A 137     8927   6050  12315    965   2301   -349       O  
ATOM   1133  CB  ASN A 137      53.004  -4.712 -10.163  1.00 69.20           C  
ANISOU 1133  CB  ASN A 137     8195   5853  12245   1225   2264     34       C  
ATOM   1134  CG  ASN A 137      51.662  -4.243 -10.690  1.00 78.21           C  
ANISOU 1134  CG  ASN A 137     9167   6976  13574   1349   2308    231       C  
ATOM   1135  OD1 ASN A 137      51.463  -3.056 -10.945  1.00 75.35           O  
ANISOU 1135  OD1 ASN A 137     8806   6491  13334   1391   2398    287       O  
ATOM   1136  ND2 ASN A 137      50.733  -5.178 -10.855  1.00 89.62           N  
ANISOU 1136  ND2 ASN A 137    10462   8544  15047   1403   2243    341       N  
ATOM   1137  N   ALA A 138      56.231  -5.434 -10.758  1.00 58.28           N  
ANISOU 1137  N   ALA A 138     7054   4528  10562    983   1983   -157       N  
ATOM   1138  CA  ALA A 138      57.415  -5.937 -10.080  1.00 60.08           C  
ANISOU 1138  CA  ALA A 138     7428   4778  10621    849   1952   -344       C  
ATOM   1139  C   ALA A 138      58.559  -4.932 -10.153  1.00 63.82           C  
ANISOU 1139  C   ALA A 138     8037   5145  11067    754   1966   -423       C  
ATOM   1140  O   ALA A 138      58.680  -4.155 -11.104  1.00 58.84           O  
ANISOU 1140  O   ALA A 138     7369   4455  10532    791   1934   -302       O  
ATOM   1141  CB  ALA A 138      57.859  -7.264 -10.688  1.00 56.49           C  
ANISOU 1141  CB  ALA A 138     6906   4560   9999    790   1718   -275       C  
ATOM   1142  N  AARG A 139      59.410  -4.962  -9.129  0.67 62.99           N  
ANISOU 1142  N  AARG A 139     8091   5022  10820    620   2008   -625       N  
ATOM   1143  N  BARG A 139      59.404  -4.954  -9.125  0.34 63.80           N  
ANISOU 1143  N  BARG A 139     8193   5124  10923    620   2010   -626       N  
ATOM   1144  CA AARG A 139      60.563  -4.070  -9.077  0.67 64.28           C  
ANISOU 1144  CA AARG A 139     8389   5097  10939    504   2014   -716       C  
ATOM   1145  CA BARG A 139      60.559  -4.067  -9.085  0.34 64.63           C  
ANISOU 1145  CA BARG A 139     8432   5141  10985    504   2014   -715       C  
ATOM   1146  C  AARG A 139      61.673  -4.535 -10.014  0.67 60.40           C  
ANISOU 1146  C  AARG A 139     7869   4720  10360    430   1808   -646       C  
ATOM   1147  C  BARG A 139      61.653  -4.538 -10.038  0.34 60.30           C  
ANISOU 1147  C  BARG A 139     7853   4707  10350    433   1807   -641       C  
ATOM   1148  O  AARG A 139      62.294  -3.717 -10.705  0.67 57.60           O  
ANISOU 1148  O  AARG A 139     7541   4269  10077    411   1795   -601       O  
ATOM   1149  O  BARG A 139      62.241  -3.729 -10.767  0.34 59.57           O  
ANISOU 1149  O  BARG A 139     7781   4520  10334    420   1792   -590       O  
ATOM   1150  CB AARG A 139      61.080  -3.978  -7.641  0.67 67.01           C  
ANISOU 1150  CB AARG A 139     8907   5423  11131    362   2103   -945       C  
ATOM   1151  CB BARG A 139      61.095  -3.981  -7.657  0.34 67.71           C  
ANISOU 1151  CB BARG A 139     8995   5512  11220    362   2101   -943       C  
ATOM   1152  CG AARG A 139      62.235  -3.019  -7.465  0.67 72.40           C  
ANISOU 1152  CG AARG A 139     9732   6020  11759    225   2111  -1046       C  
ATOM   1153  CG BARG A 139      62.076  -2.854  -7.440  0.34 72.57           C  
ANISOU 1153  CG BARG A 139     9752   6022  11800    241   2137  -1041       C  
ATOM   1154  CD AARG A 139      62.375  -2.581  -6.017  0.67 78.39           C  
ANISOU 1154  CD AARG A 139    10658   6733  12394    108   2240  -1249       C  
ATOM   1155  CD BARG A 139      62.969  -3.127  -6.249  0.34 73.89           C  
ANISOU 1155  CD BARG A 139    10079   6229  11767     56   2132  -1248       C  
ATOM   1156  NE AARG A 139      63.418  -1.571  -5.864  0.67 75.09           N  
ANISOU 1156  NE AARG A 139    10370   6228  11933    -25   2247  -1336       N  
ATOM   1157  NE BARG A 139      62.259  -3.101  -4.975  0.34 76.16           N  
ANISOU 1157  NE BARG A 139    10447   6506  11985     45   2281  -1372       N  
ATOM   1158  CZ AARG A 139      63.236  -0.272  -6.071  0.67 74.51           C  
ANISOU 1158  CZ AARG A 139    10327   6010  11973     12   2357  -1312       C  
ATOM   1159  CZ BARG A 139      62.830  -3.383  -3.809  0.34 69.31           C  
ANISOU 1159  CZ BARG A 139     9721   5689  10926   -113   2288  -1548       C  
ATOM   1160  NH1AARG A 139      64.246   0.567  -5.913  0.67 76.41           N  
ANISOU 1160  NH1AARG A 139    10687   6180  12164   -122   2352  -1397       N  
ATOM   1161  NH1BARG A 139      64.114  -3.714  -3.766  0.34 63.18           N  
ANISOU 1161  NH1BARG A 139     9008   4981  10018   -273   2146  -1613       N  
ATOM   1162  NH2AARG A 139      62.047   0.188  -6.436  0.67 76.90           N  
ANISOU 1162  NH2AARG A 139    10536   6241  12443    178   2468  -1198       N  
ATOM   1163  NH2BARG A 139      62.122  -3.334  -2.689  0.34 69.39           N  
ANISOU 1163  NH2BARG A 139     9805   5687  10873   -119   2432  -1649       N  
ATOM   1164  N   ASN A 140      61.928  -5.839 -10.049  1.00 52.31           N  
ANISOU 1164  N   ASN A 140     6791   3913   9172    385   1649   -628       N  
ATOM   1165  CA  ASN A 140      62.983  -6.425 -10.864  1.00 50.53           C  
ANISOU 1165  CA  ASN A 140     6536   3827   8836    311   1456   -565       C  
ATOM   1166  C   ASN A 140      62.420  -7.628 -11.595  1.00 50.34           C  
ANISOU 1166  C   ASN A 140     6372   3978   8778    383   1322   -425       C  
ATOM   1167  O   ASN A 140      61.770  -8.474 -10.978  1.00 49.25           O  
ANISOU 1167  O   ASN A 140     6201   3931   8580    403   1327   -454       O  
ATOM   1168  CB  ASN A 140      64.165  -6.844  -9.994  1.00 51.23           C  
ANISOU 1168  CB  ASN A 140     6731   4004   8730    144   1396   -718       C  
ATOM   1169  CG  ASN A 140      64.869  -5.657  -9.389  1.00 55.98           C  
ANISOU 1169  CG  ASN A 140     7477   4444   9349     43   1501   -852       C  
ATOM   1170  OD1 ASN A 140      65.598  -4.953 -10.082  1.00 54.12           O  
ANISOU 1170  OD1 ASN A 140     7258   4137   9169      9   1474   -812       O  
ATOM   1171  ND2 ASN A 140      64.637  -5.410  -8.096  1.00 54.74           N  
ANISOU 1171  ND2 ASN A 140     7432   4224   9143    -13   1629  -1014       N  
ATOM   1172  N   GLY A 141      62.652  -7.707 -12.898  1.00 48.45           N  
ANISOU 1172  N   GLY A 141     6057   3781   8569    414   1208   -276       N  
ATOM   1173  CA  GLY A 141      62.035  -8.783 -13.644  1.00 43.94           C  
ANISOU 1173  CA  GLY A 141     5365   3361   7969    476   1088   -143       C  
ATOM   1174  C   GLY A 141      62.511  -8.863 -15.075  1.00 46.11           C  
ANISOU 1174  C   GLY A 141     5589   3688   8242    479    959      1       C  
ATOM   1175  O   GLY A 141      63.070  -7.907 -15.632  1.00 48.39           O  
ANISOU 1175  O   GLY A 141     5914   3872   8601    467    979     36       O  
ATOM   1176  N   VAL A 142      62.285 -10.038 -15.658  1.00 42.28           N  
ANISOU 1176  N   VAL A 142     5029   3366   7670    487    831     83       N  
ATOM   1177  CA  VAL A 142      62.420 -10.275 -17.088  1.00 41.00           C  
ANISOU 1177  CA  VAL A 142     4811   3270   7499    502    711    238       C  
ATOM   1178  C   VAL A 142      61.117 -10.883 -17.581  1.00 48.95           C  
ANISOU 1178  C   VAL A 142     5702   4349   8548    587    661    366       C  
ATOM   1179  O   VAL A 142      60.566 -11.784 -16.937  1.00 46.92           O  
ANISOU 1179  O   VAL A 142     5414   4179   8236    590    654    321       O  
ATOM   1180  CB  VAL A 142      63.614 -11.194 -17.409  1.00 39.80           C  
ANISOU 1180  CB  VAL A 142     4695   3251   7174    402    595    204       C  
ATOM   1181  CG1 VAL A 142      63.525 -11.673 -18.837  1.00 35.52           C  
ANISOU 1181  CG1 VAL A 142     4098   2796   6602    419    479    357       C  
ATOM   1182  CG2 VAL A 142      64.921 -10.419 -17.185  1.00 41.81           C  
ANISOU 1182  CG2 VAL A 142     5042   3429   7416    318    631    119       C  
ATOM   1183  N   LEU A 143      60.622 -10.382 -18.710  1.00 40.29           N  
ANISOU 1183  N   LEU A 143     4540   3218   7549    649    624    534       N  
ATOM   1184  CA  LEU A 143      59.341 -10.783 -19.276  1.00 42.53           C  
ANISOU 1184  CA  LEU A 143     4702   3562   7894    725    568    683       C  
ATOM   1185  C   LEU A 143      59.554 -11.254 -20.708  1.00 46.65           C  
ANISOU 1185  C   LEU A 143     5199   4190   8335    693    414    824       C  
ATOM   1186  O   LEU A 143      60.255 -10.589 -21.478  1.00 45.61           O  
ANISOU 1186  O   LEU A 143     5111   4008   8212    672    397    877       O  
ATOM   1187  CB  LEU A 143      58.360  -9.599 -19.262  1.00 40.01           C  
ANISOU 1187  CB  LEU A 143     4315   3088   7798    840    677    779       C  
ATOM   1188  CG  LEU A 143      57.040  -9.789 -20.011  1.00 47.13           C  
ANISOU 1188  CG  LEU A 143     5069   4040   8798    924    610    977       C  
ATOM   1189  CD1 LEU A 143      56.168 -10.816 -19.313  1.00 47.20           C  
ANISOU 1189  CD1 LEU A 143     5009   4152   8774    936    604    940       C  
ATOM   1190  CD2 LEU A 143      56.289  -8.468 -20.161  1.00 44.77           C  
ANISOU 1190  CD2 LEU A 143     4703   3570   8737   1041    717   1097       C  
ATOM   1191  N   ILE A 144      58.962 -12.392 -21.074  1.00 39.71           N  
ANISOU 1191  N   ILE A 144     4259   3456   7372    680    307    882       N  
ATOM   1192  CA  ILE A 144      58.880 -12.772 -22.482  1.00 38.20           C  
ANISOU 1192  CA  ILE A 144     4040   3359   7116    653    167   1034       C  
ATOM   1193  C   ILE A 144      57.424 -12.721 -22.930  1.00 45.03           C  
ANISOU 1193  C   ILE A 144     4771   4245   8093    726    121   1204       C  
ATOM   1194  O   ILE A 144      56.500 -12.996 -22.156  1.00 43.47           O  
ANISOU 1194  O   ILE A 144     4497   4054   7965    775    166   1186       O  
ATOM   1195  CB  ILE A 144      59.481 -14.157 -22.788  1.00 37.03           C  
ANISOU 1195  CB  ILE A 144     3943   3364   6763    557     64    977       C  
ATOM   1196  CG1 ILE A 144      58.787 -15.248 -21.975  1.00 41.74           C  
ANISOU 1196  CG1 ILE A 144     4495   4046   7316    555     56    911       C  
ATOM   1197  CG2 ILE A 144      61.012 -14.144 -22.559  1.00 37.32           C  
ANISOU 1197  CG2 ILE A 144     4095   3382   6702    487     98    846       C  
ATOM   1198  CD1 ILE A 144      59.147 -16.645 -22.409  1.00 41.64           C  
ANISOU 1198  CD1 ILE A 144     4521   4177   7124    471    -49    886       C  
ATOM   1199  N   THR A 145      57.220 -12.351 -24.191  1.00 44.11           N  
ANISOU 1199  N   THR A 145     4621   4144   7995    729     30   1380       N  
ATOM   1200  CA  THR A 145      55.896 -12.418 -24.798  1.00 45.45           C  
ANISOU 1200  CA  THR A 145     4655   4365   8250    777    -53   1570       C  
ATOM   1201  C   THR A 145      56.023 -12.889 -26.235  1.00 53.23           C  
ANISOU 1201  C   THR A 145     5657   5470   9099    698   -219   1703       C  
ATOM   1202  O   THR A 145      57.103 -12.863 -26.829  1.00 53.24           O  
ANISOU 1202  O   THR A 145     5768   5478   8980    631   -242   1669       O  
ATOM   1203  CB  THR A 145      55.160 -11.075 -24.799  1.00 47.85           C  
ANISOU 1203  CB  THR A 145     4866   4524   8792    896     29   1703       C  
ATOM   1204  OG1 THR A 145      55.882 -10.137 -25.614  1.00 49.55           O  
ANISOU 1204  OG1 THR A 145     5142   4659   9025    890     26   1777       O  
ATOM   1205  CG2 THR A 145      55.014 -10.543 -23.391  1.00 47.24           C  
ANISOU 1205  CG2 THR A 145     4789   4312   8849    971    214   1565       C  
ATOM   1206  N   GLU A 146      54.890 -13.304 -26.793  1.00 49.87           N  
ANISOU 1206  N   GLU A 146     5119   5138   8692    702   -331   1859       N  
ATOM   1207  CA  GLU A 146      54.831 -13.677 -28.194  1.00 51.59           C  
ANISOU 1207  CA  GLU A 146     5350   5470   8783    620   -496   2006       C  
ATOM   1208  C   GLU A 146      54.467 -12.514 -29.104  1.00 56.48           C  
ANISOU 1208  C   GLU A 146     5908   6027   9526    672   -533   2223       C  
ATOM   1209  O   GLU A 146      54.678 -12.609 -30.317  1.00 62.97           O  
ANISOU 1209  O   GLU A 146     6773   6925  10227    596   -656   2338       O  
ATOM   1210  CB  GLU A 146      53.826 -14.814 -28.385  1.00 51.35           C  
ANISOU 1210  CB  GLU A 146     5237   5588   8684    568   -621   2065       C  
ATOM   1211  CG  GLU A 146      54.237 -16.109 -27.719  1.00 44.43           C  
ANISOU 1211  CG  GLU A 146     4436   4789   7655    497   -609   1871       C  
ATOM   1212  CD  GLU A 146      53.165 -17.183 -27.854  1.00 59.26           C  
ANISOU 1212  CD  GLU A 146     6229   6801   9486    445   -724   1932       C  
ATOM   1213  OE1 GLU A 146      51.966 -16.831 -27.852  1.00 61.13           O  
ANISOU 1213  OE1 GLU A 146     6310   7042   9875    505   -757   2083       O  
ATOM   1214  OE2 GLU A 146      53.519 -18.370 -27.986  1.00 54.45           O  
ANISOU 1214  OE2 GLU A 146     5704   6289   8696    343   -780   1837       O  
ATOM   1215  N   GLY A 147      53.936 -11.424 -28.553  1.00 56.89           N  
ANISOU 1215  N   GLY A 147     5865   5938   9811    797   -424   2283       N  
ATOM   1216  CA  GLY A 147      53.550 -10.272 -29.344  1.00 61.71           C  
ANISOU 1216  CA  GLY A 147     6407   6473  10568    863   -447   2502       C  
ATOM   1217  C   GLY A 147      53.796  -8.962 -28.625  1.00 61.22           C  
ANISOU 1217  C   GLY A 147     6347   6199  10714    978   -262   2462       C  
ATOM   1218  O   GLY A 147      54.524  -8.925 -27.628  1.00 64.25           O  
ANISOU 1218  O   GLY A 147     6822   6504  11087    979   -127   2247       O  
ATOM   1219  N   SER A 148      53.188  -7.884 -29.114  1.00 60.03           N  
ANISOU 1219  N   SER A 148     6123   6004  10681   1027   -240   2603       N  
ATOM   1220  CA  SER A 148      53.428  -6.560 -28.559  1.00 60.89           C  
ANISOU 1220  CA  SER A 148     6259   5932  10944   1105    -58   2542       C  
ATOM   1221  C   SER A 148      52.832  -6.425 -27.162  1.00 64.81           C  
ANISOU 1221  C   SER A 148     6704   6345  11576   1185    107   2409       C  
ATOM   1222  O   SER A 148      51.816  -7.043 -26.829  1.00 66.03           O  
ANISOU 1222  O   SER A 148     6747   6583  11761   1206     81   2439       O  
ATOM   1223  CB  SER A 148      52.836  -5.483 -29.471  1.00 70.80           C  
ANISOU 1223  CB  SER A 148     7438   7167  12294   1138    -82   2741       C  
ATOM   1224  OG  SER A 148      53.425  -5.522 -30.759  1.00 81.38           O  
ANISOU 1224  OG  SER A 148     8842   8580  13501   1059   -222   2860       O  
ATOM   1225  N   VAL A 149      53.478  -5.598 -26.343  1.00 63.59           N  
ANISOU 1225  N   VAL A 149     6639   6025  11496   1221    283   2258       N  
ATOM   1226  CA  VAL A 149      52.974  -5.197 -25.034  1.00 62.08           C  
ANISOU 1226  CA  VAL A 149     6427   5729  11434   1293    469   2130       C  
ATOM   1227  C   VAL A 149      52.769  -3.690 -25.066  1.00 68.59           C  
ANISOU 1227  C   VAL A 149     7242   6403  12415   1358    600   2180       C  
ATOM   1228  O   VAL A 149      53.683  -2.947 -25.444  1.00 59.55           O  
ANISOU 1228  O   VAL A 149     6196   5171  11258   1333    624   2165       O  
ATOM   1229  CB  VAL A 149      53.943  -5.589 -23.903  1.00 63.18           C  
ANISOU 1229  CB  VAL A 149     6698   5802  11504   1260    569   1882       C  
ATOM   1230  CG1 VAL A 149      53.430  -5.076 -22.563  1.00 61.13           C  
ANISOU 1230  CG1 VAL A 149     6436   5429  11363   1323    771   1747       C  
ATOM   1231  CG2 VAL A 149      54.145  -7.094 -23.870  1.00 61.05           C  
ANISOU 1231  CG2 VAL A 149     6432   5675  11091   1201    443   1838       C  
ATOM   1232  N   LYS A 150      51.576  -3.241 -24.672  1.00 66.66           N  
ANISOU 1232  N   LYS A 150     6880   6126  12323   1438    689   2244       N  
ATOM   1233  CA  LYS A 150      51.241  -1.827 -24.776  1.00 69.69           C  
ANISOU 1233  CA  LYS A 150     7237   6371  12872   1507    811   2319       C  
ATOM   1234  C   LYS A 150      52.209  -0.984 -23.955  1.00 65.42           C  
ANISOU 1234  C   LYS A 150     6852   5652  12354   1503    987   2124       C  
ATOM   1235  O   LYS A 150      52.424  -1.243 -22.767  1.00 71.62           O  
ANISOU 1235  O   LYS A 150     7708   6385  13117   1496   1106   1926       O  
ATOM   1236  CB  LYS A 150      49.798  -1.580 -24.322  1.00 70.04           C  
ANISOU 1236  CB  LYS A 150     7128   6402  13080   1593    900   2402       C  
ATOM   1237  CG  LYS A 150      49.308  -0.173 -24.625  1.00 82.88           C  
ANISOU 1237  CG  LYS A 150     8699   7902  14892   1669   1003   2528       C  
ATOM   1238  CD  LYS A 150      47.890   0.074 -24.119  1.00 93.48           C  
ANISOU 1238  CD  LYS A 150     9890   9220  16410   1757   1109   2610       C  
ATOM   1239  CE  LYS A 150      47.881   0.716 -22.734  1.00 97.42           C  
ANISOU 1239  CE  LYS A 150    10463   9544  17006   1808   1364   2420       C  
ATOM   1240  NZ  LYS A 150      46.503   1.115 -22.301  1.00 94.83           N  
ANISOU 1240  NZ  LYS A 150     9989   9172  16869   1900   1490   2517       N  
ATOM   1241  N   GLY A 151      52.812   0.006 -24.607  1.00 62.38           N  
ANISOU 1241  N   GLY A 151     6523   5178  11999   1497    998   2180       N  
ATOM   1242  CA  GLY A 151      53.675   0.962 -23.946  1.00 69.15           C  
ANISOU 1242  CA  GLY A 151     7522   5860  12892   1486   1161   2018       C  
ATOM   1243  C   GLY A 151      55.083   0.493 -23.660  1.00 77.25           C  
ANISOU 1243  C   GLY A 151     8707   6884  13760   1387   1137   1839       C  
ATOM   1244  O   GLY A 151      55.814   1.197 -22.956  1.00 84.90           O  
ANISOU 1244  O   GLY A 151     9800   7714  14744   1360   1272   1679       O  
ATOM   1245  N   LEU A 152      55.494  -0.666 -24.177  1.00 62.17           N  
ANISOU 1245  N   LEU A 152     6800   5120  11700   1325    970   1860       N  
ATOM   1246  CA  LEU A 152      56.844  -1.174 -23.960  1.00 64.85           C  
ANISOU 1246  CA  LEU A 152     7280   5464  11897   1228    942   1705       C  
ATOM   1247  C   LEU A 152      57.515  -1.490 -25.288  1.00 66.60           C  
ANISOU 1247  C   LEU A 152     7519   5775  12012   1167    775   1838       C  
ATOM   1248  O   LEU A 152      56.930  -2.173 -26.135  1.00 63.14           O  
ANISOU 1248  O   LEU A 152     6988   5476  11526   1172    627   1997       O  
ATOM   1249  CB  LEU A 152      56.826  -2.425 -23.081  1.00 62.24           C  
ANISOU 1249  CB  LEU A 152     6958   5216  11475   1201    928   1564       C  
ATOM   1250  CG  LEU A 152      56.344  -2.180 -21.653  1.00 63.25           C  
ANISOU 1250  CG  LEU A 152     7101   5255  11675   1240   1105   1401       C  
ATOM   1251  CD1 LEU A 152      56.426  -3.441 -20.833  1.00 66.82           C  
ANISOU 1251  CD1 LEU A 152     7571   5794  12023   1205   1083   1263       C  
ATOM   1252  CD2 LEU A 152      57.161  -1.064 -21.020  1.00 70.93           C  
ANISOU 1252  CD2 LEU A 152     8211   6057  12682   1206   1258   1251       C  
ATOM   1253  N   GLN A 153      58.745  -0.999 -25.461  1.00 55.86           N  
ANISOU 1253  N   GLN A 153     6281   4337  10607   1100    800   1770       N  
ATOM   1254  CA  GLN A 153      59.545  -1.369 -26.622  1.00 54.26           C  
ANISOU 1254  CA  GLN A 153     6117   4215  10284   1028    661   1869       C  
ATOM   1255  C   GLN A 153      60.145  -2.751 -26.404  1.00 54.55           C  
ANISOU 1255  C   GLN A 153     6197   4358  10172    956    577   1773       C  
ATOM   1256  O   GLN A 153      60.763  -2.987 -25.364  1.00 49.60           O  
ANISOU 1256  O   GLN A 153     5645   3679   9522    918    659   1577       O  
ATOM   1257  CB  GLN A 153      60.664  -0.365 -26.865  1.00 59.56           C  
ANISOU 1257  CB  GLN A 153     6899   4766  10966    975    726   1832       C  
ATOM   1258  CG  GLN A 153      60.161   0.977 -27.350  1.00 81.31           C  
ANISOU 1258  CG  GLN A 153     9615   7423  13858   1040    785   1961       C  
ATOM   1259  CD  GLN A 153      58.971   0.831 -28.282  1.00 92.07           C  
ANISOU 1259  CD  GLN A 153    10838   8891  15252   1106    674   2190       C  
ATOM   1260  OE1 GLN A 153      57.839   1.143 -27.911  1.00100.62           O  
ANISOU 1260  OE1 GLN A 153    11820   9952  16459   1193    729   2236       O  
ATOM   1261  NE2 GLN A 153      59.220   0.347 -29.496  1.00 93.03           N  
ANISOU 1261  NE2 GLN A 153    10956   9133  15258   1056    518   2337       N  
ATOM   1262  N   PRO A 154      59.978  -3.677 -27.345  1.00 53.87           N  
ANISOU 1262  N   PRO A 154     6068   4421   9979    929    416   1906       N  
ATOM   1263  CA  PRO A 154      60.528  -5.022 -27.188  1.00 49.21           C  
ANISOU 1263  CA  PRO A 154     5525   3998   9176    833    332   1777       C  
ATOM   1264  C   PRO A 154      61.943  -5.140 -27.729  1.00 52.46           C  
ANISOU 1264  C   PRO A 154     6052   4449   9432    721    301   1718       C  
ATOM   1265  O   PRO A 154      62.377  -4.382 -28.597  1.00 48.95           O  
ANISOU 1265  O   PRO A 154     5639   3945   9016    709    294   1833       O  
ATOM   1266  CB  PRO A 154      59.568  -5.877 -28.026  1.00 49.43           C  
ANISOU 1266  CB  PRO A 154     5456   4191   9132    841    176   1940       C  
ATOM   1267  CG  PRO A 154      59.170  -4.949 -29.136  1.00 54.14           C  
ANISOU 1267  CG  PRO A 154     6005   4729   9837    889    134   2182       C  
ATOM   1268  CD  PRO A 154      59.107  -3.569 -28.532  1.00 57.75           C  
ANISOU 1268  CD  PRO A 154     6464   5005  10474    959    297   2139       C  
ATOM   1269  N   SER A 155      62.661  -6.119 -27.191  1.00 47.84           N  
ANISOU 1269  N   SER A 155     5524   3966   8688    640    287   1542       N  
ATOM   1270  CA  SER A 155      63.909  -6.599 -27.768  1.00 49.20           C  
ANISOU 1270  CA  SER A 155     5783   4223   8689    533    238   1496       C  
ATOM   1271  C   SER A 155      63.634  -7.969 -28.373  1.00 44.42           C  
ANISOU 1271  C   SER A 155     5160   3812   7907    490    108   1529       C  
ATOM   1272  O   SER A 155      63.163  -8.871 -27.673  1.00 44.92           O  
ANISOU 1272  O   SER A 155     5190   3953   7924    495     90   1442       O  
ATOM   1273  CB  SER A 155      65.014  -6.679 -26.715  1.00 51.16           C  
ANISOU 1273  CB  SER A 155     6106   4436   8898    470    321   1281       C  
ATOM   1274  OG  SER A 155      66.083  -7.504 -27.160  1.00 46.39           O  
ANISOU 1274  OG  SER A 155     5557   3950   8118    374    265   1231       O  
ATOM   1275  N   VAL A 156      63.903  -8.113 -29.668  1.00 40.78           N  
ANISOU 1275  N   VAL A 156     4728   3423   7343    442     23   1655       N  
ATOM   1276  CA  VAL A 156      63.627  -9.368 -30.362  1.00 44.38           C  
ANISOU 1276  CA  VAL A 156     5186   4054   7623    388    -98   1692       C  
ATOM   1277  C   VAL A 156      64.657 -10.406 -29.939  1.00 46.78           C  
ANISOU 1277  C   VAL A 156     5561   4438   7775    310    -81   1513       C  
ATOM   1278  O   VAL A 156      65.866 -10.208 -30.113  1.00 42.41           O  
ANISOU 1278  O   VAL A 156     5081   3859   7176    257    -33   1457       O  
ATOM   1279  CB  VAL A 156      63.639  -9.158 -31.881  1.00 47.79           C  
ANISOU 1279  CB  VAL A 156     5647   4534   7978    348   -184   1877       C  
ATOM   1280  CG1 VAL A 156      63.486 -10.490 -32.586  1.00 48.04           C  
ANISOU 1280  CG1 VAL A 156     5708   4740   7804    270   -296   1888       C  
ATOM   1281  CG2 VAL A 156      62.514  -8.213 -32.288  1.00 48.42           C  
ANISOU 1281  CG2 VAL A 156     5636   4547   8214    430   -217   2079       C  
ATOM   1282  N   GLY A 157      64.183 -11.529 -29.393  1.00 43.81           N  
ANISOU 1282  N   GLY A 157     5158   4159   7330    305   -119   1433       N  
ATOM   1283  CA  GLY A 157      65.076 -12.554 -28.896  1.00 39.52           C  
ANISOU 1283  CA  GLY A 157     4669   3685   6662    244   -100   1272       C  
ATOM   1284  C   GLY A 157      65.556 -13.493 -29.985  1.00 40.21           C  
ANISOU 1284  C   GLY A 157     4823   3890   6566    165   -166   1303       C  
ATOM   1285  O   GLY A 157      65.309 -13.284 -31.177  1.00 39.67           O  
ANISOU 1285  O   GLY A 157     4774   3850   6448    142   -227   1444       O  
ATOM   1286  N   PRO A 158      66.272 -14.544 -29.600  1.00 40.32           N  
ANISOU 1286  N   PRO A 158     4878   3970   6473    118   -150   1173       N  
ATOM   1287  CA  PRO A 158      66.742 -15.516 -30.595  1.00 40.27           C  
ANISOU 1287  CA  PRO A 158     4945   4062   6292     44   -190   1186       C  
ATOM   1288  C   PRO A 158      65.566 -16.239 -31.234  1.00 44.19           C  
ANISOU 1288  C   PRO A 158     5428   4654   6708     27   -297   1272       C  
ATOM   1289  O   PRO A 158      64.430 -16.203 -30.748  1.00 42.81           O  
ANISOU 1289  O   PRO A 158     5172   4483   6610     74   -340   1305       O  
ATOM   1290  CB  PRO A 158      67.621 -16.473 -29.783  1.00 46.37           C  
ANISOU 1290  CB  PRO A 158     5742   4868   7010     19   -138   1027       C  
ATOM   1291  CG  PRO A 158      67.121 -16.355 -28.390  1.00 45.74           C  
ANISOU 1291  CG  PRO A 158     5591   4750   7036     74   -116    945       C  
ATOM   1292  CD  PRO A 158      66.621 -14.935 -28.223  1.00 40.34           C  
ANISOU 1292  CD  PRO A 158     4862   3959   6507    130    -92   1015       C  
ATOM   1293  N   LYS A 159      65.848 -16.886 -32.367  1.00 40.43           N  
ANISOU 1293  N   LYS A 159     5035   4254   6071    -49   -337   1313       N  
ATOM   1294  CA  LYS A 159      64.800 -17.631 -33.062  1.00 46.34           C  
ANISOU 1294  CA  LYS A 159     5788   5101   6717    -93   -449   1391       C  
ATOM   1295  C   LYS A 159      64.458 -18.925 -32.338  1.00 43.84           C  
ANISOU 1295  C   LYS A 159     5459   4848   6349   -105   -463   1278       C  
ATOM   1296  O   LYS A 159      63.317 -19.395 -32.427  1.00 40.34           O  
ANISOU 1296  O   LYS A 159     4972   4467   5887   -117   -554   1331       O  
ATOM   1297  CB  LYS A 159      65.220 -17.928 -34.502  1.00 43.01           C  
ANISOU 1297  CB  LYS A 159     5481   4738   6121   -186   -480   1459       C  
ATOM   1298  CG  LYS A 159      65.242 -16.690 -35.420  1.00 51.94           C  
ANISOU 1298  CG  LYS A 159     6622   5827   7285   -184   -499   1617       C  
ATOM   1299  CD  LYS A 159      65.862 -17.011 -36.770  1.00 56.40           C  
ANISOU 1299  CD  LYS A 159     7321   6447   7661   -284   -504   1661       C  
ATOM   1300  CE  LYS A 159      65.879 -15.787 -37.677  1.00 66.75           C  
ANISOU 1300  CE  LYS A 159     8644   7720   9000   -287   -525   1829       C  
ATOM   1301  NZ  LYS A 159      66.593 -16.079 -38.945  1.00 73.67           N  
ANISOU 1301  NZ  LYS A 159     9663   8646   9683   -388   -508   1861       N  
ATOM   1302  N   GLN A 160      65.419 -19.507 -31.623  1.00 39.80           N  
ANISOU 1302  N   GLN A 160     4979   4322   5821   -104   -378   1132       N  
ATOM   1303  CA  GLN A 160      65.262 -20.815 -31.003  1.00 40.02           C  
ANISOU 1303  CA  GLN A 160     5011   4407   5789   -122   -381   1026       C  
ATOM   1304  C   GLN A 160      64.901 -20.698 -29.522  1.00 40.70           C  
ANISOU 1304  C   GLN A 160     5002   4456   6005    -50   -351    950       C  
ATOM   1305  O   GLN A 160      65.149 -19.681 -28.865  1.00 44.26           O  
ANISOU 1305  O   GLN A 160     5407   4828   6582      6   -298    939       O  
ATOM   1306  CB  GLN A 160      66.535 -21.659 -31.162  1.00 38.06           C  
ANISOU 1306  CB  GLN A 160     4855   4169   5438   -166   -304    925       C  
ATOM   1307  CG  GLN A 160      67.719 -21.261 -30.258  1.00 39.84           C  
ANISOU 1307  CG  GLN A 160     5057   4328   5751   -124   -203    835       C  
ATOM   1308  CD  GLN A 160      68.582 -20.145 -30.860  1.00 40.49           C  
ANISOU 1308  CD  GLN A 160     5165   4351   5868   -127   -154    889       C  
ATOM   1309  OE1 GLN A 160      68.109 -19.348 -31.672  1.00 40.85           O  
ANISOU 1309  OE1 GLN A 160     5218   4384   5920   -132   -196   1003       O  
ATOM   1310  NE2 GLN A 160      69.851 -20.092 -30.454  1.00 39.97           N  
ANISOU 1310  NE2 GLN A 160     5106   4250   5830   -126    -67    816       N  
ATOM   1311  N   ALA A 161      64.292 -21.766 -29.010  1.00 37.68           N  
ANISOU 1311  N   ALA A 161     4601   4131   5586    -61   -382    897       N  
ATOM   1312  CA  ALA A 161      63.998 -21.901 -27.594  1.00 33.87           C  
ANISOU 1312  CA  ALA A 161     4046   3629   5195     -7   -348    813       C  
ATOM   1313  C   ALA A 161      64.101 -23.374 -27.236  1.00 35.25           C  
ANISOU 1313  C   ALA A 161     4254   3865   5274    -45   -349    724       C  
ATOM   1314  O   ALA A 161      64.291 -24.233 -28.101  1.00 38.74           O  
ANISOU 1314  O   ALA A 161     4773   4355   5591   -111   -374    728       O  
ATOM   1315  CB  ALA A 161      62.615 -21.338 -27.242  1.00 37.84           C  
ANISOU 1315  CB  ALA A 161     4447   4123   5809     45   -393    890       C  
ATOM   1316  N   SER A 162      63.991 -23.664 -25.945  1.00 32.96           N  
ANISOU 1316  N   SER A 162     3915   3567   5042     -8   -314    640       N  
ATOM   1317  CA  SER A 162      64.161 -25.019 -25.439  1.00 33.76           C  
ANISOU 1317  CA  SER A 162     4042   3714   5071    -35   -304    556       C  
ATOM   1318  C   SER A 162      62.798 -25.617 -25.125  1.00 33.18           C  
ANISOU 1318  C   SER A 162     3914   3689   5005    -38   -364    579       C  
ATOM   1319  O   SER A 162      62.021 -25.035 -24.365  1.00 36.19           O  
ANISOU 1319  O   SER A 162     4210   4050   5489     13   -361    594       O  
ATOM   1320  CB  SER A 162      65.041 -25.034 -24.186  1.00 36.64           C  
ANISOU 1320  CB  SER A 162     4394   4048   5482     -4   -229    455       C  
ATOM   1321  OG  SER A 162      65.187 -26.343 -23.669  1.00 37.32           O  
ANISOU 1321  OG  SER A 162     4498   4174   5507    -24   -221    388       O  
ATOM   1322  N   LEU A 163      62.522 -26.792 -25.675  1.00 33.59           N  
ANISOU 1322  N   LEU A 163     4014   3797   4950   -102   -407    578       N  
ATOM   1323  CA  LEU A 163      61.280 -27.500 -25.379  1.00 35.74           C  
ANISOU 1323  CA  LEU A 163     4236   4122   5224   -120   -466    596       C  
ATOM   1324  C   LEU A 163      61.646 -28.890 -24.873  1.00 35.64           C  
ANISOU 1324  C   LEU A 163     4272   4129   5139   -152   -434    503       C  
ATOM   1325  O   LEU A 163      62.153 -29.716 -25.640  1.00 37.54           O  
ANISOU 1325  O   LEU A 163     4609   4383   5271   -213   -433    482       O  
ATOM   1326  CB  LEU A 163      60.375 -27.573 -26.610  1.00 33.71           C  
ANISOU 1326  CB  LEU A 163     3986   3915   4906   -184   -569    704       C  
ATOM   1327  CG  LEU A 163      59.081 -28.379 -26.415  1.00 34.98           C  
ANISOU 1327  CG  LEU A 163     4091   4138   5063   -223   -642    733       C  
ATOM   1328  CD1 LEU A 163      58.225 -27.795 -25.314  1.00 40.93           C  
ANISOU 1328  CD1 LEU A 163     4710   4876   5965   -142   -626    753       C  
ATOM   1329  CD2 LEU A 163      58.278 -28.467 -27.720  1.00 35.63           C  
ANISOU 1329  CD2 LEU A 163     4188   4282   5069   -309   -761    847       C  
ATOM   1330  N   ASN A 164      61.412 -29.136 -23.581  1.00 30.35           N  
ANISOU 1330  N   ASN A 164     3544   3456   4531   -110   -400    448       N  
ATOM   1331  CA  ASN A 164      61.757 -30.421 -22.967  1.00 35.06           C  
ANISOU 1331  CA  ASN A 164     4177   4067   5075   -132   -367    370       C  
ATOM   1332  C   ASN A 164      63.212 -30.798 -23.242  1.00 38.02           C  
ANISOU 1332  C   ASN A 164     4639   4414   5394   -141   -306    317       C  
ATOM   1333  O   ASN A 164      63.542 -31.950 -23.512  1.00 32.87           O  
ANISOU 1333  O   ASN A 164     4055   3769   4667   -182   -290    283       O  
ATOM   1334  CB  ASN A 164      60.802 -31.507 -23.448  1.00 32.74           C  
ANISOU 1334  CB  ASN A 164     3902   3823   4715   -202   -431    394       C  
ATOM   1335  CG  ASN A 164      59.371 -31.112 -23.260  1.00 37.69           C  
ANISOU 1335  CG  ASN A 164     4427   4483   5411   -195   -494    465       C  
ATOM   1336  OD1 ASN A 164      59.013 -30.591 -22.207  1.00 35.86           O  
ANISOU 1336  OD1 ASN A 164     4111   4238   5277   -130   -460    455       O  
ATOM   1337  ND2 ASN A 164      58.545 -31.306 -24.285  1.00 38.38           N  
ANISOU 1337  ND2 ASN A 164     4518   4614   5450   -263   -584    542       N  
ATOM   1338  N   GLY A 165      64.096 -29.810 -23.181  1.00 38.67           N  
ANISOU 1338  N   GLY A 165     4715   4458   5520   -102   -265    313       N  
ATOM   1339  CA  GLY A 165      65.509 -30.056 -23.374  1.00 40.50           C  
ANISOU 1339  CA  GLY A 165     5004   4663   5720   -104   -202    274       C  
ATOM   1340  C   GLY A 165      65.972 -30.084 -24.810  1.00 40.64           C  
ANISOU 1340  C   GLY A 165     5107   4674   5662   -148   -197    307       C  
ATOM   1341  O   GLY A 165      67.172 -30.234 -25.046  1.00 40.43           O  
ANISOU 1341  O   GLY A 165     5123   4621   5618   -145   -130    282       O  
ATOM   1342  N   VAL A 166      65.065 -29.952 -25.771  1.00 34.05           N  
ANISOU 1342  N   VAL A 166     4295   3864   4778   -191   -264    368       N  
ATOM   1343  CA  VAL A 166      65.390 -29.937 -27.196  1.00 34.13           C  
ANISOU 1343  CA  VAL A 166     4400   3874   4694   -248   -266    406       C  
ATOM   1344  C   VAL A 166      65.389 -28.492 -27.648  1.00 37.54           C  
ANISOU 1344  C   VAL A 166     4800   4289   5176   -225   -289    480       C  
ATOM   1345  O   VAL A 166      64.341 -27.831 -27.612  1.00 37.03           O  
ANISOU 1345  O   VAL A 166     4668   4240   5160   -213   -361    546       O  
ATOM   1346  CB  VAL A 166      64.368 -30.741 -28.017  1.00 36.64           C  
ANISOU 1346  CB  VAL A 166     4774   4240   4908   -331   -340    435       C  
ATOM   1347  CG1 VAL A 166      64.751 -30.760 -29.499  1.00 36.42           C  
ANISOU 1347  CG1 VAL A 166     4866   4214   4758   -404   -337    466       C  
ATOM   1348  CG2 VAL A 166      64.214 -32.139 -27.455  1.00 38.86           C  
ANISOU 1348  CG2 VAL A 166     5079   4528   5157   -353   -319    364       C  
ATOM   1349  N   THR A 167      66.536 -27.996 -28.107  1.00 36.57           N  
ANISOU 1349  N   THR A 167     4718   4129   5046   -218   -224    478       N  
ATOM   1350  CA  THR A 167      66.581 -26.635 -28.623  1.00 37.91           C  
ANISOU 1350  CA  THR A 167     4868   4275   5261   -202   -241    554       C  
ATOM   1351  C   THR A 167      66.181 -26.645 -30.090  1.00 40.16           C  
ANISOU 1351  C   THR A 167     5235   4592   5432   -274   -293    633       C  
ATOM   1352  O   THR A 167      66.744 -27.400 -30.890  1.00 42.22           O  
ANISOU 1352  O   THR A 167     5602   4861   5577   -332   -253    606       O  
ATOM   1353  CB  THR A 167      67.963 -26.010 -28.447  1.00 39.95           C  
ANISOU 1353  CB  THR A 167     5129   4481   5571   -172   -152    526       C  
ATOM   1354  OG1 THR A 167      68.270 -25.950 -27.052  1.00 41.57           O  
ANISOU 1354  OG1 THR A 167     5258   4666   5871   -120   -121    460       O  
ATOM   1355  CG2 THR A 167      67.944 -24.592 -28.995  1.00 37.29           C  
ANISOU 1355  CG2 THR A 167     4774   4109   5283   -160   -168    609       C  
ATOM   1356  N   LEU A 168      65.198 -25.819 -30.438  1.00 37.06           N  
ANISOU 1356  N   LEU A 168     4795   4215   5073   -273   -379    733       N  
ATOM   1357  CA  LEU A 168      64.653 -25.863 -31.784  1.00 35.97           C  
ANISOU 1357  CA  LEU A 168     4726   4124   4816   -354   -456    824       C  
ATOM   1358  C   LEU A 168      64.055 -24.511 -32.164  1.00 41.14           C  
ANISOU 1358  C   LEU A 168     5316   4769   5548   -326   -521    955       C  
ATOM   1359  O   LEU A 168      63.669 -23.713 -31.308  1.00 38.10           O  
ANISOU 1359  O   LEU A 168     4819   4346   5311   -246   -522    975       O  
ATOM   1360  CB  LEU A 168      63.605 -26.973 -31.888  1.00 36.09           C  
ANISOU 1360  CB  LEU A 168     4756   4206   4752   -420   -537    819       C  
ATOM   1361  CG  LEU A 168      62.419 -26.881 -30.919  1.00 45.68           C  
ANISOU 1361  CG  LEU A 168     5837   5439   6080   -372   -602    843       C  
ATOM   1362  CD1 LEU A 168      61.290 -26.080 -31.545  1.00 42.90           C  
ANISOU 1362  CD1 LEU A 168     5419   5125   5756   -386   -719    992       C  
ATOM   1363  CD2 LEU A 168      61.903 -28.276 -30.493  1.00 44.95           C  
ANISOU 1363  CD2 LEU A 168     5759   5388   5933   -418   -621    772       C  
ATOM   1364  N   ILE A 169      63.984 -24.275 -33.470  1.00 39.64           N  
ANISOU 1364  N   ILE A 169     5201   4610   5250   -397   -571   1048       N  
ATOM   1365  CA  ILE A 169      63.219 -23.179 -34.048  1.00 41.47           C  
ANISOU 1365  CA  ILE A 169     5377   4850   5529   -389   -660   1204       C  
ATOM   1366  C   ILE A 169      61.835 -23.733 -34.371  1.00 46.61           C  
ANISOU 1366  C   ILE A 169     5995   5587   6127   -450   -797   1280       C  
ATOM   1367  O   ILE A 169      61.696 -24.624 -35.214  1.00 43.06           O  
ANISOU 1367  O   ILE A 169     5650   5204   5508   -561   -846   1277       O  
ATOM   1368  CB  ILE A 169      63.912 -22.616 -35.293  1.00 36.68           C  
ANISOU 1368  CB  ILE A 169     4872   4237   4826   -441   -645   1276       C  
ATOM   1369  CG1 ILE A 169      65.305 -22.083 -34.909  1.00 46.06           C  
ANISOU 1369  CG1 ILE A 169     6079   5341   6082   -384   -507   1201       C  
ATOM   1370  CG2 ILE A 169      63.055 -21.528 -35.957  1.00 38.16           C  
ANISOU 1370  CG2 ILE A 169     5002   4440   5058   -438   -751   1460       C  
ATOM   1371  CD1 ILE A 169      66.075 -21.457 -36.060  1.00 45.53           C  
ANISOU 1371  CD1 ILE A 169     6105   5259   5937   -428   -472   1271       C  
ATOM   1372  N   GLY A 170      60.816 -23.224 -33.684  1.00 44.43           N  
ANISOU 1372  N   GLY A 170     5574   5307   5999   -382   -851   1346       N  
ATOM   1373  CA  GLY A 170      59.509 -23.863 -33.726  1.00 38.66           C  
ANISOU 1373  CA  GLY A 170     4784   4658   5248   -431   -970   1404       C  
ATOM   1374  C   GLY A 170      58.793 -23.635 -35.043  1.00 45.21           C  
ANISOU 1374  C   GLY A 170     5633   5564   5979   -524  -1111   1571       C  
ATOM   1375  O   GLY A 170      58.831 -22.548 -35.619  1.00 43.26           O  
ANISOU 1375  O   GLY A 170     5366   5296   5774   -498  -1135   1696       O  
ATOM   1376  N   GLU A 171      58.113 -24.681 -35.517  1.00 42.73           N  
ANISOU 1376  N   GLU A 171     5362   5343   5532   -640  -1210   1578       N  
ATOM   1377  CA  GLU A 171      57.224 -24.573 -36.666  1.00 47.84           C  
ANISOU 1377  CA  GLU A 171     6011   6084   6083   -747  -1373   1745       C  
ATOM   1378  C   GLU A 171      55.769 -24.785 -36.294  1.00 45.10           C  
ANISOU 1378  C   GLU A 171     5508   5803   5824   -753  -1498   1840       C  
ATOM   1379  O   GLU A 171      54.897 -24.081 -36.804  1.00 47.69           O  
ANISOU 1379  O   GLU A 171     5735   6178   6206   -759  -1621   2030       O  
ATOM   1380  CB  GLU A 171      57.628 -25.576 -37.751  1.00 50.97           C  
ANISOU 1380  CB  GLU A 171     6605   6541   6218   -912  -1401   1690       C  
ATOM   1381  CG  GLU A 171      59.098 -25.491 -38.145  1.00 51.48           C  
ANISOU 1381  CG  GLU A 171     6827   6542   6192   -910  -1260   1591       C  
ATOM   1382  CD  GLU A 171      59.478 -26.483 -39.234  1.00 66.10           C  
ANISOU 1382  CD  GLU A 171     8886   8444   7787  -1073  -1265   1531       C  
ATOM   1383  OE1 GLU A 171      58.659 -27.375 -39.554  1.00 66.06           O  
ANISOU 1383  OE1 GLU A 171     8915   8517   7669  -1194  -1370   1536       O  
ATOM   1384  OE2 GLU A 171      60.600 -26.372 -39.773  1.00 67.63           O  
ANISOU 1384  OE2 GLU A 171     9212   8595   7890  -1086  -1156   1478       O  
ATOM   1385  N   ALA A 172      55.493 -25.738 -35.409  1.00 39.99           N  
ANISOU 1385  N   ALA A 172     4832   5160   5202   -750  -1466   1723       N  
ATOM   1386  CA  ALA A 172      54.156 -25.941 -34.864  1.00 50.21           C  
ANISOU 1386  CA  ALA A 172     5962   6507   6609   -740  -1557   1800       C  
ATOM   1387  C   ALA A 172      53.925 -25.135 -33.597  1.00 47.62           C  
ANISOU 1387  C   ALA A 172     5468   6098   6528   -566  -1467   1800       C  
ATOM   1388  O   ALA A 172      52.790 -25.055 -33.124  1.00 49.62           O  
ANISOU 1388  O   ALA A 172     5560   6382   6911   -532  -1525   1888       O  
ATOM   1389  CB  ALA A 172      53.920 -27.432 -34.570  1.00 48.07           C  
ANISOU 1389  CB  ALA A 172     5751   6282   6233   -838  -1568   1676       C  
ATOM   1390  N   VAL A 173      54.980 -24.548 -33.039  1.00 41.35           N  
ANISOU 1390  N   VAL A 173     4712   5200   5798   -463  -1321   1702       N  
ATOM   1391  CA  VAL A 173      54.909 -23.761 -31.816  1.00 44.80           C  
ANISOU 1391  CA  VAL A 173     5025   5549   6449   -310  -1216   1676       C  
ATOM   1392  C   VAL A 173      55.842 -22.569 -32.001  1.00 50.44           C  
ANISOU 1392  C   VAL A 173     5778   6171   7216   -236  -1135   1689       C  
ATOM   1393  O   VAL A 173      56.806 -22.634 -32.768  1.00 44.23           O  
ANISOU 1393  O   VAL A 173     5130   5382   6293   -296  -1119   1656       O  
ATOM   1394  CB  VAL A 173      55.289 -24.608 -30.573  1.00 47.07           C  
ANISOU 1394  CB  VAL A 173     5331   5805   6748   -278  -1107   1489       C  
ATOM   1395  CG1 VAL A 173      56.780 -24.995 -30.588  1.00 39.73           C  
ANISOU 1395  CG1 VAL A 173     4562   4832   5703   -298  -1005   1335       C  
ATOM   1396  CG2 VAL A 173      54.903 -23.892 -29.284  1.00 59.65           C  
ANISOU 1396  CG2 VAL A 173     6788   7326   8552   -141  -1017   1475       C  
ATOM   1397  N   LYS A 174      55.522 -21.456 -31.340  1.00 41.23           N  
ANISOU 1397  N   LYS A 174     4490   4925   6252   -111  -1079   1745       N  
ATOM   1398  CA  LYS A 174      56.321 -20.236 -31.444  1.00 42.62           C  
ANISOU 1398  CA  LYS A 174     4692   4999   6502    -40   -998   1763       C  
ATOM   1399  C   LYS A 174      57.471 -20.302 -30.448  1.00 44.52           C  
ANISOU 1399  C   LYS A 174     5002   5159   6755      6   -848   1569       C  
ATOM   1400  O   LYS A 174      57.258 -20.587 -29.263  1.00 43.15           O  
ANISOU 1400  O   LYS A 174     4774   4960   6661     60   -781   1470       O  
ATOM   1401  CB  LYS A 174      55.450 -19.007 -31.184  1.00 50.67           C  
ANISOU 1401  CB  LYS A 174     5558   5955   7740     72   -994   1910       C  
ATOM   1402  CG  LYS A 174      56.019 -17.701 -31.700  1.00 65.59           C  
ANISOU 1402  CG  LYS A 174     7470   7753   9696    121   -956   1994       C  
ATOM   1403  CD  LYS A 174      54.896 -16.711 -31.955  1.00 73.54           C  
ANISOU 1403  CD  LYS A 174     8325   8735  10883    197  -1011   2207       C  
ATOM   1404  CE  LYS A 174      55.416 -15.287 -32.054  1.00 83.88           C  
ANISOU 1404  CE  LYS A 174     9638   9910  12321    282   -926   2267       C  
ATOM   1405  NZ  LYS A 174      56.510 -15.147 -33.055  1.00 89.92           N  
ANISOU 1405  NZ  LYS A 174    10550  10684  12931    203   -942   2268       N  
ATOM   1406  N   THR A 175      58.696 -20.080 -30.935  1.00 41.90           N  
ANISOU 1406  N   THR A 175     4788   4793   6338    -22   -798   1519       N  
ATOM   1407  CA  THR A 175      59.881 -20.084 -30.078  1.00 36.72           C  
ANISOU 1407  CA  THR A 175     4191   4066   5694     11   -668   1354       C  
ATOM   1408  C   THR A 175      60.570 -18.727 -30.057  1.00 42.61           C  
ANISOU 1408  C   THR A 175     4941   4703   6545     73   -590   1378       C  
ATOM   1409  O   THR A 175      61.561 -18.553 -29.331  1.00 43.15           O  
ANISOU 1409  O   THR A 175     5047   4708   6639     97   -488   1254       O  
ATOM   1410  CB  THR A 175      60.885 -21.171 -30.519  1.00 36.58           C  
ANISOU 1410  CB  THR A 175     4310   4098   5492    -78   -654   1250       C  
ATOM   1411  OG1 THR A 175      61.179 -21.032 -31.918  1.00 39.56           O  
ANISOU 1411  OG1 THR A 175     4772   4508   5750   -152   -707   1341       O  
ATOM   1412  CG2 THR A 175      60.321 -22.578 -30.257  1.00 39.30           C  
ANISOU 1412  CG2 THR A 175     4658   4525   5749   -133   -700   1188       C  
ATOM   1413  N   GLN A 176      60.051 -17.765 -30.810  1.00 44.88           N  
ANISOU 1413  N   GLN A 176     5184   4967   6899     95   -641   1541       N  
ATOM   1414  CA  GLN A 176      60.614 -16.430 -30.958  1.00 50.99           C  
ANISOU 1414  CA  GLN A 176     5965   5632   7776    146   -575   1591       C  
ATOM   1415  C   GLN A 176      59.894 -15.495 -29.992  1.00 51.14           C  
ANISOU 1415  C   GLN A 176     5868   5552   8012    259   -515   1613       C  
ATOM   1416  O   GLN A 176      58.700 -15.232 -30.158  1.00 49.67           O  
ANISOU 1416  O   GLN A 176     5576   5380   7917    300   -577   1749       O  
ATOM   1417  CB  GLN A 176      60.421 -15.969 -32.399  1.00 55.97           C  
ANISOU 1417  CB  GLN A 176     6621   6297   8349    102   -668   1772       C  
ATOM   1418  CG  GLN A 176      60.651 -14.515 -32.614  1.00 66.91           C  
ANISOU 1418  CG  GLN A 176     7986   7568   9870    164   -619   1870       C  
ATOM   1419  CD  GLN A 176      62.098 -14.241 -32.817  1.00 50.93           C  
ANISOU 1419  CD  GLN A 176     6075   5493   7784    130   -532   1786       C  
ATOM   1420  OE1 GLN A 176      62.630 -14.454 -33.906  1.00 62.65           O  
ANISOU 1420  OE1 GLN A 176     7651   7031   9123     50   -570   1835       O  
ATOM   1421  NE2 GLN A 176      62.763 -13.789 -31.769  1.00 62.00           N  
ANISOU 1421  NE2 GLN A 176     7474   6795   9290    180   -414   1658       N  
ATOM   1422  N   PHE A 177      60.604 -14.996 -28.984  1.00 40.24           N  
ANISOU 1422  N   PHE A 177     4505   4070   6714    305   -391   1484       N  
ATOM   1423  CA  PHE A 177      59.988 -14.151 -27.970  1.00 39.31           C  
ANISOU 1423  CA  PHE A 177     4300   3845   6792    405   -308   1475       C  
ATOM   1424  C   PHE A 177      60.489 -12.720 -28.076  1.00 44.54           C  
ANISOU 1424  C   PHE A 177     4979   4365   7578    451   -227   1517       C  
ATOM   1425  O   PHE A 177      61.617 -12.475 -28.508  1.00 40.67           O  
ANISOU 1425  O   PHE A 177     4580   3853   7020    402   -205   1485       O  
ATOM   1426  CB  PHE A 177      60.289 -14.665 -26.561  1.00 42.34           C  
ANISOU 1426  CB  PHE A 177     4696   4215   7176    414   -221   1283       C  
ATOM   1427  CG  PHE A 177      59.972 -16.114 -26.367  1.00 43.70           C  
ANISOU 1427  CG  PHE A 177     4866   4515   7224    364   -284   1224       C  
ATOM   1428  CD1 PHE A 177      58.725 -16.618 -26.709  1.00 49.04           C  
ANISOU 1428  CD1 PHE A 177     5458   5270   7907    368   -374   1331       C  
ATOM   1429  CD2 PHE A 177      60.927 -16.977 -25.855  1.00 39.20           C  
ANISOU 1429  CD2 PHE A 177     4374   3984   6536    309   -255   1070       C  
ATOM   1430  CE1 PHE A 177      58.433 -17.971 -26.532  1.00 42.29           C  
ANISOU 1430  CE1 PHE A 177     4606   4525   6937    313   -430   1273       C  
ATOM   1431  CE2 PHE A 177      60.652 -18.331 -25.676  1.00 43.18           C  
ANISOU 1431  CE2 PHE A 177     4881   4594   6931    264   -305   1017       C  
ATOM   1432  CZ  PHE A 177      59.404 -18.823 -26.014  1.00 40.71           C  
ANISOU 1432  CZ  PHE A 177     4494   4352   6621    264   -390   1114       C  
ATOM   1433  N   ASN A 178      59.630 -11.784 -27.674  1.00 39.93           N  
ANISOU 1433  N   ASN A 178     4306   3680   7186    548   -176   1592       N  
ATOM   1434  CA  ASN A 178      60.064 -10.455 -27.281  1.00 47.22           C  
ANISOU 1434  CA  ASN A 178     5249   4434   8258    603    -55   1574       C  
ATOM   1435  C   ASN A 178      60.547 -10.496 -25.838  1.00 45.70           C  
ANISOU 1435  C   ASN A 178     5096   4178   8090    608     67   1364       C  
ATOM   1436  O   ASN A 178      59.977 -11.202 -25.000  1.00 43.73           O  
ANISOU 1436  O   ASN A 178     4806   3978   7833    624     78   1285       O  
ATOM   1437  CB  ASN A 178      58.917  -9.440 -27.402  1.00 45.17           C  
ANISOU 1437  CB  ASN A 178     4878   4076   8208    712    -31   1741       C  
ATOM   1438  CG  ASN A 178      58.542  -9.129 -28.839  1.00 51.11           C  
ANISOU 1438  CG  ASN A 178     5595   4871   8954    705   -149   1971       C  
ATOM   1439  OD1 ASN A 178      59.378  -9.136 -29.737  1.00 53.38           O  
ANISOU 1439  OD1 ASN A 178     5969   5195   9119    631   -200   2001       O  
ATOM   1440  ND2 ASN A 178      57.271  -8.823 -29.057  1.00 51.41           N  
ANISOU 1440  ND2 ASN A 178     5501   4904   9129    783   -189   2144       N  
ATOM   1441  N   TYR A 179      61.594  -9.727 -25.543  1.00 42.81           N  
ANISOU 1441  N   TYR A 179     4810   3704   7750    587    155   1277       N  
ATOM   1442  CA  TYR A 179      62.159  -9.646 -24.201  1.00 39.85           C  
ANISOU 1442  CA  TYR A 179     4486   3266   7388    573    264   1082       C  
ATOM   1443  C   TYR A 179      62.033  -8.239 -23.641  1.00 42.83           C  
ANISOU 1443  C   TYR A 179     4870   3451   7952    635    398   1069       C  
ATOM   1444  O   TYR A 179      62.194  -7.251 -24.371  1.00 44.95           O  
ANISOU 1444  O   TYR A 179     5147   3623   8309    656    414   1179       O  
ATOM   1445  CB  TYR A 179      63.638 -10.040 -24.191  1.00 41.90           C  
ANISOU 1445  CB  TYR A 179     4844   3571   7507    471    254    966       C  
ATOM   1446  CG  TYR A 179      63.876 -11.524 -24.201  1.00 35.57           C  
ANISOU 1446  CG  TYR A 179     4051   2934   6532    412    172    907       C  
ATOM   1447  CD1 TYR A 179      63.816 -12.248 -25.382  1.00 41.73           C  
ANISOU 1447  CD1 TYR A 179     4828   3826   7200    380     65   1010       C  
ATOM   1448  CD2 TYR A 179      64.179 -12.206 -23.025  1.00 35.03           C  
ANISOU 1448  CD2 TYR A 179     4002   2902   6406    383    204    747       C  
ATOM   1449  CE1 TYR A 179      64.045 -13.627 -25.388  1.00 39.11           C  
ANISOU 1449  CE1 TYR A 179     4515   3628   6715    325      4    949       C  
ATOM   1450  CE2 TYR A 179      64.417 -13.568 -23.028  1.00 36.50           C  
ANISOU 1450  CE2 TYR A 179     4198   3226   6446    334    136    700       C  
ATOM   1451  CZ  TYR A 179      64.338 -14.268 -24.211  1.00 40.09           C  
ANISOU 1451  CZ  TYR A 179     4651   3778   6804    308     42    799       C  
ATOM   1452  OH  TYR A 179      64.563 -15.624 -24.206  1.00 43.23           O  
ANISOU 1452  OH  TYR A 179     5065   4295   7064    260    -11    746       O  
ATOM   1453  N   TYR A 180      61.768  -8.161 -22.333  1.00 45.26           N  
ANISOU 1453  N   TYR A 180     5184   3698   8314    658    501    931       N  
ATOM   1454  CA  TYR A 180      61.687  -6.906 -21.596  1.00 47.26           C  
ANISOU 1454  CA  TYR A 180     5468   3758   8731    705    653    876       C  
ATOM   1455  C   TYR A 180      62.350  -7.125 -20.249  1.00 47.21           C  
ANISOU 1455  C   TYR A 180     5547   3739   8653    637    730    655       C  
ATOM   1456  O   TYR A 180      62.327  -8.231 -19.716  1.00 44.31           O  
ANISOU 1456  O   TYR A 180     5174   3501   8162    601    683    572       O  
ATOM   1457  CB  TYR A 180      60.236  -6.432 -21.376  1.00 46.10           C  
ANISOU 1457  CB  TYR A 180     5220   3526   8768    833    726    971       C  
ATOM   1458  CG  TYR A 180      59.371  -6.526 -22.606  1.00 51.26           C  
ANISOU 1458  CG  TYR A 180     5761   4243   9473    895    616   1204       C  
ATOM   1459  CD1 TYR A 180      58.861  -7.760 -23.026  1.00 52.90           C  
ANISOU 1459  CD1 TYR A 180     5901   4635   9562    875    480   1263       C  
ATOM   1460  CD2 TYR A 180      59.054  -5.393 -23.346  1.00 46.52           C  
ANISOU 1460  CD2 TYR A 180     5124   3516   9037    966    645   1369       C  
ATOM   1461  CE1 TYR A 180      58.072  -7.857 -24.158  1.00 52.78           C  
ANISOU 1461  CE1 TYR A 180     5788   4688   9578    911    366   1478       C  
ATOM   1462  CE2 TYR A 180      58.253  -5.480 -24.480  1.00 55.22           C  
ANISOU 1462  CE2 TYR A 180     6117   4686  10176   1014    529   1598       C  
ATOM   1463  CZ  TYR A 180      57.767  -6.719 -24.877  1.00 55.64           C  
ANISOU 1463  CZ  TYR A 180     6108   4934  10097    980    385   1649       C  
ATOM   1464  OH  TYR A 180      56.986  -6.835 -25.999  1.00 52.36           O  
ANISOU 1464  OH  TYR A 180     5592   4599   9701   1006    256   1874       O  
ATOM   1465  N   LYS A 181      62.936  -6.067 -19.699  1.00 41.01           N  
ANISOU 1465  N   LYS A 181     4844   2796   7942    612    845    563       N  
ATOM   1466  CA  LYS A 181      63.639  -6.167 -18.426  1.00 47.20           C  
ANISOU 1466  CA  LYS A 181     5722   3565   8647    526    911    355       C  
ATOM   1467  C   LYS A 181      63.434  -4.893 -17.621  1.00 43.15           C  
ANISOU 1467  C   LYS A 181     5273   2840   8284    552   1084    273       C  
ATOM   1468  O   LYS A 181      63.472  -3.790 -18.171  1.00 52.26           O  
ANISOU 1468  O   LYS A 181     6439   3846   9572    587   1142    351       O  
ATOM   1469  CB  LYS A 181      65.140  -6.407 -18.622  1.00 50.41           C  
ANISOU 1469  CB  LYS A 181     6199   4038   8918    400    839    291       C  
ATOM   1470  CG  LYS A 181      65.896  -6.592 -17.319  1.00 44.15           C  
ANISOU 1470  CG  LYS A 181     5491   3254   8032    298    880     93       C  
ATOM   1471  CD  LYS A 181      67.383  -6.854 -17.545  1.00 50.01           C  
ANISOU 1471  CD  LYS A 181     6277   4068   8655    176    801     52       C  
ATOM   1472  CE  LYS A 181      68.037  -7.298 -16.245  1.00 56.23           C  
ANISOU 1472  CE  LYS A 181     7126   4909   9329     72    808   -122       C  
ATOM   1473  NZ  LYS A 181      69.509  -7.392 -16.339  1.00 65.82           N  
ANISOU 1473  NZ  LYS A 181     8375   6177  10458    -50    744   -160       N  
ATOM   1474  N   LYS A 182      63.225  -5.059 -16.318  1.00 50.90           N  
ANISOU 1474  N   LYS A 182     6303   3803   9234    530   1173    113       N  
ATOM   1475  CA  LYS A 182      63.099  -3.965 -15.367  1.00 50.66           C  
ANISOU 1475  CA  LYS A 182     6362   3574   9311    531   1354     -6       C  
ATOM   1476  C   LYS A 182      64.155  -4.117 -14.284  1.00 48.48           C  
ANISOU 1476  C   LYS A 182     6213   3323   8886    381   1366   -212       C  
ATOM   1477  O   LYS A 182      64.397  -5.224 -13.795  1.00 51.07           O  
ANISOU 1477  O   LYS A 182     6535   3816   9053    322   1282   -278       O  
ATOM   1478  CB  LYS A 182      61.713  -3.939 -14.712  1.00 56.75           C  
ANISOU 1478  CB  LYS A 182     7083   4286  10192    646   1477     -9       C  
ATOM   1479  CG  LYS A 182      60.618  -3.360 -15.575  1.00 67.20           C  
ANISOU 1479  CG  LYS A 182     8290   5535  11707    794   1509    187       C  
ATOM   1480  CD  LYS A 182      59.267  -3.501 -14.890  1.00 68.20           C  
ANISOU 1480  CD  LYS A 182     8346   5672  11897    889   1608    188       C  
ATOM   1481  CE  LYS A 182      59.109  -2.492 -13.773  1.00 61.49           C  
ANISOU 1481  CE  LYS A 182     7598   4687  11079    873   1801     41       C  
ATOM   1482  NZ  LYS A 182      57.773  -2.623 -13.120  1.00 67.17           N  
ANISOU 1482  NZ  LYS A 182     8242   5413  11866    965   1911     50       N  
ATOM   1483  N   VAL A 183      64.784  -3.005 -13.910  1.00 48.28           N  
ANISOU 1483  N   VAL A 183     6299   3131   8914    313   1466   -306       N  
ATOM   1484  CA  VAL A 183      65.736  -2.981 -12.807  1.00 53.01           C  
ANISOU 1484  CA  VAL A 183     7026   3735   9382    157   1486   -503       C  
ATOM   1485  C   VAL A 183      65.328  -1.847 -11.884  1.00 52.42           C  
ANISOU 1485  C   VAL A 183     7065   3438   9413    157   1692   -630       C  
ATOM   1486  O   VAL A 183      65.238  -0.693 -12.321  1.00 54.37           O  
ANISOU 1486  O   VAL A 183     7324   3569   9764    194   1758   -571       O  
ATOM   1487  CB  VAL A 183      67.188  -2.802 -13.288  1.00 61.57           C  
ANISOU 1487  CB  VAL A 183     8148   4852  10393     28   1385   -505       C  
ATOM   1488  CG1 VAL A 183      68.143  -2.745 -12.101  1.00 60.21           C  
ANISOU 1488  CG1 VAL A 183     8100   4688  10090   -145   1396   -699       C  
ATOM   1489  CG2 VAL A 183      67.584  -3.934 -14.229  1.00 58.02           C  
ANISOU 1489  CG2 VAL A 183     7593   4610   9843     34   1204   -382       C  
ATOM   1490  N   ASP A 184      65.055  -2.176 -10.622  1.00 57.26           N  
ANISOU 1490  N   ASP A 184     7750   4071   9936    111   1765   -785       N  
ATOM   1491  CA  ASP A 184      64.629  -1.201  -9.612  1.00 58.38           C  
ANISOU 1491  CA  ASP A 184     7997   4098  10086     96   1936   -907       C  
ATOM   1492  C   ASP A 184      63.456  -0.356 -10.105  1.00 62.82           C  
ANISOU 1492  C   ASP A 184     8482   4562  10826    261   2048   -778       C  
ATOM   1493  O   ASP A 184      63.447   0.873  -9.988  1.00 62.78           O  
ANISOU 1493  O   ASP A 184     8542   4424  10888    257   2159   -801       O  
ATOM   1494  CB  ASP A 184      65.793  -0.309  -9.181  1.00 65.66           C  
ANISOU 1494  CB  ASP A 184     9064   4946  10938    -69   1951  -1032       C  
ATOM   1495  CG  ASP A 184      66.921  -1.097  -8.554  1.00 76.76           C  
ANISOU 1495  CG  ASP A 184    10543   6459  12164   -249   1842  -1162       C  
ATOM   1496  OD1 ASP A 184      66.647  -2.131  -7.909  1.00 81.34           O  
ANISOU 1496  OD1 ASP A 184    11116   7141  12647   -261   1818  -1224       O  
ATOM   1497  OD2 ASP A 184      68.088  -0.684  -8.711  1.00 86.64           O  
ANISOU 1497  OD2 ASP A 184    11849   7696  13372   -381   1776  -1194       O  
ATOM   1498  N   GLY A 185      62.453  -1.031 -10.664  1.00 57.00           N  
ANISOU 1498  N   GLY A 185     7598   3893  10165    403   2015   -635       N  
ATOM   1499  CA  GLY A 185      61.243  -0.376 -11.118  1.00 60.46           C  
ANISOU 1499  CA  GLY A 185     7936   4264  10771    558   2105   -494       C  
ATOM   1500  C   GLY A 185      61.356   0.356 -12.435  1.00 64.00           C  
ANISOU 1500  C   GLY A 185     8314   4661  11340    617   2051   -317       C  
ATOM   1501  O   GLY A 185      60.368   0.956 -12.873  1.00 64.76           O  
ANISOU 1501  O   GLY A 185     8320   4702  11582    741   2117   -185       O  
ATOM   1502  N   VAL A 186      62.514   0.316 -13.090  1.00 63.02           N  
ANISOU 1502  N   VAL A 186     8224   4558  11163    531   1932   -301       N  
ATOM   1503  CA  VAL A 186      62.762   1.079 -14.306  1.00 61.69           C  
ANISOU 1503  CA  VAL A 186     8011   4337  11091    567   1886   -144       C  
ATOM   1504  C   VAL A 186      62.919   0.112 -15.470  1.00 57.72           C  
ANISOU 1504  C   VAL A 186     7399   3966  10567    597   1707     15       C  
ATOM   1505  O   VAL A 186      63.745  -0.811 -15.415  1.00 56.28           O  
ANISOU 1505  O   VAL A 186     7242   3874  10266    507   1604    -46       O  
ATOM   1506  CB  VAL A 186      64.005   1.978 -14.165  1.00 67.76           C  
ANISOU 1506  CB  VAL A 186     8915   5008  11822    434   1909   -246       C  
ATOM   1507  CG1 VAL A 186      64.376   2.580 -15.507  1.00 66.13           C  
ANISOU 1507  CG1 VAL A 186     8660   4770  11696    461   1840    -76       C  
ATOM   1508  CG2 VAL A 186      63.750   3.075 -13.142  1.00 66.00           C  
ANISOU 1508  CG2 VAL A 186     8802   4642  11634    412   2091   -382       C  
ATOM   1509  N   VAL A 187      62.136   0.328 -16.527  1.00 49.50           N  
ANISOU 1509  N   VAL A 187     6236   2936   9636    715   1670    221       N  
ATOM   1510  CA  VAL A 187      62.258  -0.495 -17.722  1.00 56.19           C  
ANISOU 1510  CA  VAL A 187     6989   3907  10455    737   1500    384       C  
ATOM   1511  C   VAL A 187      63.605  -0.224 -18.378  1.00 56.48           C  
ANISOU 1511  C   VAL A 187     7095   3927  10439    634   1428    390       C  
ATOM   1512  O   VAL A 187      64.010   0.932 -18.549  1.00 56.16           O  
ANISOU 1512  O   VAL A 187     7112   3770  10455    610   1493    390       O  
ATOM   1513  CB  VAL A 187      61.095  -0.224 -18.689  1.00 64.76           C  
ANISOU 1513  CB  VAL A 187     7933   5011  11660    872   1472    608       C  
ATOM   1514  CG1 VAL A 187      61.274  -1.040 -19.960  1.00 60.58           C  
ANISOU 1514  CG1 VAL A 187     7326   4614  11079    875   1290    777       C  
ATOM   1515  CG2 VAL A 187      59.748  -0.543 -18.020  1.00 59.63           C  
ANISOU 1515  CG2 VAL A 187     7199   4387  11070    967   1544    610       C  
ATOM   1516  N   GLN A 188      64.317  -1.289 -18.720  1.00 53.14           N  
ANISOU 1516  N   GLN A 188     6666   3614   9909    570   1301    392       N  
ATOM   1517  CA  GLN A 188      65.626  -1.176 -19.344  1.00 56.77           C  
ANISOU 1517  CA  GLN A 188     7179   4095  10298    462   1226    399       C  
ATOM   1518  C   GLN A 188      65.507  -1.185 -20.861  1.00 56.07           C  
ANISOU 1518  C   GLN A 188     7011   4058  10235    516   1123    621       C  
ATOM   1519  O   GLN A 188      64.627  -1.836 -21.430  1.00 59.29           O  
ANISOU 1519  O   GLN A 188     7320   4573  10636    598   1045    750       O  
ATOM   1520  CB  GLN A 188      66.532  -2.333 -18.914  1.00 57.65           C  
ANISOU 1520  CB  GLN A 188     7314   4396  10193    343   1120    277       C  
ATOM   1521  CG  GLN A 188      66.698  -2.467 -17.422  1.00 63.28           C  
ANISOU 1521  CG  GLN A 188     8106   5094  10846    272   1194     67       C  
ATOM   1522  CD  GLN A 188      67.323  -1.238 -16.810  1.00 68.56           C  
ANISOU 1522  CD  GLN A 188     8894   5569  11588    193   1317    -51       C  
ATOM   1523  OE1 GLN A 188      66.625  -0.343 -16.329  1.00 71.47           O  
ANISOU 1523  OE1 GLN A 188     9299   5777  12078    251   1459    -85       O  
ATOM   1524  NE2 GLN A 188      68.649  -1.183 -16.829  1.00 70.20           N  
ANISOU 1524  NE2 GLN A 188     9157   5811  11705     54   1261   -111       N  
ATOM   1525  N   GLN A 189      66.406  -0.453 -21.515  1.00 51.33           N  
ANISOU 1525  N   GLN A 189     6460   3384   9659    458   1122    667       N  
ATOM   1526  CA  GLN A 189      66.657  -0.632 -22.940  1.00 50.31           C  
ANISOU 1526  CA  GLN A 189     6284   3342   9490    462   1008    850       C  
ATOM   1527  C   GLN A 189      67.713  -1.723 -23.081  1.00 49.37           C  
ANISOU 1527  C   GLN A 189     6181   3415   9162    349    894    781       C  
ATOM   1528  O   GLN A 189      68.881  -1.505 -22.747  1.00 51.24           O  
ANISOU 1528  O   GLN A 189     6488   3631   9350    238    913    673       O  
ATOM   1529  CB  GLN A 189      67.134   0.660 -23.596  1.00 54.52           C  
ANISOU 1529  CB  GLN A 189     6859   3752  10106    446   1056    928       C  
ATOM   1530  CG  GLN A 189      66.115   1.784 -23.601  1.00 72.45           C  
ANISOU 1530  CG  GLN A 189     9099   5919  12511    551   1145    997       C  
ATOM   1531  CD  GLN A 189      66.443   2.845 -24.636  1.00 92.38           C  
ANISOU 1531  CD  GLN A 189    11635   8374  15092    552   1148   1135       C  
ATOM   1532  OE1 GLN A 189      67.085   2.561 -25.651  1.00 94.89           O  
ANISOU 1532  OE1 GLN A 189    11952   8760  15343    506   1056   1241       O  
ATOM   1533  NE2 GLN A 189      66.007   4.076 -24.384  1.00 99.60           N  
ANISOU 1533  NE2 GLN A 189    12564   9151  16129    601   1262   1135       N  
ATOM   1534  N   LEU A 190      67.310  -2.883 -23.569  1.00 42.38           N  
ANISOU 1534  N   LEU A 190     5230   2712   8161    374    780    846       N  
ATOM   1535  CA  LEU A 190      68.263  -3.981 -23.715  1.00 40.73           C  
ANISOU 1535  CA  LEU A 190     5033   2677   7764    280    686    786       C  
ATOM   1536  C   LEU A 190      69.222  -3.683 -24.869  1.00 46.06           C  
ANISOU 1536  C   LEU A 190     5734   3362   8404    222    648    885       C  
ATOM   1537  O   LEU A 190      68.825  -3.070 -25.863  1.00 43.66           O  
ANISOU 1537  O   LEU A 190     5412   3001   8174    274    641   1050       O  
ATOM   1538  CB  LEU A 190      67.525  -5.301 -23.955  1.00 43.74           C  
ANISOU 1538  CB  LEU A 190     5348   3234   8036    320    585    828       C  
ATOM   1539  CG  LEU A 190      66.763  -5.863 -22.748  1.00 52.85           C  
ANISOU 1539  CG  LEU A 190     6478   4416   9187    355    614    711       C  
ATOM   1540  CD1 LEU A 190      65.813  -6.965 -23.178  1.00 52.93           C  
ANISOU 1540  CD1 LEU A 190     6411   4573   9128    408    518    795       C  
ATOM   1541  CD2 LEU A 190      67.742  -6.388 -21.683  1.00 47.02           C  
ANISOU 1541  CD2 LEU A 190     5795   3730   8341    255    624    523       C  
ATOM   1542  N   PRO A 191      70.486  -4.094 -24.766  1.00 45.60           N  
ANISOU 1542  N   PRO A 191     5712   3374   8240    116    626    799       N  
ATOM   1543  CA  PRO A 191      71.475  -3.717 -25.787  1.00 49.67           C  
ANISOU 1543  CA  PRO A 191     6254   3884   8736     57    614    884       C  
ATOM   1544  C   PRO A 191      71.286  -4.488 -27.086  1.00 49.92           C  
ANISOU 1544  C   PRO A 191     6257   4052   8660     79    523   1028       C  
ATOM   1545  O   PRO A 191      70.751  -5.600 -27.112  1.00 49.11           O  
ANISOU 1545  O   PRO A 191     6119   4083   8456    106    454   1024       O  
ATOM   1546  CB  PRO A 191      72.813  -4.086 -25.134  1.00 49.50           C  
ANISOU 1546  CB  PRO A 191     6260   3914   8634    -60    617    742       C  
ATOM   1547  CG  PRO A 191      72.455  -5.269 -24.242  1.00 49.64           C  
ANISOU 1547  CG  PRO A 191     6249   4056   8554    -50    574    632       C  
ATOM   1548  CD  PRO A 191      71.067  -4.943 -23.710  1.00 44.66           C  
ANISOU 1548  CD  PRO A 191     5604   3348   8017     47    611    631       C  
ATOM   1549  N   GLU A 192      71.752  -3.877 -28.178  1.00 47.27           N  
ANISOU 1549  N   GLU A 192     5944   3676   8339     58    527   1154       N  
ATOM   1550  CA  GLU A 192      71.950  -4.614 -29.421  1.00 44.94           C  
ANISOU 1550  CA  GLU A 192     5650   3515   7909     40    454   1265       C  
ATOM   1551  C   GLU A 192      72.808  -5.834 -29.146  1.00 46.99           C  
ANISOU 1551  C   GLU A 192     5913   3918   8023    -27    426   1150       C  
ATOM   1552  O   GLU A 192      73.797  -5.745 -28.417  1.00 41.78           O  
ANISOU 1552  O   GLU A 192     5264   3235   7375    -93    470   1032       O  
ATOM   1553  CB  GLU A 192      72.653  -3.744 -30.466  1.00 46.19           C  
ANISOU 1553  CB  GLU A 192     5849   3606   8096      0    485   1386       C  
ATOM   1554  CG  GLU A 192      71.792  -2.720 -31.127  1.00 57.52           C  
ANISOU 1554  CG  GLU A 192     7278   4930   9647     70    490   1555       C  
ATOM   1555  CD  GLU A 192      72.455  -2.139 -32.355  1.00 56.94           C  
ANISOU 1555  CD  GLU A 192     7247   4833   9555     24    500   1696       C  
ATOM   1556  OE1 GLU A 192      73.566  -2.602 -32.731  1.00 49.58           O  
ANISOU 1556  OE1 GLU A 192     6347   3979   8512    -60    507   1659       O  
ATOM   1557  OE2 GLU A 192      71.864  -1.218 -32.944  1.00 55.72           O  
ANISOU 1557  OE2 GLU A 192     7090   4580   9502     75    507   1851       O  
ATOM   1558  N   THR A 193      72.439  -6.973 -29.735  1.00 37.36           N  
ANISOU 1558  N   THR A 193     4684   2842   6670    -15    353   1189       N  
ATOM   1559  CA  THR A 193      73.148  -8.204 -29.418  1.00 39.15           C  
ANISOU 1559  CA  THR A 193     4910   3194   6772    -64    336   1081       C  
ATOM   1560  C   THR A 193      73.098  -9.160 -30.607  1.00 43.23           C  
ANISOU 1560  C   THR A 193     5451   3837   7138    -76    282   1165       C  
ATOM   1561  O   THR A 193      72.127  -9.171 -31.374  1.00 38.84           O  
ANISOU 1561  O   THR A 193     4898   3305   6554    -38    227   1281       O  
ATOM   1562  CB  THR A 193      72.555  -8.851 -28.147  1.00 38.97           C  
ANISOU 1562  CB  THR A 193     4850   3204   6752    -32    318    956       C  
ATOM   1563  OG1 THR A 193      73.321 -10.010 -27.776  1.00 37.60           O  
ANISOU 1563  OG1 THR A 193     4672   3142   6472    -79    304    858       O  
ATOM   1564  CG2 THR A 193      71.059  -9.252 -28.341  1.00 38.76           C  
ANISOU 1564  CG2 THR A 193     4792   3220   6715     45    255   1024       C  
ATOM   1565  N   TYR A 194      74.189  -9.912 -30.793  1.00 39.33           N  
ANISOU 1565  N   TYR A 194     4976   3418   6551   -135    305   1112       N  
ATOM   1566  CA  TYR A 194      74.145 -11.135 -31.575  1.00 36.58           C  
ANISOU 1566  CA  TYR A 194     4657   3196   6046   -149    269   1134       C  
ATOM   1567  C   TYR A 194      73.561 -12.251 -30.718  1.00 36.18           C  
ANISOU 1567  C   TYR A 194     4574   3222   5951   -121    224   1035       C  
ATOM   1568  O   TYR A 194      73.442 -12.126 -29.500  1.00 37.28           O  
ANISOU 1568  O   TYR A 194     4669   3326   6167   -102    231    941       O  
ATOM   1569  CB  TYR A 194      75.543 -11.530 -32.080  1.00 36.65           C  
ANISOU 1569  CB  TYR A 194     4696   3244   5988   -212    332   1116       C  
ATOM   1570  CG  TYR A 194      76.165 -10.552 -33.049  1.00 37.09           C  
ANISOU 1570  CG  TYR A 194     4789   3236   6067   -248    382   1222       C  
ATOM   1571  CD1 TYR A 194      75.862 -10.592 -34.401  1.00 35.15           C  
ANISOU 1571  CD1 TYR A 194     4608   3027   5721   -261    366   1346       C  
ATOM   1572  CD2 TYR A 194      77.080  -9.599 -32.611  1.00 35.66           C  
ANISOU 1572  CD2 TYR A 194     4584   2962   6002   -281    445   1199       C  
ATOM   1573  CE1 TYR A 194      76.427  -9.700 -35.289  1.00 39.60           C  
ANISOU 1573  CE1 TYR A 194     5210   3535   6301   -297    415   1450       C  
ATOM   1574  CE2 TYR A 194      77.659  -8.696 -33.493  1.00 40.39           C  
ANISOU 1574  CE2 TYR A 194     5217   3501   6630   -318    496   1299       C  
ATOM   1575  CZ  TYR A 194      77.330  -8.745 -34.830  1.00 37.00           C  
ANISOU 1575  CZ  TYR A 194     4850   3107   6100   -322    484   1427       C  
ATOM   1576  OH  TYR A 194      77.909  -7.849 -35.700  1.00 39.27           O  
ANISOU 1576  OH  TYR A 194     5175   3334   6410   -360    538   1534       O  
ATOM   1577  N   PHE A 195      73.185 -13.354 -31.362  1.00 36.07           N  
ANISOU 1577  N   PHE A 195     4590   3310   5804   -127    181   1056       N  
ATOM   1578  CA  PHE A 195      72.736 -14.548 -30.659  1.00 37.17           C  
ANISOU 1578  CA  PHE A 195     4707   3527   5889   -111    145    966       C  
ATOM   1579  C   PHE A 195      73.511 -15.761 -31.141  1.00 34.25           C  
ANISOU 1579  C   PHE A 195     4380   3241   5391   -153    172    928       C  
ATOM   1580  O   PHE A 195      73.757 -15.907 -32.340  1.00 40.17           O  
ANISOU 1580  O   PHE A 195     5196   4019   6048   -188    185    999       O  
ATOM   1581  CB  PHE A 195      71.237 -14.808 -30.860  1.00 39.71           C  
ANISOU 1581  CB  PHE A 195     5017   3886   6185    -74     59   1025       C  
ATOM   1582  CG  PHE A 195      70.370 -13.762 -30.242  1.00 40.31           C  
ANISOU 1582  CG  PHE A 195     5036   3876   6403    -16     46   1056       C  
ATOM   1583  CD1 PHE A 195      70.299 -13.636 -28.864  1.00 41.52           C  
ANISOU 1583  CD1 PHE A 195     5141   3987   6647     14     75    947       C  
ATOM   1584  CD2 PHE A 195      69.621 -12.915 -31.030  1.00 38.95           C  
ANISOU 1584  CD2 PHE A 195     4860   3664   6274      8     10   1197       C  
ATOM   1585  CE1 PHE A 195      69.492 -12.675 -28.292  1.00 39.54           C  
ANISOU 1585  CE1 PHE A 195     4847   3645   6530     70     85    967       C  
ATOM   1586  CE2 PHE A 195      68.813 -11.945 -30.460  1.00 41.50           C  
ANISOU 1586  CE2 PHE A 195     5126   3894   6748     73     15   1231       C  
ATOM   1587  CZ  PHE A 195      68.754 -11.826 -29.090  1.00 37.97           C  
ANISOU 1587  CZ  PHE A 195     4639   3396   6392    105     61   1110       C  
ATOM   1588  N   THR A 196      73.886 -16.630 -30.205  1.00 33.90           N  
ANISOU 1588  N   THR A 196     4305   3235   5343   -149    186    819       N  
ATOM   1589  CA  THR A 196      74.416 -17.924 -30.601  1.00 33.68           C  
ANISOU 1589  CA  THR A 196     4314   3280   5202   -174    214    784       C  
ATOM   1590  C   THR A 196      73.279 -18.785 -31.135  1.00 39.56           C  
ANISOU 1590  C   THR A 196     5104   4090   5839   -173    148    809       C  
ATOM   1591  O   THR A 196      72.101 -18.505 -30.906  1.00 39.03           O  
ANISOU 1591  O   THR A 196     5010   4021   5799   -146     74    839       O  
ATOM   1592  CB  THR A 196      75.123 -18.634 -29.438  1.00 36.68           C  
ANISOU 1592  CB  THR A 196     4640   3680   5617   -168    243    678       C  
ATOM   1593  OG1 THR A 196      74.243 -18.705 -28.317  1.00 36.17           O  
ANISOU 1593  OG1 THR A 196     4528   3619   5598   -134    186    625       O  
ATOM   1594  CG2 THR A 196      76.411 -17.875 -29.037  1.00 33.83           C  
ANISOU 1594  CG2 THR A 196     4235   3270   5349   -191    304    663       C  
ATOM   1595  N   GLN A 197      73.648 -19.834 -31.872  1.00 37.66           N  
ANISOU 1595  N   GLN A 197     4931   3901   5477   -207    180    798       N  
ATOM   1596  CA  GLN A 197      72.689 -20.607 -32.653  1.00 38.94           C  
ANISOU 1596  CA  GLN A 197     5161   4123   5510   -235    122    829       C  
ATOM   1597  C   GLN A 197      72.299 -21.926 -31.996  1.00 39.16           C  
ANISOU 1597  C   GLN A 197     5181   4199   5498   -226    103    743       C  
ATOM   1598  O   GLN A 197      71.326 -22.554 -32.438  1.00 41.42           O  
ANISOU 1598  O   GLN A 197     5511   4535   5693   -253     37    762       O  
ATOM   1599  CB  GLN A 197      73.257 -20.860 -34.058  1.00 34.75           C  
ANISOU 1599  CB  GLN A 197     4742   3611   4851   -294    177    876       C  
ATOM   1600  CG  GLN A 197      73.499 -19.566 -34.867  1.00 38.13           C  
ANISOU 1600  CG  GLN A 197     5190   3998   5301   -311    187    983       C  
ATOM   1601  CD  GLN A 197      72.188 -18.883 -35.255  1.00 48.97           C  
ANISOU 1601  CD  GLN A 197     6557   5379   6671   -310     71   1089       C  
ATOM   1602  OE1 GLN A 197      71.213 -19.545 -35.623  1.00 47.38           O  
ANISOU 1602  OE1 GLN A 197     6390   5240   6373   -337     -9   1110       O  
ATOM   1603  NE2 GLN A 197      72.156 -17.558 -35.154  1.00 46.53           N  
ANISOU 1603  NE2 GLN A 197     6198   5004   6477   -280     62   1162       N  
ATOM   1604  N   SER A 198      73.031 -22.359 -30.967  1.00 35.74           N  
ANISOU 1604  N   SER A 198     4101   4654   4822   -318    222    810       N  
ATOM   1605  CA  SER A 198      72.625 -23.482 -30.116  1.00 40.83           C  
ANISOU 1605  CA  SER A 198     4827   5352   5334   -469    416   1110       C  
ATOM   1606  C   SER A 198      72.541 -24.800 -30.888  1.00 36.62           C  
ANISOU 1606  C   SER A 198     4566   4382   4966   -682    389   1312       C  
ATOM   1607  O   SER A 198      71.726 -25.669 -30.563  1.00 42.15           O  
ANISOU 1607  O   SER A 198     5272   5021   5720   -948    536   1532       O  
ATOM   1608  CB  SER A 198      71.290 -23.193 -29.423  1.00 43.12           C  
ANISOU 1608  CB  SER A 198     4786   5970   5627   -626    605   1103       C  
ATOM   1609  OG  SER A 198      71.384 -22.091 -28.544  1.00 47.80           O  
ANISOU 1609  OG  SER A 198     5169   6958   6034   -412    681    884       O  
ATOM   1610  N   ARG A 199      73.384 -24.979 -31.897  1.00 36.01           N  
ANISOU 1610  N   ARG A 199     4718   3990   4974   -586    225   1224       N  
ATOM   1611  CA  ARG A 199      73.400 -26.222 -32.658  1.00 43.38           C  
ANISOU 1611  CA  ARG A 199     5950   4471   6060   -758    207   1327       C  
ATOM   1612  C   ARG A 199      74.349 -27.234 -32.007  1.00 50.40           C  
ANISOU 1612  C   ARG A 199     7147   5163   6840   -583    314   1613       C  
ATOM   1613  O   ARG A 199      75.065 -26.924 -31.055  1.00 43.88           O  
ANISOU 1613  O   ARG A 199     6280   4613   5778   -322    355   1730       O  
ATOM   1614  CB  ARG A 199      73.787 -25.932 -34.108  1.00 39.68           C  
ANISOU 1614  CB  ARG A 199     5574   3803   5699   -726      7   1066       C  
ATOM   1615  CG  ARG A 199      72.737 -25.110 -34.836  1.00 47.72           C  
ANISOU 1615  CG  ARG A 199     6310   4983   6840   -908   -129    871       C  
ATOM   1616  CD  ARG A 199      73.203 -24.603 -36.189  1.00 46.53           C  
ANISOU 1616  CD  ARG A 199     6232   4746   6701   -832   -330    664       C  
ATOM   1617  NE  ARG A 199      74.188 -23.532 -36.084  1.00 41.05           N  
ANISOU 1617  NE  ARG A 199     5477   4209   5910   -523   -360    598       N  
ATOM   1618  CZ  ARG A 199      74.555 -22.762 -37.105  1.00 40.78           C  
ANISOU 1618  CZ  ARG A 199     5431   4186   5878   -445   -503    472       C  
ATOM   1619  NH1 ARG A 199      74.004 -22.941 -38.300  1.00 42.91           N  
ANISOU 1619  NH1 ARG A 199     5747   4377   6181   -622   -649    396       N  
ATOM   1620  NH2 ARG A 199      75.468 -21.806 -36.935  1.00 37.04           N  
ANISOU 1620  NH2 ARG A 199     4893   3823   5357   -216   -506    430       N  
ATOM   1621  N   ASN A 200      74.332 -28.471 -32.509  1.00 53.20           N  
ANISOU 1621  N   ASN A 200     7807   5031   7373   -726    348   1725       N  
ATOM   1622  CA  ASN A 200      75.232 -29.506 -32.003  1.00 48.31           C  
ANISOU 1622  CA  ASN A 200     7505   4126   6724   -510    444   2029       C  
ATOM   1623  C   ASN A 200      76.007 -30.136 -33.161  1.00 54.08           C  
ANISOU 1623  C   ASN A 200     8545   4375   7629   -387    369   1854       C  
ATOM   1624  O   ASN A 200      75.676 -29.955 -34.338  1.00 52.98           O  
ANISOU 1624  O   ASN A 200     8414   4109   7608   -559    260   1523       O  
ATOM   1625  CB  ASN A 200      74.484 -30.569 -31.179  1.00 58.87           C  
ANISOU 1625  CB  ASN A 200     8964   5268   8135   -768    646   2431       C  
ATOM   1626  CG  ASN A 200      73.430 -31.305 -31.974  1.00 75.82           C  
ANISOU 1626  CG  ASN A 200    11205   6992  10609  -1238    666   2332       C  
ATOM   1627  OD1 ASN A 200      73.743 -32.156 -32.809  1.00 85.74           O  
ANISOU 1627  OD1 ASN A 200    12704   7806  12068  -1254    559   2181       O  
ATOM   1628  ND2 ASN A 200      72.166 -31.007 -31.693  1.00 70.18           N  
ANISOU 1628  ND2 ASN A 200    10190   6548   9928  -1608    731   2341       N  
ATOM   1629  N   LEU A 201      77.073 -30.862 -32.804  1.00 58.52           N  
ANISOU 1629  N   LEU A 201     9302   4765   8168    -60    396   2045       N  
ATOM   1630  CA  LEU A 201      78.033 -31.336 -33.802  1.00 71.17           C  
ANISOU 1630  CA  LEU A 201    11037   6110   9893    158    311   1797       C  
ATOM   1631  C   LEU A 201      77.391 -32.302 -34.788  1.00 76.48           C  
ANISOU 1631  C   LEU A 201    11881   6323  10854   -135    311   1591       C  
ATOM   1632  O   LEU A 201      77.473 -32.111 -36.008  1.00 89.71           O  
ANISOU 1632  O   LEU A 201    13598   7916  12572   -172    258   1222       O  
ATOM   1633  CB  LEU A 201      79.220 -32.014 -33.115  1.00 72.63           C  
ANISOU 1633  CB  LEU A 201    11277   6292  10029    542    311   2023       C  
ATOM   1634  CG  LEU A 201      80.456 -31.179 -32.810  1.00 64.73           C  
ANISOU 1634  CG  LEU A 201    10082   5707   8804    940    248   2007       C  
ATOM   1635  CD1 LEU A 201      81.648 -32.094 -32.625  1.00 77.62           C  
ANISOU 1635  CD1 LEU A 201    11780   7213  10500   1284    235   2120       C  
ATOM   1636  CD2 LEU A 201      80.698 -30.183 -33.923  1.00 66.89           C  
ANISOU 1636  CD2 LEU A 201    10258   6094   9063    956    197   1641       C  
ATOM   1637  N   GLN A 202      76.751 -33.351 -34.273  1.00 72.01           N  
ANISOU 1637  N   GLN A 202    11421   5477  10463   -358    368   1821       N  
ATOM   1638  CA  GLN A 202      76.349 -34.470 -35.119  1.00 85.95           C  
ANISOU 1638  CA  GLN A 202    13361   6750  12546   -578    364   1628       C  
ATOM   1639  C   GLN A 202      75.235 -34.081 -36.083  1.00 93.52           C  
ANISOU 1639  C   GLN A 202    14216   7733  13584   -990    326   1281       C  
ATOM   1640  O   GLN A 202      75.181 -34.582 -37.213  1.00104.75           O  
ANISOU 1640  O   GLN A 202    15768   8894  15139  -1092    277    918       O  
ATOM   1641  CB  GLN A 202      75.908 -35.635 -34.245  1.00 87.58           C  
ANISOU 1641  CB  GLN A 202    13703   6646  12928   -747    416   2004       C  
ATOM   1642  CG  GLN A 202      76.946 -36.048 -33.224  1.00100.74           C  
ANISOU 1642  CG  GLN A 202    15490   8330  14458   -352    435   2372       C  
ATOM   1643  CD  GLN A 202      76.439 -37.134 -32.307  1.00119.43           C  
ANISOU 1643  CD  GLN A 202    18037  10412  16929   -553    490   2792       C  
ATOM   1644  OE1 GLN A 202      75.266 -37.147 -31.934  1.00133.41           O  
ANISOU 1644  OE1 GLN A 202    19750  12233  18705   -990    545   2936       O  
ATOM   1645  NE2 GLN A 202      77.316 -38.062 -31.945  1.00122.43           N  
ANISOU 1645  NE2 GLN A 202    18631  10493  17393   -244    484   3004       N  
ATOM   1646  N   GLU A 203      74.335 -33.199 -35.656  1.00 80.27           N  
ANISOU 1646  N   GLU A 203    12304   6400  11795  -1233    339   1366       N  
ATOM   1647  CA  GLU A 203      73.196 -32.793 -36.465  1.00 74.77           C  
ANISOU 1647  CA  GLU A 203    11455   5816  11137  -1642    257   1063       C  
ATOM   1648  C   GLU A 203      73.300 -31.337 -36.900  1.00 57.98           C  
ANISOU 1648  C   GLU A 203     9174   4110   8747  -1568     94    886       C  
ATOM   1649  O   GLU A 203      72.280 -30.656 -37.034  1.00 59.88           O  
ANISOU 1649  O   GLU A 203     9148   4631   8972  -1869    -22    820       O  
ATOM   1650  CB  GLU A 203      71.897 -33.017 -35.698  1.00 79.15           C  
ANISOU 1650  CB  GLU A 203    11803   6447  11826  -2045    373   1286       C  
ATOM   1651  CG  GLU A 203      71.895 -34.266 -34.832  1.00 86.34           C  
ANISOU 1651  CG  GLU A 203    12831   7005  12969  -2071    535   1667       C  
ATOM   1652  CD  GLU A 203      70.734 -34.291 -33.859  1.00 92.61           C  
ANISOU 1652  CD  GLU A 203    13396   7999  13791  -2402    754   1947       C  
ATOM   1653  OE1 GLU A 203      70.092 -35.355 -33.717  1.00105.65           O  
ANISOU 1653  OE1 GLU A 203    15056   9357  15728  -2675    835   2067       O  
ATOM   1654  OE2 GLU A 203      70.461 -33.239 -33.240  1.00 93.04           O  
ANISOU 1654  OE2 GLU A 203    13278   8524  13550  -2411    826   2026       O  
ATOM   1655  N   PHE A 204      74.520 -30.844 -37.124  1.00 53.21           N  
ANISOU 1655  N   PHE A 204     8678   3567   7974  -1163     58    829       N  
ATOM   1656  CA  PHE A 204      74.692 -29.447 -37.483  1.00 48.91           C  
ANISOU 1656  CA  PHE A 204     7904   3451   7230  -1040    -95    695       C  
ATOM   1657  C   PHE A 204      74.042 -29.172 -38.831  1.00 57.56           C  
ANISOU 1657  C   PHE A 204     8954   4601   8314  -1304   -294    365       C  
ATOM   1658  O   PHE A 204      74.279 -29.888 -39.805  1.00 65.74           O  
ANISOU 1658  O   PHE A 204    10263   5352   9364  -1365   -321    121       O  
ATOM   1659  CB  PHE A 204      76.176 -29.076 -37.524  1.00 46.14           C  
ANISOU 1659  CB  PHE A 204     7630   3171   6730   -573    -66    686       C  
ATOM   1660  CG  PHE A 204      76.425 -27.616 -37.714  1.00 48.17           C  
ANISOU 1660  CG  PHE A 204     7587   3887   6828   -433   -182    594       C  
ATOM   1661  CD1 PHE A 204      76.383 -27.044 -38.976  1.00 48.04           C  
ANISOU 1661  CD1 PHE A 204     7547   3966   6742   -495   -322    348       C  
ATOM   1662  CD2 PHE A 204      76.707 -26.803 -36.627  1.00 52.21           C  
ANISOU 1662  CD2 PHE A 204     7856   4729   7252   -250   -149    755       C  
ATOM   1663  CE1 PHE A 204      76.610 -25.697 -39.151  1.00 45.97           C  
ANISOU 1663  CE1 PHE A 204     7033   4052   6383   -377   -414    320       C  
ATOM   1664  CE2 PHE A 204      76.940 -25.447 -36.796  1.00 48.95           C  
ANISOU 1664  CE2 PHE A 204     7192   4649   6758   -146   -245    647       C  
ATOM   1665  CZ  PHE A 204      76.887 -24.897 -38.057  1.00 52.45           C  
ANISOU 1665  CZ  PHE A 204     7624   5114   7191   -210   -370    457       C  
ATOM   1666  N   LYS A 205      73.218 -28.130 -38.878  1.00 52.90           N  
ANISOU 1666  N   LYS A 205     7995   4421   7683  -1425   -431    349       N  
ATOM   1667  CA  LYS A 205      72.532 -27.742 -40.091  1.00 57.69           C  
ANISOU 1667  CA  LYS A 205     8494   5182   8244  -1645   -665    111       C  
ATOM   1668  C   LYS A 205      72.867 -26.297 -40.431  1.00 52.96           C  
ANISOU 1668  C   LYS A 205     7664   4966   7492  -1387   -784    106       C  
ATOM   1669  O   LYS A 205      72.722 -25.410 -39.575  1.00 49.12           O  
ANISOU 1669  O   LYS A 205     6898   4724   7043  -1246   -741    260       O  
ATOM   1670  CB  LYS A 205      71.011 -27.914 -39.947  1.00 55.36           C  
ANISOU 1670  CB  LYS A 205     7921   4999   8112  -2073   -752    129       C  
ATOM   1671  CG  LYS A 205      70.593 -29.348 -39.636  1.00 57.68           C  
ANISOU 1671  CG  LYS A 205     8418   4894   8604  -2389   -610    146       C  
ATOM   1672  CD  LYS A 205      69.126 -29.556 -39.882  1.00 64.61           C  
ANISOU 1672  CD  LYS A 205     8974   5957   9619  -2804   -706     59       C  
ATOM   1673  CE  LYS A 205      68.687 -30.940 -39.421  1.00 75.12           C  
ANISOU 1673  CE  LYS A 205    10421   6928  11193  -3052   -490    105       C  
ATOM   1674  NZ  LYS A 205      69.672 -31.999 -39.792  1.00 85.25           N  
ANISOU 1674  NZ  LYS A 205    12161   7708  12523  -2893   -384    -16       N  
ATOM   1675  N   PRO A 206      73.321 -26.021 -41.648  1.00 52.13           N  
ANISOU 1675  N   PRO A 206     7684   4911   7213  -1326   -915    -66       N  
ATOM   1676  CA  PRO A 206      73.626 -24.639 -42.024  1.00 46.76           C  
ANISOU 1676  CA  PRO A 206     6804   4543   6419  -1113  -1018    -10       C  
ATOM   1677  C   PRO A 206      72.368 -23.787 -42.034  1.00 49.79           C  
ANISOU 1677  C   PRO A 206     6805   5215   6900  -1248  -1205     66       C  
ATOM   1678  O   PRO A 206      71.267 -24.266 -42.310  1.00 54.47           O  
ANISOU 1678  O   PRO A 206     7288   5850   7557  -1554  -1338      2       O  
ATOM   1679  CB  PRO A 206      74.215 -24.780 -43.432  1.00 46.46           C  
ANISOU 1679  CB  PRO A 206     7013   4504   6134  -1100  -1101   -192       C  
ATOM   1680  CG  PRO A 206      73.593 -26.016 -43.958  1.00 46.55           C  
ANISOU 1680  CG  PRO A 206     7232   4312   6142  -1419  -1163   -415       C  
ATOM   1681  CD  PRO A 206      73.497 -26.950 -42.774  1.00 50.46           C  
ANISOU 1681  CD  PRO A 206     7804   4479   6890  -1477   -968   -331       C  
ATOM   1682  N   ARG A 207      72.543 -22.499 -41.727  1.00 48.64           N  
ANISOU 1682  N   ARG A 207     6431   5256   6795  -1013  -1215    192       N  
ATOM   1683  CA  ARG A 207      71.421 -21.570 -41.649  1.00 50.00           C  
ANISOU 1683  CA  ARG A 207     6214   5671   7114  -1036  -1364    278       C  
ATOM   1684  C   ARG A 207      71.587 -20.356 -42.557  1.00 55.01           C  
ANISOU 1684  C   ARG A 207     6765   6449   7687   -867  -1540    365       C  
ATOM   1685  O   ARG A 207      70.808 -19.405 -42.443  1.00 50.78           O  
ANISOU 1685  O   ARG A 207     5906   6066   7320   -782  -1649    471       O  
ATOM   1686  CB  ARG A 207      71.201 -21.131 -40.195  1.00 48.15           C  
ANISOU 1686  CB  ARG A 207     5743   5484   7066   -908  -1177    350       C  
ATOM   1687  CG  ARG A 207      70.500 -22.217 -39.356  1.00 53.82           C  
ANISOU 1687  CG  ARG A 207     6420   6164   7864  -1148  -1040    358       C  
ATOM   1688  CD  ARG A 207      70.357 -21.861 -37.881  1.00 44.82           C  
ANISOU 1688  CD  ARG A 207     5079   5142   6807  -1021   -816    429       C  
ATOM   1689  NE  ARG A 207      69.756 -22.978 -37.163  1.00 48.34           N  
ANISOU 1689  NE  ARG A 207     5524   5550   7292  -1280   -660    506       N  
ATOM   1690  CZ  ARG A 207      69.665 -23.080 -35.841  1.00 50.64           C  
ANISOU 1690  CZ  ARG A 207     5723   5950   7567  -1238   -420    608       C  
ATOM   1691  NH1 ARG A 207      70.137 -22.117 -35.061  1.00 47.95           N  
ANISOU 1691  NH1 ARG A 207     5280   5780   7160   -941   -326    575       N  
ATOM   1692  NH2 ARG A 207      69.093 -24.151 -35.295  1.00 43.21           N  
ANISOU 1692  NH2 ARG A 207     4800   4953   6663  -1518   -270    740       N  
ATOM   1693  N   SER A 208      72.570 -20.367 -43.455  1.00 51.04           N  
ANISOU 1693  N   SER A 208     6538   5899   6957   -804  -1551    346       N  
ATOM   1694  CA  SER A 208      72.726 -19.330 -44.465  1.00 50.37           C  
ANISOU 1694  CA  SER A 208     6418   5956   6764   -695  -1712    491       C  
ATOM   1695  C   SER A 208      73.450 -19.934 -45.656  1.00 54.47           C  
ANISOU 1695  C   SER A 208     7267   6505   6923   -771  -1732    398       C  
ATOM   1696  O   SER A 208      74.048 -21.008 -45.564  1.00 45.74           O  
ANISOU 1696  O   SER A 208     6419   5243   5718   -828  -1576    204       O  
ATOM   1697  CB  SER A 208      73.520 -18.136 -43.936  1.00 48.53           C  
ANISOU 1697  CB  SER A 208     6112   5638   6689   -437  -1580    624       C  
ATOM   1698  OG  SER A 208      74.873 -18.517 -43.752  1.00 48.42           O  
ANISOU 1698  OG  SER A 208     6337   5501   6560   -366  -1366    545       O  
ATOM   1699  N   GLN A 209      73.429 -19.206 -46.775  1.00 52.29           N  
ANISOU 1699  N   GLN A 209     6988   6433   6446   -741  -1906    554       N  
ATOM   1700  CA  GLN A 209      74.159 -19.660 -47.954  1.00 51.30           C  
ANISOU 1700  CA  GLN A 209     7170   6416   5908   -795  -1892    464       C  
ATOM   1701  C   GLN A 209      75.656 -19.717 -47.687  1.00 50.43           C  
ANISOU 1701  C   GLN A 209     7248   6145   5769   -625  -1574    426       C  
ATOM   1702  O   GLN A 209      76.343 -20.629 -48.164  1.00 57.49           O  
ANISOU 1702  O   GLN A 209     8411   7013   6419   -650  -1439    208       O  
ATOM   1703  CB  GLN A 209      73.873 -18.751 -49.149  1.00 53.28           C  
ANISOU 1703  CB  GLN A 209     7366   6972   5906   -779  -2128    724       C  
ATOM   1704  CG  GLN A 209      74.486 -19.267 -50.435  1.00 58.55           C  
ANISOU 1704  CG  GLN A 209     8344   7854   6048   -862  -2116    606       C  
ATOM   1705  CD  GLN A 209      73.889 -20.597 -50.863  1.00 62.60           C  
ANISOU 1705  CD  GLN A 209     9014   8433   6338  -1125  -2244    214       C  
ATOM   1706  OE1 GLN A 209      72.668 -20.763 -50.888  1.00 70.03           O  
ANISOU 1706  OE1 GLN A 209     9764   9499   7346  -1308  -2530    181       O  
ATOM   1707  NE2 GLN A 209      74.747 -21.554 -51.197  1.00 58.41           N  
ANISOU 1707  NE2 GLN A 209     8815   7805   5572  -1149  -2025   -104       N  
ATOM   1708  N   MET A 210      76.185 -18.754 -46.930  1.00 44.37           N  
ANISOU 1708  N   MET A 210     6323   5274   5260   -449  -1452    608       N  
ATOM   1709  CA  MET A 210      77.605 -18.793 -46.601  1.00 44.79           C  
ANISOU 1709  CA  MET A 210     6477   5227   5313   -310  -1176    568       C  
ATOM   1710  C   MET A 210      77.953 -20.060 -45.826  1.00 50.82           C  
ANISOU 1710  C   MET A 210     7369   5813   6127   -287  -1016    322       C  
ATOM   1711  O   MET A 210      79.005 -20.667 -46.056  1.00 48.46           O  
ANISOU 1711  O   MET A 210     7242   5484   5686   -192   -825    205       O  
ATOM   1712  CB  MET A 210      78.009 -17.547 -45.807  1.00 43.19           C  
ANISOU 1712  CB  MET A 210     6057   4936   5419   -184  -1110    750       C  
ATOM   1713  CG  MET A 210      79.496 -17.515 -45.441  1.00 42.51           C  
ANISOU 1713  CG  MET A 210     5997   4809   5347    -73   -859    710       C  
ATOM   1714  SD  MET A 210      79.944 -16.209 -44.276  1.00 47.23           S  
ANISOU 1714  SD  MET A 210     6334   5278   6335      6   -801    794       S  
ATOM   1715  CE  MET A 210      79.501 -14.742 -45.216  1.00 49.61           C  
ANISOU 1715  CE  MET A 210     6567   5557   6724    -44   -936   1117       C  
ATOM   1716  N   GLU A 211      77.069 -20.488 -44.918  1.00 46.59           N  
ANISOU 1716  N   GLU A 211     6742   5161   5798   -360  -1076    266       N  
ATOM   1717  CA  GLU A 211      77.332 -21.701 -44.150  1.00 48.51           C  
ANISOU 1717  CA  GLU A 211     7127   5200   6106   -343   -926    115       C  
ATOM   1718  C   GLU A 211      77.217 -22.946 -45.021  1.00 50.74           C  
ANISOU 1718  C   GLU A 211     7703   5383   6191   -478   -932   -110       C  
ATOM   1719  O   GLU A 211      77.986 -23.900 -44.853  1.00 48.33           O  
ANISOU 1719  O   GLU A 211     7612   4876   5875   -370   -749   -240       O  
ATOM   1720  CB  GLU A 211      76.382 -21.782 -42.953  1.00 43.17           C  
ANISOU 1720  CB  GLU A 211     6268   4460   5676   -417   -958    163       C  
ATOM   1721  CG  GLU A 211      76.716 -20.790 -41.859  1.00 46.45           C  
ANISOU 1721  CG  GLU A 211     6453   4933   6265   -249   -885    279       C  
ATOM   1722  CD  GLU A 211      76.004 -21.081 -40.558  1.00 46.75           C  
ANISOU 1722  CD  GLU A 211     6354   4948   6462   -287   -834    297       C  
ATOM   1723  OE1 GLU A 211      74.969 -21.785 -40.587  1.00 49.56           O  
ANISOU 1723  OE1 GLU A 211     6707   5267   6855   -489   -889    275       O  
ATOM   1724  OE2 GLU A 211      76.484 -20.603 -39.507  1.00 43.64           O  
ANISOU 1724  OE2 GLU A 211     5843   4604   6134   -140   -733    325       O  
ATOM   1725  N   ILE A 212      76.259 -22.960 -45.952  1.00 47.47           N  
ANISOU 1725  N   ILE A 212     7298   5107   5630   -702  -1152   -176       N  
ATOM   1726  CA  ILE A 212      76.202 -24.041 -46.933  1.00 49.22           C  
ANISOU 1726  CA  ILE A 212     7819   5271   5610   -859  -1176   -467       C  
ATOM   1727  C   ILE A 212      77.515 -24.111 -47.706  1.00 55.06           C  
ANISOU 1727  C   ILE A 212     8775   6067   6076   -657   -981   -566       C  
ATOM   1728  O   ILE A 212      78.107 -25.186 -47.869  1.00 50.41           O  
ANISOU 1728  O   ILE A 212     8460   5258   5436   -594   -805   -825       O  
ATOM   1729  CB  ILE A 212      74.999 -23.851 -47.877  1.00 53.50           C  
ANISOU 1729  CB  ILE A 212     8280   6079   5969  -1138  -1499   -514       C  
ATOM   1730  CG1 ILE A 212      73.681 -24.027 -47.116  1.00 50.79           C  
ANISOU 1730  CG1 ILE A 212     7692   5682   5923  -1363  -1655   -470       C  
ATOM   1731  CG2 ILE A 212      75.080 -24.821 -49.062  1.00 56.81           C  
ANISOU 1731  CG2 ILE A 212     9031   6517   6038  -1306  -1537   -881       C  
ATOM   1732  CD1 ILE A 212      72.450 -23.938 -47.991  1.00 59.50           C  
ANISOU 1732  CD1 ILE A 212     8645   7085   6877  -1650  -2007   -527       C  
ATOM   1733  N   ASP A 213      78.000 -22.956 -48.174  1.00 50.43           N  
ANISOU 1733  N   ASP A 213     8057   5761   5342   -542   -985   -349       N  
ATOM   1734  CA  ASP A 213      79.258 -22.919 -48.917  1.00 52.76           C  
ANISOU 1734  CA  ASP A 213     8494   6185   5369   -370   -763   -401       C  
ATOM   1735  C   ASP A 213      80.424 -23.397 -48.060  1.00 51.35           C  
ANISOU 1735  C   ASP A 213     8331   5782   5398   -110   -473   -448       C  
ATOM   1736  O   ASP A 213      81.289 -24.143 -48.538  1.00 48.68           O  
ANISOU 1736  O   ASP A 213     8188   5407   4902     36   -256   -666       O  
ATOM   1737  CB  ASP A 213      79.524 -21.504 -49.431  1.00 54.08           C  
ANISOU 1737  CB  ASP A 213     8481   6655   5410   -337   -805    -71       C  
ATOM   1738  CG  ASP A 213      78.609 -21.115 -50.571  1.00 55.71           C  
ANISOU 1738  CG  ASP A 213     8716   7162   5288   -527  -1078      7       C  
ATOM   1739  OD1 ASP A 213      77.888 -21.993 -51.088  1.00 58.15           O  
ANISOU 1739  OD1 ASP A 213     9190   7505   5400   -704  -1228   -269       O  
ATOM   1740  OD2 ASP A 213      78.605 -19.924 -50.946  1.00 59.69           O  
ANISOU 1740  OD2 ASP A 213     9075   7865   5740   -508  -1157    356       O  
ATOM   1741  N   PHE A 214      80.462 -22.980 -46.790  1.00 46.95           N  
ANISOU 1741  N   PHE A 214     7554   5106   5179    -26   -469   -259       N  
ATOM   1742  CA  PHE A 214      81.556 -23.389 -45.912  1.00 48.58           C  
ANISOU 1742  CA  PHE A 214     7729   5173   5556    232   -247   -261       C  
ATOM   1743  C   PHE A 214      81.622 -24.901 -45.779  1.00 46.56           C  
ANISOU 1743  C   PHE A 214     7748   4600   5344    307   -138   -495       C  
ATOM   1744  O   PHE A 214      82.708 -25.490 -45.804  1.00 45.81           O  
ANISOU 1744  O   PHE A 214     7734   4430   5240    571     82   -588       O  
ATOM   1745  CB  PHE A 214      81.406 -22.758 -44.529  1.00 47.02           C  
ANISOU 1745  CB  PHE A 214     7272   4945   5649    268   -305    -58       C  
ATOM   1746  CG  PHE A 214      82.460 -23.205 -43.549  1.00 51.96           C  
ANISOU 1746  CG  PHE A 214     7840   5495   6409    528   -138    -35       C  
ATOM   1747  CD1 PHE A 214      83.684 -22.561 -43.489  1.00 44.76           C  
ANISOU 1747  CD1 PHE A 214     6732   4783   5492    695    -20     37       C  
ATOM   1748  CD2 PHE A 214      82.234 -24.288 -42.701  1.00 48.98           C  
ANISOU 1748  CD2 PHE A 214     7587   4862   6163    598   -108    -54       C  
ATOM   1749  CE1 PHE A 214      84.664 -22.976 -42.591  1.00 42.91           C  
ANISOU 1749  CE1 PHE A 214     6390   4550   5364    950     90     68       C  
ATOM   1750  CE2 PHE A 214      83.204 -24.707 -41.805  1.00 44.02           C  
ANISOU 1750  CE2 PHE A 214     6894   4202   5628    876     12     26       C  
ATOM   1751  CZ  PHE A 214      84.422 -24.056 -41.746  1.00 47.63           C  
ANISOU 1751  CZ  PHE A 214     7121   4914   6062   1066     94     76       C  
ATOM   1752  N   LEU A 215      80.469 -25.547 -45.635  1.00 46.76           N  
ANISOU 1752  N   LEU A 215     7901   4413   5452     79   -280   -584       N  
ATOM   1753  CA  LEU A 215      80.468 -26.993 -45.470  1.00 48.60           C  
ANISOU 1753  CA  LEU A 215     8426   4241   5798    108   -172   -787       C  
ATOM   1754  C   LEU A 215      80.763 -27.708 -46.781  1.00 52.84           C  
ANISOU 1754  C   LEU A 215     9270   4726   6081    104    -84  -1157       C  
ATOM   1755  O   LEU A 215      81.412 -28.763 -46.779  1.00 56.35           O  
ANISOU 1755  O   LEU A 215     9956   4846   6611    312    120  -1350       O  
ATOM   1756  CB  LEU A 215      79.130 -27.442 -44.887  1.00 54.01           C  
ANISOU 1756  CB  LEU A 215     9125   4714   6681   -199   -332   -756       C  
ATOM   1757  CG  LEU A 215      78.931 -26.996 -43.439  1.00 51.74           C  
ANISOU 1757  CG  LEU A 215     8581   4450   6627   -144   -339   -434       C  
ATOM   1758  CD1 LEU A 215      77.504 -27.262 -42.997  1.00 55.63           C  
ANISOU 1758  CD1 LEU A 215     9014   4848   7274   -489   -478   -389       C  
ATOM   1759  CD2 LEU A 215      79.937 -27.704 -42.530  1.00 50.73           C  
ANISOU 1759  CD2 LEU A 215     8543   4086   6646    179   -133   -322       C  
ATOM   1760  N   GLU A 216      80.323 -27.144 -47.905  1.00 53.18           N  
ANISOU 1760  N   GLU A 216     9313   5095   5797   -100   -228  -1258       N  
ATOM   1761  CA  GLU A 216      80.459 -27.841 -49.181  1.00 65.62           C  
ANISOU 1761  CA  GLU A 216    11200   6685   7046   -153   -166  -1668       C  
ATOM   1762  C   GLU A 216      81.831 -27.623 -49.809  1.00 65.60           C  
ANISOU 1762  C   GLU A 216    11211   6915   6798    171    117  -1726       C  
ATOM   1763  O   GLU A 216      82.426 -28.567 -50.339  1.00 69.06           O  
ANISOU 1763  O   GLU A 216    11919   7182   7137    334    337  -2089       O  
ATOM   1764  CB  GLU A 216      79.354 -27.398 -50.143  1.00 74.78           C  
ANISOU 1764  CB  GLU A 216    12352   8174   7888   -520   -472  -1744       C  
ATOM   1765  CG  GLU A 216      78.125 -28.306 -50.136  1.00 98.48           C  
ANISOU 1765  CG  GLU A 216    15504  10904  11010   -888   -682  -2003       C  
ATOM   1766  CD  GLU A 216      76.869 -27.636 -50.690  1.00112.41           C  
ANISOU 1766  CD  GLU A 216    17078  13058  12575  -1241  -1064  -1926       C  
ATOM   1767  OE1 GLU A 216      76.987 -26.631 -51.427  1.00115.73           O  
ANISOU 1767  OE1 GLU A 216    17370  13953  12650  -1195  -1164  -1750       O  
ATOM   1768  OE2 GLU A 216      75.757 -28.117 -50.379  1.00115.10           O  
ANISOU 1768  OE2 GLU A 216    17376  13238  13120  -1564  -1265  -2009       O  
ATOM   1769  N   LEU A 217      82.353 -26.399 -49.755  1.00 58.76           N  
ANISOU 1769  N   LEU A 217    10049   6419   5858    264    137  -1389       N  
ATOM   1770  CA  LEU A 217      83.569 -26.056 -50.480  1.00 62.10           C  
ANISOU 1770  CA  LEU A 217    10427   7157   6010    489    406  -1406       C  
ATOM   1771  C   LEU A 217      84.825 -26.461 -49.709  1.00 59.85           C  
ANISOU 1771  C   LEU A 217    10031   6706   6002    880    695  -1381       C  
ATOM   1772  O   LEU A 217      84.818 -26.623 -48.484  1.00 62.42           O  
ANISOU 1772  O   LEU A 217    10240   6768   6711    979    646  -1212       O  
ATOM   1773  CB  LEU A 217      83.623 -24.553 -50.764  1.00 62.44           C  
ANISOU 1773  CB  LEU A 217    10193   7629   5904    381    318  -1019       C  
ATOM   1774  CG  LEU A 217      82.502 -23.944 -51.603  1.00 59.77           C  
ANISOU 1774  CG  LEU A 217     9899   7549   5263     64     20   -931       C  
ATOM   1775  CD1 LEU A 217      82.619 -22.426 -51.623  1.00 62.94           C  
ANISOU 1775  CD1 LEU A 217    10016   8226   5671     18    -48   -461       C  
ATOM   1776  CD2 LEU A 217      82.543 -24.505 -53.010  1.00 58.77           C  
ANISOU 1776  CD2 LEU A 217    10064   7679   4588     -1     89  -1268       C  
ATOM   1777  N   ALA A 218      85.922 -26.608 -50.452  1.00 62.43           N  
ANISOU 1777  N   ALA A 218    10368   7253   6101   1116   1001  -1537       N  
ATOM   1778  CA  ALA A 218      87.236 -26.723 -49.840  1.00 57.50           C  
ANISOU 1778  CA  ALA A 218     9509   6633   5706   1504   1266  -1448       C  
ATOM   1779  C   ALA A 218      87.627 -25.397 -49.184  1.00 63.70           C  
ANISOU 1779  C   ALA A 218     9866   7705   6634   1446   1192  -1014       C  
ATOM   1780  O   ALA A 218      87.040 -24.344 -49.451  1.00 65.96           O  
ANISOU 1780  O   ALA A 218    10066   8197   6799   1148   1012   -797       O  
ATOM   1781  CB  ALA A 218      88.280 -27.138 -50.876  1.00 59.82           C  
ANISOU 1781  CB  ALA A 218     9862   7162   5706   1763   1641  -1735       C  
ATOM   1782  N   MET A 219      88.644 -25.463 -48.314  1.00 66.28           N  
ANISOU 1782  N   MET A 219     9916   8030   7237   1742   1324   -895       N  
ATOM   1783  CA  MET A 219      89.025 -24.305 -47.504  1.00 55.71           C  
ANISOU 1783  CA  MET A 219     8171   6906   6089   1666   1227   -553       C  
ATOM   1784  C   MET A 219      89.438 -23.124 -48.380  1.00 56.39           C  
ANISOU 1784  C   MET A 219     8064   7414   5947   1469   1328   -397       C  
ATOM   1785  O   MET A 219      88.927 -22.008 -48.221  1.00 55.33           O  
ANISOU 1785  O   MET A 219     7816   7343   5864   1185   1136   -152       O  
ATOM   1786  CB  MET A 219      90.153 -24.690 -46.539  1.00 60.85           C  
ANISOU 1786  CB  MET A 219     8538   7570   7012   2033   1344   -495       C  
ATOM   1787  CG  MET A 219      90.644 -23.545 -45.635  1.00 54.09           C  
ANISOU 1787  CG  MET A 219     7241   6964   6348   1936   1228   -217       C  
ATOM   1788  SD  MET A 219      91.991 -23.973 -44.485  1.00 59.58           S  
ANISOU 1788  SD  MET A 219     7532   7799   7308   2358   1296   -140       S  
ATOM   1789  CE  MET A 219      93.335 -24.399 -45.592  1.00 61.09           C  
ANISOU 1789  CE  MET A 219     7555   8293   7365   2673   1714   -299       C  
ATOM   1790  N   ASP A 220      90.357 -23.353 -49.323  1.00 57.05           N  
ANISOU 1790  N   ASP A 220     8113   7777   5787   1624   1652   -524       N  
ATOM   1791  CA  ASP A 220      90.841 -22.251 -50.149  1.00 65.92           C  
ANISOU 1791  CA  ASP A 220     9038   9324   6684   1424   1799   -313       C  
ATOM   1792  C   ASP A 220      89.760 -21.724 -51.084  1.00 65.60           C  
ANISOU 1792  C   ASP A 220     9274   9345   6307   1093   1633   -226       C  
ATOM   1793  O   ASP A 220      89.710 -20.516 -51.343  1.00 68.15           O  
ANISOU 1793  O   ASP A 220     9446   9852   6596    839   1580    110       O  
ATOM   1794  CB  ASP A 220      92.073 -22.684 -50.943  1.00 78.04           C  
ANISOU 1794  CB  ASP A 220    10448  11203   8000   1679   2232   -475       C  
ATOM   1795  CG  ASP A 220      93.215 -23.124 -50.047  1.00 95.76           C  
ANISOU 1795  CG  ASP A 220    12330  13461  10595   2042   2381   -510       C  
ATOM   1796  OD1 ASP A 220      93.746 -24.237 -50.262  1.00103.92           O  
ANISOU 1796  OD1 ASP A 220    13441  14447  11596   2432   2620   -805       O  
ATOM   1797  OD2 ASP A 220      93.563 -22.368 -49.111  1.00 94.08           O  
ANISOU 1797  OD2 ASP A 220    11753  13299  10696   1952   2243   -258       O  
ATOM   1798  N   GLU A 221      88.894 -22.602 -51.600  1.00 68.31           N  
ANISOU 1798  N   GLU A 221    10010   9529   6414   1084   1534   -513       N  
ATOM   1799  CA  GLU A 221      87.776 -22.138 -52.416  1.00 67.34           C  
ANISOU 1799  CA  GLU A 221    10112   9508   5965    776   1300   -424       C  
ATOM   1800  C   GLU A 221      86.873 -21.199 -51.629  1.00 56.48           C  
ANISOU 1800  C   GLU A 221     8607   7944   4908    557    945    -95       C  
ATOM   1801  O   GLU A 221      86.457 -20.151 -52.138  1.00 57.86           O  
ANISOU 1801  O   GLU A 221     8739   8296   4949    340    819    220       O  
ATOM   1802  CB  GLU A 221      86.965 -23.323 -52.934  1.00 71.58           C  
ANISOU 1802  CB  GLU A 221    11055   9881   6259    770   1205   -852       C  
ATOM   1803  CG  GLU A 221      87.664 -24.184 -53.961  1.00 88.61           C  
ANISOU 1803  CG  GLU A 221    13416  12246   8005    955   1547  -1251       C  
ATOM   1804  CD  GLU A 221      86.813 -25.368 -54.384  1.00110.48           C  
ANISOU 1804  CD  GLU A 221    16611  14769  10599    903   1424  -1743       C  
ATOM   1805  OE1 GLU A 221      86.049 -25.889 -53.540  1.00114.21           O  
ANISOU 1805  OE1 GLU A 221    17172  14779  11445    847   1182  -1813       O  
ATOM   1806  OE2 GLU A 221      86.901 -25.774 -55.563  1.00124.52           O  
ANISOU 1806  OE2 GLU A 221    18632  16828  11852    889   1575  -2072       O  
ATOM   1807  N   PHE A 222      86.558 -21.560 -50.384  1.00 52.54           N  
ANISOU 1807  N   PHE A 222     8050   7087   4826    633    796   -152       N  
ATOM   1808  CA  PHE A 222      85.653 -20.742 -49.580  1.00 52.61           C  
ANISOU 1808  CA  PHE A 222     7936   6924   5129    458    493     89       C  
ATOM   1809  C   PHE A 222      86.275 -19.391 -49.245  1.00 55.97           C  
ANISOU 1809  C   PHE A 222     8040   7465   5759    388    536    421       C  
ATOM   1810  O   PHE A 222      85.624 -18.348 -49.368  1.00 51.47           O  
ANISOU 1810  O   PHE A 222     7419   6887   5250    200    355    684       O  
ATOM   1811  CB  PHE A 222      85.274 -21.480 -48.298  1.00 47.90           C  
ANISOU 1811  CB  PHE A 222     7344   5981   4875    560    382    -46       C  
ATOM   1812  CG  PHE A 222      84.427 -20.664 -47.370  1.00 48.56           C  
ANISOU 1812  CG  PHE A 222     7269   5930   5251    418    130    153       C  
ATOM   1813  CD1 PHE A 222      83.052 -20.655 -47.504  1.00 48.39           C  
ANISOU 1813  CD1 PHE A 222     7360   5817   5210    236   -124    158       C  
ATOM   1814  CD2 PHE A 222      85.005 -19.895 -46.369  1.00 48.28           C  
ANISOU 1814  CD2 PHE A 222     6946   5891   5507    467    148    301       C  
ATOM   1815  CE1 PHE A 222      82.262 -19.901 -46.658  1.00 47.42           C  
ANISOU 1815  CE1 PHE A 222     7062   5591   5365    148   -317    315       C  
ATOM   1816  CE2 PHE A 222      84.220 -19.124 -45.523  1.00 46.05           C  
ANISOU 1816  CE2 PHE A 222     6532   5488   5478    356    -53    419       C  
ATOM   1817  CZ  PHE A 222      82.844 -19.132 -45.668  1.00 46.39           C  
ANISOU 1817  CZ  PHE A 222     6686   5430   5511    219   -268    430       C  
ATOM   1818  N   ILE A 223      87.529 -19.397 -48.790  1.00 52.18           N  
ANISOU 1818  N   ILE A 223     7325   7073   5428    541    764    408       N  
ATOM   1819  CA  ILE A 223      88.184 -18.153 -48.405  1.00 51.91           C  
ANISOU 1819  CA  ILE A 223     6964   7125   5636    421    804    671       C  
ATOM   1820  C   ILE A 223      88.299 -17.217 -49.600  1.00 59.34           C  
ANISOU 1820  C   ILE A 223     7915   8292   6341    214    903    955       C  
ATOM   1821  O   ILE A 223      88.168 -15.994 -49.461  1.00 58.76           O  
ANISOU 1821  O   ILE A 223     7705   8138   6481     14    814   1245       O  
ATOM   1822  CB  ILE A 223      89.553 -18.471 -47.771  1.00 52.66           C  
ANISOU 1822  CB  ILE A 223     6761   7351   5897    618   1019    573       C  
ATOM   1823  CG1 ILE A 223      89.352 -19.074 -46.377  1.00 48.90           C  
ANISOU 1823  CG1 ILE A 223     6239   6648   5692    786    850    426       C  
ATOM   1824  CG2 ILE A 223      90.435 -17.234 -47.708  1.00 50.21           C  
ANISOU 1824  CG2 ILE A 223     6093   7213   5769    429   1124    808       C  
ATOM   1825  CD1 ILE A 223      90.638 -19.558 -45.731  1.00 48.46           C  
ANISOU 1825  CD1 ILE A 223     5890   6755   5766   1045   1007    342       C  
ATOM   1826  N   GLU A 224      88.509 -17.771 -50.793  1.00 61.13           N  
ANISOU 1826  N   GLU A 224     8326   8788   6114    260   1093    882       N  
ATOM   1827  CA  GLU A 224      88.566 -16.943 -51.992  1.00 61.04           C  
ANISOU 1827  CA  GLU A 224     8358   9055   5779     64   1192   1202       C  
ATOM   1828  C   GLU A 224      87.200 -16.359 -52.315  1.00 64.73           C  
ANISOU 1828  C   GLU A 224     9021   9394   6179   -104    849   1427       C  
ATOM   1829  O   GLU A 224      87.087 -15.163 -52.608  1.00 62.83           O  
ANISOU 1829  O   GLU A 224     8704   9151   6016   -284    799   1847       O  
ATOM   1830  CB  GLU A 224      89.091 -17.760 -53.170  1.00 73.01           C  
ANISOU 1830  CB  GLU A 224    10040  10957   6745    175   1490   1011       C  
ATOM   1831  CG  GLU A 224      89.225 -16.971 -54.458  1.00 91.06           C  
ANISOU 1831  CG  GLU A 224    12379  13628   8590    -23   1635   1373       C  
ATOM   1832  CD  GLU A 224      88.822 -17.778 -55.677  1.00109.11           C  
ANISOU 1832  CD  GLU A 224    15015  16239  10202     23   1682   1144       C  
ATOM   1833  OE1 GLU A 224      87.809 -17.424 -56.320  1.00114.80           O  
ANISOU 1833  OE1 GLU A 224    15952  17040  10627   -135   1410   1338       O  
ATOM   1834  OE2 GLU A 224      89.515 -18.771 -55.989  1.00113.92           O  
ANISOU 1834  OE2 GLU A 224    15675  17032  10577    232   1981    749       O  
ATOM   1835  N   ARG A 225      86.149 -17.182 -52.245  1.00 59.85           N  
ANISOU 1835  N   ARG A 225     8632   8650   5459    -47    606   1170       N  
ATOM   1836  CA  ARG A 225      84.824 -16.734 -52.659  1.00 65.17           C  
ANISOU 1836  CA  ARG A 225     9443   9292   6025   -184    265   1365       C  
ATOM   1837  C   ARG A 225      84.322 -15.587 -51.791  1.00 61.39           C  
ANISOU 1837  C   ARG A 225     8765   8500   6060   -254     59   1657       C  
ATOM   1838  O   ARG A 225      83.715 -14.635 -52.296  1.00 59.48           O  
ANISOU 1838  O   ARG A 225     8531   8271   5796   -357   -109   2034       O  
ATOM   1839  CB  ARG A 225      83.837 -17.899 -52.619  1.00 66.06           C  
ANISOU 1839  CB  ARG A 225     9774   9324   6003   -151     52    986       C  
ATOM   1840  CG  ARG A 225      82.382 -17.476 -52.794  1.00 65.06           C  
ANISOU 1840  CG  ARG A 225     9684   9165   5871   -282   -348   1158       C  
ATOM   1841  CD  ARG A 225      81.480 -18.678 -52.960  1.00 69.34           C  
ANISOU 1841  CD  ARG A 225    10427   9700   6218   -326   -537    764       C  
ATOM   1842  NE  ARG A 225      81.892 -19.487 -54.102  1.00 77.34           N  
ANISOU 1842  NE  ARG A 225    11700  11026   6661   -337   -385    494       N  
ATOM   1843  CZ  ARG A 225      81.268 -20.588 -54.500  1.00 81.82           C  
ANISOU 1843  CZ  ARG A 225    12497  11618   6974   -415   -509     79       C  
ATOM   1844  NH1 ARG A 225      80.196 -21.015 -53.846  1.00 87.15           N  
ANISOU 1844  NH1 ARG A 225    13147  12032   7936   -515   -786    -60       N  
ATOM   1845  NH2 ARG A 225      81.716 -21.262 -55.553  1.00 81.30           N  
ANISOU 1845  NH2 ARG A 225    12680  11842   6370   -412   -340   -220       N  
ATOM   1846  N   TYR A 226      84.553 -15.661 -50.482  1.00 56.05           N  
ANISOU 1846  N   TYR A 226     8633   6795   5870    845    710   1282       N  
ATOM   1847  CA  TYR A 226      84.101 -14.629 -49.563  1.00 57.57           C  
ANISOU 1847  CA  TYR A 226     8716   6864   6293    750    686   1352       C  
ATOM   1848  C   TYR A 226      85.198 -13.624 -49.229  1.00 57.36           C  
ANISOU 1848  C   TYR A 226     8613   6720   6463    704    888   1523       C  
ATOM   1849  O   TYR A 226      85.023 -12.809 -48.317  1.00 56.82           O  
ANISOU 1849  O   TYR A 226     8445   6525   6621    611    878   1554       O  
ATOM   1850  CB  TYR A 226      83.517 -15.279 -48.301  1.00 52.43           C  
ANISOU 1850  CB  TYR A 226     7973   6148   5801    615    536   1162       C  
ATOM   1851  CG  TYR A 226      82.205 -15.973 -48.619  1.00 55.11           C  
ANISOU 1851  CG  TYR A 226     8360   6580   6000    649    326   1026       C  
ATOM   1852  CD1 TYR A 226      82.175 -17.310 -49.001  1.00 46.52           C  
ANISOU 1852  CD1 TYR A 226     7336   5566   4774    667    248    859       C  
ATOM   1853  CD2 TYR A 226      81.002 -15.268 -48.604  1.00 53.13           C  
ANISOU 1853  CD2 TYR A 226     8087   6341   5760    670    205   1065       C  
ATOM   1854  CE1 TYR A 226      80.978 -17.934 -49.327  1.00 56.16           C  
ANISOU 1854  CE1 TYR A 226     8587   6861   5890    689     46    725       C  
ATOM   1855  CE2 TYR A 226      79.805 -15.884 -48.926  1.00 55.76           C  
ANISOU 1855  CE2 TYR A 226     8442   6764   5980    698      8    941       C  
ATOM   1856  CZ  TYR A 226      79.799 -17.217 -49.282  1.00 55.28           C  
ANISOU 1856  CZ  TYR A 226     8436   6768   5800    700    -75    767       C  
ATOM   1857  OH  TYR A 226      78.611 -17.828 -49.606  1.00 58.09           O  
ANISOU 1857  OH  TYR A 226     8799   7202   6071    716   -282    632       O  
ATOM   1858  N   LYS A 227      86.308 -13.651 -49.968  1.00 57.58           N  
ANISOU 1858  N   LYS A 227     8680   6785   6413    770   1072   1633       N  
ATOM   1859  CA  LYS A 227      87.377 -12.656 -49.873  1.00 58.80           C  
ANISOU 1859  CA  LYS A 227     8757   6833   6752    736   1281   1823       C  
ATOM   1860  C   LYS A 227      87.844 -12.479 -48.426  1.00 53.18           C  
ANISOU 1860  C   LYS A 227     7887   5966   6353    563   1274   1740       C  
ATOM   1861  O   LYS A 227      87.834 -11.383 -47.866  1.00 54.84           O  
ANISOU 1861  O   LYS A 227     8013   6042   6781    495   1302   1826       O  
ATOM   1862  CB  LYS A 227      86.920 -11.321 -50.474  1.00 63.94           C  
ANISOU 1862  CB  LYS A 227     9440   7452   7402    812   1336   2045       C  
ATOM   1863  CG  LYS A 227      86.216 -11.430 -51.831  1.00 72.24           C  
ANISOU 1863  CG  LYS A 227    10652   8676   8121   1003   1299   2118       C  
ATOM   1864  CD  LYS A 227      87.173 -11.248 -53.003  1.00 87.49           C  
ANISOU 1864  CD  LYS A 227    12658  10688   9896   1138   1526   2319       C  
ATOM   1865  CE  LYS A 227      86.422 -10.966 -54.312  1.00 91.93           C  
ANISOU 1865  CE  LYS A 227    13375  11409  10145   1347   1500   2446       C  
ATOM   1866  NZ  LYS A 227      85.618 -12.131 -54.792  1.00 95.86           N  
ANISOU 1866  NZ  LYS A 227    13985  12085  10351   1435   1294   2229       N  
ATOM   1867  N   LEU A 228      88.259 -13.589 -47.818  1.00 51.78           N  
ANISOU 1867  N   LEU A 228     7673   5808   6193    502   1231   1565       N  
ATOM   1868  CA  LEU A 228      88.626 -13.597 -46.410  1.00 50.05           C  
ANISOU 1868  CA  LEU A 228     7315   5474   6227    359   1195   1460       C  
ATOM   1869  C   LEU A 228      90.133 -13.695 -46.182  1.00 52.38           C  
ANISOU 1869  C   LEU A 228     7516   5729   6657    313   1357   1494       C  
ATOM   1870  O   LEU A 228      90.561 -13.928 -45.045  1.00 44.43           O  
ANISOU 1870  O   LEU A 228     6397   4657   5826    212   1319   1384       O  
ATOM   1871  CB  LEU A 228      87.901 -14.736 -45.688  1.00 42.76           C  
ANISOU 1871  CB  LEU A 228     6401   4588   5257    319   1016   1245       C  
ATOM   1872  CG  LEU A 228      86.406 -14.502 -45.460  1.00 45.65           C  
ANISOU 1872  CG  LEU A 228     6793   4958   5592    318    842   1196       C  
ATOM   1873  CD1 LEU A 228      85.682 -15.797 -45.038  1.00 47.19           C  
ANISOU 1873  CD1 LEU A 228     7010   5208   5712    294    685   1004       C  
ATOM   1874  CD2 LEU A 228      86.214 -13.442 -44.404  1.00 52.19           C  
ANISOU 1874  CD2 LEU A 228     7514   5659   6657    233    822   1220       C  
ATOM   1875  N   GLU A 229      90.944 -13.500 -47.222  1.00 52.57           N  
ANISOU 1875  N   GLU A 229     7573   5799   6602    394   1538   1650       N  
ATOM   1876  CA  GLU A 229      92.396 -13.541 -47.067  1.00 58.85           C  
ANISOU 1876  CA  GLU A 229     8257   6562   7541    354   1706   1700       C  
ATOM   1877  C   GLU A 229      92.852 -12.530 -46.020  1.00 58.41           C  
ANISOU 1877  C   GLU A 229     8032   6341   7818    214   1722   1726       C  
ATOM   1878  O   GLU A 229      92.408 -11.380 -46.013  1.00 55.71           O  
ANISOU 1878  O   GLU A 229     7677   5901   7590    190   1724   1831       O  
ATOM   1879  CB  GLU A 229      93.086 -13.250 -48.403  1.00 61.53           C  
ANISOU 1879  CB  GLU A 229     8652   6971   7757    471   1921   1908       C  
ATOM   1880  CG  GLU A 229      92.649 -14.137 -49.563  1.00 75.75           C  
ANISOU 1880  CG  GLU A 229    10635   8946   9202    636   1907   1885       C  
ATOM   1881  CD  GLU A 229      91.366 -13.660 -50.227  1.00 88.69           C  
ANISOU 1881  CD  GLU A 229    12404  10631  10664    721   1806   1940       C  
ATOM   1882  OE1 GLU A 229      90.730 -12.721 -49.703  1.00 92.01           O  
ANISOU 1882  OE1 GLU A 229    12776  10943  11240    650   1735   1982       O  
ATOM   1883  OE2 GLU A 229      90.995 -14.226 -51.277  1.00 94.06           O  
ANISOU 1883  OE2 GLU A 229    13235  11460  11045    870   1792   1932       O  
ATOM   1884  N   GLY A 230      93.728 -12.968 -45.120  1.00 58.26           N  
ANISOU 1884  N   GLY A 230     7886   6290   7958    130   1724   1619       N  
ATOM   1885  CA  GLY A 230      94.245 -12.086 -44.098  1.00 53.88           C  
ANISOU 1885  CA  GLY A 230     7164   5590   7718      2   1721   1610       C  
ATOM   1886  C   GLY A 230      93.448 -12.047 -42.811  1.00 51.42           C  
ANISOU 1886  C   GLY A 230     6821   5221   7495    -74   1519   1434       C  
ATOM   1887  O   GLY A 230      93.851 -11.344 -41.874  1.00 51.72           O  
ANISOU 1887  O   GLY A 230     6725   5144   7783   -172   1493   1392       O  
ATOM   1888  N   TYR A 231      92.327 -12.762 -42.730  1.00 42.00           N  
ANISOU 1888  N   TYR A 231     5742   4105   6112    -28   1376   1328       N  
ATOM   1889  CA  TYR A 231      91.565 -12.836 -41.492  1.00 43.65           C  
ANISOU 1889  CA  TYR A 231     5918   4278   6389    -86   1201   1170       C  
ATOM   1890  C   TYR A 231      91.834 -14.109 -40.715  1.00 42.19           C  
ANISOU 1890  C   TYR A 231     5707   4162   6160    -97   1129   1009       C  
ATOM   1891  O   TYR A 231      91.126 -14.383 -39.740  1.00 43.31           O  
ANISOU 1891  O   TYR A 231     5840   4301   6314   -124    991    885       O  
ATOM   1892  CB  TYR A 231      90.069 -12.704 -41.776  1.00 45.33           C  
ANISOU 1892  CB  TYR A 231     6246   4517   6462    -37   1088   1169       C  
ATOM   1893  CG  TYR A 231      89.725 -11.318 -42.249  1.00 48.51           C  
ANISOU 1893  CG  TYR A 231     6657   4827   6946    -27   1137   1319       C  
ATOM   1894  CD1 TYR A 231      89.663 -10.256 -41.353  1.00 50.72           C  
ANISOU 1894  CD1 TYR A 231     6844   4968   7458   -100   1101   1301       C  
ATOM   1895  CD2 TYR A 231      89.507 -11.058 -43.594  1.00 49.98           C  
ANISOU 1895  CD2 TYR A 231     6948   5062   6979     66   1224   1480       C  
ATOM   1896  CE1 TYR A 231      89.358  -8.963 -41.784  1.00 50.89           C  
ANISOU 1896  CE1 TYR A 231     6877   4882   7578    -88   1152   1445       C  
ATOM   1897  CE2 TYR A 231      89.201  -9.770 -44.033  1.00 54.66           C  
ANISOU 1897  CE2 TYR A 231     7552   5563   7654     87   1279   1641       C  
ATOM   1898  CZ  TYR A 231      89.129  -8.732 -43.123  1.00 51.54           C  
ANISOU 1898  CZ  TYR A 231     7062   5009   7510      5   1246   1625       C  
ATOM   1899  OH  TYR A 231      88.832  -7.460 -43.560  1.00 64.86           O  
ANISOU 1899  OH  TYR A 231     8764   6584   9296     30   1306   1788       O  
ATOM   1900  N   ALA A 232      92.816 -14.905 -41.142  1.00 44.94           N  
ANISOU 1900  N   ALA A 232     6048   4574   6454    -65   1228   1018       N  
ATOM   1901  CA  ALA A 232      93.265 -16.091 -40.405  1.00 44.65           C  
ANISOU 1901  CA  ALA A 232     5976   4590   6401    -68   1181    883       C  
ATOM   1902  C   ALA A 232      92.150 -17.118 -40.188  1.00 40.13           C  
ANISOU 1902  C   ALA A 232     5509   4073   5666    -36   1046    770       C  
ATOM   1903  O   ALA A 232      92.130 -17.817 -39.166  1.00 40.46           O  
ANISOU 1903  O   ALA A 232     5510   4121   5742    -58    964    655       O  
ATOM   1904  CB  ALA A 232      93.887 -15.701 -39.061  1.00 46.23           C  
ANISOU 1904  CB  ALA A 232     6017   4727   6822   -149   1134    805       C  
ATOM   1905  N   PHE A 233      91.220 -17.244 -41.143  1.00 41.31           N  
ANISOU 1905  N   PHE A 233     5789   4263   5643     20   1021    804       N  
ATOM   1906  CA  PHE A 233      90.192 -18.275 -41.013  1.00 40.54           C  
ANISOU 1906  CA  PHE A 233     5778   4210   5416     40    894    693       C  
ATOM   1907  C   PHE A 233      90.801 -19.670 -41.015  1.00 43.51           C  
ANISOU 1907  C   PHE A 233     6179   4630   5722     75    917    609       C  
ATOM   1908  O   PHE A 233      90.293 -20.564 -40.334  1.00 41.82           O  
ANISOU 1908  O   PHE A 233     5974   4415   5500     60    821    503       O  
ATOM   1909  CB  PHE A 233      89.155 -18.146 -42.127  1.00 47.58           C  
ANISOU 1909  CB  PHE A 233     6794   5147   6138     99    853    735       C  
ATOM   1910  CG  PHE A 233      87.938 -17.364 -41.721  1.00 49.13           C  
ANISOU 1910  CG  PHE A 233     6979   5307   6380     66    741    741       C  
ATOM   1911  CD1 PHE A 233      88.067 -16.202 -40.977  1.00 57.56           C  
ANISOU 1911  CD1 PHE A 233     7951   6293   7626     11    754    788       C  
ATOM   1912  CD2 PHE A 233      86.665 -17.794 -42.069  1.00 54.20           C  
ANISOU 1912  CD2 PHE A 233     7700   5995   6899     93    619    690       C  
ATOM   1913  CE1 PHE A 233      86.951 -15.477 -40.590  1.00 60.85           C  
ANISOU 1913  CE1 PHE A 233     8360   6676   8085     -4    658    790       C  
ATOM   1914  CE2 PHE A 233      85.544 -17.070 -41.690  1.00 48.14           C  
ANISOU 1914  CE2 PHE A 233     6909   5203   6180     72    522    702       C  
ATOM   1915  CZ  PHE A 233      85.690 -15.913 -40.950  1.00 54.93           C  
ANISOU 1915  CZ  PHE A 233     7683   5983   7206     30    547    754       C  
ATOM   1916  N   GLU A 234      91.899 -19.866 -41.752  1.00 46.38           N  
ANISOU 1916  N   GLU A 234     6549   5029   6045    128   1054    664       N  
ATOM   1917  CA  GLU A 234      92.569 -21.164 -41.767  1.00 48.63           C  
ANISOU 1917  CA  GLU A 234     6856   5349   6272    175   1088    586       C  
ATOM   1918  C   GLU A 234      92.863 -21.640 -40.351  1.00 51.06           C  
ANISOU 1918  C   GLU A 234     7061   5620   6718    122   1029    501       C  
ATOM   1919  O   GLU A 234      92.723 -22.828 -40.039  1.00 53.68           O  
ANISOU 1919  O   GLU A 234     7434   5958   7005    146    980    408       O  
ATOM   1920  CB  GLU A 234      93.864 -21.071 -42.580  1.00 49.03           C  
ANISOU 1920  CB  GLU A 234     6886   5440   6302    238   1265    676       C  
ATOM   1921  CG  GLU A 234      93.681 -20.629 -44.023  1.00 58.00           C  
ANISOU 1921  CG  GLU A 234     8131   6632   7275    318   1348    780       C  
ATOM   1922  CD  GLU A 234      93.766 -19.115 -44.204  1.00 72.07           C  
ANISOU 1922  CD  GLU A 234     9847   8375   9162    277   1419    937       C  
ATOM   1923  OE1 GLU A 234      93.553 -18.362 -43.227  1.00 63.41           O  
ANISOU 1923  OE1 GLU A 234     8648   7197   8248    179   1353    933       O  
ATOM   1924  OE2 GLU A 234      94.055 -18.682 -45.339  1.00 75.15           O  
ANISOU 1924  OE2 GLU A 234    10291   8811   9450    354   1547   1067       O  
ATOM   1925  N   HIS A 235      93.252 -20.710 -39.476  1.00 44.38           N  
ANISOU 1925  N   HIS A 235     6084   4735   6044     57   1028    530       N  
ATOM   1926  CA  HIS A 235      93.549 -21.003 -38.079  1.00 42.02           C  
ANISOU 1926  CA  HIS A 235     5682   4419   5864     22    964    453       C  
ATOM   1927  C   HIS A 235      92.274 -20.975 -37.236  1.00 38.06           C  
ANISOU 1927  C   HIS A 235     5202   3894   5365    -15    824    392       C  
ATOM   1928  O   HIS A 235      91.900 -21.979 -36.616  1.00 39.35           O  
ANISOU 1928  O   HIS A 235     5388   4067   5496      0    762    321       O  
ATOM   1929  CB  HIS A 235      94.590 -19.987 -37.582  1.00 38.44           C  
ANISOU 1929  CB  HIS A 235     5074   3939   5591    -25   1018    494       C  
ATOM   1930  CG  HIS A 235      94.902 -20.067 -36.121  1.00 45.81           C  
ANISOU 1930  CG  HIS A 235     5894   4870   6643    -52    935    408       C  
ATOM   1931  ND1 HIS A 235      95.928 -20.842 -35.616  1.00 43.60           N  
ANISOU 1931  ND1 HIS A 235     5539   4632   6397    -15    960    368       N  
ATOM   1932  CD2 HIS A 235      94.359 -19.424 -35.061  1.00 43.84           C  
ANISOU 1932  CD2 HIS A 235     5591   4590   6475    -96    828    355       C  
ATOM   1933  CE1 HIS A 235      95.983 -20.692 -34.303  1.00 44.96           C  
ANISOU 1933  CE1 HIS A 235     5620   4807   6655    -33    864    295       C  
ATOM   1934  NE2 HIS A 235      95.040 -19.836 -33.941  1.00 44.20           N  
ANISOU 1934  NE2 HIS A 235     5539   4669   6587    -81    785    281       N  
ATOM   1935  N   ILE A 236      91.558 -19.846 -37.260  1.00 38.20           N  
ANISOU 1935  N   ILE A 236     5214   3878   5422    -56    784    431       N  
ATOM   1936  CA  ILE A 236      90.474 -19.606 -36.303  1.00 36.06           C  
ANISOU 1936  CA  ILE A 236     4931   3588   5184    -87    665    380       C  
ATOM   1937  C   ILE A 236      89.308 -20.564 -36.532  1.00 37.90           C  
ANISOU 1937  C   ILE A 236     5263   3843   5296    -68    593    341       C  
ATOM   1938  O   ILE A 236      88.744 -21.117 -35.580  1.00 37.87           O  
ANISOU 1938  O   ILE A 236     5240   3841   5308    -75    522    285       O  
ATOM   1939  CB  ILE A 236      89.991 -18.144 -36.391  1.00 37.15           C  
ANISOU 1939  CB  ILE A 236     5044   3676   5395   -122    649    434       C  
ATOM   1940  CG1 ILE A 236      91.107 -17.156 -36.042  1.00 33.64           C  
ANISOU 1940  CG1 ILE A 236     4483   3183   5115   -158    707    458       C  
ATOM   1941  CG2 ILE A 236      88.768 -17.946 -35.507  1.00 34.10           C  
ANISOU 1941  CG2 ILE A 236     4655   3281   5021   -134    534    383       C  
ATOM   1942  CD1 ILE A 236      90.768 -15.710 -36.427  1.00 46.41           C  
ANISOU 1942  CD1 ILE A 236     6092   4724   6817   -188    722    535       C  
ATOM   1943  N   VAL A 237      88.875 -20.714 -37.778  1.00 37.33           N  
ANISOU 1943  N   VAL A 237     5290   3786   5106    -42    606    372       N  
ATOM   1944  CA  VAL A 237      87.663 -21.471 -38.070  1.00 38.25           C  
ANISOU 1944  CA  VAL A 237     5488   3916   5130    -37    515    325       C  
ATOM   1945  C   VAL A 237      87.975 -22.907 -38.477  1.00 40.83           C  
ANISOU 1945  C   VAL A 237     5883   4253   5377     -1    531    261       C  
ATOM   1946  O   VAL A 237      87.336 -23.841 -38.000  1.00 42.60           O  
ANISOU 1946  O   VAL A 237     6119   4458   5609    -16    464    197       O  
ATOM   1947  CB  VAL A 237      86.809 -20.757 -39.143  1.00 40.47           C  
ANISOU 1947  CB  VAL A 237     5837   4215   5323    -21    483    376       C  
ATOM   1948  CG1 VAL A 237      85.537 -21.551 -39.381  1.00 40.55           C  
ANISOU 1948  CG1 VAL A 237     5906   4242   5260    -23    369    310       C  
ATOM   1949  CG2 VAL A 237      86.472 -19.324 -38.704  1.00 37.13           C  
ANISOU 1949  CG2 VAL A 237     5350   3762   4998    -49    470    441       C  
ATOM   1950  N   TYR A 238      88.936 -23.106 -39.379  1.00 40.70           N  
ANISOU 1950  N   TYR A 238     5912   4262   5290     51    627    282       N  
ATOM   1951  CA  TYR A 238      89.216 -24.466 -39.852  1.00 37.26           C  
ANISOU 1951  CA  TYR A 238     5555   3829   4772    100    642    209       C  
ATOM   1952  C   TYR A 238      90.035 -25.282 -38.859  1.00 41.14           C  
ANISOU 1952  C   TYR A 238     5985   4294   5353    104    678    174       C  
ATOM   1953  O   TYR A 238      89.898 -26.514 -38.818  1.00 42.56           O  
ANISOU 1953  O   TYR A 238     6217   4442   5510    126    654    102       O  
ATOM   1954  CB  TYR A 238      89.941 -24.408 -41.196  1.00 39.91           C  
ANISOU 1954  CB  TYR A 238     5968   4214   4980    178    742    243       C  
ATOM   1955  CG  TYR A 238      89.061 -23.946 -42.331  1.00 48.61           C  
ANISOU 1955  CG  TYR A 238     7166   5359   5944    207    694    263       C  
ATOM   1956  CD1 TYR A 238      88.318 -24.862 -43.072  1.00 45.14           C  
ANISOU 1956  CD1 TYR A 238     6841   4934   5376    245    608    162       C  
ATOM   1957  CD2 TYR A 238      88.964 -22.597 -42.661  1.00 47.25           C  
ANISOU 1957  CD2 TYR A 238     6969   5208   5775    202    728    378       C  
ATOM   1958  CE1 TYR A 238      87.507 -24.449 -44.112  1.00 49.50           C  
ANISOU 1958  CE1 TYR A 238     7477   5543   5787    285    546    171       C  
ATOM   1959  CE2 TYR A 238      88.153 -22.172 -43.702  1.00 45.82           C  
ANISOU 1959  CE2 TYR A 238     6878   5077   5456    248    682    408       C  
ATOM   1960  CZ  TYR A 238      87.429 -23.105 -44.423  1.00 51.55           C  
ANISOU 1960  CZ  TYR A 238     7713   5838   6034    293    586    301       C  
ATOM   1961  OH  TYR A 238      86.619 -22.692 -45.450  1.00 50.36           O  
ANISOU 1961  OH  TYR A 238     7648   5754   5733    351    522    322       O  
ATOM   1962  N   GLY A 239      90.877 -24.633 -38.070  1.00 42.77           N  
ANISOU 1962  N   GLY A 239     6079   4507   5665     89    729    220       N  
ATOM   1963  CA  GLY A 239      91.763 -25.324 -37.143  1.00 41.94           C  
ANISOU 1963  CA  GLY A 239     5904   4397   5633    111    761    195       C  
ATOM   1964  C   GLY A 239      93.085 -25.715 -37.781  1.00 41.86           C  
ANISOU 1964  C   GLY A 239     5895   4415   5596    179    880    210       C  
ATOM   1965  O   GLY A 239      93.180 -26.003 -38.970  1.00 43.36           O  
ANISOU 1965  O   GLY A 239     6178   4620   5675    228    934    209       O  
ATOM   1966  N   ASP A 240      94.129 -25.725 -36.958  1.00 40.56           N  
ANISOU 1966  N   ASP A 240     5616   4266   5527    193    921    219       N  
ATOM   1967  CA  ASP A 240      95.487 -26.087 -37.364  1.00 40.77           C  
ANISOU 1967  CA  ASP A 240     5605   4327   5558    261   1038    238       C  
ATOM   1968  C   ASP A 240      95.892 -27.310 -36.545  1.00 40.10           C  
ANISOU 1968  C   ASP A 240     5505   4232   5499    318   1026    188       C  
ATOM   1969  O   ASP A 240      96.079 -27.213 -35.329  1.00 40.31           O  
ANISOU 1969  O   ASP A 240     5432   4268   5614    304    974    182       O  
ATOM   1970  CB  ASP A 240      96.446 -24.907 -37.139  1.00 44.63           C  
ANISOU 1970  CB  ASP A 240     5945   4846   6168    227   1097    303       C  
ATOM   1971  CG  ASP A 240      97.880 -25.196 -37.582  1.00 47.95           C  
ANISOU 1971  CG  ASP A 240     6297   5310   6613    294   1230    337       C  
ATOM   1972  OD1 ASP A 240      98.195 -26.347 -37.963  1.00 46.99           O  
ANISOU 1972  OD1 ASP A 240     6246   5198   6409    381   1278    305       O  
ATOM   1973  OD2 ASP A 240      98.705 -24.254 -37.543  1.00 46.54           O  
ANISOU 1973  OD2 ASP A 240     5985   5148   6550    259   1290    396       O  
ATOM   1974  N   PHE A 241      96.020 -28.462 -37.206  1.00 40.62           N  
ANISOU 1974  N   PHE A 241     5674   4277   5481    392   1070    150       N  
ATOM   1975  CA  PHE A 241      96.314 -29.718 -36.528  1.00 42.10           C  
ANISOU 1975  CA  PHE A 241     5869   4433   5695    456   1064    110       C  
ATOM   1976  C   PHE A 241      97.741 -30.178 -36.786  1.00 44.69           C  
ANISOU 1976  C   PHE A 241     6146   4801   6033    556   1180    124       C  
ATOM   1977  O   PHE A 241      98.038 -31.374 -36.671  1.00 42.29           O  
ANISOU 1977  O   PHE A 241     5889   4460   5718    638   1202     88       O  
ATOM   1978  CB  PHE A 241      95.311 -30.796 -36.955  1.00 40.64           C  
ANISOU 1978  CB  PHE A 241     5836   4164   5441    465   1014     42       C  
ATOM   1979  CG  PHE A 241      93.874 -30.417 -36.695  1.00 37.65           C  
ANISOU 1979  CG  PHE A 241     5489   3749   5065    369    900     32       C  
ATOM   1980  CD1 PHE A 241      93.200 -29.552 -37.556  1.00 43.72           C  
ANISOU 1980  CD1 PHE A 241     6303   4542   5767    319    873     37       C  
ATOM   1981  CD2 PHE A 241      93.198 -30.908 -35.583  1.00 38.84           C  
ANISOU 1981  CD2 PHE A 241     5619   3851   5286    340    830     31       C  
ATOM   1982  CE1 PHE A 241      91.879 -29.191 -37.311  1.00 48.59           C  
ANISOU 1982  CE1 PHE A 241     6935   5133   6394    239    768     30       C  
ATOM   1983  CE2 PHE A 241      91.872 -30.547 -35.333  1.00 49.49           C  
ANISOU 1983  CE2 PHE A 241     6982   5176   6648    257    737     30       C  
ATOM   1984  CZ  PHE A 241      91.217 -29.687 -36.192  1.00 42.33           C  
ANISOU 1984  CZ  PHE A 241     6111   4293   5681    206    702     24       C  
ATOM   1985  N   SER A 242      98.634 -29.249 -37.128  1.00 40.19           N  
ANISOU 1985  N   SER A 242     5473   4299   5498    551   1259    181       N  
ATOM   1986  CA  SER A 242      99.982 -29.616 -37.539  1.00 45.51           C  
ANISOU 1986  CA  SER A 242     6088   5022   6183    647   1387    204       C  
ATOM   1987  C   SER A 242     100.959 -29.697 -36.375  1.00 42.96           C  
ANISOU 1987  C   SER A 242     5596   4740   5986    676   1378    217       C  
ATOM   1988  O   SER A 242     102.007 -30.331 -36.512  1.00 47.74           O  
ANISOU 1988  O   SER A 242     6154   5379   6605    776   1466    225       O  
ATOM   1989  CB  SER A 242     100.505 -28.622 -38.586  1.00 50.69           C  
ANISOU 1989  CB  SER A 242     6704   5732   6822    635   1500    277       C  
ATOM   1990  OG  SER A 242     100.698 -27.339 -38.021  1.00 49.29           O  
ANISOU 1990  OG  SER A 242     6378   5575   6776    537   1474    331       O  
ATOM   1991  N   HIS A 243     100.643 -29.090 -35.236  1.00 40.90           N  
ANISOU 1991  N   HIS A 243     5245   4486   5809    603   1269    214       N  
ATOM   1992  CA  HIS A 243     101.528 -29.076 -34.080  1.00 42.90           C  
ANISOU 1992  CA  HIS A 243     5334   4796   6168    636   1234    214       C  
ATOM   1993  C   HIS A 243     100.861 -29.780 -32.910  1.00 45.66           C  
ANISOU 1993  C   HIS A 243     5725   5122   6501    662   1126    182       C  
ATOM   1994  O   HIS A 243      99.660 -30.058 -32.928  1.00 42.67           O  
ANISOU 1994  O   HIS A 243     5475   4677   6059    624   1074    166       O  
ATOM   1995  CB  HIS A 243     101.905 -27.644 -33.693  1.00 44.30           C  
ANISOU 1995  CB  HIS A 243     5347   5016   6467    543   1200    230       C  
ATOM   1996  CG  HIS A 243     102.458 -26.858 -34.836  1.00 62.86           C  
ANISOU 1996  CG  HIS A 243     7655   7376   8854    506   1321    289       C  
ATOM   1997  ND1 HIS A 243     103.606 -27.231 -35.498  1.00 66.41           N  
ANISOU 1997  ND1 HIS A 243     8042   7871   9321    584   1457    330       N  
ATOM   1998  CD2 HIS A 243     102.002 -25.749 -35.462  1.00 67.44           C  
ANISOU 1998  CD2 HIS A 243     8249   7924   9449    412   1340    330       C  
ATOM   1999  CE1 HIS A 243     103.848 -26.371 -36.471  1.00 70.36           C  
ANISOU 1999  CE1 HIS A 243     8515   8372   9846    537   1562    400       C  
ATOM   2000  NE2 HIS A 243     102.889 -25.463 -36.472  1.00 69.10           N  
ANISOU 2000  NE2 HIS A 243     8405   8162   9687    433   1492    405       N  
ATOM   2001  N   SER A 244     101.669 -30.069 -31.886  1.00 43.27           N  
ANISOU 2001  N   SER A 244     5302   4882   6257    734   1095    181       N  
ATOM   2002  CA  SER A 244     101.156 -30.782 -30.721  1.00 44.68           C  
ANISOU 2002  CA  SER A 244     5513   5052   6409    787   1010    175       C  
ATOM   2003  C   SER A 244     100.023 -30.008 -30.058  1.00 40.80           C  
ANISOU 2003  C   SER A 244     5040   4552   5909    694    903    160       C  
ATOM   2004  O   SER A 244      99.057 -30.610 -29.577  1.00 40.51           O  
ANISOU 2004  O   SER A 244     5100   4469   5823    704    863    170       O  
ATOM   2005  CB  SER A 244     102.277 -31.051 -29.719  1.00 43.92           C  
ANISOU 2005  CB  SER A 244     5270   5052   6365    892    984    179       C  
ATOM   2006  OG  SER A 244     102.765 -29.835 -29.193  1.00 50.87           O  
ANISOU 2006  OG  SER A 244     5985   6016   7328    834    915    150       O  
ATOM   2007  N   GLN A 245     100.117 -28.676 -30.014  1.00 35.45           N  
ANISOU 2007  N   GLN A 245     4266   3912   5291    606    863    139       N  
ATOM   2008  CA  GLN A 245      98.992 -27.878 -29.539  1.00 35.61           C  
ANISOU 2008  CA  GLN A 245     4315   3914   5300    522    773    120       C  
ATOM   2009  C   GLN A 245      98.108 -27.515 -30.725  1.00 35.47           C  
ANISOU 2009  C   GLN A 245     4413   3818   5246    433    812    135       C  
ATOM   2010  O   GLN A 245      98.577 -26.952 -31.722  1.00 38.23           O  
ANISOU 2010  O   GLN A 245     4744   4161   5623    393    882    152       O  
ATOM   2011  CB  GLN A 245      99.442 -26.609 -28.798  1.00 41.68           C  
ANISOU 2011  CB  GLN A 245     4931   4747   6160    479    693     75       C  
ATOM   2012  CG  GLN A 245      98.660 -26.373 -27.484  1.00 62.51           C  
ANISOU 2012  CG  GLN A 245     7568   7421   8762    495    574     39       C  
ATOM   2013  CD  GLN A 245      98.159 -24.935 -27.275  1.00 76.33           C  
ANISOU 2013  CD  GLN A 245     9275   9160  10568    399    500    -10       C  
ATOM   2014  OE1 GLN A 245      98.248 -24.085 -28.161  1.00 79.60           O  
ANISOU 2014  OE1 GLN A 245     9673   9520  11053    308    540     -4       O  
ATOM   2015  NE2 GLN A 245      97.623 -24.672 -26.088  1.00 75.84           N  
ANISOU 2015  NE2 GLN A 245     9199   9146  10470    434    400    -55       N  
ATOM   2016  N   LEU A 246      96.830 -27.856 -30.611  1.00 36.09           N  
ANISOU 2016  N   LEU A 246     4605   3846   5263    409    769    137       N  
ATOM   2017  CA  LEU A 246      95.852 -27.571 -31.646  1.00 35.06           C  
ANISOU 2017  CA  LEU A 246     4583   3651   5086    334    780    143       C  
ATOM   2018  C   LEU A 246      95.647 -26.062 -31.766  1.00 37.95           C  
ANISOU 2018  C   LEU A 246     4890   4028   5500    248    748    144       C  
ATOM   2019  O   LEU A 246      95.372 -25.382 -30.777  1.00 40.92           O  
ANISOU 2019  O   LEU A 246     5199   4430   5919    227    670    122       O  
ATOM   2020  CB  LEU A 246      94.542 -28.284 -31.303  1.00 36.34           C  
ANISOU 2020  CB  LEU A 246     4845   3761   5202    326    728    142       C  
ATOM   2021  CG  LEU A 246      93.504 -28.565 -32.391  1.00 49.07           C  
ANISOU 2021  CG  LEU A 246     6586   5301   6756    276    729    134       C  
ATOM   2022  CD1 LEU A 246      92.540 -29.670 -31.939  1.00 44.01           C  
ANISOU 2022  CD1 LEU A 246     6016   4596   6110    284    695    134       C  
ATOM   2023  CD2 LEU A 246      92.728 -27.308 -32.738  1.00 47.04           C  
ANISOU 2023  CD2 LEU A 246     6326   5051   6497    192    683    139       C  
ATOM   2024  N   GLY A 247      95.790 -25.537 -32.982  1.00 37.97           N  
ANISOU 2024  N   GLY A 247     4922   4010   5493    211    813    171       N  
ATOM   2025  CA  GLY A 247      95.647 -24.109 -33.216  1.00 39.06           C  
ANISOU 2025  CA  GLY A 247     5010   4138   5692    134    801    191       C  
ATOM   2026  C   GLY A 247      94.225 -23.754 -33.598  1.00 41.91           C  
ANISOU 2026  C   GLY A 247     5474   4457   5992     85    750    199       C  
ATOM   2027  O   GLY A 247      93.616 -24.416 -34.441  1.00 39.94           O  
ANISOU 2027  O   GLY A 247     5344   4188   5646     98    766    205       O  
ATOM   2028  N   GLY A 248      93.701 -22.702 -32.966  1.00 36.97           N  
ANISOU 2028  N   GLY A 248     4798   3821   5428     35    680    189       N  
ATOM   2029  CA  GLY A 248      92.390 -22.174 -33.330  1.00 34.60           C  
ANISOU 2029  CA  GLY A 248     4574   3487   5087     -8    632    205       C  
ATOM   2030  C   GLY A 248      91.246 -23.131 -33.031  1.00 35.12           C  
ANISOU 2030  C   GLY A 248     4721   3549   5074      8    573    182       C  
ATOM   2031  O   GLY A 248      91.183 -23.776 -31.970  1.00 37.24           O  
ANISOU 2031  O   GLY A 248     4962   3838   5351     40    538    154       O  
ATOM   2032  N   LEU A 249      90.329 -23.221 -34.002  1.00 37.82           N  
ANISOU 2032  N   LEU A 249     5160   3867   5344    -12    564    200       N  
ATOM   2033  CA  LEU A 249      89.102 -24.018 -33.939  1.00 36.12           C  
ANISOU 2033  CA  LEU A 249     5012   3634   5078    -18    502    180       C  
ATOM   2034  C   LEU A 249      88.138 -23.482 -32.867  1.00 39.40           C  
ANISOU 2034  C   LEU A 249     5377   4056   5539    -40    428    178       C  
ATOM   2035  O   LEU A 249      87.816 -24.145 -31.885  1.00 37.27           O  
ANISOU 2035  O   LEU A 249     5084   3794   5283    -20    404    167       O  
ATOM   2036  CB  LEU A 249      89.413 -25.506 -33.717  1.00 39.78           C  
ANISOU 2036  CB  LEU A 249     5510   4084   5523     23    524    152       C  
ATOM   2037  CG  LEU A 249      88.307 -26.471 -34.161  1.00 41.70           C  
ANISOU 2037  CG  LEU A 249     5838   4280   5725      6    480    126       C  
ATOM   2038  CD1 LEU A 249      88.191 -26.550 -35.685  1.00 43.52           C  
ANISOU 2038  CD1 LEU A 249     6166   4501   5867      6    487    104       C  
ATOM   2039  CD2 LEU A 249      88.544 -27.868 -33.576  1.00 44.52           C  
ANISOU 2039  CD2 LEU A 249     6209   4598   6109     43    500    110       C  
ATOM   2040  N   HIS A 250      87.619 -22.272 -33.119  1.00 34.79           N  
ANISOU 2040  N   HIS A 250     4780   3466   4971    -70    399    198       N  
ATOM   2041  CA  HIS A 250      86.796 -21.550 -32.146  1.00 34.77           C  
ANISOU 2041  CA  HIS A 250     4725   3472   5013    -78    338    192       C  
ATOM   2042  C   HIS A 250      85.341 -21.386 -32.558  1.00 37.94           C  
ANISOU 2042  C   HIS A 250     5165   3865   5385   -100    282    211       C  
ATOM   2043  O   HIS A 250      84.554 -20.823 -31.790  1.00 37.31           O  
ANISOU 2043  O   HIS A 250     5043   3797   5338    -96    238    210       O  
ATOM   2044  CB  HIS A 250      87.421 -20.170 -31.888  1.00 33.94           C  
ANISOU 2044  CB  HIS A 250     4555   3357   4985    -86    344    189       C  
ATOM   2045  CG  HIS A 250      88.793 -20.269 -31.302  1.00 34.83           C  
ANISOU 2045  CG  HIS A 250     4598   3487   5148    -67    378    156       C  
ATOM   2046  ND1 HIS A 250      89.020 -20.796 -30.050  1.00 36.50           N  
ANISOU 2046  ND1 HIS A 250     4761   3746   5364    -22    349    113       N  
ATOM   2047  CD2 HIS A 250      90.011 -19.946 -31.802  1.00 37.21           C  
ANISOU 2047  CD2 HIS A 250     4862   3775   5500    -79    438    167       C  
ATOM   2048  CE1 HIS A 250      90.318 -20.780 -29.796  1.00 40.24           C  
ANISOU 2048  CE1 HIS A 250     5167   4237   5885     -6    375     86       C  
ATOM   2049  NE2 HIS A 250      90.942 -20.268 -30.844  1.00 35.82           N  
ANISOU 2049  NE2 HIS A 250     4606   3638   5365    -47    432    119       N  
ATOM   2050  N  ALEU A 251      84.965 -21.840 -33.745  0.38 35.95           N  
ANISOU 2050  N  ALEU A 251     4990   3602   5069   -114    277    221       N  
ATOM   2051  N  BLEU A 251      84.965 -21.858 -33.740  0.62 35.98           N  
ANISOU 2051  N  BLEU A 251     4993   3605   5073   -114    277    221       N  
ATOM   2052  CA ALEU A 251      83.598 -21.740 -34.236  0.38 37.87           C  
ANISOU 2052  CA ALEU A 251     5260   3846   5284   -134    208    231       C  
ATOM   2053  CA BLEU A 251      83.608 -21.747 -34.256  0.62 37.72           C  
ANISOU 2053  CA BLEU A 251     5241   3826   5264   -134    209    231       C  
ATOM   2054  C  ALEU A 251      83.019 -23.133 -34.393  0.38 39.98           C  
ANISOU 2054  C  ALEU A 251     5560   4100   5530   -149    177    197       C  
ATOM   2055  C  BLEU A 251      83.017 -23.138 -34.403  0.62 40.19           C  
ANISOU 2055  C  BLEU A 251     5587   4126   5556   -150    177    197       C  
ATOM   2056  O  ALEU A 251      83.663 -24.007 -34.980  0.38 41.29           O  
ANISOU 2056  O  ALEU A 251     5784   4249   5656   -141    209    168       O  
ATOM   2057  O  BLEU A 251      83.653 -24.017 -34.990  0.62 41.49           O  
ANISOU 2057  O  BLEU A 251     5810   4274   5680   -141    208    168       O  
ATOM   2058  CB ALEU A 251      83.545 -21.008 -35.573  0.38 41.45           C  
ANISOU 2058  CB ALEU A 251     5772   4302   5674   -128    207    265       C  
ATOM   2059  CB BLEU A 251      83.596 -21.040 -35.611  0.62 41.42           C  
ANISOU 2059  CB BLEU A 251     5772   4299   5668   -128    210    264       C  
ATOM   2060  CG ALEU A 251      83.137 -19.550 -35.453  0.38 45.51           C  
ANISOU 2060  CG ALEU A 251     6250   4809   6232   -124    191    312       C  
ATOM   2061  CG BLEU A 251      83.433 -19.528 -35.595  0.62 44.13           C  
ANISOU 2061  CG BLEU A 251     6083   4633   6053   -122    210    316       C  
ATOM   2062  CD1ALEU A 251      84.307 -18.721 -34.943  0.38 51.43           C  
ANISOU 2062  CD1ALEU A 251     6950   5531   7060   -123    258    325       C  
ATOM   2063  CD1BLEU A 251      82.064 -19.135 -35.029  0.62 35.36           C  
ANISOU 2063  CD1BLEU A 251     4930   3531   4976   -126    130    317       C  
ATOM   2064  CD2ALEU A 251      82.626 -19.045 -36.790  0.38 49.21           C  
ANISOU 2064  CD2ALEU A 251     6786   5291   6620   -106    169    360       C  
ATOM   2065  CD2BLEU A 251      84.561 -18.878 -34.806  0.62 47.85           C  
ANISOU 2065  CD2BLEU A 251     6490   5078   6612   -123    269    316       C  
ATOM   2066  N   LEU A 252      81.796 -23.329 -33.892  1.00 33.90           N  
ANISOU 2066  N   LEU A 252     4749   3331   4801   -172    119    201       N  
ATOM   2067  CA  LEU A 252      81.198 -24.661 -33.920  1.00 33.16           C  
ANISOU 2067  CA  LEU A 252     4666   3203   4730   -202     91    173       C  
ATOM   2068  C   LEU A 252      81.137 -25.224 -35.341  1.00 39.14           C  
ANISOU 2068  C   LEU A 252     5512   3941   5418   -215     50    119       C  
ATOM   2069  O   LEU A 252      81.445 -26.403 -35.554  1.00 39.90           O  
ANISOU 2069  O   LEU A 252     5653   3989   5520   -221     62     72       O  
ATOM   2070  CB  LEU A 252      79.806 -24.628 -33.282  1.00 33.78           C  
ANISOU 2070  CB  LEU A 252     4667   3290   4878   -229     39    199       C  
ATOM   2071  CG  LEU A 252      79.167 -26.024 -33.201  1.00 41.52           C  
ANISOU 2071  CG  LEU A 252     5637   4214   5926   -275     19    180       C  
ATOM   2072  CD1 LEU A 252      80.016 -26.947 -32.323  1.00 46.36           C  
ANISOU 2072  CD1 LEU A 252     6251   4790   6573   -250    102    198       C  
ATOM   2073  CD2 LEU A 252      77.752 -25.951 -32.671  1.00 42.46           C  
ANISOU 2073  CD2 LEU A 252     5659   4345   6128   -307    -24    219       C  
ATOM   2074  N   ILE A 253      80.786 -24.397 -36.336  1.00 36.92           N  
ANISOU 2074  N   ILE A 253     5266   3697   5064   -205      4    123       N  
ATOM   2075  CA  ILE A 253      80.715 -24.916 -37.706  1.00 40.42           C  
ANISOU 2075  CA  ILE A 253     5803   4144   5411   -195    -44     63       C  
ATOM   2076  C   ILE A 253      82.052 -25.520 -38.149  1.00 38.47           C  
ANISOU 2076  C   ILE A 253     5634   3879   5102   -156     40     33       C  
ATOM   2077  O   ILE A 253      82.081 -26.484 -38.923  1.00 40.71           O  
ANISOU 2077  O   ILE A 253     5994   4141   5334   -146     11    -47       O  
ATOM   2078  CB  ILE A 253      80.220 -23.825 -38.686  1.00 38.24           C  
ANISOU 2078  CB  ILE A 253     5556   3929   5043   -164    -96     94       C  
ATOM   2079  CG1 ILE A 253      79.860 -24.448 -40.040  1.00 41.22           C  
ANISOU 2079  CG1 ILE A 253     6026   4330   5306   -143   -179     15       C  
ATOM   2080  CG2 ILE A 253      81.250 -22.691 -38.864  1.00 37.09           C  
ANISOU 2080  CG2 ILE A 253     5431   3807   4854   -117      0    172       C  
ATOM   2081  CD1 ILE A 253      79.125 -23.505 -40.985  1.00 41.59           C  
ANISOU 2081  CD1 ILE A 253     6097   4452   5253   -101   -256     48       C  
ATOM   2082  N   GLY A 254      83.172 -24.998 -37.654  1.00 38.61           N  
ANISOU 2082  N   GLY A 254     5628   3907   5135   -129    140     85       N  
ATOM   2083  CA  GLY A 254      84.457 -25.565 -38.034  1.00 36.20           C  
ANISOU 2083  CA  GLY A 254     5378   3594   4784    -85    227     65       C  
ATOM   2084  C   GLY A 254      84.677 -26.934 -37.413  1.00 40.39           C  
ANISOU 2084  C   GLY A 254     5908   4063   5377    -92    240     14       C  
ATOM   2085  O   GLY A 254      85.242 -27.833 -38.044  1.00 39.40           O  
ANISOU 2085  O   GLY A 254     5858   3912   5202    -56    269    -43       O  
ATOM   2086  N   LEU A 255      84.230 -27.106 -36.166  1.00 38.01           N  
ANISOU 2086  N   LEU A 255     5525   3736   5180   -125    227     40       N  
ATOM   2087  CA  LEU A 255      84.219 -28.427 -35.554  1.00 41.46           C  
ANISOU 2087  CA  LEU A 255     5960   4102   5689   -132    238     14       C  
ATOM   2088  C   LEU A 255      83.303 -29.372 -36.317  1.00 41.40           C  
ANISOU 2088  C   LEU A 255     6010   4030   5690   -171    159    -64       C  
ATOM   2089  O   LEU A 255      83.645 -30.538 -36.530  1.00 39.11           O  
ANISOU 2089  O   LEU A 255     5775   3665   5420   -158    176   -120       O  
ATOM   2090  CB  LEU A 255      83.776 -28.332 -34.095  1.00 42.74           C  
ANISOU 2090  CB  LEU A 255     6025   4268   5948   -148    245     77       C  
ATOM   2091  CG  LEU A 255      84.759 -27.797 -33.052  1.00 41.19           C  
ANISOU 2091  CG  LEU A 255     5769   4122   5761    -98    312    126       C  
ATOM   2092  CD1 LEU A 255      84.831 -26.272 -33.075  1.00 39.88           C  
ANISOU 2092  CD1 LEU A 255     5563   4021   5569   -100    299    148       C  
ATOM   2093  CD2 LEU A 255      84.350 -28.293 -31.672  1.00 44.21           C  
ANISOU 2093  CD2 LEU A 255     6086   4496   6216    -87    325    176       C  
ATOM   2094  N   ALA A 256      82.131 -28.883 -36.734  1.00 41.54           N  
ANISOU 2094  N   ALA A 256     6009   4071   5701   -216     64    -75       N  
ATOM   2095  CA  ALA A 256      81.195 -29.725 -37.478  1.00 47.48           C  
ANISOU 2095  CA  ALA A 256     6799   4768   6475   -260    -37   -167       C  
ATOM   2096  C   ALA A 256      81.821 -30.234 -38.769  1.00 44.98           C  
ANISOU 2096  C   ALA A 256     6608   4443   6038   -209    -46   -268       C  
ATOM   2097  O   ALA A 256      81.691 -31.420 -39.108  1.00 44.31           O  
ANISOU 2097  O   ALA A 256     6574   4268   5993   -224    -83   -366       O  
ATOM   2098  CB  ALA A 256      79.906 -28.949 -37.769  1.00 40.20           C  
ANISOU 2098  CB  ALA A 256     5824   3899   5552   -302   -144   -159       C  
ATOM   2099  N   LYS A 257      82.522 -29.358 -39.494  1.00 45.61           N  
ANISOU 2099  N   LYS A 257     6740   4613   5976   -143     -5   -244       N  
ATOM   2100  CA  LYS A 257      83.130 -29.766 -40.757  1.00 47.45           C  
ANISOU 2100  CA  LYS A 257     7098   4863   6067    -72      2   -329       C  
ATOM   2101  C   LYS A 257      84.216 -30.812 -40.529  1.00 50.23           C  
ANISOU 2101  C   LYS A 257     7492   5144   6448    -30     96   -364       C  
ATOM   2102  O   LYS A 257      84.296 -31.813 -41.253  1.00 49.42           O  
ANISOU 2102  O   LYS A 257     7482   4988   6306      1     66   -482       O  
ATOM   2103  CB  LYS A 257      83.698 -28.547 -41.488  1.00 44.16           C  
ANISOU 2103  CB  LYS A 257     6715   4558   5505     -3     57   -258       C  
ATOM   2104  CG  LYS A 257      84.170 -28.835 -42.920  1.00 44.63           C  
ANISOU 2104  CG  LYS A 257     6909   4668   5381     92     65   -332       C  
ATOM   2105  CD  LYS A 257      84.714 -27.563 -43.574  1.00 48.43           C  
ANISOU 2105  CD  LYS A 257     7411   5257   5733    160    145   -222       C  
ATOM   2106  CE  LYS A 257      85.283 -27.821 -44.967  1.00 48.99           C  
ANISOU 2106  CE  LYS A 257     7617   5397   5599    279    182   -272       C  
ATOM   2107  NZ  LYS A 257      84.235 -28.134 -45.980  1.00 49.00           N  
ANISOU 2107  NZ  LYS A 257     7707   5440   5473    309     27   -387       N  
ATOM   2108  N   ARG A 258      85.059 -30.601 -39.518  1.00 47.60           N  
ANISOU 2108  N   ARG A 258     7092   4811   6184    -20    203   -272       N  
ATOM   2109  CA  ARG A 258      86.099 -31.579 -39.209  1.00 47.79           C  
ANISOU 2109  CA  ARG A 258     7142   4774   6242     30    292   -292       C  
ATOM   2110  C   ARG A 258      85.493 -32.901 -38.767  1.00 48.28           C  
ANISOU 2110  C   ARG A 258     7211   4702   6430    -13    244   -355       C  
ATOM   2111  O   ARG A 258      85.968 -33.975 -39.158  1.00 49.98           O  
ANISOU 2111  O   ARG A 258     7505   4839   6647     32    267   -436       O  
ATOM   2112  CB  ARG A 258      87.012 -31.027 -38.119  1.00 46.43           C  
ANISOU 2112  CB  ARG A 258     6876   4642   6125     49    391   -182       C  
ATOM   2113  CG  ARG A 258      88.029 -32.019 -37.599  1.00 54.57           C  
ANISOU 2113  CG  ARG A 258     7910   5618   7207    107    476   -184       C  
ATOM   2114  CD  ARG A 258      89.374 -31.738 -38.193  1.00 54.67           C  
ANISOU 2114  CD  ARG A 258     7944   5697   7131    193    578   -173       C  
ATOM   2115  NE  ARG A 258      90.383 -32.714 -37.800  1.00 50.84           N  
ANISOU 2115  NE  ARG A 258     7463   5167   6688    266    659   -180       N  
ATOM   2116  CZ  ARG A 258      91.502 -32.909 -38.487  1.00 54.83           C  
ANISOU 2116  CZ  ARG A 258     8007   5705   7121    358    751   -198       C  
ATOM   2117  NH1 ARG A 258      91.716 -32.199 -39.584  1.00 55.55           N  
ANISOU 2117  NH1 ARG A 258     8140   5874   7090    384    779   -202       N  
ATOM   2118  NH2 ARG A 258      92.394 -33.810 -38.093  1.00 49.27           N  
ANISOU 2118  NH2 ARG A 258     7298   4959   6461    434    822   -202       N  
ATOM   2119  N   PHE A 259      84.425 -32.838 -37.965  1.00 47.30           N  
ANISOU 2119  N   PHE A 259     7003   4545   6424    -99    183   -313       N  
ATOM   2120  CA  PHE A 259      83.861 -34.040 -37.355  1.00 50.72           C  
ANISOU 2120  CA  PHE A 259     7416   4840   7014   -149    162   -334       C  
ATOM   2121  C   PHE A 259      83.276 -34.990 -38.396  1.00 57.67           C  
ANISOU 2121  C   PHE A 259     8383   5622   7909   -176     65   -487       C  
ATOM   2122  O   PHE A 259      83.383 -36.217 -38.258  1.00 55.82           O  
ANISOU 2122  O   PHE A 259     8183   5245   7781   -179     79   -539       O  
ATOM   2123  CB  PHE A 259      82.799 -33.641 -36.326  1.00 49.67           C  
ANISOU 2123  CB  PHE A 259     7163   4713   6996   -228    131   -241       C  
ATOM   2124  CG  PHE A 259      82.194 -34.807 -35.598  1.00 64.09           C  
ANISOU 2124  CG  PHE A 259     8950   6398   9003   -282    134   -224       C  
ATOM   2125  CD1 PHE A 259      82.902 -35.457 -34.594  1.00 70.58           C  
ANISOU 2125  CD1 PHE A 259     9756   7166   9895   -234    241   -141       C  
ATOM   2126  CD2 PHE A 259      80.918 -35.249 -35.909  1.00 62.51           C  
ANISOU 2126  CD2 PHE A 259     8719   6118   8913   -378     31   -281       C  
ATOM   2127  CE1 PHE A 259      82.351 -36.537 -33.920  1.00 75.87           C  
ANISOU 2127  CE1 PHE A 259    10392   7696  10741   -276    262    -99       C  
ATOM   2128  CE2 PHE A 259      80.357 -36.324 -35.236  1.00 75.63           C  
ANISOU 2128  CE2 PHE A 259    10331   7632  10771   -437     48   -249       C  
ATOM   2129  CZ  PHE A 259      81.075 -36.970 -34.243  1.00 73.91           C  
ANISOU 2129  CZ  PHE A 259    10109   7352  10620   -384    172   -150       C  
ATOM   2130  N   LYS A 260      82.644 -34.452 -39.441  1.00 61.95           N  
ANISOU 2130  N   LYS A 260     8961   6232   8347   -190    -41   -565       N  
ATOM   2131  CA  LYS A 260      82.056 -35.321 -40.458  1.00 69.80           C  
ANISOU 2131  CA  LYS A 260    10034   7144   9342   -210   -160   -737       C  
ATOM   2132  C   LYS A 260      83.116 -36.100 -41.225  1.00 69.82           C  
ANISOU 2132  C   LYS A 260    10173   7105   9250   -108   -109   -845       C  
ATOM   2133  O   LYS A 260      82.816 -37.163 -41.779  1.00 73.35           O  
ANISOU 2133  O   LYS A 260    10690   7431   9748   -119   -185   -999       O  
ATOM   2134  CB  LYS A 260      81.182 -34.508 -41.420  1.00 74.19           C  
ANISOU 2134  CB  LYS A 260    10599   7810   9779   -224   -293   -795       C  
ATOM   2135  CG  LYS A 260      81.940 -33.565 -42.339  1.00 86.30           C  
ANISOU 2135  CG  LYS A 260    12217   9498  11074   -113   -252   -781       C  
ATOM   2136  CD  LYS A 260      81.033 -32.947 -43.411  1.00 95.17           C  
ANISOU 2136  CD  LYS A 260    13370  10724  12067   -106   -396   -849       C  
ATOM   2137  CE  LYS A 260      79.937 -32.070 -42.808  1.00 97.17           C  
ANISOU 2137  CE  LYS A 260    13490  11023  12407   -190   -461   -751       C  
ATOM   2138  NZ  LYS A 260      79.162 -31.318 -43.846  1.00 93.48           N  
ANISOU 2138  NZ  LYS A 260    13048  10677  11794   -158   -591   -791       N  
ATOM   2139  N   GLU A 261      84.348 -35.609 -41.245  1.00 59.42           N  
ANISOU 2139  N   GLU A 261     8886   5878   7811    -10     20   -772       N  
ATOM   2140  CA  GLU A 261      85.449 -36.291 -41.905  1.00 69.13           C  
ANISOU 2140  CA  GLU A 261    10233   7085   8948    105     94   -854       C  
ATOM   2141  C   GLU A 261      86.317 -37.092 -40.942  1.00 65.25           C  
ANISOU 2141  C   GLU A 261     9717   6493   8584    135    214   -793       C  
ATOM   2142  O   GLU A 261      86.827 -38.150 -41.320  1.00 62.30           O  
ANISOU 2142  O   GLU A 261     9434   6017   8220    201    241   -895       O  
ATOM   2143  CB  GLU A 261      86.313 -35.265 -42.652  1.00 85.61           C  
ANISOU 2143  CB  GLU A 261    12361   9343  10822    206    173   -805       C  
ATOM   2144  CG  GLU A 261      87.818 -35.389 -42.435  1.00 98.50           C  
ANISOU 2144  CG  GLU A 261    14003  11000  12423    309    339   -742       C  
ATOM   2145  CD  GLU A 261      88.549 -34.063 -42.610  1.00107.92           C  
ANISOU 2145  CD  GLU A 261    15154  12354  13499    355    435   -614       C  
ATOM   2146  OE1 GLU A 261      87.870 -33.017 -42.719  1.00114.55           O  
ANISOU 2146  OE1 GLU A 261    15952  13271  14300    301    378   -558       O  
ATOM   2147  OE2 GLU A 261      89.801 -34.066 -42.633  1.00106.97           O  
ANISOU 2147  OE2 GLU A 261    15031  12272  13339    443    569   -567       O  
ATOM   2148  N   SER A 262      86.462 -36.640 -39.694  1.00 55.70           N  
ANISOU 2148  N   SER A 262     8389   5306   7468    100    280   -636       N  
ATOM   2149  CA  SER A 262      87.456 -37.174 -38.781  1.00 53.04           C  
ANISOU 2149  CA  SER A 262     8023   4923   7208    159    401   -555       C  
ATOM   2150  C   SER A 262      87.021 -36.954 -37.336  1.00 47.20           C  
ANISOU 2150  C   SER A 262     7157   4173   6604     93    416   -415       C  
ATOM   2151  O   SER A 262      86.727 -35.812 -36.965  1.00 55.09           O  
ANISOU 2151  O   SER A 262     8076   5287   7567     55    400   -335       O  
ATOM   2152  CB  SER A 262      88.799 -36.491 -39.041  1.00 61.71           C  
ANISOU 2152  CB  SER A 262     9123   6156   8170    264    511   -505       C  
ATOM   2153  OG  SER A 262      89.833 -37.086 -38.288  1.00 67.84           O  
ANISOU 2153  OG  SER A 262     9872   6895   9009    339    617   -446       O  
ATOM   2154  N   PRO A 263      86.978 -37.991 -36.508  1.00 49.82           N  
ANISOU 2154  N   PRO A 263     7473   4371   7085     91    451   -377       N  
ATOM   2155  CA  PRO A 263      86.434 -37.833 -35.156  1.00 53.04           C  
ANISOU 2155  CA  PRO A 263     7768   4776   7607     40    468   -238       C  
ATOM   2156  C   PRO A 263      87.436 -37.227 -34.184  1.00 54.99           C  
ANISOU 2156  C   PRO A 263     7944   5144   7804    121    559   -115       C  
ATOM   2157  O   PRO A 263      88.653 -37.294 -34.365  1.00 49.03           O  
ANISOU 2157  O   PRO A 263     7216   4431   6980    218    628   -123       O  
ATOM   2158  CB  PRO A 263      86.092 -39.269 -34.755  1.00 60.63           C  
ANISOU 2158  CB  PRO A 263     8752   5537   8746     24    485   -239       C  
ATOM   2159  CG  PRO A 263      87.118 -40.089 -35.486  1.00 56.44           C  
ANISOU 2159  CG  PRO A 263     8334   4936   8176    122    530   -337       C  
ATOM   2160  CD  PRO A 263      87.312 -39.398 -36.810  1.00 54.90           C  
ANISOU 2160  CD  PRO A 263     8206   4846   7806    138    476   -462       C  
ATOM   2161  N   PHE A 264      86.896 -36.625 -33.130  1.00 44.01           N  
ANISOU 2161  N   PHE A 264     6454   3816   6451     84    554     -7       N  
ATOM   2162  CA  PHE A 264      87.734 -36.099 -32.067  1.00 45.28           C  
ANISOU 2162  CA  PHE A 264     6541   4089   6574    161    619     96       C  
ATOM   2163  C   PHE A 264      86.947 -36.120 -30.766  1.00 49.15           C  
ANISOU 2163  C   PHE A 264     6950   4580   7144    140    627    213       C  
ATOM   2164  O   PHE A 264      85.726 -36.294 -30.751  1.00 45.60           O  
ANISOU 2164  O   PHE A 264     6483   4065   6777     52    584    222       O  
ATOM   2165  CB  PHE A 264      88.250 -34.696 -32.395  1.00 45.15           C  
ANISOU 2165  CB  PHE A 264     6489   4227   6439    167    604     80       C  
ATOM   2166  CG  PHE A 264      87.181 -33.745 -32.847  1.00 40.12           C  
ANISOU 2166  CG  PHE A 264     5836   3631   5776     74    523     55       C  
ATOM   2167  CD1 PHE A 264      86.422 -33.042 -31.926  1.00 47.96           C  
ANISOU 2167  CD1 PHE A 264     6744   4681   6798     37    495    126       C  
ATOM   2168  CD2 PHE A 264      86.924 -33.566 -34.201  1.00 48.28           C  
ANISOU 2168  CD2 PHE A 264     6943   4656   6746     39    474    -39       C  
ATOM   2169  CE1 PHE A 264      85.431 -32.166 -32.346  1.00 53.26           C  
ANISOU 2169  CE1 PHE A 264     7396   5389   7450    -37    422    107       C  
ATOM   2170  CE2 PHE A 264      85.937 -32.693 -34.628  1.00 54.30           C  
ANISOU 2170  CE2 PHE A 264     7689   5463   7479    -32    394    -53       C  
ATOM   2171  CZ  PHE A 264      85.190 -31.992 -33.700  1.00 54.28           C  
ANISOU 2171  CZ  PHE A 264     7595   5507   7522    -73    369     22       C  
ATOM   2172  N   GLU A 265      87.673 -35.964 -29.665  1.00 37.58           N  
ANISOU 2172  N   GLU A 265     5428   3199   5652    232    682    303       N  
ATOM   2173  CA  GLU A 265      87.106 -36.013 -28.326  1.00 40.89           C  
ANISOU 2173  CA  GLU A 265     5777   3646   6114    253    708    427       C  
ATOM   2174  C   GLU A 265      87.029 -34.606 -27.762  1.00 44.48           C  
ANISOU 2174  C   GLU A 265     6153   4266   6480    257    671    442       C  
ATOM   2175  O   GLU A 265      87.990 -33.834 -27.885  1.00 44.65           O  
ANISOU 2175  O   GLU A 265     6157   4389   6419    299    660    397       O  
ATOM   2176  CB  GLU A 265      87.950 -36.905 -27.420  1.00 46.32           C  
ANISOU 2176  CB  GLU A 265     6465   4317   6819    379    791    519       C  
ATOM   2177  CG  GLU A 265      87.936 -38.348 -27.884  1.00 68.85           C  
ANISOU 2177  CG  GLU A 265     9396   6976   9786    379    835    514       C  
ATOM   2178  CD  GLU A 265      86.857 -39.169 -27.218  1.00 78.74           C  
ANISOU 2178  CD  GLU A 265    10632   8105  11179    341    873    625       C  
ATOM   2179  OE1 GLU A 265      86.173 -38.628 -26.320  1.00 72.74           O  
ANISOU 2179  OE1 GLU A 265     9797   7434  10406    334    879    721       O  
ATOM   2180  OE2 GLU A 265      86.702 -40.354 -27.590  1.00 84.71           O  
ANISOU 2180  OE2 GLU A 265    11448   8671  12065    321    904    618       O  
ATOM   2181  N   LEU A 266      85.877 -34.274 -27.164  1.00 37.40           N  
ANISOU 2181  N   LEU A 266     5206   3390   5615    212    655    501       N  
ATOM   2182  CA  LEU A 266      85.650 -32.991 -26.498  1.00 38.70           C  
ANISOU 2182  CA  LEU A 266     5299   3699   5706    227    621    514       C  
ATOM   2183  C   LEU A 266      85.289 -33.284 -25.051  1.00 48.51           C  
ANISOU 2183  C   LEU A 266     6489   4990   6952    309    676    641       C  
ATOM   2184  O   LEU A 266      84.226 -33.851 -24.779  1.00 51.24           O  
ANISOU 2184  O   LEU A 266     6818   5266   7383    269    708    720       O  
ATOM   2185  CB  LEU A 266      84.531 -32.199 -27.165  1.00 43.41           C  
ANISOU 2185  CB  LEU A 266     5883   4294   6319    118    554    468       C  
ATOM   2186  CG  LEU A 266      84.612 -31.634 -28.580  1.00 46.79           C  
ANISOU 2186  CG  LEU A 266     6357   4704   6716     45    491    358       C  
ATOM   2187  CD1 LEU A 266      83.342 -30.850 -28.850  1.00 51.42           C  
ANISOU 2187  CD1 LEU A 266     6908   5311   7318    -34    427    350       C  
ATOM   2188  CD2 LEU A 266      85.828 -30.742 -28.767  1.00 44.85           C  
ANISOU 2188  CD2 LEU A 266     6110   4548   6384     92    489    310       C  
ATOM   2189  N  AGLU A 267      86.170 -32.934 -24.121  0.71 36.73           N  
ANISOU 2189  N  AGLU A 267     4965   3620   5369    428    689    664       N  
ATOM   2190  N  BGLU A 267      86.172 -32.899 -24.132  0.29 36.71           N  
ANISOU 2190  N  BGLU A 267     4962   3620   5365    427    687    661       N  
ATOM   2191  CA AGLU A 267      85.858 -33.079 -22.705  0.71 37.01           C  
ANISOU 2191  CA AGLU A 267     4956   3738   5366    534    737    782       C  
ATOM   2192  CA BGLU A 267      85.917 -33.020 -22.700  0.29 38.98           C  
ANISOU 2192  CA BGLU A 267     5206   3996   5610    537    733    776       C  
ATOM   2193  C  AGLU A 267      85.220 -31.776 -22.242  0.71 41.91           C  
ANISOU 2193  C  AGLU A 267     5522   4480   5923    528    686    752       C  
ATOM   2194  C  BGLU A 267      85.214 -31.740 -22.261  0.29 40.30           C  
ANISOU 2194  C  BGLU A 267     5317   4277   5718    526    684    749       C  
ATOM   2195  O  AGLU A 267      85.853 -30.714 -22.281  0.71 34.60           O  
ANISOU 2195  O  AGLU A 267     4575   3646   4926    544    620    654       O  
ATOM   2196  O  BGLU A 267      85.797 -30.653 -22.325  0.29 34.61           O  
ANISOU 2196  O  BGLU A 267     4576   3646   4929    537    617    649       O  
ATOM   2197  CB AGLU A 267      87.099 -33.423 -21.880  0.71 43.36           C  
ANISOU 2197  CB AGLU A 267     5756   4627   6092    687    763    815       C  
ATOM   2198  CB BGLU A 267      87.224 -33.233 -21.936  0.29 46.59           C  
ANISOU 2198  CB BGLU A 267     6161   5052   6489    685    749    793       C  
ATOM   2199  CG AGLU A 267      86.990 -33.088 -20.389  0.71 53.84           C  
ANISOU 2199  CG AGLU A 267     7035   6111   7312    827    778    896       C  
ATOM   2200  CG BGLU A 267      87.297 -34.491 -21.076  0.29 60.69           C  
ANISOU 2200  CG BGLU A 267     7963   6805   8290    799    843    945       C  
ATOM   2201  CD AGLU A 267      86.175 -34.096 -19.582  0.71 69.48           C  
ANISOU 2201  CD AGLU A 267     9021   8050   9330    886    886   1077       C  
ATOM   2202  CD BGLU A 267      86.543 -34.360 -19.759  0.29 68.22           C  
ANISOU 2202  CD BGLU A 267     8875   7863   9181    892    888   1068       C  
ATOM   2203  OE1AGLU A 267      85.940 -35.220 -20.082  0.71 71.42           O  
ANISOU 2203  OE1AGLU A 267     9306   8130   9702    831    949   1143       O  
ATOM   2204  OE1BGLU A 267      85.670 -35.213 -19.479  0.29 71.68           O  
ANISOU 2204  OE1BGLU A 267     9320   8210   9704    882    978   1207       O  
ATOM   2205  OE2AGLU A 267      85.777 -33.764 -18.435  0.71 67.90           O  
ANISOU 2205  OE2AGLU A 267     8783   7981   9036    994    911   1154       O  
ATOM   2206  OE2BGLU A 267      86.825 -33.406 -19.001  0.29 69.01           O  
ANISOU 2206  OE2BGLU A 267     8933   8135   9152    980    836   1026       O  
ATOM   2207  N   ASP A 268      83.950 -31.861 -21.850  1.00 38.43           N  
ANISOU 2207  N   ASP A 268     5051   4027   5524    502    721    836       N  
ATOM   2208  CA  ASP A 268      83.144 -30.707 -21.439  1.00 34.82           C  
ANISOU 2208  CA  ASP A 268     4542   3670   5019    501    685    817       C  
ATOM   2209  C   ASP A 268      83.355 -30.525 -19.938  1.00 43.60           C  
ANISOU 2209  C   ASP A 268     5622   4934   6012    669    723    885       C  
ATOM   2210  O   ASP A 268      82.577 -31.009 -19.116  1.00 37.60           O  
ANISOU 2210  O   ASP A 268     4836   4197   5254    729    806   1020       O  
ATOM   2211  CB  ASP A 268      81.681 -30.976 -21.793  1.00 40.15           C  
ANISOU 2211  CB  ASP A 268     5187   4260   5807    397    710    878       C  
ATOM   2212  CG  ASP A 268      80.765 -29.778 -21.577  1.00 42.87           C  
ANISOU 2212  CG  ASP A 268     5477   4694   6119    388    671    852       C  
ATOM   2213  OD1 ASP A 268      81.218 -28.698 -21.135  1.00 42.55           O  
ANISOU 2213  OD1 ASP A 268     5429   4769   5970    460    624    779       O  
ATOM   2214  OD2 ASP A 268      79.556 -29.924 -21.873  1.00 47.79           O  
ANISOU 2214  OD2 ASP A 268     6058   5262   6839    305    684    899       O  
ATOM   2215  N   PHE A 269      84.445 -29.828 -19.563  1.00 36.81           N  
ANISOU 2215  N   PHE A 269     4759   4183   5044    755    661    792       N  
ATOM   2216  CA  PHE A 269      84.867 -29.925 -18.163  1.00 36.84           C  
ANISOU 2216  CA  PHE A 269     4746   4334   4919    938    687    849       C  
ATOM   2217  C   PHE A 269      84.106 -28.980 -17.233  1.00 34.07           C  
ANISOU 2217  C   PHE A 269     4356   4118   4472   1019    675    844       C  
ATOM   2218  O   PHE A 269      84.186 -29.158 -16.010  1.00 39.41           O  
ANISOU 2218  O   PHE A 269     5024   4925   5025   1188    713    915       O  
ATOM   2219  CB  PHE A 269      86.397 -29.738 -18.010  1.00 36.56           C  
ANISOU 2219  CB  PHE A 269     4709   4371   4812   1016    619    753       C  
ATOM   2220  CG  PHE A 269      86.947 -28.469 -18.617  1.00 37.08           C  
ANISOU 2220  CG  PHE A 269     4751   4453   4887    942    508    577       C  
ATOM   2221  CD1 PHE A 269      87.489 -28.474 -19.894  1.00 40.69           C  
ANISOU 2221  CD1 PHE A 269     5225   4798   5437    816    486    510       C  
ATOM   2222  CD2 PHE A 269      86.956 -27.284 -17.899  1.00 43.38           C  
ANISOU 2222  CD2 PHE A 269     5509   5374   5601   1006    432    480       C  
ATOM   2223  CE1 PHE A 269      88.013 -27.312 -20.456  1.00 38.36           C  
ANISOU 2223  CE1 PHE A 269     4902   4509   5164    748    404    374       C  
ATOM   2224  CE2 PHE A 269      87.470 -26.112 -18.456  1.00 44.60           C  
ANISOU 2224  CE2 PHE A 269     5635   5516   5794    930    337    326       C  
ATOM   2225  CZ  PHE A 269      87.998 -26.129 -19.740  1.00 39.18           C  
ANISOU 2225  CZ  PHE A 269     4961   4714   5213    798    330    286       C  
ATOM   2226  N   ILE A 270      83.331 -28.039 -17.767  1.00 32.84           N  
ANISOU 2226  N   ILE A 270     4181   3935   4361    919    630    770       N  
ATOM   2227  CA  ILE A 270      82.346 -27.280 -16.991  1.00 35.38           C  
ANISOU 2227  CA  ILE A 270     4468   4359   4618    988    642    785       C  
ATOM   2228  C   ILE A 270      80.984 -27.500 -17.643  1.00 40.34           C  
ANISOU 2228  C   ILE A 270     5071   4883   5373    863    695    865       C  
ATOM   2229  O   ILE A 270      80.558 -26.684 -18.479  1.00 37.84           O  
ANISOU 2229  O   ILE A 270     4744   4514   5118    753    629    776       O  
ATOM   2230  CB  ILE A 270      82.658 -25.772 -16.945  1.00 39.71           C  
ANISOU 2230  CB  ILE A 270     5002   4976   5108   1002    528    608       C  
ATOM   2231  CG1 ILE A 270      84.134 -25.501 -16.673  1.00 48.69           C  
ANISOU 2231  CG1 ILE A 270     6146   6176   6178   1069    444    490       C  
ATOM   2232  CG2 ILE A 270      81.797 -25.077 -15.893  1.00 41.54           C  
ANISOU 2232  CG2 ILE A 270     5208   5338   5240   1128    546    617       C  
ATOM   2233  CD1 ILE A 270      84.499 -24.038 -16.903  1.00 48.71           C  
ANISOU 2233  CD1 ILE A 270     6130   6189   6190   1034    326    306       C  
ATOM   2234  N   PRO A 271      80.279 -28.563 -17.309  1.00 34.86           N  
ANISOU 2234  N   PRO A 271     4359   4154   4732    874    809   1034       N  
ATOM   2235  CA  PRO A 271      79.085 -28.921 -18.084  1.00 37.35           C  
ANISOU 2235  CA  PRO A 271     4637   4346   5209    728    842   1098       C  
ATOM   2236  C   PRO A 271      77.854 -28.133 -17.672  1.00 33.90           C  
ANISOU 2236  C   PRO A 271     4131   3987   4761    752    864   1126       C  
ATOM   2237  O   PRO A 271      77.072 -28.552 -16.815  1.00 40.33           O  
ANISOU 2237  O   PRO A 271     4896   4857   5573    830    977   1277       O  
ATOM   2238  CB  PRO A 271      78.925 -30.421 -17.806  1.00 41.17           C  
ANISOU 2238  CB  PRO A 271     5119   4747   5778    733    962   1272       C  
ATOM   2239  CG  PRO A 271      79.536 -30.617 -16.448  1.00 42.99           C  
ANISOU 2239  CG  PRO A 271     5366   5121   5850    938   1028   1355       C  
ATOM   2240  CD  PRO A 271      80.676 -29.625 -16.366  1.00 36.13           C  
ANISOU 2240  CD  PRO A 271     4534   4357   4836   1006    907   1178       C  
ATOM   2241  N   MET A 272      77.684 -26.973 -18.293  1.00 37.56           N  
ANISOU 2241  N   MET A 272     4592   4456   5224    693    763    989       N  
ATOM   2242  CA  MET A 272      76.524 -26.125 -18.073  1.00 37.03           C  
ANISOU 2242  CA  MET A 272     4460   4448   5160    710    769    996       C  
ATOM   2243  C   MET A 272      76.203 -25.429 -19.383  1.00 33.65           C  
ANISOU 2243  C   MET A 272     4031   3929   4824    564    665    888       C  
ATOM   2244  O   MET A 272      76.978 -25.465 -20.340  1.00 41.87           O  
ANISOU 2244  O   MET A 272     5130   4886   5895    472    591    800       O  
ATOM   2245  CB  MET A 272      76.788 -25.087 -16.982  1.00 40.12           C  
ANISOU 2245  CB  MET A 272     4860   5001   5382    884    754    928       C  
ATOM   2246  CG  MET A 272      78.017 -24.250 -17.281  1.00 44.30           C  
ANISOU 2246  CG  MET A 272     5451   5532   5848    885    631    747       C  
ATOM   2247  SD  MET A 272      78.409 -23.135 -15.927  1.00 46.25           S  
ANISOU 2247  SD  MET A 272     5707   5958   5907   1093    593    639       S  
ATOM   2248  CE  MET A 272      77.110 -21.917 -16.112  1.00 52.22           C  
ANISOU 2248  CE  MET A 272     6419   6720   6705   1083    576    596       C  
ATOM   2249  N   ASP A 273      75.059 -24.765 -19.407  1.00 31.91           N  
ANISOU 2249  N   ASP A 273     3746   3740   4640    558    664    902       N  
ATOM   2250  CA  ASP A 273      74.682 -23.980 -20.567  1.00 32.20           C  
ANISOU 2250  CA  ASP A 273     3780   3712   4744    449    564    811       C  
ATOM   2251  C   ASP A 273      75.394 -22.632 -20.483  1.00 38.15           C  
ANISOU 2251  C   ASP A 273     4584   4511   5400    514    485    670       C  
ATOM   2252  O   ASP A 273      75.241 -21.916 -19.489  1.00 40.58           O  
ANISOU 2252  O   ASP A 273     4876   4922   5620    646    505    650       O  
ATOM   2253  CB  ASP A 273      73.173 -23.781 -20.580  1.00 33.38           C  
ANISOU 2253  CB  ASP A 273     3826   3881   4976    432    593    885       C  
ATOM   2254  CG  ASP A 273      72.636 -23.433 -21.958  1.00 41.87           C  
ANISOU 2254  CG  ASP A 273     4886   4871   6150    298    492    829       C  
ATOM   2255  OD1 ASP A 273      73.315 -23.742 -22.961  1.00 40.77           O  
ANISOU 2255  OD1 ASP A 273     4816   4641   6034    200    425    764       O  
ATOM   2256  OD2 ASP A 273      71.518 -22.875 -22.033  1.00 39.06           O  
ANISOU 2256  OD2 ASP A 273     4449   4549   5842    303    484    854       O  
ATOM   2257  N   SER A 274      76.163 -22.281 -21.505  1.00 34.24           N  
ANISOU 2257  N   SER A 274     4148   3936   4926    427    400    573       N  
ATOM   2258  CA  SER A 274      76.738 -20.934 -21.520  1.00 37.39           C  
ANISOU 2258  CA  SER A 274     4580   4350   5276    467    329    449       C  
ATOM   2259  C   SER A 274      77.018 -20.508 -22.954  1.00 33.83           C  
ANISOU 2259  C   SER A 274     4170   3796   4889    347    254    392       C  
ATOM   2260  O   SER A 274      77.184 -21.335 -23.851  1.00 37.38           O  
ANISOU 2260  O   SER A 274     4644   4176   5383    250    251    419       O  
ATOM   2261  CB  SER A 274      78.005 -20.834 -20.656  1.00 44.60           C  
ANISOU 2261  CB  SER A 274     5529   5320   6096    561    323    379       C  
ATOM   2262  OG  SER A 274      78.979 -21.769 -21.047  1.00 45.22           O  
ANISOU 2262  OG  SER A 274     5646   5352   6184    507    330    390       O  
ATOM   2263  N   THR A 275      77.051 -19.187 -23.148  1.00 32.97           N  
ANISOU 2263  N   THR A 275     4070   3675   4781    365    200    315       N  
ATOM   2264  CA  THR A 275      77.262 -18.609 -24.477  1.00 28.89           C  
ANISOU 2264  CA  THR A 275     3592   3068   4316    273    141    281       C  
ATOM   2265  C   THR A 275      78.573 -19.073 -25.113  1.00 29.76           C  
ANISOU 2265  C   THR A 275     3759   3125   4423    210    136    250       C  
ATOM   2266  O   THR A 275      78.626 -19.389 -26.311  1.00 33.77           O  
ANISOU 2266  O   THR A 275     4302   3573   4956    124    119    268       O  
ATOM   2267  CB  THR A 275      77.232 -17.089 -24.352  1.00 32.38           C  
ANISOU 2267  CB  THR A 275     4036   3496   4771    323     99    210       C  
ATOM   2268  OG1 THR A 275      75.892 -16.685 -24.033  1.00 35.76           O  
ANISOU 2268  OG1 THR A 275     4412   3966   5210    377    106    248       O  
ATOM   2269  CG2 THR A 275      77.715 -16.429 -25.634  1.00 33.78           C  
ANISOU 2269  CG2 THR A 275     4260   3578   4997    243     56    188       C  
ATOM   2270  N   VAL A 276      79.653 -19.062 -24.353  1.00 32.72           N  
ANISOU 2270  N   VAL A 276     4140   3530   4762    261    144    196       N  
ATOM   2271  CA  VAL A 276      80.929 -19.619 -24.791  1.00 33.82           C  
ANISOU 2271  CA  VAL A 276     4314   3635   4900    219    151    174       C  
ATOM   2272  C   VAL A 276      81.111 -20.950 -24.071  1.00 31.43           C  
ANISOU 2272  C   VAL A 276     4006   3382   4555    259    203    226       C  
ATOM   2273  O   VAL A 276      80.862 -21.041 -22.861  1.00 31.97           O  
ANISOU 2273  O   VAL A 276     4043   3533   4572    357    225    239       O  
ATOM   2274  CB  VAL A 276      82.098 -18.656 -24.484  1.00 35.89           C  
ANISOU 2274  CB  VAL A 276     4570   3892   5175    245    116     76       C  
ATOM   2275  CG1 VAL A 276      83.458 -19.311 -24.831  1.00 35.21           C  
ANISOU 2275  CG1 VAL A 276     4499   3789   5092    213    134     62       C  
ATOM   2276  CG2 VAL A 276      81.930 -17.330 -25.220  1.00 33.13           C  
ANISOU 2276  CG2 VAL A 276     4227   3468   4891    202     79     43       C  
ATOM   2277  N   LYS A 277      81.516 -21.987 -24.805  1.00 31.88           N  
ANISOU 2277  N   LYS A 277     4098   3387   4628    198    228    260       N  
ATOM   2278  CA  LYS A 277      81.783 -23.300 -24.219  1.00 34.61           C  
ANISOU 2278  CA  LYS A 277     4446   3753   4952    235    283    317       C  
ATOM   2279  C   LYS A 277      83.275 -23.599 -24.304  1.00 35.66           C  
ANISOU 2279  C   LYS A 277     4602   3881   5066    251    286    273       C  
ATOM   2280  O   LYS A 277      83.926 -23.271 -25.297  1.00 40.43           O  
ANISOU 2280  O   LYS A 277     5232   4432   5696    189    266    228       O  
ATOM   2281  CB  LYS A 277      80.987 -24.408 -24.918  1.00 35.29           C  
ANISOU 2281  CB  LYS A 277     4548   3767   5092    160    311    388       C  
ATOM   2282  CG  LYS A 277      79.471 -24.410 -24.615  1.00 37.37           C  
ANISOU 2282  CG  LYS A 277     4759   4046   5394    152    322    455       C  
ATOM   2283  CD  LYS A 277      79.156 -24.747 -23.145  1.00 37.26           C  
ANISOU 2283  CD  LYS A 277     4698   4116   5344    260    390    530       C  
ATOM   2284  CE  LYS A 277      79.704 -26.113 -22.734  1.00 34.65           C  
ANISOU 2284  CE  LYS A 277     4386   3762   5017    287    458    601       C  
ATOM   2285  NZ  LYS A 277      79.477 -26.388 -21.263  1.00 37.65           N  
ANISOU 2285  NZ  LYS A 277     4728   4242   5337    418    535    692       N  
ATOM   2286  N   ASN A 278      83.818 -24.224 -23.265  1.00 34.25           N  
ANISOU 2286  N   ASN A 278     4408   3766   4839    344    317    296       N  
ATOM   2287  CA  ASN A 278      85.240 -24.545 -23.220  1.00 33.65           C  
ANISOU 2287  CA  ASN A 278     4336   3703   4747    377    317    258       C  
ATOM   2288  C   ASN A 278      85.422 -26.048 -23.200  1.00 31.52           C  
ANISOU 2288  C   ASN A 278     4098   3400   4480    396    382    341       C  
ATOM   2289  O   ASN A 278      84.837 -26.729 -22.354  1.00 35.74           O  
ANISOU 2289  O   ASN A 278     4624   3966   4990    460    429    427       O  
ATOM   2290  CB  ASN A 278      85.887 -23.921 -22.002  1.00 30.77           C  
ANISOU 2290  CB  ASN A 278     3923   3449   4318    488    277    198       C  
ATOM   2291  CG  ASN A 278      85.647 -22.431 -21.965  1.00 57.26           C  
ANISOU 2291  CG  ASN A 278     7251   6814   7691    471    210    105       C  
ATOM   2292  OD1 ASN A 278      86.293 -21.680 -22.687  1.00 44.50           O  
ANISOU 2292  OD1 ASN A 278     5625   5144   6136    403    174     36       O  
ATOM   2293  ND2 ASN A 278      84.648 -22.007 -21.195  1.00 66.57           N  
ANISOU 2293  ND2 ASN A 278     8418   8049   8828    531    206    115       N  
ATOM   2294  N   TYR A 279      86.276 -26.552 -24.096  1.00 32.10           N  
ANISOU 2294  N   TYR A 279     4204   3409   4583    353    395    321       N  
ATOM   2295  CA  TYR A 279      86.491 -27.983 -24.227  1.00 33.26           C  
ANISOU 2295  CA  TYR A 279     4391   3497   4750    369    456    386       C  
ATOM   2296  C   TYR A 279      87.973 -28.301 -24.179  1.00 33.77           C  
ANISOU 2296  C   TYR A 279     4449   3589   4795    431    466    356       C  
ATOM   2297  O   TYR A 279      88.797 -27.567 -24.733  1.00 33.57           O  
ANISOU 2297  O   TYR A 279     4404   3575   4776    402    435    280       O  
ATOM   2298  CB  TYR A 279      85.934 -28.526 -25.550  1.00 34.06           C  
ANISOU 2298  CB  TYR A 279     4551   3475   4913    259    466    385       C  
ATOM   2299  CG  TYR A 279      84.456 -28.305 -25.734  1.00 34.69           C  
ANISOU 2299  CG  TYR A 279     4624   3525   5030    189    446    412       C  
ATOM   2300  CD1 TYR A 279      83.530 -29.039 -25.000  1.00 39.71           C  
ANISOU 2300  CD1 TYR A 279     5238   4148   5703    207    488    505       C  
ATOM   2301  CD2 TYR A 279      83.982 -27.374 -26.647  1.00 34.70           C  
ANISOU 2301  CD2 TYR A 279     4632   3514   5037    111    391    357       C  
ATOM   2302  CE1 TYR A 279      82.172 -28.852 -25.168  1.00 36.32           C  
ANISOU 2302  CE1 TYR A 279     4780   3695   5325    141    472    533       C  
ATOM   2303  CE2 TYR A 279      82.609 -27.173 -26.815  1.00 34.71           C  
ANISOU 2303  CE2 TYR A 279     4614   3497   5076     56    365    382       C  
ATOM   2304  CZ  TYR A 279      81.721 -27.930 -26.079  1.00 40.47           C  
ANISOU 2304  CZ  TYR A 279     5309   4216   5852     67    403    465       C  
ATOM   2305  OH  TYR A 279      80.370 -27.750 -26.230  1.00 40.94           O  
ANISOU 2305  OH  TYR A 279     5327   4262   5965     11    380    494       O  
ATOM   2306  N   PHE A 280      88.289 -29.417 -23.539  1.00 31.93           N  
ANISOU 2306  N   PHE A 280     4226   3358   4548    518    517    428       N  
ATOM   2307  CA  PHE A 280      89.596 -30.048 -23.655  1.00 29.82           C  
ANISOU 2307  CA  PHE A 280     3961   3092   4277    580    541    418       C  
ATOM   2308  C   PHE A 280      89.513 -30.981 -24.863  1.00 35.69           C  
ANISOU 2308  C   PHE A 280     4780   3694   5085    508    588    425       C  
ATOM   2309  O   PHE A 280      88.864 -32.034 -24.804  1.00 35.85           O  
ANISOU 2309  O   PHE A 280     4846   3627   5148    506    636    497       O  
ATOM   2310  CB  PHE A 280      89.920 -30.775 -22.349  1.00 33.31           C  
ANISOU 2310  CB  PHE A 280     4382   3609   4665    727    571    501       C  
ATOM   2311  CG  PHE A 280      91.354 -31.250 -22.214  1.00 33.78           C  
ANISOU 2311  CG  PHE A 280     4418   3709   4708    823    579    488       C  
ATOM   2312  CD1 PHE A 280      92.126 -31.597 -23.320  1.00 36.21           C  
ANISOU 2312  CD1 PHE A 280     4749   3940   5070    778    603    446       C  
ATOM   2313  CD2 PHE A 280      91.925 -31.350 -20.953  1.00 39.47           C  
ANISOU 2313  CD2 PHE A 280     5089   4561   5348    976    561    521       C  
ATOM   2314  CE1 PHE A 280      93.449 -32.046 -23.159  1.00 42.31           C  
ANISOU 2314  CE1 PHE A 280     5485   4758   5833    878    616    441       C  
ATOM   2315  CE2 PHE A 280      93.237 -31.795 -20.784  1.00 47.25           C  
ANISOU 2315  CE2 PHE A 280     6038   5596   6319   1076    558    512       C  
ATOM   2316  CZ  PHE A 280      93.998 -32.143 -21.889  1.00 45.11           C  
ANISOU 2316  CZ  PHE A 280     5779   5240   6119   1024    589    474       C  
ATOM   2317  N   ILE A 281      90.139 -30.591 -25.973  1.00 34.35           N  
ANISOU 2317  N   ILE A 281     4624   3499   4927    451    578    348       N  
ATOM   2318  CA  ILE A 281      89.945 -31.269 -27.250  1.00 35.47           C  
ANISOU 2318  CA  ILE A 281     4850   3522   5106    384    607    326       C  
ATOM   2319  C   ILE A 281      91.172 -32.100 -27.593  1.00 38.76           C  
ANISOU 2319  C   ILE A 281     5287   3913   5525    456    661    317       C  
ATOM   2320  O   ILE A 281      92.314 -31.651 -27.420  1.00 35.24           O  
ANISOU 2320  O   ILE A 281     4780   3551   5059    510    663    293       O  
ATOM   2321  CB  ILE A 281      89.625 -30.280 -28.385  1.00 40.46           C  
ANISOU 2321  CB  ILE A 281     5499   4145   5728    285    569    260       C  
ATOM   2322  CG1 ILE A 281      89.483 -31.041 -29.701  1.00 41.54           C  
ANISOU 2322  CG1 ILE A 281     5731   4179   5875    241    590    224       C  
ATOM   2323  CG2 ILE A 281      90.700 -29.207 -28.511  1.00 37.38           C  
ANISOU 2323  CG2 ILE A 281     5045   3836   5319    297    560    218       C  
ATOM   2324  CD1 ILE A 281      89.052 -30.165 -30.860  1.00 47.26           C  
ANISOU 2324  CD1 ILE A 281     6486   4903   6568    161    553    174       C  
ATOM   2325  N   THR A 282      90.929 -33.322 -28.077  1.00 34.84           N  
ANISOU 2325  N   THR A 282     4873   3297   5070    456    703    330       N  
ATOM   2326  CA  THR A 282      91.980 -34.210 -28.579  1.00 34.70           C  
ANISOU 2326  CA  THR A 282     4894   3230   5058    527    761    312       C  
ATOM   2327  C   THR A 282      91.583 -34.690 -29.967  1.00 39.23           C  
ANISOU 2327  C   THR A 282     5571   3687   5646    460    767    240       C  
ATOM   2328  O   THR A 282      90.548 -35.347 -30.121  1.00 38.37           O  
ANISOU 2328  O   THR A 282     5518   3466   5592    405    751    242       O  
ATOM   2329  CB  THR A 282      92.185 -35.399 -27.645  1.00 34.24           C  
ANISOU 2329  CB  THR A 282     4844   3128   5039    631    811    397       C  
ATOM   2330  OG1 THR A 282      92.529 -34.920 -26.343  1.00 38.71           O  
ANISOU 2330  OG1 THR A 282     5318   3826   5562    711    794    458       O  
ATOM   2331  CG2 THR A 282      93.318 -36.315 -28.158  1.00 37.10           C  
ANISOU 2331  CG2 THR A 282     5245   3437   5413    721    874    376       C  
ATOM   2332  N   ASP A 283      92.396 -34.367 -30.972  1.00 37.84           N  
ANISOU 2332  N   ASP A 283     5414   3540   5423    471    789    175       N  
ATOM   2333  CA  ASP A 283      92.103 -34.780 -32.341  1.00 39.03           C  
ANISOU 2333  CA  ASP A 283     5672   3604   5552    433    791     94       C  
ATOM   2334  C   ASP A 283      92.581 -36.206 -32.563  1.00 39.70           C  
ANISOU 2334  C   ASP A 283     5832   3576   5674    514    848     72       C  
ATOM   2335  O   ASP A 283      93.772 -36.493 -32.415  1.00 40.88           O  
ANISOU 2335  O   ASP A 283     5956   3762   5814    618    914     88       O  
ATOM   2336  CB  ASP A 283      92.766 -33.856 -33.352  1.00 40.68           C  
ANISOU 2336  CB  ASP A 283     5878   3898   5682    429    810     50       C  
ATOM   2337  CG  ASP A 283      92.383 -34.207 -34.770  1.00 50.34           C  
ANISOU 2337  CG  ASP A 283     7220   5057   6848    408    804    -37       C  
ATOM   2338  OD1 ASP A 283      91.188 -34.064 -35.117  1.00 50.76           O  
ANISOU 2338  OD1 ASP A 283     7317   5071   6899    324    728    -69       O  
ATOM   2339  OD2 ASP A 283      93.265 -34.643 -35.527  1.00 48.48           O  
ANISOU 2339  OD2 ASP A 283     7034   4819   6566    486    872    -77       O  
ATOM   2340  N   ALA A 284      91.663 -37.096 -32.945  1.00 40.45           N  
ANISOU 2340  N   ALA A 284     6016   3528   5825    468    821     29       N  
ATOM   2341  CA  ALA A 284      92.011 -38.510 -33.010  1.00 43.34           C  
ANISOU 2341  CA  ALA A 284     6456   3754   6259    542    872     11       C  
ATOM   2342  C   ALA A 284      92.957 -38.822 -34.167  1.00 49.45           C  
ANISOU 2342  C   ALA A 284     7307   4523   6961    621    921    -86       C  
ATOM   2343  O   ALA A 284      93.796 -39.722 -34.048  1.00 46.35           O  
ANISOU 2343  O   ALA A 284     6941   4072   6599    732    991    -81       O  
ATOM   2344  CB  ALA A 284      90.743 -39.365 -33.114  1.00 44.70           C  
ANISOU 2344  CB  ALA A 284     6690   3752   6542    457    822    -20       C  
ATOM   2345  N   GLN A 285      92.843 -38.106 -35.286  1.00 42.00           N  
ANISOU 2345  N   GLN A 285     6401   3642   5914    582    892   -167       N  
ATOM   2346  CA  GLN A 285      93.668 -38.435 -36.448  1.00 45.46           C  
ANISOU 2346  CA  GLN A 285     6924   4083   6266    671    949   -258       C  
ATOM   2347  C   GLN A 285      95.127 -38.040 -36.235  1.00 44.68           C  
ANISOU 2347  C   GLN A 285     6742   4109   6126    777   1050   -194       C  
ATOM   2348  O   GLN A 285      96.038 -38.796 -36.598  1.00 41.90           O  
ANISOU 2348  O   GLN A 285     6431   3727   5762    895   1130   -226       O  
ATOM   2349  CB  GLN A 285      93.115 -37.757 -37.705  1.00 46.04           C  
ANISOU 2349  CB  GLN A 285     7065   4208   6222    617    896   -346       C  
ATOM   2350  CG  GLN A 285      93.900 -38.090 -38.983  1.00 51.05           C  
ANISOU 2350  CG  GLN A 285     7801   4861   6736    727    962   -441       C  
ATOM   2351  CD  GLN A 285      93.820 -39.561 -39.368  1.00 58.74           C  
ANISOU 2351  CD  GLN A 285     8899   5665   7754    789    958   -560       C  
ATOM   2352  OE1 GLN A 285      92.734 -40.132 -39.454  1.00 65.64           O  
ANISOU 2352  OE1 GLN A 285     9835   6410   8697    710    860   -639       O  
ATOM   2353  NE2 GLN A 285      94.976 -40.183 -39.594  1.00 55.96           N  
ANISOU 2353  NE2 GLN A 285     8577   5307   7378    930   1065   -577       N  
ATOM   2354  N   THR A 286      95.375 -36.865 -35.648  1.00 41.74           N  
ANISOU 2354  N   THR A 286     6244   3872   5744    738   1045   -110       N  
ATOM   2355  CA  THR A 286      96.724 -36.318 -35.595  1.00 41.72           C  
ANISOU 2355  CA  THR A 286     6142   3993   5717    815   1127    -63       C  
ATOM   2356  C   THR A 286      97.370 -36.366 -34.220  1.00 40.71           C  
ANISOU 2356  C   THR A 286     5888   3914   5668    865   1135     23       C  
ATOM   2357  O   THR A 286      98.600 -36.330 -34.136  1.00 43.99           O  
ANISOU 2357  O   THR A 286     6221   4406   6087    956   1204     49       O  
ATOM   2358  CB  THR A 286      96.729 -34.859 -36.072  1.00 41.79           C  
ANISOU 2358  CB  THR A 286     6091   4121   5668    742   1120    -43       C  
ATOM   2359  OG1 THR A 286      96.001 -34.053 -35.133  1.00 41.89           O  
ANISOU 2359  OG1 THR A 286     6025   4162   5729    644   1035      6       O  
ATOM   2360  CG2 THR A 286      96.078 -34.747 -37.447  1.00 39.56           C  
ANISOU 2360  CG2 THR A 286     5935   3815   5282    711   1108   -117       C  
ATOM   2361  N   GLY A 287      96.590 -36.435 -33.149  1.00 37.14           N  
ANISOU 2361  N   GLY A 287     5411   3432   5271    818   1066     70       N  
ATOM   2362  CA  GLY A 287      97.160 -36.257 -31.834  1.00 37.65           C  
ANISOU 2362  CA  GLY A 287     5352   3579   5376    872   1059    150       C  
ATOM   2363  C   GLY A 287      97.328 -34.816 -31.402  1.00 36.40           C  
ANISOU 2363  C   GLY A 287     5067   3559   5206    811   1012    169       C  
ATOM   2364  O   GLY A 287      97.799 -34.576 -30.283  1.00 42.23           O  
ANISOU 2364  O   GLY A 287     5696   4381   5967    859    985    214       O  
ATOM   2365  N   SER A 288      96.960 -33.850 -32.245  1.00 38.96           N  
ANISOU 2365  N   SER A 288     5403   3906   5495    715    997    133       N  
ATOM   2366  CA  SER A 288      96.927 -32.456 -31.817  1.00 37.71           C  
ANISOU 2366  CA  SER A 288     5136   3843   5348    643    945    148       C  
ATOM   2367  C   SER A 288      95.840 -32.279 -30.755  1.00 40.63           C  
ANISOU 2367  C   SER A 288     5500   4205   5732    596    859    173       C  
ATOM   2368  O   SER A 288      94.749 -32.850 -30.870  1.00 39.66           O  
ANISOU 2368  O   SER A 288     5471   3992   5604    558    837    172       O  
ATOM   2369  CB  SER A 288      96.660 -31.551 -33.021  1.00 41.59           C  
ANISOU 2369  CB  SER A 288     5663   4339   5802    560    959    123       C  
ATOM   2370  OG  SER A 288      97.064 -30.218 -32.761  1.00 43.11           O  
ANISOU 2370  OG  SER A 288     5734   4614   6033    511    941    141       O  
ATOM   2371  N   SER A 289      96.149 -31.523 -29.698  1.00 35.91           N  
ANISOU 2371  N   SER A 289     4785   3702   5156    606    810    190       N  
ATOM   2372  CA  SER A 289      95.218 -31.367 -28.576  1.00 38.69           C  
ANISOU 2372  CA  SER A 289     5126   4069   5504    593    740    217       C  
ATOM   2373  C   SER A 289      95.357 -29.984 -27.935  1.00 38.37           C  
ANISOU 2373  C   SER A 289     4975   4129   5475    560    671    192       C  
ATOM   2374  O   SER A 289      96.341 -29.270 -28.145  1.00 36.53           O  
ANISOU 2374  O   SER A 289     4652   3952   5276    555    674    160       O  
ATOM   2375  CB  SER A 289      95.429 -32.468 -27.517  1.00 37.37           C  
ANISOU 2375  CB  SER A 289     4957   3907   5334    711    753    275       C  
ATOM   2376  OG  SER A 289      96.693 -32.368 -26.876  1.00 39.57           O  
ANISOU 2376  OG  SER A 289     5127   4291   5616    810    749    275       O  
ATOM   2377  N   LYS A 290      94.351 -29.603 -27.144  1.00 32.67           N  
ANISOU 2377  N   LYS A 290     4255   3422   4734    536    611    203       N  
ATOM   2378  CA  LYS A 290      94.398 -28.318 -26.451  1.00 36.13           C  
ANISOU 2378  CA  LYS A 290     4600   3945   5182    516    536    161       C  
ATOM   2379  C   LYS A 290      93.523 -28.383 -25.206  1.00 36.72           C  
ANISOU 2379  C   LYS A 290     4679   4065   5210    564    488    189       C  
ATOM   2380  O   LYS A 290      92.381 -28.849 -25.274  1.00 36.35           O  
ANISOU 2380  O   LYS A 290     4708   3956   5147    535    507    237       O  
ATOM   2381  CB  LYS A 290      93.953 -27.172 -27.377  1.00 35.87           C  
ANISOU 2381  CB  LYS A 290     4577   3871   5180    397    524    127       C  
ATOM   2382  CG  LYS A 290      93.951 -25.789 -26.708  1.00 36.39           C  
ANISOU 2382  CG  LYS A 290     4554   3994   5280    370    446     73       C  
ATOM   2383  CD  LYS A 290      94.086 -24.639 -27.741  1.00 40.14           C  
ANISOU 2383  CD  LYS A 290     5010   4421   5819    269    458     52       C  
ATOM   2384  CE  LYS A 290      92.905 -24.623 -28.724  1.00 37.43           C  
ANISOU 2384  CE  LYS A 290     4779   4002   5441    199    481     88       C  
ATOM   2385  NZ  LYS A 290      93.163 -23.704 -29.877  1.00 40.53           N  
ANISOU 2385  NZ  LYS A 290     5169   4353   5876    127    517     95       N  
ATOM   2386  N  ACYS A 291      94.065 -27.911 -24.075  0.66 34.16           N  
ANISOU 2386  N  ACYS A 291     4264   3852   4864    643    426    156       N  
ATOM   2387  N  BCYS A 291      94.063 -27.909 -24.081  0.34 34.96           N  
ANISOU 2387  N  BCYS A 291     4366   3953   4965    642    426    156       N  
ATOM   2388  CA ACYS A 291      93.384 -28.048 -22.785  0.66 35.64           C  
ANISOU 2388  CA ACYS A 291     4454   4111   4977    728    392    189       C  
ATOM   2389  CA BCYS A 291      93.387 -28.055 -22.795  0.34 36.47           C  
ANISOU 2389  CA BCYS A 291     4559   4215   5082    728    392    190       C  
ATOM   2390  C  ACYS A 291      92.152 -27.156 -22.691  0.66 37.21           C  
ANISOU 2390  C  ACYS A 291     4674   4296   5167    659    357    171       C  
ATOM   2391  C  BCYS A 291      92.156 -27.160 -22.694  0.34 36.86           C  
ANISOU 2391  C  BCYS A 291     4629   4252   5123    659    357    171       C  
ATOM   2392  O  ACYS A 291      91.122 -27.566 -22.142  0.66 37.52           O  
ANISOU 2392  O  ACYS A 291     4757   4337   5162    690    378    240       O  
ATOM   2393  O  BCYS A 291      91.122 -27.579 -22.159  0.34 38.00           O  
ANISOU 2393  O  BCYS A 291     4819   4397   5224    689    379    240       O  
ATOM   2394  CB ACYS A 291      94.344 -27.721 -21.641  0.66 41.00           C  
ANISOU 2394  CB ACYS A 291     5032   4931   5613    847    318    136       C  
ATOM   2395  CB BCYS A 291      94.365 -27.747 -21.664  0.34 41.53           C  
ANISOU 2395  CB BCYS A 291     5101   4997   5682    847    320    137       C  
ATOM   2396  SG ACYS A 291      95.715 -28.855 -21.457  0.66 39.56           S  
ANISOU 2396  SG ACYS A 291     4811   4795   5424    972    351    175       S  
ATOM   2397  SG BCYS A 291      95.227 -26.186 -21.899  0.34 53.89           S  
ANISOU 2397  SG BCYS A 291     6547   6597   7333    771    228     -8       S  
ATOM   2398  N   VAL A 292      92.248 -25.919 -23.167  1.00 31.22           N  
ANISOU 2398  N   VAL A 292     3876   3525   4460    573    309     88       N  
ATOM   2399  CA  VAL A 292      91.127 -24.970 -23.128  1.00 32.72           C  
ANISOU 2399  CA  VAL A 292     4083   3698   4652    514    274     66       C  
ATOM   2400  C   VAL A 292      90.923 -24.448 -24.541  1.00 37.89           C  
ANISOU 2400  C   VAL A 292     4770   4248   5377    384    297     58       C  
ATOM   2401  O   VAL A 292      91.667 -23.570 -25.006  1.00 39.91           O  
ANISOU 2401  O   VAL A 292     4974   4489   5699    335    277      0       O  
ATOM   2402  CB  VAL A 292      91.345 -23.814 -22.148  1.00 37.78           C  
ANISOU 2402  CB  VAL A 292     4648   4425   5281    561    181    -33       C  
ATOM   2403  CG1 VAL A 292      90.126 -22.883 -22.172  1.00 36.39           C  
ANISOU 2403  CG1 VAL A 292     4499   4218   5111    511    157    -50       C  
ATOM   2404  CG2 VAL A 292      91.580 -24.344 -20.738  1.00 38.12           C  
ANISOU 2404  CG2 VAL A 292     4666   4598   5222    717    152    -27       C  
ATOM   2405  N   CYS A 293      89.922 -24.987 -25.224  1.00 31.41           N  
ANISOU 2405  N   CYS A 293     4030   3356   4548    332    339    120       N  
ATOM   2406  CA  CYS A 293      89.521 -24.535 -26.550  1.00 31.52           C  
ANISOU 2406  CA  CYS A 293     4089   3289   4599    229    352    119       C  
ATOM   2407  C   CYS A 293      88.140 -23.907 -26.407  1.00 36.25           C  
ANISOU 2407  C   CYS A 293     4704   3877   5192    195    316    130       C  
ATOM   2408  O   CYS A 293      87.137 -24.611 -26.250  1.00 36.66           O  
ANISOU 2408  O   CYS A 293     4791   3915   5223    197    329    182       O  
ATOM   2409  CB  CYS A 293      89.505 -25.693 -27.546  1.00 35.05           C  
ANISOU 2409  CB  CYS A 293     4614   3667   5037    204    411    160       C  
ATOM   2410  SG  CYS A 293      89.342 -25.149 -29.271  1.00 44.70           S  
ANISOU 2410  SG  CYS A 293     5895   4820   6268    110    427    150       S  
ATOM   2411  N   SER A 294      88.088 -22.588 -26.462  1.00 31.83           N  
ANISOU 2411  N   SER A 294     4110   3317   4666    165    274     83       N  
ATOM   2412  CA  SER A 294      86.816 -21.880 -26.340  1.00 29.50           C  
ANISOU 2412  CA  SER A 294     3823   3014   4370    146    240     90       C  
ATOM   2413  C   SER A 294      86.084 -21.912 -27.674  1.00 34.42           C  
ANISOU 2413  C   SER A 294     4508   3567   5002     67    254    131       C  
ATOM   2414  O   SER A 294      86.663 -21.602 -28.717  1.00 36.56           O  
ANISOU 2414  O   SER A 294     4802   3796   5293     21    272    128       O  
ATOM   2415  CB  SER A 294      87.062 -20.440 -25.893  1.00 29.95           C  
ANISOU 2415  CB  SER A 294     3827   3082   4473    153    187     17       C  
ATOM   2416  OG  SER A 294      87.601 -20.415 -24.579  1.00 38.94           O  
ANISOU 2416  OG  SER A 294     4909   4301   5584    241    152    -41       O  
ATOM   2417  N   VAL A 295      84.811 -22.285 -27.638  1.00 32.10           N  
ANISOU 2417  N   VAL A 295     4236   3269   4692     58    244    171       N  
ATOM   2418  CA  VAL A 295      84.029 -22.563 -28.835  1.00 32.40           C  
ANISOU 2418  CA  VAL A 295     4328   3255   4728     -7    238    200       C  
ATOM   2419  C   VAL A 295      82.703 -21.828 -28.723  1.00 33.77           C  
ANISOU 2419  C   VAL A 295     4479   3437   4915    -17    195    217       C  
ATOM   2420  O   VAL A 295      82.019 -21.922 -27.698  1.00 33.70           O  
ANISOU 2420  O   VAL A 295     4427   3470   4908     24    194    236       O  
ATOM   2421  CB  VAL A 295      83.793 -24.073 -29.025  1.00 37.18           C  
ANISOU 2421  CB  VAL A 295     4970   3831   5326    -18    264    228       C  
ATOM   2422  CG1 VAL A 295      82.858 -24.328 -30.190  1.00 39.40           C  
ANISOU 2422  CG1 VAL A 295     5297   4065   5607    -83    231    233       C  
ATOM   2423  CG2 VAL A 295      85.131 -24.797 -29.255  1.00 31.68           C  
ANISOU 2423  CG2 VAL A 295     4302   3121   4616      3    312    211       C  
ATOM   2424  N   ILE A 296      82.349 -21.096 -29.772  1.00 35.35           N  
ANISOU 2424  N   ILE A 296     4707   3606   5117    -57    167    221       N  
ATOM   2425  CA  ILE A 296      81.083 -20.381 -29.842  1.00 37.30           C  
ANISOU 2425  CA  ILE A 296     4933   3859   5379    -60    122    241       C  
ATOM   2426  C   ILE A 296      80.387 -20.749 -31.152  1.00 33.36           C  
ANISOU 2426  C   ILE A 296     4482   3336   4857   -110     88    262       C  
ATOM   2427  O   ILE A 296      81.047 -20.927 -32.182  1.00 37.76           O  
ANISOU 2427  O   ILE A 296     5100   3869   5376   -131    100    254       O  
ATOM   2428  CB  ILE A 296      81.320 -18.853 -29.710  1.00 36.17           C  
ANISOU 2428  CB  ILE A 296     4772   3705   5266    -38    109    222       C  
ATOM   2429  CG1 ILE A 296      80.013 -18.111 -29.452  1.00 31.11           C  
ANISOU 2429  CG1 ILE A 296     4098   3079   4645    -12     69    240       C  
ATOM   2430  CG2 ILE A 296      82.079 -18.285 -30.932  1.00 35.48           C  
ANISOU 2430  CG2 ILE A 296     4734   3567   5180    -72    124    233       C  
ATOM   2431  CD1 ILE A 296      80.229 -16.621 -29.167  1.00 33.64           C  
ANISOU 2431  CD1 ILE A 296     4402   3368   5013     21     56    210       C  
ATOM   2432  N   ASP A 297      79.055 -20.892 -31.106  1.00 36.21           N  
ANISOU 2432  N   ASP A 297     4807   3713   5238   -120     44    285       N  
ATOM   2433  CA  ASP A 297      78.269 -21.189 -32.302  1.00 37.26           C  
ANISOU 2433  CA  ASP A 297     4970   3836   5352   -162    -16    288       C  
ATOM   2434  C   ASP A 297      77.564 -19.910 -32.740  1.00 38.87           C  
ANISOU 2434  C   ASP A 297     5161   4057   5550   -139    -62    314       C  
ATOM   2435  O   ASP A 297      76.402 -19.674 -32.434  1.00 38.19           O  
ANISOU 2435  O   ASP A 297     5011   3999   5501   -130   -102    336       O  
ATOM   2436  CB  ASP A 297      77.263 -22.320 -32.053  1.00 38.13           C  
ANISOU 2436  CB  ASP A 297     5033   3943   5512   -200    -42    294       C  
ATOM   2437  CG  ASP A 297      76.444 -22.658 -33.308  1.00 42.52           C  
ANISOU 2437  CG  ASP A 297     5610   4491   6054   -245   -131    270       C  
ATOM   2438  OD1 ASP A 297      76.893 -22.325 -34.424  1.00 43.81           O  
ANISOU 2438  OD1 ASP A 297     5853   4656   6138   -236   -157    246       O  
ATOM   2439  OD2 ASP A 297      75.342 -23.246 -33.179  1.00 42.26           O  
ANISOU 2439  OD2 ASP A 297     5508   4457   6092   -283   -176    275       O  
ATOM   2440  N   LEU A 298      78.301 -19.065 -33.443  1.00 37.99           N  
ANISOU 2440  N   LEU A 298     5106   3927   5402   -123    -47    322       N  
ATOM   2441  CA  LEU A 298      77.713 -17.937 -34.142  1.00 36.17           C  
ANISOU 2441  CA  LEU A 298     4886   3699   5157    -95    -87    362       C  
ATOM   2442  C   LEU A 298      77.402 -18.357 -35.563  1.00 37.88           C  
ANISOU 2442  C   LEU A 298     5167   3935   5289   -106   -140    367       C  
ATOM   2443  O   LEU A 298      78.113 -19.175 -36.150  1.00 40.07           O  
ANISOU 2443  O   LEU A 298     5507   4207   5510   -126   -120    338       O  
ATOM   2444  CB  LEU A 298      78.669 -16.739 -34.163  1.00 33.51           C  
ANISOU 2444  CB  LEU A 298     4573   3317   4843    -70    -32    385       C  
ATOM   2445  CG  LEU A 298      78.889 -16.023 -32.837  1.00 39.15           C  
ANISOU 2445  CG  LEU A 298     5225   4010   5639    -45     -7    358       C  
ATOM   2446  CD1 LEU A 298      80.080 -15.072 -32.956  1.00 35.90           C  
ANISOU 2446  CD1 LEU A 298     4832   3532   5275    -44     46    362       C  
ATOM   2447  CD2 LEU A 298      77.617 -15.266 -32.426  1.00 40.77           C  
ANISOU 2447  CD2 LEU A 298     5381   4230   5881      0    -53    376       C  
ATOM   2448  N   LEU A 299      76.346 -17.775 -36.122  1.00 36.46           N  
ANISOU 2448  N   LEU A 299     4974   3786   5092    -79   -212    400       N  
ATOM   2449  CA  LEU A 299      76.145 -17.867 -37.560  1.00 37.78           C  
ANISOU 2449  CA  LEU A 299     5214   3987   5152    -60   -270    409       C  
ATOM   2450  C   LEU A 299      77.399 -17.350 -38.249  1.00 38.46           C  
ANISOU 2450  C   LEU A 299     5391   4048   5174    -32   -186    450       C  
ATOM   2451  O   LEU A 299      77.938 -16.305 -37.872  1.00 39.82           O  
ANISOU 2451  O   LEU A 299     5554   4175   5403    -12   -118    503       O  
ATOM   2452  CB  LEU A 299      74.923 -17.048 -37.980  1.00 38.71           C  
ANISOU 2452  CB  LEU A 299     5299   4148   5263    -13   -354    457       C  
ATOM   2453  CG  LEU A 299      74.535 -17.090 -39.454  1.00 42.17           C  
ANISOU 2453  CG  LEU A 299     5806   4646   5570     29   -438    466       C  
ATOM   2454  CD1 LEU A 299      73.724 -18.353 -39.726  1.00 46.69           C  
ANISOU 2454  CD1 LEU A 299     6346   5262   6133    -19   -550    374       C  
ATOM   2455  CD2 LEU A 299      73.761 -15.833 -39.833  1.00 47.17           C  
ANISOU 2455  CD2 LEU A 299     6424   5306   6191    108   -480    553       C  
ATOM   2456  N   LEU A 300      77.892 -18.095 -39.237  1.00 38.80           N  
ANISOU 2456  N   LEU A 300     5518   4116   5109    -28   -185    423       N  
ATOM   2457  CA  LEU A 300      79.183 -17.735 -39.825  1.00 41.17           C  
ANISOU 2457  CA  LEU A 300     5891   4397   5353      1    -79    471       C  
ATOM   2458  C   LEU A 300      79.177 -16.305 -40.360  1.00 39.78           C  
ANISOU 2458  C   LEU A 300     5737   4212   5167     59    -46    586       C  
ATOM   2459  O   LEU A 300      80.175 -15.583 -40.230  1.00 40.48           O  
ANISOU 2459  O   LEU A 300     5827   4244   5311     60     61    647       O  
ATOM   2460  CB  LEU A 300      79.549 -18.720 -40.929  1.00 42.57           C  
ANISOU 2460  CB  LEU A 300     6165   4620   5390     22    -88    424       C  
ATOM   2461  CG  LEU A 300      80.984 -18.599 -41.429  1.00 43.33           C  
ANISOU 2461  CG  LEU A 300     6324   4705   5436     52     44    469       C  
ATOM   2462  CD1 LEU A 300      81.957 -18.680 -40.270  1.00 40.74           C  
ANISOU 2462  CD1 LEU A 300     5927   4312   5242     -1    131    455       C  
ATOM   2463  CD2 LEU A 300      81.248 -19.695 -42.433  1.00 45.96           C  
ANISOU 2463  CD2 LEU A 300     6753   5088   5621     87     29    400       C  
ATOM   2464  N   ASP A 301      78.057 -15.878 -40.956  1.00 40.78           N  
ANISOU 2464  N   ASP A 301     5873   4387   5236    108   -137    621       N  
ATOM   2465  CA  ASP A 301      77.943 -14.513 -41.460  1.00 40.63           C  
ANISOU 2465  CA  ASP A 301     5876   4350   5211    176   -106    746       C  
ATOM   2466  C   ASP A 301      78.128 -13.497 -40.341  1.00 39.82           C  
ANISOU 2466  C   ASP A 301     5698   4149   5284    151    -50    777       C  
ATOM   2467  O   ASP A 301      78.698 -12.419 -40.557  1.00 40.58           O  
ANISOU 2467  O   ASP A 301     5813   4176   5428    179     34    874       O  
ATOM   2468  CB  ASP A 301      76.580 -14.294 -42.131  1.00 44.15           C  
ANISOU 2468  CB  ASP A 301     6326   4874   5575    241   -234    768       C  
ATOM   2469  CG  ASP A 301      76.178 -15.433 -43.057  1.00 52.93           C  
ANISOU 2469  CG  ASP A 301     7492   6088   6531    257   -335    687       C  
ATOM   2470  OD1 ASP A 301      76.124 -16.590 -42.590  1.00 44.86           O  
ANISOU 2470  OD1 ASP A 301     6438   5066   5542    183   -376    568       O  
ATOM   2471  OD2 ASP A 301      75.888 -15.164 -44.243  1.00 53.42           O  
ANISOU 2471  OD2 ASP A 301     7630   6229   6440    349   -380    740       O  
ATOM   2472  N   ASP A 302      77.618 -13.811 -39.146  1.00 41.58           N  
ANISOU 2472  N   ASP A 302     5834   4361   5603    106    -95    695       N  
ATOM   2473  CA  ASP A 302      77.761 -12.906 -38.009  1.00 39.62           C  
ANISOU 2473  CA  ASP A 302     5520   4031   5504     97    -56    695       C  
ATOM   2474  C   ASP A 302      79.209 -12.831 -37.548  1.00 44.44           C  
ANISOU 2474  C   ASP A 302     6127   4571   6186     51     46    676       C  
ATOM   2475  O   ASP A 302      79.718 -11.743 -37.246  1.00 38.99           O  
ANISOU 2475  O   ASP A 302     5419   3790   5605     55    101    712       O  
ATOM   2476  CB  ASP A 302      76.874 -13.358 -36.845  1.00 41.83           C  
ANISOU 2476  CB  ASP A 302     5712   4340   5842     78   -119    615       C  
ATOM   2477  CG  ASP A 302      75.399 -13.007 -37.037  1.00 46.11           C  
ANISOU 2477  CG  ASP A 302     6216   4931   6374    129   -210    645       C  
ATOM   2478  OD1 ASP A 302      75.087 -12.076 -37.806  1.00 44.34           O  
ANISOU 2478  OD1 ASP A 302     6026   4694   6126    192   -222    730       O  
ATOM   2479  OD2 ASP A 302      74.554 -13.673 -36.395  1.00 46.95           O  
ANISOU 2479  OD2 ASP A 302     6248   5087   6503    111   -264    593       O  
ATOM   2480  N   PHE A 303      79.886 -13.976 -37.475  1.00 38.05           N  
ANISOU 2480  N   PHE A 303     5329   3796   5332      8     68    615       N  
ATOM   2481  CA  PHE A 303      81.294 -13.954 -37.091  1.00 37.98           C  
ANISOU 2481  CA  PHE A 303     5306   3735   5390    -28    159    599       C  
ATOM   2482  C   PHE A 303      82.136 -13.189 -38.112  1.00 38.17           C  
ANISOU 2482  C   PHE A 303     5377   3714   5411    -11    252    704       C  
ATOM   2483  O   PHE A 303      83.058 -12.455 -37.743  1.00 37.55           O  
ANISOU 2483  O   PHE A 303     5257   3552   5457    -37    323    722       O  
ATOM   2484  CB  PHE A 303      81.803 -15.388 -36.914  1.00 38.06           C  
ANISOU 2484  CB  PHE A 303     5323   3795   5343    -60    166    525       C  
ATOM   2485  CG  PHE A 303      83.256 -15.460 -36.542  1.00 38.61           C  
ANISOU 2485  CG  PHE A 303     5365   3829   5475    -87    253    507       C  
ATOM   2486  CD1 PHE A 303      83.675 -15.107 -35.264  1.00 43.37           C  
ANISOU 2486  CD1 PHE A 303     5887   4394   6197   -108    254    451       C  
ATOM   2487  CD2 PHE A 303      84.198 -15.873 -37.466  1.00 42.75           C  
ANISOU 2487  CD2 PHE A 303     5940   4367   5936    -82    330    542       C  
ATOM   2488  CE1 PHE A 303      85.013 -15.162 -34.924  1.00 43.89           C  
ANISOU 2488  CE1 PHE A 303     5912   4436   6329   -132    318    427       C  
ATOM   2489  CE2 PHE A 303      85.532 -15.937 -37.135  1.00 48.54           C  
ANISOU 2489  CE2 PHE A 303     6629   5073   6739   -106    411    531       C  
ATOM   2490  CZ  PHE A 303      85.941 -15.580 -35.865  1.00 46.96           C  
ANISOU 2490  CZ  PHE A 303     6337   4835   6670   -135    399    472       C  
ATOM   2491  N   VAL A 304      81.817 -13.321 -39.402  1.00 37.16           N  
ANISOU 2491  N   VAL A 304     5333   3640   5147     38    251    777       N  
ATOM   2492  CA  VAL A 304      82.548 -12.569 -40.421  1.00 36.17           C  
ANISOU 2492  CA  VAL A 304     5256   3482   5003     73    356    906       C  
ATOM   2493  C   VAL A 304      82.332 -11.072 -40.239  1.00 45.63           C  
ANISOU 2493  C   VAL A 304     6425   4576   6337     88    380    996       C  
ATOM   2494  O   VAL A 304      83.274 -10.275 -40.361  1.00 41.24           O  
ANISOU 2494  O   VAL A 304     5850   3927   5894     70    489   1075       O  
ATOM   2495  CB  VAL A 304      82.133 -13.026 -41.830  1.00 38.91           C  
ANISOU 2495  CB  VAL A 304     5710   3931   5142    149    339    962       C  
ATOM   2496  CG1 VAL A 304      82.610 -12.009 -42.887  1.00 39.76           C  
ANISOU 2496  CG1 VAL A 304     5872   4011   5222    214    451   1136       C  
ATOM   2497  CG2 VAL A 304      82.673 -14.408 -42.112  1.00 42.37           C  
ANISOU 2497  CG2 VAL A 304     6187   4442   5469    138    346    876       C  
ATOM   2498  N   GLU A 305      81.088 -10.659 -39.971  1.00 42.58           N  
ANISOU 2498  N   GLU A 305     6028   4194   5955    122    283    987       N  
ATOM   2499  CA  GLU A 305      80.820  -9.245 -39.714  1.00 38.91           C  
ANISOU 2499  CA  GLU A 305     5538   3617   5631    146    300   1058       C  
ATOM   2500  C   GLU A 305      81.649  -8.737 -38.539  1.00 37.50           C  
ANISOU 2500  C   GLU A 305     5276   3319   5655     75    341    986       C  
ATOM   2501  O   GLU A 305      82.259  -7.662 -38.609  1.00 41.39           O  
ANISOU 2501  O   GLU A 305     5751   3681   6293     64    419   1058       O  
ATOM   2502  CB  GLU A 305      79.329  -9.024 -39.442  1.00 39.23           C  
ANISOU 2502  CB  GLU A 305     5563   3695   5648    199    184   1036       C  
ATOM   2503  CG  GLU A 305      78.963  -7.552 -39.251  1.00 44.36           C  
ANISOU 2503  CG  GLU A 305     6198   4223   6436    245    199   1113       C  
ATOM   2504  CD  GLU A 305      77.459  -7.322 -39.130  1.00 46.36           C  
ANISOU 2504  CD  GLU A 305     6435   4528   6653    319     91   1109       C  
ATOM   2505  OE1 GLU A 305      76.871  -7.658 -38.079  1.00 45.83           O  
ANISOU 2505  OE1 GLU A 305     6299   4490   6625    302     23    993       O  
ATOM   2506  OE2 GLU A 305      76.870  -6.802 -40.095  1.00 50.97           O  
ANISOU 2506  OE2 GLU A 305     7069   5132   7165    405     78   1232       O  
ATOM   2507  N   ILE A 306      81.691  -9.511 -37.451  1.00 39.00           N  
ANISOU 2507  N   ILE A 306     5409   3549   5859     31    287    841       N  
ATOM   2508  CA  ILE A 306      82.404  -9.080 -36.249  1.00 39.41           C  
ANISOU 2508  CA  ILE A 306     5382   3514   6080    -19    298    746       C  
ATOM   2509  C   ILE A 306      83.885  -8.888 -36.541  1.00 39.42           C  
ANISOU 2509  C   ILE A 306     5360   3445   6174    -75    404    783       C  
ATOM   2510  O   ILE A 306      84.460  -7.833 -36.241  1.00 39.82           O  
ANISOU 2510  O   ILE A 306     5362   3362   6407   -105    443    792       O  
ATOM   2511  CB  ILE A 306      82.189 -10.083 -35.101  1.00 40.37           C  
ANISOU 2511  CB  ILE A 306     5457   3719   6161    -35    228    604       C  
ATOM   2512  CG1 ILE A 306      80.745 -10.026 -34.578  1.00 38.91           C  
ANISOU 2512  CG1 ILE A 306     5263   3581   5941     18    139    571       C  
ATOM   2513  CG2 ILE A 306      83.202  -9.829 -33.988  1.00 37.70           C  
ANISOU 2513  CG2 ILE A 306     5044   3321   5960    -78    240    501       C  
ATOM   2514  CD1 ILE A 306      80.325 -11.335 -33.881  1.00 41.25           C  
ANISOU 2514  CD1 ILE A 306     5534   3991   6148     10     89    487       C  
ATOM   2515  N   ILE A 307      84.530  -9.901 -37.133  1.00 37.19           N  
ANISOU 2515  N   ILE A 307     5104   3246   5780    -90    452    800       N  
ATOM   2516  CA  ILE A 307      85.975  -9.806 -37.324  1.00 40.78           C  
ANISOU 2516  CA  ILE A 307     5515   3649   6330   -140    558    830       C  
ATOM   2517  C   ILE A 307      86.321  -8.770 -38.388  1.00 40.05           C  
ANISOU 2517  C   ILE A 307     5449   3466   6303   -128    669   1002       C  
ATOM   2518  O   ILE A 307      87.345  -8.080 -38.286  1.00 42.00           O  
ANISOU 2518  O   ILE A 307     5624   3601   6733   -182    753   1037       O  
ATOM   2519  CB  ILE A 307      86.560 -11.200 -37.641  1.00 41.66           C  
ANISOU 2519  CB  ILE A 307     5649   3877   6303   -143    586    800       C  
ATOM   2520  CG1 ILE A 307      88.082 -11.174 -37.527  1.00 40.69           C  
ANISOU 2520  CG1 ILE A 307     5448   3712   6302   -195    683    803       C  
ATOM   2521  CG2 ILE A 307      86.148 -11.679 -39.025  1.00 43.29           C  
ANISOU 2521  CG2 ILE A 307     5966   4166   6315    -81    619    900       C  
ATOM   2522  CD1 ILE A 307      88.695 -12.574 -37.542  1.00 40.73           C  
ANISOU 2522  CD1 ILE A 307     5457   3823   6194   -190    700    744       C  
ATOM   2523  N   LYS A 308      85.459  -8.578 -39.383  1.00 40.54           N  
ANISOU 2523  N   LYS A 308     5604   3564   6233    -54    671   1117       N  
ATOM   2524  CA  LYS A 308      85.721  -7.534 -40.362  1.00 43.75           C  
ANISOU 2524  CA  LYS A 308     6042   3883   6698    -24    785   1304       C  
ATOM   2525  C   LYS A 308      85.430  -6.134 -39.832  1.00 45.74           C  
ANISOU 2525  C   LYS A 308     6250   3963   7166    -38    774   1328       C  
ATOM   2526  O   LYS A 308      85.662  -5.162 -40.548  1.00 42.37           O  
ANISOU 2526  O   LYS A 308     5841   3430   6829    -18    877   1494       O  
ATOM   2527  CB  LYS A 308      84.907  -7.771 -41.631  1.00 51.21           C  
ANISOU 2527  CB  LYS A 308     7108   4940   7411     82    783   1424       C  
ATOM   2528  CG  LYS A 308      85.459  -8.873 -42.524  1.00 54.62           C  
ANISOU 2528  CG  LYS A 308     7601   5508   7644    114    841   1446       C  
ATOM   2529  CD  LYS A 308      84.618  -8.979 -43.783  1.00 63.92           C  
ANISOU 2529  CD  LYS A 308     8901   6797   8588    234    822   1551       C  
ATOM   2530  CE  LYS A 308      85.233  -9.918 -44.800  1.00 71.56           C  
ANISOU 2530  CE  LYS A 308     9945   7893   9352    287    896   1582       C  
ATOM   2531  NZ  LYS A 308      84.349 -10.059 -45.998  1.00 80.24           N  
ANISOU 2531  NZ  LYS A 308    11168   9120  10199    418    847   1656       N  
ATOM   2532  N   SER A 309      84.943  -6.004 -38.602  1.00 40.65           N  
ANISOU 2532  N   SER A 309     5552   3284   6609    -63    661   1170       N  
ATOM   2533  CA  SER A 309      84.620  -4.697 -38.046  1.00 42.96           C  
ANISOU 2533  CA  SER A 309     5809   3409   7103    -64    640   1165       C  
ATOM   2534  C   SER A 309      85.617  -4.263 -36.978  1.00 47.15           C  
ANISOU 2534  C   SER A 309     6229   3814   7873   -158    640   1037       C  
ATOM   2535  O   SER A 309      85.333  -3.335 -36.213  1.00 43.39           O  
ANISOU 2535  O   SER A 309     5717   3206   7564   -161    588    962       O  
ATOM   2536  CB  SER A 309      83.196  -4.708 -37.494  1.00 44.72           C  
ANISOU 2536  CB  SER A 309     6059   3688   7245      5    510   1085       C  
ATOM   2537  OG  SER A 309      82.282  -5.095 -38.508  1.00 52.66           O  
ANISOU 2537  OG  SER A 309     7152   4814   8044     88    494   1194       O  
ATOM   2538  N   GLN A 310      86.795  -4.890 -36.934  1.00 41.88           N  
ANISOU 2538  N   GLN A 310     4950   3692   7271     -8    728   1393       N  
ATOM   2539  CA  GLN A 310      87.809  -4.578 -35.936  1.00 41.78           C  
ANISOU 2539  CA  GLN A 310     4837   3613   7424      5    788   1133       C  
ATOM   2540  C   GLN A 310      88.989  -3.841 -36.559  1.00 43.88           C  
ANISOU 2540  C   GLN A 310     5049   3768   7857    -26    948   1116       C  
ATOM   2541  O   GLN A 310      89.320  -4.019 -37.736  1.00 45.32           O  
ANISOU 2541  O   GLN A 310     5318   3952   7952    -55   1003   1254       O  
ATOM   2542  CB  GLN A 310      88.309  -5.848 -35.227  1.00 37.13           C  
ANISOU 2542  CB  GLN A 310     4306   3154   6650     18    677    949       C  
ATOM   2543  CG  GLN A 310      87.196  -6.708 -34.607  1.00 38.08           C  
ANISOU 2543  CG  GLN A 310     4508   3381   6580     36    533    950       C  
ATOM   2544  CD  GLN A 310      86.233  -5.897 -33.744  1.00 44.28           C  
ANISOU 2544  CD  GLN A 310     5202   4102   7521     47    534    930       C  
ATOM   2545  OE1 GLN A 310      86.652  -5.037 -32.969  1.00 42.08           O  
ANISOU 2545  OE1 GLN A 310     4814   3725   7448     39    612    783       O  
ATOM   2546  NE2 GLN A 310      84.932  -6.160 -33.891  1.00 37.94           N  
ANISOU 2546  NE2 GLN A 310     4440   3352   6624     52    466   1075       N  
ATOM   2547  N   ASP A 311      89.600  -2.976 -35.754  1.00 42.13           N  
ANISOU 2547  N   ASP A 311     4692   3445   7869    -43   1038    937       N  
ATOM   2548  CA  ASP A 311      90.866  -2.354 -36.105  1.00 42.51           C  
ANISOU 2548  CA  ASP A 311     4664   3404   8085    -92   1190    856       C  
ATOM   2549  C   ASP A 311      91.995  -3.349 -35.856  1.00 40.80           C  
ANISOU 2549  C   ASP A 311     4427   3313   7764    -94   1126    694       C  
ATOM   2550  O   ASP A 311      92.039  -3.998 -34.804  1.00 42.62           O  
ANISOU 2550  O   ASP A 311     4626   3654   7912    -72    990    544       O  
ATOM   2551  CB  ASP A 311      91.064  -1.089 -35.277  1.00 42.57           C  
ANISOU 2551  CB  ASP A 311     4539   3267   8370   -142   1315    705       C  
ATOM   2552  CG  ASP A 311      92.420  -0.440 -35.509  1.00 51.88           C  
ANISOU 2552  CG  ASP A 311     5619   4365   9728   -222   1473    583       C  
ATOM   2553  OD1 ASP A 311      93.423  -0.935 -34.959  1.00 49.50           O  
ANISOU 2553  OD1 ASP A 311     5231   4173   9403   -259   1412    388       O  
ATOM   2554  OD2 ASP A 311      92.474   0.575 -36.230  1.00 51.03           O  
ANISOU 2554  OD2 ASP A 311     5510   4084   9793   -249   1662    692       O  
ATOM   2555  N   LEU A 312      92.908  -3.471 -36.819  1.00 45.31           N  
ANISOU 2555  N   LEU A 312     5013   3859   8343   -114   1235    738       N  
ATOM   2556  CA  LEU A 312      93.925  -4.521 -36.791  1.00 45.23           C  
ANISOU 2556  CA  LEU A 312     4986   3954   8246    -87   1204    639       C  
ATOM   2557  C   LEU A 312      95.333  -3.978 -36.574  1.00 50.89           C  
ANISOU 2557  C   LEU A 312     5510   4637   9189   -134   1314    478       C  
ATOM   2558  O   LEU A 312      96.314  -4.651 -36.916  1.00 49.63           O  
ANISOU 2558  O   LEU A 312     5314   4524   9021   -110   1359    448       O  
ATOM   2559  CB  LEU A 312      93.870  -5.333 -38.085  1.00 44.27           C  
ANISOU 2559  CB  LEU A 312     5051   3840   7930    -81   1262    808       C  
ATOM   2560  CG  LEU A 312      92.500  -5.882 -38.492  1.00 41.80           C  
ANISOU 2560  CG  LEU A 312     4932   3583   7368    -77   1157    983       C  
ATOM   2561  CD1 LEU A 312      92.574  -6.630 -39.815  1.00 47.06           C  
ANISOU 2561  CD1 LEU A 312     5799   4258   7822   -124   1240   1123       C  
ATOM   2562  CD2 LEU A 312      91.944  -6.767 -37.397  1.00 46.16           C  
ANISOU 2562  CD2 LEU A 312     5496   4256   7784    -18    975    889       C  
ATOM   2563  N   SER A 313      95.461  -2.791 -35.991  1.00 45.53           N  
ANISOU 2563  N   SER A 313     4700   3877   8723   -209   1373    368       N  
ATOM   2564  CA  SER A 313      96.736  -2.082 -35.993  1.00 49.86           C  
ANISOU 2564  CA  SER A 313     5070   4375   9499   -296   1513    231       C  
ATOM   2565  C   SER A 313      97.599  -2.343 -34.759  1.00 52.94           C  
ANISOU 2565  C   SER A 313     5256   4920   9940   -330   1385      5       C  
ATOM   2566  O   SER A 313      98.681  -1.761 -34.650  1.00 51.66           O  
ANISOU 2566  O   SER A 313     4910   4750   9968   -426   1479   -126       O  
ATOM   2567  CB  SER A 313      96.487  -0.578 -36.122  1.00 52.14           C  
ANISOU 2567  CB  SER A 313     5340   4471  10001   -391   1691    230       C  
ATOM   2568  OG  SER A 313      95.789  -0.125 -34.980  1.00 51.65           O  
ANISOU 2568  OG  SER A 313     5251   4405   9969   -422   1614    122       O  
ATOM   2569  N   VAL A 314      97.172  -3.211 -33.848  1.00 50.19           N  
ANISOU 2569  N   VAL A 314     4932   4722   9418   -264   1172    -35       N  
ATOM   2570  CA  VAL A 314      97.837  -3.411 -32.566  1.00 47.79           C  
ANISOU 2570  CA  VAL A 314     4449   4585   9126   -307   1014   -225       C  
ATOM   2571  C   VAL A 314      98.099  -4.906 -32.373  1.00 49.78           C  
ANISOU 2571  C   VAL A 314     4713   5004   9199   -163    851   -169       C  
ATOM   2572  O   VAL A 314      97.346  -5.749 -32.870  1.00 48.08           O  
ANISOU 2572  O   VAL A 314     4694   4771   8804    -54    830    -26       O  
ATOM   2573  CB  VAL A 314      96.971  -2.799 -31.434  1.00 63.27           C  
ANISOU 2573  CB  VAL A 314     6445   6535  11059   -393    937   -343       C  
ATOM   2574  CG1 VAL A 314      96.926  -3.670 -30.195  1.00 62.09           C  
ANISOU 2574  CG1 VAL A 314     6274   6588  10729   -366    693   -434       C  
ATOM   2575  CG2 VAL A 314      97.417  -1.351 -31.117  1.00 57.46           C  
ANISOU 2575  CG2 VAL A 314     5584   5692  10555   -584   1090   -511       C  
ATOM   2576  N   VAL A 315      99.198  -5.237 -31.679  1.00 45.22           N  
ANISOU 2576  N   VAL A 315     3916   4588   8676   -168    746   -273       N  
ATOM   2577  CA  VAL A 315      99.601  -6.640 -31.531  1.00 42.66           C  
ANISOU 2577  CA  VAL A 315     3578   4403   8229     -7    625   -194       C  
ATOM   2578  C   VAL A 315      98.494  -7.466 -30.878  1.00 48.11           C  
ANISOU 2578  C   VAL A 315     4469   5148   8661     75    458   -150       C  
ATOM   2579  O   VAL A 315      98.134  -8.547 -31.365  1.00 47.58           O  
ANISOU 2579  O   VAL A 315     4568   5065   8445    210    468    -19       O  
ATOM   2580  CB  VAL A 315     100.916  -6.747 -30.737  1.00 49.66           C  
ANISOU 2580  CB  VAL A 315     4154   5483   9233    -27    505   -292       C  
ATOM   2581  CG1 VAL A 315     101.237  -8.216 -30.446  1.00 48.55           C  
ANISOU 2581  CG1 VAL A 315     3999   5476   8972    170    373   -181       C  
ATOM   2582  CG2 VAL A 315     102.055  -6.103 -31.513  1.00 56.34           C  
ANISOU 2582  CG2 VAL A 315     4794   6273  10342    -96    696   -321       C  
ATOM   2583  N   SER A 316      97.957  -6.989 -29.753  1.00 44.04           N  
ANISOU 2583  N   SER A 316     3955   4693   8087    -22    325   -272       N  
ATOM   2584  CA  SER A 316      96.949  -7.745 -29.019  1.00 41.21           C  
ANISOU 2584  CA  SER A 316     3776   4390   7490     40    173   -250       C  
ATOM   2585  C   SER A 316      96.049  -6.796 -28.243  1.00 45.07           C  
ANISOU 2585  C   SER A 316     4327   4830   7968   -104    157   -375       C  
ATOM   2586  O   SER A 316      96.506  -5.782 -27.711  1.00 45.24           O  
ANISOU 2586  O   SER A 316     4207   4859   8124   -262    177   -530       O  
ATOM   2587  CB  SER A 316      97.584  -8.755 -28.053  1.00 47.50           C  
ANISOU 2587  CB  SER A 316     4483   5393   8174    124    -33   -260       C  
ATOM   2588  OG  SER A 316      98.386  -8.097 -27.082  1.00 55.56           O  
ANISOU 2588  OG  SER A 316     5276   6557   9278    -14   -149   -413       O  
ATOM   2589  N   LYS A 317      94.770  -7.145 -28.164  1.00 41.08           N  
ANISOU 2589  N   LYS A 317     4034   4269   7308    -60    138   -315       N  
ATOM   2590  CA  LYS A 317      93.843  -6.355 -27.371  1.00 42.53           C  
ANISOU 2590  CA  LYS A 317     4282   4391   7488   -176    146   -426       C  
ATOM   2591  C   LYS A 317      92.587  -7.179 -27.148  1.00 43.53           C  
ANISOU 2591  C   LYS A 317     4617   4517   7404    -94     77   -347       C  
ATOM   2592  O   LYS A 317      92.369  -8.204 -27.801  1.00 39.00           O  
ANISOU 2592  O   LYS A 317     4151   3963   6702     32     56   -201       O  
ATOM   2593  CB  LYS A 317      93.511  -5.017 -28.046  1.00 46.35           C  
ANISOU 2593  CB  LYS A 317     4745   4674   8190   -262    358   -422       C  
ATOM   2594  CG  LYS A 317      92.622  -5.129 -29.283  1.00 43.47           C  
ANISOU 2594  CG  LYS A 317     4514   4182   7820   -163    464   -208       C  
ATOM   2595  CD  LYS A 317      91.959  -3.778 -29.577  1.00 47.29           C  
ANISOU 2595  CD  LYS A 317     4997   4469   8503   -236    648   -191       C  
ATOM   2596  CE  LYS A 317      91.112  -3.798 -30.846  1.00 49.83           C  
ANISOU 2596  CE  LYS A 317     5423   4692   8820   -150    730     56       C  
ATOM   2597  NZ  LYS A 317      90.643  -2.413 -31.205  1.00 45.38           N  
ANISOU 2597  NZ  LYS A 317     4826   3924   8491   -196    925    111       N  
ATOM   2598  N   VAL A 318      91.767  -6.707 -26.211  1.00 39.44           N  
ANISOU 2598  N   VAL A 318     4163   3968   6855   -185     68   -458       N  
ATOM   2599  CA  VAL A 318      90.484  -7.322 -25.891  1.00 40.06           C  
ANISOU 2599  CA  VAL A 318     4424   4033   6762   -137     28   -409       C  
ATOM   2600  C   VAL A 318      89.399  -6.616 -26.692  1.00 43.22           C  
ANISOU 2600  C   VAL A 318     4870   4260   7290   -132    189   -298       C  
ATOM   2601  O   VAL A 318      89.321  -5.383 -26.685  1.00 42.89           O  
ANISOU 2601  O   VAL A 318     4752   4086   7457   -218    332   -355       O  
ATOM   2602  CB  VAL A 318      90.195  -7.229 -24.383  1.00 55.59           C  
ANISOU 2602  CB  VAL A 318     6438   6060   8623   -245    -53   -592       C  
ATOM   2603  CG1 VAL A 318      88.783  -7.729 -24.076  1.00 48.39           C  
ANISOU 2603  CG1 VAL A 318     5709   5105   7572   -209    -51   -551       C  
ATOM   2604  CG2 VAL A 318      91.244  -8.000 -23.577  1.00 55.59           C  
ANISOU 2604  CG2 VAL A 318     6388   6266   8470   -241   -251   -658       C  
ATOM   2605  N   VAL A 319      88.568  -7.398 -27.378  1.00 34.63           N  
ANISOU 2605  N   VAL A 319     3905   3176   6078    -39    170   -131       N  
ATOM   2606  CA  VAL A 319      87.431  -6.911 -28.152  1.00 36.46           C  
ANISOU 2606  CA  VAL A 319     4169   3293   6393    -24    275     22       C  
ATOM   2607  C   VAL A 319      86.155  -7.368 -27.449  1.00 39.75           C  
ANISOU 2607  C   VAL A 319     4695   3725   6682    -23    230     12       C  
ATOM   2608  O   VAL A 319      86.027  -8.549 -27.097  1.00 39.27           O  
ANISOU 2608  O   VAL A 319     4753   3777   6392     11    112      0       O  
ATOM   2609  CB  VAL A 319      87.493  -7.438 -29.600  1.00 39.62           C  
ANISOU 2609  CB  VAL A 319     4616   3710   6729     41    284    229       C  
ATOM   2610  CG1 VAL A 319      86.156  -7.315 -30.282  1.00 39.24           C  
ANISOU 2610  CG1 VAL A 319     4620   3618   6670     52    317    415       C  
ATOM   2611  CG2 VAL A 319      88.567  -6.677 -30.403  1.00 43.61           C  
ANISOU 2611  CG2 VAL A 319     5006   4148   7416     25    391    254       C  
ATOM   2612  N   LYS A 320      85.221  -6.434 -27.233  1.00 36.75           N  
ANISOU 2612  N   LYS A 320     4277   3219   6468    -58    347     20       N  
ATOM   2613  CA  LYS A 320      83.959  -6.716 -26.551  1.00 40.44           C  
ANISOU 2613  CA  LYS A 320     4820   3678   6866    -64    343      5       C  
ATOM   2614  C   LYS A 320      82.830  -6.853 -27.566  1.00 41.23           C  
ANISOU 2614  C   LYS A 320     4918   3770   6978     -6    358    248       C  
ATOM   2615  O   LYS A 320      82.625  -5.964 -28.404  1.00 40.21           O  
ANISOU 2615  O   LYS A 320     4685   3544   7049     18    458    403       O  
ATOM   2616  CB  LYS A 320      83.606  -5.612 -25.554  1.00 44.32           C  
ANISOU 2616  CB  LYS A 320     5264   4025   7551   -145    494   -152       C  
ATOM   2617  CG  LYS A 320      84.607  -5.411 -24.426  1.00 51.05           C  
ANISOU 2617  CG  LYS A 320     6127   4908   8361   -256    471   -412       C  
ATOM   2618  CD  LYS A 320      84.669  -6.615 -23.505  1.00 57.34           C  
ANISOU 2618  CD  LYS A 320     7060   5867   8861   -269    297   -514       C  
ATOM   2619  CE  LYS A 320      85.593  -6.354 -22.319  1.00 68.76           C  
ANISOU 2619  CE  LYS A 320     8508   7372  10248   -403    252   -754       C  
ATOM   2620  NZ  LYS A 320      85.163  -5.182 -21.511  1.00 74.51           N  
ANISOU 2620  NZ  LYS A 320     9234   7940  11136   -549    444   -928       N  
ATOM   2621  N   VAL A 321      82.079  -7.945 -27.469  1.00 36.17           N  
ANISOU 2621  N   VAL A 321     4389   3235   6119      5    260    288       N  
ATOM   2622  CA  VAL A 321      80.961  -8.217 -28.371  1.00 38.46           C  
ANISOU 2622  CA  VAL A 321     4674   3566   6374     24    241    512       C  
ATOM   2623  C   VAL A 321      79.769  -8.642 -27.526  1.00 39.96           C  
ANISOU 2623  C   VAL A 321     4912   3774   6498      0    237    460       C  
ATOM   2624  O   VAL A 321      79.854  -9.628 -26.790  1.00 37.48           O  
ANISOU 2624  O   VAL A 321     4742   3535   5965    -24    164    324       O  
ATOM   2625  CB  VAL A 321      81.295  -9.317 -29.395  1.00 34.66           C  
ANISOU 2625  CB  VAL A 321     4304   3218   5649     25    132    626       C  
ATOM   2626  CG1 VAL A 321      80.202  -9.398 -30.460  1.00 39.33           C  
ANISOU 2626  CG1 VAL A 321     4869   3871   6206      2    106    872       C  
ATOM   2627  CG2 VAL A 321      82.684  -9.099 -30.018  1.00 35.01           C  
ANISOU 2627  CG2 VAL A 321     4327   3243   5731     45    151    620       C  
ATOM   2628  N   THR A 322      78.652  -7.931 -27.652  1.00 35.43           N  
ANISOU 2628  N   THR A 322     4213   3128   6120     12    325    584       N  
ATOM   2629  CA  THR A 322      77.446  -8.336 -26.937  1.00 30.52           C  
ANISOU 2629  CA  THR A 322     3615   2522   5459    -14    342    551       C  
ATOM   2630  C   THR A 322      76.798  -9.519 -27.660  1.00 33.28           C  
ANISOU 2630  C   THR A 322     4040   3049   5557    -46    204    691       C  
ATOM   2631  O   THR A 322      76.414  -9.418 -28.832  1.00 36.63           O  
ANISOU 2631  O   THR A 322     4377   3543   5997    -44    154    927       O  
ATOM   2632  CB  THR A 322      76.464  -7.173 -26.799  1.00 40.56           C  
ANISOU 2632  CB  THR A 322     4702   3647   7063     23    508    646       C  
ATOM   2633  OG1 THR A 322      77.090  -6.100 -26.078  1.00 39.03           O  
ANISOU 2633  OG1 THR A 322     4476   3267   7086     21    673    480       O  
ATOM   2634  CG2 THR A 322      75.222  -7.624 -26.024  1.00 39.00           C  
ANISOU 2634  CG2 THR A 322     4517   3462   6839     -8    547    599       C  
ATOM   2635  N   ILE A 323      76.670 -10.640 -26.953  1.00 35.89           N  
ANISOU 2635  N   ILE A 323     4544   3453   5641    -94    148    546       N  
ATOM   2636  CA  ILE A 323      76.134 -11.881 -27.503  1.00 31.09           C  
ANISOU 2636  CA  ILE A 323     4053   2997   4762   -155     45    627       C  
ATOM   2637  C   ILE A 323      75.230 -12.501 -26.449  1.00 32.36           C  
ANISOU 2637  C   ILE A 323     4302   3165   4830   -206     77    499       C  
ATOM   2638  O   ILE A 323      75.604 -12.574 -25.272  1.00 33.45           O  
ANISOU 2638  O   ILE A 323     4541   3230   4937   -199    122    293       O  
ATOM   2639  CB  ILE A 323      77.265 -12.867 -27.884  1.00 33.37           C  
ANISOU 2639  CB  ILE A 323     4531   3354   4795   -157    -34    576       C  
ATOM   2640  CG1 ILE A 323      78.339 -12.174 -28.754  1.00 37.49           C  
ANISOU 2640  CG1 ILE A 323     4971   3840   5434   -106    -31    659       C  
ATOM   2641  CG2 ILE A 323      76.688 -14.076 -28.609  1.00 34.12           C  
ANISOU 2641  CG2 ILE A 323     4762   3583   4618   -248    -99    665       C  
ATOM   2642  CD1 ILE A 323      79.483 -13.111 -29.184  1.00 36.28           C  
ANISOU 2642  CD1 ILE A 323     4981   3735   5070    -96    -74    620       C  
ATOM   2643  N   ASP A 324      74.045 -12.948 -26.867  1.00 34.20           N  
ANISOU 2643  N   ASP A 324     4495   3494   5004   -274     51    621       N  
ATOM   2644  CA  ASP A 324      73.057 -13.493 -25.933  1.00 29.97           C  
ANISOU 2644  CA  ASP A 324     4022   2961   4406   -335    105    511       C  
ATOM   2645  C   ASP A 324      72.850 -12.543 -24.755  1.00 34.72           C  
ANISOU 2645  C   ASP A 324     4542   3394   5256   -290    256    375       C  
ATOM   2646  O   ASP A 324      72.678 -12.970 -23.610  1.00 36.94           O  
ANISOU 2646  O   ASP A 324     4969   3626   5441   -329    320    182       O  
ATOM   2647  CB  ASP A 324      73.470 -14.882 -25.435  1.00 29.93           C  
ANISOU 2647  CB  ASP A 324     4308   3002   4060   -386     63    352       C  
ATOM   2648  CG  ASP A 324      73.584 -15.902 -26.543  1.00 37.20           C  
ANISOU 2648  CG  ASP A 324     5347   4059   4728   -457    -32    459       C  
ATOM   2649  OD1 ASP A 324      72.962 -15.717 -27.619  1.00 35.08           O  
ANISOU 2649  OD1 ASP A 324     4942   3894   4492   -519    -83    653       O  
ATOM   2650  OD2 ASP A 324      74.290 -16.931 -26.324  1.00 39.12           O  
ANISOU 2650  OD2 ASP A 324     5832   4306   4727   -458    -46    353       O  
ATOM   2651  N   TYR A 325      72.905 -11.236 -25.043  1.00 38.71           N  
ANISOU 2651  N   TYR A 325     4836   3797   6077   -217    334    473       N  
ATOM   2652  CA  TYR A 325      72.684 -10.129 -24.115  1.00 38.01           C  
ANISOU 2652  CA  TYR A 325     4649   3515   6278   -183    527    367       C  
ATOM   2653  C   TYR A 325      73.823  -9.907 -23.124  1.00 41.07           C  
ANISOU 2653  C   TYR A 325     5193   3802   6610   -197    571    112       C  
ATOM   2654  O   TYR A 325      73.710  -9.010 -22.289  1.00 47.25           O  
ANISOU 2654  O   TYR A 325     5937   4418   7598   -208    750    -16       O  
ATOM   2655  CB  TYR A 325      71.379 -10.274 -23.310  1.00 37.29           C  
ANISOU 2655  CB  TYR A 325     4528   3381   6260   -228    656    312       C  
ATOM   2656  CG  TYR A 325      70.131 -10.227 -24.159  1.00 38.49           C  
ANISOU 2656  CG  TYR A 325     4448   3625   6553   -216    637    576       C  
ATOM   2657  CD1 TYR A 325      69.737  -9.042 -24.788  1.00 42.33           C  
ANISOU 2657  CD1 TYR A 325     4652   4034   7397   -117    716    803       C  
ATOM   2658  CD2 TYR A 325      69.328 -11.352 -24.314  1.00 35.95           C  
ANISOU 2658  CD2 TYR A 325     4178   3469   6012   -310    544    609       C  
ATOM   2659  CE1 TYR A 325      68.587  -8.988 -25.562  1.00 42.91           C  
ANISOU 2659  CE1 TYR A 325     4480   4223   7603   -102    672   1082       C  
ATOM   2660  CE2 TYR A 325      68.167 -11.308 -25.090  1.00 39.13           C  
ANISOU 2660  CE2 TYR A 325     4338   3994   6535   -325    503    860       C  
ATOM   2661  CZ  TYR A 325      67.808 -10.122 -25.712  1.00 41.82           C  
ANISOU 2661  CZ  TYR A 325     4378   4282   7229   -215    552   1107       C  
ATOM   2662  OH  TYR A 325      66.668 -10.070 -26.480  1.00 43.84           O  
ANISOU 2662  OH  TYR A 325     4364   4687   7605   -225    484   1390       O  
ATOM   2663  N   THR A 326      74.919 -10.664 -23.191  1.00 38.09           N  
ANISOU 2663  N   THR A 326     4981   3521   5970   -206    424     38       N  
ATOM   2664  CA  THR A 326      76.042 -10.435 -22.288  1.00 40.22           C  
ANISOU 2664  CA  THR A 326     5360   3736   6186   -227    431   -176       C  
ATOM   2665  C   THR A 326      77.266  -9.979 -23.085  1.00 38.52           C  
ANISOU 2665  C   THR A 326     5067   3535   6032   -175    362   -111       C  
ATOM   2666  O   THR A 326      77.371 -10.216 -24.292  1.00 37.17           O  
ANISOU 2666  O   THR A 326     4840   3441   5842   -127    280     79       O  
ATOM   2667  CB  THR A 326      76.346 -11.708 -21.463  1.00 37.14           C  
ANISOU 2667  CB  THR A 326     5217   3440   5453   -271    329   -322       C  
ATOM   2668  OG1 THR A 326      77.069 -11.359 -20.275  1.00 49.50           O  
ANISOU 2668  OG1 THR A 326     6873   4955   6982   -327    357   -538       O  
ATOM   2669  CG2 THR A 326      77.157 -12.704 -22.259  1.00 36.91           C  
ANISOU 2669  CG2 THR A 326     5273   3545   5205   -220    163   -228       C  
ATOM   2670  N   GLU A 327      78.194  -9.295 -22.410  1.00 36.71           N  
ANISOU 2670  N   GLU A 327     4841   3235   5873   -206    405   -275       N  
ATOM   2671  CA  GLU A 327      79.430  -8.849 -23.060  1.00 33.48           C  
ANISOU 2671  CA  GLU A 327     4353   2839   5530   -173    353   -242       C  
ATOM   2672  C   GLU A 327      80.454  -9.981 -23.043  1.00 36.39           C  
ANISOU 2672  C   GLU A 327     4848   3359   5619   -152    173   -277       C  
ATOM   2673  O   GLU A 327      80.969 -10.344 -21.983  1.00 42.84           O  
ANISOU 2673  O   GLU A 327     5773   4221   6284   -199    116   -444       O  
ATOM   2674  CB  GLU A 327      79.996  -7.609 -22.370  1.00 48.48           C  
ANISOU 2674  CB  GLU A 327     6185   4604   7630   -243    486   -409       C  
ATOM   2675  CG  GLU A 327      79.392  -6.284 -22.836  1.00 77.23           C  
ANISOU 2675  CG  GLU A 327     9660   8059  11625   -220    695   -312       C  
ATOM   2676  CD  GLU A 327      80.370  -5.114 -22.701  1.00102.11           C  
ANISOU 2676  CD  GLU A 327    12737  11092  14970   -279    810   -428       C  
ATOM   2677  OE1 GLU A 327      81.345  -5.237 -21.927  1.00106.48           O  
ANISOU 2677  OE1 GLU A 327    13366  11710  15384   -377    741   -633       O  
ATOM   2678  OE2 GLU A 327      80.171  -4.078 -23.377  1.00108.66           O  
ANISOU 2678  OE2 GLU A 327    13429  11771  16086   -234    967   -304       O  
ATOM   2679  N   ILE A 328      80.759 -10.538 -24.215  1.00 35.19           N  
ANISOU 2679  N   ILE A 328     4686   3283   5400    -85     93   -110       N  
ATOM   2680  CA  ILE A 328      81.777 -11.582 -24.355  1.00 36.05           C  
ANISOU 2680  CA  ILE A 328     4897   3505   5295    -41    -34   -115       C  
ATOM   2681  C   ILE A 328      83.097 -10.921 -24.733  1.00 39.79           C  
ANISOU 2681  C   ILE A 328     5245   3969   5905    -18    -40   -126       C  
ATOM   2682  O   ILE A 328      83.148 -10.124 -25.675  1.00 36.86           O  
ANISOU 2682  O   ILE A 328     4750   3534   5722     -8     32    -19       O  
ATOM   2683  CB  ILE A 328      81.374 -12.620 -25.416  1.00 33.49           C  
ANISOU 2683  CB  ILE A 328     4664   3250   4809     -7    -74     51       C  
ATOM   2684  CG1 ILE A 328      80.066 -13.306 -25.021  1.00 36.73           C  
ANISOU 2684  CG1 ILE A 328     5191   3682   5081    -53    -65     50       C  
ATOM   2685  CG2 ILE A 328      82.507 -13.644 -25.630  1.00 35.59           C  
ANISOU 2685  CG2 ILE A 328     5033   3590   4900     57   -150     54       C  
ATOM   2686  CD1 ILE A 328      80.176 -14.133 -23.730  1.00 36.77           C  
ANISOU 2686  CD1 ILE A 328     5371   3714   4884    -62   -106   -107       C  
ATOM   2687  N   SER A 329      84.165 -11.261 -24.019  1.00 39.65           N  
ANISOU 2687  N   SER A 329     5250   4021   5792    -13   -127   -242       N  
ATOM   2688  CA  SER A 329      85.495 -10.759 -24.348  1.00 37.62           C  
ANISOU 2688  CA  SER A 329     4856   3782   5657      0   -144   -257       C  
ATOM   2689  C   SER A 329      86.185 -11.699 -25.333  1.00 41.69           C  
ANISOU 2689  C   SER A 329     5400   4360   6082    103   -188   -122       C  
ATOM   2690  O   SER A 329      86.267 -12.908 -25.096  1.00 39.75           O  
ANISOU 2690  O   SER A 329     5288   4186   5628    164   -262   -100       O  
ATOM   2691  CB  SER A 329      86.343 -10.607 -23.087  1.00 36.51           C  
ANISOU 2691  CB  SER A 329     4688   3713   5470    -62   -229   -436       C  
ATOM   2692  OG  SER A 329      85.829  -9.597 -22.261  1.00 43.98           O  
ANISOU 2692  OG  SER A 329     5617   4577   6518   -189   -142   -584       O  
ATOM   2693  N   PHE A 330      86.669 -11.137 -26.438  1.00 38.07           N  
ANISOU 2693  N   PHE A 330     4831   3853   5781    117   -116    -31       N  
ATOM   2694  CA  PHE A 330      87.482 -11.847 -27.420  1.00 36.75           C  
ANISOU 2694  CA  PHE A 330     4679   3718   5566    195   -112     77       C  
ATOM   2695  C   PHE A 330      88.914 -11.327 -27.354  1.00 39.20           C  
ANISOU 2695  C   PHE A 330     4815   4049   6031    205   -115     13       C  
ATOM   2696  O   PHE A 330      89.137 -10.130 -27.168  1.00 38.34           O  
ANISOU 2696  O   PHE A 330     4566   3888   6112    128    -69    -64       O  
ATOM   2697  CB  PHE A 330      86.973 -11.634 -28.852  1.00 35.00           C  
ANISOU 2697  CB  PHE A 330     4478   3433   5386    181    -15    241       C  
ATOM   2698  CG  PHE A 330      85.712 -12.386 -29.203  1.00 34.33           C  
ANISOU 2698  CG  PHE A 330     4556   3369   5116    160    -24    337       C  
ATOM   2699  CD1 PHE A 330      84.480 -11.989 -28.698  1.00 35.25           C  
ANISOU 2699  CD1 PHE A 330     4673   3469   5253    110    -32    327       C  
ATOM   2700  CD2 PHE A 330      85.751 -13.428 -30.114  1.00 39.43           C  
ANISOU 2700  CD2 PHE A 330     5350   4047   5587    171     -1    438       C  
ATOM   2701  CE1 PHE A 330      83.319 -12.656 -29.052  1.00 35.19           C  
ANISOU 2701  CE1 PHE A 330     4784   3501   5088     72    -46    419       C  
ATOM   2702  CE2 PHE A 330      84.594 -14.105 -30.479  1.00 43.21           C  
ANISOU 2702  CE2 PHE A 330     5976   4561   5882    111     -9    516       C  
ATOM   2703  CZ  PHE A 330      83.376 -13.715 -29.945  1.00 40.36           C  
ANISOU 2703  CZ  PHE A 330     5586   4208   5542     61    -45    510       C  
ATOM   2704  N   MET A 331      89.879 -12.213 -27.544  1.00 34.19           N  
ANISOU 2704  N   MET A 331     4181   3478   5332    296   -148     50       N  
ATOM   2705  CA  MET A 331      91.270 -11.805 -27.698  1.00 35.27           C  
ANISOU 2705  CA  MET A 331     4124   3643   5636    313   -138     21       C  
ATOM   2706  C   MET A 331      91.574 -11.665 -29.182  1.00 41.23           C  
ANISOU 2706  C   MET A 331     4869   4309   6488    331     13    140       C  
ATOM   2707  O   MET A 331      91.359 -12.602 -29.954  1.00 41.42           O  
ANISOU 2707  O   MET A 331     5046   4312   6382    389     70    250       O  
ATOM   2708  CB  MET A 331      92.219 -12.824 -27.061  1.00 39.70           C  
ANISOU 2708  CB  MET A 331     4654   4323   6108    421   -246     20       C  
ATOM   2709  CG  MET A 331      92.191 -12.836 -25.548  1.00 55.74           C  
ANISOU 2709  CG  MET A 331     6667   6470   8042    381   -415    -95       C  
ATOM   2710  SD  MET A 331      92.689 -11.250 -24.835  1.00 65.40           S  
ANISOU 2710  SD  MET A 331     7669   7728   9452    198   -448   -278       S  
ATOM   2711  CE  MET A 331      94.141 -10.837 -25.812  1.00 49.70           C  
ANISOU 2711  CE  MET A 331     5434   5742   7709    229   -366   -233       C  
ATOM   2712  N   LEU A 332      92.068 -10.497 -29.578  1.00 37.52           N  
ANISOU 2712  N   LEU A 332     4241   3781   6235    262     94    110       N  
ATOM   2713  CA  LEU A 332      92.436 -10.225 -30.961  1.00 35.18           C  
ANISOU 2713  CA  LEU A 332     3934   3394   6038    260    249    217       C  
ATOM   2714  C   LEU A 332      93.942 -10.029 -31.024  1.00 41.01           C  
ANISOU 2714  C   LEU A 332     4473   4160   6948    281    288    164       C  
ATOM   2715  O   LEU A 332      94.479  -9.123 -30.372  1.00 42.94           O  
ANISOU 2715  O   LEU A 332     4535   4431   7350    206    259     40       O  
ATOM   2716  CB  LEU A 332      91.715  -8.984 -31.493  1.00 38.65           C  
ANISOU 2716  CB  LEU A 332     4362   3721   6604    168    342    258       C  
ATOM   2717  CG  LEU A 332      92.164  -8.553 -32.892  1.00 41.75           C  
ANISOU 2717  CG  LEU A 332     4745   4020   7100    148    503    372       C  
ATOM   2718  CD1 LEU A 332      91.797  -9.634 -33.919  1.00 37.79           C  
ANISOU 2718  CD1 LEU A 332     4445   3526   6387    181    540    520       C  
ATOM   2719  CD2 LEU A 332      91.548  -7.201 -33.277  1.00 40.40           C  
ANISOU 2719  CD2 LEU A 332     4535   3729   7087     72    594    427       C  
ATOM   2720  N   TRP A 333      94.615 -10.886 -31.791  1.00 40.30           N  
ANISOU 2720  N   TRP A 333     4417   4064   6833    368    371    249       N  
ATOM   2721  CA  TRP A 333      96.047 -10.801 -32.033  1.00 39.34           C  
ANISOU 2721  CA  TRP A 333     4095   3958   6896    402    444    226       C  
ATOM   2722  C   TRP A 333      96.285 -10.523 -33.509  1.00 43.81           C  
ANISOU 2722  C   TRP A 333     4716   4391   7540    369    664    316       C  
ATOM   2723  O   TRP A 333      95.751 -11.234 -34.370  1.00 43.09           O  
ANISOU 2723  O   TRP A 333     4847   4238   7287    388    752    425       O  
ATOM   2724  CB  TRP A 333      96.754 -12.096 -31.636  1.00 41.44           C  
ANISOU 2724  CB  TRP A 333     4337   4311   7099    554    391    260       C  
ATOM   2725  CG  TRP A 333      96.784 -12.340 -30.167  1.00 47.37           C  
ANISOU 2725  CG  TRP A 333     5002   5215   7782    585    166    187       C  
ATOM   2726  CD1 TRP A 333      95.773 -12.846 -29.393  1.00 44.46           C  
ANISOU 2726  CD1 TRP A 333     4809   4886   7198    595     37    177       C  
ATOM   2727  CD2 TRP A 333      97.889 -12.105 -29.287  1.00 45.66           C  
ANISOU 2727  CD2 TRP A 333     4506   5145   7696    591     38    117       C  
ATOM   2728  NE1 TRP A 333      96.188 -12.935 -28.081  1.00 46.17           N  
ANISOU 2728  NE1 TRP A 333     4896   5259   7390    607   -158    107       N  
ATOM   2729  CE2 TRP A 333      97.479 -12.487 -27.990  1.00 44.46           C  
ANISOU 2729  CE2 TRP A 333     4394   5124   7376    600   -176     75       C  
ATOM   2730  CE3 TRP A 333      99.182 -11.603 -29.466  1.00 50.88           C  
ANISOU 2730  CE3 TRP A 333     4882   5855   8595    574     80     87       C  
ATOM   2731  CZ2 TRP A 333      98.318 -12.380 -26.882  1.00 47.96           C  
ANISOU 2731  CZ2 TRP A 333     4607   5758   7856    583   -368     15       C  
ATOM   2732  CZ3 TRP A 333     100.016 -11.504 -28.367  1.00 55.55           C  
ANISOU 2732  CZ3 TRP A 333     5219   6645   9244    559   -113     26       C  
ATOM   2733  CH2 TRP A 333      99.582 -11.890 -27.091  1.00 54.01           C  
ANISOU 2733  CH2 TRP A 333     5077   6593   8853    560   -345     -4       C  
ATOM   2734  N   CYS A 334      97.116  -9.518 -33.794  1.00 42.43           N  
ANISOU 2734  N   CYS A 334     4351   4174   7595    300    759    264       N  
ATOM   2735  CA  CYS A 334      97.386  -9.083 -35.155  1.00 44.95           C  
ANISOU 2735  CA  CYS A 334     4722   4358   7999    248    980    342       C  
ATOM   2736  C   CYS A 334      98.884  -8.942 -35.383  1.00 48.64           C  
ANISOU 2736  C   CYS A 334     4962   4824   8696    263   1102    290       C  
ATOM   2737  O   CYS A 334      99.662  -8.727 -34.451  1.00 47.51           O  
ANISOU 2737  O   CYS A 334     4568   4791   8691    269    997    181       O  
ATOM   2738  CB  CYS A 334      96.714  -7.750 -35.462  1.00 44.02           C  
ANISOU 2738  CB  CYS A 334     4626   4143   7958    125   1028    353       C  
ATOM   2739  SG  CYS A 334      94.902  -7.832 -35.395  1.00 46.64           S  
ANISOU 2739  SG  CYS A 334     5190   4468   8062    110    916    455       S  
ATOM   2740  N   LYS A 335      99.276  -9.042 -36.651  1.00 45.62           N  
ANISOU 2740  N   LYS A 335     4666   4323   8347    251   1328    371       N  
ATOM   2741  CA  LYS A 335     100.661  -8.813 -37.038  1.00 52.86           C  
ANISOU 2741  CA  LYS A 335     5370   5208   9506    251   1495    328       C  
ATOM   2742  C   LYS A 335     100.679  -8.195 -38.427  1.00 56.54           C  
ANISOU 2742  C   LYS A 335     5971   5503  10007    146   1746    398       C  
ATOM   2743  O   LYS A 335     100.063  -8.730 -39.354  1.00 51.33           O  
ANISOU 2743  O   LYS A 335     5589   4765   9147    136   1844    514       O  
ATOM   2744  CB  LYS A 335     101.478 -10.111 -37.016  1.00 57.95           C  
ANISOU 2744  CB  LYS A 335     5959   5895  10164    406   1546    362       C  
ATOM   2745  CG  LYS A 335     102.921  -9.918 -37.472  1.00 65.40           C  
ANISOU 2745  CG  LYS A 335     6657   6802  11389    417   1745    331       C  
ATOM   2746  CD  LYS A 335     103.692 -11.235 -37.485  1.00 75.21           C  
ANISOU 2746  CD  LYS A 335     7840   8060  12676    600   1830    393       C  
ATOM   2747  CE  LYS A 335     104.093 -11.664 -36.080  1.00 85.01           C  
ANISOU 2747  CE  LYS A 335     8820   9508  13974    724   1565    369       C  
ATOM   2748  NZ  LYS A 335     105.580 -11.664 -35.906  1.00 96.06           N  
ANISOU 2748  NZ  LYS A 335     9830  10982  15685    796   1626    356       N  
ATOM   2749  N   ASP A 336     101.371  -7.064 -38.551  1.00 58.71           N  
ANISOU 2749  N   ASP A 336     6060   5726  10520     49   1850    325       N  
ATOM   2750  CA  ASP A 336     101.546  -6.366 -39.826  1.00 61.17           C  
ANISOU 2750  CA  ASP A 336     6480   5867  10894    -57   2106    389       C  
ATOM   2751  C   ASP A 336     100.211  -6.110 -40.525  1.00 61.40           C  
ANISOU 2751  C   ASP A 336     6815   5818  10697   -116   2099    536       C  
ATOM   2752  O   ASP A 336     100.088  -6.253 -41.743  1.00 66.60           O  
ANISOU 2752  O   ASP A 336     7689   6374  11243   -169   2274    655       O  
ATOM   2753  CB  ASP A 336     102.500  -7.135 -40.739  1.00 64.33           C  
ANISOU 2753  CB  ASP A 336     6903   6199  11342    -16   2349    421       C  
ATOM   2754  CG  ASP A 336     103.894  -7.269 -40.145  1.00 76.78           C  
ANISOU 2754  CG  ASP A 336     8122   7855  13196     46   2376    305       C  
ATOM   2755  OD1 ASP A 336     104.356  -6.310 -39.488  1.00 77.13           O  
ANISOU 2755  OD1 ASP A 336     7909   7954  13442    -30   2308    189       O  
ATOM   2756  OD2 ASP A 336     104.523  -8.338 -40.326  1.00 83.88           O  
ANISOU 2756  OD2 ASP A 336     8992   8761  14117    166   2471    334       O  
ATOM   2757  N   GLY A 337      99.194  -5.739 -39.746  1.00 57.69           N  
ANISOU 2757  N   GLY A 337     6360   5404  10155   -116   1894    536       N  
ATOM   2758  CA  GLY A 337      97.911  -5.380 -40.316  1.00 49.33           C  
ANISOU 2758  CA  GLY A 337     5528   4288   8926   -163   1867    695       C  
ATOM   2759  C   GLY A 337      96.994  -6.532 -40.669  1.00 56.49           C  
ANISOU 2759  C   GLY A 337     6682   5263   9519   -127   1776    814       C  
ATOM   2760  O   GLY A 337      95.915  -6.289 -41.225  1.00 53.83           O  
ANISOU 2760  O   GLY A 337     6519   4909   9026   -180   1739    969       O  
ATOM   2761  N   HIS A 338      97.381  -7.773 -40.373  1.00 53.85           N  
ANISOU 2761  N   HIS A 338     6364   5005   9093    -45   1746    756       N  
ATOM   2762  CA  HIS A 338      96.534  -8.940 -40.588  1.00 55.70           C  
ANISOU 2762  CA  HIS A 338     6839   5297   9027    -26   1676    837       C  
ATOM   2763  C   HIS A 338      96.194  -9.600 -39.256  1.00 51.16           C  
ANISOU 2763  C   HIS A 338     6191   4845   8404     81   1459    749       C  
ATOM   2764  O   HIS A 338      96.940  -9.485 -38.281  1.00 47.57           O  
ANISOU 2764  O   HIS A 338     5505   4443   8128    154   1391    625       O  
ATOM   2765  CB  HIS A 338      97.211  -9.982 -41.491  1.00 60.42           C  
ANISOU 2765  CB  HIS A 338     7591   5837   9528    -26   1886    857       C  
ATOM   2766  CG  HIS A 338      97.669  -9.442 -42.809  1.00 86.18           C  
ANISOU 2766  CG  HIS A 338    10950   8974  12821   -143   2130    929       C  
ATOM   2767  ND1 HIS A 338      96.797  -8.950 -43.757  1.00 92.63           N  
ANISOU 2767  ND1 HIS A 338    11975   9762  13458   -280   2143   1084       N  
ATOM   2768  CD2 HIS A 338      98.907  -9.332 -43.345  1.00 94.55           C  
ANISOU 2768  CD2 HIS A 338    11927   9931  14066   -149   2374    878       C  
ATOM   2769  CE1 HIS A 338      97.480  -8.554 -44.816  1.00 95.28           C  
ANISOU 2769  CE1 HIS A 338    12377   9978  13845   -371   2384   1123       C  
ATOM   2770  NE2 HIS A 338      98.762  -8.774 -44.592  1.00 93.91           N  
ANISOU 2770  NE2 HIS A 338    12033   9750  13900   -296   2542    989       N  
ATOM   2771  N   VAL A 339      95.068 -10.317 -39.230  1.00 46.70           N  
ANISOU 2771  N   VAL A 339     5828   4338   7580     73   1349    818       N  
ATOM   2772  CA  VAL A 339      94.718 -11.117 -38.060  1.00 38.30           C  
ANISOU 2772  CA  VAL A 339     4748   3376   6430    168   1173    745       C  
ATOM   2773  C   VAL A 339      95.686 -12.278 -37.899  1.00 42.96           C  
ANISOU 2773  C   VAL A 339     5330   3970   7024    281   1256    694       C  
ATOM   2774  O   VAL A 339      96.021 -12.971 -38.869  1.00 42.55           O  
ANISOU 2774  O   VAL A 339     5439   3840   6887    264   1451    746       O  
ATOM   2775  CB  VAL A 339      93.282 -11.656 -38.169  1.00 44.75           C  
ANISOU 2775  CB  VAL A 339     5792   4245   6968    115   1067    831       C  
ATOM   2776  CG1 VAL A 339      92.921 -12.403 -36.895  1.00 40.81           C  
ANISOU 2776  CG1 VAL A 339     5280   3837   6391    208    900    746       C  
ATOM   2777  CG2 VAL A 339      92.307 -10.528 -38.436  1.00 41.71           C  
ANISOU 2777  CG2 VAL A 339     5392   3852   6602     24   1002    926       C  
ATOM   2778  N   GLU A 340      96.123 -12.517 -36.662  1.00 41.69           N  
ANISOU 2778  N   GLU A 340     4990   3895   6957    395   1117    603       N  
ATOM   2779  CA  GLU A 340      96.779 -13.778 -36.319  1.00 43.46           C  
ANISOU 2779  CA  GLU A 340     5221   4138   7156    538   1153    597       C  
ATOM   2780  C   GLU A 340      95.812 -14.770 -35.683  1.00 46.37           C  
ANISOU 2780  C   GLU A 340     5780   4561   7276    582   1025    611       C  
ATOM   2781  O   GLU A 340      95.731 -15.928 -36.113  1.00 43.98           O  
ANISOU 2781  O   GLU A 340     5687   4201   6822    622   1150    660       O  
ATOM   2782  CB  GLU A 340      97.965 -13.539 -35.382  1.00 49.67           C  
ANISOU 2782  CB  GLU A 340     5677   5007   8187    642   1073    521       C  
ATOM   2783  CG  GLU A 340      99.113 -12.809 -36.036  1.00 73.54           C  
ANISOU 2783  CG  GLU A 340     8500   7971  11470    609   1241    501       C  
ATOM   2784  CD  GLU A 340     100.455 -13.237 -35.485  1.00 85.24           C  
ANISOU 2784  CD  GLU A 340     9702   9522  13162    751   1244    482       C  
ATOM   2785  OE1 GLU A 340     100.587 -13.344 -34.246  1.00 90.21           O  
ANISOU 2785  OE1 GLU A 340    10166  10304  13806    817   1015    442       O  
ATOM   2786  OE2 GLU A 340     101.371 -13.482 -36.299  1.00 88.08           O  
ANISOU 2786  OE2 GLU A 340    10007   9790  13671    792   1478    516       O  
ATOM   2787  N   THR A 341      95.087 -14.345 -34.650  1.00 40.75           N  
ANISOU 2787  N   THR A 341     5014   3945   6525    564    805    559       N  
ATOM   2788  CA  THR A 341      93.943 -15.111 -34.175  1.00 39.71           C  
ANISOU 2788  CA  THR A 341     5090   3852   6146    563    700    572       C  
ATOM   2789  C   THR A 341      92.940 -14.180 -33.504  1.00 41.10           C  
ANISOU 2789  C   THR A 341     5218   4086   6311    476    529    527       C  
ATOM   2790  O   THR A 341      93.227 -13.017 -33.204  1.00 39.74           O  
ANISOU 2790  O   THR A 341     4849   3923   6327    435    486    471       O  
ATOM   2791  CB  THR A 341      94.353 -16.231 -33.214  1.00 45.01           C  
ANISOU 2791  CB  THR A 341     5762   4574   6765    719    636    556       C  
ATOM   2792  OG1 THR A 341      93.211 -17.045 -32.938  1.00 45.67           O  
ANISOU 2792  OG1 THR A 341     6093   4666   6593    697    585    571       O  
ATOM   2793  CG2 THR A 341      94.868 -15.656 -31.907  1.00 39.37           C  
ANISOU 2793  CG2 THR A 341     4789   3981   6191    770    437    475       C  
ATOM   2794  N   PHE A 342      91.761 -14.741 -33.237  1.00 40.55           N  
ANISOU 2794  N   PHE A 342     5336   4044   6027    445    456    546       N  
ATOM   2795  CA  PHE A 342      90.623 -14.004 -32.701  1.00 36.54           C  
ANISOU 2795  CA  PHE A 342     4814   3571   5498    365    332    522       C  
ATOM   2796  C   PHE A 342      89.738 -15.050 -32.045  1.00 40.76           C  
ANISOU 2796  C   PHE A 342     5530   4154   5804    382    252    509       C  
ATOM   2797  O   PHE A 342      89.139 -15.860 -32.754  1.00 42.78           O  
ANISOU 2797  O   PHE A 342     5994   4392   5868    335    321    579       O  
ATOM   2798  CB  PHE A 342      89.897 -13.273 -33.828  1.00 36.86           C  
ANISOU 2798  CB  PHE A 342     4901   3564   5541    248    400    629       C  
ATOM   2799  CG  PHE A 342      88.729 -12.430 -33.386  1.00 40.88           C  
ANISOU 2799  CG  PHE A 342     5362   4088   6083    186    306    638       C  
ATOM   2800  CD1 PHE A 342      88.892 -11.417 -32.451  1.00 40.12           C  
ANISOU 2800  CD1 PHE A 342     5083   3977   6183    196    256    536       C  
ATOM   2801  CD2 PHE A 342      87.482 -12.608 -33.965  1.00 41.89           C  
ANISOU 2801  CD2 PHE A 342     5619   4240   6057    105    288    754       C  
ATOM   2802  CE1 PHE A 342      87.811 -10.616 -32.070  1.00 39.37           C  
ANISOU 2802  CE1 PHE A 342     4948   3860   6151    147    220    547       C  
ATOM   2803  CE2 PHE A 342      86.396 -11.814 -33.594  1.00 43.45           C  
ANISOU 2803  CE2 PHE A 342     5741   4443   6326     67    222    788       C  
ATOM   2804  CZ  PHE A 342      86.562 -10.820 -32.646  1.00 39.36           C  
ANISOU 2804  CZ  PHE A 342     5052   3877   6025    100    206    684       C  
ATOM   2805  N   TYR A 343      89.685 -15.078 -30.716  1.00 36.90           N  
ANISOU 2805  N   TYR A 343     4981   3724   5314    429    122    414       N  
ATOM   2806  CA  TYR A 343      88.933 -16.143 -30.060  1.00 35.78           C  
ANISOU 2806  CA  TYR A 343     5028   3616   4952    451     66    400       C  
ATOM   2807  C   TYR A 343      88.179 -15.629 -28.845  1.00 39.04           C  
ANISOU 2807  C   TYR A 343     5399   4076   5360    409    -63    305       C  
ATOM   2808  O   TYR A 343      88.636 -14.700 -28.166  1.00 38.42           O  
ANISOU 2808  O   TYR A 343     5140   4019   5437    398   -126    220       O  
ATOM   2809  CB  TYR A 343      89.851 -17.308 -29.635  1.00 36.07           C  
ANISOU 2809  CB  TYR A 343     5117   3663   4924    593     78    404       C  
ATOM   2810  CG  TYR A 343      90.980 -16.939 -28.694  1.00 38.82           C  
ANISOU 2810  CG  TYR A 343     5241   4082   5425    684    -30    348       C  
ATOM   2811  CD1 TYR A 343      90.808 -16.981 -27.314  1.00 42.11           C  
ANISOU 2811  CD1 TYR A 343     5639   4587   5773    697   -191    273       C  
ATOM   2812  CD2 TYR A 343      92.228 -16.566 -29.187  1.00 43.08           C  
ANISOU 2812  CD2 TYR A 343     5588   4615   6165    736     30    370       C  
ATOM   2813  CE1 TYR A 343      91.850 -16.655 -26.452  1.00 42.19           C  
ANISOU 2813  CE1 TYR A 343     5442   4698   5890    747   -314    228       C  
ATOM   2814  CE2 TYR A 343      93.271 -16.244 -28.335  1.00 41.27           C  
ANISOU 2814  CE2 TYR A 343     5128   4484   6070    796    -86    324       C  
ATOM   2815  CZ  TYR A 343      93.076 -16.294 -26.970  1.00 44.28           C  
ANISOU 2815  CZ  TYR A 343     5493   4974   6359    795   -271    257       C  
ATOM   2816  OH  TYR A 343      94.111 -15.978 -26.124  1.00 54.72           O  
ANISOU 2816  OH  TYR A 343     6582   6427   7782    822   -411    218       O  
ATOM   2817  N   PRO A 344      87.027 -16.226 -28.536  1.00 42.68           N  
ANISOU 2817  N   PRO A 344     6032   4547   5639    366    -85    305       N  
ATOM   2818  CA  PRO A 344      86.298 -15.836 -27.326  1.00 40.46           C  
ANISOU 2818  CA  PRO A 344     5734   4294   5344    323   -176    204       C  
ATOM   2819  C   PRO A 344      86.970 -16.422 -26.102  1.00 41.01           C  
ANISOU 2819  C   PRO A 344     5827   4422   5334    404   -270    126       C  
ATOM   2820  O   PRO A 344      87.624 -17.466 -26.167  1.00 40.38           O  
ANISOU 2820  O   PRO A 344     5833   4353   5158    509   -260    179       O  
ATOM   2821  CB  PRO A 344      84.910 -16.449 -27.540  1.00 42.01           C  
ANISOU 2821  CB  PRO A 344     6111   4486   5366    250   -148    244       C  
ATOM   2822  CG  PRO A 344      85.205 -17.719 -28.299  1.00 41.77           C  
ANISOU 2822  CG  PRO A 344     6262   4445   5164    287    -74    321       C  
ATOM   2823  CD  PRO A 344      86.379 -17.364 -29.221  1.00 45.78           C  
ANISOU 2823  CD  PRO A 344     6655   4922   5816    337    -10    379       C  
ATOM   2824  N   LYS A 345      86.817 -15.737 -24.977  1.00 46.05           N  
ANISOU 2824  N   LYS A 345     6392   5092   6011    351   -352      8       N  
ATOM   2825  CA  LYS A 345      87.410 -16.188 -23.728  1.00 53.02           C  
ANISOU 2825  CA  LYS A 345     7296   6059   6791    397   -472    -59       C  
ATOM   2826  C   LYS A 345      86.359 -16.832 -22.829  1.00 61.54           C  
ANISOU 2826  C   LYS A 345     8583   7139   7659    359   -495   -108       C  
ATOM   2827  O   LYS A 345      85.194 -16.416 -22.812  1.00 52.85           O  
ANISOU 2827  O   LYS A 345     7530   5985   6565    260   -436   -152       O  
ATOM   2828  CB  LYS A 345      88.091 -15.036 -22.986  1.00 53.32           C  
ANISOU 2828  CB  LYS A 345     7134   6152   6974    323   -550   -178       C  
ATOM   2829  CG  LYS A 345      89.560 -14.869 -23.345  1.00 62.87           C  
ANISOU 2829  CG  LYS A 345     8144   7422   8323    392   -588   -139       C  
ATOM   2830  CD  LYS A 345      90.294 -13.984 -22.344  1.00 68.25           C  
ANISOU 2830  CD  LYS A 345     8651   8204   9076    293   -702   -273       C  
ATOM   2831  CE  LYS A 345      89.894 -12.531 -22.508  1.00 70.79           C  
ANISOU 2831  CE  LYS A 345     8876   8435   9585    139   -602   -386       C  
ATOM   2832  NZ  LYS A 345      90.550 -11.639 -21.505  1.00 75.78           N  
ANISOU 2832  NZ  LYS A 345     9370   9153  10268     -8   -683   -550       N  
ATOM   2833  N   LEU A 346      86.789 -17.860 -22.095  1.00 66.30           N  
ANISOU 2833  N   LEU A 346     9304   7800   8088    448   -571    -86       N  
ATOM   2834  CA  LEU A 346      86.031 -18.448 -20.999  1.00 75.78           C  
ANISOU 2834  CA  LEU A 346    10704   9013   9075    411   -609   -144       C  
ATOM   2835  C   LEU A 346      85.464 -17.350 -20.111  1.00 69.58           C  
ANISOU 2835  C   LEU A 346     9867   8235   8336    255   -633   -304       C  
ATOM   2836  O   LEU A 346      86.211 -16.583 -19.499  1.00 66.32           O  
ANISOU 2836  O   LEU A 346     9312   7893   7995    205   -723   -384       O  
ATOM   2837  CB  LEU A 346      86.941 -19.388 -20.202  1.00 82.73           C  
ANISOU 2837  CB  LEU A 346    11647   9979   9808    537   -723    -83       C  
ATOM   2838  CG  LEU A 346      86.694 -19.678 -18.716  1.00 90.91           C  
ANISOU 2838  CG  LEU A 346    12824  11083  10634    491   -833   -152       C  
ATOM   2839  CD1 LEU A 346      85.385 -20.421 -18.480  1.00 99.05           C  
ANISOU 2839  CD1 LEU A 346    14132  12024  11478    444   -728   -178       C  
ATOM   2840  CD2 LEU A 346      87.865 -20.461 -18.143  1.00 89.95           C  
ANISOU 2840  CD2 LEU A 346    12686  11072  10419    644   -973    -32       C  
ATOM   2841  N   GLN A 347      84.134 -17.263 -20.058  1.00 70.73           N  
ANISOU 2841  N   GLN A 347    10123   8303   8447    164   -536   -353       N  
ATOM   2842  CA  GLN A 347      83.441 -16.106 -19.486  1.00 78.45           C  
ANISOU 2842  CA  GLN A 347    11037   9235   9537     20   -482   -493       C  
ATOM   2843  C   GLN A 347      83.847 -15.774 -18.049  1.00 90.71           C  
ANISOU 2843  C   GLN A 347    12622  10851  10992    -70   -569   -641       C  
ATOM   2844  O   GLN A 347      83.695 -16.585 -17.139  1.00 99.93           O  
ANISOU 2844  O   GLN A 347    13980  12063  11926    -74   -626   -665       O  
ATOM   2845  CB  GLN A 347      81.924 -16.324 -19.547  1.00 77.51           C  
ANISOU 2845  CB  GLN A 347    11040   9033   9378    -43   -362   -502       C  
ATOM   2846  CG  GLN A 347      81.324 -16.159 -20.940  1.00 66.37           C  
ANISOU 2846  CG  GLN A 347     9538   7573   8108    -27   -276   -376       C  
ATOM   2847  CD  GLN A 347      79.974 -16.849 -21.081  1.00 56.91           C  
ANISOU 2847  CD  GLN A 347     8476   6348   6798    -76   -200   -346       C  
ATOM   2848  OE1 GLN A 347      79.798 -17.702 -21.940  1.00 43.22           O  
ANISOU 2848  OE1 GLN A 347     6822   4635   4963    -48   -189   -237       O  
ATOM   2849  NE2 GLN A 347      79.020 -16.488 -20.223  1.00 63.98           N  
ANISOU 2849  NE2 GLN A 347     9404   7195   7711   -167   -128   -453       N  
TER    2850      GLN A 347                                                      
ATOM   2851  N  AASN B   0      94.774 -18.402   1.771  0.59 63.60           N  
ANISOU 2851  N  AASN B   0     9570   6847   7746  -2096    256    567       N  
ATOM   2852  N  BASN B   0      86.248 -21.188  -2.093  0.41 41.17           N  
ANISOU 2852  N  BASN B   0     7006   4256   4380   -195   -942   1234       N  
ATOM   2853  CA AASN B   0      94.874 -19.835   1.517  0.59 58.54           C  
ANISOU 2853  CA AASN B   0     8578   6612   7052  -1970    358    429       C  
ATOM   2854  CA BASN B   0      87.418 -20.512  -1.581  0.41 56.81           C  
ANISOU 2854  CA BASN B   0     9092   6066   6425   -440   -782   1238       C  
ATOM   2855  C  AASN B   0      93.813 -20.617   2.295  0.59 62.70           C  
ANISOU 2855  C  AASN B   0     8954   7155   7714  -1503    197    353       C  
ATOM   2856  C  BASN B   0      87.885 -21.114  -0.273  0.41 50.76           C  
ANISOU 2856  C  BASN B   0     7993   5402   5891   -382   -608    960       C  
ATOM   2857  O  AASN B   0      94.133 -21.427   3.167  0.59 58.65           O  
ANISOU 2857  O  AASN B   0     8130   6823   7329  -1365    221    150       O  
ATOM   2858  O  BASN B   0      87.269 -22.054   0.250  0.41 48.64           O  
ANISOU 2858  O  BASN B   0     7447   5310   5726   -160   -606    791       O  
ATOM   2859  CB AASN B   0      96.265 -20.335   1.864  0.59 57.98           C  
ANISOU 2859  CB AASN B   0     8137   6845   7046  -2186    555    173       C  
ATOM   2860  CB BASN B   0      87.137 -19.020  -1.395  0.41 59.33           C  
ANISOU 2860  CB BASN B   0     9762   5932   6848   -368   -993   1421       C  
ATOM   2861  N  AMET B   1      92.547 -20.369   1.969  0.59 60.71           N  
ANISOU 2861  N  AMET B   1     8925   6718   7424  -1273     25    522       N  
ATOM   2862  N  BMET B   1      88.964 -20.557   0.265  0.41 58.34           N  
ANISOU 2862  N  BMET B   1     8995   6249   6921   -601   -477    922       N  
ATOM   2863  CA AMET B   1      91.421 -21.029   2.618  0.59 60.61           C  
ANISOU 2863  CA AMET B   1     8776   6730   7521   -874   -107    450       C  
ATOM   2864  CA BMET B   1      89.633 -21.036   1.490  0.41 62.60           C  
ANISOU 2864  CA BMET B   1     9249   6895   7642   -595   -333    678       C  
ATOM   2865  C  AMET B   1      91.082 -22.313   1.866  0.59 54.42           C  
ANISOU 2865  C  AMET B   1     7823   6235   6620   -793    -56    433       C  
ATOM   2866  C  BMET B   1      90.205 -22.431   1.195  0.41 52.27           C  
ANISOU 2866  C  BMET B   1     7648   5957   6254   -680   -151    540       C  
ATOM   2867  O  AMET B   1      90.907 -22.288   0.644  0.59 54.17           O  
ANISOU 2867  O  AMET B   1     7941   6250   6389   -907    -51    577       O  
ATOM   2868  O  BMET B   1      90.801 -22.638   0.124  0.41 57.31           O  
ANISOU 2868  O  BMET B   1     8328   6748   6697   -926    -30    595       O  
ATOM   2869  CB AMET B   1      90.214 -20.090   2.650  0.59 69.17           C  
ANISOU 2869  CB AMET B   1    10132   7492   8660   -653   -327    587       C  
ATOM   2870  CB BMET B   1      88.698 -20.949   2.681  0.41 69.19           C  
ANISOU 2870  CB BMET B   1     9986   7614   8689   -259   -461    555       C  
ATOM   2871  CG AMET B   1      89.008 -20.607   3.420  0.59 70.54           C  
ANISOU 2871  CG AMET B   1    10139   7701   8961   -270   -442    473       C  
ATOM   2872  CG BMET B   1      89.057 -19.860   3.677  0.41 73.22           C  
ANISOU 2872  CG BMET B   1    10607   7851   9361   -283   -489    488       C  
ATOM   2873  SD AMET B   1      89.300 -20.789   5.196  0.59 75.74           S  
ANISOU 2873  SD AMET B   1    10571   8400   9804   -174   -389    211       S  
ATOM   2874  SD BMET B   1      88.932 -20.385   5.400  0.41 70.58           S  
ANISOU 2874  SD BMET B   1     9982   7634   9199    -92   -449    207       S  
ATOM   2875  CE AMET B   1      89.956 -19.170   5.601  0.59 76.84           C  
ANISOU 2875  CE AMET B   1    10978   8180  10038   -353   -425    216       C  
ATOM   2876  CE BMET B   1      89.845 -21.922   5.321  0.41 71.36           C  
ANISOU 2876  CE BMET B   1     9781   8122   9211   -228   -274    128       C  
ATOM   2877  N  ASER B   2      90.989 -23.429   2.589  0.59 47.33           N  
ANISOU 2877  N  ASER B   2     6640   5516   5827   -614    -28    260       N  
ATOM   2878  N  BSER B   2      90.079 -23.394   2.114  0.41 46.42           N  
ANISOU 2878  N  BSER B   2     6627   5355   5654   -496   -123    355       N  
ATOM   2879  CA ASER B   2      90.810 -24.714   1.924  0.59 42.28           C  
ANISOU 2879  CA ASER B   2     5835   5121   5108   -566     37    203       C  
ATOM   2880  CA BSER B   2      90.791 -24.660   1.955  0.41 42.93           C  
ANISOU 2880  CA BSER B   2     5926   5192   5194   -564     31    208       C  
ATOM   2881  C  ASER B   2      90.398 -25.778   2.925  0.59 36.53           C  
ANISOU 2881  C  ASER B   2     4882   4473   4527   -332      8     63       C  
ATOM   2882  C  BSER B   2      90.348 -25.751   2.920  0.41 37.42           C  
ANISOU 2882  C  BSER B   2     5002   4579   4638   -326      3     68       C  
ATOM   2883  O  ASER B   2      90.555 -25.622   4.138  0.59 37.95           O  
ANISOU 2883  O  ASER B   2     4998   4586   4834   -254    -26     -7       O  
ATOM   2884  O  BSER B   2      90.440 -25.581   4.136  0.41 39.14           O  
ANISOU 2884  O  BSER B   2     5162   4725   4984   -240    -36      1       O  
ATOM   2885  CB ASER B   2      92.090 -25.156   1.234  0.59 47.03           C  
ANISOU 2885  CB ASER B   2     6309   5934   5624   -827    233    111       C  
ATOM   2886  CB BSER B   2      92.297 -24.428   2.113  0.41 45.37           C  
ANISOU 2886  CB BSER B   2     6141   5571   5527   -823    183    114       C  
ATOM   2887  OG ASER B   2      93.037 -25.578   2.200  0.59 40.74           O  
ANISOU 2887  OG ASER B   2     5267   5218   4996   -822    295    -70       O  
ATOM   2888  OG BSER B   2      92.997 -25.653   2.286  0.41 40.27           O  
ANISOU 2888  OG BSER B   2     5193   5160   4950   -798    288    -78       O  
ATOM   2889  N   LEU B   3      89.909 -26.893   2.381  1.00 34.43           N  
ANISOU 2889  N   LEU B   3     4512   4353   4216   -253     27     20       N  
ATOM   2890  CA  LEU B   3      89.536 -28.032   3.214  1.00 35.40           C  
ANISOU 2890  CA  LEU B   3     4458   4533   4460    -81     13    -90       C  
ATOM   2891  C   LEU B   3      90.714 -28.518   4.048  1.00 33.63           C  
ANISOU 2891  C   LEU B   3     4068   4355   4352   -107     71   -209       C  
ATOM   2892  O   LEU B   3      90.575 -28.776   5.249  1.00 33.22           O  
ANISOU 2892  O   LEU B   3     3966   4260   4395     10      9   -238       O  
ATOM   2893  CB  LEU B   3      89.011 -29.165   2.327  1.00 33.81           C  
ANISOU 2893  CB  LEU B   3     4187   4464   4196    -54     42   -139       C  
ATOM   2894  CG  LEU B   3      88.837 -30.526   2.997  1.00 40.74           C  
ANISOU 2894  CG  LEU B   3     4908   5374   5198     62     52   -251       C  
ATOM   2895  CD1 LEU B   3      87.767 -30.430   4.067  1.00 41.68           C  
ANISOU 2895  CD1 LEU B   3     5045   5412   5377    199    -38   -210       C  
ATOM   2896  CD2 LEU B   3      88.471 -31.576   1.944  1.00 41.96           C  
ANISOU 2896  CD2 LEU B   3     5012   5638   5293     40     97   -333       C  
ATOM   2897  N   GLU B   4      91.887 -28.644   3.421  1.00 32.54           N  
ANISOU 2897  N   GLU B   4     3837   4329   4196   -264    184   -289       N  
ATOM   2898  CA  GLU B   4      93.063 -29.137   4.129  1.00 40.40           C  
ANISOU 2898  CA  GLU B   4     4625   5397   5328   -259    207   -432       C  
ATOM   2899  C   GLU B   4      93.520 -28.162   5.209  1.00 36.33           C  
ANISOU 2899  C   GLU B   4     4139   4799   4868   -300    140   -415       C  
ATOM   2900  O   GLU B   4      94.052 -28.591   6.239  1.00 35.93           O  
ANISOU 2900  O   GLU B   4     3953   4773   4924   -211     67   -494       O  
ATOM   2901  CB  GLU B   4      94.192 -29.421   3.125  1.00 38.46           C  
ANISOU 2901  CB  GLU B   4     4222   5332   5059   -426    366   -574       C  
ATOM   2902  CG  GLU B   4      93.957 -30.681   2.238  1.00 41.70           C  
ANISOU 2902  CG  GLU B   4     4542   5846   5455   -356    435   -685       C  
ATOM   2903  CD  GLU B   4      92.916 -30.503   1.104  1.00 54.69           C  
ANISOU 2903  CD  GLU B   4     6384   7504   6893   -426    461   -575       C  
ATOM   2904  OE1 GLU B   4      92.256 -29.437   1.006  1.00 45.00           O  
ANISOU 2904  OE1 GLU B   4     5374   6177   5546   -483    395   -386       O  
ATOM   2905  OE2 GLU B   4      92.770 -31.446   0.293  1.00 54.83           O  
ANISOU 2905  OE2 GLU B   4     6334   7627   6871   -414    530   -694       O  
ATOM   2906  N   ASN B   5      93.322 -26.853   4.995  1.00 34.06           N  
ANISOU 2906  N   ASN B   5     4044   4395   4504   -433    142   -314       N  
ATOM   2907  CA  ASN B   5      93.673 -25.868   6.015  1.00 33.28           C  
ANISOU 2907  CA  ASN B   5     3998   4186   4462   -483     79   -328       C  
ATOM   2908  C   ASN B   5      92.693 -25.892   7.178  1.00 35.92           C  
ANISOU 2908  C   ASN B   5     4396   4420   4833   -270    -46   -309       C  
ATOM   2909  O   ASN B   5      93.097 -25.738   8.336  1.00 34.54           O  
ANISOU 2909  O   ASN B   5     4168   4249   4708   -251   -110   -388       O  
ATOM   2910  CB  ASN B   5      93.740 -24.469   5.396  1.00 35.28           C  
ANISOU 2910  CB  ASN B   5     4478   4286   4642   -698    114   -227       C  
ATOM   2911  CG  ASN B   5      94.047 -23.381   6.426  1.00 40.45           C  
ANISOU 2911  CG  ASN B   5     5214   4783   5373   -765     48   -271       C  
ATOM   2912  OD1 ASN B   5      93.174 -22.578   6.771  1.00 38.23           O  
ANISOU 2912  OD1 ASN B   5     5141   4281   5104   -670    -43   -205       O  
ATOM   2913  ND2 ASN B   5      95.295 -23.344   6.914  1.00 40.43           N  
ANISOU 2913  ND2 ASN B   5     5028   4901   5432   -923     86   -415       N  
ATOM   2914  N   VAL B   6      91.396 -26.047   6.896  1.00 34.16           N  
ANISOU 2914  N   VAL B   6     4276   4134   4568   -128    -79   -226       N  
ATOM   2915  CA  VAL B   6      90.432 -26.208   7.983  1.00 34.02           C  
ANISOU 2915  CA  VAL B   6     4272   4082   4572     50   -153   -246       C  
ATOM   2916  C   VAL B   6      90.809 -27.404   8.848  1.00 33.42           C  
ANISOU 2916  C   VAL B   6     4045   4131   4520    112   -170   -305       C  
ATOM   2917  O   VAL B   6      90.814 -27.325  10.086  1.00 32.37           O  
ANISOU 2917  O   VAL B   6     3915   4006   4380    151   -227   -350       O  
ATOM   2918  CB  VAL B   6      89.004 -26.345   7.420  1.00 32.74           C  
ANISOU 2918  CB  VAL B   6     4172   3892   4377    181   -175   -182       C  
ATOM   2919  CG1 VAL B   6      88.047 -26.698   8.541  1.00 34.84           C  
ANISOU 2919  CG1 VAL B   6     4394   4187   4655    322   -202   -242       C  
ATOM   2920  CG2 VAL B   6      88.580 -25.040   6.761  1.00 35.16           C  
ANISOU 2920  CG2 VAL B   6     4663   4026   4670    171   -227   -104       C  
ATOM   2921  N   ALA B   7      91.169 -28.522   8.209  1.00 33.48           N  
ANISOU 2921  N   ALA B   7     3941   4230   4551    120   -134   -310       N  
ATOM   2922  CA  ALA B   7      91.545 -29.714   8.960  1.00 37.72           C  
ANISOU 2922  CA  ALA B   7     4372   4825   5136    203   -188   -341       C  
ATOM   2923  C   ALA B   7      92.830 -29.500   9.751  1.00 32.51           C  
ANISOU 2923  C   ALA B   7     3614   4216   4524    166   -262   -414       C  
ATOM   2924  O   ALA B   7      92.957 -29.996  10.878  1.00 33.41           O  
ANISOU 2924  O   ALA B   7     3719   4346   4628    242   -373   -405       O  
ATOM   2925  CB  ALA B   7      91.691 -30.897   8.011  1.00 35.95           C  
ANISOU 2925  CB  ALA B   7     4053   4642   4963    235   -139   -368       C  
ATOM   2926  N   PHE B   8      93.800 -28.777   9.180  1.00 34.21           N  
ANISOU 2926  N   PHE B   8     3753   4474   4773     27   -208   -485       N  
ATOM   2927  CA  PHE B   8      95.006 -28.450   9.937  1.00 37.07           C  
ANISOU 2927  CA  PHE B   8     3985   4913   5188    -35   -286   -587       C  
ATOM   2928  C   PHE B   8      94.660 -27.718  11.229  1.00 39.75           C  
ANISOU 2928  C   PHE B   8     4449   5199   5454    -32   -384   -578       C  
ATOM   2929  O   PHE B   8      95.203 -28.029  12.298  1.00 36.53           O  
ANISOU 2929  O   PHE B   8     3971   4868   5040     16   -522   -621       O  
ATOM   2930  CB  PHE B   8      95.960 -27.608   9.086  1.00 33.56           C  
ANISOU 2930  CB  PHE B   8     3454   4525   4771   -258   -172   -673       C  
ATOM   2931  CG  PHE B   8      97.187 -27.145   9.835  1.00 32.01           C  
ANISOU 2931  CG  PHE B   8     3092   4431   4637   -363   -246   -813       C  
ATOM   2932  CD1 PHE B   8      97.193 -25.945  10.525  1.00 38.21           C  
ANISOU 2932  CD1 PHE B   8     4002   5134   5380   -495   -284   -830       C  
ATOM   2933  CD2 PHE B   8      98.338 -27.920   9.850  1.00 39.95           C  
ANISOU 2933  CD2 PHE B   8     3798   5619   5763   -320   -294   -958       C  
ATOM   2934  CE1 PHE B   8      98.326 -25.523  11.221  1.00 39.86           C  
ANISOU 2934  CE1 PHE B   8     4044   5460   5642   -618   -364   -984       C  
ATOM   2935  CE2 PHE B   8      99.468 -27.507  10.543  1.00 42.00           C  
ANISOU 2935  CE2 PHE B   8     3860   6010   6087   -413   -389  -1110       C  
ATOM   2936  CZ  PHE B   8      99.464 -26.310  11.227  1.00 47.69           C  
ANISOU 2936  CZ  PHE B   8     4711   6668   6742   -580   -423  -1121       C  
ATOM   2937  N   ASN B   9      93.763 -26.736  11.151  1.00 35.53           N  
ANISOU 2937  N   ASN B   9     4102   4538   4861    -74   -329   -537       N  
ATOM   2938  CA  ASN B   9      93.382 -25.996  12.349  1.00 37.29           C  
ANISOU 2938  CA  ASN B   9     4437   4714   5020    -67   -395   -585       C  
ATOM   2939  C   ASN B   9      92.663 -26.887  13.358  1.00 33.09           C  
ANISOU 2939  C   ASN B   9     3933   4248   4392     73   -459   -546       C  
ATOM   2940  O   ASN B   9      92.913 -26.787  14.565  1.00 39.59           O  
ANISOU 2940  O   ASN B   9     4772   5141   5129     63   -553   -603       O  
ATOM   2941  CB  ASN B   9      92.506 -24.796  11.973  1.00 34.37           C  
ANISOU 2941  CB  ASN B   9     4251   4159   4650    -92   -333   -575       C  
ATOM   2942  CG  ASN B   9      93.331 -23.585  11.554  1.00 35.46           C  
ANISOU 2942  CG  ASN B   9     4443   4184   4845   -295   -307   -625       C  
ATOM   2943  OD1 ASN B   9      93.544 -22.665  12.336  1.00 37.50           O  
ANISOU 2943  OD1 ASN B   9     4773   4364   5110   -371   -349   -735       O  
ATOM   2944  ND2 ASN B   9      93.807 -23.593  10.320  1.00 39.29           N  
ANISOU 2944  ND2 ASN B   9     4905   4667   5357   -416   -226   -556       N  
ATOM   2945  N   VAL B  10      91.753 -27.744  12.895  1.00 33.62           N  
ANISOU 2945  N   VAL B  10     4021   4303   4450    171   -407   -450       N  
ATOM   2946  CA  VAL B  10      91.049 -28.628  13.824  1.00 33.20           C  
ANISOU 2946  CA  VAL B  10     4016   4306   4290    244   -441   -397       C  
ATOM   2947  C   VAL B  10      92.050 -29.502  14.578  1.00 38.91           C  
ANISOU 2947  C   VAL B  10     4684   5108   4992    264   -591   -364       C  
ATOM   2948  O   VAL B  10      92.005 -29.615  15.809  1.00 38.83           O  
ANISOU 2948  O   VAL B  10     4752   5167   4835    254   -679   -351       O  
ATOM   2949  CB  VAL B  10      90.002 -29.472  13.078  1.00 35.20           C  
ANISOU 2949  CB  VAL B  10     4280   4532   4563    303   -357   -315       C  
ATOM   2950  CG1 VAL B  10      89.502 -30.603  13.973  1.00 42.43           C  
ANISOU 2950  CG1 VAL B  10     5253   5493   5375    320   -387   -235       C  
ATOM   2951  CG2 VAL B  10      88.809 -28.572  12.612  1.00 35.05           C  
ANISOU 2951  CG2 VAL B  10     4310   4463   4542    324   -263   -356       C  
ATOM   2952  N   VAL B  11      93.001 -30.087  13.852  1.00 39.31           N  
ANISOU 2952  N   VAL B  11     4595   5161   5181    299   -633   -366       N  
ATOM   2953  CA  VAL B  11      93.954 -31.016  14.459  1.00 38.52           C  
ANISOU 2953  CA  VAL B  11     4415   5110   5112    382   -818   -342       C  
ATOM   2954  C   VAL B  11      94.901 -30.300  15.416  1.00 41.45           C  
ANISOU 2954  C   VAL B  11     4729   5592   5428    327   -963   -432       C  
ATOM   2955  O   VAL B  11      95.270 -30.843  16.465  1.00 53.74           O  
ANISOU 2955  O   VAL B  11     6318   7206   6894    387  -1161   -377       O  
ATOM   2956  CB  VAL B  11      94.718 -31.760  13.347  1.00 43.25           C  
ANISOU 2956  CB  VAL B  11     4829   5693   5912    456   -807   -390       C  
ATOM   2957  CG1 VAL B  11      95.907 -32.503  13.912  1.00 51.83           C  
ANISOU 2957  CG1 VAL B  11     5772   6829   7091    582  -1032   -420       C  
ATOM   2958  CG2 VAL B  11      93.767 -32.704  12.635  1.00 45.24           C  
ANISOU 2958  CG2 VAL B  11     5162   5836   6191    514   -710   -307       C  
ATOM   2959  N   ASN B  12      95.315 -29.080  15.082  1.00 40.54           N  
ANISOU 2959  N   ASN B  12     4547   5501   5354    196   -885   -565       N  
ATOM   2960  CA  ASN B  12      96.351 -28.395  15.848  1.00 39.88           C  
ANISOU 2960  CA  ASN B  12     4367   5534   5251    109  -1019   -695       C  
ATOM   2961  C   ASN B  12      95.821 -27.425  16.893  1.00 48.24           C  
ANISOU 2961  C   ASN B  12     5600   6599   6130     13  -1026   -751       C  
ATOM   2962  O   ASN B  12      96.503 -27.192  17.898  1.00 46.59           O  
ANISOU 2962  O   ASN B  12     5356   6516   5830    -32  -1194   -835       O  
ATOM   2963  CB  ASN B  12      97.285 -27.637  14.902  1.00 44.42           C  
ANISOU 2963  CB  ASN B  12     4757   6136   5986    -36   -925   -837       C  
ATOM   2964  CG  ASN B  12      98.216 -28.565  14.157  1.00 55.12           C  
ANISOU 2964  CG  ASN B  12     5852   7578   7513     48   -954   -880       C  
ATOM   2965  OD1 ASN B  12      99.272 -28.923  14.666  1.00 58.83           O  
ANISOU 2965  OD1 ASN B  12     6111   8190   8051    105  -1139   -975       O  
ATOM   2966  ND2 ASN B  12      97.815 -28.986  12.957  1.00 45.16           N  
ANISOU 2966  ND2 ASN B  12     4589   6246   6323     74   -786   -834       N  
ATOM   2967  N   LYS B  13      94.632 -26.852  16.690  1.00 42.09           N  
ANISOU 2967  N   LYS B  13     4989   5702   5302     -8   -860   -736       N  
ATOM   2968  CA  LYS B  13      94.098 -25.824  17.577  1.00 42.34           C  
ANISOU 2968  CA  LYS B  13     5164   5723   5202    -83   -834   -855       C  
ATOM   2969  C   LYS B  13      92.736 -26.171  18.166  1.00 40.79           C  
ANISOU 2969  C   LYS B  13     5119   5540   4841    -11   -758   -801       C  
ATOM   2970  O   LYS B  13      92.211 -25.387  18.967  1.00 41.16           O  
ANISOU 2970  O   LYS B  13     5266   5606   4766    -57   -716   -941       O  
ATOM   2971  CB  LYS B  13      93.991 -24.480  16.837  1.00 45.36           C  
ANISOU 2971  CB  LYS B  13     5591   5930   5715   -183   -709   -961       C  
ATOM   2972  CG  LYS B  13      95.265 -24.051  16.103  1.00 54.12           C  
ANISOU 2972  CG  LYS B  13     6559   7028   6976   -330   -722  -1016       C  
ATOM   2973  CD  LYS B  13      96.439 -23.866  17.043  1.00 58.36           C  
ANISOU 2973  CD  LYS B  13     6972   7730   7473   -438   -884  -1162       C  
ATOM   2974  CE  LYS B  13      96.367 -22.550  17.796  1.00 64.27           C  
ANISOU 2974  CE  LYS B  13     7852   8401   8167   -583   -885  -1352       C  
ATOM   2975  NZ  LYS B  13      97.624 -22.291  18.572  1.00 67.62           N  
ANISOU 2975  NZ  LYS B  13     8125   9005   8562   -734  -1051  -1525       N  
ATOM   2976  N   GLY B  14      92.135 -27.299  17.779  1.00 37.54           N  
ANISOU 2976  N   GLY B  14     4714   5122   4427     82   -720   -636       N  
ATOM   2977  CA  GLY B  14      90.847 -27.708  18.299  1.00 41.58           C  
ANISOU 2977  CA  GLY B  14     5338   5676   4783    102   -622   -593       C  
ATOM   2978  C   GLY B  14      89.653 -27.119  17.575  1.00 46.86           C  
ANISOU 2978  C   GLY B  14     6013   6248   5544    146   -443   -657       C  
ATOM   2979  O   GLY B  14      88.511 -27.499  17.876  1.00 38.82           O  
ANISOU 2979  O   GLY B  14     5030   5293   4427    158   -338   -651       O  
ATOM   2980  N   HIS B  15      89.883 -26.215  16.627  1.00 40.52           N  
ANISOU 2980  N   HIS B  15     5174   5300   4920    161   -417   -714       N  
ATOM   2981  CA  HIS B  15      88.835 -25.489  15.907  1.00 39.32           C  
ANISOU 2981  CA  HIS B  15     5046   5024   4871    236   -311   -768       C  
ATOM   2982  C   HIS B  15      89.525 -24.577  14.900  1.00 39.18           C  
ANISOU 2982  C   HIS B  15     5044   4827   5015    200   -336   -766       C  
ATOM   2983  O   HIS B  15      90.757 -24.542  14.852  1.00 37.53           O  
ANISOU 2983  O   HIS B  15     4796   4633   4832     93   -398   -758       O  
ATOM   2984  CB  HIS B  15      87.958 -24.669  16.855  1.00 38.07           C  
ANISOU 2984  CB  HIS B  15     4940   4890   4633    265   -248   -966       C  
ATOM   2985  CG  HIS B  15      88.640 -23.451  17.402  1.00 42.09           C  
ANISOU 2985  CG  HIS B  15     5519   5312   5160    199   -300  -1140       C  
ATOM   2986  ND1 HIS B  15      88.111 -22.181  17.286  1.00 43.10           N  
ANISOU 2986  ND1 HIS B  15     5712   5253   5409    266   -268  -1311       N  
ATOM   2987  CD2 HIS B  15      89.815 -23.308  18.062  1.00 40.08           C  
ANISOU 2987  CD2 HIS B  15     5276   5120   4833     70   -399  -1184       C  
ATOM   2988  CE1 HIS B  15      88.932 -21.310  17.850  1.00 46.70           C  
ANISOU 2988  CE1 HIS B  15     6238   5639   5865    156   -325  -1456       C  
ATOM   2989  NE2 HIS B  15      89.973 -21.969  18.330  1.00 43.20           N  
ANISOU 2989  NE2 HIS B  15     5748   5369   5296     26   -403  -1388       N  
ATOM   2990  N   PHE B  16      88.774 -23.832  14.099  1.00 37.05           N  
ANISOU 2990  N   PHE B  16     4832   4395   4849    273   -298   -772       N  
ATOM   2991  CA  PHE B  16      89.406 -22.941  13.134  1.00 37.40           C  
ANISOU 2991  CA  PHE B  16     4955   4246   5009    195   -321   -729       C  
ATOM   2992  C   PHE B  16      89.935 -21.713  13.861  1.00 40.41           C  
ANISOU 2992  C   PHE B  16     5435   4497   5422    101   -357   -888       C  
ATOM   2993  O   PHE B  16      89.185 -21.004  14.540  1.00 41.09           O  
ANISOU 2993  O   PHE B  16     5591   4500   5520    194   -355  -1044       O  
ATOM   2994  CB  PHE B  16      88.460 -22.526  12.006  1.00 36.09           C  
ANISOU 2994  CB  PHE B  16     4868   3921   4924    307   -320   -644       C  
ATOM   2995  CG  PHE B  16      89.169 -21.780  10.902  1.00 37.91           C  
ANISOU 2995  CG  PHE B  16     5223   3966   5215    175   -340   -534       C  
ATOM   2996  CD1 PHE B  16      89.937 -22.472   9.969  1.00 42.35           C  
ANISOU 2996  CD1 PHE B  16     5720   4634   5738     46   -297   -408       C  
ATOM   2997  CD2 PHE B  16      89.138 -20.396  10.843  1.00 44.37           C  
ANISOU 2997  CD2 PHE B  16     6234   4501   6122    151   -392   -571       C  
ATOM   2998  CE1 PHE B  16      90.622 -21.788   8.973  1.00 45.40           C  
ANISOU 2998  CE1 PHE B  16     6227   4891   6133   -137   -280   -312       C  
ATOM   2999  CE2 PHE B  16      89.818 -19.710   9.847  1.00 46.19           C  
ANISOU 2999  CE2 PHE B  16     6625   4549   6377    -31   -400   -438       C  
ATOM   3000  CZ  PHE B  16      90.555 -20.407   8.909  1.00 42.04           C  
ANISOU 3000  CZ  PHE B  16     6028   4177   5771   -194   -331   -305       C  
ATOM   3001  N   ASP B  17      91.233 -21.458  13.704  1.00 37.97           N  
ANISOU 3001  N   ASP B  17     5113   4178   5138    -94   -381   -884       N  
ATOM   3002  CA  ASP B  17      91.915 -20.370  14.396  1.00 43.52           C  
ANISOU 3002  CA  ASP B  17     5891   4774   5870   -242   -418  -1053       C  
ATOM   3003  C   ASP B  17      92.731 -19.526  13.421  1.00 50.63           C  
ANISOU 3003  C   ASP B  17     6885   5473   6878   -455   -401   -992       C  
ATOM   3004  O   ASP B  17      93.604 -18.762  13.844  1.00 45.67           O  
ANISOU 3004  O   ASP B  17     6284   4783   6284   -659   -422  -1123       O  
ATOM   3005  CB  ASP B  17      92.791 -20.946  15.518  1.00 53.98           C  
ANISOU 3005  CB  ASP B  17     7072   6359   7081   -324   -482  -1156       C  
ATOM   3006  CG  ASP B  17      93.362 -19.884  16.442  1.00 66.37           C  
ANISOU 3006  CG  ASP B  17     8704   7868   8646   -474   -535  -1383       C  
ATOM   3007  OD1 ASP B  17      92.580 -19.105  17.032  1.00 63.59           O  
ANISOU 3007  OD1 ASP B  17     8489   7380   8293   -403   -518  -1539       O  
ATOM   3008  OD2 ASP B  17      94.603 -19.842  16.588  1.00 64.43           O  
ANISOU 3008  OD2 ASP B  17     8348   7725   8406   -664   -594  -1438       O  
ATOM   3009  N   GLY B  18      92.460 -19.646  12.122  1.00 47.43           N  
ANISOU 3009  N   GLY B  18     6538   4979   6503   -444   -358   -800       N  
ATOM   3010  CA  GLY B  18      93.161 -18.843  11.137  1.00 47.25           C  
ANISOU 3010  CA  GLY B  18     6651   4771   6532   -689   -320   -709       C  
ATOM   3011  C   GLY B  18      94.647 -19.115  11.005  1.00 49.10           C  
ANISOU 3011  C   GLY B  18     6702   5203   6750   -971   -260   -754       C  
ATOM   3012  O   GLY B  18      95.377 -18.256  10.507  1.00 47.90           O  
ANISOU 3012  O   GLY B  18     6656   4910   6635  -1258   -209   -744       O  
ATOM   3013  N   GLN B  19      95.121 -20.291  11.422  1.00 42.03           N  
ANISOU 3013  N   GLN B  19     5533   4626   5811   -903   -269   -808       N  
ATOM   3014  CA  GLN B  19      96.541 -20.608  11.320  1.00 39.50           C  
ANISOU 3014  CA  GLN B  19     4971   4526   5510  -1120   -235   -896       C  
ATOM   3015  C   GLN B  19      96.855 -21.159   9.936  1.00 42.55           C  
ANISOU 3015  C   GLN B  19     5277   5010   5880  -1206   -106   -778       C  
ATOM   3016  O   GLN B  19      96.013 -21.789   9.294  1.00 43.84           O  
ANISOU 3016  O   GLN B  19     5496   5166   5996  -1028    -83   -641       O  
ATOM   3017  CB  GLN B  19      96.948 -21.629  12.384  1.00 42.62           C  
ANISOU 3017  CB  GLN B  19     5116   5195   5882   -971   -350  -1007       C  
ATOM   3018  CG  GLN B  19      96.716 -21.160  13.808  1.00 53.50           C  
ANISOU 3018  CG  GLN B  19     6567   6548   7213   -920   -472  -1142       C  
ATOM   3019  CD  GLN B  19      97.517 -19.914  14.150  1.00 67.10           C  
ANISOU 3019  CD  GLN B  19     8331   8175   8989  -1204   -481  -1314       C  
ATOM   3020  OE1 GLN B  19      98.701 -19.812  13.831  1.00 74.55           O  
ANISOU 3020  OE1 GLN B  19     9091   9243   9992  -1438   -456  -1393       O  
ATOM   3021  NE2 GLN B  19      96.866 -18.954  14.793  1.00 64.53           N  
ANISOU 3021  NE2 GLN B  19     8234   7631   8656  -1194   -508  -1403       N  
ATOM   3022  N   GLN B  20      98.082 -20.932   9.474  1.00 44.00           N  
ANISOU 3022  N   GLN B  20     5310   5316   6092  -1502    -10   -862       N  
ATOM   3023  CA  GLN B  20      98.468 -21.489   8.185  1.00 50.61           C  
ANISOU 3023  CA  GLN B  20     6038   6304   6887  -1612    146   -804       C  
ATOM   3024  C   GLN B  20      98.918 -22.937   8.343  1.00 44.62           C  
ANISOU 3024  C   GLN B  20     4927   5849   6177  -1409    118   -915       C  
ATOM   3025  O   GLN B  20      99.474 -23.333   9.370  1.00 49.15           O  
ANISOU 3025  O   GLN B  20     5286   6562   6827  -1309    -12  -1059       O  
ATOM   3026  CB  GLN B  20      99.572 -20.653   7.533  1.00 57.47           C  
ANISOU 3026  CB  GLN B  20     6880   7207   7751  -2054    305   -866       C  
ATOM   3027  CG  GLN B  20      99.068 -19.327   6.979  1.00 71.81           C  
ANISOU 3027  CG  GLN B  20     9123   8662   9501  -2274    347   -682       C  
ATOM   3028  CD  GLN B  20      99.791 -18.909   5.715  1.00 89.75           C  
ANISOU 3028  CD  GLN B  20    11448  10987  11665  -2701    565   -616       C  
ATOM   3029  OE1 GLN B  20      99.185 -18.797   4.646  1.00 99.86           O  
ANISOU 3029  OE1 GLN B  20    12988  12154  12800  -2738    625   -392       O  
ATOM   3030  NE2 GLN B  20     101.095 -18.678   5.828  1.00 90.00           N  
ANISOU 3030  NE2 GLN B  20    11226  11221  11747  -3046    685   -818       N  
ATOM   3031  N   GLY B  21      98.657 -23.732   7.311  1.00 44.84           N  
ANISOU 3031  N   GLY B  21     4917   5963   6156  -1340    220   -848       N  
ATOM   3032  CA  GLY B  21      99.056 -25.127   7.337  1.00 44.78           C  
ANISOU 3032  CA  GLY B  21     4604   6184   6226  -1134    196   -964       C  
ATOM   3033  C   GLY B  21      98.057 -26.022   6.638  1.00 46.77           C  
ANISOU 3033  C   GLY B  21     4955   6399   6418   -929    222   -844       C  
ATOM   3034  O   GLY B  21      96.929 -25.605   6.347  1.00 42.31           O  
ANISOU 3034  O   GLY B  21     4675   5647   5752   -892    215   -666       O  
ATOM   3035  N   GLU B  22      98.459 -27.261   6.363  1.00 43.96           N  
ANISOU 3035  N   GLU B  22     4351   6212   6141   -784    238   -963       N  
ATOM   3036  CA  GLU B  22      97.610 -28.215   5.668  1.00 39.40           C  
ANISOU 3036  CA  GLU B  22     3841   5610   5521   -616    270   -896       C  
ATOM   3037  C   GLU B  22      97.881 -29.615   6.204  1.00 43.33           C  
ANISOU 3037  C   GLU B  22     4121   6166   6175   -340    153  -1008       C  
ATOM   3038  O   GLU B  22      99.012 -29.936   6.568  1.00 42.25           O  
ANISOU 3038  O   GLU B  22     3703   6170   6180   -309    106  -1189       O  
ATOM   3039  CB  GLU B  22      97.863 -28.185   4.154  1.00 48.65           C  
ANISOU 3039  CB  GLU B  22     4992   6911   6582   -826    492   -943       C  
ATOM   3040  CG  GLU B  22      97.288 -26.987   3.425  1.00 65.42           C  
ANISOU 3040  CG  GLU B  22     7434   8917   8508  -1065    572   -749       C  
ATOM   3041  CD  GLU B  22      98.352 -26.167   2.710  1.00 83.73           C  
ANISOU 3041  CD  GLU B  22     9702  11369  10742  -1452    767   -820       C  
ATOM   3042  OE1 GLU B  22      98.399 -24.937   2.930  1.00 83.78           O  
ANISOU 3042  OE1 GLU B  22     9910  11220  10702  -1658    755   -704       O  
ATOM   3043  OE2 GLU B  22      99.142 -26.755   1.933  1.00 95.28           O  
ANISOU 3043  OE2 GLU B  22    10923  13089  12189  -1567    945  -1010       O  
ATOM   3044  N   VAL B  23      96.836 -30.440   6.250  1.00 40.07           N  
ANISOU 3044  N   VAL B  23     3842   5634   5747   -142     90   -904       N  
ATOM   3045  CA  VAL B  23      96.995 -31.880   6.481  1.00 43.51           C  
ANISOU 3045  CA  VAL B  23     4136   6066   6330     98     -3   -988       C  
ATOM   3046  C   VAL B  23      96.247 -32.646   5.396  1.00 43.87           C  
ANISOU 3046  C   VAL B  23     4251   6083   6334    129    108   -993       C  
ATOM   3047  O   VAL B  23      95.259 -32.137   4.848  1.00 41.02           O  
ANISOU 3047  O   VAL B  23     4097   5677   5813     31    178   -863       O  
ATOM   3048  CB  VAL B  23      96.500 -32.299   7.877  1.00 41.72           C  
ANISOU 3048  CB  VAL B  23     4025   5699   6129    286   -222   -856       C  
ATOM   3049  CG1 VAL B  23      97.364 -31.686   8.962  1.00 45.40           C  
ANISOU 3049  CG1 VAL B  23     4394   6230   6625    266   -360   -892       C  
ATOM   3050  CG2 VAL B  23      95.047 -31.924   8.068  1.00 36.55           C  
ANISOU 3050  CG2 VAL B  23     3651   4915   5322    264   -208   -665       C  
ATOM   3051  N   PRO B  24      96.667 -33.866   5.062  1.00 45.79           N  
ANISOU 3051  N   PRO B  24     4326   6345   6727    278    107  -1158       N  
ATOM   3052  CA  PRO B  24      95.919 -34.657   4.073  1.00 39.58           C  
ANISOU 3052  CA  PRO B  24     3614   5524   5901    297    204  -1196       C  
ATOM   3053  C   PRO B  24      94.583 -35.101   4.635  1.00 40.00           C  
ANISOU 3053  C   PRO B  24     3905   5378   5915    395     91   -999       C  
ATOM   3054  O   PRO B  24      94.482 -35.488   5.802  1.00 39.45           O  
ANISOU 3054  O   PRO B  24     3888   5175   5927    531    -76   -900       O  
ATOM   3055  CB  PRO B  24      96.828 -35.864   3.810  1.00 40.69           C  
ANISOU 3055  CB  PRO B  24     3502   5691   6270    468    201  -1461       C  
ATOM   3056  CG  PRO B  24      98.113 -35.588   4.533  1.00 48.58           C  
ANISOU 3056  CG  PRO B  24     4253   6786   7419    527    109  -1569       C  
ATOM   3057  CD  PRO B  24      97.812 -34.608   5.613  1.00 44.58           C  
ANISOU 3057  CD  PRO B  24     3909   6226   6805    460    -16  -1333       C  
ATOM   3058  N   VAL B  25      93.557 -35.075   3.780  1.00 35.54           N  
ANISOU 3058  N   VAL B  25     3478   4818   5209    306    182   -952       N  
ATOM   3059  CA  VAL B  25      92.176 -35.331   4.178  1.00 33.27           C  
ANISOU 3059  CA  VAL B  25     3378   4400   4863    343    110   -792       C  
ATOM   3060  C   VAL B  25      91.540 -36.329   3.222  1.00 36.08           C  
ANISOU 3060  C   VAL B  25     3749   4741   5217    340    173   -896       C  
ATOM   3061  O   VAL B  25      91.779 -36.279   2.011  1.00 36.57           O  
ANISOU 3061  O   VAL B  25     3754   4945   5197    244    297  -1030       O  
ATOM   3062  CB  VAL B  25      91.367 -34.022   4.196  1.00 40.62           C  
ANISOU 3062  CB  VAL B  25     4455   5364   5617    238    116   -629       C  
ATOM   3063  CG1 VAL B  25      89.874 -34.300   4.394  1.00 38.52           C  
ANISOU 3063  CG1 VAL B  25     4313   5028   5296    269     70   -530       C  
ATOM   3064  CG2 VAL B  25      91.918 -33.104   5.273  1.00 36.56           C  
ANISOU 3064  CG2 VAL B  25     3945   4827   5118    238     46   -556       C  
ATOM   3065  N   SER B  26      90.723 -37.235   3.768  1.00 35.37           N  
ANISOU 3065  N   SER B  26     3749   4492   5197    411     95   -840       N  
ATOM   3066  CA  SER B  26      89.889 -38.155   2.999  1.00 35.04           C  
ANISOU 3066  CA  SER B  26     3748   4414   5153    374    138   -929       C  
ATOM   3067  C   SER B  26      88.431 -37.877   3.326  1.00 31.58           C  
ANISOU 3067  C   SER B  26     3432   3970   4598    304    106   -776       C  
ATOM   3068  O   SER B  26      88.069 -37.759   4.498  1.00 35.44           O  
ANISOU 3068  O   SER B  26     3991   4374   5102    332     36   -631       O  
ATOM   3069  CB  SER B  26      90.218 -39.632   3.314  1.00 34.58           C  
ANISOU 3069  CB  SER B  26     3683   4135   5319    493     81  -1034       C  
ATOM   3070  OG  SER B  26      91.495 -39.960   2.858  1.00 53.42           O  
ANISOU 3070  OG  SER B  26     5904   6550   7844    590    114  -1245       O  
ATOM   3071  N   ILE B  27      87.596 -37.783   2.298  1.00 33.19           N  
ANISOU 3071  N   ILE B  27     3644   4292   4676    210    153   -830       N  
ATOM   3072  CA  ILE B  27      86.147 -37.671   2.458  1.00 28.75           C  
ANISOU 3072  CA  ILE B  27     3130   3758   4034    154    116   -750       C  
ATOM   3073  C   ILE B  27      85.505 -38.981   2.016  1.00 29.54           C  
ANISOU 3073  C   ILE B  27     3229   3795   4199     86    137   -886       C  
ATOM   3074  O   ILE B  27      85.681 -39.405   0.868  1.00 33.60           O  
ANISOU 3074  O   ILE B  27     3706   4380   4678     39    185  -1057       O  
ATOM   3075  CB  ILE B  27      85.570 -36.519   1.621  1.00 34.77           C  
ANISOU 3075  CB  ILE B  27     3897   4707   4607    113     98   -705       C  
ATOM   3076  CG1 ILE B  27      86.256 -35.190   1.954  1.00 44.06           C  
ANISOU 3076  CG1 ILE B  27     5111   5897   5732    150     81   -581       C  
ATOM   3077  CG2 ILE B  27      84.061 -36.461   1.804  1.00 33.09           C  
ANISOU 3077  CG2 ILE B  27     3670   4548   4356     94     39   -671       C  
ATOM   3078  CD1 ILE B  27      85.964 -34.704   3.317  1.00 44.85           C  
ANISOU 3078  CD1 ILE B  27     5237   5913   5892    219     31   -467       C  
ATOM   3079  N  AILE B  28      84.765 -39.622   2.912  0.52 31.28           N  
ANISOU 3079  N  AILE B  28     3499   3889   4496     46    115   -824       N  
ATOM   3080  N  BILE B  28      84.710 -39.583   2.904  0.48 31.03           N  
ANISOU 3080  N  BILE B  28     3466   3866   4457     43    114   -821       N  
ATOM   3081  CA AILE B  28      84.077 -40.867   2.580  0.52 33.28           C  
ANISOU 3081  CA AILE B  28     3773   4048   4823    -67    138   -946       C  
ATOM   3082  CA BILE B  28      83.930 -40.780   2.581  0.48 31.72           C  
ANISOU 3082  CA BILE B  28     3570   3874   4608    -77    137   -939       C  
ATOM   3083  C  AILE B  28      82.661 -40.778   3.116  0.52 31.16           C  
ANISOU 3083  C  AILE B  28     3490   3856   4495   -191    139   -878       C  
ATOM   3084  C  BILE B  28      82.897 -40.993   3.680  0.48 32.87           C  
ANISOU 3084  C  BILE B  28     3760   3969   4760   -180    137   -820       C  
ATOM   3085  O  AILE B  28      82.464 -40.571   4.319  0.52 29.52           O  
ANISOU 3085  O  AILE B  28     3332   3597   4290   -197    138   -730       O  
ATOM   3086  O  BILE B  28      83.137 -40.634   4.837  0.48 31.85           O  
ANISOU 3086  O  BILE B  28     3692   3782   4628   -134    119   -659       O  
ATOM   3087  CB AILE B  28      84.801 -42.101   3.140  0.52 36.95           C  
ANISOU 3087  CB AILE B  28     4341   4206   5494    -25    121   -966       C  
ATOM   3088  CB BILE B  28      84.840 -42.017   2.411  0.48 37.81           C  
ANISOU 3088  CB BILE B  28     4396   4404   5566    -32    146  -1068       C  
ATOM   3089  CG1AILE B  28      86.224 -42.152   2.585  0.52 34.90           C  
ANISOU 3089  CG1AILE B  28     4022   3916   5322    128    124  -1094       C  
ATOM   3090  CG1BILE B  28      84.034 -43.254   1.975  0.48 37.79           C  
ANISOU 3090  CG1BILE B  28     4436   4280   5642   -183    172  -1220       C  
ATOM   3091  CG2AILE B  28      84.045 -43.367   2.771  0.52 39.66           C  
ANISOU 3091  CG2AILE B  28     4740   4404   5926   -174    147  -1100       C  
ATOM   3092  CG2BILE B  28      85.615 -42.295   3.686  0.48 39.97           C  
ANISOU 3092  CG2BILE B  28     4766   4446   5973     79     79   -914       C  
ATOM   3093  CD1AILE B  28      87.017 -43.334   3.030  0.52 34.75           C  
ANISOU 3093  CD1AILE B  28     4075   3581   5547    241     64  -1147       C  
ATOM   3094  CD1BILE B  28      84.881 -44.491   1.751  0.48 45.47           C  
ANISOU 3094  CD1BILE B  28     5478   4963   6836   -113    167  -1383       C  
ATOM   3095  N  AASN B  29      81.682 -40.951   2.227  0.52 32.91           N  
ANISOU 3095  N  AASN B  29     3624   4229   4651   -304    145  -1013       N  
ATOM   3096  N  BASN B  29      81.738 -41.563   3.327  0.48 33.18           N  
ANISOU 3096  N  BASN B  29     3756   4064   4788   -346    168   -918       N  
ATOM   3097  CA AASN B  29      80.284 -40.695   2.541  0.52 35.56           C  
ANISOU 3097  CA AASN B  29     3859   4725   4929   -410    143  -1006       C  
ATOM   3098  CA BASN B  29      80.718 -41.967   4.304  0.48 36.12           C  
ANISOU 3098  CA BASN B  29     4152   4406   5166   -516    213   -847       C  
ATOM   3099  C  AASN B  29      80.165 -39.333   3.213  0.52 39.94           C  
ANISOU 3099  C  AASN B  29     4367   5403   5405   -281    110   -863       C  
ATOM   3100  C  BASN B  29      80.132 -40.771   5.047  0.48 39.36           C  
ANISOU 3100  C  BASN B  29     4469   5026   5459   -475    221   -746       C  
ATOM   3101  O  AASN B  29      80.548 -38.314   2.626  0.52 39.26           O  
ANISOU 3101  O  AASN B  29     4266   5417   5235   -149     45   -832       O  
ATOM   3102  O  BASN B  29      79.777 -40.876   6.229  0.48 29.17           O  
ANISOU 3102  O  BASN B  29     3234   3703   4147   -570    276   -643       O  
ATOM   3103  CB AASN B  29      79.724 -41.832   3.398  0.52 35.28           C  
ANISOU 3103  CB AASN B  29     3888   4520   4995   -603    214  -1000       C  
ATOM   3104  CB BASN B  29      81.272 -42.980   5.311  0.48 43.88           C  
ANISOU 3104  CB BASN B  29     5347   5062   6263   -564    216   -724       C  
ATOM   3105  CG AASN B  29      79.714 -43.158   2.654  0.52 47.27           C  
ANISOU 3105  CG AASN B  29     5463   5881   6617   -742    235  -1174       C  
ATOM   3106  CG BASN B  29      81.879 -44.181   4.641  0.48 40.94           C  
ANISOU 3106  CG BASN B  29     5073   4422   6058   -559    191   -850       C  
ATOM   3107  OD1AASN B  29      79.420 -43.200   1.459  0.52 50.95           O  
ANISOU 3107  OD1AASN B  29     5830   6501   7029   -772    209  -1356       O  
ATOM   3108  OD1BASN B  29      82.964 -44.633   5.006  0.48 45.04           O  
ANISOU 3108  OD1BASN B  29     5721   4689   6702   -418    123   -787       O  
ATOM   3109  ND2AASN B  29      80.050 -44.243   3.348  0.52 45.21           N  
ANISOU 3109  ND2AASN B  29     5384   5297   6496   -828    266  -1118       N  
ATOM   3110  ND2BASN B  29      81.182 -44.705   3.642  0.48 33.72           N  
ANISOU 3110  ND2BASN B  29     4084   3568   5160   -699    230  -1057       N  
ATOM   3111  N  AASN B  30      79.677 -39.309   4.449  0.52 38.64           N  
ANISOU 3111  N  AASN B  30     4205   5218   5258   -336    162   -783       N  
ATOM   3112  N  BASN B  30      80.040 -39.629   4.358  0.48 38.09           N  
ANISOU 3112  N  BASN B  30     4186   5072   5216   -340    164   -782       N  
ATOM   3113  CA AASN B  30      79.472 -38.077   5.198  0.52 36.16           C  
ANISOU 3113  CA AASN B  30     3839   5015   4884   -222    148   -702       C  
ATOM   3114  CA BASN B  30      79.597 -38.371   4.963  0.48 37.86           C  
ANISOU 3114  CA BASN B  30     4072   5198   5113   -242    147   -718       C  
ATOM   3115  C  AASN B  30      80.520 -37.876   6.286  0.52 34.85           C  
ANISOU 3115  C  AASN B  30     3826   4692   4725   -156    162   -554       C  
ATOM   3116  C  BASN B  30      80.464 -37.997   6.162  0.48 34.85           C  
ANISOU 3116  C  BASN B  30     3819   4691   4730   -170    164   -568       C  
ATOM   3117  O  AASN B  30      80.241 -37.241   7.307  0.52 34.39           O  
ANISOU 3117  O  AASN B  30     3756   4693   4616   -140    193   -506       O  
ATOM   3118  O  BASN B  30      80.006 -37.353   7.106  0.48 38.22           O  
ANISOU 3118  O  BASN B  30     4212   5203   5106   -162    197   -534       O  
ATOM   3119  CB AASN B  30      78.074 -38.062   5.819  0.52 39.84           C  
ANISOU 3119  CB AASN B  30     4150   5654   5333   -338    215   -778       C  
ATOM   3120  CB BASN B  30      78.119 -38.442   5.358  0.48 38.63           C  
ANISOU 3120  CB BASN B  30     4005   5478   5197   -372    202   -809       C  
ATOM   3121  CG AASN B  30      77.112 -37.131   5.089  0.52 40.01           C  
ANISOU 3121  CG AASN B  30     3952   5919   5329   -224    123   -894       C  
ATOM   3122  CG BASN B  30      77.401 -37.126   5.145  0.48 43.08           C  
ANISOU 3122  CG BASN B  30     4390   6262   5717   -211    124   -862       C  
ATOM   3123  OD1AASN B  30      77.511 -36.103   4.541  0.52 39.25           O  
ANISOU 3123  OD1AASN B  30     3877   5836   5201    -27      6   -847       O  
ATOM   3124  OD1BASN B  30      77.908 -36.230   4.465  0.48 40.17           O  
ANISOU 3124  OD1BASN B  30     4056   5892   5315    -31     10   -815       O  
ATOM   3125  ND2AASN B  30      75.841 -37.491   5.085  0.52 41.19           N  
ANISOU 3125  ND2AASN B  30     3896   6259   5497   -355    162  -1045       N  
ATOM   3126  ND2BASN B  30      76.222 -36.997   5.731  0.48 34.99           N  
ANISOU 3126  ND2BASN B  30     3175   5419   4699   -278    185   -967       N  
ATOM   3127  N   THR B  31      81.728 -38.409   6.113  1.00 33.06           N  
ANISOU 3127  N   THR B  31     3719   4283   4559   -114    135   -510       N  
ATOM   3128  CA  THR B  31      82.694 -38.283   7.193  1.00 32.10           C  
ANISOU 3128  CA  THR B  31     3717   4035   4446    -49    111   -379       C  
ATOM   3129  C   THR B  31      84.000 -37.721   6.647  1.00 36.31           C  
ANISOU 3129  C   THR B  31     4247   4538   5010     98     52   -381       C  
ATOM   3130  O   THR B  31      84.388 -38.019   5.516  1.00 35.97           O  
ANISOU 3130  O   THR B  31     4166   4495   5007    115     54   -479       O  
ATOM   3131  CB  THR B  31      82.924 -39.642   7.877  1.00 40.96           C  
ANISOU 3131  CB  THR B  31     4992   4936   5636   -148    111   -306       C  
ATOM   3132  OG1 THR B  31      81.666 -40.141   8.356  1.00 41.58           O  
ANISOU 3132  OG1 THR B  31     5076   5062   5661   -356    201   -306       O  
ATOM   3133  CG2 THR B  31      83.885 -39.513   9.050  1.00 43.76           C  
ANISOU 3133  CG2 THR B  31     5475   5183   5970    -71     37   -154       C  
ATOM   3134  N   VAL B  32      84.655 -36.890   7.455  1.00 31.87           N  
ANISOU 3134  N   VAL B  32     3717   3979   4414    175     15   -299       N  
ATOM   3135  CA  VAL B  32      85.969 -36.327   7.149  1.00 30.62           C  
ANISOU 3135  CA  VAL B  32     3540   3806   4289    271    -27   -306       C  
ATOM   3136  C   VAL B  32      87.015 -37.041   7.989  1.00 31.93           C  
ANISOU 3136  C   VAL B  32     3762   3829   4539    325   -100   -254       C  
ATOM   3137  O   VAL B  32      86.888 -37.107   9.219  1.00 33.64           O  
ANISOU 3137  O   VAL B  32     4070   4007   4703    307   -144   -146       O  
ATOM   3138  CB  VAL B  32      86.010 -34.817   7.440  1.00 31.48           C  
ANISOU 3138  CB  VAL B  32     3640   4005   4316    308    -40   -271       C  
ATOM   3139  CG1 VAL B  32      87.375 -34.243   7.034  1.00 32.22           C  
ANISOU 3139  CG1 VAL B  32     3706   4096   4441    343    -60   -292       C  
ATOM   3140  CG2 VAL B  32      84.866 -34.123   6.752  1.00 33.53           C  
ANISOU 3140  CG2 VAL B  32     3859   4370   4512    302    -22   -303       C  
ATOM   3141  N   TYR B  33      88.062 -37.542   7.335  1.00 33.60           N  
ANISOU 3141  N   TYR B  33     3914   3982   4871    396   -123   -342       N  
ATOM   3142  CA  TYR B  33      89.188 -38.179   7.989  1.00 32.18           C  
ANISOU 3142  CA  TYR B  33     3741   3671   4813    506   -237   -324       C  
ATOM   3143  C   TYR B  33      90.467 -37.430   7.662  1.00 38.66           C  
ANISOU 3143  C   TYR B  33     4411   4599   5678    575   -248   -418       C  
ATOM   3144  O   TYR B  33      90.580 -36.753   6.633  1.00 37.63           O  
ANISOU 3144  O   TYR B  33     4192   4604   5503    517   -142   -514       O  
ATOM   3145  CB  TYR B  33      89.383 -39.638   7.543  1.00 31.15           C  
ANISOU 3145  CB  TYR B  33     3631   3348   4855    563   -266   -406       C  
ATOM   3146  CG  TYR B  33      88.183 -40.521   7.731  1.00 36.74           C  
ANISOU 3146  CG  TYR B  33     4493   3924   5544    444   -239   -337       C  
ATOM   3147  CD1 TYR B  33      87.139 -40.493   6.820  1.00 39.63           C  
ANISOU 3147  CD1 TYR B  33     4821   4389   5847    316   -116   -428       C  
ATOM   3148  CD2 TYR B  33      88.114 -41.420   8.798  1.00 39.91           C  
ANISOU 3148  CD2 TYR B  33     5081   4100   5981    438   -349   -180       C  
ATOM   3149  CE1 TYR B  33      86.042 -41.314   6.975  1.00 38.68           C  
ANISOU 3149  CE1 TYR B  33     4806   4172   5721    168    -80   -397       C  
ATOM   3150  CE2 TYR B  33      87.015 -42.248   8.967  1.00 38.31           C  
ANISOU 3150  CE2 TYR B  33     5031   3772   5754    267   -298   -116       C  
ATOM   3151  CZ  TYR B  33      85.978 -42.176   8.047  1.00 47.83           C  
ANISOU 3151  CZ  TYR B  33     6153   5105   6918    125   -152   -244       C  
ATOM   3152  OH  TYR B  33      84.873 -42.971   8.176  1.00 52.08           O  
ANISOU 3152  OH  TYR B  33     6800   5552   7438    -82    -87   -217       O  
ATOM   3153  N   THR B  34      91.452 -37.601   8.531  1.00 36.68           N  
ANISOU 3153  N   THR B  34     4134   4296   5507    682   -387   -389       N  
ATOM   3154  CA  THR B  34      92.803 -37.178   8.220  1.00 35.02           C  
ANISOU 3154  CA  THR B  34     3724   4191   5391    747   -405   -528       C  
ATOM   3155  C   THR B  34      93.763 -38.319   8.515  1.00 41.93           C  
ANISOU 3155  C   THR B  34     4518   4931   6483    943   -565   -600       C  
ATOM   3156  O   THR B  34      93.517 -39.158   9.387  1.00 41.06           O  
ANISOU 3156  O   THR B  34     4568   4627   6406   1026   -722   -458       O  
ATOM   3157  CB  THR B  34      93.194 -35.918   8.998  1.00 44.28           C  
ANISOU 3157  CB  THR B  34     4880   5486   6457    690   -448   -469       C  
ATOM   3158  OG1 THR B  34      94.450 -35.445   8.511  1.00 42.90           O  
ANISOU 3158  OG1 THR B  34     4484   5446   6370    688   -422   -633       O  
ATOM   3159  CG2 THR B  34      93.319 -36.214  10.485  1.00 40.10           C  
ANISOU 3159  CG2 THR B  34     4459   4880   5898    766   -645   -330       C  
ATOM   3160  N  ALYS B  35      94.854 -38.347   7.758  0.57 42.92           N  
ANISOU 3160  N  ALYS B  35     4396   5158   6755   1013   -523   -826       N  
ATOM   3161  N  BLYS B  35      94.867 -38.356   7.772  0.43 42.47           N  
ANISOU 3161  N  BLYS B  35     4337   5099   6700   1016   -527   -826       N  
ATOM   3162  CA ALYS B  35      95.852 -39.389   7.910  0.57 44.59           C  
ANISOU 3162  CA ALYS B  35     4465   5252   7224   1251   -684   -959       C  
ATOM   3163  CA BLYS B  35      95.844 -39.430   7.905  0.43 45.23           C  
ANISOU 3163  CA BLYS B  35     4550   5326   7311   1255   -686   -960       C  
ATOM   3164  C  ALYS B  35      96.790 -39.013   9.051  0.57 51.06           C  
ANISOU 3164  C  ALYS B  35     5194   6128   8078   1358   -907   -902       C  
ATOM   3165  C  BLYS B  35      96.853 -39.071   8.991  0.43 50.60           C  
ANISOU 3165  C  BLYS B  35     5117   6068   8038   1370   -907   -922       C  
ATOM   3166  O  ALYS B  35      97.314 -37.894   9.097  0.57 49.58           O  
ANISOU 3166  O  ALYS B  35     4862   6170   7808   1243   -850   -957       O  
ATOM   3167  O  BLYS B  35      97.513 -38.029   8.916  0.43 52.69           O  
ANISOU 3167  O  BLYS B  35     5196   6571   8252   1272   -843  -1015       O  
ATOM   3168  CB ALYS B  35      96.624 -39.579   6.603  0.57 49.61           C  
ANISOU 3168  CB ALYS B  35     4822   6025   8005   1278   -520  -1290       C  
ATOM   3169  CB BLYS B  35      96.552 -39.696   6.577  0.43 48.79           C  
ANISOU 3169  CB BLYS B  35     4734   5896   7909   1286   -521  -1288       C  
ATOM   3170  CG ALYS B  35      97.352 -40.911   6.495  0.57 43.21           C  
ANISOU 3170  CG ALYS B  35     3876   5031   7508   1560   -654  -1489       C  
ATOM   3171  CG BLYS B  35      95.775 -40.577   5.606  0.43 47.65           C  
ANISOU 3171  CG BLYS B  35     4688   5624   7793   1262   -392  -1384       C  
ATOM   3172  CD ALYS B  35      98.310 -40.959   5.307  0.57 54.76           C  
ANISOU 3172  CD ALYS B  35     4986   6709   9110   1585   -469  -1886       C  
ATOM   3173  CD BLYS B  35      96.272 -42.026   5.562  0.43 49.27           C  
ANISOU 3173  CD BLYS B  35     4838   5572   8309   1528   -526  -1555       C  
ATOM   3174  CE ALYS B  35      97.613 -41.345   4.012  0.57 55.75           C  
ANISOU 3174  CE ALYS B  35     5173   6845   9163   1455   -224  -2038       C  
ATOM   3175  CE BLYS B  35      95.516 -42.833   4.501  0.43 47.10           C  
ANISOU 3175  CE BLYS B  35     4653   5188   8055   1462   -372  -1705       C  
ATOM   3176  NZ ALYS B  35      98.592 -41.823   2.991  0.57 67.11           N  
ANISOU 3176  NZ ALYS B  35     6371   8433  10695   1466    -90  -2385       N  
ATOM   3177  NZ BLYS B  35      95.786 -44.293   4.552  0.43 63.88           N  
ANISOU 3177  NZ BLYS B  35     6811   6965  10497   1711   -520  -1845       N  
ATOM   3178  N   VAL B  36      96.964 -39.930   9.997  1.00 50.61           N  
ANISOU 3178  N   VAL B  36     5252   5853   8126   1557  -1179   -776       N  
ATOM   3179  CA  VAL B  36      97.897 -39.754  11.104  1.00 51.50           C  
ANISOU 3179  CA  VAL B  36     5281   6016   8271   1696  -1458   -724       C  
ATOM   3180  C   VAL B  36      98.743 -41.013  11.151  1.00 64.81           C  
ANISOU 3180  C   VAL B  36     6854   7499  10273   2030  -1709   -830       C  
ATOM   3181  O   VAL B  36      98.234 -42.101  11.458  1.00 64.57           O  
ANISOU 3181  O   VAL B  36     7098   7150  10285   2122  -1833   -664       O  
ATOM   3182  CB  VAL B  36      97.194 -39.509  12.447  1.00 49.57           C  
ANISOU 3182  CB  VAL B  36     5358   5710   7768   1602  -1602   -402       C  
ATOM   3183  CG1 VAL B  36      98.214 -39.421  13.567  1.00 53.82           C  
ANISOU 3183  CG1 VAL B  36     5815   6314   8320   1755  -1932   -358       C  
ATOM   3184  CG2 VAL B  36      96.330 -38.263  12.388  1.00 48.14           C  
ANISOU 3184  CG2 VAL B  36     5264   5706   7319   1317  -1359   -346       C  
ATOM   3185  N   ASP B  37     100.023 -40.875  10.820  1.00 70.58           N  
ANISOU 3185  N   ASP B  37     7257   8431  11131   2095  -1696  -1082       N  
ATOM   3186  CA  ASP B  37     100.972 -41.977  10.897  1.00 66.58           C  
ANISOU 3186  CA  ASP B  37     6672   7794  10831   2327  -1868  -1182       C  
ATOM   3187  C   ASP B  37     100.460 -43.201  10.143  1.00 60.04           C  
ANISOU 3187  C   ASP B  37     5985   6676  10150   2410  -1792  -1236       C  
ATOM   3188  O   ASP B  37     100.478 -44.330  10.643  1.00 69.22           O  
ANISOU 3188  O   ASP B  37     7347   7534  11420   2586  -2011  -1109       O  
ATOM   3189  CB  ASP B  37     101.293 -42.311  12.353  1.00 82.05           C  
ANISOU 3189  CB  ASP B  37     8808   9632  12737   2469  -2237   -924       C  
ATOM   3190  CG  ASP B  37     102.453 -41.497  12.891  1.00 95.27           C  
ANISOU 3190  CG  ASP B  37    10199  11610  14391   2478  -2353  -1034       C  
ATOM   3191  OD1 ASP B  37     103.615 -41.857  12.594  1.00102.43           O  
ANISOU 3191  OD1 ASP B  37    10823  12599  15498   2626  -2401  -1276       O  
ATOM   3192  OD2 ASP B  37     102.206 -40.490  13.589  1.00 97.93           O  
ANISOU 3192  OD2 ASP B  37    10584  12109  14514   2327  -2392   -905       O  
ATOM   3193  N   GLY B  38      99.992 -42.961   8.923  1.00 58.03           N  
ANISOU 3193  N   GLY B  38     5641   6520   9890   2264  -1481  -1427       N  
ATOM   3194  CA  GLY B  38      99.617 -44.026   8.022  1.00 63.92           C  
ANISOU 3194  CA  GLY B  38     6459   7057  10771   2310  -1372  -1565       C  
ATOM   3195  C   GLY B  38      98.180 -44.502   8.105  1.00 56.16           C  
ANISOU 3195  C   GLY B  38     5838   5780   9722   2230  -1354  -1347       C  
ATOM   3196  O   GLY B  38      97.777 -45.327   7.275  1.00 65.18           O  
ANISOU 3196  O   GLY B  38     7041   6761  10965   2226  -1238  -1488       O  
ATOM   3197  N   VAL B  39      97.390 -44.036   9.078  1.00 46.55           N  
ANISOU 3197  N   VAL B  39     5585   5866   6236   1582   -401   -815       N  
ATOM   3198  CA  VAL B  39      96.011 -44.497   9.197  1.00 45.63           C  
ANISOU 3198  CA  VAL B  39     5653   5636   6050   1527   -354   -724       C  
ATOM   3199  C   VAL B  39      95.065 -43.308   9.301  1.00 43.27           C  
ANISOU 3199  C   VAL B  39     5349   5352   5741   1374   -344   -683       C  
ATOM   3200  O   VAL B  39      95.438 -42.207   9.709  1.00 43.41           O  
ANISOU 3200  O   VAL B  39     5258   5451   5786   1344   -398   -712       O  
ATOM   3201  CB  VAL B  39      95.795 -45.461  10.393  1.00 41.07           C  
ANISOU 3201  CB  VAL B  39     5235   4971   5398   1677   -406   -671       C  
ATOM   3202  CG1 VAL B  39      96.712 -46.699  10.273  1.00 52.27           C  
ANISOU 3202  CG1 VAL B  39     6673   6361   6824   1844   -415   -707       C  
ATOM   3203  CG2 VAL B  39      96.006 -44.746  11.714  1.00 41.97           C  
ANISOU 3203  CG2 VAL B  39     5330   5138   5479   1739   -517   -668       C  
ATOM   3204  N   ASP B  40      93.813 -43.561   8.934  1.00 34.41           N  
ANISOU 3204  N   ASP B  40     4344   4145   4584   1280   -276   -622       N  
ATOM   3205  CA  ASP B  40      92.786 -42.530   8.895  1.00 32.35           C  
ANISOU 3205  CA  ASP B  40     4087   3889   4317   1136   -258   -583       C  
ATOM   3206  C   ASP B  40      92.151 -42.356  10.264  1.00 38.17           C  
ANISOU 3206  C   ASP B  40     4915   4587   5002   1169   -310   -530       C  
ATOM   3207  O   ASP B  40      91.807 -43.336  10.932  1.00 39.31           O  
ANISOU 3207  O   ASP B  40     5194   4643   5096   1254   -307   -489       O  
ATOM   3208  CB  ASP B  40      91.735 -42.899   7.851  1.00 39.70           C  
ANISOU 3208  CB  ASP B  40     5090   4756   5240   1028   -169   -558       C  
ATOM   3209  CG  ASP B  40      92.314 -42.932   6.449  1.00 51.27           C  
ANISOU 3209  CG  ASP B  40     6473   6267   6740    989   -114   -610       C  
ATOM   3210  OD1 ASP B  40      93.090 -42.015   6.128  1.00 54.61           O  
ANISOU 3210  OD1 ASP B  40     6766   6781   7203    960   -122   -648       O  
ATOM   3211  OD2 ASP B  40      92.004 -43.866   5.675  1.00 56.72           O  
ANISOU 3211  OD2 ASP B  40     7232   6899   7420    984    -56   -618       O  
ATOM   3212  N   VAL B  41      92.010 -41.104  10.686  1.00 31.77           N  
ANISOU 3212  N   VAL B  41     4036   3835   4201   1104   -349   -530       N  
ATOM   3213  CA  VAL B  41      91.367 -40.751  11.944  1.00 30.56           C  
ANISOU 3213  CA  VAL B  41     3961   3654   3997   1120   -392   -486       C  
ATOM   3214  C   VAL B  41      90.192 -39.840  11.629  1.00 39.06           C  
ANISOU 3214  C   VAL B  41     5040   4719   5083    966   -347   -451       C  
ATOM   3215  O   VAL B  41      90.356 -38.837  10.928  1.00 38.27           O  
ANISOU 3215  O   VAL B  41     4828   4682   5032    873   -339   -478       O  
ATOM   3216  CB  VAL B  41      92.341 -40.051  12.909  1.00 34.11           C  
ANISOU 3216  CB  VAL B  41     4324   4189   4446   1202   -498   -533       C  
ATOM   3217  CG1 VAL B  41      91.641 -39.743  14.224  1.00 37.08           C  
ANISOU 3217  CG1 VAL B  41     4802   4534   4754   1227   -538   -486       C  
ATOM   3218  CG2 VAL B  41      93.586 -40.916  13.131  1.00 39.91           C  
ANISOU 3218  CG2 VAL B  41     5033   4951   5180   1365   -556   -581       C  
ATOM   3219  N   GLU B  42      89.020 -40.174  12.168  1.00 34.59           N  
ANISOU 3219  N   GLU B  42     4601   4068   4474    945   -313   -391       N  
ATOM   3220  CA  GLU B  42      87.813 -39.380  11.937  1.00 34.44           C  
ANISOU 3220  CA  GLU B  42     4586   4034   4468    811   -274   -362       C  
ATOM   3221  C   GLU B  42      87.901 -38.025  12.635  1.00 37.15           C  
ANISOU 3221  C   GLU B  42     4861   4439   4815    784   -330   -370       C  
ATOM   3222  O   GLU B  42      88.107 -37.948  13.850  1.00 38.06           O  
ANISOU 3222  O   GLU B  42     5018   4557   4887    864   -383   -364       O  
ATOM   3223  CB  GLU B  42      86.580 -40.143  12.432  1.00 39.39           C  
ANISOU 3223  CB  GLU B  42     5356   4551   5060    800   -216   -307       C  
ATOM   3224  CG  GLU B  42      85.302 -39.316  12.467  1.00 42.00           C  
ANISOU 3224  CG  GLU B  42     5687   4865   5404    682   -185   -281       C  
ATOM   3225  CD  GLU B  42      84.083 -40.147  12.862  1.00 58.65           C  
ANISOU 3225  CD  GLU B  42     7923   6864   7499    660   -111   -241       C  
ATOM   3226  OE1 GLU B  42      83.948 -41.292  12.367  1.00 53.62           O  
ANISOU 3226  OE1 GLU B  42     7346   6159   6869    670    -58   -243       O  
ATOM   3227  OE2 GLU B  42      83.270 -39.659  13.675  1.00 68.59           O  
ANISOU 3227  OE2 GLU B  42     9221   8098   8743    630    -96   -212       O  
ATOM   3228  N   LEU B  43      87.727 -36.952  11.869  1.00 31.94           N  
ANISOU 3228  N   LEU B  43     4108   3826   4202    675   -318   -384       N  
ATOM   3229  CA  LEU B  43      87.648 -35.608  12.436  1.00 36.61           C  
ANISOU 3229  CA  LEU B  43     4643   4461   4808    631   -356   -392       C  
ATOM   3230  C   LEU B  43      86.224 -35.089  12.552  1.00 40.69           C  
ANISOU 3230  C   LEU B  43     5212   4931   5318    543   -320   -346       C  
ATOM   3231  O   LEU B  43      85.965 -34.201  13.376  1.00 37.13           O  
ANISOU 3231  O   LEU B  43     4756   4492   4861    529   -349   -343       O  
ATOM   3232  CB  LEU B  43      88.436 -34.609  11.581  1.00 35.34           C  
ANISOU 3232  CB  LEU B  43     4345   4374   4710    569   -359   -436       C  
ATOM   3233  CG  LEU B  43      89.927 -34.788  11.401  1.00 44.12           C  
ANISOU 3233  CG  LEU B  43     5359   5549   5855    634   -391   -501       C  
ATOM   3234  CD1 LEU B  43      90.437 -33.611  10.585  1.00 42.50           C  
ANISOU 3234  CD1 LEU B  43     5030   5399   5719    541   -366   -536       C  
ATOM   3235  CD2 LEU B  43      90.607 -34.864  12.760  1.00 46.03           C  
ANISOU 3235  CD2 LEU B  43     5598   5819   6072    746   -482   -535       C  
ATOM   3236  N   PHE B  44      85.303 -35.581  11.721  1.00 34.39           N  
ANISOU 3236  N   PHE B  44     4455   4084   4526    482   -258   -320       N  
ATOM   3237  CA  PHE B  44      83.977 -34.964  11.679  1.00 34.05           C  
ANISOU 3237  CA  PHE B  44     4432   4011   4494    395   -229   -291       C  
ATOM   3238  C   PHE B  44      82.989 -35.879  10.972  1.00 37.25           C  
ANISOU 3238  C   PHE B  44     4894   4355   4904    354   -171   -277       C  
ATOM   3239  O   PHE B  44      83.259 -36.335   9.858  1.00 36.79           O  
ANISOU 3239  O   PHE B  44     4814   4309   4857    340   -154   -297       O  
ATOM   3240  CB  PHE B  44      84.054 -33.621  10.953  1.00 32.29           C  
ANISOU 3240  CB  PHE B  44     4115   3844   4311    318   -240   -302       C  
ATOM   3241  CG  PHE B  44      82.723 -32.941  10.777  1.00 32.88           C  
ANISOU 3241  CG  PHE B  44     4200   3893   4401    239   -219   -276       C  
ATOM   3242  CD1 PHE B  44      82.161 -32.220  11.824  1.00 32.39           C  
ANISOU 3242  CD1 PHE B  44     4153   3817   4336    232   -233   -263       C  
ATOM   3243  CD2 PHE B  44      82.038 -33.010   9.567  1.00 34.71           C  
ANISOU 3243  CD2 PHE B  44     4424   4118   4645    179   -190   -272       C  
ATOM   3244  CE1 PHE B  44      80.925 -31.586  11.668  1.00 31.35           C  
ANISOU 3244  CE1 PHE B  44     4023   3663   4226    167   -213   -245       C  
ATOM   3245  CE2 PHE B  44      80.803 -32.366   9.407  1.00 32.57           C  
ANISOU 3245  CE2 PHE B  44     4154   3829   4391    119   -183   -255       C  
ATOM   3246  CZ  PHE B  44      80.247 -31.671  10.464  1.00 30.57           C  
ANISOU 3246  CZ  PHE B  44     3909   3560   4146    113   -192   -242       C  
ATOM   3247  N   GLU B  45      81.850 -36.148  11.600  1.00 36.45           N  
ANISOU 3247  N   GLU B  45     4863   4190   4798    333   -136   -252       N  
ATOM   3248  CA  GLU B  45      80.768 -36.902  10.984  1.00 34.79           C  
ANISOU 3248  CA  GLU B  45     4690   3920   4610    278    -80   -254       C  
ATOM   3249  C   GLU B  45      79.617 -35.944  10.727  1.00 33.27           C  
ANISOU 3249  C   GLU B  45     4453   3737   4451    191    -78   -253       C  
ATOM   3250  O   GLU B  45      79.111 -35.313  11.666  1.00 36.83           O  
ANISOU 3250  O   GLU B  45     4915   4177   4903    185    -76   -234       O  
ATOM   3251  CB  GLU B  45      80.300 -38.060  11.865  1.00 38.91           C  
ANISOU 3251  CB  GLU B  45     5323   4346   5114    315    -23   -234       C  
ATOM   3252  CG  GLU B  45      79.170 -38.838  11.207  1.00 45.33           C  
ANISOU 3252  CG  GLU B  45     6161   5093   5970    244     41   -253       C  
ATOM   3253  CD  GLU B  45      78.520 -39.869  12.120  1.00 56.56           C  
ANISOU 3253  CD  GLU B  45     7696   6404   7390    258    122   -231       C  
ATOM   3254  OE1 GLU B  45      78.862 -39.922  13.320  1.00 59.53           O  
ANISOU 3254  OE1 GLU B  45     8146   6754   7717    330    129   -192       O  
ATOM   3255  OE2 GLU B  45      77.652 -40.618  11.623  1.00 63.58           O  
ANISOU 3255  OE2 GLU B  45     8603   7229   8326    196    183   -258       O  
ATOM   3256  N   ASN B  46      79.208 -35.831   9.463  1.00 32.72           N  
ANISOU 3256  N   ASN B  46     4337   3690   4405    134    -80   -275       N  
ATOM   3257  CA  ASN B  46      78.204 -34.841   9.079  1.00 32.04           C  
ANISOU 3257  CA  ASN B  46     4201   3623   4348     68    -94   -276       C  
ATOM   3258  C   ASN B  46      76.810 -35.361   9.410  1.00 34.96           C  
ANISOU 3258  C   ASN B  46     4599   3929   4755     26    -50   -288       C  
ATOM   3259  O   ASN B  46      76.376 -36.368   8.846  1.00 34.02           O  
ANISOU 3259  O   ASN B  46     4499   3772   4654      4    -20   -320       O  
ATOM   3260  CB  ASN B  46      78.329 -34.537   7.591  1.00 32.42           C  
ANISOU 3260  CB  ASN B  46     4203   3723   4393     40   -120   -296       C  
ATOM   3261  CG  ASN B  46      77.306 -33.533   7.108  1.00 33.32           C  
ANISOU 3261  CG  ASN B  46     4274   3858   4527    -10   -144   -296       C  
ATOM   3262  OD1 ASN B  46      76.838 -32.685   7.870  1.00 33.12           O  
ANISOU 3262  OD1 ASN B  46     4234   3829   4523    -21   -151   -276       O  
ATOM   3263  ND2 ASN B  46      76.944 -33.632   5.821  1.00 31.44           N  
ANISOU 3263  ND2 ASN B  46     4021   3645   4281    -34   -162   -321       N  
ATOM   3264  N   LYS B  47      76.117 -34.682  10.330  1.00 34.90           N  
ANISOU 3264  N   LYS B  47     4589   3907   4766     11    -39   -271       N  
ATOM   3265  CA  LYS B  47      74.719 -34.966  10.638  1.00 36.30           C  
ANISOU 3265  CA  LYS B  47     4770   4028   4993    -39     11   -289       C  
ATOM   3266  C   LYS B  47      73.781 -33.896  10.090  1.00 39.02           C  
ANISOU 3266  C   LYS B  47     5034   4413   5379    -87    -26   -307       C  
ATOM   3267  O   LYS B  47      72.586 -33.931  10.387  1.00 38.59           O  
ANISOU 3267  O   LYS B  47     4960   4323   5379   -128     10   -330       O  
ATOM   3268  CB  LYS B  47      74.515 -35.106  12.151  1.00 40.17           C  
ANISOU 3268  CB  LYS B  47     5328   4462   5473    -16     68   -260       C  
ATOM   3269  CG  LYS B  47      75.396 -36.172  12.820  1.00 46.94           C  
ANISOU 3269  CG  LYS B  47     6285   5273   6278     52    102   -235       C  
ATOM   3270  CD  LYS B  47      75.322 -37.504  12.092  1.00 53.11           C  
ANISOU 3270  CD  LYS B  47     7096   6002   7079     37    142   -262       C  
ATOM   3271  CE  LYS B  47      73.949 -38.143  12.198  1.00 64.42           C  
ANISOU 3271  CE  LYS B  47     8542   7354   8580    -34    227   -290       C  
ATOM   3272  NZ  LYS B  47      73.657 -38.615  13.575  1.00 68.91           N  
ANISOU 3272  NZ  LYS B  47     9214   7837   9133    -11    319   -253       N  
ATOM   3273  N   THR B  48      74.292 -32.951   9.295  1.00 35.91           N  
ANISOU 3273  N   THR B  48     4594   4086   4963    -79    -90   -298       N  
ATOM   3274  CA  THR B  48      73.471 -31.877   8.751  1.00 33.77           C  
ANISOU 3274  CA  THR B  48     4261   3849   4720   -106   -131   -306       C  
ATOM   3275  C   THR B  48      72.941 -32.262   7.369  1.00 34.07           C  
ANISOU 3275  C   THR B  48     4268   3910   4766   -129   -164   -348       C  
ATOM   3276  O   THR B  48      73.290 -33.306   6.804  1.00 36.91           O  
ANISOU 3276  O   THR B  48     4653   4261   5109   -129   -152   -374       O  
ATOM   3277  CB  THR B  48      74.271 -30.583   8.642  1.00 36.08           C  
ANISOU 3277  CB  THR B  48     4538   4190   4983    -84   -174   -268       C  
ATOM   3278  OG1 THR B  48      75.020 -30.612   7.419  1.00 33.54           O  
ANISOU 3278  OG1 THR B  48     4212   3910   4624    -75   -203   -267       O  
ATOM   3279  CG2 THR B  48      75.231 -30.426   9.810  1.00 31.65           C  
ANISOU 3279  CG2 THR B  48     4008   3618   4398    -51   -158   -241       C  
ATOM   3280  N   THR B  49      72.116 -31.388   6.797  1.00 33.31           N  
ANISOU 3280  N   THR B  49     4120   3846   4690   -140   -211   -360       N  
ATOM   3281  CA  THR B  49      71.656 -31.542   5.420  1.00 35.57           C  
ANISOU 3281  CA  THR B  49     4380   4170   4966   -145   -264   -401       C  
ATOM   3282  C   THR B  49      72.550 -30.806   4.405  1.00 34.16           C  
ANISOU 3282  C   THR B  49     4220   4045   4712   -112   -308   -364       C  
ATOM   3283  O   THR B  49      72.222 -30.774   3.213  1.00 33.52           O  
ANISOU 3283  O   THR B  49     4134   4002   4601   -102   -358   -389       O  
ATOM   3284  CB  THR B  49      70.196 -31.076   5.302  1.00 38.55           C  
ANISOU 3284  CB  THR B  49     4691   4553   5403   -162   -299   -443       C  
ATOM   3285  OG1 THR B  49      70.080 -29.712   5.722  1.00 39.45           O  
ANISOU 3285  OG1 THR B  49     4788   4679   5520   -140   -319   -398       O  
ATOM   3286  CG2 THR B  49      69.290 -31.948   6.204  1.00 35.98           C  
ANISOU 3286  CG2 THR B  49     4342   4168   5161   -207   -233   -492       C  
ATOM   3287  N   LEU B  50      73.672 -30.249   4.844  1.00 33.23           N  
ANISOU 3287  N   LEU B  50     4129   3931   4567    -94   -287   -310       N  
ATOM   3288  CA  LEU B  50      74.657 -29.599   3.981  1.00 32.66           C  
ANISOU 3288  CA  LEU B  50     4076   3898   4435    -73   -301   -274       C  
ATOM   3289  C   LEU B  50      75.671 -30.618   3.466  1.00 32.39           C  
ANISOU 3289  C   LEU B  50     4072   3874   4361    -64   -274   -289       C  
ATOM   3290  O   LEU B  50      75.812 -31.705   4.041  1.00 33.30           O  
ANISOU 3290  O   LEU B  50     4199   3958   4496    -67   -244   -314       O  
ATOM   3291  CB  LEU B  50      75.386 -28.499   4.761  1.00 29.60           C  
ANISOU 3291  CB  LEU B  50     3686   3505   4057    -68   -284   -225       C  
ATOM   3292  CG  LEU B  50      74.576 -27.276   5.190  1.00 38.91           C  
ANISOU 3292  CG  LEU B  50     4842   4672   5269    -70   -305   -205       C  
ATOM   3293  CD1 LEU B  50      75.393 -26.392   6.109  1.00 36.10           C  
ANISOU 3293  CD1 LEU B  50     4486   4303   4929    -71   -282   -173       C  
ATOM   3294  CD2 LEU B  50      74.149 -26.506   3.973  1.00 41.49           C  
ANISOU 3294  CD2 LEU B  50     5178   5024   5564    -54   -347   -188       C  
ATOM   3295  N   PRO B  51      76.399 -30.309   2.379  1.00 31.97           N  
ANISOU 3295  N   PRO B  51     4040   3858   4251    -50   -277   -273       N  
ATOM   3296  CA  PRO B  51      77.490 -31.206   1.956  1.00 30.81           C  
ANISOU 3296  CA  PRO B  51     3915   3721   4071    -38   -242   -288       C  
ATOM   3297  C   PRO B  51      78.518 -31.360   3.064  1.00 28.99           C  
ANISOU 3297  C   PRO B  51     3672   3473   3869    -27   -206   -274       C  
ATOM   3298  O   PRO B  51      78.795 -30.424   3.821  1.00 32.76           O  
ANISOU 3298  O   PRO B  51     4128   3948   4371    -31   -205   -244       O  
ATOM   3299  CB  PRO B  51      78.094 -30.505   0.730  1.00 31.13           C  
ANISOU 3299  CB  PRO B  51     3978   3802   4046    -26   -236   -263       C  
ATOM   3300  CG  PRO B  51      76.955 -29.598   0.219  1.00 35.87           C  
ANISOU 3300  CG  PRO B  51     4586   4413   4631    -24   -289   -247       C  
ATOM   3301  CD  PRO B  51      76.206 -29.175   1.452  1.00 33.44           C  
ANISOU 3301  CD  PRO B  51     4238   4073   4395    -39   -305   -241       C  
ATOM   3302  N   VAL B  52      79.097 -32.564   3.138  1.00 28.35           N  
ANISOU 3302  N   VAL B  52     3608   3380   3784     -8   -181   -303       N  
ATOM   3303  CA  VAL B  52      80.005 -32.912   4.234  1.00 31.92           C  
ANISOU 3303  CA  VAL B  52     4054   3816   4257     20   -160   -298       C  
ATOM   3304  C   VAL B  52      81.124 -31.878   4.400  1.00 28.88           C  
ANISOU 3304  C   VAL B  52     3631   3467   3876     27   -154   -274       C  
ATOM   3305  O   VAL B  52      81.446 -31.467   5.519  1.00 30.57           O  
ANISOU 3305  O   VAL B  52     3825   3674   4117     38   -163   -265       O  
ATOM   3306  CB  VAL B  52      80.573 -34.333   4.023  1.00 33.36           C  
ANISOU 3306  CB  VAL B  52     4267   3982   4427     53   -134   -331       C  
ATOM   3307  CG1 VAL B  52      81.221 -34.473   2.621  1.00 30.17           C  
ANISOU 3307  CG1 VAL B  52     3862   3619   3980     57   -118   -349       C  
ATOM   3308  CG2 VAL B  52      81.575 -34.688   5.126  1.00 35.20           C  
ANISOU 3308  CG2 VAL B  52     4497   4204   4673    103   -125   -326       C  
ATOM   3309  N   ASN B  53      81.759 -31.454   3.308  1.00 30.21           N  
ANISOU 3309  N   ASN B  53     3788   3671   4018     19   -134   -270       N  
ATOM   3310  CA  ASN B  53      82.916 -30.567   3.474  1.00 29.40           C  
ANISOU 3310  CA  ASN B  53     3640   3594   3936     16   -111   -260       C  
ATOM   3311  C   ASN B  53      82.502 -29.163   3.912  1.00 34.44           C  
ANISOU 3311  C   ASN B  53     4262   4224   4601    -17   -125   -227       C  
ATOM   3312  O   ASN B  53      83.273 -28.468   4.587  1.00 33.06           O  
ANISOU 3312  O   ASN B  53     4043   4055   4465    -22   -119   -231       O  
ATOM   3313  CB  ASN B  53      83.732 -30.477   2.184  1.00 34.03           C  
ANISOU 3313  CB  ASN B  53     4225   4213   4491     10    -62   -264       C  
ATOM   3314  CG  ASN B  53      82.937 -29.904   1.030  1.00 36.45           C  
ANISOU 3314  CG  ASN B  53     4580   4523   4746    -14    -59   -234       C  
ATOM   3315  OD1 ASN B  53      81.852 -30.392   0.712  1.00 33.30           O  
ANISOU 3315  OD1 ASN B  53     4219   4114   4318     -9    -97   -241       O  
ATOM   3316  ND2 ASN B  53      83.471 -28.856   0.399  1.00 33.90           N  
ANISOU 3316  ND2 ASN B  53     4256   4212   4414    -36    -14   -204       N  
ATOM   3317  N   VAL B  54      81.295 -28.742   3.543  1.00 30.70           N  
ANISOU 3317  N   VAL B  54     3819   3734   4110    -34   -148   -204       N  
ATOM   3318  CA  VAL B  54      80.780 -27.442   3.966  1.00 34.67           C  
ANISOU 3318  CA  VAL B  54     4313   4220   4639    -57   -162   -173       C  
ATOM   3319  C   VAL B  54      80.419 -27.470   5.445  1.00 32.84           C  
ANISOU 3319  C   VAL B  54     4065   3965   4449    -50   -188   -184       C  
ATOM   3320  O   VAL B  54      80.802 -26.576   6.212  1.00 30.99           O  
ANISOU 3320  O   VAL B  54     3803   3723   4248    -60   -188   -180       O  
ATOM   3321  CB  VAL B  54      79.571 -27.066   3.094  1.00 33.26           C  
ANISOU 3321  CB  VAL B  54     4171   4036   4428    -61   -187   -151       C  
ATOM   3322  CG1 VAL B  54      78.932 -25.761   3.589  1.00 30.45           C  
ANISOU 3322  CG1 VAL B  54     3809   3655   4105    -73   -205   -120       C  
ATOM   3323  CG2 VAL B  54      80.014 -26.966   1.623  1.00 32.07           C  
ANISOU 3323  CG2 VAL B  54     4057   3911   4217    -57   -159   -135       C  
ATOM   3324  N   ALA B  55      79.685 -28.508   5.866  1.00 33.10           N  
ANISOU 3324  N   ALA B  55     4118   3980   4478    -35   -203   -202       N  
ATOM   3325  CA  ALA B  55      79.310 -28.654   7.268  1.00 31.38           C  
ANISOU 3325  CA  ALA B  55     3903   3734   4286    -24   -212   -208       C  
ATOM   3326  C   ALA B  55      80.535 -28.682   8.161  1.00 30.79           C  
ANISOU 3326  C   ALA B  55     3811   3671   4217      5   -212   -222       C  
ATOM   3327  O   ALA B  55      80.521 -28.129   9.269  1.00 31.78           O  
ANISOU 3327  O   ALA B  55     3931   3786   4359     12   -226   -223       O  
ATOM   3328  CB  ALA B  55      78.492 -29.935   7.460  1.00 31.35           C  
ANISOU 3328  CB  ALA B  55     3933   3699   4278    -16   -204   -226       C  
ATOM   3329  N   PHE B  56      81.588 -29.373   7.710  1.00 29.50           N  
ANISOU 3329  N   PHE B  56     3638   3532   4039     28   -200   -240       N  
ATOM   3330  CA  PHE B  56      82.851 -29.443   8.441  1.00 29.13           C  
ANISOU 3330  CA  PHE B  56     3558   3508   4002     66   -212   -266       C  
ATOM   3331  C   PHE B  56      83.432 -28.051   8.668  1.00 30.76           C  
ANISOU 3331  C   PHE B  56     3708   3734   4245     37   -217   -272       C  
ATOM   3332  O   PHE B  56      83.853 -27.706   9.779  1.00 30.50           O  
ANISOU 3332  O   PHE B  56     3654   3706   4227     58   -247   -296       O  
ATOM   3333  CB  PHE B  56      83.832 -30.302   7.637  1.00 30.41           C  
ANISOU 3333  CB  PHE B  56     3706   3697   4152     92   -191   -288       C  
ATOM   3334  CG  PHE B  56      85.210 -30.418   8.239  1.00 31.19           C  
ANISOU 3334  CG  PHE B  56     3753   3830   4270    139   -208   -327       C  
ATOM   3335  CD1 PHE B  56      85.385 -30.848   9.540  1.00 31.32           C  
ANISOU 3335  CD1 PHE B  56     3787   3838   4276    200   -249   -341       C  
ATOM   3336  CD2 PHE B  56      86.335 -30.141   7.477  1.00 35.24           C  
ANISOU 3336  CD2 PHE B  56     4200   4383   4809    128   -180   -354       C  
ATOM   3337  CE1 PHE B  56      86.667 -30.996  10.090  1.00 37.18           C  
ANISOU 3337  CE1 PHE B  56     4475   4619   5032    260   -282   -387       C  
ATOM   3338  CE2 PHE B  56      87.623 -30.288   8.014  1.00 36.80           C  
ANISOU 3338  CE2 PHE B  56     4329   4619   5036    175   -202   -405       C  
ATOM   3339  CZ  PHE B  56      87.783 -30.711   9.324  1.00 33.49           C  
ANISOU 3339  CZ  PHE B  56     3922   4198   4605    245   -262   -425       C  
ATOM   3340  N   GLU B  57      83.444 -27.227   7.628  1.00 31.89           N  
ANISOU 3340  N   GLU B  57     3835   3883   4400    -11   -187   -254       N  
ATOM   3341  CA  GLU B  57      84.018 -25.893   7.773  1.00 31.54           C  
ANISOU 3341  CA  GLU B  57     3741   3841   4401    -48   -176   -261       C  
ATOM   3342  C   GLU B  57      83.175 -25.017   8.706  1.00 32.61           C  
ANISOU 3342  C   GLU B  57     3891   3945   4554    -61   -203   -250       C  
ATOM   3343  O   GLU B  57      83.722 -24.290   9.547  1.00 31.93           O  
ANISOU 3343  O   GLU B  57     3766   3861   4505    -68   -219   -281       O  
ATOM   3344  CB  GLU B  57      84.169 -25.252   6.394  1.00 34.40           C  
ANISOU 3344  CB  GLU B  57     4107   4202   4762    -92   -121   -232       C  
ATOM   3345  CG  GLU B  57      84.766 -23.846   6.428  1.00 36.74           C  
ANISOU 3345  CG  GLU B  57     4362   4484   5113   -141    -88   -236       C  
ATOM   3346  CD  GLU B  57      85.051 -23.301   5.036  1.00 45.13           C  
ANISOU 3346  CD  GLU B  57     5444   5538   6165   -178    -13   -201       C  
ATOM   3347  OE1 GLU B  57      85.170 -24.109   4.095  1.00 49.85           O  
ANISOU 3347  OE1 GLU B  57     6067   6158   6715   -161     10   -192       O  
ATOM   3348  OE2 GLU B  57      85.159 -22.067   4.884  1.00 46.27           O  
ANISOU 3348  OE2 GLU B  57     5587   5647   6345   -223     27   -183       O  
ATOM   3349  N   LEU B  58      81.845 -25.082   8.593  1.00 31.87           N  
ANISOU 3349  N   LEU B  58     3848   3824   4439    -64   -211   -215       N  
ATOM   3350  CA  LEU B  58      81.000 -24.297   9.492  1.00 32.89           C  
ANISOU 3350  CA  LEU B  58     3987   3921   4587    -71   -230   -209       C  
ATOM   3351  C   LEU B  58      81.161 -24.755  10.937  1.00 35.68           C  
ANISOU 3351  C   LEU B  58     4347   4277   4934    -33   -258   -240       C  
ATOM   3352  O   LEU B  58      81.212 -23.934  11.860  1.00 32.57           O  
ANISOU 3352  O   LEU B  58     3942   3873   4560    -36   -274   -259       O  
ATOM   3353  CB  LEU B  58      79.530 -24.392   9.069  1.00 30.10           C  
ANISOU 3353  CB  LEU B  58     3673   3544   4221    -75   -232   -177       C  
ATOM   3354  CG  LEU B  58      79.138 -23.857   7.685  1.00 43.19           C  
ANISOU 3354  CG  LEU B  58     5341   5200   5868    -95   -220   -142       C  
ATOM   3355  CD1 LEU B  58      77.616 -23.888   7.482  1.00 44.68           C  
ANISOU 3355  CD1 LEU B  58     5551   5371   6054    -88   -243   -129       C  
ATOM   3356  CD2 LEU B  58      79.665 -22.473   7.472  1.00 42.03           C  
ANISOU 3356  CD2 LEU B  58     5182   5036   5749   -122   -198   -125       C  
ATOM   3357  N   TRP B  59      81.244 -26.063  11.153  1.00 27.67           N  
ANISOU 3357  N   TRP B  59     3360   3270   3884      8   -263   -247       N  
ATOM   3358  CA  TRP B  59      81.494 -26.571  12.497  1.00 32.18           C  
ANISOU 3358  CA  TRP B  59     3956   3839   4430     61   -288   -270       C  
ATOM   3359  C   TRP B  59      82.836 -26.079  13.029  1.00 33.25           C  
ANISOU 3359  C   TRP B  59     4038   4013   4582     81   -323   -317       C  
ATOM   3360  O   TRP B  59      82.942 -25.630  14.180  1.00 33.39           O  
ANISOU 3360  O   TRP B  59     4061   4033   4593    104   -355   -344       O  
ATOM   3361  CB  TRP B  59      81.453 -28.100  12.484  1.00 30.49           C  
ANISOU 3361  CB  TRP B  59     3792   3617   4177    106   -277   -263       C  
ATOM   3362  CG  TRP B  59      81.914 -28.689  13.784  1.00 32.60           C  
ANISOU 3362  CG  TRP B  59     4100   3882   4403    178   -303   -280       C  
ATOM   3363  CD1 TRP B  59      81.224 -28.697  14.981  1.00 37.69           C  
ANISOU 3363  CD1 TRP B  59     4807   4495   5018    203   -300   -271       C  
ATOM   3364  CD2 TRP B  59      83.150 -29.359  14.032  1.00 35.89           C  
ANISOU 3364  CD2 TRP B  59     4507   4332   4799    245   -336   -310       C  
ATOM   3365  NE1 TRP B  59      81.972 -29.327  15.947  1.00 40.14           N  
ANISOU 3365  NE1 TRP B  59     5160   4815   5276    287   -333   -288       N  
ATOM   3366  CE2 TRP B  59      83.155 -29.742  15.394  1.00 43.84           C  
ANISOU 3366  CE2 TRP B  59     5580   5325   5752    318   -362   -313       C  
ATOM   3367  CE3 TRP B  59      84.264 -29.661  13.245  1.00 38.40           C  
ANISOU 3367  CE3 TRP B  59     4765   4690   5135    258   -345   -336       C  
ATOM   3368  CZ2 TRP B  59      84.221 -30.417  15.976  1.00 46.33           C  
ANISOU 3368  CZ2 TRP B  59     5906   5667   6028    411   -409   -341       C  
ATOM   3369  CZ3 TRP B  59      85.325 -30.347  13.827  1.00 49.48           C  
ANISOU 3369  CZ3 TRP B  59     6165   6121   6513    345   -387   -369       C  
ATOM   3370  CH2 TRP B  59      85.295 -30.713  15.179  1.00 50.37           C  
ANISOU 3370  CH2 TRP B  59     6347   6222   6569    425   -426   -371       C  
ATOM   3371  N   ALA B  60      83.885 -26.170  12.209  1.00 30.46           N  
ANISOU 3371  N   ALA B  60     3628   3694   4250     73   -316   -337       N  
ATOM   3372  CA  ALA B  60      85.193 -25.704  12.662  1.00 31.67           C  
ANISOU 3372  CA  ALA B  60     3708   3889   4438     86   -348   -398       C  
ATOM   3373  C   ALA B  60      85.175 -24.214  12.980  1.00 34.31           C  
ANISOU 3373  C   ALA B  60     4004   4210   4822     31   -349   -419       C  
ATOM   3374  O   ALA B  60      85.930 -23.749  13.842  1.00 33.43           O  
ANISOU 3374  O   ALA B  60     3845   4124   4734     46   -393   -482       O  
ATOM   3375  CB  ALA B  60      86.254 -25.993  11.606  1.00 33.94           C  
ANISOU 3375  CB  ALA B  60     3931   4209   4754     75   -320   -419       C  
ATOM   3376  N   LYS B  61      84.330 -23.457  12.300  1.00 34.60           N  
ANISOU 3376  N   LYS B  61     4062   4208   4878    -28   -307   -373       N  
ATOM   3377  CA  LYS B  61      84.244 -22.017  12.496  1.00 33.63           C  
ANISOU 3377  CA  LYS B  61     3914   4057   4806    -81   -296   -385       C  
ATOM   3378  C   LYS B  61      83.171 -21.618  13.503  1.00 36.25           C  
ANISOU 3378  C   LYS B  61     4298   4356   5120    -67   -319   -376       C  
ATOM   3379  O   LYS B  61      82.788 -20.444  13.543  1.00 34.59           O  
ANISOU 3379  O   LYS B  61     4085   4109   4949   -108   -302   -373       O  
ATOM   3380  CB  LYS B  61      83.999 -21.329  11.146  1.00 33.54           C  
ANISOU 3380  CB  LYS B  61     3906   4016   4823   -141   -233   -336       C  
ATOM   3381  CG  LYS B  61      85.256 -21.366  10.261  1.00 37.93           C  
ANISOU 3381  CG  LYS B  61     4400   4598   5412   -168   -192   -359       C  
ATOM   3382  CD  LYS B  61      85.040 -20.782   8.871  1.00 36.92           C  
ANISOU 3382  CD  LYS B  61     4301   4438   5290   -217   -119   -301       C  
ATOM   3383  CE  LYS B  61      86.354 -20.761   8.093  1.00 39.50           C  
ANISOU 3383  CE  LYS B  61     4567   4788   5656   -251    -58   -330       C  
ATOM   3384  NZ  LYS B  61      86.205 -20.255   6.697  1.00 37.05           N  
ANISOU 3384  NZ  LYS B  61     4302   4442   5331   -290     25   -267       N  
ATOM   3385  N   ARG B  62      82.711 -22.550  14.333  1.00 31.96           N  
ANISOU 3385  N   ARG B  62     3805   3819   4518     -9   -347   -373       N  
ATOM   3386  CA  ARG B  62      81.627 -22.266  15.271  1.00 30.53           C  
ANISOU 3386  CA  ARG B  62     3679   3605   4315      4   -351   -362       C  
ATOM   3387  C   ARG B  62      82.077 -21.267  16.332  1.00 34.56           C  
ANISOU 3387  C   ARG B  62     4169   4118   4846      5   -385   -422       C  
ATOM   3388  O   ARG B  62      83.261 -21.173  16.679  1.00 31.36           O  
ANISOU 3388  O   ARG B  62     3712   3751   4453     19   -425   -484       O  
ATOM   3389  CB  ARG B  62      81.153 -23.560  15.942  1.00 34.15           C  
ANISOU 3389  CB  ARG B  62     4207   4063   4705     66   -355   -346       C  
ATOM   3390  CG  ARG B  62      82.216 -24.184  16.863  1.00 34.88           C  
ANISOU 3390  CG  ARG B  62     4306   4195   4753    137   -407   -392       C  
ATOM   3391  CD  ARG B  62      81.896 -25.639  17.199  1.00 41.40           C  
ANISOU 3391  CD  ARG B  62     5211   5008   5509    200   -395   -360       C  
ATOM   3392  NE  ARG B  62      82.901 -26.222  18.083  1.00 40.97           N  
ANISOU 3392  NE  ARG B  62     5176   4990   5402    287   -453   -399       N  
ATOM   3393  CZ  ARG B  62      84.078 -26.716  17.685  1.00 46.63           C  
ANISOU 3393  CZ  ARG B  62     5842   5751   6126    321   -489   -429       C  
ATOM   3394  NH1 ARG B  62      84.433 -26.694  16.402  1.00 34.28           N  
ANISOU 3394  NH1 ARG B  62     4208   4199   4619    268   -462   -423       N  
ATOM   3395  NH2 ARG B  62      84.919 -27.220  18.577  1.00 44.49           N  
ANISOU 3395  NH2 ARG B  62     5590   5514   5802    415   -553   -468       N  
ATOM   3396  N   ASN B  63      81.117 -20.499  16.849  1.00 33.31           N  
ANISOU 3396  N   ASN B  63     4042   3919   4694     -9   -370   -414       N  
ATOM   3397  CA  ASN B  63      81.431 -19.538  17.902  1.00 34.49           C  
ANISOU 3397  CA  ASN B  63     4181   4064   4858     -8   -401   -478       C  
ATOM   3398  C   ASN B  63      81.719 -20.289  19.204  1.00 31.43           C  
ANISOU 3398  C   ASN B  63     3840   3711   4391     71   -451   -516       C  
ATOM   3399  O   ASN B  63      80.901 -21.107  19.647  1.00 35.95           O  
ANISOU 3399  O   ASN B  63     4490   4270   4901    113   -430   -476       O  
ATOM   3400  CB  ASN B  63      80.253 -18.563  18.085  1.00 33.77           C  
ANISOU 3400  CB  ASN B  63     4121   3918   4794    -36   -367   -457       C  
ATOM   3401  CG  ASN B  63      80.628 -17.338  18.889  1.00 40.23           C  
ANISOU 3401  CG  ASN B  63     4918   4720   5648    -53   -388   -527       C  
ATOM   3402  OD1 ASN B  63      81.229 -17.442  19.952  1.00 39.31           O  
ANISOU 3402  OD1 ASN B  63     4807   4636   5494    -14   -438   -593       O  
ATOM   3403  ND2 ASN B  63      80.289 -16.157  18.368  1.00 43.08           N  
ANISOU 3403  ND2 ASN B  63     5261   5027   6079   -107   -353   -516       N  
ATOM   3404  N   ILE B  64      82.878 -20.013  19.812  1.00 32.15           N  
ANISOU 3404  N   ILE B  64     3887   3845   4485     92   -513   -597       N  
ATOM   3405  CA  ILE B  64      83.348 -20.714  21.013  1.00 36.41           C  
ANISOU 3405  CA  ILE B  64     4471   4426   4937    185   -579   -641       C  
ATOM   3406  C   ILE B  64      83.324 -19.809  22.248  1.00 39.52           C  
ANISOU 3406  C   ILE B  64     4886   4820   5311    203   -620   -713       C  
ATOM   3407  O   ILE B  64      83.993 -20.093  23.244  1.00 39.00           O  
ANISOU 3407  O   ILE B  64     4839   4800   5179    280   -696   -776       O  
ATOM   3408  CB  ILE B  64      84.752 -21.325  20.815  1.00 35.75           C  
ANISOU 3408  CB  ILE B  64     4320   4407   4857    224   -640   -691       C  
ATOM   3409  CG1 ILE B  64      85.801 -20.234  20.553  1.00 38.58           C  
ANISOU 3409  CG1 ILE B  64     4554   4788   5315    163   -669   -780       C  
ATOM   3410  CG2 ILE B  64      84.728 -22.381  19.706  1.00 35.78           C  
ANISOU 3410  CG2 ILE B  64     4322   4409   4862    222   -597   -621       C  
ATOM   3411  CD1 ILE B  64      87.247 -20.687  20.800  1.00 41.23           C  
ANISOU 3411  CD1 ILE B  64     4809   5201   5657    219   -752   -868       C  
ATOM   3412  N   LYS B  65      82.590 -18.721  22.198  1.00 35.98           N  
ANISOU 3412  N   LYS B  65     4436   4321   4914    141   -576   -709       N  
ATOM   3413  CA  LYS B  65      82.297 -17.935  23.382  1.00 37.97           C  
ANISOU 3413  CA  LYS B  65     4729   4560   5137    160   -599   -768       C  
ATOM   3414  C   LYS B  65      80.869 -18.223  23.815  1.00 37.03           C  
ANISOU 3414  C   LYS B  65     4714   4397   4960    183   -534   -701       C  
ATOM   3415  O   LYS B  65      80.105 -18.828  23.057  1.00 36.67           O  
ANISOU 3415  O   LYS B  65     4685   4324   4924    165   -472   -617       O  
ATOM   3416  CB  LYS B  65      82.468 -16.438  23.075  1.00 37.80           C  
ANISOU 3416  CB  LYS B  65     4634   4502   5225     74   -587   -821       C  
ATOM   3417  CG  LYS B  65      83.851 -16.077  22.554  1.00 47.50           C  
ANISOU 3417  CG  LYS B  65     5748   5764   6535     31   -627   -892       C  
ATOM   3418  CD  LYS B  65      83.927 -14.583  22.254  1.00 64.05           C  
ANISOU 3418  CD  LYS B  65     7788   7802   8745    -62   -592   -937       C  
ATOM   3419  CE  LYS B  65      82.931 -14.211  21.157  1.00 76.21           C  
ANISOU 3419  CE  LYS B  65     9352   9269  10334   -118   -498   -831       C  
ATOM   3420  NZ  LYS B  65      82.650 -12.747  21.098  1.00 76.24           N  
ANISOU 3420  NZ  LYS B  65     9346   9196  10425   -184   -457   -857       N  
ATOM   3421  N   PRO B  66      80.467 -17.838  25.031  1.00 35.15           N  
ANISOU 3421  N   PRO B  66     4545   4150   4662    224   -541   -741       N  
ATOM   3422  CA  PRO B  66      79.056 -18.009  25.401  1.00 36.98           C  
ANISOU 3422  CA  PRO B  66     4863   4331   4856    234   -459   -682       C  
ATOM   3423  C   PRO B  66      78.184 -17.268  24.406  1.00 34.63           C  
ANISOU 3423  C   PRO B  66     4512   3979   4666    153   -394   -638       C  
ATOM   3424  O   PRO B  66      78.440 -16.107  24.087  1.00 36.49           O  
ANISOU 3424  O   PRO B  66     4687   4194   4983    101   -405   -677       O  
ATOM   3425  CB  PRO B  66      78.973 -17.394  26.803  1.00 35.85           C  
ANISOU 3425  CB  PRO B  66     4786   4190   4645    280   -482   -755       C  
ATOM   3426  CG  PRO B  66      80.402 -17.488  27.336  1.00 36.30           C  
ANISOU 3426  CG  PRO B  66     4821   4316   4656    332   -596   -841       C  
ATOM   3427  CD  PRO B  66      81.244 -17.210  26.124  1.00 34.16           C  
ANISOU 3427  CD  PRO B  66     4420   4059   4501    261   -622   -851       C  
ATOM   3428  N   VAL B  67      77.170 -17.956  23.883  1.00 35.75           N  
ANISOU 3428  N   VAL B  67     4678   4095   4812    145   -326   -560       N  
ATOM   3429  CA  VAL B  67      76.218 -17.327  22.965  1.00 33.40           C  
ANISOU 3429  CA  VAL B  67     4335   3751   4605     88   -274   -520       C  
ATOM   3430  C   VAL B  67      74.810 -17.642  23.451  1.00 37.60           C  
ANISOU 3430  C   VAL B  67     4921   4247   5118    105   -198   -489       C  
ATOM   3431  O   VAL B  67      74.603 -18.613  24.200  1.00 33.56           O  
ANISOU 3431  O   VAL B  67     4483   3743   4526    149   -170   -478       O  
ATOM   3432  CB  VAL B  67      76.421 -17.806  21.505  1.00 33.03           C  
ANISOU 3432  CB  VAL B  67     4230   3713   4606     50   -275   -465       C  
ATOM   3433  CG1 VAL B  67      77.724 -17.210  20.859  1.00 33.63           C  
ANISOU 3433  CG1 VAL B  67     4238   3811   4729     15   -326   -496       C  
ATOM   3434  CG2 VAL B  67      76.434 -19.324  21.435  1.00 31.29           C  
ANISOU 3434  CG2 VAL B  67     4047   3518   4323     84   -265   -427       C  
ATOM   3435  N   PRO B  68      73.815 -16.845  23.037  1.00 33.36           N  
ANISOU 3435  N   PRO B  68     4351   3668   4658     73   -157   -477       N  
ATOM   3436  CA  PRO B  68      72.427 -17.151  23.404  1.00 33.32           C  
ANISOU 3436  CA  PRO B  68     4373   3632   4655     83    -78   -457       C  
ATOM   3437  C   PRO B  68      72.047 -18.557  22.981  1.00 32.35           C  
ANISOU 3437  C   PRO B  68     4261   3519   4512     84    -42   -408       C  
ATOM   3438  O   PRO B  68      72.451 -19.025  21.917  1.00 32.73           O  
ANISOU 3438  O   PRO B  68     4267   3588   4582     62    -74   -377       O  
ATOM   3439  CB  PRO B  68      71.618 -16.114  22.617  1.00 35.38           C  
ANISOU 3439  CB  PRO B  68     4568   3856   5018     52    -66   -448       C  
ATOM   3440  CG  PRO B  68      72.570 -14.962  22.440  1.00 34.78           C  
ANISOU 3440  CG  PRO B  68     4468   3773   4972     34   -122   -480       C  
ATOM   3441  CD  PRO B  68      73.905 -15.614  22.225  1.00 33.37           C  
ANISOU 3441  CD  PRO B  68     4289   3643   4749     31   -177   -482       C  
ATOM   3442  N   GLU B  69      71.245 -19.221  23.815  1.00 32.88           N  
ANISOU 3442  N   GLU B  69     4389   3566   4539    105     35   -403       N  
ATOM   3443  CA  GLU B  69      70.692 -20.500  23.402  1.00 38.91           C  
ANISOU 3443  CA  GLU B  69     5158   4320   5305     93     89   -364       C  
ATOM   3444  C   GLU B  69      69.856 -20.316  22.140  1.00 42.00           C  
ANISOU 3444  C   GLU B  69     5451   4705   5803     47     91   -349       C  
ATOM   3445  O   GLU B  69      69.234 -19.270  21.922  1.00 34.31           O  
ANISOU 3445  O   GLU B  69     4423   3716   4896     36     88   -366       O  
ATOM   3446  CB  GLU B  69      69.856 -21.101  24.522  1.00 39.91           C  
ANISOU 3446  CB  GLU B  69     5366   4410   5386    114    195   -365       C  
ATOM   3447  CG  GLU B  69      70.703 -21.618  25.659  1.00 43.14           C  
ANISOU 3447  CG  GLU B  69     5897   4829   5665    175    190   -366       C  
ATOM   3448  CD  GLU B  69      69.913 -22.449  26.628  1.00 49.04           C  
ANISOU 3448  CD  GLU B  69     6747   5531   6356    196    314   -349       C  
ATOM   3449  OE1 GLU B  69      69.191 -21.852  27.461  1.00 42.99           O  
ANISOU 3449  OE1 GLU B  69     6010   4740   5584    204    381   -375       O  
ATOM   3450  OE2 GLU B  69      70.004 -23.700  26.551  1.00 43.59           O  
ANISOU 3450  OE2 GLU B  69     6111   4823   5628    204    353   -309       O  
ATOM   3451  N   VAL B  70      69.862 -21.346  21.294  1.00 39.39           N  
ANISOU 3451  N   VAL B  70     5100   4384   5482     27     90   -321       N  
ATOM   3452  CA  VAL B  70      69.193 -21.262  19.997  1.00 39.04           C  
ANISOU 3452  CA  VAL B  70     4966   4345   5523     -7     71   -312       C  
ATOM   3453  C   VAL B  70      67.701 -20.980  20.151  1.00 32.43           C  
ANISOU 3453  C   VAL B  70     4081   3479   4763    -20    134   -336       C  
ATOM   3454  O   VAL B  70      67.110 -20.263  19.325  1.00 37.87           O  
ANISOU 3454  O   VAL B  70     4692   4172   5524    -26     99   -343       O  
ATOM   3455  CB  VAL B  70      69.457 -22.553  19.205  1.00 38.83           C  
ANISOU 3455  CB  VAL B  70     4938   4333   5484    -23     65   -290       C  
ATOM   3456  CG1 VAL B  70      68.557 -22.630  17.985  1.00 43.92           C  
ANISOU 3456  CG1 VAL B  70     5497   4984   6209    -54     52   -295       C  
ATOM   3457  CG2 VAL B  70      70.912 -22.603  18.789  1.00 34.83           C  
ANISOU 3457  CG2 VAL B  70     4449   3862   4924     -9     -8   -273       C  
ATOM   3458  N   LYS B  71      67.067 -21.501  21.213  1.00 32.29           N  
ANISOU 3458  N   LYS B  71     4109   3428   4729    -18    232   -351       N  
ATOM   3459  CA  LYS B  71      65.645 -21.222  21.401  1.00 36.33           C  
ANISOU 3459  CA  LYS B  71     4563   3914   5328    -32    304   -384       C  
ATOM   3460  C   LYS B  71      65.386 -19.720  21.554  1.00 35.28           C  
ANISOU 3460  C   LYS B  71     4394   3778   5233     -9    272   -406       C  
ATOM   3461  O   LYS B  71      64.372 -19.204  21.061  1.00 35.10           O  
ANISOU 3461  O   LYS B  71     4282   3751   5304    -12    273   -430       O  
ATOM   3462  CB  LYS B  71      65.094 -21.998  22.601  1.00 35.96           C  
ANISOU 3462  CB  LYS B  71     4586   3825   5251    -37    434   -394       C  
ATOM   3463  CG  LYS B  71      65.653 -21.594  23.966  1.00 38.58           C  
ANISOU 3463  CG  LYS B  71     5032   4144   5482      7    464   -392       C  
ATOM   3464  CD  LYS B  71      65.121 -22.490  25.105  1.00 39.02           C  
ANISOU 3464  CD  LYS B  71     5183   4153   5491      9    607   -390       C  
ATOM   3465  CE  LYS B  71      66.007 -22.408  26.349  1.00 44.80           C  
ANISOU 3465  CE  LYS B  71     6060   4883   6079     69    610   -378       C  
ATOM   3466  NZ  LYS B  71      65.557 -23.345  27.431  1.00 41.82           N  
ANISOU 3466  NZ  LYS B  71     5804   4453   5634     81    756   -362       N  
ATOM   3467  N   ILE B  72      66.302 -18.996  22.202  1.00 33.34           N  
ANISOU 3467  N   ILE B  72     4213   3535   4922     18    238   -405       N  
ATOM   3468  CA  ILE B  72      66.132 -17.543  22.335  1.00 35.78           C  
ANISOU 3468  CA  ILE B  72     4496   3829   5270     38    211   -429       C  
ATOM   3469  C   ILE B  72      66.269 -16.871  20.975  1.00 38.76           C  
ANISOU 3469  C   ILE B  72     4801   4218   5707     33    123   -409       C  
ATOM   3470  O   ILE B  72      65.459 -16.020  20.596  1.00 34.50           O  
ANISOU 3470  O   ILE B  72     4202   3661   5244     48    115   -422       O  
ATOM   3471  CB  ILE B  72      67.145 -16.963  23.341  1.00 37.00           C  
ANISOU 3471  CB  ILE B  72     4734   3981   5342     62    192   -445       C  
ATOM   3472  CG1 ILE B  72      66.934 -17.578  24.722  1.00 35.38           C  
ANISOU 3472  CG1 ILE B  72     4620   3762   5060     82    280   -462       C  
ATOM   3473  CG2 ILE B  72      67.028 -15.435  23.389  1.00 36.27           C  
ANISOU 3473  CG2 ILE B  72     4617   3864   5302     75    164   -474       C  
ATOM   3474  CD1 ILE B  72      65.596 -17.222  25.342  1.00 42.13           C  
ANISOU 3474  CD1 ILE B  72     5457   4581   5969     87    382   -495       C  
ATOM   3475  N   LEU B  73      67.295 -17.246  20.217  1.00 32.43           N  
ANISOU 3475  N   LEU B  73     4009   3446   4867     20     58   -376       N  
ATOM   3476  CA  LEU B  73      67.481 -16.660  18.891  1.00 33.96           C  
ANISOU 3476  CA  LEU B  73     4155   3648   5101     18    -14   -349       C  
ATOM   3477  C   LEU B  73      66.294 -16.960  17.985  1.00 36.07           C  
ANISOU 3477  C   LEU B  73     4347   3924   5436     21    -17   -348       C  
ATOM   3478  O   LEU B  73      65.810 -16.071  17.268  1.00 33.72           O  
ANISOU 3478  O   LEU B  73     4007   3616   5191     46    -58   -343       O  
ATOM   3479  CB  LEU B  73      68.782 -17.182  18.261  1.00 33.76           C  
ANISOU 3479  CB  LEU B  73     4153   3654   5020      0    -64   -318       C  
ATOM   3480  CG  LEU B  73      70.094 -16.883  18.999  1.00 39.01           C  
ANISOU 3480  CG  LEU B  73     4873   4323   5628      0    -81   -330       C  
ATOM   3481  CD1 LEU B  73      71.267 -17.525  18.261  1.00 38.10           C  
ANISOU 3481  CD1 LEU B  73     4760   4244   5473    -16   -125   -305       C  
ATOM   3482  CD2 LEU B  73      70.326 -15.387  19.160  1.00 37.91           C  
ANISOU 3482  CD2 LEU B  73     4732   4149   5523      3    -99   -347       C  
ATOM   3483  N   ASN B  74      65.810 -18.212  17.997  1.00 31.66           N  
ANISOU 3483  N   ASN B  74     3770   3379   4878      0     22   -359       N  
ATOM   3484  CA  ASN B  74      64.628 -18.548  17.213  1.00 34.63           C  
ANISOU 3484  CA  ASN B  74     4061   3768   5330     -2     17   -381       C  
ATOM   3485  C   ASN B  74      63.436 -17.698  17.638  1.00 35.36           C  
ANISOU 3485  C   ASN B  74     4096   3836   5503     25     48   -420       C  
ATOM   3486  O   ASN B  74      62.690 -17.183  16.796  1.00 33.77           O  
ANISOU 3486  O   ASN B  74     3820   3645   5366     55     -4   -432       O  
ATOM   3487  CB  ASN B  74      64.283 -20.037  17.373  1.00 35.37           C  
ANISOU 3487  CB  ASN B  74     4148   3867   5424    -40     77   -399       C  
ATOM   3488  CG  ASN B  74      65.250 -20.945  16.651  1.00 41.70           C  
ANISOU 3488  CG  ASN B  74     4984   4694   6164    -59     36   -367       C  
ATOM   3489  OD1 ASN B  74      66.044 -20.496  15.820  1.00 40.87           O  
ANISOU 3489  OD1 ASN B  74     4890   4613   6027    -45    -42   -334       O  
ATOM   3490  ND2 ASN B  74      65.182 -22.242  16.955  1.00 38.83           N  
ANISOU 3490  ND2 ASN B  74     4644   4321   5788    -90     97   -376       N  
ATOM   3491  N   ASN B  75      63.232 -17.556  18.944  1.00 32.20           N  
ANISOU 3491  N   ASN B  75     3732   3406   5098     23    133   -444       N  
ATOM   3492  CA  ASN B  75      62.062 -16.827  19.422  1.00 31.62           C  
ANISOU 3492  CA  ASN B  75     3601   3308   5106     49    179   -490       C  
ATOM   3493  C   ASN B  75      62.109 -15.363  19.018  1.00 42.51           C  
ANISOU 3493  C   ASN B  75     4968   4671   6511     98    110   -480       C  
ATOM   3494  O   ASN B  75      61.056 -14.733  18.864  1.00 38.01           O  
ANISOU 3494  O   ASN B  75     4324   4091   6027    135    109   -513       O  
ATOM   3495  CB  ASN B  75      61.955 -16.932  20.938  1.00 35.32           C  
ANISOU 3495  CB  ASN B  75     4132   3745   5543     40    291   -514       C  
ATOM   3496  CG  ASN B  75      61.515 -18.310  21.401  1.00 36.81           C  
ANISOU 3496  CG  ASN B  75     4327   3930   5730     -2    392   -529       C  
ATOM   3497  OD1 ASN B  75      61.154 -19.175  20.599  1.00 36.57           O  
ANISOU 3497  OD1 ASN B  75     4236   3918   5742    -32    380   -535       O  
ATOM   3498  ND2 ASN B  75      61.524 -18.507  22.700  1.00 34.94           N  
ANISOU 3498  ND2 ASN B  75     4172   3663   5442     -5    495   -539       N  
ATOM   3499  N   LEU B  76      63.307 -14.808  18.862  1.00 36.53           N  
ANISOU 3499  N   LEU B  76     4281   3907   5690    100     57   -439       N  
ATOM   3500  CA  LEU B  76      63.474 -13.419  18.452  1.00 40.54           C  
ANISOU 3500  CA  LEU B  76     4797   4384   6223    140      4   -422       C  
ATOM   3501  C   LEU B  76      63.503 -13.242  16.939  1.00 42.29           C  
ANISOU 3501  C   LEU B  76     4988   4623   6457    163    -85   -381       C  
ATOM   3502  O   LEU B  76      63.713 -12.121  16.469  1.00 44.54           O  
ANISOU 3502  O   LEU B  76     5296   4873   6755    198   -126   -354       O  
ATOM   3503  CB  LEU B  76      64.759 -12.839  19.054  1.00 33.25           C  
ANISOU 3503  CB  LEU B  76     3961   3436   5236    123      1   -410       C  
ATOM   3504  CG  LEU B  76      64.741 -12.690  20.579  1.00 36.81           C  
ANISOU 3504  CG  LEU B  76     4459   3866   5664    121     75   -457       C  
ATOM   3505  CD1 LEU B  76      66.131 -12.325  21.112  1.00 35.76           C  
ANISOU 3505  CD1 LEU B  76     4402   3724   5461    102     53   -458       C  
ATOM   3506  CD2 LEU B  76      63.721 -11.633  20.978  1.00 36.94           C  
ANISOU 3506  CD2 LEU B  76     4444   3837   5755    163    108   -494       C  
ATOM   3507  N   GLY B  77      63.304 -14.311  16.170  1.00 38.50           N  
ANISOU 3507  N   GLY B  77     4468   4190   5969    146   -111   -375       N  
ATOM   3508  CA  GLY B  77      63.241 -14.205  14.723  1.00 40.65           C  
ANISOU 3508  CA  GLY B  77     4718   4486   6242    177   -198   -342       C  
ATOM   3509  C   GLY B  77      64.567 -14.076  14.006  1.00 38.70           C  
ANISOU 3509  C   GLY B  77     4545   4240   5920    161   -238   -281       C  
ATOM   3510  O   GLY B  77      64.588 -13.623  12.860  1.00 39.86           O  
ANISOU 3510  O   GLY B  77     4700   4389   6056    199   -301   -243       O  
ATOM   3511  N   VAL B  78      65.676 -14.488  14.625  1.00 35.71           N  
ANISOU 3511  N   VAL B  78     4220   3862   5486    111   -203   -272       N  
ATOM   3512  CA  VAL B  78      66.985 -14.367  13.989  1.00 33.25           C  
ANISOU 3512  CA  VAL B  78     3964   3553   5116     90   -230   -225       C  
ATOM   3513  C   VAL B  78      67.086 -15.316  12.795  1.00 39.37           C  
ANISOU 3513  C   VAL B  78     4725   4377   5856     85   -273   -202       C  
ATOM   3514  O   VAL B  78      66.815 -16.518  12.904  1.00 38.89           O  
ANISOU 3514  O   VAL B  78     4636   4353   5788     62   -260   -228       O  
ATOM   3515  CB  VAL B  78      68.093 -14.641  15.015  1.00 34.68           C  
ANISOU 3515  CB  VAL B  78     4189   3732   5255     46   -192   -239       C  
ATOM   3516  CG1 VAL B  78      69.455 -14.792  14.315  1.00 32.98           C  
ANISOU 3516  CG1 VAL B  78     4008   3533   4991     18   -215   -204       C  
ATOM   3517  CG2 VAL B  78      68.133 -13.518  16.056  1.00 33.79           C  
ANISOU 3517  CG2 VAL B  78     4101   3569   5170     54   -162   -266       C  
ATOM   3518  N   ASP B  79      67.499 -14.781  11.646  1.00 35.92           N  
ANISOU 3518  N   ASP B  79     4318   3936   5393    106   -316   -154       N  
ATOM   3519  CA  ASP B  79      67.655 -15.554  10.413  1.00 37.95           C  
ANISOU 3519  CA  ASP B  79     4576   4239   5603    110   -359   -132       C  
ATOM   3520  C   ASP B  79      69.095 -15.963  10.123  1.00 37.93           C  
ANISOU 3520  C   ASP B  79     4622   4249   5540     66   -342   -103       C  
ATOM   3521  O   ASP B  79      69.324 -16.958   9.428  1.00 33.49           O  
ANISOU 3521  O   ASP B  79     4057   3731   4937     54   -359   -101       O  
ATOM   3522  CB  ASP B  79      67.149 -14.735   9.217  1.00 39.05           C  
ANISOU 3522  CB  ASP B  79     4732   4369   5737    175   -417    -94       C  
ATOM   3523  CG  ASP B  79      65.675 -14.417   9.310  1.00 47.30           C  
ANISOU 3523  CG  ASP B  79     5714   5414   6845    234   -452   -131       C  
ATOM   3524  OD1 ASP B  79      64.893 -15.359   9.554  1.00 52.07           O  
ANISOU 3524  OD1 ASP B  79     6243   6058   7481    222   -456   -189       O  
ATOM   3525  OD2 ASP B  79      65.301 -13.223   9.161  1.00 41.64           O  
ANISOU 3525  OD2 ASP B  79     5018   4651   6151    292   -469   -106       O  
ATOM   3526  N   ILE B  80      70.065 -15.205  10.613  1.00 34.40           N  
ANISOU 3526  N   ILE B  80     4212   3764   5093     41   -308    -88       N  
ATOM   3527  CA  ILE B  80      71.441 -15.319  10.135  1.00 32.41           C  
ANISOU 3527  CA  ILE B  80     3996   3520   4799      5   -292    -62       C  
ATOM   3528  C   ILE B  80      72.319 -14.558  11.116  1.00 35.72           C  
ANISOU 3528  C   ILE B  80     4427   3899   5244    -30   -255    -80       C  
ATOM   3529  O   ILE B  80      71.834 -13.646  11.796  1.00 34.93           O  
ANISOU 3529  O   ILE B  80     4329   3753   5189    -16   -244    -95       O  
ATOM   3530  CB  ILE B  80      71.539 -14.760   8.698  1.00 34.13           C  
ANISOU 3530  CB  ILE B  80     4257   3725   4986     32   -310     -3       C  
ATOM   3531  CG1 ILE B  80      72.877 -15.113   8.025  1.00 33.77           C  
ANISOU 3531  CG1 ILE B  80     4241   3697   4894     -6   -283     21       C  
ATOM   3532  CG2 ILE B  80      71.276 -13.250   8.677  1.00 32.77           C  
ANISOU 3532  CG2 ILE B  80     4122   3479   4850     60   -299     27       C  
ATOM   3533  CD1 ILE B  80      72.834 -14.877   6.500  1.00 33.11           C  
ANISOU 3533  CD1 ILE B  80     4212   3612   4755     29   -296     80       C  
ATOM   3534  N   ALA B  81      73.606 -14.908  11.205  1.00 32.93           N  
ANISOU 3534  N   ALA B  81     4078   3565   4870    -71   -237    -89       N  
ATOM   3535  CA  ALA B  81      74.532 -14.233  12.109  1.00 33.76           C  
ANISOU 3535  CA  ALA B  81     4182   3642   5004   -105   -212   -124       C  
ATOM   3536  C   ALA B  81      75.569 -13.438  11.326  1.00 36.23           C  
ANISOU 3536  C   ALA B  81     4513   3920   5331   -140   -181    -98       C  
ATOM   3537  O   ALA B  81      75.964 -13.822  10.222  1.00 36.13           O  
ANISOU 3537  O   ALA B  81     4514   3928   5287   -145   -173    -59       O  
ATOM   3538  CB  ALA B  81      75.244 -15.231  13.031  1.00 33.42           C  
ANISOU 3538  CB  ALA B  81     4116   3649   4934   -120   -219   -173       C  
ATOM   3539  N   ALA B  82      76.022 -12.324  11.913  1.00 35.71           N  
ANISOU 3539  N   ALA B  82     4451   3798   5319   -169   -154   -126       N  
ATOM   3540  CA  ALA B  82      77.060 -11.503  11.298  1.00 33.00           C  
ANISOU 3540  CA  ALA B  82     4121   3407   5008   -217   -105   -112       C  
ATOM   3541  C   ALA B  82      78.444 -12.075  11.631  1.00 34.69           C  
ANISOU 3541  C   ALA B  82     4284   3670   5227   -265    -99   -168       C  
ATOM   3542  O   ALA B  82      78.901 -12.001  12.780  1.00 37.19           O  
ANISOU 3542  O   ALA B  82     4564   3998   5569   -282   -117   -242       O  
ATOM   3543  CB  ALA B  82      76.938 -10.057  11.777  1.00 37.10           C  
ANISOU 3543  CB  ALA B  82     4664   3836   5597   -232    -74   -128       C  
ATOM   3544  N   ASN B  83      79.105 -12.663  10.626  1.00 35.61           N  
ANISOU 3544  N   ASN B  83     4397   3819   5315   -280    -77   -137       N  
ATOM   3545  CA  ASN B  83      80.531 -13.033  10.695  1.00 36.48           C  
ANISOU 3545  CA  ASN B  83     4451   3966   5445   -327    -58   -188       C  
ATOM   3546  C   ASN B  83      80.845 -14.021  11.817  1.00 34.20           C  
ANISOU 3546  C   ASN B  83     4111   3749   5134   -306   -118   -258       C  
ATOM   3547  O   ASN B  83      81.900 -13.954  12.449  1.00 40.21           O  
ANISOU 3547  O   ASN B  83     4815   4531   5932   -335   -126   -332       O  
ATOM   3548  CB  ASN B  83      81.399 -11.778  10.804  1.00 42.67           C  
ANISOU 3548  CB  ASN B  83     5217   4681   6314   -394      1   -224       C  
ATOM   3549  CG  ASN B  83      81.163 -10.844   9.643  1.00 48.70           C  
ANISOU 3549  CG  ASN B  83     6052   5361   7090   -410     76   -144       C  
ATOM   3550  OD1 ASN B  83      80.222 -10.055   9.655  1.00 49.38           O  
ANISOU 3550  OD1 ASN B  83     6196   5383   7183   -382     76   -104       O  
ATOM   3551  ND2 ASN B  83      81.977 -10.968   8.604  1.00 50.20           N  
ANISOU 3551  ND2 ASN B  83     6247   5551   7276   -444    142   -114       N  
ATOM   3552  N   THR B  84      79.929 -14.954  12.059  1.00 33.48           N  
ANISOU 3552  N   THR B  84     4041   3696   4983   -253   -162   -237       N  
ATOM   3553  CA  THR B  84      80.183 -16.072  12.957  1.00 32.87           C  
ANISOU 3553  CA  THR B  84     3941   3681   4867   -222   -208   -283       C  
ATOM   3554  C   THR B  84      79.217 -17.178  12.571  1.00 37.50           C  
ANISOU 3554  C   THR B  84     4560   4293   5395   -180   -222   -236       C  
ATOM   3555  O   THR B  84      78.326 -16.983  11.740  1.00 38.67           O  
ANISOU 3555  O   THR B  84     4737   4419   5538   -174   -210   -183       O  
ATOM   3556  CB  THR B  84      80.014 -15.678  14.435  1.00 40.70           C  
ANISOU 3556  CB  THR B  84     4931   4664   5868   -207   -239   -343       C  
ATOM   3557  OG1 THR B  84      80.411 -16.768  15.279  1.00 42.49           O  
ANISOU 3557  OG1 THR B  84     5151   4949   6044   -167   -281   -383       O  
ATOM   3558  CG2 THR B  84      78.561 -15.316  14.742  1.00 38.24           C  
ANISOU 3558  CG2 THR B  84     4665   4312   5551   -182   -235   -312       C  
ATOM   3559  N   VAL B  85      79.396 -18.341  13.189  1.00 33.79           N  
ANISOU 3559  N   VAL B  85     4087   3869   4882   -148   -250   -261       N  
ATOM   3560  CA  VAL B  85      78.470 -19.466  13.046  1.00 31.78           C  
ANISOU 3560  CA  VAL B  85     3863   3630   4583   -116   -256   -232       C  
ATOM   3561  C   VAL B  85      77.980 -19.827  14.436  1.00 33.00           C  
ANISOU 3561  C   VAL B  85     4041   3783   4714    -83   -269   -261       C  
ATOM   3562  O   VAL B  85      78.786 -20.148  15.318  1.00 32.98           O  
ANISOU 3562  O   VAL B  85     4038   3804   4688    -61   -291   -302       O  
ATOM   3563  CB  VAL B  85      79.128 -20.693  12.396  1.00 31.70           C  
ANISOU 3563  CB  VAL B  85     3845   3662   4536   -105   -258   -226       C  
ATOM   3564  CG1 VAL B  85      78.197 -21.935  12.528  1.00 31.72           C  
ANISOU 3564  CG1 VAL B  85     3882   3671   4500    -75   -259   -212       C  
ATOM   3565  CG2 VAL B  85      79.501 -20.418  10.956  1.00 35.23           C  
ANISOU 3565  CG2 VAL B  85     4283   4112   4992   -133   -233   -194       C  
ATOM   3566  N   ILE B  86      76.670 -19.778  14.636  1.00 33.21           N  
ANISOU 3566  N   ILE B  86     4090   3782   4745    -74   -254   -243       N  
ATOM   3567  CA  ILE B  86      76.071 -20.259  15.872  1.00 30.13           C  
ANISOU 3567  CA  ILE B  86     3735   3384   4327    -45   -244   -262       C  
ATOM   3568  C   ILE B  86      75.774 -21.737  15.645  1.00 31.12           C  
ANISOU 3568  C   ILE B  86     3883   3524   4417    -28   -230   -244       C  
ATOM   3569  O   ILE B  86      74.899 -22.085  14.845  1.00 32.56           O  
ANISOU 3569  O   ILE B  86     4054   3698   4618    -42   -215   -222       O  
ATOM   3570  CB  ILE B  86      74.802 -19.474  16.241  1.00 31.82           C  
ANISOU 3570  CB  ILE B  86     3954   3558   4577    -46   -221   -261       C  
ATOM   3571  CG1 ILE B  86      75.104 -17.965  16.380  1.00 30.76           C  
ANISOU 3571  CG1 ILE B  86     3804   3397   4486    -63   -231   -278       C  
ATOM   3572  CG2 ILE B  86      74.225 -20.005  17.554  1.00 36.38           C  
ANISOU 3572  CG2 ILE B  86     4576   4126   5122    -18   -192   -282       C  
ATOM   3573  CD1 ILE B  86      76.229 -17.662  17.335  1.00 36.78           C  
ANISOU 3573  CD1 ILE B  86     4572   4173   5230    -60   -253   -330       C  
ATOM   3574  N   TRP B  87      76.538 -22.610  16.299  1.00 31.02           N  
ANISOU 3574  N   TRP B  87     3901   3531   4353      4   -238   -259       N  
ATOM   3575  CA  TRP B  87      76.328 -24.043  16.112  1.00 31.38           C  
ANISOU 3575  CA  TRP B  87     3979   3577   4367     21   -216   -242       C  
ATOM   3576  C   TRP B  87      75.210 -24.518  17.026  1.00 31.19           C  
ANISOU 3576  C   TRP B  87     4008   3515   4330     33   -165   -239       C  
ATOM   3577  O   TRP B  87      75.206 -24.216  18.223  1.00 34.54           O  
ANISOU 3577  O   TRP B  87     4474   3928   4724     61   -156   -254       O  
ATOM   3578  CB  TRP B  87      77.613 -24.824  16.396  1.00 29.78           C  
ANISOU 3578  CB  TRP B  87     3795   3404   4114     63   -244   -255       C  
ATOM   3579  CG  TRP B  87      77.533 -26.282  15.952  1.00 31.29           C  
ANISOU 3579  CG  TRP B  87     4019   3588   4281     79   -220   -235       C  
ATOM   3580  CD1 TRP B  87      77.342 -27.368  16.752  1.00 33.29           C  
ANISOU 3580  CD1 TRP B  87     4348   3814   4486    121   -190   -227       C  
ATOM   3581  CD2 TRP B  87      77.633 -26.783  14.608  1.00 34.74           C  
ANISOU 3581  CD2 TRP B  87     4424   4038   4737     53   -219   -223       C  
ATOM   3582  NE1 TRP B  87      77.303 -28.516  15.994  1.00 33.31           N  
ANISOU 3582  NE1 TRP B  87     4363   3804   4488    118   -167   -213       N  
ATOM   3583  CE2 TRP B  87      77.491 -28.191  14.676  1.00 31.42           C  
ANISOU 3583  CE2 TRP B  87     4055   3594   4288     78   -189   -215       C  
ATOM   3584  CE3 TRP B  87      77.836 -26.179  13.357  1.00 33.73           C  
ANISOU 3584  CE3 TRP B  87     4240   3934   4643     15   -234   -218       C  
ATOM   3585  CZ2 TRP B  87      77.558 -29.009  13.542  1.00 33.12           C  
ANISOU 3585  CZ2 TRP B  87     4259   3814   4510     64   -181   -212       C  
ATOM   3586  CZ3 TRP B  87      77.914 -26.980  12.235  1.00 30.77           C  
ANISOU 3586  CZ3 TRP B  87     3860   3569   4263      7   -227   -210       C  
ATOM   3587  CH2 TRP B  87      77.759 -28.390  12.331  1.00 31.47           C  
ANISOU 3587  CH2 TRP B  87     3992   3638   4327     29   -203   -212       C  
ATOM   3588  N   ASP B  88      74.270 -25.277  16.466  1.00 32.93           N  
ANISOU 3588  N   ASP B  88     4225   3713   4574     10   -126   -225       N  
ATOM   3589  CA  ASP B  88      73.120 -25.779  17.211  1.00 36.20           C  
ANISOU 3589  CA  ASP B  88     4677   4083   4996      7    -56   -226       C  
ATOM   3590  C   ASP B  88      73.465 -27.180  17.700  1.00 36.46           C  
ANISOU 3590  C   ASP B  88     4787   4094   4973     38    -18   -215       C  
ATOM   3591  O   ASP B  88      73.384 -28.146  16.946  1.00 34.11           O  
ANISOU 3591  O   ASP B  88     4486   3787   4688     22     -4   -209       O  
ATOM   3592  CB  ASP B  88      71.889 -25.763  16.314  1.00 32.59           C  
ANISOU 3592  CB  ASP B  88     4158   3614   4611    -38    -37   -233       C  
ATOM   3593  CG  ASP B  88      70.618 -26.195  17.034  1.00 39.60           C  
ANISOU 3593  CG  ASP B  88     5061   4455   5531    -54     47   -248       C  
ATOM   3594  OD1 ASP B  88      70.692 -26.875  18.085  1.00 43.22           O  
ANISOU 3594  OD1 ASP B  88     5599   4879   5944    -33    108   -240       O  
ATOM   3595  OD2 ASP B  88      69.540 -25.852  16.519  1.00 40.35           O  
ANISOU 3595  OD2 ASP B  88     5088   4546   5698    -84     54   -268       O  
ATOM   3596  N   TYR B  89      73.849 -27.302  18.969  1.00 34.73           N  
ANISOU 3596  N   TYR B  89     4648   3862   4688     88     -2   -212       N  
ATOM   3597  CA  TYR B  89      74.296 -28.598  19.463  1.00 37.37           C  
ANISOU 3597  CA  TYR B  89     5074   4170   4956    135     28   -192       C  
ATOM   3598  C   TYR B  89      73.140 -29.569  19.684  1.00 44.22           C  
ANISOU 3598  C   TYR B  89     5992   4966   5844    108    137   -179       C  
ATOM   3599  O   TYR B  89      73.378 -30.770  19.787  1.00 42.39           O  
ANISOU 3599  O   TYR B  89     5833   4696   5576    134    176   -159       O  
ATOM   3600  CB  TYR B  89      75.094 -28.429  20.760  1.00 39.33           C  
ANISOU 3600  CB  TYR B  89     5404   4429   5111    214      1   -195       C  
ATOM   3601  CG  TYR B  89      76.511 -27.908  20.548  1.00 34.41           C  
ANISOU 3601  CG  TYR B  89     4733   3873   4466    249   -106   -219       C  
ATOM   3602  CD1 TYR B  89      76.761 -26.547  20.399  1.00 33.48           C  
ANISOU 3602  CD1 TYR B  89     4538   3795   4390    220   -159   -252       C  
ATOM   3603  CD2 TYR B  89      77.594 -28.785  20.492  1.00 35.81           C  
ANISOU 3603  CD2 TYR B  89     4942   4071   4595    310   -146   -216       C  
ATOM   3604  CE1 TYR B  89      78.069 -26.076  20.215  1.00 31.19           C  
ANISOU 3604  CE1 TYR B  89     4196   3561   4096    241   -244   -285       C  
ATOM   3605  CE2 TYR B  89      78.889 -28.328  20.299  1.00 37.67           C  
ANISOU 3605  CE2 TYR B  89     5117   4371   4826    339   -238   -251       C  
ATOM   3606  CZ  TYR B  89      79.124 -26.979  20.165  1.00 35.99           C  
ANISOU 3606  CZ  TYR B  89     4821   4195   4660    299   -283   -287       C  
ATOM   3607  OH  TYR B  89      80.417 -26.529  19.981  1.00 38.34           O  
ANISOU 3607  OH  TYR B  89     5048   4551   4967    317   -362   -332       O  
ATOM   3608  N   LYS B  90      71.902 -29.086  19.772  1.00 38.61           N  
ANISOU 3608  N   LYS B  90     5242   4230   5196     57    194   -194       N  
ATOM   3609  CA  LYS B  90      70.771 -30.007  19.881  1.00 42.02           C  
ANISOU 3609  CA  LYS B  90     5699   4594   5672     16    306   -195       C  
ATOM   3610  C   LYS B  90      70.520 -30.717  18.558  1.00 43.41           C  
ANISOU 3610  C   LYS B  90     5807   4769   5916    -35    296   -211       C  
ATOM   3611  O   LYS B  90      70.125 -31.884  18.536  1.00 45.47           O  
ANISOU 3611  O   LYS B  90     6111   4971   6194    -57    375   -211       O  
ATOM   3612  CB  LYS B  90      69.509 -29.259  20.317  1.00 44.33           C  
ANISOU 3612  CB  LYS B  90     5948   4867   6027    -24    369   -220       C  
ATOM   3613  CG  LYS B  90      69.645 -28.453  21.601  1.00 57.25           C  
ANISOU 3613  CG  LYS B  90     7650   6505   7600     22    383   -214       C  
ATOM   3614  CD  LYS B  90      69.301 -29.240  22.847  1.00 61.83           C  
ANISOU 3614  CD  LYS B  90     8363   7014   8116     48    506   -191       C  
ATOM   3615  CE  LYS B  90      69.206 -28.311  24.062  1.00 64.69           C  
ANISOU 3615  CE  LYS B  90     8779   7380   8419     89    525   -198       C  
ATOM   3616  NZ  LYS B  90      70.417 -27.441  24.214  1.00 54.26           N  
ANISOU 3616  NZ  LYS B  90     7458   6128   7030    147    393   -204       N  
ATOM   3617  N   ARG B  91      70.724 -30.020  17.448  1.00 32.88           N  
ANISOU 3617  N   ARG B  91     4376   3497   4620    -54    205   -228       N  
ATOM   3618  CA  ARG B  91      70.538 -30.583  16.117  1.00 33.96           C  
ANISOU 3618  CA  ARG B  91     4451   3646   4807    -93    179   -249       C  
ATOM   3619  C   ARG B  91      71.846 -31.036  15.481  1.00 39.57           C  
ANISOU 3619  C   ARG B  91     5184   4389   5462    -58    116   -232       C  
ATOM   3620  O   ARG B  91      71.811 -31.636  14.404  1.00 39.68           O  
ANISOU 3620  O   ARG B  91     5164   4410   5502    -84     99   -250       O  
ATOM   3621  CB  ARG B  91      69.855 -29.550  15.195  1.00 35.53           C  
ANISOU 3621  CB  ARG B  91     4538   3890   5072   -126    120   -277       C  
ATOM   3622  CG  ARG B  91      68.376 -29.245  15.511  1.00 39.44           C  
ANISOU 3622  CG  ARG B  91     4978   4358   5651   -166    177   -313       C  
ATOM   3623  CD  ARG B  91      67.909 -27.978  14.755  1.00 40.20           C  
ANISOU 3623  CD  ARG B  91     4977   4504   5792   -168     99   -330       C  
ATOM   3624  NE  ARG B  91      68.195 -28.102  13.330  1.00 46.72           N  
ANISOU 3624  NE  ARG B  91     5760   5374   6618   -172     19   -338       N  
ATOM   3625  CZ  ARG B  91      69.068 -27.367  12.654  1.00 39.28           C  
ANISOU 3625  CZ  ARG B  91     4818   4477   5631   -144    -59   -308       C  
ATOM   3626  NH1 ARG B  91      69.244 -27.619  11.364  1.00 40.86           N  
ANISOU 3626  NH1 ARG B  91     4992   4712   5822   -147   -115   -316       N  
ATOM   3627  NH2 ARG B  91      69.739 -26.366  13.243  1.00 36.84           N  
ANISOU 3627  NH2 ARG B  91     4533   4176   5288   -116    -76   -276       N  
ATOM   3628  N   ASP B  92      72.991 -30.755  16.110  1.00 35.80           N  
ANISOU 3628  N   ASP B  92     4755   3935   4913      0     79   -206       N  
ATOM   3629  CA  ASP B  92      74.294 -31.077  15.531  1.00 33.49           C  
ANISOU 3629  CA  ASP B  92     4465   3680   4578     37     19   -199       C  
ATOM   3630  C   ASP B  92      74.420 -30.471  14.132  1.00 33.65           C  
ANISOU 3630  C   ASP B  92     4396   3755   4636      1    -41   -213       C  
ATOM   3631  O   ASP B  92      74.777 -31.151  13.163  1.00 35.91           O  
ANISOU 3631  O   ASP B  92     4671   4052   4922     -4    -54   -220       O  
ATOM   3632  CB  ASP B  92      74.494 -32.605  15.507  1.00 43.39           C  
ANISOU 3632  CB  ASP B  92     5791   4885   5810     57     67   -192       C  
ATOM   3633  CG  ASP B  92      75.948 -33.018  15.477  1.00 65.99           C  
ANISOU 3633  CG  ASP B  92     8685   7777   8612    126     17   -181       C  
ATOM   3634  OD1 ASP B  92      76.837 -32.137  15.490  1.00 70.26           O  
ANISOU 3634  OD1 ASP B  92     9183   8379   9133    151    -52   -185       O  
ATOM   3635  OD2 ASP B  92      76.201 -34.243  15.443  1.00 76.58           O  
ANISOU 3635  OD2 ASP B  92    10090   9075   9933    154     52   -174       O  
ATOM   3636  N   ALA B  93      74.077 -29.184  14.017  1.00 29.41           N  
ANISOU 3636  N   ALA B  93     3803   3244   4127    -19    -73   -216       N  
ATOM   3637  CA  ALA B  93      74.008 -28.542  12.714  1.00 29.14           C  
ANISOU 3637  CA  ALA B  93     3702   3250   4122    -47   -120   -220       C  
ATOM   3638  C   ALA B  93      74.065 -27.034  12.913  1.00 31.45           C  
ANISOU 3638  C   ALA B  93     3960   3561   4427    -48   -152   -212       C  
ATOM   3639  O   ALA B  93      73.837 -26.549  14.025  1.00 32.32           O  
ANISOU 3639  O   ALA B  93     4090   3653   4538    -37   -134   -213       O  
ATOM   3640  CB  ALA B  93      72.727 -28.948  11.965  1.00 31.26           C  
ANISOU 3640  CB  ALA B  93     3934   3503   4440    -86   -105   -245       C  
ATOM   3641  N   PRO B  94      74.363 -26.268  11.861  1.00 35.82           N  
ANISOU 3641  N   PRO B  94     4475   4147   4989    -59   -193   -203       N  
ATOM   3642  CA  PRO B  94      74.340 -24.802  11.997  1.00 36.20           C  
ANISOU 3642  CA  PRO B  94     4499   4197   5058    -63   -213   -193       C  
ATOM   3643  C   PRO B  94      72.953 -24.337  12.403  1.00 32.55           C  
ANISOU 3643  C   PRO B  94     4020   3708   4641    -70   -198   -203       C  
ATOM   3644  O   PRO B  94      71.946 -24.876  11.943  1.00 30.82           O  
ANISOU 3644  O   PRO B  94     3780   3483   4448    -82   -191   -217       O  
ATOM   3645  CB  PRO B  94      74.703 -24.299  10.592  1.00 35.23           C  
ANISOU 3645  CB  PRO B  94     4354   4100   4931    -72   -243   -175       C  
ATOM   3646  CG  PRO B  94      75.422 -25.450   9.942  1.00 38.64           C  
ANISOU 3646  CG  PRO B  94     4799   4556   5327    -68   -241   -179       C  
ATOM   3647  CD  PRO B  94      74.736 -26.685  10.499  1.00 33.77           C  
ANISOU 3647  CD  PRO B  94     4202   3915   4713    -66   -214   -200       C  
ATOM   3648  N   ALA B  95      72.896 -23.325  13.271  1.00 30.27           N  
ANISOU 3648  N   ALA B  95     3734   3403   4367    -64   -194   -204       N  
ATOM   3649  CA  ALA B  95      71.575 -22.804  13.627  1.00 34.86           C  
ANISOU 3649  CA  ALA B  95     4290   3957   4996    -66   -176   -217       C  
ATOM   3650  C   ALA B  95      70.899 -22.117  12.448  1.00 37.57           C  
ANISOU 3650  C   ALA B  95     4590   4310   5375    -66   -215   -208       C  
ATOM   3651  O   ALA B  95      69.662 -22.056  12.407  1.00 35.16           O  
ANISOU 3651  O   ALA B  95     4247   3995   5118    -64   -210   -229       O  
ATOM   3652  CB  ALA B  95      71.674 -21.840  14.812  1.00 32.57           C  
ANISOU 3652  CB  ALA B  95     4019   3645   4710    -55   -160   -226       C  
ATOM   3653  N   HIS B  96      71.682 -21.629  11.481  1.00 34.66           N  
ANISOU 3653  N   HIS B  96     4226   3959   4982    -63   -251   -180       N  
ATOM   3654  CA  HIS B  96      71.193 -20.824  10.367  1.00 36.38           C  
ANISOU 3654  CA  HIS B  96     4429   4181   5213    -47   -290   -160       C  
ATOM   3655  C   HIS B  96      71.738 -21.371   9.054  1.00 34.22           C  
ANISOU 3655  C   HIS B  96     4169   3941   4893    -47   -315   -142       C  
ATOM   3656  O   HIS B  96      72.890 -21.791   8.989  1.00 42.11           O  
ANISOU 3656  O   HIS B  96     5190   4954   5856    -62   -299   -133       O  
ATOM   3657  CB  HIS B  96      71.606 -19.358  10.583  1.00 31.94           C  
ANISOU 3657  CB  HIS B  96     3882   3587   4665    -40   -289   -135       C  
ATOM   3658  CG  HIS B  96      71.189 -18.843  11.926  1.00 31.68           C  
ANISOU 3658  CG  HIS B  96     3844   3523   4670    -39   -262   -161       C  
ATOM   3659  ND1 HIS B  96      72.091 -18.538  12.922  1.00 35.16           N  
ANISOU 3659  ND1 HIS B  96     4307   3951   5101    -53   -240   -173       N  
ATOM   3660  CD2 HIS B  96      69.956 -18.686  12.468  1.00 33.08           C  
ANISOU 3660  CD2 HIS B  96     3994   3684   4893    -24   -251   -186       C  
ATOM   3661  CE1 HIS B  96      71.432 -18.162  14.006  1.00 36.05           C  
ANISOU 3661  CE1 HIS B  96     4419   4038   5242    -43   -217   -200       C  
ATOM   3662  NE2 HIS B  96      70.135 -18.250  13.759  1.00 32.74           N  
ANISOU 3662  NE2 HIS B  96     3968   3614   4858    -28   -216   -206       N  
ATOM   3663  N  AILE B  97      70.910 -21.337   8.008  0.44 43.46           N  
ANISOU 3663  N  AILE B  97     5324   5128   6061    -25   -357   -142       N  
ATOM   3664  N  BILE B  97      70.911 -21.331   8.007  0.56 43.13           N  
ANISOU 3664  N  BILE B  97     5283   5086   6019    -24   -357   -141       N  
ATOM   3665  CA AILE B  97      71.265 -22.011   6.761  0.44 51.03           C  
ANISOU 3665  CA AILE B  97     6301   6122   6965    -20   -382   -136       C  
ATOM   3666  CA BILE B  97      71.266 -22.003   6.760  0.56 51.23           C  
ANISOU 3666  CA BILE B  97     6327   6148   6991    -20   -382   -135       C  
ATOM   3667  C  AILE B  97      72.324 -21.241   5.976  0.44 46.94           C  
ANISOU 3667  C  AILE B  97     5833   5604   6399    -13   -376    -83       C  
ATOM   3668  C  BILE B  97      72.357 -21.243   6.014  0.56 47.23           C  
ANISOU 3668  C  BILE B  97     5870   5640   6436    -14   -374    -83       C  
ATOM   3669  O  AILE B  97      73.153 -21.850   5.288  0.44 41.80           O  
ANISOU 3669  O  AILE B  97     5206   4978   5699    -22   -365    -76       O  
ATOM   3670  O  BILE B  97      73.235 -21.853   5.389  0.56 41.63           O  
ANISOU 3670  O  BILE B  97     5184   4955   5680    -26   -360    -76       O  
ATOM   3671  CB AILE B  97      70.004 -22.249   5.910  0.44 57.57           C  
ANISOU 3671  CB AILE B  97     7098   6976   7801      9   -440   -165       C  
ATOM   3672  CB BILE B  97      70.013 -22.200   5.885  0.56 57.65           C  
ANISOU 3672  CB BILE B  97     7109   6986   7810     10   -441   -163       C  
ATOM   3673  CG1AILE B  97      70.338 -23.100   4.684  0.44 59.39           C  
ANISOU 3673  CG1AILE B  97     7351   7246   7967     14   -467   -174       C  
ATOM   3674  CG1BILE B  97      68.947 -21.155   6.231  0.56 57.89           C  
ANISOU 3674  CG1BILE B  97     7107   6994   7894     43   -466   -166       C  
ATOM   3675  CG2AILE B  97      69.371 -20.929   5.493  0.44 57.94           C  
ANISOU 3675  CG2AILE B  97     7148   7011   7856     58   -482   -137       C  
ATOM   3676  CG2BILE B  97      69.468 -23.621   6.034  0.56 60.28           C  
ANISOU 3676  CG2BILE B  97     7402   7334   8166    -16   -435   -226       C  
ATOM   3677  CD1AILE B  97      70.951 -24.448   5.026  0.44 63.29           C  
ANISOU 3677  CD1AILE B  97     7846   7745   8455    -26   -425   -202       C  
ATOM   3678  CD1BILE B  97      68.963 -19.933   5.331  0.56 56.97           C  
ANISOU 3678  CD1BILE B  97     7033   6871   7742     96   -506   -114       C  
ATOM   3679  N   SER B  98      72.319 -19.913   6.049  1.00 38.43           N  
ANISOU 3679  N   SER B  98     4774   4492   5337      1   -372    -47       N  
ATOM   3680  CA  SER B  98      73.273 -19.086   5.318  1.00 35.46           C  
ANISOU 3680  CA  SER B  98     4450   4098   4925      0   -347      5       C  
ATOM   3681  C   SER B  98      74.225 -18.382   6.272  1.00 33.34           C  
ANISOU 3681  C   SER B  98     4179   3792   4697    -38   -296      7       C  
ATOM   3682  O   SER B  98      74.039 -18.373   7.492  1.00 34.63           O  
ANISOU 3682  O   SER B  98     4310   3943   4906    -51   -291    -26       O  
ATOM   3683  CB  SER B  98      72.549 -18.054   4.448  1.00 39.66           C  
ANISOU 3683  CB  SER B  98     5023   4607   5438     53   -380     48       C  
ATOM   3684  OG  SER B  98      71.855 -18.729   3.419  1.00 41.96           O  
ANISOU 3684  OG  SER B  98     5320   4945   5678     94   -438     38       O  
ATOM   3685  N   THR B  99      75.277 -17.798   5.701  1.00 31.45           N  
ANISOU 3685  N   THR B  99     3975   3535   4441    -58   -253     41       N  
ATOM   3686  CA  THR B  99      76.253 -17.089   6.509  1.00 29.46           C  
ANISOU 3686  CA  THR B  99     3709   3248   4238   -101   -206     29       C  
ATOM   3687  C   THR B  99      76.602 -15.743   5.881  1.00 33.10           C  
ANISOU 3687  C   THR B  99     4221   3647   4708   -109   -161     79       C  
ATOM   3688  O   THR B  99      76.235 -15.428   4.746  1.00 36.42           O  
ANISOU 3688  O   THR B  99     4702   4056   5082    -75   -161    133       O  
ATOM   3689  CB  THR B  99      77.537 -17.912   6.703  1.00 35.55           C  
ANISOU 3689  CB  THR B  99     4448   4057   5002   -137   -179     -4       C  
ATOM   3690  OG1 THR B  99      78.045 -18.298   5.423  1.00 36.23           O  
ANISOU 3690  OG1 THR B  99     4564   4166   5036   -137   -155     26       O  
ATOM   3691  CG2 THR B  99      77.260 -19.165   7.546  1.00 35.38           C  
ANISOU 3691  CG2 THR B  99     4391   4078   4975   -126   -214    -50       C  
ATOM   3692  N   ILE B 100      77.349 -14.957   6.654  1.00 32.90           N  
ANISOU 3692  N   ILE B 100     4176   3580   4744   -154   -119     57       N  
ATOM   3693  CA  ILE B 100      77.850 -13.655   6.246  1.00 31.16           C  
ANISOU 3693  CA  ILE B 100     4000   3285   4555   -180    -55     93       C  
ATOM   3694  C   ILE B 100      79.327 -13.642   6.605  1.00 35.93           C  
ANISOU 3694  C   ILE B 100     4556   3892   5205   -250      1     47       C  
ATOM   3695  O   ILE B 100      79.673 -13.673   7.791  1.00 37.36           O  
ANISOU 3695  O   ILE B 100     4677   4084   5436   -275    -17    -20       O  
ATOM   3696  CB  ILE B 100      77.118 -12.507   6.943  1.00 35.20           C  
ANISOU 3696  CB  ILE B 100     4528   3727   5121   -165    -63     94       C  
ATOM   3697  CG1 ILE B 100      75.635 -12.516   6.561  1.00 37.51           C  
ANISOU 3697  CG1 ILE B 100     4851   4022   5377    -87   -124    130       C  
ATOM   3698  CG2 ILE B 100      77.768 -11.165   6.576  1.00 35.59           C  
ANISOU 3698  CG2 ILE B 100     4627   3682   5213   -203     19    126       C  
ATOM   3699  CD1 ILE B 100      74.780 -11.571   7.406  1.00 38.69           C  
ANISOU 3699  CD1 ILE B 100     5000   4115   5585    -62   -139    117       C  
ATOM   3700  N   GLY B 101      80.192 -13.630   5.592  1.00 35.31           N  
ANISOU 3700  N   GLY B 101     4501   3808   5107   -279     68     77       N  
ATOM   3701  CA  GLY B 101      81.630 -13.553   5.816  1.00 36.64           C  
ANISOU 3701  CA  GLY B 101     4610   3978   5334   -349    131     25       C  
ATOM   3702  C   GLY B 101      82.264 -14.751   6.506  1.00 43.43           C  
ANISOU 3702  C   GLY B 101     5382   4923   6196   -352     86    -48       C  
ATOM   3703  O   GLY B 101      83.272 -14.585   7.201  1.00 43.65           O  
ANISOU 3703  O   GLY B 101     5336   4958   6292   -398    103   -119       O  
ATOM   3704  N   VAL B 102      81.727 -15.961   6.318  1.00 35.16           N  
ANISOU 3704  N   VAL B 102     4340   3939   5078   -302     30    -39       N  
ATOM   3705  CA  VAL B 102      82.224 -17.161   6.990  1.00 35.56           C  
ANISOU 3705  CA  VAL B 102     4327   4061   5124   -290    -14   -100       C  
ATOM   3706  C   VAL B 102      82.786 -18.180   6.000  1.00 40.55           C  
ANISOU 3706  C   VAL B 102     4959   4742   5705   -281     10    -90       C  
ATOM   3707  O   VAL B 102      83.883 -18.710   6.195  1.00 41.91           O  
ANISOU 3707  O   VAL B 102     5069   4952   5901   -296     24   -141       O  
ATOM   3708  CB  VAL B 102      81.129 -17.813   7.865  1.00 39.72           C  
ANISOU 3708  CB  VAL B 102     4859   4609   5622   -241    -92   -111       C  
ATOM   3709  CG1 VAL B 102      81.657 -19.111   8.478  1.00 40.37           C  
ANISOU 3709  CG1 VAL B 102     4899   4753   5686   -219   -128   -160       C  
ATOM   3710  CG2 VAL B 102      80.675 -16.854   8.960  1.00 39.96           C  
ANISOU 3710  CG2 VAL B 102     4885   4597   5702   -247   -111   -133       C  
ATOM   3711  N   CYS B 103      82.031 -18.493   4.952  1.00 38.78           N  
ANISOU 3711  N   CYS B 103     4803   4521   5411   -250      8    -32       N  
ATOM   3712  CA  CYS B 103      82.285 -19.677   4.140  1.00 37.67           C  
ANISOU 3712  CA  CYS B 103     4671   4433   5210   -228     11    -32       C  
ATOM   3713  C   CYS B 103      81.772 -19.426   2.730  1.00 38.73           C  
ANISOU 3713  C   CYS B 103     4892   4552   5272   -209     38     34       C  
ATOM   3714  O   CYS B 103      80.614 -19.034   2.553  1.00 39.89           O  
ANISOU 3714  O   CYS B 103     5089   4678   5391   -176     -5     71       O  
ATOM   3715  CB  CYS B 103      81.610 -20.906   4.754  1.00 42.02           C  
ANISOU 3715  CB  CYS B 103     5207   5024   5736   -186    -64    -62       C  
ATOM   3716  SG  CYS B 103      81.438 -22.349   3.640  1.00 44.94           S  
ANISOU 3716  SG  CYS B 103     5611   5442   6024   -152    -73    -58       S  
ATOM   3717  N   SER B 104      82.634 -19.645   1.731  1.00 35.34           N  
ANISOU 3717  N   SER B 104     4480   4136   4809   -222    108     45       N  
ATOM   3718  CA  SER B 104      82.285 -19.276   0.362  1.00 38.78           C  
ANISOU 3718  CA  SER B 104     5017   4554   5162   -200    145    112       C  
ATOM   3719  C   SER B 104      81.131 -20.096  -0.209  1.00 41.23           C  
ANISOU 3719  C   SER B 104     5376   4904   5386   -137     62    122       C  
ATOM   3720  O   SER B 104      80.498 -19.646  -1.170  1.00 39.20           O  
ANISOU 3720  O   SER B 104     5208   4632   5054    -98     56    176       O  
ATOM   3721  CB  SER B 104      83.509 -19.393  -0.552  1.00 48.52           C  
ANISOU 3721  CB  SER B 104     6263   5796   6377   -230    253    116       C  
ATOM   3722  OG  SER B 104      83.901 -20.748  -0.706  1.00 60.04           O  
ANISOU 3722  OG  SER B 104     7684   7321   7808   -213    235     68       O  
ATOM   3723  N   MET B 105      80.833 -21.279   0.340  1.00 37.59           N  
ANISOU 3723  N   MET B 105     4862   4489   4931   -122     -3     68       N  
ATOM   3724  CA  MET B 105      79.682 -22.021  -0.173  1.00 37.27           C  
ANISOU 3724  CA  MET B 105     4856   4479   4826    -73    -79     64       C  
ATOM   3725  C   MET B 105      78.360 -21.537   0.415  1.00 38.65           C  
ANISOU 3725  C   MET B 105     5025   4633   5028    -50   -154     70       C  
ATOM   3726  O   MET B 105      77.321 -21.695  -0.226  1.00 38.57           O  
ANISOU 3726  O   MET B 105     5049   4638   4966     -5   -214     75       O  
ATOM   3727  CB  MET B 105      79.825 -23.525   0.095  1.00 34.17           C  
ANISOU 3727  CB  MET B 105     4419   4131   4434    -70   -106      3       C  
ATOM   3728  CG  MET B 105      80.509 -24.304  -1.040  1.00 41.53           C  
ANISOU 3728  CG  MET B 105     5386   5098   5295    -60    -65     -7       C  
ATOM   3729  SD  MET B 105      79.660 -24.203  -2.631  1.00 42.86           S  
ANISOU 3729  SD  MET B 105     5659   5285   5342     -9    -95     26       S  
ATOM   3730  CE  MET B 105      77.984 -24.661  -2.165  1.00 47.11           C  
ANISOU 3730  CE  MET B 105     6170   5833   5898     20   -217    -12       C  
ATOM   3731  N   THR B 106      78.363 -20.985   1.631  1.00 34.39           N  
ANISOU 3731  N   THR B 106     4436   4061   4569    -75   -154     60       N  
ATOM   3732  CA  THR B 106      77.120 -20.603   2.293  1.00 34.54           C  
ANISOU 3732  CA  THR B 106     4441   4062   4622    -53   -214     56       C  
ATOM   3733  C   THR B 106      76.932 -19.098   2.429  1.00 37.65           C  
ANISOU 3733  C   THR B 106     4863   4397   5045    -51   -196    101       C  
ATOM   3734  O   THR B 106      75.820 -18.661   2.755  1.00 33.75           O  
ANISOU 3734  O   THR B 106     4366   3886   4573    -20   -246    104       O  
ATOM   3735  CB  THR B 106      77.035 -21.229   3.690  1.00 33.73           C  
ANISOU 3735  CB  THR B 106     4270   3964   4581    -73   -232      4       C  
ATOM   3736  OG1 THR B 106      78.168 -20.823   4.457  1.00 33.46           O  
ANISOU 3736  OG1 THR B 106     4207   3914   4592   -110   -186     -6       O  
ATOM   3737  CG2 THR B 106      76.994 -22.780   3.585  1.00 36.56           C  
ANISOU 3737  CG2 THR B 106     4612   4366   4914    -67   -251    -39       C  
ATOM   3738  N   ASP B 107      77.972 -18.300   2.198  1.00 34.40           N  
ANISOU 3738  N   ASP B 107     4476   3949   4644    -84   -121    132       N  
ATOM   3739  CA  ASP B 107      77.846 -16.855   2.344  1.00 37.11           C  
ANISOU 3739  CA  ASP B 107     4856   4222   5024    -88    -91    173       C  
ATOM   3740  C   ASP B 107      76.824 -16.300   1.369  1.00 36.95           C  
ANISOU 3740  C   ASP B 107     4918   4181   4939    -20   -126    232       C  
ATOM   3741  O   ASP B 107      76.846 -16.615   0.179  1.00 35.87           O  
ANISOU 3741  O   ASP B 107     4846   4070   4715     13   -124    264       O  
ATOM   3742  CB  ASP B 107      79.185 -16.166   2.090  1.00 36.98           C  
ANISOU 3742  CB  ASP B 107     4855   4163   5033   -144     14    192       C  
ATOM   3743  CG  ASP B 107      80.088 -16.149   3.306  1.00 40.47           C  
ANISOU 3743  CG  ASP B 107     5207   4604   5566   -206     38    128       C  
ATOM   3744  OD1 ASP B 107      79.704 -16.681   4.374  1.00 40.80           O  
ANISOU 3744  OD1 ASP B 107     5189   4674   5637   -198    -25     78       O  
ATOM   3745  OD2 ASP B 107      81.203 -15.596   3.172  1.00 44.29           O  
ANISOU 3745  OD2 ASP B 107     5682   5056   6091   -260    122    125       O  
ATOM   3746  N   ILE B 108      75.948 -15.430   1.861  1.00 33.56           N  
ANISOU 3746  N   ILE B 108     4494   3708   4550      9   -160    245       N  
ATOM   3747  CA  ILE B 108      75.166 -14.595   0.956  1.00 35.59           C  
ANISOU 3747  CA  ILE B 108     4841   3928   4752     83   -184    310       C  
ATOM   3748  C   ILE B 108      75.774 -13.213   0.802  1.00 39.11           C  
ANISOU 3748  C   ILE B 108     5362   4277   5221     64    -94    372       C  
ATOM   3749  O   ILE B 108      75.319 -12.442  -0.058  1.00 38.41           O  
ANISOU 3749  O   ILE B 108     5376   4143   5075    130    -94    442       O  
ATOM   3750  CB  ILE B 108      73.705 -14.468   1.424  1.00 38.10           C  
ANISOU 3750  CB  ILE B 108     5123   4254   5099    144   -280    287       C  
ATOM   3751  CG1 ILE B 108      73.640 -13.783   2.784  1.00 44.73           C  
ANISOU 3751  CG1 ILE B 108     5909   5042   6043    108   -259    260       C  
ATOM   3752  CG2 ILE B 108      73.052 -15.851   1.483  1.00 41.68           C  
ANISOU 3752  CG2 ILE B 108     5504   4794   5538    155   -356    222       C  
ATOM   3753  CD1 ILE B 108      72.234 -13.522   3.234  1.00 40.33           C  
ANISOU 3753  CD1 ILE B 108     5317   4484   5522    169   -334    238       C  
ATOM   3754  N   ALA B 109      76.794 -12.889   1.594  1.00 34.29           N  
ANISOU 3754  N   ALA B 109     4706   3631   4692    -21    -17    344       N  
ATOM   3755  CA  ALA B 109      77.437 -11.584   1.647  1.00 36.24           C  
ANISOU 3755  CA  ALA B 109     5004   3776   4991    -61     80    382       C  
ATOM   3756  C   ALA B 109      78.715 -11.738   2.455  1.00 40.62           C  
ANISOU 3756  C   ALA B 109     5471   4333   5629   -162    145    317       C  
ATOM   3757  O   ALA B 109      78.878 -12.704   3.209  1.00 37.50           O  
ANISOU 3757  O   ALA B 109     4982   4012   5255   -183     97    246       O  
ATOM   3758  CB  ALA B 109      76.525 -10.529   2.287  1.00 38.45           C  
ANISOU 3758  CB  ALA B 109     5299   3985   5325    -24     48    392       C  
ATOM   3759  N   LYS B 110      79.622 -10.779   2.284  1.00 40.99           N  
ANISOU 3759  N   LYS B 110     5552   4297   5724   -222    256    337       N  
ATOM   3760  CA  LYS B 110      80.806 -10.711   3.129  1.00 37.12           C  
ANISOU 3760  CA  LYS B 110     4966   3803   5335   -318    312    260       C  
ATOM   3761  C   LYS B 110      80.594  -9.836   4.357  1.00 40.05           C  
ANISOU 3761  C   LYS B 110     5297   4116   5804   -344    296    212       C  
ATOM   3762  O   LYS B 110      81.192 -10.098   5.407  1.00 41.08           O  
ANISOU 3762  O   LYS B 110     5325   4280   6002   -394    278    122       O  
ATOM   3763  CB  LYS B 110      82.000 -10.198   2.315  1.00 45.46           C  
ANISOU 3763  CB  LYS B 110     6060   4802   6411   -386    454    287       C  
ATOM   3764  CG  LYS B 110      82.386 -11.154   1.201  1.00 56.41           C  
ANISOU 3764  CG  LYS B 110     7475   6254   7703   -368    480    317       C  
ATOM   3765  CD  LYS B 110      83.703 -10.784   0.545  1.00 78.69           C  
ANISOU 3765  CD  LYS B 110    10309   9030  10559   -448    635    324       C  
ATOM   3766  CE  LYS B 110      84.161 -11.893  -0.401  1.00 89.74           C  
ANISOU 3766  CE  LYS B 110    11716  10511  11871   -431    657    332       C  
ATOM   3767  NZ  LYS B 110      85.354 -11.500  -1.204  1.00 96.19           N  
ANISOU 3767  NZ  LYS B 110    12560  11277  12710   -503    827    350       N  
ATOM   3768  N   LYS B 111      79.752  -8.811   4.253  1.00 36.75           N  
ANISOU 3768  N   LYS B 111     4961   3614   5390   -302    298    266       N  
ATOM   3769  CA  LYS B 111      79.455  -7.914   5.356  1.00 39.56           C  
ANISOU 3769  CA  LYS B 111     5291   3905   5834   -318    287    223       C  
ATOM   3770  C   LYS B 111      77.952  -7.735   5.487  1.00 35.92           C  
ANISOU 3770  C   LYS B 111     4872   3439   5338   -221    200    258       C  
ATOM   3771  O   LYS B 111      77.234  -7.731   4.483  1.00 38.84           O  
ANISOU 3771  O   LYS B 111     5325   3804   5629   -144    180    337       O  
ATOM   3772  CB  LYS B 111      80.110  -6.540   5.147  1.00 39.08           C  
ANISOU 3772  CB  LYS B 111     5289   3710   5849   -380    409    244       C  
ATOM   3773  CG  LYS B 111      81.618  -6.608   4.902  1.00 49.35           C  
ANISOU 3773  CG  LYS B 111     6543   5006   7202   -484    514    206       C  
ATOM   3774  CD  LYS B 111      82.213  -5.214   4.709  1.00 54.59           C  
ANISOU 3774  CD  LYS B 111     7264   5521   7955   -556    651    222       C  
ATOM   3775  CE  LYS B 111      83.626  -5.279   4.142  1.00 61.74           C  
ANISOU 3775  CE  LYS B 111     8137   6416   8906   -656    779    201       C  
ATOM   3776  NZ  LYS B 111      84.124  -3.909   3.796  1.00 68.91           N  
ANISOU 3776  NZ  LYS B 111     9122   7161   9899   -728    935    230       N  
ATOM   3777  N   PRO B 112      77.450  -7.550   6.712  1.00 39.47           N  
ANISOU 3777  N   PRO B 112     5264   3889   5845   -217    149    194       N  
ATOM   3778  CA  PRO B 112      75.994  -7.411   6.897  1.00 43.12           C  
ANISOU 3778  CA  PRO B 112     5747   4350   6286   -125     72    215       C  
ATOM   3779  C   PRO B 112      75.423  -6.122   6.319  1.00 50.94           C  
ANISOU 3779  C   PRO B 112     6845   5226   7285    -72    106    289       C  
ATOM   3780  O   PRO B 112      74.196  -5.993   6.253  1.00 51.02           O  
ANISOU 3780  O   PRO B 112     6874   5238   7274     20     39    313       O  
ATOM   3781  CB  PRO B 112      75.820  -7.449   8.424  1.00 44.43           C  
ANISOU 3781  CB  PRO B 112     5831   4535   6517   -149     36    122       C  
ATOM   3782  CG  PRO B 112      77.188  -7.735   8.999  1.00 50.28           C  
ANISOU 3782  CG  PRO B 112     6508   5301   7297   -242     74     51       C  
ATOM   3783  CD  PRO B 112      78.192  -7.354   7.966  1.00 42.62           C  
ANISOU 3783  CD  PRO B 112     5581   4283   6330   -292    163     96       C  
ATOM   3784  N   THR B 113      76.262  -5.175   5.900  1.00 51.89           N  
ANISOU 3784  N   THR B 113     7033   5243   7440   -123    211    324       N  
ATOM   3785  CA  THR B 113      75.777  -3.945   5.283  1.00 57.48           C  
ANISOU 3785  CA  THR B 113     7866   5826   8149    -66    256    407       C  
ATOM   3786  C   THR B 113      75.340  -4.134   3.841  1.00 58.65           C  
ANISOU 3786  C   THR B 113     8120   5983   8180     24    242    514       C  
ATOM   3787  O   THR B 113      74.724  -3.223   3.277  1.00 54.45           O  
ANISOU 3787  O   THR B 113     7703   5360   7625    106    253    592       O  
ATOM   3788  CB  THR B 113      76.852  -2.861   5.324  1.00 55.96           C  
ANISOU 3788  CB  THR B 113     7719   5504   8041   -160    391    408       C  
ATOM   3789  OG1 THR B 113      78.056  -3.355   4.719  1.00 59.03           O  
ANISOU 3789  OG1 THR B 113     8096   5921   8413   -241    468    411       O  
ATOM   3790  CG2 THR B 113      77.126  -2.452   6.748  1.00 57.57           C  
ANISOU 3790  CG2 THR B 113     7832   5683   8360   -231    392    298       C  
ATOM   3791  N   GLU B 114      75.643  -5.274   3.231  1.00 46.06           N  
ANISOU 3791  N   GLU B 114     6499   4495   6507     19    216    516       N  
ATOM   3792  CA  GLU B 114      75.248  -5.503   1.850  1.00 44.29           C  
ANISOU 3792  CA  GLU B 114     6380   4289   6158    108    195    607       C  
ATOM   3793  C   GLU B 114      73.727  -5.605   1.753  1.00 45.60           C  
ANISOU 3793  C   GLU B 114     6550   4496   6279    239     63    619       C  
ATOM   3794  O   GLU B 114      73.057  -6.079   2.676  1.00 51.13           O  
ANISOU 3794  O   GLU B 114     7139   5260   7028    246    -20    544       O  
ATOM   3795  CB  GLU B 114      75.939  -6.760   1.315  1.00 50.17           C  
ANISOU 3795  CB  GLU B 114     7084   5142   6837     67    196    589       C  
ATOM   3796  CG  GLU B 114      77.464  -6.602   1.237  1.00 48.44           C  
ANISOU 3796  CG  GLU B 114     6861   4880   6663    -54    335    580       C  
ATOM   3797  CD  GLU B 114      78.170  -7.869   0.787  1.00 53.40           C  
ANISOU 3797  CD  GLU B 114     7438   5617   7236    -90    337    552       C  
ATOM   3798  OE1 GLU B 114      79.161  -8.270   1.441  1.00 52.27           O  
ANISOU 3798  OE1 GLU B 114     7191   5505   7166   -187    377    477       O  
ATOM   3799  OE2 GLU B 114      77.722  -8.478  -0.212  1.00 53.21           O  
ANISOU 3799  OE2 GLU B 114     7474   5650   7094    -16    292    599       O  
ATOM   3800  N  ATHR B 115      73.188  -5.163   0.610  0.43 46.23           N  
ANISOU 3800  N  ATHR B 115     6762   4540   6265    348     46    712       N  
ATOM   3801  N  BTHR B 115      73.188  -5.153   0.614  0.57 46.09           N  
ANISOU 3801  N  BTHR B 115     6744   4520   6247    348     46    712       N  
ATOM   3802  CA ATHR B 115      71.741  -4.993   0.475  0.43 48.74           C  
ANISOU 3802  CA ATHR B 115     7090   4877   6553    487    -78    723       C  
ATOM   3803  CA BTHR B 115      71.741  -4.991   0.475  0.57 48.80           C  
ANISOU 3803  CA BTHR B 115     7097   4884   6560    487    -78    723       C  
ATOM   3804  C  ATHR B 115      70.981  -6.300   0.651  0.43 47.62           C  
ANISOU 3804  C  ATHR B 115     6821   4884   6388    514   -207    646       C  
ATOM   3805  C  BTHR B 115      70.989  -6.302   0.676  0.57 47.76           C  
ANISOU 3805  C  BTHR B 115     6836   4902   6408    511   -206    644       C  
ATOM   3806  O  ATHR B 115      69.819  -6.284   1.071  0.43 46.95           O  
ANISOU 3806  O  ATHR B 115     6673   4828   6338    588   -304    607       O  
ATOM   3807  O  BTHR B 115      69.853  -6.293   1.162  0.57 46.54           O  
ANISOU 3807  O  BTHR B 115     6614   4776   6294    579   -300    602       O  
ATOM   3808  CB ATHR B 115      71.401  -4.378  -0.885  0.43 51.21           C  
ANISOU 3808  CB ATHR B 115     7577   5134   6746    612    -82    837       C  
ATOM   3809  CB BTHR B 115      71.410  -4.388  -0.896  0.57 51.42           C  
ANISOU 3809  CB BTHR B 115     7604   5161   6771    611    -82    838       C  
ATOM   3810  OG1ATHR B 115      71.970  -5.179  -1.930  0.43 49.81           O  
ANISOU 3810  OG1ATHR B 115     7451   5024   6451    604    -68    869       O  
ATOM   3811  OG1BTHR B 115      72.132  -3.161  -1.066  0.57 54.96           O  
ANISOU 3811  OG1BTHR B 115     8184   5453   7245    580     59    915       O  
ATOM   3812  CG2ATHR B 115      71.934  -2.955  -0.982  0.43 54.36           C  
ANISOU 3812  CG2ATHR B 115     8114   5360   7180    599     50    918       C  
ATOM   3813  CG2BTHR B 115      69.920  -4.102  -1.025  0.57 45.98           C  
ANISOU 3813  CG2BTHR B 115     6920   4490   6061    768   -219    842       C  
ATOM   3814  N   ILE B 116      71.607  -7.437   0.335  1.00 46.03           N  
ANISOU 3814  N   ILE B 116     6578   4773   6138    453   -203    619       N  
ATOM   3815  CA  ILE B 116      70.921  -8.723   0.482  1.00 39.89           C  
ANISOU 3815  CA  ILE B 116     5686   4124   5345    470   -312    543       C  
ATOM   3816  C   ILE B 116      70.565  -9.007   1.937  1.00 42.74           C  
ANISOU 3816  C   ILE B 116     5907   4509   5821    415   -333    451       C  
ATOM   3817  O   ILE B 116      69.623  -9.762   2.216  1.00 43.76           O  
ANISOU 3817  O   ILE B 116     5946   4718   5965    448   -423    390       O  
ATOM   3818  CB  ILE B 116      71.770  -9.867  -0.112  1.00 49.11           C  
ANISOU 3818  CB  ILE B 116     6847   5370   6442    411   -289    532       C  
ATOM   3819  CG1 ILE B 116      70.913 -11.116  -0.286  1.00 55.34           C  
ANISOU 3819  CG1 ILE B 116     7551   6277   7196    451   -407    466       C  
ATOM   3820  CG2 ILE B 116      72.951 -10.198   0.797  1.00 43.73           C  
ANISOU 3820  CG2 ILE B 116     6092   4685   5838    278   -199    484       C  
ATOM   3821  CD1 ILE B 116      70.893 -11.646  -1.695  1.00 64.91           C  
ANISOU 3821  CD1 ILE B 116     8845   7545   8274    514   -447    499       C  
ATOM   3822  N   CYS B 117      71.289  -8.407   2.887  1.00 42.95           N  
ANISOU 3822  N   CYS B 117     5918   4467   5933    332   -248    436       N  
ATOM   3823  CA  CYS B 117      71.035  -8.679   4.300  1.00 44.44           C  
ANISOU 3823  CA  CYS B 117     5992   4679   6215    283   -261    350       C  
ATOM   3824  C   CYS B 117      69.929  -7.820   4.885  1.00 48.46           C  
ANISOU 3824  C   CYS B 117     6488   5137   6787    351   -297    337       C  
ATOM   3825  O   CYS B 117      69.452  -8.125   5.982  1.00 45.31           O  
ANISOU 3825  O   CYS B 117     5995   4767   6452    331   -317    265       O  
ATOM   3826  CB  CYS B 117      72.293  -8.448   5.130  1.00 43.99           C  
ANISOU 3826  CB  CYS B 117     5915   4581   6219    170   -168    320       C  
ATOM   3827  SG  CYS B 117      73.672  -9.499   4.657  1.00 47.52           S  
ANISOU 3827  SG  CYS B 117     6348   5092   6616     85   -121    314       S  
ATOM   3828  N   ALA B 118      69.552  -6.736   4.209  1.00 42.88           N  
ANISOU 3828  N   ALA B 118     5881   4350   6062    434   -296    408       N  
ATOM   3829  CA  ALA B 118      68.566  -5.818   4.769  1.00 45.79           C  
ANISOU 3829  CA  ALA B 118     6241   4658   6498    505   -323    396       C  
ATOM   3830  C   ALA B 118      67.263  -6.500   5.165  1.00 46.33           C  
ANISOU 3830  C   ALA B 118     6196   4815   6593    564   -422    326       C  
ATOM   3831  O   ALA B 118      66.768  -6.211   6.267  1.00 45.63           O  
ANISOU 3831  O   ALA B 118     6040   4707   6591    555   -414    268       O  
ATOM   3832  CB  ALA B 118      68.299  -4.663   3.785  1.00 47.36           C  
ANISOU 3832  CB  ALA B 118     6580   4760   6654    610   -320    494       C  
ATOM   3833  N   PRO B 119      66.673  -7.403   4.369  1.00 46.14           N  
ANISOU 3833  N   PRO B 119     6140   4886   6506    618   -509    318       N  
ATOM   3834  CA  PRO B 119      65.420  -8.044   4.796  1.00 56.51           C  
ANISOU 3834  CA  PRO B 119     7328   6277   7867    660   -591    237       C  
ATOM   3835  C   PRO B 119      65.584  -9.084   5.892  1.00 50.55           C  
ANISOU 3835  C   PRO B 119     6462   5580   7163    555   -559    153       C  
ATOM   3836  O   PRO B 119      64.572  -9.523   6.452  1.00 47.41           O  
ANISOU 3836  O   PRO B 119     5959   5228   6825    573   -596     81       O  
ATOM   3837  CB  PRO B 119      64.907  -8.712   3.511  1.00 54.44           C  
ANISOU 3837  CB  PRO B 119     7073   6095   7516    738   -691    247       C  
ATOM   3838  CG  PRO B 119      65.674  -8.078   2.404  1.00 62.36           C  
ANISOU 3838  CG  PRO B 119     8232   7043   8420    774   -666    352       C  
ATOM   3839  CD  PRO B 119      67.007  -7.781   2.986  1.00 53.50           C  
ANISOU 3839  CD  PRO B 119     7153   5852   7322    654   -539    379       C  
ATOM   3840  N   LEU B 120      66.806  -9.508   6.198  1.00 45.48           N  
ANISOU 3840  N   LEU B 120     5841   4939   6502    451   -489    159       N  
ATOM   3841  CA  LEU B 120      67.031 -10.584   7.151  1.00 41.99           C  
ANISOU 3841  CA  LEU B 120     5313   4553   6088    366   -464     90       C  
ATOM   3842  C   LEU B 120      67.301 -10.034   8.545  1.00 42.66           C  
ANISOU 3842  C   LEU B 120     5382   4585   6244    315   -398     54       C  
ATOM   3843  O   LEU B 120      67.988  -9.022   8.703  1.00 41.42           O  
ANISOU 3843  O   LEU B 120     5288   4350   6100    298   -349     86       O  
ATOM   3844  CB  LEU B 120      68.217 -11.440   6.716  1.00 37.34           C  
ANISOU 3844  CB  LEU B 120     4750   4002   5433    295   -436    107       C  
ATOM   3845  CG  LEU B 120      68.125 -12.061   5.325  1.00 39.50           C  
ANISOU 3845  CG  LEU B 120     5053   4331   5622    337   -492    137       C  
ATOM   3846  CD1 LEU B 120      69.412 -12.787   5.052  1.00 39.65           C  
ANISOU 3846  CD1 LEU B 120     5099   4376   5590    262   -444    151       C  
ATOM   3847  CD2 LEU B 120      66.933 -13.009   5.266  1.00 41.20           C  
ANISOU 3847  CD2 LEU B 120     5178   4623   5853    372   -568     72       C  
ATOM   3848  N   THR B 121      66.796 -10.729   9.560  1.00 35.45           N  
ANISOU 3848  N   THR B 121     4387   3712   5372    288   -391    -15       N  
ATOM   3849  CA  THR B 121      67.125 -10.369  10.943  1.00 37.54           C  
ANISOU 3849  CA  THR B 121     4643   3937   5682    240   -330    -56       C  
ATOM   3850  C   THR B 121      68.501 -10.940  11.285  1.00 37.66           C  
ANISOU 3850  C   THR B 121     4680   3971   5658    156   -291    -60       C  
ATOM   3851  O   THR B 121      68.667 -12.140  11.523  1.00 36.97           O  
ANISOU 3851  O   THR B 121     4557   3946   5543    121   -292    -87       O  
ATOM   3852  CB  THR B 121      66.026 -10.843  11.889  1.00 38.99           C  
ANISOU 3852  CB  THR B 121     4748   4150   5917    251   -325   -124       C  
ATOM   3853  OG1 THR B 121      64.835 -10.096  11.609  1.00 39.24           O  
ANISOU 3853  OG1 THR B 121     4753   4157   6000    335   -360   -128       O  
ATOM   3854  CG2 THR B 121      66.416 -10.614  13.348  1.00 32.41           C  
ANISOU 3854  CG2 THR B 121     3919   3287   5107    205   -261   -169       C  
ATOM   3855  N   VAL B 122      69.497 -10.064  11.296  1.00 36.80           N  
ANISOU 3855  N   VAL B 122     4626   3804   5553    125   -255    -36       N  
ATOM   3856  CA  VAL B 122      70.893 -10.436  11.479  1.00 33.37           C  
ANISOU 3856  CA  VAL B 122     4203   3384   5092     51   -223    -44       C  
ATOM   3857  C   VAL B 122      71.217 -10.385  12.965  1.00 36.80           C  
ANISOU 3857  C   VAL B 122     4615   3813   5554     14   -197   -113       C  
ATOM   3858  O   VAL B 122      70.885  -9.408  13.646  1.00 36.55           O  
ANISOU 3858  O   VAL B 122     4594   3722   5571     26   -178   -137       O  
ATOM   3859  CB  VAL B 122      71.808  -9.481  10.686  1.00 35.83           C  
ANISOU 3859  CB  VAL B 122     4579   3631   5405     31   -188      7       C  
ATOM   3860  CG1 VAL B 122      73.291  -9.777  10.936  1.00 34.78           C  
ANISOU 3860  CG1 VAL B 122     4437   3513   5265    -50   -152    -18       C  
ATOM   3861  CG2 VAL B 122      71.457  -9.542   9.193  1.00 37.15           C  
ANISOU 3861  CG2 VAL B 122     4790   3805   5522     82   -214     81       C  
ATOM   3862  N   PHE B 123      71.895 -11.414  13.464  1.00 33.78           N  
ANISOU 3862  N   PHE B 123     4209   3490   5137    -25   -197   -145       N  
ATOM   3863  CA  PHE B 123      72.373 -11.425  14.842  1.00 32.79           C  
ANISOU 3863  CA  PHE B 123     4076   3368   5016    -52   -182   -210       C  
ATOM   3864  C   PHE B 123      73.732 -10.733  14.948  1.00 36.69           C  
ANISOU 3864  C   PHE B 123     4581   3830   5528   -103   -164   -231       C  
ATOM   3865  O   PHE B 123      74.680 -11.099  14.240  1.00 35.51           O  
ANISOU 3865  O   PHE B 123     4427   3706   5361   -135   -163   -212       O  
ATOM   3866  CB  PHE B 123      72.478 -12.860  15.362  1.00 31.22           C  
ANISOU 3866  CB  PHE B 123     3857   3241   4764    -56   -192   -234       C  
ATOM   3867  CG  PHE B 123      73.141 -12.966  16.709  1.00 31.40           C  
ANISOU 3867  CG  PHE B 123     3887   3275   4767    -70   -186   -296       C  
ATOM   3868  CD1 PHE B 123      72.477 -12.560  17.856  1.00 39.32           C  
ANISOU 3868  CD1 PHE B 123     4904   4255   5781    -49   -168   -339       C  
ATOM   3869  CD2 PHE B 123      74.424 -13.462  16.826  1.00 38.23           C  
ANISOU 3869  CD2 PHE B 123     4747   4178   5600    -97   -202   -317       C  
ATOM   3870  CE1 PHE B 123      73.087 -12.659  19.103  1.00 39.20           C  
ANISOU 3870  CE1 PHE B 123     4909   4255   5730    -52   -170   -399       C  
ATOM   3871  CE2 PHE B 123      75.036 -13.566  18.067  1.00 38.98           C  
ANISOU 3871  CE2 PHE B 123     4851   4291   5667    -95   -214   -380       C  
ATOM   3872  CZ  PHE B 123      74.354 -13.175  19.207  1.00 37.89           C  
ANISOU 3872  CZ  PHE B 123     4740   4132   5527    -71   -200   -420       C  
ATOM   3873  N   PHE B 124      73.825  -9.756  15.860  1.00 31.54           N  
ANISOU 3873  N   PHE B 124     3940   3127   4918   -113   -148   -282       N  
ATOM   3874  CA  PHE B 124      75.021  -8.954  16.100  1.00 30.42           C  
ANISOU 3874  CA  PHE B 124     3797   2945   4815   -168   -130   -324       C  
ATOM   3875  C   PHE B 124      75.498  -9.144  17.538  1.00 39.65           C  
ANISOU 3875  C   PHE B 124     4950   4148   5969   -178   -150   -417       C  
ATOM   3876  O   PHE B 124      74.691  -9.207  18.470  1.00 33.88           O  
ANISOU 3876  O   PHE B 124     4233   3420   5219   -140   -154   -446       O  
ATOM   3877  CB  PHE B 124      74.754  -7.439  15.861  1.00 31.48           C  
ANISOU 3877  CB  PHE B 124     3969   2971   5022   -173    -91   -312       C  
ATOM   3878  CG  PHE B 124      74.389  -7.092  14.434  1.00 34.36           C  
ANISOU 3878  CG  PHE B 124     4371   3292   5392   -151    -71   -217       C  
ATOM   3879  CD1 PHE B 124      75.375  -6.938  13.468  1.00 35.74           C  
ANISOU 3879  CD1 PHE B 124     4560   3447   5572   -198    -37   -181       C  
ATOM   3880  CD2 PHE B 124      73.065  -6.935  14.058  1.00 34.68           C  
ANISOU 3880  CD2 PHE B 124     4433   3316   5429    -79    -87   -169       C  
ATOM   3881  CE1 PHE B 124      75.050  -6.611  12.157  1.00 37.17           C  
ANISOU 3881  CE1 PHE B 124     4797   3587   5741   -169    -16    -89       C  
ATOM   3882  CE2 PHE B 124      72.725  -6.609  12.745  1.00 34.00           C  
ANISOU 3882  CE2 PHE B 124     4391   3194   5332    -43    -82    -84       C  
ATOM   3883  CZ  PHE B 124      73.714  -6.444  11.793  1.00 36.77           C  
ANISOU 3883  CZ  PHE B 124     4776   3521   5673    -85    -46    -39       C  
ATOM   3884  N   ASP B 125      76.814  -9.173  17.723  1.00 41.53           N  
ANISOU 3884  N   ASP B 125     5158   4406   6214   -225   -161   -469       N  
ATOM   3885  CA  ASP B 125      77.443  -9.462  19.014  1.00 40.13           C  
ANISOU 3885  CA  ASP B 125     4964   4276   6007   -223   -200   -563       C  
ATOM   3886  C   ASP B 125      78.272  -8.243  19.416  1.00 37.32           C  
ANISOU 3886  C   ASP B 125     4590   3863   5726   -277   -190   -646       C  
ATOM   3887  O   ASP B 125      79.360  -8.019  18.874  1.00 42.08           O  
ANISOU 3887  O   ASP B 125     5151   4460   6377   -335   -179   -665       O  
ATOM   3888  CB  ASP B 125      78.284 -10.738  18.890  1.00 40.76           C  
ANISOU 3888  CB  ASP B 125     5012   4445   6030   -219   -237   -566       C  
ATOM   3889  CG  ASP B 125      78.871 -11.216  20.211  1.00 49.40           C  
ANISOU 3889  CG  ASP B 125     6102   5598   7070   -192   -291   -654       C  
ATOM   3890  OD1 ASP B 125      78.759 -10.514  21.237  1.00 42.57           O  
ANISOU 3890  OD1 ASP B 125     5255   4710   6211   -185   -302   -724       O  
ATOM   3891  OD2 ASP B 125      79.466 -12.324  20.215  1.00 44.59           O  
ANISOU 3891  OD2 ASP B 125     5476   5061   6407   -170   -326   -654       O  
ATOM   3892  N   GLY B 126      77.759  -7.448  20.363  1.00 37.67           N  
ANISOU 3892  N   GLY B 126     4663   3862   5786   -263   -187   -701       N  
ATOM   3893  CA  GLY B 126      78.448  -6.248  20.826  1.00 37.44           C  
ANISOU 3893  CA  GLY B 126     4620   3771   5836   -316   -177   -793       C  
ATOM   3894  C   GLY B 126      79.806  -6.494  21.456  1.00 44.30           C  
ANISOU 3894  C   GLY B 126     5429   4700   6702   -348   -231   -902       C  
ATOM   3895  O   GLY B 126      80.559  -5.535  21.666  1.00 45.36           O  
ANISOU 3895  O   GLY B 126     5531   4784   6919   -409   -222   -990       O  
ATOM   3896  N   ARG B 127      80.134  -7.745  21.778  1.00 37.12           N  
ANISOU 3896  N   ARG B 127     4504   3894   5705   -306   -288   -907       N  
ATOM   3897  CA  ARG B 127      81.481  -8.048  22.237  1.00 43.54           C  
ANISOU 3897  CA  ARG B 127     5250   4775   6518   -324   -351  -1008       C  
ATOM   3898  C   ARG B 127      82.504  -7.959  21.113  1.00 47.16           C  
ANISOU 3898  C   ARG B 127     5634   5225   7059   -398   -319   -998       C  
ATOM   3899  O   ARG B 127      83.700  -7.877  21.389  1.00 51.81           O  
ANISOU 3899  O   ARG B 127     6145   5850   7692   -433   -357  -1102       O  
ATOM   3900  CB  ARG B 127      81.513  -9.440  22.871  1.00 45.77           C  
ANISOU 3900  CB  ARG B 127     5551   5162   6677   -243   -418  -1005       C  
ATOM   3901  CG  ARG B 127      80.642  -9.553  24.124  1.00 43.30           C  
ANISOU 3901  CG  ARG B 127     5319   4860   6274   -171   -440  -1028       C  
ATOM   3902  CD  ARG B 127      80.496 -11.006  24.536  1.00 40.11           C  
ANISOU 3902  CD  ARG B 127     4958   4538   5745    -91   -476   -989       C  
ATOM   3903  NE  ARG B 127      79.860 -11.794  23.482  1.00 40.52           N  
ANISOU 3903  NE  ARG B 127     5018   4586   5791    -90   -427   -865       N  
ATOM   3904  CZ  ARG B 127      79.527 -13.080  23.611  1.00 40.85           C  
ANISOU 3904  CZ  ARG B 127     5104   4677   5743    -32   -432   -810       C  
ATOM   3905  NH1 ARG B 127      79.762 -13.724  24.750  1.00 37.20           N  
ANISOU 3905  NH1 ARG B 127     4690   4265   5178     38   -481   -856       N  
ATOM   3906  NH2 ARG B 127      78.947 -13.716  22.610  1.00 36.39           N  
ANISOU 3906  NH2 ARG B 127     4539   4104   5185    -40   -389   -713       N  
ATOM   3907  N   VAL B 128      82.071  -7.980  19.856  1.00 40.28           N  
ANISOU 3907  N   VAL B 128     4784   4311   6211   -417   -251   -882       N  
ATOM   3908  CA  VAL B 128      82.981  -7.903  18.717  1.00 43.65           C  
ANISOU 3908  CA  VAL B 128     5156   4723   6705   -485   -201   -860       C  
ATOM   3909  C   VAL B 128      83.048  -6.454  18.250  1.00 45.59           C  
ANISOU 3909  C   VAL B 128     5413   4845   7064   -562   -117   -865       C  
ATOM   3910  O   VAL B 128      82.009  -5.806  18.068  1.00 41.04           O  
ANISOU 3910  O   VAL B 128     4912   4189   6491   -543    -78   -800       O  
ATOM   3911  CB  VAL B 128      82.528  -8.816  17.566  1.00 42.03           C  
ANISOU 3911  CB  VAL B 128     4981   4544   6443   -455   -175   -732       C  
ATOM   3912  CG1 VAL B 128      83.496  -8.684  16.389  1.00 44.98           C  
ANISOU 3912  CG1 VAL B 128     5309   4901   6882   -525   -110   -712       C  
ATOM   3913  CG2 VAL B 128      82.387 -10.272  18.028  1.00 48.66           C  
ANISOU 3913  CG2 VAL B 128     5821   5490   7176   -380   -246   -724       C  
ATOM   3914  N   ASP B 129      84.267  -5.953  18.034  1.00 41.60           N  
ANISOU 3914  N   ASP B 129     4832   4318   6657   -647    -84   -943       N  
ATOM   3915  CA  ASP B 129      84.452  -4.574  17.589  1.00 48.75           C  
ANISOU 3915  CA  ASP B 129     5751   5091   7681   -732     14   -952       C  
ATOM   3916  C   ASP B 129      83.628  -4.268  16.342  1.00 43.94           C  
ANISOU 3916  C   ASP B 129     5238   4398   7060   -722    102   -797       C  
ATOM   3917  O   ASP B 129      83.639  -5.029  15.372  1.00 45.01           O  
ANISOU 3917  O   ASP B 129     5384   4574   7144   -703    121   -705       O  
ATOM   3918  CB  ASP B 129      85.932  -4.307  17.303  1.00 59.29           C  
ANISOU 3918  CB  ASP B 129     6979   6422   9126   -833     56  -1046       C  
ATOM   3919  CG  ASP B 129      86.739  -4.092  18.563  1.00 78.74           C  
ANISOU 3919  CG  ASP B 129     9348   8932  11640   -858    -24  -1228       C  
ATOM   3920  OD1 ASP B 129      87.830  -4.689  18.688  1.00 88.66           O  
ANISOU 3920  OD1 ASP B 129    10494  10278  12917   -876    -69  -1316       O  
ATOM   3921  OD2 ASP B 129      86.271  -3.330  19.436  1.00 89.33           O  
ANISOU 3921  OD2 ASP B 129    10725  10223  12995   -852    -48  -1289       O  
ATOM   3922  N   GLY B 130      82.903  -3.146  16.383  1.00 42.65           N  
ANISOU 3922  N   GLY B 130     5149   4115   6939   -724    150   -771       N  
ATOM   3923  CA  GLY B 130      82.164  -2.664  15.235  1.00 44.48           C  
ANISOU 3923  CA  GLY B 130     5480   4254   7167   -706    230   -633       C  
ATOM   3924  C   GLY B 130      80.747  -3.188  15.090  1.00 38.82           C  
ANISOU 3924  C   GLY B 130     4832   3570   6346   -596    181   -532       C  
ATOM   3925  O   GLY B 130      79.992  -2.654  14.270  1.00 43.51           O  
ANISOU 3925  O   GLY B 130     5512   4083   6936   -562    229   -428       O  
ATOM   3926  N   GLN B 131      80.354  -4.221  15.835  1.00 38.04           N  
ANISOU 3926  N   GLN B 131     4702   3586   6167   -536     89   -558       N  
ATOM   3927  CA  GLN B 131      79.056  -4.824  15.543  1.00 36.93           C  
ANISOU 3927  CA  GLN B 131     4611   3479   5941   -445     55   -465       C  
ATOM   3928  C   GLN B 131      77.880  -4.019  16.111  1.00 35.43           C  
ANISOU 3928  C   GLN B 131     4474   3220   5766   -394     53   -462       C  
ATOM   3929  O   GLN B 131      76.782  -4.069  15.544  1.00 40.05           O  
ANISOU 3929  O   GLN B 131     5109   3791   6319   -327     51   -375       O  
ATOM   3930  CB  GLN B 131      79.031  -6.274  16.032  1.00 37.08           C  
ANISOU 3930  CB  GLN B 131     4585   3631   5871   -404    -22   -484       C  
ATOM   3931  CG  GLN B 131      80.025  -7.171  15.233  1.00 38.40           C  
ANISOU 3931  CG  GLN B 131     4708   3866   6016   -436    -18   -464       C  
ATOM   3932  CD  GLN B 131      79.426  -8.490  14.783  1.00 54.44           C  
ANISOU 3932  CD  GLN B 131     6748   5982   7954   -375    -58   -396       C  
ATOM   3933  OE1 GLN B 131      78.533  -9.039  15.430  1.00 47.49           O  
ANISOU 3933  OE1 GLN B 131     5881   5142   7022   -317   -104   -396       O  
ATOM   3934  NE2 GLN B 131      79.923  -9.010  13.667  1.00 64.90           N  
ANISOU 3934  NE2 GLN B 131     8067   7331   9259   -391    -32   -342       N  
ATOM   3935  N   VAL B 132      78.061  -3.283  17.212  1.00 37.12           N  
ANISOU 3935  N   VAL B 132     4678   3394   6031   -418     50   -564       N  
ATOM   3936  CA  VAL B 132      76.993  -2.378  17.655  1.00 41.33           C  
ANISOU 3936  CA  VAL B 132     5267   3845   6593   -372     65   -562       C  
ATOM   3937  C   VAL B 132      76.672  -1.362  16.562  1.00 42.34           C  
ANISOU 3937  C   VAL B 132     5466   3846   6776   -370    138   -472       C  
ATOM   3938  O   VAL B 132      75.500  -1.094  16.265  1.00 38.52           O  
ANISOU 3938  O   VAL B 132     5033   3324   6278   -292    137   -404       O  
ATOM   3939  CB  VAL B 132      77.373  -1.680  18.975  1.00 45.37           C  
ANISOU 3939  CB  VAL B 132     5760   4325   7151   -406     56   -698       C  
ATOM   3940  CG1 VAL B 132      76.368  -0.574  19.302  1.00 43.56           C  
ANISOU 3940  CG1 VAL B 132     5594   3989   6969   -365     89   -697       C  
ATOM   3941  CG2 VAL B 132      77.434  -2.675  20.117  1.00 39.67           C  
ANISOU 3941  CG2 VAL B 132     4998   3726   6348   -376    -21   -773       C  
ATOM   3942  N   ASP B 133      77.702  -0.790  15.936  1.00 42.92           N  
ANISOU 3942  N   ASP B 133     5544   3849   6914   -451    205   -471       N  
ATOM   3943  CA  ASP B 133      77.465   0.176  14.863  1.00 44.25           C  
ANISOU 3943  CA  ASP B 133     5803   3885   7126   -446    287   -375       C  
ATOM   3944  C   ASP B 133      76.833  -0.477  13.637  1.00 42.32           C  
ANISOU 3944  C   ASP B 133     5603   3681   6795   -373    274   -240       C  
ATOM   3945  O   ASP B 133      76.022   0.156  12.949  1.00 40.67           O  
ANISOU 3945  O   ASP B 133     5481   3389   6582   -306    299   -150       O  
ATOM   3946  CB  ASP B 133      78.769   0.876  14.483  1.00 54.97           C  
ANISOU 3946  CB  ASP B 133     7157   5155   8575   -560    381   -408       C  
ATOM   3947  CG  ASP B 133      79.322   1.716  15.615  1.00 77.76           C  
ANISOU 3947  CG  ASP B 133    10005   7980  11561   -633    397   -550       C  
ATOM   3948  OD1 ASP B 133      80.443   1.425  16.084  1.00 87.19           O  
ANISOU 3948  OD1 ASP B 133    11107   9229  12792   -716    385   -657       O  
ATOM   3949  OD2 ASP B 133      78.616   2.649  16.054  1.00 85.44           O  
ANISOU 3949  OD2 ASP B 133    11035   8854  12575   -600    413   -563       O  
ATOM   3950  N   LEU B 134      77.189  -1.730  13.339  1.00 37.07           N  
ANISOU 3950  N   LEU B 134     4884   3142   6060   -377    231   -228       N  
ATOM   3951  CA  LEU B 134      76.505  -2.438  12.257  1.00 37.07           C  
ANISOU 3951  CA  LEU B 134     4920   3192   5973   -304    204   -117       C  
ATOM   3952  C   LEU B 134      75.024  -2.632  12.576  1.00 39.71           C  
ANISOU 3952  C   LEU B 134     5263   3556   6268   -199    135    -97       C  
ATOM   3953  O   LEU B 134      74.166  -2.530  11.688  1.00 40.42           O  
ANISOU 3953  O   LEU B 134     5410   3626   6321   -120    123     -8       O  
ATOM   3954  CB  LEU B 134      77.176  -3.790  12.000  1.00 37.97           C  
ANISOU 3954  CB  LEU B 134     4969   3434   6025   -331    170   -125       C  
ATOM   3955  CG  LEU B 134      78.585  -3.735  11.401  1.00 44.42           C  
ANISOU 3955  CG  LEU B 134     5771   4234   6874   -423    244   -132       C  
ATOM   3956  CD1 LEU B 134      79.258  -5.120  11.447  1.00 37.62           C  
ANISOU 3956  CD1 LEU B 134     4826   3506   5960   -442    198   -167       C  
ATOM   3957  CD2 LEU B 134      78.504  -3.225   9.980  1.00 44.29           C  
ANISOU 3957  CD2 LEU B 134     5855   4136   6837   -406    319    -15       C  
ATOM   3958  N   PHE B 135      74.706  -2.919  13.837  1.00 38.21           N  
ANISOU 3958  N   PHE B 135     5017   3417   6086   -194     90   -183       N  
ATOM   3959  CA  PHE B 135      73.305  -3.057  14.232  1.00 36.02           C  
ANISOU 3959  CA  PHE B 135     4736   3161   5788   -104     42   -177       C  
ATOM   3960  C   PHE B 135      72.551  -1.752  14.024  1.00 40.70           C  
ANISOU 3960  C   PHE B 135     5399   3630   6436    -49     74   -142       C  
ATOM   3961  O   PHE B 135      71.430  -1.749  13.503  1.00 39.76           O  
ANISOU 3961  O   PHE B 135     5301   3511   6296     43     43    -84       O  
ATOM   3962  CB  PHE B 135      73.226  -3.517  15.691  1.00 36.37           C  
ANISOU 3962  CB  PHE B 135     4724   3269   5828   -116     11   -279       C  
ATOM   3963  CG  PHE B 135      71.834  -3.496  16.277  1.00 37.04           C  
ANISOU 3963  CG  PHE B 135     4803   3360   5912    -36    -12   -290       C  
ATOM   3964  CD1 PHE B 135      70.941  -4.527  16.017  1.00 33.17           C  
ANISOU 3964  CD1 PHE B 135     4279   2955   5370     18    -53   -257       C  
ATOM   3965  CD2 PHE B 135      71.431  -2.453  17.098  1.00 39.45           C  
ANISOU 3965  CD2 PHE B 135     5130   3585   6275    -20     14   -343       C  
ATOM   3966  CE1 PHE B 135      69.667  -4.521  16.573  1.00 40.34           C  
ANISOU 3966  CE1 PHE B 135     5167   3870   6292     84    -62   -278       C  
ATOM   3967  CE2 PHE B 135      70.163  -2.442  17.652  1.00 42.77           C  
ANISOU 3967  CE2 PHE B 135     5537   4013   6700     53      4   -360       C  
ATOM   3968  CZ  PHE B 135      69.281  -3.483  17.384  1.00 36.29           C  
ANISOU 3968  CZ  PHE B 135     4674   3281   5835    103    -32   -328       C  
ATOM   3969  N   ARG B 136      73.164  -0.626  14.399  1.00 36.08           N  
ANISOU 3969  N   ARG B 136     4848   2935   5926   -102    135   -182       N  
ATOM   3970  CA  ARG B 136      72.506   0.659  14.199  1.00 39.10           C  
ANISOU 3970  CA  ARG B 136     5310   3182   6366    -48    174   -147       C  
ATOM   3971  C   ARG B 136      72.221   0.922  12.728  1.00 47.36           C  
ANISOU 3971  C   ARG B 136     6439   4175   7380     11    190    -19       C  
ATOM   3972  O   ARG B 136      71.233   1.585  12.400  1.00 41.89           O  
ANISOU 3972  O   ARG B 136     5804   3414   6697    110    182     33       O  
ATOM   3973  CB  ARG B 136      73.356   1.794  14.772  1.00 43.38           C  
ANISOU 3973  CB  ARG B 136     5879   3603   7001   -132    248   -217       C  
ATOM   3974  CG  ARG B 136      73.481   1.808  16.287  1.00 43.79           C  
ANISOU 3974  CG  ARG B 136     5870   3687   7083   -168    226   -352       C  
ATOM   3975  CD  ARG B 136      74.204   3.074  16.671  1.00 47.09           C  
ANISOU 3975  CD  ARG B 136     6324   3967   7603   -242    299   -419       C  
ATOM   3976  NE  ARG B 136      74.517   3.234  18.088  1.00 43.93           N  
ANISOU 3976  NE  ARG B 136     5874   3585   7233   -287    280   -564       N  
ATOM   3977  CZ  ARG B 136      73.701   3.795  18.975  1.00 48.19           C  
ANISOU 3977  CZ  ARG B 136     6431   4084   7795   -234    274   -620       C  
ATOM   3978  NH1 ARG B 136      72.494   4.205  18.604  1.00 46.48           N  
ANISOU 3978  NH1 ARG B 136     6267   3812   7581   -133    281   -545       N  
ATOM   3979  NH2 ARG B 136      74.094   3.945  20.232  1.00 45.28           N  
ANISOU 3979  NH2 ARG B 136     6028   3733   7442   -277    258   -756       N  
ATOM   3980  N   ASN B 137      73.065   0.416  11.828  1.00 41.43           N  
ANISOU 3980  N   ASN B 137     5700   3455   6585    -37    212     32       N  
ATOM   3981  CA  ASN B 137      72.819   0.617  10.408  1.00 46.29           C  
ANISOU 3981  CA  ASN B 137     6411   4028   7150     27    229    157       C  
ATOM   3982  C   ASN B 137      71.933  -0.464   9.789  1.00 47.88           C  
ANISOU 3982  C   ASN B 137     6583   4353   7255    118    134    204       C  
ATOM   3983  O   ASN B 137      71.414  -0.258   8.687  1.00 51.49           O  
ANISOU 3983  O   ASN B 137     7121   4782   7659    205    120    300       O  
ATOM   3984  CB  ASN B 137      74.149   0.708   9.649  1.00 48.35           C  
ANISOU 3984  CB  ASN B 137     6713   4246   7410    -68    319    192       C  
ATOM   3985  CG  ASN B 137      74.884   2.023   9.927  1.00 74.50           C  
ANISOU 3985  CG  ASN B 137    10082   7398  10829   -146    431    166       C  
ATOM   3986  OD1 ASN B 137      76.076   2.033  10.233  1.00 85.68           O  
ANISOU 3986  OD1 ASN B 137    11450   8804  12299   -268    491    100       O  
ATOM   3987  ND2 ASN B 137      74.161   3.138   9.833  1.00 73.16           N  
ANISOU 3987  ND2 ASN B 137    10007   7096  10694    -75    458    210       N  
ATOM   3988  N   ALA B 138      71.730  -1.588  10.467  1.00 41.05           N  
ANISOU 3988  N   ALA B 138     5612   3618   6367    103     69    138       N  
ATOM   3989  CA  ALA B 138      70.949  -2.674   9.883  1.00 42.29           C  
ANISOU 3989  CA  ALA B 138     5732   3889   6446    173    -13    169       C  
ATOM   3990  C   ALA B 138      69.461  -2.343   9.907  1.00 45.41           C  
ANISOU 3990  C   ALA B 138     6125   4275   6852    293    -73    179       C  
ATOM   3991  O   ALA B 138      68.969  -1.658  10.802  1.00 46.41           O  
ANISOU 3991  O   ALA B 138     6238   4348   7047    311    -62    130       O  
ATOM   3992  CB  ALA B 138      71.188  -3.975  10.645  1.00 34.02           C  
ANISOU 3992  CB  ALA B 138     4580   2969   5378    117    -50     94       C  
ATOM   3993  N  AARG B 139      68.740  -2.847   8.905  0.65 43.24           N  
ANISOU 3993  N  AARG B 139     5860   4058   6513    379   -140    234       N  
ATOM   3994  N  BARG B 139      68.742  -2.848   8.904  0.35 43.93           N  
ANISOU 3994  N  BARG B 139     5947   4145   6600    379   -140    234       N  
ATOM   3995  CA AARG B 139      67.295  -2.647   8.874  0.65 45.59           C  
ANISOU 3995  CA AARG B 139     6131   4364   6826    500   -211    231       C  
ATOM   3996  CA BARG B 139      67.297  -2.653   8.862  0.35 46.07           C  
ANISOU 3996  CA BARG B 139     6192   4426   6886    500   -211    231       C  
ATOM   3997  C  AARG B 139      66.589  -3.606   9.826  0.65 43.64           C  
ANISOU 3997  C  AARG B 139     5753   4221   6605    488   -254    139       C  
ATOM   3998  C  BARG B 139      66.588  -3.608   9.817  0.35 43.25           C  
ANISOU 3998  C  BARG B 139     5705   4172   6556    488   -254    140       C  
ATOM   3999  O  AARG B 139      65.614  -3.229  10.487  0.65 40.94           O  
ANISOU 3999  O  AARG B 139     5367   3865   6324    543   -269     94       O  
ATOM   4000  O  BARG B 139      65.612  -3.227  10.474  0.35 41.69           O  
ANISOU 4000  O  BARG B 139     5463   3960   6419    544   -269     95       O  
ATOM   4001  CB AARG B 139      66.783  -2.819   7.444  0.65 53.17           C  
ANISOU 4001  CB AARG B 139     7144   5352   7705    602   -278    310       C  
ATOM   4002  CB BARG B 139      66.794  -2.841   7.430  0.35 52.70           C  
ANISOU 4002  CB BARG B 139     7084   5294   7644    602   -279    311       C  
ATOM   4003  CG AARG B 139      65.290  -2.640   7.266  0.65 58.86           C  
ANISOU 4003  CG AARG B 139     7829   6094   8443    741   -369    301       C  
ATOM   4004  CG BARG B 139      65.411  -2.281   7.148  0.35 58.71           C  
ANISOU 4004  CG BARG B 139     7846   6036   8423    750   -354    322       C  
ATOM   4005  CD AARG B 139      64.925  -2.676   5.787  0.65 64.28           C  
ANISOU 4005  CD AARG B 139     8590   6800   9035    852   -442    381       C  
ATOM   4006  CD BARG B 139      65.064  -2.454   5.674  0.35 63.79           C  
ANISOU 4006  CD BARG B 139     8559   6712   8967    855   -429    400       C  
ATOM   4007  NE AARG B 139      63.490  -2.527   5.562  0.65 67.64           N  
ANISOU 4007  NE AARG B 139     8966   7256   9477    996   -547    361       N  
ATOM   4008  NE BARG B 139      63.717  -1.991   5.349  0.35 66.39           N  
ANISOU 4008  NE BARG B 139     8877   7039   9310   1013   -522    402       N  
ATOM   4009  CZ AARG B 139      62.853  -1.360   5.508  0.65 66.46           C  
ANISOU 4009  CZ AARG B 139     8876   7012   9365   1110   -559    392       C  
ATOM   4010  CZ BARG B 139      62.632  -2.758   5.394  0.35 67.13           C  
ANISOU 4010  CZ BARG B 139     8844   7244   9419   1071   -622    332       C  
ATOM   4011  NH1AARG B 139      61.546  -1.334   5.296  0.65 69.87           N  
ANISOU 4011  NH1AARG B 139     9241   7490   9817   1246   -665    360       N  
ATOM   4012  NH1BARG B 139      62.729  -4.032   5.758  0.35 62.09           N  
ANISOU 4012  NH1BARG B 139     8093   6718   8782    979   -633    263       N  
ATOM   4013  NH2AARG B 139      63.518  -0.222   5.670  0.65 63.83           N  
ANISOU 4013  NH2AARG B 139     8661   6535   9054   1090   -463    448       N  
ATOM   4014  NH2BARG B 139      61.448  -2.250   5.077  0.35 67.11           N  
ANISOU 4014  NH2BARG B 139     8825   7236   9436   1222   -710    328       N  
ATOM   4015  N   ASN B 140      67.080  -4.841   9.915  1.00 38.99           N  
ANISOU 4015  N   ASN B 140     5108   3731   5975    415   -262    111       N  
ATOM   4016  CA  ASN B 140      66.512  -5.867  10.779  1.00 39.41           C  
ANISOU 4016  CA  ASN B 140     5053   3875   6045    394   -285     33       C  
ATOM   4017  C   ASN B 140      67.642  -6.554  11.521  1.00 39.04           C  
ANISOU 4017  C   ASN B 140     4988   3863   5980    283   -240     -6       C  
ATOM   4018  O   ASN B 140      68.614  -6.982  10.899  1.00 39.31           O  
ANISOU 4018  O   ASN B 140     5052   3919   5965    235   -232     28       O  
ATOM   4019  CB  ASN B 140      65.733  -6.892   9.960  1.00 39.41           C  
ANISOU 4019  CB  ASN B 140     5000   3970   6003    444   -361     38       C  
ATOM   4020  CG  ASN B 140      64.536  -6.291   9.311  1.00 44.92           C  
ANISOU 4020  CG  ASN B 140     5696   4650   6720    567   -425     58       C  
ATOM   4021  OD1 ASN B 140      63.526  -6.065   9.972  1.00 41.82           O  
ANISOU 4021  OD1 ASN B 140     5237   4257   6397    612   -435      4       O  
ATOM   4022  ND2 ASN B 140      64.641  -5.986   8.011  1.00 41.80           N  
ANISOU 4022  ND2 ASN B 140     5381   4241   6262    631   -467    134       N  
ATOM   4023  N   GLY B 141      67.517  -6.671  12.838  1.00 36.25           N  
ANISOU 4023  N   GLY B 141     4590   3517   5664    251   -212    -78       N  
ATOM   4024  CA  GLY B 141      68.591  -7.322  13.567  1.00 35.96           C  
ANISOU 4024  CA  GLY B 141     4544   3518   5602    163   -183   -117       C  
ATOM   4025  C   GLY B 141      68.251  -7.535  15.024  1.00 36.69           C  
ANISOU 4025  C   GLY B 141     4598   3627   5717    148   -159   -195       C  
ATOM   4026  O   GLY B 141      67.285  -6.978  15.556  1.00 37.19           O  
ANISOU 4026  O   GLY B 141     4646   3656   5827    196   -148   -224       O  
ATOM   4027  N   VAL B 142      69.084  -8.360  15.657  1.00 34.17           N  
ANISOU 4027  N   VAL B 142     4268   3358   5356     89   -149   -229       N  
ATOM   4028  CA  VAL B 142      69.072  -8.602  17.095  1.00 33.11           C  
ANISOU 4028  CA  VAL B 142     4124   3240   5216     72   -122   -300       C  
ATOM   4029  C   VAL B 142      70.497  -8.406  17.592  1.00 38.04           C  
ANISOU 4029  C   VAL B 142     4775   3857   5820     13   -116   -333       C  
ATOM   4030  O   VAL B 142      71.445  -8.922  16.988  1.00 36.88           O  
ANISOU 4030  O   VAL B 142     4627   3744   5643    -24   -132   -309       O  
ATOM   4031  CB  VAL B 142      68.557 -10.019  17.427  1.00 35.99           C  
ANISOU 4031  CB  VAL B 142     4453   3683   5540     75   -123   -314       C  
ATOM   4032  CG1 VAL B 142      68.861 -10.397  18.873  1.00 33.59           C  
ANISOU 4032  CG1 VAL B 142     4166   3397   5200     56    -91   -375       C  
ATOM   4033  CG2 VAL B 142      67.061 -10.090  17.156  1.00 31.05           C  
ANISOU 4033  CG2 VAL B 142     3780   3059   4957    128   -122   -310       C  
ATOM   4034  N   LEU B 143      70.657  -7.634  18.669  1.00 32.61           N  
ANISOU 4034  N   LEU B 143     4108   3128   5156      5    -94   -396       N  
ATOM   4035  CA  LEU B 143      71.962  -7.310  19.230  1.00 30.09           C  
ANISOU 4035  CA  LEU B 143     3802   2800   4830    -49    -96   -451       C  
ATOM   4036  C   LEU B 143      72.046  -7.799  20.672  1.00 35.23           C  
ANISOU 4036  C   LEU B 143     4460   3496   5429    -42    -99   -527       C  
ATOM   4037  O   LEU B 143      71.091  -7.649  21.431  1.00 38.49           O  
ANISOU 4037  O   LEU B 143     4886   3896   5843     -4    -73   -553       O  
ATOM   4038  CB  LEU B 143      72.213  -5.778  19.168  1.00 31.23           C  
ANISOU 4038  CB  LEU B 143     3974   2841   5052    -67    -70   -470       C  
ATOM   4039  CG  LEU B 143      73.415  -5.216  19.925  1.00 33.28           C  
ANISOU 4039  CG  LEU B 143     4237   3079   5330   -125    -69   -556       C  
ATOM   4040  CD1 LEU B 143      74.716  -5.677  19.288  1.00 39.63           C  
ANISOU 4040  CD1 LEU B 143     5013   3921   6125   -184    -85   -546       C  
ATOM   4041  CD2 LEU B 143      73.360  -3.670  19.998  1.00 31.51           C  
ANISOU 4041  CD2 LEU B 143     4045   2734   5192   -138    -30   -584       C  
ATOM   4042  N   ILE B 144      73.181  -8.405  21.049  1.00 32.03           N  
ANISOU 4042  N   ILE B 144     4050   3146   4975    -72   -129   -563       N  
ATOM   4043  CA  ILE B 144      73.466  -8.666  22.459  1.00 35.53           C  
ANISOU 4043  CA  ILE B 144     4518   3624   5359    -58   -142   -643       C  
ATOM   4044  C   ILE B 144      74.698  -7.867  22.857  1.00 37.39           C  
ANISOU 4044  C   ILE B 144     4746   3840   5621   -101   -170   -724       C  
ATOM   4045  O   ILE B 144      75.599  -7.643  22.047  1.00 35.36           O  
ANISOU 4045  O   ILE B 144     4454   3574   5409   -150   -181   -714       O  
ATOM   4046  CB  ILE B 144      73.663 -10.164  22.790  1.00 35.72           C  
ANISOU 4046  CB  ILE B 144     4550   3734   5289    -35   -162   -630       C  
ATOM   4047  CG1 ILE B 144      74.864 -10.746  22.032  1.00 33.84           C  
ANISOU 4047  CG1 ILE B 144     4276   3540   5041    -68   -204   -612       C  
ATOM   4048  CG2 ILE B 144      72.372 -10.917  22.497  1.00 33.94           C  
ANISOU 4048  CG2 ILE B 144     4326   3517   5052     -3   -122   -568       C  
ATOM   4049  CD1 ILE B 144      75.363 -12.084  22.583  1.00 40.41           C  
ANISOU 4049  CD1 ILE B 144     5125   4450   5778    -38   -235   -621       C  
ATOM   4050  N   THR B 145      74.708  -7.385  24.102  1.00 34.05           N  
ANISOU 4050  N   THR B 145     4354   3408   5177    -85   -176   -813       N  
ATOM   4051  CA  THR B 145      75.880  -6.721  24.664  1.00 35.08           C  
ANISOU 4051  CA  THR B 145     4470   3532   5328   -122   -215   -917       C  
ATOM   4052  C   THR B 145      76.032  -7.128  26.116  1.00 37.24           C  
ANISOU 4052  C   THR B 145     4786   3864   5501    -75   -254  -1002       C  
ATOM   4053  O   THR B 145      75.098  -7.631  26.746  1.00 39.91           O  
ANISOU 4053  O   THR B 145     5177   4218   5767    -18   -225   -981       O  
ATOM   4054  CB  THR B 145      75.776  -5.197  24.630  1.00 41.14           C  
ANISOU 4054  CB  THR B 145     5242   4194   6197   -158   -180   -960       C  
ATOM   4055  OG1 THR B 145      74.691  -4.808  25.485  1.00 46.36           O  
ANISOU 4055  OG1 THR B 145     5954   4823   6838   -108   -148   -984       O  
ATOM   4056  CG2 THR B 145      75.537  -4.681  23.212  1.00 38.27           C  
ANISOU 4056  CG2 THR B 145     4861   3757   5921   -191   -134   -867       C  
ATOM   4057  N   GLU B 146      77.211  -6.844  26.661  1.00 32.75           N  
ANISOU 4057  N   GLU B 146     4193   3320   4929    -98   -315  -1107       N  
ATOM   4058  CA  GLU B 146      77.466  -7.026  28.079  1.00 36.93           C  
ANISOU 4058  CA  GLU B 146     4772   3902   5359    -45   -366  -1206       C  
ATOM   4059  C   GLU B 146      77.190  -5.778  28.898  1.00 46.15           C  
ANISOU 4059  C   GLU B 146     5970   5004   6560    -51   -351  -1304       C  
ATOM   4060  O   GLU B 146      77.128  -5.866  30.128  1.00 50.74           O  
ANISOU 4060  O   GLU B 146     6614   5621   7044      5   -380  -1382       O  
ATOM   4061  CB  GLU B 146      78.918  -7.468  28.298  1.00 35.49           C  
ANISOU 4061  CB  GLU B 146     4540   3798   5147    -51   -462  -1284       C  
ATOM   4062  CG  GLU B 146      79.197  -8.862  27.739  1.00 38.67           C  
ANISOU 4062  CG  GLU B 146     4929   4275   5491    -23   -482  -1199       C  
ATOM   4063  CD  GLU B 146      80.649  -9.270  27.895  1.00 52.92           C  
ANISOU 4063  CD  GLU B 146     6672   6156   7278    -21   -579  -1280       C  
ATOM   4064  OE1 GLU B 146      81.530  -8.393  27.775  1.00 55.56           O  
ANISOU 4064  OE1 GLU B 146     6929   6472   7708    -84   -608  -1375       O  
ATOM   4065  OE2 GLU B 146      80.905 -10.463  28.154  1.00 47.63           O  
ANISOU 4065  OE2 GLU B 146     6030   5564   6506     46   -623  -1254       O  
ATOM   4066  N   GLY B 147      77.031  -4.621  28.250  1.00 47.20           N  
ANISOU 4066  N   GLY B 147     6073   5039   6822   -112   -304  -1303       N  
ATOM   4067  CA  GLY B 147      76.822  -3.369  28.948  1.00 40.20           C  
ANISOU 4067  CA  GLY B 147     5215   4076   5984   -123   -284  -1401       C  
ATOM   4068  C   GLY B 147      75.861  -2.485  28.175  1.00 39.78           C  
ANISOU 4068  C   GLY B 147     5170   3909   6036   -142   -197  -1328       C  
ATOM   4069  O   GLY B 147      75.327  -2.879  27.135  1.00 38.93           O  
ANISOU 4069  O   GLY B 147     5047   3791   5952   -139   -160  -1204       O  
ATOM   4070  N   SER B 148      75.663  -1.274  28.695  1.00 39.33           N  
ANISOU 4070  N   SER B 148     5140   3765   6040   -154   -170  -1412       N  
ATOM   4071  CA  SER B 148      74.709  -0.364  28.076  1.00 44.20           C  
ANISOU 4071  CA  SER B 148     5775   4265   6752   -153    -90  -1349       C  
ATOM   4072  C   SER B 148      75.235   0.147  26.740  1.00 46.30           C  
ANISOU 4072  C   SER B 148     5999   4457   7134   -224    -65  -1286       C  
ATOM   4073  O   SER B 148      76.445   0.257  26.520  1.00 41.66           O  
ANISOU 4073  O   SER B 148     5366   3877   6587   -296    -94  -1339       O  
ATOM   4074  CB  SER B 148      74.392   0.813  29.009  1.00 43.74           C  
ANISOU 4074  CB  SER B 148     5764   4125   6732   -145    -63  -1461       C  
ATOM   4075  OG  SER B 148      75.542   1.589  29.306  1.00 46.30           O  
ANISOU 4075  OG  SER B 148     6063   4411   7117   -217    -97  -1588       O  
ATOM   4076  N   VAL B 149      74.300   0.430  25.835  1.00 41.52           N  
ANISOU 4076  N   VAL B 149     5412   3785   6578   -198     -7  -1173       N  
ATOM   4077  CA  VAL B 149      74.567   1.070  24.553  1.00 39.94           C  
ANISOU 4077  CA  VAL B 149     5205   3491   6478   -245     35  -1098       C  
ATOM   4078  C   VAL B 149      73.846   2.406  24.568  1.00 44.33           C  
ANISOU 4078  C   VAL B 149     5814   3906   7123   -225     97  -1106       C  
ATOM   4079  O   VAL B 149      72.647   2.455  24.867  1.00 38.94           O  
ANISOU 4079  O   VAL B 149     5160   3214   6420   -146    115  -1080       O  
ATOM   4080  CB  VAL B 149      74.078   0.222  23.367  1.00 39.21           C  
ANISOU 4080  CB  VAL B 149     5101   3443   6354   -212     37   -951       C  
ATOM   4081  CG1 VAL B 149      74.330   0.970  22.059  1.00 39.00           C  
ANISOU 4081  CG1 VAL B 149     5091   3312   6416   -250     87   -870       C  
ATOM   4082  CG2 VAL B 149      74.738  -1.154  23.369  1.00 39.60           C  
ANISOU 4082  CG2 VAL B 149     5103   3628   6315   -224    -20   -942       C  
ATOM   4083  N   LYS B 150      74.563   3.483  24.248  1.00 40.27           N  
ANISOU 4083  N   LYS B 150     5311   3275   6713   -297    137  -1144       N  
ATOM   4084  CA  LYS B 150      74.029   4.811  24.531  1.00 38.56           C  
ANISOU 4084  CA  LYS B 150     5153   2915   6583   -282    194  -1184       C  
ATOM   4085  C   LYS B 150      72.733   5.056  23.760  1.00 41.88           C  
ANISOU 4085  C   LYS B 150     5618   3274   7018   -192    234  -1055       C  
ATOM   4086  O   LYS B 150      72.653   4.799  22.556  1.00 42.69           O  
ANISOU 4086  O   LYS B 150     5726   3371   7124   -182    244   -931       O  
ATOM   4087  CB  LYS B 150      75.063   5.905  24.225  1.00 43.43           C  
ANISOU 4087  CB  LYS B 150     5778   3403   7322   -386    244  -1243       C  
ATOM   4088  CG  LYS B 150      75.633   5.977  22.804  1.00 37.44           C  
ANISOU 4088  CG  LYS B 150     5021   2589   6618   -440    293  -1132       C  
ATOM   4089  CD  LYS B 150      76.754   7.064  22.754  1.00 38.89           C  
ANISOU 4089  CD  LYS B 150     5203   2640   6932   -560    357  -1224       C  
ATOM   4090  CE  LYS B 150      77.323   7.240  21.350  1.00 49.02           C  
ANISOU 4090  CE  LYS B 150     6504   3848   8273   -618    432  -1113       C  
ATOM   4091  NZ  LYS B 150      77.988   5.999  20.869  1.00 55.71           N  
ANISOU 4091  NZ  LYS B 150     7277   4842   9049   -644    384  -1073       N  
ATOM   4092  N   GLY B 151      71.704   5.521  24.483  1.00 38.36           N  
ANISOU 4092  N   GLY B 151     5206   2793   6578   -118    251  -1092       N  
ATOM   4093  CA  GLY B 151      70.398   5.805  23.919  1.00 42.80           C  
ANISOU 4093  CA  GLY B 151     5798   3302   7162    -17    279   -995       C  
ATOM   4094  C   GLY B 151      69.474   4.610  23.700  1.00 39.47           C  
ANISOU 4094  C   GLY B 151     5332   3009   6656     58    241   -917       C  
ATOM   4095  O   GLY B 151      68.256   4.805  23.577  1.00 43.28           O  
ANISOU 4095  O   GLY B 151     5820   3467   7156    151    257   -877       O  
ATOM   4096  N   LEU B 152      69.994   3.394  23.646  1.00 35.75           N  
ANISOU 4096  N   LEU B 152     4814   2668   6103     23    194   -901       N  
ATOM   4097  CA  LEU B 152      69.167   2.203  23.391  1.00 36.08           C  
ANISOU 4097  CA  LEU B 152     4812   2823   6072     82    166   -831       C  
ATOM   4098  C   LEU B 152      68.615   1.627  24.691  1.00 43.20           C  
ANISOU 4098  C   LEU B 152     5701   3804   6909    114    167   -910       C  
ATOM   4099  O   LEU B 152      69.367   1.406  25.645  1.00 39.40           O  
ANISOU 4099  O   LEU B 152     5228   3366   6377     71    151   -999       O  
ATOM   4100  CB  LEU B 152      69.972   1.125  22.664  1.00 40.33           C  
ANISOU 4100  CB  LEU B 152     5316   3455   6554     32    124   -772       C  
ATOM   4101  CG  LEU B 152      70.560   1.483  21.298  1.00 46.51           C  
ANISOU 4101  CG  LEU B 152     6115   4176   7380     -2    131   -684       C  
ATOM   4102  CD1 LEU B 152      71.016   0.227  20.565  1.00 43.56           C  
ANISOU 4102  CD1 LEU B 152     5701   3912   6937    -25     91   -618       C  
ATOM   4103  CD2 LEU B 152      69.589   2.299  20.453  1.00 44.94           C  
ANISOU 4103  CD2 LEU B 152     5957   3878   7238     75    158   -602       C  
ATOM   4104  N   GLN B 153      67.311   1.366  24.723  1.00 43.90           N  
ANISOU 4104  N   GLN B 153     5769   3913   6998    193    187   -879       N  
ATOM   4105  CA  GLN B 153      66.689   0.811  25.923  1.00 38.23           C  
ANISOU 4105  CA  GLN B 153     5045   3261   6220    225    212   -945       C  
ATOM   4106  C   GLN B 153      66.858  -0.707  25.935  1.00 37.60           C  
ANISOU 4106  C   GLN B 153     4933   3310   6045    207    185   -911       C  
ATOM   4107  O   GLN B 153      66.426  -1.374  24.988  1.00 40.20           O  
ANISOU 4107  O   GLN B 153     5216   3677   6379    223    168   -824       O  
ATOM   4108  CB  GLN B 153      65.214   1.181  25.976  1.00 39.31           C  
ANISOU 4108  CB  GLN B 153     5161   3361   6412    312    259   -938       C  
ATOM   4109  CG  GLN B 153      64.939   2.689  25.744  1.00 38.31           C  
ANISOU 4109  CG  GLN B 153     5070   3096   6391    349    284   -951       C  
ATOM   4110  CD  GLN B 153      65.698   3.593  26.695  1.00 42.91           C  
ANISOU 4110  CD  GLN B 153     5715   3608   6982    305    305  -1059       C  
ATOM   4111  OE1 GLN B 153      65.299   3.769  27.842  1.00 39.66           O  
ANISOU 4111  OE1 GLN B 153     5323   3198   6548    330    344  -1150       O  
ATOM   4112  NE2 GLN B 153      66.786   4.205  26.207  1.00 37.62           N  
ANISOU 4112  NE2 GLN B 153     5077   2869   6349    239    285  -1056       N  
ATOM   4113  N   PRO B 154      67.468  -1.290  26.969  1.00 38.59           N  
ANISOU 4113  N   PRO B 154     5084   3499   6078    180    177   -977       N  
ATOM   4114  CA  PRO B 154      67.783  -2.722  26.942  1.00 40.91           C  
ANISOU 4114  CA  PRO B 154     5361   3901   6280    163    151   -939       C  
ATOM   4115  C   PRO B 154      66.671  -3.602  27.502  1.00 40.66           C  
ANISOU 4115  C   PRO B 154     5324   3923   6203    210    206   -930       C  
ATOM   4116  O   PRO B 154      65.819  -3.170  28.278  1.00 37.87           O  
ANISOU 4116  O   PRO B 154     4988   3540   5862    252    268   -980       O  
ATOM   4117  CB  PRO B 154      69.023  -2.811  27.842  1.00 40.52           C  
ANISOU 4117  CB  PRO B 154     5355   3886   6154    125    111  -1021       C  
ATOM   4118  CG  PRO B 154      68.764  -1.754  28.895  1.00 42.86           C  
ANISOU 4118  CG  PRO B 154     5700   4120   6466    147    146  -1123       C  
ATOM   4119  CD  PRO B 154      67.994  -0.630  28.182  1.00 43.28           C  
ANISOU 4119  CD  PRO B 154     5734   4066   6645    167    184  -1093       C  
ATOM   4120  N   SER B 155      66.726  -4.870  27.106  1.00 38.44           N  
ANISOU 4120  N   SER B 155     5017   3718   5869    198    191   -871       N  
ATOM   4121  CA  SER B 155      65.997  -5.958  27.751  1.00 42.05           C  
ANISOU 4121  CA  SER B 155     5482   4232   6262    222    249   -868       C  
ATOM   4122  C   SER B 155      67.022  -6.884  28.394  1.00 39.78           C  
ANISOU 4122  C   SER B 155     5253   4012   5852    202    219   -882       C  
ATOM   4123  O   SER B 155      67.943  -7.347  27.717  1.00 37.56           O  
ANISOU 4123  O   SER B 155     4955   3764   5553    168    152   -844       O  
ATOM   4124  CB  SER B 155      65.150  -6.736  26.743  1.00 43.70           C  
ANISOU 4124  CB  SER B 155     5616   4468   6520    227    260   -792       C  
ATOM   4125  OG  SER B 155      64.628  -7.927  27.332  1.00 39.87           O  
ANISOU 4125  OG  SER B 155     5141   4033   5974    232    322   -788       O  
ATOM   4126  N   VAL B 156      66.869  -7.151  29.690  1.00 36.05           N  
ANISOU 4126  N   VAL B 156     4853   3557   5288    230    268   -937       N  
ATOM   4127  CA  VAL B 156      67.799  -8.039  30.385  1.00 38.60           C  
ANISOU 4127  CA  VAL B 156     5245   3942   5478    233    235   -950       C  
ATOM   4128  C   VAL B 156      67.469  -9.482  30.015  1.00 41.51           C  
ANISOU 4128  C   VAL B 156     5605   4358   5809    231    266   -872       C  
ATOM   4129  O   VAL B 156      66.338  -9.943  30.208  1.00 40.06           O  
ANISOU 4129  O   VAL B 156     5416   4165   5638    246    361   -852       O  
ATOM   4130  CB  VAL B 156      67.747  -7.826  31.905  1.00 44.99           C  
ANISOU 4130  CB  VAL B 156     6157   4754   6185    277    276  -1033       C  
ATOM   4131  CG1 VAL B 156      68.587  -8.878  32.615  1.00 42.20           C  
ANISOU 4131  CG1 VAL B 156     5887   4468   5679    301    241  -1036       C  
ATOM   4132  CG2 VAL B 156      68.256  -6.421  32.268  1.00 48.70           C  
ANISOU 4132  CG2 VAL B 156     6636   5176   6690    272    232  -1126       C  
ATOM   4133  N   GLY B 157      68.455 -10.199  29.481  1.00 39.93           N  
ANISOU 4133  N   GLY B 157     5397   4204   5571    209    192   -835       N  
ATOM   4134  CA  GLY B 157      68.233 -11.551  29.014  1.00 36.47           C  
ANISOU 4134  CA  GLY B 157     4949   3802   5107    203    215   -763       C  
ATOM   4135  C   GLY B 157      68.279 -12.587  30.118  1.00 34.65           C  
ANISOU 4135  C   GLY B 157     4824   3601   4742    241    265   -765       C  
ATOM   4136  O   GLY B 157      68.340 -12.268  31.312  1.00 37.66           O  
ANISOU 4136  O   GLY B 157     5292   3979   5039    281    289   -822       O  
ATOM   4137  N   PRO B 158      68.252 -13.860  29.733  1.00 37.56           N  
ANISOU 4137  N   PRO B 158     5196   3995   5081    234    284   -702       N  
ATOM   4138  CA  PRO B 158      68.366 -14.933  30.727  1.00 39.24           C  
ANISOU 4138  CA  PRO B 158     5527   4224   5158    276    335   -690       C  
ATOM   4139  C   PRO B 158      69.740 -14.932  31.383  1.00 37.51           C  
ANISOU 4139  C   PRO B 158     5384   4049   4818    320    234   -728       C  
ATOM   4140  O   PRO B 158      70.721 -14.416  30.844  1.00 41.28           O  
ANISOU 4140  O   PRO B 158     5803   4551   5330    301    124   -753       O  
ATOM   4141  CB  PRO B 158      68.133 -16.211  29.909  1.00 36.43           C  
ANISOU 4141  CB  PRO B 158     5140   3876   4825    249    364   -615       C  
ATOM   4142  CG  PRO B 158      68.454 -15.849  28.494  1.00 39.69           C  
ANISOU 4142  CG  PRO B 158     5432   4301   5348    202    278   -594       C  
ATOM   4143  CD  PRO B 158      68.196 -14.360  28.347  1.00 34.04           C  
ANISOU 4143  CD  PRO B 158     4657   3558   4718    191    254   -640       C  
ATOM   4144  N   LYS B 159      69.798 -15.529  32.575  1.00 37.66           N  
ANISOU 4144  N   LYS B 159     5539   4078   4694    382    278   -737       N  
ATOM   4145  CA  LYS B 159      71.070 -15.635  33.284  1.00 43.50           C  
ANISOU 4145  CA  LYS B 159     6358   4868   5303    443    172   -780       C  
ATOM   4146  C   LYS B 159      72.055 -16.568  32.576  1.00 43.61           C  
ANISOU 4146  C   LYS B 159     6345   4924   5301    445     86   -735       C  
ATOM   4147  O   LYS B 159      73.276 -16.367  32.681  1.00 41.90           O  
ANISOU 4147  O   LYS B 159     6120   4757   5042    471    -38   -784       O  
ATOM   4148  CB  LYS B 159      70.831 -16.119  34.716  1.00 41.45           C  
ANISOU 4148  CB  LYS B 159     6269   4605   4874    525    242   -790       C  
ATOM   4149  CG  LYS B 159      70.125 -15.117  35.645  1.00 43.75           C  
ANISOU 4149  CG  LYS B 159     6608   4866   5148    541    310   -858       C  
ATOM   4150  CD  LYS B 159      70.053 -15.689  37.060  1.00 55.51           C  
ANISOU 4150  CD  LYS B 159     8289   6360   6442    634    373   -864       C  
ATOM   4151  CE  LYS B 159      69.395 -14.730  38.040  1.00 71.92           C  
ANISOU 4151  CE  LYS B 159    10428   8411   8487    657    445   -938       C  
ATOM   4152  NZ  LYS B 159      69.611 -15.182  39.448  1.00 83.63           N  
ANISOU 4152  NZ  LYS B 159    12114   9911   9749    763    474   -956       N  
ATOM   4153  N   GLN B 160      71.563 -17.593  31.869  1.00 38.33           N  
ANISOU 4153  N   GLN B 160     5658   4238   4668    417    151   -652       N  
ATOM   4154  CA  GLN B 160      72.406 -18.631  31.288  1.00 38.60           C  
ANISOU 4154  CA  GLN B 160     5687   4305   4675    429     89   -606       C  
ATOM   4155  C   GLN B 160      72.666 -18.392  29.799  1.00 41.20           C  
ANISOU 4155  C   GLN B 160     5867   4644   5144    354     33   -587       C  
ATOM   4156  O   GLN B 160      71.933 -17.670  29.115  1.00 39.15           O  
ANISOU 4156  O   GLN B 160     5518   4355   5004    294     65   -585       O  
ATOM   4157  CB  GLN B 160      71.780 -20.026  31.477  1.00 38.33           C  
ANISOU 4157  CB  GLN B 160     5745   4237   4581    450    200   -529       C  
ATOM   4158  CG  GLN B 160      70.563 -20.323  30.575  1.00 39.65           C  
ANISOU 4158  CG  GLN B 160     5829   4356   4879    370    306   -480       C  
ATOM   4159  CD  GLN B 160      69.229 -19.898  31.206  1.00 42.76           C  
ANISOU 4159  CD  GLN B 160     6246   4701   5301    354    441   -496       C  
ATOM   4160  OE1 GLN B 160      69.180 -18.966  32.001  1.00 41.56           O  
ANISOU 4160  OE1 GLN B 160     6128   4550   5113    382    438   -551       O  
ATOM   4161  NE2 GLN B 160      68.150 -20.591  30.850  1.00 42.76           N  
ANISOU 4161  NE2 GLN B 160     6222   4656   5370    309    562   -456       N  
ATOM   4162  N   ALA B 161      73.737 -19.017  29.306  1.00 33.34           N  
ANISOU 4162  N   ALA B 161     4851   3690   4125    368    -52   -572       N  
ATOM   4163  CA  ALA B 161      74.071 -18.988  27.889  1.00 33.38           C  
ANISOU 4163  CA  ALA B 161     4735   3706   4241    305    -95   -547       C  
ATOM   4164  C   ALA B 161      74.703 -20.324  27.531  1.00 34.87           C  
ANISOU 4164  C   ALA B 161     4950   3920   4379    334   -118   -501       C  
ATOM   4165  O   ALA B 161      74.957 -21.162  28.397  1.00 42.36           O  
ANISOU 4165  O   ALA B 161     6009   4875   5209    407   -111   -490       O  
ATOM   4166  CB  ALA B 161      75.008 -17.812  27.542  1.00 35.59           C  
ANISOU 4166  CB  ALA B 161     4928   4013   4582    276   -193   -611       C  
ATOM   4167  N   SER B 162      74.944 -20.525  26.239  1.00 34.63           N  
ANISOU 4167  N   SER B 162     4825   3899   4433    283   -142   -471       N  
ATOM   4168  CA  SER B 162      75.529 -21.767  25.750  1.00 35.32           C  
ANISOU 4168  CA  SER B 162     4926   4006   4488    305   -161   -430       C  
ATOM   4169  C   SER B 162      77.006 -21.559  25.435  1.00 37.69           C  
ANISOU 4169  C   SER B 162     5168   4365   4788    321   -274   -472       C  
ATOM   4170  O   SER B 162      77.361 -20.686  24.636  1.00 36.86           O  
ANISOU 4170  O   SER B 162     4961   4272   4773    263   -312   -496       O  
ATOM   4171  CB  SER B 162      74.806 -22.265  24.500  1.00 33.21           C  
ANISOU 4171  CB  SER B 162     4597   3712   4308    241   -108   -376       C  
ATOM   4172  OG  SER B 162      75.419 -23.475  24.041  1.00 37.90           O  
ANISOU 4172  OG  SER B 162     5209   4322   4870    265   -124   -344       O  
ATOM   4173  N   LEU B 163      77.857 -22.386  26.027  1.00 37.31           N  
ANISOU 4173  N   LEU B 163     5184   4349   4643    402   -323   -480       N  
ATOM   4174  CA  LEU B 163      79.288 -22.366  25.734  1.00 37.15           C  
ANISOU 4174  CA  LEU B 163     5096   4390   4627    426   -431   -527       C  
ATOM   4175  C   LEU B 163      79.683 -23.750  25.229  1.00 35.87           C  
ANISOU 4175  C   LEU B 163     4958   4236   4434    464   -429   -476       C  
ATOM   4176  O   LEU B 163      79.711 -24.704  26.007  1.00 36.00           O  
ANISOU 4176  O   LEU B 163     5090   4244   4344    550   -421   -451       O  
ATOM   4177  CB  LEU B 163      80.095 -21.987  26.974  1.00 34.14           C  
ANISOU 4177  CB  LEU B 163     4759   4055   4158    506   -518   -606       C  
ATOM   4178  CG  LEU B 163      81.614 -21.988  26.790  1.00 38.43           C  
ANISOU 4178  CG  LEU B 163     5219   4670   4712    539   -637   -675       C  
ATOM   4179  CD1 LEU B 163      81.996 -21.036  25.671  1.00 37.72           C  
ANISOU 4179  CD1 LEU B 163     4979   4586   4767    432   -646   -706       C  
ATOM   4180  CD2 LEU B 163      82.317 -21.598  28.088  1.00 39.21           C  
ANISOU 4180  CD2 LEU B 163     5360   4819   4720    626   -736   -768       C  
ATOM   4181  N   ASN B 164      79.989 -23.854  23.934  1.00 35.20           N  
ANISOU 4181  N   ASN B 164     4775   4161   4437    405   -432   -459       N  
ATOM   4182  CA  ASN B 164      80.397 -25.128  23.324  1.00 38.67           C  
ANISOU 4182  CA  ASN B 164     5227   4606   4861    435   -430   -418       C  
ATOM   4183  C   ASN B 164      79.382 -26.231  23.593  1.00 39.43           C  
ANISOU 4183  C   ASN B 164     5437   4640   4904    457   -337   -349       C  
ATOM   4184  O   ASN B 164      79.735 -27.397  23.821  1.00 35.87           O  
ANISOU 4184  O   ASN B 164     5063   4180   4385    528   -336   -321       O  
ATOM   4185  CB  ASN B 164      81.785 -25.538  23.807  1.00 38.33           C  
ANISOU 4185  CB  ASN B 164     5184   4622   4757    528   -529   -467       C  
ATOM   4186  CG  ASN B 164      82.794 -24.441  23.587  1.00 38.41           C  
ANISOU 4186  CG  ASN B 164     5069   4691   4836    496   -611   -551       C  
ATOM   4187  OD1 ASN B 164      82.788 -23.802  22.537  1.00 40.34           O  
ANISOU 4187  OD1 ASN B 164     5214   4931   5183    404   -588   -551       O  
ATOM   4188  ND2 ASN B 164      83.633 -24.182  24.583  1.00 36.96           N  
ANISOU 4188  ND2 ASN B 164     4892   4557   4595    572   -703   -627       N  
ATOM   4189  N   GLY B 165      78.106 -25.863  23.556  1.00 40.13           N  
ANISOU 4189  N   GLY B 165     5536   4680   5033    395   -254   -324       N  
ATOM   4190  CA  GLY B 165      77.037 -26.809  23.788  1.00 43.16           C  
ANISOU 4190  CA  GLY B 165     6010   4997   5390    395   -149   -269       C  
ATOM   4191  C   GLY B 165      76.692 -27.037  25.236  1.00 44.97           C  
ANISOU 4191  C   GLY B 165     6378   5195   5512    464   -104   -262       C  
ATOM   4192  O   GLY B 165      75.762 -27.801  25.518  1.00 41.59           O  
ANISOU 4192  O   GLY B 165     6034   4702   5067    459      5   -217       O  
ATOM   4193  N   VAL B 166      77.404 -26.405  26.160  1.00 35.81           N  
ANISOU 4193  N   VAL B 166     5247   4078   4280    529   -180   -308       N  
ATOM   4194  CA  VAL B 166      77.122 -26.514  27.587  1.00 36.91           C  
ANISOU 4194  CA  VAL B 166     5532   4196   4298    607   -145   -306       C  
ATOM   4195  C   VAL B 166      76.348 -25.277  28.004  1.00 39.05           C  
ANISOU 4195  C   VAL B 166     5774   4458   4604    557   -113   -342       C  
ATOM   4196  O   VAL B 166      76.866 -24.157  27.914  1.00 37.07           O  
ANISOU 4196  O   VAL B 166     5435   4254   4395    536   -197   -405       O  
ATOM   4197  CB  VAL B 166      78.417 -26.658  28.404  1.00 34.26           C  
ANISOU 4197  CB  VAL B 166     5255   3918   3844    728   -264   -345       C  
ATOM   4198  CG1 VAL B 166      78.107 -26.802  29.898  1.00 37.75           C  
ANISOU 4198  CG1 VAL B 166     5871   4337   4136    823   -228   -339       C  
ATOM   4199  CG2 VAL B 166      79.225 -27.834  27.895  1.00 39.82           C  
ANISOU 4199  CG2 VAL B 166     5971   4632   4528    783   -301   -314       C  
ATOM   4200  N   THR B 167      75.108 -25.464  28.462  1.00 36.65           N  
ANISOU 4200  N   THR B 167     5544   4090   4293    535     16   -308       N  
ATOM   4201  CA  THR B 167      74.331 -24.333  28.952  1.00 42.92           C  
ANISOU 4201  CA  THR B 167     6319   4872   5115    499     56   -345       C  
ATOM   4202  C   THR B 167      74.679 -24.088  30.413  1.00 43.72           C  
ANISOU 4202  C   THR B 167     6552   4989   5072    596     34   -379       C  
ATOM   4203  O   THR B 167      74.629 -25.006  31.235  1.00 40.38           O  
ANISOU 4203  O   THR B 167     6281   4536   4524    673     88   -339       O  
ATOM   4204  CB  THR B 167      72.835 -24.581  28.780  1.00 43.72           C  
ANISOU 4204  CB  THR B 167     6422   4904   5286    432    206   -308       C  
ATOM   4205  OG1 THR B 167      72.547 -24.681  27.382  1.00 43.27           O  
ANISOU 4205  OG1 THR B 167     6233   4845   5361    348    201   -292       O  
ATOM   4206  CG2 THR B 167      72.040 -23.418  29.368  1.00 41.42           C  
ANISOU 4206  CG2 THR B 167     6116   4600   5021    409    250   -350       C  
ATOM   4207  N   LEU B 168      75.060 -22.855  30.733  1.00 37.06           N  
ANISOU 4207  N   LEU B 168     5658   4187   4237    595    -47   -454       N  
ATOM   4208  CA  LEU B 168      75.598 -22.592  32.059  1.00 38.20           C  
ANISOU 4208  CA  LEU B 168     5917   4363   4236    696   -101   -505       C  
ATOM   4209  C   LEU B 168      75.380 -21.132  32.420  1.00 39.05           C  
ANISOU 4209  C   LEU B 168     5971   4481   4386    661   -124   -585       C  
ATOM   4210  O   LEU B 168      75.202 -20.276  31.551  1.00 39.73           O  
ANISOU 4210  O   LEU B 168     5918   4564   4614    571   -136   -607       O  
ATOM   4211  CB  LEU B 168      77.087 -22.950  32.129  1.00 41.41           C  
ANISOU 4211  CB  LEU B 168     6322   4839   4572    778   -252   -539       C  
ATOM   4212  CG  LEU B 168      78.038 -22.271  31.136  1.00 44.55           C  
ANISOU 4212  CG  LEU B 168     6542   5293   5092    720   -370   -597       C  
ATOM   4213  CD1 LEU B 168      78.593 -20.989  31.711  1.00 46.01           C  
ANISOU 4213  CD1 LEU B 168     6681   5523   5278    725   -466   -707       C  
ATOM   4214  CD2 LEU B 168      79.188 -23.224  30.756  1.00 40.86           C  
ANISOU 4214  CD2 LEU B 168     6060   4872   4593    781   -460   -586       C  
ATOM   4215  N   ILE B 169      75.376 -20.868  33.724  1.00 40.15           N  
ANISOU 4215  N   ILE B 169     6235   4627   4393    740   -124   -627       N  
ATOM   4216  CA  ILE B 169      75.424 -19.516  34.258  1.00 45.06           C  
ANISOU 4216  CA  ILE B 169     6827   5267   5027    730   -170   -724       C  
ATOM   4217  C   ILE B 169      76.879 -19.222  34.587  1.00 46.17           C  
ANISOU 4217  C   ILE B 169     6946   5488   5109    794   -345   -813       C  
ATOM   4218  O   ILE B 169      77.477 -19.881  35.446  1.00 44.06           O  
ANISOU 4218  O   ILE B 169     6801   5258   4682    910   -402   -822       O  
ATOM   4219  CB  ILE B 169      74.526 -19.361  35.491  1.00 46.36           C  
ANISOU 4219  CB  ILE B 169     7139   5394   5080    778    -63   -730       C  
ATOM   4220  CG1 ILE B 169      73.077 -19.702  35.122  1.00 44.27           C  
ANISOU 4220  CG1 ILE B 169     6873   5051   4895    709    118   -651       C  
ATOM   4221  CG2 ILE B 169      74.648 -17.943  36.058  1.00 42.52           C  
ANISOU 4221  CG2 ILE B 169     6623   4926   4605    773   -119   -842       C  
ATOM   4222  CD1 ILE B 169      72.116 -19.644  36.279  1.00 51.20           C  
ANISOU 4222  CD1 ILE B 169     7892   5884   5676    748    254   -650       C  
ATOM   4223  N   GLY B 170      77.455 -18.247  33.892  1.00 45.23           N  
ANISOU 4223  N   GLY B 170     6671   5394   5120    721   -429   -882       N  
ATOM   4224  CA  GLY B 170      78.900 -18.088  33.914  1.00 45.93           C  
ANISOU 4224  CA  GLY B 170     6695   5559   5197    759   -590   -968       C  
ATOM   4225  C   GLY B 170      79.391 -17.508  35.229  1.00 51.12           C  
ANISOU 4225  C   GLY B 170     7430   6261   5732    844   -679  -1082       C  
ATOM   4226  O   GLY B 170      78.782 -16.602  35.804  1.00 45.08           O  
ANISOU 4226  O   GLY B 170     6697   5467   4966    824   -636  -1131       O  
ATOM   4227  N   GLU B 171      80.514 -18.049  35.706  1.00 44.84           N  
ANISOU 4227  N   GLU B 171     6664   5541   4831    948   -811  -1132       N  
ATOM   4228  CA  GLU B 171      81.264 -17.501  36.830  1.00 48.77           C  
ANISOU 4228  CA  GLU B 171     7205   6104   5221   1036   -942  -1267       C  
ATOM   4229  C   GLU B 171      82.633 -16.993  36.419  1.00 52.54           C  
ANISOU 4229  C   GLU B 171     7512   6654   5795   1013  -1101  -1389       C  
ATOM   4230  O   GLU B 171      83.073 -15.953  36.907  1.00 50.74           O  
ANISOU 4230  O   GLU B 171     7233   6455   5590    999  -1183  -1527       O  
ATOM   4231  CB  GLU B 171      81.431 -18.553  37.935  1.00 49.57           C  
ANISOU 4231  CB  GLU B 171     7504   6240   5091   1206   -976  -1238       C  
ATOM   4232  CG  GLU B 171      80.155 -19.294  38.299  1.00 51.74           C  
ANISOU 4232  CG  GLU B 171     7955   6434   5268   1232   -799  -1104       C  
ATOM   4233  CD  GLU B 171      80.373 -20.328  39.393  1.00 66.62           C  
ANISOU 4233  CD  GLU B 171    10056   8342   6914   1406   -824  -1068       C  
ATOM   4234  OE1 GLU B 171      81.528 -20.477  39.847  1.00 67.94           O  
ANISOU 4234  OE1 GLU B 171    10231   8595   6989   1518   -996  -1150       O  
ATOM   4235  OE2 GLU B 171      79.395 -20.993  39.798  1.00 65.14           O  
ANISOU 4235  OE2 GLU B 171    10032   8084   6633   1435   -669   -962       O  
ATOM   4236  N   ALA B 172      83.319 -17.708  35.527  1.00 48.06           N  
ANISOU 4236  N   ALA B 172     6852   6115   5293   1003  -1139  -1348       N  
ATOM   4237  CA  ALA B 172      84.570 -17.233  34.955  1.00 50.08           C  
ANISOU 4237  CA  ALA B 172     6923   6431   5674    958  -1262  -1458       C  
ATOM   4238  C   ALA B 172      84.349 -16.409  33.696  1.00 48.67           C  
ANISOU 4238  C   ALA B 172     6587   6196   5711    788  -1182  -1442       C  
ATOM   4239  O   ALA B 172      85.281 -15.744  33.234  1.00 50.33           O  
ANISOU 4239  O   ALA B 172     6640   6436   6046    723  -1254  -1544       O  
ATOM   4240  CB  ALA B 172      85.499 -18.423  34.646  1.00 48.40           C  
ANISOU 4240  CB  ALA B 172     6688   6281   5422   1046  -1344  -1432       C  
ATOM   4241  N   VAL B 173      83.137 -16.444  33.137  1.00 44.82           N  
ANISOU 4241  N   VAL B 173     6139   5623   5266    718  -1032  -1320       N  
ATOM   4242  CA  VAL B 173      82.772 -15.721  31.927  1.00 46.88           C  
ANISOU 4242  CA  VAL B 173     6280   5823   5709    574   -949  -1285       C  
ATOM   4243  C   VAL B 173      81.383 -15.140  32.142  1.00 46.77           C  
ANISOU 4243  C   VAL B 173     6341   5729   5701    533   -829  -1236       C  
ATOM   4244  O   VAL B 173      80.609 -15.619  32.970  1.00 44.34           O  
ANISOU 4244  O   VAL B 173     6174   5407   5266    605   -778  -1192       O  
ATOM   4245  CB  VAL B 173      82.765 -16.625  30.672  1.00 47.03           C  
ANISOU 4245  CB  VAL B 173     6247   5832   5790    537   -898  -1170       C  
ATOM   4246  CG1 VAL B 173      84.145 -17.180  30.399  1.00 50.45           C  
ANISOU 4246  CG1 VAL B 173     6595   6343   6232    577  -1008  -1223       C  
ATOM   4247  CG2 VAL B 173      81.783 -17.772  30.855  1.00 39.56           C  
ANISOU 4247  CG2 VAL B 173     5439   4854   4736    596   -810  -1045       C  
ATOM   4248  N   LYS B 174      81.057 -14.118  31.361  1.00 41.68           N  
ANISOU 4248  N   LYS B 174     5603   5026   5207    420   -774  -1239       N  
ATOM   4249  CA  LYS B 174      79.750 -13.474  31.441  1.00 40.90           C  
ANISOU 4249  CA  LYS B 174     5553   4850   5138    381   -664  -1198       C  
ATOM   4250  C   LYS B 174      78.787 -14.147  30.472  1.00 37.15           C  
ANISOU 4250  C   LYS B 174     5079   4330   4705    346   -557  -1057       C  
ATOM   4251  O   LYS B 174      79.088 -14.265  29.280  1.00 40.65           O  
ANISOU 4251  O   LYS B 174     5429   4769   5246    285   -554  -1012       O  
ATOM   4252  CB  LYS B 174      79.877 -11.987  31.110  1.00 45.58           C  
ANISOU 4252  CB  LYS B 174     6054   5394   5871    289   -663  -1275       C  
ATOM   4253  CG  LYS B 174      78.723 -11.133  31.580  1.00 66.06           C  
ANISOU 4253  CG  LYS B 174     8706   7916   8476    276   -580  -1279       C  
ATOM   4254  CD  LYS B 174      79.195  -9.688  31.753  1.00 74.76           C  
ANISOU 4254  CD  LYS B 174     9747   8984   9674    218   -616  -1403       C  
ATOM   4255  CE  LYS B 174      78.176  -8.847  32.498  1.00 84.37           C  
ANISOU 4255  CE  LYS B 174    11038  10139  10878    228   -549  -1434       C  
ATOM   4256  NZ  LYS B 174      76.877  -8.791  31.780  1.00 86.45           N  
ANISOU 4256  NZ  LYS B 174    11307  10331  11209    198   -428  -1317       N  
ATOM   4257  N   THR B 175      77.634 -14.596  30.987  1.00 37.68           N  
ANISOU 4257  N   THR B 175     5251   4366   4699    384   -466   -995       N  
ATOM   4258  CA  THR B 175      76.584 -15.214  30.173  1.00 33.30           C  
ANISOU 4258  CA  THR B 175     4694   3768   4190    350   -362   -880       C  
ATOM   4259  C   THR B 175      75.285 -14.417  30.182  1.00 35.47           C  
ANISOU 4259  C   THR B 175     4972   3976   4530    312   -263   -866       C  
ATOM   4260  O   THR B 175      74.333 -14.790  29.492  1.00 38.33           O  
ANISOU 4260  O   THR B 175     5313   4302   4946    280   -182   -786       O  
ATOM   4261  CB  THR B 175      76.298 -16.650  30.644  1.00 34.52           C  
ANISOU 4261  CB  THR B 175     4958   3938   4219    423   -321   -812       C  
ATOM   4262  OG1 THR B 175      75.971 -16.647  32.035  1.00 38.75           O  
ANISOU 4262  OG1 THR B 175     5625   4473   4626    498   -297   -847       O  
ATOM   4263  CG2 THR B 175      77.514 -17.545  30.430  1.00 35.65           C  
ANISOU 4263  CG2 THR B 175     5091   4142   4312    467   -415   -810       C  
ATOM   4264  N   GLN B 176      75.232 -13.319  30.925  1.00 37.52           N  
ANISOU 4264  N   GLN B 176     5248   4216   4791    315   -273   -950       N  
ATOM   4265  CA  GLN B 176      74.040 -12.490  31.045  1.00 36.60           C  
ANISOU 4265  CA  GLN B 176     5136   4034   4736    291   -183   -950       C  
ATOM   4266  C   GLN B 176      74.181 -11.305  30.094  1.00 42.50           C  
ANISOU 4266  C   GLN B 176     5776   4738   5635    216   -202   -969       C  
ATOM   4267  O   GLN B 176      75.079 -10.475  30.272  1.00 40.59           O  
ANISOU 4267  O   GLN B 176     5503   4500   5420    196   -273  -1055       O  
ATOM   4268  CB  GLN B 176      73.905 -12.039  32.499  1.00 43.88           C  
ANISOU 4268  CB  GLN B 176     6159   4956   5555    350   -175  -1034       C  
ATOM   4269  CG  GLN B 176      72.995 -10.872  32.743  1.00 58.50           C  
ANISOU 4269  CG  GLN B 176     8006   6744   7478    328   -107  -1073       C  
ATOM   4270  CD  GLN B 176      71.562 -11.302  32.813  1.00 48.14           C  
ANISOU 4270  CD  GLN B 176     6729   5393   6168    339     25  -1003       C  
ATOM   4271  OE1 GLN B 176      71.110 -11.852  33.826  1.00 51.56           O  
ANISOU 4271  OE1 GLN B 176     7272   5835   6485    396     89  -1004       O  
ATOM   4272  NE2 GLN B 176      70.827 -11.059  31.734  1.00 50.84           N  
ANISOU 4272  NE2 GLN B 176     6978   5694   6645    286     70   -946       N  
ATOM   4273  N   PHE B 177      73.316 -11.229  29.078  1.00 35.76           N  
ANISOU 4273  N   PHE B 177     4867   3842   4880    175   -141   -893       N  
ATOM   4274  CA  PHE B 177      73.397 -10.176  28.069  1.00 33.86           C  
ANISOU 4274  CA  PHE B 177     4543   3551   4772    115   -151   -890       C  
ATOM   4275  C   PHE B 177      72.203  -9.228  28.133  1.00 41.81           C  
ANISOU 4275  C   PHE B 177     5550   4485   5850    115    -79   -892       C  
ATOM   4276  O   PHE B 177      71.113  -9.608  28.556  1.00 34.09           O  
ANISOU 4276  O   PHE B 177     4607   3501   4846    148     -7   -869       O  
ATOM   4277  CB  PHE B 177      73.464 -10.777  26.660  1.00 33.49           C  
ANISOU 4277  CB  PHE B 177     4430   3514   4780     79   -155   -799       C  
ATOM   4278  CG  PHE B 177      74.505 -11.851  26.512  1.00 40.04           C  
ANISOU 4278  CG  PHE B 177     5256   4413   5545     86   -213   -787       C  
ATOM   4279  CD1 PHE B 177      75.824 -11.593  26.833  1.00 42.54           C  
ANISOU 4279  CD1 PHE B 177     5555   4762   5844     79   -292   -861       C  
ATOM   4280  CD2 PHE B 177      74.165 -13.110  26.041  1.00 38.64           C  
ANISOU 4280  CD2 PHE B 177     5085   4264   5331    100   -190   -709       C  
ATOM   4281  CE1 PHE B 177      76.790 -12.590  26.701  1.00 40.04           C  
ANISOU 4281  CE1 PHE B 177     5229   4513   5473     97   -349   -855       C  
ATOM   4282  CE2 PHE B 177      75.123 -14.106  25.906  1.00 40.77           C  
ANISOU 4282  CE2 PHE B 177     5356   4592   5543    114   -241   -699       C  
ATOM   4283  CZ  PHE B 177      76.432 -13.842  26.234  1.00 40.81           C  
ANISOU 4283  CZ  PHE B 177     5342   4634   5529    117   -322   -769       C  
ATOM   4284  N   ASN B 178      72.429  -7.980  27.714  1.00 33.97           N  
ANISOU 4284  N   ASN B 178     4519   3434   4956     77    -92   -925       N  
ATOM   4285  CA  ASN B 178      71.343  -7.115  27.269  1.00 33.72           C  
ANISOU 4285  CA  ASN B 178     4466   3326   5019     77    -34   -899       C  
ATOM   4286  C   ASN B 178      70.953  -7.513  25.853  1.00 37.05           C  
ANISOU 4286  C   ASN B 178     4830   3745   5501     60    -28   -796       C  
ATOM   4287  O   ASN B 178      71.818  -7.845  25.036  1.00 35.42           O  
ANISOU 4287  O   ASN B 178     4593   3564   5302     24    -72   -763       O  
ATOM   4288  CB  ASN B 178      71.779  -5.643  27.274  1.00 34.30           C  
ANISOU 4288  CB  ASN B 178     4532   3323   5176     46    -46   -964       C  
ATOM   4289  CG  ASN B 178      71.839  -5.046  28.659  1.00 39.04           C  
ANISOU 4289  CG  ASN B 178     5190   3911   5732     70    -42  -1076       C  
ATOM   4290  OD1 ASN B 178      71.145  -5.482  29.579  1.00 41.05           O  
ANISOU 4290  OD1 ASN B 178     5498   4192   5909    120     -2  -1092       O  
ATOM   4291  ND2 ASN B 178      72.653  -4.009  28.807  1.00 44.80           N  
ANISOU 4291  ND2 ASN B 178     5913   4595   6514     30    -75  -1158       N  
ATOM   4292  N   TYR B 179      69.652  -7.454  25.554  1.00 36.47           N  
ANISOU 4292  N   TYR B 179     4740   3643   5473     88     26   -755       N  
ATOM   4293  CA  TYR B 179      69.118  -7.746  24.226  1.00 33.60           C  
ANISOU 4293  CA  TYR B 179     4322   3278   5165     86     23   -670       C  
ATOM   4294  C   TYR B 179      68.472  -6.510  23.619  1.00 38.64           C  
ANISOU 4294  C   TYR B 179     4942   3836   5905    102     37   -656       C  
ATOM   4295  O   TYR B 179      67.791  -5.755  24.316  1.00 38.65           O  
ANISOU 4295  O   TYR B 179     4958   3790   5937    133     77   -703       O  
ATOM   4296  CB  TYR B 179      68.064  -8.837  24.285  1.00 33.14           C  
ANISOU 4296  CB  TYR B 179     4246   3262   5083    112     66   -637       C  
ATOM   4297  CG  TYR B 179      68.639 -10.221  24.339  1.00 35.97           C  
ANISOU 4297  CG  TYR B 179     4619   3691   5358     97     50   -613       C  
ATOM   4298  CD1 TYR B 179      69.183 -10.731  25.518  1.00 35.16           C  
ANISOU 4298  CD1 TYR B 179     4581   3620   5158    108     57   -657       C  
ATOM   4299  CD2 TYR B 179      68.639 -11.022  23.206  1.00 41.36           C  
ANISOU 4299  CD2 TYR B 179     5259   4405   6052     81     26   -549       C  
ATOM   4300  CE1 TYR B 179      69.704 -12.035  25.557  1.00 37.39           C  
ANISOU 4300  CE1 TYR B 179     4887   3960   5361    106     43   -629       C  
ATOM   4301  CE2 TYR B 179      69.156 -12.303  23.232  1.00 42.30           C  
ANISOU 4301  CE2 TYR B 179     5394   4579   6099     70     15   -528       C  
ATOM   4302  CZ  TYR B 179      69.694 -12.799  24.401  1.00 39.44           C  
ANISOU 4302  CZ  TYR B 179     5097   4242   5645     85     25   -565       C  
ATOM   4303  OH  TYR B 179      70.182 -14.081  24.400  1.00 43.20           O  
ANISOU 4303  OH  TYR B 179     5597   4764   6051     86     15   -538       O  
ATOM   4304  N   TYR B 180      68.648  -6.348  22.306  1.00 35.25           N  
ANISOU 4304  N   TYR B 180     4485   3390   5519     90      7   -589       N  
ATOM   4305  CA  TYR B 180      68.015  -5.281  21.540  1.00 33.29           C  
ANISOU 4305  CA  TYR B 180     4230   3065   5355    121     13   -556       C  
ATOM   4306  C   TYR B 180      67.548  -5.848  20.203  1.00 37.51           C  
ANISOU 4306  C   TYR B 180     4726   3628   5898    142    -16   -472       C  
ATOM   4307  O   TYR B 180      68.151  -6.786  19.672  1.00 37.76           O  
ANISOU 4307  O   TYR B 180     4746   3720   5880    110    -44   -438       O  
ATOM   4308  CB  TYR B 180      68.978  -4.120  21.292  1.00 34.45           C  
ANISOU 4308  CB  TYR B 180     4414   3132   5545     84      8   -568       C  
ATOM   4309  CG  TYR B 180      69.759  -3.662  22.511  1.00 37.04           C  
ANISOU 4309  CG  TYR B 180     4772   3443   5859     48     18   -665       C  
ATOM   4310  CD1 TYR B 180      70.919  -4.322  22.908  1.00 37.81           C  
ANISOU 4310  CD1 TYR B 180     4867   3604   5895     -1    -15   -702       C  
ATOM   4311  CD2 TYR B 180      69.362  -2.538  23.238  1.00 38.52           C  
ANISOU 4311  CD2 TYR B 180     4990   3552   6096     69     52   -728       C  
ATOM   4312  CE1 TYR B 180      71.647  -3.898  24.012  1.00 36.99           C  
ANISOU 4312  CE1 TYR B 180     4786   3494   5774    -26    -23   -803       C  
ATOM   4313  CE2 TYR B 180      70.094  -2.094  24.344  1.00 35.22           C  
ANISOU 4313  CE2 TYR B 180     4600   3120   5661     37     52   -830       C  
ATOM   4314  CZ  TYR B 180      71.238  -2.801  24.730  1.00 35.78           C  
ANISOU 4314  CZ  TYR B 180     4664   3265   5665    -10      9   -870       C  
ATOM   4315  OH  TYR B 180      71.982  -2.397  25.821  1.00 38.91           O  
ANISOU 4315  OH  TYR B 180     5085   3660   6040    -33     -8   -983       O  
ATOM   4316  N   LYS B 181      66.481  -5.269  19.648  1.00 37.31           N  
ANISOU 4316  N   LYS B 181     4681   3561   5932    203    -15   -445       N  
ATOM   4317  CA  LYS B 181      65.944  -5.779  18.388  1.00 33.41           C  
ANISOU 4317  CA  LYS B 181     4151   3102   5441    236    -56   -377       C  
ATOM   4318  C   LYS B 181      65.403  -4.636  17.531  1.00 38.03           C  
ANISOU 4318  C   LYS B 181     4754   3609   6085    302    -73   -334       C  
ATOM   4319  O   LYS B 181      64.847  -3.659  18.049  1.00 41.29           O  
ANISOU 4319  O   LYS B 181     5179   3954   6556    344    -46   -366       O  
ATOM   4320  CB  LYS B 181      64.854  -6.822  18.657  1.00 37.56           C  
ANISOU 4320  CB  LYS B 181     4607   3698   5965    260    -48   -400       C  
ATOM   4321  CG  LYS B 181      64.161  -7.386  17.422  1.00 38.32           C  
ANISOU 4321  CG  LYS B 181     4650   3838   6072    298    -99   -353       C  
ATOM   4322  CD  LYS B 181      63.116  -8.425  17.858  1.00 36.59           C  
ANISOU 4322  CD  LYS B 181     4353   3681   5870    304    -74   -396       C  
ATOM   4323  CE  LYS B 181      62.081  -8.682  16.779  1.00 45.29           C  
ANISOU 4323  CE  LYS B 181     5380   4815   7014    360   -129   -382       C  
ATOM   4324  NZ  LYS B 181      62.518  -9.684  15.787  1.00 46.60           N  
ANISOU 4324  NZ  LYS B 181     5539   5041   7127    332   -180   -342       N  
ATOM   4325  N   LYS B 182      65.595  -4.756  16.216  1.00 36.71           N  
ANISOU 4325  N   LYS B 182     4601   3450   5899    317   -117   -260       N  
ATOM   4326  CA  LYS B 182      65.115  -3.782  15.241  1.00 38.78           C  
ANISOU 4326  CA  LYS B 182     4898   3642   6195    395   -142   -202       C  
ATOM   4327  C   LYS B 182      64.294  -4.492  14.176  1.00 39.59           C  
ANISOU 4327  C   LYS B 182     4953   3813   6275    458   -209   -162       C  
ATOM   4328  O   LYS B 182      64.673  -5.572  13.714  1.00 36.70           O  
ANISOU 4328  O   LYS B 182     4566   3526   5854    417   -234   -146       O  
ATOM   4329  CB  LYS B 182      66.272  -3.054  14.545  1.00 39.97           C  
ANISOU 4329  CB  LYS B 182     5139   3717   6330    358   -125   -143       C  
ATOM   4330  CG  LYS B 182      66.969  -2.010  15.368  1.00 53.46           C  
ANISOU 4330  CG  LYS B 182     6898   5330   8083    310    -65   -184       C  
ATOM   4331  CD  LYS B 182      68.224  -1.507  14.653  1.00 46.96           C  
ANISOU 4331  CD  LYS B 182     6149   4442   7252    250    -34   -134       C  
ATOM   4332  CE  LYS B 182      67.874  -0.630  13.462  1.00 42.30           C  
ANISOU 4332  CE  LYS B 182     5638   3762   6672    326    -34    -41       C  
ATOM   4333  NZ  LYS B 182      69.074   0.092  12.950  1.00 41.18           N  
ANISOU 4333  NZ  LYS B 182     5580   3524   6540    259     29      0       N  
ATOM   4334  N   VAL B 183      63.189  -3.876  13.762  1.00 39.64           N  
ANISOU 4334  N   VAL B 183     4944   3790   6327    562   -244   -153       N  
ATOM   4335  CA  VAL B 183      62.342  -4.418  12.707  1.00 39.98           C  
ANISOU 4335  CA  VAL B 183     4938   3899   6355    638   -324   -128       C  
ATOM   4336  C   VAL B 183      62.050  -3.301  11.719  1.00 44.70           C  
ANISOU 4336  C   VAL B 183     5609   4418   6955    746   -366    -58       C  
ATOM   4337  O   VAL B 183      61.505  -2.260  12.104  1.00 42.73           O  
ANISOU 4337  O   VAL B 183     5376   4090   6769    813   -350    -71       O  
ATOM   4338  CB  VAL B 183      61.035  -5.006  13.267  1.00 46.26           C  
ANISOU 4338  CB  VAL B 183     5607   4759   7210    674   -337   -208       C  
ATOM   4339  CG1 VAL B 183      60.108  -5.429  12.134  1.00 46.51           C  
ANISOU 4339  CG1 VAL B 183     5577   4855   7240    761   -434   -198       C  
ATOM   4340  CG2 VAL B 183      61.346  -6.183  14.182  1.00 42.70           C  
ANISOU 4340  CG2 VAL B 183     5106   4376   6743    570   -285   -263       C  
ATOM   4341  N   ASP B 184      62.405  -3.517  10.451  1.00 45.51           N  
ANISOU 4341  N   ASP B 184     5535   4129   7628   -423   -946    615       N  
ATOM   4342  CA  ASP B 184      62.162  -2.545   9.380  1.00 48.70           C  
ANISOU 4342  CA  ASP B 184     5797   4526   8179   -519  -1038    833       C  
ATOM   4343  C   ASP B 184      62.709  -1.168   9.739  1.00 51.10           C  
ANISOU 4343  C   ASP B 184     5756   4894   8767   -336   -737    743       C  
ATOM   4344  O   ASP B 184      62.065  -0.141   9.507  1.00 47.51           O  
ANISOU 4344  O   ASP B 184     4970   4416   8665   -390   -708    969       O  
ATOM   4345  CB  ASP B 184      60.675  -2.456   9.031  1.00 57.52           C  
ANISOU 4345  CB  ASP B 184     6698   5581   9578   -799  -1311   1262       C  
ATOM   4346  CG  ASP B 184      60.114  -3.775   8.526  1.00 74.77           C  
ANISOU 4346  CG  ASP B 184     9285   7672  11452  -1077  -1713   1406       C  
ATOM   4347  OD1 ASP B 184      58.957  -4.093   8.868  1.00 78.33           O  
ANISOU 4347  OD1 ASP B 184     9528   8087  12148  -1272  -1906   1727       O  
ATOM   4348  OD2 ASP B 184      60.837  -4.500   7.804  1.00 75.79           O  
ANISOU 4348  OD2 ASP B 184     9965   7739  11092  -1094  -1816   1224       O  
ATOM   4349  N   GLY B 185      63.907  -1.155  10.316  1.00 46.16           N  
ANISOU 4349  N   GLY B 185     5212   4332   7996   -136   -526    454       N  
ATOM   4350  CA  GLY B 185      64.629   0.059  10.638  1.00 46.54           C  
ANISOU 4350  CA  GLY B 185     5032   4421   8232    -11   -304    359       C  
ATOM   4351  C   GLY B 185      64.272   0.699  11.962  1.00 48.02           C  
ANISOU 4351  C   GLY B 185     5016   4546   8684     22    -86    281       C  
ATOM   4352  O   GLY B 185      64.882   1.711  12.319  1.00 49.27           O  
ANISOU 4352  O   GLY B 185     5074   4689   8955     81     77    187       O  
ATOM   4353  N   VAL B 186      63.328   0.138  12.707  1.00 44.14           N  
ANISOU 4353  N   VAL B 186     4509   3992   8271    -20    -67    329       N  
ATOM   4354  CA  VAL B 186      62.826   0.741  13.935  1.00 50.06           C  
ANISOU 4354  CA  VAL B 186     5140   4626   9256     37    212    292       C  
ATOM   4355  C   VAL B 186      63.173  -0.166  15.104  1.00 46.45           C  
ANISOU 4355  C   VAL B 186     4892   4190   8567     69    260     64       C  
ATOM   4356  O   VAL B 186      62.900  -1.375  15.067  1.00 45.56           O  
ANISOU 4356  O   VAL B 186     4884   4130   8296     28     91     91       O  
ATOM   4357  CB  VAL B 186      61.308   0.975  13.862  1.00 52.78           C  
ANISOU 4357  CB  VAL B 186     5221   4860   9973     -3    273    651       C  
ATOM   4358  CG1 VAL B 186      60.788   1.541  15.175  1.00 54.22           C  
ANISOU 4358  CG1 VAL B 186     5358   4869  10373    123    676    629       C  
ATOM   4359  CG2 VAL B 186      60.983   1.889  12.696  1.00 56.34           C  
ANISOU 4359  CG2 VAL B 186     5432   5300  10674    -60    202    926       C  
ATOM   4360  N   VAL B 187      63.777   0.414  16.142  1.00 41.75           N  
ANISOU 4360  N   VAL B 187     4394   3537   7932    111    464   -148       N  
ATOM   4361  CA  VAL B 187      64.037  -0.352  17.351  1.00 39.08           C  
ANISOU 4361  CA  VAL B 187     4256   3208   7385    110    509   -334       C  
ATOM   4362  C   VAL B 187      62.709  -0.764  17.965  1.00 45.30           C  
ANISOU 4362  C   VAL B 187     4990   3889   8333    142    652   -198       C  
ATOM   4363  O   VAL B 187      61.753   0.020  18.026  1.00 49.26           O  
ANISOU 4363  O   VAL B 187     5339   4233   9146    198    886     -8       O  
ATOM   4364  CB  VAL B 187      64.913   0.448  18.328  1.00 44.91           C  
ANISOU 4364  CB  VAL B 187     5175   3870   8018     70    646   -546       C  
ATOM   4365  CG1 VAL B 187      65.053  -0.294  19.646  1.00 48.29           C  
ANISOU 4365  CG1 VAL B 187     5833   4290   8227     32    686   -705       C  
ATOM   4366  CG2 VAL B 187      66.289   0.689  17.716  1.00 39.99           C  
ANISOU 4366  CG2 VAL B 187     4533   3390   7271     26    454   -580       C  
ATOM   4367  N  AGLN B 188      62.626  -2.010  18.424  0.66 41.45           N  
ANISOU 4367  N  AGLN B 188     4603   3479   7668    126    539   -244       N  
ATOM   4368  N  BGLN B 188      62.642  -2.018  18.378  0.34 41.13           N  
ANISOU 4368  N  BGLN B 188     4559   3442   7625    125    530   -242       N  
ATOM   4369  CA AGLN B 188      61.362  -2.588  18.870  0.66 44.87           C  
ANISOU 4369  CA AGLN B 188     4939   3843   8268    147    615    -43       C  
ATOM   4370  CA BGLN B 188      61.444  -2.607  18.938  0.34 44.55           C  
ANISOU 4370  CA BGLN B 188     4918   3806   8202    148    618    -68       C  
ATOM   4371  C  AGLN B 188      61.449  -2.970  20.342  0.66 45.76           C  
ANISOU 4371  C  AGLN B 188     5251   3907   8228    192    812   -227       C  
ATOM   4372  C  BGLN B 188      61.587  -2.693  20.444  0.34 43.94           C  
ANISOU 4372  C  BGLN B 188     5050   3652   7993    198    866   -268       C  
ATOM   4373  O  AGLN B 188      62.359  -3.716  20.740  0.66 45.95           O  
ANISOU 4373  O  AGLN B 188     5461   4051   7948    146    666   -444       O  
ATOM   4374  O  BGLN B 188      62.684  -2.903  20.971  0.34 53.68           O  
ANISOU 4374  O  BGLN B 188     6503   4960   8934    149    796   -529       O  
ATOM   4375  CB AGLN B 188      61.005  -3.833  18.031  0.66 48.17           C  
ANISOU 4375  CB AGLN B 188     5326   4369   8608     48    258    121       C  
ATOM   4376  CB BGLN B 188      61.187  -3.991  18.344  0.34 46.36           C  
ANISOU 4376  CB BGLN B 188     5155   4150   8310     62    284     43       C  
ATOM   4377  CG AGLN B 188      59.503  -4.043  17.837  0.66 52.55           C  
ANISOU 4377  CG AGLN B 188     5628   4849   9490     -7    218    538       C  
ATOM   4378  CG BGLN B 188      60.681  -3.924  16.926  0.34 47.74           C  
ANISOU 4378  CG BGLN B 188     5193   4334   8614    -44     33    318       C  
ATOM   4379  CD AGLN B 188      59.170  -5.284  17.023  0.66 52.42           C  
ANISOU 4379  CD AGLN B 188     5686   4895   9336   -190   -211    704       C  
ATOM   4380  CD BGLN B 188      59.309  -3.297  16.855  0.34 54.55           C  
ANISOU 4380  CD BGLN B 188     5724   5084   9919    -57    148    724       C  
ATOM   4381  OE1AGLN B 188      59.385  -6.416  17.470  0.66 50.53           O  
ANISOU 4381  OE1AGLN B 188     5644   4699   8858   -210   -324    570       O  
ATOM   4382  OE1BGLN B 188      58.465  -3.538  17.718  0.34 58.37           O  
ANISOU 4382  OE1BGLN B 188     6092   5497  10588     -1    323    888       O  
ATOM   4383  NE2AGLN B 188      58.632  -5.076  15.824  0.66 53.35           N  
ANISOU 4383  NE2AGLN B 188     5690   4995   9586   -351   -468   1012       N  
ATOM   4384  NE2BGLN B 188      59.079  -2.475  15.837  0.34 60.91           N  
ANISOU 4384  NE2BGLN B 188     6349   5870  10923   -114     80    939       N  
ATOM   4385  N   GLN B 189      60.476  -2.502  21.132  1.00 45.18           N  
ANISOU 4385  N   GLN B 189     5141   3649   8377    293   1167    -92       N  
ATOM   4386  CA  GLN B 189      60.414  -2.798  22.557  1.00 46.63           C  
ANISOU 4386  CA  GLN B 189     5570   3743   8403    345   1412   -240       C  
ATOM   4387  C   GLN B 189      60.213  -4.295  22.760  1.00 57.26           C  
ANISOU 4387  C   GLN B 189     6879   5245   9633    304   1175   -198       C  
ATOM   4388  O   GLN B 189      59.193  -4.845  22.338  1.00 53.64           O  
ANISOU 4388  O   GLN B 189     6166   4801   9415    314   1091    126       O  
ATOM   4389  CB  GLN B 189      59.266  -2.026  23.191  1.00 54.93           C  
ANISOU 4389  CB  GLN B 189     6591   4525   9756    522   1919    -17       C  
ATOM   4390  CG  GLN B 189      59.101  -2.249  24.684  1.00 61.48           C  
ANISOU 4390  CG  GLN B 189     7754   5205  10400    603   2256   -151       C  
ATOM   4391  CD  GLN B 189      60.169  -1.531  25.484  1.00 72.97           C  
ANISOU 4391  CD  GLN B 189     9721   6529  11475    506   2363   -550       C  
ATOM   4392  OE1 GLN B 189      60.886  -0.684  24.951  1.00 77.28           O  
ANISOU 4392  OE1 GLN B 189    10324   7056  11981    415   2262   -673       O  
ATOM   4393  NE2 GLN B 189      60.287  -1.870  26.766  1.00 71.22           N  
ANISOU 4393  NE2 GLN B 189     9889   6212  10960    489   2532   -725       N  
ATOM   4394  N   LEU B 190      61.169  -4.953  23.410  1.00 42.79           N  
ANISOU 4394  N   LEU B 190     5288   3519   7450    234   1047   -475       N  
ATOM   4395  CA  LEU B 190      60.995  -6.363  23.718  1.00 36.47           C  
ANISOU 4395  CA  LEU B 190     4479   2840   6538    209    866   -444       C  
ATOM   4396  C   LEU B 190      60.030  -6.530  24.894  1.00 42.68           C  
ANISOU 4396  C   LEU B 190     5298   3499   7419    308   1181   -337       C  
ATOM   4397  O   LEU B 190      60.049  -5.728  25.832  1.00 47.53           O  
ANISOU 4397  O   LEU B 190     6144   3944   7973    368   1536   -453       O  
ATOM   4398  CB  LEU B 190      62.349  -7.015  24.034  1.00 42.70           C  
ANISOU 4398  CB  LEU B 190     5468   3786   6968    122    656   -707       C  
ATOM   4399  CG  LEU B 190      63.253  -7.151  22.810  1.00 50.73           C  
ANISOU 4399  CG  LEU B 190     6436   4931   7909     85    384   -728       C  
ATOM   4400  CD1 LEU B 190      64.650  -7.672  23.182  1.00 47.84           C  
ANISOU 4400  CD1 LEU B 190     6203   4706   7266     37    254   -882       C  
ATOM   4401  CD2 LEU B 190      62.600  -8.059  21.765  1.00 43.34           C  
ANISOU 4401  CD2 LEU B 190     5399   4022   7046     81    164   -539       C  
ATOM   4402  N   PRO B 191      59.174  -7.552  24.867  1.00 45.63           N  
ANISOU 4402  N   PRO B 191     5488   3922   7926    319   1072    -94       N  
ATOM   4403  CA  PRO B 191      58.163  -7.694  25.920  1.00 44.95           C  
ANISOU 4403  CA  PRO B 191     5370   3713   7994    450   1414     97       C  
ATOM   4404  C   PRO B 191      58.768  -8.131  27.243  1.00 43.29           C  
ANISOU 4404  C   PRO B 191     5498   3517   7433    445   1529   -194       C  
ATOM   4405  O   PRO B 191      59.817  -8.777  27.296  1.00 45.09           O  
ANISOU 4405  O   PRO B 191     5870   3908   7354    316   1235   -446       O  
ATOM   4406  CB  PRO B 191      57.231  -8.776  25.362  1.00 49.88           C  
ANISOU 4406  CB  PRO B 191     5680   4424   8849    394   1128    472       C  
ATOM   4407  CG  PRO B 191      58.155  -9.629  24.516  1.00 43.13           C  
ANISOU 4407  CG  PRO B 191     4933   3741   7714    217    637    266       C  
ATOM   4408  CD  PRO B 191      59.073  -8.621  23.859  1.00 42.95           C  
ANISOU 4408  CD  PRO B 191     5009   3720   7591    202    637     44       C  
ATOM   4409  N   GLU B 192      58.086  -7.771  28.326  1.00 45.85           N  
ANISOU 4409  N   GLU B 192     5957   3652   7813    596   1991   -114       N  
ATOM   4410  CA  GLU B 192      58.369  -8.385  29.618  1.00 46.88           C  
ANISOU 4410  CA  GLU B 192     6390   3790   7631    581   2091   -298       C  
ATOM   4411  C   GLU B 192      58.137  -9.885  29.517  1.00 48.54           C  
ANISOU 4411  C   GLU B 192     6360   4212   7873    528   1750   -162       C  
ATOM   4412  O   GLU B 192      57.160 -10.332  28.912  1.00 49.39           O  
ANISOU 4412  O   GLU B 192     6104   4340   8323    574   1660    207       O  
ATOM   4413  CB  GLU B 192      57.482  -7.776  30.707  1.00 52.84           C  
ANISOU 4413  CB  GLU B 192     7360   4257   8459    799   2719   -167       C  
ATOM   4414  CG  GLU B 192      57.617  -6.270  30.806  1.00 56.54           C  
ANISOU 4414  CG  GLU B 192     8153   4438   8893    868   3117   -287       C  
ATOM   4415  CD  GLU B 192      59.060  -5.833  31.006  1.00 79.29           C  
ANISOU 4415  CD  GLU B 192    11470   7346  11311    607   2866   -738       C  
ATOM   4416  OE1 GLU B 192      59.715  -6.359  31.933  1.00 83.02           O  
ANISOU 4416  OE1 GLU B 192    12279   7875  11389    450   2745   -962       O  
ATOM   4417  OE2 GLU B 192      59.543  -4.976  30.232  1.00 83.95           O  
ANISOU 4417  OE2 GLU B 192    12038   7910  11950    537   2761   -818       O  
ATOM   4418  N   THR B 193      59.045 -10.672  30.098  1.00 41.94           N  
ANISOU 4418  N   THR B 193     5728   3522   6687    401   1533   -418       N  
ATOM   4419  CA  THR B 193      59.057 -12.101  29.810  1.00 40.46           C  
ANISOU 4419  CA  THR B 193     5353   3525   6495    332   1162   -336       C  
ATOM   4420  C   THR B 193      59.580 -12.896  31.004  1.00 48.07           C  
ANISOU 4420  C   THR B 193     6533   4577   7156    278   1152   -501       C  
ATOM   4421  O   THR B 193      60.388 -12.402  31.797  1.00 41.58           O  
ANISOU 4421  O   THR B 193     6033   3730   6036    197   1252   -743       O  
ATOM   4422  CB  THR B 193      59.905 -12.391  28.549  1.00 42.64           C  
ANISOU 4422  CB  THR B 193     5558   3936   6707    214    750   -431       C  
ATOM   4423  OG1 THR B 193      59.798 -13.771  28.197  1.00 37.75           O  
ANISOU 4423  OG1 THR B 193     4843   3424   6076    161    439   -331       O  
ATOM   4424  CG2 THR B 193      61.382 -12.035  28.773  1.00 45.10           C  
ANISOU 4424  CG2 THR B 193     6104   4328   6702    116    675   -739       C  
ATOM   4425  N   TYR B 194      59.068 -14.119  31.153  1.00 45.62           N  
ANISOU 4425  N   TYR B 194     6055   4354   6922    290   1007   -332       N  
ATOM   4426  CA  TYR B 194      59.751 -15.117  31.960  1.00 45.92           C  
ANISOU 4426  CA  TYR B 194     6226   4533   6688    208    864   -474       C  
ATOM   4427  C   TYR B 194      60.838 -15.778  31.116  1.00 38.36           C  
ANISOU 4427  C   TYR B 194     5242   3729   5605    100    474   -592       C  
ATOM   4428  O   TYR B 194      60.843 -15.674  29.888  1.00 44.47           O  
ANISOU 4428  O   TYR B 194     5909   4488   6500     97    308   -541       O  
ATOM   4429  CB  TYR B 194      58.774 -16.182  32.472  1.00 44.09           C  
ANISOU 4429  CB  TYR B 194     5830   4320   6603    275    880   -227       C  
ATOM   4430  CG  TYR B 194      57.739 -15.683  33.458  1.00 42.73           C  
ANISOU 4430  CG  TYR B 194     5690   3991   6553    438   1347    -49       C  
ATOM   4431  CD1 TYR B 194      58.012 -15.641  34.817  1.00 43.10           C  
ANISOU 4431  CD1 TYR B 194     6061   4008   6308    447   1604   -203       C  
ATOM   4432  CD2 TYR B 194      56.489 -15.258  33.027  1.00 50.67           C  
ANISOU 4432  CD2 TYR B 194     6422   4863   7970    586   1553    323       C  
ATOM   4433  CE1 TYR B 194      57.068 -15.183  35.727  1.00 46.29           C  
ANISOU 4433  CE1 TYR B 194     6583   4218   6787    641   2121    -33       C  
ATOM   4434  CE2 TYR B 194      55.535 -14.801  33.923  1.00 53.65           C  
ANISOU 4434  CE2 TYR B 194     6818   5066   8499    802   2080    559       C  
ATOM   4435  CZ  TYR B 194      55.830 -14.769  35.273  1.00 54.95           C  
ANISOU 4435  CZ  TYR B 194     7376   5172   8331    850   2396    358       C  
ATOM   4436  OH  TYR B 194      54.880 -14.318  36.168  1.00 57.13           O  
ANISOU 4436  OH  TYR B 194     7755   5227   8725   1108   3004    601       O  
ATOM   4437  N   PHE B 195      61.755 -16.478  31.779  1.00 36.23           N  
ANISOU 4437  N   PHE B 195     5083   3592   5093     20    356   -710       N  
ATOM   4438  CA  PHE B 195      62.749 -17.289  31.086  1.00 36.38           C  
ANISOU 4438  CA  PHE B 195     5064   3733   5027    -19     78   -741       C  
ATOM   4439  C   PHE B 195      62.701 -18.726  31.589  1.00 40.59           C  
ANISOU 4439  C   PHE B 195     5560   4349   5513    -16    -39   -662       C  
ATOM   4440  O   PHE B 195      62.549 -18.953  32.789  1.00 42.00           O  
ANISOU 4440  O   PHE B 195     5785   4572   5599    -48     60   -663       O  
ATOM   4441  CB  PHE B 195      64.155 -16.708  31.291  1.00 40.84           C  
ANISOU 4441  CB  PHE B 195     5734   4387   5396   -120     36   -868       C  
ATOM   4442  CG  PHE B 195      64.377 -15.420  30.557  1.00 44.22           C  
ANISOU 4442  CG  PHE B 195     6185   4738   5878   -128     89   -933       C  
ATOM   4443  CD1 PHE B 195      64.241 -15.378  29.177  1.00 38.95           C  
ANISOU 4443  CD1 PHE B 195     5411   4029   5360    -41      8   -882       C  
ATOM   4444  CD2 PHE B 195      64.723 -14.261  31.234  1.00 42.53           C  
ANISOU 4444  CD2 PHE B 195     6153   4468   5537   -246    205  -1042       C  
ATOM   4445  CE1 PHE B 195      64.441 -14.187  28.479  1.00 44.37           C  
ANISOU 4445  CE1 PHE B 195     6095   4654   6110    -45     56   -927       C  
ATOM   4446  CE2 PHE B 195      64.926 -13.073  30.547  1.00 43.10           C  
ANISOU 4446  CE2 PHE B 195     6246   4457   5673   -256    249  -1093       C  
ATOM   4447  CZ  PHE B 195      64.788 -13.043  29.161  1.00 35.46           C  
ANISOU 4447  CZ  PHE B 195     5093   3485   4896   -141    179  -1030       C  
ATOM   4448  N   THR B 196      62.826 -19.689  30.674  1.00 39.12           N  
ANISOU 4448  N   THR B 196     5345   4156   5364     18   -233   -594       N  
ATOM   4449  CA  THR B 196      63.024 -21.076  31.076  1.00 42.63           C  
ANISOU 4449  CA  THR B 196     5796   4660   5742     25   -341   -532       C  
ATOM   4450  C   THR B 196      64.439 -21.254  31.628  1.00 41.85           C  
ANISOU 4450  C   THR B 196     5715   4711   5475      1   -338   -578       C  
ATOM   4451  O   THR B 196      65.326 -20.428  31.400  1.00 37.24           O  
ANISOU 4451  O   THR B 196     5141   4171   4837    -28   -314   -628       O  
ATOM   4452  CB  THR B 196      62.772 -22.042  29.909  1.00 41.81           C  
ANISOU 4452  CB  THR B 196     5779   4431   5677     56   -526   -448       C  
ATOM   4453  OG1 THR B 196      63.515 -21.632  28.749  1.00 39.92           O  
ANISOU 4453  OG1 THR B 196     5658   4131   5378    102   -540   -511       O  
ATOM   4454  CG2 THR B 196      61.273 -22.111  29.561  1.00 35.47           C  
ANISOU 4454  CG2 THR B 196     4913   3499   5065     -4   -632   -282       C  
ATOM   4455  N   GLN B 197      64.642 -22.342  32.374  1.00 39.47           N  
ANISOU 4455  N   GLN B 197     5385   4494   5119     -6   -383   -503       N  
ATOM   4456  CA  GLN B 197      65.861 -22.517  33.155  1.00 41.53           C  
ANISOU 4456  CA  GLN B 197     5601   4922   5259    -76   -401   -451       C  
ATOM   4457  C   GLN B 197      66.876 -23.455  32.502  1.00 41.70           C  
ANISOU 4457  C   GLN B 197     5582   4959   5304     44   -434   -312       C  
ATOM   4458  O   GLN B 197      68.010 -23.549  32.989  1.00 41.53           O  
ANISOU 4458  O   GLN B 197     5447   5082   5249     -4   -451   -166       O  
ATOM   4459  CB  GLN B 197      65.515 -23.022  34.560  1.00 41.88           C  
ANISOU 4459  CB  GLN B 197     5630   5061   5221   -171   -397   -415       C  
ATOM   4460  CG  GLN B 197      64.641 -22.056  35.357  1.00 41.45           C  
ANISOU 4460  CG  GLN B 197     5691   4954   5104   -251   -256   -522       C  
ATOM   4461  CD  GLN B 197      65.406 -20.816  35.808  1.00 54.16           C  
ANISOU 4461  CD  GLN B 197     7455   6590   6532   -424   -233   -612       C  
ATOM   4462  OE1 GLN B 197      66.526 -20.912  36.311  1.00 49.20           O  
ANISOU 4462  OE1 GLN B 197     6825   6099   5770   -587   -375   -531       O  
ATOM   4463  NE2 GLN B 197      64.806 -19.648  35.619  1.00 47.41           N  
ANISOU 4463  NE2 GLN B 197     6736   5590   5688   -409    -71   -733       N  
ATOM   4464  N   SER B 198      66.499 -24.139  31.424  1.00 40.25           N  
ANISOU 4464  N   SER B 198     5519   4603   5172    187   -434   -311       N  
ATOM   4465  CA  SER B 198      67.440 -24.869  30.569  1.00 42.70           C  
ANISOU 4465  CA  SER B 198     5914   4832   5477    363   -356   -192       C  
ATOM   4466  C   SER B 198      68.186 -25.964  31.327  1.00 42.64           C  
ANISOU 4466  C   SER B 198     5794   4924   5481    415   -315      6       C  
ATOM   4467  O   SER B 198      69.361 -26.228  31.061  1.00 45.31           O  
ANISOU 4467  O   SER B 198     6062   5289   5863    551   -184    210       O  
ATOM   4468  CB  SER B 198      68.437 -23.912  29.906  1.00 41.66           C  
ANISOU 4468  CB  SER B 198     5732   4734   5362    419   -267   -150       C  
ATOM   4469  OG  SER B 198      67.784 -22.955  29.097  1.00 42.00           O  
ANISOU 4469  OG  SER B 198     5881   4671   5405    388   -295   -313       O  
ATOM   4470  N   ARG B 199      67.509 -26.609  32.273  1.00 37.35           N  
ANISOU 4470  N   ARG B 199     5077   4310   4803    323   -403     -2       N  
ATOM   4471  CA  ARG B 199      68.110 -27.695  33.031  1.00 39.81           C  
ANISOU 4471  CA  ARG B 199     5268   4719   5140    359   -379    199       C  
ATOM   4472  C   ARG B 199      67.785 -29.036  32.373  1.00 41.99           C  
ANISOU 4472  C   ARG B 199     5776   4756   5424    528   -326    232       C  
ATOM   4473  O   ARG B 199      67.009 -29.119  31.421  1.00 43.62           O  
ANISOU 4473  O   ARG B 199     6265   4726   5582    554   -370     97       O  
ATOM   4474  CB  ARG B 199      67.628 -27.666  34.483  1.00 40.27           C  
ANISOU 4474  CB  ARG B 199     5180   4966   5157    158   -494    188       C  
ATOM   4475  CG  ARG B 199      68.078 -26.417  35.238  1.00 45.47           C  
ANISOU 4475  CG  ARG B 199     5744   5804   5728    -51   -545    167       C  
ATOM   4476  CD  ARG B 199      67.428 -26.277  36.601  1.00 41.21           C  
ANISOU 4476  CD  ARG B 199     5220   5370   5067   -244   -604    106       C  
ATOM   4477  NE  ARG B 199      66.012 -25.938  36.490  1.00 46.77           N  
ANISOU 4477  NE  ARG B 199     6049   5938   5785   -208   -540    -84       N  
ATOM   4478  CZ  ARG B 199      65.263 -25.500  37.499  1.00 51.02           C  
ANISOU 4478  CZ  ARG B 199     6665   6498   6223   -313   -480   -154       C  
ATOM   4479  NH1 ARG B 199      65.793 -25.352  38.706  1.00 51.09           N  
ANISOU 4479  NH1 ARG B 199     6724   6647   6039   -505   -515   -107       N  
ATOM   4480  NH2 ARG B 199      63.981 -25.218  37.305  1.00 43.65           N  
ANISOU 4480  NH2 ARG B 199     5776   5428   5380   -231   -373   -223       N  
ATOM   4481  N   ASN B 200      68.409 -30.096  32.869  1.00 46.24           N  
ANISOU 4481  N   ASN B 200     6226   5332   6011    618   -246    442       N  
ATOM   4482  CA  ASN B 200      68.139 -31.429  32.351  1.00 51.63           C  
ANISOU 4482  CA  ASN B 200     7195   5747   6676    770   -176    477       C  
ATOM   4483  C   ASN B 200      67.838 -32.378  33.503  1.00 48.08           C  
ANISOU 4483  C   ASN B 200     6577   5414   6277    694   -267    583       C  
ATOM   4484  O   ASN B 200      68.087 -32.077  34.674  1.00 53.28           O  
ANISOU 4484  O   ASN B 200     6904   6367   6975    554   -340    674       O  
ATOM   4485  CB  ASN B 200      69.297 -31.954  31.493  1.00 61.63           C  
ANISOU 4485  CB  ASN B 200     8628   6827   7964   1066    142    672       C  
ATOM   4486  CG  ASN B 200      70.602 -32.000  32.241  1.00 70.82           C  
ANISOU 4486  CG  ASN B 200     9370   8241   9296   1142    288   1026       C  
ATOM   4487  OD1 ASN B 200      70.863 -32.941  32.989  1.00 77.56           O  
ANISOU 4487  OD1 ASN B 200    10069   9161  10240   1174    324   1237       O  
ATOM   4488  ND2 ASN B 200      71.440 -30.988  32.036  1.00 73.25           N  
ANISOU 4488  ND2 ASN B 200     9469   8693   9671   1149    349   1147       N  
ATOM   4489  N   LEU B 201      67.289 -33.541  33.142  1.00 50.19           N  
ANISOU 4489  N   LEU B 201     7133   5422   6516    760   -280    577       N  
ATOM   4490  CA  LEU B 201      66.716 -34.452  34.132  1.00 61.15           C  
ANISOU 4490  CA  LEU B 201     8393   6885   7955    668   -410    652       C  
ATOM   4491  C   LEU B 201      67.762 -34.955  35.116  1.00 64.11           C  
ANISOU 4491  C   LEU B 201     8434   7488   8437    734   -283    922       C  
ATOM   4492  O   LEU B 201      67.578 -34.859  36.334  1.00 82.16           O  
ANISOU 4492  O   LEU B 201    10416  10051  10751    565   -415    978       O  
ATOM   4493  CB  LEU B 201      66.049 -35.632  33.428  1.00 64.46           C  
ANISOU 4493  CB  LEU B 201     9248   6931   8314    709   -464    626       C  
ATOM   4494  CG  LEU B 201      64.543 -35.527  33.241  1.00 66.79           C  
ANISOU 4494  CG  LEU B 201     9672   7122   8583    482   -784    503       C  
ATOM   4495  CD1 LEU B 201      63.956 -36.917  33.092  1.00 71.34           C  
ANISOU 4495  CD1 LEU B 201    10560   7415   9133    440   -919    580       C  
ATOM   4496  CD2 LEU B 201      63.925 -34.800  34.416  1.00 67.53           C  
ANISOU 4496  CD2 LEU B 201     9313   7562   8784    325   -904    508       C  
ATOM   4497  N   GLN B 202      68.866 -35.501  34.605  1.00 68.42           N  
ANISOU 4497  N   GLN B 202     9043   7906   9048    981     -6   1136       N  
ATOM   4498  CA  GLN B 202      69.831 -36.178  35.471  1.00 84.58           C  
ANISOU 4498  CA  GLN B 202    10744  10134  11256   1055    119   1500       C  
ATOM   4499  C   GLN B 202      70.490 -35.202  36.439  1.00 90.16           C  
ANISOU 4499  C   GLN B 202    10987  11254  12017    846    -13   1659       C  
ATOM   4500  O   GLN B 202      70.581 -35.468  37.644  1.00 97.50           O  
ANISOU 4500  O   GLN B 202    11621  12438  12985    673   -157   1825       O  
ATOM   4501  CB  GLN B 202      70.891 -36.874  34.624  1.00 90.22           C  
ANISOU 4501  CB  GLN B 202    11619  10588  12073   1418    529   1771       C  
ATOM   4502  CG  GLN B 202      70.347 -37.580  33.404  1.00105.91           C  
ANISOU 4502  CG  GLN B 202    14269  12074  13900   1604    685   1564       C  
ATOM   4503  CD  GLN B 202      71.205 -37.333  32.180  1.00122.63           C  
ANISOU 4503  CD  GLN B 202    16678  13925  15990   1914   1080   1652       C  
ATOM   4504  OE1 GLN B 202      71.373 -38.215  31.336  1.00132.73           O  
ANISOU 4504  OE1 GLN B 202    18489  14762  17179   2187   1409   1687       O  
ATOM   4505  NE2 GLN B 202      71.753 -36.125  32.077  1.00124.30           N  
ANISOU 4505  NE2 GLN B 202    16592  14375  16261   1876   1071   1699       N  
ATOM   4506  N   GLU B 203      70.961 -34.066  35.926  1.00 80.63           N  
ANISOU 4506  N   GLU B 203     9752  10097  10787    828     11   1623       N  
ATOM   4507  CA  GLU B 203      71.723 -33.100  36.706  1.00 78.20           C  
ANISOU 4507  CA  GLU B 203     9085  10122  10507    594   -138   1814       C  
ATOM   4508  C   GLU B 203      70.850 -31.983  37.267  1.00 68.38           C  
ANISOU 4508  C   GLU B 203     7913   9008   9060    285   -401   1471       C  
ATOM   4509  O   GLU B 203      71.344 -30.875  37.497  1.00 68.47           O  
ANISOU 4509  O   GLU B 203     7821   9175   9018     93   -512   1504       O  
ATOM   4510  CB  GLU B 203      72.839 -32.499  35.856  1.00 82.97           C  
ANISOU 4510  CB  GLU B 203     9595  10697  11232    751     48   2047       C  
ATOM   4511  CG  GLU B 203      73.530 -33.471  34.921  1.00 93.31           C  
ANISOU 4511  CG  GLU B 203    10997  11742  12713   1173    459   2323       C  
ATOM   4512  CD  GLU B 203      74.621 -32.799  34.108  1.00103.29           C  
ANISOU 4512  CD  GLU B 203    12138  12988  14120   1354    686   2607       C  
ATOM   4513  OE1 GLU B 203      75.703 -33.404  33.940  1.00109.78           O  
ANISOU 4513  OE1 GLU B 203    12738  13776  15198   1625   1006   3128       O  
ATOM   4514  OE2 GLU B 203      74.397 -31.659  33.645  1.00104.43           O  
ANISOU 4514  OE2 GLU B 203    12382  13150  14148   1239    568   2353       O  
ATOM   4515  N   PHE B 204      69.566 -32.244  37.484  1.00 61.99           N  
ANISOU 4515  N   PHE B 204     8182   7933   7440    424  -1392   -456       N  
ATOM   4516  CA  PHE B 204      68.662 -31.182  37.900  1.00 50.16           C  
ANISOU 4516  CA  PHE B 204     6901   6390   5768    252  -1216   -377       C  
ATOM   4517  C   PHE B 204      69.034 -30.676  39.287  1.00 56.69           C  
ANISOU 4517  C   PHE B 204     7970   7188   6380    188  -1350   -298       C  
ATOM   4518  O   PHE B 204      69.107 -31.450  40.244  1.00 65.21           O  
ANISOU 4518  O   PHE B 204     9238   8156   7382    265  -1489   -187       O  
ATOM   4519  CB  PHE B 204      67.217 -31.673  37.890  1.00 47.72           C  
ANISOU 4519  CB  PHE B 204     6756   5891   5484    253  -1013   -299       C  
ATOM   4520  CG  PHE B 204      66.218 -30.579  38.114  1.00 46.54           C  
ANISOU 4520  CG  PHE B 204     6756   5710   5219    110   -802   -262       C  
ATOM   4521  CD1 PHE B 204      65.928 -30.131  39.397  1.00 54.43           C  
ANISOU 4521  CD1 PHE B 204     8038   6625   6017     40   -780   -189       C  
ATOM   4522  CD2 PHE B 204      65.582 -29.979  37.040  1.00 46.52           C  
ANISOU 4522  CD2 PHE B 204     6601   5768   5305     53   -635   -310       C  
ATOM   4523  CE1 PHE B 204      65.018 -29.112  39.601  1.00 60.85           C  
ANISOU 4523  CE1 PHE B 204     8962   7395   6761    -64   -575   -203       C  
ATOM   4524  CE2 PHE B 204      64.668 -28.961  37.239  1.00 52.33           C  
ANISOU 4524  CE2 PHE B 204     7451   6444   5990    -42   -463   -280       C  
ATOM   4525  CZ  PHE B 204      64.389 -28.527  38.519  1.00 57.84           C  
ANISOU 4525  CZ  PHE B 204     8411   7037   6528    -91   -423   -246       C  
ATOM   4526  N   LYS B 205      69.251 -29.367  39.394  1.00 52.34           N  
ANISOU 4526  N   LYS B 205     7426   6734   5726     34  -1316   -352       N  
ATOM   4527  CA  LYS B 205      69.541 -28.712  40.655  1.00 62.42           C  
ANISOU 4527  CA  LYS B 205     8935   8003   6779    -62  -1424   -334       C  
ATOM   4528  C   LYS B 205      68.492 -27.645  40.934  1.00 58.10           C  
ANISOU 4528  C   LYS B 205     8588   7358   6128   -199  -1186   -353       C  
ATOM   4529  O   LYS B 205      68.187 -26.835  40.047  1.00 57.34           O  
ANISOU 4529  O   LYS B 205     8359   7272   6155   -271  -1040   -404       O  
ATOM   4530  CB  LYS B 205      70.939 -28.080  40.636  1.00 68.53           C  
ANISOU 4530  CB  LYS B 205     9515   8965   7558   -131  -1645   -433       C  
ATOM   4531  CG  LYS B 205      72.066 -29.099  40.661  1.00 72.18           C  
ANISOU 4531  CG  LYS B 205     9782   9528   8114     29  -1923   -432       C  
ATOM   4532  CD  LYS B 205      73.426 -28.432  40.504  1.00 79.89           C  
ANISOU 4532  CD  LYS B 205    10490  10729   9135    -57  -2114   -552       C  
ATOM   4533  CE  LYS B 205      74.548 -29.380  40.894  1.00 87.42           C  
ANISOU 4533  CE  LYS B 205    11282  11773  10160    120  -2442   -550       C  
ATOM   4534  NZ  LYS B 205      74.366 -30.726  40.285  1.00 91.80           N  
ANISOU 4534  NZ  LYS B 205    11717  12241  10923    361  -2427   -524       N  
ATOM   4535  N   PRO B 206      67.910 -27.618  42.130  1.00 56.88           N  
ANISOU 4535  N   PRO B 206     8746   7112   5753   -233  -1139   -311       N  
ATOM   4536  CA  PRO B 206      66.922 -26.581  42.448  1.00 58.68           C  
ANISOU 4536  CA  PRO B 206     9142   7247   5906   -339   -898   -381       C  
ATOM   4537  C   PRO B 206      67.575 -25.214  42.558  1.00 61.85           C  
ANISOU 4537  C   PRO B 206     9526   7688   6286   -478   -969   -526       C  
ATOM   4538  O   PRO B 206      68.751 -25.088  42.906  1.00 65.70           O  
ANISOU 4538  O   PRO B 206     9969   8292   6700   -527  -1219   -570       O  
ATOM   4539  CB  PRO B 206      66.358 -27.035  43.797  1.00 59.19           C  
ANISOU 4539  CB  PRO B 206     9533   7266   5690   -348   -849   -319       C  
ATOM   4540  CG  PRO B 206      67.484 -27.815  44.414  1.00 67.52           C  
ANISOU 4540  CG  PRO B 206    10627   8417   6610   -302  -1174   -231       C  
ATOM   4541  CD  PRO B 206      68.169 -28.513  43.270  1.00 64.64           C  
ANISOU 4541  CD  PRO B 206     9942   8086   6532   -178  -1310   -198       C  
ATOM   4542  N   ARG B 207      66.791 -24.174  42.265  1.00 58.00           N  
ANISOU 4542  N   ARG B 207     9063   7082   5891   -543   -759   -603       N  
ATOM   4543  CA  ARG B 207      67.309 -22.812  42.224  1.00 52.52           C  
ANISOU 4543  CA  ARG B 207     8350   6355   5251   -688   -809   -734       C  
ATOM   4544  C   ARG B 207      66.534 -21.868  43.135  1.00 56.96           C  
ANISOU 4544  C   ARG B 207     9171   6760   5710   -750   -649   -887       C  
ATOM   4545  O   ARG B 207      66.660 -20.645  43.005  1.00 59.96           O  
ANISOU 4545  O   ARG B 207     9551   7022   6208   -858   -639  -1007       O  
ATOM   4546  CB  ARG B 207      67.317 -22.293  40.784  1.00 51.23           C  
ANISOU 4546  CB  ARG B 207     7925   6173   5367   -716   -753   -678       C  
ATOM   4547  CG  ARG B 207      68.306 -23.050  39.911  1.00 54.61           C  
ANISOU 4547  CG  ARG B 207     8073   6806   5870   -688   -911   -598       C  
ATOM   4548  CD  ARG B 207      68.380 -22.557  38.479  1.00 55.13           C  
ANISOU 4548  CD  ARG B 207     7887   6920   6141   -750   -848   -533       C  
ATOM   4549  NE  ARG B 207      69.476 -23.231  37.781  1.00 58.44           N  
ANISOU 4549  NE  ARG B 207     8029   7582   6595   -739   -987   -518       N  
ATOM   4550  CZ  ARG B 207      69.694 -23.177  36.471  1.00 58.22           C  
ANISOU 4550  CZ  ARG B 207     7744   7696   6681   -781   -938   -462       C  
ATOM   4551  NH1 ARG B 207      68.884 -22.477  35.688  1.00 49.10           N  
ANISOU 4551  NH1 ARG B 207     6588   6454   5613   -838   -787   -372       N  
ATOM   4552  NH2 ARG B 207      70.727 -23.828  35.945  1.00 52.44           N  
ANISOU 4552  NH2 ARG B 207     6746   7208   5969   -760  -1044   -500       N  
ATOM   4553  N   SER B 208      65.743 -22.410  44.056  1.00 59.56           N  
ANISOU 4553  N   SER B 208     9720   7080   5830   -692   -515   -895       N  
ATOM   4554  CA  SER B 208      65.039 -21.606  45.044  1.00 63.00           C  
ANISOU 4554  CA  SER B 208    10402   7417   6119   -745   -340  -1089       C  
ATOM   4555  C   SER B 208      64.674 -22.510  46.207  1.00 60.23           C  
ANISOU 4555  C   SER B 208    10292   7179   5414   -727   -286  -1051       C  
ATOM   4556  O   SER B 208      64.705 -23.736  46.092  1.00 56.29           O  
ANISOU 4556  O   SER B 208     9760   6762   4867   -654   -344   -841       O  
ATOM   4557  CB  SER B 208      63.780 -20.954  44.463  1.00 64.47           C  
ANISOU 4557  CB  SER B 208    10522   7408   6565   -679    -52  -1138       C  
ATOM   4558  OG  SER B 208      62.744 -21.910  44.306  1.00 59.01           O  
ANISOU 4558  OG  SER B 208     9799   6738   5883   -569    144  -1008       O  
ATOM   4559  N   GLN B 209      64.320 -21.886  47.331  1.00 58.07           N  
ANISOU 4559  N   GLN B 209    10270   6905   4889   -803   -169  -1258       N  
ATOM   4560  CA  GLN B 209      63.894 -22.666  48.488  1.00 62.76           C  
ANISOU 4560  CA  GLN B 209    11121   7639   5088   -823    -80  -1210       C  
ATOM   4561  C   GLN B 209      62.636 -23.462  48.174  1.00 62.31           C  
ANISOU 4561  C   GLN B 209    11011   7536   5128   -732    214  -1056       C  
ATOM   4562  O   GLN B 209      62.464 -24.587  48.659  1.00 63.93           O  
ANISOU 4562  O   GLN B 209    11332   7840   5117   -734    217   -855       O  
ATOM   4563  CB  GLN B 209      63.656 -21.755  49.691  1.00 66.04           C  
ANISOU 4563  CB  GLN B 209    11804   8091   5199   -933     43  -1516       C  
ATOM   4564  CG  GLN B 209      63.306 -22.513  50.960  1.00 73.93           C  
ANISOU 4564  CG  GLN B 209    13095   9294   5701   -996    130  -1457       C  
ATOM   4565  CD  GLN B 209      64.404 -23.477  51.378  1.00 78.60           C  
ANISOU 4565  CD  GLN B 209    13776  10064   6025  -1029   -248  -1210       C  
ATOM   4566  OE1 GLN B 209      65.590 -23.164  51.281  1.00 80.96           O  
ANISOU 4566  OE1 GLN B 209    14008  10403   6350  -1064   -587  -1253       O  
ATOM   4567  NE2 GLN B 209      64.012 -24.656  51.839  1.00 82.07           N  
ANISOU 4567  NE2 GLN B 209    14350  10600   6232  -1021   -199   -941       N  
ATOM   4568  N   MET B 210      61.745 -22.893  47.362  1.00 57.58           N  
ANISOU 4568  N   MET B 210    10232   6778   4868   -659    444  -1133       N  
ATOM   4569  CA  MET B 210      60.537 -23.614  46.986  1.00 56.73           C  
ANISOU 4569  CA  MET B 210    10025   6637   4893   -583    707  -1004       C  
ATOM   4570  C   MET B 210      60.872 -24.865  46.182  1.00 57.10           C  
ANISOU 4570  C   MET B 210     9920   6707   5067   -527    540   -720       C  
ATOM   4571  O   MET B 210      60.277 -25.930  46.396  1.00 56.15           O  
ANISOU 4571  O   MET B 210     9843   6616   4874   -526    650   -556       O  
ATOM   4572  CB  MET B 210      59.604 -22.700  46.195  1.00 55.11           C  
ANISOU 4572  CB  MET B 210     9619   6262   5059   -499    921  -1137       C  
ATOM   4573  CG  MET B 210      58.330 -23.393  45.759  1.00 53.83           C  
ANISOU 4573  CG  MET B 210     9307   6083   5064   -428   1175  -1026       C  
ATOM   4574  SD  MET B 210      57.353 -22.443  44.583  1.00 61.60           S  
ANISOU 4574  SD  MET B 210     9989   6877   6537   -295   1321  -1111       S  
ATOM   4575  CE  MET B 210      56.939 -20.992  45.559  1.00 58.57           C  
ANISOU 4575  CE  MET B 210     9756   6383   6113   -288   1527  -1477       C  
ATOM   4576  N   GLU B 211      61.828 -24.762  45.257  1.00 53.67           N  
ANISOU 4576  N   GLU B 211     9303   6258   4831   -492    284   -673       N  
ATOM   4577  CA  GLU B 211      62.229 -25.946  44.507  1.00 53.92           C  
ANISOU 4577  CA  GLU B 211     9183   6319   4986   -424    124   -463       C  
ATOM   4578  C   GLU B 211      62.945 -26.947  45.402  1.00 56.82           C  
ANISOU 4578  C   GLU B 211     9737   6777   5075   -443    -78   -323       C  
ATOM   4579  O   GLU B 211      62.771 -28.160  45.244  1.00 63.57           O  
ANISOU 4579  O   GLU B 211    10575   7604   5974   -391   -103   -138       O  
ATOM   4580  CB  GLU B 211      63.108 -25.555  43.324  1.00 50.52           C  
ANISOU 4580  CB  GLU B 211     8496   5897   4802   -393    -71   -475       C  
ATOM   4581  CG  GLU B 211      62.393 -24.724  42.281  1.00 51.24           C  
ANISOU 4581  CG  GLU B 211     8396   5895   5179   -369     87   -531       C  
ATOM   4582  CD  GLU B 211      63.108 -24.754  40.950  1.00 57.48           C  
ANISOU 4582  CD  GLU B 211     8919   6743   6179   -348    -73   -467       C  
ATOM   4583  OE1 GLU B 211      64.342 -24.954  40.959  1.00 51.77           O  
ANISOU 4583  OE1 GLU B 211     8153   6125   5391   -374   -304   -459       O  
ATOM   4584  OE2 GLU B 211      62.436 -24.598  39.903  1.00 53.50           O  
ANISOU 4584  OE2 GLU B 211     8234   6203   5889   -308     29   -429       O  
ATOM   4585  N   ILE B 212      63.761 -26.460  46.341  1.00 53.43           N  
ANISOU 4585  N   ILE B 212     9488   6442   4371   -519   -247   -405       N  
ATOM   4586  CA  ILE B 212      64.370 -27.352  47.324  1.00 59.80           C  
ANISOU 4586  CA  ILE B 212    10505   7347   4869   -539   -461   -246       C  
ATOM   4587  C   ILE B 212      63.289 -28.079  48.117  1.00 65.46           C  
ANISOU 4587  C   ILE B 212    11450   8055   5366   -586   -221   -109       C  
ATOM   4588  O   ILE B 212      63.353 -29.301  48.305  1.00 62.98           O  
ANISOU 4588  O   ILE B 212    11207   7716   5005   -557   -324    144       O  
ATOM   4589  CB  ILE B 212      65.320 -26.568  48.249  1.00 63.13           C  
ANISOU 4589  CB  ILE B 212    11087   7903   4997   -637   -678   -391       C  
ATOM   4590  CG1 ILE B 212      66.528 -26.045  47.465  1.00 63.68           C  
ANISOU 4590  CG1 ILE B 212    10900   7996   5301   -616   -948   -480       C  
ATOM   4591  CG2 ILE B 212      65.771 -27.435  49.425  1.00 63.63           C  
ANISOU 4591  CG2 ILE B 212    11415   8092   4669   -670   -891   -204       C  
ATOM   4592  CD1 ILE B 212      67.465 -25.174  48.293  1.00 70.47           C  
ANISOU 4592  CD1 ILE B 212    11877   8978   5921   -742  -1172   -657       C  
ATOM   4593  N   ASP B 213      62.273 -27.341  48.581  1.00 62.43           N  
ANISOU 4593  N   ASP B 213    11171   7681   4867   -664    112   -275       N  
ATOM   4594  CA  ASP B 213      61.173 -27.958  49.319  1.00 62.21           C  
ANISOU 4594  CA  ASP B 213    11327   7683   4627   -741    400   -164       C  
ATOM   4595  C   ASP B 213      60.416 -28.966  48.457  1.00 59.31           C  
ANISOU 4595  C   ASP B 213    10776   7180   4578   -680    524     28       C  
ATOM   4596  O   ASP B 213      60.048 -30.047  48.934  1.00 60.01           O  
ANISOU 4596  O   ASP B 213    11006   7260   4535   -740    571    267       O  
ATOM   4597  CB  ASP B 213      60.212 -26.885  49.842  1.00 61.48           C  
ANISOU 4597  CB  ASP B 213    11305   7635   4419   -809    764   -445       C  
ATOM   4598  CG  ASP B 213      60.816 -26.040  50.952  1.00 69.64           C  
ANISOU 4598  CG  ASP B 213    12591   8818   5050   -909    679   -657       C  
ATOM   4599  OD1 ASP B 213      61.724 -26.526  51.657  1.00 70.63           O  
ANISOU 4599  OD1 ASP B 213    12914   9071   4850   -969    389   -515       O  
ATOM   4600  OD2 ASP B 213      60.371 -24.885  51.127  1.00 71.09           O  
ANISOU 4600  OD2 ASP B 213    12772   8985   5254   -923    889   -978       O  
ATOM   4601  N   PHE B 214      60.166 -28.630  47.189  1.00 55.11           N  
ANISOU 4601  N   PHE B 214     9939   6540   4460   -579    570    -67       N  
ATOM   4602  CA  PHE B 214      59.437 -29.549  46.318  1.00 57.72           C  
ANISOU 4602  CA  PHE B 214    10081   6758   5092   -533    671     71       C  
ATOM   4603  C   PHE B 214      60.175 -30.873  46.162  1.00 57.11           C  
ANISOU 4603  C   PHE B 214    10027   6617   5056   -490    393    312       C  
ATOM   4604  O   PHE B 214      59.556 -31.944  46.158  1.00 56.53           O  
ANISOU 4604  O   PHE B 214     9978   6448   5054   -524    481    490       O  
ATOM   4605  CB  PHE B 214      59.208 -28.916  44.946  1.00 53.81           C  
ANISOU 4605  CB  PHE B 214     9262   6200   4985   -435    702    -68       C  
ATOM   4606  CG  PHE B 214      58.582 -29.857  43.946  1.00 55.23           C  
ANISOU 4606  CG  PHE B 214     9228   6291   5467   -391    751     39       C  
ATOM   4607  CD1 PHE B 214      57.202 -29.992  43.870  1.00 54.72           C  
ANISOU 4607  CD1 PHE B 214     9081   6194   5517   -435   1055     30       C  
ATOM   4608  CD2 PHE B 214      59.373 -30.612  43.086  1.00 51.61           C  
ANISOU 4608  CD2 PHE B 214     8632   5792   5184   -309    495    118       C  
ATOM   4609  CE1 PHE B 214      56.621 -30.853  42.951  1.00 54.76           C  
ANISOU 4609  CE1 PHE B 214     8882   6124   5800   -417   1080    104       C  
ATOM   4610  CE2 PHE B 214      58.798 -31.479  42.171  1.00 46.69           C  
ANISOU 4610  CE2 PHE B 214     7822   5088   4829   -280    535    169       C  
ATOM   4611  CZ  PHE B 214      57.419 -31.598  42.101  1.00 48.04           C  
ANISOU 4611  CZ  PHE B 214     7925   5222   5106   -344    816    166       C  
ATOM   4612  N   LEU B 215      61.496 -30.821  46.006  1.00 57.77           N  
ANISOU 4612  N   LEU B 215    10082   6734   5134   -413     54    309       N  
ATOM   4613  CA  LEU B 215      62.245 -32.060  45.857  1.00 62.51           C  
ANISOU 4613  CA  LEU B 215    10678   7253   5821   -331   -228    508       C  
ATOM   4614  C   LEU B 215      62.310 -32.828  47.166  1.00 67.51           C  
ANISOU 4614  C   LEU B 215    11646   7885   6119   -412   -307    754       C  
ATOM   4615  O   LEU B 215      62.332 -34.063  47.156  1.00 77.14           O  
ANISOU 4615  O   LEU B 215    12913   8954   7442   -377   -419    984       O  
ATOM   4616  CB  LEU B 215      63.648 -31.760  45.336  1.00 63.67           C  
ANISOU 4616  CB  LEU B 215    10655   7467   6072   -219   -557    416       C  
ATOM   4617  CG  LEU B 215      63.680 -31.228  43.903  1.00 63.30           C  
ANISOU 4617  CG  LEU B 215    10268   7428   6355   -152   -505    237       C  
ATOM   4618  CD1 LEU B 215      65.094 -30.839  43.503  1.00 58.12           C  
ANISOU 4618  CD1 LEU B 215     9442   6883   5757    -87   -793    143       C  
ATOM   4619  CD2 LEU B 215      63.105 -32.260  42.944  1.00 54.09           C  
ANISOU 4619  CD2 LEU B 215     8932   6132   5488    -80   -434    295       C  
ATOM   4620  N   GLU B 216      62.302 -32.121  48.295  1.00 62.50           N  
ANISOU 4620  N   GLU B 216    11259   7409   5080   -530   -248    712       N  
ATOM   4621  CA  GLU B 216      62.522 -32.737  49.599  1.00 75.77           C  
ANISOU 4621  CA  GLU B 216    13285   9152   6352   -625   -370    957       C  
ATOM   4622  C   GLU B 216      61.232 -33.205  50.269  1.00 79.04           C  
ANISOU 4622  C   GLU B 216    13902   9557   6572   -795    -14   1112       C  
ATOM   4623  O   GLU B 216      61.200 -34.296  50.850  1.00 77.42           O  
ANISOU 4623  O   GLU B 216    13905   9277   6232   -857   -104   1441       O  
ATOM   4624  CB  GLU B 216      63.255 -31.752  50.517  1.00 83.30           C  
ANISOU 4624  CB  GLU B 216    14412  10330   6909   -690   -512    811       C  
ATOM   4625  CG  GLU B 216      63.709 -32.349  51.835  1.00 99.94           C  
ANISOU 4625  CG  GLU B 216    16873  12551   8548   -779   -733   1074       C  
ATOM   4626  CD  GLU B 216      64.559 -33.590  51.644  1.00111.89           C  
ANISOU 4626  CD  GLU B 216    18362  13913  10237   -640  -1135   1386       C  
ATOM   4627  OE1 GLU B 216      64.202 -34.650  52.202  1.00116.76           O  
ANISOU 4627  OE1 GLU B 216    19204  14436  10726   -699  -1149   1730       O  
ATOM   4628  OE2 GLU B 216      65.579 -33.507  50.925  1.00113.63           O  
ANISOU 4628  OE2 GLU B 216    18329  14099  10745   -472  -1431   1287       O  
ATOM   4629  N   LEU B 217      60.168 -32.410  50.210  1.00 73.19           N  
ANISOU 4629  N   LEU B 217    13094   8886   5829   -875    386    892       N  
ATOM   4630  CA  LEU B 217      58.966 -32.728  50.966  1.00 74.25           C  
ANISOU 4630  CA  LEU B 217    13400   9077   5734  -1060    760    999       C  
ATOM   4631  C   LEU B 217      58.075 -33.709  50.205  1.00 74.84           C  
ANISOU 4631  C   LEU B 217    13301   8947   6187  -1073    924   1156       C  
ATOM   4632  O   LEU B 217      58.236 -33.945  49.002  1.00 71.87           O  
ANISOU 4632  O   LEU B 217    12647   8405   6256   -928    802   1102       O  
ATOM   4633  CB  LEU B 217      58.175 -31.460  51.278  1.00 76.04           C  
ANISOU 4633  CB  LEU B 217    13598   9470   5823  -1124   1134    659       C  
ATOM   4634  CG  LEU B 217      58.917 -30.314  51.962  1.00 71.54           C  
ANISOU 4634  CG  LEU B 217    13177   9081   4925  -1128   1019    409       C  
ATOM   4635  CD1 LEU B 217      57.987 -29.125  52.123  1.00 72.80           C  
ANISOU 4635  CD1 LEU B 217    13265   9328   5067  -1159   1420     42       C  
ATOM   4636  CD2 LEU B 217      59.462 -30.768  53.305  1.00 77.26           C  
ANISOU 4636  CD2 LEU B 217    14290   9988   5078  -1270    855    618       C  
ATOM   4637  N   ALA B 218      57.109 -34.275  50.928  1.00 74.58           N  
ANISOU 4637  N   ALA B 218    13432   8950   5957  -1272   1217   1338       N  
ATOM   4638  CA  ALA B 218      56.071 -35.074  50.299  1.00 72.47           C  
ANISOU 4638  CA  ALA B 218    12986   8512   6037  -1338   1440   1442       C  
ATOM   4639  C   ALA B 218      55.033 -34.167  49.643  1.00 80.64           C  
ANISOU 4639  C   ALA B 218    13705   9615   7319  -1310   1793   1109       C  
ATOM   4640  O   ALA B 218      54.957 -32.964  49.915  1.00 85.85           O  
ANISOU 4640  O   ALA B 218    14346  10447   7825  -1274   1933    830       O  
ATOM   4641  CB  ALA B 218      55.399 -35.996  51.315  1.00 75.39           C  
ANISOU 4641  CB  ALA B 218    13628   8900   6117  -1600   1641   1777       C  
ATOM   4642  N   MET B 219      54.222 -34.770  48.767  1.00 80.57           N  
ANISOU 4642  N   MET B 219    13442   9452   7717  -1324   1916   1138       N  
ATOM   4643  CA  MET B 219      53.291 -33.998  47.947  1.00 74.05           C  
ANISOU 4643  CA  MET B 219    12266   8668   7203  -1259   2168    850       C  
ATOM   4644  C   MET B 219      52.326 -33.189  48.810  1.00 71.99           C  
ANISOU 4644  C   MET B 219    12030   8628   6695  -1375   2598    682       C  
ATOM   4645  O   MET B 219      52.166 -31.979  48.612  1.00 71.45           O  
ANISOU 4645  O   MET B 219    11816   8648   6683  -1252   2698    377       O  
ATOM   4646  CB  MET B 219      52.527 -34.936  47.008  1.00 70.00           C  
ANISOU 4646  CB  MET B 219    11500   7979   7116  -1301   2219    934       C  
ATOM   4647  CG  MET B 219      51.630 -34.228  45.998  1.00 71.54           C  
ANISOU 4647  CG  MET B 219    11298   8212   7671  -1212   2393    665       C  
ATOM   4648  SD  MET B 219      50.808 -35.329  44.819  1.00 70.78           S  
ANISOU 4648  SD  MET B 219    10890   7937   8066  -1271   2392    725       S  
ATOM   4649  CE  MET B 219      49.548 -36.070  45.859  1.00 73.25           C  
ANISOU 4649  CE  MET B 219    11285   8293   8255  -1593   2810    908       C  
ATOM   4650  N   ASP B 220      51.675 -33.843  49.777  1.00 68.69           N  
ANISOU 4650  N   ASP B 220    11794   8298   6008  -1615   2863    874       N  
ATOM   4651  CA  ASP B 220      50.686 -33.155  50.603  1.00 84.21           C  
ANISOU 4651  CA  ASP B 220    13751  10510   7734  -1738   3325    687       C  
ATOM   4652  C   ASP B 220      51.311 -32.055  51.449  1.00 80.80           C  
ANISOU 4652  C   ASP B 220    13544  10270   6884  -1680   3314    466       C  
ATOM   4653  O   ASP B 220      50.674 -31.023  51.685  1.00 82.85           O  
ANISOU 4653  O   ASP B 220    13682  10678   7119  -1641   3620    132       O  
ATOM   4654  CB  ASP B 220      49.965 -34.157  51.501  1.00 95.77           C  
ANISOU 4654  CB  ASP B 220    15389  12058   8940  -2050   3610    979       C  
ATOM   4655  CG  ASP B 220      49.139 -35.153  50.714  1.00112.07           C  
ANISOU 4655  CG  ASP B 220    17195  13935  11450  -2150   3690   1139       C  
ATOM   4656  OD1 ASP B 220      48.602 -34.773  49.651  1.00114.82           O  
ANISOU 4656  OD1 ASP B 220    17154  14215  12256  -2006   3726    911       O  
ATOM   4657  OD2 ASP B 220      49.028 -36.317  51.158  1.00120.88           O  
ANISOU 4657  OD2 ASP B 220    18504  14963  12461  -2382   3700   1502       O  
ATOM   4658  N   GLU B 221      52.544 -32.258  51.920  1.00 81.58           N  
ANISOU 4658  N   GLU B 221    13958  10364   6673  -1670   2955    628       N  
ATOM   4659  CA  GLU B 221      53.196 -31.249  52.748  1.00 87.97           C  
ANISOU 4659  CA  GLU B 221    14992  11364   7070  -1643   2906    407       C  
ATOM   4660  C   GLU B 221      53.609 -30.039  51.925  1.00 77.27           C  
ANISOU 4660  C   GLU B 221    13412   9919   6030  -1401   2762     56       C  
ATOM   4661  O   GLU B 221      53.413 -28.894  52.353  1.00 79.48           O  
ANISOU 4661  O   GLU B 221    13700  10320   6179  -1369   2948   -288       O  
ATOM   4662  CB  GLU B 221      54.410 -31.847  53.450  1.00 93.96           C  
ANISOU 4662  CB  GLU B 221    16120  12151   7430  -1703   2517    697       C  
ATOM   4663  CG  GLU B 221      54.072 -32.828  54.544  1.00109.18           C  
ANISOU 4663  CG  GLU B 221    18279  14208   8998  -1934   2610   1036       C  
ATOM   4664  CD  GLU B 221      55.073 -33.957  54.619  1.00117.60           C  
ANISOU 4664  CD  GLU B 221    19564  15116  10004  -1937   2158   1469       C  
ATOM   4665  OE1 GLU B 221      54.673 -35.078  55.001  1.00124.98           O  
ANISOU 4665  OE1 GLU B 221    20562  15995  10928  -2083   2188   1823       O  
ATOM   4666  OE2 GLU B 221      56.255 -33.725  54.277  1.00113.86           O  
ANISOU 4666  OE2 GLU B 221    19172  14558   9530  -1785   1762   1450       O  
ATOM   4667  N   PHE B 222      54.195 -30.267  50.748  1.00 63.98           N  
ANISOU 4667  N   PHE B 222    11532   8019   4758  -1240   2436    132       N  
ATOM   4668  CA  PHE B 222      54.580 -29.141  49.905  1.00 67.44           C  
ANISOU 4668  CA  PHE B 222    11758   8372   5494  -1043   2301   -148       C  
ATOM   4669  C   PHE B 222      53.366 -28.299  49.538  1.00 69.49           C  
ANISOU 4669  C   PHE B 222    11744   8629   6031   -980   2664   -426       C  
ATOM   4670  O   PHE B 222      53.392 -27.067  49.641  1.00 69.96           O  
ANISOU 4670  O   PHE B 222    11774   8700   6109   -891   2727   -733       O  
ATOM   4671  CB  PHE B 222      55.292 -29.627  48.644  1.00 58.46           C  
ANISOU 4671  CB  PHE B 222    10430   7047   4734   -908   1944     -6       C  
ATOM   4672  CG  PHE B 222      55.659 -28.512  47.708  1.00 57.93           C  
ANISOU 4672  CG  PHE B 222    10142   6904   4963   -742   1816   -239       C  
ATOM   4673  CD1 PHE B 222      56.848 -27.818  47.871  1.00 66.38           C  
ANISOU 4673  CD1 PHE B 222    11327   7996   5900   -700   1543   -336       C  
ATOM   4674  CD2 PHE B 222      54.804 -28.137  46.683  1.00 55.60           C  
ANISOU 4674  CD2 PHE B 222     9525   6523   5077   -648   1961   -346       C  
ATOM   4675  CE1 PHE B 222      57.189 -26.778  47.017  1.00 64.41           C  
ANISOU 4675  CE1 PHE B 222    10886   7661   5926   -585   1435   -517       C  
ATOM   4676  CE2 PHE B 222      55.134 -27.096  45.830  1.00 59.00           C  
ANISOU 4676  CE2 PHE B 222     9779   6876   5763   -513   1833   -508       C  
ATOM   4677  CZ  PHE B 222      56.329 -26.415  45.999  1.00 63.03           C  
ANISOU 4677  CZ  PHE B 222    10420   7388   6142   -492   1581   -586       C  
ATOM   4678  N   ILE B 223      52.285 -28.954  49.109  1.00 65.40           N  
ANISOU 4678  N   ILE B 223    11009   8080   5758  -1023   2893   -329       N  
ATOM   4679  CA  ILE B 223      51.083 -28.228  48.714  1.00 67.77           C  
ANISOU 4679  CA  ILE B 223    10997   8385   6369   -943   3214   -577       C  
ATOM   4680  C   ILE B 223      50.488 -27.486  49.901  1.00 76.36           C  
ANISOU 4680  C   ILE B 223    12202   9662   7148  -1012   3596   -842       C  
ATOM   4681  O   ILE B 223      49.957 -26.377  49.750  1.00 77.95           O  
ANISOU 4681  O   ILE B 223    12217   9841   7558   -871   3768  -1165       O  
ATOM   4682  CB  ILE B 223      50.077 -29.200  48.069  1.00 67.04           C  
ANISOU 4682  CB  ILE B 223    10640   8248   6585  -1009   3357   -409       C  
ATOM   4683  CG1 ILE B 223      50.571 -29.592  46.672  1.00 64.65           C  
ANISOU 4683  CG1 ILE B 223    10146   7760   6658   -886   2997   -283       C  
ATOM   4684  CG2 ILE B 223      48.688 -28.594  48.005  1.00 62.95           C  
ANISOU 4684  CG2 ILE B 223     9810   7803   6306   -972   3753   -650       C  
ATOM   4685  CD1 ILE B 223      49.746 -30.667  46.005  1.00 64.31           C  
ANISOU 4685  CD1 ILE B 223     9874   7657   6904   -971   3065   -123       C  
ATOM   4686  N   GLU B 224      50.588 -28.064  51.100  1.00 83.74           N  
ANISOU 4686  N   GLU B 224    13455  10785   7578  -1223   3725   -717       N  
ATOM   4687  CA  GLU B 224      50.122 -27.370  52.296  1.00 87.91           C  
ANISOU 4687  CA  GLU B 224    14130  11548   7726  -1308   4092   -999       C  
ATOM   4688  C   GLU B 224      50.983 -26.148  52.595  1.00 90.27           C  
ANISOU 4688  C   GLU B 224    14586  11829   7882  -1187   3917  -1309       C  
ATOM   4689  O   GLU B 224      50.462 -25.044  52.798  1.00 91.72           O  
ANISOU 4689  O   GLU B 224    14614  12025   8208  -1069   4100  -1683       O  
ATOM   4690  CB  GLU B 224      50.112 -28.328  53.488  1.00 91.09           C  
ANISOU 4690  CB  GLU B 224    14788  12170   7653  -1556   4134   -722       C  
ATOM   4691  CG  GLU B 224      49.844 -27.646  54.820  1.00 99.14           C  
ANISOU 4691  CG  GLU B 224    15896  13463   8308  -1606   4312   -970       C  
ATOM   4692  CD  GLU B 224      49.697 -28.632  55.965  1.00111.73           C  
ANISOU 4692  CD  GLU B 224    17700  15299   9456  -1850   4373   -664       C  
ATOM   4693  OE1 GLU B 224      49.727 -29.855  55.707  1.00113.49           O  
ANISOU 4693  OE1 GLU B 224    17982  15435   9705  -1981   4281   -252       O  
ATOM   4694  OE2 GLU B 224      49.549 -28.183  57.123  1.00119.15           O  
ANISOU 4694  OE2 GLU B 224    18745  16504  10024  -1911   4510   -832       O  
ATOM   4695  N   ARG B 225      52.308 -26.324  52.613  1.00 88.49           N  
ANISOU 4695  N   ARG B 225    14598  11551   7472  -1192   3482  -1146       N  
ATOM   4696  CA  ARG B 225      53.200 -25.232  52.995  1.00 88.71           C  
ANISOU 4696  CA  ARG B 225    14798  11580   7330  -1131   3295  -1429       C  
ATOM   4697  C   ARG B 225      53.052 -24.034  52.068  1.00 82.25           C  
ANISOU 4697  C   ARG B 225    13695  10527   7030   -907   3269  -1727       C  
ATOM   4698  O   ARG B 225      53.045 -22.885  52.525  1.00 83.03           O  
ANISOU 4698  O   ARG B 225    13850  10619   7078   -857   3376  -2112       O  
ATOM   4699  CB  ARG B 225      54.650 -25.713  53.006  1.00 87.79           C  
ANISOU 4699  CB  ARG B 225    14902  11440   7013  -1166   2798  -1172       C  
ATOM   4700  CG  ARG B 225      55.662 -24.588  53.147  1.00 84.93           C  
ANISOU 4700  CG  ARG B 225    14644  11038   6587  -1105   2540  -1450       C  
ATOM   4701  CD  ARG B 225      57.073 -25.124  53.257  1.00 84.24           C  
ANISOU 4701  CD  ARG B 225    14744  10979   6284  -1151   2058  -1200       C  
ATOM   4702  NE  ARG B 225      57.197 -26.085  54.350  1.00 89.25           N  
ANISOU 4702  NE  ARG B 225    15694  11847   6370  -1332   2049   -945       N  
ATOM   4703  CZ  ARG B 225      58.345 -26.628  54.739  1.00 89.52           C  
ANISOU 4703  CZ  ARG B 225    15918  11952   6142  -1379   1635   -709       C  
ATOM   4704  NH1 ARG B 225      59.477 -26.301  54.128  1.00 89.94           N  
ANISOU 4704  NH1 ARG B 225    15890  11887   6395  -1277   1237   -736       N  
ATOM   4705  NH2 ARG B 225      58.362 -27.495  55.742  1.00 96.47           N  
ANISOU 4705  NH2 ARG B 225    16972  13020   6662  -1502   1588   -429       N  
ATOM   4706  N   TYR B 226      52.938 -24.274  50.764  1.00 73.13           N  
ANISOU 4706  N   TYR B 226    12245   9169   6372   -778   3117  -1556       N  
ATOM   4707  CA  TYR B 226      52.865 -23.186  49.801  1.00 72.80           C  
ANISOU 4707  CA  TYR B 226    11950   8897   6815   -577   3038  -1756       C  
ATOM   4708  C   TYR B 226      51.439 -22.872  49.371  1.00 73.32           C  
ANISOU 4708  C   TYR B 226    11683   8907   7266   -459   3381  -1901       C  
ATOM   4709  O   TYR B 226      51.243 -22.132  48.402  1.00 69.64           O  
ANISOU 4709  O   TYR B 226    10968   8233   7260   -280   3290  -1979       O  
ATOM   4710  CB  TYR B 226      53.758 -23.496  48.597  1.00 65.67           C  
ANISOU 4710  CB  TYR B 226    10933   7837   6179   -510   2620  -1497       C  
ATOM   4711  CG  TYR B 226      55.221 -23.401  48.967  1.00 67.02           C  
ANISOU 4711  CG  TYR B 226    11363   8037   6066   -580   2269  -1459       C  
ATOM   4712  CD1 TYR B 226      55.946 -24.534  49.301  1.00 65.45           C  
ANISOU 4712  CD1 TYR B 226    11341   7956   5570   -689   2065  -1176       C  
ATOM   4713  CD2 TYR B 226      55.861 -22.169  49.036  1.00 64.24           C  
ANISOU 4713  CD2 TYR B 226    11071   7582   5758   -540   2136  -1714       C  
ATOM   4714  CE1 TYR B 226      57.274 -24.452  49.664  1.00 69.31           C  
ANISOU 4714  CE1 TYR B 226    12028   8492   5816   -740   1726  -1147       C  
ATOM   4715  CE2 TYR B 226      57.192 -22.076  49.397  1.00 68.81           C  
ANISOU 4715  CE2 TYR B 226    11852   8208   6085   -624   1810  -1695       C  
ATOM   4716  CZ  TYR B 226      57.894 -23.222  49.709  1.00 69.31           C  
ANISOU 4716  CZ  TYR B 226    12059   8424   5854   -716   1602  -1414       C  
ATOM   4717  OH  TYR B 226      59.221 -23.144  50.069  1.00 73.67           O  
ANISOU 4717  OH  TYR B 226    12774   9042   6178   -785   1254  -1396       O  
ATOM   4718  N   LYS B 227      50.444 -23.401  50.085  1.00 75.88           N  
ANISOU 4718  N   LYS B 227    11993   9426   7413   -562   3768  -1928       N  
ATOM   4719  CA  LYS B 227      49.049 -22.987  49.942  1.00 75.70           C  
ANISOU 4719  CA  LYS B 227    11644   9405   7715   -456   4150  -2148       C  
ATOM   4720  C   LYS B 227      48.570 -23.135  48.496  1.00 69.83           C  
ANISOU 4720  C   LYS B 227    10513   8480   7540   -304   4006  -1984       C  
ATOM   4721  O   LYS B 227      48.088 -22.190  47.869  1.00 70.80           O  
ANISOU 4721  O   LYS B 227    10376   8434   8089    -94   4017  -2172       O  
ATOM   4722  CB  LYS B 227      48.862 -21.551  50.449  1.00 76.08           C  
ANISOU 4722  CB  LYS B 227    11693   9385   7828   -314   4303  -2608       C  
ATOM   4723  CG  LYS B 227      49.148 -21.356  51.947  1.00 85.82           C  
ANISOU 4723  CG  LYS B 227    13210  10858   8540   -455   4366  -2762       C  
ATOM   4724  CD  LYS B 227      50.595 -20.939  52.203  1.00 92.22           C  
ANISOU 4724  CD  LYS B 227    14368  11599   9074   -503   4022  -2798       C  
ATOM   4725  CE  LYS B 227      50.859 -20.611  53.677  1.00 99.54           C  
ANISOU 4725  CE  LYS B 227    15539  12771   9511   -621   4060  -2992       C  
ATOM   4726  NZ  LYS B 227      51.012 -21.815  54.548  1.00 99.73           N  
ANISOU 4726  NZ  LYS B 227    15787  13108   8997   -859   4087  -2696       N  
ATOM   4727  N   LEU B 228      48.702 -24.358  47.976  1.00 62.65           N  
ANISOU 4727  N   LEU B 228     9574   7601   6629   -415   3854  -1628       N  
ATOM   4728  CA  LEU B 228      48.416 -24.647  46.576  1.00 64.68           C  
ANISOU 4728  CA  LEU B 228     9507   7723   7345   -309   3660  -1456       C  
ATOM   4729  C   LEU B 228      47.149 -25.476  46.386  1.00 67.10           C  
ANISOU 4729  C   LEU B 228     9526   8132   7835   -385   3927  -1374       C  
ATOM   4730  O   LEU B 228      46.950 -26.054  45.311  1.00 62.09           O  
ANISOU 4730  O   LEU B 228     8665   7431   7495   -363   3750  -1192       O  
ATOM   4731  CB  LEU B 228      49.609 -25.352  45.934  1.00 60.65           C  
ANISOU 4731  CB  LEU B 228     9140   7142   6764   -356   3240  -1166       C  
ATOM   4732  CG  LEU B 228      50.767 -24.429  45.558  1.00 63.68           C  
ANISOU 4732  CG  LEU B 228     9637   7390   7170   -245   2914  -1228       C  
ATOM   4733  CD1 LEU B 228      51.988 -25.241  45.154  1.00 55.02           C  
ANISOU 4733  CD1 LEU B 228     8685   6284   5936   -314   2553   -970       C  
ATOM   4734  CD2 LEU B 228      50.334 -23.515  44.428  1.00 62.99           C  
ANISOU 4734  CD2 LEU B 228     9239   7140   7553    -48   2834  -1310       C  
ATOM   4735  N   GLU B 229      46.295 -25.549  47.403  1.00 64.61           N  
ANISOU 4735  N   GLU B 229     9208   7998   7343   -493   4354  -1519       N  
ATOM   4736  CA  GLU B 229      45.024 -26.255  47.271  1.00 77.63           C  
ANISOU 4736  CA  GLU B 229    10542   9761   9193   -589   4645  -1469       C  
ATOM   4737  C   GLU B 229      44.157 -25.616  46.193  1.00 74.29           C  
ANISOU 4737  C   GLU B 229     9647   9235   9346   -357   4622  -1604       C  
ATOM   4738  O   GLU B 229      44.015 -24.393  46.128  1.00 75.42           O  
ANISOU 4738  O   GLU B 229     9684   9286   9687   -129   4645  -1870       O  
ATOM   4739  CB  GLU B 229      44.264 -26.254  48.602  1.00 80.81           C  
ANISOU 4739  CB  GLU B 229    10999  10412   9291   -742   5136  -1642       C  
ATOM   4740  CG  GLU B 229      44.909 -27.065  49.712  1.00 94.34           C  
ANISOU 4740  CG  GLU B 229    13152  12275  10417  -1012   5145  -1431       C  
ATOM   4741  CD  GLU B 229      45.976 -26.294  50.469  1.00106.07           C  
ANISOU 4741  CD  GLU B 229    15020  13770  11513   -963   5004  -1578       C  
ATOM   4742  OE1 GLU B 229      46.327 -25.172  50.042  1.00106.04           O  
ANISOU 4742  OE1 GLU B 229    14967  13610  11712   -734   4884  -1830       O  
ATOM   4743  OE2 GLU B 229      46.459 -26.812  51.499  1.00111.50           O  
ANISOU 4743  OE2 GLU B 229    16050  14615  11701  -1160   4988  -1431       O  
ATOM   4744  N   GLY B 230      43.558 -26.454  45.351  1.00 73.86           N  
ANISOU 4744  N   GLY B 230     9308   9184   9570   -418   4560  -1420       N  
ATOM   4745  CA  GLY B 230      42.717 -25.978  44.277  1.00 71.03           C  
ANISOU 4745  CA  GLY B 230     8489   8762   9738   -217   4490  -1504       C  
ATOM   4746  C   GLY B 230      43.441 -25.630  42.994  1.00 63.66           C  
ANISOU 4746  C   GLY B 230     7527   7640   9021    -45   4012  -1379       C  
ATOM   4747  O   GLY B 230      42.785 -25.230  42.023  1.00 63.92           O  
ANISOU 4747  O   GLY B 230     7193   7627   9469    121   3897  -1406       O  
ATOM   4748  N   TYR B 231      44.767 -25.765  42.949  1.00 57.98           N  
ANISOU 4748  N   TYR B 231     7167   6834   8029    -86   3726  -1237       N  
ATOM   4749  CA  TYR B 231      45.529 -25.484  41.739  1.00 56.63           C  
ANISOU 4749  CA  TYR B 231     6974   6527   8015     38   3300  -1110       C  
ATOM   4750  C   TYR B 231      46.017 -26.746  41.043  1.00 59.02           C  
ANISOU 4750  C   TYR B 231     7316   6851   8256   -107   3060   -861       C  
ATOM   4751  O   TYR B 231      46.818 -26.653  40.107  1.00 59.44           O  
ANISOU 4751  O   TYR B 231     7395   6837   8354    -41   2721   -757       O  
ATOM   4752  CB  TYR B 231      46.697 -24.550  42.059  1.00 56.55           C  
ANISOU 4752  CB  TYR B 231     7274   6399   7814    121   3137  -1175       C  
ATOM   4753  CG  TYR B 231      46.216 -23.177  42.456  1.00 61.93           C  
ANISOU 4753  CG  TYR B 231     7874   6986   8669    308   3303  -1448       C  
ATOM   4754  CD1 TYR B 231      45.799 -22.265  41.495  1.00 59.94           C  
ANISOU 4754  CD1 TYR B 231     7346   6590   8840    529   3152  -1479       C  
ATOM   4755  CD2 TYR B 231      46.140 -22.803  43.794  1.00 65.24           C  
ANISOU 4755  CD2 TYR B 231     8491   7460   8836    268   3612  -1684       C  
ATOM   4756  CE1 TYR B 231      45.332 -21.000  41.859  1.00 59.15           C  
ANISOU 4756  CE1 TYR B 231     7164   6347   8965    728   3293  -1741       C  
ATOM   4757  CE2 TYR B 231      45.676 -21.548  44.164  1.00 71.01           C  
ANISOU 4757  CE2 TYR B 231     9137   8082   9760    456   3778  -1992       C  
ATOM   4758  CZ  TYR B 231      45.276 -20.652  43.192  1.00 68.01           C  
ANISOU 4758  CZ  TYR B 231     8476   7506   9860    697   3614  -2021       C  
ATOM   4759  OH  TYR B 231      44.819 -19.406  43.556  1.00 78.02           O  
ANISOU 4759  OH  TYR B 231     9658   8609  11376    908   3761  -2333       O  
ATOM   4760  N   ALA B 232      45.560 -27.923  41.483  1.00 63.68           N  
ANISOU 4760  N   ALA B 232     7914   7528   8753   -313   3239   -773       N  
ATOM   4761  CA  ALA B 232      45.723 -29.178  40.741  1.00 59.50           C  
ANISOU 4761  CA  ALA B 232     7344   6984   8281   -443   3044   -583       C  
ATOM   4762  C   ALA B 232      47.190 -29.554  40.536  1.00 56.95           C  
ANISOU 4762  C   ALA B 232     7328   6576   7733   -451   2723   -446       C  
ATOM   4763  O   ALA B 232      47.561 -30.115  39.501  1.00 51.68           O  
ANISOU 4763  O   ALA B 232     6577   5874   7185   -444   2457   -363       O  
ATOM   4764  CB  ALA B 232      44.991 -29.117  39.397  1.00 57.41           C  
ANISOU 4764  CB  ALA B 232     6669   6737   8408   -351   2892   -602       C  
ATOM   4765  N   PHE B 233      48.042 -29.269  41.523  1.00 56.13           N  
ANISOU 4765  N   PHE B 233     7569   6459   7299   -468   2744   -444       N  
ATOM   4766  CA  PHE B 233      49.454 -29.612  41.388  1.00 53.72           C  
ANISOU 4766  CA  PHE B 233     7520   6090   6800   -465   2435   -325       C  
ATOM   4767  C   PHE B 233      49.674 -31.122  41.377  1.00 54.96           C  
ANISOU 4767  C   PHE B 233     7772   6197   6912   -617   2353   -138       C  
ATOM   4768  O   PHE B 233      50.597 -31.611  40.712  1.00 56.59           O  
ANISOU 4768  O   PHE B 233     8024   6340   7138   -577   2058    -64       O  
ATOM   4769  CB  PHE B 233      50.257 -28.956  42.511  1.00 60.04           C  
ANISOU 4769  CB  PHE B 233     8647   6906   7258   -461   2463   -378       C  
ATOM   4770  CG  PHE B 233      51.003 -27.726  42.082  1.00 54.89           C  
ANISOU 4770  CG  PHE B 233     7999   6210   6647   -303   2270   -491       C  
ATOM   4771  CD1 PHE B 233      50.367 -26.727  41.369  1.00 62.65           C  
ANISOU 4771  CD1 PHE B 233     8722   7157   7926   -162   2298   -614       C  
ATOM   4772  CD2 PHE B 233      52.346 -27.572  42.393  1.00 51.71           C  
ANISOU 4772  CD2 PHE B 233     7852   5791   6005   -305   2044   -457       C  
ATOM   4773  CE1 PHE B 233      51.058 -25.591  40.971  1.00 64.99           C  
ANISOU 4773  CE1 PHE B 233     9040   7375   8277    -45   2115   -681       C  
ATOM   4774  CE2 PHE B 233      53.041 -26.444  41.997  1.00 50.98           C  
ANISOU 4774  CE2 PHE B 233     7755   5649   5967   -201   1873   -551       C  
ATOM   4775  CZ  PHE B 233      52.393 -25.447  41.293  1.00 56.05           C  
ANISOU 4775  CZ  PHE B 233     8165   6228   6902    -80   1916   -654       C  
ATOM   4776  N   GLU B 234      48.842 -31.872  42.101  1.00 55.78           N  
ANISOU 4776  N   GLU B 234     7900   6319   6974   -795   2616    -65       N  
ATOM   4777  CA  GLU B 234      48.901 -33.330  42.040  1.00 58.31           C  
ANISOU 4777  CA  GLU B 234     8294   6533   7328   -954   2542    125       C  
ATOM   4778  C   GLU B 234      48.904 -33.812  40.594  1.00 63.50           C  
ANISOU 4778  C   GLU B 234     8693   7120   8313   -892   2300     94       C  
ATOM   4779  O   GLU B 234      49.661 -34.720  40.230  1.00 65.32           O  
ANISOU 4779  O   GLU B 234     9029   7226   8564   -904   2062    187       O  
ATOM   4780  CB  GLU B 234      47.718 -33.938  42.800  1.00 62.93           C  
ANISOU 4780  CB  GLU B 234     8842   7158   7910  -1182   2901    196       C  
ATOM   4781  CG  GLU B 234      47.499 -33.379  44.208  1.00 82.51           C  
ANISOU 4781  CG  GLU B 234    11530   9779  10039  -1262   3215    177       C  
ATOM   4782  CD  GLU B 234      46.691 -32.083  44.224  1.00 94.66           C  
ANISOU 4782  CD  GLU B 234    12821  11468  11679  -1136   3461    -95       C  
ATOM   4783  OE1 GLU B 234      46.416 -31.528  43.137  1.00 98.50           O  
ANISOU 4783  OE1 GLU B 234    12999  11931  12496   -965   3336   -228       O  
ATOM   4784  OE2 GLU B 234      46.327 -31.621  45.327  1.00101.02           O  
ANISOU 4784  OE2 GLU B 234    13740  12412  12230  -1204   3774   -178       O  
ATOM   4785  N   HIS B 235      48.081 -33.187  39.751  1.00 57.85           N  
ANISOU 4785  N   HIS B 235     7635   6491   7853   -812   2343    -51       N  
ATOM   4786  CA  HIS B 235      48.008 -33.543  38.340  1.00 58.32           C  
ANISOU 4786  CA  HIS B 235     7438   6542   8178   -763   2112   -102       C  
ATOM   4787  C   HIS B 235      49.125 -32.872  37.545  1.00 50.65           C  
ANISOU 4787  C   HIS B 235     6498   5599   7146   -578   1816   -147       C  
ATOM   4788  O   HIS B 235      49.949 -33.552  36.925  1.00 48.27           O  
ANISOU 4788  O   HIS B 235     6246   5249   6845   -566   1579   -127       O  
ATOM   4789  CB  HIS B 235      46.629 -33.159  37.795  1.00 56.81           C  
ANISOU 4789  CB  HIS B 235     6858   6459   8267   -764   2255   -212       C  
ATOM   4790  CG  HIS B 235      46.423 -33.485  36.348  1.00 57.02           C  
ANISOU 4790  CG  HIS B 235     6606   6524   8534   -734   2014   -275       C  
ATOM   4791  ND1 HIS B 235      45.978 -34.719  35.916  1.00 55.34           N  
ANISOU 4791  ND1 HIS B 235     6280   6254   8492   -901   1978   -274       N  
ATOM   4792  CD2 HIS B 235      46.567 -32.726  35.235  1.00 51.89           C  
ANISOU 4792  CD2 HIS B 235     5773   5977   7966   -574   1797   -342       C  
ATOM   4793  CE1 HIS B 235      45.875 -34.708  34.598  1.00 57.75           C  
ANISOU 4793  CE1 HIS B 235     6342   6647   8952   -840   1746   -371       C  
ATOM   4794  NE2 HIS B 235      46.227 -33.511  34.160  1.00 53.86           N  
ANISOU 4794  NE2 HIS B 235     5807   6267   8390   -644   1633   -394       N  
ATOM   4795  N   ILE B 236      49.198 -31.537  37.601  1.00 44.04           N  
ANISOU 4795  N   ILE B 236     5636   4833   6263   -442   1840   -214       N  
ATOM   4796  CA  ILE B 236      50.022 -30.775  36.657  1.00 43.81           C  
ANISOU 4796  CA  ILE B 236     5561   4850   6234   -299   1581   -242       C  
ATOM   4797  C   ILE B 236      51.505 -31.061  36.854  1.00 49.52           C  
ANISOU 4797  C   ILE B 236     6546   5532   6738   -287   1389   -188       C  
ATOM   4798  O   ILE B 236      52.253 -31.244  35.886  1.00 48.19           O  
ANISOU 4798  O   ILE B 236     6314   5409   6588   -241   1157   -197       O  
ATOM   4799  CB  ILE B 236      49.753 -29.267  36.793  1.00 41.12           C  
ANISOU 4799  CB  ILE B 236     5164   4530   5928   -171   1653   -306       C  
ATOM   4800  CG1 ILE B 236      48.298 -28.934  36.462  1.00 45.55           C  
ANISOU 4800  CG1 ILE B 236     5404   5138   6765   -136   1802   -369       C  
ATOM   4801  CG2 ILE B 236      50.731 -28.492  35.909  1.00 37.43           C  
ANISOU 4801  CG2 ILE B 236     4699   4090   5432    -68   1386   -285       C  
ATOM   4802  CD1 ILE B 236      47.888 -27.495  36.878  1.00 49.13           C  
ANISOU 4802  CD1 ILE B 236     5814   5552   7299      9   1929   -459       C  
ATOM   4803  N   VAL B 237      51.968 -31.033  38.095  1.00 49.48           N  
ANISOU 4803  N   VAL B 237     7280   5848   5669   -483   1489   -473       N  
ATOM   4804  CA  VAL B 237      53.393 -31.047  38.386  1.00 51.34           C  
ANISOU 4804  CA  VAL B 237     7649   6114   5746   -516   1284   -456       C  
ATOM   4805  C   VAL B 237      53.872 -32.431  38.798  1.00 45.63           C  
ANISOU 4805  C   VAL B 237     7024   5420   4894   -560   1169   -357       C  
ATOM   4806  O   VAL B 237      54.890 -32.908  38.301  1.00 49.94           O  
ANISOU 4806  O   VAL B 237     7522   5994   5460   -532    967   -292       O  
ATOM   4807  CB  VAL B 237      53.726 -29.999  39.467  1.00 50.24           C  
ANISOU 4807  CB  VAL B 237     7713   5936   5439   -584   1343   -558       C  
ATOM   4808  CG1 VAL B 237      55.215 -30.027  39.762  1.00 50.59           C  
ANISOU 4808  CG1 VAL B 237     7864   6018   5340   -634   1090   -529       C  
ATOM   4809  CG2 VAL B 237      53.270 -28.614  39.011  1.00 46.32           C  
ANISOU 4809  CG2 VAL B 237     7118   5377   5105   -525   1466   -654       C  
ATOM   4810  N   TYR B 238      53.161 -33.080  39.725  1.00 45.40           N  
ANISOU 4810  N   TYR B 238     7136   5371   4743   -630   1310   -339       N  
ATOM   4811  CA  TYR B 238      53.572 -34.404  40.184  1.00 50.53           C  
ANISOU 4811  CA  TYR B 238     7906   6025   5269   -674   1204   -225       C  
ATOM   4812  C   TYR B 238      53.247 -35.489  39.170  1.00 49.06           C  
ANISOU 4812  C   TYR B 238     7545   5836   5260   -622   1175   -150       C  
ATOM   4813  O   TYR B 238      53.947 -36.507  39.116  1.00 51.30           O  
ANISOU 4813  O   TYR B 238     7866   6108   5517   -614   1026    -53       O  
ATOM   4814  CB  TYR B 238      52.909 -34.738  41.521  1.00 52.52           C  
ANISOU 4814  CB  TYR B 238     8403   6245   5309   -787   1381   -224       C  
ATOM   4815  CG  TYR B 238      53.375 -33.867  42.666  1.00 57.79           C  
ANISOU 4815  CG  TYR B 238     9323   6907   5726   -875   1384   -294       C  
ATOM   4816  CD1 TYR B 238      54.488 -34.220  43.422  1.00 54.94           C  
ANISOU 4816  CD1 TYR B 238     9171   6564   5139   -942   1148   -214       C  
ATOM   4817  CD2 TYR B 238      52.706 -32.690  42.991  1.00 60.82           C  
ANISOU 4817  CD2 TYR B 238     9743   7259   6108   -897   1615   -441       C  
ATOM   4818  CE1 TYR B 238      54.922 -33.429  44.472  1.00 57.97           C  
ANISOU 4818  CE1 TYR B 238     9812   6948   5266  -1054   1122   -283       C  
ATOM   4819  CE2 TYR B 238      53.137 -31.885  44.039  1.00 59.68           C  
ANISOU 4819  CE2 TYR B 238     9867   7096   5714  -1000   1629   -529       C  
ATOM   4820  CZ  TYR B 238      54.245 -32.263  44.775  1.00 57.85           C  
ANISOU 4820  CZ  TYR B 238     9859   6896   5225  -1090   1372   -451       C  
ATOM   4821  OH  TYR B 238      54.689 -31.477  45.811  1.00 57.71           O  
ANISOU 4821  OH  TYR B 238    10129   6865   4933  -1221   1354   -540       O  
ATOM   4822  N   GLY B 239      52.201 -35.299  38.368  1.00 48.24           N  
ANISOU 4822  N   GLY B 239     7254   5731   5344   -590   1308   -191       N  
ATOM   4823  CA  GLY B 239      51.803 -36.308  37.404  1.00 47.64           C  
ANISOU 4823  CA  GLY B 239     7035   5650   5416   -573   1279   -136       C  
ATOM   4824  C   GLY B 239      50.933 -37.396  38.000  1.00 49.39           C  
ANISOU 4824  C   GLY B 239     7331   5831   5603   -656   1417    -86       C  
ATOM   4825  O   GLY B 239      51.076 -37.744  39.175  1.00 47.03           O  
ANISOU 4825  O   GLY B 239     7248   5507   5115   -722   1466    -49       O  
ATOM   4826  N   ASP B 240      50.026 -37.939  37.194  1.00 45.19           N  
ANISOU 4826  N   ASP B 240     6634   5293   5243   -670   1473    -78       N  
ATOM   4827  CA  ASP B 240      49.082 -38.965  37.623  1.00 45.83           C  
ANISOU 4827  CA  ASP B 240     6748   5330   5337   -766   1620    -36       C  
ATOM   4828  C   ASP B 240      49.358 -40.220  36.806  1.00 46.31           C  
ANISOU 4828  C   ASP B 240     6782   5352   5462   -776   1493     26       C  
ATOM   4829  O   ASP B 240      49.172 -40.218  35.584  1.00 43.80           O  
ANISOU 4829  O   ASP B 240     6291   5055   5295   -753   1413     -2       O  
ATOM   4830  CB  ASP B 240      47.643 -38.471  37.438  1.00 52.44           C  
ANISOU 4830  CB  ASP B 240     7388   6179   6356   -794   1814    -91       C  
ATOM   4831  CG  ASP B 240      46.594 -39.530  37.760  1.00 61.03           C  
ANISOU 4831  CG  ASP B 240     8463   7223   7503   -911   1977    -51       C  
ATOM   4832  OD1 ASP B 240      46.949 -40.634  38.228  1.00 58.77           O  
ANISOU 4832  OD1 ASP B 240     8358   6884   7088   -975   1959     22       O  
ATOM   4833  OD2 ASP B 240      45.396 -39.243  37.538  1.00 63.16           O  
ANISOU 4833  OD2 ASP B 240     8524   7502   7971   -939   2123    -85       O  
ATOM   4834  N   PHE B 241      49.807 -41.284  37.479  1.00 44.20           N  
ANISOU 4834  N   PHE B 241     6705   5017   5073   -817   1472    110       N  
ATOM   4835  CA  PHE B 241      50.223 -42.516  36.813  1.00 46.75           C  
ANISOU 4835  CA  PHE B 241     7039   5267   5456   -815   1365    166       C  
ATOM   4836  C   PHE B 241      49.235 -43.663  37.011  1.00 49.94           C  
ANISOU 4836  C   PHE B 241     7478   5592   5905   -937   1500    210       C  
ATOM   4837  O   PHE B 241      49.594 -44.827  36.797  1.00 49.21           O  
ANISOU 4837  O   PHE B 241     7467   5399   5829   -951   1442    270       O  
ATOM   4838  CB  PHE B 241      51.612 -42.931  37.299  1.00 44.54           C  
ANISOU 4838  CB  PHE B 241     6927   4939   5059   -749   1207    250       C  
ATOM   4839  CG  PHE B 241      52.675 -41.891  37.051  1.00 43.68           C  
ANISOU 4839  CG  PHE B 241     6764   4901   4933   -646   1063    210       C  
ATOM   4840  CD1 PHE B 241      52.814 -40.804  37.908  1.00 51.27           C  
ANISOU 4840  CD1 PHE B 241     7795   5925   5759   -651   1077    182       C  
ATOM   4841  CD2 PHE B 241      53.527 -41.993  35.962  1.00 45.50           C  
ANISOU 4841  CD2 PHE B 241     6884   5123   5279   -560    935    190       C  
ATOM   4842  CE1 PHE B 241      53.782 -39.842  37.683  1.00 48.00           C  
ANISOU 4842  CE1 PHE B 241     7330   5568   5340   -577    945    142       C  
ATOM   4843  CE2 PHE B 241      54.503 -41.028  35.728  1.00 51.61           C  
ANISOU 4843  CE2 PHE B 241     7598   5958   6054   -481    821    154       C  
ATOM   4844  CZ  PHE B 241      54.628 -39.947  36.589  1.00 47.91           C  
ANISOU 4844  CZ  PHE B 241     7187   5554   5463   -492    816    133       C  
ATOM   4845  N   SER B 242      47.991 -43.367  37.393  1.00 46.52           N  
ANISOU 4845  N   SER B 242     6972   5186   5517  -1025   1694    177       N  
ATOM   4846  CA  SER B 242      47.053 -44.431  37.729  1.00 50.77           C  
ANISOU 4846  CA  SER B 242     7548   5646   6097  -1163   1848    223       C  
ATOM   4847  C   SER B 242      46.244 -44.939  36.540  1.00 52.24           C  
ANISOU 4847  C   SER B 242     7523   5823   6503  -1230   1829    182       C  
ATOM   4848  O   SER B 242      45.691 -46.041  36.620  1.00 53.56           O  
ANISOU 4848  O   SER B 242     7734   5901   6717  -1351   1908    223       O  
ATOM   4849  CB  SER B 242      46.099 -43.971  38.843  1.00 56.37           C  
ANISOU 4849  CB  SER B 242     8291   6373   6754  -1248   2109    212       C  
ATOM   4850  OG  SER B 242      45.338 -42.850  38.444  1.00 56.87           O  
ANISOU 4850  OG  SER B 242     8108   6522   6976  -1217   2189    116       O  
ATOM   4851  N   HIS B 243      46.160 -44.186  35.447  1.00 47.98           N  
ANISOU 4851  N   HIS B 243     6776   5367   6087  -1171   1717    109       N  
ATOM   4852  CA  HIS B 243      45.394 -44.603  34.280  1.00 50.43           C  
ANISOU 4852  CA  HIS B 243     6901   5680   6578  -1254   1658     72       C  
ATOM   4853  C   HIS B 243      46.331 -44.942  33.127  1.00 49.81           C  
ANISOU 4853  C   HIS B 243     6864   5580   6480  -1202   1456     46       C  
ATOM   4854  O   HIS B 243      47.516 -44.598  33.143  1.00 45.16           O  
ANISOU 4854  O   HIS B 243     6377   4997   5786  -1078   1367     49       O  
ATOM   4855  CB  HIS B 243      44.412 -43.509  33.847  1.00 56.44           C  
ANISOU 4855  CB  HIS B 243     7391   6546   7509  -1249   1678     25       C  
ATOM   4856  CG  HIS B 243      43.600 -42.950  34.975  1.00 73.79           C  
ANISOU 4856  CG  HIS B 243     9534   8759   9745  -1268   1916     28       C  
ATOM   4857  ND1 HIS B 243      42.551 -43.637  35.550  1.00 73.71           N  
ANISOU 4857  ND1 HIS B 243     9479   8700   9826  -1410   2115     51       N  
ATOM   4858  CD2 HIS B 243      43.683 -41.769  35.635  1.00 74.64           C  
ANISOU 4858  CD2 HIS B 243     9635   8910   9812  -1172   2015     -2       C  
ATOM   4859  CE1 HIS B 243      42.026 -42.906  36.516  1.00 74.87           C  
ANISOU 4859  CE1 HIS B 243     9595   8865   9987  -1396   2344     34       C  
ATOM   4860  NE2 HIS B 243      42.694 -41.769  36.589  1.00 76.82           N  
ANISOU 4860  NE2 HIS B 243     9874   9163  10151  -1252   2287     -4       N  
ATOM   4861  N   SER B 244      45.787 -45.617  32.106  1.00 43.63           N  
ANISOU 4861  N   SER B 244     6004   4770   5803  -1310   1391     12       N  
ATOM   4862  CA  SER B 244      46.626 -45.978  30.964  1.00 42.78           C  
ANISOU 4862  CA  SER B 244     5964   4627   5663  -1281   1240    -34       C  
ATOM   4863  C   SER B 244      47.215 -44.745  30.293  1.00 44.46           C  
ANISOU 4863  C   SER B 244     6099   4948   5846  -1160   1121    -72       C  
ATOM   4864  O   SER B 244      48.360 -44.785  29.825  1.00 41.90           O  
ANISOU 4864  O   SER B 244     5876   4596   5448  -1075   1050    -94       O  
ATOM   4865  CB  SER B 244      45.847 -46.823  29.953  1.00 47.31           C  
ANISOU 4865  CB  SER B 244     6489   5157   6329  -1452   1187    -81       C  
ATOM   4866  OG  SER B 244      44.831 -46.091  29.305  1.00 58.54           O  
ANISOU 4866  OG  SER B 244     7685   6695   7862  -1519   1109   -104       O  
ATOM   4867  N   GLN B 245      46.470 -43.642  30.242  1.00 40.51           N  
ANISOU 4867  N   GLN B 245     5414   4557   5421  -1148   1113    -74       N  
ATOM   4868  CA  GLN B 245      47.033 -42.376  29.781  1.00 41.48           C  
ANISOU 4868  CA  GLN B 245     5481   4765   5515  -1028   1020    -93       C  
ATOM   4869  C   GLN B 245      47.595 -41.591  30.964  1.00 43.47           C  
ANISOU 4869  C   GLN B 245     5788   5035   5694   -910   1110    -71       C  
ATOM   4870  O   GLN B 245      46.901 -41.364  31.959  1.00 41.37           O  
ANISOU 4870  O   GLN B 245     5486   4774   5459   -927   1250    -52       O  
ATOM   4871  CB  GLN B 245      46.002 -41.533  29.024  1.00 51.06           C  
ANISOU 4871  CB  GLN B 245     6473   6065   6862  -1062    938    -94       C  
ATOM   4872  CG  GLN B 245      46.574 -40.942  27.712  1.00 71.97           C  
ANISOU 4872  CG  GLN B 245     9128   8759   9458  -1029    762   -117       C  
ATOM   4873  CD  GLN B 245      46.217 -39.477  27.470  1.00 83.50           C  
ANISOU 4873  CD  GLN B 245    10429  10299  11000   -948    701    -88       C  
ATOM   4874  OE1 GLN B 245      45.867 -38.741  28.394  1.00 94.42           O  
ANISOU 4874  OE1 GLN B 245    11723  11695  12460   -873    814    -70       O  
ATOM   4875  NE2 GLN B 245      46.313 -39.051  26.216  1.00 80.47           N  
ANISOU 4875  NE2 GLN B 245    10029   9954  10590   -967    531    -83       N  
ATOM   4876  N   LEU B 246      48.855 -41.187  30.841  1.00 39.09           N  
ANISOU 4876  N   LEU B 246     5326   4484   5042   -805   1039    -82       N  
ATOM   4877  CA  LEU B 246      49.548 -40.420  31.869  1.00 45.89           C  
ANISOU 4877  CA  LEU B 246     6258   5363   5815   -711   1080    -69       C  
ATOM   4878  C   LEU B 246      48.943 -39.025  31.998  1.00 44.74           C  
ANISOU 4878  C   LEU B 246     5982   5288   5731   -672   1120    -93       C  
ATOM   4879  O   LEU B 246      48.803 -38.302  31.015  1.00 46.43           O  
ANISOU 4879  O   LEU B 246     6079   5545   6018   -646   1032   -110       O  
ATOM   4880  CB  LEU B 246      51.035 -40.328  31.504  1.00 41.70           C  
ANISOU 4880  CB  LEU B 246     5811   4822   5213   -623    972    -76       C  
ATOM   4881  CG  LEU B 246      52.078 -40.223  32.616  1.00 51.74           C  
ANISOU 4881  CG  LEU B 246     7210   6074   6377   -557    963    -40       C  
ATOM   4882  CD1 LEU B 246      53.464 -40.595  32.084  1.00 47.20           C  
ANISOU 4882  CD1 LEU B 246     6672   5459   5801   -487    859    -36       C  
ATOM   4883  CD2 LEU B 246      52.093 -38.826  33.193  1.00 58.56           C  
ANISOU 4883  CD2 LEU B 246     8047   7003   7199   -517    984    -67       C  
ATOM   4884  N   GLY B 247      48.576 -38.643  33.229  1.00 43.84           N  
ANISOU 4884  N   GLY B 247     5907   5169   5582   -670   1263    -91       N  
ATOM   4885  CA  GLY B 247      47.943 -37.360  33.465  1.00 48.53           C  
ANISOU 4885  CA  GLY B 247     6386   5796   6259   -627   1349   -126       C  
ATOM   4886  C   GLY B 247      48.951 -36.307  33.877  1.00 43.11           C  
ANISOU 4886  C   GLY B 247     5797   5120   5464   -543   1318   -158       C  
ATOM   4887  O   GLY B 247      49.795 -36.549  34.743  1.00 43.24           O  
ANISOU 4887  O   GLY B 247     5996   5119   5316   -546   1316   -151       O  
ATOM   4888  N   GLY B 248      48.866 -35.136  33.244  1.00 43.65           N  
ANISOU 4888  N   GLY B 248     5747   5210   5629   -477   1276   -184       N  
ATOM   4889  CA  GLY B 248      49.693 -34.008  33.665  1.00 41.57           C  
ANISOU 4889  CA  GLY B 248     5567   4942   5286   -414   1269   -226       C  
ATOM   4890  C   GLY B 248      51.175 -34.210  33.395  1.00 42.74           C  
ANISOU 4890  C   GLY B 248     5825   5104   5311   -396   1111   -216       C  
ATOM   4891  O   GLY B 248      51.582 -34.695  32.330  1.00 43.16           O  
ANISOU 4891  O   GLY B 248     5832   5171   5394   -392    992   -191       O  
ATOM   4892  N   LEU B 249      51.995 -33.814  34.380  1.00 44.63           N  
ANISOU 4892  N   LEU B 249     6210   5334   5413   -394   1115   -242       N  
ATOM   4893  CA  LEU B 249      53.456 -33.905  34.338  1.00 41.25           C  
ANISOU 4893  CA  LEU B 249     5859   4917   4896   -377    965   -228       C  
ATOM   4894  C   LEU B 249      54.055 -32.947  33.309  1.00 42.93           C  
ANISOU 4894  C   LEU B 249     5980   5145   5188   -329    881   -252       C  
ATOM   4895  O   LEU B 249      54.692 -33.374  32.339  1.00 43.14           O  
ANISOU 4895  O   LEU B 249     5955   5182   5253   -313    788   -228       O  
ATOM   4896  CB  LEU B 249      53.906 -35.348  34.059  1.00 40.04           C  
ANISOU 4896  CB  LEU B 249     5730   4752   4729   -388    887   -164       C  
ATOM   4897  CG  LEU B 249      55.316 -35.746  34.504  1.00 44.77           C  
ANISOU 4897  CG  LEU B 249     6419   5342   5249   -371    756   -125       C  
ATOM   4898  CD1 LEU B 249      55.458 -35.669  36.030  1.00 40.77           C  
ANISOU 4898  CD1 LEU B 249     6086   4830   4576   -418    762   -107       C  
ATOM   4899  CD2 LEU B 249      55.657 -37.149  33.992  1.00 52.57           C  
ANISOU 4899  CD2 LEU B 249     7398   6287   6288   -356    706    -67       C  
ATOM   4900  N   HIS B 250      53.886 -31.642  33.527  1.00 37.88           N  
ANISOU 4900  N   HIS B 250     5334   4490   4569   -312    933   -304       N  
ATOM   4901  CA  HIS B 250      54.271 -30.638  32.541  1.00 38.25           C  
ANISOU 4901  CA  HIS B 250     5301   4532   4700   -275    875   -314       C  
ATOM   4902  C   HIS B 250      55.413 -29.733  32.977  1.00 38.20           C  
ANISOU 4902  C   HIS B 250     5370   4511   4631   -286    824   -358       C  
ATOM   4903  O   HIS B 250      55.793 -28.830  32.217  1.00 40.89           O  
ANISOU 4903  O   HIS B 250     5661   4835   5040   -267    790   -366       O  
ATOM   4904  CB  HIS B 250      53.054 -29.778  32.188  1.00 40.77           C  
ANISOU 4904  CB  HIS B 250     5520   4817   5153   -238    966   -321       C  
ATOM   4905  CG  HIS B 250      51.920 -30.570  31.618  1.00 42.62           C  
ANISOU 4905  CG  HIS B 250     5640   5070   5482   -242    981   -271       C  
ATOM   4906  ND1 HIS B 250      51.949 -31.088  30.341  1.00 40.32           N  
ANISOU 4906  ND1 HIS B 250     5280   4812   5227   -254    866   -220       N  
ATOM   4907  CD2 HIS B 250      50.739 -30.952  32.156  1.00 43.11           C  
ANISOU 4907  CD2 HIS B 250     5648   5122   5608   -255   1101   -270       C  
ATOM   4908  CE1 HIS B 250      50.824 -31.747  30.113  1.00 42.53           C  
ANISOU 4908  CE1 HIS B 250     5469   5104   5588   -280    886   -187       C  
ATOM   4909  NE2 HIS B 250      50.074 -31.678  31.198  1.00 44.37           N  
ANISOU 4909  NE2 HIS B 250     5690   5312   5857   -278   1031   -213       N  
ATOM   4910  N   LEU B 251      55.949 -29.913  34.179  1.00 39.21           N  
ANISOU 4910  N   LEU B 251     5628   4642   4628   -331    808   -381       N  
ATOM   4911  CA  LEU B 251      57.069 -29.115  34.667  1.00 39.75           C  
ANISOU 4911  CA  LEU B 251     5768   4703   4631   -369    726   -424       C  
ATOM   4912  C   LEU B 251      58.281 -30.018  34.814  1.00 44.49           C  
ANISOU 4912  C   LEU B 251     6373   5344   5186   -387    566   -368       C  
ATOM   4913  O   LEU B 251      58.169 -31.122  35.350  1.00 42.86           O  
ANISOU 4913  O   LEU B 251     6223   5152   4911   -394    543   -315       O  
ATOM   4914  CB  LEU B 251      56.750 -28.462  36.014  1.00 38.55           C  
ANISOU 4914  CB  LEU B 251     5785   4514   4348   -429    813   -501       C  
ATOM   4915  CG  LEU B 251      56.033 -27.103  36.015  1.00 47.11           C  
ANISOU 4915  CG  LEU B 251     6877   5520   5504   -412    964   -587       C  
ATOM   4916  CD1 LEU B 251      56.985 -25.984  35.557  1.00 47.53           C  
ANISOU 4916  CD1 LEU B 251     6911   5540   5608   -427    880   -623       C  
ATOM   4917  CD2 LEU B 251      54.771 -27.125  35.157  1.00 50.21           C  
ANISOU 4917  CD2 LEU B 251     7116   5891   6072   -326   1080   -553       C  
ATOM   4918  N   LEU B 252      59.441 -29.542  34.358  1.00 39.09           N  
ANISOU 4918  N   LEU B 252     5623   4669   4562   -394    461   -372       N  
ATOM   4919  CA  LEU B 252      60.624 -30.402  34.356  1.00 45.48           C  
ANISOU 4919  CA  LEU B 252     6377   5506   5398   -389    317   -310       C  
ATOM   4920  C   LEU B 252      60.965 -30.885  35.762  1.00 41.37           C  
ANISOU 4920  C   LEU B 252     5989   4997   4732   -442    204   -276       C  
ATOM   4921  O   LEU B 252      61.364 -32.044  35.952  1.00 44.05           O  
ANISOU 4921  O   LEU B 252     6315   5341   5080   -413    115   -190       O  
ATOM   4922  CB  LEU B 252      61.817 -29.666  33.738  1.00 39.20           C  
ANISOU 4922  CB  LEU B 252     5469   4712   4711   -404    246   -328       C  
ATOM   4923  CG  LEU B 252      63.076 -30.535  33.616  1.00 42.81           C  
ANISOU 4923  CG  LEU B 252     5813   5187   5267   -381    117   -263       C  
ATOM   4924  CD1 LEU B 252      62.809 -31.731  32.682  1.00 43.92           C  
ANISOU 4924  CD1 LEU B 252     5883   5314   5493   -300    194   -218       C  
ATOM   4925  CD2 LEU B 252      64.280 -29.731  33.139  1.00 43.71           C  
ANISOU 4925  CD2 LEU B 252     5798   5303   5507   -416     64   -287       C  
ATOM   4926  N   ILE B 253      60.796 -30.021  36.767  1.00 41.31           N  
ANISOU 4926  N   ILE B 253     6133   4982   4581   -524    208   -340       N  
ATOM   4927  CA  ILE B 253      61.146 -30.405  38.131  1.00 41.87           C  
ANISOU 4927  CA  ILE B 253     6378   5067   4464   -604     82   -305       C  
ATOM   4928  C   ILE B 253      60.318 -31.598  38.596  1.00 44.33           C  
ANISOU 4928  C   ILE B 253     6790   5372   4683   -585    148   -235       C  
ATOM   4929  O   ILE B 253      60.794 -32.426  39.384  1.00 46.76           O  
ANISOU 4929  O   ILE B 253     7192   5687   4886   -615      2   -141       O  
ATOM   4930  CB  ILE B 253      60.996 -29.197  39.079  1.00 45.15           C  
ANISOU 4930  CB  ILE B 253     6982   5460   4711   -718    115   -416       C  
ATOM   4931  CG1 ILE B 253      61.586 -29.524  40.451  1.00 46.94           C  
ANISOU 4931  CG1 ILE B 253     7413   5711   4710   -834    -70   -375       C  
ATOM   4932  CG2 ILE B 253      59.530 -28.775  39.194  1.00 43.58           C  
ANISOU 4932  CG2 ILE B 253     6875   5213   4468   -705    385   -500       C  
ATOM   4933  CD1 ILE B 253      61.678 -28.320  41.400  1.00 46.36           C  
ANISOU 4933  CD1 ILE B 253     7556   5612   4444   -982    -70   -501       C  
ATOM   4934  N   GLY B 254      59.085 -31.727  38.104  1.00 43.77           N  
ANISOU 4934  N   GLY B 254     6689   5279   4661   -540    355   -265       N  
ATOM   4935  CA  GLY B 254      58.278 -32.881  38.471  1.00 41.70           C  
ANISOU 4935  CA  GLY B 254     6503   5004   4338   -536    434   -199       C  
ATOM   4936  C   GLY B 254      58.780 -34.157  37.822  1.00 44.21           C  
ANISOU 4936  C   GLY B 254     6707   5315   4774   -466    332    -93       C  
ATOM   4937  O   GLY B 254      58.737 -35.230  38.427  1.00 47.37           O  
ANISOU 4937  O   GLY B 254     7208   5691   5098   -479    292     -1       O  
ATOM   4938  N   LEU B 255      59.253 -34.062  36.577  1.00 44.67           N  
ANISOU 4938  N   LEU B 255     6575   5378   5019   -395    308   -105       N  
ATOM   4939  CA  LEU B 255      59.937 -35.197  35.966  1.00 52.74           C  
ANISOU 4939  CA  LEU B 255     7496   6374   6167   -327    226    -25       C  
ATOM   4940  C   LEU B 255      61.201 -35.542  36.734  1.00 50.33           C  
ANISOU 4940  C   LEU B 255     7212   6064   5845   -328     16     62       C  
ATOM   4941  O   LEU B 255      61.530 -36.719  36.902  1.00 44.00           O  
ANISOU 4941  O   LEU B 255     6417   5215   5087   -284    -57    165       O  
ATOM   4942  CB  LEU B 255      60.283 -34.899  34.509  1.00 46.72           C  
ANISOU 4942  CB  LEU B 255     6556   5615   5581   -272    267    -72       C  
ATOM   4943  CG  LEU B 255      59.202 -35.016  33.443  1.00 48.86           C  
ANISOU 4943  CG  LEU B 255     6780   5880   5907   -260    415   -114       C  
ATOM   4944  CD1 LEU B 255      58.271 -33.829  33.501  1.00 50.04           C  
ANISOU 4944  CD1 LEU B 255     6948   6056   6010   -294    505   -181       C  
ATOM   4945  CD2 LEU B 255      59.869 -35.121  32.068  1.00 47.25           C  
ANISOU 4945  CD2 LEU B 255     6447   5664   5841   -218    424   -133       C  
ATOM   4946  N   ALA B 256      61.922 -34.522  37.209  1.00 41.25           N  
ANISOU 4946  N   ALA B 256     6070   4955   4648   -380    -98     28       N  
ATOM   4947  CA  ALA B 256      63.146 -34.766  37.965  1.00 48.22           C  
ANISOU 4947  CA  ALA B 256     6952   5844   5526   -397   -344    121       C  
ATOM   4948  C   ALA B 256      62.855 -35.537  39.242  1.00 48.00           C  
ANISOU 4948  C   ALA B 256     7147   5798   5294   -449   -434    223       C  
ATOM   4949  O   ALA B 256      63.575 -36.484  39.578  1.00 55.37           O  
ANISOU 4949  O   ALA B 256     8060   6697   6282   -406   -611    362       O  
ATOM   4950  CB  ALA B 256      63.844 -33.445  38.287  1.00 45.69           C  
ANISOU 4950  CB  ALA B 256     6621   5571   5169   -483   -450     50       C  
ATOM   4951  N   LYS B 257      61.798 -35.153  39.962  1.00 48.34           N  
ANISOU 4951  N   LYS B 257     7406   5851   5111   -539   -301    164       N  
ATOM   4952  CA  LYS B 257      61.455 -35.849  41.196  1.00 49.09           C  
ANISOU 4952  CA  LYS B 257     7754   5925   4973   -613   -351    259       C  
ATOM   4953  C   LYS B 257      61.089 -37.303  40.919  1.00 48.38           C  
ANISOU 4953  C   LYS B 257     7645   5766   4969   -535   -302    374       C  
ATOM   4954  O   LYS B 257      61.543 -38.216  41.619  1.00 59.31           O  
ANISOU 4954  O   LYS B 257     9134   7110   6291   -538   -470    527       O  
ATOM   4955  CB  LYS B 257      60.309 -35.125  41.905  1.00 48.80           C  
ANISOU 4955  CB  LYS B 257     7939   5899   4704   -724   -141    147       C  
ATOM   4956  CG  LYS B 257      60.005 -35.668  43.298  1.00 49.39           C  
ANISOU 4956  CG  LYS B 257     8332   5956   4479   -841   -171    230       C  
ATOM   4957  CD  LYS B 257      59.000 -34.778  44.025  1.00 51.19           C  
ANISOU 4957  CD  LYS B 257     8781   6185   4482   -961     70     87       C  
ATOM   4958  CE  LYS B 257      58.677 -35.307  45.413  1.00 58.32           C  
ANISOU 4958  CE  LYS B 257    10041   7067   5050  -1101     76    162       C  
ATOM   4959  NZ  LYS B 257      59.792 -35.085  46.369  1.00 62.21           N  
ANISOU 4959  NZ  LYS B 257    10730   7592   5317  -1214   -242    230       N  
ATOM   4960  N   ARG B 258      60.277 -37.540  39.885  1.00 47.66           N  
ANISOU 4960  N   ARG B 258     7430   5654   5026   -472    -89    308       N  
ATOM   4961  CA  ARG B 258      59.880 -38.910  39.565  1.00 50.03           C  
ANISOU 4961  CA  ARG B 258     7722   5874   5412   -418    -28    396       C  
ATOM   4962  C   ARG B 258      61.078 -39.739  39.124  1.00 49.65           C  
ANISOU 4962  C   ARG B 258     7532   5766   5565   -308   -205    503       C  
ATOM   4963  O   ARG B 258      61.212 -40.906  39.510  1.00 55.12           O  
ANISOU 4963  O   ARG B 258     8303   6372   6270   -278   -273    639       O  
ATOM   4964  CB  ARG B 258      58.812 -38.905  38.475  1.00 45.70           C  
ANISOU 4964  CB  ARG B 258     7060   5322   4982   -395    205    293       C  
ATOM   4965  CG  ARG B 258      58.426 -40.300  37.974  1.00 53.41           C  
ANISOU 4965  CG  ARG B 258     8018   6206   6068   -356    272    357       C  
ATOM   4966  CD  ARG B 258      57.192 -40.821  38.678  1.00 60.43           C  
ANISOU 4966  CD  ARG B 258     9076   7065   6819   -449    424    383       C  
ATOM   4967  NE  ARG B 258      56.860 -42.193  38.288  1.00 65.26           N  
ANISOU 4967  NE  ARG B 258     9694   7572   7532   -433    477    450       N  
ATOM   4968  CZ  ARG B 258      55.897 -42.911  38.859  1.00 67.91           C  
ANISOU 4968  CZ  ARG B 258    10170   7853   7779   -519    604    498       C  
ATOM   4969  NH1 ARG B 258      55.180 -42.378  39.837  1.00 76.93           N  
ANISOU 4969  NH1 ARG B 258    11456   9043   8731   -621    709    482       N  
ATOM   4970  NH2 ARG B 258      55.653 -44.161  38.467  1.00 54.74           N  
ANISOU 4970  NH2 ARG B 258     8511   6072   6216   -514    647    554       N  
ATOM   4971  N   PHE B 259      61.970 -39.136  38.332  1.00 50.77           N  
ANISOU 4971  N   PHE B 259     7465   5942   5884   -245   -269    447       N  
ATOM   4972  CA  PHE B 259      63.094 -39.863  37.751  1.00 58.76           C  
ANISOU 4972  CA  PHE B 259     8295   6886   7145   -126   -379    523       C  
ATOM   4973  C   PHE B 259      64.018 -40.425  38.822  1.00 61.86           C  
ANISOU 4973  C   PHE B 259     8743   7241   7522   -111   -648    700       C  
ATOM   4974  O   PHE B 259      64.512 -41.554  38.693  1.00 58.61           O  
ANISOU 4974  O   PHE B 259     8268   6718   7283     -8   -711    819       O  
ATOM   4975  CB  PHE B 259      63.871 -38.945  36.806  1.00 62.87           C  
ANISOU 4975  CB  PHE B 259     8592   7459   7838    -91   -372    423       C  
ATOM   4976  CG  PHE B 259      64.973 -39.638  36.064  1.00 70.27           C  
ANISOU 4976  CG  PHE B 259     9315   8318   9065     33   -412    471       C  
ATOM   4977  CD1 PHE B 259      64.682 -40.489  35.007  1.00 74.37           C  
ANISOU 4977  CD1 PHE B 259     9779   8748   9729    108   -228    433       C  
ATOM   4978  CD2 PHE B 259      66.297 -39.444  36.422  1.00 75.02           C  
ANISOU 4978  CD2 PHE B 259     9767   8928   9809     68   -626    548       C  
ATOM   4979  CE1 PHE B 259      65.695 -41.136  34.321  1.00 82.68           C  
ANISOU 4979  CE1 PHE B 259    10647   9707  11062    225   -218    459       C  
ATOM   4980  CE2 PHE B 259      67.314 -40.084  35.740  1.00 79.69           C  
ANISOU 4980  CE2 PHE B 259    10130   9433  10714    195   -630    590       C  
ATOM   4981  CZ  PHE B 259      67.015 -40.932  34.690  1.00 77.90           C  
ANISOU 4981  CZ  PHE B 259     9865   9104  10628    279   -407    539       C  
ATOM   4982  N   LYS B 260      64.264 -39.656  39.888  1.00 59.78           N  
ANISOU 4982  N   LYS B 260     8605   7055   7053   -216   -819    724       N  
ATOM   4983  CA  LYS B 260      65.157 -40.128  40.942  1.00 67.41           C  
ANISOU 4983  CA  LYS B 260     9638   7996   7978   -224  -1129    910       C  
ATOM   4984  C   LYS B 260      64.621 -41.382  41.618  1.00 70.08           C  
ANISOU 4984  C   LYS B 260    10191   8234   8202   -220  -1138   1065       C  
ATOM   4985  O   LYS B 260      65.399 -42.179  42.152  1.00 76.38           O  
ANISOU 4985  O   LYS B 260    10990   8958   9072   -164  -1381   1260       O  
ATOM   4986  CB  LYS B 260      65.392 -39.021  41.973  1.00 71.98           C  
ANISOU 4986  CB  LYS B 260    10370   8681   8298   -380  -1302    884       C  
ATOM   4987  CG  LYS B 260      66.507 -38.056  41.588  1.00 85.42           C  
ANISOU 4987  CG  LYS B 260    11832  10450  10173   -379  -1449    823       C  
ATOM   4988  CD  LYS B 260      67.862 -38.765  41.527  1.00 95.20           C  
ANISOU 4988  CD  LYS B 260    12830  11637  11702   -266  -1721    993       C  
ATOM   4989  CE  LYS B 260      68.902 -37.948  40.763  1.00 96.07           C  
ANISOU 4989  CE  LYS B 260    12619  11795  12088   -237  -1768    912       C  
ATOM   4990  NZ  LYS B 260      68.623 -37.896  39.296  1.00 90.68           N  
ANISOU 4990  NZ  LYS B 260    11747  11082  11625   -134  -1446    771       N  
ATOM   4991  N   GLU B 261      63.305 -41.584  41.593  1.00 71.59           N  
ANISOU 4991  N   GLU B 261    10550   8411   8238   -279   -880    994       N  
ATOM   4992  CA  GLU B 261      62.679 -42.735  42.229  1.00 73.44           C  
ANISOU 4992  CA  GLU B 261    11007   8544   8352   -303   -845   1132       C  
ATOM   4993  C   GLU B 261      62.360 -43.861  41.256  1.00 66.33           C  
ANISOU 4993  C   GLU B 261     9992   7514   7698   -188   -678   1141       C  
ATOM   4994  O   GLU B 261      62.571 -45.032  41.583  1.00 61.55           O  
ANISOU 4994  O   GLU B 261     9462   6773   7151   -135   -762   1311       O  
ATOM   4995  CB  GLU B 261      61.396 -42.303  42.946  1.00 83.49           C  
ANISOU 4995  CB  GLU B 261    12552   9871   9301   -466   -649   1054       C  
ATOM   4996  CG  GLU B 261      61.633 -41.309  44.071  1.00 96.03           C  
ANISOU 4996  CG  GLU B 261    14340  11558  10590   -607   -790   1042       C  
ATOM   4997  CD  GLU B 261      62.856 -41.657  44.910  1.00103.13           C  
ANISOU 4997  CD  GLU B 261    15307  12438  11439   -609  -1178   1245       C  
ATOM   4998  OE1 GLU B 261      63.897 -40.982  44.754  1.00105.68           O  
ANISOU 4998  OE1 GLU B 261    15454  12824  11875   -582  -1393   1228       O  
ATOM   4999  OE2 GLU B 261      62.781 -42.609  45.717  1.00103.94           O  
ANISOU 4999  OE2 GLU B 261    15632  12460  11402   -642  -1279   1434       O  
ATOM   5000  N   SER B 262      61.873 -43.539  40.064  1.00 57.84           N  
ANISOU 5000  N   SER B 262     8751   6464   6762   -157   -454    965       N  
ATOM   5001  CA  SER B 262      61.442 -44.564  39.125  1.00 58.86           C  
ANISOU 5001  CA  SER B 262     8813   6472   7078    -88   -280    945       C  
ATOM   5002  C   SER B 262      61.717 -44.108  37.697  1.00 58.54           C  
ANISOU 5002  C   SER B 262     8526   6463   7255    -15   -169    786       C  
ATOM   5003  O   SER B 262      61.235 -43.047  37.288  1.00 54.49           O  
ANISOU 5003  O   SER B 262     7965   6069   6670    -75    -70    643       O  
ATOM   5004  CB  SER B 262      59.955 -44.860  39.333  1.00 57.39           C  
ANISOU 5004  CB  SER B 262     8805   6278   6724   -207    -63    903       C  
ATOM   5005  OG  SER B 262      59.532 -45.940  38.534  1.00 68.08           O  
ANISOU 5005  OG  SER B 262    10124   7501   8241   -170     78    892       O  
ATOM   5006  N   PRO B 263      62.469 -44.874  36.910  1.00 59.62           N  
ANISOU 5006  N   PRO B 263     8515   6482   7655    111   -167    807       N  
ATOM   5007  CA  PRO B 263      62.863 -44.405  35.577  1.00 59.83           C  
ANISOU 5007  CA  PRO B 263     8333   6536   7862    166    -54    658       C  
ATOM   5008  C   PRO B 263      61.709 -44.442  34.586  1.00 56.38           C  
ANISOU 5008  C   PRO B 263     7929   6108   7384     97    179    510       C  
ATOM   5009  O   PRO B 263      60.728 -45.173  34.745  1.00 54.28           O  
ANISOU 5009  O   PRO B 263     7802   5781   7040     36    271    526       O  
ATOM   5010  CB  PRO B 263      63.966 -45.387  35.173  1.00 68.91           C  
ANISOU 5010  CB  PRO B 263     9350   7526   9308    318    -91    733       C  
ATOM   5011  CG  PRO B 263      63.603 -46.645  35.891  1.00 68.94           C  
ANISOU 5011  CG  PRO B 263     9526   7379   9288    330   -126    882       C  
ATOM   5012  CD  PRO B 263      63.014 -46.209  37.211  1.00 70.55           C  
ANISOU 5012  CD  PRO B 263     9930   7685   9191    209   -252    970       C  
ATOM   5013  N   PHE B 264      61.843 -43.630  33.540  1.00 51.73           N  
ANISOU 5013  N   PHE B 264     7209   5595   6849     96    264    373       N  
ATOM   5014  CA  PHE B 264      60.864 -43.616  32.466  1.00 43.27           C  
ANISOU 5014  CA  PHE B 264     6156   4537   5748     28    443    243       C  
ATOM   5015  C   PHE B 264      61.556 -43.227  31.167  1.00 47.11           C  
ANISOU 5015  C   PHE B 264     6504   5029   6367     71    524    134       C  
ATOM   5016  O   PHE B 264      62.700 -42.768  31.161  1.00 50.14           O  
ANISOU 5016  O   PHE B 264     6758   5429   6864    142    458    149       O  
ATOM   5017  CB  PHE B 264      59.703 -42.677  32.783  1.00 39.91           C  
ANISOU 5017  CB  PHE B 264     5791   4244   5130    -83    470    196       C  
ATOM   5018  CG  PHE B 264      60.143 -41.313  33.224  1.00 47.03           C  
ANISOU 5018  CG  PHE B 264     6638   5268   5964    -87    380    182       C  
ATOM   5019  CD1 PHE B 264      60.513 -40.363  32.294  1.00 50.22           C  
ANISOU 5019  CD1 PHE B 264     6922   5736   6422    -78    410     89       C  
ATOM   5020  CD2 PHE B 264      60.207 -40.990  34.572  1.00 53.28           C  
ANISOU 5020  CD2 PHE B 264     7523   6098   6622   -116    268    260       C  
ATOM   5021  CE1 PHE B 264      60.932 -39.100  32.696  1.00 59.90           C  
ANISOU 5021  CE1 PHE B 264     8106   7054   7598    -93    332     72       C  
ATOM   5022  CE2 PHE B 264      60.619 -39.734  34.984  1.00 57.14           C  
ANISOU 5022  CE2 PHE B 264     7985   6685   7041   -140    187    229       C  
ATOM   5023  CZ  PHE B 264      60.981 -38.786  34.044  1.00 56.39           C  
ANISOU 5023  CZ  PHE B 264     7753   6644   7029   -126    220    134       C  
ATOM   5024  N   GLU B 265      60.842 -43.427  30.060  1.00 41.40           N  
ANISOU 5024  N   GLU B 265     5816   4290   5624      9    666     26       N  
ATOM   5025  CA  GLU B 265      61.366 -43.226  28.717  1.00 41.37           C  
ANISOU 5025  CA  GLU B 265     5742   4272   5703     20    780    -85       C  
ATOM   5026  C   GLU B 265      60.754 -41.964  28.126  1.00 44.59           C  
ANISOU 5026  C   GLU B 265     6139   4825   5978    -69    789   -159       C  
ATOM   5027  O   GLU B 265      59.538 -41.769  28.210  1.00 43.24           O  
ANISOU 5027  O   GLU B 265     6035   4713   5682   -156    780   -167       O  
ATOM   5028  CB  GLU B 265      61.046 -44.433  27.831  1.00 47.26           C  
ANISOU 5028  CB  GLU B 265     6581   4876   6500     -5    924   -154       C  
ATOM   5029  CG  GLU B 265      61.744 -44.433  26.486  1.00 73.58           C  
ANISOU 5029  CG  GLU B 265     9884   8158   9915      6   1075   -274       C  
ATOM   5030  CD  GLU B 265      63.140 -45.022  26.565  1.00 91.89           C  
ANISOU 5030  CD  GLU B 265    12093  10341  12481    154   1129   -246       C  
ATOM   5031  OE1 GLU B 265      63.325 -46.024  27.296  1.00 92.59           O  
ANISOU 5031  OE1 GLU B 265    12195  10298  12686    234   1090   -155       O  
ATOM   5032  OE2 GLU B 265      64.050 -44.477  25.905  1.00100.61           O  
ANISOU 5032  OE2 GLU B 265    13088  11461  13678    190   1214   -306       O  
ATOM   5033  N   LEU B 266      61.596 -41.111  27.535  1.00 41.44           N  
ANISOU 5033  N   LEU B 266     5645   4473   5628    -46    811   -204       N  
ATOM   5034  CA  LEU B 266      61.163 -39.885  26.861  1.00 41.37           C  
ANISOU 5034  CA  LEU B 266     5632   4576   5511   -121    822   -260       C  
ATOM   5035  C   LEU B 266      61.619 -39.938  25.410  1.00 44.76           C  
ANISOU 5035  C   LEU B 266     6074   4966   5967   -148    963   -354       C  
ATOM   5036  O   LEU B 266      62.823 -39.861  25.133  1.00 50.60           O  
ANISOU 5036  O   LEU B 266     6723   5666   6837    -89   1030   -373       O  
ATOM   5037  CB  LEU B 266      61.745 -38.640  27.531  1.00 43.04           C  
ANISOU 5037  CB  LEU B 266     5751   4876   5727    -97    727   -225       C  
ATOM   5038  CG  LEU B 266      61.347 -38.234  28.942  1.00 46.97           C  
ANISOU 5038  CG  LEU B 266     6269   5428   6149    -98    599   -155       C  
ATOM   5039  CD1 LEU B 266      62.013 -36.907  29.280  1.00 48.36           C  
ANISOU 5039  CD1 LEU B 266     6372   5677   6327   -102    529   -158       C  
ATOM   5040  CD2 LEU B 266      59.846 -38.120  29.034  1.00 46.87           C  
ANISOU 5040  CD2 LEU B 266     6345   5456   6009   -168    619   -164       C  
ATOM   5041  N  AGLU B 267      60.673 -40.071  24.482  0.57 39.12           N  
ANISOU 5041  N  AGLU B 267     5473   4260   5131   -250   1010   -411       N  
ATOM   5042  N  BGLU B 267      60.668 -40.056  24.489  0.43 39.14           N  
ANISOU 5042  N  BGLU B 267     5474   4264   5132   -250   1009   -410       N  
ATOM   5043  CA AGLU B 267      60.984 -40.014  23.055  0.57 38.10           C  
ANISOU 5043  CA AGLU B 267     5413   4104   4958   -313   1141   -503       C  
ATOM   5044  CA BGLU B 267      60.966 -40.006  23.063  0.43 38.99           C  
ANISOU 5044  CA BGLU B 267     5526   4219   5070   -314   1138   -502       C  
ATOM   5045  C  AGLU B 267      60.859 -38.560  22.617  0.57 42.44           C  
ANISOU 5045  C  AGLU B 267     5946   4767   5412   -366   1094   -492       C  
ATOM   5046  C  BGLU B 267      60.856 -38.552  22.619  0.43 41.88           C  
ANISOU 5046  C  BGLU B 267     5874   4696   5340   -366   1093   -491       C  
ATOM   5047  O  AGLU B 267      59.769 -37.979  22.661  0.57 38.31           O  
ANISOU 5047  O  AGLU B 267     5452   4322   4783   -424    986   -455       O  
ATOM   5048  O  BGLU B 267      59.768 -37.967  22.648  0.43 38.92           O  
ANISOU 5048  O  BGLU B 267     5529   4400   4858   -425    986   -455       O  
ATOM   5049  CB AGLU B 267      60.070 -40.934  22.247  0.57 42.30           C  
ANISOU 5049  CB AGLU B 267     6105   4581   5385   -422   1187   -568       C  
ATOM   5050  CB BGLU B 267      60.023 -40.903  22.268  0.43 42.29           C  
ANISOU 5050  CB BGLU B 267     6103   4585   5379   -424   1180   -565       C  
ATOM   5051  CG AGLU B 267      59.930 -40.584  20.754  0.57 46.93           C  
ANISOU 5051  CG AGLU B 267     6825   5185   5820   -548   1261   -650       C  
ATOM   5052  CG BGLU B 267      60.062 -42.376  22.647  0.43 44.52           C  
ANISOU 5052  CG BGLU B 267     6429   4727   5759   -386   1241   -580       C  
ATOM   5053  CD AGLU B 267      61.061 -41.101  19.883  0.57 57.50           C  
ANISOU 5053  CD AGLU B 267     8227   6411   7211   -540   1485   -756       C  
ATOM   5054  CD BGLU B 267      59.185 -43.210  21.739  0.43 57.44           C  
ANISOU 5054  CD BGLU B 267     8240   6303   7280   -526   1289   -665       C  
ATOM   5055  OE1AGLU B 267      61.217 -40.599  18.737  0.57 54.14           O  
ANISOU 5055  OE1AGLU B 267     7914   6005   6650   -639   1570   -816       O  
ATOM   5056  OE1BGLU B 267      59.162 -42.916  20.524  0.43 54.16           O  
ANISOU 5056  OE1BGLU B 267     7934   5905   6739   -631   1351   -748       O  
ATOM   5057  OE2AGLU B 267      61.792 -42.010  20.335  0.57 62.09           O  
ANISOU 5057  OE2AGLU B 267     8750   6871   7971   -434   1585   -774       O  
ATOM   5058  OE2BGLU B 267      58.508 -44.141  22.239  0.43 58.79           O  
ANISOU 5058  OE2BGLU B 267     8454   6409   7474   -550   1259   -647       O  
ATOM   5059  N   ASP B 268      61.989 -37.968  22.227  1.00 41.05           N  
ANISOU 5059  N   ASP B 268     5709   4587   5302   -340   1181   -515       N  
ATOM   5060  CA  ASP B 268      62.072 -36.560  21.837  1.00 38.39           C  
ANISOU 5060  CA  ASP B 268     5359   4331   4898   -386   1155   -496       C  
ATOM   5061  C   ASP B 268      61.814 -36.507  20.332  1.00 42.99           C  
ANISOU 5061  C   ASP B 268     6106   4903   5326   -506   1253   -554       C  
ATOM   5062  O   ASP B 268      62.734 -36.508  19.513  1.00 42.45           O  
ANISOU 5062  O   ASP B 268     6069   4786   5272   -532   1425   -616       O  
ATOM   5063  CB  ASP B 268      63.452 -36.027  22.228  1.00 50.30           C  
ANISOU 5063  CB  ASP B 268     6713   5830   6567   -318   1202   -489       C  
ATOM   5064  CG  ASP B 268      63.650 -34.536  21.966  1.00 50.08           C  
ANISOU 5064  CG  ASP B 268     6666   5867   6495   -369   1180   -466       C  
ATOM   5065  OD1 ASP B 268      62.738 -33.832  21.493  1.00 42.03           O  
ANISOU 5065  OD1 ASP B 268     5749   4892   5326   -440   1122   -442       O  
ATOM   5066  OD2 ASP B 268      64.771 -34.068  22.251  1.00 46.27           O  
ANISOU 5066  OD2 ASP B 268     6050   5377   6152   -337   1215   -465       O  
ATOM   5067  N   PHE B 269      60.527 -36.516  19.951  1.00 37.55           N  
ANISOU 5067  N   PHE B 269     5529   4254   4483   -592   1146   -534       N  
ATOM   5068  CA  PHE B 269      60.258 -36.827  18.545  1.00 38.10           C  
ANISOU 5068  CA  PHE B 269     5796   4300   4380   -728   1218   -595       C  
ATOM   5069  C   PHE B 269      60.437 -35.625  17.623  1.00 36.96           C  
ANISOU 5069  C   PHE B 269     5732   4200   4109   -808   1227   -565       C  
ATOM   5070  O   PHE B 269      60.412 -35.798  16.399  1.00 38.85           O  
ANISOU 5070  O   PHE B 269     6170   4417   4176   -937   1305   -615       O  
ATOM   5071  CB  PHE B 269      58.858 -37.458  18.370  1.00 37.72           C  
ANISOU 5071  CB  PHE B 269     5841   4270   4222   -816   1082   -586       C  
ATOM   5072  CG  PHE B 269      57.731 -36.655  18.969  1.00 35.75           C  
ANISOU 5072  CG  PHE B 269     5493   4113   3976   -803    874   -477       C  
ATOM   5073  CD1 PHE B 269      57.312 -36.883  20.269  1.00 35.85           C  
ANISOU 5073  CD1 PHE B 269     5367   4138   4118   -712    811   -436       C  
ATOM   5074  CD2 PHE B 269      57.086 -35.677  18.222  1.00 38.48           C  
ANISOU 5074  CD2 PHE B 269     5896   4522   4204   -883    753   -409       C  
ATOM   5075  CE1 PHE B 269      56.255 -36.147  20.820  1.00 47.10           C  
ANISOU 5075  CE1 PHE B 269     6698   5632   5566   -698    667   -352       C  
ATOM   5076  CE2 PHE B 269      56.044 -34.932  18.760  1.00 38.55           C  
ANISOU 5076  CE2 PHE B 269     5790   4594   4265   -852    582   -308       C  
ATOM   5077  CZ  PHE B 269      55.625 -35.164  20.060  1.00 40.35           C  
ANISOU 5077  CZ  PHE B 269     5867   4828   4635   -758    557   -290       C  
ATOM   5078  N   ILE B 270      60.655 -34.431  18.170  1.00 36.16           N  
ANISOU 5078  N   ILE B 270     5511   4148   4080   -749   1159   -488       N  
ATOM   5079  CA  ILE B 270      61.088 -33.266  17.400  1.00 38.59           C  
ANISOU 5079  CA  ILE B 270     5885   4470   4308   -813   1202   -454       C  
ATOM   5080  C   ILE B 270      62.360 -32.756  18.067  1.00 42.34           C  
ANISOU 5080  C   ILE B 270     6192   4926   4969   -727   1306   -466       C  
ATOM   5081  O   ILE B 270      62.285 -31.842  18.901  1.00 42.46           O  
ANISOU 5081  O   ILE B 270     6091   4976   5067   -670   1195   -402       O  
ATOM   5082  CB  ILE B 270      60.024 -32.154  17.378  1.00 46.12           C  
ANISOU 5082  CB  ILE B 270     6854   5482   5187   -837    999   -336       C  
ATOM   5083  CG1 ILE B 270      58.659 -32.697  16.966  1.00 49.15           C  
ANISOU 5083  CG1 ILE B 270     7331   5896   5448   -908    841   -306       C  
ATOM   5084  CG2 ILE B 270      60.455 -31.016  16.456  1.00 43.91           C  
ANISOU 5084  CG2 ILE B 270     6686   5193   4806   -919   1044   -286       C  
ATOM   5085  CD1 ILE B 270      57.521 -31.717  17.258  1.00 50.94           C  
ANISOU 5085  CD1 ILE B 270     7486   6169   5698   -883    628   -179       C  
ATOM   5086  N   PRO B 271      63.531 -33.331  17.773  1.00 37.37           N  
ANISOU 5086  N   PRO B 271     5534   4235   4431   -718   1516   -550       N  
ATOM   5087  CA  PRO B 271      64.754 -33.031  18.562  1.00 42.05           C  
ANISOU 5087  CA  PRO B 271     5910   4812   5257   -629   1580   -556       C  
ATOM   5088  C   PRO B 271      65.423 -31.712  18.181  1.00 39.86           C  
ANISOU 5088  C   PRO B 271     5614   4545   4987   -691   1643   -526       C  
ATOM   5089  O   PRO B 271      66.390 -31.642  17.431  1.00 43.71           O  
ANISOU 5089  O   PRO B 271     6109   4987   5513   -744   1859   -577       O  
ATOM   5090  CB  PRO B 271      65.655 -34.233  18.258  1.00 39.89           C  
ANISOU 5090  CB  PRO B 271     5599   4449   5108   -592   1794   -653       C  
ATOM   5091  CG  PRO B 271      65.244 -34.661  16.870  1.00 46.50           C  
ANISOU 5091  CG  PRO B 271     6696   5250   5722   -719   1935   -721       C  
ATOM   5092  CD  PRO B 271      63.737 -34.440  16.823  1.00 44.04           C  
ANISOU 5092  CD  PRO B 271     6525   5009   5198   -780   1700   -653       C  
ATOM   5093  N   MET B 272      64.888 -30.624  18.727  1.00 40.50           N  
ANISOU 5093  N   MET B 272     5673   4673   5043   -687   1469   -444       N  
ATOM   5094  CA  MET B 272      65.458 -29.296  18.540  1.00 41.39           C  
ANISOU 5094  CA  MET B 272     5765   4779   5182   -744   1504   -406       C  
ATOM   5095  C   MET B 272      65.348 -28.529  19.853  1.00 37.44           C  
ANISOU 5095  C   MET B 272     5125   4304   4794   -678   1330   -364       C  
ATOM   5096  O   MET B 272      64.718 -28.982  20.807  1.00 43.24           O  
ANISOU 5096  O   MET B 272     5811   5069   5550   -598   1191   -356       O  
ATOM   5097  CB  MET B 272      64.742 -28.544  17.418  1.00 42.48           C  
ANISOU 5097  CB  MET B 272     6127   4912   5099   -855   1493   -343       C  
ATOM   5098  CG  MET B 272      63.265 -28.315  17.732  1.00 43.82           C  
ANISOU 5098  CG  MET B 272     6357   5120   5172   -822   1261   -264       C  
ATOM   5099  SD  MET B 272      62.408 -27.586  16.336  1.00 54.49           S  
ANISOU 5099  SD  MET B 272     7964   6461   6279   -947   1200   -160       S  
ATOM   5100  CE  MET B 272      63.036 -25.904  16.386  1.00 54.20           C  
ANISOU 5100  CE  MET B 272     7908   6369   6315   -975   1231    -85       C  
ATOM   5101  N   ASP B 273      65.986 -27.360  19.898  1.00 34.87           N  
ANISOU 5101  N   ASP B 273     4757   3959   4535   -728   1356   -343       N  
ATOM   5102  CA  ASP B 273      65.908 -26.482  21.060  1.00 42.25           C  
ANISOU 5102  CA  ASP B 273     5602   4898   5551   -697   1209   -319       C  
ATOM   5103  C   ASP B 273      64.604 -25.692  20.991  1.00 34.67           C  
ANISOU 5103  C   ASP B 273     4780   3929   4464   -695   1094   -250       C  
ATOM   5104  O   ASP B 273      64.330 -25.047  19.973  1.00 41.88           O  
ANISOU 5104  O   ASP B 273     5828   4808   5277   -763   1135   -194       O  
ATOM   5105  CB  ASP B 273      67.104 -25.527  21.070  1.00 42.80           C  
ANISOU 5105  CB  ASP B 273     5577   4932   5752   -773   1289   -331       C  
ATOM   5106  CG  ASP B 273      67.402 -24.957  22.451  1.00 49.01           C  
ANISOU 5106  CG  ASP B 273     6240   5726   6656   -753   1143   -345       C  
ATOM   5107  OD1 ASP B 273      67.035 -25.607  23.456  1.00 44.60           O  
ANISOU 5107  OD1 ASP B 273     5634   5209   6104   -672   1014   -357       O  
ATOM   5108  OD2 ASP B 273      68.019 -23.860  22.527  1.00 41.54           O  
ANISOU 5108  OD2 ASP B 273     5262   4738   5784   -836   1162   -346       O  
ATOM   5109  N   SER B 274      63.798 -25.749  22.050  1.00 40.07           N  
ANISOU 5109  N   SER B 274     5432   4635   5159   -618    956   -246       N  
ATOM   5110  CA  SER B 274      62.577 -24.947  22.057  1.00 41.87           C  
ANISOU 5110  CA  SER B 274     5747   4836   5327   -598    866   -182       C  
ATOM   5111  C   SER B 274      62.119 -24.681  23.483  1.00 35.91           C  
ANISOU 5111  C   SER B 274     4933   4080   4633   -531    777   -210       C  
ATOM   5112  O   SER B 274      62.412 -25.446  24.407  1.00 38.95           O  
ANISOU 5112  O   SER B 274     5243   4507   5048   -496    749   -260       O  
ATOM   5113  CB  SER B 274      61.448 -25.606  21.245  1.00 47.27           C  
ANISOU 5113  CB  SER B 274     6521   5547   5891   -589    823   -132       C  
ATOM   5114  OG  SER B 274      61.144 -26.901  21.716  1.00 49.08           O  
ANISOU 5114  OG  SER B 274     6703   5830   6117   -541    800   -176       O  
ATOM   5115  N   THR B 275      61.393 -23.569  23.646  1.00 34.04           N  
ANISOU 5115  N   THR B 275     4744   3780   4410   -515    742   -171       N  
ATOM   5116  CA  THR B 275      60.920 -23.178  24.970  1.00 30.81           C  
ANISOU 5116  CA  THR B 275     4312   3346   4048   -464    702   -215       C  
ATOM   5117  C   THR B 275      60.034 -24.255  25.591  1.00 36.22           C  
ANISOU 5117  C   THR B 275     4968   4094   4700   -397    664   -227       C  
ATOM   5118  O   THR B 275      60.145 -24.547  26.788  1.00 37.58           O  
ANISOU 5118  O   THR B 275     5120   4286   4871   -382    650   -286       O  
ATOM   5119  CB  THR B 275      60.177 -21.842  24.870  1.00 33.90           C  
ANISOU 5119  CB  THR B 275     4762   3630   4488   -442    703   -169       C  
ATOM   5120  OG1 THR B 275      61.099 -20.827  24.465  1.00 37.76           O  
ANISOU 5120  OG1 THR B 275     5290   4045   5011   -521    746   -164       O  
ATOM   5121  CG2 THR B 275      59.551 -21.456  26.200  1.00 34.76           C  
ANISOU 5121  CG2 THR B 275     4869   3696   4642   -388    707   -233       C  
ATOM   5122  N   VAL B 276      59.149 -24.852  24.799  1.00 34.57           N  
ANISOU 5122  N   VAL B 276     4768   3915   4454   -374    642   -169       N  
ATOM   5123  CA  VAL B 276      58.329 -25.983  25.229  1.00 34.98           C  
ANISOU 5123  CA  VAL B 276     4787   4022   4482   -334    617   -176       C  
ATOM   5124  C   VAL B 276      58.840 -27.216  24.494  1.00 32.81           C  
ANISOU 5124  C   VAL B 276     4521   3801   4146   -370    627   -183       C  
ATOM   5125  O   VAL B 276      59.020 -27.183  23.271  1.00 36.77           O  
ANISOU 5125  O   VAL B 276     5075   4299   4597   -420    639   -149       O  
ATOM   5126  CB  VAL B 276      56.831 -25.759  24.942  1.00 39.80           C  
ANISOU 5126  CB  VAL B 276     5380   4615   5128   -292    575   -110       C  
ATOM   5127  CG1 VAL B 276      56.017 -27.008  25.331  1.00 39.74           C  
ANISOU 5127  CG1 VAL B 276     5327   4665   5106   -275    562   -120       C  
ATOM   5128  CG2 VAL B 276      56.303 -24.541  25.669  1.00 39.44           C  
ANISOU 5128  CG2 VAL B 276     5318   4486   5180   -238    604   -113       C  
ATOM   5129  N   LYS B 277      59.082 -28.293  25.234  1.00 35.36           N  
ANISOU 5129  N   LYS B 277     4811   4158   4465   -350    632   -225       N  
ATOM   5130  CA  LYS B 277      59.528 -29.555  24.655  1.00 40.38           C  
ANISOU 5130  CA  LYS B 277     5455   4815   5072   -368    662   -242       C  
ATOM   5131  C   LYS B 277      58.398 -30.573  24.753  1.00 40.44           C  
ANISOU 5131  C   LYS B 277     5475   4844   5048   -358    632   -230       C  
ATOM   5132  O   LYS B 277      57.639 -30.574  25.722  1.00 39.68           O  
ANISOU 5132  O   LYS B 277     5352   4754   4971   -325    608   -223       O  
ATOM   5133  CB  LYS B 277      60.780 -30.090  25.365  1.00 37.70           C  
ANISOU 5133  CB  LYS B 277     5057   4475   4792   -347    682   -282       C  
ATOM   5134  CG  LYS B 277      62.059 -29.334  25.046  1.00 42.35           C  
ANISOU 5134  CG  LYS B 277     5602   5046   5443   -379    724   -299       C  
ATOM   5135  CD  LYS B 277      62.419 -29.476  23.562  1.00 38.79           C  
ANISOU 5135  CD  LYS B 277     5195   4578   4964   -431    828   -304       C  
ATOM   5136  CE  LYS B 277      62.582 -30.951  23.160  1.00 40.02           C  
ANISOU 5136  CE  LYS B 277     5360   4726   5120   -415    893   -335       C  
ATOM   5137  NZ  LYS B 277      63.075 -31.085  21.748  1.00 41.15           N  
ANISOU 5137  NZ  LYS B 277     5574   4840   5220   -482   1034   -365       N  
ATOM   5138  N   ASN B 278      58.278 -31.429  23.743  1.00 39.59           N  
ANISOU 5138  N   ASN B 278     5419   4738   4887   -404    651   -235       N  
ATOM   5139  CA  ASN B 278      57.200 -32.404  23.689  1.00 41.89           C  
ANISOU 5139  CA  ASN B 278     5725   5041   5150   -424    616   -227       C  
ATOM   5140  C   ASN B 278      57.787 -33.799  23.618  1.00 35.80           C  
ANISOU 5140  C   ASN B 278     4988   4240   4374   -432    679   -277       C  
ATOM   5141  O   ASN B 278      58.623 -34.080  22.750  1.00 37.39           O  
ANISOU 5141  O   ASN B 278     5242   4414   4551   -461    754   -317       O  
ATOM   5142  CB  ASN B 278      56.288 -32.137  22.502  1.00 36.09           C  
ANISOU 5142  CB  ASN B 278     5041   4322   4349   -496    547   -183       C  
ATOM   5143  CG  ASN B 278      55.707 -30.745  22.556  1.00 59.89           C  
ANISOU 5143  CG  ASN B 278     8008   7338   7408   -467    481   -114       C  
ATOM   5144  OD1 ASN B 278      54.686 -30.519  23.189  1.00 49.75           O  
ANISOU 5144  OD1 ASN B 278     6642   6060   6202   -428    438    -81       O  
ATOM   5145  ND2 ASN B 278      56.396 -29.790  21.937  1.00 67.50           N  
ANISOU 5145  ND2 ASN B 278     9022   8281   8343   -482    496    -93       N  
ATOM   5146  N   TYR B 279      57.329 -34.667  24.516  1.00 35.10           N  
ANISOU 5146  N   TYR B 279     4879   4143   4316   -406    669   -275       N  
ATOM   5147  CA  TYR B 279      57.847 -36.022  24.629  1.00 33.22           C  
ANISOU 5147  CA  TYR B 279     4673   3849   4102   -395    726   -308       C  
ATOM   5148  C   TYR B 279      56.714 -37.027  24.551  1.00 36.93           C  
ANISOU 5148  C   TYR B 279     5186   4302   4543   -453    710   -308       C  
ATOM   5149  O   TYR B 279      55.615 -36.794  25.069  1.00 36.29           O  
ANISOU 5149  O   TYR B 279     5065   4258   4466   -470    659   -270       O  
ATOM   5150  CB  TYR B 279      58.589 -36.230  25.949  1.00 32.95           C  
ANISOU 5150  CB  TYR B 279     4586   3795   4137   -314    717   -286       C  
ATOM   5151  CG  TYR B 279      59.739 -35.277  26.145  1.00 33.40           C  
ANISOU 5151  CG  TYR B 279     4580   3869   4241   -274    710   -287       C  
ATOM   5152  CD1 TYR B 279      60.916 -35.413  25.406  1.00 38.21           C  
ANISOU 5152  CD1 TYR B 279     5160   4442   4916   -263    782   -321       C  
ATOM   5153  CD2 TYR B 279      59.655 -34.240  27.070  1.00 39.65           C  
ANISOU 5153  CD2 TYR B 279     5342   4702   5022   -260    648   -265       C  
ATOM   5154  CE1 TYR B 279      61.983 -34.534  25.585  1.00 37.26           C  
ANISOU 5154  CE1 TYR B 279     4955   4336   4865   -244    776   -321       C  
ATOM   5155  CE2 TYR B 279      60.715 -33.354  27.252  1.00 40.78           C  
ANISOU 5155  CE2 TYR B 279     5429   4854   5212   -249    629   -272       C  
ATOM   5156  CZ  TYR B 279      61.866 -33.510  26.510  1.00 40.02           C  
ANISOU 5156  CZ  TYR B 279     5280   4732   5196   -243    684   -295       C  
ATOM   5157  OH  TYR B 279      62.900 -32.637  26.695  1.00 44.40           O  
ANISOU 5157  OH  TYR B 279     5756   5295   5820   -248    666   -300       O  
ATOM   5158  N   PHE B 280      57.006 -38.147  23.903  1.00 35.65           N  
ANISOU 5158  N   PHE B 280     5103   4072   4372   -490    774   -357       N  
ATOM   5159  CA  PHE B 280      56.213 -39.367  24.007  1.00 36.05           C  
ANISOU 5159  CA  PHE B 280     5205   4072   4420   -545    779   -368       C  
ATOM   5160  C   PHE B 280      56.771 -40.117  25.214  1.00 37.64           C  
ANISOU 5160  C   PHE B 280     5387   4207   4706   -456    812   -337       C  
ATOM   5161  O   PHE B 280      57.868 -40.684  25.146  1.00 37.83           O  
ANISOU 5161  O   PHE B 280     5425   4150   4797   -394    879   -359       O  
ATOM   5162  CB  PHE B 280      56.330 -40.161  22.704  1.00 35.23           C  
ANISOU 5162  CB  PHE B 280     5228   3903   4254   -637    841   -450       C  
ATOM   5163  CG  PHE B 280      55.374 -41.330  22.572  1.00 35.41           C  
ANISOU 5163  CG  PHE B 280     5324   3871   4260   -739    832   -476       C  
ATOM   5164  CD1 PHE B 280      54.922 -42.035  23.679  1.00 37.50           C  
ANISOU 5164  CD1 PHE B 280     5553   4096   4601   -713    831   -431       C  
ATOM   5165  CD2 PHE B 280      54.950 -41.733  21.318  1.00 41.24           C  
ANISOU 5165  CD2 PHE B 280     6190   4588   4890   -883    826   -546       C  
ATOM   5166  CE1 PHE B 280      54.053 -43.128  23.540  1.00 40.17           C  
ANISOU 5166  CE1 PHE B 280     5958   4369   4935   -825    834   -456       C  
ATOM   5167  CE2 PHE B 280      54.086 -42.809  21.162  1.00 45.51           C  
ANISOU 5167  CE2 PHE B 280     6803   5071   5417  -1002    809   -580       C  
ATOM   5168  CZ  PHE B 280      53.635 -43.510  22.277  1.00 44.55           C  
ANISOU 5168  CZ  PHE B 280     6623   4905   5401   -972    818   -536       C  
ATOM   5169  N   ILE B 281      56.041 -40.098  26.327  1.00 36.29           N  
ANISOU 5169  N   ILE B 281     5184   4063   4541   -449    770   -278       N  
ATOM   5170  CA  ILE B 281      56.558 -40.583  27.602  1.00 36.28           C  
ANISOU 5170  CA  ILE B 281     5189   4015   4580   -375    770   -221       C  
ATOM   5171  C   ILE B 281      55.922 -41.923  27.951  1.00 41.36           C  
ANISOU 5171  C   ILE B 281     5908   4570   5238   -421    807   -200       C  
ATOM   5172  O   ILE B 281      54.710 -42.107  27.791  1.00 36.17           O  
ANISOU 5172  O   ILE B 281     5256   3933   4555   -518    814   -209       O  
ATOM   5173  CB  ILE B 281      56.330 -39.557  28.728  1.00 37.83           C  
ANISOU 5173  CB  ILE B 281     5343   4293   4739   -347    722   -174       C  
ATOM   5174  CG1 ILE B 281      56.778 -40.134  30.063  1.00 39.89           C  
ANISOU 5174  CG1 ILE B 281     5656   4507   4994   -302    699   -103       C  
ATOM   5175  CG2 ILE B 281      54.869 -39.141  28.795  1.00 42.89           C  
ANISOU 5175  CG2 ILE B 281     5956   4990   5352   -418    734   -173       C  
ATOM   5176  CD1 ILE B 281      56.789 -39.129  31.191  1.00 45.93           C  
ANISOU 5176  CD1 ILE B 281     6423   5340   5688   -289    657    -75       C  
ATOM   5177  N   THR B 282      56.750 -42.854  28.433  1.00 35.53           N  
ANISOU 5177  N   THR B 282     5216   3723   4561   -354    824   -163       N  
ATOM   5178  CA  THR B 282      56.308 -44.157  28.926  1.00 35.36           C  
ANISOU 5178  CA  THR B 282     5286   3586   4563   -386    860   -121       C  
ATOM   5179  C   THR B 282      56.915 -44.386  30.305  1.00 41.52           C  
ANISOU 5179  C   THR B 282     6096   4328   5352   -303    804     -6       C  
ATOM   5180  O   THR B 282      58.144 -44.443  30.444  1.00 40.38           O  
ANISOU 5180  O   THR B 282     5915   4138   5287   -194    758     28       O  
ATOM   5181  CB  THR B 282      56.721 -45.293  27.980  1.00 35.53           C  
ANISOU 5181  CB  THR B 282     5374   3459   4666   -390    942   -185       C  
ATOM   5182  OG1 THR B 282      56.248 -45.018  26.657  1.00 38.63           O  
ANISOU 5182  OG1 THR B 282     5776   3896   5008   -488    975   -294       O  
ATOM   5183  CG2 THR B 282      56.126 -46.613  28.465  1.00 37.32           C  
ANISOU 5183  CG2 THR B 282     5710   3551   4921   -443    984   -142       C  
ATOM   5184  N   ASP B 283      56.061 -44.529  31.316  1.00 39.09           N  
ANISOU 5184  N   ASP B 283     5852   4035   4965   -362    805     60       N  
ATOM   5185  CA  ASP B 283      56.513 -44.772  32.684  1.00 38.37           C  
ANISOU 5185  CA  ASP B 283     5842   3910   4828   -316    740    183       C  
ATOM   5186  C   ASP B 283      56.823 -46.251  32.881  1.00 46.10           C  
ANISOU 5186  C   ASP B 283     6920   4707   5888   -288    752    262       C  
ATOM   5187  O   ASP B 283      55.950 -47.110  32.694  1.00 44.33           O  
ANISOU 5187  O   ASP B 283     6769   4401   5673   -377    844    251       O  
ATOM   5188  CB  ASP B 283      55.459 -44.317  33.688  1.00 40.96           C  
ANISOU 5188  CB  ASP B 283     6230   4314   5017   -406    776    214       C  
ATOM   5189  CG  ASP B 283      55.930 -44.464  35.115  1.00 49.44           C  
ANISOU 5189  CG  ASP B 283     7435   5364   5984   -386    701    339       C  
ATOM   5190  OD1 ASP B 283      56.893 -43.764  35.493  1.00 51.12           O  
ANISOU 5190  OD1 ASP B 283     7624   5631   6169   -319    579    363       O  
ATOM   5191  OD2 ASP B 283      55.350 -45.276  35.858  1.00 47.82           O  
ANISOU 5191  OD2 ASP B 283     7368   5086   5718   -452    755    419       O  
ATOM   5192  N   ALA B 284      58.055 -46.551  33.294  1.00 44.77           N  
ANISOU 5192  N   ALA B 284     6747   4465   5798   -168    652    351       N  
ATOM   5193  CA  ALA B 284      58.488 -47.944  33.326  1.00 44.73           C  
ANISOU 5193  CA  ALA B 284     6815   4256   5925   -108    664    429       C  
ATOM   5194  C   ALA B 284      57.840 -48.724  34.468  1.00 49.41           C  
ANISOU 5194  C   ALA B 284     7587   4768   6420   -175    657    565       C  
ATOM   5195  O   ALA B 284      57.631 -49.934  34.346  1.00 48.46           O  
ANISOU 5195  O   ALA B 284     7561   4469   6384   -186    726    602       O  
ATOM   5196  CB  ALA B 284      60.013 -48.020  33.419  1.00 47.28           C  
ANISOU 5196  CB  ALA B 284     7040   4514   6410     56    549    502       C  
ATOM   5197  N   GLN B 285      57.501 -48.059  35.574  1.00 45.57           N  
ANISOU 5197  N   GLN B 285     7171   4397   5747   -232    594    635       N  
ATOM   5198  CA  GLN B 285      56.966 -48.783  36.725  1.00 47.93           C  
ANISOU 5198  CA  GLN B 285     7672   4616   5924   -307    600    777       C  
ATOM   5199  C   GLN B 285      55.501 -49.161  36.531  1.00 45.61           C  
ANISOU 5199  C   GLN B 285     7437   4309   5584   -463    791    710       C  
ATOM   5200  O   GLN B 285      55.094 -50.273  36.890  1.00 51.76           O  
ANISOU 5200  O   GLN B 285     8358   4936   6372   -521    853    798       O  
ATOM   5201  CB  GLN B 285      57.132 -47.951  38.001  1.00 49.57           C  
ANISOU 5201  CB  GLN B 285     7974   4942   5917   -337    486    863       C  
ATOM   5202  CG  GLN B 285      56.619 -48.646  39.261  1.00 58.23           C  
ANISOU 5202  CG  GLN B 285     9324   5960   6840   -434    500   1019       C  
ATOM   5203  CD  GLN B 285      57.338 -49.955  39.549  1.00 64.60           C  
ANISOU 5203  CD  GLN B 285    10234   6558   7754   -351    389   1202       C  
ATOM   5204  OE1 GLN B 285      58.565 -50.011  39.555  1.00 66.97           O  
ANISOU 5204  OE1 GLN B 285    10459   6818   8171   -210    195   1285       O  
ATOM   5205  NE2 GLN B 285      56.570 -51.018  39.782  1.00 67.51           N  
ANISOU 5205  NE2 GLN B 285    10762   6781   8110   -438    515   1271       N  
ATOM   5206  N   THR B 286      54.698 -48.266  35.956  1.00 42.94           N  
ANISOU 5206  N   THR B 286     6979   4118   5218   -535    879    567       N  
ATOM   5207  CA  THR B 286      53.257 -48.491  35.879  1.00 43.66           C  
ANISOU 5207  CA  THR B 286     7082   4219   5287   -691   1041    516       C  
ATOM   5208  C   THR B 286      52.767 -48.881  34.493  1.00 43.51           C  
ANISOU 5208  C   THR B 286     6955   4166   5412   -740   1103    389       C  
ATOM   5209  O   THR B 286      51.755 -49.587  34.382  1.00 46.00           O  
ANISOU 5209  O   THR B 286     7302   4417   5759   -875   1210    376       O  
ATOM   5210  CB  THR B 286      52.507 -47.232  36.321  1.00 47.27           C  
ANISOU 5210  CB  THR B 286     7477   4853   5631   -751   1101    459       C  
ATOM   5211  OG1 THR B 286      52.770 -46.181  35.383  1.00 44.54           O  
ANISOU 5211  OG1 THR B 286     6952   4626   5344   -687   1046    343       O  
ATOM   5212  CG2 THR B 286      52.963 -46.796  37.706  1.00 47.25           C  
ANISOU 5212  CG2 THR B 286     7626   4885   5442   -735   1048    562       C  
ATOM   5213  N   GLY B 287      53.454 -48.449  33.434  1.00 43.87           N  
ANISOU 5213  N   GLY B 287     6886   4250   5534   -655   1040    296       N  
ATOM   5214  CA  GLY B 287      52.921 -48.579  32.094  1.00 37.53           C  
ANISOU 5214  CA  GLY B 287     6002   3450   4809   -730   1084    164       C  
ATOM   5215  C   GLY B 287      52.019 -47.442  31.666  1.00 43.35           C  
ANISOU 5215  C   GLY B 287     6594   4365   5510   -801   1087     83       C  
ATOM   5216  O   GLY B 287      51.486 -47.478  30.547  1.00 48.27           O  
ANISOU 5216  O   GLY B 287     7154   5008   6179   -882   1088    -13       O  
ATOM   5217  N   SER B 288      51.816 -46.442  32.521  1.00 39.71           N  
ANISOU 5217  N   SER B 288     6091   4025   4972   -777   1083    120       N  
ATOM   5218  CA  SER B 288      51.156 -45.216  32.095  1.00 44.26           C  
ANISOU 5218  CA  SER B 288     6514   4753   5550   -799   1078     51       C  
ATOM   5219  C   SER B 288      52.003 -44.520  31.032  1.00 44.76           C  
ANISOU 5219  C   SER B 288     6506   4870   5631   -715    984    -17       C  
ATOM   5220  O   SER B 288      53.233 -44.461  31.146  1.00 44.83           O  
ANISOU 5220  O   SER B 288     6555   4849   5627   -606    932      3       O  
ATOM   5221  CB  SER B 288      50.944 -44.307  33.305  1.00 44.43           C  
ANISOU 5221  CB  SER B 288     6540   4857   5486   -776   1122     93       C  
ATOM   5222  OG  SER B 288      49.973 -43.315  33.038  1.00 45.79           O  
ANISOU 5222  OG  SER B 288     6558   5136   5705   -813   1164     38       O  
ATOM   5223  N   SER B 289      51.352 -44.015  29.977  1.00 39.84           N  
ANISOU 5223  N   SER B 289     5774   4319   5044   -774    958    -88       N  
ATOM   5224  CA  SER B 289      52.078 -43.384  28.873  1.00 41.52           C  
ANISOU 5224  CA  SER B 289     5950   4575   5252   -721    886   -148       C  
ATOM   5225  C   SER B 289      51.228 -42.280  28.253  1.00 38.40           C  
ANISOU 5225  C   SER B 289     5423   4299   4868   -763    835   -174       C  
ATOM   5226  O   SER B 289      50.025 -42.182  28.508  1.00 37.50           O  
ANISOU 5226  O   SER B 289     5221   4221   4805   -838    855   -155       O  
ATOM   5227  CB  SER B 289      52.480 -44.407  27.798  1.00 38.13           C  
ANISOU 5227  CB  SER B 289     5607   4041   4840   -765    893   -210       C  
ATOM   5228  OG  SER B 289      51.332 -44.945  27.145  1.00 40.48           O  
ANISOU 5228  OG  SER B 289     5900   4329   5153   -920    887   -250       O  
ATOM   5229  N   LYS B 290      51.868 -41.449  27.422  1.00 37.34           N  
ANISOU 5229  N   LYS B 290     5266   4215   4707   -714    774   -207       N  
ATOM   5230  CA  LYS B 290      51.179 -40.344  26.753  1.00 40.58           C  
ANISOU 5230  CA  LYS B 290     5566   4721   5131   -739    701   -208       C  
ATOM   5231  C   LYS B 290      51.983 -39.932  25.527  1.00 40.67           C  
ANISOU 5231  C   LYS B 290     5627   4746   5082   -730    645   -250       C  
ATOM   5232  O   LYS B 290      53.196 -39.729  25.632  1.00 37.64           O  
ANISOU 5232  O   LYS B 290     5290   4340   4673   -644    680   -264       O  
ATOM   5233  CB  LYS B 290      51.000 -39.154  27.705  1.00 37.44           C  
ANISOU 5233  CB  LYS B 290     5079   4383   4762   -656    726   -171       C  
ATOM   5234  CG  LYS B 290      50.376 -37.929  27.044  1.00 41.31           C  
ANISOU 5234  CG  LYS B 290     5450   4945   5302   -652    653   -157       C  
ATOM   5235  CD  LYS B 290      49.647 -37.029  28.058  1.00 41.85           C  
ANISOU 5235  CD  LYS B 290     5409   5039   5454   -600    723   -130       C  
ATOM   5236  CE  LYS B 290      50.609 -36.392  29.055  1.00 45.48           C  
ANISOU 5236  CE  LYS B 290     5945   5489   5846   -507    787   -144       C  
ATOM   5237  NZ  LYS B 290      49.856 -35.734  30.174  1.00 46.90           N  
ANISOU 5237  NZ  LYS B 290     6070   5669   6080   -481    903   -143       N  
ATOM   5238  N  ACYS B 291      51.306 -39.793  24.373  0.76 36.34           N  
ANISOU 5238  N  ACYS B 291     5067   4232   4507   -831    555   -262       N  
ATOM   5239  N  BCYS B 291      51.302 -39.791  24.384  0.24 37.66           N  
ANISOU 5239  N  BCYS B 291     5233   4399   4675   -830    555   -261       N  
ATOM   5240  CA ACYS B 291      52.017 -39.548  23.114  0.76 36.48           C  
ANISOU 5240  CA ACYS B 291     5184   4251   4426   -859    522   -304       C  
ATOM   5241  CA BCYS B 291      52.004 -39.560  23.124  0.24 38.37           C  
ANISOU 5241  CA BCYS B 291     5423   4490   4666   -860    522   -304       C  
ATOM   5242  C  ACYS B 291      52.583 -38.139  23.043  0.76 41.29           C  
ANISOU 5242  C  ACYS B 291     5748   4916   5024   -769    500   -271       C  
ATOM   5243  C  BCYS B 291      52.577 -38.151  23.045  0.24 39.80           C  
ANISOU 5243  C  BCYS B 291     5558   4727   4835   -769    500   -271       C  
ATOM   5244  O  ACYS B 291      53.679 -37.928  22.509  0.76 35.80           O  
ANISOU 5244  O  ACYS B 291     5133   4201   4269   -742    548   -307       O  
ATOM   5245  O  BCYS B 291      53.690 -37.956  22.544  0.24 38.67           O  
ANISOU 5245  O  BCYS B 291     5496   4563   4635   -740    551   -308       O  
ATOM   5246  CB ACYS B 291      51.097 -39.769  21.916  0.76 39.00           C  
ANISOU 5246  CB ACYS B 291     5540   4596   4684  -1019    400   -314       C  
ATOM   5247  CB BCYS B 291      51.067 -39.821  21.947  0.24 41.76           C  
ANISOU 5247  CB BCYS B 291     5887   4942   5036  -1021    402   -314       C  
ATOM   5248  SG ACYS B 291      50.405 -41.422  21.760  0.76 42.84           S  
ANISOU 5248  SG ACYS B 291     6106   5002   5171  -1175    412   -373       S  
ATOM   5249  SG BCYS B 291      49.500 -38.927  22.029  0.24 52.14           S  
ANISOU 5249  SG BCYS B 291     6997   6355   6460  -1055    240   -212       S  
ATOM   5250  N   VAL B 292      51.834 -37.153  23.506  1.00 36.49           N  
ANISOU 5250  N   VAL B 292     5011   4366   4489   -729    443   -206       N  
ATOM   5251  CA  VAL B 292      52.294 -35.765  23.482  1.00 38.43           C  
ANISOU 5251  CA  VAL B 292     5220   4642   4739   -648    427   -173       C  
ATOM   5252  C   VAL B 292      52.207 -35.247  24.910  1.00 40.93           C  
ANISOU 5252  C   VAL B 292     5448   4960   5145   -549    494   -156       C  
ATOM   5253  O   VAL B 292      51.116 -34.923  25.402  1.00 37.85           O  
ANISOU 5253  O   VAL B 292     4946   4587   4848   -542    487   -120       O  
ATOM   5254  CB  VAL B 292      51.494 -34.886  22.519  1.00 40.88           C  
ANISOU 5254  CB  VAL B 292     5487   4995   5051   -694    289   -107       C  
ATOM   5255  CG1 VAL B 292      52.100 -33.482  22.502  1.00 37.29           C  
ANISOU 5255  CG1 VAL B 292     5023   4542   4604   -610    294    -73       C  
ATOM   5256  CG2 VAL B 292      51.511 -35.485  21.110  1.00 40.66           C  
ANISOU 5256  CG2 VAL B 292     5596   4969   4885   -829    210   -127       C  
ATOM   5257  N   CYS B 293      53.349 -35.189  25.585  1.00 33.04           N  
ANISOU 5257  N   CYS B 293     4496   3937   4119   -482    564   -186       N  
ATOM   5258  CA  CYS B 293      53.448 -34.607  26.920  1.00 33.93           C  
ANISOU 5258  CA  CYS B 293     4576   4050   4266   -410    617   -181       C  
ATOM   5259  C   CYS B 293      54.328 -33.366  26.814  1.00 40.54           C  
ANISOU 5259  C   CYS B 293     5416   4891   5095   -360    606   -188       C  
ATOM   5260  O   CYS B 293      55.550 -33.475  26.662  1.00 36.54           O  
ANISOU 5260  O   CYS B 293     4955   4373   4557   -347    613   -212       O  
ATOM   5261  CB  CYS B 293      54.019 -35.604  27.917  1.00 36.23           C  
ANISOU 5261  CB  CYS B 293     4930   4308   4527   -395    668   -193       C  
ATOM   5262  SG  CYS B 293      53.927 -35.029  29.621  1.00 44.06           S  
ANISOU 5262  SG  CYS B 293     5936   5302   5502   -353    726   -187       S  
ATOM   5263  N   SER B 294      53.701 -32.196  26.889  1.00 41.15           N  
ANISOU 5263  N   SER B 294     5435   4972   5228   -333    598   -165       N  
ATOM   5264  CA  SER B 294      54.415 -30.927  26.789  1.00 38.24           C  
ANISOU 5264  CA  SER B 294     5078   4586   4863   -298    594   -169       C  
ATOM   5265  C   SER B 294      55.047 -30.568  28.127  1.00 35.93           C  
ANISOU 5265  C   SER B 294     4819   4278   4555   -265    648   -214       C  
ATOM   5266  O   SER B 294      54.379 -30.582  29.163  1.00 38.82           O  
ANISOU 5266  O   SER B 294     5184   4636   4932   -252    707   -228       O  
ATOM   5267  CB  SER B 294      53.459 -29.826  26.348  1.00 41.60           C  
ANISOU 5267  CB  SER B 294     5436   4993   5376   -275    562   -119       C  
ATOM   5268  OG  SER B 294      53.012 -30.048  25.017  1.00 45.34           O  
ANISOU 5268  OG  SER B 294     5903   5488   5836   -325    465    -62       O  
ATOM   5269  N   VAL B 295      56.336 -30.240  28.107  1.00 36.77           N  
ANISOU 5269  N   VAL B 295     4960   4380   4632   -267    631   -237       N  
ATOM   5270  CA  VAL B 295      57.114 -30.042  29.323  1.00 34.86           C  
ANISOU 5270  CA  VAL B 295     4759   4130   4355   -263    634   -274       C  
ATOM   5271  C   VAL B 295      57.850 -28.721  29.215  1.00 34.82           C  
ANISOU 5271  C   VAL B 295     4758   4099   4374   -272    624   -298       C  
ATOM   5272  O   VAL B 295      58.502 -28.446  28.200  1.00 35.20           O  
ANISOU 5272  O   VAL B 295     4782   4144   4450   -287    610   -285       O  
ATOM   5273  CB  VAL B 295      58.118 -31.190  29.561  1.00 37.70           C  
ANISOU 5273  CB  VAL B 295     5130   4505   4688   -267    593   -268       C  
ATOM   5274  CG1 VAL B 295      58.974 -30.892  30.792  1.00 40.15           C  
ANISOU 5274  CG1 VAL B 295     5482   4816   4959   -277    542   -286       C  
ATOM   5275  CG2 VAL B 295      57.386 -32.519  29.747  1.00 35.80           C  
ANISOU 5275  CG2 VAL B 295     4910   4268   4427   -267    612   -243       C  
ATOM   5276  N   ILE B 296      57.767 -27.913  30.261  1.00 34.71           N  
ANISOU 5276  N   ILE B 296     4792   4054   4340   -277    648   -341       N  
ATOM   5277  CA  ILE B 296      58.486 -26.643  30.290  1.00 36.86           C  
ANISOU 5277  CA  ILE B 296     5085   4283   4636   -304    640   -377       C  
ATOM   5278  C   ILE B 296      59.321 -26.586  31.565  1.00 36.59           C  
ANISOU 5278  C   ILE B 296     5120   4255   4526   -355    592   -430       C  
ATOM   5279  O   ILE B 296      58.897 -27.093  32.609  1.00 42.19           O  
ANISOU 5279  O   ILE B 296     5903   4979   5149   -362    604   -446       O  
ATOM   5280  CB  ILE B 296      57.506 -25.449  30.178  1.00 36.78           C  
ANISOU 5280  CB  ILE B 296     5087   4196   4693   -272    716   -386       C  
ATOM   5281  CG1 ILE B 296      58.274 -24.142  29.933  1.00 36.66           C  
ANISOU 5281  CG1 ILE B 296     5099   4112   4718   -307    713   -410       C  
ATOM   5282  CG2 ILE B 296      56.594 -25.370  31.409  1.00 37.91           C  
ANISOU 5282  CG2 ILE B 296     5287   4309   4809   -256    808   -438       C  
ATOM   5283  CD1 ILE B 296      57.371 -22.976  29.535  1.00 38.16           C  
ANISOU 5283  CD1 ILE B 296     5290   4198   5011   -258    779   -390       C  
ATOM   5284  N   ASP B 297      60.517 -25.992  31.479  1.00 37.12           N  
ANISOU 5284  N   ASP B 297     5170   4315   4620   -407    530   -451       N  
ATOM   5285  CA  ASP B 297      61.380 -25.845  32.654  1.00 40.14           C  
ANISOU 5285  CA  ASP B 297     5611   4707   4932   -480    437   -494       C  
ATOM   5286  C   ASP B 297      61.348 -24.395  33.137  1.00 40.36           C  
ANISOU 5286  C   ASP B 297     5733   4656   4944   -542    477   -577       C  
ATOM   5287  O   ASP B 297      62.262 -23.604  32.901  1.00 38.17           O  
ANISOU 5287  O   ASP B 297     5427   4351   4724   -607    433   -602       O  
ATOM   5288  CB  ASP B 297      62.818 -26.297  32.356  1.00 38.59           C  
ANISOU 5288  CB  ASP B 297     5301   4554   4808   -508    321   -460       C  
ATOM   5289  CG  ASP B 297      63.716 -26.225  33.601  1.00 50.20           C  
ANISOU 5289  CG  ASP B 297     6814   6045   6214   -593    167   -482       C  
ATOM   5290  OD1 ASP B 297      63.177 -26.245  34.730  1.00 49.74           O  
ANISOU 5290  OD1 ASP B 297     6910   5984   6004   -626    150   -512       O  
ATOM   5291  OD2 ASP B 297      64.956 -26.126  33.448  1.00 55.53           O  
ANISOU 5291  OD2 ASP B 297     7374   6738   6988   -638     64   -469       O  
ATOM   5292  N   LEU B 298      60.277 -24.052  33.837  1.00 42.59           N  
ANISOU 5292  N   LEU B 298     6131   4890   5161   -527    581   -628       N  
ATOM   5293  CA  LEU B 298      60.193 -22.787  34.548  1.00 43.86           C  
ANISOU 5293  CA  LEU B 298     6423   4955   5286   -591    644   -731       C  
ATOM   5294  C   LEU B 298      60.674 -22.977  35.976  1.00 42.81           C  
ANISOU 5294  C   LEU B 298     6448   4849   4970   -700    562   -795       C  
ATOM   5295  O   LEU B 298      60.528 -24.055  36.556  1.00 44.26           O  
ANISOU 5295  O   LEU B 298     6668   5104   5046   -696    516   -754       O  
ATOM   5296  CB  LEU B 298      58.749 -22.279  34.562  1.00 46.16           C  
ANISOU 5296  CB  LEU B 298     6753   5157   5630   -511    834   -761       C  
ATOM   5297  CG  LEU B 298      58.177 -21.768  33.247  1.00 48.65           C  
ANISOU 5297  CG  LEU B 298     6943   5416   6124   -416    890   -692       C  
ATOM   5298  CD1 LEU B 298      56.656 -21.599  33.373  1.00 40.67           C  
ANISOU 5298  CD1 LEU B 298     5919   4338   5197   -319   1051   -696       C  
ATOM   5299  CD2 LEU B 298      58.871 -20.441  32.871  1.00 40.27           C  
ANISOU 5299  CD2 LEU B 298     5912   4251   5137   -466    885   -725       C  
ATOM   5300  N   LEU B 299      61.235 -21.917  36.554  1.00 37.56           N  
ANISOU 5300  N   LEU B 299     5898   4116   4257   -812    538   -893       N  
ATOM   5301  CA  LEU B 299      61.420 -21.914  37.997  1.00 44.08           C  
ANISOU 5301  CA  LEU B 299     6939   4947   4864   -937    484   -974       C  
ATOM   5302  C   LEU B 299      60.067 -22.180  38.643  1.00 50.81           C  
ANISOU 5302  C   LEU B 299     7928   5764   5616   -888    687  -1016       C  
ATOM   5303  O   LEU B 299      59.056 -21.604  38.236  1.00 45.40           O  
ANISOU 5303  O   LEU B 299     7216   4985   5050   -797    895  -1051       O  
ATOM   5304  CB  LEU B 299      61.990 -20.570  38.466  1.00 39.86           C  
ANISOU 5304  CB  LEU B 299     6539   4312   4293  -1078    472  -1103       C  
ATOM   5305  CG  LEU B 299      62.462 -20.506  39.923  1.00 49.63           C  
ANISOU 5305  CG  LEU B 299     8023   5562   5270  -1258    355  -1192       C  
ATOM   5306  CD1 LEU B 299      63.747 -21.303  40.093  1.00 52.37           C  
ANISOU 5306  CD1 LEU B 299     8270   6043   5585  -1334     41  -1091       C  
ATOM   5307  CD2 LEU B 299      62.645 -19.065  40.380  1.00 54.52           C  
ANISOU 5307  CD2 LEU B 299     8825   6041   5848  -1395    422  -1358       C  
ATOM   5308  N   LEU B 300      60.030 -23.089  39.617  1.00 46.08           N  
ANISOU 5308  N   LEU B 300     7460   5234   4816   -943    629   -996       N  
ATOM   5309  CA  LEU B 300      58.737 -23.434  40.202  1.00 48.26           C  
ANISOU 5309  CA  LEU B 300     7852   5478   5005   -905    851  -1028       C  
ATOM   5310  C   LEU B 300      58.043 -22.206  40.785  1.00 51.76           C  
ANISOU 5310  C   LEU B 300     8473   5777   5415   -945   1093  -1194       C  
ATOM   5311  O   LEU B 300      56.814 -22.095  40.705  1.00 57.40           O  
ANISOU 5311  O   LEU B 300     9161   6423   6227   -851   1347  -1224       O  
ATOM   5312  CB  LEU B 300      58.898 -24.516  41.269  1.00 45.45           C  
ANISOU 5312  CB  LEU B 300     7665   5203   4401   -991    752   -980       C  
ATOM   5313  CG  LEU B 300      57.587 -25.144  41.745  1.00 53.94           C  
ANISOU 5313  CG  LEU B 300     8826   6262   5406   -952    989   -981       C  
ATOM   5314  CD1 LEU B 300      56.794 -25.673  40.551  1.00 51.17           C  
ANISOU 5314  CD1 LEU B 300     8201   5926   5313   -786   1081   -892       C  
ATOM   5315  CD2 LEU B 300      57.862 -26.258  42.739  1.00 55.55           C  
ANISOU 5315  CD2 LEU B 300     9213   6539   5353  -1047    866   -904       C  
ATOM   5316  N   ASP B 301      58.809 -21.265  41.348  1.00 54.57           N  
ANISOU 5316  N   ASP B 301     8998   6074   5662  -1085   1025  -1306       N  
ATOM   5317  CA  ASP B 301      58.211 -20.032  41.856  1.00 56.62           C  
ANISOU 5317  CA  ASP B 301     9441   6164   5907  -1124   1274  -1483       C  
ATOM   5318  C   ASP B 301      57.512 -19.261  40.744  1.00 55.29           C  
ANISOU 5318  C   ASP B 301     9067   5880   6059   -957   1447  -1474       C  
ATOM   5319  O   ASP B 301      56.443 -18.678  40.961  1.00 57.54           O  
ANISOU 5319  O   ASP B 301     9406   6027   6430   -890   1732  -1565       O  
ATOM   5320  CB  ASP B 301      59.276 -19.151  42.508  1.00 57.85           C  
ANISOU 5320  CB  ASP B 301     9804   6272   5906  -1322   1135  -1603       C  
ATOM   5321  CG  ASP B 301      60.077 -19.884  43.557  1.00 60.84           C  
ANISOU 5321  CG  ASP B 301    10375   6772   5971  -1500    892  -1582       C  
ATOM   5322  OD1 ASP B 301      60.731 -20.890  43.209  1.00 64.68           O  
ANISOU 5322  OD1 ASP B 301    10691   7404   6480  -1470    640  -1419       O  
ATOM   5323  OD2 ASP B 301      60.063 -19.447  44.724  1.00 70.16           O  
ANISOU 5323  OD2 ASP B 301    11886   7891   6881  -1672    949  -1727       O  
ATOM   5324  N   ASP B 302      58.103 -19.244  39.546  1.00 50.99           N  
ANISOU 5324  N   ASP B 302     8290   5380   5702   -890   1281  -1359       N  
ATOM   5325  CA  ASP B 302      57.486 -18.541  38.424  1.00 53.62           C  
ANISOU 5325  CA  ASP B 302     8447   5609   6318   -742   1400  -1317       C  
ATOM   5326  C   ASP B 302      56.190 -19.212  37.994  1.00 51.80           C  
ANISOU 5326  C   ASP B 302     8060   5402   6221   -580   1540  -1232       C  
ATOM   5327  O   ASP B 302      55.195 -18.532  37.723  1.00 50.39           O  
ANISOU 5327  O   ASP B 302     7823   5089   6235   -469   1737  -1253       O  
ATOM   5328  CB  ASP B 302      58.456 -18.469  37.241  1.00 47.69           C  
ANISOU 5328  CB  ASP B 302     7517   4913   5692   -734   1195  -1206       C  
ATOM   5329  CG  ASP B 302      59.599 -17.490  37.473  1.00 50.13           C  
ANISOU 5329  CG  ASP B 302     7933   5153   5961   -886   1099  -1293       C  
ATOM   5330  OD1 ASP B 302      59.454 -16.592  38.330  1.00 54.23           O  
ANISOU 5330  OD1 ASP B 302     8663   5536   6405   -971   1221  -1447       O  
ATOM   5331  OD2 ASP B 302      60.639 -17.610  36.789  1.00 52.77           O  
ANISOU 5331  OD2 ASP B 302     8142   5561   6348   -929    917  -1217       O  
ATOM   5332  N   PHE B 303      56.187 -20.545  37.897  1.00 48.34           N  
ANISOU 5332  N   PHE B 303     7537   5121   5708   -566   1431  -1129       N  
ATOM   5333  CA  PHE B 303      54.962 -21.241  37.520  1.00 47.76           C  
ANISOU 5333  CA  PHE B 303     7314   5073   5759   -441   1550  -1053       C  
ATOM   5334  C   PHE B 303      53.863 -21.012  38.553  1.00 48.52           C  
ANISOU 5334  C   PHE B 303     7532   5073   5829   -437   1834  -1166       C  
ATOM   5335  O   PHE B 303      52.704 -20.770  38.194  1.00 48.88           O  
ANISOU 5335  O   PHE B 303     7435   5042   6097   -315   2013  -1150       O  
ATOM   5336  CB  PHE B 303      55.231 -22.737  37.336  1.00 42.78           C  
ANISOU 5336  CB  PHE B 303     6610   4609   5037   -451   1392   -939       C  
ATOM   5337  CG  PHE B 303      54.017 -23.512  36.900  1.00 46.15           C  
ANISOU 5337  CG  PHE B 303     6878   5065   5591   -352   1491   -861       C  
ATOM   5338  CD1 PHE B 303      53.536 -23.401  35.600  1.00 51.04           C  
ANISOU 5338  CD1 PHE B 303     7280   5679   6434   -244   1454   -766       C  
ATOM   5339  CD2 PHE B 303      53.343 -24.332  37.793  1.00 50.85           C  
ANISOU 5339  CD2 PHE B 303     7552   5691   6079   -384   1615   -878       C  
ATOM   5340  CE1 PHE B 303      52.407 -24.109  35.197  1.00 49.10           C  
ANISOU 5340  CE1 PHE B 303     6879   5465   6314   -174   1515   -694       C  
ATOM   5341  CE2 PHE B 303      52.215 -25.034  37.399  1.00 48.41           C  
ANISOU 5341  CE2 PHE B 303     7080   5405   5910   -312   1708   -810       C  
ATOM   5342  CZ  PHE B 303      51.750 -24.925  36.098  1.00 46.13           C  
ANISOU 5342  CZ  PHE B 303     6554   5117   5856   -209   1646   -720       C  
ATOM   5343  N   VAL B 304      54.215 -21.070  39.841  1.00 47.95           N  
ANISOU 5343  N   VAL B 304     7726   5001   5492   -577   1882  -1278       N  
ATOM   5344  CA  VAL B 304      53.252 -20.777  40.900  1.00 54.13           C  
ANISOU 5344  CA  VAL B 304     8676   5676   6214   -600   2197  -1413       C  
ATOM   5345  C   VAL B 304      52.693 -19.367  40.742  1.00 55.06           C  
ANISOU 5345  C   VAL B 304     8779   5588   6553   -520   2423  -1522       C  
ATOM   5346  O   VAL B 304      51.478 -19.150  40.844  1.00 57.03           O  
ANISOU 5346  O   VAL B 304     8946   5733   6990   -415   2705  -1559       O  
ATOM   5347  CB  VAL B 304      53.902 -20.978  42.283  1.00 54.16           C  
ANISOU 5347  CB  VAL B 304     9028   5710   5840   -800   2173  -1517       C  
ATOM   5348  CG1 VAL B 304      53.074 -20.301  43.365  1.00 52.12           C  
ANISOU 5348  CG1 VAL B 304     9009   5296   5498   -852   2538  -1706       C  
ATOM   5349  CG2 VAL B 304      54.057 -22.468  42.579  1.00 53.83           C  
ANISOU 5349  CG2 VAL B 304     9002   5835   5617   -848   2029  -1394       C  
ATOM   5350  N   GLU B 305      53.569 -18.389  40.495  1.00 54.43           N  
ANISOU 5350  N   GLU B 305     8767   5432   6481   -566   2309  -1571       N  
ATOM   5351  CA  GLU B 305      53.104 -17.027  40.246  1.00 56.80           C  
ANISOU 5351  CA  GLU B 305     9052   5511   7018   -480   2506  -1656       C  
ATOM   5352  C   GLU B 305      52.146 -16.984  39.061  1.00 56.78           C  
ANISOU 5352  C   GLU B 305     8721   5472   7382   -265   2544  -1509       C  
ATOM   5353  O   GLU B 305      51.091 -16.339  39.128  1.00 57.55           O  
ANISOU 5353  O   GLU B 305     8750   5398   7717   -144   2810  -1558       O  
ATOM   5354  CB  GLU B 305      54.298 -16.099  40.009  1.00 56.81           C  
ANISOU 5354  CB  GLU B 305     9156   5450   6978   -578   2334  -1699       C  
ATOM   5355  CG  GLU B 305      53.934 -14.629  39.847  1.00 64.63           C  
ANISOU 5355  CG  GLU B 305    10184   6177   8194   -512   2538  -1797       C  
ATOM   5356  CD  GLU B 305      55.152 -13.752  39.597  1.00 70.18           C  
ANISOU 5356  CD  GLU B 305    10990   6817   8856   -634   2364  -1835       C  
ATOM   5357  OE1 GLU B 305      55.728 -13.824  38.493  1.00 66.84           O  
ANISOU 5357  OE1 GLU B 305    10382   6469   8544   -597   2142  -1681       O  
ATOM   5358  OE2 GLU B 305      55.544 -12.999  40.511  1.00 79.67           O  
ANISOU 5358  OE2 GLU B 305    12471   7892   9907   -785   2459  -2026       O  
ATOM   5359  N   ILE B 306      52.484 -17.691  37.978  1.00 50.13           N  
ANISOU 5359  N   ILE B 306     7671   4783   6591   -220   2281  -1328       N  
ATOM   5360  CA  ILE B 306      51.657 -17.673  36.772  1.00 51.58           C  
ANISOU 5360  CA  ILE B 306     7565   4949   7084    -46   2256  -1172       C  
ATOM   5361  C   ILE B 306      50.280 -18.271  37.050  1.00 56.68           C  
ANISOU 5361  C   ILE B 306     8069   5600   7868     47   2454  -1156       C  
ATOM   5362  O   ILE B 306      49.248 -17.688  36.697  1.00 57.17           O  
ANISOU 5362  O   ILE B 306     7956   5526   8238    194   2602  -1125       O  
ATOM   5363  CB  ILE B 306      52.360 -18.415  35.620  1.00 49.45           C  
ANISOU 5363  CB  ILE B 306     7158   4852   6780    -55   1947  -1004       C  
ATOM   5364  CG1 ILE B 306      53.587 -17.644  35.122  1.00 46.22           C  
ANISOU 5364  CG1 ILE B 306     6828   4406   6328   -124   1789  -1001       C  
ATOM   5365  CG2 ILE B 306      51.398 -18.641  34.468  1.00 49.45           C  
ANISOU 5365  CG2 ILE B 306     6890   4864   7036     91   1900   -841       C  
ATOM   5366  CD1 ILE B 306      54.561 -18.521  34.333  1.00 43.70           C  
ANISOU 5366  CD1 ILE B 306     6437   4270   5897   -183   1529   -888       C  
ATOM   5367  N   ILE B 307      50.237 -19.450  37.677  1.00 53.74           N  
ANISOU 5367  N   ILE B 307     7751   5374   7292    -36   2457  -1165       N  
ATOM   5368  CA  ILE B 307      48.958 -20.142  37.805  1.00 54.10           C  
ANISOU 5368  CA  ILE B 307     7629   5443   7486     36   2626  -1127       C  
ATOM   5369  C   ILE B 307      48.074 -19.455  38.841  1.00 58.25           C  
ANISOU 5369  C   ILE B 307     8239   5790   8102     62   3015  -1288       C  
ATOM   5370  O   ILE B 307      46.854 -19.375  38.669  1.00 60.07           O  
ANISOU 5370  O   ILE B 307     8243   5945   8636    188   3205  -1258       O  
ATOM   5371  CB  ILE B 307      49.168 -21.639  38.116  1.00 57.10           C  
ANISOU 5371  CB  ILE B 307     8050   6014   7632    -67   2521  -1076       C  
ATOM   5372  CG1 ILE B 307      47.854 -22.405  37.910  1.00 52.99           C  
ANISOU 5372  CG1 ILE B 307     7292   5527   7316      5   2642  -1000       C  
ATOM   5373  CG2 ILE B 307      49.725 -21.846  39.533  1.00 55.30           C  
ANISOU 5373  CG2 ILE B 307     8156   5797   7058   -226   2623  -1213       C  
ATOM   5374  CD1 ILE B 307      47.943 -23.907  38.161  1.00 48.12           C  
ANISOU 5374  CD1 ILE B 307     6710   5071   6503    -93   2558   -939       C  
ATOM   5375  N   LYS B 308      48.670 -18.914  39.909  1.00 58.13           N  
ANISOU 5375  N   LYS B 308     8547   5696   7843    -59   3144  -1464       N  
ATOM   5376  CA  LYS B 308      47.887 -18.246  40.945  1.00 63.83           C  
ANISOU 5376  CA  LYS B 308     9404   6232   8616    -54   3555  -1648       C  
ATOM   5377  C   LYS B 308      47.292 -16.923  40.485  1.00 62.18           C  
ANISOU 5377  C   LYS B 308     9051   5786   8788    115   3725  -1680       C  
ATOM   5378  O   LYS B 308      46.411 -16.393  41.165  1.00 65.26           O  
ANISOU 5378  O   LYS B 308     9446   6030   9321    152   4040  -1772       O  
ATOM   5379  CB  LYS B 308      48.732 -18.013  42.203  1.00 64.17           C  
ANISOU 5379  CB  LYS B 308     9878   6251   8251   -260   3626  -1837       C  
ATOM   5380  CG  LYS B 308      48.785 -19.220  43.139  1.00 68.81           C  
ANISOU 5380  CG  LYS B 308    10656   6994   8496   -415   3648  -1848       C  
ATOM   5381  CD  LYS B 308      49.443 -18.879  44.467  1.00 74.29           C  
ANISOU 5381  CD  LYS B 308    11756   7664   8807   -631   3671  -1986       C  
ATOM   5382  CE  LYS B 308      49.436 -20.073  45.408  1.00 75.52           C  
ANISOU 5382  CE  LYS B 308    12101   7962   8632   -783   3663  -1953       C  
ATOM   5383  NZ  LYS B 308      50.164 -19.792  46.676  1.00 84.33           N  
ANISOU 5383  NZ  LYS B 308    13614   9071   9357  -1007   3609  -2049       N  
ATOM   5384  N   SER B 309      47.736 -16.378  39.361  1.00 63.57           N  
ANISOU 5384  N   SER B 309     9086   5941   9129    199   3471  -1556       N  
ATOM   5385  CA  SER B 309      47.175 -15.128  38.873  1.00 70.95           C  
ANISOU 5385  CA  SER B 309     9885   6633  10441    370   3605  -1553       C  
ATOM   5386  C   SER B 309      46.017 -15.338  37.905  1.00 71.84           C  
ANISOU 5386  C   SER B 309     9585   6743  10967    572   3574  -1361       C  
ATOM   5387  O   SER B 309      45.456 -14.355  37.411  1.00 76.18           O  
ANISOU 5387  O   SER B 309     9977   7088  11879    740   3653  -1315       O  
ATOM   5388  CB  SER B 309      48.269 -14.288  38.208  1.00 68.19           C  
ANISOU 5388  CB  SER B 309     9633   6226  10048    339   3362  -1518       C  
ATOM   5389  OG  SER B 309      48.706 -14.887  37.004  1.00 71.38           O  
ANISOU 5389  OG  SER B 309     9857   6813  10451    355   2997  -1303       O  
ATOM   5390  N   GLN B 310      45.633 -16.585  37.642  1.00 66.58           N  
ANISOU 5390  N   GLN B 310     7634   6913  10750    368   3193  -1597       N  
ATOM   5391  CA  GLN B 310      44.607 -16.880  36.652  1.00 67.32           C  
ANISOU 5391  CA  GLN B 310     7352   6984  11245    454   3032  -1208       C  
ATOM   5392  C   GLN B 310      43.202 -16.768  37.232  1.00 71.66           C  
ANISOU 5392  C   GLN B 310     7599   7420  12211    501   3449  -1224       C  
ATOM   5393  O   GLN B 310      42.960 -17.054  38.410  1.00 68.87           O  
ANISOU 5393  O   GLN B 310     7403   7137  11628    406   3812  -1503       O  
ATOM   5394  CB  GLN B 310      44.793 -18.286  36.082  1.00 59.63           C  
ANISOU 5394  CB  GLN B 310     6505   6289   9862    333   2639   -980       C  
ATOM   5395  CG  GLN B 310      46.099 -18.488  35.345  1.00 61.16           C  
ANISOU 5395  CG  GLN B 310     6934   6583   9720    298   2248   -932       C  
ATOM   5396  CD  GLN B 310      46.289 -17.491  34.217  1.00 66.54           C  
ANISOU 5396  CD  GLN B 310     7400   7130  10752    403   2056   -739       C  
ATOM   5397  OE1 GLN B 310      45.372 -17.232  33.441  1.00 61.38           O  
ANISOU 5397  OE1 GLN B 310     6388   6424  10508    450   1976   -446       O  
ATOM   5398  NE2 GLN B 310      47.484 -16.928  34.123  1.00 56.84           N  
ANISOU 5398  NE2 GLN B 310     6364   5860   9371    420   1962   -860       N  
ATOM   5399  N   ASP B 311      42.268 -16.371  36.370  1.00 72.65           N  
ANISOU 5399  N   ASP B 311     7262   7392  12948    628   3384   -885       N  
ATOM   5400  CA  ASP B 311      40.850 -16.354  36.704  1.00 74.47           C  
ANISOU 5400  CA  ASP B 311     7116   7518  13660    681   3706   -787       C  
ATOM   5401  C   ASP B 311      40.275 -17.750  36.489  1.00 75.68           C  
ANISOU 5401  C   ASP B 311     7243   7961  13553    540   3490   -553       C  
ATOM   5402  O   ASP B 311      40.364 -18.302  35.387  1.00 71.86           O  
ANISOU 5402  O   ASP B 311     6700   7630  12971    473   3006   -226       O  
ATOM   5403  CB  ASP B 311      40.132 -15.312  35.848  1.00 70.58           C  
ANISOU 5403  CB  ASP B 311     6179   6752  13888    824   3591   -425       C  
ATOM   5404  CG  ASP B 311      38.652 -15.238  36.133  1.00 83.08           C  
ANISOU 5404  CG  ASP B 311     7431   8211  15925    846   3799   -257       C  
ATOM   5405  OD1 ASP B 311      37.884 -15.995  35.504  1.00 88.59           O  
ANISOU 5405  OD1 ASP B 311     7825   9069  16765    817   3587    112       O  
ATOM   5406  OD2 ASP B 311      38.255 -14.435  37.002  1.00 89.37           O  
ANISOU 5406  OD2 ASP B 311     8267   8755  16932    864   4175   -501       O  
ATOM   5407  N   LEU B 312      39.695 -18.327  37.542  1.00 80.27           N  
ANISOU 5407  N   LEU B 312     7885   8623  13992    457   3851   -732       N  
ATOM   5408  CA  LEU B 312      39.268 -19.721  37.531  1.00 82.76           C  
ANISOU 5408  CA  LEU B 312     8250   9196  14000    288   3672   -556       C  
ATOM   5409  C   LEU B 312      37.764 -19.884  37.332  1.00 84.67           C  
ANISOU 5409  C   LEU B 312     7984   9390  14796    311   3800   -267       C  
ATOM   5410  O   LEU B 312      37.204 -20.910  37.731  1.00 85.29           O  
ANISOU 5410  O   LEU B 312     8075   9634  14698    167   3853   -208       O  
ATOM   5411  CB  LEU B 312      39.697 -20.413  38.828  1.00 81.92           C  
ANISOU 5411  CB  LEU B 312     8559   9266  13300    132   3925   -864       C  
ATOM   5412  CG  LEU B 312      41.171 -20.299  39.229  1.00 71.60           C  
ANISOU 5412  CG  LEU B 312     7734   8040  11431     73   3818  -1132       C  
ATOM   5413  CD1 LEU B 312      41.451 -21.134  40.467  1.00 72.45           C  
ANISOU 5413  CD1 LEU B 312     8186   8383  10958   -130   3998  -1301       C  
ATOM   5414  CD2 LEU B 312      42.068 -20.715  38.078  1.00 65.02           C  
ANISOU 5414  CD2 LEU B 312     7024   7270  10410     71   3254   -929       C  
ATOM   5415  N   SER B 313      37.098 -18.913  36.711  1.00 84.59           N  
ANISOU 5415  N   SER B 313     7525   9155  15462    475   3806    -38       N  
ATOM   5416  CA  SER B 313      35.643 -18.936  36.610  1.00 87.84           C  
ANISOU 5416  CA  SER B 313     7528   9494  16352    492   3843    257       C  
ATOM   5417  C   SER B 313      35.131 -19.412  35.256  1.00 82.96           C  
ANISOU 5417  C   SER B 313     6518   9022  15979    411   3339    781       C  
ATOM   5418  O   SER B 313      33.914 -19.440  35.051  1.00 85.23           O  
ANISOU 5418  O   SER B 313     6452   9270  16660    410   3292   1081       O  
ATOM   5419  CB  SER B 313      35.069 -17.548  36.924  1.00 90.87           C  
ANISOU 5419  CB  SER B 313     7754   9503  17269    672   4108    211       C  
ATOM   5420  OG  SER B 313      35.746 -16.530  36.209  1.00 93.92           O  
ANISOU 5420  OG  SER B 313     8116   9705  17865    786   3912    289       O  
ATOM   5421  N   VAL B 314      36.018 -19.792  34.337  1.00 82.81           N  
ANISOU 5421  N   VAL B 314     6663   9189  15614    300   2885    882       N  
ATOM   5422  CA  VAL B 314      35.638 -20.290  33.020  1.00 83.70           C  
ANISOU 5422  CA  VAL B 314     6540   9507  15754    122   2321   1325       C  
ATOM   5423  C   VAL B 314      35.971 -21.771  32.947  1.00 78.92           C  
ANISOU 5423  C   VAL B 314     6320   9170  14497   -146   2076   1210       C  
ATOM   5424  O   VAL B 314      36.943 -22.238  33.551  1.00 73.91           O  
ANISOU 5424  O   VAL B 314     6186   8564  13332   -165   2171    855       O  
ATOM   5425  CB  VAL B 314      36.357 -19.530  31.885  1.00 87.68           C  
ANISOU 5425  CB  VAL B 314     7028  10021  16266    151   1920   1527       C  
ATOM   5426  CG1 VAL B 314      35.404 -19.287  30.724  1.00 95.50           C  
ANISOU 5426  CG1 VAL B 314     7447  11107  17730     58   1534   2123       C  
ATOM   5427  CG2 VAL B 314      36.949 -18.229  32.401  1.00 91.30           C  
ANISOU 5427  CG2 VAL B 314     7530  10165  16995    422   2257   1311       C  
ATOM   5428  N  AVAL B 315      35.158 -22.511  32.188  0.44 71.94           N  
ANISOU 5428  N  AVAL B 315     5176   8469  13691   -371   1749   1531       N  
ATOM   5429  N  BVAL B 315      35.157 -22.519  32.196  0.56 71.50           N  
ANISOU 5429  N  BVAL B 315     5122   8414  13633   -371   1752   1529       N  
ATOM   5430  CA AVAL B 315      35.388 -23.945  32.030  0.44 70.31           C  
ANISOU 5430  CA AVAL B 315     5293   8462  12960   -649   1527   1421       C  
ATOM   5431  CA BVAL B 315      35.407 -23.952  32.044  0.56 70.08           C  
ANISOU 5431  CA BVAL B 315     5273   8432  12922   -648   1531   1414       C  
ATOM   5432  C  AVAL B 315      36.718 -24.201  31.327  0.44 69.37           C  
ANISOU 5432  C  AVAL B 315     5623   8445  12288   -739   1207   1245       C  
ATOM   5433  C  BVAL B 315      36.742 -24.188  31.343  0.56 69.43           C  
ANISOU 5433  C  BVAL B 315     5638   8449  12292   -733   1212   1238       C  
ATOM   5434  O  AVAL B 315      37.504 -25.061  31.746  0.44 66.50           O  
ANISOU 5434  O  AVAL B 315     5701   8096  11472   -804   1252    955       O  
ATOM   5435  O  BVAL B 315      37.553 -25.018  31.774  0.56 65.98           O  
ANISOU 5435  O  BVAL B 315     5646   8022  11400   -792   1263    944       O  
ATOM   5436  CB AVAL B 315      34.208 -24.597  31.284  0.44 74.10           C  
ANISOU 5436  CB AVAL B 315     5374   9113  13669   -917   1230   1788       C  
ATOM   5437  CB BVAL B 315      34.242 -24.629  31.299  0.56 74.06           C  
ANISOU 5437  CB BVAL B 315     5388   9108  13642   -919   1231   1774       C  
ATOM   5438  CG1AVAL B 315      33.847 -23.799  30.031  0.44 77.15           C  
ANISOU 5438  CG1AVAL B 315     5347   9605  14361   -971    826   2217       C  
ATOM   5439  CG1BVAL B 315      34.678 -25.975  30.736  0.56 74.18           C  
ANISOU 5439  CG1BVAL B 315     5758   9308  13119  -1248    906   1644       C  
ATOM   5440  CG2AVAL B 315      34.526 -26.047  30.939  0.44 73.74           C  
ANISOU 5440  CG2AVAL B 315     5676   9232  13110  -1238    975   1640       C  
ATOM   5441  CG2BVAL B 315      33.049 -24.810  32.235  0.56 72.14           C  
ANISOU 5441  CG2BVAL B 315     4806   8773  13829   -870   1616   1861       C  
ATOM   5442  N   SER B 316      36.998 -23.456  30.261  1.00 67.93           N  
ANISOU 5442  N   SER B 316     5312   8330  12167   -744    893   1446       N  
ATOM   5443  CA  SER B 316      38.250 -23.623  29.535  1.00 70.09           C  
ANISOU 5443  CA  SER B 316     5980   8713  11940   -834    625   1285       C  
ATOM   5444  C   SER B 316      38.575 -22.353  28.769  1.00 64.66           C  
ANISOU 5444  C   SER B 316     5108   8020  11438   -724    451   1510       C  
ATOM   5445  O   SER B 316      37.699 -21.762  28.136  1.00 66.62           O  
ANISOU 5445  O   SER B 316     4885   8325  12103   -761    269   1935       O  
ATOM   5446  CB  SER B 316      38.188 -24.812  28.568  1.00 70.95           C  
ANISOU 5446  CB  SER B 316     6201   9068  11689  -1211    257   1306       C  
ATOM   5447  OG  SER B 316      37.289 -24.557  27.503  1.00 76.84           O  
ANISOU 5447  OG  SER B 316     6527  10022  12647  -1424    -96   1720       O  
ATOM   5448  N   LYS B 317      39.841 -21.950  28.816  1.00 65.38           N  
ANISOU 5448  N   LYS B 317     5547   8046  11249   -603    489   1272       N  
ATOM   5449  CA  LYS B 317      40.297 -20.851  27.982  1.00 70.59           C  
ANISOU 5449  CA  LYS B 317     6081   8720  12020   -543    288   1491       C  
ATOM   5450  C   LYS B 317      41.770 -21.057  27.662  1.00 62.40           C  
ANISOU 5450  C   LYS B 317     5512   7752  10445   -583    192   1209       C  
ATOM   5451  O   LYS B 317      42.458 -21.868  28.290  1.00 53.61           O  
ANISOU 5451  O   LYS B 317     4785   6603   8980   -581    342    845       O  
ATOM   5452  CB  LYS B 317      40.053 -19.482  28.642  1.00 79.37           C  
ANISOU 5452  CB  LYS B 317     6916   9517  13722   -220    595   1573       C  
ATOM   5453  CG  LYS B 317      40.794 -19.220  29.945  1.00 77.14           C  
ANISOU 5453  CG  LYS B 317     6965   8989  13355      5   1032   1113       C  
ATOM   5454  CD  LYS B 317      40.654 -17.750  30.348  1.00 77.91           C  
ANISOU 5454  CD  LYS B 317     6796   8761  14045    274   1314   1164       C  
ATOM   5455  CE  LYS B 317      41.407 -17.429  31.634  1.00 82.95           C  
ANISOU 5455  CE  LYS B 317     7782   9192  14542    428   1742    665       C  
ATOM   5456  NZ  LYS B 317      41.361 -15.973  31.966  1.00 83.73           N  
ANISOU 5456  NZ  LYS B 317     7655   8935  15225    656   2040    640       N  
ATOM   5457  N   VAL B 318      42.233 -20.342  26.643  1.00 56.86           N  
ANISOU 5457  N   VAL B 318     4739   7162   9705   -634    -71   1429       N  
ATOM   5458  CA  VAL B 318      43.650 -20.300  26.293  1.00 59.27           C  
ANISOU 5458  CA  VAL B 318     5419   7514   9586   -643   -131   1205       C  
ATOM   5459  C   VAL B 318      44.267 -19.085  26.967  1.00 61.63           C  
ANISOU 5459  C   VAL B 318     5727   7530  10162   -336    105   1131       C  
ATOM   5460  O   VAL B 318      43.728 -17.979  26.879  1.00 62.07           O  
ANISOU 5460  O   VAL B 318     5419   7441  10722   -204    124   1430       O  
ATOM   5461  CB  VAL B 318      43.856 -20.246  24.769  1.00 59.56           C  
ANISOU 5461  CB  VAL B 318     5398   7876   9354   -928   -533   1471       C  
ATOM   5462  CG1 VAL B 318      45.339 -20.082  24.437  1.00 57.34           C  
ANISOU 5462  CG1 VAL B 318     5466   7623   8698   -910   -536   1248       C  
ATOM   5463  CG2 VAL B 318      43.291 -21.497  24.110  1.00 65.53           C  
ANISOU 5463  CG2 VAL B 318     6193   8920   9784  -1296   -746   1455       C  
ATOM   5464  N   VAL B 319      45.394 -19.291  27.643  1.00 52.05           N  
ANISOU 5464  N   VAL B 319     4902   6217   8656   -238    283    747       N  
ATOM   5465  CA  VAL B 319      46.113 -18.231  28.336  1.00 52.11           C  
ANISOU 5465  CA  VAL B 319     4982   5975   8843     -6    502    601       C  
ATOM   5466  C   VAL B 319      47.474 -18.088  27.667  1.00 56.60           C  
ANISOU 5466  C   VAL B 319     5794   6640   9071    -56    332    536       C  
ATOM   5467  O   VAL B 319      48.212 -19.073  27.540  1.00 53.08           O  
ANISOU 5467  O   VAL B 319     5650   6333   8185   -170    273    327       O  
ATOM   5468  CB  VAL B 319      46.258 -18.536  29.838  1.00 52.39           C  
ANISOU 5468  CB  VAL B 319     5241   5846   8818    115    857    225       C  
ATOM   5469  CG1 VAL B 319      47.149 -17.511  30.503  1.00 59.25           C  
ANISOU 5469  CG1 VAL B 319     6242   6504   9766    276   1050     15       C  
ATOM   5470  CG2 VAL B 319      44.874 -18.554  30.509  1.00 55.45           C  
ANISOU 5470  CG2 VAL B 319     5354   6133   9582    168   1088    290       C  
ATOM   5471  N   LYS B 320      47.798 -16.871  27.226  1.00 48.02           N  
ANISOU 5471  N   LYS B 320     4550   5456   8239     27    274    732       N  
ATOM   5472  CA  LYS B 320      49.085 -16.581  26.600  1.00 50.79           C  
ANISOU 5472  CA  LYS B 320     5090   5887   8320    -15    139    704       C  
ATOM   5473  C   LYS B 320      50.031 -15.993  27.643  1.00 50.24           C  
ANISOU 5473  C   LYS B 320     5224   5564   8303    167    383    392       C  
ATOM   5474  O   LYS B 320      49.693 -15.007  28.305  1.00 55.04           O  
ANISOU 5474  O   LYS B 320     5676   5894   9342    325    585    378       O  
ATOM   5475  CB  LYS B 320      48.910 -15.609  25.434  1.00 63.14           C  
ANISOU 5475  CB  LYS B 320     6350   7525  10114    -78   -103   1164       C  
ATOM   5476  CG  LYS B 320      47.900 -16.044  24.389  1.00 66.86           C  
ANISOU 5476  CG  LYS B 320     6571   8295  10537   -313   -393   1543       C  
ATOM   5477  CD  LYS B 320      48.559 -16.826  23.270  1.00 72.21           C  
ANISOU 5477  CD  LYS B 320     7471   9360  10608   -612   -633   1519       C  
ATOM   5478  CE  LYS B 320      47.586 -17.053  22.125  1.00 80.43           C  
ANISOU 5478  CE  LYS B 320     8245  10751  11565   -921   -968   1936       C  
ATOM   5479  NZ  LYS B 320      47.045 -15.770  21.603  1.00 89.77           N  
ANISOU 5479  NZ  LYS B 320     8987  11904  13219   -886  -1153   2522       N  
ATOM   5480  N   VAL B 321      51.212 -16.589  27.782  1.00 44.54           N  
ANISOU 5480  N   VAL B 321     4828   4926   7167    125    372    138       N  
ATOM   5481  CA  VAL B 321      52.243 -16.111  28.699  1.00 46.82           C  
ANISOU 5481  CA  VAL B 321     5317   5042   7429    235    533   -132       C  
ATOM   5482  C   VAL B 321      53.524 -15.888  27.904  1.00 45.25           C  
ANISOU 5482  C   VAL B 321     5223   4939   7032    181    374    -88       C  
ATOM   5483  O   VAL B 321      53.919 -16.750  27.111  1.00 39.98           O  
ANISOU 5483  O   VAL B 321     4656   4494   6041     54    234    -65       O  
ATOM   5484  CB  VAL B 321      52.485 -17.113  29.843  1.00 46.66           C  
ANISOU 5484  CB  VAL B 321     5560   5039   7129    231    679   -441       C  
ATOM   5485  CG1 VAL B 321      53.518 -16.566  30.831  1.00 44.39           C  
ANISOU 5485  CG1 VAL B 321     5460   4625   6783    287    805   -686       C  
ATOM   5486  CG2 VAL B 321      51.158 -17.444  30.547  1.00 49.72           C  
ANISOU 5486  CG2 VAL B 321     5837   5379   7678    251    850   -461       C  
ATOM   5487  N   THR B 322      54.173 -14.738  28.114  1.00 41.38           N  
ANISOU 5487  N   THR B 322     4705   4266   6753    263    425    -99       N  
ATOM   5488  CA  THR B 322      55.429 -14.450  27.425  1.00 37.61           C  
ANISOU 5488  CA  THR B 322     4305   3866   6121    213    297    -47       C  
ATOM   5489  C   THR B 322      56.572 -15.155  28.148  1.00 35.57           C  
ANISOU 5489  C   THR B 322     4326   3642   5546    209    351   -345       C  
ATOM   5490  O   THR B 322      56.796 -14.925  29.342  1.00 38.29           O  
ANISOU 5490  O   THR B 322     4777   3840   5932    264    489   -570       O  
ATOM   5491  CB  THR B 322      55.687 -12.944  27.345  1.00 42.51           C  
ANISOU 5491  CB  THR B 322     4760   4254   7138    284    320     88       C  
ATOM   5492  OG1 THR B 322      54.579 -12.314  26.702  1.00 45.24           O  
ANISOU 5492  OG1 THR B 322     4787   4542   7862    300    259    442       O  
ATOM   5493  CG2 THR B 322      56.936 -12.678  26.509  1.00 42.23           C  
ANISOU 5493  CG2 THR B 322     4775   4335   6938    207    178    197       C  
ATOM   5494  N   ILE B 323      57.273 -16.034  27.430  1.00 35.08           N  
ANISOU 5494  N   ILE B 323     4371   3782   5178    122    252   -341       N  
ATOM   5495  CA  ILE B 323      58.351 -16.856  27.978  1.00 38.31           C  
ANISOU 5495  CA  ILE B 323     4982   4217   5357    126    287   -546       C  
ATOM   5496  C   ILE B 323      59.453 -16.940  26.929  1.00 33.98           C  
ANISOU 5496  C   ILE B 323     4443   3795   4674     61    214   -479       C  
ATOM   5497  O   ILE B 323      59.178 -17.223  25.760  1.00 36.37           O  
ANISOU 5497  O   ILE B 323     4693   4270   4857    -51    155   -363       O  
ATOM   5498  CB  ILE B 323      57.867 -18.274  28.355  1.00 35.31           C  
ANISOU 5498  CB  ILE B 323     4709   3901   4806    100    334   -658       C  
ATOM   5499  CG1 ILE B 323      56.647 -18.201  29.281  1.00 40.69           C  
ANISOU 5499  CG1 ILE B 323     5355   4495   5611    141    431   -696       C  
ATOM   5500  CG2 ILE B 323      58.967 -19.036  29.055  1.00 37.07           C  
ANISOU 5500  CG2 ILE B 323     5085   4104   4896    124    362   -793       C  
ATOM   5501  CD1 ILE B 323      56.159 -19.564  29.773  1.00 41.74           C  
ANISOU 5501  CD1 ILE B 323     5585   4674   5602    105    482   -778       C  
ATOM   5502  N   ASP B 324      60.695 -16.675  27.335  1.00 31.44           N  
ANISOU 5502  N   ASP B 324     4179   3412   4355     98    222   -551       N  
ATOM   5503  CA  ASP B 324      61.813 -16.672  26.386  1.00 37.86           C  
ANISOU 5503  CA  ASP B 324     4971   4329   5083     45    196   -489       C  
ATOM   5504  C   ASP B 324      61.504 -15.763  25.197  1.00 38.06           C  
ANISOU 5504  C   ASP B 324     4854   4452   5156    -40    122   -251       C  
ATOM   5505  O   ASP B 324      61.833 -16.079  24.051  1.00 36.43           O  
ANISOU 5505  O   ASP B 324     4634   4445   4762   -162    115   -179       O  
ATOM   5506  CB  ASP B 324      62.146 -18.093  25.891  1.00 36.99           C  
ANISOU 5506  CB  ASP B 324     4946   4336   4774     -5    268   -598       C  
ATOM   5507  CG  ASP B 324      62.651 -19.024  26.992  1.00 38.81           C  
ANISOU 5507  CG  ASP B 324     5268   4455   5021     80    320   -737       C  
ATOM   5508  OD1 ASP B 324      63.155 -18.530  28.029  1.00 37.92           O  
ANISOU 5508  OD1 ASP B 324     5166   4248   4994    139    275   -742       O  
ATOM   5509  OD2 ASP B 324      62.584 -20.281  26.791  1.00 38.52           O  
ANISOU 5509  OD2 ASP B 324     5287   4431   4919     60    404   -830       O  
ATOM   5510  N   TYR B 325      60.825 -14.640  25.469  1.00 36.87           N  
ANISOU 5510  N   TYR B 325     4583   4159   5268      6     82   -118       N  
ATOM   5511  CA  TYR B 325      60.420 -13.616  24.505  1.00 33.75           C  
ANISOU 5511  CA  TYR B 325     3992   3798   5033    -58    -16    204       C  
ATOM   5512  C   TYR B 325      59.314 -14.049  23.547  1.00 44.38           C  
ANISOU 5512  C   TYR B 325     5246   5370   6246   -184   -113    406       C  
ATOM   5513  O   TYR B 325      58.987 -13.287  22.638  1.00 44.38           O  
ANISOU 5513  O   TYR B 325     5059   5464   6338   -278   -239    754       O  
ATOM   5514  CB  TYR B 325      61.588 -13.100  23.650  1.00 37.07           C  
ANISOU 5514  CB  TYR B 325     4371   4319   5394   -142    -58    350       C  
ATOM   5515  CG  TYR B 325      62.647 -12.380  24.444  1.00 37.92           C  
ANISOU 5515  CG  TYR B 325     4502   4205   5702    -58    -12    238       C  
ATOM   5516  CD1 TYR B 325      62.368 -11.170  25.080  1.00 43.17           C  
ANISOU 5516  CD1 TYR B 325     5068   4578   6757     14     -3    279       C  
ATOM   5517  CD2 TYR B 325      63.925 -12.900  24.551  1.00 34.11           C  
ANISOU 5517  CD2 TYR B 325     4118   3788   5055    -69     32     88       C  
ATOM   5518  CE1 TYR B 325      63.342 -10.505  25.811  1.00 40.22           C  
ANISOU 5518  CE1 TYR B 325     4729   4012   6540     33     30    139       C  
ATOM   5519  CE2 TYR B 325      64.905 -12.248  25.279  1.00 34.31           C  
ANISOU 5519  CE2 TYR B 325     4142   3641   5252    -34     33     10       C  
ATOM   5520  CZ  TYR B 325      64.606 -11.057  25.909  1.00 37.49           C  
ANISOU 5520  CZ  TYR B 325     4482   3786   5977     -3     22     20       C  
ATOM   5521  OH  TYR B 325      65.582 -10.405  26.625  1.00 41.24           O  
ANISOU 5521  OH  TYR B 325     4969   4103   6596    -24     14    -91       O  
ATOM   5522  N   THR B 326      58.721 -15.227  23.709  1.00 35.69           N  
ANISOU 5522  N   THR B 326     4251   4368   4941   -218    -80    237       N  
ATOM   5523  CA  THR B 326      57.675 -15.667  22.791  1.00 36.21           C  
ANISOU 5523  CA  THR B 326     4228   4676   4855   -393   -197    415       C  
ATOM   5524  C   THR B 326      56.378 -15.912  23.564  1.00 36.05           C  
ANISOU 5524  C   THR B 326     4139   4529   5031   -309   -177    392       C  
ATOM   5525  O   THR B 326      56.385 -16.110  24.784  1.00 40.63           O  
ANISOU 5525  O   THR B 326     4815   4891   5732   -149    -34    154       O  
ATOM   5526  CB  THR B 326      58.116 -16.937  22.015  1.00 39.30           C  
ANISOU 5526  CB  THR B 326     4796   5333   4804   -586   -159    222       C  
ATOM   5527  OG1 THR B 326      57.306 -17.108  20.844  1.00 44.31           O  
ANISOU 5527  OG1 THR B 326     5340   6284   5213   -854   -314    434       O  
ATOM   5528  CG2 THR B 326      58.003 -18.185  22.886  1.00 38.40           C  
ANISOU 5528  CG2 THR B 326     4854   5098   4639   -507    -21   -115       C  
ATOM   5529  N   GLU B 327      55.255 -15.876  22.842  1.00 41.24           N  
ANISOU 5529  N   GLU B 327     4608   5351   5711   -446   -329    671       N  
ATOM   5530  CA  GLU B 327      53.945 -16.122  23.439  1.00 43.80           C  
ANISOU 5530  CA  GLU B 327     4812   5581   6250   -389   -311    696       C  
ATOM   5531  C   GLU B 327      53.707 -17.624  23.496  1.00 40.14           C  
ANISOU 5531  C   GLU B 327     4538   5256   5457   -509   -271    430       C  
ATOM   5532  O   GLU B 327      53.493 -18.264  22.461  1.00 42.67           O  
ANISOU 5532  O   GLU B 327     4874   5867   5471   -766   -401    486       O  
ATOM   5533  CB  GLU B 327      52.834 -15.448  22.637  1.00 50.66           C  
ANISOU 5533  CB  GLU B 327     5337   6564   7346   -495   -521   1172       C  
ATOM   5534  CG  GLU B 327      52.882 -13.929  22.609  1.00 71.20           C  
ANISOU 5534  CG  GLU B 327     7682   8948  10423   -358   -547   1500       C  
ATOM   5535  CD  GLU B 327      52.678 -13.315  23.977  1.00 87.09           C  
ANISOU 5535  CD  GLU B 327     9655  10522  12912    -71   -289   1301       C  
ATOM   5536  OE1 GLU B 327      53.680 -12.860  24.571  1.00 92.35           O  
ANISOU 5536  OE1 GLU B 327    10481  10990  13616     45   -145   1065       O  
ATOM   5537  OE2 GLU B 327      51.521 -13.295  24.457  1.00 91.37           O  
ANISOU 5537  OE2 GLU B 327    10004  10933  13778     10   -218   1367       O  
ATOM   5538  N   ILE B 328      53.713 -18.187  24.696  1.00 39.64           N  
ANISOU 5538  N   ILE B 328     4614   4994   5454   -356    -91    149       N  
ATOM   5539  CA  ILE B 328      53.398 -19.599  24.893  1.00 39.02           C  
ANISOU 5539  CA  ILE B 328     4684   4975   5167   -448    -36    -68       C  
ATOM   5540  C   ILE B 328      51.925 -19.717  25.264  1.00 46.45           C  
ANISOU 5540  C   ILE B 328     5442   5888   6317   -454    -49     57       C  
ATOM   5541  O   ILE B 328      51.446 -19.019  26.168  1.00 41.32           O  
ANISOU 5541  O   ILE B 328     4673   5040   5989   -273     62    100       O  
ATOM   5542  CB  ILE B 328      54.294 -20.226  25.971  1.00 41.50           C  
ANISOU 5542  CB  ILE B 328     5230   5112   5424   -306    144   -368       C  
ATOM   5543  CG1 ILE B 328      55.759 -20.152  25.528  1.00 36.90           C  
ANISOU 5543  CG1 ILE B 328     4774   4559   4686   -306    155   -458       C  
ATOM   5544  CG2 ILE B 328      53.875 -21.690  26.228  1.00 36.48           C  
ANISOU 5544  CG2 ILE B 328     4710   4483   4668   -391    208   -537       C  
ATOM   5545  CD1 ILE B 328      56.017 -20.815  24.184  1.00 38.66           C  
ANISOU 5545  CD1 ILE B 328     5047   5009   4632   -534    105   -493       C  
ATOM   5546  N   SER B 329      51.201 -20.586  24.561  1.00 45.18           N  
ANISOU 5546  N   SER B 329     5251   5927   5989   -683   -163     95       N  
ATOM   5547  CA  SER B 329      49.792 -20.827  24.850  1.00 52.08           C  
ANISOU 5547  CA  SER B 329     5927   6798   7063   -722   -190    230       C  
ATOM   5548  C   SER B 329      49.654 -21.933  25.887  1.00 50.98           C  
ANISOU 5548  C   SER B 329     5960   6515   6896   -665      1    -46       C  
ATOM   5549  O   SER B 329      50.205 -23.026  25.710  1.00 44.38           O  
ANISOU 5549  O   SER B 329     5347   5709   5806   -776     35   -276       O  
ATOM   5550  CB  SER B 329      49.026 -21.207  23.580  1.00 51.08           C  
ANISOU 5550  CB  SER B 329     5660   6988   6761  -1054   -446    436       C  
ATOM   5551  OG  SER B 329      48.971 -20.128  22.666  1.00 54.92           O  
ANISOU 5551  OG  SER B 329     5924   7639   7303  -1130   -659    807       O  
ATOM   5552  N   PHE B 330      48.919 -21.646  26.964  1.00 47.81           N  
ANISOU 5552  N   PHE B 330     5440   5944   6781   -500    150    -14       N  
ATOM   5553  CA  PHE B 330      48.552 -22.632  27.974  1.00 43.31           C  
ANISOU 5553  CA  PHE B 330     4978   5274   6202   -479    320   -185       C  
ATOM   5554  C   PHE B 330      47.062 -22.943  27.888  1.00 49.73           C  
ANISOU 5554  C   PHE B 330     5540   6150   7207   -591    280     -8       C  
ATOM   5555  O   PHE B 330      46.240 -22.046  27.679  1.00 48.91           O  
ANISOU 5555  O   PHE B 330     5128   6054   7403   -551    230    249       O  
ATOM   5556  CB  PHE B 330      48.874 -22.144  29.391  1.00 43.61           C  
ANISOU 5556  CB  PHE B 330     5101   5118   6352   -255    563   -316       C  
ATOM   5557  CG  PHE B 330      50.345 -22.117  29.718  1.00 46.19           C  
ANISOU 5557  CG  PHE B 330     5687   5392   6473   -177    595   -497       C  
ATOM   5558  CD1 PHE B 330      51.166 -21.114  29.216  1.00 45.07           C  
ANISOU 5558  CD1 PHE B 330     5538   5244   6344   -115    521   -463       C  
ATOM   5559  CD2 PHE B 330      50.900 -23.079  30.552  1.00 45.24           C  
ANISOU 5559  CD2 PHE B 330     5782   5222   6184   -173    689   -650       C  
ATOM   5560  CE1 PHE B 330      52.514 -21.083  29.520  1.00 42.96           C  
ANISOU 5560  CE1 PHE B 330     5472   4935   5918    -55    540   -606       C  
ATOM   5561  CE2 PHE B 330      52.248 -23.055  30.860  1.00 45.04           C  
ANISOU 5561  CE2 PHE B 330     5940   5158   6016   -109    689   -756       C  
ATOM   5562  CZ  PHE B 330      53.054 -22.054  30.341  1.00 43.91           C  
ANISOU 5562  CZ  PHE B 330     5784   5019   5881    -51    617   -747       C  
ATOM   5563  N   MET B 331      46.718 -24.214  28.063  1.00 47.85           N  
ANISOU 5563  N   MET B 331     5400   5927   6853   -731    307   -120       N  
ATOM   5564  CA  MET B 331      45.326 -24.634  28.178  1.00 51.85           C  
ANISOU 5564  CA  MET B 331     5674   6472   7554   -842    300     28       C  
ATOM   5565  C   MET B 331      44.940 -24.603  29.650  1.00 52.40           C  
ANISOU 5565  C   MET B 331     5733   6367   7808   -656    595    -30       C  
ATOM   5566  O   MET B 331      45.598 -25.243  30.474  1.00 47.88           O  
ANISOU 5566  O   MET B 331     5420   5703   7069   -606    742   -223       O  
ATOM   5567  CB  MET B 331      45.124 -26.039  27.607  1.00 66.39           C  
ANISOU 5567  CB  MET B 331     7627   8403   9196  -1128    193    -79       C  
ATOM   5568  CG  MET B 331      44.987 -26.093  26.102  1.00 84.77           C  
ANISOU 5568  CG  MET B 331     9885  10985  11340  -1426    -98      6       C  
ATOM   5569  SD  MET B 331      43.567 -25.140  25.533  1.00104.13           S  
ANISOU 5569  SD  MET B 331    11848  13630  14087  -1518   -333    473       S  
ATOM   5570  CE  MET B 331      42.263 -25.793  26.571  1.00 94.66           C  
ANISOU 5570  CE  MET B 331    10455  12298  13213  -1496   -163    529       C  
ATOM   5571  N   LEU B 332      43.889 -23.859  29.986  1.00 55.29           N  
ANISOU 5571  N   LEU B 332     5786   6695   8528   -569    694    153       N  
ATOM   5572  CA  LEU B 332      43.414 -23.767  31.362  1.00 50.83           C  
ANISOU 5572  CA  LEU B 332     5193   5994   8126   -429   1032     71       C  
ATOM   5573  C   LEU B 332      42.022 -24.379  31.445  1.00 57.54           C  
ANISOU 5573  C   LEU B 332     5774   6886   9201   -552   1066    239       C  
ATOM   5574  O   LEU B 332      41.089 -23.904  30.790  1.00 53.12           O  
ANISOU 5574  O   LEU B 332     4845   6377   8960   -592    944    506       O  
ATOM   5575  CB  LEU B 332      43.401 -22.316  31.856  1.00 55.89           C  
ANISOU 5575  CB  LEU B 332     5688   6488   9058   -204   1240     69       C  
ATOM   5576  CG  LEU B 332      42.799 -22.127  33.252  1.00 56.19           C  
ANISOU 5576  CG  LEU B 332     5680   6407   9261   -100   1655    -62       C  
ATOM   5577  CD1 LEU B 332      43.572 -22.923  34.288  1.00 52.23           C  
ANISOU 5577  CD1 LEU B 332     5569   5943   8334   -145   1790   -309       C  
ATOM   5578  CD2 LEU B 332      42.728 -20.653  33.641  1.00 56.68           C  
ANISOU 5578  CD2 LEU B 332     5578   6274   9685    100   1907   -119       C  
ATOM   5579  N   TRP B 333      41.891 -25.436  32.239  1.00 50.36           N  
ANISOU 5579  N   TRP B 333     5022   5961   8151   -627   1212    128       N  
ATOM   5580  CA  TRP B 333      40.613 -26.087  32.486  1.00 53.64           C  
ANISOU 5580  CA  TRP B 333     5199   6403   8778   -750   1287    272       C  
ATOM   5581  C   TRP B 333      40.259 -25.921  33.953  1.00 60.85           C  
ANISOU 5581  C   TRP B 333     6114   7232   9775   -624   1704    186       C  
ATOM   5582  O   TRP B 333      41.079 -26.215  34.830  1.00 58.37           O  
ANISOU 5582  O   TRP B 333     6123   6895   9162   -588   1851      1       O  
ATOM   5583  CB  TRP B 333      40.666 -27.572  32.127  1.00 51.18           C  
ANISOU 5583  CB  TRP B 333     5054   6139   8254   -999   1120    235       C  
ATOM   5584  CG  TRP B 333      40.703 -27.839  30.664  1.00 61.24           C  
ANISOU 5584  CG  TRP B 333     6285   7537   9444  -1215    756    291       C  
ATOM   5585  CD1 TRP B 333      41.814 -27.958  29.878  1.00 65.92           C  
ANISOU 5585  CD1 TRP B 333     7136   8164   9745  -1268    579    135       C  
ATOM   5586  CD2 TRP B 333      39.577 -28.033  29.801  1.00 66.34           C  
ANISOU 5586  CD2 TRP B 333     6609   8329  10268  -1455    530    515       C  
ATOM   5587  NE1 TRP B 333      41.448 -28.213  28.579  1.00 67.86           N  
ANISOU 5587  NE1 TRP B 333     7271   8585   9926  -1547    280    214       N  
ATOM   5588  CE2 TRP B 333      40.080 -28.263  28.505  1.00 70.16           C  
ANISOU 5588  CE2 TRP B 333     7207   8961  10488  -1681    214    461       C  
ATOM   5589  CE3 TRP B 333      38.191 -28.035  29.999  1.00 76.83           C  
ANISOU 5589  CE3 TRP B 333     7546   9694  11951  -1525    565    765       C  
ATOM   5590  CZ2 TRP B 333      39.249 -28.491  27.413  1.00 65.73           C  
ANISOU 5590  CZ2 TRP B 333     6408   8621   9947  -2012    -98    647       C  
ATOM   5591  CZ3 TRP B 333      37.366 -28.262  28.912  1.00 76.31           C  
ANISOU 5591  CZ3 TRP B 333     7206   9821  11968  -1824    234    987       C  
ATOM   5592  CH2 TRP B 333      37.897 -28.487  27.635  1.00 73.46           C  
ANISOU 5592  CH2 TRP B 333     6991   9641  11278  -2083   -110    926       C  
ATOM   5593  N   CYS B 334      39.043 -25.454  34.217  1.00 61.12           N  
ANISOU 5593  N   CYS B 334     5771   7238  10213   -581   1897    337       N  
ATOM   5594  CA  CYS B 334      38.572 -25.239  35.574  1.00 63.52           C  
ANISOU 5594  CA  CYS B 334     6043   7483  10610   -493   2359    230       C  
ATOM   5595  C   CYS B 334      37.204 -25.871  35.756  1.00 66.57           C  
ANISOU 5595  C   CYS B 334     6105   7905  11284   -615   2472    431       C  
ATOM   5596  O   CYS B 334      36.457 -26.082  34.797  1.00 66.12           O  
ANISOU 5596  O   CYS B 334     5738   7894  11490   -725   2204    686       O  
ATOM   5597  CB  CYS B 334      38.484 -23.751  35.918  1.00 63.38           C  
ANISOU 5597  CB  CYS B 334     5854   7323  10905   -266   2647    140       C  
ATOM   5598  SG  CYS B 334      40.064 -22.919  35.898  1.00 63.70           S  
ANISOU 5598  SG  CYS B 334     6263   7303  10636   -139   2572   -117       S  
ATOM   5599  N   LYS B 335      36.887 -26.161  37.017  1.00 68.35           N  
ANISOU 5599  N   LYS B 335     6399   8138  11434   -627   2870    327       N  
ATOM   5600  CA  LYS B 335      35.570 -26.655  37.399  1.00 73.62           C  
ANISOU 5600  CA  LYS B 335     6741   8832  12399   -726   3080    503       C  
ATOM   5601  C   LYS B 335      35.291 -26.203  38.824  1.00 77.80           C  
ANISOU 5601  C   LYS B 335     7291   9349  12919   -649   3663    313       C  
ATOM   5602  O   LYS B 335      36.051 -26.534  39.740  1.00 75.93           O  
ANISOU 5602  O   LYS B 335     7451   9196  12203   -708   3809    122       O  
ATOM   5603  CB  LYS B 335      35.486 -28.179  37.288  1.00 70.93           C  
ANISOU 5603  CB  LYS B 335     6535   8575  11839   -979   2863    620       C  
ATOM   5604  CG  LYS B 335      34.113 -28.739  37.632  1.00 81.49           C  
ANISOU 5604  CG  LYS B 335     7518   9944  13501  -1111   3053    831       C  
ATOM   5605  CD  LYS B 335      33.955 -30.189  37.184  1.00 87.33           C  
ANISOU 5605  CD  LYS B 335     8325  10716  14140  -1388   2752    973       C  
ATOM   5606  CE  LYS B 335      32.578 -30.728  37.565  1.00 91.00           C  
ANISOU 5606  CE  LYS B 335     8416  11212  14949  -1536   2947   1200       C  
ATOM   5607  NZ  LYS B 335      32.313 -32.071  36.981  1.00 93.43           N  
ANISOU 5607  NZ  LYS B 335     8734  11516  15250  -1836   2629   1336       N  
ATOM   5608  N   ASP B 336      34.218 -25.428  38.994  1.00 82.26           N  
ANISOU 5608  N   ASP B 336     7417   9819  14021   -535   3999    374       N  
ATOM   5609  CA  ASP B 336      33.755 -24.974  40.308  1.00 86.44           C  
ANISOU 5609  CA  ASP B 336     7937  10331  14574   -485   4599    154       C  
ATOM   5610  C   ASP B 336      34.812 -24.145  41.035  1.00 83.16           C  
ANISOU 5610  C   ASP B 336     7920   9890  13788   -398   4816   -242       C  
ATOM   5611  O   ASP B 336      34.996 -24.269  42.248  1.00 82.44           O  
ANISOU 5611  O   ASP B 336     8132   9923  13267   -497   5112   -473       O  
ATOM   5612  CB  ASP B 336      33.307 -26.156  41.167  1.00 89.30           C  
ANISOU 5612  CB  ASP B 336     8406  10872  14650   -707   4762    222       C  
ATOM   5613  CG  ASP B 336      32.159 -26.918  40.542  1.00 94.86           C  
ANISOU 5613  CG  ASP B 336     8715  11588  15741   -812   4558    586       C  
ATOM   5614  OD1 ASP B 336      31.175 -26.271  40.122  1.00 99.73           O  
ANISOU 5614  OD1 ASP B 336     8932  12091  16870   -676   4541    722       O  
ATOM   5615  OD2 ASP B 336      32.251 -28.159  40.455  1.00 96.27           O  
ANISOU 5615  OD2 ASP B 336     8992  11868  15719  -1042   4381    746       O  
ATOM   5616  N   GLY B 337      35.506 -23.288  40.290  1.00 78.91           N  
ANISOU 5616  N   GLY B 337     7377   9212  13393   -243   4635   -303       N  
ATOM   5617  CA  GLY B 337      36.470 -22.385  40.882  1.00 80.78           C  
ANISOU 5617  CA  GLY B 337     7962   9389  13340   -168   4790   -675       C  
ATOM   5618  C   GLY B 337      37.806 -22.999  41.227  1.00 77.24           C  
ANISOU 5618  C   GLY B 337     8025   9135  12187   -313   4604   -814       C  
ATOM   5619  O   GLY B 337      38.616 -22.343  41.895  1.00 76.23           O  
ANISOU 5619  O   GLY B 337     8187   9016  11762   -316   4789  -1137       O  
ATOM   5620  N   HIS B 338      38.065 -24.232  40.803  1.00 77.55           N  
ANISOU 5620  N   HIS B 338     8198   9312  11955   -444   4193   -572       N  
ATOM   5621  CA  HIS B 338      39.357 -24.869  40.999  1.00 75.60           C  
ANISOU 5621  CA  HIS B 338     8402   9200  11122   -552   3912   -620       C  
ATOM   5622  C   HIS B 338      39.950 -25.240  39.647  1.00 61.72           C  
ANISOU 5622  C   HIS B 338     6662   7380   9409   -508   3369   -445       C  
ATOM   5623  O   HIS B 338      39.226 -25.437  38.667  1.00 62.47           O  
ANISOU 5623  O   HIS B 338     6460   7415   9862   -496   3171   -233       O  
ATOM   5624  CB  HIS B 338      39.231 -26.109  41.890  1.00 80.83           C  
ANISOU 5624  CB  HIS B 338     9236  10057  11417   -774   3990   -503       C  
ATOM   5625  CG  HIS B 338      38.688 -25.814  43.254  1.00 92.65           C  
ANISOU 5625  CG  HIS B 338    10754  11687  12762   -879   4542   -678       C  
ATOM   5626  ND1 HIS B 338      37.343 -25.877  43.550  1.00101.18           N  
ANISOU 5626  ND1 HIS B 338    11501  12756  14186   -902   4908   -610       N  
ATOM   5627  CD2 HIS B 338      39.306 -25.431  44.396  1.00 96.86           C  
ANISOU 5627  CD2 HIS B 338    11596  12390  12815  -1000   4808   -936       C  
ATOM   5628  CE1 HIS B 338      37.158 -25.558  44.819  1.00103.70           C  
ANISOU 5628  CE1 HIS B 338    11964  13223  14215  -1004   5302   -825       C  
ATOM   5629  NE2 HIS B 338      38.334 -25.282  45.355  1.00102.99           N  
ANISOU 5629  NE2 HIS B 338    12268  13259  13605  -1085   5247  -1030       N  
ATOM   5630  N   VAL B 339      41.279 -25.302  39.594  1.00 57.35           N  
ANISOU 5630  N   VAL B 339     6446   6860   8482   -511   3137   -540       N  
ATOM   5631  CA  VAL B 339      41.959 -25.744  38.383  1.00 53.76           C  
ANISOU 5631  CA  VAL B 339     6053   6364   8012   -497   2681   -423       C  
ATOM   5632  C   VAL B 339      41.759 -27.243  38.220  1.00 60.96           C  
ANISOU 5632  C   VAL B 339     7006   7315   8840   -663   2505   -234       C  
ATOM   5633  O   VAL B 339      41.886 -28.009  39.183  1.00 60.42           O  
ANISOU 5633  O   VAL B 339     7104   7326   8527   -777   2626   -194       O  
ATOM   5634  CB  VAL B 339      43.454 -25.392  38.441  1.00 52.62           C  
ANISOU 5634  CB  VAL B 339     6225   6228   7540   -448   2530   -575       C  
ATOM   5635  CG1 VAL B 339      44.184 -25.917  37.203  1.00 50.88           C  
ANISOU 5635  CG1 VAL B 339     6070   5966   7298   -447   2122   -482       C  
ATOM   5636  CG2 VAL B 339      43.652 -23.892  38.563  1.00 55.98           C  
ANISOU 5636  CG2 VAL B 339     6606   6573   8092   -307   2705   -780       C  
ATOM   5637  N   GLU B 340      41.420 -27.668  37.004  1.00 59.47           N  
ANISOU 5637  N   GLU B 340     6659   7078   8859   -708   2223   -106       N  
ATOM   5638  CA  GLU B 340      41.517 -29.082  36.653  1.00 62.00           C  
ANISOU 5638  CA  GLU B 340     7076   7376   9106   -877   2022     -2       C  
ATOM   5639  C   GLU B 340      42.889 -29.374  36.052  1.00 56.59           C  
ANISOU 5639  C   GLU B 340     6659   6636   8206   -857   1767    -97       C  
ATOM   5640  O   GLU B 340      43.626 -30.225  36.560  1.00 51.40           O  
ANISOU 5640  O   GLU B 340     6222   5936   7372   -902   1753    -80       O  
ATOM   5641  CB  GLU B 340      40.390 -29.483  35.694  1.00 67.25           C  
ANISOU 5641  CB  GLU B 340     7440   8037  10074  -1012   1873    143       C  
ATOM   5642  CG  GLU B 340      38.998 -29.315  36.295  1.00 84.58           C  
ANISOU 5642  CG  GLU B 340     9314  10271  12550  -1036   2138    278       C  
ATOM   5643  CD  GLU B 340      37.915 -30.001  35.485  1.00 95.18           C  
ANISOU 5643  CD  GLU B 340    10369  11628  14168  -1235   1957    465       C  
ATOM   5644  OE1 GLU B 340      37.592 -31.170  35.793  1.00 99.94           O  
ANISOU 5644  OE1 GLU B 340    11012  12202  14758  -1414   1977    537       O  
ATOM   5645  OE2 GLU B 340      37.387 -29.372  34.541  1.00100.02           O  
ANISOU 5645  OE2 GLU B 340    10700  12284  15019  -1236   1779    567       O  
ATOM   5646  N   THR B 341      43.258 -28.648  34.995  1.00 47.84           N  
ANISOU 5646  N   THR B 341     5510   5528   7139   -788   1577   -165       N  
ATOM   5647  CA  THR B 341      44.632 -28.698  34.505  1.00 52.11           C  
ANISOU 5647  CA  THR B 341     6291   6028   7479   -741   1402   -279       C  
ATOM   5648  C   THR B 341      45.016 -27.358  33.886  1.00 51.96           C  
ANISOU 5648  C   THR B 341     6214   6046   7483   -607   1325   -341       C  
ATOM   5649  O   THR B 341      44.170 -26.501  33.609  1.00 50.86           O  
ANISOU 5649  O   THR B 341     5820   5938   7567   -565   1356   -263       O  
ATOM   5650  CB  THR B 341      44.842 -29.837  33.503  1.00 53.34           C  
ANISOU 5650  CB  THR B 341     6508   6117   7641   -904   1200   -300       C  
ATOM   5651  OG1 THR B 341      46.229 -29.897  33.152  1.00 52.83           O  
ANISOU 5651  OG1 THR B 341     6662   5993   7419   -838   1105   -423       O  
ATOM   5652  CG2 THR B 341      44.001 -29.622  32.250  1.00 54.24           C  
ANISOU 5652  CG2 THR B 341     6401   6321   7887  -1040   1022   -261       C  
ATOM   5653  N   PHE B 342      46.327 -27.194  33.683  1.00 46.64           N  
ANISOU 5653  N   PHE B 342     5752   5348   6623   -537   1227   -447       N  
ATOM   5654  CA  PHE B 342      46.909 -25.963  33.154  1.00 47.75           C  
ANISOU 5654  CA  PHE B 342     5871   5505   6765   -418   1153   -498       C  
ATOM   5655  C   PHE B 342      48.225 -26.398  32.520  1.00 48.71           C  
ANISOU 5655  C   PHE B 342     6198   5606   6703   -431    990   -584       C  
ATOM   5656  O   PHE B 342      49.170 -26.708  33.246  1.00 48.68           O  
ANISOU 5656  O   PHE B 342     6382   5556   6559   -380   1036   -637       O  
ATOM   5657  CB  PHE B 342      47.133 -24.940  34.259  1.00 44.10           C  
ANISOU 5657  CB  PHE B 342     5449   5022   6287   -280   1364   -581       C  
ATOM   5658  CG  PHE B 342      47.714 -23.628  33.790  1.00 46.04           C  
ANISOU 5658  CG  PHE B 342     5660   5234   6600   -161   1311   -632       C  
ATOM   5659  CD1 PHE B 342      47.002 -22.800  32.936  1.00 49.76           C  
ANISOU 5659  CD1 PHE B 342     5860   5687   7358   -124   1249   -507       C  
ATOM   5660  CD2 PHE B 342      48.946 -23.192  34.264  1.00 50.92           C  
ANISOU 5660  CD2 PHE B 342     6486   5834   7027   -100   1317   -764       C  
ATOM   5661  CE1 PHE B 342      47.520 -21.569  32.537  1.00 53.03           C  
ANISOU 5661  CE1 PHE B 342     6221   6039   7890    -16   1210   -509       C  
ATOM   5662  CE2 PHE B 342      49.478 -21.976  33.864  1.00 52.19           C  
ANISOU 5662  CE2 PHE B 342     6607   5939   7282     -4   1280   -808       C  
ATOM   5663  CZ  PHE B 342      48.766 -21.160  33.000  1.00 51.53           C  
ANISOU 5663  CZ  PHE B 342     6262   5810   7508     44   1236   -680       C  
ATOM   5664  N   TYR B 343      48.272 -26.452  31.188  1.00 43.78           N  
ANISOU 5664  N   TYR B 343     5521   5035   6080   -524    808   -581       N  
ATOM   5665  CA  TYR B 343      49.453 -27.020  30.553  1.00 44.80           C  
ANISOU 5665  CA  TYR B 343     5833   5131   6059   -561    723   -702       C  
ATOM   5666  C   TYR B 343      49.857 -26.253  29.302  1.00 44.64           C  
ANISOU 5666  C   TYR B 343     5769   5225   5969   -595    572   -708       C  
ATOM   5667  O   TYR B 343      48.999 -25.751  28.564  1.00 46.96           O  
ANISOU 5667  O   TYR B 343     5873   5648   6321   -692    456   -582       O  
ATOM   5668  CB  TYR B 343      49.243 -28.506  30.201  1.00 44.85           C  
ANISOU 5668  CB  TYR B 343     5902   5064   6076   -740    720   -771       C  
ATOM   5669  CG  TYR B 343      48.169 -28.809  29.182  1.00 45.84           C  
ANISOU 5669  CG  TYR B 343     5886   5302   6228   -976    604   -752       C  
ATOM   5670  CD1 TYR B 343      48.469 -28.867  27.829  1.00 47.99           C  
ANISOU 5670  CD1 TYR B 343     6189   5689   6357  -1154    470   -859       C  
ATOM   5671  CD2 TYR B 343      46.864 -29.077  29.575  1.00 46.39           C  
ANISOU 5671  CD2 TYR B 343     5788   5393   6446  -1060    626   -625       C  
ATOM   5672  CE1 TYR B 343      47.494 -29.163  26.891  1.00 55.07           C  
ANISOU 5672  CE1 TYR B 343     6962   6746   7215  -1440    325   -833       C  
ATOM   5673  CE2 TYR B 343      45.885 -29.382  28.644  1.00 51.51           C  
ANISOU 5673  CE2 TYR B 343     6282   6169   7120  -1316    479   -580       C  
ATOM   5674  CZ  TYR B 343      46.205 -29.419  27.304  1.00 55.09           C  
ANISOU 5674  CZ  TYR B 343     6780   6764   7390  -1520    310   -681       C  
ATOM   5675  OH  TYR B 343      45.231 -29.711  26.380  1.00 55.76           O  
ANISOU 5675  OH  TYR B 343     6714   7033   7440  -1839    126   -624       O  
ATOM   5676  N   PRO B 344      51.156 -26.174  29.026  1.00 49.01           N  
ANISOU 5676  N   PRO B 344     6468   5747   6405   -536    561   -812       N  
ATOM   5677  CA  PRO B 344      51.614 -25.506  27.809  1.00 46.68           C  
ANISOU 5677  CA  PRO B 344     6143   5586   6006   -598    436   -807       C  
ATOM   5678  C   PRO B 344      51.396 -26.397  26.602  1.00 49.40           C  
ANISOU 5678  C   PRO B 344     6518   6038   6214   -864    366   -910       C  
ATOM   5679  O   PRO B 344      51.380 -27.627  26.699  1.00 47.29           O  
ANISOU 5679  O   PRO B 344     6353   5658   5958   -958    454  -1062       O  
ATOM   5680  CB  PRO B 344      53.107 -25.282  28.077  1.00 48.88           C  
ANISOU 5680  CB  PRO B 344     6565   5777   6228   -453    491   -899       C  
ATOM   5681  CG  PRO B 344      53.489 -26.449  28.940  1.00 48.26           C  
ANISOU 5681  CG  PRO B 344     6611   5530   6195   -412    608   -983       C  
ATOM   5682  CD  PRO B 344      52.272 -26.779  29.780  1.00 48.21           C  
ANISOU 5682  CD  PRO B 344     6539   5500   6278   -433    655   -898       C  
ATOM   5683  N   LYS B 345      51.203 -25.761  25.454  1.00 44.36           N  
ANISOU 5683  N   LYS B 345     5785   5623   5448  -1018    210   -819       N  
ATOM   5684  CA  LYS B 345      50.887 -26.489  24.239  1.00 55.15           C  
ANISOU 5684  CA  LYS B 345     7183   7173   6601  -1355    125   -925       C  
ATOM   5685  C   LYS B 345      52.091 -26.537  23.311  1.00 64.02           C  
ANISOU 5685  C   LYS B 345     8462   8379   7486  -1448    176  -1114       C  
ATOM   5686  O   LYS B 345      52.956 -25.653  23.333  1.00 57.37           O  
ANISOU 5686  O   LYS B 345     7620   7539   6640  -1280    183  -1039       O  
ATOM   5687  CB  LYS B 345      49.683 -25.877  23.513  1.00 55.39           C  
ANISOU 5687  CB  LYS B 345     6972   7476   6599  -1560   -120   -644       C  
ATOM   5688  CG  LYS B 345      48.348 -26.275  24.144  1.00 62.33           C  
ANISOU 5688  CG  LYS B 345     7687   8298   7699  -1584   -142   -525       C  
ATOM   5689  CD  LYS B 345      47.248 -26.422  23.109  1.00 74.80           C  
ANISOU 5689  CD  LYS B 345     9084  10174   9165  -1954   -394   -361       C  
ATOM   5690  CE  LYS B 345      46.743 -25.069  22.637  1.00 78.64           C  
ANISOU 5690  CE  LYS B 345     9266  10862   9751  -1939   -624     67       C  
ATOM   5691  NZ  LYS B 345      45.563 -25.212  21.730  1.00 78.32           N  
ANISOU 5691  NZ  LYS B 345     8984  11138   9636  -2317   -920    323       N  
ATOM   5692  N   LEU B 346      52.137 -27.609  22.517  1.00 73.45           N  
ANISOU 5692  N   LEU B 346     9785   9622   8500  -1734    246  -1388       N  
ATOM   5693  CA  LEU B 346      53.143 -27.782  21.479  1.00 75.26           C  
ANISOU 5693  CA  LEU B 346    10160   9962   8472  -1900    351  -1628       C  
ATOM   5694  C   LEU B 346      53.252 -26.514  20.643  1.00 70.09           C  
ANISOU 5694  C   LEU B 346     9402   9644   7584  -1988    156  -1374       C  
ATOM   5695  O   LEU B 346      52.270 -26.074  20.039  1.00 72.65           O  
ANISOU 5695  O   LEU B 346     9578  10260   7763  -2222    -94  -1132       O  
ATOM   5696  CB  LEU B 346      52.760 -28.989  20.611  1.00 79.00           C  
ANISOU 5696  CB  LEU B 346    10758  10509   8749  -2304    430  -1962       C  
ATOM   5697  CG  LEU B 346      53.682 -29.564  19.528  1.00 85.08           C  
ANISOU 5697  CG  LEU B 346    11721  11349   9258  -2559    657  -2366       C  
ATOM   5698  CD1 LEU B 346      53.497 -31.076  19.443  1.00 85.36           C  
ANISOU 5698  CD1 LEU B 346    11898  11140   9395  -2764    890  -2790       C  
ATOM   5699  CD2 LEU B 346      53.407 -28.935  18.166  1.00 85.53           C  
ANISOU 5699  CD2 LEU B 346    11763  11920   8813  -2968    463  -2294       C  
ATOM   5700  N   GLN B 347      54.436 -25.904  20.647  1.00 69.68           N  
ANISOU 5700  N   GLN B 347     9393   9545   7538  -1801    252  -1374       N  
ATOM   5701  CA  GLN B 347      54.667 -24.671  19.892  1.00 73.80           C  
ANISOU 5701  CA  GLN B 347     9810  10350   7881  -1869     86  -1102       C  
ATOM   5702  C   GLN B 347      54.405 -24.880  18.407  1.00 77.30           C  
ANISOU 5702  C   GLN B 347    10295  11213   7863  -2348     -4  -1155       C  
ATOM   5703  O   GLN B 347      53.840 -24.014  17.743  1.00 84.37           O  
ANISOU 5703  O   GLN B 347    11027  12432   8597  -2529   -277   -791       O  
ATOM   5704  CB  GLN B 347      56.101 -24.158  20.091  1.00 75.74           C  
ANISOU 5704  CB  GLN B 347    10112  10462   8203  -1631    242  -1150       C  
ATOM   5705  CG  GLN B 347      56.366 -23.453  21.420  1.00 74.62           C  
ANISOU 5705  CG  GLN B 347     9890  10031   8430  -1229    235   -986       C  
ATOM   5706  CD  GLN B 347      57.854 -23.202  21.656  1.00 70.27           C  
ANISOU 5706  CD  GLN B 347     9402   9338   7958  -1037    391  -1078       C  
ATOM   5707  OE1 GLN B 347      58.480 -23.868  22.480  1.00 55.14           O  
ANISOU 5707  OE1 GLN B 347     7562   7163   6226   -854    548  -1247       O  
ATOM   5708  NE2 GLN B 347      58.425 -22.245  20.923  1.00 71.22           N  
ANISOU 5708  NE2 GLN B 347     9463   9638   7958  -1095    332   -923       N  
TER    5709      GLN B 347                                                      
HETATM 5710  N1  U5P A 401      92.364 -20.489 -25.572  1.00 38.09           N  
HETATM 5711  C2  U5P A 401      90.987 -20.500 -25.695  1.00 34.32           C  
HETATM 5712  N3  U5P A 401      90.304 -19.900 -24.664  1.00 35.93           N  
HETATM 5713  C4  U5P A 401      90.850 -19.317 -23.537  1.00 39.74           C  
HETATM 5714  C5  U5P A 401      92.283 -19.352 -23.479  1.00 46.07           C  
HETATM 5715  C6  U5P A 401      92.976 -19.931 -24.473  1.00 49.56           C  
HETATM 5716  O2  U5P A 401      90.419 -21.003 -26.655  1.00 38.61           O  
HETATM 5717  O4  U5P A 401      90.106 -18.825 -22.687  1.00 42.84           O  
HETATM 5718  C1' U5P A 401      93.133 -21.158 -26.660  1.00 37.39           C  
HETATM 5719  C2' U5P A 401      93.326 -20.273 -27.892  1.00 40.17           C  
HETATM 5720  O2' U5P A 401      93.381 -21.118 -29.027  1.00 42.07           O  
HETATM 5721  C3' U5P A 401      94.704 -19.693 -27.630  1.00 49.71           C  
HETATM 5722  C4' U5P A 401      95.434 -20.867 -26.996  1.00 51.87           C  
HETATM 5723  O3' U5P A 401      95.335 -19.196 -28.797  1.00 43.54           O  
HETATM 5724  O4' U5P A 401      94.417 -21.499 -26.174  1.00 40.97           O  
HETATM 5725  C5' U5P A 401      96.627 -20.505 -26.152  1.00 56.16           C  
HETATM 5726  O5' U5P A 401      96.239 -19.704 -25.047  1.00 60.76           O  
HETATM 5727  P   U5P A 401      97.322 -18.995 -24.117  1.00 73.98           P  
HETATM 5728  O1P U5P A 401      98.112 -18.107 -25.060  1.00 72.06           O  
HETATM 5729  O2P U5P A 401      96.532 -18.296 -23.025  1.00 74.74           O  
HETATM 5730  O3P U5P A 401      98.161 -20.135 -23.567  1.00 80.84           O  
HETATM 5731  C   TRS A 402      66.626 -37.992 -15.210  1.00 70.29           C  
HETATM 5732  C1  TRS A 402      67.005 -38.226 -16.670  1.00 75.13           C  
HETATM 5733  C2  TRS A 402      65.471 -38.918 -14.831  1.00 66.19           C  
HETATM 5734  C3  TRS A 402      66.186 -36.553 -14.977  1.00 61.06           C  
HETATM 5735  N   TRS A 402      67.814 -38.249 -14.371  1.00 65.85           N  
HETATM 5736  O1  TRS A 402      68.352 -37.859 -16.893  1.00 77.44           O  
HETATM 5737  O2  TRS A 402      65.920 -39.857 -13.888  1.00 50.42           O  
HETATM 5738  O3  TRS A 402      66.933 -36.024 -13.897  1.00 51.18           O  
HETATM 5739  C1  EDO A 403      58.719 -32.240   0.142  1.00 68.58           C  
HETATM 5740  O1  EDO A 403      57.667 -32.335   1.118  1.00 50.69           O  
HETATM 5741  C2  EDO A 403      58.348 -31.308  -1.011  1.00 75.29           C  
HETATM 5742  O2  EDO A 403      57.966 -30.013  -0.524  1.00 62.50           O  
HETATM 5743  C   ACT A 404     100.053 -15.416 -30.087  1.00 87.88           C  
HETATM 5744  O   ACT A 404     100.132 -15.181 -31.286  1.00 87.75           O  
HETATM 5745  OXT ACT A 404      99.009 -15.868 -29.487  1.00 89.58           O  
HETATM 5746  CH3 ACT A 404     101.248 -15.188 -29.132  1.00 78.66           C  
HETATM 5747  C1  EDO A 405      79.162 -29.655 -29.307  1.00 81.16           C  
HETATM 5748  O1  EDO A 405      77.976 -30.005 -30.031  1.00 74.74           O  
HETATM 5749  C2  EDO A 405      79.327 -30.568 -28.094  1.00 81.91           C  
HETATM 5750  O2  EDO A 405      79.329 -31.939 -28.514  1.00 81.44           O  
HETATM 5751  C1  EDO A 406      71.788 -15.190 -11.339  1.00 92.43           C  
HETATM 5752  O1  EDO A 406      71.930 -13.769 -11.460  1.00 91.88           O  
HETATM 5753  C2  EDO A 406      71.834 -15.837 -12.721  1.00 92.96           C  
HETATM 5754  O2  EDO A 406      73.154 -15.750 -13.278  1.00 89.31           O  
HETATM 5755  C1  EDO A 407     100.435  -4.967 -35.242  1.00 63.48           C  
HETATM 5756  O1  EDO A 407     101.720  -5.245 -35.810  1.00 76.73           O  
HETATM 5757  C2  EDO A 407      99.584  -4.335 -36.332  1.00 62.61           C  
HETATM 5758  O2  EDO A 407      99.033  -5.350 -37.166  1.00 52.63           O  
HETATM 5759  C1  EDO A 408      68.458 -24.763 -22.706  1.00 71.86           C  
HETATM 5760  O1  EDO A 408      69.792 -24.662 -23.246  1.00 59.17           O  
HETATM 5761  C2  EDO A 408      68.484 -25.014 -21.202  1.00 74.96           C  
HETATM 5762  O2  EDO A 408      67.694 -26.167 -20.845  1.00 78.97           O  
HETATM 5763  C1  EDO A 409      71.294  -7.440 -19.033  1.00 74.82           C  
HETATM 5764  O1  EDO A 409      71.778  -7.278 -20.372  1.00 76.49           O  
HETATM 5765  C2  EDO A 409      72.351  -8.153 -18.195  1.00 73.76           C  
HETATM 5766  O2  EDO A 409      71.781  -8.684 -16.988  1.00 75.00           O  
HETATM 5767  S   SO4 A 410      93.423  -7.856 -44.224  1.00157.95           S  
HETATM 5768  O1  SO4 A 410      92.975  -6.477 -44.400  1.00159.36           O  
HETATM 5769  O2  SO4 A 410      93.913  -8.376 -45.499  1.00157.37           O  
HETATM 5770  O3  SO4 A 410      92.305  -8.672 -43.763  1.00158.32           O  
HETATM 5771  O4  SO4 A 410      94.496  -7.898 -43.234  1.00158.46           O  
HETATM 5772  N1  U5P B 401      48.928 -32.608  25.951  1.00 48.53           N  
HETATM 5773  C2  U5P B 401      50.129 -31.931  26.061  1.00 42.42           C  
HETATM 5774  N3  U5P B 401      50.414 -31.077  25.024  1.00 40.49           N  
HETATM 5775  C4  U5P B 401      49.639 -30.847  23.904  1.00 50.37           C  
HETATM 5776  C5  U5P B 401      48.411 -31.590  23.859  1.00 51.81           C  
HETATM 5777  C6  U5P B 401      48.107 -32.430  24.862  1.00 52.40           C  
HETATM 5778  O2  U5P B 401      50.878 -32.073  27.016  1.00 41.48           O  
HETATM 5779  O4  U5P B 401      50.031 -30.048  23.054  1.00 46.13           O  
HETATM 5780  C1' U5P B 401      48.597 -33.553  27.046  1.00 54.52           C  
HETATM 5781  C2' U5P B 401      47.950 -32.864  28.254  1.00 54.07           C  
HETATM 5782  O2' U5P B 401      48.313 -33.591  29.418  1.00 50.54           O  
HETATM 5783  C3' U5P B 401      46.476 -33.079  27.956  1.00 63.85           C  
HETATM 5784  C4' U5P B 401      46.467 -34.476  27.356  1.00 63.56           C  
HETATM 5785  O3' U5P B 401      45.634 -32.945  29.088  1.00 61.01           O  
HETATM 5786  O4' U5P B 401      47.678 -34.511  26.556  1.00 56.00           O  
HETATM 5787  C5' U5P B 401      45.274 -34.812  26.503  1.00 63.12           C  
HETATM 5788  O5' U5P B 401      45.231 -33.999  25.342  1.00 70.84           O  
HETATM 5789  P   U5P B 401      43.910 -33.913  24.454  1.00 78.72           P  
HETATM 5790  O1P U5P B 401      44.280 -33.007  23.296  1.00 80.62           O  
HETATM 5791  O2P U5P B 401      43.627 -35.332  23.994  1.00 90.41           O  
HETATM 5792  O3P U5P B 401      42.880 -33.285  25.373  1.00 77.07           O  
HETATM 5793  C   TRS B 402      80.817 -33.779  15.938  1.00 81.01           C  
HETATM 5794  C1  TRS B 402      81.958 -34.052  14.955  1.00 72.28           C  
HETATM 5795  C2  TRS B 402      79.788 -34.909  15.900  1.00 87.78           C  
HETATM 5796  C3  TRS B 402      80.141 -32.439  15.640  1.00 65.50           C  
HETATM 5797  N   TRS B 402      81.391 -33.724  17.288  1.00 81.60           N  
HETATM 5798  O1  TRS B 402      81.799 -35.325  14.361  1.00 50.26           O  
HETATM 5799  O2  TRS B 402      79.130 -34.963  14.650  1.00 83.18           O  
HETATM 5800  O3  TRS B 402      79.223 -32.569  14.569  1.00 54.03           O  
HETATM 5801  C1  EDO B 403      72.175   4.778  28.050  1.00 36.28           C  
HETATM 5802  O1  EDO B 403      71.955   5.430  26.815  1.00 39.42           O  
HETATM 5803  C2  EDO B 403      71.010   3.883  28.421  1.00 48.88           C  
HETATM 5804  O2  EDO B 403      71.336   3.403  29.734  1.00 64.70           O  
HETATM 5805  C1  EDO B 404      63.583  -9.353  32.061  1.00 63.75           C  
HETATM 5806  O1  EDO B 404      63.905  -9.221  30.673  1.00 56.54           O  
HETATM 5807  C2  EDO B 404      62.156  -9.876  32.221  1.00 62.17           C  
HETATM 5808  O2  EDO B 404      61.227  -9.135  31.417  1.00 50.11           O  
HETATM 5809  C   ACT B 405      33.893 -23.071  36.492  1.00 86.99           C  
HETATM 5810  O   ACT B 405      34.068 -23.106  35.282  1.00 89.28           O  
HETATM 5811  OXT ACT B 405      34.808 -22.839  37.366  1.00 76.03           O  
HETATM 5812  CH3 ACT B 405      32.501 -23.311  37.110  1.00 87.86           C  
HETATM 5813  C1  EDO B 406      52.627 -10.282  27.849  1.00 86.67           C  
HETATM 5814  O1  EDO B 406      53.847 -10.282  28.611  1.00 87.64           O  
HETATM 5815  C2  EDO B 406      51.794 -11.525  28.167  1.00 85.98           C  
HETATM 5816  O2  EDO B 406      51.337 -12.184  26.976  1.00 75.59           O  
HETATM 5817  C   ACT B 407      73.308  -7.373  31.910  1.00 95.07           C  
HETATM 5818  O   ACT B 407      74.400  -7.410  31.229  1.00 89.97           O  
HETATM 5819  OXT ACT B 407      72.178  -7.466  31.447  1.00 89.45           O  
HETATM 5820  CH3 ACT B 407      73.547  -7.199  33.424  1.00 95.03           C  
HETATM 5821  C   ACT B 408      78.458  -2.544  24.839  1.00 79.70           C  
HETATM 5822  O   ACT B 408      77.919  -1.452  24.735  1.00 81.11           O  
HETATM 5823  OXT ACT B 408      78.519  -3.245  25.917  1.00 74.30           O  
HETATM 5824  CH3 ACT B 408      79.140  -3.211  23.636  1.00 70.10           C  
HETATM 5825  C   FMT B 409      71.435 -35.241  15.443  1.00 94.21           C  
HETATM 5826  O1  FMT B 409      70.642 -35.051  16.365  1.00 94.77           O  
HETATM 5827  O2  FMT B 409      71.187 -35.928  14.452  1.00 93.12           O  
HETATM 5828  C   FMT B 410      77.038 -34.929  19.126  1.00 81.00           C  
HETATM 5829  O1  FMT B 410      78.036 -35.311  18.509  1.00 83.35           O  
HETATM 5830  O2  FMT B 410      75.874 -35.081  18.741  1.00 74.95           O  
HETATM 5831  C1  EDO B 411      80.077 -39.244  16.259  1.00 88.29           C  
HETATM 5832  O1  EDO B 411      81.177 -38.959  17.131  1.00 92.09           O  
HETATM 5833  C2  EDO B 411      78.906 -38.320  16.576  1.00 84.15           C  
HETATM 5834  O2  EDO B 411      78.195 -38.018  15.367  1.00 72.82           O  
HETATM 5835  O   HOH A 501      90.353 -36.512 -36.128  1.00 47.62           O  
HETATM 5836  O   HOH A 502      67.360 -33.768 -17.049  1.00 40.96           O  
HETATM 5837  O   HOH A 503      97.691 -22.927 -30.103  1.00 65.17           O  
HETATM 5838  O   HOH A 504      88.535 -16.728 -19.375  1.00 59.80           O  
HETATM 5839  O   HOH A 505      71.547  -0.278 -35.120  1.00 54.98           O  
HETATM 5840  O   HOH A 506      64.465 -17.098 -26.094  1.00 38.61           O  
HETATM 5841  O   HOH A 507      78.791 -29.097 -25.000  1.00 53.18           O  
HETATM 5842  O   HOH A 508      69.549 -10.232  -8.900  1.00 47.20           O  
HETATM 5843  O   HOH A 509      65.515 -42.523 -14.240  1.00 46.97           O  
HETATM 5844  O   HOH A 510      75.590 -24.380 -23.677  1.00 39.55           O  
HETATM 5845  O   HOH A 511      71.896 -12.159  -9.585  1.00 77.52           O  
HETATM 5846  O   HOH A 512      90.865 -10.230 -47.567  1.00 59.88           O  
HETATM 5847  O   HOH A 513      91.536  -4.804 -43.262  1.00 51.50           O  
HETATM 5848  O   HOH A 514      78.002 -24.504 -52.244  1.00 71.87           O  
HETATM 5849  O   HOH A 515      89.119  -5.550 -41.951  1.00 52.69           O  
HETATM 5850  O   HOH A 516      70.322 -26.465  -9.504  1.00 42.77           O  
HETATM 5851  O   HOH A 517      62.831 -26.017 -36.991  1.00 59.66           O  
HETATM 5852  O   HOH A 518      67.305  -8.269 -30.875  1.00 50.30           O  
HETATM 5853  O   HOH A 519      74.914 -16.113 -46.385  1.00 46.95           O  
HETATM 5854  O   HOH A 520      69.190 -39.611  -0.727  1.00 38.00           O  
HETATM 5855  O   HOH A 521      59.453 -20.756  -9.391  1.00 38.73           O  
HETATM 5856  O   HOH A 522      83.078 -27.074 -20.487  1.00 35.00           O  
HETATM 5857  O   HOH A 523      85.204 -31.318 -15.085  1.00 44.29           O  
HETATM 5858  O   HOH A 524      50.786 -15.327 -26.136  1.00 61.81           O  
HETATM 5859  O   HOH A 525      93.224  -1.708 -32.505  1.00 48.95           O  
HETATM 5860  O   HOH A 526      73.543 -24.354 -16.956  1.00 41.13           O  
HETATM 5861  O   HOH A 527      51.884 -21.638  -8.633  1.00 56.49           O  
HETATM 5862  O   HOH A 528      55.297 -33.157  -2.044  1.00 48.54           O  
HETATM 5863  O   HOH A 529      57.133 -14.716   1.594  1.00 73.25           O  
HETATM 5864  O   HOH A 530      85.089 -24.484 -46.545  1.00 44.97           O  
HETATM 5865  O   HOH A 531      56.633 -42.360   1.410  1.00 40.06           O  
HETATM 5866  O   HOH A 532      73.775 -31.447 -11.706  1.00 44.22           O  
HETATM 5867  O   HOH A 533      75.178 -15.959 -14.912  1.00 67.47           O  
HETATM 5868  O   HOH A 534      55.191 -29.245  -2.262  1.00 49.63           O  
HETATM 5869  O   HOH A 535      71.019 -28.150 -30.097  1.00 61.79           O  
HETATM 5870  O   HOH A 536      66.700 -12.705 -33.324  1.00 50.24           O  
HETATM 5871  O   HOH A 537      56.120 -27.662 -40.155  1.00 56.08           O  
HETATM 5872  O   HOH A 538      82.718  -6.623 -20.168  1.00 67.76           O  
HETATM 5873  O   HOH A 539      80.314 -23.426 -19.501  1.00 47.04           O  
HETATM 5874  O   HOH A 540      93.553 -19.130 -31.370  1.00 41.55           O  
HETATM 5875  O   HOH A 541      55.364 -57.943 -12.335  1.00 46.81           O  
HETATM 5876  O   HOH A 542      97.740 -21.805 -37.608  1.00 46.77           O  
HETATM 5877  O   HOH A 543      71.311 -49.124  -0.960  1.00 44.67           O  
HETATM 5878  O   HOH A 544      81.742 -10.225 -46.324  1.00 69.36           O  
HETATM 5879  O   HOH A 545      95.567  -4.263 -42.872  1.00 64.23           O  
HETATM 5880  O   HOH A 546      71.923 -28.224 -36.074  1.00 64.92           O  
HETATM 5881  O   HOH A 547      55.429 -30.265 -15.453  1.00 37.52           O  
HETATM 5882  O   HOH A 548      96.674 -32.943 -24.296  1.00 37.86           O  
HETATM 5883  O   HOH A 549      59.332 -21.427 -37.962  1.00 67.01           O  
HETATM 5884  O   HOH A 550      58.963  -7.705 -31.926  1.00 55.16           O  
HETATM 5885  O   HOH A 551      65.943  -3.443  -5.717  1.00 73.17           O  
HETATM 5886  O   HOH A 552      55.412 -25.619 -13.670  1.00 67.09           O  
HETATM 5887  O   HOH A 553      55.251 -20.296 -27.387  1.00 45.68           O  
HETATM 5888  O   HOH A 554      81.766 -33.373 -18.193  1.00 62.34           O  
HETATM 5889  O   HOH A 555      75.217 -19.398 -18.613  1.00 37.54           O  
HETATM 5890  O   HOH A 556      98.873 -33.015 -28.402  1.00 37.14           O  
HETATM 5891  O   HOH A 557      64.054 -25.756 -19.649  1.00 32.40           O  
HETATM 5892  O   HOH A 558      75.185 -10.556 -18.557  1.00 50.84           O  
HETATM 5893  O   HOH A 559      97.116 -17.153 -38.047  1.00 44.18           O  
HETATM 5894  O   HOH A 560      89.523  -1.143 -29.130  1.00 50.56           O  
HETATM 5895  O   HOH A 561      62.728 -34.474 -23.122  1.00 56.45           O  
HETATM 5896  O   HOH A 562      95.002  -6.745 -32.015  1.00 42.39           O  
HETATM 5897  O   HOH A 563      72.979 -10.505 -37.244  1.00 58.10           O  
HETATM 5898  O   HOH A 564      67.707  -8.486  -9.079  1.00 53.56           O  
HETATM 5899  O   HOH A 565      83.395  -9.551 -21.117  1.00 52.54           O  
HETATM 5900  O   HOH A 566      52.952 -47.749  -9.380  1.00 46.86           O  
HETATM 5901  O   HOH A 567      87.396  -3.211 -39.902  1.00 46.17           O  
HETATM 5902  O   HOH A 568      98.621 -27.195 -34.446  1.00 42.48           O  
HETATM 5903  O   HOH A 569      91.259 -16.324 -44.037  1.00 47.36           O  
HETATM 5904  O   HOH A 570      75.236 -11.374 -40.404  1.00 54.40           O  
HETATM 5905  O   HOH A 571      48.815  -9.867 -17.586  1.00 54.95           O  
HETATM 5906  O   HOH A 572      62.608  -4.523 -24.133  1.00 43.77           O  
HETATM 5907  O   HOH A 573      66.020 -24.129  -2.295  1.00 52.02           O  
HETATM 5908  O   HOH A 574      74.943 -15.789 -34.761  1.00 47.31           O  
HETATM 5909  O   HOH A 575      77.291 -28.584 -21.266  1.00 42.67           O  
HETATM 5910  O   HOH A 576      54.884 -24.303 -15.764  1.00 52.15           O  
HETATM 5911  O   HOH A 577      68.864 -25.118 -41.413  1.00 60.49           O  
HETATM 5912  O   HOH A 578      64.490 -22.004  -1.413  1.00 54.19           O  
HETATM 5913  O   HOH A 579      75.652 -30.703 -20.217  1.00 44.29           O  
HETATM 5914  O   HOH A 580      70.076 -10.067 -11.314  1.00 52.59           O  
HETATM 5915  O   HOH A 581      94.144  -4.401 -33.153  1.00 41.32           O  
HETATM 5916  O   HOH A 582      68.819 -18.311 -35.909  1.00 54.41           O  
HETATM 5917  O   HOH A 583      68.927 -19.098 -27.058  1.00 38.82           O  
HETATM 5918  O   HOH A 584      62.948  -3.919 -21.877  1.00 43.95           O  
HETATM 5919  O   HOH A 585      53.339 -28.989 -14.204  1.00 54.30           O  
HETATM 5920  O   HOH A 586      60.981  -8.477  -8.381  1.00 68.89           O  
HETATM 5921  O   HOH A 587      60.349 -26.941 -21.936  1.00 33.80           O  
HETATM 5922  O   HOH A 588      99.147 -24.321 -32.093  1.00 49.05           O  
HETATM 5923  O   HOH A 589      75.906 -22.633 -25.876  1.00 38.50           O  
HETATM 5924  O   HOH A 590      60.486 -29.760 -19.915  1.00 39.86           O  
HETATM 5925  O   HOH A 591      75.673 -24.875 -29.361  1.00 42.43           O  
HETATM 5926  O   HOH A 592      72.888 -12.920 -34.041  1.00 44.67           O  
HETATM 5927  O   HOH A 593      49.470 -32.935 -19.233  1.00 57.31           O  
HETATM 5928  O   HOH A 594      70.904 -21.153 -13.987  1.00 55.27           O  
HETATM 5929  O   HOH A 595      61.645 -51.138  -2.704  1.00 41.90           O  
HETATM 5930  O   HOH A 596      72.590 -23.872 -25.768  1.00 41.55           O  
HETATM 5931  O   HOH A 597      49.488 -35.756 -19.778  1.00 45.72           O  
HETATM 5932  O   HOH A 598      69.252 -24.337 -32.287  1.00 45.02           O  
HETATM 5933  O   HOH A 599      53.647 -24.184  -3.567  1.00 52.87           O  
HETATM 5934  O   HOH A 600      88.785  -6.105 -39.526  1.00 40.63           O  
HETATM 5935  O   HOH A 601      63.257 -27.129 -21.885  1.00 32.57           O  
HETATM 5936  O   HOH A 602      94.492 -25.098 -41.208  1.00 66.09           O  
HETATM 5937  O   HOH A 603      68.188  -5.864 -28.087  1.00 43.92           O  
HETATM 5938  O   HOH A 604      51.298 -15.989 -12.289  1.00 69.09           O  
HETATM 5939  O   HOH A 605      66.427  -6.991 -13.196  1.00 49.47           O  
HETATM 5940  O   HOH A 606      66.392 -45.918   1.535  1.00 33.73           O  
HETATM 5941  O   HOH A 607      99.477 -33.371 -37.926  1.00 47.45           O  
HETATM 5942  O   HOH A 608      55.537 -20.124 -17.695  1.00 54.95           O  
HETATM 5943  O   HOH A 609      66.260 -18.792  -6.890  1.00 45.16           O  
HETATM 5944  O   HOH A 610      47.168 -18.663 -18.412  1.00 60.45           O  
HETATM 5945  O   HOH A 611      68.754 -17.556 -14.719  1.00 36.22           O  
HETATM 5946  O   HOH A 612      79.935  -5.956 -35.696  1.00 37.93           O  
HETATM 5947  O   HOH A 613      90.117 -34.551 -25.022  1.00 36.99           O  
HETATM 5948  O   HOH A 614      56.126  -4.482 -27.452  1.00 63.91           O  
HETATM 5949  O   HOH A 615      63.256 -43.622 -15.022  1.00 58.13           O  
HETATM 5950  O   HOH A 616      94.513 -15.170 -43.328  1.00 62.42           O  
HETATM 5951  O   HOH A 617      55.582 -55.345 -13.433  1.00 48.58           O  
HETATM 5952  O   HOH A 618      68.790 -29.558 -28.601  1.00 50.18           O  
HETATM 5953  O   HOH A 619      57.930 -36.124 -15.134  1.00 46.84           O  
HETATM 5954  O   HOH A 620      76.138 -17.671 -20.535  1.00 35.98           O  
HETATM 5955  O   HOH A 621      48.352 -10.172 -12.519  1.00 53.55           O  
HETATM 5956  O   HOH A 622      96.093 -28.603 -40.000  1.00 50.70           O  
HETATM 5957  O   HOH A 623      80.271  -3.703 -39.870  1.00 42.67           O  
HETATM 5958  O   HOH A 624      83.959 -13.411 -22.224  1.00 42.59           O  
HETATM 5959  O   HOH A 625      77.827 -21.035 -28.442  1.00 34.55           O  
HETATM 5960  O   HOH A 626      75.155  -6.615 -22.031  1.00 63.57           O  
HETATM 5961  O   HOH A 627      63.095 -16.450 -28.270  1.00 41.62           O  
HETATM 5962  O   HOH A 628      88.535  -2.951 -33.058  1.00 42.21           O  
HETATM 5963  O   HOH A 629      51.444 -51.214  -7.216  1.00 59.88           O  
HETATM 5964  O   HOH A 630      57.569 -12.857 -31.162  1.00 66.66           O  
HETATM 5965  O   HOH A 631     100.623 -10.976 -32.712  1.00 67.69           O  
HETATM 5966  O   HOH A 632      49.993 -12.197 -19.342  1.00 58.74           O  
HETATM 5967  O   HOH A 633      82.997 -19.794 -20.604  1.00 55.76           O  
HETATM 5968  O   HOH A 634      87.524 -27.615 -39.887  1.00 46.33           O  
HETATM 5969  O   HOH A 635      53.504 -28.028 -24.202  1.00 60.22           O  
HETATM 5970  O   HOH A 636      52.737 -13.633 -24.985  1.00 50.89           O  
HETATM 5971  O   HOH A 637      47.453 -32.930  -6.922  1.00 54.55           O  
HETATM 5972  O   HOH A 638      68.914 -18.866  -8.690  1.00 48.95           O  
HETATM 5973  O   HOH A 639      76.778 -12.687 -45.296  1.00 65.53           O  
HETATM 5974  O   HOH A 640      54.689 -21.935  -0.508  1.00 59.18           O  
HETATM 5975  O   HOH A 641      62.977 -22.035 -12.203  1.00 35.62           O  
HETATM 5976  O   HOH A 642      58.758 -48.818  -5.058  1.00 35.99           O  
HETATM 5977  O   HOH A 643      91.737 -26.069 -49.411  1.00 70.61           O  
HETATM 5978  O   HOH A 644      73.605 -29.590  -1.094  1.00 49.12           O  
HETATM 5979  O   HOH A 645      79.420 -21.858 -35.658  1.00 39.37           O  
HETATM 5980  O   HOH A 646      97.044 -17.138 -27.812  1.00 63.19           O  
HETATM 5981  O   HOH A 647      65.543 -23.741 -20.761  1.00 36.08           O  
HETATM 5982  O   HOH A 648      50.586 -52.369 -10.021  1.00 57.97           O  
HETATM 5983  O   HOH A 649      68.391 -34.781 -11.441  1.00 31.86           O  
HETATM 5984  O   HOH A 650      61.312 -18.742 -34.354  1.00 45.10           O  
HETATM 5985  O   HOH A 651      57.801 -11.772   1.525  1.00 59.09           O  
HETATM 5986  O   HOH A 652      79.187 -26.022 -28.179  1.00 52.31           O  
HETATM 5987  O   HOH A 653      96.682 -26.757 -24.152  1.00 51.52           O  
HETATM 5988  O   HOH A 654      99.209  -4.882 -28.015  1.00 53.60           O  
HETATM 5989  O   HOH A 655      95.577 -21.462 -30.836  1.00 39.76           O  
HETATM 5990  O   HOH A 656      61.618 -26.422 -18.164  1.00 33.67           O  
HETATM 5991  O   HOH A 657      73.553 -22.192 -15.030  1.00 37.50           O  
HETATM 5992  O   HOH A 658      76.249 -31.098 -15.766  1.00 49.53           O  
HETATM 5993  O   HOH A 659      71.096 -32.531  -0.571  1.00 42.53           O  
HETATM 5994  O   HOH A 660      92.747  -4.705 -24.391  1.00 56.07           O  
HETATM 5995  O   HOH A 661      70.110 -40.281 -14.827  1.00 58.19           O  
HETATM 5996  O   HOH A 662      70.898 -17.586 -28.350  1.00 37.24           O  
HETATM 5997  O   HOH A 663      54.621 -44.972  -0.794  1.00 39.65           O  
HETATM 5998  O   HOH A 664      59.710 -11.408 -31.483  1.00 59.71           O  
HETATM 5999  O   HOH A 665      82.630 -34.424 -21.682  1.00 45.99           O  
HETATM 6000  O   HOH A 666      63.645 -49.839 -13.101  1.00 38.93           O  
HETATM 6001  O   HOH A 667      82.253 -24.543 -20.854  1.00 39.70           O  
HETATM 6002  O   HOH A 668      93.348  -2.121 -39.344  1.00 43.58           O  
HETATM 6003  O   HOH A 669      83.698 -36.188 -27.271  1.00 49.69           O  
HETATM 6004  O   HOH A 670      62.162 -20.650  -9.873  1.00 35.73           O  
HETATM 6005  O   HOH A 671      66.053 -29.253 -33.021  1.00 65.78           O  
HETATM 6006  O   HOH A 672     101.248 -29.682 -26.717  1.00 61.04           O  
HETATM 6007  O   HOH A 673      58.167 -35.060  -3.454  1.00 57.43           O  
HETATM 6008  O   HOH A 674      64.224 -52.131  -9.796  1.00 38.49           O  
HETATM 6009  O   HOH A 675      42.084 -35.431 -10.818  1.00 51.14           O  
HETATM 6010  O   HOH A 676      75.836 -15.312 -17.383  1.00 50.57           O  
HETATM 6011  O   HOH A 677      62.898  -8.454   0.477  1.00 54.05           O  
HETATM 6012  O   HOH A 678      59.604  -0.954  -7.571  1.00 78.32           O  
HETATM 6013  O   HOH A 679     101.984 -32.559 -38.425  1.00 56.60           O  
HETATM 6014  O   HOH A 680      71.811 -35.101  -3.900  1.00 46.11           O  
HETATM 6015  O   HOH A 681      75.260 -21.998 -29.081  1.00 37.30           O  
HETATM 6016  O   HOH A 682      64.515 -23.910 -11.255  1.00 38.83           O  
HETATM 6017  O   HOH A 683      81.332 -33.822 -25.380  1.00 68.93           O  
HETATM 6018  O   HOH A 684      94.430 -23.908 -24.006  1.00 45.61           O  
HETATM 6019  O   HOH A 685      45.253 -43.548  -6.778  1.00 51.68           O  
HETATM 6020  O   HOH A 686      46.984 -45.581  -8.463  1.00 55.54           O  
HETATM 6021  O   HOH A 687      52.930 -21.286 -29.915  1.00 55.73           O  
HETATM 6022  O   HOH A 688      95.332  -9.755 -47.707  1.00 76.54           O  
HETATM 6023  O   HOH A 689      54.439 -26.189 -18.314  1.00 42.04           O  
HETATM 6024  O   HOH A 690      45.546 -37.164  -4.488  1.00 45.40           O  
HETATM 6025  O   HOH A 691      68.052 -24.978 -38.568  1.00 71.75           O  
HETATM 6026  O   HOH A 692      99.981 -11.383 -40.711  1.00 73.29           O  
HETATM 6027  O   HOH A 693      91.764 -27.909 -40.773  1.00 51.98           O  
HETATM 6028  O   HOH A 694      66.437 -19.122 -26.234  1.00 34.44           O  
HETATM 6029  O   HOH A 695      94.087 -34.406 -40.476  1.00 61.46           O  
HETATM 6030  O   HOH A 696      76.441 -27.983 -47.473  1.00 67.31           O  
HETATM 6031  O   HOH A 697      71.808 -28.982  -8.178  1.00 33.86           O  
HETATM 6032  O   HOH A 698      61.784 -55.020  -7.509  1.00 39.71           O  
HETATM 6033  O   HOH A 699      79.462 -23.356 -28.314  1.00 48.89           O  
HETATM 6034  O   HOH A 700      64.808  -2.996 -25.218  1.00 47.98           O  
HETATM 6035  O   HOH A 701     101.095  -3.119 -30.698  1.00 54.78           O  
HETATM 6036  O   HOH A 702      59.002 -19.902 -33.931  1.00 48.54           O  
HETATM 6037  O   HOH A 703      53.442 -55.425 -15.286  1.00 64.96           O  
HETATM 6038  O   HOH A 704      71.115 -10.506 -33.890  1.00 51.37           O  
HETATM 6039  O   HOH A 705      48.619 -45.601 -11.403  1.00 45.47           O  
HETATM 6040  O   HOH A 706      68.757 -17.045 -33.549  1.00 56.74           O  
HETATM 6041  O   HOH A 707      68.566   1.103 -20.043  1.00 57.66           O  
HETATM 6042  O   HOH A 708     102.487 -26.807 -30.439  1.00 49.05           O  
HETATM 6043  O   HOH A 709      69.690  -7.144 -31.058  1.00 52.86           O  
HETATM 6044  O   HOH A 710      51.978 -23.175 -36.811  1.00 76.42           O  
HETATM 6045  O   HOH A 711      57.682  -1.042 -10.495  1.00 66.11           O  
HETATM 6046  O   HOH A 712      71.924 -16.533 -46.921  1.00 58.81           O  
HETATM 6047  O   HOH A 713      48.491 -46.655 -14.742  1.00 73.96           O  
HETATM 6048  O   HOH A 714      98.721 -23.321 -34.525  1.00 57.42           O  
HETATM 6049  O   HOH A 715      70.091  -3.974 -17.229  1.00 69.35           O  
HETATM 6050  O   HOH A 716      89.354 -28.151 -46.778  1.00 71.37           O  
HETATM 6051  O   HOH A 717      51.654  -8.431 -31.849  1.00 74.91           O  
HETATM 6052  O   HOH A 718      65.252 -26.426 -35.454  1.00 62.35           O  
HETATM 6053  O   HOH A 719      78.963  -5.189 -41.910  1.00 67.88           O  
HETATM 6054  O   HOH A 720      76.963 -32.335 -39.175  1.00 67.78           O  
HETATM 6055  O   HOH A 721      98.836 -29.085 -26.054  1.00 63.95           O  
HETATM 6056  O   HOH A 722      77.089  -7.987 -19.628  1.00 62.00           O  
HETATM 6057  O   HOH A 723      87.387 -40.266 -30.787  1.00 74.13           O  
HETATM 6058  O   HOH A 724      69.425 -10.361  -6.679  1.00 72.01           O  
HETATM 6059  O   HOH A 725      55.995 -19.583   0.518  1.00 53.93           O  
HETATM 6060  O   HOH A 726      95.675 -18.565 -40.405  1.00 55.36           O  
HETATM 6061  O   HOH A 727      71.560 -26.980 -27.174  1.00 62.16           O  
HETATM 6062  O   HOH A 728      70.962 -35.432  -1.429  1.00 44.32           O  
HETATM 6063  O   HOH A 729      52.950 -27.044  -2.824  1.00 65.76           O  
HETATM 6064  O   HOH A 730      95.911  -1.700 -39.379  1.00 62.56           O  
HETATM 6065  O   HOH A 731      96.704 -21.614 -40.288  1.00 72.47           O  
HETATM 6066  O   HOH A 732      97.728  -7.681 -48.048  1.00 84.72           O  
HETATM 6067  O   HOH A 733      87.812 -29.154 -42.118  1.00 61.62           O  
HETATM 6068  O   HOH A 734      93.309  -3.388 -41.789  1.00 62.67           O  
HETATM 6069  O   HOH A 735      94.254 -29.076 -41.319  1.00 53.88           O  
HETATM 6070  O   HOH A 736      73.815 -25.748 -27.122  1.00 49.58           O  
HETATM 6071  O   HOH A 737      69.128 -14.974 -34.503  1.00 75.68           O  
HETATM 6072  O   HOH A 738      54.335 -26.713 -26.406  1.00 44.86           O  
HETATM 6073  O   HOH A 739     101.911 -24.496 -31.385  1.00 60.60           O  
HETATM 6074  O   HOH A 740      50.907 -47.674 -11.369  1.00 59.26           O  
HETATM 6075  O   HOH A 741      91.102 -27.017 -43.515  1.00 59.22           O  
HETATM 6076  O   HOH A 742      88.935 -28.260 -44.079  1.00 52.08           O  
HETATM 6077  O   HOH B 501      58.741 -45.506  36.435  1.00 51.17           O  
HETATM 6078  O   HOH B 502      80.993 -42.258   0.022  1.00 68.09           O  
HETATM 6079  O   HOH B 503      45.266 -29.850  24.035  1.00 59.41           O  
HETATM 6080  O   HOH B 504      75.898  -9.416  -1.371  1.00 69.27           O  
HETATM 6081  O   HOH B 505      69.091 -11.705  35.100  1.00 54.74           O  
HETATM 6082  O   HOH B 506      71.040 -15.283  26.348  1.00 42.37           O  
HETATM 6083  O   HOH B 507      60.398 -33.404  20.898  1.00 36.72           O  
HETATM 6084  O   HOH B 508      70.778 -25.893  20.342  1.00 49.57           O  
HETATM 6085  O   HOH B 509      77.335 -31.020  17.633  1.00 48.47           O  
HETATM 6086  O   HOH B 510      83.904 -12.510   8.548  1.00 56.39           O  
HETATM 6087  O   HOH B 511      62.940 -12.432   9.148  1.00 44.36           O  
HETATM 6088  O   HOH B 512      83.905 -19.825  40.272  1.00 49.95           O  
HETATM 6089  O   HOH B 513      74.444 -35.680  16.526  1.00 61.82           O  
HETATM 6090  O   HOH B 514      80.367  -0.859  17.149  1.00 43.34           O  
HETATM 6091  O   HOH B 515      65.094  -3.428  21.580  1.00 36.86           O  
HETATM 6092  O   HOH B 516      63.093 -23.018  19.071  1.00 38.85           O  
HETATM 6093  O   HOH B 517      65.343 -27.299  24.316  1.00 41.31           O  
HETATM 6094  O   HOH B 518      61.548 -19.426  35.247  1.00 54.17           O  
HETATM 6095  O   HOH B 519      70.874 -26.381   9.824  1.00 43.26           O  
HETATM 6096  O   HOH B 520      90.974 -32.671  -1.065  1.00 37.15           O  
HETATM 6097  O   HOH B 521      65.521 -27.681  29.905  1.00 44.91           O  
HETATM 6098  O   HOH B 522      77.739 -15.818  38.021  1.00 63.89           O  
HETATM 6099  O   HOH B 523      60.690 -38.187  15.483  1.00 44.46           O  
HETATM 6100  O   HOH B 524      83.252 -17.946  13.116  1.00 57.18           O  
HETATM 6101  O   HOH B 525      51.012 -19.045  21.501  1.00 62.93           O  
HETATM 6102  O   HOH B 526      49.840 -46.704  28.703  1.00 37.83           O  
HETATM 6103  O   HOH B 527      70.455 -24.657  24.185  1.00 49.58           O  
HETATM 6104  O   HOH B 528      56.753  -2.712  19.491  1.00 77.28           O  
HETATM 6105  O   HOH B 529      73.453 -19.763   1.636  1.00 40.14           O  
HETATM 6106  O   HOH B 530      44.907 -36.482  37.510  1.00 50.54           O  
HETATM 6107  O   HOH B 531      69.388  -6.515   8.452  1.00 39.25           O  
HETATM 6108  O   HOH B 532      60.442 -19.860  18.173  1.00 49.94           O  
HETATM 6109  O   HOH B 533      58.424 -15.637  18.986  1.00 43.08           O  
HETATM 6110  O   HOH B 534      62.552 -12.547  11.607  1.00 51.24           O  
HETATM 6111  O   HOH B 535      58.903  -4.261  27.789  1.00 56.69           O  
HETATM 6112  O   HOH B 536      75.294   3.870  28.032  1.00 42.35           O  
HETATM 6113  O   HOH B 537      75.593 -32.189  19.724  1.00 50.18           O  
HETATM 6114  O   HOH B 538      81.249 -24.044  20.237  1.00 41.28           O  
HETATM 6115  O   HOH B 539      47.221 -31.953  31.836  1.00 47.27           O  
HETATM 6116  O   HOH B 540      67.112 -26.212  17.480  1.00 42.74           O  
HETATM 6117  O   HOH B 541      76.022 -22.458  20.014  1.00 33.99           O  
HETATM 6118  O   HOH B 542      47.377 -28.427  44.238  1.00 62.15           O  
HETATM 6119  O   HOH B 543      83.539 -37.301  14.849  1.00 52.41           O  
HETATM 6120  O   HOH B 544      80.030 -13.279  17.810  1.00 49.16           O  
HETATM 6121  O   HOH B 545      67.832 -25.175  26.198  1.00 46.55           O  
HETATM 6122  O   HOH B 546      70.477 -32.453  12.262  1.00 43.65           O  
HETATM 6123  O   HOH B 547      71.497  -0.007  26.868  1.00 37.76           O  
HETATM 6124  O   HOH B 548      83.791 -15.910   3.674  1.00 43.74           O  
HETATM 6125  O   HOH B 549      78.805 -37.036   1.074  1.00 40.54           O  
HETATM 6126  O   HOH B 550      62.761   3.142  28.345  1.00 54.95           O  
HETATM 6127  O   HOH B 551      72.378  -5.660   8.169  1.00 63.16           O  
HETATM 6128  O   HOH B 552      65.172 -32.893  25.328  1.00 56.55           O  
HETATM 6129  O   HOH B 553      68.099 -19.303   9.091  1.00 46.95           O  
HETATM 6130  O   HOH B 554      59.001  -1.587  12.738  1.00 56.53           O  
HETATM 6131  O   HOH B 555      62.301 -14.942   9.066  1.00 63.49           O  
HETATM 6132  O   HOH B 556      96.840 -35.309   9.708  1.00 49.02           O  
HETATM 6133  O   HOH B 557      71.878 -13.813  28.497  1.00 37.74           O  
HETATM 6134  O   HOH B 558      99.763 -19.504  11.007  1.00 50.36           O  
HETATM 6135  O   HOH B 559      61.538 -20.015  46.903  1.00 66.77           O  
HETATM 6136  O   HOH B 560      77.276 -16.039   9.441  1.00 34.85           O  
HETATM 6137  O   HOH B 561      85.717 -21.733  15.730  1.00 37.54           O  
HETATM 6138  O   HOH B 562      85.253 -20.797   2.506  1.00 38.94           O  
HETATM 6139  O   HOH B 563      80.617 -13.074  27.398  1.00 38.39           O  
HETATM 6140  O   HOH B 564      68.049 -18.690  36.564  1.00 63.15           O  
HETATM 6141  O   HOH B 565      95.370 -24.383   1.516  1.00 60.07           O  
HETATM 6142  O   HOH B 566      65.992 -31.728  21.633  1.00 47.54           O  
HETATM 6143  O   HOH B 567      58.053 -43.468  25.353  1.00 36.77           O  
HETATM 6144  O   HOH B 568      62.103  -7.702  28.309  1.00 41.31           O  
HETATM 6145  O   HOH B 569      46.928 -41.504  34.747  1.00 46.79           O  
HETATM 6146  O   HOH B 570      43.103 -40.241  38.801  1.00 66.50           O  
HETATM 6147  O   HOH B 571      79.144  -5.974  24.953  1.00 39.40           O  
HETATM 6148  O   HOH B 572      74.594 -14.875  34.540  1.00 39.80           O  
HETATM 6149  O   HOH B 573      78.469   1.085  28.146  1.00 40.47           O  
HETATM 6150  O   HOH B 574      80.970  -1.123  12.238  1.00 47.03           O  
HETATM 6151  O   HOH B 575      92.240 -17.816   0.949  1.00 75.64           O  
HETATM 6152  O   HOH B 576      63.495 -10.098   9.232  1.00 54.81           O  
HETATM 6153  O   HOH B 577      79.465 -10.373  -1.118  1.00 60.69           O  
HETATM 6154  O   HOH B 578      45.927 -45.248  26.950  1.00 59.16           O  
HETATM 6155  O   HOH B 579      45.092 -39.339  32.287  1.00 53.42           O  
HETATM 6156  O   HOH B 580      42.983 -32.169  38.376  1.00 56.76           O  
HETATM 6157  O   HOH B 581      92.687 -39.373   5.531  1.00 45.68           O  
HETATM 6158  O   HOH B 582      82.045  -7.990  12.265  1.00 63.23           O  
HETATM 6159  O   HOH B 583      56.982 -32.432  46.974  1.00 56.50           O  
HETATM 6160  O   HOH B 584      70.502 -17.979   7.167  1.00 47.01           O  
HETATM 6161  O   HOH B 585      81.559 -41.964  10.406  1.00 67.48           O  
HETATM 6162  O   HOH B 586      77.453 -23.106  22.232  1.00 34.96           O  
HETATM 6163  O   HOH B 587      70.560  -3.679  31.570  1.00 43.69           O  
HETATM 6164  O   HOH B 588      65.788  -3.849  23.975  1.00 35.95           O  
HETATM 6165  O   HOH B 589      73.699 -25.496  25.022  1.00 50.83           O  
HETATM 6166  O   HOH B 590      64.307 -41.475  27.823  1.00 56.56           O  
HETATM 6167  O   HOH B 591      84.022 -47.049   4.226  1.00 48.28           O  
HETATM 6168  O   HOH B 592      43.006 -32.156  28.894  1.00 75.47           O  
HETATM 6169  O   HOH B 593      86.474  -7.581  18.295  1.00 61.90           O  
HETATM 6170  O   HOH B 594      66.961 -12.667  33.669  1.00 49.16           O  
HETATM 6171  O   HOH B 595      51.671 -45.524  24.463  1.00 42.29           O  
HETATM 6172  O   HOH B 596      64.673  -0.863  29.285  1.00 60.16           O  
HETATM 6173  O   HOH B 597      68.276 -19.242  27.486  1.00 37.68           O  
HETATM 6174  O   HOH B 598      46.606 -47.901  38.457  1.00 63.69           O  
HETATM 6175  O   HOH B 599      73.700  -7.321  -1.612  1.00 53.81           O  
HETATM 6176  O   HOH B 600      64.278 -25.918  26.405  1.00 43.78           O  
HETATM 6177  O   HOH B 601      56.547 -36.323  40.066  1.00 56.95           O  
HETATM 6178  O   HOH B 602      46.196 -14.714  27.934  1.00 63.92           O  
HETATM 6179  O   HOH B 603      85.820 -13.516  31.663  1.00 54.97           O  
HETATM 6180  O   HOH B 604      60.849 -27.046  36.019  1.00 42.91           O  
HETATM 6181  O   HOH B 605      70.661 -24.380  32.926  1.00 62.24           O  
HETATM 6182  O   HOH B 606      98.754 -26.996  19.519  1.00 80.17           O  
HETATM 6183  O   HOH B 607      87.169 -24.220   2.165  1.00 51.24           O  
HETATM 6184  O   HOH B 608      74.826 -18.830  12.511  1.00 33.55           O  
HETATM 6185  O   HOH B 609      70.093 -30.867   1.422  1.00 49.73           O  
HETATM 6186  O   HOH B 610      83.955  -9.933   5.697  1.00 68.63           O  
HETATM 6187  O   HOH B 611      68.942   2.089  14.889  1.00 55.18           O  
HETATM 6188  O   HOH B 612      68.592 -32.751  20.696  1.00 52.59           O  
HETATM 6189  O   HOH B 613      53.363 -38.555  40.915  1.00 64.24           O  
HETATM 6190  O   HOH B 614      56.926 -26.993  21.266  1.00 51.64           O  
HETATM 6191  O   HOH B 615      74.955   2.417  31.911  1.00 57.48           O  
HETATM 6192  O   HOH B 616      86.821 -19.550  14.173  1.00 56.45           O  
HETATM 6193  O   HOH B 617      73.462 -22.272   2.536  1.00 45.65           O  
HETATM 6194  O   HOH B 618      59.693 -16.093  41.081  1.00 75.34           O  
HETATM 6195  O   HOH B 619      81.823 -46.184   1.340  1.00 54.29           O  
HETATM 6196  O   HOH B 620      81.740  -6.358  25.846  1.00 44.34           O  
HETATM 6197  O   HOH B 621      64.911 -38.079  18.677  1.00 58.70           O  
HETATM 6198  O   HOH B 622      83.171 -16.406  15.687  1.00 55.23           O  
HETATM 6199  O   HOH B 623      48.510 -40.155  24.454  1.00 50.80           O  
HETATM 6200  O   HOH B 624      64.726  -5.864  30.990  1.00 45.11           O  
HETATM 6201  O   HOH B 625      67.528 -18.177  15.068  1.00 37.88           O  
HETATM 6202  O   HOH B 626      81.242  -6.365   1.285  1.00 57.68           O  
HETATM 6203  O   HOH B 627      61.351 -21.951  21.098  1.00 36.09           O  
HETATM 6204  O   HOH B 628      84.495 -40.983  -1.157  1.00 32.88           O  
HETATM 6205  O   HOH B 629      79.696 -21.485  22.180  1.00 32.69           O  
HETATM 6206  O   HOH B 630      78.402 -21.773  18.503  1.00 36.21           O  
HETATM 6207  O   HOH B 631      93.682 -23.160  19.908  1.00 55.09           O  
HETATM 6208  O   HOH B 632      70.365 -28.289  36.890  1.00 68.54           O  
HETATM 6209  O   HOH B 633      91.352 -42.786   3.003  1.00 45.91           O  
HETATM 6210  O   HOH B 634      60.662 -28.894  19.759  1.00 55.51           O  
HETATM 6211  O   HOH B 635      85.997 -36.893  15.422  1.00 50.11           O  
HETATM 6212  O   HOH B 636      76.935   3.371  20.638  1.00 45.10           O  
HETATM 6213  O   HOH B 637      56.855 -20.056  20.023  1.00 60.66           O  
HETATM 6214  O   HOH B 638      63.201  -3.632  24.893  1.00 41.77           O  
HETATM 6215  O   HOH B 639      65.690   1.916  22.454  1.00 39.52           O  
HETATM 6216  O   HOH B 640      67.741 -22.344  14.482  1.00 49.55           O  
HETATM 6217  O   HOH B 641      66.131   1.908  29.824  1.00 45.98           O  
HETATM 6218  O   HOH B 642      61.777 -25.592  28.873  1.00 38.94           O  
HETATM 6219  O   HOH B 643      68.312 -33.350  16.206  1.00 50.37           O  
HETATM 6220  O   HOH B 644      64.401 -24.924  29.512  1.00 39.13           O  
HETATM 6221  O   HOH B 645      76.993 -32.478  11.940  1.00 34.96           O  
HETATM 6222  O   HOH B 646      49.195 -47.384  38.027  1.00 58.59           O  
HETATM 6223  O   HOH B 647      62.907   0.263  23.148  1.00 46.91           O  
HETATM 6224  O   HOH B 648      66.204 -24.489  15.490  1.00 43.95           O  
HETATM 6225  O   HOH B 649      80.550  -3.495  18.955  1.00 39.15           O  
HETATM 6226  O   HOH B 650      85.847 -27.388   3.902  1.00 53.30           O  
HETATM 6227  O   HOH B 651      61.900 -16.019  34.614  1.00 55.77           O  
HETATM 6228  O   HOH B 652      73.557 -32.022   0.993  1.00 42.73           O  
HETATM 6229  O   HOH B 653      82.329 -11.978  14.496  1.00 51.06           O  
HETATM 6230  O   HOH B 654      67.582  -7.247  -0.465  1.00 61.31           O  
HETATM 6231  O   HOH B 655      74.042 -28.134  28.633  1.00 57.17           O  
HETATM 6232  O   HOH B 656      80.586 -16.954  -2.190  1.00 73.92           O  
HETATM 6233  O   HOH B 657      88.910 -42.618  13.709  1.00 40.72           O  
HETATM 6234  O   HOH B 658      81.606 -14.394   0.574  1.00 63.76           O  
HETATM 6235  O   HOH B 659      64.405 -39.536  21.923  1.00 48.94           O  
HETATM 6236  O   HOH B 660      46.741 -35.236  31.279  1.00 53.25           O  
HETATM 6237  O   HOH B 661      83.322  -1.346  18.613  1.00 60.05           O  
HETATM 6238  O   HOH B 662      72.236  -1.913  30.765  1.00 50.79           O  
HETATM 6239  O   HOH B 663      56.307 -12.230  22.308  1.00 53.47           O  
HETATM 6240  O   HOH B 664      89.428 -44.884  10.327  1.00 43.38           O  
HETATM 6241  O   HOH B 665      65.890 -19.122  28.802  1.00 40.69           O  
HETATM 6242  O   HOH B 666      49.923 -41.469  40.376  1.00 55.10           O  
HETATM 6243  O   HOH B 667      74.820 -17.366  10.104  1.00 35.23           O  
HETATM 6244  O   HOH B 668      73.713 -21.538  21.175  1.00 37.68           O  
HETATM 6245  O   HOH B 669      52.440 -22.495  22.745  1.00 51.48           O  
HETATM 6246  O   HOH B 670      83.476 -23.115   0.935  1.00 57.88           O  
HETATM 6247  O   HOH B 671      75.019  -4.410  -1.529  1.00 70.87           O  
HETATM 6248  O   HOH B 672      74.318  -3.648   9.001  1.00 46.43           O  
HETATM 6249  O   HOH B 673      59.672 -30.836  21.249  1.00 39.39           O  
HETATM 6250  O   HOH B 674      62.353 -12.738  33.935  1.00 59.28           O  
HETATM 6251  O   HOH B 675      64.178 -18.966  47.584  1.00 68.58           O  
HETATM 6252  O   HOH B 676      74.584 -21.218  11.627  1.00 41.11           O  
HETATM 6253  O   HOH B 677      70.539 -18.005  26.554  1.00 37.67           O  
HETATM 6254  O   HOH B 678      70.234  -3.261   6.402  1.00 57.88           O  
HETATM 6255  O   HOH B 679      68.825 -35.368  31.421  1.00 73.96           O  
HETATM 6256  O   HOH B 680      71.860 -23.372  22.057  1.00 42.90           O  
HETATM 6257  O   HOH B 681      53.533 -12.726  30.240  1.00 51.75           O  
HETATM 6258  O   HOH B 682      52.919 -18.788  47.064  1.00 70.01           O  
HETATM 6259  O   HOH B 683      84.400 -17.869  18.453  1.00 38.53           O  
HETATM 6260  O   HOH B 684      73.355 -25.133  20.922  1.00 51.66           O  
HETATM 6261  O   HOH B 685      71.065 -29.277   8.624  1.00 36.17           O  
HETATM 6262  O   HOH B 686      76.046 -26.087  33.630  1.00 61.70           O  
HETATM 6263  O   HOH B 687     101.296 -27.631   7.220  1.00 52.69           O  
HETATM 6264  O   HOH B 688      69.159 -23.878  45.606  1.00 62.89           O  
HETATM 6265  O   HOH B 689      93.072 -46.281   7.938  1.00 46.48           O  
HETATM 6266  O   HOH B 690      93.598 -19.607   6.540  1.00 61.23           O  
HETATM 6267  O   HOH B 691      50.583 -14.757  41.639  1.00 62.93           O  
HETATM 6268  O   HOH B 692      71.250   0.415  29.354  1.00 43.32           O  
HETATM 6269  O   HOH B 693      43.474 -43.374  30.480  1.00 53.16           O  
HETATM 6270  O   HOH B 694      82.342   0.789  13.824  1.00 60.00           O  
HETATM 6271  O   HOH B 695      68.106   1.464  10.439  1.00 65.91           O  
HETATM 6272  O   HOH B 696      53.946 -45.271  40.719  1.00 59.50           O  
HETATM 6273  O   HOH B 697      99.523 -31.077  11.560  1.00 58.49           O  
HETATM 6274  O   HOH B 698      55.418  -6.425  27.696  1.00 53.59           O  
HETATM 6275  O   HOH B 699      97.761 -22.445   4.686  1.00 46.75           O  
HETATM 6276  O   HOH B 700      76.122  -1.354  31.740  1.00 65.21           O  
HETATM 6277  O   HOH B 701      77.337 -14.476  34.061  1.00 49.28           O  
HETATM 6278  O   HOH B 702      65.584  -3.137  31.372  1.00 60.91           O  
HETATM 6279  O   HOH B 703      48.812 -36.833  24.141  1.00 54.51           O  
HETATM 6280  O   HOH B 704      67.388 -17.087  33.806  1.00 61.72           O  
HETATM 6281  O   HOH B 705     100.416 -42.202  15.494  1.00 57.57           O  
HETATM 6282  O   HOH B 706     100.953 -30.268   8.997  1.00 64.91           O  
HETATM 6283  O   HOH B 707      78.529 -30.271  24.172  1.00 61.11           O  
HETATM 6284  O   HOH B 708      72.425 -33.820  19.464  1.00 67.47           O  
HETATM 6285  O   HOH B 709      49.615 -43.710  24.812  1.00 67.20           O  
HETATM 6286  O   HOH B 710      80.715  -2.445  21.052  1.00 57.43           O  
HETATM 6287  O   HOH B 711      51.892 -37.029  50.008  1.00 73.13           O  
HETATM 6288  O   HOH B 712      64.060 -18.146  13.053  1.00 70.21           O  
HETATM 6289  O   HOH B 713      60.094 -16.078  15.274  1.00 64.47           O  
HETATM 6290  O   HOH B 714      78.086  -0.049  30.456  1.00 65.73           O  
HETATM 6291  O   HOH B 715      44.711 -37.994  34.590  1.00 64.55           O  
HETATM 6292  O   HOH B 716      76.539 -23.086  35.842  1.00 66.47           O  
HETATM 6293  O   HOH B 717      47.879 -43.469  26.381  1.00 59.54           O  
HETATM 6294  O   HOH B 718      83.310 -25.381   1.670  1.00 71.10           O  
HETATM 6295  O   HOH B 719      62.870 -12.365   6.915  1.00 69.80           O  
HETATM 6296  O   HOH B 720      68.741   1.600  30.891  1.00 48.41           O  
HETATM 6297  O   HOH B 721      65.266 -35.156  45.861  1.00 74.33           O  
HETATM 6298  O   HOH B 722      61.846 -28.329  28.818  1.00 61.77           O  
HETATM 6299  O   HOH B 723      53.353 -19.650  51.397  1.00 74.72           O  
HETATM 6300  O   HOH B 724      70.247 -27.221  27.691  1.00 72.08           O  
HETATM 6301  O   HOH B 725      79.495 -13.154  -0.528  1.00 53.05           O  
HETATM 6302  O   HOH B 726      44.486 -32.549  40.466  1.00 63.12           O  
HETATM 6303  O   HOH B 727      80.500 -11.873  15.836  1.00 63.72           O  
HETATM 6304  O   HOH B 728      63.611 -46.805  30.654  1.00 79.34           O  
HETATM 6305  O   HOH B 729      75.074 -34.231   1.755  1.00 41.10           O  
HETATM 6306  O   HOH B 730      75.247 -24.542   0.193  1.00 80.33           O  
HETATM 6307  O   HOH B 731      75.171  -4.253  32.742  1.00 87.92           O  
HETATM 6308  O   HOH B 732      79.408   0.514  10.693  1.00 61.74           O  
HETATM 6309  O   HOH B 733      95.965 -23.372  21.756  1.00 60.46           O  
HETATM 6310  O   HOH B 734      73.027 -27.991   0.730  1.00 59.28           O  
HETATM 6311  O   HOH B 735      84.533 -13.089   3.865  1.00 67.62           O  
HETATM 6312  O   HOH B 736      57.037   0.329  26.026  1.00 50.30           O  
HETATM 6313  O   HOH B 737      67.647 -27.496  27.658  1.00 55.96           O  
HETATM 6314  O   HOH B 738      84.806 -17.932  26.669  1.00 49.24           O  
HETATM 6315  O   HOH B 739      80.979   0.098  27.112  1.00 55.43           O  
HETATM 6316  O   HOH B 740      85.180 -17.280  10.350  1.00 61.29           O  
HETATM 6317  O   HOH B 741      98.452 -34.139  11.487  1.00 56.56           O  
HETATM 6318  O   HOH B 742      71.755 -24.320   1.534  1.00 69.47           O  
HETATM 6319  O   HOH B 743      68.076  -2.904  32.434  1.00 54.98           O  
HETATM 6320  O   HOH B 744      60.594 -12.123   8.754  1.00 66.41           O  
CONECT 5710 5711 5715 5718                                                      
CONECT 5711 5710 5712 5716                                                      
CONECT 5712 5711 5713                                                           
CONECT 5713 5712 5714 5717                                                      
CONECT 5714 5713 5715                                                           
CONECT 5715 5710 5714                                                           
CONECT 5716 5711                                                                
CONECT 5717 5713                                                                
CONECT 5718 5710 5719 5724                                                      
CONECT 5719 5718 5720 5721                                                      
CONECT 5720 5719                                                                
CONECT 5721 5719 5722 5723                                                      
CONECT 5722 5721 5724 5725                                                      
CONECT 5723 5721                                                                
CONECT 5724 5718 5722                                                           
CONECT 5725 5722 5726                                                           
CONECT 5726 5725 5727                                                           
CONECT 5727 5726 5728 5729 5730                                                 
CONECT 5728 5727                                                                
CONECT 5729 5727                                                                
CONECT 5730 5727                                                                
CONECT 5731 5732 5733 5734 5735                                                 
CONECT 5732 5731 5736                                                           
CONECT 5733 5731 5737                                                           
CONECT 5734 5731 5738                                                           
CONECT 5735 5731                                                                
CONECT 5736 5732                                                                
CONECT 5737 5733                                                                
CONECT 5738 5734                                                                
CONECT 5739 5740 5741                                                           
CONECT 5740 5739                                                                
CONECT 5741 5739 5742                                                           
CONECT 5742 5741                                                                
CONECT 5743 5744 5745 5746                                                      
CONECT 5744 5743                                                                
CONECT 5745 5743                                                                
CONECT 5746 5743                                                                
CONECT 5747 5748 5749                                                           
CONECT 5748 5747                                                                
CONECT 5749 5747 5750                                                           
CONECT 5750 5749                                                                
CONECT 5751 5752 5753                                                           
CONECT 5752 5751                                                                
CONECT 5753 5751 5754                                                           
CONECT 5754 5753                                                                
CONECT 5755 5756 5757                                                           
CONECT 5756 5755                                                                
CONECT 5757 5755 5758                                                           
CONECT 5758 5757                                                                
CONECT 5759 5760 5761                                                           
CONECT 5760 5759                                                                
CONECT 5761 5759 5762                                                           
CONECT 5762 5761                                                                
CONECT 5763 5764 5765                                                           
CONECT 5764 5763                                                                
CONECT 5765 5763 5766                                                           
CONECT 5766 5765                                                                
CONECT 5767 5768 5769 5770 5771                                                 
CONECT 5768 5767                                                                
CONECT 5769 5767                                                                
CONECT 5770 5767                                                                
CONECT 5771 5767                                                                
CONECT 5772 5773 5777 5780                                                      
CONECT 5773 5772 5774 5778                                                      
CONECT 5774 5773 5775                                                           
CONECT 5775 5774 5776 5779                                                      
CONECT 5776 5775 5777                                                           
CONECT 5777 5772 5776                                                           
CONECT 5778 5773                                                                
CONECT 5779 5775                                                                
CONECT 5780 5772 5781 5786                                                      
CONECT 5781 5780 5782 5783                                                      
CONECT 5782 5781                                                                
CONECT 5783 5781 5784 5785                                                      
CONECT 5784 5783 5786 5787                                                      
CONECT 5785 5783                                                                
CONECT 5786 5780 5784                                                           
CONECT 5787 5784 5788                                                           
CONECT 5788 5787 5789                                                           
CONECT 5789 5788 5790 5791 5792                                                 
CONECT 5790 5789                                                                
CONECT 5791 5789                                                                
CONECT 5792 5789                                                                
CONECT 5793 5794 5795 5796 5797                                                 
CONECT 5794 5793 5798                                                           
CONECT 5795 5793 5799                                                           
CONECT 5796 5793 5800                                                           
CONECT 5797 5793                                                                
CONECT 5798 5794                                                                
CONECT 5799 5795                                                                
CONECT 5800 5796                                                                
CONECT 5801 5802 5803                                                           
CONECT 5802 5801                                                                
CONECT 5803 5801 5804                                                           
CONECT 5804 5803                                                                
CONECT 5805 5806 5807                                                           
CONECT 5806 5805                                                                
CONECT 5807 5805 5808                                                           
CONECT 5808 5807                                                                
CONECT 5809 5810 5811 5812                                                      
CONECT 5810 5809                                                                
CONECT 5811 5809                                                                
CONECT 5812 5809                                                                
CONECT 5813 5814 5815                                                           
CONECT 5814 5813                                                                
CONECT 5815 5813 5816                                                           
CONECT 5816 5815                                                                
CONECT 5817 5818 5819 5820                                                      
CONECT 5818 5817                                                                
CONECT 5819 5817                                                                
CONECT 5820 5817                                                                
CONECT 5821 5822 5823 5824                                                      
CONECT 5822 5821                                                                
CONECT 5823 5821                                                                
CONECT 5824 5821                                                                
CONECT 5825 5826 5827                                                           
CONECT 5826 5825                                                                
CONECT 5827 5825                                                                
CONECT 5828 5829 5830                                                           
CONECT 5829 5828                                                                
CONECT 5830 5828                                                                
CONECT 5831 5832 5833                                                           
CONECT 5832 5831                                                                
CONECT 5833 5831 5834                                                           
CONECT 5834 5833                                                                
MASTER      563    0   21   20   50    0   38    6 6109    2  125   58          
END                                                                             
HEADER    VIRAL PROTEIN                           26-MAR-20   7BQY              
TITLE     THE CRYSTAL STRUCTURE OF COVID-19 MAIN PROTEASE IN COMPLEX WITH AN    
TITLE    2 INHIBITOR N3 AT 1.7 ANGSTROM                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MAIN PROTEASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PP1AB,ORF1AB POLYPROTEIN;                                   
COMPND   5 EC: 3.4.22.69;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: N-[(5-METHYLISOXAZOL-3-YL)CARBONYL]ALANYL-L-VALYL-N~1~-    
COMPND   9 ((1R,2Z)-4-(BENZYLOXY)-4-OXO-1-{[(3R)-2-OXOPYRROLIDIN-3-             
COMPND  10 YL]METHYL}BUT-2-ENYL)-L-LEUCINAMIDE;                                 
COMPND  11 CHAIN: C;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 GENE: REP, 1A-1B;                                                    
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  14 ORGANISM_TAXID: 32630                                                
KEYWDS    PROTEASE, VIRAL PROTEIN                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.LIU,B.ZHANG,Z.JIN,H.YANG,Z.RAO                                      
REVDAT   5   24-JUN-20 7BQY    1       JRNL                                     
REVDAT   4   10-JUN-20 7BQY    1       COMPND                                   
REVDAT   3   27-MAY-20 7BQY    1       JRNL                                     
REVDAT   2   06-MAY-20 7BQY    1       COMPND SOURCE REMARK DBREF               
REVDAT   2 2                   1       LINK   SITE   ATOM                       
REVDAT   1   22-APR-20 7BQY    0                                                
JRNL        AUTH   Z.JIN,X.DU,Y.XU,Y.DENG,M.LIU,Y.ZHAO,B.ZHANG,X.LI,L.ZHANG,    
JRNL        AUTH 2 C.PENG,Y.DUAN,J.YU,L.WANG,K.YANG,F.LIU,R.JIANG,X.YANG,T.YOU, 
JRNL        AUTH 3 X.LIU,X.YANG,F.BAI,H.LIU,X.LIU,L.W.GUDDAT,W.XU,G.XIAO,C.QIN, 
JRNL        AUTH 4 Z.SHI,H.JIANG,Z.RAO,H.YANG                                   
JRNL        TITL   STRUCTURE OF MPROFROM SARS-COV-2 AND DISCOVERY OF ITS        
JRNL        TITL 2 INHIBITORS.                                                  
JRNL        REF    NATURE                        V. 582   289 2020              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   32272481                                                     
JRNL        DOI    10.1038/S41586-020-2223-Y                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.17.1_3660                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 40114                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2027                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 31.0000 -  4.0900    0.99     2811   161  0.1613 0.1760        
REMARK   3     2  4.0900 -  3.2500    0.99     2774   142  0.1805 0.2098        
REMARK   3     3  3.2400 -  2.8300    1.00     2782   154  0.2059 0.2500        
REMARK   3     4  2.8300 -  2.5800    1.00     2781   162  0.2136 0.2668        
REMARK   3     5  2.5800 -  2.3900    1.00     2772   164  0.2170 0.2501        
REMARK   3     6  2.3900 -  2.2500    1.00     2768   128  0.2150 0.2548        
REMARK   3     7  2.2500 -  2.1400    1.00     2835   127  0.2055 0.2181        
REMARK   3     8  2.1400 -  2.0400    1.00     2774   110  0.2064 0.2130        
REMARK   3     9  2.0400 -  1.9700    1.00     2759   153  0.2203 0.2682        
REMARK   3    10  1.9700 -  1.9000    1.00     2795   140  0.2225 0.2237        
REMARK   3    11  1.9000 -  1.8400    1.00     2772   145  0.2326 0.3237        
REMARK   3    12  1.8400 -  1.7900    0.99     2699   178  0.2621 0.2769        
REMARK   3    13  1.7900 -  1.7400    0.92     2551   138  0.2978 0.3780        
REMARK   3    14  1.7400 -  1.7000    0.80     2214   125  0.3174 0.3716        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.160           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.3330  -0.8548  12.1828              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2035 T22:   0.2372                                     
REMARK   3      T33:   0.2468 T12:  -0.0112                                     
REMARK   3      T13:  -0.0107 T23:   0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5156 L22:   2.4565                                     
REMARK   3      L33:   3.4661 L12:   0.6763                                     
REMARK   3      L13:  -0.5636 L23:   0.5375                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0502 S12:  -0.0677 S13:  -0.1355                       
REMARK   3      S21:   0.1412 S22:  -0.0879 S23:  -0.1524                       
REMARK   3      S31:  -0.3513 S32:  -0.1937 S33:   0.0034                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7BQY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1300016317.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97852                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40158                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 6LU7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% POLYETHYLENE GLYCOL (PEG) 6000, 3%    
REMARK 280  DMSO, 1MM DTT, 0.1M MES BUFFER (PH 6.0), PROTEIN CONCENTRATION      
REMARK 280  5MG/ML, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K,            
REMARK 280  EVAPORATION                                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       48.18450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.23700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       48.18450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       40.23700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 608  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 625  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 THE N-[(5-METHYLISOXAZOL-3-YL)CARBONYL]ALANYL-L-VALYL-N~1~-((1R,2Z)- 
REMARK 400 4-(BENZYLOXY)-4-OXO-1-{[(3R)-2-OXOPYRROLIDIN-3-YL]METHYL}BUT-2-ENYL) 
REMARK 400 -L-LEUCINAMIDE IS PEPTIDE-LIKE, A MEMBER OF INHIBITOR CLASS.         
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: N-[(5-METHYLISOXAZOL-3-YL)CARBONYL]ALANYL-L-VALYL-N~1~-((1R, 
REMARK 400         2Z)-4-(BENZYLOXY)-4-OXO-1-{[(3R)-2-OXOPYRROLIDIN-3-YL]       
REMARK 400         METHYL}BUT-2-ENYL)-L-LEUCINAMIDE                             
REMARK 400   CHAIN: C                                                           
REMARK 400   COMPONENT_1: PEPTIDE LIKE POLYMER                                  
REMARK 400   DESCRIPTION: NULL                                                  
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   302                                                      
REMARK 465     VAL A   303                                                      
REMARK 465     THR A   304                                                      
REMARK 465     PHE A   305                                                      
REMARK 465     GLN A   306                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   627     O    HOH A   632              2.17            
REMARK 500   O    HOH A   643     O    HOH A   651              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  33     -131.45     53.23                                   
REMARK 500    HIS A  41        1.75    -66.91                                   
REMARK 500    ASN A  51       69.59   -157.92                                   
REMARK 500    ASN A  84     -122.40     56.33                                   
REMARK 500    TYR A 154     -113.35     52.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 010 A 401 and PJE A      
REMARK 800  402                                                                 
DBREF  7BQY A    1   306  UNP    P0DTD1   R1AB_SARS2    3264   3569             
DBREF  7BQY C    1     6  PDB    7BQY     7BQY             1      6             
SEQRES   1 A  306  SER GLY PHE ARG LYS MET ALA PHE PRO SER GLY LYS VAL          
SEQRES   2 A  306  GLU GLY CYS MET VAL GLN VAL THR CYS GLY THR THR THR          
SEQRES   3 A  306  LEU ASN GLY LEU TRP LEU ASP ASP VAL VAL TYR CYS PRO          
SEQRES   4 A  306  ARG HIS VAL ILE CYS THR SER GLU ASP MET LEU ASN PRO          
SEQRES   5 A  306  ASN TYR GLU ASP LEU LEU ILE ARG LYS SER ASN HIS ASN          
SEQRES   6 A  306  PHE LEU VAL GLN ALA GLY ASN VAL GLN LEU ARG VAL ILE          
SEQRES   7 A  306  GLY HIS SER MET GLN ASN CYS VAL LEU LYS LEU LYS VAL          
SEQRES   8 A  306  ASP THR ALA ASN PRO LYS THR PRO LYS TYR LYS PHE VAL          
SEQRES   9 A  306  ARG ILE GLN PRO GLY GLN THR PHE SER VAL LEU ALA CYS          
SEQRES  10 A  306  TYR ASN GLY SER PRO SER GLY VAL TYR GLN CYS ALA MET          
SEQRES  11 A  306  ARG PRO ASN PHE THR ILE LYS GLY SER PHE LEU ASN GLY          
SEQRES  12 A  306  SER CYS GLY SER VAL GLY PHE ASN ILE ASP TYR ASP CYS          
SEQRES  13 A  306  VAL SER PHE CYS TYR MET HIS HIS MET GLU LEU PRO THR          
SEQRES  14 A  306  GLY VAL HIS ALA GLY THR ASP LEU GLU GLY ASN PHE TYR          
SEQRES  15 A  306  GLY PRO PHE VAL ASP ARG GLN THR ALA GLN ALA ALA GLY          
SEQRES  16 A  306  THR ASP THR THR ILE THR VAL ASN VAL LEU ALA TRP LEU          
SEQRES  17 A  306  TYR ALA ALA VAL ILE ASN GLY ASP ARG TRP PHE LEU ASN          
SEQRES  18 A  306  ARG PHE THR THR THR LEU ASN ASP PHE ASN LEU VAL ALA          
SEQRES  19 A  306  MET LYS TYR ASN TYR GLU PRO LEU THR GLN ASP HIS VAL          
SEQRES  20 A  306  ASP ILE LEU GLY PRO LEU SER ALA GLN THR GLY ILE ALA          
SEQRES  21 A  306  VAL LEU ASP MET CYS ALA SER LEU LYS GLU LEU LEU GLN          
SEQRES  22 A  306  ASN GLY MET ASN GLY ARG THR ILE LEU GLY SER ALA LEU          
SEQRES  23 A  306  LEU GLU ASP GLU PHE THR PRO PHE ASP VAL VAL ARG GLN          
SEQRES  24 A  306  CYS SER GLY VAL THR PHE GLN                                  
SEQRES   1 C    6  02J ALA VAL LEU PJE 010                                      
HET    02J  C   1       8                                                       
HET    PJE  C   5      13                                                       
HET    010  C   6       8                                                       
HETNAM     02J 5-METHYL-1,2-OXAZOLE-3-CARBOXYLIC ACID                           
HETNAM     PJE (E,4S)-4-AZANYL-5-[(3S)-2-OXIDANYLIDENEPYRROLIDIN-3-             
HETNAM   2 PJE  YL]PENT-2-ENOIC ACID                                            
HETNAM     010 PHENYLMETHANOL                                                   
FORMUL   2  02J    C5 H5 N O3                                                   
FORMUL   2  PJE    C9 H14 N2 O3                                                 
FORMUL   2  010    C7 H8 O                                                      
FORMUL   3  HOH   *158(H2 O)                                                    
HELIX    1 AA1 SER A   10  GLY A   15  1                                   6    
HELIX    2 AA2 HIS A   41  CYS A   44  5                                   4    
HELIX    3 AA3 THR A   45  MET A   49  5                                   5    
HELIX    4 AA4 ASN A   53  ARG A   60  1                                   8    
HELIX    5 AA5 SER A   62  HIS A   64  5                                   3    
HELIX    6 AA6 ILE A  200  ASN A  214  1                                  15    
HELIX    7 AA7 THR A  226  TYR A  237  1                                  12    
HELIX    8 AA8 THR A  243  LEU A  250  1                                   8    
HELIX    9 AA9 LEU A  250  GLY A  258  1                                   9    
HELIX   10 AB1 ALA A  260  GLY A  275  1                                  16    
HELIX   11 AB2 THR A  292  SER A  301  1                                  10    
SHEET    1 AA1 7 VAL A  73  LEU A  75  0                                        
SHEET    2 AA1 7 PHE A  66  ALA A  70 -1  N  VAL A  68   O  LEU A  75           
SHEET    3 AA1 7 MET A  17  CYS A  22 -1  N  THR A  21   O  LEU A  67           
SHEET    4 AA1 7 THR A  25  LEU A  32 -1  O  LEU A  27   N  VAL A  20           
SHEET    5 AA1 7 VAL A  35  PRO A  39 -1  O  VAL A  35   N  LEU A  32           
SHEET    6 AA1 7 VAL A  86  VAL A  91 -1  O  LEU A  89   N  VAL A  36           
SHEET    7 AA1 7 VAL A  77  GLN A  83 -1  N  ILE A  78   O  LYS A  90           
SHEET    1 AA2 5 LYS A 100  PHE A 103  0                                        
SHEET    2 AA2 5 CYS A 156  GLU A 166  1  O  VAL A 157   N  LYS A 100           
SHEET    3 AA2 5 VAL A 148  ASP A 153 -1  N  ASN A 151   O  SER A 158           
SHEET    4 AA2 5 THR A 111  TYR A 118 -1  N  SER A 113   O  PHE A 150           
SHEET    5 AA2 5 SER A 121  ALA A 129 -1  O  SER A 123   N  ALA A 116           
SHEET    1 AA3 3 LYS A 100  PHE A 103  0                                        
SHEET    2 AA3 3 CYS A 156  GLU A 166  1  O  VAL A 157   N  LYS A 100           
SHEET    3 AA3 3 HIS A 172  THR A 175 -1  O  ALA A 173   N  MET A 165           
LINK         SG  CYS A 145                 C20 PJE C   5     1555   1555  1.77  
LINK         C41 02J C   1                 N   ALA C   2     1555   1555  1.43  
LINK         C   LEU C   4                 N5  PJE C   5     1555   1555  1.43  
LINK         C22 PJE C   5                 O   010 C   6     1555   1555  1.38  
SITE     1 AC1 10 THR A  26  LEU A  27  PHE A 140  ASN A 142                    
SITE     2 AC1 10 GLY A 143  CYS A 145  HIS A 163  HIS A 164                    
SITE     3 AC1 10 GLU A 166  HIS A 172                                          
CRYST1   96.369   80.474   54.335  90.00 116.52  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010377  0.000000  0.005179        0.00000                         
SCALE2      0.000000  0.012426  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020569        0.00000                         
ATOM      1  N   SER A   1      -9.549  -4.665 -14.120  1.00 40.85           N  
ANISOU    1  N   SER A   1     5904   6429   3188   -934    116   -948       N  
ATOM      2  CA  SER A   1      -9.560  -5.744 -13.146  1.00 40.53           C  
ANISOU    2  CA  SER A   1     5619   6362   3418   -985    189  -1037       C  
ATOM      3  C   SER A   1      -8.257  -5.796 -12.355  1.00 40.78           C  
ANISOU    3  C   SER A   1     5632   6153   3709   -993    385  -1024       C  
ATOM      4  O   SER A   1      -7.444  -4.865 -12.400  1.00 39.06           O  
ANISOU    4  O   SER A   1     5559   5808   3476   -945    446   -938       O  
ATOM      5  CB  SER A   1      -9.812  -7.085 -13.826  1.00 43.77           C  
ANISOU    5  CB  SER A   1     5986   6851   3794  -1197    256  -1216       C  
ATOM      6  OG  SER A   1      -8.718  -7.428 -14.652  1.00 49.84           O  
ANISOU    6  OG  SER A   1     6922   7473   4540  -1353    470  -1303       O  
ATOM      7  N   GLY A   2      -8.069  -6.891 -11.630  1.00 36.58           N  
ANISOU    7  N   GLY A   2     4926   5563   3411  -1058    479  -1109       N  
ATOM      8  CA  GLY A   2      -6.981  -6.988 -10.680  1.00 37.58           C  
ANISOU    8  CA  GLY A   2     4985   5494   3802  -1030    616  -1084       C  
ATOM      9  C   GLY A   2      -7.459  -6.662  -9.277  1.00 36.21           C  
ANISOU    9  C   GLY A   2     4657   5337   3766   -880    497   -983       C  
ATOM     10  O   GLY A   2      -8.415  -5.903  -9.070  1.00 35.65           O  
ANISOU   10  O   GLY A   2     4574   5397   3575   -754    323   -901       O  
ATOM     11  N   PHE A   3      -6.770  -7.218  -8.279  1.00 36.96           N  
ANISOU   11  N   PHE A   3     4635   5296   4111   -881    591   -988       N  
ATOM     12  CA  PHE A   3      -7.144  -6.970  -6.891  1.00 34.23           C  
ANISOU   12  CA  PHE A   3     4160   4956   3892   -759    496   -898       C  
ATOM     13  C   PHE A   3      -5.881  -6.882  -6.053  1.00 36.25           C  
ANISOU   13  C   PHE A   3     4387   5029   4357   -735    598   -853       C  
ATOM     14  O   PHE A   3      -5.105  -7.841  -6.003  1.00 37.12           O  
ANISOU   14  O   PHE A   3     4444   5029   4631   -814    730   -923       O  
ATOM     15  CB  PHE A   3      -8.070  -8.060  -6.372  1.00 38.25           C  
ANISOU   15  CB  PHE A   3     4514   5553   4468   -805    455   -960       C  
ATOM     16  CG  PHE A   3      -8.896  -7.624  -5.206  1.00 37.05           C  
ANISOU   16  CG  PHE A   3     4248   5484   4344   -682    325   -875       C  
ATOM     17  CD1 PHE A   3      -9.981  -6.774  -5.390  1.00 35.02           C  
ANISOU   17  CD1 PHE A   3     3985   5407   3912   -576    170   -830       C  
ATOM     18  CD2 PHE A   3      -8.566  -8.029  -3.921  1.00 38.29           C  
ANISOU   18  CD2 PHE A   3     4311   5540   4699   -661    360   -838       C  
ATOM     19  CE1 PHE A   3     -10.742  -6.354  -4.300  1.00 43.61           C  
ANISOU   19  CE1 PHE A   3     4961   6575   5033   -453     73   -765       C  
ATOM     20  CE2 PHE A   3      -9.325  -7.615  -2.825  1.00 34.71           C  
ANISOU   20  CE2 PHE A   3     3766   5165   4258   -560    259   -768       C  
ATOM     21  CZ  PHE A   3     -10.408  -6.768  -3.017  1.00 38.50           C  
ANISOU   21  CZ  PHE A   3     4230   5826   4574   -456    126   -738       C  
ATOM     22  N   ARG A   4      -5.669  -5.730  -5.410  1.00 35.90           N  
ANISOU   22  N   ARG A   4     4379   4953   4307   -625    534   -740       N  
ATOM     23  CA  ARG A   4      -4.441  -5.465  -4.684  1.00 31.36           C  
ANISOU   23  CA  ARG A   4     3784   4231   3901   -617    612   -697       C  
ATOM     24  C   ARG A   4      -4.771  -5.052  -3.254  1.00 30.14           C  
ANISOU   24  C   ARG A   4     3550   4077   3823   -508    505   -604       C  
ATOM     25  O   ARG A   4      -5.863  -4.561  -2.961  1.00 32.53           O  
ANISOU   25  O   ARG A   4     3857   4484   4017   -417    383   -560       O  
ATOM     26  CB  ARG A   4      -3.625  -4.363  -5.351  1.00 34.56           C  
ANISOU   26  CB  ARG A   4     4351   4571   4209   -638    672   -664       C  
ATOM     27  CG  ARG A   4      -2.784  -4.842  -6.500  1.00 36.90           C  
ANISOU   27  CG  ARG A   4     4703   4817   4498   -771    839   -762       C  
ATOM     28  CD  ARG A   4      -1.507  -5.501  -6.011  1.00 43.74           C  
ANISOU   28  CD  ARG A   4     5438   5568   5614   -819    975   -806       C  
ATOM     29  NE  ARG A   4      -0.600  -5.788  -7.127  1.00 48.53           N  
ANISOU   29  NE  ARG A   4     6099   6125   6214   -939   1163   -907       N  
ATOM     30  CZ  ARG A   4       0.561  -6.424  -6.985  1.00 52.65           C  
ANISOU   30  CZ  ARG A   4     6498   6560   6947   -979   1310   -972       C  
ATOM     31  NH1 ARG A   4       0.941  -6.830  -5.774  1.00 48.63           N  
ANISOU   31  NH1 ARG A   4     5817   6002   6659   -904   1267   -932       N  
ATOM     32  NH2 ARG A   4       1.347  -6.651  -8.035  1.00 40.00           N  
ANISOU   32  NH2 ARG A   4     4943   4923   5331  -1086   1500  -1077       N  
ATOM     33  N   LYS A   5      -3.821  -5.263  -2.356  1.00 32.91           N  
ANISOU   33  N   LYS A   5     3824   4320   4360   -515    552   -580       N  
ATOM     34  CA  LYS A   5      -4.000  -4.743  -1.005  1.00 32.49           C  
ANISOU   34  CA  LYS A   5     3729   4260   4355   -428    457   -491       C  
ATOM     35  C   LYS A   5      -3.689  -3.259  -1.086  1.00 34.90           C  
ANISOU   35  C   LYS A   5     4178   4532   4550   -386    432   -427       C  
ATOM     36  O   LYS A   5      -2.534  -2.839  -1.112  1.00 43.67           O  
ANISOU   36  O   LYS A   5     5324   5550   5720   -442    504   -419       O  
ATOM     37  CB  LYS A   5      -3.120  -5.483  -0.007  1.00 41.16           C  
ANISOU   37  CB  LYS A   5     4706   5265   5668   -450    490   -479       C  
ATOM     38  CG  LYS A   5      -3.571  -5.281   1.437  1.00 44.71           C  
ANISOU   38  CG  LYS A   5     5109   5731   6147   -379    386   -401       C  
ATOM     39  CD  LYS A   5      -3.119  -6.438   2.307  1.00 48.37           C  
ANISOU   39  CD  LYS A   5     5455   6129   6794   -400    399   -393       C  
ATOM     40  CE  LYS A   5      -4.147  -7.542   2.353  1.00 51.96           C  
ANISOU   40  CE  LYS A   5     5862   6632   7248   -422    397   -431       C  
ATOM     41  NZ  LYS A   5      -3.671  -8.669   3.194  1.00 58.35           N  
ANISOU   41  NZ  LYS A   5     6599   7345   8228   -436    414   -409       N  
ATOM     42  N   MET A   6      -4.737  -2.465  -1.171  1.00 28.09           N  
ANISOU   42  N   MET A   6     3402   3747   3525   -289    336   -386       N  
ATOM     43  CA  MET A   6      -4.647  -1.063  -1.526  1.00 26.45           C  
ANISOU   43  CA  MET A   6     3383   3494   3171   -237    316   -327       C  
ATOM     44  C   MET A   6      -4.819  -0.182  -0.303  1.00 30.75           C  
ANISOU   44  C   MET A   6     3960   4001   3724   -141    246   -255       C  
ATOM     45  O   MET A   6      -5.743  -0.391   0.493  1.00 39.01           O  
ANISOU   45  O   MET A   6     4913   5127   4781    -52    168   -244       O  
ATOM     46  CB  MET A   6      -5.723  -0.763  -2.572  1.00 31.41           C  
ANISOU   46  CB  MET A   6     4107   4231   3598   -166    249   -328       C  
ATOM     47  CG  MET A   6      -5.849   0.624  -2.978  1.00 43.71           C  
ANISOU   47  CG  MET A   6     5885   5739   4985    -80    210   -254       C  
ATOM     48  SD  MET A   6      -7.003   0.609  -4.369  1.00 44.38           S  
ANISOU   48  SD  MET A   6     6044   5976   4843    -13    120   -265       S  
ATOM     49  CE  MET A   6      -6.246  -0.503  -5.547  1.00 40.04           C  
ANISOU   49  CE  MET A   6     5476   5428   4308   -224    253   -370       C  
ATOM     50  N   ALA A   7      -3.937   0.801  -0.164  1.00 30.67           N  
ANISOU   50  N   ALA A   7     4084   3870   3700   -176    286   -217       N  
ATOM     51  CA  ALA A   7      -4.036   1.777   0.908  1.00 34.48           C  
ANISOU   51  CA  ALA A   7     4645   4294   4164   -102    232   -159       C  
ATOM     52  C   ALA A   7      -4.709   3.037   0.389  1.00 35.32           C  
ANISOU   52  C   ALA A   7     4978   4368   4075     20    190   -107       C  
ATOM     53  O   ALA A   7      -4.744   3.310  -0.825  1.00 32.60           O  
ANISOU   53  O   ALA A   7     4764   4016   3607     12    213   -102       O  
ATOM     54  CB  ALA A   7      -2.654   2.133   1.454  1.00 30.36           C  
ANISOU   54  CB  ALA A   7     4141   3654   3739   -231    296   -155       C  
ATOM     55  N   PHE A   8      -5.232   3.825   1.331  1.00 28.73           N  
ANISOU   55  N   PHE A   8     4207   3504   3206    139    131    -66       N  
ATOM     56  CA  PHE A   8      -5.703   5.155   0.977  1.00 31.52           C  
ANISOU   56  CA  PHE A   8     4809   3776   3389    271    102     -9       C  
ATOM     57  C   PHE A   8      -4.533   6.064   0.596  1.00 34.10           C  
ANISOU   57  C   PHE A   8     5368   3922   3669    139    192     15       C  
ATOM     58  O   PHE A   8      -3.436   5.951   1.158  1.00 37.01           O  
ANISOU   58  O   PHE A   8     5686   4226   4150    -25    257    -12       O  
ATOM     59  CB  PHE A   8      -6.483   5.777   2.139  1.00 31.59           C  
ANISOU   59  CB  PHE A   8     4838   3779   3385    430     42     14       C  
ATOM     60  CG  PHE A   8      -7.820   5.150   2.342  1.00 32.80           C  
ANISOU   60  CG  PHE A   8     4802   4121   3542    580    -39     -7       C  
ATOM     61  CD1 PHE A   8      -8.850   5.415   1.454  1.00 39.90           C  
ANISOU   61  CD1 PHE A   8     5736   5112   4313    747   -111     13       C  
ATOM     62  CD2 PHE A   8      -8.038   4.252   3.375  1.00 38.42           C  
ANISOU   62  CD2 PHE A   8     5293   4927   4377    541    -44    -47       C  
ATOM     63  CE1 PHE A   8     -10.087   4.829   1.607  1.00 40.84           C  
ANISOU   63  CE1 PHE A   8     5647   5432   4437    867   -185    -19       C  
ATOM     64  CE2 PHE A   8      -9.286   3.659   3.543  1.00 40.49           C  
ANISOU   64  CE2 PHE A   8     5374   5372   4639    648   -100    -77       C  
ATOM     65  CZ  PHE A   8     -10.317   3.960   2.648  1.00 37.48           C  
ANISOU   65  CZ  PHE A   8     5003   5100   4138    809   -170    -69       C  
ATOM     66  N   PRO A   9      -4.733   6.967  -0.373  1.00 34.24           N  
ANISOU   66  N   PRO A   9     5639   3857   3512    200    196     65       N  
ATOM     67  CA  PRO A   9      -3.724   8.003  -0.625  1.00 28.45           C  
ANISOU   67  CA  PRO A   9     5170   2928   2710     70    291     93       C  
ATOM     68  C   PRO A   9      -3.452   8.766   0.653  1.00 36.92           C  
ANISOU   68  C   PRO A   9     6317   3884   3827     66    296     98       C  
ATOM     69  O   PRO A   9      -4.387   9.121   1.370  1.00 37.75           O  
ANISOU   69  O   PRO A   9     6437   4000   3907    255    219    119       O  
ATOM     70  CB  PRO A   9      -4.381   8.911  -1.669  1.00 33.00           C  
ANISOU   70  CB  PRO A   9     6038   3433   3068    211    258    170       C  
ATOM     71  CG  PRO A   9      -5.502   8.066  -2.267  1.00 38.83           C  
ANISOU   71  CG  PRO A   9     6603   4376   3772    359    151    164       C  
ATOM     72  CD  PRO A   9      -5.969   7.181  -1.145  1.00 41.48           C  
ANISOU   72  CD  PRO A   9     6628   4856   4278    405     99    108       C  
ATOM     73  N   SER A  10      -2.164   8.992   0.932  1.00 36.65           N  
ANISOU   73  N   SER A  10     6314   3752   3857   -161    391     67       N  
ATOM     74  CA  SER A  10      -1.704   9.366   2.275  1.00 33.54           C  
ANISOU   74  CA  SER A  10     5905   3297   3542   -229    389     45       C  
ATOM     75  C   SER A  10      -1.401  10.843   2.425  1.00 39.23           C  
ANISOU   75  C   SER A  10     6973   3800   4135   -271    443     73       C  
ATOM     76  O   SER A  10      -1.072  11.284   3.542  1.00 39.10           O  
ANISOU   76  O   SER A  10     6985   3719   4152   -335    441     48       O  
ATOM     77  CB  SER A  10      -0.459   8.563   2.646  1.00 33.64           C  
ANISOU   77  CB  SER A  10     5679   3376   3728   -457    437    -16       C  
ATOM     78  OG  SER A  10       0.631   8.820   1.770  1.00 36.85           O  
ANISOU   78  OG  SER A  10     6168   3716   4119   -661    556    -38       O  
ATOM     79  N   GLY A  11      -1.514  11.626   1.347  1.00 38.71           N  
ANISOU   79  N   GLY A  11     7193   3607   3908   -244    490    126       N  
ATOM     80  CA  GLY A  11      -1.086  13.023   1.402  1.00 42.82           C  
ANISOU   80  CA  GLY A  11     8082   3883   4302   -324    566    152       C  
ATOM     81  C   GLY A  11      -1.775  13.841   2.481  1.00 40.92           C  
ANISOU   81  C   GLY A  11     7993   3534   4020   -158    516    164       C  
ATOM     82  O   GLY A  11      -1.143  14.691   3.128  1.00 41.51           O  
ANISOU   82  O   GLY A  11     8257   3444   4070   -302    579    138       O  
ATOM     83  N   LYS A  12      -3.081  13.621   2.678  1.00 35.33           N  
ANISOU   83  N   LYS A  12     7207   2918   3300    139    411    193       N  
ATOM     84  CA  LYS A  12      -3.797  14.440   3.657  1.00 39.02           C  
ANISOU   84  CA  LYS A  12     7826   3277   3722    321    384    195       C  
ATOM     85  C   LYS A  12      -3.273  14.194   5.066  1.00 39.55           C  
ANISOU   85  C   LYS A  12     7740   3382   3904    170    393    116       C  
ATOM     86  O   LYS A  12      -3.349  15.092   5.909  1.00 43.34           O  
ANISOU   86  O   LYS A  12     8427   3708   4331    193    421     95       O  
ATOM     87  CB  LYS A  12      -5.303  14.166   3.612  1.00 38.71           C  
ANISOU   87  CB  LYS A  12     7673   3371   3664    665    277    226       C  
ATOM     88  CG  LYS A  12      -6.011  14.735   2.375  1.00 42.14           C  
ANISOU   88  CG  LYS A  12     8330   3738   3944    880    239    318       C  
ATOM     89  CD  LYS A  12      -7.517  14.648   2.523  1.00 49.08           C  
ANISOU   89  CD  LYS A  12     9091   4749   4807   1236    128    338       C  
ATOM     90  CE  LYS A  12      -8.213  15.484   1.462  1.00 54.84           C  
ANISOU   90  CE  LYS A  12    10097   5372   5365   1487     74    442       C  
ATOM     91  NZ  LYS A  12      -7.734  15.089   0.095  1.00 60.37           N  
ANISOU   91  NZ  LYS A  12    10833   6114   5991   1347     68    491       N  
ATOM     92  N   VAL A  13      -2.730  13.012   5.319  1.00 36.49           N  
ANISOU   92  N   VAL A  13     7015   3185   3664     18    368     73       N  
ATOM     93  CA  VAL A  13      -2.134  12.670   6.621  1.00 41.51           C  
ANISOU   93  CA  VAL A  13     7491   3876   4403   -138    354     11       C  
ATOM     94  C   VAL A  13      -0.678  13.100   6.682  1.00 41.79           C  
ANISOU   94  C   VAL A  13     7613   3812   4453   -452    429    -26       C  
ATOM     95  O   VAL A  13      -0.213  13.589   7.713  1.00 36.96           O  
ANISOU   95  O   VAL A  13     7074   3135   3836   -579    434    -71       O  
ATOM     96  CB  VAL A  13      -2.282  11.158   6.871  1.00 35.99           C  
ANISOU   96  CB  VAL A  13     6399   3422   3855   -127    282     -5       C  
ATOM     97  CG1 VAL A  13      -1.672  10.753   8.254  1.00 37.02           C  
ANISOU   97  CG1 VAL A  13     6371   3614   4080   -275    247    -51       C  
ATOM     98  CG2 VAL A  13      -3.733  10.764   6.779  1.00 40.20           C  
ANISOU   98  CG2 VAL A  13     6841   4067   4368    150    220     18       C  
ATOM     99  N   GLU A  14       0.046  12.965   5.558  1.00 39.92           N  
ANISOU   99  N   GLU A  14     7378   3568   4223   -592    494    -15       N  
ATOM    100  CA  GLU A  14       1.410  13.475   5.493  1.00 37.11           C  
ANISOU  100  CA  GLU A  14     7110   3121   3870   -902    586    -58       C  
ATOM    101  C   GLU A  14       1.484  14.928   5.935  1.00 39.77           C  
ANISOU  101  C   GLU A  14     7833   3213   4064   -963    644    -66       C  
ATOM    102  O   GLU A  14       2.452  15.339   6.593  1.00 46.22           O  
ANISOU  102  O   GLU A  14     8680   3984   4897  -1219    680   -128       O  
ATOM    103  CB  GLU A  14       1.957  13.334   4.067  1.00 38.67           C  
ANISOU  103  CB  GLU A  14     7333   3312   4048  -1011    680    -42       C  
ATOM    104  CG  GLU A  14       2.033  11.895   3.572  1.00 33.19           C  
ANISOU  104  CG  GLU A  14     6276   2839   3497   -985    649    -54       C  
ATOM    105  CD  GLU A  14       2.418  11.842   2.092  1.00 40.64           C  
ANISOU  105  CD  GLU A  14     7295   3762   4385  -1072    757    -43       C  
ATOM    106  OE1 GLU A  14       1.762  11.116   1.326  1.00 38.46           O  
ANISOU  106  OE1 GLU A  14     6926   3584   4104   -924    726    -17       O  
ATOM    107  OE2 GLU A  14       3.378  12.523   1.717  1.00 43.00           O  
ANISOU  107  OE2 GLU A  14     7751   3953   4636  -1307    877    -68       O  
ATOM    108  N   GLY A  15       0.492  15.739   5.547  1.00 41.49           N  
ANISOU  108  N   GLY A  15     8358   3268   4138   -734    655     -6       N  
ATOM    109  CA  GLY A  15       0.497  17.143   5.920  1.00 43.15           C  
ANISOU  109  CA  GLY A  15     8980   3208   4208   -765    724    -11       C  
ATOM    110  C   GLY A  15       0.440  17.391   7.413  1.00 43.36           C  
ANISOU  110  C   GLY A  15     8998   3221   4255   -789    688    -80       C  
ATOM    111  O   GLY A  15       0.670  18.524   7.842  1.00 42.31           O  
ANISOU  111  O   GLY A  15     9137   2926   4014   -868    750   -110       O  
ATOM    112  N   CYS A  16       0.178  16.356   8.197  1.00 40.19           N  
ANISOU  112  N   CYS A  16     8245   3049   3976   -725    587   -105       N  
ATOM    113  CA  CYS A  16      -0.110  16.472   9.616  1.00 46.48           C  
ANISOU  113  CA  CYS A  16     9027   3860   4773   -700    542   -161       C  
ATOM    114  C   CYS A  16       0.993  15.916  10.496  1.00 50.98           C  
ANISOU  114  C   CYS A  16     9360   4571   5440   -988    496   -226       C  
ATOM    115  O   CYS A  16       0.905  16.056  11.729  1.00 45.01           O  
ANISOU  115  O   CYS A  16     8617   3826   4661  -1018    457   -277       O  
ATOM    116  CB  CYS A  16      -1.417  15.723   9.924  1.00 40.83           C  
ANISOU  116  CB  CYS A  16     8112   3301   4101   -384    459   -133       C  
ATOM    117  SG  CYS A  16      -2.841  16.500   9.127  1.00 47.13           S  
ANISOU  117  SG  CYS A  16     9176   3954   4778     -2    486    -66       S  
ATOM    118  N   MET A  17       2.027  15.297   9.914  1.00 43.90           N  
ANISOU  118  N   MET A  17     8246   3788   4645  -1193    499   -229       N  
ATOM    119  CA  MET A  17       3.028  14.604  10.722  1.00 40.95           C  
ANISOU  119  CA  MET A  17     7583   3589   4387  -1418    426   -279       C  
ATOM    120  C   MET A  17       4.123  15.560  11.180  1.00 51.23           C  
ANISOU  120  C   MET A  17     9060   4780   5624  -1741    476   -354       C  
ATOM    121  O   MET A  17       4.678  16.325  10.384  1.00 50.40           O  
ANISOU  121  O   MET A  17     9130   4561   5458  -1876    586   -362       O  
ATOM    122  CB  MET A  17       3.652  13.435   9.965  1.00 40.26           C  
ANISOU  122  CB  MET A  17     7147   3691   4460  -1471    406   -259       C  
ATOM    123  CG  MET A  17       2.659  12.378   9.532  1.00 39.22           C  
ANISOU  123  CG  MET A  17     6822   3682   4397  -1197    355   -199       C  
ATOM    124  SD  MET A  17       1.618  11.791  10.880  1.00 39.92           S  
ANISOU  124  SD  MET A  17     6796   3877   4496   -998    236   -188       S  
ATOM    125  CE  MET A  17       2.850  11.149  12.040  1.00 44.93           C  
ANISOU  125  CE  MET A  17     7170   4661   5240  -1241    134   -226       C  
ATOM    126  N   VAL A  18       4.446  15.494  12.472  1.00 42.51           N  
ANISOU  126  N   VAL A  18     7877   3753   4521  -1858    389   -407       N  
ATOM    127  CA  VAL A  18       5.462  16.341  13.086  1.00 43.02           C  
ANISOU  127  CA  VAL A  18     8028   3800   4519  -2134    407   -478       C  
ATOM    128  C   VAL A  18       6.341  15.466  13.972  1.00 36.31           C  
ANISOU  128  C   VAL A  18     6828   3186   3783  -2308    265   -511       C  
ATOM    129  O   VAL A  18       6.030  14.315  14.250  1.00 39.43           O  
ANISOU  129  O   VAL A  18     6969   3729   4286  -2190    157   -473       O  
ATOM    130  CB  VAL A  18       4.865  17.493  13.923  1.00 51.14           C  
ANISOU  130  CB  VAL A  18     9399   4660   5370  -2078    446   -509       C  
ATOM    131  CG1 VAL A  18       4.044  18.454  13.064  1.00 51.99           C  
ANISOU  131  CG1 VAL A  18     9852   4539   5361  -1881    576   -465       C  
ATOM    132  CG2 VAL A  18       4.066  16.938  15.133  1.00 47.93           C  
ANISOU  132  CG2 VAL A  18     8962   4294   4955  -1963    339   -529       C  
ATOM    133  N   GLN A  19       7.428  16.052  14.450  1.00 51.38           N  
ANISOU  133  N   GLN A  19     8700   5165   5659  -2536    259   -566       N  
ATOM    134  CA  GLN A  19       8.349  15.400  15.365  1.00 49.50           C  
ANISOU  134  CA  GLN A  19     8147   5155   5506  -2692    110   -594       C  
ATOM    135  C   GLN A  19       8.132  15.988  16.754  1.00 39.84           C  
ANISOU  135  C   GLN A  19     7099   3902   4135  -2748     46   -635       C  
ATOM    136  O   GLN A  19       8.039  17.209  16.894  1.00 51.02           O  
ANISOU  136  O   GLN A  19     8826   5160   5400  -2803    150   -674       O  
ATOM    137  CB  GLN A  19       9.780  15.641  14.889  1.00 56.42           C  
ANISOU  137  CB  GLN A  19     8839   6145   6450  -2907    150   -635       C  
ATOM    138  CG  GLN A  19      10.823  14.731  15.459  1.00 66.37           C  
ANISOU  138  CG  GLN A  19     9688   7668   7860  -3012     -5   -648       C  
ATOM    139  CD  GLN A  19      12.170  14.920  14.778  1.00 74.67           C  
ANISOU  139  CD  GLN A  19    10546   8825   9002  -3186     60   -694       C  
ATOM    140  OE1 GLN A  19      13.090  14.122  14.959  1.00 77.89           O  
ANISOU  140  OE1 GLN A  19    10583   9444   9567  -3235    -45   -702       O  
ATOM    141  NE2 GLN A  19      12.289  15.981  13.985  1.00 76.84           N  
ANISOU  141  NE2 GLN A  19    11074   8949   9173  -3271    235   -724       N  
ATOM    142  N   VAL A  20       8.021  15.138  17.773  1.00 43.48           N  
ANISOU  142  N   VAL A  20     7385   4510   4627  -2731   -119   -623       N  
ATOM    143  CA  VAL A  20       7.939  15.595  19.160  1.00 43.60           C  
ANISOU  143  CA  VAL A  20     7538   4533   4494  -2809   -191   -665       C  
ATOM    144  C   VAL A  20       9.135  15.042  19.914  1.00 41.57           C  
ANISOU  144  C   VAL A  20     6962   4529   4304  -2985   -362   -672       C  
ATOM    145  O   VAL A  20       9.359  13.828  19.938  1.00 43.00           O  
ANISOU  145  O   VAL A  20     6824   4886   4629  -2927   -497   -617       O  
ATOM    146  CB  VAL A  20       6.637  15.153  19.855  1.00 44.76           C  
ANISOU  146  CB  VAL A  20     7811   4626   4570  -2620   -238   -645       C  
ATOM    147  CG1 VAL A  20       6.531  15.813  21.248  1.00 45.16           C  
ANISOU  147  CG1 VAL A  20     8060   4661   4437  -2708   -270   -699       C  
ATOM    148  CG2 VAL A  20       5.411  15.435  18.984  1.00 43.27           C  
ANISOU  148  CG2 VAL A  20     7862   4218   4359  -2385    -92   -629       C  
ATOM    149  N   THR A  21       9.872  15.925  20.579  1.00 49.24           N  
ANISOU  149  N   THR A  21     8025   5518   5167  -3185   -363   -736       N  
ATOM    150  CA  THR A  21      11.020  15.534  21.373  1.00 54.52           C  
ANISOU  150  CA  THR A  21     8414   6422   5878  -3348   -532   -749       C  
ATOM    151  C   THR A  21      10.789  15.999  22.797  1.00 53.12           C  
ANISOU  151  C   THR A  21     8431   6244   5509  -3428   -605   -782       C  
ATOM    152  O   THR A  21      10.429  17.157  23.023  1.00 58.68           O  
ANISOU  152  O   THR A  21     9478   6768   6049  -3490   -474   -840       O  
ATOM    153  CB  THR A  21      12.305  16.137  20.813  1.00 58.03           C  
ANISOU  153  CB  THR A  21     8748   6922   6376  -3552   -470   -808       C  
ATOM    154  OG1 THR A  21      12.521  15.605  19.501  1.00 51.07           O  
ANISOU  154  OG1 THR A  21     7674   6057   5675  -3471   -398   -777       O  
ATOM    155  CG2 THR A  21      13.484  15.785  21.686  1.00 58.31           C  
ANISOU  155  CG2 THR A  21     8495   7205   6454  -3708   -655   -830       C  
ATOM    156  N   CYS A  22      10.956  15.093  23.747  1.00 54.06           N  
ANISOU  156  N   CYS A  22     8347   6552   5642  -3413   -806   -739       N  
ATOM    157  CA  CYS A  22      10.970  15.465  25.155  1.00 55.25           C  
ANISOU  157  CA  CYS A  22     8640   6745   5608  -3523   -895   -768       C  
ATOM    158  C   CYS A  22      12.238  14.889  25.767  1.00 58.39           C  
ANISOU  158  C   CYS A  22     8701   7411   6075  -3650  -1106   -754       C  
ATOM    159  O   CYS A  22      12.436  13.670  25.766  1.00 63.22           O  
ANISOU  159  O   CYS A  22     9010   8186   6827  -3532  -1261   -670       O  
ATOM    160  CB  CYS A  22       9.710  14.963  25.867  1.00 49.92           C  
ANISOU  160  CB  CYS A  22     8116   6018   4831  -3353   -929   -722       C  
ATOM    161  SG  CYS A  22       9.666  15.347  27.621  1.00 62.99           S  
ANISOU  161  SG  CYS A  22     9959   7728   6248  -3482  -1023   -755       S  
ATOM    162  N   GLY A  23      13.107  15.763  26.252  1.00 61.61           N  
ANISOU  162  N   GLY A  23     9159   7858   6390  -3881  -1110   -833       N  
ATOM    163  CA  GLY A  23      14.393  15.306  26.747  1.00 69.61           C  
ANISOU  163  CA  GLY A  23     9841   9129   7479  -4002  -1308   -833       C  
ATOM    164  C   GLY A  23      15.182  14.651  25.633  1.00 65.90           C  
ANISOU  164  C   GLY A  23     9005   8769   7266  -3948  -1319   -813       C  
ATOM    165  O   GLY A  23      15.517  15.276  24.623  1.00 74.33           O  
ANISOU  165  O   GLY A  23    10098   9749   8397  -4024  -1153   -870       O  
ATOM    166  N   THR A  24      15.478  13.366  25.805  1.00 66.79           N  
ANISOU  166  N   THR A  24     8783   9067   7525  -3806  -1507   -729       N  
ATOM    167  CA  THR A  24      16.236  12.599  24.830  1.00 68.84           C  
ANISOU  167  CA  THR A  24     8667   9442   8048  -3724  -1525   -708       C  
ATOM    168  C   THR A  24      15.348  11.696  23.983  1.00 64.08           C  
ANISOU  168  C   THR A  24     8018   8757   7573  -3478  -1463   -622       C  
ATOM    169  O   THR A  24      15.864  10.923  23.168  1.00 69.07           O  
ANISOU  169  O   THR A  24     8342   9474   8428  -3379  -1469   -597       O  
ATOM    170  CB  THR A  24      17.303  11.763  25.539  1.00 75.41           C  
ANISOU  170  CB  THR A  24     9131  10539   8982  -3716  -1776   -678       C  
ATOM    171  OG1 THR A  24      17.853  10.811  24.624  1.00 90.20           O  
ANISOU  171  OG1 THR A  24    10638  12508  11126  -3570  -1792   -646       O  
ATOM    172  CG2 THR A  24      16.692  11.017  26.713  1.00 70.83           C  
ANISOU  172  CG2 THR A  24     8607  10018   8286  -3591  -1964   -577       C  
ATOM    173  N   THR A  25      14.031  11.768  24.153  1.00 62.92           N  
ANISOU  173  N   THR A  25     8165   8447   7293  -3378  -1397   -583       N  
ATOM    174  CA  THR A  25      13.113  10.865  23.468  1.00 63.24           C  
ANISOU  174  CA  THR A  25     8167   8422   7438  -3154  -1359   -499       C  
ATOM    175  C   THR A  25      12.435  11.598  22.319  1.00 55.93           C  
ANISOU  175  C   THR A  25     7473   7275   6502  -3141  -1117   -545       C  
ATOM    176  O   THR A  25      11.850  12.665  22.512  1.00 54.12           O  
ANISOU  176  O   THR A  25     7595   6874   6092  -3212   -997   -601       O  
ATOM    177  CB  THR A  25      12.073  10.308  24.443  1.00 63.12           C  
ANISOU  177  CB  THR A  25     8298   8394   7292  -3034  -1466   -418       C  
ATOM    178  OG1 THR A  25      12.745   9.619  25.507  1.00 64.35           O  
ANISOU  178  OG1 THR A  25     8257   8751   7444  -3038  -1696   -359       O  
ATOM    179  CG2 THR A  25      11.116   9.346  23.736  1.00 55.14           C  
ANISOU  179  CG2 THR A  25     7239   7322   6391  -2816  -1432   -332       C  
ATOM    180  N   THR A  26      12.510  11.030  21.123  1.00 56.26           N  
ANISOU  180  N   THR A  26     7331   7312   6732  -3039  -1039   -520       N  
ATOM    181  CA  THR A  26      11.891  11.632  19.953  1.00 51.64           C  
ANISOU  181  CA  THR A  26     6956   6526   6138  -3009   -818   -549       C  
ATOM    182  C   THR A  26      10.941  10.620  19.331  1.00 42.88           C  
ANISOU  182  C   THR A  26     5786   5378   5128  -2794   -806   -469       C  
ATOM    183  O   THR A  26      11.288   9.442  19.219  1.00 48.17           O  
ANISOU  183  O   THR A  26     6136   6199   5969  -2695   -913   -405       O  
ATOM    184  CB  THR A  26      12.955  12.070  18.947  1.00 56.46           C  
ANISOU  184  CB  THR A  26     7435   7157   6859  -3128   -699   -609       C  
ATOM    185  OG1 THR A  26      13.691  13.171  19.489  1.00 63.35           O  
ANISOU  185  OG1 THR A  26     8427   8034   7609  -3348   -685   -691       O  
ATOM    186  CG2 THR A  26      12.321  12.492  17.647  1.00 55.21           C  
ANISOU  186  CG2 THR A  26     7474   6806   6698  -3066   -485   -614       C  
ATOM    187  N   LEU A  27       9.730  11.057  18.985  1.00 45.18           N  
ANISOU  187  N   LEU A  27     6386   5467   5311  -2708   -683   -470       N  
ATOM    188  CA  LEU A  27       8.807  10.211  18.222  1.00 46.44           C  
ANISOU  188  CA  LEU A  27     6491   5586   5569  -2453   -627   -394       C  
ATOM    189  C   LEU A  27       7.944  11.109  17.336  1.00 34.25           C  
ANISOU  189  C   LEU A  27     5264   3814   3934  -2372   -425   -421       C  
ATOM    190  O   LEU A  27       8.208  12.302  17.198  1.00 39.74           O  
ANISOU  190  O   LEU A  27     6209   4373   4517  -2554   -329   -498       O  
ATOM    191  CB  LEU A  27       7.958   9.319  19.140  1.00 49.46           C  
ANISOU  191  CB  LEU A  27     6837   6032   5925  -2249   -745   -310       C  
ATOM    192  CG  LEU A  27       7.400   9.879  20.452  1.00 41.73           C  
ANISOU  192  CG  LEU A  27     6111   5010   4734  -2293   -801   -333       C  
ATOM    193  CD1 LEU A  27       6.405  10.991  20.201  1.00 42.95           C  
ANISOU  193  CD1 LEU A  27     6636   4944   4739  -2234   -624   -390       C  
ATOM    194  CD2 LEU A  27       6.747   8.756  21.240  1.00 39.02           C  
ANISOU  194  CD2 LEU A  27     5665   4765   4397  -2112   -916   -237       C  
ATOM    195  N   ASN A  28       6.896  10.535  16.738  1.00 40.57           N  
ANISOU  195  N   ASN A  28     6066   4573   4778  -2098   -364   -355       N  
ATOM    196  CA  ASN A  28       6.035  11.281  15.827  1.00 38.62           C  
ANISOU  196  CA  ASN A  28     6088   4133   4453  -1979   -198   -363       C  
ATOM    197  C   ASN A  28       4.785  11.790  16.526  1.00 36.83           C  
ANISOU  197  C   ASN A  28     6132   3792   4068  -1822   -176   -363       C  
ATOM    198  O   ASN A  28       4.256  11.151  17.436  1.00 36.78           O  
ANISOU  198  O   ASN A  28     6048   3879   4049  -1719   -268   -331       O  
ATOM    199  CB  ASN A  28       5.589  10.413  14.646  1.00 36.48           C  
ANISOU  199  CB  ASN A  28     5656   3894   4310  -1776   -142   -302       C  
ATOM    200  CG  ASN A  28       6.738   9.730  13.977  1.00 42.08           C  
ANISOU  200  CG  ASN A  28     6068   4728   5192  -1891   -151   -307       C  
ATOM    201  OD1 ASN A  28       7.467  10.352  13.210  1.00 39.19           O  
ANISOU  201  OD1 ASN A  28     5752   4307   4830  -2058    -50   -356       O  
ATOM    202  ND2 ASN A  28       6.925   8.443  14.274  1.00 39.61           N  
ANISOU  202  ND2 ASN A  28     5450   4577   5024  -1804   -262   -258       N  
ATOM    203  N   GLY A  29       4.278  12.918  16.035  1.00 39.12           N  
ANISOU  203  N   GLY A  29     6746   3876   4241  -1788    -42   -396       N  
ATOM    204  CA  GLY A  29       3.014  13.443  16.493  1.00 42.95           C  
ANISOU  204  CA  GLY A  29     7483   4241   4596  -1590      7   -401       C  
ATOM    205  C   GLY A  29       2.139  13.830  15.320  1.00 40.27           C  
ANISOU  205  C   GLY A  29     7297   3764   4240  -1369    126   -367       C  
ATOM    206  O   GLY A  29       2.601  13.993  14.190  1.00 39.82           O  
ANISOU  206  O   GLY A  29     7249   3655   4226  -1422    190   -352       O  
ATOM    207  N   LEU A  30       0.854  13.978  15.620  1.00 41.61           N  
ANISOU  207  N   LEU A  30     7586   3885   4338  -1119    155   -358       N  
ATOM    208  CA  LEU A  30      -0.181  14.308  14.650  1.00 45.58           C  
ANISOU  208  CA  LEU A  30     8218   4285   4814   -856    238   -320       C  
ATOM    209  C   LEU A  30      -0.668  15.723  14.935  1.00 45.88           C  
ANISOU  209  C   LEU A  30     8661   4078   4693   -794    337   -369       C  
ATOM    210  O   LEU A  30      -1.274  15.972  15.982  1.00 42.49           O  
ANISOU  210  O   LEU A  30     8325   3632   4188   -719    342   -415       O  
ATOM    211  CB  LEU A  30      -1.333  13.307  14.736  1.00 41.56           C  
ANISOU  211  CB  LEU A  30     7487   3937   4365   -597    192   -276       C  
ATOM    212  CG  LEU A  30      -2.404  13.511  13.663  1.00 39.46           C  
ANISOU  212  CG  LEU A  30     7291   3620   4083   -320    247   -234       C  
ATOM    213  CD1 LEU A  30      -1.810  13.124  12.302  1.00 43.51           C  
ANISOU  213  CD1 LEU A  30     7701   4157   4674   -381    249   -184       C  
ATOM    214  CD2 LEU A  30      -3.627  12.688  13.977  1.00 31.08           C  
ANISOU  214  CD2 LEU A  30     6030   2720   3057    -89    212   -218       C  
ATOM    215  N   TRP A  31      -0.428  16.643  13.993  1.00 39.51           N  
ANISOU  215  N   TRP A  31     8111   3070   3829   -818    427   -359       N  
ATOM    216  CA  TRP A  31      -0.723  18.058  14.175  1.00 39.44           C  
ANISOU  216  CA  TRP A  31     8536   2781   3670   -782    533   -402       C  
ATOM    217  C   TRP A  31      -2.022  18.408  13.452  1.00 50.29           C  
ANISOU  217  C   TRP A  31    10048   4054   5004   -406    579   -344       C  
ATOM    218  O   TRP A  31      -2.059  18.457  12.217  1.00 46.99           O  
ANISOU  218  O   TRP A  31     9667   3591   4597   -329    597   -272       O  
ATOM    219  CB  TRP A  31       0.445  18.895  13.665  1.00 43.90           C  
ANISOU  219  CB  TRP A  31     9278   3218   4185  -1064    602   -413       C  
ATOM    220  CG  TRP A  31       0.304  20.388  13.788  1.00 48.03           C  
ANISOU  220  CG  TRP A  31    10140   3553   4554  -1034    710   -416       C  
ATOM    221  CD1 TRP A  31      -0.442  21.094  14.692  1.00 46.49           C  
ANISOU  221  CD1 TRP A  31    10140   3260   4266   -894    750   -452       C  
ATOM    222  CD2 TRP A  31       0.944  21.355  12.952  1.00 52.77           C  
ANISOU  222  CD2 TRP A  31    10936   4041   5074  -1157    802   -387       C  
ATOM    223  NE1 TRP A  31      -0.299  22.448  14.464  1.00 49.05           N  
ANISOU  223  NE1 TRP A  31    10772   3403   4462   -919    857   -440       N  
ATOM    224  CE2 TRP A  31       0.550  22.629  13.402  1.00 51.95           C  
ANISOU  224  CE2 TRP A  31    11154   3758   4828  -1084    889   -401       C  
ATOM    225  CE3 TRP A  31       1.822  21.261  11.869  1.00 52.03           C  
ANISOU  225  CE3 TRP A  31    10779   3982   5009  -1327    831   -356       C  
ATOM    226  CZ2 TRP A  31       1.003  23.800  12.802  1.00 56.32           C  
ANISOU  226  CZ2 TRP A  31    11983   4158   5260  -1179    996   -383       C  
ATOM    227  CZ3 TRP A  31       2.265  22.419  11.273  1.00 52.73           C  
ANISOU  227  CZ3 TRP A  31    11134   3929   4971  -1422    941   -345       C  
ATOM    228  CH2 TRP A  31       1.858  23.672  11.740  1.00 54.93           C  
ANISOU  228  CH2 TRP A  31    11747   4022   5102  -1351   1019   -357       C  
ATOM    229  N   LEU A  32      -3.086  18.642  14.222  1.00 46.25           N  
ANISOU  229  N   LEU A  32     9608   3523   4444   -172    597   -378       N  
ATOM    230  CA  LEU A  32      -4.405  18.959  13.688  1.00 46.54           C  
ANISOU  230  CA  LEU A  32     9733   3498   4453    217    628   -334       C  
ATOM    231  C   LEU A  32      -4.882  20.223  14.373  1.00 51.88           C  
ANISOU  231  C   LEU A  32    10712   3989   5011    322    722   -375       C  
ATOM    232  O   LEU A  32      -4.874  20.297  15.613  1.00 51.86           O  
ANISOU  232  O   LEU A  32    10720   4007   4976    234    743   -460       O  
ATOM    233  CB  LEU A  32      -5.405  17.815  13.917  1.00 46.04           C  
ANISOU  233  CB  LEU A  32     9293   3718   4482    434    553   -316       C  
ATOM    234  CG  LEU A  32      -5.155  16.446  13.285  1.00 45.05           C  
ANISOU  234  CG  LEU A  32     8777   3852   4488    368    453   -255       C  
ATOM    235  CD1 LEU A  32      -6.059  15.404  13.894  1.00 40.01           C  
ANISOU  235  CD1 LEU A  32     7821   3462   3919    509    401   -267       C  
ATOM    236  CD2 LEU A  32      -5.313  16.477  11.741  1.00 41.64           C  
ANISOU  236  CD2 LEU A  32     8366   3391   4064    492    442   -168       C  
ATOM    237  N   ASP A  33      -5.268  21.227  13.574  1.00 45.28           N  
ANISOU  237  N   ASP A  33    10091   3010   4103    493    774   -303       N  
ATOM    238  CA  ASP A  33      -5.615  22.552  14.093  1.00 53.87           C  
ANISOU  238  CA  ASP A  33    11460   3930   5080    574    868   -320       C  
ATOM    239  C   ASP A  33      -4.429  23.002  14.946  1.00 55.87           C  
ANISOU  239  C   ASP A  33    11834   4117   5276    188    913   -391       C  
ATOM    240  O   ASP A  33      -3.277  22.872  14.507  1.00 52.79           O  
ANISOU  240  O   ASP A  33    11425   3739   4895   -106    896   -381       O  
ATOM    241  CB  ASP A  33      -6.967  22.511  14.806  1.00 59.46           C  
ANISOU  241  CB  ASP A  33    12093   4697   5804    901    883   -359       C  
ATOM    242  CG  ASP A  33      -8.115  22.121  13.876  1.00 67.97           C  
ANISOU  242  CG  ASP A  33    13016   5875   6934   1277    825   -286       C  
ATOM    243  OD1 ASP A  33      -8.197  22.669  12.751  1.00 64.70           O  
ANISOU  243  OD1 ASP A  33    12736   5374   6473   1386    814   -194       O  
ATOM    244  OD2 ASP A  33      -8.945  21.280  14.273  1.00 65.94           O  
ANISOU  244  OD2 ASP A  33    12501   5801   6752   1456    791   -324       O  
ATOM    245  N   ASP A  34      -4.639  23.485  16.170  1.00 54.49           N  
ANISOU  245  N   ASP A  34    11758   3898   5047    164    967   -470       N  
ATOM    246  CA  ASP A  34      -3.520  23.914  16.990  1.00 54.34           C  
ANISOU  246  CA  ASP A  34    11845   3839   4964   -207    996   -538       C  
ATOM    247  C   ASP A  34      -3.169  22.901  18.076  1.00 53.82           C  
ANISOU  247  C   ASP A  34    11545   3959   4947   -393    917   -618       C  
ATOM    248  O   ASP A  34      -2.777  23.297  19.182  1.00 51.81           O  
ANISOU  248  O   ASP A  34    11379   3688   4617   -587    943   -693       O  
ATOM    249  CB  ASP A  34      -3.819  25.283  17.599  1.00 56.48           C  
ANISOU  249  CB  ASP A  34    12440   3910   5111   -162   1116   -572       C  
ATOM    250  CG  ASP A  34      -4.974  25.246  18.587  1.00 57.63           C  
ANISOU  250  CG  ASP A  34    12560   4077   5259     85   1150   -632       C  
ATOM    251  OD1 ASP A  34      -5.751  24.261  18.559  1.00 56.50           O  
ANISOU  251  OD1 ASP A  34    12165   4095   5208    294   1090   -629       O  
ATOM    252  OD2 ASP A  34      -5.096  26.196  19.404  1.00 61.11           O  
ANISOU  252  OD2 ASP A  34    13230   4381   5608     59   1246   -690       O  
ATOM    253  N   VAL A  35      -3.317  21.607  17.802  1.00 49.15           N  
ANISOU  253  N   VAL A  35    10667   3544   4463   -339    820   -605       N  
ATOM    254  CA  VAL A  35      -2.989  20.566  18.776  1.00 49.07           C  
ANISOU  254  CA  VAL A  35    10439   3722   4485   -511    730   -673       C  
ATOM    255  C   VAL A  35      -2.133  19.490  18.122  1.00 52.04           C  
ANISOU  255  C   VAL A  35    10567   4237   4969   -691    618   -640       C  
ATOM    256  O   VAL A  35      -2.395  19.068  16.988  1.00 47.40           O  
ANISOU  256  O   VAL A  35     9890   3658   4463   -541    605   -573       O  
ATOM    257  CB  VAL A  35      -4.252  19.930  19.389  1.00 48.83           C  
ANISOU  257  CB  VAL A  35    10292   3797   4464   -236    735   -712       C  
ATOM    258  CG1 VAL A  35      -3.868  18.779  20.329  1.00 51.74           C  
ANISOU  258  CG1 VAL A  35    10434   4382   4842   -430    632   -762       C  
ATOM    259  CG2 VAL A  35      -5.036  20.967  20.153  1.00 50.28           C  
ANISOU  259  CG2 VAL A  35    10689   3860   4556    -83    852   -757       C  
ATOM    260  N   VAL A  36      -1.132  19.021  18.868  1.00 43.62           N  
ANISOU  260  N   VAL A  36     9371   3297   3907  -1006    531   -683       N  
ATOM    261  CA  VAL A  36      -0.310  17.882  18.476  1.00 41.65           C  
ANISOU  261  CA  VAL A  36     8778   3257   3789  -1165    405   -632       C  
ATOM    262  C   VAL A  36      -0.616  16.721  19.419  1.00 40.84           C  
ANISOU  262  C   VAL A  36     8376   3410   3731  -1127    295   -616       C  
ATOM    263  O   VAL A  36      -0.544  16.862  20.648  1.00 43.28           O  
ANISOU  263  O   VAL A  36     8765   3741   3937  -1245    271   -684       O  
ATOM    264  CB  VAL A  36       1.185  18.232  18.488  1.00 45.35           C  
ANISOU  264  CB  VAL A  36     9255   3723   4252  -1540    375   -662       C  
ATOM    265  CG1 VAL A  36       2.031  16.992  18.198  1.00 41.10           C  
ANISOU  265  CG1 VAL A  36     8320   3426   3869  -1679    242   -614       C  
ATOM    266  CG2 VAL A  36       1.477  19.366  17.501  1.00 49.00           C  
ANISOU  266  CG2 VAL A  36     9927   4013   4675  -1549    500   -628       C  
ATOM    267  N   TYR A  37      -0.998  15.592  18.841  1.00 36.61           N  
ANISOU  267  N   TYR A  37     7524   3053   3331   -967    235   -529       N  
ATOM    268  CA  TYR A  37      -1.281  14.347  19.546  1.00 36.16           C  
ANISOU  268  CA  TYR A  37     7175   3232   3334   -930    135   -492       C  
ATOM    269  C   TYR A  37      -0.073  13.423  19.436  1.00 42.85           C  
ANISOU  269  C   TYR A  37     7739   4242   4300  -1144      2   -443       C  
ATOM    270  O   TYR A  37       0.461  13.235  18.337  1.00 44.39           O  
ANISOU  270  O   TYR A  37     7823   4439   4603  -1170      3   -404       O  
ATOM    271  CB  TYR A  37      -2.528  13.666  18.935  1.00 37.72           C  
ANISOU  271  CB  TYR A  37     7209   3514   3609   -617    164   -435       C  
ATOM    272  CG  TYR A  37      -3.751  14.558  18.928  1.00 39.73           C  
ANISOU  272  CG  TYR A  37     7697   3628   3769   -363    290   -480       C  
ATOM    273  CD1 TYR A  37      -3.907  15.547  17.965  1.00 41.35           C  
ANISOU  273  CD1 TYR A  37     8130   3635   3948   -250    373   -478       C  
ATOM    274  CD2 TYR A  37      -4.740  14.433  19.906  1.00 37.90           C  
ANISOU  274  CD2 TYR A  37     7468   3460   3471   -232    331   -524       C  
ATOM    275  CE1 TYR A  37      -5.008  16.386  17.973  1.00 46.06           C  
ANISOU  275  CE1 TYR A  37     8942   4094   4465     15    479   -514       C  
ATOM    276  CE2 TYR A  37      -5.843  15.275  19.926  1.00 42.07           C  
ANISOU  276  CE2 TYR A  37     8193   3867   3926     20    454   -577       C  
ATOM    277  CZ  TYR A  37      -5.973  16.244  18.964  1.00 40.09           C  
ANISOU  277  CZ  TYR A  37     8156   3416   3662    156    520   -570       C  
ATOM    278  OH  TYR A  37      -7.057  17.100  18.965  1.00 46.08           O  
ANISOU  278  OH  TYR A  37     9110   4042   4355    441    635   -615       O  
ATOM    279  N   CYS A  38       0.344  12.807  20.545  1.00 36.64           N  
ANISOU  279  N   CYS A  38     6829   3599   3494  -1281   -113   -442       N  
ATOM    280  CA  CYS A  38       1.433  11.839  20.448  1.00 34.66           C  
ANISOU  280  CA  CYS A  38     6281   3514   3374  -1433   -251   -385       C  
ATOM    281  C   CYS A  38       1.345  10.853  21.605  1.00 36.89           C  
ANISOU  281  C   CYS A  38     6411   3966   3640  -1448   -377   -344       C  
ATOM    282  O   CYS A  38       0.582  11.075  22.551  1.00 38.13           O  
ANISOU  282  O   CYS A  38     6723   4105   3659  -1400   -347   -377       O  
ATOM    283  CB  CYS A  38       2.802  12.533  20.413  1.00 34.00           C  
ANISOU  283  CB  CYS A  38     6254   3391   3275  -1726   -286   -439       C  
ATOM    284  SG  CYS A  38       3.281  13.279  21.966  1.00 43.50           S  
ANISOU  284  SG  CYS A  38     7668   4580   4279  -1980   -353   -530       S  
ATOM    285  N   PRO A  39       2.084   9.736  21.548  1.00 35.36           N  
ANISOU  285  N   PRO A  39     5925   3930   3581  -1501   -511   -268       N  
ATOM    286  CA  PRO A  39       2.046   8.772  22.658  1.00 32.33           C  
ANISOU  286  CA  PRO A  39     5424   3690   3170  -1514   -642   -209       C  
ATOM    287  C   PRO A  39       2.657   9.388  23.894  1.00 32.58           C  
ANISOU  287  C   PRO A  39     5609   3737   3033  -1738   -732   -263       C  
ATOM    288  O   PRO A  39       3.676  10.069  23.816  1.00 37.58           O  
ANISOU  288  O   PRO A  39     6275   4350   3654  -1940   -772   -317       O  
ATOM    289  CB  PRO A  39       2.891   7.604  22.159  1.00 38.34           C  
ANISOU  289  CB  PRO A  39     5860   4580   4128  -1521   -760   -122       C  
ATOM    290  CG  PRO A  39       2.779   7.709  20.612  1.00 34.68           C  
ANISOU  290  CG  PRO A  39     5332   4042   3801  -1415   -636   -131       C  
ATOM    291  CD  PRO A  39       2.730   9.159  20.346  1.00 35.76           C  
ANISOU  291  CD  PRO A  39     5739   4024   3824  -1487   -521   -223       C  
ATOM    292  N   ARG A  40       2.074   9.067  25.048  1.00 34.89           N  
ANISOU  292  N   ARG A  40     5983   4083   3192  -1721   -771   -247       N  
ATOM    293  CA  ARG A  40       2.573   9.707  26.262  1.00 37.53           C  
ANISOU  293  CA  ARG A  40     6500   4429   3330  -1942   -852   -309       C  
ATOM    294  C   ARG A  40       3.949   9.194  26.670  1.00 42.06           C  
ANISOU  294  C   ARG A  40     6874   5160   3946  -2138  -1080   -257       C  
ATOM    295  O   ARG A  40       4.659   9.889  27.416  1.00 44.40           O  
ANISOU  295  O   ARG A  40     7294   5476   4100  -2372  -1163   -325       O  
ATOM    296  CB  ARG A  40       1.558   9.520  27.390  1.00 35.76           C  
ANISOU  296  CB  ARG A  40     6436   4223   2930  -1881   -816   -313       C  
ATOM    297  CG  ARG A  40       1.330   8.103  27.813  1.00 37.87           C  
ANISOU  297  CG  ARG A  40     6510   4634   3245  -1798   -923   -185       C  
ATOM    298  CD  ARG A  40       0.378   8.054  29.021  1.00 38.62           C  
ANISOU  298  CD  ARG A  40     6802   4743   3127  -1789   -868   -205       C  
ATOM    299  NE  ARG A  40       0.078   6.680  29.410  1.00 38.42           N  
ANISOU  299  NE  ARG A  40     6626   4836   3136  -1717   -949    -76       N  
ATOM    300  CZ  ARG A  40      -0.568   6.350  30.527  1.00 42.12           C  
ANISOU  300  CZ  ARG A  40     7230   5351   3423  -1743   -934    -61       C  
ATOM    301  NH1 ARG A  40      -0.965   7.305  31.369  1.00 45.29           N  
ANISOU  301  NH1 ARG A  40     7908   5701   3600  -1833   -840   -177       N  
ATOM    302  NH2 ARG A  40      -0.757   5.078  30.842  1.00 37.67           N  
ANISOU  302  NH2 ARG A  40     6547   4876   2889  -1696  -1010     68       N  
ATOM    303  N   HIS A  41       4.346   7.999  26.227  1.00 42.28           N  
ANISOU  303  N   HIS A  41     6597   5304   4162  -2047  -1186   -143       N  
ATOM    304  CA  HIS A  41       5.660   7.505  26.633  1.00 44.81           C  
ANISOU  304  CA  HIS A  41     6706   5784   4535  -2200  -1414    -90       C  
ATOM    305  C   HIS A  41       6.809   8.329  26.050  1.00 47.76           C  
ANISOU  305  C   HIS A  41     7016   6160   4972  -2397  -1426   -176       C  
ATOM    306  O   HIS A  41       7.974   8.012  26.325  1.00 49.19           O  
ANISOU  306  O   HIS A  41     6986   6496   5209  -2534  -1614   -150       O  
ATOM    307  CB  HIS A  41       5.807   6.012  26.294  1.00 42.46           C  
ANISOU  307  CB  HIS A  41     6110   5589   4434  -2030  -1513     51       C  
ATOM    308  CG  HIS A  41       5.889   5.706  24.830  1.00 47.15           C  
ANISOU  308  CG  HIS A  41     6513   6138   5263  -1900  -1403     57       C  
ATOM    309  ND1 HIS A  41       4.880   5.056  24.156  1.00 42.47           N  
ANISOU  309  ND1 HIS A  41     5894   5482   4759  -1681  -1275    100       N  
ATOM    310  CD2 HIS A  41       6.865   5.934  23.919  1.00 48.51           C  
ANISOU  310  CD2 HIS A  41     6511   6332   5590  -1974  -1398     18       C  
ATOM    311  CE1 HIS A  41       5.223   4.909  22.886  1.00 42.92           C  
ANISOU  311  CE1 HIS A  41     5787   5516   5005  -1622  -1201     90       C  
ATOM    312  NE2 HIS A  41       6.423   5.432  22.718  1.00 43.27           N  
ANISOU  312  NE2 HIS A  41     5740   5607   5093  -1795  -1265     41       N  
ATOM    313  N   VAL A  42       6.519   9.393  25.292  1.00 45.26           N  
ANISOU  313  N   VAL A  42     6880   5678   4637  -2421  -1233   -278       N  
ATOM    314  CA  VAL A  42       7.553  10.375  24.971  1.00 41.74           C  
ANISOU  314  CA  VAL A  42     6462   5212   4186  -2671  -1224   -379       C  
ATOM    315  C   VAL A  42       8.125  11.033  26.223  1.00 41.69           C  
ANISOU  315  C   VAL A  42     6565   5267   4008  -2840  -1294   -421       C  
ATOM    316  O   VAL A  42       9.258  11.515  26.185  1.00 46.59           O  
ANISOU  316  O   VAL A  42     7078   5958   4667  -2994  -1321   -462       O  
ATOM    317  CB  VAL A  42       7.027  11.445  23.990  1.00 43.47           C  
ANISOU  317  CB  VAL A  42     6921   5204   4390  -2642   -984   -464       C  
ATOM    318  CG1 VAL A  42       6.085  12.421  24.675  1.00 51.02           C  
ANISOU  318  CG1 VAL A  42     8273   5990   5121  -2638   -867   -544       C  
ATOM    319  CG2 VAL A  42       8.181  12.195  23.350  1.00 41.32           C  
ANISOU  319  CG2 VAL A  42     6581   4929   4188  -2813   -926   -521       C  
ATOM    320  N   ILE A  43       7.393  11.045  27.342  1.00 46.52           N  
ANISOU  320  N   ILE A  43     7381   5865   4428  -2822  -1322   -418       N  
ATOM    321  CA  ILE A  43       7.959  11.637  28.561  1.00 45.16           C  
ANISOU  321  CA  ILE A  43     7313   5757   4088  -2995  -1391   -455       C  
ATOM    322  C   ILE A  43       8.743  10.618  29.381  1.00 52.28           C  
ANISOU  322  C   ILE A  43     7956   6891   5019  -3013  -1640   -350       C  
ATOM    323  O   ILE A  43       9.119  10.894  30.534  1.00 57.56           O  
ANISOU  323  O   ILE A  43     8703   7634   5531  -3138  -1731   -361       O  
ATOM    324  CB  ILE A  43       6.888  12.279  29.465  1.00 49.61           C  
ANISOU  324  CB  ILE A  43     8243   6190   4417  -2986  -1277   -515       C  
ATOM    325  CG1 ILE A  43       6.001  11.214  30.107  1.00 50.70           C  
ANISOU  325  CG1 ILE A  43     8377   6393   4493  -2840  -1350   -427       C  
ATOM    326  CG2 ILE A  43       6.118  13.371  28.754  1.00 45.28           C  
ANISOU  326  CG2 ILE A  43     7974   5397   3834  -2935  -1029   -619       C  
ATOM    327  CD1 ILE A  43       4.881  11.786  30.945  1.00 45.41           C  
ANISOU  327  CD1 ILE A  43     8043   5604   3607  -2808  -1205   -496       C  
ATOM    328  N   CYS A  44       8.998   9.448  28.819  1.00 47.50           N  
ANISOU  328  N   CYS A  44     7050   6391   4607  -2880  -1749   -245       N  
ATOM    329  CA  CYS A  44       9.758   8.406  29.492  1.00 54.21           C  
ANISOU  329  CA  CYS A  44     7645   7441   5511  -2847  -1983   -131       C  
ATOM    330  C   CYS A  44      11.210   8.408  29.034  1.00 66.33           C  
ANISOU  330  C   CYS A  44     8867   9111   7222  -2920  -2069   -151       C  
ATOM    331  O   CYS A  44      11.524   8.736  27.886  1.00 70.85           O  
ANISOU  331  O   CYS A  44     9336   9635   7948  -2932  -1950   -211       O  
ATOM    332  CB  CYS A  44       9.163   7.031  29.213  1.00 55.62           C  
ANISOU  332  CB  CYS A  44     7685   7644   5805  -2628  -2048      7       C  
ATOM    333  SG  CYS A  44       7.546   6.758  29.912  1.00 62.57           S  
ANISOU  333  SG  CYS A  44     8876   8421   6478  -2535  -1979     44       S  
ATOM    334  N   THR A  45      12.095   8.034  29.947  1.00 71.19           N  
ANISOU  334  N   THR A  45     9336   9902   7811  -2966  -2273   -104       N  
ATOM    335  CA  THR A  45      13.424   7.579  29.582  1.00 80.44           C  
ANISOU  335  CA  THR A  45    10135  11243   9184  -2956  -2399    -93       C  
ATOM    336  C   THR A  45      13.397   6.054  29.557  1.00 85.17           C  
ANISOU  336  C   THR A  45    10506  11924   9930  -2716  -2543     64       C  
ATOM    337  O   THR A  45      12.384   5.434  29.874  1.00 84.16           O  
ANISOU  337  O   THR A  45    10526  11723   9729  -2592  -2546    161       O  
ATOM    338  CB  THR A  45      14.480   8.124  30.547  1.00 88.05           C  
ANISOU  338  CB  THR A  45    11060  12356  10041  -3144  -2542   -150       C  
ATOM    339  OG1 THR A  45      15.721   7.444  30.323  1.00 96.71           O  
ANISOU  339  OG1 THR A  45    11763  13643  11341  -3086  -2700   -126       O  
ATOM    340  CG2 THR A  45      14.037   7.920  31.985  1.00 82.83           C  
ANISOU  340  CG2 THR A  45    10602  11726   9142  -3159  -2674    -80       C  
ATOM    341  N   SER A  46      14.522   5.436  29.187  1.00 94.20           N  
ANISOU  341  N   SER A  46    11293  13215  11284  -2644  -2654     83       N  
ATOM    342  CA  SER A  46      14.505   3.999  28.920  1.00 99.19           C  
ANISOU  342  CA  SER A  46    11709  13886  12092  -2389  -2747    224       C  
ATOM    343  C   SER A  46      14.329   3.179  30.195  1.00102.67           C  
ANISOU  343  C   SER A  46    12223  14389  12398  -2297  -2950    367       C  
ATOM    344  O   SER A  46      13.799   2.061  30.145  1.00103.71           O  
ANISOU  344  O   SER A  46    12336  14474  12596  -2093  -2986    504       O  
ATOM    345  CB  SER A  46      15.772   3.581  28.180  1.00101.15           C  
ANISOU  345  CB  SER A  46    11560  14269  12603  -2321  -2791    188       C  
ATOM    346  OG  SER A  46      15.547   3.569  26.774  1.00102.90           O  
ANISOU  346  OG  SER A  46    11694  14391  13013  -2265  -2591    140       O  
ATOM    347  N   GLU A  47      14.772   3.699  31.345  1.00103.15           N  
ANISOU  347  N   GLU A  47    12380  14547  12265  -2448  -3080    340       N  
ATOM    348  CA  GLU A  47      14.582   2.992  32.611  1.00105.09           C  
ANISOU  348  CA  GLU A  47    12736  14845  12350  -2381  -3264    475       C  
ATOM    349  C   GLU A  47      13.343   3.444  33.372  1.00 96.49           C  
ANISOU  349  C   GLU A  47    12048  13625  10990  -2475  -3173    482       C  
ATOM    350  O   GLU A  47      13.101   2.957  34.482  1.00 95.28           O  
ANISOU  350  O   GLU A  47    12033  13500  10669  -2450  -3297    583       O  
ATOM    351  CB  GLU A  47      15.808   3.122  33.517  1.00113.73           C  
ANISOU  351  CB  GLU A  47    13687  16143  13383  -2469  -3488    457       C  
ATOM    352  CG  GLU A  47      17.142   2.961  32.819  1.00122.79           C  
ANISOU  352  CG  GLU A  47    14432  17444  14780  -2424  -3562    396       C  
ATOM    353  CD  GLU A  47      17.577   4.220  32.109  1.00128.75           C  
ANISOU  353  CD  GLU A  47    15147  18193  15580  -2643  -3407    205       C  
ATOM    354  OE1 GLU A  47      18.526   4.153  31.301  1.00131.56           O  
ANISOU  354  OE1 GLU A  47    15183  18642  16161  -2617  -3401    133       O  
ATOM    355  OE2 GLU A  47      16.973   5.282  32.372  1.00129.79           O  
ANISOU  355  OE2 GLU A  47    15579  18217  15517  -2841  -3280    124       O  
ATOM    356  N   ASP A  48      12.572   4.374  32.820  1.00 88.47           N  
ANISOU  356  N   ASP A  48    11228  12466   9921  -2578  -2952    369       N  
ATOM    357  CA  ASP A  48      11.222   4.609  33.299  1.00 82.99           C  
ANISOU  357  CA  ASP A  48    10884  11629   9018  -2599  -2826    374       C  
ATOM    358  C   ASP A  48      10.226   3.652  32.666  1.00 74.58           C  
ANISOU  358  C   ASP A  48     9820  10460   8056  -2396  -2749    474       C  
ATOM    359  O   ASP A  48       9.049   3.676  33.028  1.00 73.52           O  
ANISOU  359  O   ASP A  48     9949  10222   7764  -2387  -2643    482       O  
ATOM    360  CB  ASP A  48      10.796   6.051  33.017  1.00 78.97           C  
ANISOU  360  CB  ASP A  48    10605  11002   8400  -2776  -2618    202       C  
ATOM    361  CG  ASP A  48      10.907   6.943  34.238  1.00 95.25           C  
ANISOU  361  CG  ASP A  48    12905  13084  10203  -2978  -2640    128       C  
ATOM    362  OD1 ASP A  48      11.161   8.150  34.041  1.00101.10           O  
ANISOU  362  OD1 ASP A  48    13744  13774  10895  -3149  -2527    -15       O  
ATOM    363  OD2 ASP A  48      10.746   6.447  35.381  1.00 97.57           O  
ANISOU  363  OD2 ASP A  48    13299  13436  10339  -2970  -2761    214       O  
ATOM    364  N   MET A  49      10.680   2.793  31.755  1.00 70.02           N  
ANISOU  364  N   MET A  49     8953   9914   7738  -2234  -2792    542       N  
ATOM    365  CA  MET A  49       9.786   2.097  30.840  1.00 61.63           C  
ANISOU  365  CA  MET A  49     7871   8737   6807  -2069  -2679    598       C  
ATOM    366  C   MET A  49       9.232   0.785  31.390  1.00 63.88           C  
ANISOU  366  C   MET A  49     8200   9003   7070  -1904  -2767    772       C  
ATOM    367  O   MET A  49       8.262   0.262  30.824  1.00 55.94           O  
ANISOU  367  O   MET A  49     7247   7894   6115  -1795  -2661    814       O  
ATOM    368  CB  MET A  49      10.512   1.850  29.508  1.00 58.06           C  
ANISOU  368  CB  MET A  49     7099   8306   6653  -1982  -2645    572       C  
ATOM    369  CG  MET A  49      10.737   3.117  28.678  1.00 59.51           C  
ANISOU  369  CG  MET A  49     7290   8453   6867  -2138  -2487    400       C  
ATOM    370  SD  MET A  49      10.885   2.806  26.896  1.00 70.61           S  
ANISOU  370  SD  MET A  49     8441   9804   8583  -2023  -2341    368       S  
ATOM    371  CE  MET A  49      10.667   4.454  26.204  1.00 66.43           C  
ANISOU  371  CE  MET A  49     8106   9165   7971  -2232  -2122    181       C  
ATOM    372  N   LEU A  50       9.797   0.239  32.474  1.00 68.71           N  
ANISOU  372  N   LEU A  50     8805   9706   7597  -1887  -2954    873       N  
ATOM    373  CA  LEU A  50       9.264  -1.017  33.000  1.00 63.93           C  
ANISOU  373  CA  LEU A  50     8277   9055   6959  -1736  -3021   1045       C  
ATOM    374  C   LEU A  50       7.957  -0.789  33.743  1.00 58.18           C  
ANISOU  374  C   LEU A  50     7900   8239   5968  -1819  -2904   1041       C  
ATOM    375  O   LEU A  50       7.050  -1.627  33.688  1.00 56.04           O  
ANISOU  375  O   LEU A  50     7724   7878   5690  -1713  -2840   1134       O  
ATOM    376  CB  LEU A  50      10.285  -1.707  33.913  1.00 71.06           C  
ANISOU  376  CB  LEU A  50     9077  10074   7849  -1677  -3259   1159       C  
ATOM    377  CG  LEU A  50       9.920  -3.093  34.483  1.00 69.00           C  
ANISOU  377  CG  LEU A  50     8899   9754   7565  -1510  -3345   1352       C  
ATOM    378  CD1 LEU A  50       9.049  -3.046  35.742  1.00 80.10           C  
ANISOU  378  CD1 LEU A  50    10653  11119   8662  -1617  -3328   1396       C  
ATOM    379  CD2 LEU A  50       9.241  -3.966  33.412  1.00 66.20           C  
ANISOU  379  CD2 LEU A  50     8480   9262   7412  -1336  -3220   1414       C  
ATOM    380  N   ASN A  51       7.853   0.320  34.474  1.00 73.80           N  
ANISOU  380  N   ASN A  51    10073  10241   7725  -2009  -2863    927       N  
ATOM    381  CA  ASN A  51       6.661   0.613  35.271  1.00 77.26           C  
ANISOU  381  CA  ASN A  51    10844  10605   7906  -2090  -2729    899       C  
ATOM    382  C   ASN A  51       6.593   2.112  35.528  1.00 71.78           C  
ANISOU  382  C   ASN A  51    10315   9902   7055  -2284  -2618    716       C  
ATOM    383  O   ASN A  51       6.774   2.577  36.658  1.00 79.82           O  
ANISOU  383  O   ASN A  51    11496  10964   7869  -2419  -2665    688       O  
ATOM    384  CB  ASN A  51       6.673  -0.174  36.580  1.00 86.08           C  
ANISOU  384  CB  ASN A  51    12089  11758   8858  -2084  -2859   1035       C  
ATOM    385  CG  ASN A  51       5.309  -0.227  37.221  1.00 90.93           C  
ANISOU  385  CG  ASN A  51    13007  12285   9256  -2124  -2686   1028       C  
ATOM    386  OD1 ASN A  51       5.167  -0.030  38.423  1.00 95.59           O  
ANISOU  386  OD1 ASN A  51    13802  12898   9619  -2234  -2704   1028       O  
ATOM    387  ND2 ASN A  51       4.281  -0.469  36.404  1.00 93.50           N  
ANISOU  387  ND2 ASN A  51    13357  12519   9652  -2037  -2506   1012       N  
ATOM    388  N   PRO A  52       6.327   2.898  34.494  1.00 62.23           N  
ANISOU  388  N   PRO A  52     9087   8625   5935  -2301  -2463    588       N  
ATOM    389  CA  PRO A  52       6.243   4.347  34.682  1.00 57.81           C  
ANISOU  389  CA  PRO A  52     8713   8019   5235  -2471  -2335    412       C  
ATOM    390  C   PRO A  52       4.964   4.730  35.401  1.00 57.62           C  
ANISOU  390  C   PRO A  52     9013   7902   4976  -2503  -2155    351       C  
ATOM    391  O   PRO A  52       3.932   4.066  35.283  1.00 55.60           O  
ANISOU  391  O   PRO A  52     8822   7599   4705  -2385  -2058    402       O  
ATOM    392  CB  PRO A  52       6.250   4.889  33.248  1.00 53.57           C  
ANISOU  392  CB  PRO A  52     8064   7411   4881  -2441  -2214    314       C  
ATOM    393  CG  PRO A  52       5.633   3.800  32.456  1.00 54.07           C  
ANISOU  393  CG  PRO A  52     8005   7445   5095  -2252  -2196    415       C  
ATOM    394  CD  PRO A  52       5.984   2.498  33.121  1.00 56.29           C  
ANISOU  394  CD  PRO A  52     8175   7813   5401  -2161  -2382    596       C  
ATOM    395  N   ASN A  53       5.044   5.810  36.174  1.00 52.13           N  
ANISOU  395  N   ASN A  53     8519   7187   4100  -2666  -2097    234       N  
ATOM    396  CA  ASN A  53       3.847   6.501  36.629  1.00 48.83           C  
ANISOU  396  CA  ASN A  53     8402   6656   3496  -2690  -1865    121       C  
ATOM    397  C   ASN A  53       3.772   7.768  35.796  1.00 49.38           C  
ANISOU  397  C   ASN A  53     8543   6608   3612  -2727  -1698    -45       C  
ATOM    398  O   ASN A  53       4.476   8.743  36.069  1.00 52.52           O  
ANISOU  398  O   ASN A  53     9005   6995   3957  -2884  -1710   -134       O  
ATOM    399  CB  ASN A  53       3.863   6.833  38.123  1.00 55.79           C  
ANISOU  399  CB  ASN A  53     9496   7567   4135  -2836  -1886    102       C  
ATOM    400  CG  ASN A  53       2.524   7.341  38.575  1.00 58.74           C  
ANISOU  400  CG  ASN A  53    10145   7827   4345  -2820  -1629     -5       C  
ATOM    401  OD1 ASN A  53       2.159   8.482  38.293  1.00 61.69           O  
ANISOU  401  OD1 ASN A  53    10662   8086   4690  -2847  -1445   -161       O  
ATOM    402  ND2 ASN A  53       1.743   6.474  39.205  1.00 69.75           N  
ANISOU  402  ND2 ASN A  53    11608   9245   5648  -2759  -1596     76       N  
ATOM    403  N   TYR A  54       2.936   7.737  34.759  1.00 50.53           N  
ANISOU  403  N   TYR A  54     8682   6661   3856  -2581  -1543    -83       N  
ATOM    404  CA  TYR A  54       2.929   8.823  33.794  1.00 49.17           C  
ANISOU  404  CA  TYR A  54     8563   6361   3757  -2587  -1399   -219       C  
ATOM    405  C   TYR A  54       2.476  10.132  34.426  1.00 54.74           C  
ANISOU  405  C   TYR A  54     9572   6938   4287  -2670  -1213   -370       C  
ATOM    406  O   TYR A  54       2.980  11.204  34.074  1.00 47.41           O  
ANISOU  406  O   TYR A  54     8714   5921   3380  -2765  -1155   -468       O  
ATOM    407  CB  TYR A  54       2.045   8.442  32.623  1.00 51.20           C  
ANISOU  407  CB  TYR A  54     8765   6552   4135  -2397  -1281   -222       C  
ATOM    408  CG  TYR A  54       2.681   7.429  31.722  1.00 50.03           C  
ANISOU  408  CG  TYR A  54     8280   6486   4242  -2304  -1419    -92       C  
ATOM    409  CD1 TYR A  54       3.622   7.821  30.787  1.00 45.35           C  
ANISOU  409  CD1 TYR A  54     7530   5881   3819  -2354  -1462   -121       C  
ATOM    410  CD2 TYR A  54       2.351   6.073  31.807  1.00 46.45           C  
ANISOU  410  CD2 TYR A  54     7670   6110   3869  -2164  -1482     58       C  
ATOM    411  CE1 TYR A  54       4.196   6.907  29.923  1.00 48.10           C  
ANISOU  411  CE1 TYR A  54     7560   6297   4419  -2251  -1554    -14       C  
ATOM    412  CE2 TYR A  54       2.932   5.144  30.946  1.00 46.74           C  
ANISOU  412  CE2 TYR A  54     7403   6197   4158  -2057  -1583    169       C  
ATOM    413  CZ  TYR A  54       3.860   5.575  30.006  1.00 47.01           C  
ANISOU  413  CZ  TYR A  54     7272   6225   4365  -2095  -1616    128       C  
ATOM    414  OH  TYR A  54       4.451   4.685  29.129  1.00 47.43           O  
ANISOU  414  OH  TYR A  54     7024   6326   4671  -1987  -1693    220       O  
ATOM    415  N   GLU A  55       1.534  10.070  35.370  1.00 54.37           N  
ANISOU  415  N   GLU A  55     9709   6875   4073  -2638  -1104   -389       N  
ATOM    416  CA  GLU A  55       1.112  11.295  36.040  1.00 62.82           C  
ANISOU  416  CA  GLU A  55    11059   7820   4988  -2707   -923   -533       C  
ATOM    417  C   GLU A  55       2.284  11.956  36.756  1.00 59.30           C  
ANISOU  417  C   GLU A  55    10660   7412   4459  -2945  -1049   -557       C  
ATOM    418  O   GLU A  55       2.440  13.180  36.698  1.00 55.16           O  
ANISOU  418  O   GLU A  55    10302   6760   3897  -3031   -931   -678       O  
ATOM    419  CB  GLU A  55      -0.024  11.002  37.015  1.00 72.38           C  
ANISOU  419  CB  GLU A  55    12423   9036   6043  -2645   -793   -546       C  
ATOM    420  CG  GLU A  55      -1.373  11.550  36.562  1.00 82.66           C  
ANISOU  420  CG  GLU A  55    13857  10198   7351  -2451   -508   -664       C  
ATOM    421  CD  GLU A  55      -2.475  11.277  37.571  1.00 95.57           C  
ANISOU  421  CD  GLU A  55    15614  11859   8839  -2402   -362   -689       C  
ATOM    422  OE1 GLU A  55      -2.698  12.129  38.467  1.00 92.70           O  
ANISOU  422  OE1 GLU A  55    15462  11424   8335  -2481   -248   -793       O  
ATOM    423  OE2 GLU A  55      -3.119  10.209  37.464  1.00102.39           O  
ANISOU  423  OE2 GLU A  55    16359  12814   9728  -2293   -353   -607       O  
ATOM    424  N   ASP A  56       3.148  11.151  37.380  1.00 53.63           N  
ANISOU  424  N   ASP A  56     9787   6867   3721  -3046  -1291   -438       N  
ATOM    425  CA  ASP A  56       4.321  11.683  38.071  1.00 64.16           C  
ANISOU  425  CA  ASP A  56    11127   8275   4974  -3269  -1435   -456       C  
ATOM    426  C   ASP A  56       5.312  12.279  37.088  1.00 65.11           C  
ANISOU  426  C   ASP A  56    11107   8383   5248  -3341  -1475   -498       C  
ATOM    427  O   ASP A  56       5.848  13.373  37.312  1.00 59.51           O  
ANISOU  427  O   ASP A  56    10522   7622   4467  -3514  -1430   -601       O  
ATOM    428  CB  ASP A  56       5.001  10.575  38.863  1.00 72.42           C  
ANISOU  428  CB  ASP A  56    12012   9519   5986  -3311  -1697   -304       C  
ATOM    429  CG  ASP A  56       4.603  10.565  40.300  1.00 73.16           C  
ANISOU  429  CG  ASP A  56    12321   9635   5843  -3400  -1689   -306       C  
ATOM    430  OD1 ASP A  56       3.879  11.486  40.725  1.00 73.67           O  
ANISOU  430  OD1 ASP A  56    12650   9570   5771  -3446  -1480   -437       O  
ATOM    431  OD2 ASP A  56       5.023   9.622  40.998  1.00 82.19           O  
ANISOU  431  OD2 ASP A  56    13370  10920   6938  -3414  -1892   -173       O  
ATOM    432  N   LEU A  57       5.598  11.546  36.011  1.00 54.56           N  
ANISOU  432  N   LEU A  57     9509   7099   4122  -3223  -1555   -419       N  
ATOM    433  CA  LEU A  57       6.520  12.035  34.997  1.00 58.95           C  
ANISOU  433  CA  LEU A  57     9910   7649   4841  -3287  -1574   -459       C  
ATOM    434  C   LEU A  57       6.023  13.327  34.370  1.00 53.37           C  
ANISOU  434  C   LEU A  57     9436   6722   4118  -3297  -1323   -601       C  
ATOM    435  O   LEU A  57       6.827  14.223  34.089  1.00 55.74           O  
ANISOU  435  O   LEU A  57     9752   6988   4438  -3450  -1300   -674       O  
ATOM    436  CB  LEU A  57       6.723  10.963  33.922  1.00 58.03           C  
ANISOU  436  CB  LEU A  57     9484   7607   4957  -3132  -1670   -353       C  
ATOM    437  CG  LEU A  57       7.311   9.674  34.486  1.00 58.53           C  
ANISOU  437  CG  LEU A  57     9307   7870   5060  -3094  -1922   -197       C  
ATOM    438  CD1 LEU A  57       7.210   8.550  33.466  1.00 54.66           C  
ANISOU  438  CD1 LEU A  57     8560   7416   4793  -2903  -1976    -89       C  
ATOM    439  CD2 LEU A  57       8.749   9.911  34.929  1.00 65.58           C  
ANISOU  439  CD2 LEU A  57    10043   8914   5959  -3265  -2104   -200       C  
ATOM    440  N   LEU A  58       4.704  13.454  34.184  1.00 51.29           N  
ANISOU  440  N   LEU A  58     9364   6308   3817  -3131  -1129   -642       N  
ATOM    441  CA  LEU A  58       4.135  14.604  33.491  1.00 50.54           C  
ANISOU  441  CA  LEU A  58     9488   5986   3730  -3077   -889   -760       C  
ATOM    442  C   LEU A  58       4.023  15.829  34.392  1.00 53.70           C  
ANISOU  442  C   LEU A  58    10192   6265   3945  -3210   -760   -873       C  
ATOM    443  O   LEU A  58       4.262  16.949  33.933  1.00 54.22           O  
ANISOU  443  O   LEU A  58    10404   6178   4020  -3275   -634   -957       O  
ATOM    444  CB  LEU A  58       2.764  14.249  32.911  1.00 51.45           C  
ANISOU  444  CB  LEU A  58     9661   6000   3889  -2814   -735   -763       C  
ATOM    445  CG  LEU A  58       2.219  15.349  32.004  1.00 54.82           C  
ANISOU  445  CG  LEU A  58    10279   6189   4360  -2706   -507   -862       C  
ATOM    446  CD1 LEU A  58       3.267  15.734  30.975  1.00 58.84           C  
ANISOU  446  CD1 LEU A  58    10675   6672   5007  -2810   -550   -857       C  
ATOM    447  CD2 LEU A  58       0.939  14.917  31.307  1.00 50.39           C  
ANISOU  447  CD2 LEU A  58     9723   5561   3863  -2422   -377   -860       C  
ATOM    448  N   ILE A  59       3.644  15.646  35.662  1.00 54.74           N  
ANISOU  448  N   ILE A  59    10438   6453   3908  -3252   -778   -874       N  
ATOM    449  CA  ILE A  59       3.618  16.788  36.576  1.00 57.67           C  
ANISOU  449  CA  ILE A  59    11093   6717   4100  -3401   -665   -985       C  
ATOM    450  C   ILE A  59       4.998  17.404  36.712  1.00 65.52           C  
ANISOU  450  C   ILE A  59    12051   7771   5072  -3667   -782  -1009       C  
ATOM    451  O   ILE A  59       5.129  18.569  37.124  1.00 62.39           O  
ANISOU  451  O   ILE A  59    11895   7250   4559  -3810   -665  -1114       O  
ATOM    452  CB  ILE A  59       3.052  16.380  37.958  1.00 59.05           C  
ANISOU  452  CB  ILE A  59    11377   6967   4093  -3421   -678   -977       C  
ATOM    453  CG1 ILE A  59       2.718  17.618  38.790  1.00 71.73           C  
ANISOU  453  CG1 ILE A  59    13311   8418   5524  -3526   -501  -1111       C  
ATOM    454  CG2 ILE A  59       4.046  15.545  38.733  1.00 60.28           C  
ANISOU  454  CG2 ILE A  59    11351   7358   4193  -3584   -955   -872       C  
ATOM    455  CD1 ILE A  59       1.376  18.224  38.482  1.00 74.63           C  
ANISOU  455  CD1 ILE A  59    13880   8571   5903  -3304   -220  -1204       C  
ATOM    456  N   ARG A  60       6.045  16.656  36.398  1.00 59.52           N  
ANISOU  456  N   ARG A  60    10988   7205   4422  -3736  -1005   -919       N  
ATOM    457  CA  ARG A  60       7.389  17.199  36.496  1.00 61.90           C  
ANISOU  457  CA  ARG A  60    11212   7595   4714  -3983  -1117   -950       C  
ATOM    458  C   ARG A  60       7.845  17.871  35.215  1.00 61.22           C  
ANISOU  458  C   ARG A  60    11082   7402   4776  -4000  -1018   -996       C  
ATOM    459  O   ARG A  60       9.000  18.292  35.137  1.00 63.13           O  
ANISOU  459  O   ARG A  60    11225   7728   5035  -4203  -1097  -1026       O  
ATOM    460  CB  ARG A  60       8.378  16.103  36.888  1.00 62.45           C  
ANISOU  460  CB  ARG A  60    10958   7942   4829  -4044  -1413   -838       C  
ATOM    461  CG  ARG A  60       8.064  15.489  38.234  1.00 63.73           C  
ANISOU  461  CG  ARG A  60    11186   8211   4819  -4056  -1525   -782       C  
ATOM    462  CD  ARG A  60       8.800  14.192  38.427  1.00 63.68           C  
ANISOU  462  CD  ARG A  60    10854   8447   4893  -4018  -1807   -637       C  
ATOM    463  NE  ARG A  60       8.498  13.606  39.722  1.00 75.44           N  
ANISOU  463  NE  ARG A  60    12434  10027   6204  -4031  -1912   -572       N  
ATOM    464  CZ  ARG A  60       8.630  12.321  40.017  1.00 78.43           C  
ANISOU  464  CZ  ARG A  60    12620  10558   6620  -3922  -2109   -421       C  
ATOM    465  NH1 ARG A  60       9.041  11.454  39.095  1.00 80.96           N  
ANISOU  465  NH1 ARG A  60    12635  10961   7164  -3779  -2222   -323       N  
ATOM    466  NH2 ARG A  60       8.330  11.905  41.236  1.00 74.59           N  
ANISOU  466  NH2 ARG A  60    12264  10131   5946  -3953  -2181   -368       N  
ATOM    467  N   LYS A  61       6.981  17.973  34.205  1.00 58.75           N  
ANISOU  467  N   LYS A  61    10838   6916   4568  -3795   -846  -1002       N  
ATOM    468  CA  LYS A  61       7.309  18.671  32.974  1.00 58.25           C  
ANISOU  468  CA  LYS A  61    10783   6723   4628  -3801   -727  -1040       C  
ATOM    469  C   LYS A  61       6.509  19.961  32.853  1.00 59.14           C  
ANISOU  469  C   LYS A  61    11273   6548   4648  -3755   -464  -1137       C  
ATOM    470  O   LYS A  61       5.403  20.077  33.387  1.00 58.99           O  
ANISOU  470  O   LYS A  61    11458   6418   4537  -3615   -350  -1164       O  
ATOM    471  CB  LYS A  61       7.019  17.805  31.740  1.00 56.30           C  
ANISOU  471  CB  LYS A  61    10315   6490   4587  -3590   -741   -963       C  
ATOM    472  CG  LYS A  61       7.667  16.427  31.725  1.00 60.01           C  
ANISOU  472  CG  LYS A  61    10403   7219   5181  -3575   -985   -853       C  
ATOM    473  CD  LYS A  61       9.176  16.525  31.561  1.00 71.47           C  
ANISOU  473  CD  LYS A  61    11618   8828   6709  -3782  -1120   -856       C  
ATOM    474  CE  LYS A  61       9.762  15.202  31.101  1.00 75.88           C  
ANISOU  474  CE  LYS A  61    11773   9596   7462  -3695  -1316   -747       C  
ATOM    475  NZ  LYS A  61       9.182  14.049  31.840  1.00 79.06           N  
ANISOU  475  NZ  LYS A  61    12106  10105   7827  -3556  -1454   -645       N  
ATOM    476  N   SER A  62       7.060  20.900  32.086  1.00 60.14           N  
ANISOU  476  N   SER A  62    11482   6554   4813  -3856   -360  -1183       N  
ATOM    477  CA  SER A  62       6.422  22.146  31.683  1.00 61.02           C  
ANISOU  477  CA  SER A  62    11938   6374   4874  -3790   -111  -1252       C  
ATOM    478  C   SER A  62       6.346  22.211  30.159  1.00 59.09           C  
ANISOU  478  C   SER A  62    11638   6021   4793  -3647    -23  -1212       C  
ATOM    479  O   SER A  62       6.955  21.400  29.456  1.00 64.87           O  
ANISOU  479  O   SER A  62    12067   6909   5673  -3653   -148  -1151       O  
ATOM    480  CB  SER A  62       7.214  23.344  32.185  1.00 76.02           C  
ANISOU  480  CB  SER A  62    14040   8210   6635  -4074    -54  -1339       C  
ATOM    481  OG  SER A  62       8.511  23.258  31.635  1.00 78.65           O  
ANISOU  481  OG  SER A  62    14140   8690   7051  -4272   -163  -1326       O  
ATOM    482  N   ASN A  63       5.627  23.222  29.654  1.00 59.62           N  
ANISOU  482  N   ASN A  63    12008   5815   4831  -3517    194  -1246       N  
ATOM    483  CA  ASN A  63       5.490  23.400  28.203  1.00 61.78           C  
ANISOU  483  CA  ASN A  63    12279   5961   5233  -3372    290  -1202       C  
ATOM    484  C   ASN A  63       6.846  23.381  27.507  1.00 60.33           C  
ANISOU  484  C   ASN A  63    11894   5898   5129  -3599    215  -1189       C  
ATOM    485  O   ASN A  63       7.026  22.703  26.489  1.00 64.55           O  
ANISOU  485  O   ASN A  63    12204   6503   5819  -3514    170  -1128       O  
ATOM    486  CB  ASN A  63       4.764  24.715  27.891  1.00 67.59           C  
ANISOU  486  CB  ASN A  63    13403   6385   5892  -3250    523  -1238       C  
ATOM    487  CG  ASN A  63       3.273  24.638  28.142  1.00 64.72           C  
ANISOU  487  CG  ASN A  63    13178   5896   5518  -2926    619  -1238       C  
ATOM    488  OD1 ASN A  63       2.683  23.560  28.095  1.00 62.82           O  
ANISOU  488  OD1 ASN A  63    12734   5774   5360  -2746    538  -1197       O  
ATOM    489  ND2 ASN A  63       2.654  25.785  28.414  1.00 63.17           N  
ANISOU  489  ND2 ASN A  63    13322   5461   5219  -2847    797  -1289       N  
ATOM    490  N   HIS A  64       7.821  24.122  28.051  1.00 63.54           N  
ANISOU  490  N   HIS A  64    12374   6339   5431  -3895    208  -1254       N  
ATOM    491  CA  HIS A  64       9.122  24.221  27.396  1.00 70.77           C  
ANISOU  491  CA  HIS A  64    13104   7370   6417  -4118    163  -1259       C  
ATOM    492  C   HIS A  64       9.948  22.942  27.494  1.00 71.37           C  
ANISOU  492  C   HIS A  64    12730   7762   6624  -4185    -72  -1217       C  
ATOM    493  O   HIS A  64      11.075  22.925  26.984  1.00 71.19           O  
ANISOU  493  O   HIS A  64    12500   7865   6682  -4359   -119  -1228       O  
ATOM    494  CB  HIS A  64       9.915  25.406  27.959  1.00 75.08           C  
ANISOU  494  CB  HIS A  64    13858   7865   6805  -4424    229  -1352       C  
ATOM    495  CG  HIS A  64      10.316  25.243  29.392  1.00 77.15           C  
ANISOU  495  CG  HIS A  64    14070   8295   6950  -4610     87  -1400       C  
ATOM    496  ND1 HIS A  64      11.476  24.602  29.772  1.00 84.10           N  
ANISOU  496  ND1 HIS A  64    14612   9467   7875  -4812   -122  -1403       N  
ATOM    497  CD2 HIS A  64       9.714  25.641  30.537  1.00 84.22           C  
ANISOU  497  CD2 HIS A  64    15210   9108   7682  -4620    122  -1446       C  
ATOM    498  CE1 HIS A  64      11.572  24.612  31.091  1.00 86.71           C  
ANISOU  498  CE1 HIS A  64    14991   9891   8062  -4940   -221  -1442       C  
ATOM    499  NE2 HIS A  64      10.515  25.236  31.580  1.00 85.38           N  
ANISOU  499  NE2 HIS A  64    15180   9499   7763  -4837    -69  -1472       N  
ATOM    500  N   ASN A  65       9.434  21.880  28.127  1.00 61.82           N  
ANISOU  500  N   ASN A  65    11365   6683   5440  -4048   -214  -1168       N  
ATOM    501  CA  ASN A  65      10.099  20.585  28.080  1.00 58.21           C  
ANISOU  501  CA  ASN A  65    10486   6503   5129  -4051   -433  -1104       C  
ATOM    502  C   ASN A  65       9.838  19.845  26.773  1.00 59.64           C  
ANISOU  502  C   ASN A  65    10477   6676   5508  -3852   -412  -1034       C  
ATOM    503  O   ASN A  65      10.445  18.797  26.537  1.00 65.52           O  
ANISOU  503  O   ASN A  65    10860   7631   6403  -3843   -571   -979       O  
ATOM    504  CB  ASN A  65       9.645  19.709  29.248  1.00 57.64           C  
ANISOU  504  CB  ASN A  65    10341   6567   4992  -3981   -592  -1065       C  
ATOM    505  CG  ASN A  65      10.343  20.057  30.534  1.00 67.18           C  
ANISOU  505  CG  ASN A  65    11584   7897   6044  -4221   -699  -1116       C  
ATOM    506  OD1 ASN A  65       9.743  20.619  31.450  1.00 75.08           O  
ANISOU  506  OD1 ASN A  65    12867   8792   6867  -4246   -629  -1163       O  
ATOM    507  ND2 ASN A  65      11.623  19.727  30.614  1.00 77.00           N  
ANISOU  507  ND2 ASN A  65    12534   9368   7356  -4396   -868  -1111       N  
ATOM    508  N   PHE A  66       8.966  20.367  25.918  1.00 57.26           N  
ANISOU  508  N   PHE A  66    10408   6136   5211  -3685   -223  -1031       N  
ATOM    509  CA  PHE A  66       8.529  19.665  24.717  1.00 52.67           C  
ANISOU  509  CA  PHE A  66     9687   5529   4795  -3476   -197   -964       C  
ATOM    510  C   PHE A  66       8.899  20.481  23.484  1.00 58.46           C  
ANISOU  510  C   PHE A  66    10522   6121   5569  -3519    -35   -977       C  
ATOM    511  O   PHE A  66       8.569  21.667  23.406  1.00 64.32           O  
ANISOU  511  O   PHE A  66    11608   6645   6186  -3533    130  -1016       O  
ATOM    512  CB  PHE A  66       7.014  19.435  24.738  1.00 51.16           C  
ANISOU  512  CB  PHE A  66     9675   5191   4573  -3192   -126   -937       C  
ATOM    513  CG  PHE A  66       6.541  18.530  25.830  1.00 53.51           C  
ANISOU  513  CG  PHE A  66     9876   5627   4828  -3130   -267   -917       C  
ATOM    514  CD1 PHE A  66       6.494  17.158  25.644  1.00 48.20           C  
ANISOU  514  CD1 PHE A  66     8900   5128   4286  -3033   -416   -843       C  
ATOM    515  CD2 PHE A  66       6.093  19.051  27.029  1.00 59.32           C  
ANISOU  515  CD2 PHE A  66    10841   6310   5387  -3164   -238   -968       C  
ATOM    516  CE1 PHE A  66       6.047  16.325  26.649  1.00 53.77           C  
ANISOU  516  CE1 PHE A  66     9538   5959   4933  -2978   -541   -812       C  
ATOM    517  CE2 PHE A  66       5.641  18.224  28.041  1.00 59.36           C  
ANISOU  517  CE2 PHE A  66    10775   6445   5333  -3112   -355   -945       C  
ATOM    518  CZ  PHE A  66       5.619  16.862  27.858  1.00 58.00           C  
ANISOU  518  CZ  PHE A  66    10310   6451   5279  -3021   -509   -863       C  
ATOM    519  N   LEU A  67       9.558  19.847  22.516  1.00 53.05           N  
ANISOU  519  N   LEU A  67     9551   5553   5054  -3532    -74   -940       N  
ATOM    520  CA  LEU A  67       9.922  20.494  21.264  1.00 56.49           C  
ANISOU  520  CA  LEU A  67    10063   5872   5527  -3571     80   -944       C  
ATOM    521  C   LEU A  67       9.129  19.847  20.147  1.00 56.85           C  
ANISOU  521  C   LEU A  67    10060   5847   5692  -3317    127   -870       C  
ATOM    522  O   LEU A  67       9.145  18.623  20.004  1.00 57.15           O  
ANISOU  522  O   LEU A  67     9790   6046   5877  -3232      5   -823       O  
ATOM    523  CB  LEU A  67      11.418  20.367  20.970  1.00 65.41           C  
ANISOU  523  CB  LEU A  67    10902   7198   6752  -3811     24   -976       C  
ATOM    524  CG  LEU A  67      12.435  20.510  22.100  1.00 75.57           C  
ANISOU  524  CG  LEU A  67    12063   8668   7984  -4062   -104  -1039       C  
ATOM    525  CD1 LEU A  67      13.828  20.256  21.551  1.00 80.20           C  
ANISOU  525  CD1 LEU A  67    12314   9448   8709  -4239   -147  -1066       C  
ATOM    526  CD2 LEU A  67      12.352  21.887  22.747  1.00 86.34           C  
ANISOU  526  CD2 LEU A  67    13812   9863   9130  -4216      9  -1112       C  
ATOM    527  N   VAL A  68       8.423  20.656  19.372  1.00 55.30           N  
ANISOU  527  N   VAL A  68    10172   5412   5428  -3190    298   -855       N  
ATOM    528  CA  VAL A  68       7.672  20.157  18.231  1.00 51.80           C  
ANISOU  528  CA  VAL A  68     9712   4892   5079  -2953    350   -785       C  
ATOM    529  C   VAL A  68       8.292  20.750  16.981  1.00 54.98           C  
ANISOU  529  C   VAL A  68    10173   5224   5494  -3039    480   -777       C  
ATOM    530  O   VAL A  68       8.495  21.963  16.888  1.00 59.00           O  
ANISOU  530  O   VAL A  68    10968   5582   5866  -3142    604   -809       O  
ATOM    531  CB  VAL A  68       6.176  20.489  18.340  1.00 50.43           C  
ANISOU  531  CB  VAL A  68     9834   4510   4817  -2671    422   -759       C  
ATOM    532  CG1 VAL A  68       5.436  20.017  17.108  1.00 49.39           C  
ANISOU  532  CG1 VAL A  68     9685   4308   4774  -2427    468   -685       C  
ATOM    533  CG2 VAL A  68       5.590  19.847  19.619  1.00 53.58           C  
ANISOU  533  CG2 VAL A  68    10166   4997   5193  -2603    303   -779       C  
ATOM    534  N   GLN A  69       8.625  19.894  16.035  1.00 51.70           N  
ANISOU  534  N   GLN A  69     9492   4920   5231  -3011    459   -738       N  
ATOM    535  CA  GLN A  69       9.259  20.319  14.799  1.00 54.52           C  
ANISOU  535  CA  GLN A  69     9876   5238   5602  -3101    584   -734       C  
ATOM    536  C   GLN A  69       8.353  19.904  13.659  1.00 52.92           C  
ANISOU  536  C   GLN A  69     9725   4936   5445  -2851    640   -654       C  
ATOM    537  O   GLN A  69       7.973  18.736  13.567  1.00 51.91           O  
ANISOU  537  O   GLN A  69     9358   4915   5451  -2717    548   -615       O  
ATOM    538  CB  GLN A  69      10.641  19.692  14.651  1.00 62.68           C  
ANISOU  538  CB  GLN A  69    10521   6515   6778  -3315    522   -771       C  
ATOM    539  CG  GLN A  69      11.526  20.389  13.660  1.00 70.11           C  
ANISOU  539  CG  GLN A  69    11520   7425   7691  -3490    667   -803       C  
ATOM    540  CD  GLN A  69      12.984  20.252  14.024  1.00 85.16           C  
ANISOU  540  CD  GLN A  69    13127   9553   9677  -3757    611   -878       C  
ATOM    541  OE1 GLN A  69      13.320  19.787  15.117  1.00 87.04           O  
ANISOU  541  OE1 GLN A  69    13156   9951   9966  -3815    455   -903       O  
ATOM    542  NE2 GLN A  69      13.864  20.665  13.117  1.00 94.85           N  
ANISOU  542  NE2 GLN A  69    14334  10795  10908  -3921    736   -914       N  
ATOM    543  N   ALA A  70       7.986  20.862  12.819  1.00 55.88           N  
ANISOU  543  N   ALA A  70    10426   5107   5700  -2787    783   -627       N  
ATOM    544  CA  ALA A  70       7.148  20.619  11.656  1.00 59.39           C  
ANISOU  544  CA  ALA A  70    10959   5449   6156  -2553    837   -547       C  
ATOM    545  C   ALA A  70       8.026  20.957  10.457  1.00 67.00           C  
ANISOU  545  C   ALA A  70    11932   6416   7108  -2711    953   -551       C  
ATOM    546  O   ALA A  70       8.124  22.118  10.056  1.00 69.72           O  
ANISOU  546  O   ALA A  70    12596   6598   7298  -2770   1074   -555       O  
ATOM    547  CB  ALA A  70       5.877  21.457  11.707  1.00 60.59           C  
ANISOU  547  CB  ALA A  70    11495   5363   6163  -2302    891   -503       C  
ATOM    548  N   GLY A  71       8.695  19.941   9.926  1.00 70.52           N  
ANISOU  548  N   GLY A  71    12030   7050   7713  -2786    922   -555       N  
ATOM    549  CA  GLY A  71       9.625  20.117   8.832  1.00 75.01           C  
ANISOU  549  CA  GLY A  71    12556   7659   8287  -2952   1036   -575       C  
ATOM    550  C   GLY A  71      10.754  21.041   9.215  1.00 86.55           C  
ANISOU  550  C   GLY A  71    14076   9138   9671  -3243   1099   -660       C  
ATOM    551  O   GLY A  71      11.606  20.693  10.037  1.00 95.85           O  
ANISOU  551  O   GLY A  71    14978  10497  10943  -3409   1015   -723       O  
ATOM    552  N   ASN A  72      10.754  22.234   8.619  1.00 90.07           N  
ANISOU  552  N   ASN A  72    14890   9395   9937  -3303   1243   -660       N  
ATOM    553  CA  ASN A  72      11.712  23.266   8.993  1.00 94.17           C  
ANISOU  553  CA  ASN A  72    15538   9894  10349  -3585   1322   -743       C  
ATOM    554  C   ASN A  72      11.384  23.845  10.362  1.00 93.38           C  
ANISOU  554  C   ASN A  72    15588   9726  10167  -3595   1257   -770       C  
ATOM    555  O   ASN A  72      12.251  23.934  11.238  1.00 99.14           O  
ANISOU  555  O   ASN A  72    16164  10587  10919  -3819   1209   -849       O  
ATOM    556  CB  ASN A  72      11.708  24.377   7.942  1.00100.03           C  
ANISOU  556  CB  ASN A  72    16673  10430  10905  -3635   1499   -730       C  
ATOM    557  CG  ASN A  72      13.035  24.520   7.237  1.00107.09           C  
ANISOU  557  CG  ASN A  72    17446  11433  11809  -3924   1611   -804       C  
ATOM    558  OD1 ASN A  72      13.872  23.618   7.278  1.00109.32           O  
ANISOU  558  OD1 ASN A  72    17313  11955  12269  -4032   1558   -850       O  
ATOM    559  ND2 ASN A  72      13.238  25.661   6.584  1.00109.91           N  
ANISOU  559  ND2 ASN A  72    18171  11613  11976  -4046   1770   -818       N  
ATOM    560  N   VAL A  73      10.130  24.215  10.567  1.00 83.29           N  
ANISOU  560  N   VAL A  73    14598   8254   8794  -3348   1254   -709       N  
ATOM    561  CA  VAL A  73       9.754  25.142  11.625  1.00 74.93           C  
ANISOU  561  CA  VAL A  73    13817   7055   7598  -3357   1262   -737       C  
ATOM    562  C   VAL A  73       9.775  24.444  12.976  1.00 70.48           C  
ANISOU  562  C   VAL A  73    12997   6654   7127  -3376   1106   -775       C  
ATOM    563  O   VAL A  73       9.566  23.234  13.085  1.00 66.53           O  
ANISOU  563  O   VAL A  73    12181   6312   6785  -3261    982   -748       O  
ATOM    564  CB  VAL A  73       8.366  25.736  11.315  1.00 74.91           C  
ANISOU  564  CB  VAL A  73    14191   6795   7476  -3045   1315   -656       C  
ATOM    565  CG1 VAL A  73       8.019  26.855  12.277  1.00 79.68           C  
ANISOU  565  CG1 VAL A  73    15128   7223   7924  -3057   1364   -689       C  
ATOM    566  CG2 VAL A  73       8.325  26.232   9.875  1.00 74.42           C  
ANISOU  566  CG2 VAL A  73    14349   6598   7328  -3002   1439   -604       C  
ATOM    567  N   GLN A  74      10.050  25.211  14.020  1.00 73.67           N  
ANISOU  567  N   GLN A  74    13549   7019   7423  -3533   1112   -840       N  
ATOM    568  CA  GLN A  74       9.749  24.779  15.373  1.00 72.12           C  
ANISOU  568  CA  GLN A  74    13239   6911   7253  -3503    978   -867       C  
ATOM    569  C   GLN A  74       8.429  25.406  15.790  1.00 69.80           C  
ANISOU  569  C   GLN A  74    13301   6384   6837  -3259   1027   -833       C  
ATOM    570  O   GLN A  74       8.176  26.580  15.513  1.00 79.57           O  
ANISOU  570  O   GLN A  74    14912   7396   7923  -3247   1167   -830       O  
ATOM    571  CB  GLN A  74      10.857  25.173  16.351  1.00 78.29           C  
ANISOU  571  CB  GLN A  74    13947   7815   7986  -3829    942   -965       C  
ATOM    572  CG  GLN A  74      11.828  24.048  16.664  1.00 85.40           C  
ANISOU  572  CG  GLN A  74    14365   9027   9057  -3967    782   -994       C  
ATOM    573  CD  GLN A  74      13.006  24.516  17.492  1.00 96.72           C  
ANISOU  573  CD  GLN A  74    15721  10590  10436  -4294    745  -1091       C  
ATOM    574  OE1 GLN A  74      14.129  24.606  16.990  1.00105.31           O  
ANISOU  574  OE1 GLN A  74    16646  11794  11571  -4509    779  -1137       O  
ATOM    575  NE2 GLN A  74      12.761  24.816  18.768  1.00 97.10           N  
ANISOU  575  NE2 GLN A  74    15886  10626  10381  -4339    679  -1128       N  
ATOM    576  N   LEU A  75       7.585  24.616  16.433  1.00 58.79           N  
ANISOU  576  N   LEU A  75    11788   5042   5509  -3055    918   -809       N  
ATOM    577  CA  LEU A  75       6.306  25.080  16.944  1.00 58.79           C  
ANISOU  577  CA  LEU A  75    12067   4853   5417  -2803    958   -789       C  
ATOM    578  C   LEU A  75       6.431  25.269  18.445  1.00 59.31           C  
ANISOU  578  C   LEU A  75    12157   4966   5413  -2935    904   -865       C  
ATOM    579  O   LEU A  75       6.885  24.363  19.151  1.00 66.00           O  
ANISOU  579  O   LEU A  75    12703   6034   6340  -3046    760   -894       O  
ATOM    580  CB  LEU A  75       5.188  24.085  16.640  1.00 64.62           C  
ANISOU  580  CB  LEU A  75    12672   5616   6265  -2476    888   -721       C  
ATOM    581  CG  LEU A  75       4.577  24.133  15.240  1.00 74.60           C  
ANISOU  581  CG  LEU A  75    14034   6764   7549  -2246    957   -634       C  
ATOM    582  CD1 LEU A  75       5.619  23.841  14.180  1.00 78.19           C  
ANISOU  582  CD1 LEU A  75    14317   7320   8071  -2434    972   -622       C  
ATOM    583  CD2 LEU A  75       3.434  23.143  15.156  1.00 72.69           C  
ANISOU  583  CD2 LEU A  75    13651   6563   7406  -1932    878   -582       C  
ATOM    584  N   ARG A  76       6.022  26.431  18.930  1.00 62.68           N  
ANISOU  584  N   ARG A  76    12945   5185   5684  -2919   1018   -894       N  
ATOM    585  CA  ARG A  76       6.070  26.683  20.360  1.00 64.72           C  
ANISOU  585  CA  ARG A  76    13265   5470   5857  -3043    985   -969       C  
ATOM    586  C   ARG A  76       4.877  26.018  21.029  1.00 60.69           C  
ANISOU  586  C   ARG A  76    12706   4970   5382  -2768    923   -954       C  
ATOM    587  O   ARG A  76       3.728  26.246  20.642  1.00 62.48           O  
ANISOU  587  O   ARG A  76    13102   5032   5604  -2458   1000   -908       O  
ATOM    588  CB  ARG A  76       6.089  28.187  20.664  1.00 67.15           C  
ANISOU  588  CB  ARG A  76    13988   5542   5984  -3141   1144  -1015       C  
ATOM    589  CG  ARG A  76       6.015  28.491  22.153  1.00 73.42           C  
ANISOU  589  CG  ARG A  76    14880   6342   6676  -3252   1126  -1096       C  
ATOM    590  CD  ARG A  76       6.378  29.934  22.505  1.00 82.07           C  
ANISOU  590  CD  ARG A  76    16350   7239   7592  -3448   1275  -1160       C  
ATOM    591  NE  ARG A  76       5.515  30.483  23.558  1.00 93.60           N  
ANISOU  591  NE  ARG A  76    18064   8550   8950  -3335   1339  -1204       N  
ATOM    592  CZ  ARG A  76       5.481  30.052  24.823  1.00 96.16           C  
ANISOU  592  CZ  ARG A  76    18283   9005   9250  -3415   1248  -1264       C  
ATOM    593  NH1 ARG A  76       6.263  29.055  25.231  1.00 92.58           N  
ANISOU  593  NH1 ARG A  76    17473   8839   8863  -3600   1070  -1280       N  
ATOM    594  NH2 ARG A  76       4.653  30.619  25.693  1.00100.15           N  
ANISOU  594  NH2 ARG A  76    19040   9354   9658  -3301   1335  -1309       N  
ATOM    595  N   VAL A  77       5.155  25.197  22.034  1.00 61.71           N  
ANISOU  595  N   VAL A  77    12599   5305   5541  -2879    782   -993       N  
ATOM    596  CA  VAL A  77       4.107  24.542  22.808  1.00 62.08           C  
ANISOU  596  CA  VAL A  77    12601   5387   5600  -2663    727   -994       C  
ATOM    597  C   VAL A  77       3.608  25.512  23.873  1.00 64.43           C  
ANISOU  597  C   VAL A  77    13208   5530   5741  -2662    827  -1060       C  
ATOM    598  O   VAL A  77       4.392  26.009  24.692  1.00 64.62           O  
ANISOU  598  O   VAL A  77    13300   5589   5663  -2941    816  -1126       O  
ATOM    599  CB  VAL A  77       4.631  23.243  23.430  1.00 61.03           C  
ANISOU  599  CB  VAL A  77    12103   5540   5545  -2786    530   -999       C  
ATOM    600  CG1 VAL A  77       3.610  22.649  24.395  1.00 62.76           C  
ANISOU  600  CG1 VAL A  77    12311   5799   5734  -2609    485  -1013       C  
ATOM    601  CG2 VAL A  77       4.996  22.254  22.312  1.00 58.36           C  
ANISOU  601  CG2 VAL A  77    11462   5333   5379  -2746    449   -932       C  
ATOM    602  N   ILE A  78       2.300  25.777  23.877  1.00 64.37           N  
ANISOU  602  N   ILE A  78    13377   5360   5719  -2343    924  -1048       N  
ATOM    603  CA  ILE A  78       1.706  26.713  24.835  1.00 59.22           C  
ANISOU  603  CA  ILE A  78    13022   4544   4934  -2301   1041  -1114       C  
ATOM    604  C   ILE A  78       0.802  26.025  25.847  1.00 59.60           C  
ANISOU  604  C   ILE A  78    12980   4686   4981  -2145   1001  -1151       C  
ATOM    605  O   ILE A  78       0.255  26.700  26.740  1.00 60.30           O  
ANISOU  605  O   ILE A  78    13287   4660   4965  -2103   1100  -1217       O  
ATOM    606  CB  ILE A  78       0.942  27.837  24.112  1.00 60.89           C  
ANISOU  606  CB  ILE A  78    13554   4472   5109  -2059   1214  -1082       C  
ATOM    607  CG1 ILE A  78      -0.251  27.257  23.352  1.00 68.74           C  
ANISOU  607  CG1 ILE A  78    14446   5454   6218  -1654   1213  -1011       C  
ATOM    608  CG2 ILE A  78       1.869  28.557  23.150  1.00 70.05           C  
ANISOU  608  CG2 ILE A  78    14835   5540   6239  -2241   1266  -1049       C  
ATOM    609  CD1 ILE A  78      -1.035  28.288  22.584  1.00 73.62           C  
ANISOU  609  CD1 ILE A  78    15347   5820   6805  -1379   1354   -964       C  
ATOM    610  N   GLY A  79       0.598  24.714  25.724  1.00 63.35           N  
ANISOU  610  N   GLY A  79    13149   5360   5562  -2055    872  -1115       N  
ATOM    611  CA  GLY A  79      -0.146  23.977  26.730  1.00 61.10           C  
ANISOU  611  CA  GLY A  79    12764   5196   5256  -1952    831  -1153       C  
ATOM    612  C   GLY A  79       0.083  22.495  26.559  1.00 58.31           C  
ANISOU  612  C   GLY A  79    12061   5090   5003  -1969    658  -1105       C  
ATOM    613  O   GLY A  79       0.468  22.034  25.481  1.00 49.85           O  
ANISOU  613  O   GLY A  79    10832   4061   4049  -1955    599  -1041       O  
ATOM    614  N   HIS A  80      -0.165  21.737  27.624  1.00 52.82           N  
ANISOU  614  N   HIS A  80    11255   4558   4257  -2000    580  -1134       N  
ATOM    615  CA  HIS A  80      -0.021  20.289  27.508  1.00 48.88           C  
ANISOU  615  CA  HIS A  80    10440   4291   3841  -2003    414  -1081       C  
ATOM    616  C   HIS A  80      -0.992  19.588  28.447  1.00 51.21           C  
ANISOU  616  C   HIS A  80    10688   4694   4073  -1867    416  -1105       C  
ATOM    617  O   HIS A  80      -1.225  20.048  29.573  1.00 50.67           O  
ANISOU  617  O   HIS A  80    10773   4605   3875  -1930    473  -1168       O  
ATOM    618  CB  HIS A  80       1.413  19.840  27.818  1.00 55.14           C  
ANISOU  618  CB  HIS A  80    11046   5269   4636  -2336    227  -1056       C  
ATOM    619  CG  HIS A  80       1.828  20.087  29.238  1.00 55.68           C  
ANISOU  619  CG  HIS A  80    11192   5414   4551  -2555    177  -1106       C  
ATOM    620  ND1 HIS A  80       2.335  21.296  29.665  1.00 58.52           N  
ANISOU  620  ND1 HIS A  80    11781   5651   4802  -2738    257  -1169       N  
ATOM    621  CD2 HIS A  80       1.795  19.285  30.332  1.00 54.15           C  
ANISOU  621  CD2 HIS A  80    10890   5405   4280  -2623     56  -1097       C  
ATOM    622  CE1 HIS A  80       2.596  21.229  30.962  1.00 63.16           C  
ANISOU  622  CE1 HIS A  80    12395   6347   5257  -2910    185  -1205       C  
ATOM    623  NE2 HIS A  80       2.282  20.016  31.387  1.00 59.99           N  
ANISOU  623  NE2 HIS A  80    11790   6132   4870  -2841     60  -1156       N  
ATOM    624  N   SER A  81      -1.538  18.463  27.986  1.00 45.47           N  
ANISOU  624  N   SER A  81     9753   4092   3432  -1697    361  -1058       N  
ATOM    625  CA  SER A  81      -2.403  17.663  28.842  1.00 52.90           C  
ANISOU  625  CA  SER A  81    10619   5173   4308  -1592    362  -1070       C  
ATOM    626  C   SER A  81      -2.318  16.193  28.459  1.00 50.40           C  
ANISOU  626  C   SER A  81    10020   5063   4068  -1576    211   -990       C  
ATOM    627  O   SER A  81      -1.848  15.825  27.378  1.00 46.01           O  
ANISOU  627  O   SER A  81     9313   4520   3649  -1566    137   -930       O  
ATOM    628  CB  SER A  81      -3.856  18.140  28.782  1.00 58.86           C  
ANISOU  628  CB  SER A  81    11495   5813   5056  -1268    568  -1124       C  
ATOM    629  OG  SER A  81      -4.398  17.962  27.489  1.00 61.48           O  
ANISOU  629  OG  SER A  81    11744   6096   5519  -1013    611  -1086       O  
ATOM    630  N   MET A  82      -2.790  15.351  29.364  1.00 44.69           N  
ANISOU  630  N   MET A  82     9213   4503   3263  -1571    174   -976       N  
ATOM    631  CA  MET A  82      -2.830  13.918  29.126  1.00 43.33           C  
ANISOU  631  CA  MET A  82     8716   4542   3206  -1517     46   -849       C  
ATOM    632  C   MET A  82      -4.268  13.430  29.070  1.00 43.94           C  
ANISOU  632  C   MET A  82     8701   4673   3320  -1234    186   -839       C  
ATOM    633  O   MET A  82      -5.088  13.775  29.932  1.00 48.42           O  
ANISOU  633  O   MET A  82     9443   5217   3735  -1186    322   -932       O  
ATOM    634  CB  MET A  82      -2.070  13.160  30.222  1.00 44.53           C  
ANISOU  634  CB  MET A  82     8798   4869   3252  -1764   -145   -797       C  
ATOM    635  CG  MET A  82      -1.806  11.735  29.794  1.00 48.59           C  
ANISOU  635  CG  MET A  82     8955   5566   3942  -1714   -299   -635       C  
ATOM    636  SD  MET A  82      -0.883  10.800  30.993  1.00 51.17           S  
ANISOU  636  SD  MET A  82     9197   6088   4158  -1960   -549   -544       S  
ATOM    637  CE  MET A  82       0.790  11.172  30.549  1.00 53.94           C  
ANISOU  637  CE  MET A  82     9459   6448   4586  -2191   -738   -537       C  
ATOM    638  N   GLN A  83      -4.558  12.605  28.062  1.00 42.31           N  
ANISOU  638  N   GLN A  83     8212   4551   3315  -1064    157   -735       N  
ATOM    639  CA  GLN A  83      -5.850  11.953  27.891  1.00 43.86           C  
ANISOU  639  CA  GLN A  83     8250   4844   3573   -823    261   -714       C  
ATOM    640  C   GLN A  83      -5.545  10.486  27.648  1.00 40.97           C  
ANISOU  640  C   GLN A  83     7573   4658   3337   -862    114   -573       C  
ATOM    641  O   GLN A  83      -5.064  10.124  26.568  1.00 40.55           O  
ANISOU  641  O   GLN A  83     7342   4611   3456   -827     35   -498       O  
ATOM    642  CB  GLN A  83      -6.645  12.544  26.719  1.00 47.30           C  
ANISOU  642  CB  GLN A  83     8675   5174   4121   -544    391   -742       C  
ATOM    643  CG  GLN A  83      -8.050  11.971  26.581  1.00 51.00           C  
ANISOU  643  CG  GLN A  83     8969   5765   4643   -299    503   -744       C  
ATOM    644  CD  GLN A  83      -8.763  12.421  25.312  1.00 53.40           C  
ANISOU  644  CD  GLN A  83     9214   6004   5072    -17    581   -748       C  
ATOM    645  OE1 GLN A  83      -8.132  12.807  24.324  1.00 53.89           O  
ANISOU  645  OE1 GLN A  83     9303   5959   5215    -12    522   -706       O  
ATOM    646  NE2 GLN A  83     -10.088  12.385  25.343  1.00 56.67           N  
ANISOU  646  NE2 GLN A  83     9548   6493   5491    216    713   -799       N  
ATOM    647  N   ASN A  84      -5.779   9.652  28.665  1.00 42.16           N  
ANISOU  647  N   ASN A  84     7684   4940   3395   -946     82   -539       N  
ATOM    648  CA  ASN A  84      -5.514   8.212  28.582  1.00 38.51           C  
ANISOU  648  CA  ASN A  84     6969   4624   3037   -987    -53   -401       C  
ATOM    649  C   ASN A  84      -4.048   8.043  28.208  1.00 41.67           C  
ANISOU  649  C   ASN A  84     7287   5018   3527  -1137   -252   -324       C  
ATOM    650  O   ASN A  84      -3.182   8.587  28.922  1.00 40.98           O  
ANISOU  650  O   ASN A  84     7353   4903   3313  -1332   -343   -354       O  
ATOM    651  CB  ASN A  84      -6.535   7.579  27.650  1.00 35.90           C  
ANISOU  651  CB  ASN A  84     6423   4352   2864   -766     42   -373       C  
ATOM    652  CG  ASN A  84      -7.932   7.962  28.014  1.00 37.79           C  
ANISOU  652  CG  ASN A  84     6735   4609   3016   -618    246   -475       C  
ATOM    653  OD1 ASN A  84      -8.356   7.791  29.162  1.00 40.95           O  
ANISOU  653  OD1 ASN A  84     7236   5067   3257   -698    306   -508       O  
ATOM    654  ND2 ASN A  84      -8.660   8.501  27.051  1.00 38.69           N  
ANISOU  654  ND2 ASN A  84     6798   4676   3224   -397    355   -528       N  
ATOM    655  N   CYS A  85      -3.704   7.372  27.121  1.00 36.16           N  
ANISOU  655  N   CYS A  85     6355   4350   3036  -1066   -318   -241       N  
ATOM    656  CA  CYS A  85      -2.304   7.142  26.797  1.00 32.97           C  
ANISOU  656  CA  CYS A  85     5840   3961   2728  -1204   -494   -175       C  
ATOM    657  C   CYS A  85      -1.762   8.107  25.762  1.00 31.39           C  
ANISOU  657  C   CYS A  85     5673   3644   2609  -1203   -459   -232       C  
ATOM    658  O   CYS A  85      -0.683   7.861  25.201  1.00 35.11           O  
ANISOU  658  O   CYS A  85     5999   4139   3204  -1289   -572   -185       O  
ATOM    659  CB  CYS A  85      -2.098   5.692  26.354  1.00 30.92           C  
ANISOU  659  CB  CYS A  85     5307   3803   2639  -1152   -594    -46       C  
ATOM    660  SG  CYS A  85      -2.589   4.469  27.638  1.00 35.82           S  
ANISOU  660  SG  CYS A  85     5925   4538   3147  -1191   -650     45       S  
ATOM    661  N   VAL A  86      -2.459   9.197  25.500  1.00 31.56           N  
ANISOU  661  N   VAL A  86     5889   3539   2564  -1107   -300   -331       N  
ATOM    662  CA  VAL A  86      -1.907  10.180  24.583  1.00 38.18           C  
ANISOU  662  CA  VAL A  86     6815   4241   3450  -1130   -263   -378       C  
ATOM    663  C   VAL A  86      -1.676  11.514  25.291  1.00 37.96           C  
ANISOU  663  C   VAL A  86     7109   4075   3239  -1266   -207   -493       C  
ATOM    664  O   VAL A  86      -2.341  11.886  26.271  1.00 41.78           O  
ANISOU  664  O   VAL A  86     7779   4534   3560  -1255   -133   -561       O  
ATOM    665  CB  VAL A  86      -2.765  10.379  23.316  1.00 38.43           C  
ANISOU  665  CB  VAL A  86     6813   4202   3587   -886   -135   -380       C  
ATOM    666  CG1 VAL A  86      -2.696   9.118  22.441  1.00 35.11           C  
ANISOU  666  CG1 VAL A  86     6082   3904   3355   -810   -201   -278       C  
ATOM    667  CG2 VAL A  86      -4.198  10.732  23.675  1.00 44.21           C  
ANISOU  667  CG2 VAL A  86     7663   4907   4227   -685     13   -441       C  
ATOM    668  N   LEU A  87      -0.672  12.216  24.794  1.00 37.91           N  
ANISOU  668  N   LEU A  87     7171   3978   3256  -1418   -237   -522       N  
ATOM    669  CA  LEU A  87      -0.360  13.586  25.179  1.00 41.18           C  
ANISOU  669  CA  LEU A  87     7911   4219   3515  -1565   -166   -639       C  
ATOM    670  C   LEU A  87      -0.937  14.517  24.121  1.00 45.42           C  
ANISOU  670  C   LEU A  87     8622   4552   4085  -1386      2   -677       C  
ATOM    671  O   LEU A  87      -0.870  14.228  22.911  1.00 40.91           O  
ANISOU  671  O   LEU A  87     7898   3981   3665  -1282      6   -611       O  
ATOM    672  CB  LEU A  87       1.148  13.769  25.254  1.00 46.56           C  
ANISOU  672  CB  LEU A  87     8553   4936   4202  -1873   -301   -649       C  
ATOM    673  CG  LEU A  87       1.872  14.457  26.380  1.00 65.06           C  
ANISOU  673  CG  LEU A  87    11098   7264   6357  -2164   -364   -742       C  
ATOM    674  CD1 LEU A  87       1.639  13.657  27.649  1.00 65.54           C  
ANISOU  674  CD1 LEU A  87    11095   7494   6312  -2192   -477   -708       C  
ATOM    675  CD2 LEU A  87       3.327  14.479  25.979  1.00 61.23           C  
ANISOU  675  CD2 LEU A  87    10459   6847   5958  -2416   -490   -732       C  
ATOM    676  N   LYS A  88      -1.512  15.624  24.582  1.00 43.56           N  
ANISOU  676  N   LYS A  88     8717   4135   3697  -1343    140   -783       N  
ATOM    677  CA  LYS A  88      -2.058  16.672  23.727  1.00 44.88           C  
ANISOU  677  CA  LYS A  88     9120   4070   3864  -1165    298   -822       C  
ATOM    678  C   LYS A  88      -1.264  17.933  23.995  1.00 49.64           C  
ANISOU  678  C   LYS A  88    10027   4481   4354  -1395    347   -903       C  
ATOM    679  O   LYS A  88      -1.324  18.487  25.099  1.00 46.39           O  
ANISOU  679  O   LYS A  88     9758   4048   3821  -1477    387   -957       O  
ATOM    680  CB  LYS A  88      -3.549  16.881  23.988  1.00 43.41           C  
ANISOU  680  CB  LYS A  88     9028   3837   3628   -853    439   -862       C  
ATOM    681  CG  LYS A  88      -4.413  15.682  23.580  1.00 40.78           C  
ANISOU  681  CG  LYS A  88     8355   3712   3429   -619    407   -769       C  
ATOM    682  CD  LYS A  88      -5.869  16.087  23.382  1.00 50.98           C  
ANISOU  682  CD  LYS A  88     9719   4942   4710   -275    558   -808       C  
ATOM    683  CE  LYS A  88      -6.633  16.105  24.694  1.00 56.52           C  
ANISOU  683  CE  LYS A  88    10499   5695   5283   -241    645   -899       C  
ATOM    684  NZ  LYS A  88      -8.095  16.094  24.440  1.00 63.37           N  
ANISOU  684  NZ  LYS A  88    11288   6600   6189    107    769   -920       N  
ATOM    685  N   LEU A  89      -0.497  18.374  23.004  1.00 45.46           N  
ANISOU  685  N   LEU A  89     9510   3863   3898  -1488    351   -865       N  
ATOM    686  CA  LEU A  89       0.314  19.581  23.128  1.00 45.91           C  
ANISOU  686  CA  LEU A  89     9759   3798   3888  -1690    411   -886       C  
ATOM    687  C   LEU A  89      -0.369  20.693  22.342  1.00 52.83           C  
ANISOU  687  C   LEU A  89    10894   4431   4747  -1470    579   -870       C  
ATOM    688  O   LEU A  89      -0.446  20.625  21.111  1.00 53.09           O  
ANISOU  688  O   LEU A  89    10896   4410   4867  -1350    599   -808       O  
ATOM    689  CB  LEU A  89       1.735  19.337  22.619  1.00 44.89           C  
ANISOU  689  CB  LEU A  89     9448   3772   3836  -1971    308   -855       C  
ATOM    690  CG  LEU A  89       2.422  18.100  23.189  1.00 48.57           C  
ANISOU  690  CG  LEU A  89     9598   4498   4357  -2142    112   -840       C  
ATOM    691  CD1 LEU A  89       3.797  17.932  22.603  1.00 47.53           C  
ANISOU  691  CD1 LEU A  89     9255   4477   4329  -2376     31   -811       C  
ATOM    692  CD2 LEU A  89       2.533  18.274  24.728  1.00 51.51           C  
ANISOU  692  CD2 LEU A  89    10041   4947   4583  -2282     61   -892       C  
ATOM    693  N   LYS A  90      -0.869  21.709  23.047  1.00 52.45           N  
ANISOU  693  N   LYS A  90    11104   4239   4585  -1411    695   -920       N  
ATOM    694  CA  LYS A  90      -1.436  22.871  22.382  1.00 53.38           C  
ANISOU  694  CA  LYS A  90    11488   4122   4674  -1214    843   -896       C  
ATOM    695  C   LYS A  90      -0.295  23.761  21.920  1.00 56.84           C  
ANISOU  695  C   LYS A  90    12071   4459   5066  -1475    876   -882       C  
ATOM    696  O   LYS A  90       0.526  24.184  22.740  1.00 60.57           O  
ANISOU  696  O   LYS A  90    12610   4950   5452  -1761    867   -940       O  
ATOM    697  CB  LYS A  90      -2.366  23.644  23.316  1.00 57.29           C  
ANISOU  697  CB  LYS A  90    12200   4497   5071  -1058    962   -959       C  
ATOM    698  CG  LYS A  90      -3.171  24.710  22.605  1.00 62.15           C  
ANISOU  698  CG  LYS A  90    13056   4885   5672   -776   1098   -922       C  
ATOM    699  CD  LYS A  90      -4.371  25.154  23.430  1.00 71.67           C  
ANISOU  699  CD  LYS A  90    14380   6022   6831   -527   1205   -984       C  
ATOM    700  CE  LYS A  90      -5.142  26.233  22.700  1.00 76.69           C  
ANISOU  700  CE  LYS A  90    15244   6438   7455   -234   1323   -939       C  
ATOM    701  NZ  LYS A  90      -4.252  27.387  22.402  1.00 86.70           N  
ANISOU  701  NZ  LYS A  90    16803   7508   8629   -448   1385   -922       N  
ATOM    702  N   VAL A  91      -0.249  24.032  20.612  1.00 53.93           N  
ANISOU  702  N   VAL A  91    11749   3998   4745  -1380    915   -808       N  
ATOM    703  CA  VAL A  91       0.801  24.822  19.993  1.00 56.18           C  
ANISOU  703  CA  VAL A  91    12162   4201   4983  -1616    963   -792       C  
ATOM    704  C   VAL A  91       0.213  26.160  19.560  1.00 57.61           C  
ANISOU  704  C   VAL A  91    12707   4118   5064  -1442   1115   -766       C  
ATOM    705  O   VAL A  91      -1.005  26.331  19.443  1.00 60.09           O  
ANISOU  705  O   VAL A  91    13114   4336   5383  -1099   1163   -738       O  
ATOM    706  CB  VAL A  91       1.450  24.087  18.798  1.00 59.18           C  
ANISOU  706  CB  VAL A  91    12316   4692   5477  -1684    896   -730       C  
ATOM    707  CG1 VAL A  91       2.165  22.835  19.280  1.00 55.07           C  
ANISOU  707  CG1 VAL A  91    11439   4430   5055  -1879    742   -758       C  
ATOM    708  CG2 VAL A  91       0.408  23.722  17.748  1.00 59.11           C  
ANISOU  708  CG2 VAL A  91    12286   4634   5540  -1332    907   -648       C  
ATOM    709  N   ASP A  92       1.103  27.123  19.320  1.00 58.61           N  
ANISOU  709  N   ASP A  92    13036   4138   5097  -1681   1191   -778       N  
ATOM    710  CA  ASP A  92       0.703  28.489  19.015  1.00 69.58           C  
ANISOU  710  CA  ASP A  92    14811   5263   6363  -1569   1339   -760       C  
ATOM    711  C   ASP A  92       0.257  28.698  17.568  1.00 59.17           C  
ANISOU  711  C   ASP A  92    13582   3840   5060  -1334   1375   -657       C  
ATOM    712  O   ASP A  92      -0.073  29.834  17.210  1.00 62.94           O  
ANISOU  712  O   ASP A  92    14393   4094   5428  -1225   1489   -631       O  
ATOM    713  CB  ASP A  92       1.851  29.457  19.350  1.00 77.67           C  
ANISOU  713  CB  ASP A  92    16039   6212   7261  -1939   1416   -822       C  
ATOM    714  CG  ASP A  92       3.075  29.300  18.430  1.00 80.56           C  
ANISOU  714  CG  ASP A  92    16288   6673   7650  -2208   1395   -803       C  
ATOM    715  OD1 ASP A  92       3.023  28.569  17.418  1.00 76.29           O  
ANISOU  715  OD1 ASP A  92    15556   6219   7211  -2100   1340   -735       O  
ATOM    716  OD2 ASP A  92       4.105  29.951  18.724  1.00 89.50           O  
ANISOU  716  OD2 ASP A  92    17524   7792   8690  -2538   1445   -866       O  
ATOM    717  N   THR A  93       0.244  27.653  16.731  1.00 62.36           N  
ANISOU  717  N   THR A  93    13713   4395   5584  -1256   1280   -599       N  
ATOM    718  CA  THR A  93      -0.062  27.786  15.308  1.00 63.93           C  
ANISOU  718  CA  THR A  93    13985   4520   5785  -1071   1301   -502       C  
ATOM    719  C   THR A  93      -1.002  26.668  14.878  1.00 56.94           C  
ANISOU  719  C   THR A  93    12842   3763   5031   -765   1200   -445       C  
ATOM    720  O   THR A  93      -0.753  25.500  15.191  1.00 53.72           O  
ANISOU  720  O   THR A  93    12120   3554   4739   -852   1100   -471       O  
ATOM    721  CB  THR A  93       1.220  27.735  14.458  1.00 59.45           C  
ANISOU  721  CB  THR A  93    13363   4010   5214  -1380   1309   -494       C  
ATOM    722  OG1 THR A  93       2.109  28.786  14.861  1.00 68.37           O  
ANISOU  722  OG1 THR A  93    14726   5035   6217  -1676   1408   -556       O  
ATOM    723  CG2 THR A  93       0.894  27.875  12.978  1.00 67.73           C  
ANISOU  723  CG2 THR A  93    14509   4982   6243  -1198   1333   -398       C  
ATOM    724  N   ALA A  94      -2.078  27.020  14.173  1.00 57.24           N  
ANISOU  724  N   ALA A  94    13010   3695   5044   -409   1221   -371       N  
ATOM    725  CA  ALA A  94      -2.972  26.010  13.617  1.00 53.38           C  
ANISOU  725  CA  ALA A  94    12279   3337   4667   -116   1127   -314       C  
ATOM    726  C   ALA A  94      -2.361  25.441  12.345  1.00 54.25           C  
ANISOU  726  C   ALA A  94    12271   3523   4819   -218   1082   -252       C  
ATOM    727  O   ALA A  94      -1.813  26.183  11.526  1.00 56.48           O  
ANISOU  727  O   ALA A  94    12763   3689   5007   -327   1146   -217       O  
ATOM    728  CB  ALA A  94      -4.349  26.608  13.317  1.00 59.37           C  
ANISOU  728  CB  ALA A  94    13187   3986   5383    309   1151   -260       C  
ATOM    729  N   ASN A  95      -2.434  24.123  12.196  1.00 52.67           N  
ANISOU  729  N   ASN A  95    11745   3512   4754   -194    982   -245       N  
ATOM    730  CA  ASN A  95      -1.866  23.487  11.014  1.00 55.61           C  
ANISOU  730  CA  ASN A  95    11987   3965   5179   -293    946   -191       C  
ATOM    731  C   ASN A  95      -2.610  23.974   9.777  1.00 58.34           C  
ANISOU  731  C   ASN A  95    12505   4211   5449    -18    958    -94       C  
ATOM    732  O   ASN A  95      -3.819  23.731   9.652  1.00 52.32           O  
ANISOU  732  O   ASN A  95    11687   3482   4712    333    903    -53       O  
ATOM    733  CB  ASN A  95      -1.935  21.973  11.133  1.00 46.63           C  
ANISOU  733  CB  ASN A  95    10484   3032   4201   -288    841   -202       C  
ATOM    734  CG  ASN A  95      -1.288  21.254   9.932  1.00 49.39           C  
ANISOU  734  CG  ASN A  95    10684   3466   4616   -413    816   -153       C  
ATOM    735  OD1 ASN A  95      -0.831  21.890   8.972  1.00 50.31           O  
ANISOU  735  OD1 ASN A  95    10970   3495   4649   -494    879   -112       O  
ATOM    736  ND2 ASN A  95      -1.250  19.930   9.992  1.00 52.95           N  
ANISOU  736  ND2 ASN A  95    10828   4081   5208   -434    733   -162       N  
ATOM    737  N   PRO A  96      -1.944  24.679   8.857  1.00 58.01           N  
ANISOU  737  N   PRO A  96    12672   4063   5307   -162   1026    -62       N  
ATOM    738  CA  PRO A  96      -2.635  25.145   7.646  1.00 58.66           C  
ANISOU  738  CA  PRO A  96    12938   4052   5298     94   1024     30       C  
ATOM    739  C   PRO A  96      -3.041  24.014   6.716  1.00 53.22           C  
ANISOU  739  C   PRO A  96    12007   3517   4698    237    925     93       C  
ATOM    740  O   PRO A  96      -3.872  24.223   5.821  1.00 55.53           O  
ANISOU  740  O   PRO A  96    12393   3778   4930    514    885    171       O  
ATOM    741  CB  PRO A  96      -1.596  26.062   6.988  1.00 63.27           C  
ANISOU  741  CB  PRO A  96    13789   4497   5752   -176   1132     26       C  
ATOM    742  CG  PRO A  96      -0.275  25.505   7.432  1.00 56.84           C  
ANISOU  742  CG  PRO A  96    12770   3806   5021   -579   1155    -52       C  
ATOM    743  CD  PRO A  96      -0.507  25.008   8.845  1.00 55.06           C  
ANISOU  743  CD  PRO A  96    12349   3674   4898   -571   1102   -115       C  
ATOM    744  N   LYS A  97      -2.473  22.836   6.891  1.00 50.11           N  
ANISOU  744  N   LYS A  97    11309   3289   4441     54    882     61       N  
ATOM    745  CA  LYS A  97      -2.799  21.683   6.071  1.00 52.64           C  
ANISOU  745  CA  LYS A  97    11396   3755   4850    161    797    117       C  
ATOM    746  C   LYS A  97      -3.803  20.749   6.737  1.00 47.35           C  
ANISOU  746  C   LYS A  97    10472   3222   4296    411    699    111       C  
ATOM    747  O   LYS A  97      -3.946  19.607   6.300  1.00 47.67           O  
ANISOU  747  O   LYS A  97    10274   3404   4434    448    629    140       O  
ATOM    748  CB  LYS A  97      -1.520  20.929   5.718  1.00 52.14           C  
ANISOU  748  CB  LYS A  97    11153   3787   4869   -197    824     88       C  
ATOM    749  CG  LYS A  97      -0.529  21.710   4.851  1.00 56.86           C  
ANISOU  749  CG  LYS A  97    11960   4290   5356   -441    930     88       C  
ATOM    750  CD  LYS A  97       0.791  20.945   4.777  1.00 61.64           C  
ANISOU  750  CD  LYS A  97    12318   5032   6072   -805    965     31       C  
ATOM    751  CE  LYS A  97       1.750  21.572   3.797  1.00 71.74           C  
ANISOU  751  CE  LYS A  97    13759   6251   7249  -1038   1079     24       C  
ATOM    752  NZ  LYS A  97       1.379  21.245   2.385  1.00 81.34           N  
ANISOU  752  NZ  LYS A  97    15023   7467   8415   -917   1074    102       N  
ATOM    753  N   THR A  98      -4.490  21.196   7.791  1.00 50.66           N  
ANISOU  753  N   THR A  98    10937   3608   4705    573    703     68       N  
ATOM    754  CA  THR A  98      -5.428  20.325   8.500  1.00 48.57           C  
ANISOU  754  CA  THR A  98    10421   3489   4544    796    628     40       C  
ATOM    755  C   THR A  98      -6.547  19.883   7.557  1.00 48.74           C  
ANISOU  755  C   THR A  98    10327   3619   4573   1140    540    122       C  
ATOM    756  O   THR A  98      -7.255  20.743   7.002  1.00 48.35           O  
ANISOU  756  O   THR A  98    10448   3501   4421   1375    537    178       O  
ATOM    757  CB  THR A  98      -6.029  21.034   9.727  1.00 51.68           C  
ANISOU  757  CB  THR A  98    10911   3825   4902    921    672    -26       C  
ATOM    758  OG1 THR A  98      -4.987  21.413  10.633  1.00 51.63           O  
ANISOU  758  OG1 THR A  98    11001   3741   4876    588    739   -103       O  
ATOM    759  CG2 THR A  98      -6.995  20.113  10.452  1.00 48.60           C  
ANISOU  759  CG2 THR A  98    10245   3610   4611   1138    615    -72       C  
ATOM    760  N   PRO A  99      -6.740  18.582   7.344  1.00 47.44           N  
ANISOU  760  N   PRO A  99     9826   3679   4519   1161    457    129       N  
ATOM    761  CA  PRO A  99      -7.865  18.126   6.525  1.00 46.00           C  
ANISOU  761  CA  PRO A  99     9472   3667   4338   1470    358    196       C  
ATOM    762  C   PRO A  99      -9.159  18.153   7.325  1.00 55.49           C  
ANISOU  762  C   PRO A  99    10546   4969   5568   1790    329    155       C  
ATOM    763  O   PRO A  99      -9.169  18.333   8.550  1.00 51.43           O  
ANISOU  763  O   PRO A  99    10036   4422   5082   1752    389     68       O  
ATOM    764  CB  PRO A  99      -7.470  16.698   6.156  1.00 43.33           C  
ANISOU  764  CB  PRO A  99     8740   3612   4113   1281    297    187       C  
ATOM    765  CG  PRO A  99      -6.682  16.196   7.367  1.00 40.85           C  
ANISOU  765  CG  PRO A  99     8261   3358   3901   1010    335     96       C  
ATOM    766  CD  PRO A  99      -5.967  17.452   7.903  1.00 39.05           C  
ANISOU  766  CD  PRO A  99     8420   2831   3585    872    437     68       C  
ATOM    767  N   LYS A 100     -10.269  17.980   6.607  1.00 51.27           N  
ANISOU  767  N   LYS A 100     9892   4569   5018   2105    238    211       N  
ATOM    768  CA  LYS A 100     -11.490  17.568   7.282  1.00 49.59           C  
ANISOU  768  CA  LYS A 100     9397   4573   4872   2359    200    156       C  
ATOM    769  C   LYS A 100     -11.219  16.226   7.953  1.00 39.49           C  
ANISOU  769  C   LYS A 100     7725   3557   3721   2118    188     82       C  
ATOM    770  O   LYS A 100     -10.689  15.309   7.327  1.00 39.56           O  
ANISOU  770  O   LYS A 100     7551   3702   3777   1922    139    107       O  
ATOM    771  CB  LYS A 100     -12.653  17.470   6.295  1.00 52.37           C  
ANISOU  771  CB  LYS A 100     9613   5092   5192   2682     82    223       C  
ATOM    772  CG  LYS A 100     -13.960  17.022   6.927  1.00 64.76           C  
ANISOU  772  CG  LYS A 100    10843   6926   6837   2925     48    155       C  
ATOM    773  CD  LYS A 100     -15.187  17.518   6.157  1.00 78.80           C  
ANISOU  773  CD  LYS A 100    12550   8832   8559   3227    -45    202       C  
ATOM    774  CE  LYS A 100     -15.945  16.373   5.492  1.00 82.99           C  
ANISOU  774  CE  LYS A 100    12689   9705   9139   3313   -176    208       C  
ATOM    775  NZ  LYS A 100     -17.195  16.012   6.227  1.00 90.02           N  
ANISOU  775  NZ  LYS A 100    13229  10862  10112   3485   -181    119       N  
ATOM    776  N   TYR A 101     -11.516  16.119   9.252  1.00 42.54           N  
ANISOU  776  N   TYR A 101     8012   3997   4156   2117    244     -8       N  
ATOM    777  CA  TYR A 101     -11.146  14.888   9.932  1.00 39.50           C  
ANISOU  777  CA  TYR A 101     7312   3824   3875   1869    235    -62       C  
ATOM    778  C   TYR A 101     -12.103  14.556  11.068  1.00 34.24           C  
ANISOU  778  C   TYR A 101     6443   3319   3248   1992    268   -146       C  
ATOM    779  O   TYR A 101     -12.798  15.424  11.606  1.00 39.74           O  
ANISOU  779  O   TYR A 101     7286   3920   3894   2215    332   -188       O  
ATOM    780  CB  TYR A 101      -9.712  14.940  10.480  1.00 38.55           C  
ANISOU  780  CB  TYR A 101     7325   3562   3761   1514    284    -84       C  
ATOM    781  CG  TYR A 101      -9.593  15.812  11.712  1.00 42.97           C  
ANISOU  781  CG  TYR A 101     8115   3947   4263   1490    376   -157       C  
ATOM    782  CD1 TYR A 101      -9.445  17.176  11.594  1.00 47.50           C  
ANISOU  782  CD1 TYR A 101     9089   4227   4731   1568    445   -151       C  
ATOM    783  CD2 TYR A 101      -9.623  15.254  12.989  1.00 43.95           C  
ANISOU  783  CD2 TYR A 101     8080   4194   4426   1376    397   -232       C  
ATOM    784  CE1 TYR A 101      -9.337  17.987  12.716  1.00 51.81           C  
ANISOU  784  CE1 TYR A 101     9871   4601   5215   1533    541   -233       C  
ATOM    785  CE2 TYR A 101      -9.518  16.062  14.125  1.00 45.29           C  
ANISOU  785  CE2 TYR A 101     8479   4207   4521   1340    485   -309       C  
ATOM    786  CZ  TYR A 101      -9.371  17.419  13.974  1.00 50.56           C  
ANISOU  786  CZ  TYR A 101     9539   4582   5089   1414    558   -316       C  
ATOM    787  OH  TYR A 101      -9.266  18.234  15.090  1.00 54.96           O  
ANISOU  787  OH  TYR A 101    10348   4970   5563   1366    656   -407       O  
ATOM    788  N   LYS A 102     -12.107  13.263  11.414  1.00 39.25           N  
ANISOU  788  N   LYS A 102     6748   4192   3972   1835    235   -171       N  
ATOM    789  CA  LYS A 102     -12.796  12.714  12.573  1.00 45.81           C  
ANISOU  789  CA  LYS A 102     7373   5192   4841   1850    279   -250       C  
ATOM    790  C   LYS A 102     -11.852  11.769  13.287  1.00 39.86           C  
ANISOU  790  C   LYS A 102     6509   4495   4143   1518    273   -261       C  
ATOM    791  O   LYS A 102     -10.922  11.226  12.691  1.00 33.16           O  
ANISOU  791  O   LYS A 102     5620   3639   3341   1324    217   -210       O  
ATOM    792  CB  LYS A 102     -14.069  11.928  12.204  1.00 51.81           C  
ANISOU  792  CB  LYS A 102     7796   6237   5652   2033    235   -265       C  
ATOM    793  CG  LYS A 102     -14.972  12.603  11.203  1.00 59.76           C  
ANISOU  793  CG  LYS A 102     8835   7253   6619   2363    186   -230       C  
ATOM    794  CD  LYS A 102     -16.175  11.737  10.848  1.00 64.30           C  
ANISOU  794  CD  LYS A 102     9034   8151   7248   2501    128   -256       C  
ATOM    795  CE  LYS A 102     -17.070  12.465   9.839  1.00 79.11           C  
ANISOU  795  CE  LYS A 102    10935  10050   9072   2852     51   -214       C  
ATOM    796  NZ  LYS A 102     -18.420  11.853   9.671  1.00 81.39           N  
ANISOU  796  NZ  LYS A 102    10849  10671   9406   3032      3   -264       N  
ATOM    797  N   PHE A 103     -12.097  11.576  14.578  1.00 36.78           N  
ANISOU  797  N   PHE A 103     6074   4159   3742   1463    333   -328       N  
ATOM    798  CA  PHE A 103     -11.514  10.463  15.311  1.00 34.70           C  
ANISOU  798  CA  PHE A 103     5648   4007   3531   1200    309   -329       C  
ATOM    799  C   PHE A 103     -12.565   9.376  15.463  1.00 32.81           C  
ANISOU  799  C   PHE A 103     5094   4026   3346   1261    311   -352       C  
ATOM    800  O   PHE A 103     -13.688   9.660  15.906  1.00 36.86           O  
ANISOU  800  O   PHE A 103     5555   4624   3825   1446    382   -415       O  
ATOM    801  CB  PHE A 103     -11.053  10.884  16.708  1.00 34.66           C  
ANISOU  801  CB  PHE A 103     5817   3902   3451   1059    368   -382       C  
ATOM    802  CG  PHE A 103      -9.862  11.820  16.740  1.00 40.28           C  
ANISOU  802  CG  PHE A 103     6824   4375   4107    914    366   -373       C  
ATOM    803  CD1 PHE A 103      -9.081  12.064  15.612  1.00 38.40           C  
ANISOU  803  CD1 PHE A 103     6660   4032   3899    862    316   -312       C  
ATOM    804  CD2 PHE A 103      -9.506  12.423  17.943  1.00 38.22           C  
ANISOU  804  CD2 PHE A 103     6767   4005   3751    800    420   -436       C  
ATOM    805  CE1 PHE A 103      -7.987  12.911  15.674  1.00 37.48           C  
ANISOU  805  CE1 PHE A 103     6805   3708   3729    695    329   -316       C  
ATOM    806  CE2 PHE A 103      -8.424  13.276  18.023  1.00 43.56           C  
ANISOU  806  CE2 PHE A 103     7708   4475   4368    634    420   -443       C  
ATOM    807  CZ  PHE A 103      -7.655  13.526  16.895  1.00 43.25           C  
ANISOU  807  CZ  PHE A 103     7730   4334   4368    575    378   -384       C  
ATOM    808  N   VAL A 104     -12.187   8.133  15.145  1.00 33.22           N  
ANISOU  808  N   VAL A 104     4941   4199   3483   1094    247   -310       N  
ATOM    809  CA  VAL A 104     -13.075   6.981  15.214  1.00 27.96           C  
ANISOU  809  CA  VAL A 104     3988   3765   2871   1097    250   -330       C  
ATOM    810  C   VAL A 104     -12.372   5.851  15.939  1.00 28.09           C  
ANISOU  810  C   VAL A 104     3924   3818   2932    838    230   -303       C  
ATOM    811  O   VAL A 104     -11.175   5.615  15.743  1.00 31.12           O  
ANISOU  811  O   VAL A 104     4367   4101   3357    678    169   -248       O  
ATOM    812  CB  VAL A 104     -13.501   6.511  13.807  1.00 40.57           C  
ANISOU  812  CB  VAL A 104     5414   5477   4525   1186    185   -304       C  
ATOM    813  CG1 VAL A 104     -14.456   5.329  13.900  1.00 47.43           C  
ANISOU  813  CG1 VAL A 104     5990   6589   5443   1160    198   -341       C  
ATOM    814  CG2 VAL A 104     -14.143   7.673  13.070  1.00 42.49           C  
ANISOU  814  CG2 VAL A 104     5761   5673   4709   1461    180   -310       C  
ATOM    815  N   ARG A 105     -13.124   5.125  16.749  1.00 30.23           N  
ANISOU  815  N   ARG A 105     4053   4237   3197    801    284   -340       N  
ATOM    816  CA  ARG A 105     -12.647   3.888  17.352  1.00 28.02           C  
ANISOU  816  CA  ARG A 105     3685   4004   2958    579    261   -301       C  
ATOM    817  C   ARG A 105     -13.258   2.722  16.584  1.00 23.91           C  
ANISOU  817  C   ARG A 105     2919   3644   2523    564    247   -298       C  
ATOM    818  O   ARG A 105     -14.483   2.537  16.606  1.00 29.11           O  
ANISOU  818  O   ARG A 105     3425   4468   3166    652    310   -360       O  
ATOM    819  CB  ARG A 105     -13.018   3.816  18.837  1.00 34.43           C  
ANISOU  819  CB  ARG A 105     4548   4854   3681    507    340   -338       C  
ATOM    820  CG  ARG A 105     -12.491   2.590  19.550  1.00 31.83           C  
ANISOU  820  CG  ARG A 105     4175   4547   3370    284    307   -279       C  
ATOM    821  CD  ARG A 105     -12.737   2.712  21.076  1.00 26.07           C  
ANISOU  821  CD  ARG A 105     3562   3830   2513    202    383   -308       C  
ATOM    822  NE  ARG A 105     -12.288   1.469  21.733  1.00 27.58           N  
ANISOU  822  NE  ARG A 105     3727   4041   2711     -2    341   -233       N  
ATOM    823  CZ  ARG A 105     -11.033   1.214  22.093  1.00 28.83           C  
ANISOU  823  CZ  ARG A 105     3987   4091   2875   -137    227   -147       C  
ATOM    824  NH1 ARG A 105     -10.099   2.138  21.924  1.00 30.74           N  
ANISOU  824  NH1 ARG A 105     4359   4211   3110   -125    157   -140       N  
ATOM    825  NH2 ARG A 105     -10.727   0.032  22.663  1.00 27.25           N  
ANISOU  825  NH2 ARG A 105     3763   3907   2683   -288    184    -67       N  
ATOM    826  N   ILE A 106     -12.418   1.943  15.917  1.00 26.66           N  
ANISOU  826  N   ILE A 106     3221   3949   2958    446    174   -239       N  
ATOM    827  CA  ILE A 106     -12.916   0.903  15.009  1.00 27.70           C  
ANISOU  827  CA  ILE A 106     3151   4207   3166    425    162   -246       C  
ATOM    828  C   ILE A 106     -13.130  -0.409  15.756  1.00 32.81           C  
ANISOU  828  C   ILE A 106     3698   4928   3842    257    197   -238       C  
ATOM    829  O   ILE A 106     -12.584  -0.640  16.837  1.00 31.73           O  
ANISOU  829  O   ILE A 106     3658   4720   3680    142    200   -197       O  
ATOM    830  CB  ILE A 106     -11.973   0.696  13.813  1.00 31.55           C  
ANISOU  830  CB  ILE A 106     3649   4606   3731    389     90   -202       C  
ATOM    831  CG1 ILE A 106     -10.588   0.245  14.266  1.00 26.19           C  
ANISOU  831  CG1 ILE A 106     3050   3790   3112    227     48   -135       C  
ATOM    832  CG2 ILE A 106     -11.947   1.951  12.951  1.00 32.89           C  
ANISOU  832  CG2 ILE A 106     3928   4715   3854    552     67   -208       C  
ATOM    833  CD1 ILE A 106      -9.714  -0.337  13.142  1.00 31.25           C  
ANISOU  833  CD1 ILE A 106     3644   4374   3855    165      5   -106       C  
ATOM    834  N   GLN A 107     -13.969  -1.279  15.176  1.00 31.52           N  
ANISOU  834  N   GLN A 107     3348   4911   3716    233    222   -277       N  
ATOM    835  CA  GLN A 107     -14.234  -2.648  15.608  1.00 31.64           C  
ANISOU  835  CA  GLN A 107     3271   4986   3766     58    264   -272       C  
ATOM    836  C   GLN A 107     -13.216  -3.610  15.008  1.00 34.21           C  
ANISOU  836  C   GLN A 107     3607   5194   4195    -59    205   -210       C  
ATOM    837  O   GLN A 107     -12.692  -3.387  13.895  1.00 33.61           O  
ANISOU  837  O   GLN A 107     3530   5069   4171     -4    150   -205       O  
ATOM    838  CB  GLN A 107     -15.641  -3.105  15.188  1.00 35.36           C  
ANISOU  838  CB  GLN A 107     3530   5677   4228     69    326   -362       C  
ATOM    839  CG  GLN A 107     -16.793  -2.387  15.876  1.00 37.00           C  
ANISOU  839  CG  GLN A 107     3672   6036   4349    176    411   -440       C  
ATOM    840  CD  GLN A 107     -16.936  -2.776  17.341  1.00 46.81           C  
ANISOU  840  CD  GLN A 107     4981   7274   5531     39    507   -434       C  
ATOM    841  OE1 GLN A 107     -16.352  -3.764  17.797  1.00 44.86           O  
ANISOU  841  OE1 GLN A 107     4804   6936   5306   -147    505   -368       O  
ATOM    842  NE2 GLN A 107     -17.712  -1.990  18.091  1.00 40.54           N  
ANISOU  842  NE2 GLN A 107     4178   6571   4652    137    597   -501       N  
ATOM    843  N   PRO A 108     -12.928  -4.691  15.729  1.00 30.18           N  
ANISOU  843  N   PRO A 108     3122   4633   3713   -216    224   -162       N  
ATOM    844  CA  PRO A 108     -12.059  -5.719  15.166  1.00 26.84           C  
ANISOU  844  CA  PRO A 108     2699   4097   3402   -308    183   -112       C  
ATOM    845  C   PRO A 108     -12.638  -6.185  13.844  1.00 26.33           C  
ANISOU  845  C   PRO A 108     2496   4123   3384   -306    202   -184       C  
ATOM    846  O   PRO A 108     -13.853  -6.248  13.669  1.00 32.34           O  
ANISOU  846  O   PRO A 108     3136   5056   4097   -305    255   -263       O  
ATOM    847  CB  PRO A 108     -12.079  -6.846  16.210  1.00 31.07           C  
ANISOU  847  CB  PRO A 108     3281   4588   3935   -462    220    -58       C  
ATOM    848  CG  PRO A 108     -12.869  -6.382  17.330  1.00 35.82           C  
ANISOU  848  CG  PRO A 108     3915   5282   4413   -470    282    -79       C  
ATOM    849  CD  PRO A 108     -13.454  -5.033  17.064  1.00 33.77           C  
ANISOU  849  CD  PRO A 108     3613   5128   4088   -311    294   -155       C  
ATOM    850  N   GLY A 109     -11.755  -6.463  12.907  1.00 28.66           N  
ANISOU  850  N   GLY A 109     2804   4317   3768   -308    159   -165       N  
ATOM    851  CA  GLY A 109     -12.147  -6.899  11.583  1.00 29.29           C  
ANISOU  851  CA  GLY A 109     2782   4466   3879   -320    170   -235       C  
ATOM    852  C   GLY A 109     -12.186  -5.786  10.564  1.00 34.30           C  
ANISOU  852  C   GLY A 109     3410   5153   4470   -178    124   -267       C  
ATOM    853  O   GLY A 109     -12.168  -6.054   9.347  1.00 30.02           O  
ANISOU  853  O   GLY A 109     2825   4634   3948   -186    115   -309       O  
ATOM    854  N   GLN A 110     -12.228  -4.541  11.022  1.00 26.76           N  
ANISOU  854  N   GLN A 110     2521   4202   3444    -52     99   -248       N  
ATOM    855  CA  GLN A 110     -12.160  -3.385  10.140  1.00 29.92           C  
ANISOU  855  CA  GLN A 110     2967   4606   3793     93     55   -257       C  
ATOM    856  C   GLN A 110     -10.722  -3.130   9.692  1.00 29.45           C  
ANISOU  856  C   GLN A 110     3028   4371   3791     71     27   -205       C  
ATOM    857  O   GLN A 110      -9.756  -3.477  10.376  1.00 31.34           O  
ANISOU  857  O   GLN A 110     3318   4490   4099    -11     25   -154       O  
ATOM    858  CB  GLN A 110     -12.739  -2.154  10.852  1.00 30.07           C  
ANISOU  858  CB  GLN A 110     3040   4667   3718    238     56   -260       C  
ATOM    859  CG  GLN A 110     -14.227  -2.272  11.099  1.00 41.38           C  
ANISOU  859  CG  GLN A 110     4318   6307   5096    289     93   -330       C  
ATOM    860  CD  GLN A 110     -14.978  -2.648   9.830  1.00 57.13           C  
ANISOU  860  CD  GLN A 110     6164   8458   7083    311     62   -388       C  
ATOM    861  OE1 GLN A 110     -15.058  -1.850   8.890  1.00 58.42           O  
ANISOU  861  OE1 GLN A 110     6360   8639   7198    452      2   -388       O  
ATOM    862  NE2 GLN A 110     -15.514  -3.871   9.789  1.00 58.01           N  
ANISOU  862  NE2 GLN A 110     6132   8678   7230    159     99   -438       N  
ATOM    863  N   THR A 111     -10.576  -2.529   8.518  1.00 27.80           N  
ANISOU  863  N   THR A 111     2858   4157   3549    141      4   -218       N  
ATOM    864  CA  THR A 111      -9.263  -2.279   7.947  1.00 26.11           C  
ANISOU  864  CA  THR A 111     2743   3796   3383    103      0   -186       C  
ATOM    865  C   THR A 111      -8.965  -0.781   7.952  1.00 27.35           C  
ANISOU  865  C   THR A 111     3056   3878   3457    206    -21   -156       C  
ATOM    866  O   THR A 111      -9.865   0.046   8.074  1.00 31.91           O  
ANISOU  866  O   THR A 111     3669   4519   3937    340    -37   -166       O  
ATOM    867  CB  THR A 111      -9.199  -2.789   6.503  1.00 28.34           C  
ANISOU  867  CB  THR A 111     2987   4106   3676     68     12   -227       C  
ATOM    868  OG1 THR A 111     -10.306  -2.214   5.815  1.00 30.77           O  
ANISOU  868  OG1 THR A 111     3280   4546   3864    182    -23   -258       O  
ATOM    869  CG2 THR A 111      -9.333  -4.302   6.475  1.00 31.16           C  
ANISOU  869  CG2 THR A 111     3223   4492   4123    -55     48   -263       C  
ATOM    870  N   PHE A 112      -7.688  -0.443   7.780  1.00 29.09           N  
ANISOU  870  N   PHE A 112     3372   3962   3720    142    -14   -126       N  
ATOM    871  CA  PHE A 112      -7.272   0.953   7.719  1.00 30.55           C  
ANISOU  871  CA  PHE A 112     3735   4047   3825    199    -18   -102       C  
ATOM    872  C   PHE A 112      -5.874   1.007   7.136  1.00 26.37           C  
ANISOU  872  C   PHE A 112     3258   3405   3359     84      9    -91       C  
ATOM    873  O   PHE A 112      -5.155   0.012   7.118  1.00 29.59           O  
ANISOU  873  O   PHE A 112     3553   3803   3886    -20     24    -96       O  
ATOM    874  CB  PHE A 112      -7.308   1.641   9.104  1.00 29.17           C  
ANISOU  874  CB  PHE A 112     3641   3828   3613    223    -30    -83       C  
ATOM    875  CG  PHE A 112      -6.506   0.938  10.166  1.00 31.09           C  
ANISOU  875  CG  PHE A 112     3826   4039   3948     93    -44    -59       C  
ATOM    876  CD1 PHE A 112      -7.051  -0.125  10.861  1.00 32.74           C  
ANISOU  876  CD1 PHE A 112     3909   4331   4199     64    -48    -59       C  
ATOM    877  CD2 PHE A 112      -5.229   1.380  10.489  1.00 27.67           C  
ANISOU  877  CD2 PHE A 112     3470   3495   3547     -4    -58    -35       C  
ATOM    878  CE1 PHE A 112      -6.312  -0.771  11.865  1.00 32.33           C  
ANISOU  878  CE1 PHE A 112     3828   4240   4217    -41    -77    -18       C  
ATOM    879  CE2 PHE A 112      -4.477   0.735  11.488  1.00 32.98           C  
ANISOU  879  CE2 PHE A 112     4078   4154   4298   -109    -98     -4       C  
ATOM    880  CZ  PHE A 112      -5.025  -0.322  12.175  1.00 28.28           C  
ANISOU  880  CZ  PHE A 112     3380   3629   3737   -115   -113     12       C  
ATOM    881  N   SER A 113      -5.500   2.188   6.663  1.00 27.36           N  
ANISOU  881  N   SER A 113     3557   3437   3400    107     24    -78       N  
ATOM    882  CA  SER A 113      -4.155   2.437   6.174  1.00 23.91           C  
ANISOU  882  CA  SER A 113     3181   2897   3008    -21     68    -75       C  
ATOM    883  C   SER A 113      -3.285   2.965   7.306  1.00 29.32           C  
ANISOU  883  C   SER A 113     3917   3499   3724   -107     54    -58       C  
ATOM    884  O   SER A 113      -3.728   3.795   8.085  1.00 32.09           O  
ANISOU  884  O   SER A 113     4387   3817   3989    -46     31    -47       O  
ATOM    885  CB  SER A 113      -4.197   3.451   5.031  1.00 29.46           C  
ANISOU  885  CB  SER A 113     4075   3534   3585     18    101    -68       C  
ATOM    886  OG  SER A 113      -5.005   2.888   3.996  1.00 30.72           O  
ANISOU  886  OG  SER A 113     4175   3793   3704     89     94    -85       O  
ATOM    887  N   VAL A 114      -2.033   2.525   7.337  1.00 30.86           N  
ANISOU  887  N   VAL A 114     4023   3666   4035   -248     71    -64       N  
ATOM    888  CA  VAL A 114      -1.022   3.034   8.257  1.00 30.77           C  
ANISOU  888  CA  VAL A 114     4043   3596   4052   -361     48    -56       C  
ATOM    889  C   VAL A 114       0.008   3.816   7.468  1.00 30.76           C  
ANISOU  889  C   VAL A 114     4139   3511   4037   -481    118    -77       C  
ATOM    890  O   VAL A 114       0.529   3.321   6.449  1.00 33.31           O  
ANISOU  890  O   VAL A 114     4382   3848   4427   -533    182   -101       O  
ATOM    891  CB  VAL A 114      -0.334   1.885   9.015  1.00 29.14           C  
ANISOU  891  CB  VAL A 114     3627   3444   3999   -426     -4    -42       C  
ATOM    892  CG1 VAL A 114       0.914   2.437   9.731  1.00 30.84           C  
ANISOU  892  CG1 VAL A 114     3848   3623   4246   -566    -39    -41       C  
ATOM    893  CG2 VAL A 114      -1.317   1.181   9.950  1.00 31.59           C  
ANISOU  893  CG2 VAL A 114     3881   3820   4302   -339    -64    -14       C  
ATOM    894  N   LEU A 115       0.312   5.028   7.939  1.00 27.92           N  
ANISOU  894  N   LEU A 115     3962   3060   3584   -541    121    -77       N  
ATOM    895  CA  LEU A 115       1.420   5.804   7.394  1.00 29.25           C  
ANISOU  895  CA  LEU A 115     4228   3146   3741   -706    194   -103       C  
ATOM    896  C   LEU A 115       2.589   5.693   8.360  1.00 36.74           C  
ANISOU  896  C   LEU A 115     5047   4126   4787   -869    147   -120       C  
ATOM    897  O   LEU A 115       2.645   6.416   9.367  1.00 35.97           O  
ANISOU  897  O   LEU A 115     5062   3987   4619   -918     98   -121       O  
ATOM    898  CB  LEU A 115       1.033   7.258   7.167  1.00 28.52           C  
ANISOU  898  CB  LEU A 115     4454   2912   3472   -687    240    -95       C  
ATOM    899  CG  LEU A 115       2.102   8.169   6.536  1.00 35.27           C  
ANISOU  899  CG  LEU A 115     5461   3655   4283   -882    338   -122       C  
ATOM    900  CD1 LEU A 115       2.358   7.753   5.065  1.00 33.57           C  
ANISOU  900  CD1 LEU A 115     5207   3460   4087   -909    430   -129       C  
ATOM    901  CD2 LEU A 115       1.750   9.638   6.612  1.00 33.37           C  
ANISOU  901  CD2 LEU A 115     5574   3239   3867   -871    375   -109       C  
ATOM    902  N   ALA A 116       3.526   4.809   8.037  1.00 29.32           N  
ANISOU  902  N   ALA A 116     3874   3261   4005   -949    161   -140       N  
ATOM    903  CA  ALA A 116       4.724   4.635   8.853  1.00 33.30           C  
ANISOU  903  CA  ALA A 116     4211   3823   4617  -1092    100   -156       C  
ATOM    904  C   ALA A 116       5.659   5.829   8.714  1.00 38.78           C  
ANISOU  904  C   ALA A 116     5028   4454   5251  -1300    163   -203       C  
ATOM    905  O   ALA A 116       6.051   6.220   7.591  1.00 38.95           O  
ANISOU  905  O   ALA A 116     5116   4427   5255  -1384    292   -238       O  
ATOM    906  CB  ALA A 116       5.447   3.336   8.487  1.00 32.03           C  
ANISOU  906  CB  ALA A 116     3755   3758   4657  -1086    105   -167       C  
ATOM    907  N   CYS A 117       6.047   6.384   9.883  1.00 31.01           N  
ANISOU  907  N   CYS A 117     4081   3474   4227  -1405     76   -209       N  
ATOM    908  CA  CYS A 117       6.762   7.642   9.983  1.00 33.39           C  
ANISOU  908  CA  CYS A 117     4551   3700   4436  -1620    124   -259       C  
ATOM    909  C   CYS A 117       7.917   7.528  10.963  1.00 40.30           C  
ANISOU  909  C   CYS A 117     5228   4690   5395  -1797     19   -289       C  
ATOM    910  O   CYS A 117       7.820   6.819  11.965  1.00 41.26           O  
ANISOU  910  O   CYS A 117     5204   4906   5567  -1722   -125   -250       O  
ATOM    911  CB  CYS A 117       5.856   8.761  10.475  1.00 45.52           C  
ANISOU  911  CB  CYS A 117     6428   5091   5775  -1577    127   -250       C  
ATOM    912  SG  CYS A 117       4.628   9.306   9.298  1.00 48.10           S  
ANISOU  912  SG  CYS A 117     7038   5268   5970  -1393    244   -218       S  
ATOM    913  N   TYR A 118       9.000   8.244  10.673  1.00 44.16           N  
ANISOU  913  N   TYR A 118     5716   5176   5886  -2041     89   -358       N  
ATOM    914  CA  TYR A 118      10.167   8.310  11.554  1.00 44.15           C  
ANISOU  914  CA  TYR A 118     5525   5302   5948  -2245    -15   -402       C  
ATOM    915  C   TYR A 118      10.657   9.744  11.623  1.00 52.73           C  
ANISOU  915  C   TYR A 118     6853   6292   6892  -2484     60   -470       C  
ATOM    916  O   TYR A 118      10.939  10.365  10.589  1.00 48.93           O  
ANISOU  916  O   TYR A 118     6490   5730   6373  -2544    222   -500       O  
ATOM    917  CB  TYR A 118      11.283   7.372  11.083  1.00 47.52           C  
ANISOU  917  CB  TYR A 118     5561   5898   6596  -2287    -12   -429       C  
ATOM    918  CG  TYR A 118      10.793   5.948  11.068  1.00 45.25           C  
ANISOU  918  CG  TYR A 118     5070   5678   6445  -2022    -82   -357       C  
ATOM    919  CD1 TYR A 118      10.864   5.158  12.217  1.00 39.53           C  
ANISOU  919  CD1 TYR A 118     4169   5063   5787  -1931   -276   -299       C  
ATOM    920  CD2 TYR A 118      10.178   5.413   9.938  1.00 42.28           C  
ANISOU  920  CD2 TYR A 118     4719   5242   6105  -1867     42   -342       C  
ATOM    921  CE1 TYR A 118      10.376   3.879  12.228  1.00 36.86           C  
ANISOU  921  CE1 TYR A 118     3690   4755   5559  -1701   -330   -229       C  
ATOM    922  CE2 TYR A 118       9.679   4.126   9.944  1.00 41.10           C  
ANISOU  922  CE2 TYR A 118     4415   5135   6068  -1646    -13   -285       C  
ATOM    923  CZ  TYR A 118       9.785   3.362  11.094  1.00 39.47           C  
ANISOU  923  CZ  TYR A 118     4043   5019   5936  -1565   -193   -228       C  
ATOM    924  OH  TYR A 118       9.299   2.076  11.123  1.00 37.95           O  
ANISOU  924  OH  TYR A 118     3726   4844   5847  -1360   -239   -168       O  
ATOM    925  N   ASN A 119      10.762  10.267  12.848  1.00 45.63           N  
ANISOU  925  N   ASN A 119     6035   5406   5897  -2566    -56   -483       N  
ATOM    926  CA  ASN A 119      11.228  11.636  13.073  1.00 47.97           C  
ANISOU  926  CA  ASN A 119     6563   5618   6045  -2737      7   -542       C  
ATOM    927  C   ASN A 119      10.368  12.641  12.307  1.00 44.92           C  
ANISOU  927  C   ASN A 119     6584   4989   5495  -2698    174   -539       C  
ATOM    928  O   ASN A 119      10.867  13.629  11.763  1.00 50.55           O  
ANISOU  928  O   ASN A 119     7461   5622   6125  -2821    300   -578       O  
ATOM    929  CB  ASN A 119      12.706  11.788  12.706  1.00 53.26           C  
ANISOU  929  CB  ASN A 119     7003   6419   6815  -2901     46   -601       C  
ATOM    930  CG  ASN A 119      13.608  10.943  13.578  1.00 60.58           C  
ANISOU  930  CG  ASN A 119     7549   7575   7894  -2922   -138   -603       C  
ATOM    931  OD1 ASN A 119      14.022   9.855  13.184  1.00 65.88           O  
ANISOU  931  OD1 ASN A 119     7897   8374   8759  -2828   -170   -581       O  
ATOM    932  ND2 ASN A 119      13.908  11.435  14.778  1.00 65.05           N  
ANISOU  932  ND2 ASN A 119     8161   8188   8366  -3034   -260   -628       N  
ATOM    933  N   GLY A 120       9.061  12.378  12.265  1.00 43.12           N  
ANISOU  933  N   GLY A 120     6525   4643   5216  -2517    169   -487       N  
ATOM    934  CA  GLY A 120       8.117  13.278  11.648  1.00 45.85           C  
ANISOU  934  CA  GLY A 120     7261   4753   5407  -2421    296   -468       C  
ATOM    935  C   GLY A 120       8.036  13.158  10.145  1.00 48.61           C  
ANISOU  935  C   GLY A 120     7635   5048   5787  -2363    433   -442       C  
ATOM    936  O   GLY A 120       7.322  13.947   9.520  1.00 49.24           O  
ANISOU  936  O   GLY A 120     8044   4935   5729  -2272    533   -414       O  
ATOM    937  N   SER A 121       8.743  12.203   9.549  1.00 44.56           N  
ANISOU  937  N   SER A 121     6791   4699   5442  -2399    440   -448       N  
ATOM    938  CA  SER A 121       8.815  12.075   8.094  1.00 39.33           C  
ANISOU  938  CA  SER A 121     6140   4004   4797  -2374    583   -437       C  
ATOM    939  C   SER A 121       8.200  10.756   7.641  1.00 40.87           C  
ANISOU  939  C   SER A 121     6116   4298   5115  -2152    545   -388       C  
ATOM    940  O   SER A 121       8.693   9.680   8.029  1.00 45.29           O  
ANISOU  940  O   SER A 121     6323   5039   5848  -2132    459   -397       O  
ATOM    941  CB  SER A 121      10.267  12.181   7.625  1.00 51.80           C  
ANISOU  941  CB  SER A 121     7518   5711   6454  -2560    657   -500       C  
ATOM    942  OG  SER A 121      10.349  12.206   6.203  1.00 64.97           O  
ANISOU  942  OG  SER A 121     9252   7336   8099  -2557    813   -498       O  
ATOM    943  N   PRO A 122       7.146  10.785   6.817  1.00 42.94           N  
ANISOU  943  N   PRO A 122     6563   4464   5289  -1950    596   -332       N  
ATOM    944  CA  PRO A 122       6.556   9.534   6.322  1.00 43.79           C  
ANISOU  944  CA  PRO A 122     6458   4683   5498  -1733    562   -294       C  
ATOM    945  C   PRO A 122       7.560   8.687   5.557  1.00 43.55           C  
ANISOU  945  C   PRO A 122     6143   4776   5628  -1841    639   -342       C  
ATOM    946  O   PRO A 122       8.336   9.185   4.734  1.00 43.54           O  
ANISOU  946  O   PRO A 122     6207   4735   5602  -2033    781   -389       O  
ATOM    947  CB  PRO A 122       5.418  10.018   5.418  1.00 48.12           C  
ANISOU  947  CB  PRO A 122     7298   5098   5886  -1562    618   -240       C  
ATOM    948  CG  PRO A 122       5.038  11.331   5.982  1.00 55.51           C  
ANISOU  948  CG  PRO A 122     8572   5862   6659  -1576    616   -228       C  
ATOM    949  CD  PRO A 122       6.337  11.960   6.438  1.00 44.04           C  
ANISOU  949  CD  PRO A 122     7124   4386   5222  -1887    663   -297       C  
ATOM    950  N   SER A 123       7.534   7.393   5.865  1.00 48.10           N  
ANISOU  950  N   SER A 123     6413   5496   6368  -1717    553   -333       N  
ATOM    951  CA  SER A 123       8.347   6.328   5.296  1.00 47.63           C  
ANISOU  951  CA  SER A 123     6042   5560   6494  -1747    607   -376       C  
ATOM    952  C   SER A 123       7.586   5.505   4.269  1.00 45.11           C  
ANISOU  952  C   SER A 123     5716   5242   6182  -1576    664   -359       C  
ATOM    953  O   SER A 123       8.135   5.150   3.217  1.00 42.17           O  
ANISOU  953  O   SER A 123     5262   4895   5865  -1644    799   -411       O  
ATOM    954  CB  SER A 123       8.817   5.395   6.423  1.00 49.31           C  
ANISOU  954  CB  SER A 123     5940   5910   6883  -1704    458   -369       C  
ATOM    955  OG  SER A 123       9.805   4.474   5.997  1.00 61.62           O  
ANISOU  955  OG  SER A 123     7186   7585   8643  -1739    510   -419       O  
ATOM    956  N   GLY A 124       6.343   5.173   4.571  1.00 32.40           N  
ANISOU  956  N   GLY A 124     4180   3618   4515  -1370    569   -298       N  
ATOM    957  CA  GLY A 124       5.609   4.283   3.683  1.00 28.78           C  
ANISOU  957  CA  GLY A 124     3683   3184   4067  -1224    604   -292       C  
ATOM    958  C   GLY A 124       4.179   4.159   4.133  1.00 36.02           C  
ANISOU  958  C   GLY A 124     4698   4093   4896  -1025    494   -230       C  
ATOM    959  O   GLY A 124       3.800   4.589   5.230  1.00 34.43           O  
ANISOU  959  O   GLY A 124     4557   3874   4651   -984    394   -194       O  
ATOM    960  N   VAL A 125       3.376   3.553   3.278  1.00 27.20           N  
ANISOU  960  N   VAL A 125     3589   2999   3747   -911    520   -228       N  
ATOM    961  CA  VAL A 125       1.959   3.398   3.565  1.00 28.22           C  
ANISOU  961  CA  VAL A 125     3783   3148   3793   -728    428   -182       C  
ATOM    962  C   VAL A 125       1.551   1.967   3.238  1.00 33.82           C  
ANISOU  962  C   VAL A 125     4299   3946   4605   -651    421   -203       C  
ATOM    963  O   VAL A 125       2.016   1.378   2.251  1.00 33.60           O  
ANISOU  963  O   VAL A 125     4202   3934   4632   -706    517   -252       O  
ATOM    964  CB  VAL A 125       1.125   4.461   2.801  1.00 36.18           C  
ANISOU  964  CB  VAL A 125     5074   4082   4591   -660    450   -152       C  
ATOM    965  CG1 VAL A 125       1.237   4.271   1.306  1.00 41.49           C  
ANISOU  965  CG1 VAL A 125     5801   4756   5209   -700    551   -180       C  
ATOM    966  CG2 VAL A 125      -0.329   4.443   3.241  1.00 35.07           C  
ANISOU  966  CG2 VAL A 125     4973   3981   4370   -461    348   -112       C  
ATOM    967  N   TYR A 126       0.745   1.368   4.114  1.00 32.11           N  
ANISOU  967  N   TYR A 126     3998   3782   4419   -542    323   -173       N  
ATOM    968  CA  TYR A 126       0.284   0.002   3.877  1.00 31.78           C  
ANISOU  968  CA  TYR A 126     3799   3809   4467   -485    321   -194       C  
ATOM    969  C   TYR A 126      -1.060  -0.198   4.557  1.00 33.54           C  
ANISOU  969  C   TYR A 126     4030   4087   4626   -363    230   -161       C  
ATOM    970  O   TYR A 126      -1.446   0.555   5.449  1.00 33.77           O  
ANISOU  970  O   TYR A 126     4143   4105   4583   -319    168   -123       O  
ATOM    971  CB  TYR A 126       1.295  -1.075   4.331  1.00 30.00           C  
ANISOU  971  CB  TYR A 126     3359   3590   4448   -537    328   -210       C  
ATOM    972  CG  TYR A 126       1.727  -0.936   5.786  1.00 31.81           C  
ANISOU  972  CG  TYR A 126     3530   3819   4739   -547    227   -159       C  
ATOM    973  CD1 TYR A 126       0.950  -1.455   6.817  1.00 37.62           C  
ANISOU  973  CD1 TYR A 126     4236   4584   5473   -469    133   -112       C  
ATOM    974  CD2 TYR A 126       2.886  -0.268   6.103  1.00 34.00           C  
ANISOU  974  CD2 TYR A 126     3789   4075   5055   -653    228   -164       C  
ATOM    975  CE1 TYR A 126       1.343  -1.302   8.173  1.00 37.13           C  
ANISOU  975  CE1 TYR A 126     4145   4525   5437   -489     33    -62       C  
ATOM    976  CE2 TYR A 126       3.288  -0.111   7.445  1.00 38.52           C  
ANISOU  976  CE2 TYR A 126     4315   4662   5660   -676    118   -120       C  
ATOM    977  CZ  TYR A 126       2.509  -0.639   8.457  1.00 36.69           C  
ANISOU  977  CZ  TYR A 126     4072   4454   5416   -589     19    -66       C  
ATOM    978  OH  TYR A 126       2.914  -0.485   9.778  1.00 43.45           O  
ANISOU  978  OH  TYR A 126     4903   5328   6279   -623    -94    -21       O  
ATOM    979  N   GLN A 127      -1.788  -1.215   4.104  1.00 28.87           N  
ANISOU  979  N   GLN A 127     3355   3560   4056   -320    238   -188       N  
ATOM    980  CA  GLN A 127      -3.103  -1.547   4.641  1.00 30.62           C  
ANISOU  980  CA  GLN A 127     3551   3859   4224   -228    172   -173       C  
ATOM    981  C   GLN A 127      -3.001  -2.619   5.729  1.00 30.01           C  
ANISOU  981  C   GLN A 127     3337   3789   4276   -246    138   -154       C  
ATOM    982  O   GLN A 127      -2.213  -3.564   5.617  1.00 35.81           O  
ANISOU  982  O   GLN A 127     3969   4485   5151   -301    173   -168       O  
ATOM    983  CB  GLN A 127      -3.998  -2.019   3.481  1.00 35.12           C  
ANISOU  983  CB  GLN A 127     4114   4508   4723   -200    196   -221       C  
ATOM    984  CG  GLN A 127      -5.487  -2.058   3.738  1.00 33.45           C  
ANISOU  984  CG  GLN A 127     3881   4411   4416   -104    132   -221       C  
ATOM    985  CD  GLN A 127      -6.166  -0.698   3.780  1.00 29.82           C  
ANISOU  985  CD  GLN A 127     3556   3970   3805     16     82   -187       C  
ATOM    986  OE1 GLN A 127      -5.523   0.356   3.832  1.00 35.45           O  
ANISOU  986  OE1 GLN A 127     4411   4584   4477     20     92   -153       O  
ATOM    987  NE2 GLN A 127      -7.485  -0.723   3.847  1.00 33.84           N  
ANISOU  987  NE2 GLN A 127     4017   4605   4236    116     31   -199       N  
ATOM    988  N   CYS A 128      -3.848  -2.490   6.758  1.00 32.69           N  
ANISOU  988  N   CYS A 128     3685   4173   4561   -191     76   -121       N  
ATOM    989  CA  CYS A 128      -3.851  -3.318   7.973  1.00 35.43           C  
ANISOU  989  CA  CYS A 128     3953   4521   4987   -211     35    -84       C  
ATOM    990  C   CYS A 128      -5.285  -3.683   8.293  1.00 32.36           C  
ANISOU  990  C   CYS A 128     3541   4230   4525   -166     26    -96       C  
ATOM    991  O   CYS A 128      -6.205  -2.945   7.945  1.00 32.81           O  
ANISOU  991  O   CYS A 128     3645   4358   4462    -93     23   -120       O  
ATOM    992  CB  CYS A 128      -3.334  -2.549   9.225  1.00 33.43           C  
ANISOU  992  CB  CYS A 128     3761   4230   4712   -222    -28    -30       C  
ATOM    993  SG  CYS A 128      -1.609  -2.585   9.413  1.00 51.62           S  
ANISOU  993  SG  CYS A 128     6013   6454   7145   -305    -48     -6       S  
ATOM    994  N   ALA A 129      -5.488  -4.777   9.039  1.00 30.37           N  
ANISOU  994  N   ALA A 129     3220   3981   4339   -207     21    -76       N  
ATOM    995  CA  ALA A 129      -6.778  -4.973   9.692  1.00 24.26           C  
ANISOU  995  CA  ALA A 129     2429   3304   3485   -190     19    -83       C  
ATOM    996  C   ALA A 129      -6.562  -4.981  11.208  1.00 27.41           C  
ANISOU  996  C   ALA A 129     2867   3669   3879   -213    -23    -16       C  
ATOM    997  O   ALA A 129      -5.530  -5.445  11.685  1.00 30.81           O  
ANISOU  997  O   ALA A 129     3297   4009   4401   -257    -58     38       O  
ATOM    998  CB  ALA A 129      -7.431  -6.275   9.273  1.00 30.30           C  
ANISOU  998  CB  ALA A 129     3108   4112   4294   -251     66   -126       C  
ATOM    999  N   MET A 130      -7.528  -4.462  11.952  1.00 25.47           N  
ANISOU  999  N   MET A 130     2653   3504   3522   -179    -22    -23       N  
ATOM   1000  CA  MET A 130      -7.525  -4.729  13.400  1.00 27.12           C  
ANISOU 1000  CA  MET A 130     2904   3697   3704   -227    -44     33       C  
ATOM   1001  C   MET A 130      -7.892  -6.194  13.623  1.00 26.21           C  
ANISOU 1001  C   MET A 130     2730   3582   3645   -312    -11     47       C  
ATOM   1002  O   MET A 130      -9.004  -6.621  13.284  1.00 30.79           O  
ANISOU 1002  O   MET A 130     3244   4262   4194   -331     50    -12       O  
ATOM   1003  CB  MET A 130      -8.506  -3.796  14.102  1.00 30.24           C  
ANISOU 1003  CB  MET A 130     3351   4180   3960   -170    -23      4       C  
ATOM   1004  CG  MET A 130      -8.725  -4.033  15.604  1.00 31.70           C  
ANISOU 1004  CG  MET A 130     3595   4370   4078   -233    -22     45       C  
ATOM   1005  SD  MET A 130      -7.224  -3.579  16.460  1.00 33.28           S  
ANISOU 1005  SD  MET A 130     3915   4445   4286   -277   -123    127       S  
ATOM   1006  CE  MET A 130      -7.069  -1.848  16.001  1.00 31.34           C  
ANISOU 1006  CE  MET A 130     3758   4181   3967   -184   -122     72       C  
ATOM   1007  N   ARG A 131      -6.964  -6.979  14.187  1.00 25.65           N  
ANISOU 1007  N   ARG A 131     2685   3401   3659   -366    -54    125       N  
ATOM   1008  CA  ARG A 131      -7.220  -8.399  14.363  1.00 29.12           C  
ANISOU 1008  CA  ARG A 131     3110   3799   4157   -443    -17    149       C  
ATOM   1009  C   ARG A 131      -8.305  -8.595  15.425  1.00 28.08           C  
ANISOU 1009  C   ARG A 131     3022   3741   3906   -507     24    157       C  
ATOM   1010  O   ARG A 131      -8.555  -7.692  16.239  1.00 30.74           O  
ANISOU 1010  O   ARG A 131     3413   4136   4131   -484      6    165       O  
ATOM   1011  CB  ARG A 131      -5.942  -9.146  14.757  1.00 28.09           C  
ANISOU 1011  CB  ARG A 131     3007   3520   4144   -450    -85    244       C  
ATOM   1012  CG  ARG A 131      -4.755  -8.945  13.831  1.00 30.69           C  
ANISOU 1012  CG  ARG A 131     3275   3787   4601   -393   -113    230       C  
ATOM   1013  CD  ARG A 131      -5.056  -9.440  12.411  1.00 28.98           C  
ANISOU 1013  CD  ARG A 131     2989   3571   4450   -397    -21    138       C  
ATOM   1014  NE  ARG A 131      -5.752 -10.709  12.437  1.00 30.18           N  
ANISOU 1014  NE  ARG A 131     3153   3689   4624   -466     44    129       N  
ATOM   1015  CZ  ARG A 131      -6.275 -11.262  11.343  1.00 35.31           C  
ANISOU 1015  CZ  ARG A 131     3761   4355   5300   -505    130     38       C  
ATOM   1016  NH1 ARG A 131      -6.155 -10.629  10.185  1.00 29.82           N  
ANISOU 1016  NH1 ARG A 131     3014   3713   4601   -468    150    -39       N  
ATOM   1017  NH2 ARG A 131      -6.919 -12.415  11.408  1.00 33.96           N  
ANISOU 1017  NH2 ARG A 131     3616   4145   5141   -596    196     21       N  
ATOM   1018  N   PRO A 132      -8.964  -9.754  15.434  1.00 27.10           N  
ANISOU 1018  N   PRO A 132     2885   3613   3798   -602     94    147       N  
ATOM   1019  CA  PRO A 132      -9.938 -10.037  16.502  1.00 27.09           C  
ANISOU 1019  CA  PRO A 132     2933   3679   3682   -694    152    157       C  
ATOM   1020  C   PRO A 132      -9.347  -9.951  17.895  1.00 28.18           C  
ANISOU 1020  C   PRO A 132     3209   3741   3757   -713     86    270       C  
ATOM   1021  O   PRO A 132     -10.098  -9.721  18.860  1.00 27.90           O  
ANISOU 1021  O   PRO A 132     3229   3783   3587   -769    133    268       O  
ATOM   1022  CB  PRO A 132     -10.409 -11.463  16.183  1.00 32.41           C  
ANISOU 1022  CB  PRO A 132     3598   4306   4410   -818    234    140       C  
ATOM   1023  CG  PRO A 132     -10.278 -11.542  14.677  1.00 32.67           C  
ANISOU 1023  CG  PRO A 132     3525   4348   4541   -776    245     56       C  
ATOM   1024  CD  PRO A 132      -9.072 -10.735  14.320  1.00 27.33           C  
ANISOU 1024  CD  PRO A 132     2851   3605   3927   -645    151     92       C  
ATOM   1025  N   ASN A 133      -8.036 -10.156  18.029  1.00 30.66           N  
ANISOU 1025  N   ASN A 133     3574   3918   4159   -670    -21    364       N  
ATOM   1026  CA  ASN A 133      -7.382 -10.046  19.337  1.00 28.81           C  
ANISOU 1026  CA  ASN A 133     3467   3626   3853   -685   -117    479       C  
ATOM   1027  C   ASN A 133      -6.834  -8.654  19.557  1.00 30.94           C  
ANISOU 1027  C   ASN A 133     3741   3946   4067   -617   -196    465       C  
ATOM   1028  O   ASN A 133      -6.042  -8.452  20.490  1.00 31.50           O  
ANISOU 1028  O   ASN A 133     3901   3976   4093   -626   -305    552       O  
ATOM   1029  CB  ASN A 133      -6.291 -11.134  19.507  1.00 28.56           C  
ANISOU 1029  CB  ASN A 133     3482   3427   3941   -674   -206    601       C  
ATOM   1030  CG  ASN A 133      -5.065 -10.892  18.627  1.00 27.69           C  
ANISOU 1030  CG  ASN A 133     3266   3263   3992   -567   -285    596       C  
ATOM   1031  OD1 ASN A 133      -5.037  -9.955  17.848  1.00 30.88           O  
ANISOU 1031  OD1 ASN A 133     3583   3742   4409   -521   -266    506       O  
ATOM   1032  ND2 ASN A 133      -4.077 -11.767  18.729  1.00 30.14           N  
ANISOU 1032  ND2 ASN A 133     3587   3440   4425   -524   -363    691       N  
ATOM   1033  N   PHE A 134      -7.237  -7.685  18.714  1.00 23.11           N  
ANISOU 1033  N   PHE A 134     2670   3041   3071   -553   -147    358       N  
ATOM   1034  CA  PHE A 134      -6.939  -6.261  18.919  1.00 28.24           C  
ANISOU 1034  CA  PHE A 134     3359   3727   3645   -499   -188    327       C  
ATOM   1035  C   PHE A 134      -5.450  -5.954  18.820  1.00 30.07           C  
ANISOU 1035  C   PHE A 134     3590   3876   3959   -478   -310    380       C  
ATOM   1036  O   PHE A 134      -4.966  -5.000  19.426  1.00 36.48           O  
ANISOU 1036  O   PHE A 134     4477   4692   4691   -486   -373    387       O  
ATOM   1037  CB  PHE A 134      -7.500  -5.756  20.262  1.00 32.30           C  
ANISOU 1037  CB  PHE A 134     3997   4294   3980   -547   -172    335       C  
ATOM   1038  CG  PHE A 134      -8.999  -5.643  20.288  1.00 27.35           C  
ANISOU 1038  CG  PHE A 134     3339   3786   3265   -548    -33    246       C  
ATOM   1039  CD1 PHE A 134      -9.640  -4.640  19.566  1.00 36.84           C  
ANISOU 1039  CD1 PHE A 134     4479   5070   4449   -443     26    142       C  
ATOM   1040  CD2 PHE A 134      -9.758  -6.537  21.002  1.00 32.36           C  
ANISOU 1040  CD2 PHE A 134     4003   4455   3837   -649     40    267       C  
ATOM   1041  CE1 PHE A 134     -11.026  -4.538  19.559  1.00 40.19           C  
ANISOU 1041  CE1 PHE A 134     4834   5629   4806   -421    145     55       C  
ATOM   1042  CE2 PHE A 134     -11.142  -6.450  21.011  1.00 36.92           C  
ANISOU 1042  CE2 PHE A 134     4515   5170   4343   -661    178    171       C  
ATOM   1043  CZ  PHE A 134     -11.784  -5.451  20.287  1.00 37.41           C  
ANISOU 1043  CZ  PHE A 134     4479   5335   4401   -538    225     62       C  
ATOM   1044  N   THR A 135      -4.710  -6.750  18.066  1.00 26.42           N  
ANISOU 1044  N   THR A 135     3039   3343   3656   -459   -337    408       N  
ATOM   1045  CA  THR A 135      -3.399  -6.360  17.582  1.00 24.58           C  
ANISOU 1045  CA  THR A 135     2747   3065   3529   -427   -415    418       C  
ATOM   1046  C   THR A 135      -3.517  -6.059  16.095  1.00 32.22           C  
ANISOU 1046  C   THR A 135     3628   4043   4571   -379   -332    326       C  
ATOM   1047  O   THR A 135      -4.545  -6.335  15.465  1.00 30.16           O  
ANISOU 1047  O   THR A 135     3343   3824   4292   -367   -238    267       O  
ATOM   1048  CB  THR A 135      -2.347  -7.448  17.803  1.00 24.62           C  
ANISOU 1048  CB  THR A 135     2702   2983   3669   -420   -504    513       C  
ATOM   1049  OG1 THR A 135      -2.680  -8.620  17.052  1.00 31.82           O  
ANISOU 1049  OG1 THR A 135     3561   3836   4692   -400   -424    502       O  
ATOM   1050  CG2 THR A 135      -2.276  -7.847  19.313  1.00 30.81           C  
ANISOU 1050  CG2 THR A 135     3600   3753   4356   -466   -604    627       C  
ATOM   1051  N   ILE A 136      -2.449  -5.510  15.544  1.00 28.49           N  
ANISOU 1051  N   ILE A 136     3109   3544   4174   -366   -367    312       N  
ATOM   1052  CA  ILE A 136      -2.341  -5.379  14.089  1.00 32.92           C  
ANISOU 1052  CA  ILE A 136     3598   4098   4811   -335   -289    237       C  
ATOM   1053  C   ILE A 136      -1.007  -5.965  13.664  1.00 33.14           C  
ANISOU 1053  C   ILE A 136     3517   4063   5010   -334   -319    258       C  
ATOM   1054  O   ILE A 136      -0.032  -5.975  14.421  1.00 30.81           O  
ANISOU 1054  O   ILE A 136     3194   3751   4760   -349   -420    320       O  
ATOM   1055  CB  ILE A 136      -2.511  -3.919  13.591  1.00 29.02           C  
ANISOU 1055  CB  ILE A 136     3173   3637   4218   -322   -258    174       C  
ATOM   1056  CG1 ILE A 136      -1.356  -2.997  14.015  1.00 27.87           C  
ANISOU 1056  CG1 ILE A 136     3060   3465   4066   -371   -327    190       C  
ATOM   1057  CG2 ILE A 136      -3.836  -3.349  14.073  1.00 30.78           C  
ANISOU 1057  CG2 ILE A 136     3488   3923   4284   -289   -226    150       C  
ATOM   1058  CD1 ILE A 136      -1.422  -1.586  13.417  1.00 27.46           C  
ANISOU 1058  CD1 ILE A 136     3109   3404   3922   -370   -280    130       C  
ATOM   1059  N   LYS A 137      -0.980  -6.529  12.457  1.00 31.62           N  
ANISOU 1059  N   LYS A 137     3254   3845   4916   -313   -232    202       N  
ATOM   1060  CA  LYS A 137       0.258  -7.075  11.921  1.00 30.21           C  
ANISOU 1060  CA  LYS A 137     2958   3608   4911   -297   -228    200       C  
ATOM   1061  C   LYS A 137       0.844  -5.991  11.032  1.00 37.58           C  
ANISOU 1061  C   LYS A 137     3875   4570   5835   -327   -181    131       C  
ATOM   1062  O   LYS A 137       0.524  -5.885   9.837  1.00 36.71           O  
ANISOU 1062  O   LYS A 137     3773   4461   5713   -328    -78     56       O  
ATOM   1063  CB  LYS A 137      -0.007  -8.391  11.185  1.00 32.99           C  
ANISOU 1063  CB  LYS A 137     3267   3897   5370   -270   -141    171       C  
ATOM   1064  CG  LYS A 137      -0.488  -9.533  12.098  1.00 34.44           C  
ANISOU 1064  CG  LYS A 137     3494   4023   5567   -259   -178    249       C  
ATOM   1065  CD  LYS A 137      -0.978 -10.748  11.281  1.00 43.46           C  
ANISOU 1065  CD  LYS A 137     4634   5094   6786   -261    -67    197       C  
ATOM   1066  CE  LYS A 137      -1.284 -11.949  12.181  1.00 57.34           C  
ANISOU 1066  CE  LYS A 137     6460   6758   8570   -262    -93    282       C  
ATOM   1067  NZ  LYS A 137      -2.127 -12.980  11.489  1.00 61.19           N  
ANISOU 1067  NZ  LYS A 137     6988   7188   9074   -311     29    216       N  
ATOM   1068  N   GLY A 138       1.692  -5.150  11.634  1.00 32.77           N  
ANISOU 1068  N   GLY A 138     3258   3981   5211   -368   -259    156       N  
ATOM   1069  CA  GLY A 138       2.221  -3.978  10.992  1.00 34.22           C  
ANISOU 1069  CA  GLY A 138     3465   4181   5357   -427   -215     98       C  
ATOM   1070  C   GLY A 138       3.683  -4.171  10.622  1.00 27.93           C  
ANISOU 1070  C   GLY A 138     2506   3384   4724   -461   -209     78       C  
ATOM   1071  O   GLY A 138       4.215  -5.267  10.627  1.00 31.36           O  
ANISOU 1071  O   GLY A 138     2803   3797   5315   -406   -221     98       O  
ATOM   1072  N   SER A 139       4.301  -3.057  10.285  1.00 29.35           N  
ANISOU 1072  N   SER A 139     2709   3582   4862   -552   -180     32       N  
ATOM   1073  CA  SER A 139       5.735  -3.015  10.009  1.00 32.42           C  
ANISOU 1073  CA  SER A 139     2927   4000   5390   -616   -168     -2       C  
ATOM   1074  C   SER A 139       6.244  -1.750  10.687  1.00 34.04           C  
ANISOU 1074  C   SER A 139     3194   4241   5497   -742   -238     -2       C  
ATOM   1075  O   SER A 139       6.045  -0.636  10.193  1.00 32.65           O  
ANISOU 1075  O   SER A 139     3171   4039   5197   -825   -162    -49       O  
ATOM   1076  CB  SER A 139       6.012  -3.026   8.502  1.00 29.34           C  
ANISOU 1076  CB  SER A 139     2505   3589   5054   -643      3    -92       C  
ATOM   1077  OG  SER A 139       7.403  -2.949   8.245  1.00 33.93           O  
ANISOU 1077  OG  SER A 139     2905   4215   5774   -716     35   -138       O  
ATOM   1078  N   PHE A 140       6.881  -1.920  11.851  1.00 30.58           N  
ANISOU 1078  N   PHE A 140     2658   3858   5102   -759   -390     53       N  
ATOM   1079  CA  PHE A 140       7.226  -0.796  12.714  1.00 33.01           C  
ANISOU 1079  CA  PHE A 140     3050   4204   5290   -891   -479     54       C  
ATOM   1080  C   PHE A 140       8.607  -1.033  13.306  1.00 31.18           C  
ANISOU 1080  C   PHE A 140     2586   4074   5189   -951   -603     66       C  
ATOM   1081  O   PHE A 140       8.902  -2.142  13.758  1.00 37.36           O  
ANISOU 1081  O   PHE A 140     3210   4887   6098   -838   -702    132       O  
ATOM   1082  CB  PHE A 140       6.211  -0.650  13.863  1.00 35.13           C  
ANISOU 1082  CB  PHE A 140     3498   4453   5395   -853   -577    119       C  
ATOM   1083  CG  PHE A 140       4.858  -0.160  13.436  1.00 29.07           C  
ANISOU 1083  CG  PHE A 140     2950   3614   4481   -803   -472     97       C  
ATOM   1084  CD1 PHE A 140       4.687   1.126  12.989  1.00 34.10           C  
ANISOU 1084  CD1 PHE A 140     3758   4204   4994   -880   -389     38       C  
ATOM   1085  CD2 PHE A 140       3.751  -0.988  13.521  1.00 33.05           C  
ANISOU 1085  CD2 PHE A 140     3488   4100   4969   -677   -460    138       C  
ATOM   1086  CE1 PHE A 140       3.438   1.586  12.622  1.00 34.04           C  
ANISOU 1086  CE1 PHE A 140     3940   4138   4857   -800   -311     26       C  
ATOM   1087  CE2 PHE A 140       2.499  -0.538  13.155  1.00 35.27           C  
ANISOU 1087  CE2 PHE A 140     3932   4347   5122   -622   -378    113       C  
ATOM   1088  CZ  PHE A 140       2.342   0.760  12.718  1.00 30.36           C  
ANISOU 1088  CZ  PHE A 140     3467   3684   4383   -668   -311     61       C  
ATOM   1089  N   LEU A 141       9.442  -0.003  13.314  1.00 37.57           N  
ANISOU 1089  N   LEU A 141     3376   4934   5965  -1127   -601      4       N  
ATOM   1090  CA  LEU A 141      10.773  -0.048  13.903  1.00 41.58           C  
ANISOU 1090  CA  LEU A 141     3645   5574   6580  -1214   -730      0       C  
ATOM   1091  C   LEU A 141      10.845   0.991  15.020  1.00 37.45           C  
ANISOU 1091  C   LEU A 141     3264   5087   5877  -1376   -855      3       C  
ATOM   1092  O   LEU A 141       9.881   1.716  15.277  1.00 40.24           O  
ANISOU 1092  O   LEU A 141     3900   5348   6040  -1402   -819      3       O  
ATOM   1093  CB  LEU A 141      11.856   0.201  12.841  1.00 41.89           C  
ANISOU 1093  CB  LEU A 141     3492   5668   6756  -1322   -598   -103       C  
ATOM   1094  CG  LEU A 141      11.865  -0.642  11.561  1.00 45.15           C  
ANISOU 1094  CG  LEU A 141     3790   6038   7327  -1201   -428   -140       C  
ATOM   1095  CD1 LEU A 141      12.835  -0.048  10.564  1.00 46.71           C  
ANISOU 1095  CD1 LEU A 141     3885   6289   7576  -1359   -266   -253       C  
ATOM   1096  CD2 LEU A 141      12.249  -2.092  11.850  1.00 45.32           C  
ANISOU 1096  CD2 LEU A 141     3574   6103   7543  -1002   -520    -78       C  
ATOM   1097  N   ASN A 142      11.991   1.049  15.696  1.00 42.99           N  
ANISOU 1097  N   ASN A 142     3763   5931   6639  -1480  -1005     -1       N  
ATOM   1098  CA  ASN A 142      12.230   2.110  16.669  1.00 42.05           C  
ANISOU 1098  CA  ASN A 142     3770   5861   6347  -1682  -1115    -25       C  
ATOM   1099  C   ASN A 142      11.998   3.476  16.038  1.00 49.74           C  
ANISOU 1099  C   ASN A 142     4984   6733   7183  -1864   -938   -128       C  
ATOM   1100  O   ASN A 142      12.379   3.725  14.887  1.00 45.65           O  
ANISOU 1100  O   ASN A 142     4407   6191   6746  -1923   -770   -201       O  
ATOM   1101  CB  ASN A 142      13.652   2.021  17.206  1.00 50.99           C  
ANISOU 1101  CB  ASN A 142     4632   7176   7566  -1754  -1248    -59       C  
ATOM   1102  CG  ASN A 142      13.896   0.751  17.984  1.00 57.93           C  
ANISOU 1102  CG  ASN A 142     5336   8143   8534  -1549  -1434     52       C  
ATOM   1103  OD1 ASN A 142      12.958   0.107  18.450  1.00 58.87           O  
ANISOU 1103  OD1 ASN A 142     5573   8183   8611  -1418  -1510    168       O  
ATOM   1104  ND2 ASN A 142      15.164   0.383  18.136  1.00 67.14           N  
ANISOU 1104  ND2 ASN A 142     6225   9468   9816  -1520  -1505     14       N  
ATOM   1105  N   GLY A 143      11.356   4.362  16.798  1.00 45.88           N  
ANISOU 1105  N   GLY A 143     4785   6171   6476  -1949   -967   -132       N  
ATOM   1106  CA  GLY A 143      11.049   5.695  16.320  1.00 41.43           C  
ANISOU 1106  CA  GLY A 143     4503   5476   5762  -2099   -809   -217       C  
ATOM   1107  C   GLY A 143       9.737   5.814  15.574  1.00 36.32           C  
ANISOU 1107  C   GLY A 143     4100   4658   5043  -1933   -649   -199       C  
ATOM   1108  O   GLY A 143       9.339   6.929  15.225  1.00 38.96           O  
ANISOU 1108  O   GLY A 143     4708   4857   5237  -2015   -527   -252       O  
ATOM   1109  N   SER A 144       9.059   4.709  15.306  1.00 37.67           N  
ANISOU 1109  N   SER A 144     4182   4827   5302  -1704   -649   -128       N  
ATOM   1110  CA  SER A 144       7.801   4.756  14.562  1.00 34.91           C  
ANISOU 1110  CA  SER A 144     4026   4350   4889  -1547   -514   -116       C  
ATOM   1111  C   SER A 144       6.607   5.122  15.428  1.00 37.73           C  
ANISOU 1111  C   SER A 144     4630   4638   5068  -1466   -547    -85       C  
ATOM   1112  O   SER A 144       5.520   5.343  14.899  1.00 32.31           O  
ANISOU 1112  O   SER A 144     4110   3856   4309  -1340   -443    -84       O  
ATOM   1113  CB  SER A 144       7.544   3.406  13.906  1.00 35.74           C  
ANISOU 1113  CB  SER A 144     3937   4487   5154  -1361   -491    -69       C  
ATOM   1114  OG  SER A 144       7.329   2.407  14.886  1.00 37.81           O  
ANISOU 1114  OG  SER A 144     4096   4813   5455  -1254   -636     12       O  
ATOM   1115  N   CYS A 145       6.759   5.205  16.754  1.00 34.86           N  
ANISOU 1115  N   CYS A 145     4293   4329   4623  -1533   -687    -65       N  
ATOM   1116  CA  CYS A 145       5.575   5.440  17.561  1.00 30.43           C  
ANISOU 1116  CA  CYS A 145     3953   3710   3898  -1445   -694    -44       C  
ATOM   1117  C   CYS A 145       4.983   6.810  17.239  1.00 32.04           C  
ANISOU 1117  C   CYS A 145     4461   3766   3948  -1476   -560   -114       C  
ATOM   1118  O   CYS A 145       5.695   7.764  16.904  1.00 39.68           O  
ANISOU 1118  O   CYS A 145     5517   4678   4883  -1645   -509   -179       O  
ATOM   1119  CB  CYS A 145       5.923   5.311  19.063  1.00 29.22           C  
ANISOU 1119  CB  CYS A 145     3795   3644   3661  -1536   -868    -14       C  
ATOM   1120  SG  CYS A 145       6.236   3.603  19.482  1.00 37.90           S  
ANISOU 1120  SG  CYS A 145     4607   4875   4918  -1419  -1023    102       S  
ATOM   1121  N   GLY A 146       3.654   6.907  17.330  1.00 29.36           N  
ANISOU 1121  N   GLY A 146     4283   3359   3513  -1309   -495   -102       N  
ATOM   1122  CA  GLY A 146       2.985   8.117  16.919  1.00 27.84           C  
ANISOU 1122  CA  GLY A 146     4372   3015   3192  -1276   -366   -156       C  
ATOM   1123  C   GLY A 146       2.556   8.079  15.451  1.00 30.64           C  
ANISOU 1123  C   GLY A 146     4720   3312   3611  -1147   -250   -148       C  
ATOM   1124  O   GLY A 146       1.801   8.957  15.016  1.00 33.61           O  
ANISOU 1124  O   GLY A 146     5326   3562   3882  -1057   -151   -170       O  
ATOM   1125  N   SER A 147       3.056   7.117  14.687  1.00 33.49           N  
ANISOU 1125  N   SER A 147     4837   3756   4130  -1136   -261   -118       N  
ATOM   1126  CA  SER A 147       2.513   6.858  13.343  1.00 31.64           C  
ANISOU 1126  CA  SER A 147     4584   3494   3944  -1003   -163   -107       C  
ATOM   1127  C   SER A 147       1.028   6.523  13.473  1.00 35.73           C  
ANISOU 1127  C   SER A 147     5146   4023   4405   -786   -154    -79       C  
ATOM   1128  O   SER A 147       0.607   5.901  14.454  1.00 33.89           O  
ANISOU 1128  O   SER A 147     4842   3863   4170   -741   -225    -53       O  
ATOM   1129  CB  SER A 147       3.269   5.689  12.700  1.00 30.05           C  
ANISOU 1129  CB  SER A 147     4098   3393   3928  -1025   -180    -88       C  
ATOM   1130  OG  SER A 147       4.628   6.036  12.453  1.00 31.44           O  
ANISOU 1130  OG  SER A 147     4204   3577   4165  -1220   -167   -128       O  
ATOM   1131  N   VAL A 148       0.206   6.938  12.494  1.00 32.77           N  
ANISOU 1131  N   VAL A 148     4890   3585   3976   -653    -68    -83       N  
ATOM   1132  CA  VAL A 148      -1.233   6.768  12.677  1.00 25.68           C  
ANISOU 1132  CA  VAL A 148     4023   2718   3017   -452    -61    -71       C  
ATOM   1133  C   VAL A 148      -1.814   5.891  11.567  1.00 32.79           C  
ANISOU 1133  C   VAL A 148     4777   3692   3989   -333    -38    -51       C  
ATOM   1134  O   VAL A 148      -1.211   5.698  10.499  1.00 30.45           O  
ANISOU 1134  O   VAL A 148     4430   3386   3755   -386     -3    -52       O  
ATOM   1135  CB  VAL A 148      -2.019   8.091  12.736  1.00 24.24           C  
ANISOU 1135  CB  VAL A 148     4118   2412   2678   -346     -2    -96       C  
ATOM   1136  CG1 VAL A 148      -1.633   8.929  14.006  1.00 29.07           C  
ANISOU 1136  CG1 VAL A 148     4901   2947   3196   -461    -16   -132       C  
ATOM   1137  CG2 VAL A 148      -1.868   8.920  11.422  1.00 28.01           C  
ANISOU 1137  CG2 VAL A 148     4762   2769   3110   -326     73    -94       C  
ATOM   1138  N   GLY A 149      -3.008   5.372  11.865  1.00 25.61           N  
ANISOU 1138  N   GLY A 149     3804   2866   3061   -188    -51    -44       N  
ATOM   1139  CA  GLY A 149      -3.813   4.639  10.878  1.00 26.97           C  
ANISOU 1139  CA  GLY A 149     3858   3122   3269    -71    -33    -39       C  
ATOM   1140  C   GLY A 149      -5.142   5.348  10.677  1.00 33.40           C  
ANISOU 1140  C   GLY A 149     4783   3941   3966    120     -8    -52       C  
ATOM   1141  O   GLY A 149      -5.672   5.991  11.586  1.00 32.25           O  
ANISOU 1141  O   GLY A 149     4742   3771   3739    185     -2    -67       O  
ATOM   1142  N   PHE A 150      -5.702   5.210   9.466  1.00 27.81           N  
ANISOU 1142  N   PHE A 150     4045   3275   3244    219      5    -50       N  
ATOM   1143  CA  PHE A 150      -6.776   6.092   9.049  1.00 28.27           C  
ANISOU 1143  CA  PHE A 150     4232   3324   3187    417     14    -52       C  
ATOM   1144  C   PHE A 150      -7.530   5.446   7.892  1.00 29.39           C  
ANISOU 1144  C   PHE A 150     4245   3591   3333    509     -6    -52       C  
ATOM   1145  O   PHE A 150      -7.028   4.544   7.229  1.00 29.88           O  
ANISOU 1145  O   PHE A 150     4186   3696   3470    399     -5    -54       O  
ATOM   1146  CB  PHE A 150      -6.262   7.477   8.591  1.00 27.28           C  
ANISOU 1146  CB  PHE A 150     4389   3012   2965    425     49    -34       C  
ATOM   1147  CG  PHE A 150      -5.307   7.401   7.428  1.00 33.73           C  
ANISOU 1147  CG  PHE A 150     5240   3772   3802    298     74    -16       C  
ATOM   1148  CD1 PHE A 150      -3.979   7.074   7.627  1.00 33.94           C  
ANISOU 1148  CD1 PHE A 150     5215   3762   3919     78     95    -27       C  
ATOM   1149  CD2 PHE A 150      -5.746   7.661   6.131  1.00 29.40           C  
ANISOU 1149  CD2 PHE A 150     4773   3220   3177    401     76      8       C  
ATOM   1150  CE1 PHE A 150      -3.094   6.962   6.559  1.00 38.92           C  
ANISOU 1150  CE1 PHE A 150     5855   4356   4577    -45    141    -25       C  
ATOM   1151  CE2 PHE A 150      -4.860   7.571   5.041  1.00 36.29           C  
ANISOU 1151  CE2 PHE A 150     5691   4044   4054    266    119     18       C  
ATOM   1152  CZ  PHE A 150      -3.528   7.227   5.264  1.00 34.02           C  
ANISOU 1152  CZ  PHE A 150     5337   3720   3868     40    164     -5       C  
ATOM   1153  N   ASN A 151      -8.756   5.901   7.711  1.00 32.51           N  
ANISOU 1153  N   ASN A 151     4658   4051   3644    714    -26    -57       N  
ATOM   1154  CA  ASN A 151      -9.539   5.677   6.500  1.00 33.74           C  
ANISOU 1154  CA  ASN A 151     4747   4318   3755    830    -65    -53       C  
ATOM   1155  C   ASN A 151      -9.880   7.037   5.930  1.00 34.32           C  
ANISOU 1155  C   ASN A 151     5061   4282   3697   1014    -78    -14       C  
ATOM   1156  O   ASN A 151      -9.908   8.035   6.649  1.00 33.70           O  
ANISOU 1156  O   ASN A 151     5155   4078   3571   1094    -50     -9       O  
ATOM   1157  CB  ASN A 151     -10.805   4.900   6.820  1.00 33.42           C  
ANISOU 1157  CB  ASN A 151     4469   4492   3738    921    -95    -94       C  
ATOM   1158  CG  ASN A 151     -10.518   3.450   7.081  1.00 42.02           C  
ANISOU 1158  CG  ASN A 151     5350   5673   4943    737    -82   -123       C  
ATOM   1159  OD1 ASN A 151     -10.413   2.674   6.141  1.00 36.77           O  
ANISOU 1159  OD1 ASN A 151     4595   5070   4306    665    -95   -133       O  
ATOM   1160  ND2 ASN A 151     -10.357   3.076   8.348  1.00 29.33           N  
ANISOU 1160  ND2 ASN A 151     3689   4060   3395    657    -54   -133       N  
ATOM   1161  N   ILE A 152     -10.133   7.116   4.622  1.00 31.43           N  
ANISOU 1161  N   ILE A 152     4735   3949   3258   1083   -120     15       N  
ATOM   1162  CA  ILE A 152     -10.582   8.368   4.039  1.00 35.80           C  
ANISOU 1162  CA  ILE A 152     5528   4402   3674   1291   -149     69       C  
ATOM   1163  C   ILE A 152     -11.935   8.127   3.379  1.00 42.29           C  
ANISOU 1163  C   ILE A 152     6198   5433   4439   1506   -247     69       C  
ATOM   1164  O   ILE A 152     -12.104   7.145   2.650  1.00 45.44           O  
ANISOU 1164  O   ILE A 152     6416   5995   4856   1424   -288     47       O  
ATOM   1165  CB  ILE A 152      -9.557   8.938   3.040  1.00 35.88           C  
ANISOU 1165  CB  ILE A 152     5797   4229   3607   1180   -115    123       C  
ATOM   1166  CG1 ILE A 152      -8.199   9.058   3.746  1.00 42.67           C  
ANISOU 1166  CG1 ILE A 152     6743   4929   4543    938    -22    104       C  
ATOM   1167  CG2 ILE A 152     -10.005  10.290   2.564  1.00 41.45           C  
ANISOU 1167  CG2 ILE A 152     6799   4789   4160   1400   -141    192       C  
ATOM   1168  CD1 ILE A 152      -7.106   9.703   2.932  1.00 49.10           C  
ANISOU 1168  CD1 ILE A 152     7810   5557   5289    792     42    142       C  
ATOM   1169  N   ASP A 153     -12.910   8.978   3.689  1.00 46.05           N  
ANISOU 1169  N   ASP A 153     6728   5915   4854   1776   -283     81       N  
ATOM   1170  CA  ASP A 153     -14.253   8.868   3.131  1.00 51.40           C  
ANISOU 1170  CA  ASP A 153     7237   6813   5479   2012   -391     79       C  
ATOM   1171  C   ASP A 153     -14.597  10.204   2.497  1.00 50.83           C  
ANISOU 1171  C   ASP A 153     7444   6603   5267   2282   -447    164       C  
ATOM   1172  O   ASP A 153     -14.576  11.241   3.167  1.00 53.73           O  
ANISOU 1172  O   ASP A 153     8019   6783   5614   2417   -394    181       O  
ATOM   1173  CB  ASP A 153     -15.289   8.453   4.188  1.00 69.11           C  
ANISOU 1173  CB  ASP A 153     9202   9254   7804   2110   -381     -1       C  
ATOM   1174  CG  ASP A 153     -15.620   9.567   5.190  1.00 86.12           C  
ANISOU 1174  CG  ASP A 153    11502  11275   9945   2314   -323     -6       C  
ATOM   1175  OD1 ASP A 153     -16.511  10.395   4.881  1.00 93.12           O  
ANISOU 1175  OD1 ASP A 153    12440  12182  10759   2622   -382     20       O  
ATOM   1176  OD2 ASP A 153     -15.019   9.597   6.292  1.00 89.68           O  
ANISOU 1176  OD2 ASP A 153    12014  11607  10454   2174   -221    -41       O  
ATOM   1177  N   TYR A 154     -14.887  10.178   1.200  1.00 50.23           N  
ANISOU 1177  N   TYR A 154     7397   6605   5082   2355   -554    220       N  
ATOM   1178  CA  TYR A 154     -14.900  11.394   0.405  1.00 57.91           C  
ANISOU 1178  CA  TYR A 154     8711   7394   5899   2556   -606    329       C  
ATOM   1179  C   TYR A 154     -13.565  12.097   0.615  1.00 55.91           C  
ANISOU 1179  C   TYR A 154     8807   6806   5629   2372   -476    365       C  
ATOM   1180  O   TYR A 154     -12.537  11.548   0.209  1.00 73.37           O  
ANISOU 1180  O   TYR A 154    11043   8976   7859   2082   -418    357       O  
ATOM   1181  CB  TYR A 154     -16.138  12.222   0.745  1.00 70.55           C  
ANISOU 1181  CB  TYR A 154    10297   9041   7467   2949   -679    347       C  
ATOM   1182  CG  TYR A 154     -17.356  11.492   0.221  1.00 85.09           C  
ANISOU 1182  CG  TYR A 154    11785  11244   9302   3092   -828    316       C  
ATOM   1183  CD1 TYR A 154     -18.033  10.570   1.011  1.00 89.45           C  
ANISOU 1183  CD1 TYR A 154    11942  12059   9985   3048   -811    201       C  
ATOM   1184  CD2 TYR A 154     -17.773  11.655  -1.099  1.00 91.01           C  
ANISOU 1184  CD2 TYR A 154    12584  12074   9921   3177   -961    382       C  
ATOM   1185  CE1 TYR A 154     -19.125   9.870   0.520  1.00 93.60           C  
ANISOU 1185  CE1 TYR A 154    12131  12925  10509   3115   -930    154       C  
ATOM   1186  CE2 TYR A 154     -18.861  10.960  -1.598  1.00 94.61           C  
ANISOU 1186  CE2 TYR A 154    12699  12866  10382   3222  -1081    329       C  
ATOM   1187  CZ  TYR A 154     -19.534  10.070  -0.785  1.00 96.69           C  
ANISOU 1187  CZ  TYR A 154    12571  13388  10777   3181  -1061    212       C  
ATOM   1188  OH  TYR A 154     -20.618   9.378  -1.279  1.00100.84           O  
ANISOU 1188  OH  TYR A 154    12766  14241  11308   3184  -1165    150       O  
ATOM   1189  N   ASP A 155     -13.524  13.270   1.244  1.00 55.30           N  
ANISOU 1189  N   ASP A 155     8995   6495   5522   2518   -420    394       N  
ATOM   1190  CA  ASP A 155     -12.231  13.855   1.585  1.00 54.82           C  
ANISOU 1190  CA  ASP A 155     9232   6140   5458   2291   -286    403       C  
ATOM   1191  C   ASP A 155     -12.125  14.155   3.080  1.00 49.96           C  
ANISOU 1191  C   ASP A 155     8610   5435   4939   2272   -189    329       C  
ATOM   1192  O   ASP A 155     -11.481  15.118   3.494  1.00 50.05           O  
ANISOU 1192  O   ASP A 155     8937   5172   4909   2221    -98    341       O  
ATOM   1193  CB  ASP A 155     -11.941  15.091   0.739  1.00 64.95           C  
ANISOU 1193  CB  ASP A 155    10962   7147   6570   2388   -283    516       C  
ATOM   1194  CG  ASP A 155     -11.462  14.729  -0.680  1.00 78.82           C  
ANISOU 1194  CG  ASP A 155    12791   8934   8221   2241   -323    580       C  
ATOM   1195  OD1 ASP A 155     -11.133  13.548  -0.927  1.00 86.34           O  
ANISOU 1195  OD1 ASP A 155    13470  10085   9252   2023   -323    522       O  
ATOM   1196  OD2 ASP A 155     -11.410  15.619  -1.548  1.00 83.82           O  
ANISOU 1196  OD2 ASP A 155    13776   9386   8687   2342   -345    687       O  
ATOM   1197  N   CYS A 156     -12.743  13.324   3.896  1.00 41.96           N  
ANISOU 1197  N   CYS A 156     7252   4650   4040   2291   -202    246       N  
ATOM   1198  CA  CYS A 156     -12.618  13.426   5.348  1.00 41.83           C  
ANISOU 1198  CA  CYS A 156     7205   4584   4106   2233   -109    167       C  
ATOM   1199  C   CYS A 156     -11.771  12.273   5.865  1.00 39.36           C  
ANISOU 1199  C   CYS A 156     6675   4371   3910   1898    -70    111       C  
ATOM   1200  O   CYS A 156     -12.028  11.102   5.543  1.00 40.95           O  
ANISOU 1200  O   CYS A 156     6579   4803   4177   1826   -122     89       O  
ATOM   1201  CB  CYS A 156     -13.989  13.422   6.007  1.00 45.68           C  
ANISOU 1201  CB  CYS A 156     7489   5243   4624   2515   -133    115       C  
ATOM   1202  SG  CYS A 156     -13.878  13.345   7.832  1.00 47.95           S  
ANISOU 1202  SG  CYS A 156     7712   5510   4996   2406     -8      5       S  
ATOM   1203  N   VAL A 157     -10.757  12.592   6.666  1.00 38.69           N  
ANISOU 1203  N   VAL A 157     6741   4111   3848   1692     16     85       N  
ATOM   1204  CA  VAL A 157      -9.867  11.573   7.199  1.00 40.46           C  
ANISOU 1204  CA  VAL A 157     6777   4414   4182   1393     40     44       C  
ATOM   1205  C   VAL A 157     -10.411  11.115   8.551  1.00 42.19           C  
ANISOU 1205  C   VAL A 157     6807   4756   4466   1411     59    -25       C  
ATOM   1206  O   VAL A 157     -10.531  11.921   9.476  1.00 37.85           O  
ANISOU 1206  O   VAL A 157     6420   4087   3876   1472    115    -58       O  
ATOM   1207  CB  VAL A 157      -8.436  12.107   7.339  1.00 34.72           C  
ANISOU 1207  CB  VAL A 157     6280   3468   3442   1142    107     51       C  
ATOM   1208  CG1 VAL A 157      -7.520  11.015   7.875  1.00 32.04           C  
ANISOU 1208  CG1 VAL A 157     5716   3230   3227    866    110     15       C  
ATOM   1209  CG2 VAL A 157      -7.962  12.669   5.991  1.00 41.22           C  
ANISOU 1209  CG2 VAL A 157     7328   4157   4179   1122    113    118       C  
ATOM   1210  N   SER A 158     -10.745   9.823   8.669  1.00 36.39           N  
ANISOU 1210  N   SER A 158     5754   4250   3822   1346     24    -52       N  
ATOM   1211  CA  SER A 158     -11.116   9.228   9.956  1.00 42.80           C  
ANISOU 1211  CA  SER A 158     6393   5178   4690   1302     53   -111       C  
ATOM   1212  C   SER A 158      -9.876   8.540  10.514  1.00 33.58           C  
ANISOU 1212  C   SER A 158     5187   3975   3598   1008     62   -110       C  
ATOM   1213  O   SER A 158      -9.459   7.490  10.034  1.00 30.86           O  
ANISOU 1213  O   SER A 158     4670   3721   3334    874     29    -95       O  
ATOM   1214  CB  SER A 158     -12.295   8.268   9.820  1.00 41.86           C  
ANISOU 1214  CB  SER A 158     5969   5322   4615   1403     18   -141       C  
ATOM   1215  OG  SER A 158     -13.484   8.963   9.478  1.00 43.16           O  
ANISOU 1215  OG  SER A 158     6140   5545   4716   1696      1   -150       O  
ATOM   1216  N   PHE A 159      -9.271   9.168  11.525  1.00 34.71           N  
ANISOU 1216  N   PHE A 159     5499   3979   3709    915    104   -130       N  
ATOM   1217  CA  PHE A 159      -8.129   8.609  12.226  1.00 32.24           C  
ANISOU 1217  CA  PHE A 159     5145   3647   3456    656     93   -129       C  
ATOM   1218  C   PHE A 159      -8.637   7.604  13.251  1.00 31.21           C  
ANISOU 1218  C   PHE A 159     4810   3680   3370    622     86   -154       C  
ATOM   1219  O   PHE A 159      -9.571   7.902  14.011  1.00 31.08           O  
ANISOU 1219  O   PHE A 159     4807   3706   3296    744    129   -196       O  
ATOM   1220  CB  PHE A 159      -7.340   9.717  12.952  1.00 31.03           C  
ANISOU 1220  CB  PHE A 159     5261   3300   3228    556    130   -149       C  
ATOM   1221  CG  PHE A 159      -6.670  10.710  12.030  1.00 38.34           C  
ANISOU 1221  CG  PHE A 159     6425   4039   4105    531    154   -125       C  
ATOM   1222  CD1 PHE A 159      -5.457  10.403  11.417  1.00 34.57           C  
ANISOU 1222  CD1 PHE A 159     5915   3532   3687    323    137    -99       C  
ATOM   1223  CD2 PHE A 159      -7.231  11.966  11.812  1.00 35.63           C  
ANISOU 1223  CD2 PHE A 159     6347   3538   3652    713    204   -130       C  
ATOM   1224  CE1 PHE A 159      -4.824  11.344  10.598  1.00 33.41           C  
ANISOU 1224  CE1 PHE A 159     6004   3210   3479    268    181    -82       C  
ATOM   1225  CE2 PHE A 159      -6.606  12.905  10.974  1.00 38.76           C  
ANISOU 1225  CE2 PHE A 159     7005   3737   3986    673    237    -99       C  
ATOM   1226  CZ  PHE A 159      -5.401  12.579  10.365  1.00 35.60           C  
ANISOU 1226  CZ  PHE A 159     6572   3319   3635    435    229    -76       C  
ATOM   1227  N   CYS A 160      -8.048   6.412  13.244  1.00 32.11           N  
ANISOU 1227  N   CYS A 160     4742   3877   3583    462     43   -128       N  
ATOM   1228  CA  CYS A 160      -8.479   5.329  14.126  1.00 30.89           C  
ANISOU 1228  CA  CYS A 160     4410   3860   3467    410     36   -135       C  
ATOM   1229  C   CYS A 160      -7.376   4.652  14.911  1.00 29.41           C  
ANISOU 1229  C   CYS A 160     4189   3652   3334    202    -11   -101       C  
ATOM   1230  O   CYS A 160      -7.698   3.840  15.793  1.00 32.31           O  
ANISOU 1230  O   CYS A 160     4462   4106   3708    152    -16    -96       O  
ATOM   1231  CB  CYS A 160      -9.220   4.250  13.330  1.00 31.18           C  
ANISOU 1231  CB  CYS A 160     4222   4051   3574    460     27   -133       C  
ATOM   1232  SG  CYS A 160      -8.264   3.421  11.979  1.00 31.99           S  
ANISOU 1232  SG  CYS A 160     4226   4139   3790    352    -16    -95       S  
ATOM   1233  N   TYR A 161      -6.106   4.950  14.653  1.00 28.15           N  
ANISOU 1233  N   TYR A 161     4100   3387   3207     79    -47    -78       N  
ATOM   1234  CA  TYR A 161      -5.033   4.203  15.308  1.00 28.29           C  
ANISOU 1234  CA  TYR A 161     4040   3414   3296    -97   -115    -41       C  
ATOM   1235  C   TYR A 161      -3.804   5.075  15.475  1.00 28.31           C  
ANISOU 1235  C   TYR A 161     4177   3303   3276   -228   -142    -46       C  
ATOM   1236  O   TYR A 161      -3.433   5.832  14.578  1.00 27.50           O  
ANISOU 1236  O   TYR A 161     4168   3113   3166   -227   -107    -61       O  
ATOM   1237  CB  TYR A 161      -4.642   2.948  14.510  1.00 29.02           C  
ANISOU 1237  CB  TYR A 161     3929   3564   3533   -134   -143     -5       C  
ATOM   1238  CG  TYR A 161      -3.503   2.114  15.123  1.00 27.77           C  
ANISOU 1238  CG  TYR A 161     3673   3411   3468   -276   -223     43       C  
ATOM   1239  CD1 TYR A 161      -3.762   1.174  16.116  1.00 28.52           C  
ANISOU 1239  CD1 TYR A 161     3701   3567   3570   -304   -264     82       C  
ATOM   1240  CD2 TYR A 161      -2.180   2.249  14.688  1.00 25.99           C  
ANISOU 1240  CD2 TYR A 161     3417   3134   3322   -378   -256     51       C  
ATOM   1241  CE1 TYR A 161      -2.743   0.386  16.659  1.00 30.19           C  
ANISOU 1241  CE1 TYR A 161     3828   3779   3864   -403   -355    142       C  
ATOM   1242  CE2 TYR A 161      -1.160   1.459  15.209  1.00 27.91           C  
ANISOU 1242  CE2 TYR A 161     3539   3400   3665   -475   -341     97       C  
ATOM   1243  CZ  TYR A 161      -1.439   0.557  16.236  1.00 27.54           C  
ANISOU 1243  CZ  TYR A 161     3442   3403   3617   -477   -402    149       C  
ATOM   1244  OH  TYR A 161      -0.463  -0.248  16.806  1.00 29.21           O  
ANISOU 1244  OH  TYR A 161     3547   3633   3920   -545   -506    211       O  
ATOM   1245  N   MET A 162      -3.178   4.999  16.653  1.00 27.64           N  
ANISOU 1245  N   MET A 162     4115   3223   3163   -358   -205    -34       N  
ATOM   1246  CA  MET A 162      -1.851   5.564  16.848  1.00 27.14           C  
ANISOU 1246  CA  MET A 162     4116   3095   3102   -527   -256    -40       C  
ATOM   1247  C   MET A 162      -0.963   4.463  17.424  1.00 28.86           C  
ANISOU 1247  C   MET A 162     4149   3398   3417   -639   -370     17       C  
ATOM   1248  O   MET A 162      -1.393   3.719  18.309  1.00 28.74           O  
ANISOU 1248  O   MET A 162     4089   3451   3381   -623   -415     54       O  
ATOM   1249  CB  MET A 162      -1.877   6.790  17.792  1.00 31.06           C  
ANISOU 1249  CB  MET A 162     4858   3505   3437   -587   -238    -93       C  
ATOM   1250  CG  MET A 162      -0.515   7.394  17.991  1.00 30.36           C  
ANISOU 1250  CG  MET A 162     4830   3364   3341   -794   -292   -112       C  
ATOM   1251  SD  MET A 162      -0.553   8.989  18.843  1.00 38.23           S  
ANISOU 1251  SD  MET A 162     6168   4218   4138   -882   -241   -197       S  
ATOM   1252  CE  MET A 162      -0.799  10.112  17.446  1.00 39.46           C  
ANISOU 1252  CE  MET A 162     6512   4202   4280   -788   -107   -230       C  
ATOM   1253  N   HIS A 163       0.271   4.350  16.925  1.00 29.10           N  
ANISOU 1253  N   HIS A 163     4075   3426   3554   -747   -414     25       N  
ATOM   1254  CA  HIS A 163       1.094   3.184  17.232  1.00 27.14           C  
ANISOU 1254  CA  HIS A 163     3615   3261   3436   -800   -522     85       C  
ATOM   1255  C   HIS A 163       1.859   3.397  18.532  1.00 25.34           C  
ANISOU 1255  C   HIS A 163     3419   3070   3140   -940   -649    102       C  
ATOM   1256  O   HIS A 163       2.507   4.428  18.677  1.00 30.97           O  
ANISOU 1256  O   HIS A 163     4233   3747   3786  -1071   -656     50       O  
ATOM   1257  CB  HIS A 163       2.111   2.930  16.126  1.00 32.03           C  
ANISOU 1257  CB  HIS A 163     4074   3882   4212   -843   -506     77       C  
ATOM   1258  CG  HIS A 163       2.950   1.731  16.384  1.00 24.59           C  
ANISOU 1258  CG  HIS A 163     2905   3016   3422   -858   -609    135       C  
ATOM   1259  ND1 HIS A 163       2.413   0.503  16.681  1.00 29.23           N  
ANISOU 1259  ND1 HIS A 163     3408   3635   4064   -756   -643    200       N  
ATOM   1260  CD2 HIS A 163       4.292   1.578  16.432  1.00 30.82           C  
ANISOU 1260  CD2 HIS A 163     3536   3853   4319   -958   -689    140       C  
ATOM   1261  CE1 HIS A 163       3.384  -0.356  16.920  1.00 29.30           C  
ANISOU 1261  CE1 HIS A 163     3238   3688   4206   -773   -744    252       C  
ATOM   1262  NE2 HIS A 163       4.533   0.271  16.770  1.00 29.48           N  
ANISOU 1262  NE2 HIS A 163     3195   3736   4270   -885   -778    215       N  
ATOM   1263  N   HIS A 164       1.848   2.390  19.422  1.00 28.58           N  
ANISOU 1263  N   HIS A 164     3744   3550   3563   -927   -754    177       N  
ATOM   1264  CA  HIS A 164       2.571   2.510  20.700  1.00 32.75           C  
ANISOU 1264  CA  HIS A 164     4303   4132   4007  -1058   -903    206       C  
ATOM   1265  C   HIS A 164       3.607   1.417  20.946  1.00 35.24           C  
ANISOU 1265  C   HIS A 164     4398   4530   4463  -1073  -1059    292       C  
ATOM   1266  O   HIS A 164       4.629   1.691  21.582  1.00 38.96           O  
ANISOU 1266  O   HIS A 164     4828   5064   4912  -1201  -1196    299       O  
ATOM   1267  CB  HIS A 164       1.571   2.510  21.885  1.00 28.07           C  
ANISOU 1267  CB  HIS A 164     3887   3546   3233  -1041   -905    223       C  
ATOM   1268  CG  HIS A 164       0.780   3.776  22.025  1.00 33.03           C  
ANISOU 1268  CG  HIS A 164     4752   4101   3698  -1046   -783    128       C  
ATOM   1269  ND1 HIS A 164       0.894   4.620  23.114  1.00 34.01           N  
ANISOU 1269  ND1 HIS A 164     5070   4215   3639  -1170   -819     85       N  
ATOM   1270  CD2 HIS A 164      -0.176   4.313  21.235  1.00 33.37           C  
ANISOU 1270  CD2 HIS A 164     4875   4075   3729   -926   -627     69       C  
ATOM   1271  CE1 HIS A 164       0.058   5.632  22.974  1.00 31.04           C  
ANISOU 1271  CE1 HIS A 164     4889   3747   3156  -1118   -675     -2       C  
ATOM   1272  NE2 HIS A 164      -0.600   5.471  21.833  1.00 35.34           N  
ANISOU 1272  NE2 HIS A 164     5362   4260   3806   -959   -565     -6       N  
ATOM   1273  N   MET A 165       3.386   0.171  20.532  1.00 31.72           N  
ANISOU 1273  N   MET A 165     3810   4087   4153   -947  -1053    359       N  
ATOM   1274  CA  MET A 165       4.320  -0.861  20.991  1.00 36.39           C  
ANISOU 1274  CA  MET A 165     4228   4741   4859   -937  -1216    455       C  
ATOM   1275  C   MET A 165       4.228  -2.127  20.157  1.00 38.31           C  
ANISOU 1275  C   MET A 165     4313   4949   5293   -794  -1166    501       C  
ATOM   1276  O   MET A 165       3.318  -2.309  19.344  1.00 33.33           O  
ANISOU 1276  O   MET A 165     3716   4262   4685   -718  -1016    463       O  
ATOM   1277  CB  MET A 165       4.111  -1.198  22.475  1.00 49.87           C  
ANISOU 1277  CB  MET A 165     6050   6485   6412   -970  -1354    543       C  
ATOM   1278  CG  MET A 165       2.707  -1.498  22.884  1.00 49.55           C  
ANISOU 1278  CG  MET A 165     6180   6401   6246   -914  -1257    561       C  
ATOM   1279  SD  MET A 165       2.683  -1.944  24.646  1.00 58.37           S  
ANISOU 1279  SD  MET A 165     7439   7568   7173   -982  -1427    674       S  
ATOM   1280  CE  MET A 165       1.618  -3.375  24.486  1.00 50.22           C  
ANISOU 1280  CE  MET A 165     6411   6473   6198   -854  -1333    756       C  
ATOM   1281  N   GLU A 166       5.218  -2.997  20.370  1.00 34.68           N  
ANISOU 1281  N   GLU A 166     3677   4527   4972   -757  -1301    578       N  
ATOM   1282  CA  GLU A 166       5.330  -4.292  19.713  1.00 35.50           C  
ANISOU 1282  CA  GLU A 166     3635   4584   5271   -618  -1272    626       C  
ATOM   1283  C   GLU A 166       5.338  -5.369  20.786  1.00 42.45           C  
ANISOU 1283  C   GLU A 166     4542   5453   6134   -554  -1420    768       C  
ATOM   1284  O   GLU A 166       6.081  -5.253  21.760  1.00 40.27           O  
ANISOU 1284  O   GLU A 166     4246   5251   5804   -599  -1607    834       O  
ATOM   1285  CB  GLU A 166       6.620  -4.385  18.885  1.00 34.33           C  
ANISOU 1285  CB  GLU A 166     3238   4473   5332   -601  -1284    587       C  
ATOM   1286  CG  GLU A 166       6.757  -5.705  18.137  1.00 40.97           C  
ANISOU 1286  CG  GLU A 166     3939   5247   6382   -448  -1228    618       C  
ATOM   1287  CD  GLU A 166       7.878  -5.690  17.101  1.00 51.77           C  
ANISOU 1287  CD  GLU A 166     5067   6649   7953   -433  -1174    543       C  
ATOM   1288  OE1 GLU A 166       8.796  -6.519  17.225  1.00 54.38           O  
ANISOU 1288  OE1 GLU A 166     5206   7000   8454   -333  -1270    597       O  
ATOM   1289  OE2 GLU A 166       7.840  -4.869  16.157  1.00 44.37           O  
ANISOU 1289  OE2 GLU A 166     4135   5716   7006   -513  -1030    431       O  
ATOM   1290  N   LEU A 167       4.508  -6.410  20.600  1.00 38.61           N  
ANISOU 1290  N   LEU A 167     4113   4875   5682   -459  -1339    815       N  
ATOM   1291  CA  LEU A 167       4.446  -7.556  21.497  1.00 37.74           C  
ANISOU 1291  CA  LEU A 167     4062   4716   5560   -394  -1451    958       C  
ATOM   1292  C   LEU A 167       5.487  -8.596  21.103  1.00 45.05           C  
ANISOU 1292  C   LEU A 167     4794   5600   6722   -256  -1527   1022       C  
ATOM   1293  O   LEU A 167       5.997  -8.582  19.975  1.00 45.46           O  
ANISOU 1293  O   LEU A 167     4673   5648   6953   -209  -1436    936       O  
ATOM   1294  CB  LEU A 167       3.043  -8.156  21.463  1.00 37.09           C  
ANISOU 1294  CB  LEU A 167     4144   4549   5400   -385  -1306    965       C  
ATOM   1295  CG  LEU A 167       2.022  -7.169  22.023  1.00 42.65           C  
ANISOU 1295  CG  LEU A 167     5027   5306   5870   -498  -1241    908       C  
ATOM   1296  CD1 LEU A 167       0.621  -7.614  21.690  1.00 46.24           C  
ANISOU 1296  CD1 LEU A 167     5577   5713   6280   -493  -1065    872       C  
ATOM   1297  CD2 LEU A 167       2.208  -7.009  23.541  1.00 46.92           C  
ANISOU 1297  CD2 LEU A 167     5708   5894   6226   -572  -1405   1005       C  
ATOM   1298  N   PRO A 168       5.832  -9.518  22.013  1.00 51.17           N  
ANISOU 1298  N   PRO A 168     5603   6340   7501   -179  -1689   1173       N  
ATOM   1299  CA  PRO A 168       6.901 -10.482  21.708  1.00 46.84           C  
ANISOU 1299  CA  PRO A 168     4861   5748   7187    -13  -1778   1240       C  
ATOM   1300  C   PRO A 168       6.661 -11.312  20.459  1.00 45.51           C  
ANISOU 1300  C   PRO A 168     4627   5449   7215     93  -1584   1178       C  
ATOM   1301  O   PRO A 168       7.621 -11.881  19.927  1.00 51.56           O  
ANISOU 1301  O   PRO A 168     5195   6191   8203    229  -1608   1181       O  
ATOM   1302  CB  PRO A 168       6.942 -11.372  22.962  1.00 45.56           C  
ANISOU 1302  CB  PRO A 168     4838   5531   6941     54  -1965   1431       C  
ATOM   1303  CG  PRO A 168       6.423 -10.503  24.044  1.00 46.75           C  
ANISOU 1303  CG  PRO A 168     5177   5775   6812   -113  -2039   1449       C  
ATOM   1304  CD  PRO A 168       5.396  -9.610  23.420  1.00 49.32           C  
ANISOU 1304  CD  PRO A 168     5581   6114   7045   -239  -1817   1292       C  
ATOM   1305  N   THR A 169       5.429 -11.425  19.982  1.00 41.07           N  
ANISOU 1305  N   THR A 169     4216   4809   6580     37  -1395   1117       N  
ATOM   1306  CA  THR A 169       5.159 -12.229  18.803  1.00 42.78           C  
ANISOU 1306  CA  THR A 169     4390   4905   6960    113  -1215   1049       C  
ATOM   1307  C   THR A 169       5.424 -11.486  17.505  1.00 49.35           C  
ANISOU 1307  C   THR A 169     5066   5801   7883     80  -1075    886       C  
ATOM   1308  O   THR A 169       5.141 -12.029  16.433  1.00 55.77           O  
ANISOU 1308  O   THR A 169     5854   6530   8805    118   -911    807       O  
ATOM   1309  CB  THR A 169       3.718 -12.714  18.836  1.00 43.95           C  
ANISOU 1309  CB  THR A 169     4752   4962   6984     47  -1081   1047       C  
ATOM   1310  OG1 THR A 169       2.892 -11.672  19.358  1.00 48.57           O  
ANISOU 1310  OG1 THR A 169     5452   5656   7346    -92  -1071   1012       O  
ATOM   1311  CG2 THR A 169       3.597 -13.953  19.736  1.00 43.53           C  
ANISOU 1311  CG2 THR A 169     4849   4770   6919    113  -1162   1207       C  
ATOM   1312  N   GLY A 170       5.942 -10.261  17.572  1.00 49.27           N  
ANISOU 1312  N   GLY A 170     4973   5930   7818     -5  -1130    831       N  
ATOM   1313  CA  GLY A 170       6.156  -9.455  16.388  1.00 45.21           C  
ANISOU 1313  CA  GLY A 170     4352   5469   7355    -61   -992    685       C  
ATOM   1314  C   GLY A 170       4.952  -8.680  15.909  1.00 45.72           C  
ANISOU 1314  C   GLY A 170     4571   5543   7257   -164   -850    597       C  
ATOM   1315  O   GLY A 170       5.030  -8.035  14.852  1.00 49.45           O  
ANISOU 1315  O   GLY A 170     4992   6042   7753   -206   -729    485       O  
ATOM   1316  N   VAL A 171       3.836  -8.728  16.634  1.00 36.06           N  
ANISOU 1316  N   VAL A 171     3532   4302   5866   -200   -858    644       N  
ATOM   1317  CA  VAL A 171       2.648  -7.970  16.285  1.00 30.17           C  
ANISOU 1317  CA  VAL A 171     2913   3584   4965   -273   -740    564       C  
ATOM   1318  C   VAL A 171       2.617  -6.686  17.112  1.00 32.42           C  
ANISOU 1318  C   VAL A 171     3287   3954   5077   -363   -817    562       C  
ATOM   1319  O   VAL A 171       3.452  -6.485  18.005  1.00 37.57           O  
ANISOU 1319  O   VAL A 171     3913   4648   5715   -389   -968    624       O  
ATOM   1320  CB  VAL A 171       1.367  -8.800  16.474  1.00 32.87           C  
ANISOU 1320  CB  VAL A 171     3380   3870   5239   -266   -668    589       C  
ATOM   1321  CG1 VAL A 171       1.448 -10.105  15.670  1.00 37.44           C  
ANISOU 1321  CG1 VAL A 171     3896   4343   5988   -194   -587    583       C  
ATOM   1322  CG2 VAL A 171       1.102  -9.097  17.961  1.00 30.85           C  
ANISOU 1322  CG2 VAL A 171     3250   3610   4860   -291   -784    707       C  
ATOM   1323  N   HIS A 172       1.641  -5.824  16.841  1.00 29.83           N  
ANISOU 1323  N   HIS A 172     3070   3652   4611   -406   -719    488       N  
ATOM   1324  CA  HIS A 172       1.705  -4.420  17.224  1.00 29.00           C  
ANISOU 1324  CA  HIS A 172     3052   3600   4366   -484   -744    446       C  
ATOM   1325  C   HIS A 172       0.436  -4.002  17.943  1.00 29.05           C  
ANISOU 1325  C   HIS A 172     3232   3624   4180   -502   -708    441       C  
ATOM   1326  O   HIS A 172      -0.630  -4.577  17.747  1.00 28.62           O  
ANISOU 1326  O   HIS A 172     3208   3562   4106   -461   -623    434       O  
ATOM   1327  CB  HIS A 172       1.957  -3.540  15.957  1.00 28.50           C  
ANISOU 1327  CB  HIS A 172     2953   3535   4340   -501   -640    343       C  
ATOM   1328  CG  HIS A 172       3.259  -3.875  15.297  1.00 29.76           C  
ANISOU 1328  CG  HIS A 172     2931   3693   4682   -502   -655    332       C  
ATOM   1329  ND1 HIS A 172       3.336  -4.567  14.104  1.00 32.78           N  
ANISOU 1329  ND1 HIS A 172     3211   4039   5204   -444   -549    291       N  
ATOM   1330  CD2 HIS A 172       4.533  -3.670  15.699  1.00 32.45           C  
ANISOU 1330  CD2 HIS A 172     3159   4079   5092   -556   -762    351       C  
ATOM   1331  CE1 HIS A 172       4.606  -4.755  13.793  1.00 32.11           C  
ANISOU 1331  CE1 HIS A 172     2959   3970   5272   -452   -574    281       C  
ATOM   1332  NE2 HIS A 172       5.355  -4.220  14.749  1.00 35.43           N  
ANISOU 1332  NE2 HIS A 172     3354   4449   5659   -518   -709    318       N  
ATOM   1333  N   ALA A 173       0.580  -3.027  18.835  1.00 31.96           N  
ANISOU 1333  N   ALA A 173     3711   4024   4408   -575   -772    437       N  
ATOM   1334  CA  ALA A 173      -0.518  -2.588  19.676  1.00 28.67           C  
ANISOU 1334  CA  ALA A 173     3462   3628   3804   -593   -734    426       C  
ATOM   1335  C   ALA A 173      -0.492  -1.068  19.755  1.00 27.60           C  
ANISOU 1335  C   ALA A 173     3448   3493   3547   -643   -708    346       C  
ATOM   1336  O   ALA A 173       0.566  -0.426  19.701  1.00 31.55           O  
ANISOU 1336  O   ALA A 173     3930   3989   4070   -717   -773    329       O  
ATOM   1337  CB  ALA A 173      -0.426  -3.240  21.102  1.00 30.14           C  
ANISOU 1337  CB  ALA A 173     3715   3831   3905   -641   -852    528       C  
ATOM   1338  N   GLY A 174      -1.673  -0.488  19.866  1.00 28.41           N  
ANISOU 1338  N   GLY A 174     3674   3598   3522   -604   -603    291       N  
ATOM   1339  CA  GLY A 174      -1.760   0.948  19.940  1.00 29.29           C  
ANISOU 1339  CA  GLY A 174     3935   3679   3515   -628   -560    213       C  
ATOM   1340  C   GLY A 174      -3.145   1.370  20.353  1.00 23.78           C  
ANISOU 1340  C   GLY A 174     3362   2996   2677   -559   -454    164       C  
ATOM   1341  O   GLY A 174      -3.954   0.551  20.803  1.00 29.97           O  
ANISOU 1341  O   GLY A 174     4116   3833   3437   -532   -425    192       O  
ATOM   1342  N   THR A 175      -3.408   2.666  20.185  1.00 26.13           N  
ANISOU 1342  N   THR A 175     3802   3241   2884   -531   -385     86       N  
ATOM   1343  CA  THR A 175      -4.608   3.274  20.757  1.00 30.59           C  
ANISOU 1343  CA  THR A 175     4502   3816   3305   -458   -284     25       C  
ATOM   1344  C   THR A 175      -5.457   3.902  19.660  1.00 31.56           C  
ANISOU 1344  C   THR A 175     4631   3915   3446   -296   -175    -35       C  
ATOM   1345  O   THR A 175      -5.013   4.081  18.529  1.00 31.03           O  
ANISOU 1345  O   THR A 175     4518   3804   3468   -268   -180    -32       O  
ATOM   1346  CB  THR A 175      -4.263   4.353  21.792  1.00 27.17           C  
ANISOU 1346  CB  THR A 175     4285   3325   2714   -552   -296    -20       C  
ATOM   1347  OG1 THR A 175      -3.581   5.441  21.165  1.00 28.74           O  
ANISOU 1347  OG1 THR A 175     4582   3420   2919   -577   -291    -64       O  
ATOM   1348  CG2 THR A 175      -3.405   3.756  22.908  1.00 29.93           C  
ANISOU 1348  CG2 THR A 175     4633   3717   3022   -715   -432     47       C  
ATOM   1349  N   ASP A 176      -6.689   4.260  20.015  1.00 28.15           N  
ANISOU 1349  N   ASP A 176     4256   3519   2921   -184    -76    -91       N  
ATOM   1350  CA  ASP A 176      -7.409   5.243  19.210  1.00 29.95           C  
ANISOU 1350  CA  ASP A 176     4551   3702   3125    -14     11   -152       C  
ATOM   1351  C   ASP A 176      -6.787   6.624  19.447  1.00 35.36           C  
ANISOU 1351  C   ASP A 176     5481   4235   3719    -50     21   -194       C  
ATOM   1352  O   ASP A 176      -5.849   6.787  20.245  1.00 29.42           O  
ANISOU 1352  O   ASP A 176     4822   3437   2918   -221    -41   -185       O  
ATOM   1353  CB  ASP A 176      -8.906   5.192  19.536  1.00 29.05           C  
ANISOU 1353  CB  ASP A 176     4392   3690   2954    131    114   -207       C  
ATOM   1354  CG  ASP A 176      -9.207   5.478  21.007  1.00 32.81           C  
ANISOU 1354  CG  ASP A 176     5001   4174   3292     73    167   -250       C  
ATOM   1355  OD1 ASP A 176      -8.448   6.255  21.622  1.00 32.88           O  
ANISOU 1355  OD1 ASP A 176     5205   4071   3216    -22    142   -265       O  
ATOM   1356  OD2 ASP A 176     -10.236   4.982  21.519  1.00 31.96           O  
ANISOU 1356  OD2 ASP A 176     4808   4187   3150    115    244   -280       O  
ATOM   1357  N   LEU A 177      -7.310   7.647  18.775  1.00 30.85           N  
ANISOU 1357  N   LEU A 177     5028   3579   3114    108     94   -239       N  
ATOM   1358  CA  LEU A 177      -6.719   8.974  18.908  1.00 29.77           C  
ANISOU 1358  CA  LEU A 177     5157   3265   2889     65    119   -279       C  
ATOM   1359  C   LEU A 177      -7.145   9.686  20.187  1.00 33.63           C  
ANISOU 1359  C   LEU A 177     5841   3707   3232     63    189   -355       C  
ATOM   1360  O   LEU A 177      -6.671  10.790  20.444  1.00 34.54           O  
ANISOU 1360  O   LEU A 177     6205   3661   3257      5    219   -402       O  
ATOM   1361  CB  LEU A 177      -7.051   9.828  17.678  1.00 33.08           C  
ANISOU 1361  CB  LEU A 177     5675   3577   3316    237    169   -285       C  
ATOM   1362  CG  LEU A 177      -6.042   9.653  16.524  1.00 32.74           C  
ANISOU 1362  CG  LEU A 177     5583   3493   3366    138    112   -230       C  
ATOM   1363  CD1 LEU A 177      -4.729  10.309  16.975  1.00 36.36           C  
ANISOU 1363  CD1 LEU A 177     6211   3822   3780    -93     88   -246       C  
ATOM   1364  CD2 LEU A 177      -5.836   8.193  16.120  1.00 28.50           C  
ANISOU 1364  CD2 LEU A 177     4752   3116   2961     81     41   -174       C  
ATOM   1365  N   GLU A 178      -8.012   9.078  20.992  1.00 34.05           N  
ANISOU 1365  N   GLU A 178     5798   3890   3250    108    229   -374       N  
ATOM   1366  CA  GLU A 178      -8.253   9.531  22.361  1.00 38.58           C  
ANISOU 1366  CA  GLU A 178     6544   4442   3674     49    292   -445       C  
ATOM   1367  C   GLU A 178      -7.373   8.819  23.361  1.00 31.49           C  
ANISOU 1367  C   GLU A 178     5627   3603   2733   -202    188   -402       C  
ATOM   1368  O   GLU A 178      -7.498   9.067  24.569  1.00 35.95           O  
ANISOU 1368  O   GLU A 178     6338   4167   3152   -287    226   -453       O  
ATOM   1369  CB  GLU A 178      -9.722   9.346  22.735  1.00 37.67           C  
ANISOU 1369  CB  GLU A 178     6349   4440   3524    230    416   -502       C  
ATOM   1370  CG  GLU A 178     -10.655  10.082  21.773  1.00 47.47           C  
ANISOU 1370  CG  GLU A 178     7590   5640   4805    514    500   -543       C  
ATOM   1371  CD  GLU A 178     -12.113   9.936  22.143  1.00 60.25           C  
ANISOU 1371  CD  GLU A 178     9091   7399   6402    701    625   -613       C  
ATOM   1372  OE1 GLU A 178     -12.429   9.075  22.993  1.00 64.29           O  
ANISOU 1372  OE1 GLU A 178     9490   8055   6883    591    650   -620       O  
ATOM   1373  OE2 GLU A 178     -12.944  10.680  21.580  1.00 64.99           O  
ANISOU 1373  OE2 GLU A 178     9710   7969   7014    960    698   -661       O  
ATOM   1374  N   GLY A 179      -6.484   7.953  22.894  1.00 32.44           N  
ANISOU 1374  N   GLY A 179     5581   3774   2970   -314     58   -309       N  
ATOM   1375  CA  GLY A 179      -5.517   7.325  23.758  1.00 37.17           C  
ANISOU 1375  CA  GLY A 179     6161   4423   3540   -530    -70   -254       C  
ATOM   1376  C   GLY A 179      -5.981   6.067  24.442  1.00 35.25           C  
ANISOU 1376  C   GLY A 179     5782   4318   3291   -555    -93   -195       C  
ATOM   1377  O   GLY A 179      -5.288   5.585  25.348  1.00 34.81           O  
ANISOU 1377  O   GLY A 179     5749   4301   3175   -719   -203   -142       O  
ATOM   1378  N   ASN A 180      -7.113   5.494  24.039  1.00 32.04           N  
ANISOU 1378  N   ASN A 180     5240   3994   2940   -408     -2   -198       N  
ATOM   1379  CA  ASN A 180      -7.543   4.240  24.630  1.00 28.82           C  
ANISOU 1379  CA  ASN A 180     4716   3705   2529   -459    -10   -140       C  
ATOM   1380  C   ASN A 180      -6.963   3.100  23.799  1.00 34.33           C  
ANISOU 1380  C   ASN A 180     5207   4433   3403   -478   -115    -40       C  
ATOM   1381  O   ASN A 180      -7.162   3.060  22.571  1.00 31.85           O  
ANISOU 1381  O   ASN A 180     4769   4116   3217   -366    -90    -49       O  
ATOM   1382  CB  ASN A 180      -9.066   4.146  24.691  1.00 30.68           C  
ANISOU 1382  CB  ASN A 180     4896   4030   2731   -325    153   -209       C  
ATOM   1383  CG  ASN A 180      -9.700   5.316  25.392  1.00 32.66           C  
ANISOU 1383  CG  ASN A 180     5338   4243   2828   -264    283   -324       C  
ATOM   1384  OD1 ASN A 180      -9.604   5.459  26.628  1.00 36.77           O  
ANISOU 1384  OD1 ASN A 180     6020   4761   3189   -388    301   -346       O  
ATOM   1385  ND2 ASN A 180     -10.386   6.168  24.617  1.00 33.12           N  
ANISOU 1385  ND2 ASN A 180     5392   4267   2923    -61    378   -401       N  
ATOM   1386  N   PHE A 181      -6.221   2.201  24.460  1.00 31.91           N  
ANISOU 1386  N   PHE A 181     4879   4150   3097   -615   -235     55       N  
ATOM   1387  CA  PHE A 181      -5.689   1.033  23.768  1.00 28.88           C  
ANISOU 1387  CA  PHE A 181     4311   3780   2883   -620   -322    148       C  
ATOM   1388  C   PHE A 181      -6.815   0.215  23.155  1.00 31.45           C  
ANISOU 1388  C   PHE A 181     4497   4170   3282   -528   -215    138       C  
ATOM   1389  O   PHE A 181      -7.917   0.117  23.703  1.00 28.80           O  
ANISOU 1389  O   PHE A 181     4191   3902   2851   -514   -105     97       O  
ATOM   1390  CB  PHE A 181      -4.852   0.147  24.724  1.00 27.62           C  
ANISOU 1390  CB  PHE A 181     4167   3630   2695   -751   -467    261       C  
ATOM   1391  CG  PHE A 181      -3.379   0.429  24.638  1.00 30.94           C  
ANISOU 1391  CG  PHE A 181     4570   4012   3175   -823   -626    300       C  
ATOM   1392  CD1 PHE A 181      -2.594  -0.170  23.668  1.00 28.88           C  
ANISOU 1392  CD1 PHE A 181     4129   3733   3110   -788   -694    349       C  
ATOM   1393  CD2 PHE A 181      -2.792   1.364  25.484  1.00 31.87           C  
ANISOU 1393  CD2 PHE A 181     4844   4117   3148   -933   -693    269       C  
ATOM   1394  CE1 PHE A 181      -1.248   0.123  23.561  1.00 28.51           C  
ANISOU 1394  CE1 PHE A 181     4033   3673   3127   -856   -825    370       C  
ATOM   1395  CE2 PHE A 181      -1.445   1.693  25.365  1.00 37.93           C  
ANISOU 1395  CE2 PHE A 181     5569   4872   3970  -1019   -835    288       C  
ATOM   1396  CZ  PHE A 181      -0.664   1.073  24.398  1.00 31.90           C  
ANISOU 1396  CZ  PHE A 181     4598   4106   3415   -977   -900    338       C  
ATOM   1397  N   TYR A 182      -6.553  -0.294  21.955  1.00 30.77           N  
ANISOU 1397  N   TYR A 182     4256   4072   3363   -473   -236    159       N  
ATOM   1398  CA  TYR A 182      -7.222  -1.486  21.488  1.00 25.90           C  
ANISOU 1398  CA  TYR A 182     3500   3509   2833   -452   -188    181       C  
ATOM   1399  C   TYR A 182      -6.695  -2.689  22.262  1.00 25.67           C  
ANISOU 1399  C   TYR A 182     3478   3459   2816   -560   -271    292       C  
ATOM   1400  O   TYR A 182      -5.485  -2.893  22.347  1.00 32.54           O  
ANISOU 1400  O   TYR A 182     4346   4270   3749   -600   -402    365       O  
ATOM   1401  CB  TYR A 182      -6.968  -1.665  19.987  1.00 24.89           C  
ANISOU 1401  CB  TYR A 182     3232   3361   2865   -377   -191    167       C  
ATOM   1402  CG  TYR A 182      -7.638  -0.569  19.161  1.00 25.52           C  
ANISOU 1402  CG  TYR A 182     3316   3462   2918   -253   -112     73       C  
ATOM   1403  CD1 TYR A 182      -9.007  -0.630  18.887  1.00 28.64           C  
ANISOU 1403  CD1 TYR A 182     3641   3960   3282   -168     -9      9       C  
ATOM   1404  CD2 TYR A 182      -6.914   0.532  18.689  1.00 25.49           C  
ANISOU 1404  CD2 TYR A 182     3392   3378   2914   -222   -143     52       C  
ATOM   1405  CE1 TYR A 182      -9.646   0.381  18.131  1.00 26.94           C  
ANISOU 1405  CE1 TYR A 182     3428   3768   3040    -21     44    -64       C  
ATOM   1406  CE2 TYR A 182      -7.546   1.557  17.907  1.00 24.33           C  
ANISOU 1406  CE2 TYR A 182     3284   3227   2732    -89    -75    -18       C  
ATOM   1407  CZ  TYR A 182      -8.905   1.451  17.670  1.00 23.40           C  
ANISOU 1407  CZ  TYR A 182     3091   3213   2586     24      8    -69       C  
ATOM   1408  OH  TYR A 182      -9.531   2.443  16.969  1.00 24.89           O  
ANISOU 1408  OH  TYR A 182     3319   3401   2737    180     55   -125       O  
ATOM   1409  N   GLY A 183      -7.606  -3.495  22.784  1.00 27.01           N  
ANISOU 1409  N   GLY A 183     3653   3680   2931   -604   -195    305       N  
ATOM   1410  CA  GLY A 183      -7.261  -4.697  23.534  1.00 26.18           C  
ANISOU 1410  CA  GLY A 183     3592   3536   2819   -702   -259    421       C  
ATOM   1411  C   GLY A 183      -6.893  -4.366  24.965  1.00 28.37           C  
ANISOU 1411  C   GLY A 183     4050   3808   2920   -794   -330    475       C  
ATOM   1412  O   GLY A 183      -7.050  -3.244  25.418  1.00 32.29           O  
ANISOU 1412  O   GLY A 183     4641   4335   3293   -794   -301    403       O  
ATOM   1413  N   PRO A 184      -6.366  -5.358  25.678  1.00 30.16           N  
ANISOU 1413  N   PRO A 184     4345   3986   3130   -869   -429    604       N  
ATOM   1414  CA  PRO A 184      -6.074  -5.231  27.120  1.00 32.46           C  
ANISOU 1414  CA  PRO A 184     4828   4281   3223   -975   -510    673       C  
ATOM   1415  C   PRO A 184      -4.702  -4.657  27.451  1.00 38.21           C  
ANISOU 1415  C   PRO A 184     5590   4985   3943   -987   -708    723       C  
ATOM   1416  O   PRO A 184      -4.306  -4.662  28.627  1.00 37.18           O  
ANISOU 1416  O   PRO A 184     5615   4864   3649  -1081   -815    797       O  
ATOM   1417  CB  PRO A 184      -6.164  -6.687  27.577  1.00 33.79           C  
ANISOU 1417  CB  PRO A 184     5052   4397   3389  -1036   -532    806       C  
ATOM   1418  CG  PRO A 184      -5.650  -7.454  26.387  1.00 33.25           C  
ANISOU 1418  CG  PRO A 184     4812   4256   3566   -943   -573    839       C  
ATOM   1419  CD  PRO A 184      -6.151  -6.725  25.174  1.00 32.55           C  
ANISOU 1419  CD  PRO A 184     4567   4220   3582   -859   -456    692       C  
ATOM   1420  N   PHE A 185      -3.979  -4.171  26.457  1.00 30.42           N  
ANISOU 1420  N   PHE A 185     4463   3980   3115   -911   -758    682       N  
ATOM   1421  CA  PHE A 185      -2.581  -3.809  26.577  1.00 33.08           C  
ANISOU 1421  CA  PHE A 185     4771   4306   3492   -931   -947    727       C  
ATOM   1422  C   PHE A 185      -2.408  -2.503  27.332  1.00 33.60           C  
ANISOU 1422  C   PHE A 185     4983   4410   3374  -1019   -972    655       C  
ATOM   1423  O   PHE A 185      -3.304  -1.658  27.393  1.00 36.40           O  
ANISOU 1423  O   PHE A 185     5431   4779   3621  -1018   -821    542       O  
ATOM   1424  CB  PHE A 185      -1.967  -3.723  25.170  1.00 33.63           C  
ANISOU 1424  CB  PHE A 185     4640   4346   3791   -839   -948    687       C  
ATOM   1425  CG  PHE A 185      -2.253  -4.946  24.368  1.00 31.09           C  
ANISOU 1425  CG  PHE A 185     4197   3979   3638   -759   -892    730       C  
ATOM   1426  CD1 PHE A 185      -1.742  -6.165  24.780  1.00 32.74           C  
ANISOU 1426  CD1 PHE A 185     4396   4139   3903   -752  -1002    865       C  
ATOM   1427  CD2 PHE A 185      -3.071  -4.905  23.264  1.00 28.88           C  
ANISOU 1427  CD2 PHE A 185     3833   3698   3442   -693   -734    638       C  
ATOM   1428  CE1 PHE A 185      -2.021  -7.345  24.089  1.00 39.95           C  
ANISOU 1428  CE1 PHE A 185     5232   4983   4964   -690   -937    900       C  
ATOM   1429  CE2 PHE A 185      -3.356  -6.080  22.572  1.00 30.60           C  
ANISOU 1429  CE2 PHE A 185     3958   3872   3796   -647   -679    667       C  
ATOM   1430  CZ  PHE A 185      -2.828  -7.288  22.979  1.00 32.45           C  
ANISOU 1430  CZ  PHE A 185     4198   4038   4093   -650   -771    792       C  
ATOM   1431  N   VAL A 186      -1.223  -2.353  27.920  1.00 33.59           N  
ANISOU 1431  N   VAL A 186     4998   4427   3336  -1093  -1169    717       N  
ATOM   1432  CA  VAL A 186      -0.850  -1.133  28.619  1.00 35.54           C  
ANISOU 1432  CA  VAL A 186     5385   4706   3412  -1208  -1218    645       C  
ATOM   1433  C   VAL A 186       0.520  -0.686  28.128  1.00 36.23           C  
ANISOU 1433  C   VAL A 186     5335   4808   3623  -1236  -1367    638       C  
ATOM   1434  O   VAL A 186       1.324  -1.500  27.664  1.00 37.80           O  
ANISOU 1434  O   VAL A 186     5347   5014   4002  -1178  -1483    725       O  
ATOM   1435  CB  VAL A 186      -0.858  -1.359  30.154  1.00 36.41           C  
ANISOU 1435  CB  VAL A 186     5695   4860   3277  -1331  -1321    720       C  
ATOM   1436  CG1 VAL A 186      -2.281  -1.550  30.609  1.00 42.04           C  
ANISOU 1436  CG1 VAL A 186     6554   5568   3852  -1330  -1124    687       C  
ATOM   1437  CG2 VAL A 186      -0.060  -2.595  30.508  1.00 39.84           C  
ANISOU 1437  CG2 VAL A 186     6056   5307   3773  -1318  -1527    898       C  
ATOM   1438  N   ASP A 187       0.804   0.617  28.254  1.00 35.04           N  
ANISOU 1438  N   ASP A 187     5280   4660   3374  -1333  -1354    526       N  
ATOM   1439  CA  ASP A 187       2.048   1.154  27.694  1.00 33.98           C  
ANISOU 1439  CA  ASP A 187     5011   4543   3356  -1389  -1459    494       C  
ATOM   1440  C   ASP A 187       3.154   1.110  28.752  1.00 37.32           C  
ANISOU 1440  C   ASP A 187     5442   5062   3676  -1533  -1704    560       C  
ATOM   1441  O   ASP A 187       3.586   2.120  29.315  1.00 41.91           O  
ANISOU 1441  O   ASP A 187     6145   5671   4106  -1694  -1756    482       O  
ATOM   1442  CB  ASP A 187       1.839   2.554  27.095  1.00 39.75           C  
ANISOU 1442  CB  ASP A 187     5839   5207   4057  -1425  -1309    341       C  
ATOM   1443  CG  ASP A 187       1.150   3.549  28.053  1.00 40.75           C  
ANISOU 1443  CG  ASP A 187     6254   5304   3927  -1515  -1226    249       C  
ATOM   1444  OD1 ASP A 187       0.611   3.143  29.095  1.00 42.78           O  
ANISOU 1444  OD1 ASP A 187     6634   5597   4024  -1541  -1242    292       O  
ATOM   1445  OD2 ASP A 187       1.143   4.760  27.752  1.00 37.86           O  
ANISOU 1445  OD2 ASP A 187     6007   4866   3513  -1563  -1130    129       O  
ATOM   1446  N   ARG A 188       3.627  -0.115  28.995  1.00 40.55           N  
ANISOU 1446  N   ARG A 188     5719   5518   4170  -1469  -1864    708       N  
ATOM   1447  CA  ARG A 188       4.814  -0.380  29.804  1.00 48.44           C  
ANISOU 1447  CA  ARG A 188     6650   6627   5127  -1555  -2138    799       C  
ATOM   1448  C   ARG A 188       5.499  -1.622  29.256  1.00 50.33           C  
ANISOU 1448  C   ARG A 188     6631   6881   5613  -1402  -2254    926       C  
ATOM   1449  O   ARG A 188       4.847  -2.508  28.698  1.00 44.32           O  
ANISOU 1449  O   ARG A 188     5834   6033   4974  -1253  -2138    977       O  
ATOM   1450  CB  ARG A 188       4.500  -0.615  31.289  1.00 53.96           C  
ANISOU 1450  CB  ARG A 188     7582   7368   5552  -1645  -2250    880       C  
ATOM   1451  CG  ARG A 188       3.160  -0.133  31.731  1.00 61.04           C  
ANISOU 1451  CG  ARG A 188     8748   8198   6245  -1684  -2037    801       C  
ATOM   1452  CD  ARG A 188       2.725  -0.796  33.029  1.00 61.54           C  
ANISOU 1452  CD  ARG A 188     9017   8288   6078  -1734  -2114    914       C  
ATOM   1453  NE  ARG A 188       1.355  -0.397  33.331  1.00 67.28           N  
ANISOU 1453  NE  ARG A 188     9966   8958   6641  -1755  -1867    822       N  
ATOM   1454  CZ  ARG A 188       0.498  -1.110  34.054  1.00 75.97           C  
ANISOU 1454  CZ  ARG A 188    11225  10045   7596  -1757  -1802    896       C  
ATOM   1455  NH1 ARG A 188       0.863  -2.280  34.562  1.00 70.25           N  
ANISOU 1455  NH1 ARG A 188    10497   9336   6858  -1737  -1973   1079       N  
ATOM   1456  NH2 ARG A 188      -0.733  -0.651  34.261  1.00 81.62           N  
ANISOU 1456  NH2 ARG A 188    12103  10728   8180  -1775  -1557    785       N  
ATOM   1457  N   GLN A 189       6.815  -1.699  29.458  1.00 47.04           N  
ANISOU 1457  N   GLN A 189     6031   6575   5264  -1440  -2484    973       N  
ATOM   1458  CA  GLN A 189       7.605  -2.816  28.943  1.00 51.45           C  
ANISOU 1458  CA  GLN A 189     6321   7152   6074  -1275  -2602   1083       C  
ATOM   1459  C   GLN A 189       7.576  -4.003  29.908  1.00 58.10           C  
ANISOU 1459  C   GLN A 189     7241   7986   6848  -1178  -2760   1270       C  
ATOM   1460  O   GLN A 189       8.591  -4.464  30.432  1.00 60.57           O  
ANISOU 1460  O   GLN A 189     7436   8370   7207  -1117  -2923   1340       O  
ATOM   1461  CB  GLN A 189       9.020  -2.346  28.646  1.00 55.49           C  
ANISOU 1461  CB  GLN A 189     6578   7785   6722  -1321  -2703   1018       C  
ATOM   1462  CG  GLN A 189       9.013  -1.173  27.677  1.00 49.82           C  
ANISOU 1462  CG  GLN A 189     5820   7056   6052  -1446  -2547    847       C  
ATOM   1463  CD  GLN A 189      10.342  -0.961  26.987  1.00 54.84           C  
ANISOU 1463  CD  GLN A 189     6160   7783   6895  -1448  -2562    774       C  
ATOM   1464  OE1 GLN A 189      10.395  -0.757  25.772  1.00 51.39           O  
ANISOU 1464  OE1 GLN A 189     5593   7305   6630  -1432  -2420    695       O  
ATOM   1465  NE2 GLN A 189      11.419  -0.974  27.759  1.00 49.42           N  
ANISOU 1465  NE2 GLN A 189     5368   7230   6181  -1476  -2726    790       N  
ATOM   1466  N   THR A 190       6.365  -4.496  30.134  1.00 54.43           N  
ANISOU 1466  N   THR A 190     6992   7412   6277  -1144  -2634   1320       N  
ATOM   1467  CA  THR A 190       6.122  -5.675  30.948  1.00 63.63           C  
ANISOU 1467  CA  THR A 190     8285   8530   7362  -1065  -2745   1504       C  
ATOM   1468  C   THR A 190       5.737  -6.843  30.055  1.00 65.81           C  
ANISOU 1468  C   THR A 190     8472   8666   7868   -875  -2617   1563       C  
ATOM   1469  O   THR A 190       5.477  -6.688  28.859  1.00 57.73           O  
ANISOU 1469  O   THR A 190     7317   7589   7028   -819  -2424   1450       O  
ATOM   1470  CB  THR A 190       5.011  -5.413  31.966  1.00 61.02           C  
ANISOU 1470  CB  THR A 190     8290   8175   6720  -1196  -2657   1504       C  
ATOM   1471  OG1 THR A 190       3.829  -4.995  31.263  1.00 60.50           O  
ANISOU 1471  OG1 THR A 190     8288   8027   6671  -1202  -2353   1366       O  
ATOM   1472  CG2 THR A 190       5.437  -4.320  32.940  1.00 56.09           C  
ANISOU 1472  CG2 THR A 190     7771   7661   5881  -1371  -2730   1418       C  
ATOM   1473  N   ALA A 191       5.689  -8.018  30.670  1.00 61.96           N  
ANISOU 1473  N   ALA A 191     8085   8108   7349   -786  -2725   1743       N  
ATOM   1474  CA  ALA A 191       5.263  -9.233  29.988  1.00 50.10           C  
ANISOU 1474  CA  ALA A 191     6560   6446   6031   -625  -2604   1811       C  
ATOM   1475  C   ALA A 191       3.796  -9.110  29.608  1.00 50.91           C  
ANISOU 1475  C   ALA A 191     6814   6465   6063   -694  -2307   1707       C  
ATOM   1476  O   ALA A 191       2.913  -9.112  30.472  1.00 50.23           O  
ANISOU 1476  O   ALA A 191     6980   6366   5740   -802  -2249   1737       O  
ATOM   1477  CB  ALA A 191       5.497 -10.440  30.895  1.00 47.95           C  
ANISOU 1477  CB  ALA A 191     6423   6098   5698   -535  -2770   2022       C  
ATOM   1478  N   GLN A 192       3.531  -8.963  28.315  1.00 50.01           N  
ANISOU 1478  N   GLN A 192     6542   6312   6147   -637  -2117   1577       N  
ATOM   1479  CA  GLN A 192       2.182  -8.939  27.790  1.00 54.15           C  
ANISOU 1479  CA  GLN A 192     7157   6774   6643   -674  -1850   1478       C  
ATOM   1480  C   GLN A 192       2.147  -9.813  26.552  1.00 55.73           C  
ANISOU 1480  C   GLN A 192     7206   6866   7102   -541  -1735   1461       C  
ATOM   1481  O   GLN A 192       3.145  -9.943  25.837  1.00 53.38           O  
ANISOU 1481  O   GLN A 192     6697   6569   7016   -437  -1805   1454       O  
ATOM   1482  CB  GLN A 192       1.710  -7.527  27.419  1.00 46.12           C  
ANISOU 1482  CB  GLN A 192     6131   5843   5551   -769  -1714   1296       C  
ATOM   1483  CG  GLN A 192       1.649  -6.584  28.606  1.00 44.26           C  
ANISOU 1483  CG  GLN A 192     6072   5698   5048   -914  -1790   1281       C  
ATOM   1484  CD  GLN A 192       1.337  -5.176  28.195  1.00 42.88           C  
ANISOU 1484  CD  GLN A 192     5893   5576   4822   -984  -1664   1104       C  
ATOM   1485  OE1 GLN A 192       0.241  -4.882  27.700  1.00 42.54           O  
ANISOU 1485  OE1 GLN A 192     5892   5507   4763   -974  -1451   1003       O  
ATOM   1486  NE2 GLN A 192       2.310  -4.284  28.367  1.00 40.18           N  
ANISOU 1486  NE2 GLN A 192     5499   5310   4458  -1052  -1796   1063       N  
ATOM   1487  N   ALA A 193       0.997 -10.429  26.325  1.00 48.64           N  
ANISOU 1487  N   ALA A 193     6417   5884   6182   -558  -1551   1447       N  
ATOM   1488  CA  ALA A 193       0.827 -11.315  25.188  1.00 53.36           C  
ANISOU 1488  CA  ALA A 193     6910   6370   6996   -461  -1425   1420       C  
ATOM   1489  C   ALA A 193      -0.542 -11.080  24.571  1.00 53.52           C  
ANISOU 1489  C   ALA A 193     6965   6402   6969   -535  -1183   1285       C  
ATOM   1490  O   ALA A 193      -1.515 -10.804  25.281  1.00 50.52           O  
ANISOU 1490  O   ALA A 193     6741   6066   6390   -645  -1106   1269       O  
ATOM   1491  CB  ALA A 193       0.986 -12.777  25.598  1.00 59.14           C  
ANISOU 1491  CB  ALA A 193     7747   6947   7775   -388  -1489   1586       C  
ATOM   1492  N   ALA A 194      -0.604 -11.171  23.244  1.00 49.43           N  
ANISOU 1492  N   ALA A 194     6292   5858   6631   -473  -1064   1181       N  
ATOM   1493  CA  ALA A 194      -1.887 -11.147  22.559  1.00 49.12           C  
ANISOU 1493  CA  ALA A 194     6263   5835   6567   -527   -854   1063       C  
ATOM   1494  C   ALA A 194      -2.689 -12.403  22.886  1.00 50.78           C  
ANISOU 1494  C   ALA A 194     6611   5940   6743   -578   -770   1130       C  
ATOM   1495  O   ALA A 194      -2.134 -13.486  23.088  1.00 53.69           O  
ANISOU 1495  O   ALA A 194     7031   6172   7197   -523   -841   1250       O  
ATOM   1496  CB  ALA A 194      -1.669 -11.039  21.054  1.00 55.65           C  
ANISOU 1496  CB  ALA A 194     6908   6655   7582   -455   -768    949       C  
ATOM   1497  N   GLY A 195      -4.006 -12.250  22.974  1.00 42.66           N  
ANISOU 1497  N   GLY A 195     5648   4976   5586   -685   -614   1051       N  
ATOM   1498  CA  GLY A 195      -4.877 -13.404  23.033  1.00 45.87           C  
ANISOU 1498  CA  GLY A 195     6157   5297   5974   -766   -491   1075       C  
ATOM   1499  C   GLY A 195      -4.790 -14.225  21.754  1.00 45.33           C  
ANISOU 1499  C   GLY A 195     5983   5129   6110   -712   -412   1022       C  
ATOM   1500  O   GLY A 195      -4.197 -13.826  20.750  1.00 44.83           O  
ANISOU 1500  O   GLY A 195     5757   5085   6190   -616   -429    949       O  
ATOM   1501  N   THR A 196      -5.378 -15.419  21.805  1.00 45.65           N  
ANISOU 1501  N   THR A 196     6138   5053   6155   -792   -314   1056       N  
ATOM   1502  CA  THR A 196      -5.423 -16.258  20.615  1.00 44.82           C  
ANISOU 1502  CA  THR A 196     5964   4844   6222   -770   -215    987       C  
ATOM   1503  C   THR A 196      -6.192 -15.532  19.524  1.00 44.98           C  
ANISOU 1503  C   THR A 196     5814   5025   6251   -802    -98    802       C  
ATOM   1504  O   THR A 196      -7.294 -15.027  19.754  1.00 56.99           O  
ANISOU 1504  O   THR A 196     7327   6694   7631   -905    -11    727       O  
ATOM   1505  CB  THR A 196      -6.089 -17.599  20.920  1.00 49.13           C  
ANISOU 1505  CB  THR A 196     6694   5237   6737   -893   -107   1039       C  
ATOM   1506  OG1 THR A 196      -7.421 -17.366  21.393  1.00 70.87           O  
ANISOU 1506  OG1 THR A 196     9497   8124   9308  -1074     18    975       O  
ATOM   1507  CG2 THR A 196      -5.303 -18.363  21.989  1.00 50.97           C  
ANISOU 1507  CG2 THR A 196     7128   5285   6953   -840   -237   1246       C  
ATOM   1508  N   ASP A 197      -5.602 -15.452  18.347  1.00 39.66           N  
ANISOU 1508  N   ASP A 197     5001   4330   5736   -706    -97    730       N  
ATOM   1509  CA  ASP A 197      -6.303 -14.782  17.266  1.00 35.79           C  
ANISOU 1509  CA  ASP A 197     4369   3989   5240   -729     -3    568       C  
ATOM   1510  C   ASP A 197      -7.225 -15.761  16.545  1.00 40.04           C  
ANISOU 1510  C   ASP A 197     4918   4495   5803   -844    146    479       C  
ATOM   1511  O   ASP A 197      -7.144 -16.972  16.720  1.00 44.42           O  
ANISOU 1511  O   ASP A 197     5591   4876   6410   -894    186    535       O  
ATOM   1512  CB  ASP A 197      -5.314 -14.158  16.294  1.00 32.55           C  
ANISOU 1512  CB  ASP A 197     3822   3588   4958   -601    -56    520       C  
ATOM   1513  CG  ASP A 197      -5.918 -12.988  15.509  1.00 37.78           C  
ANISOU 1513  CG  ASP A 197     4371   4429   5554   -599    -12    391       C  
ATOM   1514  OD1 ASP A 197      -6.952 -12.401  15.935  1.00 38.66           O  
ANISOU 1514  OD1 ASP A 197     4493   4676   5520   -656     23    353       O  
ATOM   1515  OD2 ASP A 197      -5.328 -12.646  14.474  1.00 37.65           O  
ANISOU 1515  OD2 ASP A 197     4261   4414   5631   -530    -11    331       O  
ATOM   1516  N   THR A 198      -8.128 -15.209  15.733  1.00 36.19           N  
ANISOU 1516  N   THR A 198     4309   4175   5265   -890    225    338       N  
ATOM   1517  CA  THR A 198      -9.017 -15.997  14.883  1.00 31.28           C  
ANISOU 1517  CA  THR A 198     3660   3568   4658  -1014    354    225       C  
ATOM   1518  C   THR A 198      -9.025 -15.352  13.499  1.00 32.00           C  
ANISOU 1518  C   THR A 198     3598   3770   4790   -952    363     98       C  
ATOM   1519  O   THR A 198      -8.521 -14.246  13.310  1.00 34.45           O  
ANISOU 1519  O   THR A 198     3838   4153   5097   -830    286    100       O  
ATOM   1520  CB  THR A 198     -10.425 -16.067  15.470  1.00 39.84           C  
ANISOU 1520  CB  THR A 198     4752   4793   5592  -1175    444    179       C  
ATOM   1521  OG1 THR A 198     -10.919 -14.735  15.659  1.00 43.28           O  
ANISOU 1521  OG1 THR A 198     5079   5443   5923  -1116    411    134       O  
ATOM   1522  CG2 THR A 198     -10.399 -16.751  16.823  1.00 47.10           C  
ANISOU 1522  CG2 THR A 198     5858   5587   6450  -1258    449    311       C  
ATOM   1523  N   THR A 199      -9.585 -16.053  12.514  1.00 34.46           N  
ANISOU 1523  N   THR A 199     3877   4087   5129  -1050    458    -14       N  
ATOM   1524  CA  THR A 199      -9.656 -15.509  11.159  1.00 32.05           C  
ANISOU 1524  CA  THR A 199     3449   3893   4836  -1008    465   -133       C  
ATOM   1525  C   THR A 199     -10.988 -14.797  10.962  1.00 26.26           C  
ANISOU 1525  C   THR A 199     2597   3418   3962  -1061    480   -228       C  
ATOM   1526  O   THR A 199     -12.029 -15.291  11.417  1.00 33.92           O  
ANISOU 1526  O   THR A 199     3562   4467   4860  -1204    547   -262       O  
ATOM   1527  CB  THR A 199      -9.511 -16.644  10.136  1.00 38.07           C  
ANISOU 1527  CB  THR A 199     4245   4528   5691  -1087    554   -215       C  
ATOM   1528  OG1 THR A 199      -8.223 -17.249  10.289  1.00 35.96           O  
ANISOU 1528  OG1 THR A 199     4069   4021   5572   -996    541   -129       O  
ATOM   1529  CG2 THR A 199      -9.665 -16.123   8.690  1.00 36.33           C  
ANISOU 1529  CG2 THR A 199     3916   4436   5451  -1069    564   -344       C  
ATOM   1530  N   ILE A 200     -10.957 -13.656  10.275  1.00 29.52           N  
ANISOU 1530  N   ILE A 200     2916   3962   4338   -946    423   -271       N  
ATOM   1531  CA  ILE A 200     -12.142 -12.803  10.086  1.00 27.03           C  
ANISOU 1531  CA  ILE A 200     2478   3895   3895   -936    413   -347       C  
ATOM   1532  C   ILE A 200     -12.965 -13.371   8.930  1.00 28.22           C  
ANISOU 1532  C   ILE A 200     2540   4161   4020  -1049    463   -480       C  
ATOM   1533  O   ILE A 200     -12.727 -13.039   7.767  1.00 32.23           O  
ANISOU 1533  O   ILE A 200     3016   4703   4529   -995    435   -536       O  
ATOM   1534  CB  ILE A 200     -11.763 -11.349   9.837  1.00 26.40           C  
ANISOU 1534  CB  ILE A 200     2372   3881   3778   -758    328   -326       C  
ATOM   1535  CG1 ILE A 200     -10.798 -10.855  10.936  1.00 29.61           C  
ANISOU 1535  CG1 ILE A 200     2877   4161   4213   -676    275   -205       C  
ATOM   1536  CG2 ILE A 200     -13.023 -10.488   9.771  1.00 27.04           C  
ANISOU 1536  CG2 ILE A 200     2336   4204   3734   -712    315   -393       C  
ATOM   1537  CD1 ILE A 200      -9.865  -9.780  10.472  1.00 28.63           C  
ANISOU 1537  CD1 ILE A 200     2773   3999   4107   -542    207   -180       C  
ATOM   1538  N   THR A 201     -13.989 -14.141   9.284  1.00 28.00           N  
ANISOU 1538  N   THR A 201     2474   4216   3948  -1218    537   -535       N  
ATOM   1539  CA  THR A 201     -14.746 -14.970   8.340  1.00 35.44           C  
ANISOU 1539  CA  THR A 201     3350   5245   4869  -1387    597   -667       C  
ATOM   1540  C   THR A 201     -15.456 -14.124   7.283  1.00 39.87           C  
ANISOU 1540  C   THR A 201     3749   6061   5340  -1320    529   -765       C  
ATOM   1541  O   THR A 201     -15.377 -14.411   6.069  1.00 35.97           O  
ANISOU 1541  O   THR A 201     3245   5581   4842  -1364    523   -848       O  
ATOM   1542  CB  THR A 201     -15.754 -15.812   9.126  1.00 39.72           C  
ANISOU 1542  CB  THR A 201     3882   5844   5366  -1590    690   -700       C  
ATOM   1543  OG1 THR A 201     -15.081 -16.550  10.160  1.00 40.33           O  
ANISOU 1543  OG1 THR A 201     4140   5675   5511  -1643    744   -588       O  
ATOM   1544  CG2 THR A 201     -16.496 -16.790   8.199  1.00 36.61           C  
ANISOU 1544  CG2 THR A 201     3495   5487   4930  -1728    729   -814       C  
ATOM   1545  N   VAL A 202     -16.170 -13.080   7.723  1.00 34.37           N  
ANISOU 1545  N   VAL A 202     2933   5566   4561  -1208    476   -758       N  
ATOM   1546  CA  VAL A 202     -16.869 -12.237   6.757  1.00 37.33           C  
ANISOU 1546  CA  VAL A 202     3158   6180   4845  -1110    393   -834       C  
ATOM   1547  C   VAL A 202     -15.898 -11.651   5.737  1.00 36.20           C  
ANISOU 1547  C   VAL A 202     3104   5935   4716   -972    322   -804       C  
ATOM   1548  O   VAL A 202     -16.245 -11.501   4.556  1.00 34.70           O  
ANISOU 1548  O   VAL A 202     2852   5873   4458   -969    271   -879       O  
ATOM   1549  CB  VAL A 202     -17.681 -11.127   7.446  1.00 34.81           C  
ANISOU 1549  CB  VAL A 202     2718   6055   4451   -959    351   -819       C  
ATOM   1550  CG1 VAL A 202     -16.762 -10.125   8.161  1.00 29.44           C  
ANISOU 1550  CG1 VAL A 202     2166   5222   3796   -769    315   -697       C  
ATOM   1551  CG2 VAL A 202     -18.556 -10.402   6.421  1.00 37.55           C  
ANISOU 1551  CG2 VAL A 202     2934   6635   4700   -839    253   -887       C  
ATOM   1552  N   ASN A 203     -14.668 -11.336   6.159  1.00 28.88           N  
ANISOU 1552  N   ASN A 203     2321   4785   3866   -873    318   -697       N  
ATOM   1553  CA  ASN A 203     -13.695 -10.762   5.236  1.00 28.83           C  
ANISOU 1553  CA  ASN A 203     2397   4682   3874   -764    273   -673       C  
ATOM   1554  C   ASN A 203     -13.222 -11.804   4.229  1.00 31.67           C  
ANISOU 1554  C   ASN A 203     2811   4939   4285   -896    332   -742       C  
ATOM   1555  O   ASN A 203     -13.076 -11.503   3.028  1.00 31.57           O  
ANISOU 1555  O   ASN A 203     2808   4968   4217   -872    304   -792       O  
ATOM   1556  CB  ASN A 203     -12.498 -10.189   5.998  1.00 33.25           C  
ANISOU 1556  CB  ASN A 203     3073   5051   4509   -651    260   -555       C  
ATOM   1557  CG  ASN A 203     -12.806  -8.856   6.686  1.00 28.02           C  
ANISOU 1557  CG  ASN A 203     2399   4476   3773   -494    197   -500       C  
ATOM   1558  OD1 ASN A 203     -13.935  -8.343   6.631  1.00 28.60           O  
ANISOU 1558  OD1 ASN A 203     2368   4748   3749   -441    166   -544       O  
ATOM   1559  ND2 ASN A 203     -11.800  -8.311   7.371  1.00 27.47           N  
ANISOU 1559  ND2 ASN A 203     2431   4255   3752   -419    179   -408       N  
ATOM   1560  N   VAL A 204     -12.957 -13.029   4.697  1.00 31.47           N  
ANISOU 1560  N   VAL A 204     2841   4761   4356  -1035    420   -746       N  
ATOM   1561  CA  VAL A 204     -12.611 -14.117   3.772  1.00 30.88           C  
ANISOU 1561  CA  VAL A 204     2828   4574   4331  -1168    499   -831       C  
ATOM   1562  C   VAL A 204     -13.686 -14.265   2.715  1.00 35.18           C  
ANISOU 1562  C   VAL A 204     3279   5337   4750  -1281    483   -966       C  
ATOM   1563  O   VAL A 204     -13.387 -14.379   1.513  1.00 33.66           O  
ANISOU 1563  O   VAL A 204     3127   5136   4526  -1310    492  -1039       O  
ATOM   1564  CB  VAL A 204     -12.388 -15.434   4.535  1.00 32.22           C  
ANISOU 1564  CB  VAL A 204     3085   4548   4610  -1298    598   -813       C  
ATOM   1565  CG1 VAL A 204     -12.231 -16.602   3.568  1.00 36.23           C  
ANISOU 1565  CG1 VAL A 204     3666   4942   5157  -1450    696   -925       C  
ATOM   1566  CG2 VAL A 204     -11.144 -15.318   5.426  1.00 33.96           C  
ANISOU 1566  CG2 VAL A 204     3400   4549   4956  -1167    588   -674       C  
ATOM   1567  N   LEU A 205     -14.953 -14.285   3.143  1.00 30.33           N  
ANISOU 1567  N   LEU A 205     2533   4934   4056  -1357    462  -1008       N  
ATOM   1568  CA  LEU A 205     -16.045 -14.407   2.174  1.00 33.18           C  
ANISOU 1568  CA  LEU A 205     2793   5528   4284  -1446    419  -1129       C  
ATOM   1569  C   LEU A 205     -16.062 -13.232   1.195  1.00 36.43           C  
ANISOU 1569  C   LEU A 205     3141   6106   4594  -1299    301  -1138       C  
ATOM   1570  O   LEU A 205     -16.235 -13.424  -0.029  1.00 36.43           O  
ANISOU 1570  O   LEU A 205     3143   6191   4506  -1374    274  -1231       O  
ATOM   1571  CB  LEU A 205     -17.385 -14.542   2.915  1.00 37.28           C  
ANISOU 1571  CB  LEU A 205     3212   6219   4734  -1482    409  -1139       C  
ATOM   1572  CG  LEU A 205     -17.589 -15.875   3.643  1.00 40.10           C  
ANISOU 1572  CG  LEU A 205     3666   6427   5142  -1661    526  -1147       C  
ATOM   1573  CD1 LEU A 205     -18.782 -15.818   4.629  1.00 37.01           C  
ANISOU 1573  CD1 LEU A 205     3173   6196   4693  -1685    532  -1142       C  
ATOM   1574  CD2 LEU A 205     -17.776 -17.014   2.651  1.00 36.20           C  
ANISOU 1574  CD2 LEU A 205     3246   5893   4616  -1844    584  -1262       C  
ATOM   1575  N   ALA A 206     -15.868 -12.007   1.697  1.00 31.73           N  
ANISOU 1575  N   ALA A 206     2538   5530   3990  -1078    227  -1031       N  
ATOM   1576  CA  ALA A 206     -15.832 -10.857   0.799  1.00 32.21           C  
ANISOU 1576  CA  ALA A 206     2606   5691   3942   -908    116  -1009       C  
ATOM   1577  C   ALA A 206     -14.736 -11.007  -0.251  1.00 32.64           C  
ANISOU 1577  C   ALA A 206     2822   5576   4005   -931    152  -1019       C  
ATOM   1578  O   ALA A 206     -14.940 -10.668  -1.420  1.00 33.39           O  
ANISOU 1578  O   ALA A 206     2930   5783   3972   -919     87  -1064       O  
ATOM   1579  CB  ALA A 206     -15.631  -9.570   1.582  1.00 31.62           C  
ANISOU 1579  CB  ALA A 206     2548   5595   3870   -679     60   -891       C  
ATOM   1580  N   TRP A 207     -13.570 -11.518   0.158  1.00 29.51           N  
ANISOU 1580  N   TRP A 207     2545   4917   3752   -961    254   -977       N  
ATOM   1581  CA  TRP A 207     -12.445 -11.697  -0.755  1.00 28.82           C  
ANISOU 1581  CA  TRP A 207     2593   4662   3697   -980    317   -995       C  
ATOM   1582  C   TRP A 207     -12.721 -12.806  -1.767  1.00 32.85           C  
ANISOU 1582  C   TRP A 207     3123   5193   4166  -1178    382  -1137       C  
ATOM   1583  O   TRP A 207     -12.311 -12.707  -2.931  1.00 32.06           O  
ANISOU 1583  O   TRP A 207     3106   5082   3993  -1200    397  -1190       O  
ATOM   1584  CB  TRP A 207     -11.198 -11.985   0.074  1.00 33.66           C  
ANISOU 1584  CB  TRP A 207     3285   5014   4490   -944    401   -915       C  
ATOM   1585  CG  TRP A 207      -9.950 -12.426  -0.636  1.00 32.11           C  
ANISOU 1585  CG  TRP A 207     3196   4622   4381   -972    502   -945       C  
ATOM   1586  CD1 TRP A 207      -9.031 -11.638  -1.277  1.00 32.65           C  
ANISOU 1586  CD1 TRP A 207     3336   4635   4434   -888    510   -918       C  
ATOM   1587  CD2 TRP A 207      -9.450 -13.757  -0.695  1.00 30.36           C  
ANISOU 1587  CD2 TRP A 207     3024   4224   4287  -1087    627  -1007       C  
ATOM   1588  NE1 TRP A 207      -8.004 -12.417  -1.767  1.00 33.22           N  
ANISOU 1588  NE1 TRP A 207     3473   4528   4619   -946    638   -972       N  
ATOM   1589  CE2 TRP A 207      -8.238 -13.721  -1.416  1.00 32.03           C  
ANISOU 1589  CE2 TRP A 207     3313   4293   4562  -1053    708  -1025       C  
ATOM   1590  CE3 TRP A 207      -9.911 -14.986  -0.205  1.00 36.03           C  
ANISOU 1590  CE3 TRP A 207     3740   4879   5070  -1218    689  -1051       C  
ATOM   1591  CZ2 TRP A 207      -7.483 -14.854  -1.642  1.00 40.38           C  
ANISOU 1591  CZ2 TRP A 207     4431   5152   5759  -1116    845  -1088       C  
ATOM   1592  CZ3 TRP A 207      -9.169 -16.115  -0.460  1.00 42.26           C  
ANISOU 1592  CZ3 TRP A 207     4621   5450   5987  -1288    821  -1106       C  
ATOM   1593  CH2 TRP A 207      -7.968 -16.041  -1.165  1.00 38.51           C  
ANISOU 1593  CH2 TRP A 207     4207   4839   5585  -1223    896  -1125       C  
ATOM   1594  N   LEU A 208     -13.398 -13.877  -1.348  1.00 29.29           N  
ANISOU 1594  N   LEU A 208     2614   4764   3751  -1342    433  -1206       N  
ATOM   1595  CA  LEU A 208     -13.847 -14.864  -2.342  1.00 31.00           C  
ANISOU 1595  CA  LEU A 208     2848   5031   3897  -1555    485  -1361       C  
ATOM   1596  C   LEU A 208     -14.768 -14.219  -3.377  1.00 43.01           C  
ANISOU 1596  C   LEU A 208     4287   6845   5210  -1557    353  -1424       C  
ATOM   1597  O   LEU A 208     -14.683 -14.522  -4.584  1.00 40.07           O  
ANISOU 1597  O   LEU A 208     3989   6499   4738  -1662    368  -1525       O  
ATOM   1598  CB  LEU A 208     -14.540 -16.041  -1.650  1.00 32.13           C  
ANISOU 1598  CB  LEU A 208     2949   5163   4098  -1751    559  -1424       C  
ATOM   1599  CG  LEU A 208     -13.600 -16.960  -0.853  1.00 35.22           C  
ANISOU 1599  CG  LEU A 208     3472   5230   4680  -1774    697  -1374       C  
ATOM   1600  CD1 LEU A 208     -14.338 -18.106  -0.162  1.00 35.90           C  
ANISOU 1600  CD1 LEU A 208     3602   5266   4775  -1899    759  -1384       C  
ATOM   1601  CD2 LEU A 208     -12.410 -17.460  -1.696  1.00 36.86           C  
ANISOU 1601  CD2 LEU A 208     3837   5203   4964  -1778    806  -1420       C  
ATOM   1602  N   TYR A 209     -15.631 -13.294  -2.932  1.00 38.05           N  
ANISOU 1602  N   TYR A 209     3511   6439   4506  -1428    219  -1365       N  
ATOM   1603  CA  TYR A 209     -16.455 -12.559  -3.896  1.00 40.36           C  
ANISOU 1603  CA  TYR A 209     3723   7010   4603  -1376     67  -1400       C  
ATOM   1604  C   TYR A 209     -15.609 -11.689  -4.822  1.00 43.14           C  
ANISOU 1604  C   TYR A 209     4235   7282   4873  -1240     31  -1342       C  
ATOM   1605  O   TYR A 209     -15.911 -11.583  -6.018  1.00 42.08           O  
ANISOU 1605  O   TYR A 209     4133   7286   4570  -1289    -41  -1406       O  
ATOM   1606  CB  TYR A 209     -17.492 -11.692  -3.193  1.00 37.15           C  
ANISOU 1606  CB  TYR A 209     3125   6839   4152  -1221    -61  -1342       C  
ATOM   1607  CG  TYR A 209     -18.733 -12.429  -2.756  1.00 42.11           C  
ANISOU 1607  CG  TYR A 209     3571   7659   4771  -1368    -55  -1428       C  
ATOM   1608  CD1 TYR A 209     -19.667 -12.854  -3.682  1.00 40.12           C  
ANISOU 1608  CD1 TYR A 209     3264   7598   4381  -1475   -108  -1521       C  
ATOM   1609  CD2 TYR A 209     -18.981 -12.676  -1.401  1.00 41.72           C  
ANISOU 1609  CD2 TYR A 209     3486   7529   4836  -1352     25  -1372       C  
ATOM   1610  CE1 TYR A 209     -20.809 -13.519  -3.299  1.00 43.07           C  
ANISOU 1610  CE1 TYR A 209     3533   8088   4743  -1572    -76  -1567       C  
ATOM   1611  CE2 TYR A 209     -20.115 -13.342  -0.996  1.00 42.86           C  
ANISOU 1611  CE2 TYR A 209     3548   7781   4957  -1453     59  -1418       C  
ATOM   1612  CZ  TYR A 209     -21.028 -13.761  -1.948  1.00 40.42           C  
ANISOU 1612  CZ  TYR A 209     3167   7669   4521  -1565     12  -1519       C  
ATOM   1613  OH  TYR A 209     -22.171 -14.419  -1.584  1.00 43.11           O  
ANISOU 1613  OH  TYR A 209     3411   8133   4835  -1682     49  -1578       O  
ATOM   1614  N   ALA A 210     -14.590 -11.015  -4.279  1.00 34.76           N  
ANISOU 1614  N   ALA A 210     3276   6016   3914  -1081     72  -1220       N  
ATOM   1615  CA  ALA A 210     -13.639 -10.290  -5.123  1.00 32.09           C  
ANISOU 1615  CA  ALA A 210     3110   5568   3515   -994     79  -1173       C  
ATOM   1616  C   ALA A 210     -13.032 -11.210  -6.174  1.00 36.09           C  
ANISOU 1616  C   ALA A 210     3737   5971   4003  -1179    197  -1289       C  
ATOM   1617  O   ALA A 210     -12.892 -10.841  -7.348  1.00 42.75           O  
ANISOU 1617  O   ALA A 210     4690   6866   4688  -1192    169  -1317       O  
ATOM   1618  CB  ALA A 210     -12.526  -9.671  -4.274  1.00 29.42           C  
ANISOU 1618  CB  ALA A 210     2850   5008   3321   -856    139  -1050       C  
ATOM   1619  N   ALA A 211     -12.638 -12.415  -5.751  1.00 36.13           N  
ANISOU 1619  N   ALA A 211     3746   5814   4168  -1319    339  -1355       N  
ATOM   1620  CA  ALA A 211     -12.072 -13.387  -6.683  1.00 36.77           C  
ANISOU 1620  CA  ALA A 211     3947   5773   4250  -1491    477  -1482       C  
ATOM   1621  C   ALA A 211     -13.035 -13.666  -7.819  1.00 42.11           C  
ANISOU 1621  C   ALA A 211     4617   6674   4710  -1645    405  -1610       C  
ATOM   1622  O   ALA A 211     -12.651 -13.643  -9.000  1.00 42.75           O  
ANISOU 1622  O   ALA A 211     4832   6748   4665  -1709    441  -1678       O  
ATOM   1623  CB  ALA A 211     -11.718 -14.680  -5.949  1.00 36.63           C  
ANISOU 1623  CB  ALA A 211     3933   5551   4435  -1602    625  -1530       C  
ATOM   1624  N   VAL A 212     -14.299 -13.930  -7.480  1.00 37.13           N  
ANISOU 1624  N   VAL A 212     3826   6260   4024  -1718    304  -1651       N  
ATOM   1625  CA  VAL A 212     -15.294 -14.203  -8.515  1.00 43.43           C  
ANISOU 1625  CA  VAL A 212     4582   7312   4608  -1877    210  -1779       C  
ATOM   1626  C   VAL A 212     -15.467 -12.993  -9.428  1.00 47.35           C  
ANISOU 1626  C   VAL A 212     5118   7984   4889  -1733     47  -1717       C  
ATOM   1627  O   VAL A 212     -15.510 -13.127 -10.661  1.00 48.85           O  
ANISOU 1627  O   VAL A 212     5413   8253   4894  -1847     26  -1805       O  
ATOM   1628  CB  VAL A 212     -16.635 -14.637  -7.894  1.00 45.26           C  
ANISOU 1628  CB  VAL A 212     4593   7772   4831  -1980    129  -1834       C  
ATOM   1629  CG1 VAL A 212     -17.690 -14.757  -9.002  1.00 49.85           C  
ANISOU 1629  CG1 VAL A 212     5124   8625   5191  -2077     13  -1913       C  
ATOM   1630  CG2 VAL A 212     -16.490 -15.976  -7.185  1.00 38.46           C  
ANISOU 1630  CG2 VAL A 212     3768   6699   4146  -2139    314  -1884       C  
ATOM   1631  N   ILE A 213     -15.570 -11.795  -8.841  1.00 44.00           N  
ANISOU 1631  N   ILE A 213     4633   7612   4474  -1483    -67  -1562       N  
ATOM   1632  CA  ILE A 213     -15.700 -10.576  -9.643  1.00 44.91           C  
ANISOU 1632  CA  ILE A 213     4822   7856   4388  -1319   -221  -1479       C  
ATOM   1633  C   ILE A 213     -14.555 -10.488 -10.641  1.00 45.80           C  
ANISOU 1633  C   ILE A 213     5187   7783   4432  -1367   -111  -1489       C  
ATOM   1634  O   ILE A 213     -14.745 -10.071 -11.795  1.00 49.73           O  
ANISOU 1634  O   ILE A 213     5795   8404   4697  -1379   -203  -1501       O  
ATOM   1635  CB  ILE A 213     -15.763  -9.330  -8.739  1.00 46.53           C  
ANISOU 1635  CB  ILE A 213     4973   8057   4650  -1037   -312  -1310       C  
ATOM   1636  CG1 ILE A 213     -17.084  -9.284  -7.965  1.00 46.29           C  
ANISOU 1636  CG1 ILE A 213     4679   8275   4633   -977   -438  -1315       C  
ATOM   1637  CG2 ILE A 213     -15.629  -8.055  -9.554  1.00 44.80           C  
ANISOU 1637  CG2 ILE A 213     4904   7877   4240   -859   -433  -1205       C  
ATOM   1638  CD1 ILE A 213     -17.104  -8.243  -6.844  1.00 45.20           C  
ANISOU 1638  CD1 ILE A 213     4488   8094   4593   -721   -477  -1172       C  
ATOM   1639  N   ASN A 214     -13.364 -10.952 -10.239  1.00 39.26           N  
ANISOU 1639  N   ASN A 214     4451   6668   3799  -1407     92  -1494       N  
ATOM   1640  CA  ASN A 214     -12.179 -10.869 -11.085  1.00 49.83           C  
ANISOU 1640  CA  ASN A 214     6004   7824   5105  -1449    231  -1512       C  
ATOM   1641  C   ASN A 214     -11.906 -12.139 -11.899  1.00 50.63           C  
ANISOU 1641  C   ASN A 214     6191   7857   5189  -1696    386  -1695       C  
ATOM   1642  O   ASN A 214     -10.885 -12.201 -12.589  1.00 53.19           O  
ANISOU 1642  O   ASN A 214     6683   8023   5504  -1745    538  -1734       O  
ATOM   1643  CB  ASN A 214     -10.961 -10.499 -10.238  1.00 43.68           C  
ANISOU 1643  CB  ASN A 214     5261   6790   4546  -1326    357  -1411       C  
ATOM   1644  CG  ASN A 214     -11.007  -9.051  -9.782  1.00 53.52           C  
ANISOU 1644  CG  ASN A 214     6514   8069   5750  -1102    229  -1242       C  
ATOM   1645  OD1 ASN A 214     -10.737  -8.142 -10.565  1.00 53.62           O  
ANISOU 1645  OD1 ASN A 214     6683   8092   5599  -1044    192  -1185       O  
ATOM   1646  ND2 ASN A 214     -11.375  -8.827  -8.519  1.00 49.92           N  
ANISOU 1646  ND2 ASN A 214     5914   7624   5431   -983    167  -1162       N  
ATOM   1647  N   GLY A 215     -12.772 -13.146 -11.826  1.00 43.58           N  
ANISOU 1647  N   GLY A 215     5192   7072   4293  -1860    369  -1815       N  
ATOM   1648  CA  GLY A 215     -12.701 -14.317 -12.690  1.00 51.44           C  
ANISOU 1648  CA  GLY A 215     6288   8025   5230  -2113    499  -2006       C  
ATOM   1649  C   GLY A 215     -11.995 -15.543 -12.136  1.00 57.59           C  
ANISOU 1649  C   GLY A 215     7094   8529   6258  -2214    726  -2091       C  
ATOM   1650  O   GLY A 215     -11.716 -16.467 -12.908  1.00 53.10           O  
ANISOU 1650  O   GLY A 215     6655   7867   5655  -2404    874  -2253       O  
ATOM   1651  N   ASP A 216     -11.648 -15.557 -10.846  1.00 49.05           N  
ANISOU 1651  N   ASP A 216     5916   7302   5418  -2083    761  -1985       N  
ATOM   1652  CA  ASP A 216     -11.172 -16.756 -10.159  1.00 48.14           C  
ANISOU 1652  CA  ASP A 216     5813   6940   5537  -2159    938  -2043       C  
ATOM   1653  C   ASP A 216     -12.393 -17.512  -9.655  1.00 54.74           C  
ANISOU 1653  C   ASP A 216     6534   7902   6361  -2313    876  -2107       C  
ATOM   1654  O   ASP A 216     -13.045 -17.076  -8.702  1.00 50.65           O  
ANISOU 1654  O   ASP A 216     5859   7505   5879  -2222    752  -2003       O  
ATOM   1655  CB  ASP A 216     -10.271 -16.394  -8.979  1.00 59.41           C  
ANISOU 1655  CB  ASP A 216     7194   8174   7205  -1951    979  -1887       C  
ATOM   1656  CG  ASP A 216      -8.801 -16.509  -9.296  1.00 65.51           C  
ANISOU 1656  CG  ASP A 216     8082   8699   8108  -1890   1160  -1898       C  
ATOM   1657  OD1 ASP A 216      -8.430 -17.371 -10.122  1.00 76.98           O  
ANISOU 1657  OD1 ASP A 216     9656  10039   9553  -2028   1321  -2050       O  
ATOM   1658  OD2 ASP A 216      -8.019 -15.733  -8.702  1.00 53.39           O  
ANISOU 1658  OD2 ASP A 216     6511   7089   6686  -1710   1148  -1764       O  
ATOM   1659  N   ARG A 217     -12.705 -18.645 -10.276  1.00 56.28           N  
ANISOU 1659  N   ARG A 217     6813   8064   6506  -2500    978  -2233       N  
ATOM   1660  CA  ARG A 217     -13.923 -19.360  -9.922  1.00 54.62           C  
ANISOU 1660  CA  ARG A 217     6508   7987   6258  -2610    931  -2247       C  
ATOM   1661  C   ARG A 217     -13.730 -20.833  -9.638  1.00 43.35           C  
ANISOU 1661  C   ARG A 217     5195   6315   4960  -2716   1124  -2302       C  
ATOM   1662  O   ARG A 217     -14.721 -21.517  -9.365  1.00 46.57           O  
ANISOU 1662  O   ARG A 217     5555   6814   5327  -2832   1109  -2327       O  
ATOM   1663  CB  ARG A 217     -14.965 -19.248 -11.030  1.00 56.60           C  
ANISOU 1663  CB  ARG A 217     6722   8531   6251  -2731    809  -2317       C  
ATOM   1664  CG  ARG A 217     -15.191 -17.891 -11.584  1.00 51.41           C  
ANISOU 1664  CG  ARG A 217     6000   8117   5417  -2622    610  -2266       C  
ATOM   1665  CD  ARG A 217     -16.148 -18.081 -12.769  1.00 59.73           C  
ANISOU 1665  CD  ARG A 217     7048   9414   6235  -2757    514  -2337       C  
ATOM   1666  NE  ARG A 217     -17.387 -18.719 -12.341  1.00 54.68           N  
ANISOU 1666  NE  ARG A 217     6251   8932   5592  -2858    468  -2359       N  
ATOM   1667  CZ  ARG A 217     -18.486 -18.057 -11.998  1.00 55.12           C  
ANISOU 1667  CZ  ARG A 217     6092   9272   5579  -2773    274  -2296       C  
ATOM   1668  NH1 ARG A 217     -18.489 -16.730 -12.003  1.00 60.14           N  
ANISOU 1668  NH1 ARG A 217     6653  10053   6145  -2568     98  -2195       N  
ATOM   1669  NH2 ARG A 217     -19.577 -18.715 -11.638  1.00 50.19           N  
ANISOU 1669  NH2 ARG A 217     5334   8780   4955  -2883    266  -2332       N  
ATOM   1670  N   TRP A 218     -12.497 -21.340  -9.691  1.00 50.77           N  
ANISOU 1670  N   TRP A 218     6286   6951   6055  -2669   1306  -2321       N  
ATOM   1671  CA  TRP A 218     -12.263 -22.767  -9.547  1.00 52.77           C  
ANISOU 1671  CA  TRP A 218     6674   6960   6417  -2750   1490  -2376       C  
ATOM   1672  C   TRP A 218     -12.780 -23.311  -8.224  1.00 50.06           C  
ANISOU 1672  C   TRP A 218     6279   6553   6188  -2742   1474  -2297       C  
ATOM   1673  O   TRP A 218     -13.044 -24.512  -8.128  1.00 48.17           O  
ANISOU 1673  O   TRP A 218     6144   6188   5970  -2859   1585  -2350       O  
ATOM   1674  CB  TRP A 218     -10.767 -23.068  -9.689  1.00 52.27           C  
ANISOU 1674  CB  TRP A 218     6743   6586   6532  -2637   1673  -2385       C  
ATOM   1675  CG  TRP A 218      -9.912 -22.458  -8.597  1.00 48.97           C  
ANISOU 1675  CG  TRP A 218     6256   6025   6326  -2427   1651  -2253       C  
ATOM   1676  CD1 TRP A 218      -9.218 -21.291  -8.662  1.00 52.33           C  
ANISOU 1676  CD1 TRP A 218     6620   6484   6778  -2298   1598  -2202       C  
ATOM   1677  CD2 TRP A 218      -9.646 -23.014  -7.302  1.00 51.23           C  
ANISOU 1677  CD2 TRP A 218     6538   6107   6819  -2333   1683  -2151       C  
ATOM   1678  NE1 TRP A 218      -8.550 -21.066  -7.476  1.00 52.37           N  
ANISOU 1678  NE1 TRP A 218     6563   6333   7003  -2133   1591  -2075       N  
ATOM   1679  CE2 TRP A 218      -8.798 -22.111  -6.626  1.00 53.83           C  
ANISOU 1679  CE2 TRP A 218     6783   6372   7297  -2146   1636  -2037       C  
ATOM   1680  CE3 TRP A 218     -10.057 -24.175  -6.640  1.00 50.30           C  
ANISOU 1680  CE3 TRP A 218     6492   5857   6763  -2399   1742  -2140       C  
ATOM   1681  CZ2 TRP A 218      -8.344 -22.344  -5.326  1.00 49.40           C  
ANISOU 1681  CZ2 TRP A 218     6200   5628   6943  -2018   1637  -1907       C  
ATOM   1682  CZ3 TRP A 218      -9.602 -24.405  -5.351  1.00 55.64           C  
ANISOU 1682  CZ3 TRP A 218     7166   6338   7636  -2270   1745  -2010       C  
ATOM   1683  CH2 TRP A 218      -8.759 -23.489  -4.708  1.00 48.92           C  
ANISOU 1683  CH2 TRP A 218     6222   5438   6928  -2080   1687  -1892       C  
ATOM   1684  N   PHE A 219     -12.903 -22.463  -7.195  1.00 49.78           N  
ANISOU 1684  N   PHE A 219     6103   6591   6221  -2610   1347  -2169       N  
ATOM   1685  CA  PHE A 219     -13.316 -22.896  -5.866  1.00 47.00           C  
ANISOU 1685  CA  PHE A 219     5715   6172   5973  -2592   1335  -2076       C  
ATOM   1686  C   PHE A 219     -14.823 -22.936  -5.661  1.00 49.18           C  
ANISOU 1686  C   PHE A 219     5867   6722   6096  -2720   1231  -2095       C  
ATOM   1687  O   PHE A 219     -15.270 -23.324  -4.578  1.00 45.91           O  
ANISOU 1687  O   PHE A 219     5431   6269   5744  -2731   1233  -2028       O  
ATOM   1688  CB  PHE A 219     -12.716 -21.962  -4.820  1.00 43.94           C  
ANISOU 1688  CB  PHE A 219     5235   5735   5727  -2392   1260  -1924       C  
ATOM   1689  CG  PHE A 219     -13.027 -20.520  -5.077  1.00 44.16           C  
ANISOU 1689  CG  PHE A 219     5101   6034   5644  -2316   1095  -1891       C  
ATOM   1690  CD1 PHE A 219     -14.205 -19.956  -4.617  1.00 43.58           C  
ANISOU 1690  CD1 PHE A 219     4862   6233   5464  -2320    949  -1849       C  
ATOM   1691  CD2 PHE A 219     -12.154 -19.729  -5.805  1.00 42.28           C  
ANISOU 1691  CD2 PHE A 219     4882   5779   5403  -2236   1093  -1906       C  
ATOM   1692  CE1 PHE A 219     -14.500 -18.629  -4.863  1.00 40.67           C  
ANISOU 1692  CE1 PHE A 219     4350   6111   4993  -2224    792  -1815       C  
ATOM   1693  CE2 PHE A 219     -12.435 -18.394  -6.047  1.00 40.44           C  
ANISOU 1693  CE2 PHE A 219     4525   5785   5055  -2167    937  -1873       C  
ATOM   1694  CZ  PHE A 219     -13.613 -17.848  -5.588  1.00 44.31           C  
ANISOU 1694  CZ  PHE A 219     4851   6544   5442  -2152    779  -1826       C  
ATOM   1695  N   LEU A 220     -15.629 -22.514  -6.627  1.00 45.66           N  
ANISOU 1695  N   LEU A 220     5332   6561   5454  -2810   1135  -2176       N  
ATOM   1696  CA  LEU A 220     -17.067 -22.606  -6.412  1.00 52.75           C  
ANISOU 1696  CA  LEU A 220     6091   7725   6228  -2920   1044  -2197       C  
ATOM   1697  C   LEU A 220     -17.543 -24.057  -6.519  1.00 52.14           C  
ANISOU 1697  C   LEU A 220     6136   7550   6126  -3137   1182  -2295       C  
ATOM   1698  O   LEU A 220     -16.857 -24.930  -7.062  1.00 50.05           O  
ANISOU 1698  O   LEU A 220     6063   7056   5899  -3209   1331  -2367       O  
ATOM   1699  CB  LEU A 220     -17.819 -21.728  -7.408  1.00 54.86           C  
ANISOU 1699  CB  LEU A 220     6210   8337   6295  -2935    883  -2242       C  
ATOM   1700  CG  LEU A 220     -17.532 -20.235  -7.300  1.00 48.36           C  
ANISOU 1700  CG  LEU A 220     5264   7644   5467  -2725    729  -2144       C  
ATOM   1701  CD1 LEU A 220     -18.200 -19.468  -8.416  1.00 52.15           C  
ANISOU 1701  CD1 LEU A 220     5641   8437   5737  -2731    567  -2185       C  
ATOM   1702  CD2 LEU A 220     -18.003 -19.696  -5.934  1.00 40.16           C  
ANISOU 1702  CD2 LEU A 220     4070   6675   4513  -2594    655  -2025       C  
ATOM   1703  N   ASN A 221     -18.733 -24.315  -5.975  1.00 52.89           N  
ANISOU 1703  N   ASN A 221     6119   7818   6157  -3239   1140  -2302       N  
ATOM   1704  CA  ASN A 221     -19.353 -25.633  -6.058  1.00 55.78           C  
ANISOU 1704  CA  ASN A 221     6587   8131   6474  -3471   1261  -2403       C  
ATOM   1705  C   ASN A 221     -20.856 -25.473  -6.205  1.00 51.22           C  
ANISOU 1705  C   ASN A 221     5810   7917   5735  -3601   1157  -2461       C  
ATOM   1706  O   ASN A 221     -21.403 -24.374  -6.082  1.00 53.75           O  
ANISOU 1706  O   ASN A 221     5913   8504   6005  -3482    995  -2408       O  
ATOM   1707  CB  ASN A 221     -19.025 -26.519  -4.837  1.00 57.21           C  
ANISOU 1707  CB  ASN A 221     6910   8018   6808  -3479   1390  -2338       C  
ATOM   1708  CG  ASN A 221     -19.408 -25.877  -3.490  1.00 65.78           C  
ANISOU 1708  CG  ASN A 221     7853   9182   7957  -3362   1303  -2208       C  
ATOM   1709  OD1 ASN A 221     -20.415 -25.171  -3.365  1.00 60.09           O  
ANISOU 1709  OD1 ASN A 221     6920   8771   7139  -3360   1181  -2206       O  
ATOM   1710  ND2 ASN A 221     -18.592 -26.138  -2.474  1.00 66.81           N  
ANISOU 1710  ND2 ASN A 221     8104   9028   8252  -3260   1370  -2096       N  
ATOM   1711  N   ARG A 222     -21.524 -26.598  -6.473  1.00 55.32           N  
ANISOU 1711  N   ARG A 222     6402   8441   6176  -3845   1257  -2575       N  
ATOM   1712  CA  ARG A 222     -22.974 -26.649  -6.571  1.00 57.13           C  
ANISOU 1712  CA  ARG A 222     6446   9000   6261  -4002   1186  -2648       C  
ATOM   1713  C   ARG A 222     -23.659 -26.816  -5.218  1.00 60.14           C  
ANISOU 1713  C   ARG A 222     6748   9405   6698  -4019   1206  -2594       C  
ATOM   1714  O   ARG A 222     -24.889 -26.941  -5.181  1.00 71.25           O  
ANISOU 1714  O   ARG A 222     7997  11077   7999  -4160   1170  -2663       O  
ATOM   1715  CB  ARG A 222     -23.398 -27.801  -7.495  1.00 59.85           C  
ANISOU 1715  CB  ARG A 222     6908   9348   6484  -4285   1293  -2806       C  
ATOM   1716  CG  ARG A 222     -23.283 -29.164  -6.821  1.00 65.60           C  
ANISOU 1716  CG  ARG A 222     7856   9786   7285  -4446   1493  -2839       C  
ATOM   1717  CD  ARG A 222     -23.377 -30.329  -7.809  1.00 76.50           C  
ANISOU 1717  CD  ARG A 222     9416  11086   8564  -4704   1629  -2993       C  
ATOM   1718  NE  ARG A 222     -22.349 -31.333  -7.537  1.00 88.15           N  
ANISOU 1718  NE  ARG A 222    11194  12132  10168  -4707   1823  -2984       N  
ATOM   1719  CZ  ARG A 222     -22.497 -32.364  -6.706  1.00 93.25           C  
ANISOU 1719  CZ  ARG A 222    11992  12569  10869  -4826   1963  -2985       C  
ATOM   1720  NH1 ARG A 222     -23.644 -32.547  -6.061  1.00 89.29           N  
ANISOU 1720  NH1 ARG A 222    11373  12255  10298  -4975   1944  -3006       N  
ATOM   1721  NH2 ARG A 222     -21.494 -33.219  -6.527  1.00 95.10           N  
ANISOU 1721  NH2 ARG A 222    12501  12404  11227  -4792   2126  -2965       N  
ATOM   1722  N   PHE A 223     -22.907 -26.839  -4.119  1.00 56.30           N  
ANISOU 1722  N   PHE A 223     6367   8655   6371  -3888   1265  -2477       N  
ATOM   1723  CA  PHE A 223     -23.455 -27.116  -2.796  1.00 59.54           C  
ANISOU 1723  CA  PHE A 223     6750   9044   6829  -3925   1308  -2423       C  
ATOM   1724  C   PHE A 223     -23.919 -25.844  -2.105  1.00 64.99           C  
ANISOU 1724  C   PHE A 223     7195   9970   7530  -3737   1161  -2328       C  
ATOM   1725  O   PHE A 223     -23.611 -24.719  -2.515  1.00 64.46           O  
ANISOU 1725  O   PHE A 223     7008  10023   7461  -3543   1029  -2277       O  
ATOM   1726  CB  PHE A 223     -22.419 -27.794  -1.896  1.00 63.91           C  
ANISOU 1726  CB  PHE A 223     7549   9191   7544  -3877   1438  -2328       C  
ATOM   1727  CG  PHE A 223     -21.871 -29.077  -2.449  1.00 78.27           C  
ANISOU 1727  CG  PHE A 223     9633  10728   9377  -4026   1599  -2407       C  
ATOM   1728  CD1 PHE A 223     -22.708 -30.012  -3.034  1.00 82.97           C  
ANISOU 1728  CD1 PHE A 223    10274  11408   9843  -4295   1682  -2555       C  
ATOM   1729  CD2 PHE A 223     -20.511 -29.349  -2.375  1.00 82.87           C  
ANISOU 1729  CD2 PHE A 223    10419  10958  10108  -3891   1674  -2337       C  
ATOM   1730  CE1 PHE A 223     -22.202 -31.196  -3.539  1.00 84.35           C  
ANISOU 1730  CE1 PHE A 223    10708  11311  10030  -4428   1842  -2630       C  
ATOM   1731  CE2 PHE A 223     -19.999 -30.531  -2.884  1.00 85.08           C  
ANISOU 1731  CE2 PHE A 223    10947  10969  10412  -4005   1833  -2411       C  
ATOM   1732  CZ  PHE A 223     -20.845 -31.454  -3.465  1.00 84.68           C  
ANISOU 1732  CZ  PHE A 223    10955  10995  10225  -4273   1919  -2558       C  
ATOM   1733  N   THR A 224     -24.637 -26.037  -1.003  1.00 60.72           N  
ANISOU 1733  N   THR A 224     6596   9477   6997  -3797   1198  -2303       N  
ATOM   1734  CA  THR A 224     -24.953 -24.953  -0.090  1.00 69.61           C  
ANISOU 1734  CA  THR A 224     7535  10754   8159  -3614   1100  -2203       C  
ATOM   1735  C   THR A 224     -24.855 -25.486   1.335  1.00 67.28           C  
ANISOU 1735  C   THR A 224     7360  10255   7949  -3656   1211  -2124       C  
ATOM   1736  O   THR A 224     -24.512 -26.649   1.564  1.00 68.29           O  
ANISOU 1736  O   THR A 224     7715  10122   8109  -3808   1350  -2139       O  
ATOM   1737  CB  THR A 224     -26.339 -24.361  -0.372  1.00 73.17           C  
ANISOU 1737  CB  THR A 224     7697  11619   8483  -3641    996  -2280       C  
ATOM   1738  OG1 THR A 224     -26.497 -23.146   0.373  1.00 73.92           O  
ANISOU 1738  OG1 THR A 224     7619  11847   8621  -3411    894  -2179       O  
ATOM   1739  CG2 THR A 224     -27.428 -25.342   0.016  1.00 75.52           C  
ANISOU 1739  CG2 THR A 224     7977  12008   8709  -3909   1103  -2386       C  
ATOM   1740  N   THR A 225     -25.163 -24.625   2.298  1.00 70.43           N  
ANISOU 1740  N   THR A 225     7615  10769   8375  -3518   1152  -2039       N  
ATOM   1741  CA  THR A 225     -25.082 -24.989   3.705  1.00 61.50           C  
ANISOU 1741  CA  THR A 225     6589   9470   7310  -3549   1247  -1952       C  
ATOM   1742  C   THR A 225     -25.972 -24.045   4.491  1.00 62.90           C  
ANISOU 1742  C   THR A 225     6533   9913   7453  -3461   1184  -1929       C  
ATOM   1743  O   THR A 225     -26.370 -22.987   3.998  1.00 61.01           O  
ANISOU 1743  O   THR A 225     6074   9932   7175  -3311   1055  -1946       O  
ATOM   1744  CB  THR A 225     -23.642 -24.920   4.227  1.00 64.27           C  
ANISOU 1744  CB  THR A 225     7134   9483   7803  -3393   1264  -1803       C  
ATOM   1745  OG1 THR A 225     -23.597 -25.400   5.577  1.00 71.51           O  
ANISOU 1745  OG1 THR A 225     8176  10232   8764  -3452   1359  -1717       O  
ATOM   1746  CG2 THR A 225     -23.124 -23.482   4.197  1.00 59.89           C  
ANISOU 1746  CG2 THR A 225     6438   9020   7296  -3118   1124  -1711       C  
ATOM   1747  N   THR A 226     -26.275 -24.435   5.726  1.00 60.63           N  
ANISOU 1747  N   THR A 226     6305   9555   7177  -3552   1282  -1891       N  
ATOM   1748  CA  THR A 226     -26.936 -23.515   6.634  1.00 60.20           C  
ANISOU 1748  CA  THR A 226     6061   9703   7108  -3449   1244  -1855       C  
ATOM   1749  C   THR A 226     -25.898 -22.725   7.416  1.00 55.06           C  
ANISOU 1749  C   THR A 226     5480   8880   6561  -3223   1205  -1690       C  
ATOM   1750  O   THR A 226     -24.735 -23.123   7.537  1.00 58.15           O  
ANISOU 1750  O   THR A 226     6087   8969   7038  -3192   1236  -1597       O  
ATOM   1751  CB  THR A 226     -27.839 -24.260   7.608  1.00 64.24           C  
ANISOU 1751  CB  THR A 226     6594  10251   7565  -3674   1378  -1905       C  
ATOM   1752  OG1 THR A 226     -27.036 -25.174   8.366  1.00 65.33           O  
ANISOU 1752  OG1 THR A 226     7027  10037   7758  -3767   1496  -1814       O  
ATOM   1753  CG2 THR A 226     -28.917 -25.029   6.848  1.00 62.58           C  
ANISOU 1753  CG2 THR A 226     6299  10235   7245  -3918   1421  -2080       C  
ATOM   1754  N   LEU A 227     -26.337 -21.593   7.963  1.00 53.60           N  
ANISOU 1754  N   LEU A 227     5106   8894   6367  -3063   1141  -1658       N  
ATOM   1755  CA  LEU A 227     -25.438 -20.793   8.782  1.00 57.25           C  
ANISOU 1755  CA  LEU A 227     5625   9218   6909  -2865   1111  -1511       C  
ATOM   1756  C   LEU A 227     -24.862 -21.620   9.927  1.00 57.50           C  
ANISOU 1756  C   LEU A 227     5897   8967   6983  -2982   1235  -1417       C  
ATOM   1757  O   LEU A 227     -23.669 -21.514  10.235  1.00 51.05           O  
ANISOU 1757  O   LEU A 227     5233   7912   6252  -2877   1222  -1290       O  
ATOM   1758  CB  LEU A 227     -26.173 -19.556   9.295  1.00 59.13           C  
ANISOU 1758  CB  LEU A 227     5635   9718   7115  -2706   1053  -1512       C  
ATOM   1759  CG  LEU A 227     -25.381 -18.427   9.945  1.00 57.91           C  
ANISOU 1759  CG  LEU A 227     5487   9495   7021  -2469    999  -1383       C  
ATOM   1760  CD1 LEU A 227     -24.173 -18.008   9.106  1.00 49.38           C  
ANISOU 1760  CD1 LEU A 227     4481   8272   6009  -2309    901  -1314       C  
ATOM   1761  CD2 LEU A 227     -26.304 -17.251  10.144  1.00 62.97           C  
ANISOU 1761  CD2 LEU A 227     5883  10425   7617  -2311    942  -1422       C  
ATOM   1762  N   ASN A 228     -25.676 -22.500  10.523  1.00 64.39           N  
ANISOU 1762  N   ASN A 228     6816   9857   7791  -3209   1355  -1476       N  
ATOM   1763  CA  ASN A 228     -25.233 -23.238  11.705  1.00 62.12           C  
ANISOU 1763  CA  ASN A 228     6767   9314   7520  -3321   1472  -1376       C  
ATOM   1764  C   ASN A 228     -24.205 -24.314  11.361  1.00 64.42           C  
ANISOU 1764  C   ASN A 228     7333   9266   7879  -3387   1515  -1320       C  
ATOM   1765  O   ASN A 228     -23.199 -24.464  12.065  1.00 64.32           O  
ANISOU 1765  O   ASN A 228     7514   8989   7934  -3326   1532  -1174       O  
ATOM   1766  CB  ASN A 228     -26.437 -23.852  12.414  1.00 64.06           C  
ANISOU 1766  CB  ASN A 228     6991   9683   7665  -3554   1596  -1463       C  
ATOM   1767  CG  ASN A 228     -27.191 -22.840  13.239  1.00 70.00           C  
ANISOU 1767  CG  ASN A 228     7542  10681   8374  -3475   1590  -1473       C  
ATOM   1768  OD1 ASN A 228     -26.729 -21.713  13.429  1.00 70.85           O  
ANISOU 1768  OD1 ASN A 228     7563  10830   8526  -3245   1503  -1396       O  
ATOM   1769  ND2 ASN A 228     -28.359 -23.232  13.737  1.00 77.24           N  
ANISOU 1769  ND2 ASN A 228     8382  11761   9203  -3669   1693  -1576       N  
ATOM   1770  N   ASP A 229     -24.428 -25.069  10.283  1.00 62.81           N  
ANISOU 1770  N   ASP A 229     7151   9060   7656  -3508   1533  -1433       N  
ATOM   1771  CA  ASP A 229     -23.454 -26.086   9.883  1.00 64.29           C  
ANISOU 1771  CA  ASP A 229     7598   8915   7912  -3555   1583  -1394       C  
ATOM   1772  C   ASP A 229     -22.142 -25.443   9.443  1.00 56.16           C  
ANISOU 1772  C   ASP A 229     6593   7743   7002  -3316   1483  -1295       C  
ATOM   1773  O   ASP A 229     -21.040 -25.923   9.781  1.00 59.91           O  
ANISOU 1773  O   ASP A 229     7287   7903   7574  -3267   1513  -1179       O  
ATOM   1774  CB  ASP A 229     -24.037 -26.950   8.764  1.00 66.54           C  
ANISOU 1774  CB  ASP A 229     7889   9257   8134  -3740   1631  -1557       C  
ATOM   1775  CG  ASP A 229     -25.395 -27.532   9.122  1.00 76.04           C  
ANISOU 1775  CG  ASP A 229     9038  10639   9213  -3992   1728  -1674       C  
ATOM   1776  OD1 ASP A 229     -25.700 -27.651  10.331  1.00 71.21           O  
ANISOU 1776  OD1 ASP A 229     8483   9996   8576  -4060   1800  -1615       O  
ATOM   1777  OD2 ASP A 229     -26.161 -27.881   8.193  1.00 73.38           O  
ANISOU 1777  OD2 ASP A 229     8606  10478   8798  -4134   1737  -1829       O  
ATOM   1778  N   PHE A 230     -22.243 -24.340   8.696  1.00 53.87           N  
ANISOU 1778  N   PHE A 230     6081   7681   6706  -3161   1362  -1338       N  
ATOM   1779  CA  PHE A 230     -21.045 -23.584   8.364  1.00 52.03           C  
ANISOU 1779  CA  PHE A 230     5853   7340   6575  -2938   1271  -1247       C  
ATOM   1780  C   PHE A 230     -20.319 -23.146   9.623  1.00 49.85           C  
ANISOU 1780  C   PHE A 230     5654   6921   6366  -2826   1266  -1081       C  
ATOM   1781  O   PHE A 230     -19.094 -23.251   9.705  1.00 49.72           O  
ANISOU 1781  O   PHE A 230     5780   6653   6458  -2730   1256   -977       O  
ATOM   1782  CB  PHE A 230     -21.373 -22.362   7.508  1.00 54.94           C  
ANISOU 1782  CB  PHE A 230     5978   7993   6904  -2788   1141  -1307       C  
ATOM   1783  CG  PHE A 230     -20.193 -21.479   7.286  1.00 52.01           C  
ANISOU 1783  CG  PHE A 230     5607   7528   6625  -2568   1054  -1213       C  
ATOM   1784  CD1 PHE A 230     -19.234 -21.819   6.345  1.00 52.97           C  
ANISOU 1784  CD1 PHE A 230     5836   7473   6816  -2538   1053  -1226       C  
ATOM   1785  CD2 PHE A 230     -20.015 -20.334   8.040  1.00 47.96           C  
ANISOU 1785  CD2 PHE A 230     4998   7095   6129  -2400    989  -1119       C  
ATOM   1786  CE1 PHE A 230     -18.130 -21.030   6.157  1.00 50.84           C  
ANISOU 1786  CE1 PHE A 230     5565   7118   6634  -2352    986  -1149       C  
ATOM   1787  CE2 PHE A 230     -18.906 -19.534   7.865  1.00 49.14           C  
ANISOU 1787  CE2 PHE A 230     5155   7157   6360  -2214    917  -1037       C  
ATOM   1788  CZ  PHE A 230     -17.957 -19.881   6.907  1.00 49.87           C  
ANISOU 1788  CZ  PHE A 230     5343   7081   6526  -2193    914  -1053       C  
ATOM   1789  N   ASN A 231     -21.056 -22.649  10.615  1.00 54.31           N  
ANISOU 1789  N   ASN A 231     6125   7647   6863  -2839   1277  -1059       N  
ATOM   1790  CA  ASN A 231     -20.392 -22.154  11.817  1.00 53.45           C  
ANISOU 1790  CA  ASN A 231     6090   7425   6793  -2742   1271   -905       C  
ATOM   1791  C   ASN A 231     -19.749 -23.289  12.609  1.00 49.44           C  
ANISOU 1791  C   ASN A 231     5871   6589   6326  -2851   1363   -795       C  
ATOM   1792  O   ASN A 231     -18.717 -23.082  13.252  1.00 63.36           O  
ANISOU 1792  O   ASN A 231     7756   8161   8159  -2748   1335   -648       O  
ATOM   1793  CB  ASN A 231     -21.383 -21.363  12.675  1.00 56.39           C  
ANISOU 1793  CB  ASN A 231     6302   8053   7071  -2738   1279   -924       C  
ATOM   1794  CG  ASN A 231     -21.457 -19.897  12.273  1.00 56.48           C  
ANISOU 1794  CG  ASN A 231     6084   8295   7082  -2522   1162   -945       C  
ATOM   1795  OD1 ASN A 231     -20.458 -19.306  11.864  1.00 61.93           O  
ANISOU 1795  OD1 ASN A 231     6783   8901   7848  -2360   1080   -881       O  
ATOM   1796  ND2 ASN A 231     -22.645 -19.309  12.377  1.00 54.49           N  
ANISOU 1796  ND2 ASN A 231     5629   8329   6746  -2515   1157  -1035       N  
ATOM   1797  N   LEU A 232     -20.322 -24.491  12.553  1.00 47.65           N  
ANISOU 1797  N   LEU A 232     5766   6286   6052  -3054   1466   -861       N  
ATOM   1798  CA  LEU A 232     -19.662 -25.655  13.143  1.00 54.21           C  
ANISOU 1798  CA  LEU A 232     6902   6772   6925  -3137   1547   -754       C  
ATOM   1799  C   LEU A 232     -18.292 -25.877  12.510  1.00 59.65           C  
ANISOU 1799  C   LEU A 232     7712   7192   7759  -2995   1499   -684       C  
ATOM   1800  O   LEU A 232     -17.274 -26.025  13.214  1.00 65.75           O  
ANISOU 1800  O   LEU A 232     8663   7708   8610  -2904   1483   -522       O  
ATOM   1801  CB  LEU A 232     -20.548 -26.892  12.980  1.00 61.80           C  
ANISOU 1801  CB  LEU A 232     7967   7709   7806  -3382   1670   -863       C  
ATOM   1802  CG  LEU A 232     -21.439 -27.290  14.164  1.00 74.60           C  
ANISOU 1802  CG  LEU A 232     9661   9375   9308  -3564   1772   -851       C  
ATOM   1803  CD1 LEU A 232     -20.611 -27.427  15.436  1.00 77.49           C  
ANISOU 1803  CD1 LEU A 232    10262   9486   9696  -3508   1781   -647       C  
ATOM   1804  CD2 LEU A 232     -22.583 -26.311  14.385  1.00 76.26           C  
ANISOU 1804  CD2 LEU A 232     9587   9964   9422  -3579   1754   -949       C  
ATOM   1805  N   VAL A 233     -18.243 -25.853  11.169  1.00 57.56           N  
ANISOU 1805  N   VAL A 233     7350   6993   7529  -2966   1472   -807       N  
ATOM   1806  CA  VAL A 233     -16.955 -25.979  10.476  1.00 58.30           C  
ANISOU 1806  CA  VAL A 233     7534   6855   7763  -2824   1439   -766       C  
ATOM   1807  C   VAL A 233     -16.015 -24.831  10.845  1.00 60.09           C  
ANISOU 1807  C   VAL A 233     7681   7077   8072  -2611   1333   -645       C  
ATOM   1808  O   VAL A 233     -14.817 -25.040  11.078  1.00 62.54           O  
ANISOU 1808  O   VAL A 233     8138   7115   8507  -2498   1320   -528       O  
ATOM   1809  CB  VAL A 233     -17.160 -26.064   8.950  1.00 56.01           C  
ANISOU 1809  CB  VAL A 233     7146   6673   7463  -2846   1436   -934       C  
ATOM   1810  CG1 VAL A 233     -15.816 -26.235   8.241  1.00 63.75           C  
ANISOU 1810  CG1 VAL A 233     8228   7407   8589  -2705   1427   -907       C  
ATOM   1811  CG2 VAL A 233     -18.092 -27.189   8.608  1.00 55.96           C  
ANISOU 1811  CG2 VAL A 233     7221   6676   7363  -3075   1543  -1058       C  
ATOM   1812  N   ALA A 234     -16.539 -23.603  10.900  1.00 55.12           N  
ANISOU 1812  N   ALA A 234     6821   6745   7376  -2547   1258   -674       N  
ATOM   1813  CA  ALA A 234     -15.704 -22.434  11.173  1.00 54.97           C  
ANISOU 1813  CA  ALA A 234     6717   6747   7420  -2358   1162   -580       C  
ATOM   1814  C   ALA A 234     -15.072 -22.514  12.555  1.00 60.56           C  
ANISOU 1814  C   ALA A 234     7591   7262   8159  -2337   1168   -401       C  
ATOM   1815  O   ALA A 234     -13.866 -22.282  12.716  1.00 57.09           O  
ANISOU 1815  O   ALA A 234     7226   6632   7834  -2206   1120   -293       O  
ATOM   1816  CB  ALA A 234     -16.531 -21.154  11.043  1.00 59.09           C  
ANISOU 1816  CB  ALA A 234     6983   7623   7847  -2294   1091   -648       C  
ATOM   1817  N   MET A 235     -15.881 -22.810  13.574  1.00 61.92           N  
ANISOU 1817  N   MET A 235     7823   7485   8219  -2465   1225   -369       N  
ATOM   1818  CA  MET A 235     -15.325 -23.054  14.895  1.00 66.85           C  
ANISOU 1818  CA  MET A 235     8655   7906   8840  -2468   1233   -190       C  
ATOM   1819  C   MET A 235     -14.210 -24.087  14.820  1.00 67.46           C  
ANISOU 1819  C   MET A 235     8982   7605   9046  -2421   1239    -86       C  
ATOM   1820  O   MET A 235     -13.140 -23.890  15.410  1.00 67.18           O  
ANISOU 1820  O   MET A 235     9066   7377   9083  -2295   1174     73       O  
ATOM   1821  CB  MET A 235     -16.430 -23.492  15.860  1.00 77.42           C  
ANISOU 1821  CB  MET A 235    10057   9330  10028  -2645   1323   -195       C  
ATOM   1822  CG  MET A 235     -16.044 -23.440  17.336  1.00 89.91           C  
ANISOU 1822  CG  MET A 235    11829  10785  11549  -2646   1317    -12       C  
ATOM   1823  SD  MET A 235     -15.061 -24.841  17.910  1.00104.59           S  
ANISOU 1823  SD  MET A 235    14072  12198  13471  -2648   1327    173       S  
ATOM   1824  CE  MET A 235     -15.740 -26.197  16.949  1.00 98.97           C  
ANISOU 1824  CE  MET A 235    13410  11415  12780  -2804   1445     19       C  
ATOM   1825  N   LYS A 236     -14.418 -25.176  14.060  1.00 66.21           N  
ANISOU 1825  N   LYS A 236     8907   7333   8919  -2505   1313   -176       N  
ATOM   1826  CA  LYS A 236     -13.359 -26.184  13.970  1.00 62.45           C  
ANISOU 1826  CA  LYS A 236     8671   6484   8574  -2430   1327    -84       C  
ATOM   1827  C   LYS A 236     -12.048 -25.619  13.408  1.00 57.74           C  
ANISOU 1827  C   LYS A 236     8021   5770   8147  -2209   1246    -43       C  
ATOM   1828  O   LYS A 236     -10.968 -26.093  13.778  1.00 63.81           O  
ANISOU 1828  O   LYS A 236     8971   6237   9036  -2073   1217     98       O  
ATOM   1829  CB  LYS A 236     -13.821 -27.383  13.137  1.00 62.63           C  
ANISOU 1829  CB  LYS A 236     8783   6420   8594  -2560   1432   -214       C  
ATOM   1830  CG  LYS A 236     -12.895 -28.592  13.269  1.00 71.13           C  
ANISOU 1830  CG  LYS A 236    10148   7094   9784  -2491   1467   -110       C  
ATOM   1831  CD  LYS A 236     -13.298 -29.762  12.364  1.00 71.93           C  
ANISOU 1831  CD  LYS A 236    10350   7099   9881  -2620   1584   -254       C  
ATOM   1832  CE  LYS A 236     -12.189 -30.070  11.348  1.00 69.33           C  
ANISOU 1832  CE  LYS A 236    10062   6560   9721  -2452   1586   -289       C  
ATOM   1833  NZ  LYS A 236     -12.270 -31.451  10.792  1.00 74.40           N  
ANISOU 1833  NZ  LYS A 236    10909   6985  10377  -2542   1707   -369       N  
ATOM   1834  N   TYR A 237     -12.102 -24.606  12.538  1.00 53.99           N  
ANISOU 1834  N   TYR A 237     7300   5526   7687  -2153   1204   -158       N  
ATOM   1835  CA  TYR A 237     -10.896 -24.076  11.902  1.00 50.46           C  
ANISOU 1835  CA  TYR A 237     6778   5006   7390  -1922   1126   -141       C  
ATOM   1836  C   TYR A 237     -10.460 -22.728  12.471  1.00 46.38           C  
ANISOU 1836  C   TYR A 237     6110   4669   6844  -1720    967    -44       C  
ATOM   1837  O   TYR A 237      -9.665 -22.020  11.838  1.00 44.19           O  
ANISOU 1837  O   TYR A 237     5706   4438   6646  -1533    886    -60       O  
ATOM   1838  CB  TYR A 237     -11.093 -23.969  10.391  1.00 51.93           C  
ANISOU 1838  CB  TYR A 237     6824   5302   7603  -1964   1175   -336       C  
ATOM   1839  CG  TYR A 237     -11.132 -25.323   9.719  1.00 54.35           C  
ANISOU 1839  CG  TYR A 237     7294   5418   7937  -2042   1278   -415       C  
ATOM   1840  CD1 TYR A 237      -9.972 -25.910   9.233  1.00 57.44           C  
ANISOU 1840  CD1 TYR A 237     7800   5525   8500  -1902   1311   -399       C  
ATOM   1841  CD2 TYR A 237     -12.322 -26.020   9.591  1.00 55.84           C  
ANISOU 1841  CD2 TYR A 237     7519   5711   7986  -2247   1348   -512       C  
ATOM   1842  CE1 TYR A 237     -10.000 -27.158   8.628  1.00 56.11           C  
ANISOU 1842  CE1 TYR A 237     7795   5176   8349  -1966   1416   -478       C  
ATOM   1843  CE2 TYR A 237     -12.360 -27.269   8.988  1.00 62.54           C  
ANISOU 1843  CE2 TYR A 237     8532   6379   8852  -2331   1450   -590       C  
ATOM   1844  CZ  TYR A 237     -11.194 -27.829   8.506  1.00 61.35           C  
ANISOU 1844  CZ  TYR A 237     8509   5940   8861  -2190   1485   -573       C  
ATOM   1845  OH  TYR A 237     -11.223 -29.070   7.899  1.00 69.17           O  
ANISOU 1845  OH  TYR A 237     9672   6746   9863  -2267   1598   -658       O  
ATOM   1846  N   ASN A 238     -10.953 -22.363  13.655  1.00 45.12           N  
ANISOU 1846  N   ASN A 238     5977   4605   6563  -1770    934     48       N  
ATOM   1847  CA  ASN A 238     -10.557 -21.120  14.313  1.00 41.13           C  
ANISOU 1847  CA  ASN A 238     5366   4247   6013  -1600    793    137       C  
ATOM   1848  C   ASN A 238     -10.947 -19.903  13.467  1.00 36.70           C  
ANISOU 1848  C   ASN A 238     4559   3971   5413  -1546    757      7       C  
ATOM   1849  O   ASN A 238     -10.202 -18.934  13.334  1.00 39.75           O  
ANISOU 1849  O   ASN A 238     4853   4415   5837  -1358    647     41       O  
ATOM   1850  CB  ASN A 238      -9.060 -21.120  14.625  1.00 49.07           C  
ANISOU 1850  CB  ASN A 238     6443   5055   7147  -1368    670    285       C  
ATOM   1851  CG  ASN A 238      -8.677 -20.030  15.578  1.00 53.90           C  
ANISOU 1851  CG  ASN A 238     7007   5786   7689  -1245    530    394       C  
ATOM   1852  OD1 ASN A 238      -9.431 -19.714  16.501  1.00 62.56           O  
ANISOU 1852  OD1 ASN A 238     8140   6997   8634  -1346    540    427       O  
ATOM   1853  ND2 ASN A 238      -7.512 -19.426  15.356  1.00 57.19           N  
ANISOU 1853  ND2 ASN A 238     7340   6183   8207  -1041    410    439       N  
ATOM   1854  N   TYR A 239     -12.126 -19.971  12.877  1.00 42.50           N  
ANISOU 1854  N   TYR A 239     5194   4884   6071  -1716    848   -141       N  
ATOM   1855  CA  TYR A 239     -12.732 -18.854  12.181  1.00 42.44           C  
ANISOU 1855  CA  TYR A 239     4963   5165   5996  -1673    810   -256       C  
ATOM   1856  C   TYR A 239     -13.781 -18.249  13.098  1.00 40.93           C  
ANISOU 1856  C   TYR A 239     4696   5192   5663  -1743    824   -258       C  
ATOM   1857  O   TYR A 239     -14.388 -18.954  13.901  1.00 41.66           O  
ANISOU 1857  O   TYR A 239     4883   5251   5693  -1919    914   -236       O  
ATOM   1858  CB  TYR A 239     -13.382 -19.322  10.875  1.00 40.69           C  
ANISOU 1858  CB  TYR A 239     4656   5029   5775  -1809    886   -428       C  
ATOM   1859  CG  TYR A 239     -12.464 -19.290   9.670  1.00 36.94           C  
ANISOU 1859  CG  TYR A 239     4171   4460   5405  -1689    855   -472       C  
ATOM   1860  CD1 TYR A 239     -11.192 -19.852   9.718  1.00 38.57           C  
ANISOU 1860  CD1 TYR A 239     4520   4384   5752  -1581    852   -384       C  
ATOM   1861  CD2 TYR A 239     -12.870 -18.679   8.487  1.00 39.32           C  
ANISOU 1861  CD2 TYR A 239     4318   4963   5658  -1678    831   -600       C  
ATOM   1862  CE1 TYR A 239     -10.340 -19.822   8.597  1.00 38.48           C  
ANISOU 1862  CE1 TYR A 239     4487   4294   5838  -1477    849   -439       C  
ATOM   1863  CE2 TYR A 239     -12.034 -18.650   7.360  1.00 38.97           C  
ANISOU 1863  CE2 TYR A 239     4282   4834   5690  -1588    821   -646       C  
ATOM   1864  CZ  TYR A 239     -10.770 -19.217   7.421  1.00 41.71           C  
ANISOU 1864  CZ  TYR A 239     4762   4903   6183  -1494    842   -573       C  
ATOM   1865  OH  TYR A 239      -9.937 -19.166   6.308  1.00 42.61           O  
ANISOU 1865  OH  TYR A 239     4871   4946   6373  -1409    856   -632       O  
ATOM   1866  N   GLU A 240     -14.003 -16.944  12.957  1.00 41.11           N  
ANISOU 1866  N   GLU A 240     4559   5431   5631  -1607    748   -288       N  
ATOM   1867  CA  GLU A 240     -15.038 -16.299  13.746  1.00 44.77           C  
ANISOU 1867  CA  GLU A 240     4930   6115   5967  -1648    775   -312       C  
ATOM   1868  C   GLU A 240     -16.410 -16.765  13.299  1.00 48.50           C  
ANISOU 1868  C   GLU A 240     5263   6790   6375  -1851    880   -463       C  
ATOM   1869  O   GLU A 240     -16.639 -16.973  12.096  1.00 44.09           O  
ANISOU 1869  O   GLU A 240     4621   6290   5842  -1858    865   -566       O  
ATOM   1870  CB  GLU A 240     -14.963 -14.787  13.623  1.00 45.08           C  
ANISOU 1870  CB  GLU A 240     4844   6315   5968  -1437    677   -318       C  
ATOM   1871  CG  GLU A 240     -13.699 -14.220  14.130  1.00 50.01           C  
ANISOU 1871  CG  GLU A 240     5586   6779   6637  -1269    576   -187       C  
ATOM   1872  CD  GLU A 240     -13.835 -12.752  14.359  1.00 57.79           C  
ANISOU 1872  CD  GLU A 240     6493   7915   7550  -1109    512   -193       C  
ATOM   1873  OE1 GLU A 240     -14.031 -12.358  15.534  1.00 59.24           O  
ANISOU 1873  OE1 GLU A 240     6733   8126   7650  -1110    522   -141       O  
ATOM   1874  OE2 GLU A 240     -13.768 -12.003  13.361  1.00 52.83           O  
ANISOU 1874  OE2 GLU A 240     5765   7368   6939   -990    460   -251       O  
ATOM   1875  N   PRO A 241     -17.340 -16.950  14.230  1.00 41.27           N  
ANISOU 1875  N   PRO A 241     4344   5976   5362  -1978    964   -474       N  
ATOM   1876  CA  PRO A 241     -18.723 -17.221  13.851  1.00 48.30           C  
ANISOU 1876  CA  PRO A 241     5108   7070   6173  -2057   1005   -608       C  
ATOM   1877  C   PRO A 241     -19.224 -16.183  12.854  1.00 44.81           C  
ANISOU 1877  C   PRO A 241     4440   6874   5713  -1895    913   -707       C  
ATOM   1878  O   PRO A 241     -18.842 -15.011  12.898  1.00 42.33           O  
ANISOU 1878  O   PRO A 241     4047   6634   5403  -1718    844   -675       O  
ATOM   1879  CB  PRO A 241     -19.480 -17.150  15.184  1.00 51.03           C  
ANISOU 1879  CB  PRO A 241     5470   7503   6416  -2145   1093   -589       C  
ATOM   1880  CG  PRO A 241     -18.433 -17.429  16.228  1.00 46.94           C  
ANISOU 1880  CG  PRO A 241     5182   6739   5915  -2186   1117   -426       C  
ATOM   1881  CD  PRO A 241     -17.163 -16.859  15.697  1.00 49.58           C  
ANISOU 1881  CD  PRO A 241     5534   6954   6352  -2009   1001   -355       C  
ATOM   1882  N   LEU A 242     -20.046 -16.642  11.914  1.00 52.54           N  
ANISOU 1882  N   LEU A 242     5334   7967   6662  -1960    909   -824       N  
ATOM   1883  CA  LEU A 242     -20.675 -15.778  10.926  1.00 50.78           C  
ANISOU 1883  CA  LEU A 242     4913   7983   6399  -1824    815   -915       C  
ATOM   1884  C   LEU A 242     -22.070 -15.419  11.422  1.00 47.49           C  
ANISOU 1884  C   LEU A 242     4333   7820   5890  -1838    845   -991       C  
ATOM   1885  O   LEU A 242     -22.894 -16.306  11.655  1.00 48.38           O  
ANISOU 1885  O   LEU A 242     4449   7975   5960  -2025    927  -1057       O  
ATOM   1886  CB  LEU A 242     -20.745 -16.470   9.562  1.00 53.14           C  
ANISOU 1886  CB  LEU A 242     5214   8273   6703  -1898    787  -1001       C  
ATOM   1887  CG  LEU A 242     -21.048 -15.576   8.362  1.00 47.49           C  
ANISOU 1887  CG  LEU A 242     4341   7756   5946  -1748    668  -1065       C  
ATOM   1888  CD1 LEU A 242     -19.864 -14.668   8.055  1.00 48.06           C  
ANISOU 1888  CD1 LEU A 242     4448   7731   6079  -1559    590   -985       C  
ATOM   1889  CD2 LEU A 242     -21.403 -16.449   7.171  1.00 49.88           C  
ANISOU 1889  CD2 LEU A 242     4648   8089   6216  -1887    668  -1172       C  
ATOM   1890  N   THR A 243     -22.323 -14.126  11.599  1.00 57.54           N  
ANISOU 1890  N   THR A 243     5471   9254   7137  -1638    786   -987       N  
ATOM   1891  CA  THR A 243     -23.619 -13.651  12.058  1.00 60.96           C  
ANISOU 1891  CA  THR A 243     5732   9930   7499  -1612    814  -1063       C  
ATOM   1892  C   THR A 243     -24.511 -13.320  10.864  1.00 62.11           C  
ANISOU 1892  C   THR A 243     5691  10304   7606  -1535    719  -1165       C  
ATOM   1893  O   THR A 243     -24.039 -13.112   9.743  1.00 52.61           O  
ANISOU 1893  O   THR A 243     4490   9082   6417  -1450    619  -1162       O  
ATOM   1894  CB  THR A 243     -23.451 -12.420  12.951  1.00 61.22           C  
ANISOU 1894  CB  THR A 243     5732  10008   7522  -1424    815  -1008       C  
ATOM   1895  OG1 THR A 243     -23.176 -11.267  12.146  1.00 57.05           O  
ANISOU 1895  OG1 THR A 243     5122   9549   7005  -1176    691   -999       O  
ATOM   1896  CG2 THR A 243     -22.299 -12.626  13.935  1.00 61.26           C  
ANISOU 1896  CG2 THR A 243     5936   9783   7558  -1482    877   -890       C  
ATOM   1897  N   GLN A 244     -25.821 -13.278  11.112  1.00 59.43           N  
ANISOU 1897  N   GLN A 244     5183  10188   7208  -1572    753  -1258       N  
ATOM   1898  CA  GLN A 244     -26.715 -12.831  10.053  1.00 63.01           C  
ANISOU 1898  CA  GLN A 244     5438  10886   7619  -1475    651  -1346       C  
ATOM   1899  C   GLN A 244     -26.438 -11.376   9.695  1.00 61.73           C  
ANISOU 1899  C   GLN A 244     5209  10784   7463  -1165    532  -1296       C  
ATOM   1900  O   GLN A 244     -26.645 -10.969   8.549  1.00 66.62           O  
ANISOU 1900  O   GLN A 244     5740  11520   8052  -1053    413  -1324       O  
ATOM   1901  CB  GLN A 244     -28.178 -13.042  10.457  1.00 68.25           C  
ANISOU 1901  CB  GLN A 244     5914  11788   8229  -1570    714  -1457       C  
ATOM   1902  CG  GLN A 244     -29.180 -12.491   9.449  1.00 70.29           C  
ANISOU 1902  CG  GLN A 244     5938  12329   8441  -1449    600  -1543       C  
ATOM   1903  CD  GLN A 244     -29.362 -13.404   8.250  1.00 69.04           C  
ANISOU 1903  CD  GLN A 244     5772  12217   8242  -1617    554  -1615       C  
ATOM   1904  OE1 GLN A 244     -29.237 -14.624   8.356  1.00 69.02           O  
ANISOU 1904  OE1 GLN A 244     5889  12099   8236  -1875    647  -1646       O  
ATOM   1905  NE2 GLN A 244     -29.644 -12.813   7.095  1.00 72.64           N  
ANISOU 1905  NE2 GLN A 244     6103  12835   8659  -1469    413  -1640       N  
ATOM   1906  N   ASP A 245     -25.935 -10.585  10.644  1.00 54.23           N  
ANISOU 1906  N   ASP A 245     4317   9750   6540  -1028    566  -1221       N  
ATOM   1907  CA  ASP A 245     -25.472  -9.246  10.296  1.00 58.94           C  
ANISOU 1907  CA  ASP A 245     4902  10351   7142   -740    462  -1165       C  
ATOM   1908  C   ASP A 245     -24.400  -9.305   9.211  1.00 59.84           C  
ANISOU 1908  C   ASP A 245     5130  10328   7279   -712    367  -1113       C  
ATOM   1909  O   ASP A 245     -24.439  -8.536   8.243  1.00 56.94           O  
ANISOU 1909  O   ASP A 245     4708  10046   6882   -532    246  -1112       O  
ATOM   1910  CB  ASP A 245     -24.942  -8.537  11.535  1.00 60.80           C  
ANISOU 1910  CB  ASP A 245     5220  10486   7397   -639    534  -1097       C  
ATOM   1911  CG  ASP A 245     -24.735  -7.059  11.306  1.00 71.52           C  
ANISOU 1911  CG  ASP A 245     6555  11875   8745   -326    446  -1060       C  
ATOM   1912  OD1 ASP A 245     -25.718  -6.380  10.935  1.00 79.41           O  
ANISOU 1912  OD1 ASP A 245     7399  13061   9712   -162    390  -1113       O  
ATOM   1913  OD2 ASP A 245     -23.595  -6.574  11.497  1.00 71.30           O  
ANISOU 1913  OD2 ASP A 245     6667  11683   8740   -240    433   -979       O  
ATOM   1914  N   HIS A 246     -23.438 -10.218   9.361  1.00 59.88           N  
ANISOU 1914  N   HIS A 246     5299  10119   7335   -888    423  -1068       N  
ATOM   1915  CA  HIS A 246     -22.400 -10.408   8.349  1.00 55.59           C  
ANISOU 1915  CA  HIS A 246     4862   9437   6823   -890    356  -1033       C  
ATOM   1916  C   HIS A 246     -23.001 -10.832   7.014  1.00 59.82           C  
ANISOU 1916  C   HIS A 246     5316  10107   7306   -951    286  -1119       C  
ATOM   1917  O   HIS A 246     -22.611 -10.328   5.953  1.00 63.52           O  
ANISOU 1917  O   HIS A 246     5786  10597   7752   -839    184  -1111       O  
ATOM   1918  CB  HIS A 246     -21.400 -11.461   8.829  1.00 49.36           C  
ANISOU 1918  CB  HIS A 246     4252   8394   6108  -1080    445   -981       C  
ATOM   1919  CG  HIS A 246     -20.561 -11.031   9.994  1.00 48.79           C  
ANISOU 1919  CG  HIS A 246     4277   8182   6082  -1025    493   -883       C  
ATOM   1920  ND1 HIS A 246     -20.013 -11.931  10.882  1.00 46.91           N  
ANISOU 1920  ND1 HIS A 246     4175   7759   5888  -1196    590   -829       N  
ATOM   1921  CD2 HIS A 246     -20.150  -9.805  10.398  1.00 48.59           C  
ANISOU 1921  CD2 HIS A 246     4240   8170   6051   -823    456   -830       C  
ATOM   1922  CE1 HIS A 246     -19.307 -11.279  11.789  1.00 50.35           C  
ANISOU 1922  CE1 HIS A 246     4668   8122   6339  -1115    606   -747       C  
ATOM   1923  NE2 HIS A 246     -19.374  -9.987  11.519  1.00 50.44           N  
ANISOU 1923  NE2 HIS A 246     4590   8253   6321   -891    530   -753       N  
ATOM   1924  N   VAL A 247     -23.931 -11.791   7.050  1.00 61.05           N  
ANISOU 1924  N   VAL A 247     5408  10357   7430  -1144    345  -1205       N  
ATOM   1925  CA  VAL A 247     -24.580 -12.269   5.833  1.00 60.18           C  
ANISOU 1925  CA  VAL A 247     5214  10398   7255  -1232    288  -1300       C  
ATOM   1926  C   VAL A 247     -25.269 -11.122   5.109  1.00 62.00           C  
ANISOU 1926  C   VAL A 247     5274  10868   7415  -1006    152  -1319       C  
ATOM   1927  O   VAL A 247     -25.208 -11.015   3.877  1.00 64.19           O  
ANISOU 1927  O   VAL A 247     5532  11218   7638   -975     53  -1343       O  
ATOM   1928  CB  VAL A 247     -25.570 -13.397   6.169  1.00 54.58           C  
ANISOU 1928  CB  VAL A 247     4451   9771   6516  -1476    384  -1395       C  
ATOM   1929  CG1 VAL A 247     -26.263 -13.872   4.920  1.00 58.19           C  
ANISOU 1929  CG1 VAL A 247     4813  10403   6894  -1576    326  -1501       C  
ATOM   1930  CG2 VAL A 247     -24.852 -14.547   6.832  1.00 53.44           C  
ANISOU 1930  CG2 VAL A 247     4507   9365   6434  -1683    513  -1363       C  
ATOM   1931  N   ASP A 248     -25.928 -10.244   5.864  1.00 63.20           N  
ANISOU 1931  N   ASP A 248     5309  11141   7562   -840    148  -1307       N  
ATOM   1932  CA  ASP A 248     -26.590  -9.095   5.259  1.00 69.36           C  
ANISOU 1932  CA  ASP A 248     5941  12128   8285   -590     20  -1312       C  
ATOM   1933  C   ASP A 248     -25.578  -8.110   4.689  1.00 63.79           C  
ANISOU 1933  C   ASP A 248     5346  11312   7578   -371    -81  -1220       C  
ATOM   1934  O   ASP A 248     -25.760  -7.605   3.574  1.00 70.97           O  
ANISOU 1934  O   ASP A 248     6209  12337   8420   -246   -210  -1222       O  
ATOM   1935  CB  ASP A 248     -27.493  -8.419   6.290  1.00 74.61           C  
ANISOU 1935  CB  ASP A 248     6470  12920   8958   -460     62  -1327       C  
ATOM   1936  CG  ASP A 248     -28.553  -9.360   6.832  1.00 79.35           C  
ANISOU 1936  CG  ASP A 248     6945  13654   9549   -683    164  -1428       C  
ATOM   1937  OD1 ASP A 248     -28.902  -9.253   8.026  1.00 81.94           O  
ANISOU 1937  OD1 ASP A 248     7242  13985   9906   -692    270  -1435       O  
ATOM   1938  OD2 ASP A 248     -29.029 -10.221   6.061  1.00 86.58           O  
ANISOU 1938  OD2 ASP A 248     7802  14674  10422   -863    146  -1507       O  
ATOM   1939  N   ILE A 249     -24.499  -7.837   5.431  1.00 54.70           N  
ANISOU 1939  N   ILE A 249     4347   9942   6494   -331    -24  -1137       N  
ATOM   1940  CA  ILE A 249     -23.454  -6.944   4.936  1.00 53.21           C  
ANISOU 1940  CA  ILE A 249     4274   9638   6306   -146   -106  -1053       C  
ATOM   1941  C   ILE A 249     -22.906  -7.436   3.601  1.00 50.37           C  
ANISOU 1941  C   ILE A 249     3972   9255   5911   -243   -175  -1070       C  
ATOM   1942  O   ILE A 249     -22.496  -6.634   2.753  1.00 55.78           O  
ANISOU 1942  O   ILE A 249     4697   9954   6545    -77   -286  -1029       O  
ATOM   1943  CB  ILE A 249     -22.340  -6.798   5.989  1.00 56.87           C  
ANISOU 1943  CB  ILE A 249     4882   9874   6851   -145    -18   -975       C  
ATOM   1944  CG1 ILE A 249     -22.842  -5.975   7.179  1.00 57.79           C  
ANISOU 1944  CG1 ILE A 249     4952  10031   6972      9     31   -958       C  
ATOM   1945  CG2 ILE A 249     -21.118  -6.152   5.385  1.00 57.86           C  
ANISOU 1945  CG2 ILE A 249     5134   9865   6984    -22    -88   -903       C  
ATOM   1946  CD1 ILE A 249     -21.923  -5.983   8.375  1.00 61.62           C  
ANISOU 1946  CD1 ILE A 249     5562  10330   7520    -34    132   -897       C  
ATOM   1947  N   LEU A 250     -22.902  -8.752   3.386  1.00 47.92           N  
ANISOU 1947  N   LEU A 250     3683   8905   5619   -513   -105  -1134       N  
ATOM   1948  CA  LEU A 250     -22.438  -9.351   2.140  1.00 47.36           C  
ANISOU 1948  CA  LEU A 250     3672   8811   5511   -640   -145  -1174       C  
ATOM   1949  C   LEU A 250     -23.481  -9.299   1.042  1.00 56.74           C  
ANISOU 1949  C   LEU A 250     4725  10253   6580   -627   -254  -1247       C  
ATOM   1950  O   LEU A 250     -23.213  -9.777  -0.067  1.00 52.15           O  
ANISOU 1950  O   LEU A 250     4190   9683   5942   -741   -293  -1292       O  
ATOM   1951  CB  LEU A 250     -22.032 -10.805   2.375  1.00 45.45           C  
ANISOU 1951  CB  LEU A 250     3533   8400   5337   -925    -13  -1217       C  
ATOM   1952  CG  LEU A 250     -20.747 -11.042   3.169  1.00 40.23           C  
ANISOU 1952  CG  LEU A 250     3035   7454   4796   -960     81  -1139       C  
ATOM   1953  CD1 LEU A 250     -20.665 -12.504   3.606  1.00 42.80           C  
ANISOU 1953  CD1 LEU A 250     3455   7626   5182  -1214    212  -1175       C  
ATOM   1954  CD2 LEU A 250     -19.511 -10.655   2.352  1.00 38.16           C  
ANISOU 1954  CD2 LEU A 250     2876   7072   4552   -901     36  -1106       C  
ATOM   1955  N   GLY A 251     -24.656  -8.752   1.342  1.00 59.76           N  
ANISOU 1955  N   GLY A 251     4943  10838   6924   -498   -298  -1262       N  
ATOM   1956  CA  GLY A 251     -25.747  -8.655   0.405  1.00 57.91           C  
ANISOU 1956  CA  GLY A 251     4553  10864   6585   -468   -409  -1325       C  
ATOM   1957  C   GLY A 251     -25.358  -8.129  -0.962  1.00 59.64           C  
ANISOU 1957  C   GLY A 251     4826  11127   6705   -363   -558  -1296       C  
ATOM   1958  O   GLY A 251     -25.504  -8.829  -1.966  1.00 54.14           O  
ANISOU 1958  O   GLY A 251     4127  10509   5936   -530   -594  -1365       O  
ATOM   1959  N   PRO A 252     -24.860  -6.886  -1.033  1.00 60.60           N  
ANISOU 1959  N   PRO A 252     5020  11195   6810    -89   -647  -1195       N  
ATOM   1960  CA  PRO A 252     -24.566  -6.299  -2.355  1.00 61.86           C  
ANISOU 1960  CA  PRO A 252     5255  11402   6847     27   -805  -1155       C  
ATOM   1961  C   PRO A 252     -23.602  -7.123  -3.195  1.00 64.77           C  
ANISOU 1961  C   PRO A 252     5766  11662   7182   -203   -782  -1195       C  
ATOM   1962  O   PRO A 252     -23.784  -7.214  -4.413  1.00 59.55           O  
ANISOU 1962  O   PRO A 252     5123  11109   6393   -243   -888  -1223       O  
ATOM   1963  CB  PRO A 252     -23.975  -4.928  -2.004  1.00 60.81           C  
ANISOU 1963  CB  PRO A 252     5235  11150   6720    333   -858  -1031       C  
ATOM   1964  CG  PRO A 252     -24.513  -4.617  -0.644  1.00 71.80           C  
ANISOU 1964  CG  PRO A 252     6532  12537   8214    428   -765  -1025       C  
ATOM   1965  CD  PRO A 252     -24.614  -5.932   0.065  1.00 70.67           C  
ANISOU 1965  CD  PRO A 252     6329  12365   8158    127   -611  -1112       C  
ATOM   1966  N   LEU A 253     -22.573  -7.724  -2.585  1.00 63.12           N  
ANISOU 1966  N   LEU A 253     5667  11233   7081   -355   -644  -1200       N  
ATOM   1967  CA  LEU A 253     -21.636  -8.547  -3.351  1.00 53.91           C  
ANISOU 1967  CA  LEU A 253     4641   9944   5898   -578   -599  -1255       C  
ATOM   1968  C   LEU A 253     -22.314  -9.806  -3.868  1.00 55.63           C  
ANISOU 1968  C   LEU A 253     4804  10250   6083   -845   -547  -1376       C  
ATOM   1969  O   LEU A 253     -22.166 -10.181  -5.043  1.00 57.56           O  
ANISOU 1969  O   LEU A 253     5118  10532   6220   -966   -591  -1435       O  
ATOM   1970  CB  LEU A 253     -20.431  -8.914  -2.484  1.00 46.97           C  
ANISOU 1970  CB  LEU A 253     3877   8798   5172   -665   -455  -1231       C  
ATOM   1971  CG  LEU A 253     -19.373  -7.831  -2.310  1.00 44.29           C  
ANISOU 1971  CG  LEU A 253     3730   8239   4857   -445   -461  -1094       C  
ATOM   1972  CD1 LEU A 253     -18.453  -8.144  -1.142  1.00 40.17           C  
ANISOU 1972  CD1 LEU A 253     3313   7439   4511   -489   -306  -1039       C  
ATOM   1973  CD2 LEU A 253     -18.585  -7.680  -3.621  1.00 39.56           C  
ANISOU 1973  CD2 LEU A 253     3341   7536   4156   -461   -492  -1081       C  
ATOM   1974  N   SER A 254     -23.057 -10.481  -2.989  1.00 51.50           N  
ANISOU 1974  N   SER A 254     4177   9753   5637   -949   -446  -1417       N  
ATOM   1975  CA  SER A 254     -23.868 -11.611  -3.413  1.00 45.67           C  
ANISOU 1975  CA  SER A 254     3376   9123   4853  -1189   -402  -1533       C  
ATOM   1976  C   SER A 254     -24.746 -11.239  -4.595  1.00 48.75           C  
ANISOU 1976  C   SER A 254     3654   9781   5086  -1135   -566  -1567       C  
ATOM   1977  O   SER A 254     -24.947 -12.044  -5.506  1.00 50.68           O  
ANISOU 1977  O   SER A 254     3921  10085   5249  -1339   -566  -1659       O  
ATOM   1978  CB  SER A 254     -24.737 -12.101  -2.255  1.00 47.77           C  
ANISOU 1978  CB  SER A 254     3528   9431   5191  -1259   -302  -1561       C  
ATOM   1979  OG  SER A 254     -25.412 -13.297  -2.617  1.00 51.16           O  
ANISOU 1979  OG  SER A 254     3925   9937   5578  -1521   -240  -1678       O  
ATOM   1980  N   ALA A 255     -25.276 -10.016  -4.589  1.00 58.50           N  
ANISOU 1980  N   ALA A 255     4781  11168   6277   -855   -707  -1491       N  
ATOM   1981  CA  ALA A 255     -26.209  -9.592  -5.624  1.00 64.42           C  
ANISOU 1981  CA  ALA A 255     5414  12175   6887   -768   -881  -1505       C  
ATOM   1982  C   ALA A 255     -25.491  -9.285  -6.930  1.00 66.21           C  
ANISOU 1982  C   ALA A 255     5807  12367   6983   -749   -996  -1476       C  
ATOM   1983  O   ALA A 255     -26.021  -9.552  -8.014  1.00 72.06           O  
ANISOU 1983  O   ALA A 255     6518  13267   7593   -836  -1097  -1528       O  
ATOM   1984  CB  ALA A 255     -26.992  -8.369  -5.146  1.00 68.37           C  
ANISOU 1984  CB  ALA A 255     5768  12813   7395   -449   -985  -1426       C  
ATOM   1985  N   GLN A 256     -24.294  -8.712  -6.846  1.00 63.72           N  
ANISOU 1985  N   GLN A 256     5675  11849   6685   -643   -984  -1395       N  
ATOM   1986  CA  GLN A 256     -23.543  -8.418  -8.060  1.00 58.58           C  
ANISOU 1986  CA  GLN A 256     5221  11149   5888   -641  -1076  -1370       C  
ATOM   1987  C   GLN A 256     -23.069  -9.696  -8.737  1.00 58.18           C  
ANISOU 1987  C   GLN A 256     5279  11018   5808   -976   -968  -1494       C  
ATOM   1988  O   GLN A 256     -23.053  -9.784  -9.973  1.00 61.60           O  
ANISOU 1988  O   GLN A 256     5812  11513   6081  -1050  -1051  -1524       O  
ATOM   1989  CB  GLN A 256     -22.364  -7.511  -7.733  1.00 64.42           C  
ANISOU 1989  CB  GLN A 256     6139  11692   6647   -463  -1072  -1264       C  
ATOM   1990  CG  GLN A 256     -21.452  -7.249  -8.909  1.00 66.86           C  
ANISOU 1990  CG  GLN A 256     6698  11916   6789   -490  -1128  -1244       C  
ATOM   1991  CD  GLN A 256     -20.218  -6.476  -8.509  1.00 68.49           C  
ANISOU 1991  CD  GLN A 256     7107  11889   7026   -352  -1076  -1146       C  
ATOM   1992  OE1 GLN A 256     -20.088  -6.047  -7.356  1.00 75.94           O  
ANISOU 1992  OE1 GLN A 256     8006  12721   8127   -210  -1012  -1074       O  
ATOM   1993  NE2 GLN A 256     -19.301  -6.287  -9.456  1.00 61.38           N  
ANISOU 1993  NE2 GLN A 256     6486  10818   6018   -391  -1044  -1111       N  
ATOM   1994  N   THR A 257     -22.697 -10.705  -7.950  1.00 55.44           N  
ANISOU 1994  N   THR A 257     4939  10517   5611  -1177   -776  -1564       N  
ATOM   1995  CA  THR A 257     -22.186 -11.951  -8.515  1.00 52.39           C  
ANISOU 1995  CA  THR A 257     4685  10001   5218  -1478   -643  -1682       C  
ATOM   1996  C   THR A 257     -23.251 -13.017  -8.709  1.00 55.10           C  
ANISOU 1996  C   THR A 257     4912  10486   5539  -1694   -602  -1792       C  
ATOM   1997  O   THR A 257     -23.011 -13.983  -9.440  1.00 60.55           O  
ANISOU 1997  O   THR A 257     5720  11107   6181  -1932   -520  -1894       O  
ATOM   1998  CB  THR A 257     -21.106 -12.547  -7.614  1.00 55.43           C  
ANISOU 1998  CB  THR A 257     5186  10093   5784  -1577   -447  -1692       C  
ATOM   1999  OG1 THR A 257     -21.643 -12.722  -6.294  1.00 53.47           O  
ANISOU 1999  OG1 THR A 257     4800   9841   5675  -1544   -380  -1662       O  
ATOM   2000  CG2 THR A 257     -19.880 -11.644  -7.559  1.00 51.87           C  
ANISOU 2000  CG2 THR A 257     4874   9487   5347  -1424   -468  -1612       C  
ATOM   2001  N   GLY A 258     -24.407 -12.890  -8.059  1.00 55.69           N  
ANISOU 2001  N   GLY A 258     4769  10746   5645  -1626   -642  -1784       N  
ATOM   2002  CA  GLY A 258     -25.405 -13.939  -8.157  1.00 60.76           C  
ANISOU 2002  CA  GLY A 258     5302  11522   6263  -1853   -589  -1899       C  
ATOM   2003  C   GLY A 258     -25.053 -15.212  -7.421  1.00 60.66           C  
ANISOU 2003  C   GLY A 258     5386  11292   6369  -2092   -366  -1969       C  
ATOM   2004  O   GLY A 258     -25.591 -16.272  -7.738  1.00 57.45           O  
ANISOU 2004  O   GLY A 258     4974  10932   5920  -2334   -295  -2080       O  
ATOM   2005  N   ILE A 259     -24.161 -15.141  -6.441  1.00 57.62           N  
ANISOU 2005  N   ILE A 259     5102  10661   6129  -2027   -258  -1902       N  
ATOM   2006  CA  ILE A 259     -23.801 -16.283  -5.615  1.00 60.76           C  
ANISOU 2006  CA  ILE A 259     5613  10823   6650  -2211    -59  -1939       C  
ATOM   2007  C   ILE A 259     -24.363 -16.029  -4.224  1.00 51.94           C  
ANISOU 2007  C   ILE A 259     4373   9735   5628  -2114    -30  -1880       C  
ATOM   2008  O   ILE A 259     -23.992 -15.049  -3.568  1.00 51.60           O  
ANISOU 2008  O   ILE A 259     4303   9654   5649  -1892    -76  -1773       O  
ATOM   2009  CB  ILE A 259     -22.280 -16.488  -5.572  1.00 64.98           C  
ANISOU 2009  CB  ILE A 259     6378  11029   7284  -2219     46  -1907       C  
ATOM   2010  CG1 ILE A 259     -21.751 -16.737  -6.985  1.00 60.33           C  
ANISOU 2010  CG1 ILE A 259     5922  10412   6587  -2325     35  -1983       C  
ATOM   2011  CG2 ILE A 259     -21.910 -17.634  -4.634  1.00 63.97           C  
ANISOU 2011  CG2 ILE A 259     6376  10635   7294  -2366    237  -1921       C  
ATOM   2012  CD1 ILE A 259     -20.263 -16.616  -7.073  1.00 50.28           C  
ANISOU 2012  CD1 ILE A 259     4844   8861   5398  -2285    113  -1952       C  
ATOM   2013  N   ALA A 260     -25.286 -16.880  -3.792  1.00 56.71           N  
ANISOU 2013  N   ALA A 260     4905  10415   6225  -2286     47  -1954       N  
ATOM   2014  CA  ALA A 260     -25.884 -16.701  -2.478  1.00 54.23           C  
ANISOU 2014  CA  ALA A 260     4484  10138   5984  -2224     88  -1913       C  
ATOM   2015  C   ALA A 260     -24.803 -16.782  -1.410  1.00 44.24           C  
ANISOU 2015  C   ALA A 260     3388   8560   4863  -2176    196  -1819       C  
ATOM   2016  O   ALA A 260     -23.807 -17.492  -1.563  1.00 50.55           O  
ANISOU 2016  O   ALA A 260     4389   9098   5720  -2279    290  -1820       O  
ATOM   2017  CB  ALA A 260     -26.958 -17.757  -2.231  1.00 58.17           C  
ANISOU 2017  CB  ALA A 260     4911  10747   6442  -2465    175  -2023       C  
ATOM   2018  N   VAL A 261     -25.001 -16.039  -0.318  1.00 56.53           N  
ANISOU 2018  N   VAL A 261     4860  10140   6479  -2011    184  -1736       N  
ATOM   2019  CA  VAL A 261     -23.980 -15.998   0.724  1.00 53.99           C  
ANISOU 2019  CA  VAL A 261     4686   9542   6287  -1951    267  -1634       C  
ATOM   2020  C   VAL A 261     -23.687 -17.406   1.237  1.00 48.61           C  
ANISOU 2020  C   VAL A 261     4174   8628   5667  -2186    427  -1663       C  
ATOM   2021  O   VAL A 261     -22.525 -17.821   1.339  1.00 47.96           O  
ANISOU 2021  O   VAL A 261     4282   8266   5676  -2206    495  -1615       O  
ATOM   2022  CB  VAL A 261     -24.403 -15.051   1.860  1.00 50.89           C  
ANISOU 2022  CB  VAL A 261     4175   9233   5928  -1767    241  -1558       C  
ATOM   2023  CG1 VAL A 261     -23.376 -15.090   2.955  1.00 41.43           C  
ANISOU 2023  CG1 VAL A 261     3131   7759   4850  -1733    327  -1453       C  
ATOM   2024  CG2 VAL A 261     -24.549 -13.631   1.337  1.00 53.69           C  
ANISOU 2024  CG2 VAL A 261     4402   9768   6229  -1503     87  -1516       C  
ATOM   2025  N   LEU A 262     -24.734 -18.176   1.529  1.00 50.47           N  
ANISOU 2025  N   LEU A 262     4348   8975   5854  -2365    491  -1746       N  
ATOM   2026  CA  LEU A 262     -24.533 -19.528   2.046  1.00 56.57           C  
ANISOU 2026  CA  LEU A 262     5297   9525   6671  -2589    646  -1772       C  
ATOM   2027  C   LEU A 262     -23.918 -20.473   1.013  1.00 57.69           C  
ANISOU 2027  C   LEU A 262     5610   9506   6803  -2738    699  -1840       C  
ATOM   2028  O   LEU A 262     -23.226 -21.427   1.392  1.00 55.64           O  
ANISOU 2028  O   LEU A 262     5559   8960   6621  -2844    821  -1821       O  
ATOM   2029  CB  LEU A 262     -25.855 -20.072   2.577  1.00 60.14           C  
ANISOU 2029  CB  LEU A 262     5637  10156   7058  -2757    706  -1855       C  
ATOM   2030  CG  LEU A 262     -26.257 -19.375   3.883  1.00 57.98           C  
ANISOU 2030  CG  LEU A 262     5261   9950   6820  -2640    710  -1783       C  
ATOM   2031  CD1 LEU A 262     -27.687 -19.685   4.257  1.00 60.44           C  
ANISOU 2031  CD1 LEU A 262     5404  10506   7053  -2784    752  -1884       C  
ATOM   2032  CD2 LEU A 262     -25.300 -19.747   5.011  1.00 54.81           C  
ANISOU 2032  CD2 LEU A 262     5068   9233   6525  -2646    811  -1671       C  
ATOM   2033  N   ASP A 263     -24.118 -20.220  -0.288  1.00 57.12           N  
ANISOU 2033  N   ASP A 263     5466   9602   6636  -2740    613  -1916       N  
ATOM   2034  CA  ASP A 263     -23.372 -20.960  -1.305  1.00 55.93           C  
ANISOU 2034  CA  ASP A 263     5492   9283   6477  -2856    667  -1977       C  
ATOM   2035  C   ASP A 263     -21.870 -20.679  -1.207  1.00 46.20           C  
ANISOU 2035  C   ASP A 263     4421   7763   5368  -2714    689  -1882       C  
ATOM   2036  O   ASP A 263     -21.034 -21.601  -1.265  1.00 50.57           O  
ANISOU 2036  O   ASP A 263     5185   8033   5998  -2804    809  -1893       O  
ATOM   2037  CB  ASP A 263     -23.904 -20.608  -2.699  1.00 57.51           C  
ANISOU 2037  CB  ASP A 263     5573   9745   6532  -2879    556  -2068       C  
ATOM   2038  CG  ASP A 263     -25.320 -21.121  -2.934  1.00 78.50           C  
ANISOU 2038  CG  ASP A 263     8085  12669   9071  -3062    550  -2183       C  
ATOM   2039  OD1 ASP A 263     -25.839 -21.843  -2.059  1.00 80.57           O  
ANISOU 2039  OD1 ASP A 263     8361  12892   9361  -3196    654  -2205       O  
ATOM   2040  OD2 ASP A 263     -25.914 -20.820  -3.997  1.00 81.05           O  
ANISOU 2040  OD2 ASP A 263     8282  13245   9269  -3083    442  -2251       O  
ATOM   2041  N   MET A 264     -21.501 -19.405  -1.059  1.00 45.76           N  
ANISOU 2041  N   MET A 264     4273   7776   5339  -2486    578  -1789       N  
ATOM   2042  CA  MET A 264     -20.092 -19.092  -0.866  1.00 44.74           C  
ANISOU 2042  CA  MET A 264     4277   7390   5334  -2359    602  -1698       C  
ATOM   2043  C   MET A 264     -19.568 -19.665   0.443  1.00 42.75           C  
ANISOU 2043  C   MET A 264     4147   6876   5221  -2367    709  -1609       C  
ATOM   2044  O   MET A 264     -18.390 -20.039   0.522  1.00 44.03           O  
ANISOU 2044  O   MET A 264     4472   6758   5500  -2344    782  -1565       O  
ATOM   2045  CB  MET A 264     -19.852 -17.588  -0.920  1.00 38.91           C  
ANISOU 2045  CB  MET A 264     3417   6785   4583  -2125    465  -1619       C  
ATOM   2046  CG  MET A 264     -18.375 -17.228  -0.987  1.00 40.37           C  
ANISOU 2046  CG  MET A 264     3727   6735   4877  -2018    488  -1550       C  
ATOM   2047  SD  MET A 264     -17.769 -17.661  -2.657  1.00 40.87           S  
ANISOU 2047  SD  MET A 264     3911   6745   4873  -2132    517  -1672       S  
ATOM   2048  CE  MET A 264     -18.304 -16.189  -3.512  1.00 41.23           C  
ANISOU 2048  CE  MET A 264     3785   7127   4754  -1988    317  -1671       C  
ATOM   2049  N   CYS A 265     -20.419 -19.750   1.476  1.00 48.56           N  
ANISOU 2049  N   CYS A 265     4807   7699   5946  -2399    723  -1582       N  
ATOM   2050  CA  CYS A 265     -19.996 -20.429   2.693  1.00 47.31           C  
ANISOU 2050  CA  CYS A 265     4787   7297   5894  -2443    828  -1501       C  
ATOM   2051  C   CYS A 265     -19.708 -21.899   2.425  1.00 42.60           C  
ANISOU 2051  C   CYS A 265     4391   6468   5326  -2634    961  -1562       C  
ATOM   2052  O   CYS A 265     -18.763 -22.454   2.986  1.00 49.18           O  
ANISOU 2052  O   CYS A 265     5399   7007   6279  -2622   1040  -1484       O  
ATOM   2053  CB  CYS A 265     -21.042 -20.274   3.803  1.00 45.58           C  
ANISOU 2053  CB  CYS A 265     4456   7230   5632  -2470    834  -1478       C  
ATOM   2054  SG  CYS A 265     -21.242 -18.589   4.391  1.00 46.47           S  
ANISOU 2054  SG  CYS A 265     4373   7546   5736  -2218    710  -1390       S  
ATOM   2055  N   ALA A 266     -20.512 -22.556   1.579  1.00 46.62           N  
ANISOU 2055  N   ALA A 266     4884   7103   5726  -2810    989  -1699       N  
ATOM   2056  CA  ALA A 266     -20.215 -23.946   1.237  1.00 48.95           C  
ANISOU 2056  CA  ALA A 266     5390   7169   6042  -2990   1126  -1767       C  
ATOM   2057  C   ALA A 266     -18.874 -24.059   0.521  1.00 49.45           C  
ANISOU 2057  C   ALA A 266     5601   6991   6197  -2905   1158  -1758       C  
ATOM   2058  O   ALA A 266     -18.114 -25.021   0.734  1.00 51.46           O  
ANISOU 2058  O   ALA A 266     6065   6937   6552  -2944   1277  -1739       O  
ATOM   2059  CB  ALA A 266     -21.336 -24.535   0.376  1.00 53.70           C  
ANISOU 2059  CB  ALA A 266     5934   7977   6493  -3201   1145  -1926       C  
ATOM   2060  N   SER A 267     -18.555 -23.066  -0.315  1.00 46.35           N  
ANISOU 2060  N   SER A 267     5106   6731   5774  -2779   1058  -1770       N  
ATOM   2061  CA  SER A 267     -17.252 -23.086  -0.978  1.00 43.95           C  
ANISOU 2061  CA  SER A 267     4931   6209   5559  -2697   1100  -1769       C  
ATOM   2062  C   SER A 267     -16.119 -22.906   0.018  1.00 48.41           C  
ANISOU 2062  C   SER A 267     5573   6516   6303  -2537   1125  -1624       C  
ATOM   2063  O   SER A 267     -15.090 -23.588  -0.061  1.00 46.46           O  
ANISOU 2063  O   SER A 267     5497   5977   6178  -2516   1228  -1614       O  
ATOM   2064  CB  SER A 267     -17.194 -22.022  -2.068  1.00 54.78           C  
ANISOU 2064  CB  SER A 267     6185   7790   6840  -2615    990  -1813       C  
ATOM   2065  OG  SER A 267     -17.570 -22.613  -3.300  1.00 63.41           O  
ANISOU 2065  OG  SER A 267     7324   8959   7810  -2777   1027  -1958       O  
ATOM   2066  N   LEU A 268     -16.291 -21.986   0.966  1.00 47.45           N  
ANISOU 2066  N   LEU A 268     5326   6502   6200  -2416   1034  -1512       N  
ATOM   2067  CA  LEU A 268     -15.292 -21.799   2.010  1.00 42.70           C  
ANISOU 2067  CA  LEU A 268     4789   5680   5754  -2281   1048  -1367       C  
ATOM   2068  C   LEU A 268     -15.133 -23.064   2.847  1.00 40.72           C  
ANISOU 2068  C   LEU A 268     4719   5168   5583  -2377   1163  -1324       C  
ATOM   2069  O   LEU A 268     -14.015 -23.453   3.188  1.00 45.51           O  
ANISOU 2069  O   LEU A 268     5462   5491   6338  -2299   1220  -1248       O  
ATOM   2070  CB  LEU A 268     -15.683 -20.602   2.882  1.00 42.26           C  
ANISOU 2070  CB  LEU A 268     4569   5817   5671  -2159    936  -1270       C  
ATOM   2071  CG  LEU A 268     -14.758 -20.261   4.043  1.00 43.13           C  
ANISOU 2071  CG  LEU A 268     4724   5750   5915  -2031    934  -1116       C  
ATOM   2072  CD1 LEU A 268     -13.333 -20.108   3.564  1.00 43.21           C  
ANISOU 2072  CD1 LEU A 268     4805   5554   6058  -1916    953  -1090       C  
ATOM   2073  CD2 LEU A 268     -15.224 -18.984   4.752  1.00 44.56           C  
ANISOU 2073  CD2 LEU A 268     4740   6150   6039  -1915    830  -1045       C  
ATOM   2074  N   LYS A 269     -16.240 -23.712   3.187  1.00 41.21           N  
ANISOU 2074  N   LYS A 269     4786   5321   5550  -2543   1200  -1369       N  
ATOM   2075  CA  LYS A 269     -16.184 -24.959   3.943  1.00 53.79           C  
ANISOU 2075  CA  LYS A 269     6576   6668   7195  -2656   1315  -1331       C  
ATOM   2076  C   LYS A 269     -15.328 -26.002   3.231  1.00 52.59           C  
ANISOU 2076  C   LYS A 269     6627   6227   7128  -2681   1426  -1382       C  
ATOM   2077  O   LYS A 269     -14.446 -26.629   3.840  1.00 53.20           O  
ANISOU 2077  O   LYS A 269     6879   5997   7339  -2621   1490  -1287       O  
ATOM   2078  CB  LYS A 269     -17.597 -25.493   4.163  1.00 54.87           C  
ANISOU 2078  CB  LYS A 269     6676   6980   7193  -2861   1351  -1411       C  
ATOM   2079  CG  LYS A 269     -17.634 -26.837   4.847  1.00 58.93           C  
ANISOU 2079  CG  LYS A 269     7413   7244   7733  -3007   1481  -1385       C  
ATOM   2080  CD  LYS A 269     -19.036 -27.428   4.837  1.00 62.87           C  
ANISOU 2080  CD  LYS A 269     7876   7927   8084  -3241   1535  -1500       C  
ATOM   2081  CE  LYS A 269     -20.049 -26.440   5.394  1.00 65.64           C  
ANISOU 2081  CE  LYS A 269     7989   8608   8345  -3227   1447  -1493       C  
ATOM   2082  NZ  LYS A 269     -21.411 -27.035   5.489  1.00 73.25           N  
ANISOU 2082  NZ  LYS A 269     8905   9751   9175  -3459   1510  -1606       N  
ATOM   2083  N   GLU A 270     -15.555 -26.197   1.930  1.00 54.06           N  
ANISOU 2083  N   GLU A 270     6800   6504   7238  -2760   1452  -1532       N  
ATOM   2084  CA  GLU A 270     -14.717 -27.193   1.270  1.00 54.33           C  
ANISOU 2084  CA  GLU A 270     7036   6254   7353  -2775   1577  -1588       C  
ATOM   2085  C   GLU A 270     -13.278 -26.702   1.087  1.00 53.50           C  
ANISOU 2085  C   GLU A 270     6950   5969   7407  -2556   1570  -1524       C  
ATOM   2086  O   GLU A 270     -12.352 -27.519   1.095  1.00 53.12           O  
ANISOU 2086  O   GLU A 270     7078   5611   7492  -2498   1674  -1504       O  
ATOM   2087  CB  GLU A 270     -15.347 -27.656  -0.046  1.00 68.74           C  
ANISOU 2087  CB  GLU A 270     8869   8210   9039  -2945   1628  -1772       C  
ATOM   2088  CG  GLU A 270     -16.456 -28.723   0.155  1.00 83.64           C  
ANISOU 2088  CG  GLU A 270    10836  10126  10818  -3187   1708  -1845       C  
ATOM   2089  CD  GLU A 270     -15.976 -30.072   0.748  1.00 89.86           C  
ANISOU 2089  CD  GLU A 270    11891  10544  11706  -3235   1854  -1802       C  
ATOM   2090  OE1 GLU A 270     -15.085 -30.106   1.625  1.00 91.86           O  
ANISOU 2090  OE1 GLU A 270    12236  10555  12111  -3079   1857  -1657       O  
ATOM   2091  OE2 GLU A 270     -16.521 -31.122   0.342  1.00 99.79           O  
ANISOU 2091  OE2 GLU A 270    13278  11755  12884  -3435   1964  -1912       O  
ATOM   2092  N   LEU A 271     -13.049 -25.383   0.998  1.00 53.04           N  
ANISOU 2092  N   LEU A 271     6715   6088   7348  -2423   1454  -1483       N  
ATOM   2093  CA  LEU A 271     -11.671 -24.877   0.977  1.00 50.85           C  
ANISOU 2093  CA  LEU A 271     6445   5643   7234  -2222   1452  -1414       C  
ATOM   2094  C   LEU A 271     -10.951 -25.158   2.294  1.00 53.01           C  
ANISOU 2094  C   LEU A 271     6805   5666   7671  -2110   1461  -1249       C  
ATOM   2095  O   LEU A 271      -9.759 -25.489   2.304  1.00 51.17           O  
ANISOU 2095  O   LEU A 271     6666   5169   7609  -1974   1521  -1207       O  
ATOM   2096  CB  LEU A 271     -11.658 -23.376   0.679  1.00 47.48           C  
ANISOU 2096  CB  LEU A 271     5820   5466   6755  -2121   1325  -1400       C  
ATOM   2097  CG  LEU A 271     -11.771 -22.964  -0.794  1.00 50.51           C  
ANISOU 2097  CG  LEU A 271     6153   6014   7024  -2161   1319  -1541       C  
ATOM   2098  CD1 LEU A 271     -11.955 -21.455  -0.897  1.00 44.11           C  
ANISOU 2098  CD1 LEU A 271     5157   5463   6139  -2066   1175  -1503       C  
ATOM   2099  CD2 LEU A 271     -10.546 -23.417  -1.571  1.00 52.57           C  
ANISOU 2099  CD2 LEU A 271     6537   6035   7404  -2099   1445  -1600       C  
ATOM   2100  N   LEU A 272     -11.658 -25.002   3.418  1.00 49.35           N  
ANISOU 2100  N   LEU A 272     6306   5289   7154  -2158   1399  -1153       N  
ATOM   2101  CA  LEU A 272     -11.093 -25.302   4.730  1.00 46.91           C  
ANISOU 2101  CA  LEU A 272     6103   4754   6966  -2079   1399   -987       C  
ATOM   2102  C   LEU A 272     -10.799 -26.785   4.888  1.00 48.74           C  
ANISOU 2102  C   LEU A 272     6580   4670   7268  -2125   1519   -977       C  
ATOM   2103  O   LEU A 272      -9.771 -27.157   5.463  1.00 56.26           O  
ANISOU 2103  O   LEU A 272     7653   5341   8380  -1979   1535   -860       O  
ATOM   2104  CB  LEU A 272     -12.050 -24.855   5.833  1.00 46.19           C  
ANISOU 2104  CB  LEU A 272     5935   4848   6766  -2153   1328   -906       C  
ATOM   2105  CG  LEU A 272     -12.152 -23.351   6.039  1.00 44.78           C  
ANISOU 2105  CG  LEU A 272     5540   4926   6548  -2053   1206   -867       C  
ATOM   2106  CD1 LEU A 272     -13.206 -23.040   7.094  1.00 49.04           C  
ANISOU 2106  CD1 LEU A 272     6015   5650   6969  -2135   1166   -812       C  
ATOM   2107  CD2 LEU A 272     -10.807 -22.802   6.443  1.00 39.91           C  
ANISOU 2107  CD2 LEU A 272     4927   4138   6099  -1860   1169   -749       C  
ATOM   2108  N   GLN A 273     -11.697 -27.643   4.401  1.00 48.86           N  
ANISOU 2108  N   GLN A 273     6671   4727   7165  -2318   1597  -1095       N  
ATOM   2109  CA  GLN A 273     -11.524 -29.076   4.613  1.00 57.11           C  
ANISOU 2109  CA  GLN A 273     7968   5473   8259  -2377   1715  -1084       C  
ATOM   2110  C   GLN A 273     -10.524 -29.699   3.642  1.00 63.01           C  
ANISOU 2110  C   GLN A 273     8827   5988   9125  -2277   1815  -1160       C  
ATOM   2111  O   GLN A 273      -9.820 -30.641   4.016  1.00 70.81           O  
ANISOU 2111  O   GLN A 273    10015   6656  10234  -2192   1884  -1089       O  
ATOM   2112  CB  GLN A 273     -12.876 -29.782   4.515  1.00 59.35           C  
ANISOU 2112  CB  GLN A 273     8295   5884   8370  -2637   1776  -1186       C  
ATOM   2113  CG  GLN A 273     -13.817 -29.449   5.663  1.00 60.90           C  
ANISOU 2113  CG  GLN A 273     8424   6248   8467  -2733   1716  -1103       C  
ATOM   2114  CD  GLN A 273     -15.220 -29.978   5.451  1.00 68.32           C  
ANISOU 2114  CD  GLN A 273     9349   7375   9234  -2989   1774  -1231       C  
ATOM   2115  OE1 GLN A 273     -15.592 -30.361   4.344  1.00 75.12           O  
ANISOU 2115  OE1 GLN A 273    10205   8312  10027  -3101   1828  -1390       O  
ATOM   2116  NE2 GLN A 273     -16.009 -30.001   6.515  1.00 68.63           N  
ANISOU 2116  NE2 GLN A 273     9381   7499   9195  -3091   1767  -1168       N  
ATOM   2117  N   ASN A 274     -10.423 -29.189   2.415  1.00 64.93           N  
ANISOU 2117  N   ASN A 274     8952   6384   9334  -2273   1825  -1298       N  
ATOM   2118  CA  ASN A 274      -9.563 -29.791   1.402  1.00 67.33           C  
ANISOU 2118  CA  ASN A 274     9358   6497   9727  -2201   1944  -1396       C  
ATOM   2119  C   ASN A 274      -8.255 -29.046   1.179  1.00 67.77           C  
ANISOU 2119  C   ASN A 274     9321   6481   9950  -1957   1922  -1354       C  
ATOM   2120  O   ASN A 274      -7.313 -29.636   0.638  1.00 69.15           O  
ANISOU 2120  O   ASN A 274     9588   6436  10249  -1841   2030  -1396       O  
ATOM   2121  CB  ASN A 274     -10.298 -29.874   0.061  1.00 69.58           C  
ANISOU 2121  CB  ASN A 274     9608   6984   9845  -2385   1999  -1594       C  
ATOM   2122  CG  ASN A 274     -11.581 -30.658   0.151  1.00 80.58           C  
ANISOU 2122  CG  ASN A 274    11078   8460  11077  -2638   2036  -1660       C  
ATOM   2123  OD1 ASN A 274     -11.985 -31.094   1.232  1.00 83.28           O  
ANISOU 2123  OD1 ASN A 274    11496   8724  11422  -2688   2025  -1561       O  
ATOM   2124  ND2 ASN A 274     -12.238 -30.845  -0.989  1.00 88.49           N  
ANISOU 2124  ND2 ASN A 274    12063   9628  11929  -2809   2083  -1831       N  
ATOM   2125  N   GLY A 275      -8.170 -27.777   1.564  1.00 62.52           N  
ANISOU 2125  N   GLY A 275     8467   5997   9290  -1874   1793  -1279       N  
ATOM   2126  CA  GLY A 275      -7.043 -26.970   1.166  1.00 60.72           C  
ANISOU 2126  CA  GLY A 275     8126   5751   9195  -1680   1779  -1272       C  
ATOM   2127  C   GLY A 275      -7.191 -26.503  -0.270  1.00 58.90           C  
ANISOU 2127  C   GLY A 275     7817   5712   8852  -1754   1819  -1444       C  
ATOM   2128  O   GLY A 275      -8.229 -26.676  -0.913  1.00 62.16           O  
ANISOU 2128  O   GLY A 275     8239   6303   9076  -1948   1827  -1557       O  
ATOM   2129  N   MET A 276      -6.120 -25.901  -0.779  1.00 61.97           N  
ANISOU 2129  N   MET A 276     8126   6065   9354  -1597   1843  -1461       N  
ATOM   2130  CA  MET A 276      -6.139 -25.372  -2.133  1.00 67.86           C  
ANISOU 2130  CA  MET A 276     8815   6982   9987  -1660   1882  -1611       C  
ATOM   2131  C   MET A 276      -5.622 -26.360  -3.163  1.00 78.98           C  
ANISOU 2131  C   MET A 276    10358   8226  11424  -1675   2065  -1746       C  
ATOM   2132  O   MET A 276      -5.955 -26.226  -4.346  1.00 74.66           O  
ANISOU 2132  O   MET A 276     9819   7825  10722  -1799   2113  -1887       O  
ATOM   2133  CB  MET A 276      -5.317 -24.086  -2.211  1.00 68.41           C  
ANISOU 2133  CB  MET A 276     8728   7133  10133  -1514   1821  -1570       C  
ATOM   2134  CG  MET A 276      -5.831 -22.983  -1.306  1.00 73.12           C  
ANISOU 2134  CG  MET A 276     9182   7925  10677  -1498   1639  -1440       C  
ATOM   2135  SD  MET A 276      -5.598 -21.362  -2.041  1.00 74.87           S  
ANISOU 2135  SD  MET A 276     9246   8430  10771  -1416   1537  -1436       S  
ATOM   2136  CE  MET A 276      -6.398 -20.345  -0.813  1.00 67.10           C  
ANISOU 2136  CE  MET A 276     8136   7663   9697  -1372   1327  -1267       C  
ATOM   2137  N   ASN A 277      -4.825 -27.342  -2.735  1.00 86.60           N  
ANISOU 2137  N   ASN A 277    11434   8896  12575  -1545   2162  -1698       N  
ATOM   2138  CA  ASN A 277      -4.261 -28.371  -3.615  1.00 91.95           C  
ANISOU 2138  CA  ASN A 277    12244   9390  13301  -1533   2348  -1813       C  
ATOM   2139  C   ASN A 277      -3.455 -27.745  -4.754  1.00 88.85           C  
ANISOU 2139  C   ASN A 277    11764   9076  12919  -1473   2430  -1919       C  
ATOM   2140  O   ASN A 277      -3.652 -28.056  -5.931  1.00 91.58           O  
ANISOU 2140  O   ASN A 277    12181   9478  13138  -1606   2542  -2068       O  
ATOM   2141  CB  ASN A 277      -5.349 -29.307  -4.157  1.00 95.87           C  
ANISOU 2141  CB  ASN A 277    12898   9916  13613  -1780   2416  -1927       C  
ATOM   2142  CG  ASN A 277      -5.953 -30.204  -3.080  1.00101.31           C  
ANISOU 2142  CG  ASN A 277    13717  10461  14315  -1835   2387  -1832       C  
ATOM   2143  OD1 ASN A 277      -6.569 -31.224  -3.387  1.00103.01           O  
ANISOU 2143  OD1 ASN A 277    14091  10610  14438  -2000   2476  -1912       O  
ATOM   2144  ND2 ASN A 277      -5.786 -29.823  -1.817  1.00102.40           N  
ANISOU 2144  ND2 ASN A 277    13797  10553  14555  -1712   2267  -1660       N  
ATOM   2145  N   GLY A 278      -2.540 -26.844  -4.390  1.00 78.39           N  
ANISOU 2145  N   GLY A 278    10285   7760  11739  -1284   2377  -1839       N  
ATOM   2146  CA  GLY A 278      -1.616 -26.254  -5.335  1.00 74.51           C  
ANISOU 2146  CA  GLY A 278     9704   7323  11283  -1210   2467  -1923       C  
ATOM   2147  C   GLY A 278      -2.143 -25.082  -6.134  1.00 76.18           C  
ANISOU 2147  C   GLY A 278     9846   7815  11285  -1351   2408  -1999       C  
ATOM   2148  O   GLY A 278      -1.410 -24.553  -6.981  1.00 79.50           O  
ANISOU 2148  O   GLY A 278    10215   8290  11703  -1315   2491  -2070       O  
ATOM   2149  N   ARG A 279      -3.375 -24.651  -5.905  1.00 69.70           N  
ANISOU 2149  N   ARG A 279     9021   7183  10278  -1505   2264  -1979       N  
ATOM   2150  CA  ARG A 279      -3.932 -23.530  -6.643  1.00 58.85           C  
ANISOU 2150  CA  ARG A 279     7586   6083   8690  -1622   2180  -2035       C  
ATOM   2151  C   ARG A 279      -3.939 -22.276  -5.779  1.00 54.32           C  
ANISOU 2151  C   ARG A 279     6864   5624   8151  -1537   2007  -1905       C  
ATOM   2152  O   ARG A 279      -3.770 -22.325  -4.559  1.00 59.82           O  
ANISOU 2152  O   ARG A 279     7502   6238   8988  -1414   1926  -1756       O  
ATOM   2153  CB  ARG A 279      -5.342 -23.858  -7.133  1.00 63.46           C  
ANISOU 2153  CB  ARG A 279     8242   6846   9025  -1850   2126  -2111       C  
ATOM   2154  CG  ARG A 279      -5.368 -24.787  -8.325  1.00 68.34           C  
ANISOU 2154  CG  ARG A 279     9002   7416   9548  -1977   2290  -2263       C  
ATOM   2155  CD  ARG A 279      -6.688 -25.528  -8.407  1.00 70.69           C  
ANISOU 2155  CD  ARG A 279     9375   7807   9676  -2183   2251  -2313       C  
ATOM   2156  NE  ARG A 279      -7.001 -26.209  -7.152  1.00 78.15           N  
ANISOU 2156  NE  ARG A 279    10340   8615  10739  -2152   2217  -2213       N  
ATOM   2157  CZ  ARG A 279      -8.035 -27.030  -6.984  1.00 75.12           C  
ANISOU 2157  CZ  ARG A 279    10031   8257  10254  -2319   2209  -2243       C  
ATOM   2158  NH1 ARG A 279      -8.858 -27.267  -7.997  1.00 74.25           N  
ANISOU 2158  NH1 ARG A 279     9965   8316   9931  -2524   2225  -2373       N  
ATOM   2159  NH2 ARG A 279      -8.250 -27.607  -5.805  1.00 67.40           N  
ANISOU 2159  NH2 ARG A 279     9087   7143   9378  -2291   2185  -2141       N  
ATOM   2160  N   THR A 280      -4.134 -21.135  -6.435  1.00 54.81           N  
ANISOU 2160  N   THR A 280     6865   5924   8035  -1565   1926  -1912       N  
ATOM   2161  CA  THR A 280      -4.145 -19.842  -5.763  1.00 46.75           C  
ANISOU 2161  CA  THR A 280     5705   5078   6979  -1440   1743  -1742       C  
ATOM   2162  C   THR A 280      -5.444 -19.110  -6.062  1.00 46.18           C  
ANISOU 2162  C   THR A 280     5610   5286   6649  -1559   1588  -1743       C  
ATOM   2163  O   THR A 280      -6.156 -19.420  -7.019  1.00 45.34           O  
ANISOU 2163  O   THR A 280     5580   5275   6372  -1734   1616  -1881       O  
ATOM   2164  CB  THR A 280      -2.952 -18.970  -6.177  1.00 54.65           C  
ANISOU 2164  CB  THR A 280     6649   6086   8029  -1310   1788  -1716       C  
ATOM   2165  OG1 THR A 280      -2.964 -18.789  -7.598  1.00 57.08           O  
ANISOU 2165  OG1 THR A 280     7046   6473   8167  -1431   1886  -1862       O  
ATOM   2166  CG2 THR A 280      -1.646 -19.638  -5.768  1.00 59.74           C  
ANISOU 2166  CG2 THR A 280     7262   6486   8951  -1161   1921  -1706       C  
ATOM   2167  N   ILE A 281      -5.759 -18.137  -5.207  1.00 44.12           N  
ANISOU 2167  N   ILE A 281     5240   5163   6362  -1456   1417  -1589       N  
ATOM   2168  CA  ILE A 281      -6.912 -17.267  -5.392  1.00 39.00           C  
ANISOU 2168  CA  ILE A 281     4542   4786   5490  -1507   1255  -1567       C  
ATOM   2169  C   ILE A 281      -6.414 -15.840  -5.314  1.00 41.84           C  
ANISOU 2169  C   ILE A 281     4851   5235   5810  -1352   1163  -1449       C  
ATOM   2170  O   ILE A 281      -5.839 -15.438  -4.293  1.00 40.34           O  
ANISOU 2170  O   ILE A 281     4597   4974   5756  -1213   1122  -1321       O  
ATOM   2171  CB  ILE A 281      -8.003 -17.514  -4.336  1.00 40.02           C  
ANISOU 2171  CB  ILE A 281     4597   4997   5613  -1546   1148  -1508       C  
ATOM   2172  CG1 ILE A 281      -8.493 -18.965  -4.408  1.00 40.34           C  
ANISOU 2172  CG1 ILE A 281     4713   4928   5687  -1732   1256  -1629       C  
ATOM   2173  CG2 ILE A 281      -9.137 -16.530  -4.511  1.00 37.11           C  
ANISOU 2173  CG2 ILE A 281     4143   4922   5033  -1556    980  -1484       C  
ATOM   2174  CD1 ILE A 281      -9.473 -19.367  -3.281  1.00 41.44           C  
ANISOU 2174  CD1 ILE A 281     4794   5112   5839  -1800   1190  -1575       C  
ATOM   2175  N   LEU A 282      -6.623 -15.077  -6.385  1.00 42.44           N  
ANISOU 2175  N   LEU A 282     4975   5460   5691  -1385   1130  -1491       N  
ATOM   2176  CA  LEU A 282      -6.158 -13.693  -6.442  1.00 42.10           C  
ANISOU 2176  CA  LEU A 282     4928   5482   5586  -1259   1059  -1386       C  
ATOM   2177  C   LEU A 282      -4.684 -13.609  -6.057  1.00 42.47           C  
ANISOU 2177  C   LEU A 282     4960   5339   5836  -1161   1168  -1339       C  
ATOM   2178  O   LEU A 282      -4.268 -12.747  -5.282  1.00 40.25           O  
ANISOU 2178  O   LEU A 282     4624   5056   5613  -1041   1094  -1214       O  
ATOM   2179  CB  LEU A 282      -7.024 -12.790  -5.560  1.00 38.74           C  
ANISOU 2179  CB  LEU A 282     4418   5209   5093  -1161    870  -1259       C  
ATOM   2180  CG  LEU A 282      -8.440 -12.539  -6.083  1.00 38.07           C  
ANISOU 2180  CG  LEU A 282     4317   5364   4784  -1221    739  -1296       C  
ATOM   2181  CD1 LEU A 282      -9.273 -11.724  -5.094  1.00 32.82           C  
ANISOU 2181  CD1 LEU A 282     3547   4836   4087  -1100    576  -1180       C  
ATOM   2182  CD2 LEU A 282      -8.364 -11.832  -7.426  1.00 39.72           C  
ANISOU 2182  CD2 LEU A 282     4641   5664   4788  -1241    725  -1332       C  
ATOM   2183  N   GLY A 283      -3.897 -14.560  -6.567  1.00 45.94           N  
ANISOU 2183  N   GLY A 283     5440   5622   6393  -1214   1347  -1449       N  
ATOM   2184  CA  GLY A 283      -2.470 -14.584  -6.319  1.00 50.13           C  
ANISOU 2184  CA  GLY A 283     5926   5993   7129  -1119   1464  -1428       C  
ATOM   2185  C   GLY A 283      -2.048 -14.973  -4.921  1.00 53.20           C  
ANISOU 2185  C   GLY A 283     6207   6261   7746   -999   1420  -1322       C  
ATOM   2186  O   GLY A 283      -0.876 -14.791  -4.576  1.00 56.12           O  
ANISOU 2186  O   GLY A 283     6503   6541   8281   -899   1470  -1280       O  
ATOM   2187  N   SER A 284      -2.963 -15.482  -4.094  1.00 44.73           N  
ANISOU 2187  N   SER A 284     5121   5197   6678  -1012   1325  -1276       N  
ATOM   2188  CA  SER A 284      -2.644 -15.938  -2.747  1.00 43.02           C  
ANISOU 2188  CA  SER A 284     4836   4859   6650   -911   1279  -1168       C  
ATOM   2189  C   SER A 284      -2.882 -17.441  -2.627  1.00 40.47           C  
ANISOU 2189  C   SER A 284     4576   4371   6428   -970   1374  -1237       C  
ATOM   2190  O   SER A 284      -3.870 -17.972  -3.147  1.00 44.42           O  
ANISOU 2190  O   SER A 284     5152   4921   6806  -1118   1398  -1334       O  
ATOM   2191  CB  SER A 284      -3.481 -15.208  -1.702  1.00 40.96           C  
ANISOU 2191  CB  SER A 284     4528   4729   6304   -877   1098  -1039       C  
ATOM   2192  OG  SER A 284      -3.165 -15.670  -0.403  1.00 44.20           O  
ANISOU 2192  OG  SER A 284     4898   5023   6873   -795   1054   -932       O  
ATOM   2193  N   ALA A 285      -1.982 -18.123  -1.930  1.00 42.64           N  
ANISOU 2193  N   ALA A 285     4825   4450   6924   -857   1421  -1186       N  
ATOM   2194  CA  ALA A 285      -2.198 -19.522  -1.598  1.00 45.45           C  
ANISOU 2194  CA  ALA A 285     5270   4613   7387   -889   1497  -1217       C  
ATOM   2195  C   ALA A 285      -2.818 -19.703  -0.222  1.00 43.05           C  
ANISOU 2195  C   ALA A 285     4967   4297   7094   -874   1367  -1076       C  
ATOM   2196  O   ALA A 285      -2.988 -20.847   0.214  1.00 48.27           O  
ANISOU 2196  O   ALA A 285     5724   4776   7840   -901   1422  -1074       O  
ATOM   2197  CB  ALA A 285      -0.885 -20.304  -1.675  1.00 51.39           C  
ANISOU 2197  CB  ALA A 285     6018   5131   8378   -755   1634  -1243       C  
ATOM   2198  N   LEU A 286      -3.148 -18.613   0.463  1.00 44.61           N  
ANISOU 2198  N   LEU A 286     5080   4668   7200   -837   1210   -962       N  
ATOM   2199  CA  LEU A 286      -3.866 -18.631   1.729  1.00 44.18           C  
ANISOU 2199  CA  LEU A 286     5029   4644   7113   -845   1093   -841       C  
ATOM   2200  C   LEU A 286      -5.203 -17.926   1.560  1.00 40.38           C  
ANISOU 2200  C   LEU A 286     4523   4406   6414   -964   1016   -871       C  
ATOM   2201  O   LEU A 286      -5.383 -17.109   0.656  1.00 42.44           O  
ANISOU 2201  O   LEU A 286     4747   4822   6554   -984   1002   -935       O  
ATOM   2202  CB  LEU A 286      -3.083 -17.916   2.837  1.00 50.62           C  
ANISOU 2202  CB  LEU A 286     5764   5460   8011   -685    972   -680       C  
ATOM   2203  CG  LEU A 286      -1.826 -18.590   3.351  1.00 54.35           C  
ANISOU 2203  CG  LEU A 286     6226   5720   8703   -538    995   -610       C  
ATOM   2204  CD1 LEU A 286      -1.350 -17.876   4.605  1.00 57.23           C  
ANISOU 2204  CD1 LEU A 286     6518   6130   9098   -423    837   -446       C  
ATOM   2205  CD2 LEU A 286      -2.097 -20.066   3.605  1.00 56.06           C  
ANISOU 2205  CD2 LEU A 286     6579   5721   9002   -577   1078   -621       C  
ATOM   2206  N   LEU A 287      -6.138 -18.221   2.456  1.00 39.36           N  
ANISOU 2206  N   LEU A 287     4410   4312   6231  -1036    964   -819       N  
ATOM   2207  CA  LEU A 287      -7.403 -17.498   2.479  1.00 35.74           C  
ANISOU 2207  CA  LEU A 287     3888   4104   5586  -1117    880   -836       C  
ATOM   2208  C   LEU A 287      -7.180 -16.152   3.166  1.00 39.06           C  
ANISOU 2208  C   LEU A 287     4230   4640   5970   -974    752   -717       C  
ATOM   2209  O   LEU A 287      -6.882 -16.097   4.363  1.00 42.63           O  
ANISOU 2209  O   LEU A 287     4687   5027   6485   -904    698   -596       O  
ATOM   2210  CB  LEU A 287      -8.471 -18.328   3.183  1.00 34.08           C  
ANISOU 2210  CB  LEU A 287     3715   3898   5336  -1263    898   -841       C  
ATOM   2211  CG  LEU A 287      -8.774 -19.679   2.514  1.00 41.81           C  
ANISOU 2211  CG  LEU A 287     4798   4751   6336  -1439   1034   -972       C  
ATOM   2212  CD1 LEU A 287      -9.744 -20.470   3.352  1.00 48.40           C  
ANISOU 2212  CD1 LEU A 287     5682   5570   7136  -1600   1061   -961       C  
ATOM   2213  CD2 LEU A 287      -9.305 -19.497   1.089  1.00 44.19           C  
ANISOU 2213  CD2 LEU A 287     5067   5216   6507  -1550   1059  -1134       C  
ATOM   2214  N   GLU A 288      -7.333 -15.069   2.411  1.00 35.00           N  
ANISOU 2214  N   GLU A 288     3666   4290   5342   -938    704   -751       N  
ATOM   2215  CA  GLU A 288      -7.016 -13.722   2.894  1.00 33.79           C  
ANISOU 2215  CA  GLU A 288     3470   4217   5151   -806    602   -654       C  
ATOM   2216  C   GLU A 288      -8.164 -13.113   3.671  1.00 32.74           C  
ANISOU 2216  C   GLU A 288     3289   4254   4897   -803    512   -611       C  
ATOM   2217  O   GLU A 288      -9.307 -13.142   3.228  1.00 30.38           O  
ANISOU 2217  O   GLU A 288     2948   4116   4479   -880    502   -686       O  
ATOM   2218  CB  GLU A 288      -6.704 -12.793   1.733  1.00 33.57           C  
ANISOU 2218  CB  GLU A 288     3447   4269   5041   -769    600   -702       C  
ATOM   2219  CG  GLU A 288      -5.527 -13.231   0.886  1.00 42.13           C  
ANISOU 2219  CG  GLU A 288     4567   5208   6233   -771    710   -758       C  
ATOM   2220  CD  GLU A 288      -4.205 -12.721   1.427  1.00 61.15           C  
ANISOU 2220  CD  GLU A 288     6950   7514   8770   -660    699   -670       C  
ATOM   2221  OE1 GLU A 288      -4.214 -11.765   2.245  1.00 54.91           O  
ANISOU 2221  OE1 GLU A 288     6138   6783   7943   -589    597   -574       O  
ATOM   2222  OE2 GLU A 288      -3.159 -13.286   1.030  1.00 72.69           O  
ANISOU 2222  OE2 GLU A 288     8408   8841  10370   -646    797   -708       O  
ATOM   2223  N   ASP A 289      -7.854 -12.461   4.802  1.00 28.34           N  
ANISOU 2223  N   ASP A 289     2727   3680   4361   -710    442   -498       N  
ATOM   2224  CA  ASP A 289      -8.962 -11.967   5.607  1.00 32.20           C  
ANISOU 2224  CA  ASP A 289     3174   4320   4740   -708    383   -471       C  
ATOM   2225  C   ASP A 289      -8.819 -10.496   6.000  1.00 31.39           C  
ANISOU 2225  C   ASP A 289     3068   4289   4568   -576    298   -405       C  
ATOM   2226  O   ASP A 289      -9.525 -10.037   6.906  1.00 30.34           O  
ANISOU 2226  O   ASP A 289     2915   4247   4367   -549    258   -369       O  
ATOM   2227  CB  ASP A 289      -9.153 -12.847   6.845  1.00 29.99           C  
ANISOU 2227  CB  ASP A 289     2922   3959   4515   -774    404   -412       C  
ATOM   2228  CG  ASP A 289      -8.168 -12.533   7.978  1.00 31.04           C  
ANISOU 2228  CG  ASP A 289     3104   3969   4720   -683    349   -284       C  
ATOM   2229  OD1 ASP A 289      -7.084 -11.995   7.723  1.00 32.29           O  
ANISOU 2229  OD1 ASP A 289     3269   4060   4940   -594    319   -252       O  
ATOM   2230  OD2 ASP A 289      -8.478 -12.938   9.127  1.00 31.59           O  
ANISOU 2230  OD2 ASP A 289     3211   4011   4781   -723    342   -218       O  
ATOM   2231  N   GLU A 290      -7.992  -9.724   5.298  1.00 26.03           N  
ANISOU 2231  N   GLU A 290     2423   3575   3894   -505    285   -400       N  
ATOM   2232  CA  GLU A 290      -7.856  -8.297   5.582  1.00 24.87           C  
ANISOU 2232  CA  GLU A 290     2307   3472   3671   -395    217   -346       C  
ATOM   2233  C   GLU A 290      -8.493  -7.419   4.493  1.00 32.19           C  
ANISOU 2233  C   GLU A 290     3244   4527   4459   -343    191   -396       C  
ATOM   2234  O   GLU A 290      -8.061  -6.287   4.277  1.00 31.36           O  
ANISOU 2234  O   GLU A 290     3209   4402   4302   -262    160   -362       O  
ATOM   2235  CB  GLU A 290      -6.382  -7.957   5.844  1.00 32.83           C  
ANISOU 2235  CB  GLU A 290     3359   4335   4780   -363    213   -285       C  
ATOM   2236  CG  GLU A 290      -5.793  -8.831   7.012  1.00 38.18           C  
ANISOU 2236  CG  GLU A 290     4023   4899   5585   -390    207   -218       C  
ATOM   2237  CD  GLU A 290      -4.758  -8.147   7.942  1.00 44.07           C  
ANISOU 2237  CD  GLU A 290     4792   5577   6374   -342    142   -130       C  
ATOM   2238  OE1 GLU A 290      -4.048  -7.228   7.491  1.00 35.75           O  
ANISOU 2238  OE1 GLU A 290     3758   4513   5311   -314    135   -134       O  
ATOM   2239  OE2 GLU A 290      -4.623  -8.584   9.129  1.00 46.65           O  
ANISOU 2239  OE2 GLU A 290     5127   5860   6740   -349     98    -58       O  
ATOM   2240  N   PHE A 291      -9.547  -7.918   3.822  1.00 26.54           N  
ANISOU 2240  N   PHE A 291     2467   3944   3671   -393    196   -475       N  
ATOM   2241  CA  PHE A 291     -10.423  -7.075   2.997  1.00 26.11           C  
ANISOU 2241  CA  PHE A 291     2403   4053   3464   -319    135   -507       C  
ATOM   2242  C   PHE A 291     -11.843  -7.124   3.540  1.00 24.02           C  
ANISOU 2242  C   PHE A 291     2019   3976   3131   -303     94   -535       C  
ATOM   2243  O   PHE A 291     -12.465  -8.192   3.576  1.00 27.33           O  
ANISOU 2243  O   PHE A 291     2349   4463   3571   -429    130   -599       O  
ATOM   2244  CB  PHE A 291     -10.452  -7.522   1.526  1.00 28.33           C  
ANISOU 2244  CB  PHE A 291     2699   4375   3692   -394    158   -590       C  
ATOM   2245  CG  PHE A 291      -9.136  -7.437   0.841  1.00 28.46           C  
ANISOU 2245  CG  PHE A 291     2822   4234   3759   -415    220   -584       C  
ATOM   2246  CD1 PHE A 291      -8.726  -6.248   0.258  1.00 36.38           C  
ANISOU 2246  CD1 PHE A 291     3930   5220   4671   -330    191   -544       C  
ATOM   2247  CD2 PHE A 291      -8.308  -8.542   0.768  1.00 33.01           C  
ANISOU 2247  CD2 PHE A 291     3398   4672   4474   -520    318   -621       C  
ATOM   2248  CE1 PHE A 291      -7.501  -6.151  -0.396  1.00 34.76           C  
ANISOU 2248  CE1 PHE A 291     3816   4884   4509   -372    269   -549       C  
ATOM   2249  CE2 PHE A 291      -7.073  -8.449   0.119  1.00 35.62           C  
ANISOU 2249  CE2 PHE A 291     3800   4874   4862   -534    392   -629       C  
ATOM   2250  CZ  PHE A 291      -6.681  -7.244  -0.465  1.00 35.92           C  
ANISOU 2250  CZ  PHE A 291     3928   4918   4801   -472    372   -597       C  
ATOM   2251  N   THR A 292     -12.378  -5.965   3.928  1.00 27.29           N  
ANISOU 2251  N   THR A 292     2432   4475   3462   -152     30   -495       N  
ATOM   2252  CA  THR A 292     -13.781  -5.943   4.312  1.00 26.47           C  
ANISOU 2252  CA  THR A 292     2185   4581   3291   -118     -1   -538       C  
ATOM   2253  C   THR A 292     -14.651  -5.979   3.064  1.00 31.09           C  
ANISOU 2253  C   THR A 292     2684   5359   3769   -111    -63   -612       C  
ATOM   2254  O   THR A 292     -14.165  -5.730   1.954  1.00 34.75           O  
ANISOU 2254  O   THR A 292     3241   5782   4181    -97    -90   -611       O  
ATOM   2255  CB  THR A 292     -14.123  -4.688   5.117  1.00 32.69           C  
ANISOU 2255  CB  THR A 292     2995   5398   4027     64    -40   -484       C  
ATOM   2256  OG1 THR A 292     -14.132  -3.526   4.257  1.00 31.64           O  
ANISOU 2256  OG1 THR A 292     2947   5281   3795    228   -113   -458       O  
ATOM   2257  CG2 THR A 292     -13.164  -4.506   6.296  1.00 30.92           C  
ANISOU 2257  CG2 THR A 292     2882   4983   3881     52      3   -409       C  
ATOM   2258  N   PRO A 293     -15.933  -6.291   3.216  1.00 31.06           N  
ANISOU 2258  N   PRO A 293     2500   5581   3720   -132    -85   -680       N  
ATOM   2259  CA  PRO A 293     -16.847  -6.148   2.073  1.00 31.81           C  
ANISOU 2259  CA  PRO A 293     2491   5901   3694    -97   -179   -746       C  
ATOM   2260  C   PRO A 293     -16.806  -4.759   1.461  1.00 40.99           C  
ANISOU 2260  C   PRO A 293     3749   7075   4750    137   -283   -679       C  
ATOM   2261  O   PRO A 293     -16.874  -4.598   0.230  1.00 38.23           O  
ANISOU 2261  O   PRO A 293     3438   6791   4295    155   -358   -694       O  
ATOM   2262  CB  PRO A 293     -18.210  -6.461   2.703  1.00 38.30           C  
ANISOU 2262  CB  PRO A 293     3078   6972   4504   -123   -182   -817       C  
ATOM   2263  CG  PRO A 293     -17.888  -7.358   3.846  1.00 35.16           C  
ANISOU 2263  CG  PRO A 293     2692   6445   4222   -289    -56   -816       C  
ATOM   2264  CD  PRO A 293     -16.633  -6.824   4.406  1.00 33.99           C  
ANISOU 2264  CD  PRO A 293     2745   6031   4140   -207    -25   -707       C  
ATOM   2265  N   PHE A 294     -16.668  -3.731   2.298  1.00 40.71           N  
ANISOU 2265  N   PHE A 294     3782   6959   4727    313   -284   -603       N  
ATOM   2266  CA  PHE A 294     -16.610  -2.391   1.740  1.00 42.94           C  
ANISOU 2266  CA  PHE A 294     4196   7214   4907    537   -371   -533       C  
ATOM   2267  C   PHE A 294     -15.323  -2.164   0.965  1.00 37.19           C  
ANISOU 2267  C   PHE A 294     3698   6268   4164    487   -350   -479       C  
ATOM   2268  O   PHE A 294     -15.356  -1.505  -0.085  1.00 36.69           O  
ANISOU 2268  O   PHE A 294     3740   6223   3977    585   -428   -449       O  
ATOM   2269  CB  PHE A 294     -16.816  -1.369   2.845  1.00 48.11           C  
ANISOU 2269  CB  PHE A 294     4883   7822   5576    725   -360   -482       C  
ATOM   2270  CG  PHE A 294     -18.147  -1.515   3.514  1.00 67.91           C  
ANISOU 2270  CG  PHE A 294     7148  10569   8086    788   -367   -547       C  
ATOM   2271  CD1 PHE A 294     -19.307  -1.093   2.871  1.00 75.06           C  
ANISOU 2271  CD1 PHE A 294     7903  11720   8897    956   -479   -579       C  
ATOM   2272  CD2 PHE A 294     -18.254  -2.131   4.752  1.00 74.87           C  
ANISOU 2272  CD2 PHE A 294     7940  11447   9058    669   -263   -579       C  
ATOM   2273  CE1 PHE A 294     -20.541  -1.244   3.470  1.00 77.56           C  
ANISOU 2273  CE1 PHE A 294     7959  12285   9226   1009   -476   -654       C  
ATOM   2274  CE2 PHE A 294     -19.485  -2.283   5.359  1.00 76.25           C  
ANISOU 2274  CE2 PHE A 294     7886  11853   9231    704   -246   -651       C  
ATOM   2275  CZ  PHE A 294     -20.630  -1.839   4.717  1.00 77.83           C  
ANISOU 2275  CZ  PHE A 294     7908  12309   9353    873   -347   -696       C  
ATOM   2276  N   ASP A 295     -14.208  -2.756   1.408  1.00 29.59           N  
ANISOU 2276  N   ASP A 295     2809   5112   3320    331   -246   -470       N  
ATOM   2277  CA  ASP A 295     -12.981  -2.680   0.616  1.00 31.56           C  
ANISOU 2277  CA  ASP A 295     3237   5184   3571    259   -205   -442       C  
ATOM   2278  C   ASP A 295     -13.183  -3.316  -0.755  1.00 36.78           C  
ANISOU 2278  C   ASP A 295     3882   5944   4150    160   -227   -509       C  
ATOM   2279  O   ASP A 295     -12.701  -2.796  -1.772  1.00 34.22           O  
ANISOU 2279  O   ASP A 295     3712   5561   3727    180   -243   -483       O  
ATOM   2280  CB  ASP A 295     -11.825  -3.370   1.334  1.00 29.06           C  
ANISOU 2280  CB  ASP A 295     2946   4680   3414    116    -97   -435       C  
ATOM   2281  CG  ASP A 295     -11.464  -2.698   2.658  1.00 38.25           C  
ANISOU 2281  CG  ASP A 295     4157   5738   4639    190    -83   -367       C  
ATOM   2282  OD1 ASP A 295     -11.859  -1.526   2.840  1.00 39.18           O  
ANISOU 2282  OD1 ASP A 295     4346   5871   4671    353   -135   -324       O  
ATOM   2283  OD2 ASP A 295     -10.789  -3.362   3.493  1.00 35.04           O  
ANISOU 2283  OD2 ASP A 295     3726   5229   4359     87    -24   -358       O  
ATOM   2284  N   VAL A 296     -13.867  -4.465  -0.792  1.00 36.77           N  
ANISOU 2284  N   VAL A 296     3712   6084   4177     30   -219   -599       N  
ATOM   2285  CA  VAL A 296     -14.062  -5.173  -2.054  1.00 30.25           C  
ANISOU 2285  CA  VAL A 296     2875   5352   3267    -98   -232   -682       C  
ATOM   2286  C   VAL A 296     -14.921  -4.345  -2.999  1.00 41.99           C  
ANISOU 2286  C   VAL A 296     4368   7026   4559     43   -379   -668       C  
ATOM   2287  O   VAL A 296     -14.614  -4.213  -4.197  1.00 38.22           O  
ANISOU 2287  O   VAL A 296     4021   6541   3959     11   -404   -674       O  
ATOM   2288  CB  VAL A 296     -14.668  -6.567  -1.806  1.00 28.33           C  
ANISOU 2288  CB  VAL A 296     2460   5212   3092   -285   -187   -790       C  
ATOM   2289  CG1 VAL A 296     -15.093  -7.205  -3.127  1.00 31.35           C  
ANISOU 2289  CG1 VAL A 296     2825   5733   3354   -419   -220   -892       C  
ATOM   2290  CG2 VAL A 296     -13.665  -7.466  -1.094  1.00 30.77           C  
ANISOU 2290  CG2 VAL A 296     2813   5298   3581   -419    -45   -792       C  
ATOM   2291  N   VAL A 297     -16.024  -3.798  -2.480  1.00 35.81           N  
ANISOU 2291  N   VAL A 297     3446   6422   3739    205   -478   -652       N  
ATOM   2292  CA  VAL A 297     -16.904  -2.973  -3.310  1.00 44.40           C  
ANISOU 2292  CA  VAL A 297     4522   7700   4648    383   -641   -626       C  
ATOM   2293  C   VAL A 297     -16.166  -1.740  -3.817  1.00 50.15           C  
ANISOU 2293  C   VAL A 297     5522   8249   5282    538   -667   -510       C  
ATOM   2294  O   VAL A 297     -16.289  -1.357  -4.989  1.00 45.33           O  
ANISOU 2294  O   VAL A 297     5025   7699   4502    584   -762   -486       O  
ATOM   2295  CB  VAL A 297     -18.172  -2.585  -2.528  1.00 48.63           C  
ANISOU 2295  CB  VAL A 297     4836   8451   5192    556   -723   -633       C  
ATOM   2296  CG1 VAL A 297     -18.894  -1.440  -3.234  1.00 58.21           C  
ANISOU 2296  CG1 VAL A 297     6076   9801   6238    824   -897   -568       C  
ATOM   2297  CG2 VAL A 297     -19.092  -3.788  -2.397  1.00 46.87           C  
ANISOU 2297  CG2 VAL A 297     4338   8467   5004    374   -719   -763       C  
ATOM   2298  N   ARG A 298     -15.395  -1.095  -2.942  1.00 45.04           N  
ANISOU 2298  N   ARG A 298     5000   7382   4730    607   -585   -436       N  
ATOM   2299  CA  ARG A 298     -14.642   0.090  -3.337  1.00 46.18           C  
ANISOU 2299  CA  ARG A 298     5421   7333   4792    723   -587   -331       C  
ATOM   2300  C   ARG A 298     -13.672  -0.211  -4.465  1.00 45.81           C  
ANISOU 2300  C   ARG A 298     5550   7176   4681    553   -527   -341       C  
ATOM   2301  O   ARG A 298     -13.568   0.558  -5.429  1.00 48.94           O  
ANISOU 2301  O   ARG A 298     6146   7541   4910    629   -585   -279       O  
ATOM   2302  CB  ARG A 298     -13.882   0.651  -2.135  1.00 42.67           C  
ANISOU 2302  CB  ARG A 298     5065   6673   4474    759   -490   -277       C  
ATOM   2303  CG  ARG A 298     -12.999   1.862  -2.433  1.00 53.08           C  
ANISOU 2303  CG  ARG A 298     6683   7765   5719    833   -465   -180       C  
ATOM   2304  CD  ARG A 298     -11.890   2.066  -1.374  1.00 66.06           C  
ANISOU 2304  CD  ARG A 298     8406   9189   7507    752   -342   -158       C  
ATOM   2305  NE  ARG A 298     -10.696   1.229  -1.585  1.00 73.31           N  
ANISOU 2305  NE  ARG A 298     9330  10001   8525    516   -227   -199       N  
ATOM   2306  CZ  ARG A 298      -9.684   1.140  -0.719  1.00 52.29           C  
ANISOU 2306  CZ  ARG A 298     6679   7186   6001    418   -133   -193       C  
ATOM   2307  NH1 ARG A 298      -9.720   1.823   0.394  1.00 55.08           N  
ANISOU 2307  NH1 ARG A 298     7061   7472   6393    508   -139   -153       N  
ATOM   2308  NH2 ARG A 298      -8.633   0.377  -0.959  1.00 43.85           N  
ANISOU 2308  NH2 ARG A 298     5592   6038   5031    234    -36   -232       N  
ATOM   2309  N   GLN A 299     -12.946  -1.319  -4.366  1.00 36.23           N  
ANISOU 2309  N   GLN A 299     4278   5894   3594    329   -401   -417       N  
ATOM   2310  CA  GLN A 299     -11.867  -1.515  -5.317  1.00 35.03           C  
ANISOU 2310  CA  GLN A 299     4298   5606   3403    179   -306   -432       C  
ATOM   2311  C   GLN A 299     -12.364  -2.147  -6.607  1.00 41.36           C  
ANISOU 2311  C   GLN A 299     5091   6570   4056     79   -358   -507       C  
ATOM   2312  O   GLN A 299     -11.828  -1.858  -7.686  1.00 45.34           O  
ANISOU 2312  O   GLN A 299     5792   7013   4423     26   -333   -494       O  
ATOM   2313  CB  GLN A 299     -10.757  -2.373  -4.701  1.00 39.53           C  
ANISOU 2313  CB  GLN A 299     4824   6015   4181      7   -143   -480       C  
ATOM   2314  CG  GLN A 299      -9.605  -2.595  -5.674  1.00 36.65           C  
ANISOU 2314  CG  GLN A 299     4611   5519   3796   -143    -20   -512       C  
ATOM   2315  CD  GLN A 299      -8.447  -3.365  -5.076  1.00 35.02           C  
ANISOU 2315  CD  GLN A 299     4347   5153   3807   -273    134   -553       C  
ATOM   2316  OE1 GLN A 299      -7.574  -3.811  -5.807  1.00 31.11           O  
ANISOU 2316  OE1 GLN A 299     3916   4574   3329   -403    254   -609       O  
ATOM   2317  NE2 GLN A 299      -8.416  -3.503  -3.721  1.00 33.02           N  
ANISOU 2317  NE2 GLN A 299     3972   4858   3715   -229    131   -523       N  
ATOM   2318  N   CYS A 300     -13.384  -2.997  -6.514  1.00 38.10           N  
ANISOU 2318  N   CYS A 300     4460   6366   3652     35   -424   -592       N  
ATOM   2319  CA  CYS A 300     -13.883  -3.692  -7.692  1.00 40.81           C  
ANISOU 2319  CA  CYS A 300     4780   6876   3848    -93   -476   -683       C  
ATOM   2320  C   CYS A 300     -14.860  -2.840  -8.489  1.00 47.53           C  
ANISOU 2320  C   CYS A 300     5668   7926   4464     75   -678   -627       C  
ATOM   2321  O   CYS A 300     -14.964  -3.011  -9.717  1.00 53.40           O  
ANISOU 2321  O   CYS A 300     6509   8758   5022    -10   -731   -662       O  
ATOM   2322  CB  CYS A 300     -14.548  -4.993  -7.269  1.00 41.82           C  
ANISOU 2322  CB  CYS A 300     4667   7144   4080   -245   -455   -808       C  
ATOM   2323  SG  CYS A 300     -13.364  -6.224  -6.763  1.00 42.53           S  
ANISOU 2323  SG  CYS A 300     4767   6995   4399   -465   -226   -884       S  
ATOM   2324  N   SER A 301     -15.547  -1.918  -7.813  1.00 57.06           N  
ANISOU 2324  N   SER A 301     6811   9197   5673    319   -791   -539       N  
ATOM   2325  CA  SER A 301     -16.615  -1.069  -8.369  1.00 73.05           C  
ANISOU 2325  CA  SER A 301     8827  11424   7504    544  -1005   -474       C  
ATOM   2326  C   SER A 301     -17.446  -1.741  -9.466  1.00 83.90           C  
ANISOU 2326  C   SER A 301    10096  13077   8706    440  -1139   -562       C  
ATOM   2327  O   SER A 301     -17.729  -2.940  -9.405  1.00 85.19           O  
ANISOU 2327  O   SER A 301    10069  13361   8938    225  -1092   -698       O  
ATOM   2328  CB  SER A 301     -16.019   0.242  -8.895  1.00 66.43           C  
ANISOU 2328  CB  SER A 301     8316  10399   6527    705  -1031   -329       C  
ATOM   2329  OG  SER A 301     -15.366   0.929  -7.835  1.00 55.99           O  
ANISOU 2329  OG  SER A 301     7078   8842   5353    799   -924   -258       O  
TER    2330      SER A 301                                                      
HETATM 2331  C4  02J C   1       9.188  -7.702  27.844  1.00 80.64           C  
ANISOU 2331  C4  02J C   1     9442  10661  10537   -502  -2837   1538       C  
HETATM 2332  C5  02J C   1       9.652  -8.699  28.652  1.00 84.40           C  
ANISOU 2332  C5  02J C   1     9950  11119  10999   -371  -2985   1682       C  
HETATM 2333  C6  02J C   1      10.556  -8.531  29.869  1.00 81.91           C  
ANISOU 2333  C6  02J C   1     9642  10946  10535   -404  -3197   1727       C  
HETATM 2334  O1  02J C   1       9.174  -9.862  28.181  1.00 87.04           O  
ANISOU 2334  O1  02J C   1    10317  11285  11469   -209  -2911   1775       O  
HETATM 2335  N2  02J C   1       8.402  -9.592  27.062  1.00 80.95           N  
ANISOU 2335  N2  02J C   1     9515  10440  10800   -240  -2723   1687       N  
HETATM 2336  C3  02J C   1       8.413  -8.273  26.862  1.00 76.61           C  
ANISOU 2336  C3  02J C   1     8931  10005  10171   -410  -2659   1532       C  
HETATM 2337  C41 02J C   1       7.689  -7.531  25.740  1.00 64.96           C  
ANISOU 2337  C41 02J C   1     7456   8487   8739   -480  -2377   1350       C  
HETATM 2338  O42 02J C   1       8.006  -7.702  24.531  1.00 70.77           O1-
ANISOU 2338  O42 02J C   1     7995   9188   9704   -394  -2255   1273       O1-
ATOM   2339  N   ALA C   2       6.698  -6.708  26.360  1.00 54.61           N  
ANISOU 2339  N   ALA C   2     6401   7183   7165   -638  -2297   1299       N  
ATOM   2340  CA  ALA C   2       6.327  -5.633  25.437  1.00 48.12           C  
ANISOU 2340  CA  ALA C   2     5558   6366   6359   -720  -2097   1122       C  
ATOM   2341  C   ALA C   2       7.466  -4.614  25.236  1.00 50.31           C  
ANISOU 2341  C   ALA C   2     5666   6769   6680   -824  -2184   1031       C  
ATOM   2342  O   ALA C   2       8.263  -4.337  26.142  1.00 49.26           O  
ANISOU 2342  O   ALA C   2     5507   6752   6457   -908  -2398   1076       O  
ATOM   2343  CB  ALA C   2       5.074  -4.937  25.938  1.00 37.81           C  
ANISOU 2343  CB  ALA C   2     4521   5035   4810   -831  -1966   1064       C  
ATOM   2344  N   VAL C   3       7.541  -4.061  24.030  1.00 46.32           N  
ANISOU 2344  N   VAL C   3     5051   6245   6304   -834  -2016    902       N  
ATOM   2345  CA  VAL C   3       8.565  -3.095  23.658  1.00 43.11           C  
ANISOU 2345  CA  VAL C   3     4490   5940   5952   -954  -2049    799       C  
ATOM   2346  C   VAL C   3       7.859  -1.854  23.142  1.00 47.73           C  
ANISOU 2346  C   VAL C   3     5241   6471   6422  -1072  -1850    659       C  
ATOM   2347  O   VAL C   3       7.166  -1.917  22.119  1.00 40.62           O  
ANISOU 2347  O   VAL C   3     4363   5477   5596   -996  -1653    605       O  
ATOM   2348  CB  VAL C   3       9.511  -3.655  22.584  1.00 51.76           C  
ANISOU 2348  CB  VAL C   3     5278   7056   7333   -849  -2026    780       C  
ATOM   2349  CG1 VAL C   3      10.412  -2.572  22.038  1.00 54.94           C  
ANISOU 2349  CG1 VAL C   3     5539   7554   7782  -1005  -1996    649       C  
ATOM   2350  CG2 VAL C   3      10.326  -4.801  23.143  1.00 56.14           C  
ANISOU 2350  CG2 VAL C   3     5656   7665   8009   -710  -2241    919       C  
ATOM   2351  N   LEU C   4       8.031  -0.726  23.834  1.00 41.80           N  
ANISOU 2351  N   LEU C   4     4621   5776   5487  -1254  -1906    598       N  
ATOM   2352  CA  LEU C   4       7.494   0.541  23.338  1.00 39.64           C  
ANISOU 2352  CA  LEU C   4     4517   5432   5112  -1358  -1723    464       C  
ATOM   2353  C   LEU C   4       8.301   0.988  22.123  1.00 40.50           C  
ANISOU 2353  C   LEU C   4     4447   5550   5390  -1404  -1633    372       C  
ATOM   2354  O   LEU C   4       9.536   1.042  22.174  1.00 45.22           O  
ANISOU 2354  O   LEU C   4     4838   6263   6079  -1493  -1756    360       O  
ATOM   2355  CB  LEU C   4       7.532   1.623  24.423  1.00 44.10           C  
ANISOU 2355  CB  LEU C   4     5291   6033   5433  -1552  -1798    413       C  
ATOM   2356  CG  LEU C   4       6.731   1.311  25.689  1.00 43.38           C  
ANISOU 2356  CG  LEU C   4     5409   5938   5135  -1540  -1867    488       C  
ATOM   2357  CD1 LEU C   4       6.967   2.399  26.723  1.00 43.96           C  
ANISOU 2357  CD1 LEU C   4     5675   6057   4971  -1754  -1947    421       C  
ATOM   2358  CD2 LEU C   4       5.243   1.155  25.395  1.00 48.75           C  
ANISOU 2358  CD2 LEU C   4     6258   6499   5767  -1412  -1664    479       C  
HETATM 2359  C19 PJE C   5       8.069   1.783  19.918  1.00 40.14           C  
ANISOU 2359  C19 PJE C   5     4392   5375   5485  -1393  -1302    223       C  
HETATM 2360  C20 PJE C   5       7.974   3.290  19.645  1.00 44.69           C  
ANISOU 2360  C20 PJE C   5     5174   5883   5924  -1556  -1184    109       C  
HETATM 2361  C21 PJE C   5       9.170   3.810  19.905  1.00 60.77           C  
ANISOU 2361  C21 PJE C   5     7103   8012   7972  -1746  -1276     62       C  
HETATM 2362  C22 PJE C   5       9.588   5.268  19.777  1.00 79.15           C  
ANISOU 2362  C22 PJE C   5     9587  10300  10186  -1981  -1202    -56       C  
HETATM 2363  C25 PJE C   5       7.591   0.955  18.728  1.00 31.67           C  
ANISOU 2363  C25 PJE C   5     3227   4236   4570  -1218  -1161    235       C  
HETATM 2364  C26 PJE C   5       8.203  -0.439  18.764  1.00 32.88           C  
ANISOU 2364  C26 PJE C   5     3126   4452   4916  -1094  -1266    321       C  
HETATM 2365  C27 PJE C   5       9.679  -0.349  18.544  1.00 37.13           C  
ANISOU 2365  C27 PJE C   5     3406   5101   5599  -1182  -1340    286       C  
HETATM 2366  C28 PJE C   5      10.017  -1.695  17.867  1.00 44.94           C  
ANISOU 2366  C28 PJE C   5     4160   6087   6827   -998  -1321    331       C  
HETATM 2367  N6  PJE C   5       8.800  -2.016  17.076  1.00 42.63           N  
ANISOU 2367  N6  PJE C   5     4019   5662   6517   -889  -1142    321       N  
HETATM 2368  C29 PJE C   5       7.701  -1.269  17.588  1.00 36.51           C  
ANISOU 2368  C29 PJE C   5     3522   4833   5519   -940  -1114    317       C  
HETATM 2369  O8  PJE C   5       6.584  -1.309  17.187  1.00 35.97           O  
ANISOU 2369  O8  PJE C   5     3600   4681   5386   -872   -995    307       O  
HETATM 2370  N5  PJE C   5       7.358   1.396  21.130  1.00 37.15           N  
ANISOU 2370  N5  PJE C   5     4153   4999   4962  -1345  -1406    304       N  
HETATM 2371  O7  PJE C   5       9.137   5.934  18.804  1.00 69.70           O  
ANISOU 2371  O7  PJE C   5     8541   8972   8971  -1977  -1010   -116       O  
HETATM 2372  C   010 C   6      12.002   4.651  20.652  1.00116.08           C  
ANISOU 2372  C   010 C   6    13756  15311  15037  -2153  -1518    -45       C  
HETATM 2373  O   010 C   6      10.958   5.240  19.914  1.00103.75           O  
ANISOU 2373  O   010 C   6    12453  13568  13400  -2138  -1320    -83       O  
HETATM 2374  C1  010 C   6      14.397   4.987  21.384  1.00133.98           C  
ANISOU 2374  C1  010 C   6    15663  17853  17391  -2324  -1685   -144       C  
HETATM 2375  C2  010 C   6      15.596   5.688  21.412  1.00137.96           C  
ANISOU 2375  C2  010 C   6    16042  18453  17923  -2493  -1688   -253       C  
HETATM 2376  C3  010 C   6      15.721   6.876  20.711  1.00139.29           C  
ANISOU 2376  C3  010 C   6    16359  18520  18046  -2678  -1499   -364       C  
HETATM 2377  C4  010 C   6      14.643   7.355  19.984  1.00136.72           C  
ANISOU 2377  C4  010 C   6    16311  17998  17638  -2675  -1314   -368       C  
HETATM 2378  C5  010 C   6      13.443   6.651  19.956  1.00132.36           C  
ANISOU 2378  C5  010 C   6    15862  17365  17063  -2502  -1322   -272       C  
HETATM 2379  C6  010 C   6      13.311   5.459  20.658  1.00128.70           C  
ANISOU 2379  C6  010 C   6    15246  17002  16653  -2334  -1506   -159       C  
TER    2380      010 C   6                                                      
HETATM 2381  O   HOH A 501     -21.636 -18.198 -11.031  1.00 62.86           O  
ANISOU 2381  O   HOH A 501     6564  10837   6485  -2813     37  -2284       O  
HETATM 2382  O   HOH A 502      -3.369 -11.257  26.394  1.00 66.07           O  
ANISOU 2382  O   HOH A 502     8993   8040   8073   -828   -918   1283       O  
HETATM 2383  O   HOH A 503      -8.754   0.350   1.751  1.00 53.68           O  
ANISOU 2383  O   HOH A 503     6677   7243   6478    289    -40   -204       O  
HETATM 2384  O   HOH A 504      -3.425  -7.020   5.362  1.00 61.01           O  
ANISOU 2384  O   HOH A 504     6962   7698   8520   -339    244   -241       O  
HETATM 2385  O   HOH A 505     -25.752 -19.402  -5.722  1.00 61.31           O  
ANISOU 2385  O   HOH A 505     5666  11002   6628  -2877    193  -2233       O  
HETATM 2386  O   HOH A 506      -5.372 -10.498   3.686  1.00 37.52           O  
ANISOU 2386  O   HOH A 506     3924   4745   5586   -524    425   -454       O  
HETATM 2387  O   HOH A 507     -16.503  -4.384 -10.642  1.00 85.06           O  
ANISOU 2387  O   HOH A 507    10250  13193   8876   -207   -889   -849       O  
HETATM 2388  O   HOH A 508       8.773   6.434  36.534  1.00 63.60           O  
ANISOU 2388  O   HOH A 508     9493   8965   5709  -2953  -2584    234       O  
HETATM 2389  O   HOH A 509      -4.346 -29.119  -0.178  1.00 74.63           O  
ANISOU 2389  O   HOH A 509    10161   6850  11346  -1333   2130  -1389       O  
HETATM 2390  O   HOH A 510      -7.720 -24.674   3.116  1.00 78.21           O  
ANISOU 2390  O   HOH A 510    10036   8338  11342  -1626   1471  -1018       O  
HETATM 2391  O   HOH A 511     -29.761 -13.163   4.711  1.00 66.45           O  
ANISOU 2391  O   HOH A 511     5259  12211   7780  -1510    231  -1716       O  
HETATM 2392  O   HOH A 512       8.976  23.370  19.875  1.00 66.10           O  
ANISOU 2392  O   HOH A 512    12163   6479   6473  -3498    543   -967       O  
HETATM 2393  O   HOH A 513      -7.712 -20.163   6.599  1.00 53.45           O  
ANISOU 2393  O   HOH A 513     6415   5857   8035  -1197    896   -502       O  
HETATM 2394  O   HOH A 514     -21.405  -7.217  12.404  1.00 66.94           O  
ANISOU 2394  O   HOH A 514     6403  10774   8258   -421    514   -842       O  
HETATM 2395  O   HOH A 515      10.709  11.799  32.217  1.00 54.59           O  
ANISOU 2395  O   HOH A 515     8349   7446   4949  -3484  -1917   -431       O  
HETATM 2396  O   HOH A 516       8.420   1.079   9.017  1.00 45.28           O  
ANISOU 2396  O   HOH A 516     4671   5681   6852  -1176      5   -201       O  
HETATM 2397  O   HOH A 517      -2.018 -26.629  -1.958  1.00 74.88           O  
ANISOU 2397  O   HOH A 517     9752   7131  11569  -1011   2170  -1524       O  
HETATM 2398  O   HOH A 518     -15.310  -4.067  20.052  1.00 35.74           O  
ANISOU 2398  O   HOH A 518     3966   5582   4031   -350    528   -246       O  
HETATM 2399  O   HOH A 519     -19.484 -34.706  -6.866  1.00 82.41           O  
ANISOU 2399  O   HOH A 519    11389  10095   9828  -4699   2423  -2972       O  
HETATM 2400  O   HOH A 520     -15.967 -19.969  15.608  1.00 56.26           O  
ANISOU 2400  O   HOH A 520     6875   7148   7352  -2283   1108   -219       O  
HETATM 2401  O   HOH A 521     -17.299   1.547  -6.310  1.00 68.62           O  
ANISOU 2401  O   HOH A 521     8303  10715   7053   1186  -1100   -240       O  
HETATM 2402  O   HOH A 522     -10.405  17.442   3.704  1.00 50.19           O  
ANISOU 2402  O   HOH A 522     9745   4569   4756   2190     64    407       O  
HETATM 2403  O   HOH A 523     -15.734  -1.565   6.417  1.00 50.00           O  
ANISOU 2403  O   HOH A 523     5212   7749   6037    585   -127   -429       O  
HETATM 2404  O   HOH A 524     -26.551 -14.263  13.385  1.00 55.95           O  
ANISOU 2404  O   HOH A 524     4830   9704   6725  -1874   1012  -1268       O  
HETATM 2405  O   HOH A 525     -13.459  -1.159   5.057  1.00 38.96           O  
ANISOU 2405  O   HOH A 525     4142   6006   4656    508   -143   -334       O  
HETATM 2406  O   HOH A 526       2.525  19.214  33.848  1.00 59.73           O  
ANISOU 2406  O   HOH A 526    11722   6384   4588  -3086   -137  -1160       O  
HETATM 2407  O   HOH A 527     -10.578  20.263   9.592  1.00 59.49           O  
ANISOU 2407  O   HOH A 527    11352   5265   5986   2146    487     24       O  
HETATM 2408  O   HOH A 528      -9.821   0.501   4.827  1.00 33.69           O  
ANISOU 2408  O   HOH A 528     3989   4771   4042    410    -73   -185       O  
HETATM 2409  O   HOH A 529       2.664 -11.696  21.964  1.00 52.68           O  
ANISOU 2409  O   HOH A 529     6256   6212   7549   -177  -1332   1242       O  
HETATM 2410  O   HOH A 530      -3.370  -6.632  10.793  1.00 30.45           O  
ANISOU 2410  O   HOH A 530     3148   3796   4624   -297    -56     61       O  
HETATM 2411  O   HOH A 531     -10.001  -4.302 -10.424  1.00 50.76           O  
ANISOU 2411  O   HOH A 531     6678   7591   5019   -582     19   -790       O  
HETATM 2412  O   HOH A 532      11.279  17.345  17.967  1.00 57.15           O  
ANISOU 2412  O   HOH A 532     9085   6368   6261  -3386    -22   -794       O  
HETATM 2413  O   HOH A 533     -13.974   9.582  18.521  1.00 48.73           O  
ANISOU 2413  O   HOH A 533     7133   6163   5219   1284    545   -536       O  
HETATM 2414  O   HOH A 534     -15.724  -5.425  11.990  1.00 43.01           O  
ANISOU 2414  O   HOH A 534     4217   6752   5374   -125    244   -424       O  
HETATM 2415  O   HOH A 535     -16.532 -14.651 -12.580  1.00 48.68           O  
ANISOU 2415  O   HOH A 535     5455   8446   4595  -2260     29  -2066       O  
HETATM 2416  O   HOH A 536      -1.662  20.312  32.184  1.00 77.17           O  
ANISOU 2416  O   HOH A 536    14336   8041   6946  -2107    521  -1282       O  
HETATM 2417  O   HOH A 537      -7.896  13.083  21.688  1.00 42.94           O  
ANISOU 2417  O   HOH A 537     7796   4463   4056    211    463   -595       O  
HETATM 2418  O   HOH A 538      -1.600  -6.178  29.131  1.00 54.17           O  
ANISOU 2418  O   HOH A 538     7687   6936   5961  -1053  -1305   1116       O  
HETATM 2419  O   HOH A 539       4.261  24.699  31.411  1.00 76.24           O  
ANISOU 2419  O   HOH A 539    14695   7625   6646  -3464    441  -1382       O  
HETATM 2420  O   HOH A 540      -2.704  17.661   4.949  1.00 48.16           O  
ANISOU 2420  O   HOH A 540     9886   3759   4653    104    595    165       O  
HETATM 2421  O   HOH A 541      13.450  -2.434  19.130  1.00 73.08           O  
ANISOU 2421  O   HOH A 541     7081  10040  10645   -997  -1727    368       O  
HETATM 2422  O   HOH A 542     -16.222   1.884  18.535  1.00 41.90           O  
ANISOU 2422  O   HOH A 542     4891   6342   4686    583    515   -474       O  
HETATM 2423  O   HOH A 543     -15.845 -10.737  12.236  1.00 44.71           O  
ANISOU 2423  O   HOH A 543     4410   6800   5777   -900    470   -458       O  
HETATM 2424  O   HOH A 544      -1.602  28.674  10.557  1.00 76.09           O  
ANISOU 2424  O   HOH A 544    15958   5762   7191   -331   1344   -166       O  
HETATM 2425  O   HOH A 545       1.419   8.500  10.533  1.00 35.71           O  
ANISOU 2425  O   HOH A 545     5519   3756   4293   -835     96   -124       O  
HETATM 2426  O   HOH A 546       9.306   1.875   6.458  1.00 53.00           O  
ANISOU 2426  O   HOH A 546     5700   6610   7828  -1380    363   -354       O  
HETATM 2427  O   HOH A 547     -21.525  -6.723   0.243  1.00 49.89           O  
ANISOU 2427  O   HOH A 547     4068   9226   5661   -123   -462  -1045       O  
HETATM 2428  O   HOH A 548     -20.640 -22.271  -3.846  1.00 56.39           O  
ANISOU 2428  O   HOH A 548     6057   8789   6579  -2992    835  -2097       O  
HETATM 2429  O   HOH A 549      -9.910 -19.571  19.151  1.00 61.83           O  
ANISOU 2429  O   HOH A 549     8308   6918   8267  -1465    491    653       O  
HETATM 2430  O   HOH A 550     -15.224  -6.912   8.528  1.00 37.91           O  
ANISOU 2430  O   HOH A 550     3467   6114   4823   -261    157   -510       O  
HETATM 2431  O   HOH A 551      -8.157  -3.607   2.926  1.00 33.30           O  
ANISOU 2431  O   HOH A 551     3662   4697   4293    -69     85   -326       O  
HETATM 2432  O   HOH A 552       9.614  -1.715   9.210  1.00 46.91           O  
ANISOU 2432  O   HOH A 552     4317   6007   7501   -946    -80   -167       O  
HETATM 2433  O   HOH A 553     -18.614   0.511  17.559  1.00 44.37           O  
ANISOU 2433  O   HOH A 553     4656   7125   5077    621    603   -607       O  
HETATM 2434  O   HOH A 554      -3.746  -2.674  20.272  1.00 33.79           O  
ANISOU 2434  O   HOH A 554     4298   4343   4199   -524   -491    355       O  
HETATM 2435  O   HOH A 555      10.679   9.286  15.425  1.00 46.11           O  
ANISOU 2435  O   HOH A 555     5881   5686   5951  -2531   -443   -422       O  
HETATM 2436  O   HOH A 556     -13.426  -1.496  19.277  1.00 34.55           O  
ANISOU 2436  O   HOH A 556     4060   5172   3897    -53    331   -203       O  
HETATM 2437  O   HOH A 557      -6.187  -1.866  27.606  1.00 36.71           O  
ANISOU 2437  O   HOH A 557     5547   4889   3511   -960   -429    412       O  
HETATM 2438  O   HOH A 558      -0.943 -10.304  28.252  1.00 58.87           O  
ANISOU 2438  O   HOH A 558     8159   7212   6995   -806  -1419   1486       O  
HETATM 2439  O   HOH A 559      -8.440   5.944  31.185  1.00 45.94           O  
ANISOU 2439  O   HOH A 559     7883   5908   3664   -989    231   -385       O  
HETATM 2440  O   HOH A 560      -7.549 -19.016  12.281  1.00 56.33           O  
ANISOU 2440  O   HOH A 560     6942   6217   8244  -1015    535    111       O  
HETATM 2441  O   HOH A 561     -16.721   2.080  15.072  1.00 50.00           O  
ANISOU 2441  O   HOH A 561     5649   7492   5857    883    326   -466       O  
HETATM 2442  O   HOH A 562     -12.850  -9.673  18.739  1.00 39.14           O  
ANISOU 2442  O   HOH A 562     4478   5530   4863   -877    376     66       O  
HETATM 2443  O   HOH A 563      -2.597 -12.650  14.885  1.00 59.38           O  
ANISOU 2443  O   HOH A 563     6956   6996   8609   -352   -207    481       O  
HETATM 2444  O   HOH A 564      -6.919  19.076  17.034  1.00 53.64           O  
ANISOU 2444  O   HOH A 564    10599   4530   5251    648    733   -555       O  
HETATM 2445  O   HOH A 565     -11.857   6.829  27.498  1.00 37.08           O  
ANISOU 2445  O   HOH A 565     6207   4846   3036   -141    672   -592       O  
HETATM 2446  O   HOH A 566       3.491  -7.665  12.569  1.00 49.28           O  
ANISOU 2446  O   HOH A 566     5079   5980   7665   -249   -400    290       O  
HETATM 2447  O   HOH A 567      -7.760   4.199  28.283  1.00 35.00           O  
ANISOU 2447  O   HOH A 567     5909   4560   2831   -789     19   -165       O  
HETATM 2448  O   HOH A 568       1.351  -5.249  32.515  1.00 58.21           O  
ANISOU 2448  O   HOH A 568     8490   7649   5978  -1326  -2039   1361       O  
HETATM 2449  O   HOH A 569      -2.852  16.156  32.037  1.00 48.27           O  
ANISOU 2449  O   HOH A 569     9953   4975   3412  -1824    237  -1075       O  
HETATM 2450  O   HOH A 570       2.358   5.552  25.353  1.00 40.95           O  
ANISOU 2450  O   HOH A 570     6157   5169   4236  -1541  -1066     54       O  
HETATM 2451  O   HOH A 571     -10.253  -9.965  21.650  1.00 37.84           O  
ANISOU 2451  O   HOH A 571     4784   5008   4587   -933    129    421       O  
HETATM 2452  O   HOH A 572     -18.717 -13.052  14.910  1.00 56.62           O  
ANISOU 2452  O   HOH A 572     5834   8568   7113  -1511    851   -568       O  
HETATM 2453  O   HOH A 573      -1.031  -2.268   1.609  1.00 47.40           O  
ANISOU 2453  O   HOH A 573     5662   5900   6449   -435    430   -309       O  
HETATM 2454  O   HOH A 574       4.603  11.932  -0.759  1.00 46.33           O  
ANISOU 2454  O   HOH A 574     8149   4431   5024  -1590   1130   -107       O  
HETATM 2455  O   HOH A 575     -10.348 -10.517   2.998  1.00 30.15           O  
ANISOU 2455  O   HOH A 575     2840   4423   4193   -673    317   -640       O  
HETATM 2456  O   HOH A 576      -9.714   7.545  17.218  1.00 33.20           O  
ANISOU 2456  O   HOH A 576     5114   4036   3463    546    198   -273       O  
HETATM 2457  O   HOH A 577      -5.825   2.537  27.249  1.00 34.93           O  
ANISOU 2457  O   HOH A 577     5611   4551   3108   -880   -311     69       O  
HETATM 2458  O   HOH A 578      -5.437  -9.796  22.980  1.00 36.23           O  
ANISOU 2458  O   HOH A 578     4784   4449   4531   -755   -463    813       O  
HETATM 2459  O   HOH A 579      -1.960 -23.431  -0.415  1.00 59.09           O  
ANISOU 2459  O   HOH A 579     7332   5602   9516   -860   1750  -1233       O  
HETATM 2460  O   HOH A 580      -4.233   0.751  28.623  1.00 39.22           O  
ANISOU 2460  O   HOH A 580     6146   5150   3605  -1113   -642    317       O  
HETATM 2461  O   HOH A 581     -10.945   5.009  10.374  1.00 35.34           O  
ANISOU 2461  O   HOH A 581     4696   4700   4030    849     -1   -148       O  
HETATM 2462  O   HOH A 582      -1.685 -11.457  17.172  1.00 44.05           O  
ANISOU 2462  O   HOH A 582     5096   5131   6511   -337   -469    662       O  
HETATM 2463  O   HOH A 583       0.930   1.967  31.754  1.00 55.82           O  
ANISOU 2463  O   HOH A 583     8500   7399   5310  -1743  -1537    482       O  
HETATM 2464  O   HOH A 584     -16.762 -12.719  10.515  1.00 39.70           O  
ANISOU 2464  O   HOH A 584     3637   6261   5187  -1213    555   -636       O  
HETATM 2465  O   HOH A 585      13.040   8.663  17.071  1.00 51.61           O  
ANISOU 2465  O   HOH A 585     6024   6778   6809  -2684   -760   -445       O  
HETATM 2466  O   HOH A 586     -12.678  -1.924  21.840  1.00 44.59           O  
ANISOU 2466  O   HOH A 586     5611   6341   4992   -304    339   -108       O  
HETATM 2467  O   HOH A 587       0.418 -22.372  -7.468  1.00 78.34           O  
ANISOU 2467  O   HOH A 587     9802   8304  11659  -1111   2508  -2054       O  
HETATM 2468  O   HOH A 588      -5.745 -20.178   4.547  1.00 56.88           O  
ANISOU 2468  O   HOH A 588     6809   6126   8676  -1009    999   -638       O  
HETATM 2469  O   HOH A 589      -0.676  23.040  30.155  1.00 64.69           O  
ANISOU 2469  O   HOH A 589    13169   5952   5458  -2153    735  -1299       O  
HETATM 2470  O   HOH A 590      -9.903 -14.145  18.855  1.00 63.51           O  
ANISOU 2470  O   HOH A 590     7947   7885   8299  -1073    247    435       O  
HETATM 2471  O   HOH A 591       1.702  22.057   7.566  1.00 69.56           O  
ANISOU 2471  O   HOH A 591    13373   5986   7069  -1125   1005   -142       O  
HETATM 2472  O   HOH A 592      -1.937   1.833  29.578  1.00 40.98           O  
ANISOU 2472  O   HOH A 592     6503   5369   3698  -1352   -966    338       O  
HETATM 2473  O   HOH A 593     -14.097  13.219  15.941  1.00 47.80           O  
ANISOU 2473  O   HOH A 593     7650   5497   5014   1939    533   -483       O  
HETATM 2474  O   HOH A 594      -5.350 -11.659  -2.750  1.00 40.91           O  
ANISOU 2474  O   HOH A 594     4556   5260   5726   -855    798   -958       O  
HETATM 2475  O   HOH A 595      -6.823  10.586  31.242  1.00 48.66           O  
ANISOU 2475  O   HOH A 595     8984   5747   3759  -1083    306   -744       O  
HETATM 2476  O   HOH A 596     -12.715  -0.538   7.690  1.00 41.91           O  
ANISOU 2476  O   HOH A 596     4639   6177   5107    499    -60   -270       O  
HETATM 2477  O   HOH A 597      -9.662  -2.425  -1.291  1.00 37.97           O  
ANISOU 2477  O   HOH A 597     4465   5554   4406     38    -23   -403       O  
HETATM 2478  O   HOH A 598     -10.539  -3.372  22.930  1.00 35.28           O  
ANISOU 2478  O   HOH A 598     4621   4951   3833   -559    125    125       O  
HETATM 2479  O   HOH A 599       7.892  17.098  10.334  1.00 55.52           O  
ANISOU 2479  O   HOH A 599     9499   5442   6153  -2516    673   -494       O  
HETATM 2480  O   HOH A 600     -15.713   0.021  13.130  1.00 41.44           O  
ANISOU 2480  O   HOH A 600     4407   6411   4927    608    187   -388       O  
HETATM 2481  O   HOH A 601     -12.664  18.569  10.516  1.00 52.17           O  
ANISOU 2481  O   HOH A 601     9738   4847   5237   2553    407    -77       O  
HETATM 2482  O   HOH A 602     -16.524   8.686  15.814  1.00 50.99           O  
ANISOU 2482  O   HOH A 602     6786   6914   5674   1783    449   -525       O  
HETATM 2483  O   HOH A 603      -9.827  -2.074  25.329  1.00 38.05           O  
ANISOU 2483  O   HOH A 603     5343   5244   3870   -678     71    149       O  
HETATM 2484  O   HOH A 604      -4.810 -13.865   8.375  1.00 53.16           O  
ANISOU 2484  O   HOH A 604     5979   6303   7916   -539    349   -134       O  
HETATM 2485  O   HOH A 605      -7.489  -2.877   0.356  1.00 30.41           O  
ANISOU 2485  O   HOH A 605     3493   4298   3762    -97    129   -364       O  
HETATM 2486  O   HOH A 606     -15.079   0.623  22.617  1.00 31.80           O  
ANISOU 2486  O   HOH A 606     4009   4925   3151     19    631   -384       O  
HETATM 2487  O   HOH A 607     -12.319  -4.085 -15.252  1.00 63.69           O  
ANISOU 2487  O   HOH A 607     8755   9861   5585   -759   -409   -884       O  
HETATM 2488  O   HOH A 608       0.000 -16.827   0.000  0.50 43.41           O  
ANISOU 2488  O   HOH A 608     4682   4525   7287      0   1236      0       O  
HETATM 2489  O   HOH A 609       3.544  28.698  27.977  1.00 85.48           O  
ANISOU 2489  O   HOH A 609    16802   7839   7837  -3140   1102  -1367       O  
HETATM 2490  O   HOH A 610     -17.234  -4.860   7.422  1.00 54.21           O  
ANISOU 2490  O   HOH A 610     5316   8589   6692    107     25   -599       O  
HETATM 2491  O   HOH A 611       5.756  28.245  28.172  1.00 81.20           O  
ANISOU 2491  O   HOH A 611    15936   7631   7286  -3694    890  -1394       O  
HETATM 2492  O   HOH A 612      -7.453 -32.589  -0.294  1.00 81.72           O  
ANISOU 2492  O   HOH A 612    11648   7577  11825  -2022   2351  -1576       O  
HETATM 2493  O   HOH A 613       0.158 -12.571  18.089  1.00 57.89           O  
ANISOU 2493  O   HOH A 613     6827   6732   8439   -208   -680    858       O  
HETATM 2494  O   HOH A 614     -18.566 -20.412  14.912  1.00 59.55           O  
ANISOU 2494  O   HOH A 614     7039   7984   7606  -2485   1220   -505       O  
HETATM 2495  O   HOH A 615       0.511  24.944  30.589  1.00 66.51           O  
ANISOU 2495  O   HOH A 615    13782   5963   5527  -2520    836  -1377       O  
HETATM 2496  O   HOH A 616      -5.164  -9.730  -9.375  1.00 46.97           O  
ANISOU 2496  O   HOH A 616     5909   6327   5609  -1179    997  -1277       O  
HETATM 2497  O   HOH A 617      -9.430  -5.730  26.528  1.00 40.82           O  
ANISOU 2497  O   HOH A 617     5763   5513   4233   -983    -30    459       O  
HETATM 2498  O   HOH A 618     -13.340   2.548   4.802  1.00 52.72           O  
ANISOU 2498  O   HOH A 618     6345   7515   6171    987   -225   -198       O  
HETATM 2499  O   HOH A 619      -1.877 -15.024  18.844  1.00 66.02           O  
ANISOU 2499  O   HOH A 619     8204   7524   9358   -339   -503    961       O  
HETATM 2500  O   HOH A 620      10.635  17.388  11.547  1.00 68.33           O  
ANISOU 2500  O   HOH A 620    10709   7388   7866  -3047    604   -648       O  
HETATM 2501  O   HOH A 621      -1.621   1.769  32.215  1.00 48.14           O  
ANISOU 2501  O   HOH A 621     7767   6368   4156  -1632  -1146    408       O  
HETATM 2502  O   HOH A 622      -4.628 -12.142   5.489  1.00 48.07           O  
ANISOU 2502  O   HOH A 622     5248   5857   7158   -522    425   -343       O  
HETATM 2503  O   HOH A 623     -15.983  -0.069  20.138  1.00 35.19           O  
ANISOU 2503  O   HOH A 623     4036   5532   3803    184    579   -417       O  
HETATM 2504  O   HOH A 624     -25.825  -8.562 -11.297  1.00 82.81           O  
ANISOU 2504  O   HOH A 624     8158  14799   8508   -732  -1498  -1457       O  
HETATM 2505  O   HOH A 625       0.000  -0.007   0.000  0.50 42.92           O  
ANISOU 2505  O   HOH A 625     5431   5227   5649      0    561      0       O  
HETATM 2506  O   HOH A 626     -12.696  -5.454 -10.621  1.00 54.33           O  
ANISOU 2506  O   HOH A 626     6780   8543   5319   -601   -278   -919       O  
HETATM 2507  O   HOH A 627     -13.031 -19.490  16.895  1.00 66.61           O  
ANISOU 2507  O   HOH A 627     8503   8008   8796  -1853    838    162       O  
HETATM 2508  O   HOH A 628     -25.742 -10.819 -11.792  1.00 78.53           O  
ANISOU 2508  O   HOH A 628     7646  14221   7969  -1300  -1282  -1695       O  
HETATM 2509  O   HOH A 629     -27.840 -14.148  -0.152  1.00 57.79           O  
ANISOU 2509  O   HOH A 629     4452  11010   6493  -1687    -51  -1773       O  
HETATM 2510  O   HOH A 630       8.720  -7.819  32.342  1.00 78.42           O  
ANISOU 2510  O   HOH A 630     9901  10484   9410   -745  -3222   1810       O  
HETATM 2511  O   HOH A 631       0.618  17.325  34.862  1.00 57.51           O  
ANISOU 2511  O   HOH A 631    11320   6291   4242  -2766   -142  -1093       O  
HETATM 2512  O   HOH A 632     -12.584 -21.370  17.883  1.00 72.15           O  
ANISOU 2512  O   HOH A 632     9606   8297   9512  -2003    910    344       O  
HETATM 2513  O   HOH A 633      -0.797  17.885  32.400  1.00 57.35           O  
ANISOU 2513  O   HOH A 633    11334   5969   4488  -2273    150  -1127       O  
HETATM 2514  O   HOH A 634       4.255  19.087   7.058  1.00 67.90           O  
ANISOU 2514  O   HOH A 634    12208   6313   7276  -1723    936   -233       O  
HETATM 2515  O   HOH A 635     -11.874   8.026  18.855  1.00 40.51           O  
ANISOU 2515  O   HOH A 635     6046   5101   4245    777    384   -412       O  
HETATM 2516  O   HOH A 636     -14.811  12.340  18.267  1.00 50.84           O  
ANISOU 2516  O   HOH A 636     7839   6112   5365   1780    684   -629       O  
HETATM 2517  O   HOH A 637     -16.101  -7.721  10.873  1.00 49.11           O  
ANISOU 2517  O   HOH A 637     4842   7583   6233   -429    293   -503       O  
HETATM 2518  O   HOH A 638     -13.570   4.904   9.635  1.00 51.53           O  
ANISOU 2518  O   HOH A 638     6468   7093   6019   1196    -32   -215       O  
HETATM 2519  O   HOH A 639     -18.612  -6.240  10.403  1.00 73.56           O  
ANISOU 2519  O   HOH A 639     7587  11187   9176   -177    265   -664       O  
HETATM 2520  O   HOH A 640     -17.447  -1.357  12.228  1.00 63.18           O  
ANISOU 2520  O   HOH A 640     6768   9529   7710    547    203   -498       O  
HETATM 2521  O   HOH A 641       7.156  11.932   0.108  1.00 57.75           O  
ANISOU 2521  O   HOH A 641     9252   5972   6716  -2118   1284   -278       O  
HETATM 2522  O   HOH A 642      -6.408  18.379   3.124  1.00 63.46           O  
ANISOU 2522  O   HOH A 642    12076   5693   6341   1187    371    406       O  
HETATM 2523  O   HOH A 643      -5.699 -22.574   2.942  1.00 73.95           O  
ANISOU 2523  O   HOH A 643     9216   7924  10959  -1201   1311   -891       O  
HETATM 2524  O   HOH A 644     -10.779  -5.844  24.276  1.00 45.72           O  
ANISOU 2524  O   HOH A 644     6031   6245   5096   -831    150    285       O  
HETATM 2525  O   HOH A 645     -29.019 -15.414   3.795  1.00 59.46           O  
ANISOU 2525  O   HOH A 645     4639  11083   6870  -1973    341  -1797       O  
HETATM 2526  O   HOH A 646     -29.294 -15.104  -2.570  1.00 72.18           O  
ANISOU 2526  O   HOH A 646     6082  13264   8078  -1969   -195  -1986       O  
HETATM 2527  O   HOH A 647      -2.012 -15.671  16.017  1.00 71.32           O  
ANISOU 2527  O   HOH A 647     8677   8123  10300   -302   -239    706       O  
HETATM 2528  O   HOH A 648     -16.818 -11.498 -15.326  1.00 56.41           O  
ANISOU 2528  O   HOH A 648     6717   9836   4882  -1886   -455  -1830       O  
HETATM 2529  O   HOH A 649      -7.357 -10.047  24.842  1.00 62.15           O  
ANISOU 2529  O   HOH A 649     8327   7826   7462   -973   -287    822       O  
HETATM 2530  O   HOH A 650     -15.809 -14.184 -14.966  1.00 63.55           O  
ANISOU 2530  O   HOH A 650     7693  10328   6124  -2326     23  -2106       O  
HETATM 2531  O   HOH A 651      -5.609 -24.599   3.751  1.00 76.66           O  
ANISOU 2531  O   HOH A 651     9840   7832  11456  -1251   1446   -844       O  
HETATM 2532  O   HOH A 652      -0.907  -6.135  31.909  1.00 59.68           O  
ANISOU 2532  O   HOH A 652     8774   7709   6192  -1271  -1611   1307       O  
HETATM 2533  O   HOH A 653      -9.478  -8.840  26.138  1.00 60.86           O  
ANISOU 2533  O   HOH A 653     8276   7901   6948  -1119    -27    656       O  
HETATM 2534  O   HOH A 654      -9.498  -8.692  23.770  1.00 49.49           O  
ANISOU 2534  O   HOH A 654     6511   6481   5812   -946      3    523       O  
HETATM 2535  O   HOH A 655     -12.554 -10.421  22.951  1.00 52.87           O  
ANISOU 2535  O   HOH A 655     6740   7110   6240  -1171    403    333       O  
HETATM 2536  O   HOH A 656     -13.700  -2.019 -15.540  1.00 64.01           O  
ANISOU 2536  O   HOH A 656     8920  10101   5302   -332   -817   -615       O  
HETATM 2537  O   HOH A 657      -9.578  -8.278  28.663  1.00 50.18           O  
ANISOU 2537  O   HOH A 657     7289   6590   5189  -1297    -40    734       O  
HETATM 2538  O   HOH C 201      11.816   0.675  23.655  1.00 56.15           O  
ANISOU 2538  O   HOH C 201     5875   7956   7506  -1600  -2163    423       O  
CONECT 1120 2360                                                                
CONECT 2331 2332 2336                                                           
CONECT 2332 2331 2333 2334                                                      
CONECT 2333 2332                                                                
CONECT 2334 2332 2335                                                           
CONECT 2335 2334 2336                                                           
CONECT 2336 2331 2335 2337                                                      
CONECT 2337 2336 2338 2339                                                      
CONECT 2338 2337                                                                
CONECT 2339 2337                                                                
CONECT 2353 2370                                                                
CONECT 2359 2360 2363 2370                                                      
CONECT 2360 1120 2359 2361                                                      
CONECT 2361 2360 2362                                                           
CONECT 2362 2361 2371 2373                                                      
CONECT 2363 2359 2364                                                           
CONECT 2364 2363 2365 2368                                                      
CONECT 2365 2364 2366                                                           
CONECT 2366 2365 2367                                                           
CONECT 2367 2366 2368                                                           
CONECT 2368 2364 2367 2369                                                      
CONECT 2369 2368                                                                
CONECT 2370 2353 2359                                                           
CONECT 2371 2362                                                                
CONECT 2372 2373 2379                                                           
CONECT 2373 2362 2372                                                           
CONECT 2374 2375 2379                                                           
CONECT 2375 2374 2376                                                           
CONECT 2376 2375 2377                                                           
CONECT 2377 2376 2378                                                           
CONECT 2378 2377 2379                                                           
CONECT 2379 2372 2374 2378                                                      
MASTER      299    0    3   11   15    0    3    6 2536    2   32   25          
END                                                                             
HEADER    VIRAL PROTEIN                           09-APR-20   7BV2              
TITLE     THE NSP12-NSP7-NSP8 COMPLEX BOUND TO THE TEMPLATE-PRIMER RNA AND      
TITLE    2 TRIPHOSPHATE FORM OF REMDESIVIR(RTP)                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NSP12;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PP1AB,ORF1AB POLYPROTEIN;                                   
COMPND   5 EC: 2.7.7.48;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: NSP8;                                                      
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: PP1AB,ORF1AB POLYPROTEIN;                                   
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: NSP7;                                                      
COMPND  14 CHAIN: C;                                                            
COMPND  15 SYNONYM: PP1AB,ORF1AB POLYPROTEIN;                                   
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: PRIMER;                                                    
COMPND  19 CHAIN: P;                                                            
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: TEMPLETE;                                                  
COMPND  23 CHAIN: T;                                                            
COMPND  24 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 GENE: REP, 1A-1B;                                                    
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE  11 2;                                                                   
SOURCE  12 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE  13 ORGANISM_TAXID: 2697049;                                             
SOURCE  14 GENE: REP, 1A-1B;                                                    
SOURCE  15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE  19 2;                                                                   
SOURCE  20 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE  21 ORGANISM_TAXID: 2697049;                                             
SOURCE  22 GENE: REP, 1A-1B;                                                    
SOURCE  23 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  25 MOL_ID: 4;                                                           
SOURCE  26 SYNTHETIC: YES;                                                      
SOURCE  27 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE  28 2;                                                                   
SOURCE  29 ORGANISM_COMMON: SARS-COV-2;                                         
SOURCE  30 ORGANISM_TAXID: 2697049;                                             
SOURCE  31 MOL_ID: 5;                                                           
SOURCE  32 SYNTHETIC: YES;                                                      
SOURCE  33 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE  34 2;                                                                   
SOURCE  35 ORGANISM_COMMON: SARS-COV-2;                                         
SOURCE  36 ORGANISM_TAXID: 2697049                                              
KEYWDS    SARS-COV-2, RNA POLYMERASE, REMDESIVIR, VIRAL PROTEIN                 
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    W.YIN,C.MAO,X.LUAN,D.SHEN,Q.SHEN,H.SU,X.WANG,F.ZHOU,W.ZHAO,M.GAO,     
AUTHOR   2 S.CHANG,Y.C.XIE,G.TIAN,H.W.JIANG,S.C.TAO,J.SHEN,Y.JIANG,H.JIANG,     
AUTHOR   3 Y.XU,S.ZHANG,Y.ZHANG,H.E.XU                                          
REVDAT   6   14-OCT-20 7BV2    1       HETSYN LINK                              
REVDAT   5   15-JUL-20 7BV2    1       JRNL                                     
REVDAT   4   10-JUN-20 7BV2    1       COMPND                                   
REVDAT   3   27-MAY-20 7BV2    1       COMPND JRNL   REMARK HELIX               
REVDAT   3 2                   1       SHEET  LINK   SITE   ATOM                
REVDAT   2   06-MAY-20 7BV2    1       COMPND SOURCE JRNL   REMARK              
REVDAT   2 2                   1       DBREF  SEQADV LINK   SITE                
REVDAT   2 3                   1       ATOM                                     
REVDAT   1   22-APR-20 7BV2    0                                                
JRNL        AUTH   W.YIN,C.MAO,X.LUAN,D.D.SHEN,Q.SHEN,H.SU,X.WANG,F.ZHOU,       
JRNL        AUTH 2 W.ZHAO,M.GAO,S.CHANG,Y.C.XIE,G.TIAN,H.W.JIANG,S.C.TAO,       
JRNL        AUTH 3 J.SHEN,Y.JIANG,H.JIANG,Y.XU,S.ZHANG,Y.ZHANG,H.E.XU           
JRNL        TITL   STRUCTURAL BASIS FOR INHIBITION OF THE RNA-DEPENDENT RNA     
JRNL        TITL 2 POLYMERASE FROM SARS-COV-2 BY REMDESIVIR.                    
JRNL        REF    SCIENCE                       V. 368  1499 2020              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   32358203                                                     
JRNL        DOI    10.1126/SCIENCE.ABC1560                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 2.500                          
REMARK   3   NUMBER OF PARTICLES               : 130386                         
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 7BV2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.                               
REMARK 100 THE DEPOSITION ID IS D_1300016534.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : THE NSP12-NSP7-NSP8 COMPLEX       
REMARK 245                                    BOUND TO THE TEMPLATE-PRIMER      
REMARK 245                                    RNA AND TRIPHOSPHATE FORM OF      
REMARK 245                                    REMDESIVIR(RTP)                   
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 64.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, P, T                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     PHE A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     ASN A     9                                                      
REMARK 465     ARG A    10                                                      
REMARK 465     VAL A    11                                                      
REMARK 465     CYS A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     ARG A    18                                                      
REMARK 465     LEU A    19                                                      
REMARK 465     THR A    20                                                      
REMARK 465     PRO A    21                                                      
REMARK 465     CYS A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     THR A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     THR A    28                                                      
REMARK 465     ASP A    29                                                      
REMARK 465     VAL A    30                                                      
REMARK 465     THR A    51                                                      
REMARK 465     ASN A    52                                                      
REMARK 465     CYS A    53                                                      
REMARK 465     CYS A    54                                                      
REMARK 465     ARG A    55                                                      
REMARK 465     PHE A    56                                                      
REMARK 465     GLN A    57                                                      
REMARK 465     GLU A    58                                                      
REMARK 465     LYS A    59                                                      
REMARK 465     ASP A    60                                                      
REMARK 465     GLU A    61                                                      
REMARK 465     ASP A    62                                                      
REMARK 465     ASP A    63                                                      
REMARK 465     ASN A    64                                                      
REMARK 465     LEU A    65                                                      
REMARK 465     ILE A    66                                                      
REMARK 465     ASP A    67                                                      
REMARK 465     SER A    68                                                      
REMARK 465     TYR A    69                                                      
REMARK 465     PHE A    70                                                      
REMARK 465     VAL A    71                                                      
REMARK 465     VAL A    72                                                      
REMARK 465     LYS A    73                                                      
REMARK 465     ARG A    74                                                      
REMARK 465     HIS A    75                                                      
REMARK 465     THR A    76                                                      
REMARK 465     PHE A    77                                                      
REMARK 465     SER A    78                                                      
REMARK 465     ASN A    79                                                      
REMARK 465     TYR A    80                                                      
REMARK 465     GLN A    81                                                      
REMARK 465     HIS A    82                                                      
REMARK 465     GLU A    83                                                      
REMARK 465     PHE A   101                                                      
REMARK 465     PHE A   102                                                      
REMARK 465     LYS A   103                                                      
REMARK 465     PHE A   104                                                      
REMARK 465     ARG A   105                                                      
REMARK 465     ILE A   106                                                      
REMARK 465     ASP A   107                                                      
REMARK 465     GLY A   108                                                      
REMARK 465     ASP A   109                                                      
REMARK 465     MET A   110                                                      
REMARK 465     VAL A   111                                                      
REMARK 465     PRO A   112                                                      
REMARK 465     HIS A   113                                                      
REMARK 465     ILE A   114                                                      
REMARK 465     SER A   115                                                      
REMARK 465     ARG A   116                                                      
REMARK 465     GLN A   117                                                      
REMARK 465     THR A   896                                                      
REMARK 465     GLY A   897                                                      
REMARK 465     HIS A   898                                                      
REMARK 465     MET A   899                                                      
REMARK 465     LEU A   900                                                      
REMARK 465     ASP A   901                                                      
REMARK 465     MET A   902                                                      
REMARK 465     TYR A   903                                                      
REMARK 465     SER A   904                                                      
REMARK 465     VAL A   905                                                      
REMARK 465     MET A   906                                                      
REMARK 465     LEU A   907                                                      
REMARK 465     THR A   908                                                      
REMARK 465     ASN A   909                                                      
REMARK 465     ASP A   910                                                      
REMARK 465     VAL A   930                                                      
REMARK 465     LEU A   931                                                      
REMARK 465     GLN A   932                                                      
REMARK 465     GLY A   933                                                      
REMARK 465     GLY A   934                                                      
REMARK 465     SER A   935                                                      
REMARK 465     GLU A   936                                                      
REMARK 465     ASN A   937                                                      
REMARK 465     LEU A   938                                                      
REMARK 465     TYR A   939                                                      
REMARK 465     PHE A   940                                                      
REMARK 465     GLN A   941                                                      
REMARK 465     GLY A   942                                                      
REMARK 465     HIS A   943                                                      
REMARK 465     HIS A   944                                                      
REMARK 465     HIS A   945                                                      
REMARK 465     HIS A   946                                                      
REMARK 465     HIS A   947                                                      
REMARK 465     HIS A   948                                                      
REMARK 465     HIS A   949                                                      
REMARK 465     HIS A   950                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     ILE B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     PHE B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     PRO B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     TYR B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     ALA B    14                                                      
REMARK 465     PHE B    15                                                      
REMARK 465     ALA B    16                                                      
REMARK 465     THR B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     GLN B    19                                                      
REMARK 465     GLU B    20                                                      
REMARK 465     ALA B    21                                                      
REMARK 465     TYR B    22                                                      
REMARK 465     GLU B    23                                                      
REMARK 465     GLN B    24                                                      
REMARK 465     ALA B    25                                                      
REMARK 465     VAL B    26                                                      
REMARK 465     ALA B    27                                                      
REMARK 465     ASN B    28                                                      
REMARK 465     GLY B    29                                                      
REMARK 465     ASP B    30                                                      
REMARK 465     SER B    31                                                      
REMARK 465     GLU B    32                                                      
REMARK 465     VAL B    33                                                      
REMARK 465     VAL B    34                                                      
REMARK 465     LEU B    35                                                      
REMARK 465     LYS B    36                                                      
REMARK 465     LYS B    37                                                      
REMARK 465     LEU B    38                                                      
REMARK 465     LYS B    39                                                      
REMARK 465     LYS B    40                                                      
REMARK 465     SER B    41                                                      
REMARK 465     LEU B    42                                                      
REMARK 465     ASN B    43                                                      
REMARK 465     VAL B    44                                                      
REMARK 465     ALA B    45                                                      
REMARK 465     LYS B    46                                                      
REMARK 465     SER B    47                                                      
REMARK 465     GLU B    48                                                      
REMARK 465     PHE B    49                                                      
REMARK 465     ASP B    50                                                      
REMARK 465     ARG B    51                                                      
REMARK 465     ASP B    52                                                      
REMARK 465     ALA B    53                                                      
REMARK 465     ALA B    54                                                      
REMARK 465     MET B    55                                                      
REMARK 465     GLN B    56                                                      
REMARK 465     ARG B    57                                                      
REMARK 465     LYS B    58                                                      
REMARK 465     LEU B    59                                                      
REMARK 465     GLU B    60                                                      
REMARK 465     LYS B    61                                                      
REMARK 465     MET B    62                                                      
REMARK 465     ALA B    63                                                      
REMARK 465     ASP B    64                                                      
REMARK 465     GLN B    65                                                      
REMARK 465     ALA B    66                                                      
REMARK 465     MET B    67                                                      
REMARK 465     THR B    68                                                      
REMARK 465     GLN B    69                                                      
REMARK 465     MET B    70                                                      
REMARK 465     TYR B    71                                                      
REMARK 465     LYS B    72                                                      
REMARK 465     GLN B    73                                                      
REMARK 465     ALA B    74                                                      
REMARK 465     ARG B    75                                                      
REMARK 465     SER B    76                                                      
REMARK 465     GLU B    77                                                      
REMARK 465     ASN B   192                                                      
REMARK 465     SER B   193                                                      
REMARK 465     ALA B   194                                                      
REMARK 465     VAL B   195                                                      
REMARK 465     LYS B   196                                                      
REMARK 465     LEU B   197                                                      
REMARK 465     GLN B   198                                                      
REMARK 465     HIS B   199                                                      
REMARK 465     HIS B   200                                                      
REMARK 465     HIS B   201                                                      
REMARK 465     HIS B   202                                                      
REMARK 465     HIS B   203                                                      
REMARK 465     HIS B   204                                                      
REMARK 465     HIS B   205                                                      
REMARK 465     HIS B   206                                                      
REMARK 465     MET C     0                                                      
REMARK 465     SER C     1                                                      
REMARK 465     ALA C    65                                                      
REMARK 465     VAL C    66                                                      
REMARK 465     ASP C    67                                                      
REMARK 465     ILE C    68                                                      
REMARK 465     ASN C    69                                                      
REMARK 465     LYS C    70                                                      
REMARK 465     LEU C    71                                                      
REMARK 465     CYS C    72                                                      
REMARK 465     GLU C    73                                                      
REMARK 465     GLU C    74                                                      
REMARK 465     MET C    75                                                      
REMARK 465     LEU C    76                                                      
REMARK 465     ASP C    77                                                      
REMARK 465     ASN C    78                                                      
REMARK 465     ARG C    79                                                      
REMARK 465     ALA C    80                                                      
REMARK 465     THR C    81                                                      
REMARK 465     LEU C    82                                                      
REMARK 465     GLN C    83                                                      
REMARK 465     HIS C    84                                                      
REMARK 465     HIS C    85                                                      
REMARK 465     HIS C    86                                                      
REMARK 465     HIS C    87                                                      
REMARK 465     HIS C    88                                                      
REMARK 465     HIS C    89                                                      
REMARK 465     HIS C    90                                                      
REMARK 465     HIS C    91                                                      
REMARK 465       G P     1                                                      
REMARK 465       C P     2                                                      
REMARK 465       U P     3                                                      
REMARK 465       A P     4                                                      
REMARK 465       U P     5                                                      
REMARK 465       G P     6                                                      
REMARK 465       U P     7                                                      
REMARK 465       G P     8                                                      
REMARK 465       A P     9                                                      
REMARK 465       U T     1                                                      
REMARK 465       U T     2                                                      
REMARK 465       U T     3                                                      
REMARK 465       U T     4                                                      
REMARK 465       U T     5                                                      
REMARK 465       U T     6                                                      
REMARK 465       U T     7                                                      
REMARK 465       U T    22                                                      
REMARK 465       C T    23                                                      
REMARK 465       A T    24                                                      
REMARK 465       C T    25                                                      
REMARK 465       A T    26                                                      
REMARK 465       U T    27                                                      
REMARK 465       A T    28                                                      
REMARK 465       G T    29                                                      
REMARK 465       C T    30                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  98    CG   CD   CE   NZ                                   
REMARK 470     ASP A 100    CG   OD1  OD2                                       
REMARK 470     ASP A 218    CG   OD1  OD2                                       
REMARK 470     ASP A 824    CG   OD1  OD2                                       
REMARK 470     ASP B  78    CG   OD1  OD2                                       
REMARK 470     LYS B  79    CG   CD   CE   NZ                                   
REMARK 470     LYS B  97    CG   CD   CE   NZ                                   
REMARK 470     GLU C  50    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O4     U P    12     N1     A T    19              1.94            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500      U P  20   P       U P  20   O5'     0.083                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A 259       42.04     38.38                                   
REMARK 500    VAL A 398      -65.19   -101.98                                   
REMARK 500    ARG A 533       -9.84   -142.79                                   
REMARK 500    TYR A 606        8.11    -68.06                                   
REMARK 500    ASP A 608       30.14   -153.59                                   
REMARK 500    SER A 759     -124.35     56.81                                   
REMARK 500    TYR A 915        3.24    -69.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TYR A  606     SER A  607                 -148.17                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 295   ND1                                                    
REMARK 620 2 CYS A 301   SG  123.9                                              
REMARK 620 3 CYS A 306   SG  101.9 108.0                                        
REMARK 620 4 CYS A 310   SG  100.5 109.7 112.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 487   SG                                                     
REMARK 620 2 HIS A 642   ND1 108.3                                              
REMARK 620 3 CYS A 645   SG   98.3 124.9                                        
REMARK 620 4 CYS A 646   SG   94.1 127.2  96.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue POP A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue F86 P 101                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-30210   RELATED DB: EMDB                             
REMARK 900 THE NSP12-NSP7-NSP8 COMPLEX BOUND TO THE TEMPLATE-PRIMER RNA AND     
REMARK 900 TRIPHOSPHATE FORM OF REMDESIVIR(RTP)                                 
DBREF  7BV2 A    1   932  UNP    P0DTD1   R1AB_SARS2    4393   5324             
DBREF  7BV2 B    1   198  UNP    P0DTD1   R1AB_SARS2    3943   4140             
DBREF  7BV2 C    1    83  UNP    P0DTD1   R1AB_SARS2    3860   3942             
DBREF  7BV2 P    1    20  PDB    7BV2     7BV2             1     20             
DBREF  7BV2 T    1    30  PDB    7BV2     7BV2             1     30             
SEQADV 7BV2 MET A    0  UNP  P0DTD1              INITIATING METHIONINE          
SEQADV 7BV2 GLY A  933  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 GLY A  934  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 SER A  935  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 GLU A  936  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 ASN A  937  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 LEU A  938  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 TYR A  939  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 PHE A  940  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 GLN A  941  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 GLY A  942  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS A  943  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS A  944  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS A  945  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS A  946  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS A  947  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS A  948  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS A  949  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS A  950  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 MET B    0  UNP  P0DTD1              INITIATING METHIONINE          
SEQADV 7BV2 HIS B  199  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS B  200  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS B  201  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS B  202  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS B  203  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS B  204  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS B  205  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS B  206  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 MET C    0  UNP  P0DTD1              INITIATING METHIONINE          
SEQADV 7BV2 HIS C   84  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS C   85  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS C   86  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS C   87  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS C   88  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS C   89  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS C   90  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 7BV2 HIS C   91  UNP  P0DTD1              EXPRESSION TAG                 
SEQRES   1 A  951  MET SER ALA ASP ALA GLN SER PHE LEU ASN ARG VAL CYS          
SEQRES   2 A  951  GLY VAL SER ALA ALA ARG LEU THR PRO CYS GLY THR GLY          
SEQRES   3 A  951  THR SER THR ASP VAL VAL TYR ARG ALA PHE ASP ILE TYR          
SEQRES   4 A  951  ASN ASP LYS VAL ALA GLY PHE ALA LYS PHE LEU LYS THR          
SEQRES   5 A  951  ASN CYS CYS ARG PHE GLN GLU LYS ASP GLU ASP ASP ASN          
SEQRES   6 A  951  LEU ILE ASP SER TYR PHE VAL VAL LYS ARG HIS THR PHE          
SEQRES   7 A  951  SER ASN TYR GLN HIS GLU GLU THR ILE TYR ASN LEU LEU          
SEQRES   8 A  951  LYS ASP CYS PRO ALA VAL ALA LYS HIS ASP PHE PHE LYS          
SEQRES   9 A  951  PHE ARG ILE ASP GLY ASP MET VAL PRO HIS ILE SER ARG          
SEQRES  10 A  951  GLN ARG LEU THR LYS TYR THR MET ALA ASP LEU VAL TYR          
SEQRES  11 A  951  ALA LEU ARG HIS PHE ASP GLU GLY ASN CYS ASP THR LEU          
SEQRES  12 A  951  LYS GLU ILE LEU VAL THR TYR ASN CYS CYS ASP ASP ASP          
SEQRES  13 A  951  TYR PHE ASN LYS LYS ASP TRP TYR ASP PHE VAL GLU ASN          
SEQRES  14 A  951  PRO ASP ILE LEU ARG VAL TYR ALA ASN LEU GLY GLU ARG          
SEQRES  15 A  951  VAL ARG GLN ALA LEU LEU LYS THR VAL GLN PHE CYS ASP          
SEQRES  16 A  951  ALA MET ARG ASN ALA GLY ILE VAL GLY VAL LEU THR LEU          
SEQRES  17 A  951  ASP ASN GLN ASP LEU ASN GLY ASN TRP TYR ASP PHE GLY          
SEQRES  18 A  951  ASP PHE ILE GLN THR THR PRO GLY SER GLY VAL PRO VAL          
SEQRES  19 A  951  VAL ASP SER TYR TYR SER LEU LEU MET PRO ILE LEU THR          
SEQRES  20 A  951  LEU THR ARG ALA LEU THR ALA GLU SER HIS VAL ASP THR          
SEQRES  21 A  951  ASP LEU THR LYS PRO TYR ILE LYS TRP ASP LEU LEU LYS          
SEQRES  22 A  951  TYR ASP PHE THR GLU GLU ARG LEU LYS LEU PHE ASP ARG          
SEQRES  23 A  951  TYR PHE LYS TYR TRP ASP GLN THR TYR HIS PRO ASN CYS          
SEQRES  24 A  951  VAL ASN CYS LEU ASP ASP ARG CYS ILE LEU HIS CYS ALA          
SEQRES  25 A  951  ASN PHE ASN VAL LEU PHE SER THR VAL PHE PRO PRO THR          
SEQRES  26 A  951  SER PHE GLY PRO LEU VAL ARG LYS ILE PHE VAL ASP GLY          
SEQRES  27 A  951  VAL PRO PHE VAL VAL SER THR GLY TYR HIS PHE ARG GLU          
SEQRES  28 A  951  LEU GLY VAL VAL HIS ASN GLN ASP VAL ASN LEU HIS SER          
SEQRES  29 A  951  SER ARG LEU SER PHE LYS GLU LEU LEU VAL TYR ALA ALA          
SEQRES  30 A  951  ASP PRO ALA MET HIS ALA ALA SER GLY ASN LEU LEU LEU          
SEQRES  31 A  951  ASP LYS ARG THR THR CYS PHE SER VAL ALA ALA LEU THR          
SEQRES  32 A  951  ASN ASN VAL ALA PHE GLN THR VAL LYS PRO GLY ASN PHE          
SEQRES  33 A  951  ASN LYS ASP PHE TYR ASP PHE ALA VAL SER LYS GLY PHE          
SEQRES  34 A  951  PHE LYS GLU GLY SER SER VAL GLU LEU LYS HIS PHE PHE          
SEQRES  35 A  951  PHE ALA GLN ASP GLY ASN ALA ALA ILE SER ASP TYR ASP          
SEQRES  36 A  951  TYR TYR ARG TYR ASN LEU PRO THR MET CYS ASP ILE ARG          
SEQRES  37 A  951  GLN LEU LEU PHE VAL VAL GLU VAL VAL ASP LYS TYR PHE          
SEQRES  38 A  951  ASP CYS TYR ASP GLY GLY CYS ILE ASN ALA ASN GLN VAL          
SEQRES  39 A  951  ILE VAL ASN ASN LEU ASP LYS SER ALA GLY PHE PRO PHE          
SEQRES  40 A  951  ASN LYS TRP GLY LYS ALA ARG LEU TYR TYR ASP SER MET          
SEQRES  41 A  951  SER TYR GLU ASP GLN ASP ALA LEU PHE ALA TYR THR LYS          
SEQRES  42 A  951  ARG ASN VAL ILE PRO THR ILE THR GLN MET ASN LEU LYS          
SEQRES  43 A  951  TYR ALA ILE SER ALA LYS ASN ARG ALA ARG THR VAL ALA          
SEQRES  44 A  951  GLY VAL SER ILE CYS SER THR MET THR ASN ARG GLN PHE          
SEQRES  45 A  951  HIS GLN LYS LEU LEU LYS SER ILE ALA ALA THR ARG GLY          
SEQRES  46 A  951  ALA THR VAL VAL ILE GLY THR SER LYS PHE TYR GLY GLY          
SEQRES  47 A  951  TRP HIS ASN MET LEU LYS THR VAL TYR SER ASP VAL GLU          
SEQRES  48 A  951  ASN PRO HIS LEU MET GLY TRP ASP TYR PRO LYS CYS ASP          
SEQRES  49 A  951  ARG ALA MET PRO ASN MET LEU ARG ILE MET ALA SER LEU          
SEQRES  50 A  951  VAL LEU ALA ARG LYS HIS THR THR CYS CYS SER LEU SER          
SEQRES  51 A  951  HIS ARG PHE TYR ARG LEU ALA ASN GLU CYS ALA GLN VAL          
SEQRES  52 A  951  LEU SER GLU MET VAL MET CYS GLY GLY SER LEU TYR VAL          
SEQRES  53 A  951  LYS PRO GLY GLY THR SER SER GLY ASP ALA THR THR ALA          
SEQRES  54 A  951  TYR ALA ASN SER VAL PHE ASN ILE CYS GLN ALA VAL THR          
SEQRES  55 A  951  ALA ASN VAL ASN ALA LEU LEU SER THR ASP GLY ASN LYS          
SEQRES  56 A  951  ILE ALA ASP LYS TYR VAL ARG ASN LEU GLN HIS ARG LEU          
SEQRES  57 A  951  TYR GLU CYS LEU TYR ARG ASN ARG ASP VAL ASP THR ASP          
SEQRES  58 A  951  PHE VAL ASN GLU PHE TYR ALA TYR LEU ARG LYS HIS PHE          
SEQRES  59 A  951  SER MET MET ILE LEU SER ASP ASP ALA VAL VAL CYS PHE          
SEQRES  60 A  951  ASN SER THR TYR ALA SER GLN GLY LEU VAL ALA SER ILE          
SEQRES  61 A  951  LYS ASN PHE LYS SER VAL LEU TYR TYR GLN ASN ASN VAL          
SEQRES  62 A  951  PHE MET SER GLU ALA LYS CYS TRP THR GLU THR ASP LEU          
SEQRES  63 A  951  THR LYS GLY PRO HIS GLU PHE CYS SER GLN HIS THR MET          
SEQRES  64 A  951  LEU VAL LYS GLN GLY ASP ASP TYR VAL TYR LEU PRO TYR          
SEQRES  65 A  951  PRO ASP PRO SER ARG ILE LEU GLY ALA GLY CYS PHE VAL          
SEQRES  66 A  951  ASP ASP ILE VAL LYS THR ASP GLY THR LEU MET ILE GLU          
SEQRES  67 A  951  ARG PHE VAL SER LEU ALA ILE ASP ALA TYR PRO LEU THR          
SEQRES  68 A  951  LYS HIS PRO ASN GLN GLU TYR ALA ASP VAL PHE HIS LEU          
SEQRES  69 A  951  TYR LEU GLN TYR ILE ARG LYS LEU HIS ASP GLU LEU THR          
SEQRES  70 A  951  GLY HIS MET LEU ASP MET TYR SER VAL MET LEU THR ASN          
SEQRES  71 A  951  ASP ASN THR SER ARG TYR TRP GLU PRO GLU PHE TYR GLU          
SEQRES  72 A  951  ALA MET TYR THR PRO HIS THR VAL LEU GLN GLY GLY SER          
SEQRES  73 A  951  GLU ASN LEU TYR PHE GLN GLY HIS HIS HIS HIS HIS HIS          
SEQRES  74 A  951  HIS HIS                                                      
SEQRES   1 B  207  MET ALA ILE ALA SER GLU PHE SER SER LEU PRO SER TYR          
SEQRES   2 B  207  ALA ALA PHE ALA THR ALA GLN GLU ALA TYR GLU GLN ALA          
SEQRES   3 B  207  VAL ALA ASN GLY ASP SER GLU VAL VAL LEU LYS LYS LEU          
SEQRES   4 B  207  LYS LYS SER LEU ASN VAL ALA LYS SER GLU PHE ASP ARG          
SEQRES   5 B  207  ASP ALA ALA MET GLN ARG LYS LEU GLU LYS MET ALA ASP          
SEQRES   6 B  207  GLN ALA MET THR GLN MET TYR LYS GLN ALA ARG SER GLU          
SEQRES   7 B  207  ASP LYS ARG ALA LYS VAL THR SER ALA MET GLN THR MET          
SEQRES   8 B  207  LEU PHE THR MET LEU ARG LYS LEU ASP ASN ASP ALA LEU          
SEQRES   9 B  207  ASN ASN ILE ILE ASN ASN ALA ARG ASP GLY CYS VAL PRO          
SEQRES  10 B  207  LEU ASN ILE ILE PRO LEU THR THR ALA ALA LYS LEU MET          
SEQRES  11 B  207  VAL VAL ILE PRO ASP TYR ASN THR TYR LYS ASN THR CYS          
SEQRES  12 B  207  ASP GLY THR THR PHE THR TYR ALA SER ALA LEU TRP GLU          
SEQRES  13 B  207  ILE GLN GLN VAL VAL ASP ALA ASP SER LYS ILE VAL GLN          
SEQRES  14 B  207  LEU SER GLU ILE SER MET ASP ASN SER PRO ASN LEU ALA          
SEQRES  15 B  207  TRP PRO LEU ILE VAL THR ALA LEU ARG ALA ASN SER ALA          
SEQRES  16 B  207  VAL LYS LEU GLN HIS HIS HIS HIS HIS HIS HIS HIS              
SEQRES   1 C   92  MET SER LYS MET SER ASP VAL LYS CYS THR SER VAL VAL          
SEQRES   2 C   92  LEU LEU SER VAL LEU GLN GLN LEU ARG VAL GLU SER SER          
SEQRES   3 C   92  SER LYS LEU TRP ALA GLN CYS VAL GLN LEU HIS ASN ASP          
SEQRES   4 C   92  ILE LEU LEU ALA LYS ASP THR THR GLU ALA PHE GLU LYS          
SEQRES   5 C   92  MET VAL SER LEU LEU SER VAL LEU LEU SER MET GLN GLY          
SEQRES   6 C   92  ALA VAL ASP ILE ASN LYS LEU CYS GLU GLU MET LEU ASP          
SEQRES   7 C   92  ASN ARG ALA THR LEU GLN HIS HIS HIS HIS HIS HIS HIS          
SEQRES   8 C   92  HIS                                                          
SEQRES   1 P   20    G   C   U   A   U   G   U   G   A   G   A   U   U          
SEQRES   2 P   20    A   A   G   U   U   A   U                                  
SEQRES   1 T   30    U   U   U   U   U   U   U   U   U   U   A   U   A          
SEQRES   2 T   30    A   C   U   U   A   A   U   C   U   C   A   C   A          
SEQRES   3 T   30    U   A   G   C                                              
HET     ZN  A1001       1                                                       
HET     ZN  A1002       1                                                       
HET    POP  A1003       9                                                       
HET     MG  A1004       1                                                       
HET     MG  A1005       1                                                       
HET    F86  P 101      24                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     POP PYROPHOSPHATE 2-                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     F86 [(2~{R},3~{S},4~{R},5~{R})-5-(4-AZANYLPYRROLO[2,1-F][1,          
HETNAM   2 F86  2,4]TRIAZIN-7-YL)-5-CYANO-3,4-BIS(OXIDANYL)OXOLAN-2-            
HETNAM   3 F86  YL]METHYL DIHYDROGEN PHOSPHATE                                  
HETSYN     F86 REMDESIVIR, BOUND FORM                                           
FORMUL   6   ZN    2(ZN 2+)                                                     
FORMUL   8  POP    H2 O7 P2 2-                                                  
FORMUL   9   MG    2(MG 2+)                                                     
FORMUL  11  F86    C12 H14 N5 O7 P                                              
FORMUL  12  HOH   *5(H2 O)                                                      
HELIX    1 AA1 GLU A   84  LEU A   90  5                                   7    
HELIX    2 AA2 THR A  123  HIS A  133  1                                  11    
HELIX    3 AA3 CYS A  139  TYR A  149  1                                  11    
HELIX    4 AA4 ASP A  153  LYS A  159  5                                   7    
HELIX    5 AA5 ASP A  170  ALA A  176  1                                   7    
HELIX    6 AA6 LEU A  178  GLY A  200  1                                  23    
HELIX    7 AA7 THR A  206  GLN A  210  5                                   5    
HELIX    8 AA8 VAL A  234  THR A  248  1                                  15    
HELIX    9 AA9 ARG A  249  ASP A  260  5                                  12    
HELIX   10 AB1 PHE A  275  PHE A  287  1                                  13    
HELIX   11 AB2 ASN A  297  CYS A  301  5                                   5    
HELIX   12 AB3 ASP A  303  SER A  318  1                                  16    
HELIX   13 AB4 PRO A  322  PHE A  326  5                                   5    
HELIX   14 AB5 SER A  367  ASP A  377  1                                  11    
HELIX   15 AB6 ASP A  377  GLY A  385  1                                   9    
HELIX   16 AB7 ASN A  416  LYS A  426  1                                  11    
HELIX   17 AB8 ASN A  447  ASP A  454  1                                   8    
HELIX   18 AB9 TYR A  455  ASN A  459  5                                   5    
HELIX   19 AC1 ASP A  465  ASP A  477  1                                  13    
HELIX   20 AC2 LYS A  478  ASP A  481  5                                   4    
HELIX   21 AC3 ASN A  489  VAL A  493  5                                   5    
HELIX   22 AC4 PRO A  505  TRP A  509  5                                   5    
HELIX   23 AC5 LYS A  511  MET A  519  1                                   9    
HELIX   24 AC6 SER A  520  THR A  531  1                                  12    
HELIX   25 AC7 SER A  561  THR A  582  1                                  22    
HELIX   26 AC8 GLY A  596  TYR A  606  1                                  11    
HELIX   27 AC9 LYS A  621  MET A  626  1                                   6    
HELIX   28 AD1 PRO A  627  ALA A  639  1                                  13    
HELIX   29 AD2 ARG A  640  HIS A  642  5                                   3    
HELIX   30 AD3 SER A  647  LEU A  663  1                                  17    
HELIX   31 AD4 THR A  686  SER A  709  1                                  24    
HELIX   32 AD5 ASP A  711  ILE A  715  5                                   5    
HELIX   33 AD6 ASP A  717  ARG A  733  1                                  17    
HELIX   34 AD7 ASP A  738  HIS A  752  1                                  15    
HELIX   35 AD8 SER A  768  GLN A  773  1                                   6    
HELIX   36 AD9 SER A  778  ASN A  790  1                                  13    
HELIX   37 AE1 SER A  795  CYS A  799  5                                   5    
HELIX   38 AE2 ASP A  833  CYS A  842  1                                  10    
HELIX   39 AE3 ASP A  846  THR A  850  5                                   5    
HELIX   40 AE4 ASP A  851  TYR A  867  1                                  17    
HELIX   41 AE5 PRO A  868  HIS A  872  5                                   5    
HELIX   42 AE6 ASN A  874  LEU A  895  1                                  22    
HELIX   43 AE7 GLU A  917  ALA A  923  1                                   7    
HELIX   44 AE8 MET A  924  THR A  926  5                                   3    
HELIX   45 AE9 LYS B   79  MET B   94  1                                  16    
HELIX   46 AF1 LEU B   95  LYS B   97  5                                   3    
HELIX   47 AF2 ASN B  100  ASN B  109  1                                  10    
HELIX   48 AF3 ASN B  118  ALA B  125  1                                   8    
HELIX   49 AF4 ASP B  134  CYS B  142  1                                   9    
HELIX   50 AF5 GLN B  168  ILE B  172  5                                   5    
HELIX   51 AF6 ASN B  176  LEU B  180  5                                   5    
HELIX   52 AF7 MET C    3  LEU C   20  1                                  18    
HELIX   53 AF8 ARG C   21  SER C   24  5                                   4    
HELIX   54 AF9 SER C   25  ALA C   42  1                                  18    
HELIX   55 AG1 ASP C   44  MET C   62  1                                  19    
SHEET    1 AA1 2 TYR A  32  TYR A  38  0                                        
SHEET    2 AA1 2 ALA A  43  LEU A  49 -1  O  PHE A  48   N  ARG A  33           
SHEET    1 AA2 3 ILE A 223  GLN A 224  0                                        
SHEET    2 AA2 3 ILE A 201  VAL A 204 -1  N  VAL A 202   O  ILE A 223           
SHEET    3 AA2 3 VAL A 231  VAL A 233  1  O  VAL A 233   N  GLY A 203           
SHEET    1 AA3 4 GLY A 352  HIS A 355  0                                        
SHEET    2 AA3 4 VAL A 338  PHE A 348 -1  N  PHE A 348   O  GLY A 352           
SHEET    3 AA3 4 GLY A 327  VAL A 335 -1  N  ILE A 333   O  PHE A 340           
SHEET    4 AA3 4 HIS A 362  SER A 363  1  O  SER A 363   N  PHE A 334           
SHEET    1 AA4 4 GLY A 352  HIS A 355  0                                        
SHEET    2 AA4 4 VAL A 338  PHE A 348 -1  N  PHE A 348   O  GLY A 352           
SHEET    3 AA4 4 GLY A 327  VAL A 335 -1  N  ILE A 333   O  PHE A 340           
SHEET    4 AA4 4 VAL B 115  PRO B 116 -1  O  VAL B 115   N  VAL A 330           
SHEET    1 AA510 THR A 556  GLY A 559  0                                        
SHEET    2 AA510 ILE A 539  LEU A 544 -1  N  GLN A 541   O  GLY A 559           
SHEET    3 AA510 MET A 666  MET A 668  1  O  MET A 668   N  THR A 540           
SHEET    4 AA510 SER A 672  VAL A 675 -1  O  TYR A 674   N  VAL A 667           
SHEET    5 AA510 SER A 397  ALA A 400 -1  N  VAL A 398   O  LEU A 673           
SHEET    6 AA510 ASN A 386  ASP A 390 -1  N  ASN A 386   O  ALA A 400           
SHEET    7 AA510 LYS B 127  ILE B 132  1  O  MET B 129   N  LEU A 389           
SHEET    8 AA510 LEU B 184  ARG B 190 -1  O  VAL B 186   N  VAL B 130           
SHEET    9 AA510 ALA B 152  VAL B 160 -1  N  VAL B 160   O  ILE B 185           
SHEET   10 AA510 THR B 146  TYR B 149 -1  N  PHE B 147   O  TRP B 154           
SHEET    1 AA6 2 ASN A 414  PHE A 415  0                                        
SHEET    2 AA6 2 PHE A 843  VAL A 844 -1  O  VAL A 844   N  ASN A 414           
SHEET    1 AA7 4 PHE A 753  LEU A 758  0                                        
SHEET    2 AA7 4 ASP A 761  ASN A 767 -1  O  CYS A 765   N  SER A 754           
SHEET    3 AA7 4 PRO A 612  GLY A 616 -1  N  MET A 615   O  VAL A 764           
SHEET    4 AA7 4 TRP A 800  GLU A 802 -1  O  GLU A 802   N  LEU A 614           
SHEET    1 AA8 2 HIS A 816  GLN A 822  0                                        
SHEET    2 AA8 2 ASP A 825  TYR A 831 -1  O  VAL A 827   N  VAL A 820           
LINK         O3'   U P  20                 P1  F86 P 101     1555   1555  1.72  
LINK         ND1 HIS A 295                ZN    ZN A1001     1555   1555  2.09  
LINK         SG  CYS A 301                ZN    ZN A1001     1555   1555  2.31  
LINK         SG  CYS A 306                ZN    ZN A1001     1555   1555  2.31  
LINK         SG  CYS A 310                ZN    ZN A1001     1555   1555  2.31  
LINK         SG  CYS A 487                ZN    ZN A1002     1555   1555  2.38  
LINK         ND1 HIS A 642                ZN    ZN A1002     1555   1555  1.87  
LINK         SG  CYS A 645                ZN    ZN A1002     1555   1555  2.39  
LINK         SG  CYS A 646                ZN    ZN A1002     1555   1555  2.34  
LINK         O   POP A1003                MG    MG A1004     1555   1555  2.70  
LINK        MG    MG A1005                 OP1   U P  20     1555   1555  2.33  
CISPEP   1 PHE A  504    PRO A  505          0        -4.53                     
CISPEP   2 TRP B  182    PRO B  183          0        -1.44                     
SITE     1 AC1  4 HIS A 295  CYS A 301  CYS A 306  CYS A 310                    
SITE     1 AC2  4 CYS A 487  HIS A 642  CYS A 645  CYS A 646                    
SITE     1 AC3  4 ARG A 553  ASP A 623   MG A1004  F86 P 101                    
SITE     1 AC4  4 TYR A 619  ASP A 760  POP A1003  F86 P 101                    
SITE     1 AC5  2 ASP A 761    U P  20                                          
SITE     1 AC6 11 ARG A 555  ASP A 623  SER A 682  THR A 687                    
SITE     2 AC6 11 ASN A 691  ASP A 760  POP A1003   MG A1004                    
SITE     3 AC6 11   U P  20    U T  10    A T  11                               
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  N   VAL A  31     122.481  84.940  68.733  1.00 48.71           N  
ATOM      2  CA  VAL A  31     122.121  85.420  70.061  1.00 48.71           C  
ATOM      3  C   VAL A  31     120.850  86.260  70.000  1.00 48.71           C  
ATOM      4  O   VAL A  31     120.658  87.054  69.079  1.00 48.71           O  
ATOM      5  CB  VAL A  31     123.274  86.219  70.696  1.00 48.71           C  
ATOM      6  CG1 VAL A  31     124.373  85.278  71.170  1.00 48.71           C  
ATOM      7  CG2 VAL A  31     123.823  87.241  69.708  1.00 48.71           C  
ATOM      8  N   TYR A  32     119.984  86.081  70.992  1.00 45.47           N  
ATOM      9  CA  TYR A  32     118.719  86.798  71.031  1.00 45.47           C  
ATOM     10  C   TYR A  32     118.909  88.181  71.640  1.00 45.47           C  
ATOM     11  O   TYR A  32     119.656  88.356  72.606  1.00 45.47           O  
ATOM     12  CB  TYR A  32     117.685  86.006  71.832  1.00 45.47           C  
ATOM     13  CG  TYR A  32     117.287  84.706  71.177  1.00 45.47           C  
ATOM     14  CD1 TYR A  32     116.533  84.697  70.013  1.00 45.47           C  
ATOM     15  CD2 TYR A  32     117.673  83.487  71.718  1.00 45.47           C  
ATOM     16  CE1 TYR A  32     116.170  83.509  69.406  1.00 45.47           C  
ATOM     17  CE2 TYR A  32     117.315  82.294  71.118  1.00 45.47           C  
ATOM     18  CZ  TYR A  32     116.563  82.311  69.962  1.00 45.47           C  
ATOM     19  OH  TYR A  32     116.203  81.129  69.359  1.00 45.47           O  
ATOM     20  N   ARG A  33     118.226  89.166  71.063  1.00 32.50           N  
ATOM     21  CA  ARG A  33     118.283  90.538  71.538  1.00 32.50           C  
ATOM     22  C   ARG A  33     116.880  91.121  71.515  1.00 32.50           C  
ATOM     23  O   ARG A  33     116.033  90.698  70.726  1.00 32.50           O  
ATOM     24  CB  ARG A  33     119.223  91.393  70.679  1.00 32.50           C  
ATOM     25  CG  ARG A  33     120.703  91.160  70.932  1.00 32.50           C  
ATOM     26  CD  ARG A  33     121.083  91.438  72.374  1.00 32.50           C  
ATOM     27  NE  ARG A  33     122.532  91.458  72.557  1.00 32.50           N  
ATOM     28  CZ  ARG A  33     123.266  90.389  72.853  1.00 32.50           C  
ATOM     29  NH1 ARG A  33     122.689  89.207  73.009  1.00 32.50           N  
ATOM     30  NH2 ARG A  33     124.578  90.505  72.997  1.00 32.50           N  
ATOM     31  N   ALA A  34     116.636  92.092  72.388  1.00 24.62           N  
ATOM     32  CA  ALA A  34     115.338  92.747  72.442  1.00 24.62           C  
ATOM     33  C   ALA A  34     115.229  93.823  71.368  1.00 24.62           C  
ATOM     34  O   ALA A  34     116.157  94.609  71.159  1.00 24.62           O  
ATOM     35  CB  ALA A  34     115.107  93.355  73.824  1.00 24.62           C  
ATOM     36  N   PHE A  35     114.086  93.851  70.684  1.00 26.32           N  
ATOM     37  CA  PHE A  35     113.785  94.868  69.686  1.00 26.32           C  
ATOM     38  C   PHE A  35     112.358  95.356  69.872  1.00 26.32           C  
ATOM     39  O   PHE A  35     111.468  94.572  70.209  1.00 26.32           O  
ATOM     40  CB  PHE A  35     113.936  94.352  68.246  1.00 26.32           C  
ATOM     41  CG  PHE A  35     115.289  93.788  67.925  1.00 26.32           C  
ATOM     42  CD1 PHE A  35     115.630  92.502  68.298  1.00 26.32           C  
ATOM     43  CD2 PHE A  35     116.217  94.545  67.232  1.00 26.32           C  
ATOM     44  CE1 PHE A  35     116.872  91.986  67.995  1.00 26.32           C  
ATOM     45  CE2 PHE A  35     117.459  94.035  66.929  1.00 26.32           C  
ATOM     46  CZ  PHE A  35     117.787  92.754  67.311  1.00 26.32           C  
ATOM     47  N   ASP A  36     112.146  96.649  69.644  1.00 26.63           N  
ATOM     48  CA  ASP A  36     110.805  97.220  69.562  1.00 26.63           C  
ATOM     49  C   ASP A  36     110.455  97.356  68.084  1.00 26.63           C  
ATOM     50  O   ASP A  36     111.041  98.178  67.374  1.00 26.63           O  
ATOM     51  CB  ASP A  36     110.744  98.565  70.283  1.00 26.63           C  
ATOM     52  CG  ASP A  36     109.528  99.388  69.896  1.00 26.63           C  
ATOM     53  OD1 ASP A  36     108.436  98.807  69.729  1.00 26.63           O  
ATOM     54  OD2 ASP A  36     109.658 100.623  69.779  1.00 26.63           O  
ATOM     55  N   ILE A  37     109.501  96.554  67.621  1.00 26.53           N  
ATOM     56  CA  ILE A  37     109.219  96.391  66.199  1.00 26.53           C  
ATOM     57  C   ILE A  37     107.823  96.909  65.884  1.00 26.53           C  
ATOM     58  O   ILE A  37     106.879  96.698  66.654  1.00 26.53           O  
ATOM     59  CB  ILE A  37     109.368  94.915  65.777  1.00 26.53           C  
ATOM     60  CG1 ILE A  37     110.804  94.441  65.990  1.00 26.53           C  
ATOM     61  CG2 ILE A  37     108.965  94.714  64.327  1.00 26.53           C  
ATOM     62  CD1 ILE A  37     111.848  95.410  65.486  1.00 26.53           C  
ATOM     63  N   TYR A  38     107.702  97.604  64.751  1.00 29.03           N  
ATOM     64  CA  TYR A  38     106.403  97.911  64.154  1.00 29.03           C  
ATOM     65  C   TYR A  38     106.594  97.988  62.642  1.00 29.03           C  
ATOM     66  O   TYR A  38     106.994  99.029  62.116  1.00 29.03           O  
ATOM     67  CB  TYR A  38     105.813  99.201  64.704  1.00 29.03           C  
ATOM     68  CG  TYR A  38     104.435  99.500  64.158  1.00 29.03           C  
ATOM     69  CD1 TYR A  38     103.309  98.875  64.671  1.00 29.03           C  
ATOM     70  CD2 TYR A  38     104.262 100.413  63.128  1.00 29.03           C  
ATOM     71  CE1 TYR A  38     102.052  99.146  64.170  1.00 29.03           C  
ATOM     72  CE2 TYR A  38     103.012 100.691  62.624  1.00 29.03           C  
ATOM     73  CZ  TYR A  38     101.910 100.056  63.146  1.00 29.03           C  
ATOM     74  OH  TYR A  38     100.663 100.337  62.641  1.00 29.03           O  
ATOM     75  N   ASN A  39     106.296  96.888  61.961  1.00 39.42           N  
ATOM     76  CA  ASN A  39     106.317  96.806  60.512  1.00 39.42           C  
ATOM     77  C   ASN A  39     104.888  96.860  59.983  1.00 39.42           C  
ATOM     78  O   ASN A  39     103.935  97.120  60.721  1.00 39.42           O  
ATOM     79  CB  ASN A  39     107.016  95.523  60.056  1.00 39.42           C  
ATOM     80  CG  ASN A  39     108.416  95.392  60.603  1.00 39.42           C  
ATOM     81  OD1 ASN A  39     108.851  96.193  61.429  1.00 39.42           O  
ATOM     82  ND2 ASN A  39     109.131  94.372  60.150  1.00 39.42           N  
ATOM     83  N   ASP A  40     104.735  96.633  58.678  1.00 46.10           N  
ATOM     84  CA  ASP A  40     103.436  96.236  58.153  1.00 46.10           C  
ATOM     85  C   ASP A  40     103.141  94.772  58.448  1.00 46.10           C  
ATOM     86  O   ASP A  40     101.978  94.360  58.387  1.00 46.10           O  
ATOM     87  CB  ASP A  40     103.369  96.491  56.647  1.00 46.10           C  
ATOM     88  CG  ASP A  40     103.641  97.940  56.286  1.00 46.10           C  
ATOM     89  OD1 ASP A  40     102.704  98.760  56.368  1.00 46.10           O  
ATOM     90  OD2 ASP A  40     104.791  98.256  55.914  1.00 46.10           O  
ATOM     91  N   LYS A  41     104.169  93.982  58.764  1.00 44.15           N  
ATOM     92  CA  LYS A  41     104.031  92.547  58.975  1.00 44.15           C  
ATOM     93  C   LYS A  41     103.950  92.167  60.449  1.00 44.15           C  
ATOM     94  O   LYS A  41     103.153  91.298  60.819  1.00 44.15           O  
ATOM     95  CB  LYS A  41     105.208  91.810  58.329  1.00 44.15           C  
ATOM     96  CG  LYS A  41     105.549  92.275  56.923  1.00 44.15           C  
ATOM     97  CD  LYS A  41     104.744  91.529  55.872  1.00 44.15           C  
ATOM     98  CE  LYS A  41     104.990  90.030  55.948  1.00 44.15           C  
ATOM     99  NZ  LYS A  41     103.938  89.258  55.232  1.00 44.15           N  
ATOM    100  N   VAL A  42     104.758  92.796  61.302  1.00 37.33           N  
ATOM    101  CA  VAL A  42     104.928  92.356  62.682  1.00 37.33           C  
ATOM    102  C   VAL A  42     105.059  93.582  63.576  1.00 37.33           C  
ATOM    103  O   VAL A  42     105.622  94.605  63.179  1.00 37.33           O  
ATOM    104  CB  VAL A  42     106.159  91.420  62.816  1.00 37.33           C  
ATOM    105  CG1 VAL A  42     106.577  91.247  64.266  1.00 37.33           C  
ATOM    106  CG2 VAL A  42     105.872  90.064  62.193  1.00 37.33           C  
ATOM    107  N   ALA A  43     104.523  93.474  64.791  1.00 27.47           N  
ATOM    108  CA  ALA A  43     104.672  94.500  65.810  1.00 27.47           C  
ATOM    109  C   ALA A  43     104.882  93.825  67.158  1.00 27.47           C  
ATOM    110  O   ALA A  43     104.535  92.657  67.352  1.00 27.47           O  
ATOM    111  CB  ALA A  43     103.457  95.431  65.854  1.00 27.47           C  
ATOM    112  N   GLY A  44     105.462  94.569  68.097  1.00 21.42           N  
ATOM    113  CA  GLY A  44     105.707  94.034  69.423  1.00 21.42           C  
ATOM    114  C   GLY A  44     107.023  94.462  70.038  1.00 21.42           C  
ATOM    115  O   GLY A  44     107.742  95.288  69.471  1.00 21.42           O  
ATOM    116  N   PHE A  45     107.344  93.907  71.209  1.00 18.50           N  
ATOM    117  CA  PHE A  45     108.594  94.194  71.921  1.00 18.50           C  
ATOM    118  C   PHE A  45     109.094  92.861  72.478  1.00 18.50           C  
ATOM    119  O   PHE A  45     108.735  92.467  73.589  1.00 18.50           O  
ATOM    120  CB  PHE A  45     108.374  95.235  73.014  1.00 18.50           C  
ATOM    121  CG  PHE A  45     109.573  95.475  73.890  1.00 18.50           C  
ATOM    122  CD1 PHE A  45     110.692  96.120  73.394  1.00 18.50           C  
ATOM    123  CD2 PHE A  45     109.569  95.084  75.217  1.00 18.50           C  
ATOM    124  CE1 PHE A  45     111.791  96.349  74.199  1.00 18.50           C  
ATOM    125  CE2 PHE A  45     110.665  95.316  76.025  1.00 18.50           C  
ATOM    126  CZ  PHE A  45     111.777  95.947  75.514  1.00 18.50           C  
ATOM    127  N   ALA A  46     109.929  92.174  71.700  1.00 23.08           N  
ATOM    128  CA  ALA A  46     110.286  90.794  71.995  1.00 23.08           C  
ATOM    129  C   ALA A  46     111.713  90.515  71.549  1.00 23.08           C  
ATOM    130  O   ALA A  46     112.304  91.269  70.773  1.00 23.08           O  
ATOM    131  CB  ALA A  46     109.330  89.813  71.313  1.00 23.08           C  
ATOM    132  N   LYS A  47     112.260  89.412  72.058  1.00 25.32           N  
ATOM    133  CA  LYS A  47     113.584  88.956  71.661  1.00 25.32           C  
ATOM    134  C   LYS A  47     113.541  88.343  70.268  1.00 25.32           C  
ATOM    135  O   LYS A  47     112.660  87.533  69.963  1.00 25.32           O  
ATOM    136  CB  LYS A  47     114.124  87.936  72.663  1.00 25.32           C  
ATOM    137  CG  LYS A  47     114.612  88.537  73.961  1.00 25.32           C  
ATOM    138  CD  LYS A  47     114.722  87.483  75.040  1.00 25.32           C  
ATOM    139  CE  LYS A  47     115.621  87.948  76.165  1.00 25.32           C  
ATOM    140  NZ  LYS A  47     117.005  87.426  76.018  1.00 25.32           N  
ATOM    141  N   PHE A  48     114.496  88.729  69.425  1.00 33.55           N  
ATOM    142  CA  PHE A  48     114.612  88.214  68.070  1.00 33.55           C  
ATOM    143  C   PHE A  48     116.036  87.735  67.828  1.00 33.55           C  
ATOM    144  O   PHE A  48     116.989  88.252  68.416  1.00 33.55           O  
ATOM    145  CB  PHE A  48     114.228  89.279  67.038  1.00 33.55           C  
ATOM    146  CG  PHE A  48     112.781  89.665  67.083  1.00 33.55           C  
ATOM    147  CD1 PHE A  48     111.794  88.723  66.871  1.00 33.55           C  
ATOM    148  CD2 PHE A  48     112.406  90.967  67.357  1.00 33.55           C  
ATOM    149  CE1 PHE A  48     110.462  89.076  66.916  1.00 33.55           C  
ATOM    150  CE2 PHE A  48     111.074  91.322  67.407  1.00 33.55           C  
ATOM    151  CZ  PHE A  48     110.101  90.377  67.184  1.00 33.55           C  
ATOM    152  N   LEU A  49     116.171  86.735  66.961  1.00 44.65           N  
ATOM    153  CA  LEU A  49     117.473  86.140  66.682  1.00 44.65           C  
ATOM    154  C   LEU A  49     118.228  86.978  65.659  1.00 44.65           C  
ATOM    155  O   LEU A  49     117.923  86.929  64.463  1.00 44.65           O  
ATOM    156  CB  LEU A  49     117.301  84.711  66.174  1.00 44.65           C  
ATOM    157  CG  LEU A  49     118.560  83.849  66.087  1.00 44.65           C  
ATOM    158  CD1 LEU A  49     119.424  84.033  67.323  1.00 44.65           C  
ATOM    159  CD2 LEU A  49     118.187  82.389  65.908  1.00 44.65           C  
ATOM    160  N   LYS A  50     119.228  87.723  66.124  1.00 49.25           N  
ATOM    161  CA  LYS A  50     120.149  88.445  65.247  1.00 49.25           C  
ATOM    162  C   LYS A  50     121.584  87.985  65.483  1.00 49.25           C  
ATOM    163  O   LYS A  50     122.256  87.518  64.563  1.00 49.25           O  
ATOM    164  CB  LYS A  50     120.047  89.962  65.451  1.00 49.25           C  
ATOM    165  CG  LYS A  50     119.137  90.701  64.468  1.00 49.25           C  
ATOM    166  CD  LYS A  50     117.839  89.972  64.195  1.00 49.25           C  
ATOM    167  CE  LYS A  50     117.089  90.584  63.025  1.00 49.25           C  
ATOM    168  NZ  LYS A  50     115.691  90.079  62.946  1.00 49.25           N  
ATOM    169  N   GLU A  84     122.717 105.425  56.108  1.00 68.24           N  
ATOM    170  CA  GLU A  84     122.387 106.253  54.956  1.00 68.24           C  
ATOM    171  C   GLU A  84     123.173 107.562  55.048  1.00 68.24           C  
ATOM    172  O   GLU A  84     123.720 107.888  56.101  1.00 68.24           O  
ATOM    173  CB  GLU A  84     120.873 106.502  54.894  1.00 68.24           C  
ATOM    174  CG  GLU A  84     120.389 107.330  53.707  1.00 68.24           C  
ATOM    175  CD  GLU A  84     118.940 107.066  53.354  1.00 68.24           C  
ATOM    176  OE1 GLU A  84     118.542 107.380  52.213  1.00 68.24           O  
ATOM    177  OE2 GLU A  84     118.199 106.551  54.216  1.00 68.24           O  
ATOM    178  N   THR A  85     123.236 108.307  53.941  1.00 67.14           N  
ATOM    179  CA  THR A  85     123.980 109.561  53.892  1.00 67.14           C  
ATOM    180  C   THR A  85     123.436 110.621  54.843  1.00 67.14           C  
ATOM    181  O   THR A  85     124.036 111.697  54.944  1.00 67.14           O  
ATOM    182  CB  THR A  85     123.985 110.111  52.464  1.00 67.14           C  
ATOM    183  OG1 THR A  85     122.645 110.157  51.962  1.00 67.14           O  
ATOM    184  CG2 THR A  85     124.830 109.229  51.559  1.00 67.14           C  
ATOM    185  N   ILE A  86     122.323 110.358  55.533  1.00 62.68           N  
ATOM    186  CA  ILE A  86     121.825 111.287  56.540  1.00 62.68           C  
ATOM    187  C   ILE A  86     122.702 111.328  57.781  1.00 62.68           C  
ATOM    188  O   ILE A  86     122.496 112.187  58.645  1.00 62.68           O  
ATOM    189  CB  ILE A  86     120.380 110.938  56.948  1.00 62.68           C  
ATOM    190  CG1 ILE A  86     120.363 109.754  57.910  1.00 62.68           C  
ATOM    191  CG2 ILE A  86     119.551 110.609  55.726  1.00 62.68           C  
ATOM    192  CD1 ILE A  86     118.974 109.307  58.259  1.00 62.68           C  
ATOM    193  N   TYR A  87     123.666 110.410  57.898  1.00 63.22           N  
ATOM    194  CA  TYR A  87     124.612 110.464  59.008  1.00 63.22           C  
ATOM    195  C   TYR A  87     125.410 111.762  58.986  1.00 63.22           C  
ATOM    196  O   TYR A  87     125.759 112.302  60.042  1.00 63.22           O  
ATOM    197  CB  TYR A  87     125.546 109.255  58.959  1.00 63.22           C  
ATOM    198  CG  TYR A  87     126.789 109.403  59.805  1.00 63.22           C  
ATOM    199  CD1 TYR A  87     126.715 109.385  61.190  1.00 63.22           C  
ATOM    200  CD2 TYR A  87     128.038 109.559  59.218  1.00 63.22           C  
ATOM    201  CE1 TYR A  87     127.849 109.518  61.968  1.00 63.22           C  
ATOM    202  CE2 TYR A  87     129.176 109.694  59.988  1.00 63.22           C  
ATOM    203  CZ  TYR A  87     129.076 109.673  61.362  1.00 63.22           C  
ATOM    204  OH  TYR A  87     130.207 109.807  62.133  1.00 63.22           O  
ATOM    205  N   ASN A  88     125.715 112.272  57.789  1.00 62.07           N  
ATOM    206  CA  ASN A  88     126.410 113.549  57.673  1.00 62.07           C  
ATOM    207  C   ASN A  88     125.609 114.701  58.265  1.00 62.07           C  
ATOM    208  O   ASN A  88     126.202 115.683  58.724  1.00 62.07           O  
ATOM    209  CB  ASN A  88     126.729 113.842  56.207  1.00 62.07           C  
ATOM    210  CG  ASN A  88     128.136 113.434  55.823  1.00 62.07           C  
ATOM    211  OD1 ASN A  88     129.063 114.241  55.874  1.00 62.07           O  
ATOM    212  ND2 ASN A  88     128.301 112.176  55.433  1.00 62.07           N  
ATOM    213  N   LEU A  89     124.279 114.605  58.268  1.00 59.89           N  
ATOM    214  CA  LEU A  89     123.438 115.629  58.874  1.00 59.89           C  
ATOM    215  C   LEU A  89     123.373 115.518  60.390  1.00 59.89           C  
ATOM    216  O   LEU A  89     122.800 116.402  61.036  1.00 59.89           O  
ATOM    217  CB  LEU A  89     122.020 115.558  58.298  1.00 59.89           C  
ATOM    218  CG  LEU A  89     121.869 115.727  56.785  1.00 59.89           C  
ATOM    219  CD1 LEU A  89     120.626 115.012  56.288  1.00 59.89           C  
ATOM    220  CD2 LEU A  89     121.822 117.199  56.417  1.00 59.89           C  
ATOM    221  N   LEU A  90     123.941 114.460  60.968  1.00 57.20           N  
ATOM    222  CA  LEU A  90     123.865 114.222  62.401  1.00 57.20           C  
ATOM    223  C   LEU A  90     125.215 113.977  63.058  1.00 57.20           C  
ATOM    224  O   LEU A  90     125.271 113.911  64.290  1.00 57.20           O  
ATOM    225  CB  LEU A  90     122.953 113.020  62.695  1.00 57.20           C  
ATOM    226  CG  LEU A  90     121.444 113.256  62.643  1.00 57.20           C  
ATOM    227  CD1 LEU A  90     120.725 111.965  62.293  1.00 57.20           C  
ATOM    228  CD2 LEU A  90     120.935 113.810  63.958  1.00 57.20           C  
ATOM    229  N   LYS A  91     126.297 113.839  62.284  1.00 62.68           N  
ATOM    230  CA  LYS A  91     127.587 113.454  62.852  1.00 62.68           C  
ATOM    231  C   LYS A  91     128.091 114.460  63.881  1.00 62.68           C  
ATOM    232  O   LYS A  91     128.851 114.091  64.783  1.00 62.68           O  
ATOM    233  CB  LYS A  91     128.617 113.280  61.736  1.00 62.68           C  
ATOM    234  CG  LYS A  91     128.936 114.558  60.971  1.00 62.68           C  
ATOM    235  CD  LYS A  91     129.923 114.309  59.839  1.00 62.68           C  
ATOM    236  CE  LYS A  91     131.138 113.511  60.299  1.00 62.68           C  
ATOM    237  NZ  LYS A  91     131.731 114.031  61.566  1.00 62.68           N  
ATOM    238  N   ASP A  92     127.685 115.727  63.770  1.00 62.38           N  
ATOM    239  CA  ASP A  92     128.162 116.740  64.704  1.00 62.38           C  
ATOM    240  C   ASP A  92     127.520 116.613  66.081  1.00 62.38           C  
ATOM    241  O   ASP A  92     128.055 117.161  67.051  1.00 62.38           O  
ATOM    242  CB  ASP A  92     127.909 118.138  64.138  1.00 62.38           C  
ATOM    243  CG  ASP A  92     126.434 118.434  63.949  1.00 62.38           C  
ATOM    244  OD1 ASP A  92     125.670 117.490  63.657  1.00 62.38           O  
ATOM    245  OD2 ASP A  92     126.038 119.609  64.092  1.00 62.38           O  
ATOM    246  N   CYS A  93     126.400 115.912  66.187  1.00 54.63           N  
ATOM    247  CA  CYS A  93     125.737 115.720  67.474  1.00 54.63           C  
ATOM    248  C   CYS A  93     126.567 114.800  68.361  1.00 54.63           C  
ATOM    249  O   CYS A  93     126.931 113.699  67.926  1.00 54.63           O  
ATOM    250  CB  CYS A  93     124.340 115.144  67.267  1.00 54.63           C  
ATOM    251  SG  CYS A  93     123.474 114.712  68.793  1.00 54.63           S  
ATOM    252  N   PRO A  94     126.891 115.199  69.595  1.00 48.14           N  
ATOM    253  CA  PRO A  94     127.722 114.347  70.457  1.00 48.14           C  
ATOM    254  C   PRO A  94     127.008 113.112  70.986  1.00 48.14           C  
ATOM    255  O   PRO A  94     127.642 112.300  71.669  1.00 48.14           O  
ATOM    256  CB  PRO A  94     128.112 115.291  71.603  1.00 48.14           C  
ATOM    257  CG  PRO A  94     126.986 116.262  71.680  1.00 48.14           C  
ATOM    258  CD  PRO A  94     126.485 116.444  70.268  1.00 48.14           C  
ATOM    259  N   ALA A  95     125.718 112.946  70.703  1.00 39.77           N  
ATOM    260  CA  ALA A  95     124.972 111.753  71.077  1.00 39.77           C  
ATOM    261  C   ALA A  95     125.004 110.675  70.001  1.00 39.77           C  
ATOM    262  O   ALA A  95     124.343 109.644  70.156  1.00 39.77           O  
ATOM    263  CB  ALA A  95     123.521 112.118  71.399  1.00 39.77           C  
ATOM    264  N   VAL A  96     125.744 110.890  68.917  1.00 44.30           N  
ATOM    265  CA  VAL A  96     125.812 109.959  67.797  1.00 44.30           C  
ATOM    266  C   VAL A  96     127.094 109.147  67.899  1.00 44.30           C  
ATOM    267  O   VAL A  96     128.175 109.703  68.130  1.00 44.30           O  
ATOM    268  CB  VAL A  96     125.743 110.706  66.455  1.00 44.30           C  
ATOM    269  CG1 VAL A  96     125.701 109.722  65.305  1.00 44.30           C  
ATOM    270  CG2 VAL A  96     124.525 111.608  66.422  1.00 44.30           C  
ATOM    271  N   ALA A  97     126.976 107.833  67.731  1.00 47.66           N  
ATOM    272  CA  ALA A  97     128.151 106.982  67.652  1.00 47.66           C  
ATOM    273  C   ALA A  97     128.881 107.209  66.331  1.00 47.66           C  
ATOM    274  O   ALA A  97     128.294 107.618  65.326  1.00 47.66           O  
ATOM    275  CB  ALA A  97     127.761 105.510  67.793  1.00 47.66           C  
ATOM    276  N   LYS A  98     130.184 106.938  66.344  1.00 54.76           N  
ATOM    277  CA  LYS A  98     131.022 107.149  65.170  1.00 54.76           C  
ATOM    278  C   LYS A  98     130.826 106.012  64.173  1.00 54.76           C  
ATOM    279  O   LYS A  98     130.935 104.835  64.535  1.00 54.76           O  
ATOM    280  CB  LYS A  98     132.489 107.259  65.579  1.00 54.76           C  
ATOM    281  N   HIS A  99     130.543 106.362  62.921  1.00 60.15           N  
ATOM    282  CA  HIS A  99     130.410 105.399  61.836  1.00 60.15           C  
ATOM    283  C   HIS A  99     131.582 105.553  60.876  1.00 60.15           C  
ATOM    284  O   HIS A  99     131.918 106.673  60.476  1.00 60.15           O  
ATOM    285  CB  HIS A  99     129.090 105.589  61.085  1.00 60.15           C  
ATOM    286  CG  HIS A  99     127.876 105.248  61.892  1.00 60.15           C  
ATOM    287  ND1 HIS A  99     127.722 104.034  62.528  1.00 60.15           N  
ATOM    288  CD2 HIS A  99     126.754 105.957  62.157  1.00 60.15           C  
ATOM    289  CE1 HIS A  99     126.559 104.013  63.154  1.00 60.15           C  
ATOM    290  NE2 HIS A  99     125.952 105.167  62.945  1.00 60.15           N  
ATOM    291  N   ASP A 100     132.196 104.433  60.509  1.00 62.49           N  
ATOM    292  CA  ASP A 100     133.338 104.449  59.599  1.00 62.49           C  
ATOM    293  C   ASP A 100     132.912 104.825  58.184  1.00 62.49           C  
ATOM    294  O   ASP A 100     132.040 104.184  57.596  1.00 62.49           O  
ATOM    295  CB  ASP A 100     134.038 103.089  59.593  1.00 62.49           C  
ATOM    296  N   ARG A 118     133.438 101.525  71.138  1.00 55.07           N  
ATOM    297  CA  ARG A 118     132.549 102.320  70.299  1.00 55.07           C  
ATOM    298  C   ARG A 118     131.095 102.052  70.673  1.00 55.07           C  
ATOM    299  O   ARG A 118     130.301 102.978  70.833  1.00 55.07           O  
ATOM    300  CB  ARG A 118     132.799 102.014  68.821  1.00 55.07           C  
ATOM    301  CG  ARG A 118     131.705 102.478  67.875  1.00 55.07           C  
ATOM    302  CD  ARG A 118     131.605 101.560  66.667  1.00 55.07           C  
ATOM    303  NE  ARG A 118     130.571 101.989  65.731  1.00 55.07           N  
ATOM    304  CZ  ARG A 118     129.875 101.163  64.958  1.00 55.07           C  
ATOM    305  NH1 ARG A 118     130.103  99.858  65.009  1.00 55.07           N  
ATOM    306  NH2 ARG A 118     128.953 101.639  64.134  1.00 55.07           N  
ATOM    307  N   LEU A 119     130.759 100.773  70.820  1.00 44.72           N  
ATOM    308  CA  LEU A 119     129.439 100.355  71.265  1.00 44.72           C  
ATOM    309  C   LEU A 119     129.615  99.183  72.217  1.00 44.72           C  
ATOM    310  O   LEU A 119     130.629  98.482  72.184  1.00 44.72           O  
ATOM    311  CB  LEU A 119     128.533  99.970  70.087  1.00 44.72           C  
ATOM    312  CG  LEU A 119     128.269 101.040  69.023  1.00 44.72           C  
ATOM    313  CD1 LEU A 119     127.724 100.415  67.750  1.00 44.72           C  
ATOM    314  CD2 LEU A 119     127.320 102.105  69.545  1.00 44.72           C  
ATOM    315  N   THR A 120     128.622  98.976  73.073  1.00 34.33           N  
ATOM    316  CA  THR A 120     128.699  97.954  74.106  1.00 34.33           C  
ATOM    317  C   THR A 120     127.890  96.727  73.708  1.00 34.33           C  
ATOM    318  O   THR A 120     127.158  96.720  72.714  1.00 34.33           O  
ATOM    319  CB  THR A 120     128.212  98.493  75.455  1.00 34.33           C  
ATOM    320  OG1 THR A 120     126.927  99.100  75.297  1.00 34.33           O  
ATOM    321  CG2 THR A 120     129.188  99.523  75.995  1.00 34.33           C  
ATOM    322  N   LYS A 121     128.047  95.672  74.510  1.00 32.76           N  
ATOM    323  CA  LYS A 121     127.393  94.402  74.219  1.00 32.76           C  
ATOM    324  C   LYS A 121     125.876  94.524  74.241  1.00 32.76           C  
ATOM    325  O   LYS A 121     125.190  93.845  73.470  1.00 32.76           O  
ATOM    326  CB  LYS A 121     127.850  93.344  75.223  1.00 32.76           C  
ATOM    327  CG  LYS A 121     127.733  91.915  74.733  1.00 32.76           C  
ATOM    328  CD  LYS A 121     127.668  90.945  75.898  1.00 32.76           C  
ATOM    329  CE  LYS A 121     127.824  89.509  75.429  1.00 32.76           C  
ATOM    330  NZ  LYS A 121     126.578  88.979  74.812  1.00 32.76           N  
ATOM    331  N   TYR A 122     125.337  95.379  75.105  1.00 26.90           N  
ATOM    332  CA  TYR A 122     123.905  95.450  75.353  1.00 26.90           C  
ATOM    333  C   TYR A 122     123.401  96.864  75.107  1.00 26.90           C  
ATOM    334  O   TYR A 122     124.124  97.838  75.336  1.00 26.90           O  
ATOM    335  CB  TYR A 122     123.582  95.026  76.786  1.00 26.90           C  
ATOM    336  CG  TYR A 122     123.867  93.570  77.070  1.00 26.90           C  
ATOM    337  CD1 TYR A 122     123.238  92.566  76.352  1.00 26.90           C  
ATOM    338  CD2 TYR A 122     124.767  93.202  78.059  1.00 26.90           C  
ATOM    339  CE1 TYR A 122     123.498  91.237  76.608  1.00 26.90           C  
ATOM    340  CE2 TYR A 122     125.031  91.877  78.323  1.00 26.90           C  
ATOM    341  CZ  TYR A 122     124.395  90.899  77.596  1.00 26.90           C  
ATOM    342  OH  TYR A 122     124.657  89.575  77.857  1.00 26.90           O  
ATOM    343  N   THR A 123     122.165  96.970  74.629  1.00 19.86           N  
ATOM    344  CA  THR A 123     121.515  98.248  74.389  1.00 19.86           C  
ATOM    345  C   THR A 123     120.544  98.570  75.523  1.00 19.86           C  
ATOM    346  O   THR A 123     120.392  97.813  76.482  1.00 19.86           O  
ATOM    347  CB  THR A 123     120.791  98.238  73.044  1.00 19.86           C  
ATOM    348  OG1 THR A 123     119.945  97.086  72.969  1.00 19.86           O  
ATOM    349  CG2 THR A 123     121.791  98.192  71.912  1.00 19.86           C  
ATOM    350  N   MET A 124     119.884  99.726  75.409  1.00 17.28           N  
ATOM    351  CA  MET A 124     118.847 100.101  76.363  1.00 17.28           C  
ATOM    352  C   MET A 124     117.656  99.156  76.324  1.00 17.28           C  
ATOM    353  O   MET A 124     116.999  98.954  77.354  1.00 17.28           O  
ATOM    354  CB  MET A 124     118.377 101.531  76.088  1.00 17.28           C  
ATOM    355  CG  MET A 124     119.292 102.618  76.613  1.00 17.28           C  
ATOM    356  SD  MET A 124     119.624 102.452  78.373  1.00 17.28           S  
ATOM    357  CE  MET A 124     118.328 103.481  79.054  1.00 17.28           C  
ATOM    358  N   ALA A 125     117.372  98.559  75.167  1.00 13.38           N  
ATOM    359  CA  ALA A 125     116.262  97.623  75.073  1.00 13.38           C  
ATOM    360  C   ALA A 125     116.547  96.339  75.833  1.00 13.38           C  
ATOM    361  O   ALA A 125     115.617  95.708  76.337  1.00 13.38           O  
ATOM    362  CB  ALA A 125     115.949  97.313  73.610  1.00 13.38           C  
ATOM    363  N   ASP A 126     117.817  95.955  75.956  1.00 14.65           N  
ATOM    364  CA  ASP A 126     118.145  94.776  76.746  1.00 14.65           C  
ATOM    365  C   ASP A 126     117.853  95.008  78.222  1.00 14.65           C  
ATOM    366  O   ASP A 126     117.268  94.146  78.885  1.00 14.65           O  
ATOM    367  CB  ASP A 126     119.609  94.396  76.537  1.00 14.65           C  
ATOM    368  CG  ASP A 126     119.884  93.916  75.132  1.00 14.65           C  
ATOM    369  OD1 ASP A 126     119.058  93.151  74.599  1.00 14.65           O  
ATOM    370  OD2 ASP A 126     120.925  94.300  74.559  1.00 14.65           O  
ATOM    371  N   LEU A 127     118.225  96.176  78.744  1.00 10.27           N  
ATOM    372  CA  LEU A 127     117.899  96.509  80.126  1.00 10.27           C  
ATOM    373  C   LEU A 127     116.392  96.593  80.330  1.00 10.27           C  
ATOM    374  O   LEU A 127     115.856  96.088  81.328  1.00 10.27           O  
ATOM    375  CB  LEU A 127     118.569  97.826  80.511  1.00 10.27           C  
ATOM    376  CG  LEU A 127     118.554  98.191  81.993  1.00 10.27           C  
ATOM    377  CD1 LEU A 127     119.682  97.502  82.724  1.00 10.27           C  
ATOM    378  CD2 LEU A 127     118.647  99.693  82.154  1.00 10.27           C  
ATOM    379  N   VAL A 128     115.691  97.232  79.391  1.00  8.42           N  
ATOM    380  CA  VAL A 128     114.248  97.398  79.538  1.00  8.42           C  
ATOM    381  C   VAL A 128     113.550  96.043  79.526  1.00  8.42           C  
ATOM    382  O   VAL A 128     112.678  95.771  80.361  1.00  8.42           O  
ATOM    383  CB  VAL A 128     113.706  98.342  78.450  1.00  8.42           C  
ATOM    384  CG1 VAL A 128     112.196  98.242  78.353  1.00  8.42           C  
ATOM    385  CG2 VAL A 128     114.127  99.770  78.740  1.00  8.42           C  
ATOM    386  N   TYR A 129     113.938  95.162  78.600  1.00  8.56           N  
ATOM    387  CA  TYR A 129     113.335  93.837  78.530  1.00  8.56           C  
ATOM    388  C   TYR A 129     113.695  92.998  79.748  1.00  8.56           C  
ATOM    389  O   TYR A 129     112.866  92.224  80.237  1.00  8.56           O  
ATOM    390  CB  TYR A 129     113.769  93.128  77.247  1.00  8.56           C  
ATOM    391  CG  TYR A 129     112.952  91.898  76.921  1.00  8.56           C  
ATOM    392  CD1 TYR A 129     113.316  90.650  77.399  1.00  8.56           C  
ATOM    393  CD2 TYR A 129     111.820  91.988  76.128  1.00  8.56           C  
ATOM    394  CE1 TYR A 129     112.570  89.532  77.108  1.00  8.56           C  
ATOM    395  CE2 TYR A 129     111.070  90.874  75.830  1.00  8.56           C  
ATOM    396  CZ  TYR A 129     111.450  89.647  76.320  1.00  8.56           C  
ATOM    397  OH  TYR A 129     110.705  88.531  76.025  1.00  8.56           O  
ATOM    398  N   ALA A 130     114.931  93.114  80.239  1.00  6.82           N  
ATOM    399  CA  ALA A 130     115.339  92.328  81.396  1.00  6.82           C  
ATOM    400  C   ALA A 130     114.545  92.713  82.633  1.00  6.82           C  
ATOM    401  O   ALA A 130     114.104  91.841  83.390  1.00  6.82           O  
ATOM    402  CB  ALA A 130     116.835  92.499  81.650  1.00  6.82           C  
ATOM    403  N   LEU A 131     114.343  94.012  82.860  1.00  5.84           N  
ATOM    404  CA  LEU A 131     113.608  94.415  84.053  1.00  5.84           C  
ATOM    405  C   LEU A 131     112.096  94.337  83.880  1.00  5.84           C  
ATOM    406  O   LEU A 131     111.377  94.302  84.882  1.00  5.84           O  
ATOM    407  CB  LEU A 131     114.012  95.826  84.475  1.00  5.84           C  
ATOM    408  CG  LEU A 131     115.438  95.968  85.011  1.00  5.84           C  
ATOM    409  CD1 LEU A 131     115.877  97.419  85.009  1.00  5.84           C  
ATOM    410  CD2 LEU A 131     115.552  95.378  86.402  1.00  5.84           C  
ATOM    411  N   ARG A 132     111.584  94.267  82.657  1.00  6.15           N  
ATOM    412  CA  ARG A 132     110.131  94.163  82.375  1.00  6.15           C  
ATOM    413  C   ARG A 132     109.694  92.708  82.200  1.00  6.15           C  
ATOM    414  O   ARG A 132     108.497  92.467  82.228  1.00  6.15           O  
ATOM    415  CB  ARG A 132     109.682  95.086  81.241  1.00  6.15           C  
ATOM    416  CG  ARG A 132     109.373  96.514  81.662  1.00  6.15           C  
ATOM    417  CD  ARG A 132     109.187  97.351  80.420  1.00  6.15           C  
ATOM    418  NE  ARG A 132     107.986  98.166  80.392  1.00  6.15           N  
ATOM    419  CZ  ARG A 132     106.823  97.757  79.915  1.00  6.15           C  
ATOM    420  NH1 ARG A 132     106.694  96.535  79.435  1.00  6.15           N  
ATOM    421  NH2 ARG A 132     105.789  98.566  79.922  1.00  6.15           N  
ATOM    422  N   HIS A 133     110.630  91.777  82.022  1.00  6.27           N  
ATOM    423  CA  HIS A 133     110.283  90.376  81.843  1.00  6.27           C  
ATOM    424  C   HIS A 133     111.131  89.508  82.751  1.00  6.27           C  
ATOM    425  O   HIS A 133     111.693  88.495  82.331  1.00  6.27           O  
ATOM    426  CB  HIS A 133     110.441  89.957  80.387  1.00  6.27           C  
ATOM    427  CG  HIS A 133     109.629  90.777  79.436  1.00  6.27           C  
ATOM    428  ND1 HIS A 133     109.876  92.110  79.202  1.00  6.27           N  
ATOM    429  CD2 HIS A 133     108.552  90.456  78.682  1.00  6.27           C  
ATOM    430  CE1 HIS A 133     109.000  92.570  78.328  1.00  6.27           C  
ATOM    431  NE2 HIS A 133     108.182  91.588  78.000  1.00  6.27           N  
ATOM    432  N   PHE A 134     111.234  89.906  84.014  1.00 10.60           N  
ATOM    433  CA  PHE A 134     112.121  89.235  84.950  1.00 10.60           C  
ATOM    434  C   PHE A 134     111.703  87.790  85.186  1.00 10.60           C  
ATOM    435  O   PHE A 134     110.524  87.492  85.398  1.00 10.60           O  
ATOM    436  CB  PHE A 134     112.149  89.990  86.274  1.00 10.60           C  
ATOM    437  CG  PHE A 134     113.101  89.414  87.270  1.00 10.60           C  
ATOM    438  CD1 PHE A 134     114.464  89.519  87.084  1.00 10.60           C  
ATOM    439  CD2 PHE A 134     112.632  88.753  88.387  1.00 10.60           C  
ATOM    440  CE1 PHE A 134     115.342  88.982  87.998  1.00 10.60           C  
ATOM    441  CE2 PHE A 134     113.505  88.217  89.304  1.00 10.60           C  
ATOM    442  CZ  PHE A 134     114.861  88.331  89.108  1.00 10.60           C  
ATOM    443  N   ASP A 135     112.683  86.894  85.148  1.00 21.19           N  
ATOM    444  CA  ASP A 135     112.502  85.509  85.547  1.00 21.19           C  
ATOM    445  C   ASP A 135     113.775  85.052  86.235  1.00 21.19           C  
ATOM    446  O   ASP A 135     114.853  85.114  85.641  1.00 21.19           O  
ATOM    447  CB  ASP A 135     112.194  84.614  84.343  1.00 21.19           C  
ATOM    448  CG  ASP A 135     111.931  83.180  84.740  1.00 21.19           C  
ATOM    449  OD1 ASP A 135     111.296  82.964  85.794  1.00 21.19           O  
ATOM    450  OD2 ASP A 135     112.353  82.268  84.001  1.00 21.19           O  
ATOM    451  N   GLU A 136     113.656  84.609  87.482  1.00 20.76           N  
ATOM    452  CA  GLU A 136     114.824  84.112  88.193  1.00 20.76           C  
ATOM    453  C   GLU A 136     115.225  82.742  87.655  1.00 20.76           C  
ATOM    454  O   GLU A 136     114.379  81.905  87.331  1.00 20.76           O  
ATOM    455  CB  GLU A 136     114.561  84.064  89.702  1.00 20.76           C  
ATOM    456  CG  GLU A 136     113.787  82.863  90.249  1.00 20.76           C  
ATOM    457  CD  GLU A 136     112.441  82.626  89.587  1.00 20.76           C  
ATOM    458  OE1 GLU A 136     111.847  81.557  89.839  1.00 20.76           O  
ATOM    459  OE2 GLU A 136     111.951  83.509  88.853  1.00 20.76           O  
ATOM    460  N   GLY A 137     116.530  82.531  87.528  1.00 25.88           N  
ATOM    461  CA  GLY A 137     117.055  81.359  86.866  1.00 25.88           C  
ATOM    462  C   GLY A 137     117.064  81.437  85.356  1.00 25.88           C  
ATOM    463  O   GLY A 137     117.542  80.499  84.706  1.00 25.88           O  
ATOM    464  N   ASN A 138     116.542  82.514  84.779  1.00 27.03           N  
ATOM    465  CA  ASN A 138     116.628  82.803  83.356  1.00 27.03           C  
ATOM    466  C   ASN A 138     116.967  84.287  83.214  1.00 27.03           C  
ATOM    467  O   ASN A 138     116.360  85.035  82.452  1.00 27.03           O  
ATOM    468  CB  ASN A 138     115.328  82.419  82.649  1.00 27.03           C  
ATOM    469  CG  ASN A 138     115.397  82.611  81.147  1.00 27.03           C  
ATOM    470  OD1 ASN A 138     114.487  83.174  80.539  1.00 27.03           O  
ATOM    471  ND2 ASN A 138     116.479  82.140  80.538  1.00 27.03           N  
ATOM    472  N   CYS A 139     117.956  84.741  83.988  1.00 26.54           N  
ATOM    473  CA  CYS A 139     118.229  86.166  84.136  1.00 26.54           C  
ATOM    474  C   CYS A 139     119.719  86.483  84.037  1.00 26.54           C  
ATOM    475  O   CYS A 139     120.207  87.399  84.706  1.00 26.54           O  
ATOM    476  CB  CYS A 139     117.651  86.686  85.455  1.00 26.54           C  
ATOM    477  SG  CYS A 139     118.558  86.206  86.937  1.00 26.54           S  
ATOM    478  N   ASP A 140     120.453  85.756  83.194  1.00 30.28           N  
ATOM    479  CA  ASP A 140     121.887  85.989  83.072  1.00 30.28           C  
ATOM    480  C   ASP A 140     122.216  87.304  82.374  1.00 30.28           C  
ATOM    481  O   ASP A 140     123.293  87.861  82.610  1.00 30.28           O  
ATOM    482  CB  ASP A 140     122.544  84.828  82.326  1.00 30.28           C  
ATOM    483  CG  ASP A 140     122.720  83.602  83.200  1.00 30.28           C  
ATOM    484  OD1 ASP A 140     121.785  82.779  83.267  1.00 30.28           O  
ATOM    485  OD2 ASP A 140     123.792  83.465  83.825  1.00 30.28           O  
ATOM    486  N   THR A 141     121.318  87.818  81.532  1.00 24.45           N  
ATOM    487  CA  THR A 141     121.546  89.120  80.914  1.00 24.45           C  
ATOM    488  C   THR A 141     121.548  90.227  81.961  1.00 24.45           C  
ATOM    489  O   THR A 141     122.404  91.120  81.938  1.00 24.45           O  
ATOM    490  CB  THR A 141     120.482  89.387  79.849  1.00 24.45           C  
ATOM    491  OG1 THR A 141     120.523  88.354  78.859  1.00 24.45           O  
ATOM    492  CG2 THR A 141     120.720  90.726  79.176  1.00 24.45           C  
ATOM    493  N   LEU A 142     120.591  90.182  82.889  1.00 20.67           N  
ATOM    494  CA  LEU A 142     120.558  91.157  83.973  1.00 20.67           C  
ATOM    495  C   LEU A 142     121.799  91.047  84.848  1.00 20.67           C  
ATOM    496  O   LEU A 142     122.367  92.064  85.259  1.00 20.67           O  
ATOM    497  CB  LEU A 142     119.294  90.968  84.810  1.00 20.67           C  
ATOM    498  CG  LEU A 142     118.965  92.067  85.817  1.00 20.67           C  
ATOM    499  CD1 LEU A 142     118.701  93.378  85.105  1.00 20.67           C  
ATOM    500  CD2 LEU A 142     117.779  91.671  86.670  1.00 20.67           C  
ATOM    501  N   LYS A 143     122.230  89.820  85.151  1.00 24.19           N  
ATOM    502  CA  LYS A 143     123.445  89.638  85.937  1.00 24.19           C  
ATOM    503  C   LYS A 143     124.649  90.245  85.233  1.00 24.19           C  
ATOM    504  O   LYS A 143     125.473  90.922  85.862  1.00 24.19           O  
ATOM    505  CB  LYS A 143     123.686  88.153  86.198  1.00 24.19           C  
ATOM    506  CG  LYS A 143     122.970  87.593  87.408  1.00 24.19           C  
ATOM    507  CD  LYS A 143     122.694  86.115  87.233  1.00 24.19           C  
ATOM    508  CE  LYS A 143     121.754  85.602  88.298  1.00 24.19           C  
ATOM    509  NZ  LYS A 143     121.717  84.118  88.327  1.00 24.19           N  
ATOM    510  N   GLU A 144     124.764  90.018  83.923  1.00 27.97           N  
ATOM    511  CA  GLU A 144     125.909  90.538  83.188  1.00 27.97           C  
ATOM    512  C   GLU A 144     125.878  92.057  83.125  1.00 27.97           C  
ATOM    513  O   GLU A 144     126.923  92.707  83.226  1.00 27.97           O  
ATOM    514  CB  GLU A 144     125.953  89.937  81.785  1.00 27.97           C  
ATOM    515  CG  GLU A 144     127.250  90.207  81.044  1.00 27.97           C  
ATOM    516  CD  GLU A 144     128.330  89.191  81.364  1.00 27.97           C  
ATOM    517  OE1 GLU A 144     129.316  89.564  82.035  1.00 27.97           O  
ATOM    518  OE2 GLU A 144     128.196  88.022  80.944  1.00 27.97           O  
ATOM    519  N   ILE A 145     124.692  92.643  82.959  1.00 23.23           N  
ATOM    520  CA  ILE A 145     124.587  94.099  82.963  1.00 23.23           C  
ATOM    521  C   ILE A 145     124.968  94.662  84.328  1.00 23.23           C  
ATOM    522  O   ILE A 145     125.683  95.666  84.424  1.00 23.23           O  
ATOM    523  CB  ILE A 145     123.175  94.540  82.535  1.00 23.23           C  
ATOM    524  CG1 ILE A 145     122.979  94.303  81.037  1.00 23.23           C  
ATOM    525  CG2 ILE A 145     122.948  96.000  82.866  1.00 23.23           C  
ATOM    526  CD1 ILE A 145     121.539  94.108  80.630  1.00 23.23           C  
ATOM    527  N   LEU A 146     124.506  94.023  85.406  1.00 24.81           N  
ATOM    528  CA  LEU A 146     124.809  94.526  86.741  1.00 24.81           C  
ATOM    529  C   LEU A 146     126.290  94.411  87.080  1.00 24.81           C  
ATOM    530  O   LEU A 146     126.829  95.280  87.773  1.00 24.81           O  
ATOM    531  CB  LEU A 146     123.968  93.799  87.787  1.00 24.81           C  
ATOM    532  CG  LEU A 146     122.469  94.099  87.754  1.00 24.81           C  
ATOM    533  CD1 LEU A 146     121.717  93.202  88.718  1.00 24.81           C  
ATOM    534  CD2 LEU A 146     122.219  95.562  88.070  1.00 24.81           C  
ATOM    535  N   VAL A 147     126.964  93.361  86.616  1.00 29.43           N  
ATOM    536  CA  VAL A 147     128.380  93.219  86.946  1.00 29.43           C  
ATOM    537  C   VAL A 147     129.281  93.991  85.982  1.00 29.43           C  
ATOM    538  O   VAL A 147     130.402  94.354  86.348  1.00 29.43           O  
ATOM    539  CB  VAL A 147     128.786  91.737  87.007  1.00 29.43           C  
ATOM    540  CG1 VAL A 147     127.900  90.989  87.977  1.00 29.43           C  
ATOM    541  CG2 VAL A 147     128.733  91.105  85.629  1.00 29.43           C  
ATOM    542  N   THR A 148     128.823  94.244  84.754  1.00 29.74           N  
ATOM    543  CA  THR A 148     129.638  94.985  83.797  1.00 29.74           C  
ATOM    544  C   THR A 148     129.830  96.431  84.229  1.00 29.74           C  
ATOM    545  O   THR A 148     130.931  96.981  84.115  1.00 29.74           O  
ATOM    546  CB  THR A 148     129.003  94.927  82.410  1.00 29.74           C  
ATOM    547  OG1 THR A 148     128.662  93.573  82.094  1.00 29.74           O  
ATOM    548  CG2 THR A 148     129.963  95.460  81.360  1.00 29.74           C  
ATOM    549  N   TYR A 149     128.770  97.068  84.724  1.00 30.63           N  
ATOM    550  CA  TYR A 149     128.797  98.487  85.047  1.00 30.63           C  
ATOM    551  C   TYR A 149     128.970  98.744  86.539  1.00 30.63           C  
ATOM    552  O   TYR A 149     128.614  99.824  87.022  1.00 30.63           O  
ATOM    553  CB  TYR A 149     127.538  99.164  84.511  1.00 30.63           C  
ATOM    554  CG  TYR A 149     127.506  99.155  83.001  1.00 30.63           C  
ATOM    555  CD1 TYR A 149     128.389  99.932  82.268  1.00 30.63           C  
ATOM    556  CD2 TYR A 149     126.617  98.347  82.310  1.00 30.63           C  
ATOM    557  CE1 TYR A 149     128.378  99.917  80.892  1.00 30.63           C  
ATOM    558  CE2 TYR A 149     126.600  98.325  80.934  1.00 30.63           C  
ATOM    559  CZ  TYR A 149     127.482  99.113  80.228  1.00 30.63           C  
ATOM    560  OH  TYR A 149     127.468  99.096  78.854  1.00 30.63           O  
ATOM    561  N   ASN A 150     129.513  97.770  87.269  1.00 36.12           N  
ATOM    562  CA  ASN A 150     129.901  97.931  88.670  1.00 36.12           C  
ATOM    563  C   ASN A 150     128.729  98.366  89.545  1.00 36.12           C  
ATOM    564  O   ASN A 150     128.881  99.180  90.458  1.00 36.12           O  
ATOM    565  CB  ASN A 150     131.071  98.907  88.807  1.00 36.12           C  
ATOM    566  CG  ASN A 150     132.177  98.635  87.807  1.00 36.12           C  
ATOM    567  OD1 ASN A 150     132.724  99.556  87.203  1.00 36.12           O  
ATOM    568  ND2 ASN A 150     132.514  97.363  87.630  1.00 36.12           N  
ATOM    569  N   CYS A 151     127.544  97.826  89.263  1.00 28.28           N  
ATOM    570  CA  CYS A 151     126.458  97.919  90.232  1.00 28.28           C  
ATOM    571  C   CYS A 151     126.698  96.970  91.397  1.00 28.28           C  
ATOM    572  O   CYS A 151     126.467  97.327  92.557  1.00 28.28           O  
ATOM    573  CB  CYS A 151     125.119  97.626  89.558  1.00 28.28           C  
ATOM    574  SG  CYS A 151     124.763  98.671  88.133  1.00 28.28           S  
ATOM    575  N   CYS A 152     127.169  95.765  91.104  1.00 35.09           N  
ATOM    576  CA  CYS A 152     127.536  94.778  92.110  1.00 35.09           C  
ATOM    577  C   CYS A 152     128.654  93.921  91.522  1.00 35.09           C  
ATOM    578  O   CYS A 152     129.271  94.292  90.519  1.00 35.09           O  
ATOM    579  CB  CYS A 152     126.303  93.966  92.540  1.00 35.09           C  
ATOM    580  SG  CYS A 152     125.586  92.963  91.231  1.00 35.09           S  
ATOM    581  N   ASP A 153     128.922  92.776  92.145  1.00 41.74           N  
ATOM    582  CA  ASP A 153     129.927  91.847  91.650  1.00 41.74           C  
ATOM    583  C   ASP A 153     129.328  90.449  91.590  1.00 41.74           C  
ATOM    584  O   ASP A 153     128.234  90.195  92.099  1.00 41.74           O  
ATOM    585  CB  ASP A 153     131.193  91.867  92.514  1.00 41.74           C  
ATOM    586  CG  ASP A 153     130.888  91.902  93.992  1.00 41.74           C  
ATOM    587  OD1 ASP A 153     129.694  91.964  94.352  1.00 41.74           O  
ATOM    588  OD2 ASP A 153     131.844  91.880  94.796  1.00 41.74           O  
ATOM    589  N   ASP A 154     130.069  89.538  90.951  1.00 43.23           N  
ATOM    590  CA  ASP A 154     129.536  88.217  90.626  1.00 43.23           C  
ATOM    591  C   ASP A 154     129.065  87.461  91.860  1.00 43.23           C  
ATOM    592  O   ASP A 154     128.140  86.646  91.771  1.00 43.23           O  
ATOM    593  CB  ASP A 154     130.595  87.394  89.893  1.00 43.23           C  
ATOM    594  CG  ASP A 154     131.265  88.168  88.779  1.00 43.23           C  
ATOM    595  OD1 ASP A 154     130.688  88.240  87.674  1.00 43.23           O  
ATOM    596  OD2 ASP A 154     132.368  88.708  89.009  1.00 43.23           O  
ATOM    597  N   ASP A 155     129.681  87.711  93.014  1.00 40.51           N  
ATOM    598  CA  ASP A 155     129.346  86.969  94.221  1.00 40.51           C  
ATOM    599  C   ASP A 155     128.063  87.444  94.888  1.00 40.51           C  
ATOM    600  O   ASP A 155     127.595  86.788  95.824  1.00 40.51           O  
ATOM    601  CB  ASP A 155     130.518  87.025  95.210  1.00 40.51           C  
ATOM    602  CG  ASP A 155     130.839  88.439  95.682  1.00 40.51           C  
ATOM    603  OD1 ASP A 155     129.998  89.350  95.542  1.00 40.51           O  
ATOM    604  OD2 ASP A 155     131.957  88.639  96.202  1.00 40.51           O  
ATOM    605  N   TYR A 156     127.492  88.565  94.442  1.00 28.98           N  
ATOM    606  CA  TYR A 156     126.262  89.058  95.050  1.00 28.98           C  
ATOM    607  C   TYR A 156     125.101  88.097  94.831  1.00 28.98           C  
ATOM    608  O   TYR A 156     124.205  88.005  95.677  1.00 28.98           O  
ATOM    609  CB  TYR A 156     125.920  90.440  94.493  1.00 28.98           C  
ATOM    610  CG  TYR A 156     124.862  91.179  95.280  1.00 28.98           C  
ATOM    611  CD1 TYR A 156     125.187  91.851  96.448  1.00 28.98           C  
ATOM    612  CD2 TYR A 156     123.541  91.207  94.856  1.00 28.98           C  
ATOM    613  CE1 TYR A 156     124.231  92.529  97.170  1.00 28.98           C  
ATOM    614  CE2 TYR A 156     122.577  91.883  95.574  1.00 28.98           C  
ATOM    615  CZ  TYR A 156     122.927  92.543  96.731  1.00 28.98           C  
ATOM    616  OH  TYR A 156     121.975  93.219  97.455  1.00 28.98           O  
ATOM    617  N   PHE A 157     125.097  87.379  93.711  1.00 28.68           N  
ATOM    618  CA  PHE A 157     123.983  86.514  93.344  1.00 28.68           C  
ATOM    619  C   PHE A 157     124.043  85.139  93.995  1.00 28.68           C  
ATOM    620  O   PHE A 157     123.143  84.326  93.761  1.00 28.68           O  
ATOM    621  CB  PHE A 157     123.921  86.365  91.825  1.00 28.68           C  
ATOM    622  CG  PHE A 157     124.285  87.615  91.084  1.00 28.68           C  
ATOM    623  CD1 PHE A 157     123.564  88.778  91.267  1.00 28.68           C  
ATOM    624  CD2 PHE A 157     125.360  87.631  90.219  1.00 28.68           C  
ATOM    625  CE1 PHE A 157     123.900  89.927  90.592  1.00 28.68           C  
ATOM    626  CE2 PHE A 157     125.700  88.778  89.543  1.00 28.68           C  
ATOM    627  CZ  PHE A 157     124.969  89.927  89.730  1.00 28.68           C  
ATOM    628  N   ASN A 158     125.071  84.849  94.792  1.00 36.09           N  
ATOM    629  CA  ASN A 158     125.069  83.618  95.571  1.00 36.09           C  
ATOM    630  C   ASN A 158     124.180  83.720  96.801  1.00 36.09           C  
ATOM    631  O   ASN A 158     123.777  82.687  97.346  1.00 36.09           O  
ATOM    632  CB  ASN A 158     126.492  83.245  95.987  1.00 36.09           C  
ATOM    633  CG  ASN A 158     127.479  83.350  94.844  1.00 36.09           C  
ATOM    634  OD1 ASN A 158     128.588  83.857  95.010  1.00 36.09           O  
ATOM    635  ND2 ASN A 158     127.075  82.881  93.671  1.00 36.09           N  
ATOM    636  N   LYS A 159     123.880  84.935  97.252  1.00 30.87           N  
ATOM    637  CA  LYS A 159     122.899  85.127  98.309  1.00 30.87           C  
ATOM    638  C   LYS A 159     121.531  84.634  97.857  1.00 30.87           C  
ATOM    639  O   LYS A 159     121.125  84.844  96.712  1.00 30.87           O  
ATOM    640  CB  LYS A 159     122.824  86.603  98.691  1.00 30.87           C  
ATOM    641  CG  LYS A 159     121.732  86.936  99.691  1.00 30.87           C  
ATOM    642  CD  LYS A 159     121.962  88.287 100.353  1.00 30.87           C  
ATOM    643  CE  LYS A 159     122.673  89.264  99.427  1.00 30.87           C  
ATOM    644  NZ  LYS A 159     122.738  90.626 100.022  1.00 30.87           N  
ATOM    645  N   LYS A 160     120.825  83.961  98.761  1.00 32.43           N  
ATOM    646  CA  LYS A 160     119.474  83.512  98.459  1.00 32.43           C  
ATOM    647  C   LYS A 160     118.537  84.706  98.327  1.00 32.43           C  
ATOM    648  O   LYS A 160     118.553  85.620  99.155  1.00 32.43           O  
ATOM    649  CB  LYS A 160     118.976  82.562  99.550  1.00 32.43           C  
ATOM    650  CG  LYS A 160     117.470  82.329  99.541  1.00 32.43           C  
ATOM    651  CD  LYS A 160     117.021  81.424 100.682  1.00 32.43           C  
ATOM    652  CE  LYS A 160     117.731  81.736 101.993  1.00 32.43           C  
ATOM    653  NZ  LYS A 160     117.637  83.173 102.378  1.00 32.43           N  
ATOM    654  N   ASP A 161     117.712  84.687  97.278  1.00 25.34           N  
ATOM    655  CA  ASP A 161     116.722  85.736  97.025  1.00 25.34           C  
ATOM    656  C   ASP A 161     117.369  87.116  96.919  1.00 25.34           C  
ATOM    657  O   ASP A 161     116.878  88.092  97.486  1.00 25.34           O  
ATOM    658  CB  ASP A 161     115.629  85.734  98.096  1.00 25.34           C  
ATOM    659  CG  ASP A 161     114.764  84.492  98.046  1.00 25.34           C  
ATOM    660  OD1 ASP A 161     114.246  84.169  96.956  1.00 25.34           O  
ATOM    661  OD2 ASP A 161     114.590  83.845  99.099  1.00 25.34           O  
ATOM    662  N   TRP A 162     118.485  87.197  96.190  1.00 19.29           N  
ATOM    663  CA  TRP A 162     119.153  88.481  95.996  1.00 19.29           C  
ATOM    664  C   TRP A 162     118.262  89.475  95.264  1.00 19.29           C  
ATOM    665  O   TRP A 162     118.418  90.690  95.426  1.00 19.29           O  
ATOM    666  CB  TRP A 162     120.456  88.279  95.223  1.00 19.29           C  
ATOM    667  CG  TRP A 162     120.257  87.684  93.862  1.00 19.29           C  
ATOM    668  CD1 TRP A 162     120.283  86.362  93.535  1.00 19.29           C  
ATOM    669  CD2 TRP A 162     120.019  88.394  92.640  1.00 19.29           C  
ATOM    670  NE1 TRP A 162     120.063  86.203  92.191  1.00 19.29           N  
ATOM    671  CE2 TRP A 162     119.899  87.436  91.618  1.00 19.29           C  
ATOM    672  CE3 TRP A 162     119.889  89.747  92.314  1.00 19.29           C  
ATOM    673  CZ2 TRP A 162     119.658  87.786  90.293  1.00 19.29           C  
ATOM    674  CZ3 TRP A 162     119.650  90.091  90.999  1.00 19.29           C  
ATOM    675  CH2 TRP A 162     119.538  89.115  90.005  1.00 19.29           C  
ATOM    676  N   TYR A 163     117.337  88.977  94.454  1.00 15.51           N  
ATOM    677  CA  TYR A 163     116.473  89.767  93.591  1.00 15.51           C  
ATOM    678  C   TYR A 163     115.166  90.204  94.244  1.00 15.51           C  
ATOM    679  O   TYR A 163     114.409  90.958  93.626  1.00 15.51           O  
ATOM    680  CB  TYR A 163     116.189  88.959  92.322  1.00 15.51           C  
ATOM    681  CG  TYR A 163     115.663  87.571  92.615  1.00 15.51           C  
ATOM    682  CD1 TYR A 163     114.389  87.372  93.128  1.00 15.51           C  
ATOM    683  CD2 TYR A 163     116.465  86.458  92.417  1.00 15.51           C  
ATOM    684  CE1 TYR A 163     113.926  86.109  93.410  1.00 15.51           C  
ATOM    685  CE2 TYR A 163     116.010  85.192  92.697  1.00 15.51           C  
ATOM    686  CZ  TYR A 163     114.738  85.022  93.192  1.00 15.51           C  
ATOM    687  OH  TYR A 163     114.275  83.759  93.473  1.00 15.51           O  
ATOM    688  N   ASP A 164     114.887  89.764  95.465  1.00 15.87           N  
ATOM    689  CA  ASP A 164     113.573  89.925  96.075  1.00 15.87           C  
ATOM    690  C   ASP A 164     113.516  91.238  96.852  1.00 15.87           C  
ATOM    691  O   ASP A 164     114.301  91.447  97.781  1.00 15.87           O  
ATOM    692  CB  ASP A 164     113.283  88.728  96.981  1.00 15.87           C  
ATOM    693  CG  ASP A 164     111.907  88.775  97.601  1.00 15.87           C  
ATOM    694  OD1 ASP A 164     111.680  89.603  98.502  1.00 15.87           O  
ATOM    695  OD2 ASP A 164     111.050  87.966  97.198  1.00 15.87           O  
ATOM    696  N   PHE A 165     112.581  92.117  96.473  1.00 11.13           N  
ATOM    697  CA  PHE A 165     112.442  93.416  97.129  1.00 11.13           C  
ATOM    698  C   PHE A 165     112.105  93.311  98.610  1.00 11.13           C  
ATOM    699  O   PHE A 165     112.361  94.260  99.357  1.00 11.13           O  
ATOM    700  CB  PHE A 165     111.359  94.260  96.451  1.00 11.13           C  
ATOM    701  CG  PHE A 165     111.578  94.491  94.987  1.00 11.13           C  
ATOM    702  CD1 PHE A 165     112.605  95.305  94.553  1.00 11.13           C  
ATOM    703  CD2 PHE A 165     110.744  93.918  94.047  1.00 11.13           C  
ATOM    704  CE1 PHE A 165     112.804  95.531  93.210  1.00 11.13           C  
ATOM    705  CE2 PHE A 165     110.938  94.145  92.704  1.00 11.13           C  
ATOM    706  CZ  PHE A 165     111.970  94.951  92.286  1.00 11.13           C  
ATOM    707  N   VAL A 166     111.539  92.196  99.054  1.00 14.22           N  
ATOM    708  CA  VAL A 166     111.055  92.045 100.419  1.00 14.22           C  
ATOM    709  C   VAL A 166     112.049  91.271 101.279  1.00 14.22           C  
ATOM    710  O   VAL A 166     112.359  91.677 102.399  1.00 14.22           O  
ATOM    711  CB  VAL A 166     109.662  91.378 100.438  1.00 14.22           C  
ATOM    712  CG1 VAL A 166     109.112  91.331 101.847  1.00 14.22           C  
ATOM    713  CG2 VAL A 166     108.706  92.127  99.525  1.00 14.22           C  
ATOM    714  N   GLU A 167     112.562  90.152 100.769  1.00 22.13           N  
ATOM    715  CA  GLU A 167     113.569  89.407 101.514  1.00 22.13           C  
ATOM    716  C   GLU A 167     114.940  90.068 101.448  1.00 22.13           C  
ATOM    717  O   GLU A 167     115.746  89.898 102.367  1.00 22.13           O  
ATOM    718  CB  GLU A 167     113.657  87.969 101.004  1.00 22.13           C  
ATOM    719  CG  GLU A 167     112.553  87.064 101.520  1.00 22.13           C  
ATOM    720  CD  GLU A 167     112.960  85.601 101.546  1.00 22.13           C  
ATOM    721  OE1 GLU A 167     112.120  84.741 101.208  1.00 22.13           O  
ATOM    722  OE2 GLU A 167     114.119  85.313 101.909  1.00 22.13           O  
ATOM    723  N   ASN A 168     115.222  90.815 100.384  1.00 18.55           N  
ATOM    724  CA  ASN A 168     116.502  91.504 100.215  1.00 18.55           C  
ATOM    725  C   ASN A 168     116.243  92.927  99.738  1.00 18.55           C  
ATOM    726  O   ASN A 168     116.406  93.243  98.558  1.00 18.55           O  
ATOM    727  CB  ASN A 168     117.401  90.751  99.233  1.00 18.55           C  
ATOM    728  CG  ASN A 168     118.770  91.381  99.098  1.00 18.55           C  
ATOM    729  OD1 ASN A 168     119.255  92.038 100.015  1.00 18.55           O  
ATOM    730  ND2 ASN A 168     119.401  91.184  97.949  1.00 18.55           N  
ATOM    731  N   PRO A 169     115.838  93.816 100.649  1.00 17.03           N  
ATOM    732  CA  PRO A 169     115.580  95.209 100.247  1.00 17.03           C  
ATOM    733  C   PRO A 169     116.819  95.957  99.781  1.00 17.03           C  
ATOM    734  O   PRO A 169     116.682  97.057  99.231  1.00 17.03           O  
ATOM    735  CB  PRO A 169     114.999  95.836 101.522  1.00 17.03           C  
ATOM    736  CG  PRO A 169     115.573  95.021 102.625  1.00 17.03           C  
ATOM    737  CD  PRO A 169     115.638  93.615 102.090  1.00 17.03           C  
ATOM    738  N   ASP A 170     118.016  95.407  99.993  1.00 16.79           N  
ATOM    739  CA  ASP A 170     119.241  96.037  99.514  1.00 16.79           C  
ATOM    740  C   ASP A 170     119.323  96.067  97.991  1.00 16.79           C  
ATOM    741  O   ASP A 170     120.115  96.837  97.439  1.00 16.79           O  
ATOM    742  CB  ASP A 170     120.447  95.305 100.108  1.00 16.79           C  
ATOM    743  CG  ASP A 170     121.766  95.778  99.537  1.00 16.79           C  
ATOM    744  OD1 ASP A 170     122.061  96.985  99.642  1.00 16.79           O  
ATOM    745  OD2 ASP A 170     122.508  94.940  98.983  1.00 16.79           O  
ATOM    746  N   ILE A 171     118.519  95.254  97.300  1.00 13.15           N  
ATOM    747  CA  ILE A 171     118.583  95.190  95.841  1.00 13.15           C  
ATOM    748  C   ILE A 171     118.231  96.534  95.218  1.00 13.15           C  
ATOM    749  O   ILE A 171     118.666  96.842  94.103  1.00 13.15           O  
ATOM    750  CB  ILE A 171     117.672  94.060  95.317  1.00 13.15           C  
ATOM    751  CG1 ILE A 171     117.880  93.851  93.818  1.00 13.15           C  
ATOM    752  CG2 ILE A 171     116.212  94.365  95.593  1.00 13.15           C  
ATOM    753  CD1 ILE A 171     119.261  93.375  93.451  1.00 13.15           C  
ATOM    754  N   LEU A 172     117.449  97.358  95.919  1.00 13.21           N  
ATOM    755  CA  LEU A 172     117.130  98.686  95.407  1.00 13.21           C  
ATOM    756  C   LEU A 172     118.378  99.554  95.309  1.00 13.21           C  
ATOM    757  O   LEU A 172     118.498 100.376  94.394  1.00 13.21           O  
ATOM    758  CB  LEU A 172     116.076  99.351  96.291  1.00 13.21           C  
ATOM    759  CG  LEU A 172     114.680  98.727  96.240  1.00 13.21           C  
ATOM    760  CD1 LEU A 172     113.936  98.976  97.536  1.00 13.21           C  
ATOM    761  CD2 LEU A 172     113.892  99.261  95.058  1.00 13.21           C  
ATOM    762  N   ARG A 173     119.311  99.394  96.248  1.00 14.89           N  
ATOM    763  CA  ARG A 173     120.590 100.089  96.157  1.00 14.89           C  
ATOM    764  C   ARG A 173     121.390  99.624  94.946  1.00 14.89           C  
ATOM    765  O   ARG A 173     122.070 100.429  94.301  1.00 14.89           O  
ATOM    766  CB  ARG A 173     121.382  99.881  97.446  1.00 14.89           C  
ATOM    767  CG  ARG A 173     122.572 100.807  97.617  1.00 14.89           C  
ATOM    768  CD  ARG A 173     123.572 100.234  98.609  1.00 14.89           C  
ATOM    769  NE  ARG A 173     123.929  98.850  98.312  1.00 14.89           N  
ATOM    770  CZ  ARG A 173     124.817  98.482  97.396  1.00 14.89           C  
ATOM    771  NH1 ARG A 173     125.453  99.396  96.680  1.00 14.89           N  
ATOM    772  NH2 ARG A 173     125.075  97.197  97.200  1.00 14.89           N  
ATOM    773  N   VAL A 174     121.329  98.328  94.630  1.00 15.00           N  
ATOM    774  CA  VAL A 174     122.047  97.801  93.471  1.00 15.00           C  
ATOM    775  C   VAL A 174     121.471  98.369  92.177  1.00 15.00           C  
ATOM    776  O   VAL A 174     122.211  98.783  91.278  1.00 15.00           O  
ATOM    777  CB  VAL A 174     122.017  96.263  93.476  1.00 15.00           C  
ATOM    778  CG1 VAL A 174     122.650  95.711  92.215  1.00 15.00           C  
ATOM    779  CG2 VAL A 174     122.723  95.725  94.703  1.00 15.00           C  
ATOM    780  N   TYR A 175     120.139  98.386  92.057  1.00 10.51           N  
ATOM    781  CA  TYR A 175     119.519  98.956  90.863  1.00 10.51           C  
ATOM    782  C   TYR A 175     119.743 100.458  90.761  1.00 10.51           C  
ATOM    783  O   TYR A 175     119.808 100.996  89.652  1.00 10.51           O  
ATOM    784  CB  TYR A 175     118.019  98.660  90.826  1.00 10.51           C  
ATOM    785  CG  TYR A 175     117.654  97.207  90.651  1.00 10.51           C  
ATOM    786  CD1 TYR A 175     118.374  96.390  89.792  1.00 10.51           C  
ATOM    787  CD2 TYR A 175     116.559  96.663  91.304  1.00 10.51           C  
ATOM    788  CE1 TYR A 175     118.036  95.065  89.617  1.00 10.51           C  
ATOM    789  CE2 TYR A 175     116.212  95.340  91.131  1.00 10.51           C  
ATOM    790  CZ  TYR A 175     116.952  94.546  90.287  1.00 10.51           C  
ATOM    791  OH  TYR A 175     116.608  93.228  90.115  1.00 10.51           O  
ATOM    792  N   ALA A 176     119.846 101.151  91.894  1.00 10.28           N  
ATOM    793  CA  ALA A 176     120.025 102.597  91.877  1.00 10.28           C  
ATOM    794  C   ALA A 176     121.383 103.028  91.340  1.00 10.28           C  
ATOM    795  O   ALA A 176     121.575 104.222  91.091  1.00 10.28           O  
ATOM    796  CB  ALA A 176     119.826 103.168  93.278  1.00 10.28           C  
ATOM    797  N   ASN A 177     122.333 102.106  91.175  1.00 14.16           N  
ATOM    798  CA  ASN A 177     123.607 102.462  90.562  1.00 14.16           C  
ATOM    799  C   ASN A 177     123.488 102.665  89.058  1.00 14.16           C  
ATOM    800  O   ASN A 177     124.382 103.265  88.454  1.00 14.16           O  
ATOM    801  CB  ASN A 177     124.660 101.398  90.867  1.00 14.16           C  
ATOM    802  CG  ASN A 177     125.016 101.335  92.338  1.00 14.16           C  
ATOM    803  OD1 ASN A 177     124.676 102.229  93.109  1.00 14.16           O  
ATOM    804  ND2 ASN A 177     125.704 100.274  92.735  1.00 14.16           N  
ATOM    805  N   LEU A 178     122.411 102.177  88.443  1.00 11.33           N  
ATOM    806  CA  LEU A 178     122.165 102.392  87.024  1.00 11.33           C  
ATOM    807  C   LEU A 178     121.516 103.737  86.728  1.00 11.33           C  
ATOM    808  O   LEU A 178     121.356 104.076  85.552  1.00 11.33           O  
ATOM    809  CB  LEU A 178     121.276 101.278  86.466  1.00 11.33           C  
ATOM    810  CG  LEU A 178     121.840  99.862  86.358  1.00 11.33           C  
ATOM    811  CD1 LEU A 178     120.709  98.867  86.191  1.00 11.33           C  
ATOM    812  CD2 LEU A 178     122.823  99.750  85.206  1.00 11.33           C  
ATOM    813  N   GLY A 179     121.131 104.496  87.756  1.00 11.87           N  
ATOM    814  CA  GLY A 179     120.347 105.701  87.532  1.00 11.87           C  
ATOM    815  C   GLY A 179     121.064 106.750  86.703  1.00 11.87           C  
ATOM    816  O   GLY A 179     120.446 107.431  85.879  1.00 11.87           O  
ATOM    817  N   GLU A 180     122.373 106.904  86.911  1.00 16.58           N  
ATOM    818  CA  GLU A 180     123.112 107.914  86.161  1.00 16.58           C  
ATOM    819  C   GLU A 180     123.216 107.570  84.684  1.00 16.58           C  
ATOM    820  O   GLU A 180     123.143 108.469  83.840  1.00 16.58           O  
ATOM    821  CB  GLU A 180     124.504 108.107  86.752  1.00 16.58           C  
ATOM    822  CG  GLU A 180     124.505 108.964  87.985  1.00 16.58           C  
ATOM    823  CD  GLU A 180     123.637 110.194  87.821  1.00 16.58           C  
ATOM    824  OE1 GLU A 180     124.021 111.097  87.048  1.00 16.58           O  
ATOM    825  OE2 GLU A 180     122.564 110.256  88.455  1.00 16.58           O  
ATOM    826  N   ARG A 181     123.373 106.290  84.346  1.00 17.57           N  
ATOM    827  CA  ARG A 181     123.410 105.913  82.938  1.00 17.57           C  
ATOM    828  C   ARG A 181     122.078 106.191  82.255  1.00 17.57           C  
ATOM    829  O   ARG A 181     122.046 106.677  81.120  1.00 17.57           O  
ATOM    830  CB  ARG A 181     123.802 104.446  82.793  1.00 17.57           C  
ATOM    831  CG  ARG A 181     125.117 104.120  83.455  1.00 17.57           C  
ATOM    832  CD  ARG A 181     125.727 102.862  82.889  1.00 17.57           C  
ATOM    833  NE  ARG A 181     126.599 103.177  81.764  1.00 17.57           N  
ATOM    834  CZ  ARG A 181     127.922 103.248  81.842  1.00 17.57           C  
ATOM    835  NH1 ARG A 181     128.532 103.041  83.000  1.00 17.57           N  
ATOM    836  NH2 ARG A 181     128.634 103.540  80.764  1.00 17.57           N  
ATOM    837  N   VAL A 182     120.967 105.909  82.935  1.00 12.84           N  
ATOM    838  CA  VAL A 182     119.656 106.156  82.345  1.00 12.84           C  
ATOM    839  C   VAL A 182     119.397 107.655  82.212  1.00 12.84           C  
ATOM    840  O   VAL A 182     118.820 108.115  81.219  1.00 12.84           O  
ATOM    841  CB  VAL A 182     118.569 105.450  83.175  1.00 12.84           C  
ATOM    842  CG1 VAL A 182     117.188 105.791  82.651  1.00 12.84           C  
ATOM    843  CG2 VAL A 182     118.791 103.951  83.164  1.00 12.84           C  
ATOM    844  N   ARG A 183     119.828 108.444  83.200  1.00 12.74           N  
ATOM    845  CA  ARG A 183     119.667 109.894  83.108  1.00 12.74           C  
ATOM    846  C   ARG A 183     120.507 110.482  81.976  1.00 12.74           C  
ATOM    847  O   ARG A 183     120.040 111.359  81.234  1.00 12.74           O  
ATOM    848  CB  ARG A 183     120.025 110.537  84.445  1.00 12.74           C  
ATOM    849  CG  ARG A 183     119.589 111.977  84.588  1.00 12.74           C  
ATOM    850  CD  ARG A 183     120.007 112.535  85.933  1.00 12.74           C  
ATOM    851  NE  ARG A 183     121.327 113.158  85.888  1.00 12.74           N  
ATOM    852  CZ  ARG A 183     121.603 114.304  85.275  1.00 12.74           C  
ATOM    853  NH1 ARG A 183     120.649 114.981  84.654  1.00 12.74           N  
ATOM    854  NH2 ARG A 183     122.839 114.778  85.292  1.00 12.74           N  
ATOM    855  N   GLN A 184     121.747 110.011  81.824  1.00 14.99           N  
ATOM    856  CA  GLN A 184     122.566 110.441  80.697  1.00 14.99           C  
ATOM    857  C   GLN A 184     121.960 110.010  79.371  1.00 14.99           C  
ATOM    858  O   GLN A 184     122.052 110.744  78.382  1.00 14.99           O  
ATOM    859  CB  GLN A 184     123.987 109.896  80.837  1.00 14.99           C  
ATOM    860  CG  GLN A 184     124.777 110.477  82.001  1.00 14.99           C  
ATOM    861  CD  GLN A 184     124.675 111.990  82.098  1.00 14.99           C  
ATOM    862  OE1 GLN A 184     124.702 112.693  81.088  1.00 14.99           O  
ATOM    863  NE2 GLN A 184     124.555 112.496  83.318  1.00 14.99           N  
ATOM    864  N   ALA A 185     121.339 108.830  79.328  1.00 13.08           N  
ATOM    865  CA  ALA A 185     120.660 108.397  78.113  1.00 13.08           C  
ATOM    866  C   ALA A 185     119.493 109.315  77.776  1.00 13.08           C  
ATOM    867  O   ALA A 185     119.267 109.634  76.606  1.00 13.08           O  
ATOM    868  CB  ALA A 185     120.186 106.953  78.266  1.00 13.08           C  
ATOM    869  N   LEU A 186     118.744 109.756  78.790  1.00 12.66           N  
ATOM    870  CA  LEU A 186     117.661 110.709  78.550  1.00 12.66           C  
ATOM    871  C   LEU A 186     118.189 112.035  78.015  1.00 12.66           C  
ATOM    872  O   LEU A 186     117.622 112.607  77.071  1.00 12.66           O  
ATOM    873  CB  LEU A 186     116.869 110.943  79.834  1.00 12.66           C  
ATOM    874  CG  LEU A 186     116.014 109.806  80.387  1.00 12.66           C  
ATOM    875  CD1 LEU A 186     115.459 110.189  81.740  1.00 12.66           C  
ATOM    876  CD2 LEU A 186     114.886 109.511  79.429  1.00 12.66           C  
ATOM    877  N   LEU A 187     119.274 112.541  78.604  1.00 14.01           N  
ATOM    878  CA  LEU A 187     119.844 113.798  78.128  1.00 14.01           C  
ATOM    879  C   LEU A 187     120.356 113.670  76.697  1.00 14.01           C  
ATOM    880  O   LEU A 187     120.144 114.566  75.867  1.00 14.01           O  
ATOM    881  CB  LEU A 187     120.964 114.247  79.060  1.00 14.01           C  
ATOM    882  CG  LEU A 187     120.520 114.685  80.455  1.00 14.01           C  
ATOM    883  CD1 LEU A 187     121.722 114.943  81.335  1.00 14.01           C  
ATOM    884  CD2 LEU A 187     119.641 115.916  80.369  1.00 14.01           C  
ATOM    885  N   LYS A 188     121.025 112.558  76.387  1.00 17.39           N  
ATOM    886  CA  LYS A 188     121.514 112.348  75.031  1.00 17.39           C  
ATOM    887  C   LYS A 188     120.371 112.158  74.045  1.00 17.39           C  
ATOM    888  O   LYS A 188     120.490 112.551  72.883  1.00 17.39           O  
ATOM    889  CB  LYS A 188     122.462 111.154  74.992  1.00 17.39           C  
ATOM    890  CG  LYS A 188     123.923 111.539  75.094  1.00 17.39           C  
ATOM    891  CD  LYS A 188     124.808 110.322  75.237  1.00 17.39           C  
ATOM    892  CE  LYS A 188     126.269 110.698  75.119  1.00 17.39           C  
ATOM    893  NZ  LYS A 188     127.085 110.084  76.198  1.00 17.39           N  
ATOM    894  N   THR A 189     119.257 111.571  74.483  1.00 15.95           N  
ATOM    895  CA  THR A 189     118.090 111.477  73.614  1.00 15.95           C  
ATOM    896  C   THR A 189     117.515 112.855  73.320  1.00 15.95           C  
ATOM    897  O   THR A 189     117.092 113.129  72.193  1.00 15.95           O  
ATOM    898  CB  THR A 189     117.029 110.579  74.247  1.00 15.95           C  
ATOM    899  OG1 THR A 189     117.581 109.280  74.477  1.00 15.95           O  
ATOM    900  CG2 THR A 189     115.826 110.448  73.331  1.00 15.95           C  
ATOM    901  N   VAL A 190     117.484 113.735  74.321  1.00 17.38           N  
ATOM    902  CA  VAL A 190     117.007 115.095  74.076  1.00 17.38           C  
ATOM    903  C   VAL A 190     117.924 115.811  73.088  1.00 17.38           C  
ATOM    904  O   VAL A 190     117.458 116.507  72.175  1.00 17.38           O  
ATOM    905  CB  VAL A 190     116.874 115.867  75.402  1.00 17.38           C  
ATOM    906  CG1 VAL A 190     116.745 117.356  75.140  1.00 17.38           C  
ATOM    907  CG2 VAL A 190     115.674 115.371  76.182  1.00 17.38           C  
ATOM    908  N   GLN A 191     119.240 115.636  73.242  1.00 22.69           N  
ATOM    909  CA  GLN A 191     120.177 116.212  72.277  1.00 22.69           C  
ATOM    910  C   GLN A 191     119.955 115.643  70.880  1.00 22.69           C  
ATOM    911  O   GLN A 191     120.005 116.376  69.884  1.00 22.69           O  
ATOM    912  CB  GLN A 191     121.617 115.966  72.722  1.00 22.69           C  
ATOM    913  CG  GLN A 191     121.959 116.500  74.094  1.00 22.69           C  
ATOM    914  CD  GLN A 191     123.421 116.305  74.438  1.00 22.69           C  
ATOM    915  OE1 GLN A 191     123.758 115.642  75.418  1.00 22.69           O  
ATOM    916  NE2 GLN A 191     124.300 116.881  73.629  1.00 22.69           N  
ATOM    917  N   PHE A 192     119.719 114.335  70.788  1.00 25.30           N  
ATOM    918  CA  PHE A 192     119.505 113.693  69.498  1.00 25.30           C  
ATOM    919  C   PHE A 192     118.244 114.214  68.822  1.00 25.30           C  
ATOM    920  O   PHE A 192     118.231 114.443  67.608  1.00 25.30           O  
ATOM    921  CB  PHE A 192     119.434 112.180  69.697  1.00 25.30           C  
ATOM    922  CG  PHE A 192     119.538 111.388  68.432  1.00 25.30           C  
ATOM    923  CD1 PHE A 192     120.660 111.479  67.630  1.00 25.30           C  
ATOM    924  CD2 PHE A 192     118.522 110.530  68.058  1.00 25.30           C  
ATOM    925  CE1 PHE A 192     120.756 110.740  66.472  1.00 25.30           C  
ATOM    926  CE2 PHE A 192     118.614 109.792  66.903  1.00 25.30           C  
ATOM    927  CZ  PHE A 192     119.731 109.897  66.109  1.00 25.30           C  
ATOM    928  N   CYS A 193     117.174 114.413  69.592  1.00 25.59           N  
ATOM    929  CA  CYS A 193     115.947 114.957  69.018  1.00 25.59           C  
ATOM    930  C   CYS A 193     116.125 116.412  68.599  1.00 25.59           C  
ATOM    931  O   CYS A 193     115.556 116.839  67.590  1.00 25.59           O  
ATOM    932  CB  CYS A 193     114.789 114.812  70.001  1.00 25.59           C  
ATOM    933  SG  CYS A 193     114.480 113.134  70.579  1.00 25.59           S  
ATOM    934  N   ASP A 194     116.909 117.189  69.354  1.00 29.31           N  
ATOM    935  CA  ASP A 194     117.244 118.543  68.912  1.00 29.31           C  
ATOM    936  C   ASP A 194     117.980 118.517  67.579  1.00 29.31           C  
ATOM    937  O   ASP A 194     117.683 119.304  66.670  1.00 29.31           O  
ATOM    938  CB  ASP A 194     118.096 119.253  69.964  1.00 29.31           C  
ATOM    939  CG  ASP A 194     117.286 119.751  71.136  1.00 29.31           C  
ATOM    940  OD1 ASP A 194     116.082 119.443  71.202  1.00 29.31           O  
ATOM    941  OD2 ASP A 194     117.849 120.474  71.983  1.00 29.31           O  
ATOM    942  N   ALA A 195     118.957 117.618  67.451  1.00 31.42           N  
ATOM    943  CA  ALA A 195     119.710 117.510  66.207  1.00 31.42           C  
ATOM    944  C   ALA A 195     118.812 117.091  65.049  1.00 31.42           C  
ATOM    945  O   ALA A 195     118.945 117.607  63.935  1.00 31.42           O  
ATOM    946  CB  ALA A 195     120.867 116.527  66.377  1.00 31.42           C  
ATOM    947  N   MET A 196     117.902 116.144  65.289  1.00 34.42           N  
ATOM    948  CA  MET A 196     116.969 115.730  64.244  1.00 34.42           C  
ATOM    949  C   MET A 196     116.041 116.869  63.842  1.00 34.42           C  
ATOM    950  O   MET A 196     115.743 117.047  62.657  1.00 34.42           O  
ATOM    951  CB  MET A 196     116.160 114.518  64.706  1.00 34.42           C  
ATOM    952  CG  MET A 196     116.970 113.241  64.843  1.00 34.42           C  
ATOM    953  SD  MET A 196     115.959 111.805  65.241  1.00 34.42           S  
ATOM    954  CE  MET A 196     114.397 112.281  64.513  1.00 34.42           C  
ATOM    955  N   ARG A 197     115.558 117.640  64.818  1.00 36.90           N  
ATOM    956  CA  ARG A 197     114.701 118.781  64.517  1.00 36.90           C  
ATOM    957  C   ARG A 197     115.431 119.799  63.653  1.00 36.90           C  
ATOM    958  O   ARG A 197     114.884 120.299  62.664  1.00 36.90           O  
ATOM    959  CB  ARG A 197     114.220 119.430  65.813  1.00 36.90           C  
ATOM    960  CG  ARG A 197     113.244 120.570  65.607  1.00 36.90           C  
ATOM    961  CD  ARG A 197     113.204 121.482  66.818  1.00 36.90           C  
ATOM    962  NE  ARG A 197     114.435 122.257  66.947  1.00 36.90           N  
ATOM    963  CZ  ARG A 197     114.849 122.824  68.075  1.00 36.90           C  
ATOM    964  NH1 ARG A 197     114.130 122.703  69.182  1.00 36.90           N  
ATOM    965  NH2 ARG A 197     115.982 123.511  68.097  1.00 36.90           N  
ATOM    966  N   ASN A 198     116.671 120.128  64.021  1.00 40.13           N  
ATOM    967  CA  ASN A 198     117.440 121.085  63.231  1.00 40.13           C  
ATOM    968  C   ASN A 198     117.734 120.548  61.835  1.00 40.13           C  
ATOM    969  O   ASN A 198     117.612 121.278  60.846  1.00 40.13           O  
ATOM    970  CB  ASN A 198     118.738 121.438  63.953  1.00 40.13           C  
ATOM    971  CG  ASN A 198     118.500 121.975  65.346  1.00 40.13           C  
ATOM    972  OD1 ASN A 198     117.375 122.320  65.707  1.00 40.13           O  
ATOM    973  ND2 ASN A 198     119.559 122.044  66.143  1.00 40.13           N  
ATOM    974  N   ALA A 199     118.120 119.275  61.734  1.00 40.99           N  
ATOM    975  CA  ALA A 199     118.493 118.686  60.455  1.00 40.99           C  
ATOM    976  C   ALA A 199     117.300 118.380  59.561  1.00 40.99           C  
ATOM    977  O   ALA A 199     117.504 118.011  58.400  1.00 40.99           O  
ATOM    978  CB  ALA A 199     119.302 117.409  60.685  1.00 40.99           C  
ATOM    979  N   GLY A 200     116.073 118.513  60.060  1.00 42.76           N  
ATOM    980  CA  GLY A 200     114.920 118.222  59.232  1.00 42.76           C  
ATOM    981  C   GLY A 200     114.659 116.753  58.990  1.00 42.76           C  
ATOM    982  O   GLY A 200     114.190 116.389  57.912  1.00 42.76           O  
ATOM    983  N   ILE A 201     114.986 115.895  59.943  1.00 43.45           N  
ATOM    984  CA  ILE A 201     114.792 114.456  59.806  1.00 43.45           C  
ATOM    985  C   ILE A 201     113.524 114.035  60.537  1.00 43.45           C  
ATOM    986  O   ILE A 201     113.246 114.498  61.649  1.00 43.45           O  
ATOM    987  CB  ILE A 201     116.025 113.697  60.332  1.00 43.45           C  
ATOM    988  CG1 ILE A 201     117.112 113.651  59.259  1.00 43.45           C  
ATOM    989  CG2 ILE A 201     115.654 112.303  60.792  1.00 43.45           C  
ATOM    990  CD1 ILE A 201     118.468 113.271  59.787  1.00 43.45           C  
ATOM    991  N   VAL A 202     112.746 113.158  59.905  1.00 39.45           N  
ATOM    992  CA  VAL A 202     111.571 112.539  60.510  1.00 39.45           C  
ATOM    993  C   VAL A 202     111.892 111.074  60.769  1.00 39.45           C  
ATOM    994  O   VAL A 202     112.397 110.380  59.879  1.00 39.45           O  
ATOM    995  CB  VAL A 202     110.333 112.675  59.608  1.00 39.45           C  
ATOM    996  CG1 VAL A 202     109.101 112.133  60.312  1.00 39.45           C  
ATOM    997  CG2 VAL A 202     110.132 114.120  59.192  1.00 39.45           C  
ATOM    998  N   GLY A 203     111.602 110.601  61.974  1.00 32.66           N  
ATOM    999  CA  GLY A 203     111.901 109.220  62.308  1.00 32.66           C  
ATOM   1000  C   GLY A 203     111.407 108.864  63.693  1.00 32.66           C  
ATOM   1001  O   GLY A 203     111.154 109.734  64.533  1.00 32.66           O  
ATOM   1002  N   VAL A 204     111.284 107.558  63.915  1.00 25.77           N  
ATOM   1003  CA  VAL A 204     110.782 106.996  65.164  1.00 25.77           C  
ATOM   1004  C   VAL A 204     111.964 106.459  65.959  1.00 25.77           C  
ATOM   1005  O   VAL A 204     112.743 105.644  65.452  1.00 25.77           O  
ATOM   1006  CB  VAL A 204     109.751 105.888  64.900  1.00 25.77           C  
ATOM   1007  CG1 VAL A 204     109.515 105.067  66.157  1.00 25.77           C  
ATOM   1008  CG2 VAL A 204     108.451 106.480  64.386  1.00 25.77           C  
ATOM   1009  N   LEU A 205     112.100 106.908  67.204  1.00 22.18           N  
ATOM   1010  CA  LEU A 205     113.165 106.422  68.071  1.00 22.18           C  
ATOM   1011  C   LEU A 205     112.756 105.121  68.750  1.00 22.18           C  
ATOM   1012  O   LEU A 205     111.613 104.964  69.186  1.00 22.18           O  
ATOM   1013  CB  LEU A 205     113.524 107.466  69.129  1.00 22.18           C  
ATOM   1014  CG  LEU A 205     114.592 108.515  68.802  1.00 22.18           C  
ATOM   1015  CD1 LEU A 205     114.434 109.083  67.401  1.00 22.18           C  
ATOM   1016  CD2 LEU A 205     114.578 109.623  69.832  1.00 22.18           C  
ATOM   1017  N   THR A 206     113.699 104.184  68.837  1.00 21.50           N  
ATOM   1018  CA  THR A 206     113.467 102.902  69.486  1.00 21.50           C  
ATOM   1019  C   THR A 206     114.610 102.608  70.447  1.00 21.50           C  
ATOM   1020  O   THR A 206     115.749 103.018  70.221  1.00 21.50           O  
ATOM   1021  CB  THR A 206     113.329 101.752  68.472  1.00 21.50           C  
ATOM   1022  OG1 THR A 206     114.629 101.314  68.060  1.00 21.50           O  
ATOM   1023  CG2 THR A 206     112.533 102.182  67.251  1.00 21.50           C  
ATOM   1024  N   LEU A 207     114.288 101.890  71.526  1.00 15.49           N  
ATOM   1025  CA  LEU A 207     115.260 101.653  72.591  1.00 15.49           C  
ATOM   1026  C   LEU A 207     116.436 100.806  72.126  1.00 15.49           C  
ATOM   1027  O   LEU A 207     117.544 100.949  72.652  1.00 15.49           O  
ATOM   1028  CB  LEU A 207     114.579 100.986  73.785  1.00 15.49           C  
ATOM   1029  CG  LEU A 207     113.580 101.819  74.583  1.00 15.49           C  
ATOM   1030  CD1 LEU A 207     112.554 100.924  75.244  1.00 15.49           C  
ATOM   1031  CD2 LEU A 207     114.310 102.641  75.624  1.00 15.49           C  
ATOM   1032  N   ASP A 208     116.224  99.918  71.157  1.00 22.39           N  
ATOM   1033  CA  ASP A 208     117.296  99.047  70.699  1.00 22.39           C  
ATOM   1034  C   ASP A 208     118.332  99.768  69.848  1.00 22.39           C  
ATOM   1035  O   ASP A 208     119.378  99.183  69.552  1.00 22.39           O  
ATOM   1036  CB  ASP A 208     116.717  97.862  69.924  1.00 22.39           C  
ATOM   1037  CG  ASP A 208     115.787  98.292  68.814  1.00 22.39           C  
ATOM   1038  OD1 ASP A 208     114.849  99.062  69.097  1.00 22.39           O  
ATOM   1039  OD2 ASP A 208     115.982  97.851  67.663  1.00 22.39           O  
ATOM   1040  N   ASN A 209     118.072 101.012  69.453  1.00 23.78           N  
ATOM   1041  CA  ASN A 209     119.015 101.806  68.680  1.00 23.78           C  
ATOM   1042  C   ASN A 209     119.878 102.707  69.550  1.00 23.78           C  
ATOM   1043  O   ASN A 209     120.591 103.560  69.016  1.00 23.78           O  
ATOM   1044  CB  ASN A 209     118.277 102.654  67.644  1.00 23.78           C  
ATOM   1045  CG  ASN A 209     117.612 101.820  66.577  1.00 23.78           C  
ATOM   1046  OD1 ASN A 209     118.008 100.685  66.327  1.00 23.78           O  
ATOM   1047  ND2 ASN A 209     116.607 102.388  65.924  1.00 23.78           N  
ATOM   1048  N   GLN A 210     119.829 102.547  70.868  1.00 17.45           N  
ATOM   1049  CA  GLN A 210     120.609 103.372  71.780  1.00 17.45           C  
ATOM   1050  C   GLN A 210     121.472 102.478  72.653  1.00 17.45           C  
ATOM   1051  O   GLN A 210     120.986 101.493  73.215  1.00 17.45           O  
ATOM   1052  CB  GLN A 210     119.711 104.250  72.654  1.00 17.45           C  
ATOM   1053  CG  GLN A 210     120.479 105.181  73.572  1.00 17.45           C  
ATOM   1054  CD  GLN A 210     119.580 105.972  74.489  1.00 17.45           C  
ATOM   1055  OE1 GLN A 210     118.597 105.454  75.009  1.00 17.45           O  
ATOM   1056  NE2 GLN A 210     119.914 107.236  74.697  1.00 17.45           N  
ATOM   1057  N   ASP A 211     122.743 102.808  72.738  1.00 26.26           N  
ATOM   1058  CA  ASP A 211     123.687 102.034  73.569  1.00 26.26           C  
ATOM   1059  C   ASP A 211     123.459 102.313  75.042  1.00 26.26           C  
ATOM   1060  O   ASP A 211     122.732 103.234  75.370  1.00 26.26           O  
ATOM   1061  CB  ASP A 211     125.121 102.440  73.233  1.00 26.26           C  
ATOM   1062  CG  ASP A 211     126.136 101.356  73.488  1.00 26.26           C  
ATOM   1063  OD1 ASP A 211     125.757 100.178  73.384  1.00 26.26           O  
ATOM   1064  OD2 ASP A 211     127.287 101.704  73.798  1.00 26.26           O  
ATOM   1065  N   LEU A 212     124.037 101.489  75.896  1.00 25.05           N  
ATOM   1066  CA  LEU A 212     124.013 101.736  77.333  1.00 25.05           C  
ATOM   1067  C   LEU A 212     124.931 102.877  77.750  1.00 25.05           C  
ATOM   1068  O   LEU A 212     124.878 103.298  78.910  1.00 25.05           O  
ATOM   1069  CB  LEU A 212     124.379 100.469  78.109  1.00 25.05           C  
ATOM   1070  CG  LEU A 212     123.351  99.337  78.058  1.00 25.05           C  
ATOM   1071  CD1 LEU A 212     123.777  98.165  78.914  1.00 25.05           C  
ATOM   1072  CD2 LEU A 212     122.004  99.844  78.518  1.00 25.05           C  
ATOM   1073  N   ASN A 213     125.767 103.379  76.844  1.00 27.83           N  
ATOM   1074  CA  ASN A 213     126.434 104.658  77.037  1.00 27.83           C  
ATOM   1075  C   ASN A 213     125.606 105.826  76.523  1.00 27.83           C  
ATOM   1076  O   ASN A 213     126.067 106.969  76.595  1.00 27.83           O  
ATOM   1077  CB  ASN A 213     127.803 104.662  76.352  1.00 27.83           C  
ATOM   1078  CG  ASN A 213     128.696 103.535  76.825  1.00 27.83           C  
ATOM   1079  OD1 ASN A 213     128.640 103.130  77.984  1.00 27.83           O  
ATOM   1080  ND2 ASN A 213     129.530 103.023  75.928  1.00 27.83           N  
ATOM   1081  N   GLY A 214     124.404 105.569  76.011  1.00 21.80           N  
ATOM   1082  CA  GLY A 214     123.524 106.611  75.528  1.00 21.80           C  
ATOM   1083  C   GLY A 214     123.741 107.049  74.097  1.00 21.80           C  
ATOM   1084  O   GLY A 214     123.002 107.917  73.619  1.00 21.80           O  
ATOM   1085  N   ASN A 215     124.719 106.484  73.397  1.00 25.48           N  
ATOM   1086  CA  ASN A 215     124.976 106.887  72.021  1.00 25.48           C  
ATOM   1087  C   ASN A 215     123.955 106.273  71.072  1.00 25.48           C  
ATOM   1088  O   ASN A 215     123.615 105.091  71.175  1.00 25.48           O  
ATOM   1089  CB  ASN A 215     126.390 106.484  71.609  1.00 25.48           C  
ATOM   1090  CG  ASN A 215     127.447 107.051  72.532  1.00 25.48           C  
ATOM   1091  OD1 ASN A 215     127.493 108.256  72.774  1.00 25.48           O  
ATOM   1092  ND2 ASN A 215     128.304 106.184  73.055  1.00 25.48           N  
ATOM   1093  N   TRP A 216     123.471 107.087  70.137  1.00 21.41           N  
ATOM   1094  CA  TRP A 216     122.494 106.658  69.147  1.00 21.41           C  
ATOM   1095  C   TRP A 216     123.207 106.281  67.855  1.00 21.41           C  
ATOM   1096  O   TRP A 216     124.119 106.984  67.413  1.00 21.41           O  
ATOM   1097  CB  TRP A 216     121.493 107.780  68.889  1.00 21.41           C  
ATOM   1098  CG  TRP A 216     120.432 107.891  69.933  1.00 21.41           C  
ATOM   1099  CD1 TRP A 216     120.415 108.748  70.993  1.00 21.41           C  
ATOM   1100  CD2 TRP A 216     119.218 107.140  70.005  1.00 21.41           C  
ATOM   1101  NE1 TRP A 216     119.273 108.567  71.729  1.00 21.41           N  
ATOM   1102  CE2 TRP A 216     118.520 107.586  71.141  1.00 21.41           C  
ATOM   1103  CE3 TRP A 216     118.656 106.130  69.222  1.00 21.41           C  
ATOM   1104  CZ2 TRP A 216     117.291 107.058  71.514  1.00 21.41           C  
ATOM   1105  CZ3 TRP A 216     117.438 105.608  69.595  1.00 21.41           C  
ATOM   1106  CH2 TRP A 216     116.768 106.071  70.729  1.00 21.41           C  
ATOM   1107  N   TYR A 217     122.791 105.168  67.245  1.00 32.56           N  
ATOM   1108  CA  TYR A 217     123.585 104.638  66.142  1.00 32.56           C  
ATOM   1109  C   TYR A 217     122.814 104.106  64.939  1.00 32.56           C  
ATOM   1110  O   TYR A 217     123.459 103.573  64.033  1.00 32.56           O  
ATOM   1111  CB  TYR A 217     124.523 103.540  66.686  1.00 32.56           C  
ATOM   1112  CG  TYR A 217     123.823 102.325  67.261  1.00 32.56           C  
ATOM   1113  CD1 TYR A 217     123.152 101.424  66.445  1.00 32.56           C  
ATOM   1114  CD2 TYR A 217     123.841 102.079  68.625  1.00 32.56           C  
ATOM   1115  CE1 TYR A 217     122.519 100.321  66.970  1.00 32.56           C  
ATOM   1116  CE2 TYR A 217     123.210 100.975  69.158  1.00 32.56           C  
ATOM   1117  CZ  TYR A 217     122.551 100.101  68.325  1.00 32.56           C  
ATOM   1118  OH  TYR A 217     121.919  99.001  68.846  1.00 32.56           O  
ATOM   1119  N   ASP A 218     121.489 104.216  64.871  1.00 40.18           N  
ATOM   1120  CA  ASP A 218     120.747 103.628  63.760  1.00 40.18           C  
ATOM   1121  C   ASP A 218     119.839 104.666  63.121  1.00 40.18           C  
ATOM   1122  O   ASP A 218     118.958 105.221  63.786  1.00 40.18           O  
ATOM   1123  CB  ASP A 218     119.926 102.423  64.222  1.00 40.18           C  
ATOM   1124  N   PHE A 219     120.048 104.910  61.822  1.00 48.53           N  
ATOM   1125  CA  PHE A 219     119.357 105.961  61.083  1.00 48.53           C  
ATOM   1126  C   PHE A 219     118.668 105.480  59.811  1.00 48.53           C  
ATOM   1127  O   PHE A 219     118.150 106.315  59.062  1.00 48.53           O  
ATOM   1128  CB  PHE A 219     120.326 107.094  60.690  1.00 48.53           C  
ATOM   1129  CG  PHE A 219     121.228 107.581  61.799  1.00 48.53           C  
ATOM   1130  CD1 PHE A 219     120.832 107.548  63.123  1.00 48.53           C  
ATOM   1131  CD2 PHE A 219     122.486 108.072  61.502  1.00 48.53           C  
ATOM   1132  CE1 PHE A 219     121.666 107.992  64.123  1.00 48.53           C  
ATOM   1133  CE2 PHE A 219     123.323 108.518  62.501  1.00 48.53           C  
ATOM   1134  CZ  PHE A 219     122.909 108.478  63.812  1.00 48.53           C  
ATOM   1135  N   GLY A 220     118.653 104.175  59.535  1.00 53.97           N  
ATOM   1136  CA  GLY A 220     118.255 103.692  58.221  1.00 53.97           C  
ATOM   1137  C   GLY A 220     116.811 103.959  57.840  1.00 53.97           C  
ATOM   1138  O   GLY A 220     116.486 103.949  56.648  1.00 53.97           O  
ATOM   1139  N   ASP A 221     115.936 104.193  58.814  1.00 53.08           N  
ATOM   1140  CA  ASP A 221     114.511 104.356  58.554  1.00 53.08           C  
ATOM   1141  C   ASP A 221     114.038 105.806  58.579  1.00 53.08           C  
ATOM   1142  O   ASP A 221     112.830 106.046  58.491  1.00 53.08           O  
ATOM   1143  CB  ASP A 221     113.699 103.523  59.552  1.00 53.08           C  
ATOM   1144  CG  ASP A 221     114.237 103.616  60.968  1.00 53.08           C  
ATOM   1145  OD1 ASP A 221     115.006 104.555  61.258  1.00 53.08           O  
ATOM   1146  OD2 ASP A 221     113.893 102.744  61.791  1.00 53.08           O  
ATOM   1147  N   PHE A 222     114.943 106.774  58.695  1.00 48.85           N  
ATOM   1148  CA  PHE A 222     114.546 108.174  58.760  1.00 48.85           C  
ATOM   1149  C   PHE A 222     114.247 108.728  57.366  1.00 48.85           C  
ATOM   1150  O   PHE A 222     114.557 108.119  56.340  1.00 48.85           O  
ATOM   1151  CB  PHE A 222     115.624 109.015  59.445  1.00 48.85           C  
ATOM   1152  CG  PHE A 222     115.984 108.554  60.839  1.00 48.85           C  
ATOM   1153  CD1 PHE A 222     115.199 107.638  61.520  1.00 48.85           C  
ATOM   1154  CD2 PHE A 222     117.081 109.092  61.489  1.00 48.85           C  
ATOM   1155  CE1 PHE A 222     115.528 107.236  62.798  1.00 48.85           C  
ATOM   1156  CE2 PHE A 222     117.412 108.691  62.767  1.00 48.85           C  
ATOM   1157  CZ  PHE A 222     116.633 107.765  63.421  1.00 48.85           C  
ATOM   1158  N   ILE A 223     113.625 109.907  57.345  1.00 48.85           N  
ATOM   1159  CA  ILE A 223     113.199 110.577  56.120  1.00 48.85           C  
ATOM   1160  C   ILE A 223     113.617 112.039  56.192  1.00 48.85           C  
ATOM   1161  O   ILE A 223     113.458 112.687  57.232  1.00 48.85           O  
ATOM   1162  CB  ILE A 223     111.673 110.463  55.914  1.00 48.85           C  
ATOM   1163  CG1 ILE A 223     111.257 109.000  55.765  1.00 48.85           C  
ATOM   1164  CG2 ILE A 223     111.224 111.272  54.709  1.00 48.85           C  
ATOM   1165  CD1 ILE A 223     109.760 108.803  55.697  1.00 48.85           C  
ATOM   1166  N   GLN A 224     114.151 112.559  55.089  1.00 52.32           N  
ATOM   1167  CA  GLN A 224     114.539 113.961  55.019  1.00 52.32           C  
ATOM   1168  C   GLN A 224     113.339 114.849  54.715  1.00 52.32           C  
ATOM   1169  O   GLN A 224     112.465 114.487  53.924  1.00 52.32           O  
ATOM   1170  CB  GLN A 224     115.604 114.175  53.943  1.00 52.32           C  
ATOM   1171  CG  GLN A 224     117.003 113.743  54.327  1.00 52.32           C  
ATOM   1172  CD  GLN A 224     117.395 112.434  53.678  1.00 52.32           C  
ATOM   1173  OE1 GLN A 224     116.588 111.510  53.581  1.00 52.32           O  
ATOM   1174  NE2 GLN A 224     118.631 112.359  53.201  1.00 52.32           N  
ATOM   1175  N   THR A 225     113.304 116.016  55.353  1.00 50.83           N  
ATOM   1176  CA  THR A 225     112.378 117.083  54.989  1.00 50.83           C  
ATOM   1177  C   THR A 225     113.102 118.414  55.181  1.00 50.83           C  
ATOM   1178  O   THR A 225     114.333 118.465  55.262  1.00 50.83           O  
ATOM   1179  CB  THR A 225     111.069 116.996  55.789  1.00 50.83           C  
ATOM   1180  OG1 THR A 225     110.185 118.042  55.370  1.00 50.83           O  
ATOM   1181  CG2 THR A 225     111.321 117.133  57.278  1.00 50.83           C  
ATOM   1182  N   THR A 226     112.336 119.498  55.237  1.00 51.28           N  
ATOM   1183  CA  THR A 226     112.924 120.826  55.347  1.00 51.28           C  
ATOM   1184  C   THR A 226     113.692 120.954  56.662  1.00 51.28           C  
ATOM   1185  O   THR A 226     113.153 120.609  57.722  1.00 51.28           O  
ATOM   1186  CB  THR A 226     111.835 121.896  55.271  1.00 51.28           C  
ATOM   1187  OG1 THR A 226     110.981 121.632  54.152  1.00 51.28           O  
ATOM   1188  CG2 THR A 226     112.450 123.280  55.114  1.00 51.28           C  
ATOM   1189  N   PRO A 227     114.938 121.429  56.636  1.00 49.12           N  
ATOM   1190  CA  PRO A 227     115.688 121.589  57.888  1.00 49.12           C  
ATOM   1191  C   PRO A 227     115.014 122.586  58.819  1.00 49.12           C  
ATOM   1192  O   PRO A 227     114.423 123.576  58.383  1.00 49.12           O  
ATOM   1193  CB  PRO A 227     117.062 122.087  57.422  1.00 49.12           C  
ATOM   1194  CG  PRO A 227     116.826 122.670  56.072  1.00 49.12           C  
ATOM   1195  CD  PRO A 227     115.720 121.854  55.467  1.00 49.12           C  
ATOM   1196  N   GLY A 228     115.115 122.313  60.119  1.00 46.50           N  
ATOM   1197  CA  GLY A 228     114.416 123.085  61.121  1.00 46.50           C  
ATOM   1198  C   GLY A 228     113.000 122.638  61.396  1.00 46.50           C  
ATOM   1199  O   GLY A 228     112.353 123.202  62.287  1.00 46.50           O  
ATOM   1200  N   SER A 229     112.493 121.640  60.666  1.00 44.62           N  
ATOM   1201  CA  SER A 229     111.121 121.176  60.831  1.00 44.62           C  
ATOM   1202  C   SER A 229     111.041 119.666  61.037  1.00 44.62           C  
ATOM   1203  O   SER A 229     110.010 119.061  60.730  1.00 44.62           O  
ATOM   1204  CB  SER A 229     110.264 121.588  59.632  1.00 44.62           C  
ATOM   1205  OG  SER A 229     110.932 121.319  58.412  1.00 44.62           O  
ATOM   1206  N   GLY A 230     112.104 119.044  61.541  1.00 39.52           N  
ATOM   1207  CA  GLY A 230     112.053 117.624  61.826  1.00 39.52           C  
ATOM   1208  C   GLY A 230     111.088 117.301  62.949  1.00 39.52           C  
ATOM   1209  O   GLY A 230     110.774 118.131  63.802  1.00 39.52           O  
ATOM   1210  N   VAL A 231     110.607 116.061  62.945  1.00 33.10           N  
ATOM   1211  CA  VAL A 231     109.614 115.620  63.922  1.00 33.10           C  
ATOM   1212  C   VAL A 231     110.008 114.257  64.478  1.00 33.10           C  
ATOM   1213  O   VAL A 231     109.707 113.227  63.859  1.00 33.10           O  
ATOM   1214  CB  VAL A 231     108.205 115.560  63.308  1.00 33.10           C  
ATOM   1215  CG1 VAL A 231     107.183 115.216  64.378  1.00 33.10           C  
ATOM   1216  CG2 VAL A 231     107.847 116.874  62.633  1.00 33.10           C  
ATOM   1217  N   PRO A 232     110.679 114.197  65.629  1.00 25.31           N  
ATOM   1218  CA  PRO A 232     110.989 112.898  66.241  1.00 25.31           C  
ATOM   1219  C   PRO A 232     109.780 112.332  66.976  1.00 25.31           C  
ATOM   1220  O   PRO A 232     109.128 113.028  67.757  1.00 25.31           O  
ATOM   1221  CB  PRO A 232     112.131 113.225  67.208  1.00 25.31           C  
ATOM   1222  CG  PRO A 232     111.917 114.651  67.567  1.00 25.31           C  
ATOM   1223  CD  PRO A 232     111.260 115.320  66.383  1.00 25.31           C  
ATOM   1224  N   VAL A 233     109.485 111.061  66.721  1.00 22.43           N  
ATOM   1225  CA  VAL A 233     108.367 110.362  67.346  1.00 22.43           C  
ATOM   1226  C   VAL A 233     108.926 109.485  68.459  1.00 22.43           C  
ATOM   1227  O   VAL A 233     109.725 108.576  68.203  1.00 22.43           O  
ATOM   1228  CB  VAL A 233     107.584 109.532  66.319  1.00 22.43           C  
ATOM   1229  CG1 VAL A 233     106.675 108.537  67.017  1.00 22.43           C  
ATOM   1230  CG2 VAL A 233     106.790 110.448  65.402  1.00 22.43           C  
ATOM   1231  N   VAL A 234     108.500 109.748  69.695  1.00 16.78           N  
ATOM   1232  CA  VAL A 234     109.170 109.205  70.872  1.00 16.78           C  
ATOM   1233  C   VAL A 234     108.183 108.559  71.836  1.00 16.78           C  
ATOM   1234  O   VAL A 234     108.519 108.305  72.996  1.00 16.78           O  
ATOM   1235  CB  VAL A 234     109.972 110.305  71.590  1.00 16.78           C  
ATOM   1236  CG1 VAL A 234     111.238 110.626  70.824  1.00 16.78           C  
ATOM   1237  CG2 VAL A 234     109.119 111.548  71.768  1.00 16.78           C  
ATOM   1238  N   ASP A 235     106.954 108.312  71.377  1.00 16.39           N  
ATOM   1239  CA  ASP A 235     105.927 107.773  72.267  1.00 16.39           C  
ATOM   1240  C   ASP A 235     106.347 106.430  72.853  1.00 16.39           C  
ATOM   1241  O   ASP A 235     106.348 106.245  74.077  1.00 16.39           O  
ATOM   1242  CB  ASP A 235     104.605 107.635  71.513  1.00 16.39           C  
ATOM   1243  CG  ASP A 235     104.255 108.874  70.718  1.00 16.39           C  
ATOM   1244  OD1 ASP A 235     104.611 109.986  71.158  1.00 16.39           O  
ATOM   1245  OD2 ASP A 235     103.621 108.736  69.651  1.00 16.39           O  
ATOM   1246  N   SER A 236     106.732 105.487  71.991  1.00 12.38           N  
ATOM   1247  CA  SER A 236     107.071 104.145  72.453  1.00 12.38           C  
ATOM   1248  C   SER A 236     108.330 104.147  73.308  1.00 12.38           C  
ATOM   1249  O   SER A 236     108.401 103.433  74.313  1.00 12.38           O  
ATOM   1250  CB  SER A 236     107.239 103.209  71.260  1.00 12.38           C  
ATOM   1251  OG  SER A 236     107.435 101.876  71.690  1.00 12.38           O  
ATOM   1252  N   TYR A 237     109.321 104.961  72.942  1.00 10.39           N  
ATOM   1253  CA  TYR A 237     110.587 104.989  73.668  1.00 10.39           C  
ATOM   1254  C   TYR A 237     110.368 105.405  75.120  1.00 10.39           C  
ATOM   1255  O   TYR A 237     110.669 104.649  76.056  1.00 10.39           O  
ATOM   1256  CB  TYR A 237     111.548 105.944  72.951  1.00 10.39           C  
ATOM   1257  CG  TYR A 237     112.864 106.209  73.646  1.00 10.39           C  
ATOM   1258  CD1 TYR A 237     113.971 105.416  73.391  1.00 10.39           C  
ATOM   1259  CD2 TYR A 237     113.006 107.260  74.541  1.00 10.39           C  
ATOM   1260  CE1 TYR A 237     115.173 105.652  74.011  1.00 10.39           C  
ATOM   1261  CE2 TYR A 237     114.205 107.499  75.171  1.00 10.39           C  
ATOM   1262  CZ  TYR A 237     115.286 106.693  74.901  1.00 10.39           C  
ATOM   1263  OH  TYR A 237     116.489 106.925  75.522  1.00 10.39           O  
ATOM   1264  N   TYR A 238     109.795 106.595  75.322  1.00  6.41           N  
ATOM   1265  CA  TYR A 238     109.543 107.074  76.676  1.00  6.41           C  
ATOM   1266  C   TYR A 238     108.554 106.183  77.411  1.00  6.41           C  
ATOM   1267  O   TYR A 238     108.749 105.887  78.592  1.00  6.41           O  
ATOM   1268  CB  TYR A 238     109.038 108.515  76.655  1.00  6.41           C  
ATOM   1269  CG  TYR A 238     110.111 109.544  76.409  1.00  6.41           C  
ATOM   1270  CD1 TYR A 238     111.190 109.658  77.270  1.00  6.41           C  
ATOM   1271  CD2 TYR A 238     110.032 110.420  75.337  1.00  6.41           C  
ATOM   1272  CE1 TYR A 238     112.170 110.596  77.060  1.00  6.41           C  
ATOM   1273  CE2 TYR A 238     111.009 111.365  75.120  1.00  6.41           C  
ATOM   1274  CZ  TYR A 238     112.076 111.448  75.986  1.00  6.41           C  
ATOM   1275  OH  TYR A 238     113.055 112.388  75.778  1.00  6.41           O  
ATOM   1276  N   SER A 239     107.495 105.733  76.733  1.00  7.40           N  
ATOM   1277  CA  SER A 239     106.475 104.949  77.420  1.00  7.40           C  
ATOM   1278  C   SER A 239     107.028 103.617  77.915  1.00  7.40           C  
ATOM   1279  O   SER A 239     106.735 103.204  79.042  1.00  7.40           O  
ATOM   1280  CB  SER A 239     105.280 104.729  76.499  1.00  7.40           C  
ATOM   1281  OG  SER A 239     104.150 104.303  77.233  1.00  7.40           O  
ATOM   1282  N   LEU A 240     107.832 102.932  77.097  1.00  7.27           N  
ATOM   1283  CA  LEU A 240     108.429 101.676  77.533  1.00  7.27           C  
ATOM   1284  C   LEU A 240     109.483 101.902  78.607  1.00  7.27           C  
ATOM   1285  O   LEU A 240     109.641 101.073  79.510  1.00  7.27           O  
ATOM   1286  CB  LEU A 240     109.035 100.939  76.341  1.00  7.27           C  
ATOM   1287  CG  LEU A 240     108.083 100.172  75.423  1.00  7.27           C  
ATOM   1288  CD1 LEU A 240     108.824  99.649  74.210  1.00  7.27           C  
ATOM   1289  CD2 LEU A 240     107.446  99.031  76.180  1.00  7.27           C  
ATOM   1290  N   LEU A 241     110.220 103.011  78.528  1.00  6.80           N  
ATOM   1291  CA  LEU A 241     111.297 103.232  79.485  1.00  6.80           C  
ATOM   1292  C   LEU A 241     110.796 103.699  80.853  1.00  6.80           C  
ATOM   1293  O   LEU A 241     111.497 103.507  81.852  1.00  6.80           O  
ATOM   1294  CB  LEU A 241     112.300 104.220  78.891  1.00  6.80           C  
ATOM   1295  CG  LEU A 241     113.427 104.786  79.747  1.00  6.80           C  
ATOM   1296  CD1 LEU A 241     114.586 103.825  79.800  1.00  6.80           C  
ATOM   1297  CD2 LEU A 241     113.866 106.093  79.143  1.00  6.80           C  
ATOM   1298  N   MET A 242     109.591 104.274  80.929  1.00  6.74           N  
ATOM   1299  CA  MET A 242     109.073 104.897  82.157  1.00  6.74           C  
ATOM   1300  C   MET A 242     109.168 104.053  83.425  1.00  6.74           C  
ATOM   1301  O   MET A 242     109.548 104.607  84.463  1.00  6.74           O  
ATOM   1302  CB  MET A 242     107.611 105.323  81.953  1.00  6.74           C  
ATOM   1303  CG  MET A 242     107.419 106.614  81.188  1.00  6.74           C  
ATOM   1304  SD  MET A 242     105.701 107.131  81.114  1.00  6.74           S  
ATOM   1305  CE  MET A 242     105.769 108.296  79.761  1.00  6.74           C  
ATOM   1306  N   PRO A 243     108.810 102.763  83.443  1.00  6.32           N  
ATOM   1307  CA  PRO A 243     108.910 102.013  84.708  1.00  6.32           C  
ATOM   1308  C   PRO A 243     110.315 101.952  85.291  1.00  6.32           C  
ATOM   1309  O   PRO A 243     110.459 101.827  86.512  1.00  6.32           O  
ATOM   1310  CB  PRO A 243     108.395 100.618  84.327  1.00  6.32           C  
ATOM   1311  CG  PRO A 243     107.509 100.852  83.175  1.00  6.32           C  
ATOM   1312  CD  PRO A 243     108.149 101.961  82.401  1.00  6.32           C  
ATOM   1313  N   ILE A 244     111.354 102.028  84.461  1.00  6.62           N  
ATOM   1314  CA  ILE A 244     112.722 101.939  84.963  1.00  6.62           C  
ATOM   1315  C   ILE A 244     113.195 103.261  85.562  1.00  6.62           C  
ATOM   1316  O   ILE A 244     114.126 103.277  86.373  1.00  6.62           O  
ATOM   1317  CB  ILE A 244     113.653 101.452  83.839  1.00  6.62           C  
ATOM   1318  CG1 ILE A 244     113.095 100.169  83.229  1.00  6.62           C  
ATOM   1319  CG2 ILE A 244     115.072 101.235  84.335  1.00  6.62           C  
ATOM   1320  CD1 ILE A 244     114.079  99.442  82.384  1.00  6.62           C  
ATOM   1321  N   LEU A 245     112.570 104.380  85.196  1.00  4.17           N  
ATOM   1322  CA  LEU A 245     113.021 105.670  85.712  1.00  4.17           C  
ATOM   1323  C   LEU A 245     112.863 105.750  87.226  1.00  4.17           C  
ATOM   1324  O   LEU A 245     113.679 106.379  87.908  1.00  4.17           O  
ATOM   1325  CB  LEU A 245     112.269 106.810  85.028  1.00  4.17           C  
ATOM   1326  CG  LEU A 245     112.404 106.870  83.506  1.00  4.17           C  
ATOM   1327  CD1 LEU A 245     111.492 107.930  82.922  1.00  4.17           C  
ATOM   1328  CD2 LEU A 245     113.842 107.113  83.099  1.00  4.17           C  
ATOM   1329  N   THR A 246     111.819 105.132  87.769  1.00  7.04           N  
ATOM   1330  CA  THR A 246     111.640 105.098  89.214  1.00  7.04           C  
ATOM   1331  C   THR A 246     112.358 103.932  89.880  1.00  7.04           C  
ATOM   1332  O   THR A 246     112.723 104.034  91.056  1.00  7.04           O  
ATOM   1333  CB  THR A 246     110.151 105.045  89.563  1.00  7.04           C  
ATOM   1334  OG1 THR A 246     109.520 103.988  88.829  1.00  7.04           O  
ATOM   1335  CG2 THR A 246     109.484 106.366  89.246  1.00  7.04           C  
ATOM   1336  N   LEU A 247     112.555 102.823  89.167  1.00  7.03           N  
ATOM   1337  CA  LEU A 247     113.211 101.667  89.766  1.00  7.03           C  
ATOM   1338  C   LEU A 247     114.700 101.919  89.976  1.00  7.03           C  
ATOM   1339  O   LEU A 247     115.284 101.442  90.955  1.00  7.03           O  
ATOM   1340  CB  LEU A 247     112.978 100.431  88.900  1.00  7.03           C  
ATOM   1341  CG  LEU A 247     113.568  99.111  89.392  1.00  7.03           C  
ATOM   1342  CD1 LEU A 247     112.657  98.458  90.408  1.00  7.03           C  
ATOM   1343  CD2 LEU A 247     113.795  98.183  88.222  1.00  7.03           C  
ATOM   1344  N   THR A 248     115.332 102.654  89.069  1.00  8.09           N  
ATOM   1345  CA  THR A 248     116.731 103.025  89.214  1.00  8.09           C  
ATOM   1346  C   THR A 248     116.923 104.377  89.888  1.00  8.09           C  
ATOM   1347  O   THR A 248     118.067 104.758  90.148  1.00  8.09           O  
ATOM   1348  CB  THR A 248     117.423 103.037  87.846  1.00  8.09           C  
ATOM   1349  OG1 THR A 248     116.661 103.827  86.928  1.00  8.09           O  
ATOM   1350  CG2 THR A 248     117.557 101.625  87.301  1.00  8.09           C  
ATOM   1351  N   ARG A 249     115.838 105.088  90.197  1.00  8.39           N  
ATOM   1352  CA  ARG A 249     115.886 106.470  90.681  1.00  8.39           C  
ATOM   1353  C   ARG A 249     116.810 107.325  89.816  1.00  8.39           C  
ATOM   1354  O   ARG A 249     117.812 107.872  90.279  1.00  8.39           O  
ATOM   1355  CB  ARG A 249     116.287 106.539  92.155  1.00  8.39           C  
ATOM   1356  CG  ARG A 249     115.568 105.554  93.057  1.00  8.39           C  
ATOM   1357  CD  ARG A 249     115.811 105.879  94.526  1.00  8.39           C  
ATOM   1358  NE  ARG A 249     116.030 104.701  95.357  1.00  8.39           N  
ATOM   1359  CZ  ARG A 249     117.226 104.285  95.761  1.00  8.39           C  
ATOM   1360  NH1 ARG A 249     118.312 104.970  95.433  1.00  8.39           N  
ATOM   1361  NH2 ARG A 249     117.335 103.201  96.516  1.00  8.39           N  
ATOM   1362  N   ALA A 250     116.460 107.426  88.531  1.00  8.94           N  
ATOM   1363  CA  ALA A 250     117.306 108.129  87.572  1.00  8.94           C  
ATOM   1364  C   ALA A 250     117.471 109.602  87.930  1.00  8.94           C  
ATOM   1365  O   ALA A 250     118.549 110.175  87.741  1.00  8.94           O  
ATOM   1366  CB  ALA A 250     116.729 107.983  86.166  1.00  8.94           C  
ATOM   1367  N   LEU A 251     116.414 110.235  88.434  1.00  9.22           N  
ATOM   1368  CA  LEU A 251     116.420 111.667  88.716  1.00  9.22           C  
ATOM   1369  C   LEU A 251     116.994 112.013  90.084  1.00  9.22           C  
ATOM   1370  O   LEU A 251     116.727 113.109  90.582  1.00  9.22           O  
ATOM   1371  CB  LEU A 251     115.003 112.234  88.602  1.00  9.22           C  
ATOM   1372  CG  LEU A 251     114.356 112.295  87.219  1.00  9.22           C  
ATOM   1373  CD1 LEU A 251     113.268 113.352  87.199  1.00  9.22           C  
ATOM   1374  CD2 LEU A 251     115.384 112.556  86.139  1.00  9.22           C  
ATOM   1375  N   THR A 252     117.755 111.110  90.705  1.00 12.64           N  
ATOM   1376  CA  THR A 252     118.344 111.396  92.011  1.00 12.64           C  
ATOM   1377  C   THR A 252     119.262 112.612  91.961  1.00 12.64           C  
ATOM   1378  O   THR A 252     119.270 113.432  92.886  1.00 12.64           O  
ATOM   1379  CB  THR A 252     119.107 110.171  92.517  1.00 12.64           C  
ATOM   1380  OG1 THR A 252     118.180 109.127  92.831  1.00 12.64           O  
ATOM   1381  CG2 THR A 252     119.910 110.510  93.759  1.00 12.64           C  
ATOM   1382  N   ALA A 253     120.039 112.748  90.885  1.00 17.47           N  
ATOM   1383  CA  ALA A 253     121.001 113.840  90.787  1.00 17.47           C  
ATOM   1384  C   ALA A 253     120.343 115.214  90.819  1.00 17.47           C  
ATOM   1385  O   ALA A 253     121.007 116.193  91.169  1.00 17.47           O  
ATOM   1386  CB  ALA A 253     121.830 113.694  89.513  1.00 17.47           C  
ATOM   1387  N   GLU A 254     119.058 115.311  90.470  1.00 16.71           N  
ATOM   1388  CA  GLU A 254     118.356 116.590  90.503  1.00 16.71           C  
ATOM   1389  C   GLU A 254     118.149 117.125  91.912  1.00 16.71           C  
ATOM   1390  O   GLU A 254     117.760 118.287  92.059  1.00 16.71           O  
ATOM   1391  CB  GLU A 254     117.007 116.467  89.796  1.00 16.71           C  
ATOM   1392  CG  GLU A 254     117.114 116.272  88.299  1.00 16.71           C  
ATOM   1393  CD  GLU A 254     117.497 117.546  87.567  1.00 16.71           C  
ATOM   1394  OE1 GLU A 254     117.624 117.502  86.328  1.00 16.71           O  
ATOM   1395  OE2 GLU A 254     117.637 118.599  88.220  1.00 16.71           O  
ATOM   1396  N   SER A 255     118.382 116.314  92.940  1.00 18.59           N  
ATOM   1397  CA  SER A 255     118.325 116.786  94.316  1.00 18.59           C  
ATOM   1398  C   SER A 255     119.593 117.510  94.743  1.00 18.59           C  
ATOM   1399  O   SER A 255     119.623 118.075  95.839  1.00 18.59           O  
ATOM   1400  CB  SER A 255     118.066 115.612  95.260  1.00 18.59           C  
ATOM   1401  OG  SER A 255     116.722 115.179  95.177  1.00 18.59           O  
ATOM   1402  N   HIS A 256     120.631 117.500  93.917  1.00 24.59           N  
ATOM   1403  CA  HIS A 256     121.930 118.054  94.261  1.00 24.59           C  
ATOM   1404  C   HIS A 256     122.122 119.419  93.611  1.00 24.59           C  
ATOM   1405  O   HIS A 256     121.504 119.733  92.591  1.00 24.59           O  
ATOM   1406  CB  HIS A 256     123.049 117.110  93.820  1.00 24.59           C  
ATOM   1407  CG  HIS A 256     123.086 115.821  94.578  1.00 24.59           C  
ATOM   1408  ND1 HIS A 256     123.707 115.693  95.800  1.00 24.59           N  
ATOM   1409  CD2 HIS A 256     122.575 114.602  94.287  1.00 24.59           C  
ATOM   1410  CE1 HIS A 256     123.579 114.450  96.229  1.00 24.59           C  
ATOM   1411  NE2 HIS A 256     122.894 113.768  95.330  1.00 24.59           N  
ATOM   1412  N   VAL A 257     122.988 120.232  94.220  1.00 28.73           N  
ATOM   1413  CA  VAL A 257     123.333 121.524  93.639  1.00 28.73           C  
ATOM   1414  C   VAL A 257     124.002 121.304  92.293  1.00 28.73           C  
ATOM   1415  O   VAL A 257     124.934 120.500  92.169  1.00 28.73           O  
ATOM   1416  CB  VAL A 257     124.237 122.320  94.591  1.00 28.73           C  
ATOM   1417  CG1 VAL A 257     124.497 123.707  94.035  1.00 28.73           C  
ATOM   1418  CG2 VAL A 257     123.604 122.420  95.965  1.00 28.73           C  
ATOM   1419  N   ASP A 258     123.525 122.020  91.271  1.00 34.45           N  
ATOM   1420  CA  ASP A 258     124.086 121.881  89.899  1.00 34.45           C  
ATOM   1421  C   ASP A 258     123.961 120.434  89.420  1.00 34.45           C  
ATOM   1422  O   ASP A 258     124.868 119.997  88.688  1.00 34.45           O  
ATOM   1423  CB  ASP A 258     125.473 122.513  89.766  1.00 34.45           C  
ATOM   1424  CG  ASP A 258     126.074 122.367  88.379  1.00 34.45           C  
ATOM   1425  OD1 ASP A 258     125.311 122.461  87.397  1.00 34.45           O  
ATOM   1426  OD2 ASP A 258     127.299 122.152  88.294  1.00 34.45           O  
ATOM   1427  N   THR A 259     122.882 119.723  89.762  1.00 30.08           N  
ATOM   1428  CA  THR A 259     122.648 118.333  89.276  1.00 30.08           C  
ATOM   1429  C   THR A 259     123.949 117.523  89.221  1.00 30.08           C  
ATOM   1430  O   THR A 259     124.138 116.799  88.226  1.00 30.08           O  
ATOM   1431  CB  THR A 259     121.850 118.322  87.968  1.00 30.08           C  
ATOM   1432  OG1 THR A 259     122.759 118.528  86.887  1.00 30.08           O  
ATOM   1433  CG2 THR A 259     120.773 119.383  87.940  1.00 30.08           C  
ATOM   1434  N   ASP A 260     124.809 117.644  90.234  1.00 31.76           N  
ATOM   1435  CA  ASP A 260     126.042 116.868  90.307  1.00 31.76           C  
ATOM   1436  C   ASP A 260     126.037 116.090  91.617  1.00 31.76           C  
ATOM   1437  O   ASP A 260     125.942 116.688  92.693  1.00 31.76           O  
ATOM   1438  CB  ASP A 260     127.263 117.787  90.221  1.00 31.76           C  
ATOM   1439  CG  ASP A 260     128.579 117.028  90.217  1.00 31.76           C  
ATOM   1440  OD1 ASP A 260     128.571 115.784  90.318  1.00 31.76           O  
ATOM   1441  OD2 ASP A 260     129.633 117.688  90.113  1.00 31.76           O  
ATOM   1442  N   LEU A 261     126.154 114.762  91.525  1.00 27.40           N  
ATOM   1443  CA  LEU A 261     126.058 113.919  92.714  1.00 27.40           C  
ATOM   1444  C   LEU A 261     127.178 114.163  93.715  1.00 27.40           C  
ATOM   1445  O   LEU A 261     127.029 113.805  94.888  1.00 27.40           O  
ATOM   1446  CB  LEU A 261     126.060 112.442  92.331  1.00 27.40           C  
ATOM   1447  CG  LEU A 261     124.852 111.876  91.594  1.00 27.40           C  
ATOM   1448  CD1 LEU A 261     125.238 110.561  90.968  1.00 27.40           C  
ATOM   1449  CD2 LEU A 261     123.678 111.693  92.537  1.00 27.40           C  
ATOM   1450  N   THR A 262     128.299 114.742  93.289  1.00 34.12           N  
ATOM   1451  CA  THR A 262     129.398 114.977  94.215  1.00 34.12           C  
ATOM   1452  C   THR A 262     129.183 116.216  95.071  1.00 34.12           C  
ATOM   1453  O   THR A 262     129.821 116.348  96.120  1.00 34.12           O  
ATOM   1454  CB  THR A 262     130.718 115.102  93.451  1.00 34.12           C  
ATOM   1455  OG1 THR A 262     130.574 116.061  92.399  1.00 34.12           O  
ATOM   1456  CG2 THR A 262     131.110 113.762  92.851  1.00 34.12           C  
ATOM   1457  N   LYS A 263     128.310 117.115  94.652  1.00 33.75           N  
ATOM   1458  CA  LYS A 263     127.994 118.327  95.388  1.00 33.75           C  
ATOM   1459  C   LYS A 263     126.821 118.083  96.330  1.00 33.75           C  
ATOM   1460  O   LYS A 263     126.059 117.129  96.153  1.00 33.75           O  
ATOM   1461  CB  LYS A 263     127.691 119.456  94.404  1.00 33.75           C  
ATOM   1462  CG  LYS A 263     128.953 120.011  93.759  1.00 33.75           C  
ATOM   1463  CD  LYS A 263     128.846 121.490  93.449  1.00 33.75           C  
ATOM   1464  CE  LYS A 263     127.856 121.743  92.336  1.00 33.75           C  
ATOM   1465  NZ  LYS A 263     128.500 121.645  90.996  1.00 33.75           N  
ATOM   1466  N   PRO A 264     126.653 118.917  97.356  1.00 31.00           N  
ATOM   1467  CA  PRO A 264     125.634 118.639  98.376  1.00 31.00           C  
ATOM   1468  C   PRO A 264     124.218 118.825  97.848  1.00 31.00           C  
ATOM   1469  O   PRO A 264     123.980 119.323  96.746  1.00 31.00           O  
ATOM   1470  CB  PRO A 264     125.955 119.651  99.479  1.00 31.00           C  
ATOM   1471  CG  PRO A 264     126.609 120.771  98.765  1.00 31.00           C  
ATOM   1472  CD  PRO A 264     127.437 120.115  97.699  1.00 31.00           C  
ATOM   1473  N   TYR A 265     123.263 118.394  98.669  1.00 29.20           N  
ATOM   1474  CA  TYR A 265     121.852 118.511  98.328  1.00 29.20           C  
ATOM   1475  C   TYR A 265     121.418 119.970  98.281  1.00 29.20           C  
ATOM   1476  O   TYR A 265     121.886 120.800  99.064  1.00 29.20           O  
ATOM   1477  CB  TYR A 265     120.993 117.764  99.347  1.00 29.20           C  
ATOM   1478  CG  TYR A 265     121.167 116.266  99.348  1.00 29.20           C  
ATOM   1479  CD1 TYR A 265     120.714 115.494  98.290  1.00 29.20           C  
ATOM   1480  CD2 TYR A 265     121.770 115.621 100.416  1.00 29.20           C  
ATOM   1481  CE1 TYR A 265     120.865 114.123  98.291  1.00 29.20           C  
ATOM   1482  CE2 TYR A 265     121.927 114.252 100.426  1.00 29.20           C  
ATOM   1483  CZ  TYR A 265     121.474 113.507  99.363  1.00 29.20           C  
ATOM   1484  OH  TYR A 265     121.630 112.141  99.372  1.00 29.20           O  
ATOM   1485  N   ILE A 266     120.513 120.281  97.350  1.00 23.74           N  
ATOM   1486  CA  ILE A 266     119.846 121.577  97.367  1.00 23.74           C  
ATOM   1487  C   ILE A 266     119.067 121.717  98.663  1.00 23.74           C  
ATOM   1488  O   ILE A 266     118.377 120.786  99.096  1.00 23.74           O  
ATOM   1489  CB  ILE A 266     118.922 121.729  96.150  1.00 23.74           C  
ATOM   1490  CG1 ILE A 266     119.717 121.674  94.849  1.00 23.74           C  
ATOM   1491  CG2 ILE A 266     118.127 123.023  96.234  1.00 23.74           C  
ATOM   1492  CD1 ILE A 266     118.844 121.681  93.621  1.00 23.74           C  
ATOM   1493  N   LYS A 267     119.178 122.881  99.296  1.00 25.23           N  
ATOM   1494  CA  LYS A 267     118.437 123.188 100.514  1.00 25.23           C  
ATOM   1495  C   LYS A 267     117.321 124.158 100.152  1.00 25.23           C  
ATOM   1496  O   LYS A 267     117.584 125.316  99.807  1.00 25.23           O  
ATOM   1497  CB  LYS A 267     119.355 123.772 101.584  1.00 25.23           C  
ATOM   1498  CG  LYS A 267     118.740 123.794 102.970  1.00 25.23           C  
ATOM   1499  CD  LYS A 267     119.556 124.648 103.925  1.00 25.23           C  
ATOM   1500  CE  LYS A 267     118.678 125.251 105.009  1.00 25.23           C  
ATOM   1501  NZ  LYS A 267     117.441 125.858 104.444  1.00 25.23           N  
ATOM   1502  N   TRP A 268     116.084 123.686 100.230  1.00 21.60           N  
ATOM   1503  CA  TRP A 268     114.917 124.476  99.876  1.00 21.60           C  
ATOM   1504  C   TRP A 268     114.396 125.247 101.082  1.00 21.60           C  
ATOM   1505  O   TRP A 268     114.646 124.894 102.237  1.00 21.60           O  
ATOM   1506  CB  TRP A 268     113.805 123.582  99.329  1.00 21.60           C  
ATOM   1507  CG  TRP A 268     114.169 122.812  98.110  1.00 21.60           C  
ATOM   1508  CD1 TRP A 268     114.586 121.518  98.056  1.00 21.60           C  
ATOM   1509  CD2 TRP A 268     114.103 123.269  96.757  1.00 21.60           C  
ATOM   1510  NE1 TRP A 268     114.808 121.146  96.755  1.00 21.60           N  
ATOM   1511  CE2 TRP A 268     114.518 122.204  95.937  1.00 21.60           C  
ATOM   1512  CE3 TRP A 268     113.745 124.481  96.159  1.00 21.60           C  
ATOM   1513  CZ2 TRP A 268     114.583 122.311  94.554  1.00 21.60           C  
ATOM   1514  CZ3 TRP A 268     113.811 124.585  94.786  1.00 21.60           C  
ATOM   1515  CH2 TRP A 268     114.226 123.508  93.998  1.00 21.60           C  
ATOM   1516  N   ASP A 269     113.661 126.316 100.795  1.00 23.52           N  
ATOM   1517  CA  ASP A 269     112.924 127.014 101.836  1.00 23.52           C  
ATOM   1518  C   ASP A 269     111.797 126.125 102.345  1.00 23.52           C  
ATOM   1519  O   ASP A 269     111.036 125.556 101.558  1.00 23.52           O  
ATOM   1520  CB  ASP A 269     112.372 128.331 101.294  1.00 23.52           C  
ATOM   1521  CG  ASP A 269     111.652 129.142 102.350  1.00 23.52           C  
ATOM   1522  OD1 ASP A 269     112.112 129.156 103.510  1.00 23.52           O  
ATOM   1523  OD2 ASP A 269     110.629 129.775 102.016  1.00 23.52           O  
ATOM   1524  N   LEU A 270     111.703 125.995 103.669  1.00 20.77           N  
ATOM   1525  CA  LEU A 270     110.704 125.110 104.258  1.00 20.77           C  
ATOM   1526  C   LEU A 270     109.284 125.555 103.937  1.00 20.77           C  
ATOM   1527  O   LEU A 270     108.360 124.736 103.956  1.00 20.77           O  
ATOM   1528  CB  LEU A 270     110.902 125.027 105.771  1.00 20.77           C  
ATOM   1529  CG  LEU A 270     111.664 123.805 106.281  1.00 20.77           C  
ATOM   1530  CD1 LEU A 270     113.085 123.792 105.754  1.00 20.77           C  
ATOM   1531  CD2 LEU A 270     111.655 123.774 107.791  1.00 20.77           C  
ATOM   1532  N   LEU A 271     109.088 126.839 103.650  1.00 23.24           N  
ATOM   1533  CA  LEU A 271     107.760 127.359 103.358  1.00 23.24           C  
ATOM   1534  C   LEU A 271     107.368 127.204 101.895  1.00 23.24           C  
ATOM   1535  O   LEU A 271     106.224 127.508 101.544  1.00 23.24           O  
ATOM   1536  CB  LEU A 271     107.673 128.834 103.757  1.00 23.24           C  
ATOM   1537  CG  LEU A 271     107.477 129.188 105.236  1.00 23.24           C  
ATOM   1538  CD1 LEU A 271     108.637 128.742 106.112  1.00 23.24           C  
ATOM   1539  CD2 LEU A 271     107.242 130.676 105.386  1.00 23.24           C  
ATOM   1540  N   LYS A 272     108.280 126.754 101.039  1.00 19.63           N  
ATOM   1541  CA  LYS A 272     107.984 126.614  99.619  1.00 19.63           C  
ATOM   1542  C   LYS A 272     107.168 125.350  99.379  1.00 19.63           C  
ATOM   1543  O   LYS A 272     107.601 124.249  99.729  1.00 19.63           O  
ATOM   1544  CB  LYS A 272     109.281 126.587  98.817  1.00 19.63           C  
ATOM   1545  CG  LYS A 272     109.094 126.790  97.329  1.00 19.63           C  
ATOM   1546  CD  LYS A 272     110.126 126.029  96.536  1.00 19.63           C  
ATOM   1547  CE  LYS A 272     110.458 126.747  95.246  1.00 19.63           C  
ATOM   1548  NZ  LYS A 272     109.248 126.967  94.415  1.00 19.63           N  
ATOM   1549  N   TYR A 273     105.977 125.510  98.801  1.00 17.22           N  
ATOM   1550  CA  TYR A 273     105.088 124.386  98.546  1.00 17.22           C  
ATOM   1551  C   TYR A 273     104.676 124.224  97.089  1.00 17.22           C  
ATOM   1552  O   TYR A 273     104.078 123.201  96.753  1.00 17.22           O  
ATOM   1553  CB  TYR A 273     103.832 124.496  99.433  1.00 17.22           C  
ATOM   1554  CG  TYR A 273     102.820 125.561  99.044  1.00 17.22           C  
ATOM   1555  CD1 TYR A 273     102.035 125.440  97.904  1.00 17.22           C  
ATOM   1556  CD2 TYR A 273     102.665 126.700  99.820  1.00 17.22           C  
ATOM   1557  CE1 TYR A 273     101.129 126.411  97.556  1.00 17.22           C  
ATOM   1558  CE2 TYR A 273     101.759 127.677  99.476  1.00 17.22           C  
ATOM   1559  CZ  TYR A 273     100.994 127.526  98.344  1.00 17.22           C  
ATOM   1560  OH  TYR A 273     100.088 128.497  97.994  1.00 17.22           O  
ATOM   1561  N   ASP A 274     104.959 125.196  96.222  1.00 17.19           N  
ATOM   1562  CA  ASP A 274     104.345 125.184  94.897  1.00 17.19           C  
ATOM   1563  C   ASP A 274     105.091 124.261  93.935  1.00 17.19           C  
ATOM   1564  O   ASP A 274     104.542 123.251  93.479  1.00 17.19           O  
ATOM   1565  CB  ASP A 274     104.271 126.609  94.344  1.00 17.19           C  
ATOM   1566  CG  ASP A 274     103.194 126.770  93.289  1.00 17.19           C  
ATOM   1567  OD1 ASP A 274     102.790 125.759  92.679  1.00 17.19           O  
ATOM   1568  OD2 ASP A 274     102.744 127.913  93.071  1.00 17.19           O  
ATOM   1569  N   PHE A 275     106.337 124.597  93.605  1.00 11.37           N  
ATOM   1570  CA  PHE A 275     107.215 123.780  92.769  1.00 11.37           C  
ATOM   1571  C   PHE A 275     106.700 123.583  91.347  1.00 11.37           C  
ATOM   1572  O   PHE A 275     107.209 122.715  90.632  1.00 11.37           O  
ATOM   1573  CB  PHE A 275     107.491 122.411  93.405  1.00 11.37           C  
ATOM   1574  CG  PHE A 275     108.291 122.480  94.670  1.00 11.37           C  
ATOM   1575  CD1 PHE A 275     109.663 122.636  94.626  1.00 11.37           C  
ATOM   1576  CD2 PHE A 275     107.675 122.385  95.901  1.00 11.37           C  
ATOM   1577  CE1 PHE A 275     110.400 122.694  95.784  1.00 11.37           C  
ATOM   1578  CE2 PHE A 275     108.411 122.446  97.060  1.00 11.37           C  
ATOM   1579  CZ  PHE A 275     109.773 122.600  97.001  1.00 11.37           C  
ATOM   1580  N   THR A 276     105.698 124.351  90.917  1.00 11.55           N  
ATOM   1581  CA  THR A 276     105.184 124.206  89.557  1.00 11.55           C  
ATOM   1582  C   THR A 276     106.254 124.524  88.515  1.00 11.55           C  
ATOM   1583  O   THR A 276     106.376 123.821  87.502  1.00 11.55           O  
ATOM   1584  CB  THR A 276     103.964 125.106  89.368  1.00 11.55           C  
ATOM   1585  OG1 THR A 276     102.960 124.751  90.325  1.00 11.55           O  
ATOM   1586  CG2 THR A 276     103.394 124.950  87.975  1.00 11.55           C  
ATOM   1587  N   GLU A 277     107.047 125.571  88.752  1.00 13.24           N  
ATOM   1588  CA  GLU A 277     108.098 125.928  87.804  1.00 13.24           C  
ATOM   1589  C   GLU A 277     109.202 124.881  87.778  1.00 13.24           C  
ATOM   1590  O   GLU A 277     109.762 124.593  86.716  1.00 13.24           O  
ATOM   1591  CB  GLU A 277     108.667 127.305  88.139  1.00 13.24           C  
ATOM   1592  CG  GLU A 277     107.709 128.465  87.896  1.00 13.24           C  
ATOM   1593  CD  GLU A 277     107.156 128.497  86.479  1.00 13.24           C  
ATOM   1594  OE1 GLU A 277     107.670 129.289  85.663  1.00 13.24           O  
ATOM   1595  OE2 GLU A 277     106.193 127.757  86.185  1.00 13.24           O  
ATOM   1596  N   GLU A 278     109.525 124.295  88.932  1.00 11.64           N  
ATOM   1597  CA  GLU A 278     110.492 123.202  88.956  1.00 11.64           C  
ATOM   1598  C   GLU A 278     109.980 121.997  88.178  1.00 11.64           C  
ATOM   1599  O   GLU A 278     110.744 121.349  87.453  1.00 11.64           O  
ATOM   1600  CB  GLU A 278     110.822 122.806  90.397  1.00 11.64           C  
ATOM   1601  CG  GLU A 278     111.623 123.820  91.219  1.00 11.64           C  
ATOM   1602  CD  GLU A 278     110.995 125.198  91.298  1.00 11.64           C  
ATOM   1603  OE1 GLU A 278     109.759 125.291  91.427  1.00 11.64           O  
ATOM   1604  OE2 GLU A 278     111.745 126.193  91.242  1.00 11.64           O  
ATOM   1605  N   ARG A 279     108.691 121.681  88.317  1.00  8.11           N  
ATOM   1606  CA  ARG A 279     108.109 120.576  87.563  1.00  8.11           C  
ATOM   1607  C   ARG A 279     108.171 120.831  86.063  1.00  8.11           C  
ATOM   1608  O   ARG A 279     108.518 119.932  85.286  1.00  8.11           O  
ATOM   1609  CB  ARG A 279     106.667 120.350  88.008  1.00  8.11           C  
ATOM   1610  CG  ARG A 279     106.531 119.650  89.339  1.00  8.11           C  
ATOM   1611  CD  ARG A 279     105.088 119.663  89.810  1.00  8.11           C  
ATOM   1612  NE  ARG A 279     104.931 119.222  91.193  1.00  8.11           N  
ATOM   1613  CZ  ARG A 279     105.111 117.974  91.613  1.00  8.11           C  
ATOM   1614  NH1 ARG A 279     105.451 117.021  90.759  1.00  8.11           N  
ATOM   1615  NH2 ARG A 279     104.938 117.677  92.891  1.00  8.11           N  
ATOM   1616  N   LEU A 280     107.842 122.053  85.634  1.00  8.82           N  
ATOM   1617  CA  LEU A 280     107.940 122.375  84.213  1.00  8.82           C  
ATOM   1618  C   LEU A 280     109.377 122.322  83.715  1.00  8.82           C  
ATOM   1619  O   LEU A 280     109.627 121.864  82.592  1.00  8.82           O  
ATOM   1620  CB  LEU A 280     107.338 123.750  83.939  1.00  8.82           C  
ATOM   1621  CG  LEU A 280     105.824 123.855  84.100  1.00  8.82           C  
ATOM   1622  CD1 LEU A 280     105.379 125.294  83.971  1.00  8.82           C  
ATOM   1623  CD2 LEU A 280     105.161 122.999  83.048  1.00  8.82           C  
ATOM   1624  N   LYS A 281     110.331 122.780  84.527  1.00  8.85           N  
ATOM   1625  CA  LYS A 281     111.731 122.707  84.132  1.00  8.85           C  
ATOM   1626  C   LYS A 281     112.192 121.264  83.988  1.00  8.85           C  
ATOM   1627  O   LYS A 281     112.917 120.934  83.047  1.00  8.85           O  
ATOM   1628  CB  LYS A 281     112.604 123.456  85.136  1.00  8.85           C  
ATOM   1629  CG  LYS A 281     112.722 124.941  84.852  1.00  8.85           C  
ATOM   1630  CD  LYS A 281     113.826 125.577  85.681  1.00  8.85           C  
ATOM   1631  CE  LYS A 281     113.472 125.615  87.158  1.00  8.85           C  
ATOM   1632  NZ  LYS A 281     112.505 126.703  87.468  1.00  8.85           N  
ATOM   1633  N   LEU A 282     111.783 120.389  84.909  1.00  7.83           N  
ATOM   1634  CA  LEU A 282     112.123 118.976  84.782  1.00  7.83           C  
ATOM   1635  C   LEU A 282     111.515 118.375  83.521  1.00  7.83           C  
ATOM   1636  O   LEU A 282     112.181 117.624  82.793  1.00  7.83           O  
ATOM   1637  CB  LEU A 282     111.656 118.211  86.019  1.00  7.83           C  
ATOM   1638  CG  LEU A 282     112.518 118.317  87.276  1.00  7.83           C  
ATOM   1639  CD1 LEU A 282     111.832 117.646  88.448  1.00  7.83           C  
ATOM   1640  CD2 LEU A 282     113.877 117.698  87.033  1.00  7.83           C  
ATOM   1641  N   PHE A 283     110.254 118.711  83.237  1.00  7.28           N  
ATOM   1642  CA  PHE A 283     109.594 118.185  82.049  1.00  7.28           C  
ATOM   1643  C   PHE A 283     110.310 118.618  80.776  1.00  7.28           C  
ATOM   1644  O   PHE A 283     110.526 117.805  79.872  1.00  7.28           O  
ATOM   1645  CB  PHE A 283     108.136 118.630  82.018  1.00  7.28           C  
ATOM   1646  CG  PHE A 283     107.304 117.887  81.020  1.00  7.28           C  
ATOM   1647  CD1 PHE A 283     106.808 116.630  81.306  1.00  7.28           C  
ATOM   1648  CD2 PHE A 283     107.025 118.445  79.788  1.00  7.28           C  
ATOM   1649  CE1 PHE A 283     106.049 115.949  80.386  1.00  7.28           C  
ATOM   1650  CE2 PHE A 283     106.267 117.767  78.866  1.00  7.28           C  
ATOM   1651  CZ  PHE A 283     105.778 116.518  79.164  1.00  7.28           C  
ATOM   1652  N   ASP A 284     110.682 119.895  80.680  1.00 12.86           N  
ATOM   1653  CA  ASP A 284     111.383 120.350  79.484  1.00 12.86           C  
ATOM   1654  C   ASP A 284     112.819 119.847  79.419  1.00 12.86           C  
ATOM   1655  O   ASP A 284     113.355 119.686  78.319  1.00 12.86           O  
ATOM   1656  CB  ASP A 284     111.363 121.874  79.396  1.00 12.86           C  
ATOM   1657  CG  ASP A 284     110.125 122.396  78.697  1.00 12.86           C  
ATOM   1658  OD1 ASP A 284     109.079 121.715  78.749  1.00 12.86           O  
ATOM   1659  OD2 ASP A 284     110.199 123.483  78.087  1.00 12.86           O  
ATOM   1660  N   ARG A 285     113.454 119.598  80.563  1.00 13.18           N  
ATOM   1661  CA  ARG A 285     114.802 119.047  80.547  1.00 13.18           C  
ATOM   1662  C   ARG A 285     114.813 117.617  80.029  1.00 13.18           C  
ATOM   1663  O   ARG A 285     115.690 117.245  79.241  1.00 13.18           O  
ATOM   1664  CB  ARG A 285     115.411 119.103  81.944  1.00 13.18           C  
ATOM   1665  CG  ARG A 285     116.850 118.634  82.000  1.00 13.18           C  
ATOM   1666  CD  ARG A 285     117.468 118.913  83.349  1.00 13.18           C  
ATOM   1667  NE  ARG A 285     117.665 120.340  83.565  1.00 13.18           N  
ATOM   1668  CZ  ARG A 285     118.641 120.852  84.304  1.00 13.18           C  
ATOM   1669  NH1 ARG A 285     118.750 122.166  84.442  1.00 13.18           N  
ATOM   1670  NH2 ARG A 285     119.507 120.051  84.906  1.00 13.18           N  
ATOM   1671  N   TYR A 286     113.852 116.797  80.454  1.00 10.15           N  
ATOM   1672  CA  TYR A 286     113.931 115.372  80.164  1.00 10.15           C  
ATOM   1673  C   TYR A 286     112.906 114.875  79.158  1.00 10.15           C  
ATOM   1674  O   TYR A 286     113.131 113.833  78.543  1.00 10.15           O  
ATOM   1675  CB  TYR A 286     113.798 114.565  81.459  1.00 10.15           C  
ATOM   1676  CG  TYR A 286     114.963 114.777  82.391  1.00 10.15           C  
ATOM   1677  CD1 TYR A 286     116.222 114.285  82.085  1.00 10.15           C  
ATOM   1678  CD2 TYR A 286     114.808 115.486  83.571  1.00 10.15           C  
ATOM   1679  CE1 TYR A 286     117.289 114.489  82.930  1.00 10.15           C  
ATOM   1680  CE2 TYR A 286     115.868 115.692  84.421  1.00 10.15           C  
ATOM   1681  CZ  TYR A 286     117.106 115.192  84.098  1.00 10.15           C  
ATOM   1682  OH  TYR A 286     118.165 115.398  84.947  1.00 10.15           O  
ATOM   1683  N   PHE A 287     111.798 115.589  78.966  1.00  8.09           N  
ATOM   1684  CA  PHE A 287     110.721 115.131  78.095  1.00  8.09           C  
ATOM   1685  C   PHE A 287     110.312 116.216  77.108  1.00  8.09           C  
ATOM   1686  O   PHE A 287     109.122 116.418  76.862  1.00  8.09           O  
ATOM   1687  CB  PHE A 287     109.515 114.674  78.914  1.00  8.09           C  
ATOM   1688  CG  PHE A 287     109.838 113.605  79.909  1.00  8.09           C  
ATOM   1689  CD1 PHE A 287     109.775 112.272  79.556  1.00  8.09           C  
ATOM   1690  CD2 PHE A 287     110.221 113.934  81.195  1.00  8.09           C  
ATOM   1691  CE1 PHE A 287     110.079 111.290  80.470  1.00  8.09           C  
ATOM   1692  CE2 PHE A 287     110.528 112.955  82.110  1.00  8.09           C  
ATOM   1693  CZ  PHE A 287     110.456 111.631  81.746  1.00  8.09           C  
ATOM   1694  N   LYS A 288     111.293 116.934  76.558  1.00 13.49           N  
ATOM   1695  CA  LYS A 288     111.009 118.088  75.710  1.00 13.49           C  
ATOM   1696  C   LYS A 288     110.096 117.738  74.542  1.00 13.49           C  
ATOM   1697  O   LYS A 288     109.215 118.524  74.176  1.00 13.49           O  
ATOM   1698  CB  LYS A 288     112.321 118.680  75.199  1.00 13.49           C  
ATOM   1699  CG  LYS A 288     112.159 119.802  74.195  1.00 13.49           C  
ATOM   1700  CD  LYS A 288     113.341 120.746  74.243  1.00 13.49           C  
ATOM   1701  CE  LYS A 288     113.431 121.576  72.977  1.00 13.49           C  
ATOM   1702  NZ  LYS A 288     112.086 121.873  72.417  1.00 13.49           N  
ATOM   1703  N   TYR A 289     110.288 116.567  73.943  1.00 16.58           N  
ATOM   1704  CA  TYR A 289     109.568 116.177  72.739  1.00 16.58           C  
ATOM   1705  C   TYR A 289     108.429 115.205  72.993  1.00 16.58           C  
ATOM   1706  O   TYR A 289     107.866 114.671  72.033  1.00 16.58           O  
ATOM   1707  CB  TYR A 289     110.546 115.599  71.717  1.00 16.58           C  
ATOM   1708  CG  TYR A 289     111.495 116.651  71.215  1.00 16.58           C  
ATOM   1709  CD1 TYR A 289     111.104 117.548  70.233  1.00 16.58           C  
ATOM   1710  CD2 TYR A 289     112.746 116.808  71.782  1.00 16.58           C  
ATOM   1711  CE1 TYR A 289     111.956 118.529  69.787  1.00 16.58           C  
ATOM   1712  CE2 TYR A 289     113.603 117.786  71.346  1.00 16.58           C  
ATOM   1713  CZ  TYR A 289     113.205 118.646  70.347  1.00 16.58           C  
ATOM   1714  OH  TYR A 289     114.058 119.630  69.911  1.00 16.58           O  
ATOM   1715  N   TRP A 290     108.082 114.952  74.250  1.00 10.85           N  
ATOM   1716  CA  TRP A 290     106.847 114.244  74.538  1.00 10.85           C  
ATOM   1717  C   TRP A 290     105.676 115.079  74.032  1.00 10.85           C  
ATOM   1718  O   TRP A 290     105.521 116.245  74.402  1.00 10.85           O  
ATOM   1719  CB  TRP A 290     106.730 113.991  76.038  1.00 10.85           C  
ATOM   1720  CG  TRP A 290     105.505 113.257  76.436  1.00 10.85           C  
ATOM   1721  CD1 TRP A 290     104.383 113.786  76.986  1.00 10.85           C  
ATOM   1722  CD2 TRP A 290     105.290 111.844  76.365  1.00 10.85           C  
ATOM   1723  NE1 TRP A 290     103.469 112.798  77.235  1.00 10.85           N  
ATOM   1724  CE2 TRP A 290     104.004 111.594  76.870  1.00 10.85           C  
ATOM   1725  CE3 TRP A 290     106.059 110.767  75.918  1.00 10.85           C  
ATOM   1726  CZ2 TRP A 290     103.466 110.314  76.940  1.00 10.85           C  
ATOM   1727  CZ3 TRP A 290     105.524 109.498  75.987  1.00 10.85           C  
ATOM   1728  CH2 TRP A 290     104.241 109.282  76.492  1.00 10.85           C  
ATOM   1729  N   ASP A 291     104.847 114.476  73.183  1.00 20.10           N  
ATOM   1730  CA  ASP A 291     103.943 115.245  72.337  1.00 20.10           C  
ATOM   1731  C   ASP A 291     102.712 115.767  73.070  1.00 20.10           C  
ATOM   1732  O   ASP A 291     102.079 116.710  72.585  1.00 20.10           O  
ATOM   1733  CB  ASP A 291     103.520 114.387  71.141  1.00 20.10           C  
ATOM   1734  CG  ASP A 291     102.636 115.133  70.167  1.00 20.10           C  
ATOM   1735  OD1 ASP A 291     102.988 116.273  69.802  1.00 20.10           O  
ATOM   1736  OD2 ASP A 291     101.596 114.577  69.756  1.00 20.10           O  
ATOM   1737  N   GLN A 292     102.366 115.201  74.221  1.00 10.60           N  
ATOM   1738  CA  GLN A 292     101.129 115.550  74.904  1.00 10.60           C  
ATOM   1739  C   GLN A 292     101.364 116.628  75.960  1.00 10.60           C  
ATOM   1740  O   GLN A 292     102.438 116.717  76.558  1.00 10.60           O  
ATOM   1741  CB  GLN A 292     100.513 114.301  75.539  1.00 10.60           C  
ATOM   1742  CG  GLN A 292      99.305 114.551  76.421  1.00 10.60           C  
ATOM   1743  CD  GLN A 292      98.388 113.355  76.501  1.00 10.60           C  
ATOM   1744  OE1 GLN A 292      98.646 112.323  75.891  1.00 10.60           O  
ATOM   1745  NE2 GLN A 292      97.315 113.484  77.266  1.00 10.60           N  
ATOM   1746  N   THR A 293     100.342 117.460  76.171  1.00 10.06           N  
ATOM   1747  CA  THR A 293     100.412 118.529  77.162  1.00 10.06           C  
ATOM   1748  C   THR A 293     100.479 117.966  78.576  1.00 10.06           C  
ATOM   1749  O   THR A 293      99.759 117.028  78.925  1.00 10.06           O  
ATOM   1750  CB  THR A 293      99.196 119.450  77.037  1.00 10.06           C  
ATOM   1751  OG1 THR A 293      99.010 119.821  75.668  1.00 10.06           O  
ATOM   1752  CG2 THR A 293      99.385 120.703  77.872  1.00 10.06           C  
ATOM   1753  N   TYR A 294     101.341 118.558  79.398  1.00  6.49           N  
ATOM   1754  CA  TYR A 294     101.516 118.154  80.786  1.00  6.49           C  
ATOM   1755  C   TYR A 294     100.957 119.246  81.688  1.00  6.49           C  
ATOM   1756  O   TYR A 294     101.254 120.428  81.489  1.00  6.49           O  
ATOM   1757  CB  TYR A 294     102.997 117.916  81.086  1.00  6.49           C  
ATOM   1758  CG  TYR A 294     103.371 117.857  82.550  1.00  6.49           C  
ATOM   1759  CD1 TYR A 294     102.680 117.037  83.431  1.00  6.49           C  
ATOM   1760  CD2 TYR A 294     104.416 118.619  83.051  1.00  6.49           C  
ATOM   1761  CE1 TYR A 294     103.024 116.971  84.758  1.00  6.49           C  
ATOM   1762  CE2 TYR A 294     104.761 118.562  84.380  1.00  6.49           C  
ATOM   1763  CZ  TYR A 294     104.062 117.735  85.229  1.00  6.49           C  
ATOM   1764  OH  TYR A 294     104.400 117.673  86.558  1.00  6.49           O  
ATOM   1765  N   HIS A 295     100.145 118.856  82.667  1.00  8.34           N  
ATOM   1766  CA  HIS A 295      99.645 119.800  83.662  1.00  8.34           C  
ATOM   1767  C   HIS A 295     100.326 119.554  84.999  1.00  8.34           C  
ATOM   1768  O   HIS A 295     100.065 118.524  85.638  1.00  8.34           O  
ATOM   1769  CB  HIS A 295      98.127 119.695  83.821  1.00  8.34           C  
ATOM   1770  CG  HIS A 295      97.366 119.920  82.555  1.00  8.34           C  
ATOM   1771  ND1 HIS A 295      96.922 118.888  81.758  1.00  8.34           N  
ATOM   1772  CD2 HIS A 295      96.979 121.062  81.942  1.00  8.34           C  
ATOM   1773  CE1 HIS A 295      96.287 119.385  80.713  1.00  8.34           C  
ATOM   1774  NE2 HIS A 295      96.310 120.702  80.800  1.00  8.34           N  
ATOM   1775  N   PRO A 296     101.187 120.458  85.468  1.00  8.02           N  
ATOM   1776  CA  PRO A 296     101.758 120.285  86.811  1.00  8.02           C  
ATOM   1777  C   PRO A 296     100.702 120.230  87.891  1.00  8.02           C  
ATOM   1778  O   PRO A 296     100.922 119.612  88.938  1.00  8.02           O  
ATOM   1779  CB  PRO A 296     102.657 121.517  86.975  1.00  8.02           C  
ATOM   1780  CG  PRO A 296     102.953 121.956  85.608  1.00  8.02           C  
ATOM   1781  CD  PRO A 296     101.758 121.617  84.771  1.00  8.02           C  
ATOM   1782  N   ASN A 297      99.562 120.877  87.670  1.00  8.70           N  
ATOM   1783  CA  ASN A 297      98.460 120.915  88.620  1.00  8.70           C  
ATOM   1784  C   ASN A 297      97.283 120.211  87.960  1.00  8.70           C  
ATOM   1785  O   ASN A 297      96.699 120.738  87.008  1.00  8.70           O  
ATOM   1786  CB  ASN A 297      98.112 122.356  88.980  1.00  8.70           C  
ATOM   1787  CG  ASN A 297      99.110 122.973  89.932  1.00  8.70           C  
ATOM   1788  OD1 ASN A 297      99.673 122.292  90.783  1.00  8.70           O  
ATOM   1789  ND2 ASN A 297      99.311 124.271  89.813  1.00  8.70           N  
ATOM   1790  N   CYS A 298      96.921 119.033  88.468  1.00  9.66           N  
ATOM   1791  CA  CYS A 298      95.904 118.223  87.806  1.00  9.66           C  
ATOM   1792  C   CYS A 298      94.512 118.835  87.870  1.00  9.66           C  
ATOM   1793  O   CYS A 298      93.605 118.325  87.206  1.00  9.66           O  
ATOM   1794  CB  CYS A 298      95.879 116.811  88.395  1.00  9.66           C  
ATOM   1795  SG  CYS A 298      97.373 115.844  88.096  1.00  9.66           S  
ATOM   1796  N   VAL A 299      94.318 119.905  88.643  1.00  8.15           N  
ATOM   1797  CA  VAL A 299      93.043 120.611  88.643  1.00  8.15           C  
ATOM   1798  C   VAL A 299      92.752 121.228  87.282  1.00  8.15           C  
ATOM   1799  O   VAL A 299      91.595 121.526  86.971  1.00  8.15           O  
ATOM   1800  CB  VAL A 299      93.030 121.673  89.763  1.00  8.15           C  
ATOM   1801  CG1 VAL A 299      93.880 122.874  89.384  1.00  8.15           C  
ATOM   1802  CG2 VAL A 299      91.607 122.091  90.089  1.00  8.15           C  
ATOM   1803  N   ASN A 300      93.777 121.423  86.456  1.00  9.07           N  
ATOM   1804  CA  ASN A 300      93.616 121.960  85.112  1.00  9.07           C  
ATOM   1805  C   ASN A 300      93.404 120.886  84.055  1.00  9.07           C  
ATOM   1806  O   ASN A 300      93.279 121.222  82.874  1.00  9.07           O  
ATOM   1807  CB  ASN A 300      94.831 122.813  84.737  1.00  9.07           C  
ATOM   1808  CG  ASN A 300      95.082 123.932  85.725  1.00  9.07           C  
ATOM   1809  OD1 ASN A 300      94.190 124.723  86.022  1.00  9.07           O  
ATOM   1810  ND2 ASN A 300      96.301 124.004  86.242  1.00  9.07           N  
ATOM   1811  N   CYS A 301      93.369 119.615  84.442  1.00 12.33           N  
ATOM   1812  CA  CYS A 301      93.239 118.530  83.483  1.00 12.33           C  
ATOM   1813  C   CYS A 301      91.870 118.562  82.806  1.00 12.33           C  
ATOM   1814  O   CYS A 301      90.948 119.258  83.234  1.00 12.33           O  
ATOM   1815  CB  CYS A 301      93.459 117.186  84.173  1.00 12.33           C  
ATOM   1816  SG  CYS A 301      95.190 116.820  84.554  1.00 12.33           S  
ATOM   1817  N   LEU A 302      91.752 117.796  81.723  1.00 15.33           N  
ATOM   1818  CA  LEU A 302      90.566 117.824  80.876  1.00 15.33           C  
ATOM   1819  C   LEU A 302      89.608 116.668  81.120  1.00 15.33           C  
ATOM   1820  O   LEU A 302      88.397 116.848  80.974  1.00 15.33           O  
ATOM   1821  CB  LEU A 302      90.978 117.822  79.401  1.00 15.33           C  
ATOM   1822  CG  LEU A 302      91.872 118.980  78.961  1.00 15.33           C  
ATOM   1823  CD1 LEU A 302      92.345 118.770  77.535  1.00 15.33           C  
ATOM   1824  CD2 LEU A 302      91.141 120.302  79.095  1.00 15.33           C  
ATOM   1825  N   ASP A 303      90.115 115.490  81.468  1.00 13.61           N  
ATOM   1826  CA  ASP A 303      89.283 114.338  81.793  1.00 13.61           C  
ATOM   1827  C   ASP A 303      90.090 113.423  82.706  1.00 13.61           C  
ATOM   1828  O   ASP A 303      91.156 113.799  83.198  1.00 13.61           O  
ATOM   1829  CB  ASP A 303      88.800 113.628  80.521  1.00 13.61           C  
ATOM   1830  CG  ASP A 303      89.934 113.269  79.576  1.00 13.61           C  
ATOM   1831  OD1 ASP A 303      91.096 113.600  79.876  1.00 13.61           O  
ATOM   1832  OD2 ASP A 303      89.660 112.651  78.526  1.00 13.61           O  
ATOM   1833  N   ASP A 304      89.579 112.212  82.939  1.00 10.18           N  
ATOM   1834  CA  ASP A 304      90.294 111.277  83.802  1.00 10.18           C  
ATOM   1835  C   ASP A 304      91.515 110.673  83.118  1.00 10.18           C  
ATOM   1836  O   ASP A 304      92.503 110.370  83.796  1.00 10.18           O  
ATOM   1837  CB  ASP A 304      89.345 110.180  84.292  1.00 10.18           C  
ATOM   1838  CG  ASP A 304      88.604 109.488  83.164  1.00 10.18           C  
ATOM   1839  OD1 ASP A 304      87.983 110.185  82.338  1.00 10.18           O  
ATOM   1840  OD2 ASP A 304      88.639 108.243  83.109  1.00 10.18           O  
ATOM   1841  N   ARG A 305      91.491 110.527  81.792  1.00  8.50           N  
ATOM   1842  CA  ARG A 305      92.683 110.097  81.070  1.00  8.50           C  
ATOM   1843  C   ARG A 305      93.793 111.139  81.130  1.00  8.50           C  
ATOM   1844  O   ARG A 305      94.968 110.779  81.283  1.00  8.50           O  
ATOM   1845  CB  ARG A 305      92.327 109.798  79.614  1.00  8.50           C  
ATOM   1846  CG  ARG A 305      91.402 108.613  79.424  1.00  8.50           C  
ATOM   1847  CD  ARG A 305      90.917 108.517  77.984  1.00  8.50           C  
ATOM   1848  NE  ARG A 305      91.959 108.116  77.039  1.00  8.50           N  
ATOM   1849  CZ  ARG A 305      92.494 106.902  76.967  1.00  8.50           C  
ATOM   1850  NH1 ARG A 305      92.093 105.942  77.784  1.00  8.50           N  
ATOM   1851  NH2 ARG A 305      93.430 106.647  76.066  1.00  8.50           N  
ATOM   1852  N   CYS A 306      93.440 112.422  81.066  1.00 10.05           N  
ATOM   1853  CA  CYS A 306      94.436 113.472  81.236  1.00 10.05           C  
ATOM   1854  C   CYS A 306      94.957 113.493  82.669  1.00 10.05           C  
ATOM   1855  O   CYS A 306      96.148 113.729  82.906  1.00 10.05           O  
ATOM   1856  CB  CYS A 306      93.839 114.823  80.842  1.00 10.05           C  
ATOM   1857  SG  CYS A 306      94.999 116.199  80.872  1.00 10.05           S  
ATOM   1858  N   ILE A 307      94.072 113.256  83.641  1.00  7.62           N  
ATOM   1859  CA  ILE A 307      94.506 113.189  85.033  1.00  7.62           C  
ATOM   1860  C   ILE A 307      95.529 112.081  85.218  1.00  7.62           C  
ATOM   1861  O   ILE A 307      96.558 112.281  85.869  1.00  7.62           O  
ATOM   1862  CB  ILE A 307      93.304 113.006  85.978  1.00  7.62           C  
ATOM   1863  CG1 ILE A 307      92.488 114.293  86.073  1.00  7.62           C  
ATOM   1864  CG2 ILE A 307      93.773 112.579  87.360  1.00  7.62           C  
ATOM   1865  CD1 ILE A 307      91.223 114.145  86.875  1.00  7.62           C  
ATOM   1866  N   LEU A 308      95.270 110.900  84.651  1.00  6.58           N  
ATOM   1867  CA  LEU A 308      96.241 109.813  84.758  1.00  6.58           C  
ATOM   1868  C   LEU A 308      97.554 110.173  84.078  1.00  6.58           C  
ATOM   1869  O   LEU A 308      98.636 109.939  84.636  1.00  6.58           O  
ATOM   1870  CB  LEU A 308      95.664 108.532  84.161  1.00  6.58           C  
ATOM   1871  CG  LEU A 308      94.680 107.761  85.038  1.00  6.58           C  
ATOM   1872  CD1 LEU A 308      94.240 106.481  84.358  1.00  6.58           C  
ATOM   1873  CD2 LEU A 308      95.318 107.455  86.381  1.00  6.58           C  
ATOM   1874  N   HIS A 309      97.473 110.779  82.891  1.00  5.94           N  
ATOM   1875  CA  HIS A 309      98.677 111.164  82.164  1.00  5.94           C  
ATOM   1876  C   HIS A 309      99.556 112.096  82.990  1.00  5.94           C  
ATOM   1877  O   HIS A 309     100.758 111.857  83.145  1.00  5.94           O  
ATOM   1878  CB  HIS A 309      98.287 111.818  80.839  1.00  5.94           C  
ATOM   1879  CG  HIS A 309      99.438 112.413  80.095  1.00  5.94           C  
ATOM   1880  ND1 HIS A 309      99.926 113.674  80.361  1.00  5.94           N  
ATOM   1881  CD2 HIS A 309     100.205 111.917  79.097  1.00  5.94           C  
ATOM   1882  CE1 HIS A 309     100.937 113.932  79.555  1.00  5.94           C  
ATOM   1883  NE2 HIS A 309     101.125 112.883  78.776  1.00  5.94           N  
ATOM   1884  N   CYS A 310      98.975 113.166  83.530  1.00  9.56           N  
ATOM   1885  CA  CYS A 310      99.783 114.141  84.256  1.00  9.56           C  
ATOM   1886  C   CYS A 310     100.164 113.670  85.656  1.00  9.56           C  
ATOM   1887  O   CYS A 310     101.236 114.034  86.154  1.00  9.56           O  
ATOM   1888  CB  CYS A 310      99.063 115.487  84.303  1.00  9.56           C  
ATOM   1889  SG  CYS A 310      98.374 115.977  82.704  1.00  9.56           S  
ATOM   1890  N   ALA A 311      99.331 112.850  86.300  1.00 16.74           N  
ATOM   1891  CA  ALA A 311      99.705 112.295  87.594  1.00 16.74           C  
ATOM   1892  C   ALA A 311     100.904 111.368  87.466  1.00 16.74           C  
ATOM   1893  O   ALA A 311     101.753 111.319  88.364  1.00 16.74           O  
ATOM   1894  CB  ALA A 311      98.518 111.561  88.216  1.00 16.74           C  
ATOM   1895  N   ASN A 312     100.995 110.625  86.358  1.00 10.22           N  
ATOM   1896  CA  ASN A 312     102.151 109.755  86.166  1.00 10.22           C  
ATOM   1897  C   ASN A 312     103.450 110.554  86.121  1.00 10.22           C  
ATOM   1898  O   ASN A 312     104.439 110.175  86.758  1.00 10.22           O  
ATOM   1899  CB  ASN A 312     101.973 108.928  84.895  1.00 10.22           C  
ATOM   1900  CG  ASN A 312     102.780 107.653  84.915  1.00 10.22           C  
ATOM   1901  OD1 ASN A 312     102.521 106.753  85.709  1.00 10.22           O  
ATOM   1902  ND2 ASN A 312     103.754 107.559  84.023  1.00 10.22           N  
ATOM   1903  N   PHE A 313     103.470 111.669  85.384  1.00  9.28           N  
ATOM   1904  CA  PHE A 313     104.644 112.540  85.404  1.00  9.28           C  
ATOM   1905  C   PHE A 313     104.883 113.142  86.781  1.00  9.28           C  
ATOM   1906  O   PHE A 313     106.033 113.288  87.204  1.00  9.28           O  
ATOM   1907  CB  PHE A 313     104.520 113.648  84.360  1.00  9.28           C  
ATOM   1908  CG  PHE A 313     104.792 113.197  82.959  1.00  9.28           C  
ATOM   1909  CD1 PHE A 313     106.029 112.672  82.620  1.00  9.28           C  
ATOM   1910  CD2 PHE A 313     103.830 113.315  81.976  1.00  9.28           C  
ATOM   1911  CE1 PHE A 313     106.295 112.264  81.333  1.00  9.28           C  
ATOM   1912  CE2 PHE A 313     104.092 112.903  80.686  1.00  9.28           C  
ATOM   1913  CZ  PHE A 313     105.325 112.380  80.365  1.00  9.28           C  
ATOM   1914  N   ASN A 314     103.816 113.522  87.487  1.00 16.74           N  
ATOM   1915  CA  ASN A 314     103.985 114.116  88.811  1.00 16.74           C  
ATOM   1916  C   ASN A 314     104.622 113.141  89.798  1.00 16.74           C  
ATOM   1917  O   ASN A 314     105.342 113.559  90.710  1.00 16.74           O  
ATOM   1918  CB  ASN A 314     102.644 114.618  89.337  1.00 16.74           C  
ATOM   1919  CG  ASN A 314     102.217 115.914  88.693  1.00 16.74           C  
ATOM   1920  OD1 ASN A 314     102.946 116.490  87.891  1.00 16.74           O  
ATOM   1921  ND2 ASN A 314     101.026 116.377  89.033  1.00 16.74           N  
ATOM   1922  N   VAL A 315     104.355 111.841  89.648  1.00 16.74           N  
ATOM   1923  CA  VAL A 315     104.989 110.852  90.523  1.00 16.74           C  
ATOM   1924  C   VAL A 315     106.508 110.899  90.399  1.00 16.74           C  
ATOM   1925  O   VAL A 315     107.229 110.812  91.400  1.00 16.74           O  
ATOM   1926  CB  VAL A 315     104.450 109.437  90.242  1.00 16.74           C  
ATOM   1927  CG1 VAL A 315     105.037 108.455  91.227  1.00 16.74           C  
ATOM   1928  CG2 VAL A 315     102.963 109.420  90.393  1.00 16.74           C  
ATOM   1929  N   LEU A 316     107.021 111.008  89.174  1.00 16.74           N  
ATOM   1930  CA  LEU A 316     108.467 111.039  88.977  1.00 16.74           C  
ATOM   1931  C   LEU A 316     109.082 112.314  89.541  1.00 16.74           C  
ATOM   1932  O   LEU A 316     110.093 112.266  90.248  1.00 16.74           O  
ATOM   1933  CB  LEU A 316     108.790 110.889  87.491  1.00 16.74           C  
ATOM   1934  CG  LEU A 316     110.255 110.637  87.136  1.00 16.74           C  
ATOM   1935  CD1 LEU A 316     110.595 109.180  87.268  1.00 16.74           C  
ATOM   1936  CD2 LEU A 316     110.526 111.120  85.729  1.00 16.74           C  
ATOM   1937  N   PHE A 317     108.490 113.467  89.232  1.00  7.40           N  
ATOM   1938  CA  PHE A 317     109.060 114.739  89.667  1.00  7.40           C  
ATOM   1939  C   PHE A 317     108.969 114.930  91.175  1.00  7.40           C  
ATOM   1940  O   PHE A 317     109.827 115.596  91.759  1.00  7.40           O  
ATOM   1941  CB  PHE A 317     108.379 115.897  88.940  1.00  7.40           C  
ATOM   1942  CG  PHE A 317     108.458 115.810  87.442  1.00  7.40           C  
ATOM   1943  CD1 PHE A 317     109.416 115.025  86.824  1.00  7.40           C  
ATOM   1944  CD2 PHE A 317     107.561 116.500  86.652  1.00  7.40           C  
ATOM   1945  CE1 PHE A 317     109.486 114.944  85.452  1.00  7.40           C  
ATOM   1946  CE2 PHE A 317     107.625 116.418  85.277  1.00  7.40           C  
ATOM   1947  CZ  PHE A 317     108.587 115.638  84.679  1.00  7.40           C  
ATOM   1948  N   SER A 318     107.952 114.364  91.823  1.00  7.82           N  
ATOM   1949  CA  SER A 318     107.796 114.531  93.263  1.00  7.82           C  
ATOM   1950  C   SER A 318     108.896 113.849  94.064  1.00  7.82           C  
ATOM   1951  O   SER A 318     109.048 114.148  95.252  1.00  7.82           O  
ATOM   1952  CB  SER A 318     106.438 113.998  93.707  1.00  7.82           C  
ATOM   1953  OG  SER A 318     105.393 114.592  92.965  1.00  7.82           O  
ATOM   1954  N   THR A 319     109.662 112.946  93.453  1.00  9.28           N  
ATOM   1955  CA  THR A 319     110.779 112.325  94.152  1.00  9.28           C  
ATOM   1956  C   THR A 319     111.947 113.283  94.336  1.00  9.28           C  
ATOM   1957  O   THR A 319     112.861 112.985  95.111  1.00  9.28           O  
ATOM   1958  CB  THR A 319     111.240 111.075  93.403  1.00  9.28           C  
ATOM   1959  OG1 THR A 319     111.686 111.436  92.093  1.00  9.28           O  
ATOM   1960  CG2 THR A 319     110.108 110.074  93.289  1.00  9.28           C  
ATOM   1961  N   VAL A 320     111.933 114.424  93.646  1.00  8.43           N  
ATOM   1962  CA  VAL A 320     113.023 115.386  93.750  1.00  8.43           C  
ATOM   1963  C   VAL A 320     112.800 116.366  94.899  1.00  8.43           C  
ATOM   1964  O   VAL A 320     113.760 116.781  95.557  1.00  8.43           O  
ATOM   1965  CB  VAL A 320     113.191 116.118  92.406  1.00  8.43           C  
ATOM   1966  CG1 VAL A 320     114.232 117.216  92.507  1.00  8.43           C  
ATOM   1967  CG2 VAL A 320     113.558 115.132  91.310  1.00  8.43           C  
ATOM   1968  N   PHE A 321     111.553 116.734  95.178  1.00  6.66           N  
ATOM   1969  CA  PHE A 321     111.233 117.794  96.122  1.00  6.66           C  
ATOM   1970  C   PHE A 321     111.187 117.265  97.550  1.00  6.66           C  
ATOM   1971  O   PHE A 321     110.947 116.077  97.777  1.00  6.66           O  
ATOM   1972  CB  PHE A 321     109.899 118.435  95.749  1.00  6.66           C  
ATOM   1973  CG  PHE A 321     109.770 118.758  94.291  1.00  6.66           C  
ATOM   1974  CD1 PHE A 321     110.774 119.441  93.630  1.00  6.66           C  
ATOM   1975  CD2 PHE A 321     108.651 118.371  93.577  1.00  6.66           C  
ATOM   1976  CE1 PHE A 321     110.661 119.735  92.288  1.00  6.66           C  
ATOM   1977  CE2 PHE A 321     108.533 118.666  92.237  1.00  6.66           C  
ATOM   1978  CZ  PHE A 321     109.539 119.349  91.592  1.00  6.66           C  
ATOM   1979  N   PRO A 322     111.422 118.128  98.539  1.00  8.26           N  
ATOM   1980  CA  PRO A 322     111.488 117.673  99.934  1.00  8.26           C  
ATOM   1981  C   PRO A 322     110.157 117.125 100.413  1.00  8.26           C  
ATOM   1982  O   PRO A 322     109.090 117.642 100.050  1.00  8.26           O  
ATOM   1983  CB  PRO A 322     111.876 118.945 100.704  1.00  8.26           C  
ATOM   1984  CG  PRO A 322     111.471 120.061  99.825  1.00  8.26           C  
ATOM   1985  CD  PRO A 322     111.683 119.571  98.429  1.00  8.26           C  
ATOM   1986  N   PRO A 323     110.181 116.070 101.231  1.00  9.85           N  
ATOM   1987  CA  PRO A 323     108.923 115.491 101.728  1.00  9.85           C  
ATOM   1988  C   PRO A 323     108.080 116.440 102.564  1.00  9.85           C  
ATOM   1989  O   PRO A 323     106.856 116.271 102.620  1.00  9.85           O  
ATOM   1990  CB  PRO A 323     109.403 114.293 102.561  1.00  9.85           C  
ATOM   1991  CG  PRO A 323     110.700 113.915 101.951  1.00  9.85           C  
ATOM   1992  CD  PRO A 323     111.336 115.219 101.550  1.00  9.85           C  
ATOM   1993  N   THR A 324     108.688 117.419 103.234  1.00 10.77           N  
ATOM   1994  CA  THR A 324     107.933 118.299 104.121  1.00 10.77           C  
ATOM   1995  C   THR A 324     107.027 119.267 103.375  1.00 10.77           C  
ATOM   1996  O   THR A 324     106.186 119.908 104.012  1.00 10.77           O  
ATOM   1997  CB  THR A 324     108.879 119.090 105.022  1.00 10.77           C  
ATOM   1998  OG1 THR A 324     109.883 119.728 104.226  1.00 10.77           O  
ATOM   1999  CG2 THR A 324     109.545 118.173 106.022  1.00 10.77           C  
ATOM   2000  N   SER A 325     107.177 119.396 102.059  1.00  8.99           N  
ATOM   2001  CA  SER A 325     106.348 120.306 101.281  1.00  8.99           C  
ATOM   2002  C   SER A 325     105.008 119.703 100.887  1.00  8.99           C  
ATOM   2003  O   SER A 325     104.148 120.429 100.383  1.00  8.99           O  
ATOM   2004  CB  SER A 325     107.100 120.753 100.026  1.00  8.99           C  
ATOM   2005  OG  SER A 325     107.321 119.668  99.143  1.00  8.99           O  
ATOM   2006  N   PHE A 326     104.806 118.412 101.105  1.00  7.41           N  
ATOM   2007  CA  PHE A 326     103.595 117.732 100.681  1.00  7.41           C  
ATOM   2008  C   PHE A 326     102.582 117.672 101.819  1.00  7.41           C  
ATOM   2009  O   PHE A 326     102.931 117.729 102.997  1.00  7.41           O  
ATOM   2010  CB  PHE A 326     103.937 116.326 100.196  1.00  7.41           C  
ATOM   2011  CG  PHE A 326     104.763 116.310  98.949  1.00  7.41           C  
ATOM   2012  CD1 PHE A 326     104.224 116.694  97.739  1.00  7.41           C  
ATOM   2013  CD2 PHE A 326     106.097 115.956  98.997  1.00  7.41           C  
ATOM   2014  CE1 PHE A 326     104.990 116.692  96.595  1.00  7.41           C  
ATOM   2015  CE2 PHE A 326     106.867 115.957  97.859  1.00  7.41           C  
ATOM   2016  CZ  PHE A 326     106.314 116.328  96.657  1.00  7.41           C  
ATOM   2017  N   GLY A 327     101.310 117.557 101.448  1.00 16.74           N  
ATOM   2018  CA  GLY A 327     100.251 117.418 102.416  1.00 16.74           C  
ATOM   2019  C   GLY A 327      99.380 118.648 102.553  1.00 16.74           C  
ATOM   2020  O   GLY A 327      99.350 119.520 101.682  1.00 16.74           O  
ATOM   2021  N   PRO A 328      98.640 118.728 103.659  1.00 12.95           N  
ATOM   2022  CA  PRO A 328      97.726 119.859 103.866  1.00 12.95           C  
ATOM   2023  C   PRO A 328      98.450 121.197 103.900  1.00 12.95           C  
ATOM   2024  O   PRO A 328      99.532 121.330 104.474  1.00 12.95           O  
ATOM   2025  CB  PRO A 328      97.077 119.546 105.219  1.00 12.95           C  
ATOM   2026  CG  PRO A 328      97.271 118.092 105.421  1.00 12.95           C  
ATOM   2027  CD  PRO A 328      98.563 117.750 104.753  1.00 12.95           C  
ATOM   2028  N   LEU A 329      97.831 122.197 103.285  1.00 13.87           N  
ATOM   2029  CA  LEU A 329      98.319 123.568 103.307  1.00 13.87           C  
ATOM   2030  C   LEU A 329      97.430 124.389 104.231  1.00 13.87           C  
ATOM   2031  O   LEU A 329      96.203 124.352 104.106  1.00 13.87           O  
ATOM   2032  CB  LEU A 329      98.324 124.157 101.898  1.00 13.87           C  
ATOM   2033  CG  LEU A 329      99.164 123.414 100.860  1.00 13.87           C  
ATOM   2034  CD1 LEU A 329      98.772 123.828  99.457  1.00 13.87           C  
ATOM   2035  CD2 LEU A 329     100.638 123.641 101.097  1.00 13.87           C  
ATOM   2036  N   VAL A 330      98.040 125.132 105.147  1.00 18.02           N  
ATOM   2037  CA  VAL A 330      97.296 125.726 106.250  1.00 18.02           C  
ATOM   2038  C   VAL A 330      97.408 127.243 106.214  1.00 18.02           C  
ATOM   2039  O   VAL A 330      98.354 127.814 105.663  1.00 18.02           O  
ATOM   2040  CB  VAL A 330      97.760 125.179 107.618  1.00 18.02           C  
ATOM   2041  CG1 VAL A 330      97.672 123.668 107.636  1.00 18.02           C  
ATOM   2042  CG2 VAL A 330      99.170 125.632 107.924  1.00 18.02           C  
ATOM   2043  N   ARG A 331      96.411 127.890 106.810  1.00 27.92           N  
ATOM   2044  CA  ARG A 331      96.282 129.337 106.834  1.00 27.92           C  
ATOM   2045  C   ARG A 331      95.676 129.743 108.171  1.00 27.92           C  
ATOM   2046  O   ARG A 331      94.978 128.958 108.816  1.00 27.92           O  
ATOM   2047  CB  ARG A 331      95.411 129.816 105.662  1.00 27.92           C  
ATOM   2048  CG  ARG A 331      95.071 131.291 105.640  1.00 27.92           C  
ATOM   2049  CD  ARG A 331      93.995 131.588 104.605  1.00 27.92           C  
ATOM   2050  NE  ARG A 331      94.286 131.010 103.297  1.00 27.92           N  
ATOM   2051  CZ  ARG A 331      95.257 131.425 102.489  1.00 27.92           C  
ATOM   2052  NH1 ARG A 331      96.034 132.439 102.842  1.00 27.92           N  
ATOM   2053  NH2 ARG A 331      95.440 130.833 101.317  1.00 27.92           N  
ATOM   2054  N   LYS A 332      95.959 130.973 108.593  1.00 40.80           N  
ATOM   2055  CA  LYS A 332      95.339 131.523 109.793  1.00 40.80           C  
ATOM   2056  C   LYS A 332      93.953 132.069 109.468  1.00 40.80           C  
ATOM   2057  O   LYS A 332      93.778 132.805 108.492  1.00 40.80           O  
ATOM   2058  CB  LYS A 332      96.211 132.624 110.393  1.00 40.80           C  
ATOM   2059  CG  LYS A 332      96.163 132.688 111.907  1.00 40.80           C  
ATOM   2060  CD  LYS A 332      97.334 133.475 112.472  1.00 40.80           C  
ATOM   2061  CE  LYS A 332      97.585 133.121 113.932  1.00 40.80           C  
ATOM   2062  NZ  LYS A 332      98.191 131.772 114.096  1.00 40.80           N  
ATOM   2063  N   ILE A 333      92.970 131.710 110.290  1.00 45.76           N  
ATOM   2064  CA  ILE A 333      91.593 132.151 110.112  1.00 45.76           C  
ATOM   2065  C   ILE A 333      91.082 132.682 111.444  1.00 45.76           C  
ATOM   2066  O   ILE A 333      91.564 132.294 112.513  1.00 45.76           O  
ATOM   2067  CB  ILE A 333      90.691 131.011 109.586  1.00 45.76           C  
ATOM   2068  CG1 ILE A 333      89.522 131.565 108.775  1.00 45.76           C  
ATOM   2069  CG2 ILE A 333      90.157 130.168 110.724  1.00 45.76           C  
ATOM   2070  CD1 ILE A 333      88.690 130.483 108.127  1.00 45.76           C  
ATOM   2071  N   PHE A 334      90.113 133.591 111.378  1.00 55.79           N  
ATOM   2072  CA  PHE A 334      89.515 134.190 112.565  1.00 55.79           C  
ATOM   2073  C   PHE A 334      88.049 133.800 112.683  1.00 55.79           C  
ATOM   2074  O   PHE A 334      87.264 134.019 111.755  1.00 55.79           O  
ATOM   2075  CB  PHE A 334      89.647 135.714 112.542  1.00 55.79           C  
ATOM   2076  CG  PHE A 334      91.059 136.196 112.419  1.00 55.79           C  
ATOM   2077  CD1 PHE A 334      91.996 135.870 113.384  1.00 55.79           C  
ATOM   2078  CD2 PHE A 334      91.449 136.982 111.351  1.00 55.79           C  
ATOM   2079  CE1 PHE A 334      93.297 136.311 113.284  1.00 55.79           C  
ATOM   2080  CE2 PHE A 334      92.752 137.427 111.243  1.00 55.79           C  
ATOM   2081  CZ  PHE A 334      93.677 137.091 112.212  1.00 55.79           C  
ATOM   2082  N   VAL A 335      87.689 133.229 113.829  1.00 58.91           N  
ATOM   2083  CA  VAL A 335      86.302 132.979 114.204  1.00 58.91           C  
ATOM   2084  C   VAL A 335      86.079 133.630 115.562  1.00 58.91           C  
ATOM   2085  O   VAL A 335      86.882 133.443 116.485  1.00 58.91           O  
ATOM   2086  CB  VAL A 335      85.970 131.478 114.231  1.00 58.91           C  
ATOM   2087  CG1 VAL A 335      86.932 130.728 115.132  1.00 58.91           C  
ATOM   2088  CG2 VAL A 335      84.534 131.263 114.684  1.00 58.91           C  
ATOM   2089  N   ASP A 336      85.016 134.429 115.672  1.00 62.06           N  
ATOM   2090  CA  ASP A 336      84.774 135.282 116.834  1.00 62.06           C  
ATOM   2091  C   ASP A 336      85.932 136.243 117.080  1.00 62.06           C  
ATOM   2092  O   ASP A 336      86.115 136.729 118.200  1.00 62.06           O  
ATOM   2093  CB  ASP A 336      84.507 134.455 118.101  1.00 62.06           C  
ATOM   2094  CG  ASP A 336      83.505 133.338 117.877  1.00 62.06           C  
ATOM   2095  OD1 ASP A 336      82.399 133.616 117.373  1.00 62.06           O  
ATOM   2096  OD2 ASP A 336      83.822 132.179 118.222  1.00 62.06           O  
ATOM   2097  N   GLY A 337      86.720 136.526 116.044  1.00 58.92           N  
ATOM   2098  CA  GLY A 337      87.962 137.250 116.199  1.00 58.92           C  
ATOM   2099  C   GLY A 337      89.102 136.436 116.766  1.00 58.92           C  
ATOM   2100  O   GLY A 337      90.197 136.979 116.948  1.00 58.92           O  
ATOM   2101  N   VAL A 338      88.882 135.155 117.046  1.00 56.79           N  
ATOM   2102  CA  VAL A 338      89.888 134.280 117.644  1.00 56.79           C  
ATOM   2103  C   VAL A 338      90.581 133.483 116.542  1.00 56.79           C  
ATOM   2104  O   VAL A 338      89.905 132.912 115.673  1.00 56.79           O  
ATOM   2105  CB  VAL A 338      89.249 133.364 118.701  1.00 56.79           C  
ATOM   2106  CG1 VAL A 338      90.173 132.230 119.053  1.00 56.79           C  
ATOM   2107  CG2 VAL A 338      88.893 134.165 119.943  1.00 56.79           C  
ATOM   2108  N   PRO A 339      91.914 133.416 116.533  1.00 53.08           N  
ATOM   2109  CA  PRO A 339      92.644 132.812 115.406  1.00 53.08           C  
ATOM   2110  C   PRO A 339      92.675 131.289 115.470  1.00 53.08           C  
ATOM   2111  O   PRO A 339      93.170 130.704 116.435  1.00 53.08           O  
ATOM   2112  CB  PRO A 339      94.051 133.407 115.540  1.00 53.08           C  
ATOM   2113  CG  PRO A 339      94.196 133.659 117.001  1.00 53.08           C  
ATOM   2114  CD  PRO A 339      92.827 134.071 117.486  1.00 53.08           C  
ATOM   2115  N   PHE A 340      92.146 130.649 114.429  1.00 46.14           N  
ATOM   2116  CA  PHE A 340      92.298 129.220 114.193  1.00 46.14           C  
ATOM   2117  C   PHE A 340      93.354 128.976 113.118  1.00 46.14           C  
ATOM   2118  O   PHE A 340      93.794 129.896 112.426  1.00 46.14           O  
ATOM   2119  CB  PHE A 340      90.979 128.579 113.746  1.00 46.14           C  
ATOM   2120  CG  PHE A 340      89.986 128.356 114.851  1.00 46.14           C  
ATOM   2121  CD1 PHE A 340      90.170 128.903 116.106  1.00 46.14           C  
ATOM   2122  CD2 PHE A 340      88.853 127.594 114.619  1.00 46.14           C  
ATOM   2123  CE1 PHE A 340      89.241 128.691 117.110  1.00 46.14           C  
ATOM   2124  CE2 PHE A 340      87.928 127.375 115.620  1.00 46.14           C  
ATOM   2125  CZ  PHE A 340      88.123 127.925 116.867  1.00 46.14           C  
ATOM   2126  N   VAL A 341      93.762 127.716 112.991  1.00 30.78           N  
ATOM   2127  CA  VAL A 341      94.587 127.253 111.879  1.00 30.78           C  
ATOM   2128  C   VAL A 341      93.782 126.216 111.107  1.00 30.78           C  
ATOM   2129  O   VAL A 341      93.424 125.167 111.654  1.00 30.78           O  
ATOM   2130  CB  VAL A 341      95.921 126.669 112.367  1.00 30.78           C  
ATOM   2131  CG1 VAL A 341      96.806 126.307 111.189  1.00 30.78           C  
ATOM   2132  CG2 VAL A 341      96.625 127.656 113.277  1.00 30.78           C  
ATOM   2133  N   VAL A 342      93.505 126.494 109.835  1.00 23.45           N  
ATOM   2134  CA  VAL A 342      92.661 125.624 109.024  1.00 23.45           C  
ATOM   2135  C   VAL A 342      93.354 125.311 107.707  1.00 23.45           C  
ATOM   2136  O   VAL A 342      94.170 126.090 107.206  1.00 23.45           O  
ATOM   2137  CB  VAL A 342      91.265 126.240 108.767  1.00 23.45           C  
ATOM   2138  CG1 VAL A 342      90.590 126.593 110.075  1.00 23.45           C  
ATOM   2139  CG2 VAL A 342      91.381 127.470 107.889  1.00 23.45           C  
ATOM   2140  N   SER A 343      93.028 124.146 107.153  1.00 17.49           N  
ATOM   2141  CA  SER A 343      93.566 123.745 105.863  1.00 17.49           C  
ATOM   2142  C   SER A 343      92.771 124.385 104.733  1.00 17.49           C  
ATOM   2143  O   SER A 343      91.556 124.199 104.630  1.00 17.49           O  
ATOM   2144  CB  SER A 343      93.540 122.224 105.732  1.00 17.49           C  
ATOM   2145  OG  SER A 343      93.748 121.824 104.390  1.00 17.49           O  
ATOM   2146  N   THR A 344      93.463 125.135 103.879  1.00 14.37           N  
ATOM   2147  CA  THR A 344      92.857 125.789 102.728  1.00 14.37           C  
ATOM   2148  C   THR A 344      93.283 125.163 101.410  1.00 14.37           C  
ATOM   2149  O   THR A 344      93.023 125.737 100.350  1.00 14.37           O  
ATOM   2150  CB  THR A 344      93.189 127.280 102.725  1.00 14.37           C  
ATOM   2151  OG1 THR A 344      94.573 127.463 102.403  1.00 14.37           O  
ATOM   2152  CG2 THR A 344      92.892 127.893 104.076  1.00 14.37           C  
ATOM   2153  N   GLY A 345      93.932 124.011 101.449  1.00  9.89           N  
ATOM   2154  CA  GLY A 345      94.402 123.383 100.235  1.00  9.89           C  
ATOM   2155  C   GLY A 345      95.205 122.148 100.565  1.00  9.89           C  
ATOM   2156  O   GLY A 345      95.320 121.741 101.723  1.00  9.89           O  
ATOM   2157  N   TYR A 346      95.751 121.546  99.514  1.00  7.92           N  
ATOM   2158  CA  TYR A 346      96.531 120.331  99.676  1.00  7.92           C  
ATOM   2159  C   TYR A 346      97.557 120.275  98.557  1.00  7.92           C  
ATOM   2160  O   TYR A 346      97.252 120.625  97.416  1.00  7.92           O  
ATOM   2161  CB  TYR A 346      95.630 119.092  99.640  1.00  7.92           C  
ATOM   2162  CG  TYR A 346      96.187 117.877 100.341  1.00  7.92           C  
ATOM   2163  CD1 TYR A 346      96.981 116.960  99.672  1.00  7.92           C  
ATOM   2164  CD2 TYR A 346      95.863 117.618 101.660  1.00  7.92           C  
ATOM   2165  CE1 TYR A 346      97.472 115.847 100.309  1.00  7.92           C  
ATOM   2166  CE2 TYR A 346      96.345 116.505 102.304  1.00  7.92           C  
ATOM   2167  CZ  TYR A 346      97.152 115.622 101.625  1.00  7.92           C  
ATOM   2168  OH  TYR A 346      97.636 114.510 102.266  1.00  7.92           O  
ATOM   2169  N   HIS A 347      98.771 119.852  98.887  1.00  7.60           N  
ATOM   2170  CA  HIS A 347      99.817 119.623  97.896  1.00  7.60           C  
ATOM   2171  C   HIS A 347      99.969 118.116  97.722  1.00  7.60           C  
ATOM   2172  O   HIS A 347     100.435 117.426  98.632  1.00  7.60           O  
ATOM   2173  CB  HIS A 347     101.133 120.268  98.328  1.00  7.60           C  
ATOM   2174  CG  HIS A 347     102.238 120.122  97.326  1.00  7.60           C  
ATOM   2175  ND1 HIS A 347     103.533 120.512  97.584  1.00  7.60           N  
ATOM   2176  CD2 HIS A 347     102.234 119.650  96.057  1.00  7.60           C  
ATOM   2177  CE1 HIS A 347     104.284 120.265  96.526  1.00  7.60           C  
ATOM   2178  NE2 HIS A 347     103.519 119.744  95.585  1.00  7.60           N  
ATOM   2179  N   PHE A 348      99.565 117.604  96.564  1.00  8.32           N  
ATOM   2180  CA  PHE A 348      99.635 116.178  96.283  1.00  8.32           C  
ATOM   2181  C   PHE A 348     100.916 115.859  95.528  1.00  8.32           C  
ATOM   2182  O   PHE A 348     101.359 116.638  94.681  1.00  8.32           O  
ATOM   2183  CB  PHE A 348      98.447 115.698  95.445  1.00  8.32           C  
ATOM   2184  CG  PHE A 348      97.120 115.779  96.140  1.00  8.32           C  
ATOM   2185  CD1 PHE A 348      96.432 116.976  96.212  1.00  8.32           C  
ATOM   2186  CD2 PHE A 348      96.562 114.658  96.727  1.00  8.32           C  
ATOM   2187  CE1 PHE A 348      95.207 117.049  96.837  1.00  8.32           C  
ATOM   2188  CE2 PHE A 348      95.342 114.730  97.364  1.00  8.32           C  
ATOM   2189  CZ  PHE A 348      94.665 115.927  97.419  1.00  8.32           C  
ATOM   2190  N   ARG A 349     101.510 114.708  95.837  1.00  8.99           N  
ATOM   2191  CA  ARG A 349     102.596 114.206  95.005  1.00  8.99           C  
ATOM   2192  C   ARG A 349     102.117 113.931  93.586  1.00  8.99           C  
ATOM   2193  O   ARG A 349     102.817 114.237  92.616  1.00  8.99           O  
ATOM   2194  CB  ARG A 349     103.201 112.948  95.625  1.00  8.99           C  
ATOM   2195  CG  ARG A 349     104.280 113.225  96.644  1.00  8.99           C  
ATOM   2196  CD  ARG A 349     104.348 112.140  97.687  1.00  8.99           C  
ATOM   2197  NE  ARG A 349     105.520 112.280  98.542  1.00  8.99           N  
ATOM   2198  CZ  ARG A 349     105.467 112.437  99.859  1.00  8.99           C  
ATOM   2199  NH1 ARG A 349     104.296 112.477 100.474  1.00  8.99           N  
ATOM   2200  NH2 ARG A 349     106.586 112.555 100.559  1.00  8.99           N  
ATOM   2201  N   GLU A 350     100.917 113.371  93.447  1.00 16.74           N  
ATOM   2202  CA  GLU A 350     100.398 112.974  92.147  1.00 16.74           C  
ATOM   2203  C   GLU A 350      99.522 114.035  91.491  1.00 16.74           C  
ATOM   2204  O   GLU A 350      99.539 114.158  90.263  1.00 16.74           O  
ATOM   2205  CB  GLU A 350      99.603 111.666  92.266  1.00 16.74           C  
ATOM   2206  CG  GLU A 350     100.289 110.528  93.028  1.00 16.74           C  
ATOM   2207  CD  GLU A 350     100.285 110.713  94.541  1.00 16.74           C  
ATOM   2208  OE1 GLU A 350     101.114 110.071  95.221  1.00 16.74           O  
ATOM   2209  OE2 GLU A 350      99.453 111.496  95.050  1.00 16.74           O  
ATOM   2210  N   LEU A 351      98.749 114.799  92.259  1.00 14.37           N  
ATOM   2211  CA  LEU A 351      97.800 115.742  91.680  1.00 14.37           C  
ATOM   2212  C   LEU A 351      98.255 117.195  91.741  1.00 14.37           C  
ATOM   2213  O   LEU A 351      97.532 118.070  91.260  1.00 14.37           O  
ATOM   2214  CB  LEU A 351      96.433 115.603  92.356  1.00 14.37           C  
ATOM   2215  CG  LEU A 351      95.869 114.190  92.496  1.00 14.37           C  
ATOM   2216  CD1 LEU A 351      94.601 114.210  93.326  1.00 14.37           C  
ATOM   2217  CD2 LEU A 351      95.612 113.567  91.137  1.00 14.37           C  
ATOM   2218  N   GLY A 352      99.426 117.478  92.305  1.00 16.74           N  
ATOM   2219  CA  GLY A 352      99.860 118.859  92.400  1.00 16.74           C  
ATOM   2220  C   GLY A 352      99.113 119.635  93.474  1.00 16.74           C  
ATOM   2221  O   GLY A 352      98.606 119.076  94.449  1.00 16.74           O  
ATOM   2222  N   VAL A 353      99.047 120.950  93.288  1.00 10.92           N  
ATOM   2223  CA  VAL A 353      98.475 121.863  94.275  1.00 10.92           C  
ATOM   2224  C   VAL A 353      96.986 122.045  94.010  1.00 10.92           C  
ATOM   2225  O   VAL A 353      96.575 122.366  92.890  1.00 10.92           O  
ATOM   2226  CB  VAL A 353      99.202 123.217  94.252  1.00 10.92           C  
ATOM   2227  CG1 VAL A 353      98.682 124.115  95.358  1.00 10.92           C  
ATOM   2228  CG2 VAL A 353     100.698 123.017  94.381  1.00 10.92           C  
ATOM   2229  N   VAL A 354      96.177 121.853  95.047  1.00  8.21           N  
ATOM   2230  CA  VAL A 354      94.735 122.069  94.996  1.00  8.21           C  
ATOM   2231  C   VAL A 354      94.375 123.073  96.083  1.00  8.21           C  
ATOM   2232  O   VAL A 354      94.802 122.921  97.232  1.00  8.21           O  
ATOM   2233  CB  VAL A 354      93.962 120.749  95.185  1.00  8.21           C  
ATOM   2234  CG1 VAL A 354      92.471 120.997  95.253  1.00  8.21           C  
ATOM   2235  CG2 VAL A 354      94.297 119.773  94.075  1.00  8.21           C  
ATOM   2236  N   HIS A 355      93.611 124.102  95.723  1.00  8.78           N  
ATOM   2237  CA  HIS A 355      93.130 125.095  96.677  1.00  8.78           C  
ATOM   2238  C   HIS A 355      91.626 124.978  96.874  1.00  8.78           C  
ATOM   2239  O   HIS A 355      90.883 124.714  95.925  1.00  8.78           O  
ATOM   2240  CB  HIS A 355      93.470 126.521  96.235  1.00  8.78           C  
ATOM   2241  CG  HIS A 355      94.931 126.837  96.264  1.00  8.78           C  
ATOM   2242  ND1 HIS A 355      95.606 127.340  95.174  1.00  8.78           N  
ATOM   2243  CD2 HIS A 355      95.842 126.748  97.262  1.00  8.78           C  
ATOM   2244  CE1 HIS A 355      96.872 127.531  95.494  1.00  8.78           C  
ATOM   2245  NE2 HIS A 355      97.042 127.181  96.755  1.00  8.78           N  
ATOM   2246  N   ASN A 356      91.187 125.180  98.113  1.00 10.48           N  
ATOM   2247  CA  ASN A 356      89.765 125.164  98.421  1.00 10.48           C  
ATOM   2248  C   ASN A 356      89.094 126.433  97.916  1.00 10.48           C  
ATOM   2249  O   ASN A 356      89.644 127.532  98.020  1.00 10.48           O  
ATOM   2250  CB  ASN A 356      89.543 125.018  99.924  1.00 10.48           C  
ATOM   2251  CG  ASN A 356      90.002 123.680 100.450  1.00 10.48           C  
ATOM   2252  OD1 ASN A 356      90.265 122.756  99.685  1.00 10.48           O  
ATOM   2253  ND2 ASN A 356      90.096 123.565 101.764  1.00 10.48           N  
ATOM   2254  N   GLN A 357      87.894 126.274  97.366  1.00 13.06           N  
ATOM   2255  CA  GLN A 357      87.159 127.395  96.799  1.00 13.06           C  
ATOM   2256  C   GLN A 357      86.349 128.164  97.835  1.00 13.06           C  
ATOM   2257  O   GLN A 357      86.191 129.382  97.703  1.00 13.06           O  
ATOM   2258  CB  GLN A 357      86.237 126.897  95.686  1.00 13.06           C  
ATOM   2259  CG  GLN A 357      86.921 125.957  94.713  1.00 13.06           C  
ATOM   2260  CD  GLN A 357      86.120 125.735  93.452  1.00 13.06           C  
ATOM   2261  OE1 GLN A 357      85.443 124.721  93.304  1.00 13.06           O  
ATOM   2262  NE2 GLN A 357      86.190 126.687  92.534  1.00 13.06           N  
ATOM   2263  N   ASP A 358      85.827 127.488  98.858  1.00 19.13           N  
ATOM   2264  CA  ASP A 358      85.018 128.133  99.893  1.00 19.13           C  
ATOM   2265  C   ASP A 358      85.883 128.366 101.128  1.00 19.13           C  
ATOM   2266  O   ASP A 358      85.903 127.578 102.074  1.00 19.13           O  
ATOM   2267  CB  ASP A 358      83.783 127.299 100.215  1.00 19.13           C  
ATOM   2268  CG  ASP A 358      83.053 126.835  98.973  1.00 19.13           C  
ATOM   2269  OD1 ASP A 358      83.069 127.567  97.963  1.00 19.13           O  
ATOM   2270  OD2 ASP A 358      82.455 125.740  99.007  1.00 19.13           O  
ATOM   2271  N   VAL A 359      86.616 129.476 101.106  1.00 28.78           N  
ATOM   2272  CA  VAL A 359      87.419 129.923 102.238  1.00 28.78           C  
ATOM   2273  C   VAL A 359      87.041 131.363 102.551  1.00 28.78           C  
ATOM   2274  O   VAL A 359      86.944 132.196 101.643  1.00 28.78           O  
ATOM   2275  CB  VAL A 359      88.930 129.799 101.958  1.00 28.78           C  
ATOM   2276  CG1 VAL A 359      89.363 128.348 102.043  1.00 28.78           C  
ATOM   2277  CG2 VAL A 359      89.268 130.366 100.591  1.00 28.78           C  
ATOM   2278  N   ASN A 360      86.817 131.653 103.831  1.00 50.52           N  
ATOM   2279  CA  ASN A 360      86.445 132.991 104.278  1.00 50.52           C  
ATOM   2280  C   ASN A 360      87.245 133.346 105.524  1.00 50.52           C  
ATOM   2281  O   ASN A 360      87.128 132.682 106.556  1.00 50.52           O  
ATOM   2282  CB  ASN A 360      84.932 133.093 104.523  1.00 50.52           C  
ATOM   2283  CG  ASN A 360      84.450 134.525 104.707  1.00 50.52           C  
ATOM   2284  OD1 ASN A 360      85.007 135.465 104.142  1.00 50.52           O  
ATOM   2285  ND2 ASN A 360      83.409 134.693 105.512  1.00 50.52           N  
ATOM   2286  N   LEU A 361      88.059 134.399 105.419  1.00 58.34           N  
ATOM   2287  CA  LEU A 361      89.045 134.689 106.456  1.00 58.34           C  
ATOM   2288  C   LEU A 361      88.399 135.126 107.765  1.00 58.34           C  
ATOM   2289  O   LEU A 361      88.985 134.931 108.835  1.00 58.34           O  
ATOM   2290  CB  LEU A 361      90.024 135.761 105.971  1.00 58.34           C  
ATOM   2291  CG  LEU A 361      90.846 135.497 104.703  1.00 58.34           C  
ATOM   2292  CD1 LEU A 361      90.068 135.823 103.434  1.00 58.34           C  
ATOM   2293  CD2 LEU A 361      92.148 136.278 104.744  1.00 58.34           C  
ATOM   2294  N   HIS A 362      87.206 135.712 107.709  1.00 62.12           N  
ATOM   2295  CA  HIS A 362      86.535 136.221 108.898  1.00 62.12           C  
ATOM   2296  C   HIS A 362      85.136 135.633 108.981  1.00 62.12           C  
ATOM   2297  O   HIS A 362      84.377 135.687 108.008  1.00 62.12           O  
ATOM   2298  CB  HIS A 362      86.471 137.752 108.884  1.00 62.12           C  
ATOM   2299  CG  HIS A 362      87.775 138.408 108.549  1.00 62.12           C  
ATOM   2300  ND1 HIS A 362      88.756 138.635 109.490  1.00 62.12           N  
ATOM   2301  CD2 HIS A 362      88.261 138.881 107.377  1.00 62.12           C  
ATOM   2302  CE1 HIS A 362      89.789 139.222 108.912  1.00 62.12           C  
ATOM   2303  NE2 HIS A 362      89.515 139.382 107.630  1.00 62.12           N  
ATOM   2304  N   SER A 363      84.796 135.084 110.145  1.00 64.04           N  
ATOM   2305  CA  SER A 363      83.504 134.453 110.367  1.00 64.04           C  
ATOM   2306  C   SER A 363      82.969 134.865 111.729  1.00 64.04           C  
ATOM   2307  O   SER A 363      83.734 135.023 112.684  1.00 64.04           O  
ATOM   2308  CB  SER A 363      83.606 132.925 110.283  1.00 64.04           C  
ATOM   2309  OG  SER A 363      83.981 132.369 111.530  1.00 64.04           O  
ATOM   2310  N   SER A 364      81.648 135.037 111.810  1.00 64.53           N  
ATOM   2311  CA  SER A 364      81.029 135.484 113.052  1.00 64.53           C  
ATOM   2312  C   SER A 364      80.747 134.325 114.002  1.00 64.53           C  
ATOM   2313  O   SER A 364      80.882 134.475 115.220  1.00 64.53           O  
ATOM   2314  CB  SER A 364      79.736 136.243 112.750  1.00 64.53           C  
ATOM   2315  OG  SER A 364      80.004 137.440 112.041  1.00 64.53           O  
ATOM   2316  N   ARG A 365      80.353 133.170 113.470  1.00 64.00           N  
ATOM   2317  CA  ARG A 365      79.953 132.049 114.308  1.00 64.00           C  
ATOM   2318  C   ARG A 365      80.211 130.773 113.516  1.00 64.00           C  
ATOM   2319  O   ARG A 365      80.239 130.786 112.284  1.00 64.00           O  
ATOM   2320  CB  ARG A 365      78.477 132.179 114.720  1.00 64.00           C  
ATOM   2321  CG  ARG A 365      77.914 131.086 115.624  1.00 64.00           C  
ATOM   2322  CD  ARG A 365      76.470 131.372 116.015  1.00 64.00           C  
ATOM   2323  NE  ARG A 365      75.568 131.344 114.868  1.00 64.00           N  
ATOM   2324  CZ  ARG A 365      75.042 130.234 114.362  1.00 64.00           C  
ATOM   2325  NH1 ARG A 365      74.232 130.301 113.314  1.00 64.00           N  
ATOM   2326  NH2 ARG A 365      75.330 129.056 114.899  1.00 64.00           N  
ATOM   2327  N   LEU A 366      80.398 129.670 114.237  1.00 51.05           N  
ATOM   2328  CA  LEU A 366      80.762 128.386 113.650  1.00 51.05           C  
ATOM   2329  C   LEU A 366      79.569 127.439 113.724  1.00 51.05           C  
ATOM   2330  O   LEU A 366      79.088 127.125 114.818  1.00 51.05           O  
ATOM   2331  CB  LEU A 366      81.968 127.791 114.375  1.00 51.05           C  
ATOM   2332  CG  LEU A 366      82.919 126.933 113.547  1.00 51.05           C  
ATOM   2333  CD1 LEU A 366      83.548 127.784 112.463  1.00 51.05           C  
ATOM   2334  CD2 LEU A 366      83.986 126.309 114.431  1.00 51.05           C  
ATOM   2335  N   SER A 367      79.100 126.981 112.566  1.00 44.65           N  
ATOM   2336  CA  SER A 367      77.985 126.048 112.524  1.00 44.65           C  
ATOM   2337  C   SER A 367      78.444 124.630 112.857  1.00 44.65           C  
ATOM   2338  O   SER A 367      79.635 124.352 113.018  1.00 44.65           O  
ATOM   2339  CB  SER A 367      77.314 126.066 111.151  1.00 44.65           C  
ATOM   2340  OG  SER A 367      76.455 124.953 110.993  1.00 44.65           O  
ATOM   2341  N   PHE A 368      77.466 123.728 112.973  1.00 41.45           N  
ATOM   2342  CA  PHE A 368      77.772 122.328 113.252  1.00 41.45           C  
ATOM   2343  C   PHE A 368      78.614 121.714 112.138  1.00 41.45           C  
ATOM   2344  O   PHE A 368      79.535 120.930 112.402  1.00 41.45           O  
ATOM   2345  CB  PHE A 368      76.475 121.542 113.447  1.00 41.45           C  
ATOM   2346  CG  PHE A 368      76.671 120.183 114.052  1.00 41.45           C  
ATOM   2347  CD1 PHE A 368      77.045 120.049 115.376  1.00 41.45           C  
ATOM   2348  CD2 PHE A 368      76.474 119.040 113.301  1.00 41.45           C  
ATOM   2349  CE1 PHE A 368      77.220 118.802 115.937  1.00 41.45           C  
ATOM   2350  CE2 PHE A 368      76.652 117.790 113.859  1.00 41.45           C  
ATOM   2351  CZ  PHE A 368      77.026 117.672 115.177  1.00 41.45           C  
ATOM   2352  N   LYS A 369      78.311 122.059 110.884  1.00 34.01           N  
ATOM   2353  CA  LYS A 369      79.082 121.542 109.758  1.00 34.01           C  
ATOM   2354  C   LYS A 369      80.532 122.012 109.804  1.00 34.01           C  
ATOM   2355  O   LYS A 369      81.456 121.220 109.580  1.00 34.01           O  
ATOM   2356  CB  LYS A 369      78.429 121.968 108.446  1.00 34.01           C  
ATOM   2357  CG  LYS A 369      78.932 121.223 107.236  1.00 34.01           C  
ATOM   2358  CD  LYS A 369      78.284 121.741 105.974  1.00 34.01           C  
ATOM   2359  CE  LYS A 369      79.112 122.856 105.364  1.00 34.01           C  
ATOM   2360  NZ  LYS A 369      80.563 122.532 105.393  1.00 34.01           N  
ATOM   2361  N   GLU A 370      80.759 123.293 110.104  1.00 40.39           N  
ATOM   2362  CA  GLU A 370      82.133 123.771 110.203  1.00 40.39           C  
ATOM   2363  C   GLU A 370      82.828 123.239 111.447  1.00 40.39           C  
ATOM   2364  O   GLU A 370      84.041 123.009 111.420  1.00 40.39           O  
ATOM   2365  CB  GLU A 370      82.181 125.299 110.177  1.00 40.39           C  
ATOM   2366  CG  GLU A 370      81.584 125.922 108.926  1.00 40.39           C  
ATOM   2367  CD  GLU A 370      80.893 127.245 109.190  1.00 40.39           C  
ATOM   2368  OE1 GLU A 370      79.738 127.235 109.655  1.00 40.39           O  
ATOM   2369  OE2 GLU A 370      81.509 128.299 108.929  1.00 40.39           O  
ATOM   2370  N   LEU A 371      82.082 123.022 112.530  1.00 38.00           N  
ATOM   2371  CA  LEU A 371      82.655 122.350 113.690  1.00 38.00           C  
ATOM   2372  C   LEU A 371      83.163 120.966 113.315  1.00 38.00           C  
ATOM   2373  O   LEU A 371      84.279 120.584 113.682  1.00 38.00           O  
ATOM   2374  CB  LEU A 371      81.612 122.253 114.802  1.00 38.00           C  
ATOM   2375  CG  LEU A 371      81.517 123.418 115.786  1.00 38.00           C  
ATOM   2376  CD1 LEU A 371      80.201 123.354 116.530  1.00 38.00           C  
ATOM   2377  CD2 LEU A 371      82.677 123.387 116.758  1.00 38.00           C  
ATOM   2378  N   LEU A 372      82.365 120.213 112.554  1.00 29.97           N  
ATOM   2379  CA  LEU A 372      82.774 118.883 112.114  1.00 29.97           C  
ATOM   2380  C   LEU A 372      83.989 118.957 111.193  1.00 29.97           C  
ATOM   2381  O   LEU A 372      84.948 118.186 111.343  1.00 29.97           O  
ATOM   2382  CB  LEU A 372      81.601 118.196 111.413  1.00 29.97           C  
ATOM   2383  CG  LEU A 372      81.589 116.673 111.305  1.00 29.97           C  
ATOM   2384  CD1 LEU A 372      81.282 116.044 112.651  1.00 29.97           C  
ATOM   2385  CD2 LEU A 372      80.585 116.226 110.262  1.00 29.97           C  
ATOM   2386  N   VAL A 373      83.971 119.895 110.243  1.00 26.30           N  
ATOM   2387  CA  VAL A 373      85.063 120.018 109.280  1.00 26.30           C  
ATOM   2388  C   VAL A 373      86.372 120.359 109.981  1.00 26.30           C  
ATOM   2389  O   VAL A 373      87.423 119.785 109.671  1.00 26.30           O  
ATOM   2390  CB  VAL A 373      84.708 121.060 108.203  1.00 26.30           C  
ATOM   2391  CG1 VAL A 373      85.945 121.472 107.429  1.00 26.30           C  
ATOM   2392  CG2 VAL A 373      83.661 120.501 107.258  1.00 26.30           C  
ATOM   2393  N   TYR A 374      86.338 121.290 110.936  1.00 31.05           N  
ATOM   2394  CA  TYR A 374      87.561 121.675 111.630  1.00 31.05           C  
ATOM   2395  C   TYR A 374      87.973 120.689 112.713  1.00 31.05           C  
ATOM   2396  O   TYR A 374      89.142 120.685 113.107  1.00 31.05           O  
ATOM   2397  CB  TYR A 374      87.422 123.078 112.224  1.00 31.05           C  
ATOM   2398  CG  TYR A 374      87.077 124.135 111.202  1.00 31.05           C  
ATOM   2399  CD1 TYR A 374      87.505 124.016 109.886  1.00 31.05           C  
ATOM   2400  CD2 TYR A 374      86.342 125.256 111.551  1.00 31.05           C  
ATOM   2401  CE1 TYR A 374      87.204 124.977 108.947  1.00 31.05           C  
ATOM   2402  CE2 TYR A 374      86.035 126.224 110.616  1.00 31.05           C  
ATOM   2403  CZ  TYR A 374      86.465 126.079 109.317  1.00 31.05           C  
ATOM   2404  OH  TYR A 374      86.161 127.040 108.384  1.00 31.05           O  
ATOM   2405  N   ALA A 375      87.056 119.855 113.204  1.00 26.12           N  
ATOM   2406  CA  ALA A 375      87.471 118.777 114.091  1.00 26.12           C  
ATOM   2407  C   ALA A 375      88.164 117.668 113.312  1.00 26.12           C  
ATOM   2408  O   ALA A 375      89.120 117.058 113.804  1.00 26.12           O  
ATOM   2409  CB  ALA A 375      86.266 118.231 114.854  1.00 26.12           C  
ATOM   2410  N   ALA A 376      87.694 117.390 112.094  1.00 20.98           N  
ATOM   2411  CA  ALA A 376      88.331 116.368 111.270  1.00 20.98           C  
ATOM   2412  C   ALA A 376      89.690 116.828 110.753  1.00 20.98           C  
ATOM   2413  O   ALA A 376      90.591 116.008 110.548  1.00 20.98           O  
ATOM   2414  CB  ALA A 376      87.419 115.988 110.107  1.00 20.98           C  
ATOM   2415  N   ASP A 377      89.845 118.126 110.524  1.00 21.17           N  
ATOM   2416  CA  ASP A 377      91.044 118.662 109.892  1.00 21.17           C  
ATOM   2417  C   ASP A 377      92.271 118.391 110.762  1.00 21.17           C  
ATOM   2418  O   ASP A 377      92.271 118.740 111.950  1.00 21.17           O  
ATOM   2419  CB  ASP A 377      90.850 120.164 109.665  1.00 21.17           C  
ATOM   2420  CG  ASP A 377      92.008 120.826 108.937  1.00 21.17           C  
ATOM   2421  OD1 ASP A 377      93.013 120.164 108.616  1.00 21.17           O  
ATOM   2422  OD2 ASP A 377      91.899 122.042 108.677  1.00 21.17           O  
ATOM   2423  N   PRO A 378      93.322 117.765 110.222  1.00 17.62           N  
ATOM   2424  CA  PRO A 378      94.532 117.530 111.025  1.00 17.62           C  
ATOM   2425  C   PRO A 378      95.312 118.787 111.367  1.00 17.62           C  
ATOM   2426  O   PRO A 378      96.252 118.700 112.165  1.00 17.62           O  
ATOM   2427  CB  PRO A 378      95.367 116.587 110.145  1.00 17.62           C  
ATOM   2428  CG  PRO A 378      94.841 116.755 108.775  1.00 17.62           C  
ATOM   2429  CD  PRO A 378      93.389 117.083 108.920  1.00 17.62           C  
ATOM   2430  N   ALA A 379      94.984 119.936 110.769  1.00 18.60           N  
ATOM   2431  CA  ALA A 379      95.759 121.154 110.995  1.00 18.60           C  
ATOM   2432  C   ALA A 379      95.847 121.499 112.476  1.00 18.60           C  
ATOM   2433  O   ALA A 379      96.935 121.744 113.006  1.00 18.60           O  
ATOM   2434  CB  ALA A 379      95.146 122.313 110.211  1.00 18.60           C  
ATOM   2435  N   MET A 380      94.705 121.508 113.164  1.00 28.32           N  
ATOM   2436  CA  MET A 380      94.676 121.879 114.576  1.00 28.32           C  
ATOM   2437  C   MET A 380      95.496 120.917 115.425  1.00 28.32           C  
ATOM   2438  O   MET A 380      96.307 121.344 116.260  1.00 28.32           O  
ATOM   2439  CB  MET A 380      93.225 121.896 115.057  1.00 28.32           C  
ATOM   2440  CG  MET A 380      92.297 122.848 114.319  1.00 28.32           C  
ATOM   2441  SD  MET A 380      92.687 124.593 114.531  1.00 28.32           S  
ATOM   2442  CE  MET A 380      93.329 124.596 116.198  1.00 28.32           C  
ATOM   2443  N   HIS A 381      95.316 119.616 115.203  1.00 21.84           N  
ATOM   2444  CA  HIS A 381      95.996 118.609 116.007  1.00 21.84           C  
ATOM   2445  C   HIS A 381      97.501 118.647 115.780  1.00 21.84           C  
ATOM   2446  O   HIS A 381      98.285 118.574 116.732  1.00 21.84           O  
ATOM   2447  CB  HIS A 381      95.426 117.230 115.681  1.00 21.84           C  
ATOM   2448  CG  HIS A 381      93.949 117.126 115.896  1.00 21.84           C  
ATOM   2449  ND1 HIS A 381      93.398 116.673 117.075  1.00 21.84           N  
ATOM   2450  CD2 HIS A 381      92.908 117.433 115.087  1.00 21.84           C  
ATOM   2451  CE1 HIS A 381      92.081 116.697 116.978  1.00 21.84           C  
ATOM   2452  NE2 HIS A 381      91.758 117.155 115.783  1.00 21.84           N  
ATOM   2453  N   ALA A 382      97.924 118.762 114.520  1.00 18.45           N  
ATOM   2454  CA  ALA A 382      99.351 118.807 114.220  1.00 18.45           C  
ATOM   2455  C   ALA A 382      99.983 120.099 114.722  1.00 18.45           C  
ATOM   2456  O   ALA A 382     101.134 120.094 115.173  1.00 18.45           O  
ATOM   2457  CB  ALA A 382      99.579 118.641 112.718  1.00 18.45           C  
ATOM   2458  N   ALA A 383      99.252 121.214 114.660  1.00 21.82           N  
ATOM   2459  CA  ALA A 383      99.802 122.481 115.123  1.00 21.82           C  
ATOM   2460  C   ALA A 383      99.888 122.546 116.642  1.00 21.82           C  
ATOM   2461  O   ALA A 383     100.747 123.254 117.177  1.00 21.82           O  
ATOM   2462  CB  ALA A 383      98.967 123.642 114.589  1.00 21.82           C  
ATOM   2463  N   SER A 384      99.021 121.828 117.354  1.00 23.48           N  
ATOM   2464  CA  SER A 384      99.064 121.858 118.811  1.00 23.48           C  
ATOM   2465  C   SER A 384      99.978 120.798 119.413  1.00 23.48           C  
ATOM   2466  O   SER A 384     100.203 120.817 120.627  1.00 23.48           O  
ATOM   2467  CB  SER A 384      97.654 121.694 119.389  1.00 23.48           C  
ATOM   2468  OG  SER A 384      97.309 120.327 119.518  1.00 23.48           O  
ATOM   2469  N   GLY A 385     100.508 119.880 118.604  1.00 22.13           N  
ATOM   2470  CA  GLY A 385     101.328 118.808 119.127  1.00 22.13           C  
ATOM   2471  C   GLY A 385     102.800 119.161 119.248  1.00 22.13           C  
ATOM   2472  O   GLY A 385     103.266 120.211 118.811  1.00 22.13           O  
ATOM   2473  N   ASN A 386     103.541 118.247 119.866  1.00 20.23           N  
ATOM   2474  CA  ASN A 386     104.988 118.348 119.952  1.00 20.23           C  
ATOM   2475  C   ASN A 386     105.639 117.754 118.708  1.00 20.23           C  
ATOM   2476  O   ASN A 386     105.053 116.934 118.000  1.00 20.23           O  
ATOM   2477  CB  ASN A 386     105.508 117.625 121.194  1.00 20.23           C  
ATOM   2478  CG  ASN A 386     105.163 118.345 122.477  1.00 20.23           C  
ATOM   2479  OD1 ASN A 386     104.920 119.551 122.481  1.00 20.23           O  
ATOM   2480  ND2 ASN A 386     105.137 117.608 123.578  1.00 20.23           N  
ATOM   2481  N   LEU A 387     106.869 118.180 118.445  1.00 17.42           N  
ATOM   2482  CA  LEU A 387     107.632 117.602 117.349  1.00 17.42           C  
ATOM   2483  C   LEU A 387     108.069 116.191 117.723  1.00 17.42           C  
ATOM   2484  O   LEU A 387     108.467 115.930 118.859  1.00 17.42           O  
ATOM   2485  CB  LEU A 387     108.845 118.476 117.033  1.00 17.42           C  
ATOM   2486  CG  LEU A 387     109.770 118.073 115.883  1.00 17.42           C  
ATOM   2487  CD1 LEU A 387     108.986 117.624 114.663  1.00 17.42           C  
ATOM   2488  CD2 LEU A 387     110.711 119.205 115.535  1.00 17.42           C  
ATOM   2489  N   LEU A 388     107.990 115.272 116.766  1.00 16.72           N  
ATOM   2490  CA  LEU A 388     108.280 113.869 117.017  1.00 16.72           C  
ATOM   2491  C   LEU A 388     109.409 113.386 116.117  1.00 16.72           C  
ATOM   2492  O   LEU A 388     109.420 113.661 114.915  1.00 16.72           O  
ATOM   2493  CB  LEU A 388     107.033 113.005 116.804  1.00 16.72           C  
ATOM   2494  CG  LEU A 388     107.236 111.491 116.834  1.00 16.72           C  
ATOM   2495  CD1 LEU A 388     107.485 111.008 118.248  1.00 16.72           C  
ATOM   2496  CD2 LEU A 388     106.045 110.783 116.225  1.00 16.72           C  
ATOM   2497  N   LEU A 389     110.357 112.662 116.712  1.00 19.10           N  
ATOM   2498  CA  LEU A 389     111.457 112.013 115.999  1.00 19.10           C  
ATOM   2499  C   LEU A 389     111.429 110.539 116.392  1.00 19.10           C  
ATOM   2500  O   LEU A 389     112.030 110.142 117.392  1.00 19.10           O  
ATOM   2501  CB  LEU A 389     112.793 112.664 116.331  1.00 19.10           C  
ATOM   2502  CG  LEU A 389     114.023 112.096 115.622  1.00 19.10           C  
ATOM   2503  CD1 LEU A 389     113.737 111.838 114.152  1.00 19.10           C  
ATOM   2504  CD2 LEU A 389     115.212 113.019 115.790  1.00 19.10           C  
ATOM   2505  N   ASP A 390     110.718 109.732 115.612  1.00 21.42           N  
ATOM   2506  CA  ASP A 390     110.545 108.315 115.909  1.00 21.42           C  
ATOM   2507  C   ASP A 390     111.549 107.517 115.082  1.00 21.42           C  
ATOM   2508  O   ASP A 390     111.427 107.433 113.856  1.00 21.42           O  
ATOM   2509  CB  ASP A 390     109.111 107.884 115.615  1.00 21.42           C  
ATOM   2510  CG  ASP A 390     108.846 106.438 115.976  1.00 21.42           C  
ATOM   2511  OD1 ASP A 390     109.713 105.806 116.610  1.00 21.42           O  
ATOM   2512  OD2 ASP A 390     107.754 105.936 115.640  1.00 21.42           O  
ATOM   2513  N   LYS A 391     112.545 106.938 115.752  1.00 22.28           N  
ATOM   2514  CA  LYS A 391     113.573 106.157 115.077  1.00 22.28           C  
ATOM   2515  C   LYS A 391     113.172 104.706 114.851  1.00 22.28           C  
ATOM   2516  O   LYS A 391     113.899 103.981 114.165  1.00 22.28           O  
ATOM   2517  CB  LYS A 391     114.879 106.201 115.877  1.00 22.28           C  
ATOM   2518  CG  LYS A 391     115.410 107.599 116.167  1.00 22.28           C  
ATOM   2519  CD  LYS A 391     115.661 108.417 114.908  1.00 22.28           C  
ATOM   2520  CE  LYS A 391     116.469 107.647 113.873  1.00 22.28           C  
ATOM   2521  NZ  LYS A 391     116.564 108.387 112.588  1.00 22.28           N  
ATOM   2522  N   ARG A 392     112.044 104.262 115.410  1.00 23.67           N  
ATOM   2523  CA  ARG A 392     111.624 102.878 115.221  1.00 23.67           C  
ATOM   2524  C   ARG A 392     111.191 102.611 113.788  1.00 23.67           C  
ATOM   2525  O   ARG A 392     111.315 101.480 113.307  1.00 23.67           O  
ATOM   2526  CB  ARG A 392     110.483 102.532 116.174  1.00 23.67           C  
ATOM   2527  CG  ARG A 392     110.860 102.538 117.638  1.00 23.67           C  
ATOM   2528  CD  ARG A 392     109.626 102.401 118.505  1.00 23.67           C  
ATOM   2529  NE  ARG A 392     108.581 103.339 118.115  1.00 23.67           N  
ATOM   2530  CZ  ARG A 392     107.403 103.435 118.718  1.00 23.67           C  
ATOM   2531  NH1 ARG A 392     107.119 102.651 119.745  1.00 23.67           N  
ATOM   2532  NH2 ARG A 392     106.510 104.315 118.297  1.00 23.67           N  
ATOM   2533  N   THR A 393     110.685 103.625 113.097  1.00 22.55           N  
ATOM   2534  CA  THR A 393     110.122 103.468 111.767  1.00 22.55           C  
ATOM   2535  C   THR A 393     110.861 104.346 110.768  1.00 22.55           C  
ATOM   2536  O   THR A 393     111.460 105.364 111.127  1.00 22.55           O  
ATOM   2537  CB  THR A 393     108.622 103.808 111.756  1.00 22.55           C  
ATOM   2538  OG1 THR A 393     108.042 103.398 110.513  1.00 22.55           O  
ATOM   2539  CG2 THR A 393     108.396 105.298 111.961  1.00 22.55           C  
ATOM   2540  N   THR A 394     110.833 103.921 109.508  1.00 23.57           N  
ATOM   2541  CA  THR A 394     111.383 104.706 108.413  1.00 23.57           C  
ATOM   2542  C   THR A 394     110.394 105.724 107.867  1.00 23.57           C  
ATOM   2543  O   THR A 394     110.750 106.484 106.961  1.00 23.57           O  
ATOM   2544  CB  THR A 394     111.848 103.786 107.280  1.00 23.57           C  
ATOM   2545  OG1 THR A 394     110.793 102.882 106.928  1.00 23.57           O  
ATOM   2546  CG2 THR A 394     113.066 102.987 107.708  1.00 23.57           C  
ATOM   2547  N   CYS A 395     109.168 105.747 108.378  1.00 20.21           N  
ATOM   2548  CA  CYS A 395     108.133 106.635 107.877  1.00 20.21           C  
ATOM   2549  C   CYS A 395     108.271 108.034 108.471  1.00 20.21           C  
ATOM   2550  O   CYS A 395     108.879 108.239 109.524  1.00 20.21           O  
ATOM   2551  CB  CYS A 395     106.747 106.069 108.179  1.00 20.21           C  
ATOM   2552  SG  CYS A 395     106.383 104.526 107.311  1.00 20.21           S  
ATOM   2553  N   PHE A 396     107.688 109.000 107.770  1.00 14.57           N  
ATOM   2554  CA  PHE A 396     107.791 110.405 108.138  1.00 14.57           C  
ATOM   2555  C   PHE A 396     106.851 110.708 109.298  1.00 14.57           C  
ATOM   2556  O   PHE A 396     105.636 110.526 109.184  1.00 14.57           O  
ATOM   2557  CB  PHE A 396     107.472 111.274 106.922  1.00 14.57           C  
ATOM   2558  CG  PHE A 396     107.629 112.747 107.158  1.00 14.57           C  
ATOM   2559  CD1 PHE A 396     108.838 113.373 106.921  1.00 14.57           C  
ATOM   2560  CD2 PHE A 396     106.557 113.513 107.580  1.00 14.57           C  
ATOM   2561  CE1 PHE A 396     108.979 114.730 107.127  1.00 14.57           C  
ATOM   2562  CE2 PHE A 396     106.693 114.867 107.788  1.00 14.57           C  
ATOM   2563  CZ  PHE A 396     107.905 115.477 107.561  1.00 14.57           C  
ATOM   2564  N   SER A 397     107.413 111.173 110.410  1.00 14.87           N  
ATOM   2565  CA  SER A 397     106.635 111.537 111.585  1.00 14.87           C  
ATOM   2566  C   SER A 397     106.192 112.988 111.488  1.00 14.87           C  
ATOM   2567  O   SER A 397     106.935 113.844 111.001  1.00 14.87           O  
ATOM   2568  CB  SER A 397     107.450 111.331 112.861  1.00 14.87           C  
ATOM   2569  OG  SER A 397     107.959 110.013 112.937  1.00 14.87           O  
ATOM   2570  N   VAL A 398     104.977 113.263 111.953  1.00 13.21           N  
ATOM   2571  CA  VAL A 398     104.442 114.617 111.897  1.00 13.21           C  
ATOM   2572  C   VAL A 398     104.546 115.267 113.268  1.00 13.21           C  
ATOM   2573  O   VAL A 398     105.286 116.238 113.451  1.00 13.21           O  
ATOM   2574  CB  VAL A 398     102.985 114.627 111.406  1.00 13.21           C  
ATOM   2575  CG1 VAL A 398     102.416 116.032 111.476  1.00 13.21           C  
ATOM   2576  CG2 VAL A 398     102.898 114.080 110.003  1.00 13.21           C  
ATOM   2577  N   ALA A 399     103.815 114.730 114.240  1.00 14.93           N  
ATOM   2578  CA  ALA A 399     103.771 115.329 115.564  1.00 14.93           C  
ATOM   2579  C   ALA A 399     103.338 114.278 116.572  1.00 14.93           C  
ATOM   2580  O   ALA A 399     102.704 113.281 116.223  1.00 14.93           O  
ATOM   2581  CB  ALA A 399     102.823 116.531 115.603  1.00 14.93           C  
ATOM   2582  N   ALA A 400     103.698 114.514 117.828  1.00 17.97           N  
ATOM   2583  CA  ALA A 400     103.217 113.714 118.944  1.00 17.97           C  
ATOM   2584  C   ALA A 400     102.100 114.481 119.639  1.00 17.97           C  
ATOM   2585  O   ALA A 400     102.324 115.580 120.154  1.00 17.97           O  
ATOM   2586  CB  ALA A 400     104.350 113.398 119.919  1.00 17.97           C  
ATOM   2587  N   LEU A 401     100.900 113.902 119.652  1.00 22.89           N  
ATOM   2588  CA  LEU A 401      99.753 114.566 120.256  1.00 22.89           C  
ATOM   2589  C   LEU A 401      99.665 114.344 121.757  1.00 22.89           C  
ATOM   2590  O   LEU A 401      98.854 115.001 122.416  1.00 22.89           O  
ATOM   2591  CB  LEU A 401      98.457 114.090 119.594  1.00 22.89           C  
ATOM   2592  CG  LEU A 401      98.305 114.297 118.086  1.00 22.89           C  
ATOM   2593  CD1 LEU A 401      96.838 114.313 117.708  1.00 22.89           C  
ATOM   2594  CD2 LEU A 401      98.987 115.574 117.626  1.00 22.89           C  
ATOM   2595  N   THR A 402     100.473 113.444 122.307  1.00 30.56           N  
ATOM   2596  CA  THR A 402     100.433 113.100 123.717  1.00 30.56           C  
ATOM   2597  C   THR A 402     101.859 113.084 124.253  1.00 30.56           C  
ATOM   2598  O   THR A 402     102.807 112.790 123.522  1.00 30.56           O  
ATOM   2599  CB  THR A 402      99.743 111.730 123.919  1.00 30.56           C  
ATOM   2600  OG1 THR A 402      98.352 111.846 123.600  1.00 30.56           O  
ATOM   2601  CG2 THR A 402      99.868 111.240 125.355  1.00 30.56           C  
ATOM   2602  N   ASN A 403     102.007 113.414 125.538  1.00 36.01           N  
ATOM   2603  CA  ASN A 403     103.320 113.412 126.171  1.00 36.01           C  
ATOM   2604  C   ASN A 403     103.900 112.014 126.343  1.00 36.01           C  
ATOM   2605  O   ASN A 403     105.080 111.896 126.691  1.00 36.01           O  
ATOM   2606  CB  ASN A 403     103.246 114.098 127.536  1.00 36.01           C  
ATOM   2607  CG  ASN A 403     102.702 115.507 127.451  1.00 36.01           C  
ATOM   2608  OD1 ASN A 403     102.428 116.015 126.364  1.00 36.01           O  
ATOM   2609  ND2 ASN A 403     102.541 116.150 128.601  1.00 36.01           N  
ATOM   2610  N   ASN A 404     103.115 110.961 126.120  1.00 34.65           N  
ATOM   2611  CA  ASN A 404     103.559 109.595 126.354  1.00 34.65           C  
ATOM   2612  C   ASN A 404     103.215 108.714 125.163  1.00 34.65           C  
ATOM   2613  O   ASN A 404     102.109 108.789 124.622  1.00 34.65           O  
ATOM   2614  CB  ASN A 404     102.923 109.016 127.622  1.00 34.65           C  
ATOM   2615  CG  ASN A 404     103.474 109.640 128.887  1.00 34.65           C  
ATOM   2616  OD1 ASN A 404     104.582 110.176 128.898  1.00 34.65           O  
ATOM   2617  ND2 ASN A 404     102.701 109.573 129.964  1.00 34.65           N  
ATOM   2618  N   VAL A 405     104.172 107.874 124.767  1.00 26.94           N  
ATOM   2619  CA  VAL A 405     103.953 106.916 123.691  1.00 26.94           C  
ATOM   2620  C   VAL A 405     103.136 105.737 124.208  1.00 26.94           C  
ATOM   2621  O   VAL A 405     103.264 105.331 125.370  1.00 26.94           O  
ATOM   2622  CB  VAL A 405     105.304 106.457 123.115  1.00 26.94           C  
ATOM   2623  CG1 VAL A 405     105.107 105.551 121.913  1.00 26.94           C  
ATOM   2624  CG2 VAL A 405     106.145 107.658 122.738  1.00 26.94           C  
ATOM   2625  N   ALA A 406     102.279 105.190 123.348  1.00 25.10           N  
ATOM   2626  CA  ALA A 406     101.440 104.048 123.685  1.00 25.10           C  
ATOM   2627  C   ALA A 406     102.044 102.762 123.132  1.00 25.10           C  
ATOM   2628  O   ALA A 406     102.529 102.727 121.998  1.00 25.10           O  
ATOM   2629  CB  ALA A 406     100.024 104.232 123.141  1.00 25.10           C  
ATOM   2630  N   PHE A 407     102.000 101.701 123.941  1.00 26.61           N  
ATOM   2631  CA  PHE A 407     102.637 100.420 123.629  1.00 26.61           C  
ATOM   2632  C   PHE A 407     101.625  99.280 123.772  1.00 26.61           C  
ATOM   2633  O   PHE A 407     101.870  98.290 124.460  1.00 26.61           O  
ATOM   2634  CB  PHE A 407     103.854 100.172 124.517  1.00 26.61           C  
ATOM   2635  CG  PHE A 407     104.890 101.256 124.447  1.00 26.61           C  
ATOM   2636  CD1 PHE A 407     105.782 101.308 123.393  1.00 26.61           C  
ATOM   2637  CD2 PHE A 407     104.978 102.214 125.441  1.00 26.61           C  
ATOM   2638  CE1 PHE A 407     106.735 102.298 123.327  1.00 26.61           C  
ATOM   2639  CE2 PHE A 407     105.930 103.205 125.380  1.00 26.61           C  
ATOM   2640  CZ  PHE A 407     106.810 103.247 124.322  1.00 26.61           C  
ATOM   2641  N   GLN A 408     100.467  99.436 123.134  1.00 30.96           N  
ATOM   2642  CA  GLN A 408      99.378  98.477 123.286  1.00 30.96           C  
ATOM   2643  C   GLN A 408      99.792  97.078 122.831  1.00 30.96           C  
ATOM   2644  O   GLN A 408     100.454  96.909 121.803  1.00 30.96           O  
ATOM   2645  CB  GLN A 408      98.146  98.956 122.515  1.00 30.96           C  
ATOM   2646  CG  GLN A 408      98.137  98.632 121.027  1.00 30.96           C  
ATOM   2647  CD  GLN A 408      96.762  98.773 120.408  1.00 30.96           C  
ATOM   2648  OE1 GLN A 408      95.816  98.098 120.808  1.00 30.96           O  
ATOM   2649  NE2 GLN A 408      96.646  99.655 119.424  1.00 30.96           N  
ATOM   2650  N   THR A 409      99.425  96.079 123.629  1.00 30.45           N  
ATOM   2651  CA  THR A 409      99.761  94.684 123.394  1.00 30.45           C  
ATOM   2652  C   THR A 409      98.550  93.914 122.865  1.00 30.45           C  
ATOM   2653  O   THR A 409      97.434  94.430 122.787  1.00 30.45           O  
ATOM   2654  CB  THR A 409     100.275  94.043 124.682  1.00 30.45           C  
ATOM   2655  OG1 THR A 409      99.346  94.293 125.742  1.00 30.45           O  
ATOM   2656  CG2 THR A 409     101.619  94.631 125.067  1.00 30.45           C  
ATOM   2657  N   VAL A 410      98.784  92.656 122.493  1.00 27.90           N  
ATOM   2658  CA  VAL A 410      97.726  91.740 122.079  1.00 27.90           C  
ATOM   2659  C   VAL A 410      97.703  90.564 123.044  1.00 27.90           C  
ATOM   2660  O   VAL A 410      98.741  89.945 123.303  1.00 27.90           O  
ATOM   2661  CB  VAL A 410      97.914  91.251 120.631  1.00 27.90           C  
ATOM   2662  CG1 VAL A 410      96.866  90.209 120.286  1.00 27.90           C  
ATOM   2663  CG2 VAL A 410      97.822  92.407 119.667  1.00 27.90           C  
ATOM   2664  N   LYS A 411      96.520  90.262 123.572  1.00 29.02           N  
ATOM   2665  CA  LYS A 411      96.359  89.179 124.522  1.00 29.02           C  
ATOM   2666  C   LYS A 411      96.375  87.823 123.818  1.00 29.02           C  
ATOM   2667  O   LYS A 411      96.083  87.724 122.625  1.00 29.02           O  
ATOM   2668  CB  LYS A 411      95.050  89.345 125.286  1.00 29.02           C  
ATOM   2669  CG  LYS A 411      95.081  90.419 126.352  1.00 29.02           C  
ATOM   2670  CD  LYS A 411      93.762  90.476 127.098  1.00 29.02           C  
ATOM   2671  CE  LYS A 411      93.100  91.830 126.935  1.00 29.02           C  
ATOM   2672  NZ  LYS A 411      92.328  92.221 128.146  1.00 29.02           N  
ATOM   2673  N   PRO A 412      96.730  86.762 124.539  1.00 29.60           N  
ATOM   2674  CA  PRO A 412      96.494  85.414 124.025  1.00 29.60           C  
ATOM   2675  C   PRO A 412      95.022  85.044 124.121  1.00 29.60           C  
ATOM   2676  O   PRO A 412      94.243  85.649 124.860  1.00 29.60           O  
ATOM   2677  CB  PRO A 412      97.350  84.536 124.939  1.00 29.60           C  
ATOM   2678  CG  PRO A 412      97.323  85.260 126.233  1.00 29.60           C  
ATOM   2679  CD  PRO A 412      97.353  86.729 125.873  1.00 29.60           C  
ATOM   2680  N   GLY A 413      94.646  84.028 123.354  1.00 32.66           N  
ATOM   2681  CA  GLY A 413      93.269  83.596 123.331  1.00 32.66           C  
ATOM   2682  C   GLY A 413      92.905  82.697 124.496  1.00 32.66           C  
ATOM   2683  O   GLY A 413      93.754  82.098 125.151  1.00 32.66           O  
ATOM   2684  N   ASN A 414      91.605  82.617 124.754  1.00 33.65           N  
ATOM   2685  CA  ASN A 414      91.087  81.756 125.804  1.00 33.65           C  
ATOM   2686  C   ASN A 414      90.895  80.342 125.276  1.00 33.65           C  
ATOM   2687  O   ASN A 414      90.690  80.126 124.079  1.00 33.65           O  
ATOM   2688  CB  ASN A 414      89.767  82.304 126.338  1.00 33.65           C  
ATOM   2689  CG  ASN A 414      89.830  83.789 126.608  1.00 33.65           C  
ATOM   2690  OD1 ASN A 414      90.905  84.348 126.817  1.00 33.65           O  
ATOM   2691  ND2 ASN A 414      88.679  84.441 126.590  1.00 33.65           N  
ATOM   2692  N   PHE A 415      90.968  79.373 126.181  1.00 32.51           N  
ATOM   2693  CA  PHE A 415      90.946  77.963 125.821  1.00 32.51           C  
ATOM   2694  C   PHE A 415      89.629  77.333 126.254  1.00 32.51           C  
ATOM   2695  O   PHE A 415      89.194  77.511 127.397  1.00 32.51           O  
ATOM   2696  CB  PHE A 415      92.134  77.237 126.451  1.00 32.51           C  
ATOM   2697  CG  PHE A 415      92.239  75.797 126.062  1.00 32.51           C  
ATOM   2698  CD1 PHE A 415      92.387  75.437 124.737  1.00 32.51           C  
ATOM   2699  CD2 PHE A 415      92.234  74.805 127.023  1.00 32.51           C  
ATOM   2700  CE1 PHE A 415      92.492  74.115 124.374  1.00 32.51           C  
ATOM   2701  CE2 PHE A 415      92.346  73.480 126.664  1.00 32.51           C  
ATOM   2702  CZ  PHE A 415      92.475  73.136 125.339  1.00 32.51           C  
ATOM   2703  N   ASN A 416      88.995  76.611 125.333  1.00 34.34           N  
ATOM   2704  CA  ASN A 416      87.736  75.913 125.595  1.00 34.34           C  
ATOM   2705  C   ASN A 416      88.019  74.441 125.898  1.00 34.34           C  
ATOM   2706  O   ASN A 416      87.810  73.551 125.075  1.00 34.34           O  
ATOM   2707  CB  ASN A 416      86.787  76.074 124.412  1.00 34.34           C  
ATOM   2708  CG  ASN A 416      85.332  75.905 124.801  1.00 34.34           C  
ATOM   2709  OD1 ASN A 416      84.979  75.969 125.976  1.00 34.34           O  
ATOM   2710  ND2 ASN A 416      84.477  75.696 123.809  1.00 34.34           N  
ATOM   2711  N   LYS A 417      88.527  74.202 127.110  1.00 35.00           N  
ATOM   2712  CA  LYS A 417      88.916  72.847 127.494  1.00 35.00           C  
ATOM   2713  C   LYS A 417      87.728  71.895 127.526  1.00 35.00           C  
ATOM   2714  O   LYS A 417      87.908  70.681 127.378  1.00 35.00           O  
ATOM   2715  CB  LYS A 417      89.617  72.858 128.852  1.00 35.00           C  
ATOM   2716  CG  LYS A 417      90.543  71.671 129.064  1.00 35.00           C  
ATOM   2717  CD  LYS A 417      90.789  71.401 130.535  1.00 35.00           C  
ATOM   2718  CE  LYS A 417      91.736  70.229 130.719  1.00 35.00           C  
ATOM   2719  NZ  LYS A 417      93.157  70.661 130.836  1.00 35.00           N  
ATOM   2720  N   ASP A 418      86.514  72.414 127.725  1.00 39.08           N  
ATOM   2721  CA  ASP A 418      85.332  71.557 127.686  1.00 39.08           C  
ATOM   2722  C   ASP A 418      85.186  70.883 126.328  1.00 39.08           C  
ATOM   2723  O   ASP A 418      84.844  69.698 126.245  1.00 39.08           O  
ATOM   2724  CB  ASP A 418      84.079  72.368 128.009  1.00 39.08           C  
ATOM   2725  CG  ASP A 418      84.251  73.247 129.226  1.00 39.08           C  
ATOM   2726  OD1 ASP A 418      84.289  72.706 130.350  1.00 39.08           O  
ATOM   2727  OD2 ASP A 418      84.348  74.481 129.060  1.00 39.08           O  
ATOM   2728  N   PHE A 419      85.443  71.626 125.252  1.00 33.58           N  
ATOM   2729  CA  PHE A 419      85.369  71.062 123.910  1.00 33.58           C  
ATOM   2730  C   PHE A 419      86.594  70.207 123.595  1.00 33.58           C  
ATOM   2731  O   PHE A 419      86.489  69.200 122.887  1.00 33.58           O  
ATOM   2732  CB  PHE A 419      85.211  72.190 122.888  1.00 33.58           C  
ATOM   2733  CG  PHE A 419      85.275  71.735 121.461  1.00 33.58           C  
ATOM   2734  CD1 PHE A 419      84.171  71.170 120.853  1.00 33.58           C  
ATOM   2735  CD2 PHE A 419      86.439  71.873 120.727  1.00 33.58           C  
ATOM   2736  CE1 PHE A 419      84.226  70.751 119.544  1.00 33.58           C  
ATOM   2737  CE2 PHE A 419      86.501  71.454 119.417  1.00 33.58           C  
ATOM   2738  CZ  PHE A 419      85.393  70.894 118.824  1.00 33.58           C  
ATOM   2739  N   TYR A 420      87.765  70.600 124.102  1.00 38.91           N  
ATOM   2740  CA  TYR A 420      88.977  69.828 123.848  1.00 38.91           C  
ATOM   2741  C   TYR A 420      88.905  68.446 124.484  1.00 38.91           C  
ATOM   2742  O   TYR A 420      89.330  67.456 123.877  1.00 38.91           O  
ATOM   2743  CB  TYR A 420      90.199  70.592 124.357  1.00 38.91           C  
ATOM   2744  CG  TYR A 420      91.510  69.905 124.064  1.00 38.91           C  
ATOM   2745  CD1 TYR A 420      92.102  69.995 122.815  1.00 38.91           C  
ATOM   2746  CD2 TYR A 420      92.162  69.173 125.045  1.00 38.91           C  
ATOM   2747  CE1 TYR A 420      93.300  69.367 122.548  1.00 38.91           C  
ATOM   2748  CE2 TYR A 420      93.361  68.544 124.789  1.00 38.91           C  
ATOM   2749  CZ  TYR A 420      93.926  68.644 123.539  1.00 38.91           C  
ATOM   2750  OH  TYR A 420      95.121  68.017 123.279  1.00 38.91           O  
ATOM   2751  N   ASP A 421      88.388  68.358 125.712  1.00 39.34           N  
ATOM   2752  CA  ASP A 421      88.227  67.056 126.352  1.00 39.34           C  
ATOM   2753  C   ASP A 421      87.288  66.169 125.548  1.00 39.34           C  
ATOM   2754  O   ASP A 421      87.543  64.971 125.376  1.00 39.34           O  
ATOM   2755  CB  ASP A 421      87.709  67.233 127.777  1.00 39.34           C  
ATOM   2756  CG  ASP A 421      88.719  67.902 128.685  1.00 39.34           C  
ATOM   2757  OD1 ASP A 421      89.927  67.854 128.371  1.00 39.34           O  
ATOM   2758  OD2 ASP A 421      88.304  68.480 129.710  1.00 39.34           O  
ATOM   2759  N   PHE A 422      86.200  66.748 125.043  1.00 37.79           N  
ATOM   2760  CA  PHE A 422      85.270  66.006 124.202  1.00 37.79           C  
ATOM   2761  C   PHE A 422      85.958  65.506 122.938  1.00 37.79           C  
ATOM   2762  O   PHE A 422      85.780  64.350 122.537  1.00 37.79           O  
ATOM   2763  CB  PHE A 422      84.079  66.900 123.854  1.00 37.79           C  
ATOM   2764  CG  PHE A 422      82.912  66.165 123.270  1.00 37.79           C  
ATOM   2765  CD1 PHE A 422      82.273  65.170 123.984  1.00 37.79           C  
ATOM   2766  CD2 PHE A 422      82.448  66.477 122.006  1.00 37.79           C  
ATOM   2767  CE1 PHE A 422      81.195  64.500 123.447  1.00 37.79           C  
ATOM   2768  CE2 PHE A 422      81.374  65.808 121.465  1.00 37.79           C  
ATOM   2769  CZ  PHE A 422      80.748  64.818 122.186  1.00 37.79           C  
ATOM   2770  N   ALA A 423      86.751  66.367 122.298  1.00 38.65           N  
ATOM   2771  CA  ALA A 423      87.429  65.977 121.064  1.00 38.65           C  
ATOM   2772  C   ALA A 423      88.434  64.857 121.304  1.00 38.65           C  
ATOM   2773  O   ALA A 423      88.518  63.911 120.514  1.00 38.65           O  
ATOM   2774  CB  ALA A 423      88.115  67.189 120.438  1.00 38.65           C  
ATOM   2775  N   VAL A 424      89.212  64.949 122.385  1.00 40.42           N  
ATOM   2776  CA  VAL A 424      90.189  63.905 122.684  1.00 40.42           C  
ATOM   2777  C   VAL A 424      89.489  62.604 123.058  1.00 40.42           C  
ATOM   2778  O   VAL A 424      89.969  61.512 122.732  1.00 40.42           O  
ATOM   2779  CB  VAL A 424      91.161  64.366 123.784  1.00 40.42           C  
ATOM   2780  CG1 VAL A 424      92.238  63.322 124.006  1.00 40.42           C  
ATOM   2781  CG2 VAL A 424      91.806  65.674 123.388  1.00 40.42           C  
ATOM   2782  N   SER A 425      88.351  62.694 123.751  1.00 41.98           N  
ATOM   2783  CA  SER A 425      87.594  61.491 124.080  1.00 41.98           C  
ATOM   2784  C   SER A 425      87.158  60.749 122.823  1.00 41.98           C  
ATOM   2785  O   SER A 425      87.169  59.514 122.787  1.00 41.98           O  
ATOM   2786  CB  SER A 425      86.382  61.852 124.937  1.00 41.98           C  
ATOM   2787  OG  SER A 425      86.770  62.591 126.081  1.00 41.98           O  
ATOM   2788  N   LYS A 426      86.772  61.483 121.781  1.00 42.53           N  
ATOM   2789  CA  LYS A 426      86.313  60.876 120.539  1.00 42.53           C  
ATOM   2790  C   LYS A 426      87.448  60.457 119.614  1.00 42.53           C  
ATOM   2791  O   LYS A 426      87.176  60.006 118.497  1.00 42.53           O  
ATOM   2792  CB  LYS A 426      85.367  61.831 119.807  1.00 42.53           C  
ATOM   2793  CG  LYS A 426      83.980  61.894 120.425  1.00 42.53           C  
ATOM   2794  CD  LYS A 426      83.546  60.519 120.910  1.00 42.53           C  
ATOM   2795  CE  LYS A 426      82.268  60.582 121.723  1.00 42.53           C  
ATOM   2796  NZ  LYS A 426      82.317  61.661 122.741  1.00 42.53           N  
ATOM   2797  N   GLY A 427      88.701  60.592 120.036  1.00 41.44           N  
ATOM   2798  CA  GLY A 427      89.816  60.029 119.305  1.00 41.44           C  
ATOM   2799  C   GLY A 427      90.579  60.959 118.388  1.00 41.44           C  
ATOM   2800  O   GLY A 427      91.375  60.475 117.578  1.00 41.44           O  
ATOM   2801  N   PHE A 428      90.367  62.268 118.479  1.00 40.85           N  
ATOM   2802  CA  PHE A 428      91.190  63.191 117.713  1.00 40.85           C  
ATOM   2803  C   PHE A 428      92.537  63.409 118.401  1.00 40.85           C  
ATOM   2804  O   PHE A 428      92.783  62.952 119.520  1.00 40.85           O  
ATOM   2805  CB  PHE A 428      90.473  64.527 117.515  1.00 40.85           C  
ATOM   2806  CG  PHE A 428      89.252  64.439 116.644  1.00 40.85           C  
ATOM   2807  CD1 PHE A 428      88.046  63.988 117.151  1.00 40.85           C  
ATOM   2808  CD2 PHE A 428      89.316  64.814 115.314  1.00 40.85           C  
ATOM   2809  CE1 PHE A 428      86.930  63.907 116.344  1.00 40.85           C  
ATOM   2810  CE2 PHE A 428      88.204  64.737 114.505  1.00 40.85           C  
ATOM   2811  CZ  PHE A 428      87.010  64.283 115.020  1.00 40.85           C  
ATOM   2812  N   PHE A 429      93.423  64.110 117.695  1.00 44.64           N  
ATOM   2813  CA  PHE A 429      94.713  64.584 118.190  1.00 44.64           C  
ATOM   2814  C   PHE A 429      95.669  63.462 118.578  1.00 44.64           C  
ATOM   2815  O   PHE A 429      96.700  63.728 119.208  1.00 44.64           O  
ATOM   2816  CB  PHE A 429      94.539  65.552 119.366  1.00 44.64           C  
ATOM   2817  CG  PHE A 429      93.497  66.603 119.129  1.00 44.64           C  
ATOM   2818  CD1 PHE A 429      93.503  67.347 117.963  1.00 44.64           C  
ATOM   2819  CD2 PHE A 429      92.514  66.850 120.069  1.00 44.64           C  
ATOM   2820  CE1 PHE A 429      92.548  68.316 117.737  1.00 44.64           C  
ATOM   2821  CE2 PHE A 429      91.558  67.819 119.849  1.00 44.64           C  
ATOM   2822  CZ  PHE A 429      91.575  68.553 118.682  1.00 44.64           C  
ATOM   2823  N   LYS A 430      95.365  62.216 118.228  1.00 49.89           N  
ATOM   2824  CA  LYS A 430      96.352  61.156 118.368  1.00 49.89           C  
ATOM   2825  C   LYS A 430      97.483  61.358 117.367  1.00 49.89           C  
ATOM   2826  O   LYS A 430      97.310  61.985 116.318  1.00 49.89           O  
ATOM   2827  CB  LYS A 430      95.714  59.782 118.170  1.00 49.89           C  
ATOM   2828  CG  LYS A 430      94.301  59.650 118.711  1.00 49.89           C  
ATOM   2829  CD  LYS A 430      94.248  59.967 120.199  1.00 49.89           C  
ATOM   2830  CE  LYS A 430      93.018  59.363 120.853  1.00 49.89           C  
ATOM   2831  NZ  LYS A 430      92.902  57.906 120.573  1.00 49.89           N  
ATOM   2832  N   GLU A 431      98.655  60.829 117.707  1.00 62.05           N  
ATOM   2833  CA  GLU A 431      99.825  61.004 116.860  1.00 62.05           C  
ATOM   2834  C   GLU A 431      99.621  60.336 115.505  1.00 62.05           C  
ATOM   2835  O   GLU A 431      98.952  59.306 115.385  1.00 62.05           O  
ATOM   2836  CB  GLU A 431     101.070  60.435 117.546  1.00 62.05           C  
ATOM   2837  CG  GLU A 431     101.548  61.166 118.815  1.00 62.05           C  
ATOM   2838  CD  GLU A 431     102.752  60.539 119.527  1.00 62.05           C  
ATOM   2839  OE1 GLU A 431     103.120  59.408 119.145  1.00 62.05           O  
ATOM   2840  OE2 GLU A 431     103.372  61.171 120.409  1.00 62.05           O  
ATOM   2841  N   GLY A 432     100.206  60.942 114.475  1.00 56.82           N  
ATOM   2842  CA  GLY A 432     100.098  60.447 113.120  1.00 56.82           C  
ATOM   2843  C   GLY A 432      98.815  60.802 112.404  1.00 56.82           C  
ATOM   2844  O   GLY A 432      98.662  60.439 111.231  1.00 56.82           O  
ATOM   2845  N   SER A 433      97.891  61.496 113.060  1.00 49.71           N  
ATOM   2846  CA  SER A 433      96.667  61.915 112.396  1.00 49.71           C  
ATOM   2847  C   SER A 433      96.961  63.012 111.383  1.00 49.71           C  
ATOM   2848  O   SER A 433      97.837  63.856 111.593  1.00 49.71           O  
ATOM   2849  CB  SER A 433      95.646  62.407 113.420  1.00 49.71           C  
ATOM   2850  OG  SER A 433      94.403  62.691 112.801  1.00 49.71           O  
ATOM   2851  N   SER A 434      96.224  62.995 110.273  1.00 46.07           N  
ATOM   2852  CA  SER A 434      96.333  64.066 109.294  1.00 46.07           C  
ATOM   2853  C   SER A 434      95.659  65.346 109.760  1.00 46.07           C  
ATOM   2854  O   SER A 434      95.860  66.394 109.138  1.00 46.07           O  
ATOM   2855  CB  SER A 434      95.737  63.623 107.958  1.00 46.07           C  
ATOM   2856  OG  SER A 434      95.537  64.730 107.097  1.00 46.07           O  
ATOM   2857  N   VAL A 435      94.873  65.286 110.832  1.00 42.34           N  
ATOM   2858  CA  VAL A 435      94.168  66.438 111.377  1.00 42.34           C  
ATOM   2859  C   VAL A 435      94.853  66.840 112.676  1.00 42.34           C  
ATOM   2860  O   VAL A 435      94.922  66.045 113.621  1.00 42.34           O  
ATOM   2861  CB  VAL A 435      92.683  66.127 111.611  1.00 42.34           C  
ATOM   2862  CG1 VAL A 435      92.066  67.171 112.498  1.00 42.34           C  
ATOM   2863  CG2 VAL A 435      91.945  66.057 110.296  1.00 42.34           C  
ATOM   2864  N   GLU A 436      95.353  68.072 112.724  1.00 39.32           N  
ATOM   2865  CA  GLU A 436      96.053  68.573 113.897  1.00 39.32           C  
ATOM   2866  C   GLU A 436      95.844  70.077 113.993  1.00 39.32           C  
ATOM   2867  O   GLU A 436      95.580  70.744 112.991  1.00 39.32           O  
ATOM   2868  CB  GLU A 436      97.546  68.233 113.841  1.00 39.32           C  
ATOM   2869  CG  GLU A 436      98.218  68.632 112.540  1.00 39.32           C  
ATOM   2870  CD  GLU A 436      99.712  68.381 112.551  1.00 39.32           C  
ATOM   2871  OE1 GLU A 436     100.463  69.226 112.020  1.00 39.32           O  
ATOM   2872  OE2 GLU A 436     100.136  67.338 113.089  1.00 39.32           O  
ATOM   2873  N   LEU A 437      95.961  70.603 115.210  1.00 32.28           N  
ATOM   2874  CA  LEU A 437      95.751  72.028 115.432  1.00 32.28           C  
ATOM   2875  C   LEU A 437      96.887  72.843 114.827  1.00 32.28           C  
ATOM   2876  O   LEU A 437      98.065  72.545 115.043  1.00 32.28           O  
ATOM   2877  CB  LEU A 437      95.634  72.325 116.925  1.00 32.28           C  
ATOM   2878  CG  LEU A 437      94.397  71.818 117.665  1.00 32.28           C  
ATOM   2879  CD1 LEU A 437      94.164  72.644 118.917  1.00 32.28           C  
ATOM   2880  CD2 LEU A 437      93.179  71.870 116.762  1.00 32.28           C  
ATOM   2881  N   LYS A 438      96.527  73.873 114.060  1.00 24.79           N  
ATOM   2882  CA  LYS A 438      97.508  74.794 113.498  1.00 24.79           C  
ATOM   2883  C   LYS A 438      97.100  76.257 113.569  1.00 24.79           C  
ATOM   2884  O   LYS A 438      97.921  77.113 113.234  1.00 24.79           O  
ATOM   2885  CB  LYS A 438      97.813  74.433 112.038  1.00 24.79           C  
ATOM   2886  CG  LYS A 438      98.501  73.093 111.869  1.00 24.79           C  
ATOM   2887  CD  LYS A 438      98.614  72.703 110.411  1.00 24.79           C  
ATOM   2888  CE  LYS A 438      99.949  72.039 110.133  1.00 24.79           C  
ATOM   2889  NZ  LYS A 438     100.559  72.521 108.865  1.00 24.79           N  
ATOM   2890  N   HIS A 439      95.880  76.577 113.985  1.00 21.23           N  
ATOM   2891  CA  HIS A 439      95.387  77.946 114.036  1.00 21.23           C  
ATOM   2892  C   HIS A 439      95.249  78.376 115.488  1.00 21.23           C  
ATOM   2893  O   HIS A 439      94.558  77.717 116.271  1.00 21.23           O  
ATOM   2894  CB  HIS A 439      94.044  78.065 113.314  1.00 21.23           C  
ATOM   2895  CG  HIS A 439      94.160  78.095 111.823  1.00 21.23           C  
ATOM   2896  ND1 HIS A 439      94.205  76.951 111.057  1.00 21.23           N  
ATOM   2897  CD2 HIS A 439      94.222  79.131 110.955  1.00 21.23           C  
ATOM   2898  CE1 HIS A 439      94.301  77.281 109.782  1.00 21.23           C  
ATOM   2899  NE2 HIS A 439      94.309  78.598 109.693  1.00 21.23           N  
ATOM   2900  N   PHE A 440      95.894  79.485 115.839  1.00 24.33           N  
ATOM   2901  CA  PHE A 440      95.961  79.936 117.219  1.00 24.33           C  
ATOM   2902  C   PHE A 440      95.782  81.445 117.262  1.00 24.33           C  
ATOM   2903  O   PHE A 440      95.882  82.135 116.245  1.00 24.33           O  
ATOM   2904  CB  PHE A 440      97.299  79.549 117.863  1.00 24.33           C  
ATOM   2905  CG  PHE A 440      97.593  78.078 117.811  1.00 24.33           C  
ATOM   2906  CD1 PHE A 440      97.015  77.208 118.714  1.00 24.33           C  
ATOM   2907  CD2 PHE A 440      98.438  77.566 116.843  1.00 24.33           C  
ATOM   2908  CE1 PHE A 440      97.284  75.860 118.660  1.00 24.33           C  
ATOM   2909  CE2 PHE A 440      98.706  76.218 116.784  1.00 24.33           C  
ATOM   2910  CZ  PHE A 440      98.129  75.364 117.693  1.00 24.33           C  
ATOM   2911  N   PHE A 441      95.498  81.954 118.456  1.00 25.41           N  
ATOM   2912  CA  PHE A 441      95.662  83.373 118.735  1.00 25.41           C  
ATOM   2913  C   PHE A 441      97.107  83.611 119.157  1.00 25.41           C  
ATOM   2914  O   PHE A 441      97.552  83.081 120.179  1.00 25.41           O  
ATOM   2915  CB  PHE A 441      94.700  83.822 119.832  1.00 25.41           C  
ATOM   2916  CG  PHE A 441      93.253  83.766 119.437  1.00 25.41           C  
ATOM   2917  CD1 PHE A 441      92.782  84.502 118.371  1.00 25.41           C  
ATOM   2918  CD2 PHE A 441      92.370  82.950 120.117  1.00 25.41           C  
ATOM   2919  CE1 PHE A 441      91.452  84.446 118.010  1.00 25.41           C  
ATOM   2920  CE2 PHE A 441      91.044  82.889 119.754  1.00 25.41           C  
ATOM   2921  CZ  PHE A 441      90.586  83.635 118.697  1.00 25.41           C  
ATOM   2922  N   PHE A 442      97.839  84.399 118.377  1.00 24.85           N  
ATOM   2923  CA  PHE A 442      99.246  84.670 118.641  1.00 24.85           C  
ATOM   2924  C   PHE A 442      99.372  85.997 119.378  1.00 24.85           C  
ATOM   2925  O   PHE A 442      98.858  87.020 118.917  1.00 24.85           O  
ATOM   2926  CB  PHE A 442     100.053  84.695 117.345  1.00 24.85           C  
ATOM   2927  CG  PHE A 442     100.337  83.333 116.777  1.00 24.85           C  
ATOM   2928  CD1 PHE A 442      99.377  82.660 116.043  1.00 24.85           C  
ATOM   2929  CD2 PHE A 442     101.564  82.727 116.975  1.00 24.85           C  
ATOM   2930  CE1 PHE A 442      99.635  81.411 115.521  1.00 24.85           C  
ATOM   2931  CE2 PHE A 442     101.826  81.477 116.455  1.00 24.85           C  
ATOM   2932  CZ  PHE A 442     100.861  80.819 115.727  1.00 24.85           C  
ATOM   2933  N   ALA A 443     100.042  85.972 120.525  1.00 25.32           N  
ATOM   2934  CA  ALA A 443     100.229  87.174 121.320  1.00 25.32           C  
ATOM   2935  C   ALA A 443     101.233  88.113 120.664  1.00 25.32           C  
ATOM   2936  O   ALA A 443     102.092  87.697 119.883  1.00 25.32           O  
ATOM   2937  CB  ALA A 443     100.693  86.811 122.727  1.00 25.32           C  
ATOM   2938  N   GLN A 444     101.101  89.401 120.995  1.00 26.72           N  
ATOM   2939  CA  GLN A 444     102.011  90.433 120.436  1.00 26.72           C  
ATOM   2940  C   GLN A 444     102.411  91.388 121.561  1.00 26.72           C  
ATOM   2941  O   GLN A 444     101.524  91.779 122.343  1.00 26.72           O  
ATOM   2942  CB  GLN A 444     101.333  91.204 119.298  1.00 26.72           C  
ATOM   2943  CG  GLN A 444     100.796  90.336 118.169  1.00 26.72           C  
ATOM   2944  CD  GLN A 444     101.884  89.613 117.416  1.00 26.72           C  
ATOM   2945  OE1 GLN A 444     103.051  89.995 117.448  1.00 26.72           O  
ATOM   2946  NE2 GLN A 444     101.505  88.548 116.728  1.00 26.72           N  
ATOM   2947  N   ASP A 445     103.689  91.752 121.631  1.00 29.01           N  
ATOM   2948  CA  ASP A 445     104.215  92.677 122.620  1.00 29.01           C  
ATOM   2949  C   ASP A 445     103.979  94.121 122.176  1.00 29.01           C  
ATOM   2950  O   ASP A 445     103.360  94.388 121.144  1.00 29.01           O  
ATOM   2951  CB  ASP A 445     105.689  92.370 122.900  1.00 29.01           C  
ATOM   2952  CG  ASP A 445     106.583  92.542 121.679  1.00 29.01           C  
ATOM   2953  OD1 ASP A 445     106.266  93.338 120.773  1.00 29.01           O  
ATOM   2954  OD2 ASP A 445     107.622  91.852 121.621  1.00 29.01           O  
ATOM   2955  N   GLY A 446     104.482  95.069 122.966  1.00 25.95           N  
ATOM   2956  CA  GLY A 446     104.156  96.475 122.787  1.00 25.95           C  
ATOM   2957  C   GLY A 446     104.683  97.109 121.515  1.00 25.95           C  
ATOM   2958  O   GLY A 446     104.244  98.211 121.173  1.00 25.95           O  
ATOM   2959  N   ASN A 447     105.601  96.453 120.812  1.00 28.54           N  
ATOM   2960  CA  ASN A 447     106.118  96.988 119.559  1.00 28.54           C  
ATOM   2961  C   ASN A 447     105.251  96.639 118.357  1.00 28.54           C  
ATOM   2962  O   ASN A 447     105.556  97.088 117.249  1.00 28.54           O  
ATOM   2963  CB  ASN A 447     107.542  96.480 119.316  1.00 28.54           C  
ATOM   2964  CG  ASN A 447     108.480  96.808 120.456  1.00 28.54           C  
ATOM   2965  OD1 ASN A 447     108.348  97.844 121.105  1.00 28.54           O  
ATOM   2966  ND2 ASN A 447     109.436  95.924 120.708  1.00 28.54           N  
ATOM   2967  N   ALA A 448     104.185  95.860 118.552  1.00 25.83           N  
ATOM   2968  CA  ALA A 448     103.455  95.276 117.430  1.00 25.83           C  
ATOM   2969  C   ALA A 448     102.850  96.341 116.522  1.00 25.83           C  
ATOM   2970  O   ALA A 448     102.951  96.252 115.292  1.00 25.83           O  
ATOM   2971  CB  ALA A 448     102.366  94.346 117.956  1.00 25.83           C  
ATOM   2972  N   ALA A 449     102.204  97.351 117.108  1.00 24.54           N  
ATOM   2973  CA  ALA A 449     101.464  98.316 116.301  1.00 24.54           C  
ATOM   2974  C   ALA A 449     102.392  99.131 115.411  1.00 24.54           C  
ATOM   2975  O   ALA A 449     102.083  99.370 114.237  1.00 24.54           O  
ATOM   2976  CB  ALA A 449     100.641  99.235 117.202  1.00 24.54           C  
ATOM   2977  N   ILE A 450     103.532  99.565 115.945  1.00 22.80           N  
ATOM   2978  CA  ILE A 450     104.456 100.347 115.134  1.00 22.80           C  
ATOM   2979  C   ILE A 450     105.265  99.448 114.208  1.00 22.80           C  
ATOM   2980  O   ILE A 450     105.654  99.872 113.115  1.00 22.80           O  
ATOM   2981  CB  ILE A 450     105.363 101.212 116.026  1.00 22.80           C  
ATOM   2982  CG1 ILE A 450     106.004 102.329 115.203  1.00 22.80           C  
ATOM   2983  CG2 ILE A 450     106.423 100.370 116.721  1.00 22.80           C  
ATOM   2984  CD1 ILE A 450     105.052 103.440 114.848  1.00 22.80           C  
ATOM   2985  N   SER A 451     105.536  98.208 114.618  1.00 21.34           N  
ATOM   2986  CA  SER A 451     106.258  97.287 113.748  1.00 21.34           C  
ATOM   2987  C   SER A 451     105.439  96.945 112.512  1.00 21.34           C  
ATOM   2988  O   SER A 451     105.988  96.809 111.413  1.00 21.34           O  
ATOM   2989  CB  SER A 451     106.624  96.018 114.515  1.00 21.34           C  
ATOM   2990  OG  SER A 451     107.616  95.276 113.832  1.00 21.34           O  
ATOM   2991  N   ASP A 452     104.124  96.790 112.674  1.00 21.54           N  
ATOM   2992  CA  ASP A 452     103.276  96.454 111.536  1.00 21.54           C  
ATOM   2993  C   ASP A 452     103.132  97.643 110.596  1.00 21.54           C  
ATOM   2994  O   ASP A 452     103.183  97.490 109.371  1.00 21.54           O  
ATOM   2995  CB  ASP A 452     101.908  95.985 112.017  1.00 21.54           C  
ATOM   2996  CG  ASP A 452     100.939  95.782 110.879  1.00 21.54           C  
ATOM   2997  OD1 ASP A 452     101.313  95.116 109.892  1.00 21.54           O  
ATOM   2998  OD2 ASP A 452      99.799  96.270 110.968  1.00 21.54           O  
ATOM   2999  N   TYR A 453     102.921  98.836 111.157  1.00 18.91           N  
ATOM   3000  CA  TYR A 453     102.871 100.053 110.353  1.00 18.91           C  
ATOM   3001  C   TYR A 453     104.110 100.200 109.481  1.00 18.91           C  
ATOM   3002  O   TYR A 453     104.035 100.719 108.363  1.00 18.91           O  
ATOM   3003  CB  TYR A 453     102.712 101.273 111.261  1.00 18.91           C  
ATOM   3004  CG  TYR A 453     102.811 102.582 110.520  1.00 18.91           C  
ATOM   3005  CD1 TYR A 453     101.809 102.988 109.651  1.00 18.91           C  
ATOM   3006  CD2 TYR A 453     103.914 103.405 110.675  1.00 18.91           C  
ATOM   3007  CE1 TYR A 453     101.901 104.176 108.964  1.00 18.91           C  
ATOM   3008  CE2 TYR A 453     104.014 104.593 109.992  1.00 18.91           C  
ATOM   3009  CZ  TYR A 453     103.005 104.974 109.139  1.00 18.91           C  
ATOM   3010  OH  TYR A 453     103.099 106.157 108.456  1.00 18.91           O  
ATOM   3011  N   ASP A 454     105.268  99.759 109.938  1.00 19.60           N  
ATOM   3012  CA  ASP A 454     106.537  99.945 109.199  1.00 19.60           C  
ATOM   3013  C   ASP A 454     106.576  99.128 107.912  1.00 19.60           C  
ATOM   3014  O   ASP A 454     107.503  99.328 107.168  1.00 19.60           O  
ATOM   3015  CB  ASP A 454     107.749  99.729 110.104  1.00 19.60           C  
ATOM   3016  CG  ASP A 454     109.077 100.113 109.481  1.00 19.60           C  
ATOM   3017  OD1 ASP A 454     109.141 101.165 108.829  1.00 19.60           O  
ATOM   3018  OD2 ASP A 454     110.039  99.352 109.661  1.00 19.60           O  
ATOM   3019  N   TYR A 455     105.637  98.226 107.676  1.00 17.49           N  
ATOM   3020  CA  TYR A 455     105.623  97.536 106.389  1.00 17.49           C  
ATOM   3021  C   TYR A 455     105.189  98.425 105.229  1.00 17.49           C  
ATOM   3022  O   TYR A 455     105.184  97.956 104.087  1.00 17.49           O  
ATOM   3023  CB  TYR A 455     104.734  96.291 106.443  1.00 17.49           C  
ATOM   3024  CG  TYR A 455     105.123  95.302 107.516  1.00 17.49           C  
ATOM   3025  CD1 TYR A 455     106.437  94.881 107.650  1.00 17.49           C  
ATOM   3026  CD2 TYR A 455     104.177  94.769 108.378  1.00 17.49           C  
ATOM   3027  CE1 TYR A 455     106.801  93.976 108.626  1.00 17.49           C  
ATOM   3028  CE2 TYR A 455     104.531  93.862 109.357  1.00 17.49           C  
ATOM   3029  CZ  TYR A 455     105.844  93.468 109.475  1.00 17.49           C  
ATOM   3030  OH  TYR A 455     106.204  92.563 110.446  1.00 17.49           O  
ATOM   3031  N   TYR A 456     104.819  99.682 105.480  1.00 13.94           N  
ATOM   3032  CA  TYR A 456     104.600 100.615 104.380  1.00 13.94           C  
ATOM   3033  C   TYR A 456     105.891 100.981 103.664  1.00 13.94           C  
ATOM   3034  O   TYR A 456     105.836 101.631 102.617  1.00 13.94           O  
ATOM   3035  CB  TYR A 456     103.897 101.875 104.877  1.00 13.94           C  
ATOM   3036  CG  TYR A 456     102.420 101.681 105.121  1.00 13.94           C  
ATOM   3037  CD1 TYR A 456     101.549 101.484 104.061  1.00 13.94           C  
ATOM   3038  CD2 TYR A 456     101.896 101.688 106.403  1.00 13.94           C  
ATOM   3039  CE1 TYR A 456     100.201 101.306 104.269  1.00 13.94           C  
ATOM   3040  CE2 TYR A 456     100.545 101.509 106.621  1.00 13.94           C  
ATOM   3041  CZ  TYR A 456      99.703 101.318 105.549  1.00 13.94           C  
ATOM   3042  OH  TYR A 456      98.358 101.138 105.753  1.00 13.94           O  
ATOM   3043  N   ARG A 457     107.043 100.584 104.205  1.00 14.88           N  
ATOM   3044  CA  ARG A 457     108.318 100.751 103.518  1.00 14.88           C  
ATOM   3045  C   ARG A 457     108.386  99.970 102.212  1.00 14.88           C  
ATOM   3046  O   ARG A 457     109.273 100.231 101.395  1.00 14.88           O  
ATOM   3047  CB  ARG A 457     109.446 100.330 104.457  1.00 14.88           C  
ATOM   3048  CG  ARG A 457     109.384  98.864 104.822  1.00 14.88           C  
ATOM   3049  CD  ARG A 457     110.685  98.329 105.359  1.00 14.88           C  
ATOM   3050  NE  ARG A 457     110.550  96.912 105.678  1.00 14.88           N  
ATOM   3051  CZ  ARG A 457     110.529  96.425 106.913  1.00 14.88           C  
ATOM   3052  NH1 ARG A 457     110.623  97.242 107.949  1.00 14.88           N  
ATOM   3053  NH2 ARG A 457     110.402  95.122 107.112  1.00 14.88           N  
ATOM   3054  N   TYR A 458     107.482  99.014 101.999  1.00 13.69           N  
ATOM   3055  CA  TYR A 458     107.378  98.329 100.717  1.00 13.69           C  
ATOM   3056  C   TYR A 458     106.623  99.136  99.671  1.00 13.69           C  
ATOM   3057  O   TYR A 458     106.636  98.754  98.496  1.00 13.69           O  
ATOM   3058  CB  TYR A 458     106.698  96.968 100.890  1.00 13.69           C  
ATOM   3059  CG  TYR A 458     107.382  96.057 101.879  1.00 13.69           C  
ATOM   3060  CD1 TYR A 458     108.763  95.962 101.922  1.00 13.69           C  
ATOM   3061  CD2 TYR A 458     106.645  95.271 102.751  1.00 13.69           C  
ATOM   3062  CE1 TYR A 458     109.392  95.128 102.817  1.00 13.69           C  
ATOM   3063  CE2 TYR A 458     107.265  94.433 103.649  1.00 13.69           C  
ATOM   3064  CZ  TYR A 458     108.639  94.364 103.678  1.00 13.69           C  
ATOM   3065  OH  TYR A 458     109.264  93.527 104.570  1.00 13.69           O  
ATOM   3066  N   ASN A 459     105.963 100.223 100.059  1.00 10.21           N  
ATOM   3067  CA  ASN A 459     105.347 101.119  99.091  1.00 10.21           C  
ATOM   3068  C   ASN A 459     106.404 102.064  98.539  1.00 10.21           C  
ATOM   3069  O   ASN A 459     107.014 102.828  99.292  1.00 10.21           O  
ATOM   3070  CB  ASN A 459     104.202 101.904  99.722  1.00 10.21           C  
ATOM   3071  CG  ASN A 459     103.197 102.384  98.697  1.00 10.21           C  
ATOM   3072  OD1 ASN A 459     103.291 103.501  98.196  1.00 10.21           O  
ATOM   3073  ND2 ASN A 459     102.233 101.536  98.375  1.00 10.21           N  
ATOM   3074  N   LEU A 460     106.617 102.010  97.229  1.00  7.65           N  
ATOM   3075  CA  LEU A 460     107.624 102.809  96.566  1.00  7.65           C  
ATOM   3076  C   LEU A 460     106.994 103.599  95.428  1.00  7.65           C  
ATOM   3077  O   LEU A 460     106.034 103.130  94.810  1.00  7.65           O  
ATOM   3078  CB  LEU A 460     108.745 101.917  96.013  1.00  7.65           C  
ATOM   3079  CG  LEU A 460     109.489 101.045  97.025  1.00  7.65           C  
ATOM   3080  CD1 LEU A 460     110.246  99.949  96.307  1.00  7.65           C  
ATOM   3081  CD2 LEU A 460     110.429 101.872  97.874  1.00  7.65           C  
ATOM   3082  N   PRO A 461     107.492 104.800  95.138  1.00  6.48           N  
ATOM   3083  CA  PRO A 461     106.976 105.554  93.988  1.00  6.48           C  
ATOM   3084  C   PRO A 461     107.240 104.814  92.687  1.00  6.48           C  
ATOM   3085  O   PRO A 461     108.388 104.581  92.302  1.00  6.48           O  
ATOM   3086  CB  PRO A 461     107.738 106.881  94.062  1.00  6.48           C  
ATOM   3087  CG  PRO A 461     108.954 106.580  94.849  1.00  6.48           C  
ATOM   3088  CD  PRO A 461     108.555 105.532  95.841  1.00  6.48           C  
ATOM   3089  N   THR A 462     106.160 104.442  92.010  1.00  6.52           N  
ATOM   3090  CA  THR A 462     106.224 103.639  90.798  1.00  6.52           C  
ATOM   3091  C   THR A 462     105.652 104.442  89.639  1.00  6.52           C  
ATOM   3092  O   THR A 462     104.495 104.869  89.686  1.00  6.52           O  
ATOM   3093  CB  THR A 462     105.455 102.327  90.978  1.00  6.52           C  
ATOM   3094  OG1 THR A 462     106.006 101.594  92.077  1.00  6.52           O  
ATOM   3095  CG2 THR A 462     105.531 101.473  89.721  1.00  6.52           C  
ATOM   3096  N   MET A 463     106.461 104.646  88.607  1.00  9.03           N  
ATOM   3097  CA  MET A 463     105.980 105.217  87.360  1.00  9.03           C  
ATOM   3098  C   MET A 463     105.498 104.102  86.444  1.00  9.03           C  
ATOM   3099  O   MET A 463     106.154 103.067  86.306  1.00  9.03           O  
ATOM   3100  CB  MET A 463     107.075 106.028  86.668  1.00  9.03           C  
ATOM   3101  CG  MET A 463     106.570 107.199  85.856  1.00  9.03           C  
ATOM   3102  SD  MET A 463     107.823 107.836  84.732  1.00  9.03           S  
ATOM   3103  CE  MET A 463     107.015 109.307  84.119  1.00  9.03           C  
ATOM   3104  N   CYS A 464     104.348 104.316  85.827  1.00  8.04           N  
ATOM   3105  CA  CYS A 464     103.738 103.326  84.957  1.00  8.04           C  
ATOM   3106  C   CYS A 464     104.036 103.640  83.497  1.00  8.04           C  
ATOM   3107  O   CYS A 464     104.319 104.781  83.126  1.00  8.04           O  
ATOM   3108  CB  CYS A 464     102.226 103.270  85.186  1.00  8.04           C  
ATOM   3109  SG  CYS A 464     101.740 102.423  86.707  1.00  8.04           S  
ATOM   3110  N   ASP A 465     103.992 102.599  82.670  1.00  6.79           N  
ATOM   3111  CA  ASP A 465     103.964 102.778  81.225  1.00  6.79           C  
ATOM   3112  C   ASP A 465     102.609 103.393  80.908  1.00  6.79           C  
ATOM   3113  O   ASP A 465     101.579 102.721  81.020  1.00  6.79           O  
ATOM   3114  CB  ASP A 465     104.195 101.433  80.524  1.00  6.79           C  
ATOM   3115  CG  ASP A 465     104.025 101.488  79.006  1.00  6.79           C  
ATOM   3116  OD1 ASP A 465     103.511 102.481  78.454  1.00  6.79           O  
ATOM   3117  OD2 ASP A 465     104.441 100.511  78.348  1.00  6.79           O  
ATOM   3118  N   ILE A 466     102.592 104.674  80.535  1.00  5.13           N  
ATOM   3119  CA  ILE A 466     101.338 105.419  80.561  1.00  5.13           C  
ATOM   3120  C   ILE A 466     100.425 105.003  79.413  1.00  5.13           C  
ATOM   3121  O   ILE A 466      99.205 104.937  79.576  1.00  5.13           O  
ATOM   3122  CB  ILE A 466     101.607 106.938  80.577  1.00  5.13           C  
ATOM   3123  CG1 ILE A 466     100.305 107.704  80.804  1.00  5.13           C  
ATOM   3124  CG2 ILE A 466     102.270 107.401  79.298  1.00  5.13           C  
ATOM   3125  CD1 ILE A 466      99.669 107.447  82.147  1.00  5.13           C  
ATOM   3126  N   ARG A 467     100.987 104.711  78.240  1.00  6.90           N  
ATOM   3127  CA  ARG A 467     100.147 104.315  77.114  1.00  6.90           C  
ATOM   3128  C   ARG A 467      99.502 102.955  77.366  1.00  6.90           C  
ATOM   3129  O   ARG A 467      98.309 102.751  77.087  1.00  6.90           O  
ATOM   3130  CB  ARG A 467     100.980 104.295  75.834  1.00  6.90           C  
ATOM   3131  CG  ARG A 467     101.489 105.664  75.398  1.00  6.90           C  
ATOM   3132  CD  ARG A 467     100.366 106.653  75.150  1.00  6.90           C  
ATOM   3133  NE  ARG A 467     100.877 107.952  74.720  1.00  6.90           N  
ATOM   3134  CZ  ARG A 467     100.398 109.123  75.130  1.00  6.90           C  
ATOM   3135  NH1 ARG A 467      99.389 109.170  75.986  1.00  6.90           N  
ATOM   3136  NH2 ARG A 467     100.932 110.249  74.686  1.00  6.90           N  
ATOM   3137  N   GLN A 468     100.275 102.031  77.932  1.00  5.35           N  
ATOM   3138  CA  GLN A 468      99.752 100.724  78.307  1.00  5.35           C  
ATOM   3139  C   GLN A 468      98.649 100.851  79.350  1.00  5.35           C  
ATOM   3140  O   GLN A 468      97.594 100.220  79.235  1.00  5.35           O  
ATOM   3141  CB  GLN A 468     100.900  99.860  78.818  1.00  5.35           C  
ATOM   3142  CG  GLN A 468     100.538  98.449  79.186  1.00  5.35           C  
ATOM   3143  CD  GLN A 468     101.520  97.871  80.177  1.00  5.35           C  
ATOM   3144  OE1 GLN A 468     102.415  97.115  79.810  1.00  5.35           O  
ATOM   3145  NE2 GLN A 468     101.377  98.248  81.436  1.00  5.35           N  
ATOM   3146  N   LEU A 469      98.881 101.663  80.381  1.00  4.71           N  
ATOM   3147  CA  LEU A 469      97.877 101.861  81.421  1.00  4.71           C  
ATOM   3148  C   LEU A 469      96.614 102.510  80.863  1.00  4.71           C  
ATOM   3149  O   LEU A 469      95.499 102.163  81.267  1.00  4.71           O  
ATOM   3150  CB  LEU A 469      98.465 102.708  82.549  1.00  4.71           C  
ATOM   3151  CG  LEU A 469      97.575 102.998  83.753  1.00  4.71           C  
ATOM   3152  CD1 LEU A 469      97.023 101.709  84.314  1.00  4.71           C  
ATOM   3153  CD2 LEU A 469      98.355 103.745  84.806  1.00  4.71           C  
ATOM   3154  N   LEU A 470      96.770 103.466  79.947  1.00  5.25           N  
ATOM   3155  CA  LEU A 470      95.620 104.127  79.346  1.00  5.25           C  
ATOM   3156  C   LEU A 470      94.817 103.198  78.448  1.00  5.25           C  
ATOM   3157  O   LEU A 470      93.621 103.429  78.258  1.00  5.25           O  
ATOM   3158  CB  LEU A 470      96.066 105.351  78.547  1.00  5.25           C  
ATOM   3159  CG  LEU A 470      96.388 106.612  79.348  1.00  5.25           C  
ATOM   3160  CD1 LEU A 470      97.391 107.480  78.608  1.00  5.25           C  
ATOM   3161  CD2 LEU A 470      95.129 107.392  79.663  1.00  5.25           C  
ATOM   3162  N   PHE A 471      95.442 102.173  77.870  1.00  5.57           N  
ATOM   3163  CA  PHE A 471      94.639 101.166  77.180  1.00  5.57           C  
ATOM   3164  C   PHE A 471      93.962 100.225  78.179  1.00  5.57           C  
ATOM   3165  O   PHE A 471      92.770  99.899  78.048  1.00  5.57           O  
ATOM   3166  CB  PHE A 471      95.507 100.384  76.195  1.00  5.57           C  
ATOM   3167  CG  PHE A 471      94.798  99.232  75.550  1.00  5.57           C  
ATOM   3168  CD1 PHE A 471      93.947  99.443  74.483  1.00  5.57           C  
ATOM   3169  CD2 PHE A 471      94.977  97.942  76.011  1.00  5.57           C  
ATOM   3170  CE1 PHE A 471      93.288  98.393  73.890  1.00  5.57           C  
ATOM   3171  CE2 PHE A 471      94.322  96.891  75.418  1.00  5.57           C  
ATOM   3172  CZ  PHE A 471      93.476  97.117  74.357  1.00  5.57           C  
ATOM   3173  N   VAL A 472      94.717  99.792  79.192  1.00  4.59           N  
ATOM   3174  CA  VAL A 472      94.206  98.852  80.185  1.00  4.59           C  
ATOM   3175  C   VAL A 472      92.972  99.414  80.879  1.00  4.59           C  
ATOM   3176  O   VAL A 472      92.008  98.686  81.140  1.00  4.59           O  
ATOM   3177  CB  VAL A 472      95.319  98.485  81.187  1.00  4.59           C  
ATOM   3178  CG1 VAL A 472      94.749  97.821  82.423  1.00  4.59           C  
ATOM   3179  CG2 VAL A 472      96.334  97.566  80.529  1.00  4.59           C  
ATOM   3180  N   VAL A 473      92.966 100.719  81.170  1.00  5.86           N  
ATOM   3181  CA  VAL A 473      91.817 101.299  81.866  1.00  5.86           C  
ATOM   3182  C   VAL A 473      90.565 101.229  81.004  1.00  5.86           C  
ATOM   3183  O   VAL A 473      89.456 101.075  81.525  1.00  5.86           O  
ATOM   3184  CB  VAL A 473      92.085 102.751  82.308  1.00  5.86           C  
ATOM   3185  CG1 VAL A 473      93.175 102.792  83.326  1.00  5.86           C  
ATOM   3186  CG2 VAL A 473      92.401 103.648  81.124  1.00  5.86           C  
ATOM   3187  N   GLU A 474      90.706 101.354  79.687  1.00  8.28           N  
ATOM   3188  CA  GLU A 474      89.549 101.199  78.817  1.00  8.28           C  
ATOM   3189  C   GLU A 474      89.095  99.753  78.739  1.00  8.28           C  
ATOM   3190  O   GLU A 474      87.894  99.494  78.611  1.00  8.28           O  
ATOM   3191  CB  GLU A 474      89.858 101.731  77.418  1.00  8.28           C  
ATOM   3192  CG  GLU A 474      90.253 103.184  77.402  1.00  8.28           C  
ATOM   3193  CD  GLU A 474      89.225 104.062  78.076  1.00  8.28           C  
ATOM   3194  OE1 GLU A 474      89.622 104.996  78.801  1.00  8.28           O  
ATOM   3195  OE2 GLU A 474      88.016 103.820  77.882  1.00  8.28           O  
ATOM   3196  N   VAL A 475      90.024  98.801  78.811  1.00  6.43           N  
ATOM   3197  CA  VAL A 475      89.591  97.406  78.847  1.00  6.43           C  
ATOM   3198  C   VAL A 475      89.018  97.044  80.213  1.00  6.43           C  
ATOM   3199  O   VAL A 475      88.016  96.330  80.306  1.00  6.43           O  
ATOM   3200  CB  VAL A 475      90.741  96.472  78.443  1.00  6.43           C  
ATOM   3201  CG1 VAL A 475      90.245  95.044  78.375  1.00  6.43           C  
ATOM   3202  CG2 VAL A 475      91.278  96.891  77.103  1.00  6.43           C  
ATOM   3203  N   VAL A 476      89.637  97.527  81.290  1.00  6.31           N  
ATOM   3204  CA  VAL A 476      89.138  97.243  82.633  1.00  6.31           C  
ATOM   3205  C   VAL A 476      87.743  97.825  82.822  1.00  6.31           C  
ATOM   3206  O   VAL A 476      86.882  97.216  83.467  1.00  6.31           O  
ATOM   3207  CB  VAL A 476      90.130  97.764  83.689  1.00  6.31           C  
ATOM   3208  CG1 VAL A 476      89.485  97.823  85.065  1.00  6.31           C  
ATOM   3209  CG2 VAL A 476      91.361  96.882  83.719  1.00  6.31           C  
ATOM   3210  N   ASP A 477      87.494  99.008  82.258  1.00  8.71           N  
ATOM   3211  CA  ASP A 477      86.183  99.634  82.380  1.00  8.71           C  
ATOM   3212  C   ASP A 477      85.076  98.811  81.737  1.00  8.71           C  
ATOM   3213  O   ASP A 477      83.906  98.986  82.091  1.00  8.71           O  
ATOM   3214  CB  ASP A 477      86.217 101.029  81.762  1.00  8.71           C  
ATOM   3215  CG  ASP A 477      85.135 101.932  82.305  1.00  8.71           C  
ATOM   3216  OD1 ASP A 477      85.204 102.291  83.499  1.00  8.71           O  
ATOM   3217  OD2 ASP A 477      84.222 102.296  81.535  1.00  8.71           O  
ATOM   3218  N   LYS A 478      85.412  97.923  80.800  1.00  7.40           N  
ATOM   3219  CA  LYS A 478      84.399  97.086  80.167  1.00  7.40           C  
ATOM   3220  C   LYS A 478      83.843  96.048  81.133  1.00  7.40           C  
ATOM   3221  O   LYS A 478      82.701  95.608  80.980  1.00  7.40           O  
ATOM   3222  CB  LYS A 478      84.988  96.405  78.935  1.00  7.40           C  
ATOM   3223  CG  LYS A 478      85.135  97.335  77.754  1.00  7.40           C  
ATOM   3224  CD  LYS A 478      83.810  97.567  77.069  1.00  7.40           C  
ATOM   3225  CE  LYS A 478      83.927  98.663  76.034  1.00  7.40           C  
ATOM   3226  NZ  LYS A 478      82.666  99.441  75.918  1.00  7.40           N  
ATOM   3227  N   TYR A 479      84.636  95.644  82.125  1.00  5.96           N  
ATOM   3228  CA  TYR A 479      84.178  94.698  83.132  1.00  5.96           C  
ATOM   3229  C   TYR A 479      83.142  95.301  84.068  1.00  5.96           C  
ATOM   3230  O   TYR A 479      82.462  94.558  84.782  1.00  5.96           O  
ATOM   3231  CB  TYR A 479      85.376  94.183  83.931  1.00  5.96           C  
ATOM   3232  CG  TYR A 479      86.200  93.154  83.191  1.00  5.96           C  
ATOM   3233  CD1 TYR A 479      85.795  91.830  83.125  1.00  5.96           C  
ATOM   3234  CD2 TYR A 479      87.370  93.512  82.539  1.00  5.96           C  
ATOM   3235  CE1 TYR A 479      86.536  90.891  82.449  1.00  5.96           C  
ATOM   3236  CE2 TYR A 479      88.118  92.577  81.855  1.00  5.96           C  
ATOM   3237  CZ  TYR A 479      87.696  91.267  81.815  1.00  5.96           C  
ATOM   3238  OH  TYR A 479      88.432  90.327  81.137  1.00  5.96           O  
ATOM   3239  N   PHE A 480      83.005  96.625  84.082  1.00  8.15           N  
ATOM   3240  CA  PHE A 480      82.079  97.319  84.965  1.00  8.15           C  
ATOM   3241  C   PHE A 480      80.948  98.003  84.209  1.00  8.15           C  
ATOM   3242  O   PHE A 480      80.321  98.919  84.747  1.00  8.15           O  
ATOM   3243  CB  PHE A 480      82.849  98.321  85.824  1.00  8.15           C  
ATOM   3244  CG  PHE A 480      83.785  97.666  86.792  1.00  8.15           C  
ATOM   3245  CD1 PHE A 480      83.354  97.310  88.056  1.00  8.15           C  
ATOM   3246  CD2 PHE A 480      85.091  97.393  86.434  1.00  8.15           C  
ATOM   3247  CE1 PHE A 480      84.208  96.698  88.944  1.00  8.15           C  
ATOM   3248  CE2 PHE A 480      85.946  96.779  87.318  1.00  8.15           C  
ATOM   3249  CZ  PHE A 480      85.504  96.432  88.574  1.00  8.15           C  
ATOM   3250  N   ASP A 481      80.676  97.578  82.975  1.00 14.83           N  
ATOM   3251  CA  ASP A 481      79.658  98.235  82.161  1.00 14.83           C  
ATOM   3252  C   ASP A 481      78.243  97.949  82.652  1.00 14.83           C  
ATOM   3253  O   ASP A 481      77.342  98.767  82.436  1.00 14.83           O  
ATOM   3254  CB  ASP A 481      79.801  97.801  80.703  1.00 14.83           C  
ATOM   3255  CG  ASP A 481      80.587  98.791  79.876  1.00 14.83           C  
ATOM   3256  OD1 ASP A 481      80.990  99.838  80.424  1.00 14.83           O  
ATOM   3257  OD2 ASP A 481      80.802  98.522  78.677  1.00 14.83           O  
ATOM   3258  N   CYS A 482      78.023  96.808  83.300  1.00 17.67           N  
ATOM   3259  CA  CYS A 482      76.676  96.339  83.607  1.00 17.67           C  
ATOM   3260  C   CYS A 482      76.105  96.898  84.908  1.00 17.67           C  
ATOM   3261  O   CYS A 482      74.969  96.559  85.255  1.00 17.67           O  
ATOM   3262  CB  CYS A 482      76.657  94.809  83.653  1.00 17.67           C  
ATOM   3263  SG  CYS A 482      77.866  94.081  84.777  1.00 17.67           S  
ATOM   3264  N   TYR A 483      76.842  97.735  85.628  1.00 13.94           N  
ATOM   3265  CA  TYR A 483      76.405  98.270  86.910  1.00 13.94           C  
ATOM   3266  C   TYR A 483      75.919  99.707  86.780  1.00 13.94           C  
ATOM   3267  O   TYR A 483      76.465 100.491  86.001  1.00 13.94           O  
ATOM   3268  CB  TYR A 483      77.531  98.200  87.944  1.00 13.94           C  
ATOM   3269  CG  TYR A 483      78.247  96.872  88.010  1.00 13.94           C  
ATOM   3270  CD1 TYR A 483      77.532  95.686  88.120  1.00 13.94           C  
ATOM   3271  CD2 TYR A 483      79.630  96.798  87.941  1.00 13.94           C  
ATOM   3272  CE1 TYR A 483      78.171  94.468  88.187  1.00 13.94           C  
ATOM   3273  CE2 TYR A 483      80.282  95.581  88.005  1.00 13.94           C  
ATOM   3274  CZ  TYR A 483      79.545  94.418  88.125  1.00 13.94           C  
ATOM   3275  OH  TYR A 483      80.184  93.203  88.187  1.00 13.94           O  
ATOM   3276  N   ASP A 484      74.872 100.032  87.533  1.00 18.86           N  
ATOM   3277  CA  ASP A 484      74.370 101.390  87.654  1.00 18.86           C  
ATOM   3278  C   ASP A 484      75.085 102.128  88.783  1.00 18.86           C  
ATOM   3279  O   ASP A 484      75.594 101.525  89.730  1.00 18.86           O  
ATOM   3280  CB  ASP A 484      72.861 101.383  87.905  1.00 18.86           C  
ATOM   3281  CG  ASP A 484      72.232 102.754  87.732  1.00 18.86           C  
ATOM   3282  OD1 ASP A 484      72.867 103.627  87.104  1.00 18.86           O  
ATOM   3283  OD2 ASP A 484      71.101 102.957  88.219  1.00 18.86           O  
ATOM   3284  N   GLY A 485      75.106 103.450  88.681  1.00 15.45           N  
ATOM   3285  CA  GLY A 485      75.772 104.247  89.687  1.00 15.45           C  
ATOM   3286  C   GLY A 485      75.323 105.688  89.632  1.00 15.45           C  
ATOM   3287  O   GLY A 485      74.393 106.044  88.908  1.00 15.45           O  
ATOM   3288  N   GLY A 486      76.009 106.517  90.404  1.00 10.15           N  
ATOM   3289  CA  GLY A 486      75.681 107.921  90.529  1.00 10.15           C  
ATOM   3290  C   GLY A 486      75.380 108.315  91.965  1.00 10.15           C  
ATOM   3291  O   GLY A 486      75.208 107.484  92.853  1.00 10.15           O  
ATOM   3292  N   CYS A 487      75.325 109.627  92.166  1.00 11.38           N  
ATOM   3293  CA  CYS A 487      75.170 110.187  93.500  1.00 11.38           C  
ATOM   3294  C   CYS A 487      73.729 110.036  93.985  1.00 11.38           C  
ATOM   3295  O   CYS A 487      72.777 110.098  93.204  1.00 11.38           O  
ATOM   3296  CB  CYS A 487      75.587 111.660  93.497  1.00 11.38           C  
ATOM   3297  SG  CYS A 487      77.360 111.957  93.151  1.00 11.38           S  
ATOM   3298  N   ILE A 488      73.576 109.837  95.296  1.00  9.64           N  
ATOM   3299  CA  ILE A 488      72.272 109.694  95.930  1.00  9.64           C  
ATOM   3300  C   ILE A 488      72.151 110.726  97.044  1.00  9.64           C  
ATOM   3301  O   ILE A 488      73.125 111.370  97.434  1.00  9.64           O  
ATOM   3302  CB  ILE A 488      72.032 108.271  96.485  1.00  9.64           C  
ATOM   3303  CG1 ILE A 488      72.967 107.991  97.666  1.00  9.64           C  
ATOM   3304  CG2 ILE A 488      72.179 107.232  95.389  1.00  9.64           C  
ATOM   3305  CD1 ILE A 488      72.876 106.589  98.208  1.00  9.64           C  
ATOM   3306  N   ASN A 489      70.926 110.903  97.530  1.00 13.16           N  
ATOM   3307  CA  ASN A 489      70.675 111.814  98.635  1.00 13.16           C  
ATOM   3308  C   ASN A 489      70.966 111.139  99.973  1.00 13.16           C  
ATOM   3309  O   ASN A 489      71.018 109.914 100.083  1.00 13.16           O  
ATOM   3310  CB  ASN A 489      69.234 112.320  98.602  1.00 13.16           C  
ATOM   3311  CG  ASN A 489      68.953 113.192  97.398  1.00 13.16           C  
ATOM   3312  OD1 ASN A 489      68.012 112.948  96.645  1.00 13.16           O  
ATOM   3313  ND2 ASN A 489      69.765 114.225  97.217  1.00 13.16           N  
ATOM   3314  N   ALA A 490      71.164 111.967 101.000  1.00 15.40           N  
ATOM   3315  CA  ALA A 490      71.476 111.441 102.325  1.00 15.40           C  
ATOM   3316  C   ALA A 490      70.305 110.675 102.922  1.00 15.40           C  
ATOM   3317  O   ALA A 490      70.504 109.814 103.786  1.00 15.40           O  
ATOM   3318  CB  ALA A 490      71.888 112.576 103.260  1.00 15.40           C  
ATOM   3319  N   ASN A 491      69.082 110.977 102.485  1.00 18.01           N  
ATOM   3320  CA  ASN A 491      67.898 110.339 103.045  1.00 18.01           C  
ATOM   3321  C   ASN A 491      67.721 108.903 102.572  1.00 18.01           C  
ATOM   3322  O   ASN A 491      66.856 108.199 103.102  1.00 18.01           O  
ATOM   3323  CB  ASN A 491      66.654 111.174 102.719  1.00 18.01           C  
ATOM   3324  CG  ASN A 491      66.087 110.886 101.342  1.00 18.01           C  
ATOM   3325  OD1 ASN A 491      65.427 109.872 101.126  1.00 18.01           O  
ATOM   3326  ND2 ASN A 491      66.331 111.791 100.405  1.00 18.01           N  
ATOM   3327  N   GLN A 492      68.514 108.452 101.602  1.00 14.59           N  
ATOM   3328  CA  GLN A 492      68.401 107.099 101.074  1.00 14.59           C  
ATOM   3329  C   GLN A 492      69.690 106.300 101.213  1.00 14.59           C  
ATOM   3330  O   GLN A 492      69.827 105.249 100.578  1.00 14.59           O  
ATOM   3331  CB  GLN A 492      67.947 107.146  99.613  1.00 14.59           C  
ATOM   3332  CG  GLN A 492      68.912 107.835  98.685  1.00 14.59           C  
ATOM   3333  CD  GLN A 492      68.229 108.369  97.445  1.00 14.59           C  
ATOM   3334  OE1 GLN A 492      68.561 107.989  96.325  1.00 14.59           O  
ATOM   3335  NE2 GLN A 492      67.263 109.255  97.640  1.00 14.59           N  
ATOM   3336  N   VAL A 493      70.638 106.771 102.023  1.00 11.54           N  
ATOM   3337  CA  VAL A 493      71.831 105.992 102.329  1.00 11.54           C  
ATOM   3338  C   VAL A 493      71.479 104.875 103.303  1.00 11.54           C  
ATOM   3339  O   VAL A 493      70.748 105.084 104.280  1.00 11.54           O  
ATOM   3340  CB  VAL A 493      72.929 106.912 102.893  1.00 11.54           C  
ATOM   3341  CG1 VAL A 493      74.026 106.107 103.559  1.00 11.54           C  
ATOM   3342  CG2 VAL A 493      73.506 107.777 101.791  1.00 11.54           C  
ATOM   3343  N   ILE A 494      71.994 103.677 103.040  1.00 14.94           N  
ATOM   3344  CA  ILE A 494      71.810 102.523 103.913  1.00 14.94           C  
ATOM   3345  C   ILE A 494      73.088 102.325 104.714  1.00 14.94           C  
ATOM   3346  O   ILE A 494      74.147 102.038 104.143  1.00 14.94           O  
ATOM   3347  CB  ILE A 494      71.469 101.256 103.111  1.00 14.94           C  
ATOM   3348  CG1 ILE A 494      70.466 101.560 101.999  1.00 14.94           C  
ATOM   3349  CG2 ILE A 494      70.938 100.171 104.030  1.00 14.94           C  
ATOM   3350  CD1 ILE A 494      69.105 101.983 102.497  1.00 14.94           C  
ATOM   3351  N   VAL A 495      72.999 102.466 106.032  1.00 21.83           N  
ATOM   3352  CA  VAL A 495      74.144 102.295 106.917  1.00 21.83           C  
ATOM   3353  C   VAL A 495      73.920 101.010 107.701  1.00 21.83           C  
ATOM   3354  O   VAL A 495      72.952 100.898 108.464  1.00 21.83           O  
ATOM   3355  CB  VAL A 495      74.332 103.493 107.855  1.00 21.83           C  
ATOM   3356  CG1 VAL A 495      75.281 103.123 108.977  1.00 21.83           C  
ATOM   3357  CG2 VAL A 495      74.829 104.701 107.085  1.00 21.83           C  
ATOM   3358  N   ASN A 496      74.817 100.039 107.516  1.00 29.75           N  
ATOM   3359  CA  ASN A 496      74.598  98.706 108.071  1.00 29.75           C  
ATOM   3360  C   ASN A 496      74.632  98.706 109.594  1.00 29.75           C  
ATOM   3361  O   ASN A 496      73.808  98.046 110.236  1.00 29.75           O  
ATOM   3362  CB  ASN A 496      75.639  97.735 107.519  1.00 29.75           C  
ATOM   3363  CG  ASN A 496      75.225  97.131 106.197  1.00 29.75           C  
ATOM   3364  OD1 ASN A 496      74.067  97.233 105.790  1.00 29.75           O  
ATOM   3365  ND2 ASN A 496      76.169  96.490 105.518  1.00 29.75           N  
ATOM   3366  N   ASN A 497      75.571  99.435 110.193  1.00 35.40           N  
ATOM   3367  CA  ASN A 497      75.774  99.358 111.638  1.00 35.40           C  
ATOM   3368  C   ASN A 497      76.161 100.738 112.148  1.00 35.40           C  
ATOM   3369  O   ASN A 497      77.205 101.272 111.765  1.00 35.40           O  
ATOM   3370  CB  ASN A 497      76.844  98.324 111.982  1.00 35.40           C  
ATOM   3371  CG  ASN A 497      76.567  97.611 113.292  1.00 35.40           C  
ATOM   3372  OD1 ASN A 497      75.510  97.008 113.472  1.00 35.40           O  
ATOM   3373  ND2 ASN A 497      77.520  97.673 114.212  1.00 35.40           N  
ATOM   3374  N   LEU A 498      75.318 101.310 113.007  1.00 36.25           N  
ATOM   3375  CA  LEU A 498      75.574 102.618 113.594  1.00 36.25           C  
ATOM   3376  C   LEU A 498      76.402 102.559 114.869  1.00 36.25           C  
ATOM   3377  O   LEU A 498      77.010 103.568 115.239  1.00 36.25           O  
ATOM   3378  CB  LEU A 498      74.250 103.326 113.898  1.00 36.25           C  
ATOM   3379  CG  LEU A 498      73.394 103.793 112.724  1.00 36.25           C  
ATOM   3380  CD1 LEU A 498      72.171 104.524 113.223  1.00 36.25           C  
ATOM   3381  CD2 LEU A 498      74.212 104.723 111.869  1.00 36.25           C  
ATOM   3382  N   ASP A 499      76.444 101.416 115.547  1.00 39.44           N  
ATOM   3383  CA  ASP A 499      77.140 101.303 116.829  1.00 39.44           C  
ATOM   3384  C   ASP A 499      78.608 100.928 116.651  1.00 39.44           C  
ATOM   3385  O   ASP A 499      79.092  99.961 117.235  1.00 39.44           O  
ATOM   3386  CB  ASP A 499      76.425 100.293 117.718  1.00 39.44           C  
ATOM   3387  CG  ASP A 499      74.970 100.649 117.951  1.00 39.44           C  
ATOM   3388  OD1 ASP A 499      74.533 101.710 117.461  1.00 39.44           O  
ATOM   3389  OD2 ASP A 499      74.266  99.874 118.632  1.00 39.44           O  
ATOM   3390  N   LYS A 500      79.335 101.701 115.848  1.00 35.74           N  
ATOM   3391  CA  LYS A 500      80.750 101.451 115.623  1.00 35.74           C  
ATOM   3392  C   LYS A 500      81.506 102.773 115.592  1.00 35.74           C  
ATOM   3393  O   LYS A 500      80.912 103.854 115.573  1.00 35.74           O  
ATOM   3394  CB  LYS A 500      80.981 100.646 114.340  1.00 35.74           C  
ATOM   3395  CG  LYS A 500      80.870  99.149 114.573  1.00 35.74           C  
ATOM   3396  CD  LYS A 500      81.154  98.345 113.324  1.00 35.74           C  
ATOM   3397  CE  LYS A 500      81.007  96.860 113.594  1.00 35.74           C  
ATOM   3398  NZ  LYS A 500      81.035  96.573 115.055  1.00 35.74           N  
ATOM   3399  N   SER A 501      82.834 102.666 115.598  1.00 33.70           N  
ATOM   3400  CA  SER A 501      83.691 103.823 115.822  1.00 33.70           C  
ATOM   3401  C   SER A 501      83.561 104.852 114.707  1.00 33.70           C  
ATOM   3402  O   SER A 501      83.449 104.509 113.527  1.00 33.70           O  
ATOM   3403  CB  SER A 501      85.147 103.379 115.945  1.00 33.70           C  
ATOM   3404  OG  SER A 501      85.287 102.382 116.940  1.00 33.70           O  
ATOM   3405  N   ALA A 502      83.581 106.125 115.097  1.00 23.19           N  
ATOM   3406  CA  ALA A 502      83.575 107.247 114.171  1.00 23.19           C  
ATOM   3407  C   ALA A 502      84.974 107.745 113.832  1.00 23.19           C  
ATOM   3408  O   ALA A 502      85.105 108.708 113.072  1.00 23.19           O  
ATOM   3409  CB  ALA A 502      82.748 108.399 114.747  1.00 23.19           C  
ATOM   3410  N   GLY A 503      86.016 107.119 114.373  1.00 22.23           N  
ATOM   3411  CA  GLY A 503      87.375 107.538 114.107  1.00 22.23           C  
ATOM   3412  C   GLY A 503      87.785 108.741 114.934  1.00 22.23           C  
ATOM   3413  O   GLY A 503      87.016 109.302 115.713  1.00 22.23           O  
ATOM   3414  N   PHE A 504      89.036 109.146 114.745  1.00 19.58           N  
ATOM   3415  CA  PHE A 504      89.664 110.234 115.485  1.00 19.58           C  
ATOM   3416  C   PHE A 504      89.355 111.573 114.821  1.00 19.58           C  
ATOM   3417  O   PHE A 504      89.399 111.678 113.592  1.00 19.58           O  
ATOM   3418  CB  PHE A 504      91.177 110.029 115.549  1.00 19.58           C  
ATOM   3419  CG  PHE A 504      91.904 111.058 116.368  1.00 19.58           C  
ATOM   3420  CD1 PHE A 504      92.117 110.860 117.718  1.00 19.58           C  
ATOM   3421  CD2 PHE A 504      92.391 112.214 115.785  1.00 19.58           C  
ATOM   3422  CE1 PHE A 504      92.787 111.800 118.469  1.00 19.58           C  
ATOM   3423  CE2 PHE A 504      93.062 113.154 116.534  1.00 19.58           C  
ATOM   3424  CZ  PHE A 504      93.261 112.946 117.876  1.00 19.58           C  
ATOM   3425  N   PRO A 505      89.038 112.622 115.596  1.00 22.19           N  
ATOM   3426  CA  PRO A 505      88.856 112.635 117.047  1.00 22.19           C  
ATOM   3427  C   PRO A 505      87.420 112.350 117.465  1.00 22.19           C  
ATOM   3428  O   PRO A 505      87.082 112.485 118.638  1.00 22.19           O  
ATOM   3429  CB  PRO A 505      89.250 114.060 117.419  1.00 22.19           C  
ATOM   3430  CG  PRO A 505      88.730 114.847 116.281  1.00 22.19           C  
ATOM   3431  CD  PRO A 505      88.978 113.988 115.051  1.00 22.19           C  
ATOM   3432  N   PHE A 506      86.581 111.982 116.495  1.00 21.15           N  
ATOM   3433  CA  PHE A 506      85.159 111.797 116.763  1.00 21.15           C  
ATOM   3434  C   PHE A 506      84.898 110.629 117.704  1.00 21.15           C  
ATOM   3435  O   PHE A 506      83.898 110.633 118.428  1.00 21.15           O  
ATOM   3436  CB  PHE A 506      84.412 111.609 115.447  1.00 21.15           C  
ATOM   3437  CG  PHE A 506      84.612 112.737 114.482  1.00 21.15           C  
ATOM   3438  CD1 PHE A 506      84.242 114.025 114.821  1.00 21.15           C  
ATOM   3439  CD2 PHE A 506      85.190 112.516 113.248  1.00 21.15           C  
ATOM   3440  CE1 PHE A 506      84.429 115.066 113.940  1.00 21.15           C  
ATOM   3441  CE2 PHE A 506      85.377 113.552 112.362  1.00 21.15           C  
ATOM   3442  CZ  PHE A 506      84.998 114.828 112.709  1.00 21.15           C  
ATOM   3443  N   ASN A 507      85.779 109.629 117.721  1.00 24.55           N  
ATOM   3444  CA  ASN A 507      85.609 108.511 118.640  1.00 24.55           C  
ATOM   3445  C   ASN A 507      85.781 108.918 120.095  1.00 24.55           C  
ATOM   3446  O   ASN A 507      85.465 108.124 120.987  1.00 24.55           O  
ATOM   3447  CB  ASN A 507      86.578 107.377 118.278  1.00 24.55           C  
ATOM   3448  CG  ASN A 507      88.042 107.768 118.424  1.00 24.55           C  
ATOM   3449  OD1 ASN A 507      88.383 108.756 119.070  1.00 24.55           O  
ATOM   3450  ND2 ASN A 507      88.917 106.986 117.807  1.00 24.55           N  
ATOM   3451  N   LYS A 508      86.277 110.128 120.349  1.00 28.32           N  
ATOM   3452  CA  LYS A 508      86.458 110.608 121.710  1.00 28.32           C  
ATOM   3453  C   LYS A 508      85.135 110.917 122.399  1.00 28.32           C  
ATOM   3454  O   LYS A 508      85.089 110.953 123.632  1.00 28.32           O  
ATOM   3455  CB  LYS A 508      87.352 111.848 121.694  1.00 28.32           C  
ATOM   3456  CG  LYS A 508      87.911 112.263 123.037  1.00 28.32           C  
ATOM   3457  CD  LYS A 508      89.401 112.535 122.925  1.00 28.32           C  
ATOM   3458  CE  LYS A 508      89.705 113.485 121.779  1.00 28.32           C  
ATOM   3459  NZ  LYS A 508      91.168 113.700 121.619  1.00 28.32           N  
ATOM   3460  N   TRP A 509      84.058 111.129 121.641  1.00 30.97           N  
ATOM   3461  CA  TRP A 509      82.776 111.490 122.234  1.00 30.97           C  
ATOM   3462  C   TRP A 509      81.604 110.600 121.838  1.00 30.97           C  
ATOM   3463  O   TRP A 509      80.593 110.615 122.548  1.00 30.97           O  
ATOM   3464  CB  TRP A 509      82.410 112.945 121.896  1.00 30.97           C  
ATOM   3465  CG  TRP A 509      83.561 113.905 121.934  1.00 30.97           C  
ATOM   3466  CD1 TRP A 509      84.208 114.360 123.044  1.00 30.97           C  
ATOM   3467  CD2 TRP A 509      84.161 114.576 120.819  1.00 30.97           C  
ATOM   3468  NE1 TRP A 509      85.195 115.244 122.688  1.00 30.97           N  
ATOM   3469  CE2 TRP A 509      85.184 115.397 121.327  1.00 30.97           C  
ATOM   3470  CE3 TRP A 509      83.941 114.550 119.440  1.00 30.97           C  
ATOM   3471  CZ2 TRP A 509      85.984 116.185 120.506  1.00 30.97           C  
ATOM   3472  CZ3 TRP A 509      84.737 115.333 118.627  1.00 30.97           C  
ATOM   3473  CH2 TRP A 509      85.745 116.139 119.162  1.00 30.97           C  
ATOM   3474  N   GLY A 510      81.685 109.840 120.751  1.00 28.64           N  
ATOM   3475  CA  GLY A 510      80.538 109.031 120.375  1.00 28.64           C  
ATOM   3476  C   GLY A 510      80.836 108.102 119.220  1.00 28.64           C  
ATOM   3477  O   GLY A 510      81.910 108.143 118.614  1.00 28.64           O  
ATOM   3478  N   LYS A 511      79.858 107.245 118.939  1.00 32.06           N  
ATOM   3479  CA  LYS A 511      79.877 106.330 117.808  1.00 32.06           C  
ATOM   3480  C   LYS A 511      79.237 106.987 116.586  1.00 32.06           C  
ATOM   3481  O   LYS A 511      78.762 108.123 116.636  1.00 32.06           O  
ATOM   3482  CB  LYS A 511      79.143 105.035 118.157  1.00 32.06           C  
ATOM   3483  CG  LYS A 511      79.311 104.582 119.601  1.00 32.06           C  
ATOM   3484  CD  LYS A 511      80.732 104.147 119.910  1.00 32.06           C  
ATOM   3485  CE  LYS A 511      81.078 102.857 119.192  1.00 32.06           C  
ATOM   3486  NZ  LYS A 511      82.545 102.624 119.139  1.00 32.06           N  
ATOM   3487  N   ALA A 512      79.232 106.251 115.470  1.00 29.07           N  
ATOM   3488  CA  ALA A 512      78.628 106.756 114.240  1.00 29.07           C  
ATOM   3489  C   ALA A 512      77.148 107.075 114.415  1.00 29.07           C  
ATOM   3490  O   ALA A 512      76.613 107.950 113.721  1.00 29.07           O  
ATOM   3491  CB  ALA A 512      78.819 105.741 113.113  1.00 29.07           C  
ATOM   3492  N   ARG A 513      76.468 106.362 115.319  1.00 34.07           N  
ATOM   3493  CA  ARG A 513      75.071 106.660 115.621  1.00 34.07           C  
ATOM   3494  C   ARG A 513      74.889 108.111 116.039  1.00 34.07           C  
ATOM   3495  O   ARG A 513      73.940 108.774 115.609  1.00 34.07           O  
ATOM   3496  CB  ARG A 513      74.563 105.726 116.721  1.00 34.07           C  
ATOM   3497  CG  ARG A 513      73.087 105.894 117.050  1.00 34.07           C  
ATOM   3498  CD  ARG A 513      72.583 104.804 117.986  1.00 34.07           C  
ATOM   3499  NE  ARG A 513      72.738 103.468 117.426  1.00 34.07           N  
ATOM   3500  CZ  ARG A 513      71.911 102.938 116.530  1.00 34.07           C  
ATOM   3501  NH1 ARG A 513      70.863 103.629 116.103  1.00 34.07           N  
ATOM   3502  NH2 ARG A 513      72.124 101.715 116.067  1.00 34.07           N  
ATOM   3503  N   LEU A 514      75.800 108.624 116.869  1.00 28.52           N  
ATOM   3504  CA  LEU A 514      75.678 109.991 117.364  1.00 28.52           C  
ATOM   3505  C   LEU A 514      75.673 110.991 116.218  1.00 28.52           C  
ATOM   3506  O   LEU A 514      74.840 111.901 116.174  1.00 28.52           O  
ATOM   3507  CB  LEU A 514      76.825 110.292 118.329  1.00 28.52           C  
ATOM   3508  CG  LEU A 514      77.036 111.722 118.835  1.00 28.52           C  
ATOM   3509  CD1 LEU A 514      75.728 112.392 119.220  1.00 28.52           C  
ATOM   3510  CD2 LEU A 514      78.005 111.729 120.000  1.00 28.52           C  
ATOM   3511  N   TYR A 515      76.592 110.828 115.272  1.00 26.55           N  
ATOM   3512  CA  TYR A 515      76.742 111.816 114.213  1.00 26.55           C  
ATOM   3513  C   TYR A 515      75.687 111.652 113.126  1.00 26.55           C  
ATOM   3514  O   TYR A 515      75.272 112.641 112.514  1.00 26.55           O  
ATOM   3515  CB  TYR A 515      78.162 111.752 113.652  1.00 26.55           C  
ATOM   3516  CG  TYR A 515      79.197 111.955 114.737  1.00 26.55           C  
ATOM   3517  CD1 TYR A 515      79.651 113.225 115.054  1.00 26.55           C  
ATOM   3518  CD2 TYR A 515      79.698 110.883 115.461  1.00 26.55           C  
ATOM   3519  CE1 TYR A 515      80.579 113.421 116.050  1.00 26.55           C  
ATOM   3520  CE2 TYR A 515      80.626 111.071 116.459  1.00 26.55           C  
ATOM   3521  CZ  TYR A 515      81.065 112.342 116.749  1.00 26.55           C  
ATOM   3522  OH  TYR A 515      81.995 112.538 117.741  1.00 26.55           O  
ATOM   3523  N   TYR A 516      75.239 110.422 112.864  1.00 24.31           N  
ATOM   3524  CA  TYR A 516      74.122 110.259 111.939  1.00 24.31           C  
ATOM   3525  C   TYR A 516      72.810 110.766 112.530  1.00 24.31           C  
ATOM   3526  O   TYR A 516      71.935 111.215 111.783  1.00 24.31           O  
ATOM   3527  CB  TYR A 516      73.990 108.801 111.509  1.00 24.31           C  
ATOM   3528  CG  TYR A 516      74.848 108.449 110.320  1.00 24.31           C  
ATOM   3529  CD1 TYR A 516      74.441 108.775 109.037  1.00 24.31           C  
ATOM   3530  CD2 TYR A 516      76.061 107.798 110.475  1.00 24.31           C  
ATOM   3531  CE1 TYR A 516      75.214 108.464 107.942  1.00 24.31           C  
ATOM   3532  CE2 TYR A 516      76.843 107.483 109.384  1.00 24.31           C  
ATOM   3533  CZ  TYR A 516      76.413 107.816 108.120  1.00 24.31           C  
ATOM   3534  OH  TYR A 516      77.180 107.504 107.023  1.00 24.31           O  
ATOM   3535  N   ASP A 517      72.648 110.705 113.854  1.00 34.50           N  
ATOM   3536  CA  ASP A 517      71.431 111.226 114.466  1.00 34.50           C  
ATOM   3537  C   ASP A 517      71.466 112.744 114.599  1.00 34.50           C  
ATOM   3538  O   ASP A 517      70.447 113.410 114.388  1.00 34.50           O  
ATOM   3539  CB  ASP A 517      71.216 110.586 115.837  1.00 34.50           C  
ATOM   3540  CG  ASP A 517      70.908 109.106 115.748  1.00 34.50           C  
ATOM   3541  OD1 ASP A 517      70.633 108.620 114.632  1.00 34.50           O  
ATOM   3542  OD2 ASP A 517      70.942 108.429 116.796  1.00 34.50           O  
ATOM   3543  N   SER A 518      72.624 113.305 114.953  1.00 34.55           N  
ATOM   3544  CA  SER A 518      72.710 114.739 115.207  1.00 34.55           C  
ATOM   3545  C   SER A 518      72.560 115.553 113.930  1.00 34.55           C  
ATOM   3546  O   SER A 518      71.977 116.643 113.958  1.00 34.55           O  
ATOM   3547  CB  SER A 518      74.035 115.069 115.888  1.00 34.55           C  
ATOM   3548  OG  SER A 518      74.026 114.659 117.243  1.00 34.55           O  
ATOM   3549  N   MET A 519      73.074 115.050 112.811  1.00 32.85           N  
ATOM   3550  CA  MET A 519      73.010 115.776 111.552  1.00 32.85           C  
ATOM   3551  C   MET A 519      71.694 115.492 110.840  1.00 32.85           C  
ATOM   3552  O   MET A 519      71.332 114.332 110.626  1.00 32.85           O  
ATOM   3553  CB  MET A 519      74.182 115.387 110.653  1.00 32.85           C  
ATOM   3554  CG  MET A 519      75.551 115.644 111.249  1.00 32.85           C  
ATOM   3555  SD  MET A 519      76.854 115.585 110.006  1.00 32.85           S  
ATOM   3556  CE  MET A 519      76.853 117.280 109.433  1.00 32.85           C  
ATOM   3557  N   SER A 520      70.981 116.552 110.476  1.00 30.39           N  
ATOM   3558  CA  SER A 520      69.809 116.398 109.631  1.00 30.39           C  
ATOM   3559  C   SER A 520      70.233 116.029 108.211  1.00 30.39           C  
ATOM   3560  O   SER A 520      71.409 116.096 107.848  1.00 30.39           O  
ATOM   3561  CB  SER A 520      68.976 117.680 109.625  1.00 30.39           C  
ATOM   3562  OG  SER A 520      69.793 118.823 109.450  1.00 30.39           O  
ATOM   3563  N   TYR A 521      69.253 115.614 107.406  1.00 25.99           N  
ATOM   3564  CA  TYR A 521      69.549 115.261 106.022  1.00 25.99           C  
ATOM   3565  C   TYR A 521      70.054 116.458 105.227  1.00 25.99           C  
ATOM   3566  O   TYR A 521      70.907 116.299 104.346  1.00 25.99           O  
ATOM   3567  CB  TYR A 521      68.316 114.659 105.351  1.00 25.99           C  
ATOM   3568  CG  TYR A 521      67.903 113.324 105.922  1.00 25.99           C  
ATOM   3569  CD1 TYR A 521      68.853 112.381 106.280  1.00 25.99           C  
ATOM   3570  CD2 TYR A 521      66.565 113.007 106.103  1.00 25.99           C  
ATOM   3571  CE1 TYR A 521      68.484 111.160 106.799  1.00 25.99           C  
ATOM   3572  CE2 TYR A 521      66.186 111.787 106.620  1.00 25.99           C  
ATOM   3573  CZ  TYR A 521      67.150 110.867 106.968  1.00 25.99           C  
ATOM   3574  OH  TYR A 521      66.781 109.650 107.486  1.00 25.99           O  
ATOM   3575  N   GLU A 522      69.560 117.661 105.527  1.00 29.27           N  
ATOM   3576  CA  GLU A 522      70.051 118.842 104.829  1.00 29.27           C  
ATOM   3577  C   GLU A 522      71.481 119.186 105.222  1.00 29.27           C  
ATOM   3578  O   GLU A 522      72.254 119.633 104.369  1.00 29.27           O  
ATOM   3579  CB  GLU A 522      69.132 120.036 105.093  1.00 29.27           C  
ATOM   3580  CG  GLU A 522      67.684 119.825 104.667  1.00 29.27           C  
ATOM   3581  CD  GLU A 522      66.848 119.138 105.732  1.00 29.27           C  
ATOM   3582  OE1 GLU A 522      66.307 118.047 105.455  1.00 29.27           O  
ATOM   3583  OE2 GLU A 522      66.732 119.691 106.846  1.00 29.27           O  
ATOM   3584  N   ASP A 523      71.865 118.945 106.477  1.00 27.52           N  
ATOM   3585  CA  ASP A 523      73.252 119.145 106.881  1.00 27.52           C  
ATOM   3586  C   ASP A 523      74.176 118.132 106.219  1.00 27.52           C  
ATOM   3587  O   ASP A 523      75.283 118.480 105.796  1.00 27.52           O  
ATOM   3588  CB  ASP A 523      73.374 119.059 108.402  1.00 27.52           C  
ATOM   3589  CG  ASP A 523      73.126 120.390 109.083  1.00 27.52           C  
ATOM   3590  OD1 ASP A 523      73.086 121.421 108.378  1.00 27.52           O  
ATOM   3591  OD2 ASP A 523      72.973 120.406 110.322  1.00 27.52           O  
ATOM   3592  N   GLN A 524      73.739 116.875 106.122  1.00 21.95           N  
ATOM   3593  CA  GLN A 524      74.528 115.864 105.428  1.00 21.95           C  
ATOM   3594  C   GLN A 524      74.687 116.211 103.954  1.00 21.95           C  
ATOM   3595  O   GLN A 524      75.773 116.056 103.383  1.00 21.95           O  
ATOM   3596  CB  GLN A 524      73.869 114.498 105.593  1.00 21.95           C  
ATOM   3597  CG  GLN A 524      74.089 113.865 106.949  1.00 21.95           C  
ATOM   3598  CD  GLN A 524      73.299 112.588 107.125  1.00 21.95           C  
ATOM   3599  OE1 GLN A 524      73.183 111.784 106.204  1.00 21.95           O  
ATOM   3600  NE2 GLN A 524      72.750 112.394 108.314  1.00 21.95           N  
ATOM   3601  N   ASP A 525      73.613 116.689 103.322  1.00 22.29           N  
ATOM   3602  CA  ASP A 525      73.691 117.094 101.923  1.00 22.29           C  
ATOM   3603  C   ASP A 525      74.601 118.300 101.729  1.00 22.29           C  
ATOM   3604  O   ASP A 525      75.314 118.375 100.724  1.00 22.29           O  
ATOM   3605  CB  ASP A 525      72.294 117.395 101.388  1.00 22.29           C  
ATOM   3606  CG  ASP A 525      71.428 116.158 101.305  1.00 22.29           C  
ATOM   3607  OD1 ASP A 525      71.991 115.047 101.241  1.00 22.29           O  
ATOM   3608  OD2 ASP A 525      70.187 116.293 101.295  1.00 22.29           O  
ATOM   3609  N   ALA A 526      74.594 119.246 102.671  1.00 18.08           N  
ATOM   3610  CA  ALA A 526      75.477 120.402 102.567  1.00 18.08           C  
ATOM   3611  C   ALA A 526      76.930 120.037 102.833  1.00 18.08           C  
ATOM   3612  O   ALA A 526      77.832 120.679 102.287  1.00 18.08           O  
ATOM   3613  CB  ALA A 526      75.028 121.497 103.533  1.00 18.08           C  
ATOM   3614  N   LEU A 527      77.179 119.033 103.674  1.00 14.93           N  
ATOM   3615  CA  LEU A 527      78.536 118.520 103.826  1.00 14.93           C  
ATOM   3616  C   LEU A 527      79.009 117.820 102.558  1.00 14.93           C  
ATOM   3617  O   LEU A 527      80.161 117.985 102.145  1.00 14.93           O  
ATOM   3618  CB  LEU A 527      78.612 117.568 105.018  1.00 14.93           C  
ATOM   3619  CG  LEU A 527      80.022 117.166 105.455  1.00 14.93           C  
ATOM   3620  CD1 LEU A 527      80.729 118.309 106.153  1.00 14.93           C  
ATOM   3621  CD2 LEU A 527      79.975 115.940 106.344  1.00 14.93           C  
ATOM   3622  N   PHE A 528      78.139 117.020 101.939  1.00 10.14           N  
ATOM   3623  CA  PHE A 528      78.510 116.355 100.695  1.00 10.14           C  
ATOM   3624  C   PHE A 528      78.772 117.361  99.582  1.00 10.14           C  
ATOM   3625  O   PHE A 528      79.727 117.208  98.813  1.00 10.14           O  
ATOM   3626  CB  PHE A 528      77.425 115.361 100.287  1.00 10.14           C  
ATOM   3627  CG  PHE A 528      77.760 114.571  99.058  1.00 10.14           C  
ATOM   3628  CD1 PHE A 528      78.878 113.762  99.021  1.00 10.14           C  
ATOM   3629  CD2 PHE A 528      76.936 114.609  97.954  1.00 10.14           C  
ATOM   3630  CE1 PHE A 528      79.184 113.036  97.895  1.00 10.14           C  
ATOM   3631  CE2 PHE A 528      77.232 113.876  96.833  1.00 10.14           C  
ATOM   3632  CZ  PHE A 528      78.359 113.092  96.801  1.00 10.14           C  
ATOM   3633  N   ALA A 529      77.928 118.389  99.470  1.00 11.14           N  
ATOM   3634  CA  ALA A 529      78.141 119.415  98.455  1.00 11.14           C  
ATOM   3635  C   ALA A 529      79.433 120.184  98.695  1.00 11.14           C  
ATOM   3636  O   ALA A 529      80.058 120.664  97.744  1.00 11.14           O  
ATOM   3637  CB  ALA A 529      76.954 120.375  98.419  1.00 11.14           C  
ATOM   3638  N   TYR A 530      79.838 120.319  99.956  1.00 12.28           N  
ATOM   3639  CA  TYR A 530      81.059 121.047 100.276  1.00 12.28           C  
ATOM   3640  C   TYR A 530      82.295 120.294  99.795  1.00 12.28           C  
ATOM   3641  O   TYR A 530      83.277 120.912  99.372  1.00 12.28           O  
ATOM   3642  CB  TYR A 530      81.111 121.307 101.783  1.00 12.28           C  
ATOM   3643  CG  TYR A 530      82.386 121.927 102.296  1.00 12.28           C  
ATOM   3644  CD1 TYR A 530      82.525 123.304 102.369  1.00 12.28           C  
ATOM   3645  CD2 TYR A 530      83.433 121.141 102.749  1.00 12.28           C  
ATOM   3646  CE1 TYR A 530      83.680 123.879 102.848  1.00 12.28           C  
ATOM   3647  CE2 TYR A 530      84.592 121.708 103.231  1.00 12.28           C  
ATOM   3648  CZ  TYR A 530      84.710 123.076 103.280  1.00 12.28           C  
ATOM   3649  OH  TYR A 530      85.865 123.643 103.760  1.00 12.28           O  
ATOM   3650  N   THR A 531      82.269 118.960  99.851  1.00  8.84           N  
ATOM   3651  CA  THR A 531      83.394 118.163  99.375  1.00  8.84           C  
ATOM   3652  C   THR A 531      83.497 118.116  97.857  1.00  8.84           C  
ATOM   3653  O   THR A 531      84.505 117.625  97.343  1.00  8.84           O  
ATOM   3654  CB  THR A 531      83.318 116.737  99.926  1.00  8.84           C  
ATOM   3655  OG1 THR A 531      82.246 116.029  99.296  1.00  8.84           O  
ATOM   3656  CG2 THR A 531      83.122 116.745 101.424  1.00  8.84           C  
ATOM   3657  N   LYS A 532      82.496 118.599  97.131  1.00  8.44           N  
ATOM   3658  CA  LYS A 532      82.630 118.748  95.689  1.00  8.44           C  
ATOM   3659  C   LYS A 532      83.310 120.050  95.304  1.00  8.44           C  
ATOM   3660  O   LYS A 532      83.513 120.301  94.113  1.00  8.44           O  
ATOM   3661  CB  LYS A 532      81.264 118.661  95.011  1.00  8.44           C  
ATOM   3662  CG  LYS A 532      80.494 117.399  95.315  1.00  8.44           C  
ATOM   3663  CD  LYS A 532      79.474 117.140  94.232  1.00  8.44           C  
ATOM   3664  CE  LYS A 532      78.665 115.898  94.512  1.00  8.44           C  
ATOM   3665  NZ  LYS A 532      77.320 115.968  93.889  1.00  8.44           N  
ATOM   3666  N   ARG A 533      83.802 120.837  96.251  1.00  9.90           N  
ATOM   3667  CA  ARG A 533      84.421 122.140  95.947  1.00  9.90           C  
ATOM   3668  C   ARG A 533      85.608 122.363  96.880  1.00  9.90           C  
ATOM   3669  O   ARG A 533      86.343 123.279  96.641  1.00  9.90           O  
ATOM   3670  CB  ARG A 533      83.399 123.276  96.025  1.00  9.90           C  
ATOM   3671  CG  ARG A 533      82.060 123.026  95.354  1.00  9.90           C  
ATOM   3672  CD  ARG A 533      81.637 124.267  94.609  1.00  9.90           C  
ATOM   3673  NE  ARG A 533      81.981 125.469  95.347  1.00  9.90           N  
ATOM   3674  CZ  ARG A 533      82.144 126.662  94.793  1.00  9.90           C  
ATOM   3675  NH1 ARG A 533      82.464 127.703  95.539  1.00  9.90           N  
ATOM   3676  NH2 ARG A 533      81.999 126.811  93.492  1.00  9.90           N  
ATOM   3677  N   ASN A 534      85.782 121.525  97.898  1.00  9.92           N  
ATOM   3678  CA  ASN A 534      86.851 121.729  98.861  1.00  9.92           C  
ATOM   3679  C   ASN A 534      87.401 120.374  99.280  1.00  9.92           C  
ATOM   3680  O   ASN A 534      86.678 119.376  99.300  1.00  9.92           O  
ATOM   3681  CB  ASN A 534      86.342 122.490 100.088  1.00  9.92           C  
ATOM   3682  CG  ASN A 534      85.706 123.814  99.728  1.00  9.92           C  
ATOM   3683  OD1 ASN A 534      86.388 124.817  99.554  1.00  9.92           O  
ATOM   3684  ND2 ASN A 534      84.389 123.815  99.594  1.00  9.92           N  
ATOM   3685  N   VAL A 535      88.682 120.348  99.622  1.00  7.69           N  
ATOM   3686  CA  VAL A 535      89.330 119.141 100.121  1.00  7.69           C  
ATOM   3687  C   VAL A 535      89.303 119.152 101.643  1.00  7.69           C  
ATOM   3688  O   VAL A 535      89.714 120.133 102.273  1.00  7.69           O  
ATOM   3689  CB  VAL A 535      90.769 119.029  99.593  1.00  7.69           C  
ATOM   3690  CG1 VAL A 535      91.470 117.842 100.219  1.00  7.69           C  
ATOM   3691  CG2 VAL A 535      90.764 118.893  98.089  1.00  7.69           C  
ATOM   3692  N   ILE A 536      88.813 118.069 102.232  1.00  9.82           N  
ATOM   3693  CA  ILE A 536      88.826 117.882 103.683  1.00  9.82           C  
ATOM   3694  C   ILE A 536      89.838 116.786 103.996  1.00  9.82           C  
ATOM   3695  O   ILE A 536      89.565 115.608 103.710  1.00  9.82           O  
ATOM   3696  CB  ILE A 536      87.438 117.518 104.222  1.00  9.82           C  
ATOM   3697  CG1 ILE A 536      86.504 118.720 104.172  1.00  9.82           C  
ATOM   3698  CG2 ILE A 536      87.535 117.043 105.661  1.00  9.82           C  
ATOM   3699  CD1 ILE A 536      85.059 118.331 104.088  1.00  9.82           C  
ATOM   3700  N   PRO A 537      91.007 117.109 104.543  1.00 12.44           N  
ATOM   3701  CA  PRO A 537      91.896 116.059 105.047  1.00 12.44           C  
ATOM   3702  C   PRO A 537      91.409 115.518 106.383  1.00 12.44           C  
ATOM   3703  O   PRO A 537      90.849 116.249 107.203  1.00 12.44           O  
ATOM   3704  CB  PRO A 537      93.245 116.771 105.178  1.00 12.44           C  
ATOM   3705  CG  PRO A 537      92.900 118.190 105.399  1.00 12.44           C  
ATOM   3706  CD  PRO A 537      91.590 118.452 104.700  1.00 12.44           C  
ATOM   3707  N   THR A 538      91.626 114.222 106.597  1.00 14.00           N  
ATOM   3708  CA  THR A 538      91.178 113.548 107.807  1.00 14.00           C  
ATOM   3709  C   THR A 538      92.302 112.672 108.345  1.00 14.00           C  
ATOM   3710  O   THR A 538      93.298 112.414 107.666  1.00 14.00           O  
ATOM   3711  CB  THR A 538      89.922 112.702 107.558  1.00 14.00           C  
ATOM   3712  OG1 THR A 538      90.137 111.842 106.434  1.00 14.00           O  
ATOM   3713  CG2 THR A 538      88.713 113.589 107.289  1.00 14.00           C  
ATOM   3714  N   ILE A 539      92.130 112.213 109.583  1.00 15.44           N  
ATOM   3715  CA  ILE A 539      93.108 111.384 110.278  1.00 15.44           C  
ATOM   3716  C   ILE A 539      92.552 109.973 110.403  1.00 15.44           C  
ATOM   3717  O   ILE A 539      91.445 109.777 110.916  1.00 15.44           O  
ATOM   3718  CB  ILE A 539      93.450 111.957 111.664  1.00 15.44           C  
ATOM   3719  CG1 ILE A 539      94.299 113.220 111.533  1.00 15.44           C  
ATOM   3720  CG2 ILE A 539      94.170 110.922 112.509  1.00 15.44           C  
ATOM   3721  CD1 ILE A 539      93.993 114.260 112.580  1.00 15.44           C  
ATOM   3722  N   THR A 540      93.315 108.993 109.926  1.00 17.89           N  
ATOM   3723  CA  THR A 540      92.963 107.592 110.104  1.00 17.89           C  
ATOM   3724  C   THR A 540      93.649 107.022 111.343  1.00 17.89           C  
ATOM   3725  O   THR A 540      94.824 107.290 111.598  1.00 17.89           O  
ATOM   3726  CB  THR A 540      93.355 106.790 108.863  1.00 17.89           C  
ATOM   3727  OG1 THR A 540      92.518 107.170 107.764  1.00 17.89           O  
ATOM   3728  CG2 THR A 540      93.195 105.311 109.109  1.00 17.89           C  
ATOM   3729  N   GLN A 541      92.907 106.235 112.114  1.00 25.73           N  
ATOM   3730  CA  GLN A 541      93.424 105.582 113.308  1.00 25.73           C  
ATOM   3731  C   GLN A 541      93.630 104.098 113.044  1.00 25.73           C  
ATOM   3732  O   GLN A 541      92.780 103.443 112.435  1.00 25.73           O  
ATOM   3733  CB  GLN A 541      92.469 105.770 114.485  1.00 25.73           C  
ATOM   3734  CG  GLN A 541      93.063 105.399 115.823  1.00 25.73           C  
ATOM   3735  CD  GLN A 541      92.262 105.951 116.976  1.00 25.73           C  
ATOM   3736  OE1 GLN A 541      91.049 106.125 116.874  1.00 25.73           O  
ATOM   3737  NE2 GLN A 541      92.937 106.238 118.081  1.00 25.73           N  
ATOM   3738  N   MET A 542      94.760 103.568 113.501  1.00 30.80           N  
ATOM   3739  CA  MET A 542      95.111 102.172 113.276  1.00 30.80           C  
ATOM   3740  C   MET A 542      95.042 101.396 114.583  1.00 30.80           C  
ATOM   3741  O   MET A 542      95.593 101.829 115.599  1.00 30.80           O  
ATOM   3742  CB  MET A 542      96.501 102.046 112.658  1.00 30.80           C  
ATOM   3743  CG  MET A 542      96.527 102.331 111.169  1.00 30.80           C  
ATOM   3744  SD  MET A 542      97.711 101.279 110.322  1.00 30.80           S  
ATOM   3745  CE  MET A 542      99.162 101.585 111.316  1.00 30.80           C  
ATOM   3746  N   ASN A 543      94.367 100.249 114.548  1.00 35.85           N  
ATOM   3747  CA  ASN A 543      94.150  99.421 115.725  1.00 35.85           C  
ATOM   3748  C   ASN A 543      94.515  97.976 115.417  1.00 35.85           C  
ATOM   3749  O   ASN A 543      94.301  97.498 114.300  1.00 35.85           O  
ATOM   3750  CB  ASN A 543      92.691  99.495 116.189  1.00 35.85           C  
ATOM   3751  CG  ASN A 543      92.164 100.914 116.231  1.00 35.85           C  
ATOM   3752  OD1 ASN A 543      92.520 101.696 117.111  1.00 35.85           O  
ATOM   3753  ND2 ASN A 543      91.309 101.255 115.273  1.00 35.85           N  
ATOM   3754  N   LEU A 544      95.064  97.290 116.415  1.00 30.19           N  
ATOM   3755  CA  LEU A 544      95.382  95.874 116.289  1.00 30.19           C  
ATOM   3756  C   LEU A 544      94.118  95.022 116.330  1.00 30.19           C  
ATOM   3757  O   LEU A 544      93.193  95.290 117.101  1.00 30.19           O  
ATOM   3758  CB  LEU A 544      96.334  95.457 117.410  1.00 30.19           C  
ATOM   3759  CG  LEU A 544      97.756  96.014 117.354  1.00 30.19           C  
ATOM   3760  CD1 LEU A 544      98.524  95.671 118.606  1.00 30.19           C  
ATOM   3761  CD2 LEU A 544      98.466  95.408 116.168  1.00 30.19           C  
ATOM   3762  N   LYS A 545      94.076  93.995 115.484  1.00 31.06           N  
ATOM   3763  CA  LYS A 545      92.989  93.028 115.522  1.00 31.06           C  
ATOM   3764  C   LYS A 545      93.231  91.955 116.574  1.00 31.06           C  
ATOM   3765  O   LYS A 545      94.343  91.758 117.070  1.00 31.06           O  
ATOM   3766  CB  LYS A 545      92.792  92.338 114.174  1.00 31.06           C  
ATOM   3767  CG  LYS A 545      92.323  93.221 113.051  1.00 31.06           C  
ATOM   3768  CD  LYS A 545      91.655  92.378 111.974  1.00 31.06           C  
ATOM   3769  CE  LYS A 545      90.437  91.641 112.509  1.00 31.06           C  
ATOM   3770  NZ  LYS A 545      89.591  92.494 113.386  1.00 31.06           N  
ATOM   3771  N   TYR A 546      92.155  91.248 116.899  1.00 30.97           N  
ATOM   3772  CA  TYR A 546      92.185  90.068 117.751  1.00 30.97           C  
ATOM   3773  C   TYR A 546      91.509  88.963 116.950  1.00 30.97           C  
ATOM   3774  O   TYR A 546      90.278  88.927 116.858  1.00 30.97           O  
ATOM   3775  CB  TYR A 546      91.466  90.353 119.069  1.00 30.97           C  
ATOM   3776  CG  TYR A 546      91.691  89.357 120.181  1.00 30.97           C  
ATOM   3777  CD1 TYR A 546      92.661  88.371 120.083  1.00 30.97           C  
ATOM   3778  CD2 TYR A 546      90.951  89.433 121.352  1.00 30.97           C  
ATOM   3779  CE1 TYR A 546      92.870  87.472 121.112  1.00 30.97           C  
ATOM   3780  CE2 TYR A 546      91.152  88.542 122.385  1.00 30.97           C  
ATOM   3781  CZ  TYR A 546      92.111  87.564 122.261  1.00 30.97           C  
ATOM   3782  OH  TYR A 546      92.306  86.679 123.295  1.00 30.97           O  
ATOM   3783  N   ALA A 547      92.306  88.078 116.350  1.00 24.09           N  
ATOM   3784  CA  ALA A 547      91.773  87.125 115.384  1.00 24.09           C  
ATOM   3785  C   ALA A 547      92.676  85.904 115.295  1.00 24.09           C  
ATOM   3786  O   ALA A 547      93.889  86.005 115.488  1.00 24.09           O  
ATOM   3787  CB  ALA A 547      91.624  87.765 114.000  1.00 24.09           C  
ATOM   3788  N   ILE A 548      92.068  84.753 114.998  1.00 22.54           N  
ATOM   3789  CA  ILE A 548      92.806  83.500 114.901  1.00 22.54           C  
ATOM   3790  C   ILE A 548      93.559  83.445 113.580  1.00 22.54           C  
ATOM   3791  O   ILE A 548      93.118  84.004 112.567  1.00 22.54           O  
ATOM   3792  CB  ILE A 548      91.847  82.305 115.060  1.00 22.54           C  
ATOM   3793  CG1 ILE A 548      92.577  81.097 115.641  1.00 22.54           C  
ATOM   3794  CG2 ILE A 548      91.215  81.927 113.737  1.00 22.54           C  
ATOM   3795  CD1 ILE A 548      91.651  80.035 116.167  1.00 22.54           C  
ATOM   3796  N   SER A 549      94.721  82.795 113.589  1.00 22.74           N  
ATOM   3797  CA  SER A 549      95.504  82.644 112.372  1.00 22.74           C  
ATOM   3798  C   SER A 549      96.536  81.546 112.559  1.00 22.74           C  
ATOM   3799  O   SER A 549      96.806  81.103 113.678  1.00 22.74           O  
ATOM   3800  CB  SER A 549      96.197  83.950 111.981  1.00 22.74           C  
ATOM   3801  OG  SER A 549      97.196  83.722 111.004  1.00 22.74           O  
ATOM   3802  N   ALA A 550      97.102  81.107 111.436  1.00 23.93           N  
ATOM   3803  CA  ALA A 550      98.247  80.208 111.438  1.00 23.93           C  
ATOM   3804  C   ALA A 550      99.581  80.945 111.436  1.00 23.93           C  
ATOM   3805  O   ALA A 550     100.626  80.297 111.545  1.00 23.93           O  
ATOM   3806  CB  ALA A 550      98.182  79.268 110.233  1.00 23.93           C  
ATOM   3807  N   LYS A 551      99.571  82.270 111.312  1.00 30.57           N  
ATOM   3808  CA  LYS A 551     100.780  83.064 111.146  1.00 30.57           C  
ATOM   3809  C   LYS A 551     100.996  83.969 112.352  1.00 30.57           C  
ATOM   3810  O   LYS A 551     100.038  84.472 112.946  1.00 30.57           O  
ATOM   3811  CB  LYS A 551     100.708  83.907 109.872  1.00 30.57           C  
ATOM   3812  CG  LYS A 551     100.216  83.141 108.656  1.00 30.57           C  
ATOM   3813  CD  LYS A 551     101.029  83.479 107.421  1.00 30.57           C  
ATOM   3814  CE  LYS A 551     100.265  83.149 106.151  1.00 30.57           C  
ATOM   3815  NZ  LYS A 551     101.146  83.181 104.952  1.00 30.57           N  
ATOM   3816  N   ASN A 552     102.268  84.164 112.707  1.00 33.09           N  
ATOM   3817  CA  ASN A 552     102.643  84.986 113.852  1.00 33.09           C  
ATOM   3818  C   ASN A 552     102.364  86.470 113.641  1.00 33.09           C  
ATOM   3819  O   ASN A 552     102.342  87.225 114.618  1.00 33.09           O  
ATOM   3820  CB  ASN A 552     104.124  84.771 114.164  1.00 33.09           C  
ATOM   3821  CG  ASN A 552     104.530  85.351 115.496  1.00 33.09           C  
ATOM   3822  OD1 ASN A 552     103.734  85.407 116.432  1.00 33.09           O  
ATOM   3823  ND2 ASN A 552     105.778  85.774 115.594  1.00 33.09           N  
ATOM   3824  N   ARG A 553     102.151  86.899 112.398  1.00 36.45           N  
ATOM   3825  CA  ARG A 553     101.998  88.316 112.087  1.00 36.45           C  
ATOM   3826  C   ARG A 553     100.863  88.965 112.873  1.00 36.45           C  
ATOM   3827  O   ARG A 553      99.785  88.388 113.036  1.00 36.45           O  
ATOM   3828  CB  ARG A 553     101.742  88.498 110.592  1.00 36.45           C  
ATOM   3829  CG  ARG A 553     102.960  88.344 109.709  1.00 36.45           C  
ATOM   3830  CD  ARG A 553     102.673  88.807 108.283  1.00 36.45           C  
ATOM   3831  NE  ARG A 553     102.070  90.140 108.239  1.00 36.45           N  
ATOM   3832  CZ  ARG A 553     100.769  90.374 108.090  1.00 36.45           C  
ATOM   3833  NH1 ARG A 553      99.922  89.362 107.964  1.00 36.45           N  
ATOM   3834  NH2 ARG A 553     100.315  91.620 108.066  1.00 36.45           N  
ATOM   3835  N   ALA A 554     101.087  90.202 113.322  1.00 30.50           N  
ATOM   3836  CA  ALA A 554     100.005  90.960 113.989  1.00 30.50           C  
ATOM   3837  C   ALA A 554      99.261  91.735 112.900  1.00 30.50           C  
ATOM   3838  O   ALA A 554      99.940  92.340 112.047  1.00 30.50           O  
ATOM   3839  CB  ALA A 554     100.609  91.917 114.977  1.00 30.50           C  
ATOM   3840  N   ARG A 555      97.927  91.742 112.943  1.00 31.47           N  
ATOM   3841  CA  ARG A 555      97.144  92.435 111.889  1.00 31.47           C  
ATOM   3842  C   ARG A 555      96.526  93.712 112.464  1.00 31.47           C  
ATOM   3843  O   ARG A 555      95.900  93.628 113.533  1.00 31.47           O  
ATOM   3844  CB  ARG A 555      96.055  91.521 111.326  1.00 31.47           C  
ATOM   3845  CG  ARG A 555      95.487  92.021 110.005  1.00 31.47           C  
ATOM   3846  CD  ARG A 555      94.374  91.178 109.415  1.00 31.47           C  
ATOM   3847  NE  ARG A 555      94.083  91.601 108.052  1.00 31.47           N  
ATOM   3848  CZ  ARG A 555      93.434  92.714 107.731  1.00 31.47           C  
ATOM   3849  NH1 ARG A 555      93.004  93.527 108.680  1.00 31.47           N  
ATOM   3850  NH2 ARG A 555      93.219  93.014 106.463  1.00 31.47           N  
ATOM   3851  N   THR A 556      96.698  94.844 111.774  1.00 32.96           N  
ATOM   3852  CA  THR A 556      96.060  96.109 112.218  1.00 32.96           C  
ATOM   3853  C   THR A 556      94.923  96.470 111.262  1.00 32.96           C  
ATOM   3854  O   THR A 556      94.976  96.037 110.094  1.00 32.96           O  
ATOM   3855  CB  THR A 556      97.020  97.306 112.224  1.00 32.96           C  
ATOM   3856  OG1 THR A 556      97.679  97.380 110.960  1.00 32.96           O  
ATOM   3857  CG2 THR A 556      98.017  97.294 113.360  1.00 32.96           C  
ATOM   3858  N   VAL A 557      93.918  97.197 111.753  1.00 30.01           N  
ATOM   3859  CA  VAL A 557      92.820  97.676 110.864  1.00 30.01           C  
ATOM   3860  C   VAL A 557      92.799  99.205 110.906  1.00 30.01           C  
ATOM   3861  O   VAL A 557      93.086  99.766 111.978  1.00 30.01           O  
ATOM   3862  CB  VAL A 557      91.453  97.068 111.225  1.00 30.01           C  
ATOM   3863  CG1 VAL A 557      91.287  95.689 110.616  1.00 30.01           C  
ATOM   3864  CG2 VAL A 557      91.219  97.035 112.726  1.00 30.01           C  
ATOM   3865  N   ALA A 558      92.529  99.844 109.767  1.00 23.96           N  
ATOM   3866  CA  ALA A 558      92.542 101.319 109.693  1.00 23.96           C  
ATOM   3867  C   ALA A 558      91.130 101.871 109.890  1.00 23.96           C  
ATOM   3868  O   ALA A 558      90.273 101.592 109.043  1.00 23.96           O  
ATOM   3869  CB  ALA A 558      93.120 101.737 108.371  1.00 23.96           C  
ATOM   3870  N   GLY A 559      90.904 102.628 110.967  1.00 20.75           N  
ATOM   3871  CA  GLY A 559      89.614 103.248 111.203  1.00 20.75           C  
ATOM   3872  C   GLY A 559      89.520 104.660 110.662  1.00 20.75           C  
ATOM   3873  O   GLY A 559      90.213 105.560 111.142  1.00 20.75           O  
ATOM   3874  N   VAL A 560      88.667 104.870 109.662  1.00 19.04           N  
ATOM   3875  CA  VAL A 560      88.566 106.174 109.017  1.00 19.04           C  
ATOM   3876  C   VAL A 560      87.544 107.049 109.742  1.00 19.04           C  
ATOM   3877  O   VAL A 560      86.691 106.572 110.495  1.00 19.04           O  
ATOM   3878  CB  VAL A 560      88.222 106.021 107.526  1.00 19.04           C  
ATOM   3879  CG1 VAL A 560      89.236 105.120 106.847  1.00 19.04           C  
ATOM   3880  CG2 VAL A 560      86.831 105.455 107.362  1.00 19.04           C  
ATOM   3881  N   SER A 561      87.649 108.358 109.513  1.00 17.75           N  
ATOM   3882  CA  SER A 561      86.772 109.325 110.161  1.00 17.75           C  
ATOM   3883  C   SER A 561      85.348 109.226 109.632  1.00 17.75           C  
ATOM   3884  O   SER A 561      85.120 108.881 108.470  1.00 17.75           O  
ATOM   3885  CB  SER A 561      87.294 110.744 109.948  1.00 17.75           C  
ATOM   3886  OG  SER A 561      88.550 110.932 110.568  1.00 17.75           O  
ATOM   3887  N   ILE A 562      84.382 109.533 110.503  1.00 17.74           N  
ATOM   3888  CA  ILE A 562      82.978 109.555 110.098  1.00 17.74           C  
ATOM   3889  C   ILE A 562      82.743 110.599 109.017  1.00 17.74           C  
ATOM   3890  O   ILE A 562      81.872 110.429 108.155  1.00 17.74           O  
ATOM   3891  CB  ILE A 562      82.068 109.787 111.326  1.00 17.74           C  
ATOM   3892  CG1 ILE A 562      80.594 109.615 110.955  1.00 17.74           C  
ATOM   3893  CG2 ILE A 562      82.283 111.166 111.912  1.00 17.74           C  
ATOM   3894  CD1 ILE A 562      80.230 108.218 110.524  1.00 17.74           C  
ATOM   3895  N   CYS A 563      83.512 111.691 109.038  1.00 15.71           N  
ATOM   3896  CA  CYS A 563      83.348 112.742 108.038  1.00 15.71           C  
ATOM   3897  C   CYS A 563      83.639 112.220 106.637  1.00 15.71           C  
ATOM   3898  O   CYS A 563      82.932 112.554 105.680  1.00 15.71           O  
ATOM   3899  CB  CYS A 563      84.258 113.923 108.375  1.00 15.71           C  
ATOM   3900  SG  CYS A 563      84.082 115.362 107.303  1.00 15.71           S  
ATOM   3901  N   SER A 564      84.675 111.394 106.499  1.00 13.29           N  
ATOM   3902  CA  SER A 564      85.003 110.806 105.208  1.00 13.29           C  
ATOM   3903  C   SER A 564      84.013 109.716 104.819  1.00 13.29           C  
ATOM   3904  O   SER A 564      83.576 109.653 103.664  1.00 13.29           O  
ATOM   3905  CB  SER A 564      86.423 110.243 105.245  1.00 13.29           C  
ATOM   3906  OG  SER A 564      86.740 109.581 104.035  1.00 13.29           O  
ATOM   3907  N   THR A 565      83.655 108.856 105.774  1.00 13.46           N  
ATOM   3908  CA  THR A 565      82.752 107.745 105.495  1.00 13.46           C  
ATOM   3909  C   THR A 565      81.391 108.245 105.029  1.00 13.46           C  
ATOM   3910  O   THR A 565      80.797 107.692 104.097  1.00 13.46           O  
ATOM   3911  CB  THR A 565      82.598 106.876 106.743  1.00 13.46           C  
ATOM   3912  OG1 THR A 565      83.887 106.582 107.284  1.00 13.46           O  
ATOM   3913  CG2 THR A 565      81.910 105.577 106.400  1.00 13.46           C  
ATOM   3914  N   MET A 566      80.877 109.289 105.679  1.00 14.20           N  
ATOM   3915  CA  MET A 566      79.528 109.762 105.392  1.00 14.20           C  
ATOM   3916  C   MET A 566      79.401 110.252 103.956  1.00 14.20           C  
ATOM   3917  O   MET A 566      78.405 109.967 103.283  1.00 14.20           O  
ATOM   3918  CB  MET A 566      79.152 110.859 106.386  1.00 14.20           C  
ATOM   3919  CG  MET A 566      77.864 111.585 106.081  1.00 14.20           C  
ATOM   3920  SD  MET A 566      77.456 112.750 107.389  1.00 14.20           S  
ATOM   3921  CE  MET A 566      77.554 111.682 108.822  1.00 14.20           C  
ATOM   3922  N   THR A 567      80.398 110.990 103.467  1.00 10.64           N  
ATOM   3923  CA  THR A 567      80.365 111.457 102.085  1.00 10.64           C  
ATOM   3924  C   THR A 567      80.736 110.361 101.094  1.00 10.64           C  
ATOM   3925  O   THR A 567      80.216 110.348  99.970  1.00 10.64           O  
ATOM   3926  CB  THR A 567      81.292 112.660 101.910  1.00 10.64           C  
ATOM   3927  OG1 THR A 567      82.638 112.279 102.216  1.00 10.64           O  
ATOM   3928  CG2 THR A 567      80.873 113.794 102.820  1.00 10.64           C  
ATOM   3929  N   ASN A 568      81.612 109.430 101.478  1.00 10.95           N  
ATOM   3930  CA  ASN A 568      81.953 108.349 100.561  1.00 10.95           C  
ATOM   3931  C   ASN A 568      80.776 107.417 100.323  1.00 10.95           C  
ATOM   3932  O   ASN A 568      80.620 106.901  99.214  1.00 10.95           O  
ATOM   3933  CB  ASN A 568      83.157 107.569 101.084  1.00 10.95           C  
ATOM   3934  CG  ASN A 568      84.472 108.182 100.661  1.00 10.95           C  
ATOM   3935  OD1 ASN A 568      84.559 109.384 100.417  1.00 10.95           O  
ATOM   3936  ND2 ASN A 568      85.504 107.358 100.566  1.00 10.95           N  
ATOM   3937  N   ARG A 569      79.944 107.180 101.339  1.00 10.26           N  
ATOM   3938  CA  ARG A 569      78.730 106.399 101.114  1.00 10.26           C  
ATOM   3939  C   ARG A 569      77.798 107.103 100.140  1.00 10.26           C  
ATOM   3940  O   ARG A 569      77.226 106.469  99.247  1.00 10.26           O  
ATOM   3941  CB  ARG A 569      78.015 106.129 102.435  1.00 10.26           C  
ATOM   3942  CG  ARG A 569      78.868 105.435 103.464  1.00 10.26           C  
ATOM   3943  CD  ARG A 569      78.083 104.380 104.205  1.00 10.26           C  
ATOM   3944  NE  ARG A 569      78.895 103.706 105.212  1.00 10.26           N  
ATOM   3945  CZ  ARG A 569      78.859 103.984 106.510  1.00 10.26           C  
ATOM   3946  NH1 ARG A 569      78.067 104.944 106.959  1.00 10.26           N  
ATOM   3947  NH2 ARG A 569      79.628 103.317 107.356  1.00 10.26           N  
ATOM   3948  N   GLN A 570      77.664 108.421 100.277  1.00  8.60           N  
ATOM   3949  CA  GLN A 570      76.758 109.177  99.424  1.00  8.60           C  
ATOM   3950  C   GLN A 570      77.287 109.280  97.999  1.00  8.60           C  
ATOM   3951  O   GLN A 570      76.513 109.511  97.065  1.00  8.60           O  
ATOM   3952  CB  GLN A 570      76.532 110.558 100.038  1.00  8.60           C  
ATOM   3953  CG  GLN A 570      75.254 111.238  99.618  1.00  8.60           C  
ATOM   3954  CD  GLN A 570      74.886 112.386 100.529  1.00  8.60           C  
ATOM   3955  OE1 GLN A 570      75.200 112.373 101.717  1.00  8.60           O  
ATOM   3956  NE2 GLN A 570      74.202 113.381  99.983  1.00  8.60           N  
ATOM   3957  N   PHE A 571      78.599 109.117  97.817  1.00  7.46           N  
ATOM   3958  CA  PHE A 571      79.176 109.061  96.475  1.00  7.46           C  
ATOM   3959  C   PHE A 571      79.112 107.669  95.852  1.00  7.46           C  
ATOM   3960  O   PHE A 571      78.800 107.540  94.664  1.00  7.46           O  
ATOM   3961  CB  PHE A 571      80.623 109.549  96.506  1.00  7.46           C  
ATOM   3962  CG  PHE A 571      81.124 110.040  95.180  1.00  7.46           C  
ATOM   3963  CD1 PHE A 571      80.654 111.214  94.627  1.00  7.46           C  
ATOM   3964  CD2 PHE A 571      82.091 109.326  94.494  1.00  7.46           C  
ATOM   3965  CE1 PHE A 571      81.119 111.648  93.402  1.00  7.46           C  
ATOM   3966  CE2 PHE A 571      82.562 109.760  93.276  1.00  7.46           C  
ATOM   3967  CZ  PHE A 571      82.080 110.924  92.730  1.00  7.46           C  
ATOM   3968  N   HIS A 572      79.417 106.621  96.617  1.00  7.68           N  
ATOM   3969  CA  HIS A 572      79.703 105.316  96.033  1.00  7.68           C  
ATOM   3970  C   HIS A 572      78.634 104.255  96.253  1.00  7.68           C  
ATOM   3971  O   HIS A 572      78.661 103.240  95.553  1.00  7.68           O  
ATOM   3972  CB  HIS A 572      81.035 104.777  96.569  1.00  7.68           C  
ATOM   3973  CG  HIS A 572      82.238 105.393  95.931  1.00  7.68           C  
ATOM   3974  ND1 HIS A 572      82.425 105.428  94.568  1.00  7.68           N  
ATOM   3975  CD2 HIS A 572      83.303 106.029  96.473  1.00  7.68           C  
ATOM   3976  CE1 HIS A 572      83.563 106.040  94.298  1.00  7.68           C  
ATOM   3977  NE2 HIS A 572      84.115 106.416  95.437  1.00  7.68           N  
ATOM   3978  N   GLN A 573      77.705 104.443  97.193  1.00  9.30           N  
ATOM   3979  CA  GLN A 573      76.905 103.310  97.652  1.00  9.30           C  
ATOM   3980  C   GLN A 573      76.019 102.723  96.560  1.00  9.30           C  
ATOM   3981  O   GLN A 573      75.763 101.516  96.569  1.00  9.30           O  
ATOM   3982  CB  GLN A 573      76.054 103.714  98.850  1.00  9.30           C  
ATOM   3983  CG  GLN A 573      75.849 102.581  99.825  1.00  9.30           C  
ATOM   3984  CD  GLN A 573      74.760 102.865 100.821  1.00  9.30           C  
ATOM   3985  OE1 GLN A 573      73.723 103.430 100.480  1.00  9.30           O  
ATOM   3986  NE2 GLN A 573      74.984 102.471 102.066  1.00  9.30           N  
ATOM   3987  N   LYS A 574      75.537 103.542  95.623  1.00 16.74           N  
ATOM   3988  CA  LYS A 574      74.681 103.023  94.559  1.00 16.74           C  
ATOM   3989  C   LYS A 574      75.418 101.998  93.702  1.00 16.74           C  
ATOM   3990  O   LYS A 574      74.889 100.915  93.416  1.00 16.74           O  
ATOM   3991  CB  LYS A 574      74.177 104.182  93.703  1.00 16.74           C  
ATOM   3992  CG  LYS A 574      73.195 103.801  92.621  1.00 16.74           C  
ATOM   3993  CD  LYS A 574      72.133 104.865  92.479  1.00 16.74           C  
ATOM   3994  CE  LYS A 574      71.770 105.092  91.028  1.00 16.74           C  
ATOM   3995  NZ  LYS A 574      70.968 106.333  90.863  1.00 16.74           N  
ATOM   3996  N   LEU A 575      76.656 102.307  93.316  1.00  8.44           N  
ATOM   3997  CA  LEU A 575      77.450 101.373  92.529  1.00  8.44           C  
ATOM   3998  C   LEU A 575      77.851 100.149  93.339  1.00  8.44           C  
ATOM   3999  O   LEU A 575      77.871  99.033  92.811  1.00  8.44           O  
ATOM   4000  CB  LEU A 575      78.688 102.072  91.980  1.00  8.44           C  
ATOM   4001  CG  LEU A 575      79.591 101.196  91.113  1.00  8.44           C  
ATOM   4002  CD1 LEU A 575      79.092 101.129  89.692  1.00  8.44           C  
ATOM   4003  CD2 LEU A 575      81.003 101.723  91.160  1.00  8.44           C  
ATOM   4004  N   LEU A 576      78.202 100.335  94.611  1.00  7.27           N  
ATOM   4005  CA  LEU A 576      78.595  99.189  95.423  1.00  7.27           C  
ATOM   4006  C   LEU A 576      77.428  98.230  95.612  1.00  7.27           C  
ATOM   4007  O   LEU A 576      77.597  97.009  95.516  1.00  7.27           O  
ATOM   4008  CB  LEU A 576      79.131  99.657  96.773  1.00  7.27           C  
ATOM   4009  CG  LEU A 576      80.336 100.601  96.787  1.00  7.27           C  
ATOM   4010  CD1 LEU A 576      81.066 100.514  98.115  1.00  7.27           C  
ATOM   4011  CD2 LEU A 576      81.288 100.331  95.631  1.00  7.27           C  
ATOM   4012  N   LYS A 577      76.232  98.769  95.855  1.00  9.07           N  
ATOM   4013  CA  LYS A 577      75.048  97.928  95.965  1.00  9.07           C  
ATOM   4014  C   LYS A 577      74.735  97.242  94.645  1.00  9.07           C  
ATOM   4015  O   LYS A 577      74.337  96.071  94.633  1.00  9.07           O  
ATOM   4016  CB  LYS A 577      73.851  98.764  96.417  1.00  9.07           C  
ATOM   4017  CG  LYS A 577      73.966  99.335  97.818  1.00  9.07           C  
ATOM   4018  CD  LYS A 577      73.926  98.266  98.882  1.00  9.07           C  
ATOM   4019  CE  LYS A 577      74.017  98.878 100.267  1.00  9.07           C  
ATOM   4020  NZ  LYS A 577      74.047  97.842 101.330  1.00  9.07           N  
ATOM   4021  N   SER A 578      74.924  97.944  93.525  1.00  7.48           N  
ATOM   4022  CA  SER A 578      74.653  97.338  92.226  1.00  7.48           C  
ATOM   4023  C   SER A 578      75.620  96.198  91.936  1.00  7.48           C  
ATOM   4024  O   SER A 578      75.229  95.178  91.359  1.00  7.48           O  
ATOM   4025  CB  SER A 578      74.726  98.398  91.130  1.00  7.48           C  
ATOM   4026  OG  SER A 578      74.123  97.936  89.937  1.00  7.48           O  
ATOM   4027  N   ILE A 579      76.889  96.358  92.311  1.00  8.52           N  
ATOM   4028  CA  ILE A 579      77.860  95.281  92.137  1.00  8.52           C  
ATOM   4029  C   ILE A 579      77.499  94.097  93.023  1.00  8.52           C  
ATOM   4030  O   ILE A 579      77.479  92.945  92.575  1.00  8.52           O  
ATOM   4031  CB  ILE A 579      79.287  95.779  92.429  1.00  8.52           C  
ATOM   4032  CG1 ILE A 579      79.784  96.698  91.319  1.00  8.52           C  
ATOM   4033  CG2 ILE A 579      80.233  94.609  92.589  1.00  8.52           C  
ATOM   4034  CD1 ILE A 579      80.996  97.510  91.702  1.00  8.52           C  
ATOM   4035  N   ALA A 580      77.208  94.362  94.298  1.00  8.31           N  
ATOM   4036  CA  ALA A 580      76.921  93.285  95.235  1.00  8.31           C  
ATOM   4037  C   ALA A 580      75.608  92.576  94.933  1.00  8.31           C  
ATOM   4038  O   ALA A 580      75.395  91.464  95.424  1.00  8.31           O  
ATOM   4039  CB  ALA A 580      76.907  93.819  96.665  1.00  8.31           C  
ATOM   4040  N   ALA A 581      74.719  93.188  94.151  1.00  9.07           N  
ATOM   4041  CA  ALA A 581      73.456  92.551  93.803  1.00  9.07           C  
ATOM   4042  C   ALA A 581      73.517  91.720  92.527  1.00  9.07           C  
ATOM   4043  O   ALA A 581      72.585  90.953  92.265  1.00  9.07           O  
ATOM   4044  CB  ALA A 581      72.356  93.606  93.660  1.00  9.07           C  
ATOM   4045  N   THR A 582      74.574  91.849  91.732  1.00 10.94           N  
ATOM   4046  CA  THR A 582      74.639  91.195  90.433  1.00 10.94           C  
ATOM   4047  C   THR A 582      75.169  89.770  90.560  1.00 10.94           C  
ATOM   4048  O   THR A 582      76.064  89.486  91.361  1.00 10.94           O  
ATOM   4049  CB  THR A 582      75.519  92.012  89.481  1.00 10.94           C  
ATOM   4050  OG1 THR A 582      74.862  93.244  89.165  1.00 10.94           O  
ATOM   4051  CG2 THR A 582      75.794  91.260  88.192  1.00 10.94           C  
ATOM   4052  N   ARG A 583      74.603  88.867  89.759  1.00 11.74           N  
ATOM   4053  CA  ARG A 583      75.039  87.480  89.705  1.00 11.74           C  
ATOM   4054  C   ARG A 583      75.517  87.134  88.303  1.00 11.74           C  
ATOM   4055  O   ARG A 583      75.030  87.681  87.309  1.00 11.74           O  
ATOM   4056  CB  ARG A 583      73.920  86.516  90.108  1.00 11.74           C  
ATOM   4057  CG  ARG A 583      73.168  86.922  91.353  1.00 11.74           C  
ATOM   4058  CD  ARG A 583      73.821  86.366  92.598  1.00 11.74           C  
ATOM   4059  NE  ARG A 583      73.392  87.105  93.778  1.00 11.74           N  
ATOM   4060  CZ  ARG A 583      74.099  88.066  94.358  1.00 11.74           C  
ATOM   4061  NH1 ARG A 583      73.623  88.682  95.428  1.00 11.74           N  
ATOM   4062  NH2 ARG A 583      75.278  88.415  93.870  1.00 11.74           N  
ATOM   4063  N   GLY A 584      76.475  86.214  88.232  1.00 16.74           N  
ATOM   4064  CA  GLY A 584      77.005  85.760  86.964  1.00 16.74           C  
ATOM   4065  C   GLY A 584      78.054  86.648  86.339  1.00 16.74           C  
ATOM   4066  O   GLY A 584      78.456  86.391  85.200  1.00 16.74           O  
ATOM   4067  N   ALA A 585      78.514  87.679  87.042  1.00 10.70           N  
ATOM   4068  CA  ALA A 585      79.508  88.600  86.518  1.00 10.70           C  
ATOM   4069  C   ALA A 585      80.912  88.165  86.934  1.00 10.70           C  
ATOM   4070  O   ALA A 585      81.100  87.191  87.665  1.00 10.70           O  
ATOM   4071  CB  ALA A 585      79.207  90.021  86.988  1.00 10.70           C  
ATOM   4072  N   THR A 586      81.920  88.898  86.452  1.00  6.26           N  
ATOM   4073  CA  THR A 586      83.301  88.582  86.808  1.00  6.26           C  
ATOM   4074  C   THR A 586      83.557  88.814  88.291  1.00  6.26           C  
ATOM   4075  O   THR A 586      84.162  87.971  88.962  1.00  6.26           O  
ATOM   4076  CB  THR A 586      84.265  89.410  85.959  1.00  6.26           C  
ATOM   4077  OG1 THR A 586      84.201  88.970  84.599  1.00  6.26           O  
ATOM   4078  CG2 THR A 586      85.687  89.258  86.457  1.00  6.26           C  
ATOM   4079  N   VAL A 587      83.094  89.941  88.821  1.00  6.36           N  
ATOM   4080  CA  VAL A 587      83.220  90.235  90.244  1.00  6.36           C  
ATOM   4081  C   VAL A 587      82.114  89.496  90.984  1.00  6.36           C  
ATOM   4082  O   VAL A 587      80.930  89.650  90.668  1.00  6.36           O  
ATOM   4083  CB  VAL A 587      83.154  91.746  90.503  1.00  6.36           C  
ATOM   4084  CG1 VAL A 587      83.160  92.037  91.989  1.00  6.36           C  
ATOM   4085  CG2 VAL A 587      84.307  92.443  89.816  1.00  6.36           C  
ATOM   4086  N   VAL A 588      82.498  88.679  91.958  1.00  6.29           N  
ATOM   4087  CA  VAL A 588      81.566  87.818  92.670  1.00  6.29           C  
ATOM   4088  C   VAL A 588      81.386  88.260  94.120  1.00  6.29           C  
ATOM   4089  O   VAL A 588      80.982  87.466  94.963  1.00  6.29           O  
ATOM   4090  CB  VAL A 588      81.992  86.346  92.572  1.00  6.29           C  
ATOM   4091  CG1 VAL A 588      82.134  85.961  91.128  1.00  6.29           C  
ATOM   4092  CG2 VAL A 588      83.311  86.132  93.287  1.00  6.29           C  
ATOM   4093  N   ILE A 589      81.686  89.524  94.422  1.00  6.67           N  
ATOM   4094  CA  ILE A 589      81.351  90.075  95.728  1.00  6.67           C  
ATOM   4095  C   ILE A 589      79.839  90.064  95.893  1.00  6.67           C  
ATOM   4096  O   ILE A 589      79.097  90.451  94.983  1.00  6.67           O  
ATOM   4097  CB  ILE A 589      81.920  91.493  95.872  1.00  6.67           C  
ATOM   4098  CG1 ILE A 589      83.393  91.444  96.270  1.00  6.67           C  
ATOM   4099  CG2 ILE A 589      81.146  92.279  96.909  1.00  6.67           C  
ATOM   4100  CD1 ILE A 589      84.164  92.670  95.847  1.00  6.67           C  
ATOM   4101  N   GLY A 590      79.373  89.609  97.052  1.00  8.33           N  
ATOM   4102  CA  GLY A 590      77.962  89.575  97.346  1.00  8.33           C  
ATOM   4103  C   GLY A 590      77.261  88.285  96.988  1.00  8.33           C  
ATOM   4104  O   GLY A 590      76.115  88.087  97.401  1.00  8.33           O  
ATOM   4105  N   THR A 591      77.903  87.410  96.220  1.00  8.67           N  
ATOM   4106  CA  THR A 591      77.321  86.116  95.898  1.00  8.67           C  
ATOM   4107  C   THR A 591      77.517  85.161  97.069  1.00  8.67           C  
ATOM   4108  O   THR A 591      78.614  85.069  97.629  1.00  8.67           O  
ATOM   4109  CB  THR A 591      77.955  85.541  94.631  1.00  8.67           C  
ATOM   4110  OG1 THR A 591      77.567  86.328  93.500  1.00  8.67           O  
ATOM   4111  CG2 THR A 591      77.481  84.121  94.403  1.00  8.67           C  
ATOM   4112  N   SER A 592      76.451  84.463  97.449  1.00  9.93           N  
ATOM   4113  CA  SER A 592      76.532  83.492  98.529  1.00  9.93           C  
ATOM   4114  C   SER A 592      77.051  82.157  98.014  1.00  9.93           C  
ATOM   4115  O   SER A 592      76.734  81.736  96.899  1.00  9.93           O  
ATOM   4116  CB  SER A 592      75.163  83.300  99.180  1.00  9.93           C  
ATOM   4117  OG  SER A 592      75.282  82.656 100.434  1.00  9.93           O  
ATOM   4118  N   LYS A 593      77.865  81.495  98.836  1.00  8.19           N  
ATOM   4119  CA  LYS A 593      78.321  80.148  98.527  1.00  8.19           C  
ATOM   4120  C   LYS A 593      77.282  79.090  98.868  1.00  8.19           C  
ATOM   4121  O   LYS A 593      77.392  77.955  98.394  1.00  8.19           O  
ATOM   4122  CB  LYS A 593      79.621  79.853  99.276  1.00  8.19           C  
ATOM   4123  CG  LYS A 593      79.433  79.604 100.758  1.00  8.19           C  
ATOM   4124  CD  LYS A 593      80.718  79.139 101.404  1.00  8.19           C  
ATOM   4125  CE  LYS A 593      80.584  79.099 102.909  1.00  8.19           C  
ATOM   4126  NZ  LYS A 593      81.900  78.947 103.577  1.00  8.19           N  
ATOM   4127  N   PHE A 594      76.281  79.435  99.671  1.00 11.20           N  
ATOM   4128  CA  PHE A 594      75.271  78.492 100.116  1.00 11.20           C  
ATOM   4129  C   PHE A 594      74.185  78.313  99.059  1.00 11.20           C  
ATOM   4130  O   PHE A 594      74.023  79.126  98.146  1.00 11.20           O  
ATOM   4131  CB  PHE A 594      74.651  78.960 101.429  1.00 11.20           C  
ATOM   4132  CG  PHE A 594      75.601  78.951 102.586  1.00 11.20           C  
ATOM   4133  CD1 PHE A 594      76.049  77.760 103.117  1.00 11.20           C  
ATOM   4134  CD2 PHE A 594      76.049  80.134 103.142  1.00 11.20           C  
ATOM   4135  CE1 PHE A 594      76.920  77.749 104.183  1.00 11.20           C  
ATOM   4136  CE2 PHE A 594      76.920  80.125 104.207  1.00 11.20           C  
ATOM   4137  CZ  PHE A 594      77.355  78.933 104.726  1.00 11.20           C  
ATOM   4138  N   TYR A 595      73.432  77.223  99.209  1.00 15.07           N  
ATOM   4139  CA  TYR A 595      72.293  76.900  98.349  1.00 15.07           C  
ATOM   4140  C   TYR A 595      72.696  76.798  96.880  1.00 15.07           C  
ATOM   4141  O   TYR A 595      71.991  77.277  95.992  1.00 15.07           O  
ATOM   4142  CB  TYR A 595      71.159  77.907  98.530  1.00 15.07           C  
ATOM   4143  CG  TYR A 595      70.687  78.029  99.956  1.00 15.07           C  
ATOM   4144  CD1 TYR A 595      69.829  77.090 100.504  1.00 15.07           C  
ATOM   4145  CD2 TYR A 595      71.079  79.097 100.747  1.00 15.07           C  
ATOM   4146  CE1 TYR A 595      69.395  77.198 101.803  1.00 15.07           C  
ATOM   4147  CE2 TYR A 595      70.647  79.213 102.047  1.00 15.07           C  
ATOM   4148  CZ  TYR A 595      69.804  78.262 102.569  1.00 15.07           C  
ATOM   4149  OH  TYR A 595      69.366  78.373 103.865  1.00 15.07           O  
ATOM   4150  N   GLY A 596      73.828  76.152  96.619  1.00 10.87           N  
ATOM   4151  CA  GLY A 596      74.281  75.938  95.263  1.00 10.87           C  
ATOM   4152  C   GLY A 596      75.051  77.081  94.642  1.00 10.87           C  
ATOM   4153  O   GLY A 596      75.434  76.976  93.472  1.00 10.87           O  
ATOM   4154  N   GLY A 597      75.284  78.168  95.377  1.00  8.88           N  
ATOM   4155  CA  GLY A 597      75.974  79.312  94.802  1.00  8.88           C  
ATOM   4156  C   GLY A 597      77.391  79.000  94.360  1.00  8.88           C  
ATOM   4157  O   GLY A 597      77.851  79.497  93.331  1.00  8.88           O  
ATOM   4158  N   TRP A 598      78.108  78.192  95.144  1.00  5.69           N  
ATOM   4159  CA  TRP A 598      79.478  77.828  94.795  1.00  5.69           C  
ATOM   4160  C   TRP A 598      79.530  77.088  93.462  1.00  5.69           C  
ATOM   4161  O   TRP A 598      80.399  77.358  92.618  1.00  5.69           O  
ATOM   4162  CB  TRP A 598      80.071  76.982  95.924  1.00  5.69           C  
ATOM   4163  CG  TRP A 598      81.538  76.731  95.835  1.00  5.69           C  
ATOM   4164  CD1 TRP A 598      82.151  75.670  95.246  1.00  5.69           C  
ATOM   4165  CD2 TRP A 598      82.581  77.555  96.363  1.00  5.69           C  
ATOM   4166  NE1 TRP A 598      83.511  75.782  95.368  1.00  5.69           N  
ATOM   4167  CE2 TRP A 598      83.801  76.931  96.053  1.00  5.69           C  
ATOM   4168  CE3 TRP A 598      82.600  78.761  97.069  1.00  5.69           C  
ATOM   4169  CZ2 TRP A 598      85.030  77.473  96.419  1.00  5.69           C  
ATOM   4170  CZ3 TRP A 598      83.820  79.297  97.433  1.00  5.69           C  
ATOM   4171  CH2 TRP A 598      85.018  78.654  97.108  1.00  5.69           C  
ATOM   4172  N   HIS A 599      78.585  76.169  93.246  1.00  9.05           N  
ATOM   4173  CA  HIS A 599      78.488  75.464  91.973  1.00  9.05           C  
ATOM   4174  C   HIS A 599      78.223  76.424  90.821  1.00  9.05           C  
ATOM   4175  O   HIS A 599      78.827  76.298  89.749  1.00  9.05           O  
ATOM   4176  CB  HIS A 599      77.387  74.409  92.051  1.00  9.05           C  
ATOM   4177  CG  HIS A 599      77.396  73.441  90.911  1.00  9.05           C  
ATOM   4178  ND1 HIS A 599      78.301  72.408  90.818  1.00  9.05           N  
ATOM   4179  CD2 HIS A 599      76.609  73.351  89.814  1.00  9.05           C  
ATOM   4180  CE1 HIS A 599      78.075  71.724  89.712  1.00  9.05           C  
ATOM   4181  NE2 HIS A 599      77.052  72.275  89.085  1.00  9.05           N  
ATOM   4182  N   ASN A 600      77.321  77.387  91.019  1.00  7.44           N  
ATOM   4183  CA  ASN A 600      77.032  78.351  89.965  1.00  7.44           C  
ATOM   4184  C   ASN A 600      78.239  79.223  89.657  1.00  7.44           C  
ATOM   4185  O   ASN A 600      78.482  79.547  88.492  1.00  7.44           O  
ATOM   4186  CB  ASN A 600      75.842  79.224  90.355  1.00  7.44           C  
ATOM   4187  CG  ASN A 600      74.610  78.417  90.677  1.00  7.44           C  
ATOM   4188  OD1 ASN A 600      74.463  77.283  90.231  1.00  7.44           O  
ATOM   4189  ND2 ASN A 600      73.712  79.000  91.457  1.00  7.44           N  
ATOM   4190  N   MET A 601      79.009  79.606  90.677  1.00  7.30           N  
ATOM   4191  CA  MET A 601      80.211  80.396  90.436  1.00  7.30           C  
ATOM   4192  C   MET A 601      81.239  79.611  89.631  1.00  7.30           C  
ATOM   4193  O   MET A 601      81.860  80.152  88.705  1.00  7.30           O  
ATOM   4194  CB  MET A 601      80.809  80.856  91.764  1.00  7.30           C  
ATOM   4195  CG  MET A 601      80.106  82.043  92.386  1.00  7.30           C  
ATOM   4196  SD  MET A 601      80.333  82.097  94.171  1.00  7.30           S  
ATOM   4197  CE  MET A 601      81.860  83.013  94.298  1.00  7.30           C  
ATOM   4198  N   LEU A 602      81.434  78.332  89.962  1.00  7.58           N  
ATOM   4199  CA  LEU A 602      82.400  77.548  89.198  1.00  7.58           C  
ATOM   4200  C   LEU A 602      81.927  77.308  87.768  1.00  7.58           C  
ATOM   4201  O   LEU A 602      82.733  77.345  86.832  1.00  7.58           O  
ATOM   4202  CB  LEU A 602      82.711  76.227  89.898  1.00  7.58           C  
ATOM   4203  CG  LEU A 602      83.280  76.331  91.313  1.00  7.58           C  
ATOM   4204  CD1 LEU A 602      83.837  74.998  91.753  1.00  7.58           C  
ATOM   4205  CD2 LEU A 602      84.349  77.397  91.391  1.00  7.58           C  
ATOM   4206  N   LYS A 603      80.630  77.065  87.566  1.00  8.22           N  
ATOM   4207  CA  LYS A 603      80.142  76.898  86.198  1.00  8.22           C  
ATOM   4208  C   LYS A 603      80.153  78.210  85.426  1.00  8.22           C  
ATOM   4209  O   LYS A 603      80.198  78.198  84.192  1.00  8.22           O  
ATOM   4210  CB  LYS A 603      78.741  76.287  86.190  1.00  8.22           C  
ATOM   4211  CG  LYS A 603      78.615  74.961  86.922  1.00  8.22           C  
ATOM   4212  CD  LYS A 603      79.838  74.077  86.726  1.00  8.22           C  
ATOM   4213  CE  LYS A 603      79.815  73.378  85.376  1.00  8.22           C  
ATOM   4214  NZ  LYS A 603      78.716  72.380  85.278  1.00  8.22           N  
ATOM   4215  N   THR A 604      80.105  79.345  86.122  1.00  8.48           N  
ATOM   4216  CA  THR A 604      80.223  80.630  85.444  1.00  8.48           C  
ATOM   4217  C   THR A 604      81.659  80.885  85.001  1.00  8.48           C  
ATOM   4218  O   THR A 604      81.896  81.368  83.889  1.00  8.48           O  
ATOM   4219  CB  THR A 604      79.725  81.753  86.356  1.00  8.48           C  
ATOM   4220  OG1 THR A 604      78.309  81.635  86.526  1.00  8.48           O  
ATOM   4221  CG2 THR A 604      80.044  83.113  85.762  1.00  8.48           C  
ATOM   4222  N   VAL A 605      82.634  80.570  85.856  1.00  8.27           N  
ATOM   4223  CA  VAL A 605      84.025  80.799  85.467  1.00  8.27           C  
ATOM   4224  C   VAL A 605      84.461  79.797  84.396  1.00  8.27           C  
ATOM   4225  O   VAL A 605      85.235  80.135  83.494  1.00  8.27           O  
ATOM   4226  CB  VAL A 605      84.955  80.782  86.695  1.00  8.27           C  
ATOM   4227  CG1 VAL A 605      84.990  79.419  87.344  1.00  8.27           C  
ATOM   4228  CG2 VAL A 605      86.353  81.229  86.308  1.00  8.27           C  
ATOM   4229  N   TYR A 606      83.961  78.559  84.462  1.00  8.11           N  
ATOM   4230  CA  TYR A 606      84.306  77.550  83.459  1.00  8.11           C  
ATOM   4231  C   TYR A 606      83.732  77.863  82.080  1.00  8.11           C  
ATOM   4232  O   TYR A 606      83.856  77.039  81.170  1.00  8.11           O  
ATOM   4233  CB  TYR A 606      83.827  76.163  83.895  1.00  8.11           C  
ATOM   4234  CG  TYR A 606      84.511  75.569  85.104  1.00  8.11           C  
ATOM   4235  CD1 TYR A 606      85.513  76.249  85.776  1.00  8.11           C  
ATOM   4236  CD2 TYR A 606      84.143  74.319  85.576  1.00  8.11           C  
ATOM   4237  CE1 TYR A 606      86.130  75.699  86.879  1.00  8.11           C  
ATOM   4238  CE2 TYR A 606      84.754  73.766  86.676  1.00  8.11           C  
ATOM   4239  CZ  TYR A 606      85.744  74.457  87.322  1.00  8.11           C  
ATOM   4240  OH  TYR A 606      86.349  73.899  88.417  1.00  8.11           O  
ATOM   4241  N   SER A 607      83.150  79.049  81.895  1.00 13.35           N  
ATOM   4242  CA  SER A 607      82.021  79.336  80.986  1.00 13.35           C  
ATOM   4243  C   SER A 607      82.125  78.538  79.687  1.00 13.35           C  
ATOM   4244  O   SER A 607      81.269  77.675  79.447  1.00 13.35           O  
ATOM   4245  CB  SER A 607      81.973  80.846  80.806  1.00 13.35           C  
ATOM   4246  OG  SER A 607      81.147  81.198  79.711  1.00 13.35           O  
ATOM   4247  N   ASP A 608      83.117  78.776  78.836  1.00 16.89           N  
ATOM   4248  CA  ASP A 608      83.226  78.032  77.585  1.00 16.89           C  
ATOM   4249  C   ASP A 608      84.665  77.954  77.083  1.00 16.89           C  
ATOM   4250  O   ASP A 608      84.907  77.887  75.875  1.00 16.89           O  
ATOM   4251  CB  ASP A 608      82.295  78.616  76.517  1.00 16.89           C  
ATOM   4252  CG  ASP A 608      82.775  79.951  75.968  1.00 16.89           C  
ATOM   4253  OD1 ASP A 608      83.556  80.646  76.647  1.00 16.89           O  
ATOM   4254  OD2 ASP A 608      82.365  80.297  74.843  1.00 16.89           O  
ATOM   4255  N   VAL A 609      85.630  77.962  78.000  1.00 13.03           N  
ATOM   4256  CA  VAL A 609      87.026  77.797  77.623  1.00 13.03           C  
ATOM   4257  C   VAL A 609      87.220  76.386  77.087  1.00 13.03           C  
ATOM   4258  O   VAL A 609      86.727  75.413  77.671  1.00 13.03           O  
ATOM   4259  CB  VAL A 609      87.936  78.088  78.823  1.00 13.03           C  
ATOM   4260  CG1 VAL A 609      89.388  78.042  78.410  1.00 13.03           C  
ATOM   4261  CG2 VAL A 609      87.584  79.432  79.440  1.00 13.03           C  
ATOM   4262  N   GLU A 610      87.934  76.263  75.968  1.00 16.75           N  
ATOM   4263  CA  GLU A 610      87.926  75.030  75.191  1.00 16.75           C  
ATOM   4264  C   GLU A 610      89.179  74.175  75.343  1.00 16.75           C  
ATOM   4265  O   GLU A 610      89.210  73.060  74.812  1.00 16.75           O  
ATOM   4266  CB  GLU A 610      87.686  75.348  73.710  1.00 16.75           C  
ATOM   4267  CG  GLU A 610      88.596  76.408  73.131  1.00 16.75           C  
ATOM   4268  CD  GLU A 610      87.965  77.114  71.946  1.00 16.75           C  
ATOM   4269  OE1 GLU A 610      86.725  77.053  71.813  1.00 16.75           O  
ATOM   4270  OE2 GLU A 610      88.704  77.730  71.150  1.00 16.75           O  
ATOM   4271  N   ASN A 611      90.205  74.647  76.050  1.00 13.83           N  
ATOM   4272  CA  ASN A 611      91.300  73.783  76.503  1.00 13.83           C  
ATOM   4273  C   ASN A 611      91.598  74.099  77.963  1.00 13.83           C  
ATOM   4274  O   ASN A 611      92.711  74.493  78.318  1.00 13.83           O  
ATOM   4275  CB  ASN A 611      92.539  73.965  75.629  1.00 13.83           C  
ATOM   4276  CG  ASN A 611      92.414  73.274  74.290  1.00 13.83           C  
ATOM   4277  OD1 ASN A 611      92.487  72.051  74.202  1.00 13.83           O  
ATOM   4278  ND2 ASN A 611      92.233  74.058  73.236  1.00 13.83           N  
ATOM   4279  N   PRO A 612      90.619  73.903  78.845  1.00 11.14           N  
ATOM   4280  CA  PRO A 612      90.635  74.610  80.131  1.00 11.14           C  
ATOM   4281  C   PRO A 612      91.613  74.006  81.127  1.00 11.14           C  
ATOM   4282  O   PRO A 612      91.605  72.800  81.378  1.00 11.14           O  
ATOM   4283  CB  PRO A 612      89.191  74.472  80.623  1.00 11.14           C  
ATOM   4284  CG  PRO A 612      88.713  73.225  79.987  1.00 11.14           C  
ATOM   4285  CD  PRO A 612      89.360  73.171  78.644  1.00 11.14           C  
ATOM   4286  N   HIS A 613      92.453  74.866  81.696  1.00 10.28           N  
ATOM   4287  CA  HIS A 613      93.124  74.648  82.969  1.00 10.28           C  
ATOM   4288  C   HIS A 613      92.733  75.773  83.917  1.00 10.28           C  
ATOM   4289  O   HIS A 613      92.202  76.804  83.504  1.00 10.28           O  
ATOM   4290  CB  HIS A 613      94.650  74.591  82.815  1.00 10.28           C  
ATOM   4291  CG  HIS A 613      95.148  73.392  82.070  1.00 10.28           C  
ATOM   4292  ND1 HIS A 613      94.299  72.495  81.460  1.00 10.28           N  
ATOM   4293  CD2 HIS A 613      96.403  72.959  81.807  1.00 10.28           C  
ATOM   4294  CE1 HIS A 613      95.009  71.548  80.875  1.00 10.28           C  
ATOM   4295  NE2 HIS A 613      96.289  71.808  81.069  1.00 10.28           N  
ATOM   4296  N   LEU A 614      92.998  75.569  85.202  1.00  9.43           N  
ATOM   4297  CA  LEU A 614      92.709  76.569  86.216  1.00  9.43           C  
ATOM   4298  C   LEU A 614      94.003  77.074  86.836  1.00  9.43           C  
ATOM   4299  O   LEU A 614      94.990  76.342  86.943  1.00  9.43           O  
ATOM   4300  CB  LEU A 614      91.788  76.015  87.306  1.00  9.43           C  
ATOM   4301  CG  LEU A 614      90.424  75.487  86.860  1.00  9.43           C  
ATOM   4302  CD1 LEU A 614      89.710  74.826  88.019  1.00  9.43           C  
ATOM   4303  CD2 LEU A 614      89.572  76.595  86.268  1.00  9.43           C  
ATOM   4304  N   MET A 615      93.988  78.341  87.237  1.00  9.02           N  
ATOM   4305  CA  MET A 615      95.159  78.999  87.788  1.00  9.02           C  
ATOM   4306  C   MET A 615      94.725  79.938  88.902  1.00  9.02           C  
ATOM   4307  O   MET A 615      93.631  80.505  88.868  1.00  9.02           O  
ATOM   4308  CB  MET A 615      95.919  79.771  86.697  1.00  9.02           C  
ATOM   4309  CG  MET A 615      97.181  80.473  87.159  1.00  9.02           C  
ATOM   4310  SD  MET A 615      97.452  82.040  86.312  1.00  9.02           S  
ATOM   4311  CE  MET A 615      97.328  81.537  84.601  1.00  9.02           C  
ATOM   4312  N   GLY A 616      95.590  80.090  89.889  1.00  9.99           N  
ATOM   4313  CA  GLY A 616      95.372  81.054  90.951  1.00  9.99           C  
ATOM   4314  C   GLY A 616      96.706  81.580  91.419  1.00  9.99           C  
ATOM   4315  O   GLY A 616      97.724  80.885  91.352  1.00  9.99           O  
ATOM   4316  N   TRP A 617      96.704  82.821  91.893  1.00 10.96           N  
ATOM   4317  CA  TRP A 617      97.932  83.490  92.287  1.00 10.96           C  
ATOM   4318  C   TRP A 617      97.682  84.267  93.568  1.00 10.96           C  
ATOM   4319  O   TRP A 617      96.544  84.419  94.016  1.00 10.96           O  
ATOM   4320  CB  TRP A 617      98.446  84.419  91.180  1.00 10.96           C  
ATOM   4321  CG  TRP A 617      97.490  85.507  90.817  1.00 10.96           C  
ATOM   4322  CD1 TRP A 617      97.259  86.657  91.508  1.00 10.96           C  
ATOM   4323  CD2 TRP A 617      96.615  85.536  89.687  1.00 10.96           C  
ATOM   4324  NE1 TRP A 617      96.305  87.406  90.875  1.00 10.96           N  
ATOM   4325  CE2 TRP A 617      95.891  86.740  89.753  1.00 10.96           C  
ATOM   4326  CE3 TRP A 617      96.375  84.663  88.627  1.00 10.96           C  
ATOM   4327  CZ2 TRP A 617      94.948  87.096  88.799  1.00 10.96           C  
ATOM   4328  CZ3 TRP A 617      95.440  85.014  87.684  1.00 10.96           C  
ATOM   4329  CH2 TRP A 617      94.735  86.221  87.775  1.00 10.96           C  
ATOM   4330  N   ASP A 618      98.795  84.780  94.068  1.00 15.79           N  
ATOM   4331  CA  ASP A 618      98.728  85.587  95.303  1.00 15.79           C  
ATOM   4332  C   ASP A 618      99.461  86.898  95.097  1.00 15.79           C  
ATOM   4333  O   ASP A 618     100.473  86.890  94.408  1.00 15.79           O  
ATOM   4334  CB  ASP A 618      99.380  84.875  96.489  1.00 15.79           C  
ATOM   4335  CG  ASP A 618      98.605  83.679  97.014  1.00 15.79           C  
ATOM   4336  OD1 ASP A 618      97.423  83.545  96.662  1.00 15.79           O  
ATOM   4337  OD2 ASP A 618      99.195  82.882  97.765  1.00 15.79           O  
ATOM   4338  N   TYR A 619      98.935  87.980  95.654  1.00 10.60           N  
ATOM   4339  CA  TYR A 619      99.657  89.242  95.690  1.00 10.60           C  
ATOM   4340  C   TYR A 619     100.426  89.335  96.998  1.00 10.60           C  
ATOM   4341  O   TYR A 619      99.799  89.420  98.065  1.00 10.60           O  
ATOM   4342  CB  TYR A 619      98.707  90.421  95.555  1.00 10.60           C  
ATOM   4343  CG  TYR A 619      98.027  90.526  94.216  1.00 10.60           C  
ATOM   4344  CD1 TYR A 619      98.691  91.066  93.127  1.00 10.60           C  
ATOM   4345  CD2 TYR A 619      96.718  90.114  94.043  1.00 10.60           C  
ATOM   4346  CE1 TYR A 619      98.079  91.175  91.902  1.00 10.60           C  
ATOM   4347  CE2 TYR A 619      96.100  90.220  92.822  1.00 10.60           C  
ATOM   4348  CZ  TYR A 619      96.783  90.750  91.755  1.00 10.60           C  
ATOM   4349  OH  TYR A 619      96.169  90.856  90.533  1.00 10.60           O  
ATOM   4350  N   PRO A 620     101.755  89.315  96.978  1.00 11.58           N  
ATOM   4351  CA  PRO A 620     102.506  89.551  98.215  1.00 11.58           C  
ATOM   4352  C   PRO A 620     102.360  90.995  98.668  1.00 11.58           C  
ATOM   4353  O   PRO A 620     102.456  91.926  97.865  1.00 11.58           O  
ATOM   4354  CB  PRO A 620     103.954  89.231  97.822  1.00 11.58           C  
ATOM   4355  CG  PRO A 620     103.876  88.535  96.500  1.00 11.58           C  
ATOM   4356  CD  PRO A 620     102.639  89.037  95.839  1.00 11.58           C  
ATOM   4357  N   LYS A 621     102.122  91.173  99.969  1.00 13.49           N  
ATOM   4358  CA  LYS A 621     102.100  92.498 100.595  1.00 13.49           C  
ATOM   4359  C   LYS A 621     101.108  93.433  99.905  1.00 13.49           C  
ATOM   4360  O   LYS A 621     101.386  94.618  99.718  1.00 13.49           O  
ATOM   4361  CB  LYS A 621     103.498  93.122 100.601  1.00 13.49           C  
ATOM   4362  CG  LYS A 621     104.571  92.269 101.260  1.00 13.49           C  
ATOM   4363  CD  LYS A 621     104.504  92.326 102.774  1.00 13.49           C  
ATOM   4364  CE  LYS A 621     105.439  91.305 103.399  1.00 13.49           C  
ATOM   4365  NZ  LYS A 621     105.302  89.969 102.764  1.00 13.49           N  
ATOM   4366  N   CYS A 622      99.948  92.895  99.514  1.00 15.10           N  
ATOM   4367  CA  CYS A 622      99.022  93.627  98.650  1.00 15.10           C  
ATOM   4368  C   CYS A 622      98.599  94.965  99.247  1.00 15.10           C  
ATOM   4369  O   CYS A 622      98.584  95.986  98.552  1.00 15.10           O  
ATOM   4370  CB  CYS A 622      97.791  92.766  98.367  1.00 15.10           C  
ATOM   4371  SG  CYS A 622      96.752  93.342  97.004  1.00 15.10           S  
ATOM   4372  N   ASP A 623      98.244  94.977 100.532  1.00 16.17           N  
ATOM   4373  CA  ASP A 623      97.718  96.191 101.150  1.00 16.17           C  
ATOM   4374  C   ASP A 623      98.781  97.274 101.296  1.00 16.17           C  
ATOM   4375  O   ASP A 623      98.443  98.459 101.390  1.00 16.17           O  
ATOM   4376  CB  ASP A 623      97.095  95.854 102.507  1.00 16.17           C  
ATOM   4377  CG  ASP A 623      98.039  95.080 103.415  1.00 16.17           C  
ATOM   4378  OD1 ASP A 623      98.436  93.956 103.045  1.00 16.17           O  
ATOM   4379  OD2 ASP A 623      98.370  95.583 104.507  1.00 16.17           O  
ATOM   4380  N   ARG A 624     100.057  96.898 101.323  1.00 13.75           N  
ATOM   4381  CA  ARG A 624     101.144  97.841 101.552  1.00 13.75           C  
ATOM   4382  C   ARG A 624     101.865  98.257 100.278  1.00 13.75           C  
ATOM   4383  O   ARG A 624     102.282  99.410 100.161  1.00 13.75           O  
ATOM   4384  CB  ARG A 624     102.161  97.238 102.524  1.00 13.75           C  
ATOM   4385  CG  ARG A 624     101.540  96.588 103.739  1.00 13.75           C  
ATOM   4386  CD  ARG A 624     100.918  97.610 104.663  1.00 13.75           C  
ATOM   4387  NE  ARG A 624     100.332  96.971 105.835  1.00 13.75           N  
ATOM   4388  CZ  ARG A 624     100.550  97.352 107.087  1.00 13.75           C  
ATOM   4389  NH1 ARG A 624     101.354  98.373 107.346  1.00 13.75           N  
ATOM   4390  NH2 ARG A 624      99.971  96.703 108.082  1.00 13.75           N  
ATOM   4391  N   ALA A 625     102.026  97.346  99.322  1.00 10.21           N  
ATOM   4392  CA  ALA A 625     102.899  97.567  98.179  1.00 10.21           C  
ATOM   4393  C   ALA A 625     102.200  98.175  96.968  1.00 10.21           C  
ATOM   4394  O   ALA A 625     102.873  98.460  95.973  1.00 10.21           O  
ATOM   4395  CB  ALA A 625     103.565  96.250  97.771  1.00 10.21           C  
ATOM   4396  N   MET A 626     100.889  98.373  97.017  1.00 10.45           N  
ATOM   4397  CA  MET A 626     100.137  98.849  95.858  1.00 10.45           C  
ATOM   4398  C   MET A 626     100.576 100.244  95.421  1.00 10.45           C  
ATOM   4399  O   MET A 626     100.552 101.177  96.238  1.00 10.45           O  
ATOM   4400  CB  MET A 626      98.649  98.853  96.175  1.00 10.45           C  
ATOM   4401  CG  MET A 626      97.778  99.306  95.020  1.00 10.45           C  
ATOM   4402  SD  MET A 626      96.059  99.431  95.514  1.00 10.45           S  
ATOM   4403  CE  MET A 626      95.240  99.442  93.931  1.00 10.45           C  
ATOM   4404  N   PRO A 627     100.972 100.433  94.163  1.00  7.21           N  
ATOM   4405  CA  PRO A 627     101.359 101.771  93.697  1.00  7.21           C  
ATOM   4406  C   PRO A 627     100.190 102.749  93.711  1.00  7.21           C  
ATOM   4407  O   PRO A 627      99.038 102.374  93.491  1.00  7.21           O  
ATOM   4408  CB  PRO A 627     101.856 101.516  92.269  1.00  7.21           C  
ATOM   4409  CG  PRO A 627     102.277 100.096  92.273  1.00  7.21           C  
ATOM   4410  CD  PRO A 627     101.295  99.400  93.168  1.00  7.21           C  
ATOM   4411  N   ASN A 628     100.509 104.021  93.965  1.00  9.04           N  
ATOM   4412  CA  ASN A 628      99.482 105.059  94.020  1.00  9.04           C  
ATOM   4413  C   ASN A 628      98.795 105.256  92.675  1.00  9.04           C  
ATOM   4414  O   ASN A 628      97.614 105.616  92.631  1.00  9.04           O  
ATOM   4415  CB  ASN A 628     100.096 106.371  94.500  1.00  9.04           C  
ATOM   4416  CG  ASN A 628     100.572 106.297  95.932  1.00  9.04           C  
ATOM   4417  OD1 ASN A 628     100.239 105.366  96.657  1.00  9.04           O  
ATOM   4418  ND2 ASN A 628     101.359 107.278  96.346  1.00  9.04           N  
ATOM   4419  N   MET A 629      99.516 105.031  91.573  1.00  8.77           N  
ATOM   4420  CA  MET A 629      98.922 105.163  90.246  1.00  8.77           C  
ATOM   4421  C   MET A 629      97.736 104.232  90.063  1.00  8.77           C  
ATOM   4422  O   MET A 629      96.696 104.639  89.537  1.00  8.77           O  
ATOM   4423  CB  MET A 629      99.974 104.890  89.172  1.00  8.77           C  
ATOM   4424  CG  MET A 629     101.044 105.948  89.067  1.00  8.77           C  
ATOM   4425  SD  MET A 629     100.320 107.594  89.103  1.00  8.77           S  
ATOM   4426  CE  MET A 629      99.317 107.541  87.620  1.00  8.77           C  
ATOM   4427  N   LEU A 630      97.863 102.983  90.501  1.00  6.92           N  
ATOM   4428  CA  LEU A 630      96.785 102.028  90.301  1.00  6.92           C  
ATOM   4429  C   LEU A 630      95.627 102.252  91.262  1.00  6.92           C  
ATOM   4430  O   LEU A 630      94.481 101.971  90.904  1.00  6.92           O  
ATOM   4431  CB  LEU A 630      97.331 100.606  90.418  1.00  6.92           C  
ATOM   4432  CG  LEU A 630      98.448 100.309  89.409  1.00  6.92           C  
ATOM   4433  CD1 LEU A 630      99.084  98.953  89.657  1.00  6.92           C  
ATOM   4434  CD2 LEU A 630      97.938 100.411  87.983  1.00  6.92           C  
ATOM   4435  N   ARG A 631      95.885 102.808  92.446  1.00  8.08           N  
ATOM   4436  CA  ARG A 631      94.794 103.206  93.330  1.00  8.08           C  
ATOM   4437  C   ARG A 631      94.023 104.400  92.774  1.00  8.08           C  
ATOM   4438  O   ARG A 631      92.789 104.434  92.839  1.00  8.08           O  
ATOM   4439  CB  ARG A 631      95.346 103.505  94.722  1.00  8.08           C  
ATOM   4440  CG  ARG A 631      94.307 103.853  95.766  1.00  8.08           C  
ATOM   4441  CD  ARG A 631      93.624 102.636  96.349  1.00  8.08           C  
ATOM   4442  NE  ARG A 631      92.347 102.991  96.965  1.00  8.08           N  
ATOM   4443  CZ  ARG A 631      91.258 103.361  96.301  1.00  8.08           C  
ATOM   4444  NH1 ARG A 631      91.262 103.425  94.979  1.00  8.08           N  
ATOM   4445  NH2 ARG A 631      90.154 103.664  96.964  1.00  8.08           N  
ATOM   4446  N   ILE A 632      94.726 105.380  92.207  1.00  6.92           N  
ATOM   4447  CA  ILE A 632      94.034 106.503  91.582  1.00  6.92           C  
ATOM   4448  C   ILE A 632      93.256 106.024  90.362  1.00  6.92           C  
ATOM   4449  O   ILE A 632      92.130 106.469  90.106  1.00  6.92           O  
ATOM   4450  CB  ILE A 632      95.040 107.615  91.232  1.00  6.92           C  
ATOM   4451  CG1 ILE A 632      95.327 108.467  92.464  1.00  6.92           C  
ATOM   4452  CG2 ILE A 632      94.510 108.500  90.116  1.00  6.92           C  
ATOM   4453  CD1 ILE A 632      96.404 109.494  92.252  1.00  6.92           C  
ATOM   4454  N   MET A 633      93.838 105.094  89.606  1.00  8.31           N  
ATOM   4455  CA  MET A 633      93.141 104.442  88.504  1.00  8.31           C  
ATOM   4456  C   MET A 633      91.850 103.778  88.974  1.00  8.31           C  
ATOM   4457  O   MET A 633      90.788 103.949  88.363  1.00  8.31           O  
ATOM   4458  CB  MET A 633      94.095 103.429  87.861  1.00  8.31           C  
ATOM   4459  CG  MET A 633      93.574 102.653  86.667  1.00  8.31           C  
ATOM   4460  SD  MET A 633      92.398 101.321  86.987  1.00  8.31           S  
ATOM   4461  CE  MET A 633      93.280 100.376  88.220  1.00  8.31           C  
ATOM   4462  N   ALA A 634      91.926 103.016  90.065  1.00  8.84           N  
ATOM   4463  CA  ALA A 634      90.749 102.325  90.574  1.00  8.84           C  
ATOM   4464  C   ALA A 634      89.684 103.312  91.034  1.00  8.84           C  
ATOM   4465  O   ALA A 634      88.485 103.066  90.858  1.00  8.84           O  
ATOM   4466  CB  ALA A 634      91.147 101.387  91.712  1.00  8.84           C  
ATOM   4467  N   SER A 635      90.100 104.429  91.634  1.00 16.74           N  
ATOM   4468  CA  SER A 635      89.138 105.456  92.022  1.00 16.74           C  
ATOM   4469  C   SER A 635      88.471 106.088  90.805  1.00 16.74           C  
ATOM   4470  O   SER A 635      87.280 106.415  90.844  1.00 16.74           O  
ATOM   4471  CB  SER A 635      89.817 106.526  92.873  1.00 16.74           C  
ATOM   4472  OG  SER A 635      90.476 105.950  93.981  1.00 16.74           O  
ATOM   4473  N   LEU A 636      89.224 106.293  89.722  1.00  7.96           N  
ATOM   4474  CA  LEU A 636      88.624 106.898  88.534  1.00  7.96           C  
ATOM   4475  C   LEU A 636      87.690 105.939  87.805  1.00  7.96           C  
ATOM   4476  O   LEU A 636      86.706 106.383  87.204  1.00  7.96           O  
ATOM   4477  CB  LEU A 636      89.699 107.417  87.576  1.00  7.96           C  
ATOM   4478  CG  LEU A 636      90.676 108.469  88.102  1.00  7.96           C  
ATOM   4479  CD1 LEU A 636      91.888 108.565  87.204  1.00  7.96           C  
ATOM   4480  CD2 LEU A 636      89.996 109.818  88.220  1.00  7.96           C  
ATOM   4481  N   VAL A 637      87.977 104.635  87.824  1.00  7.71           N  
ATOM   4482  CA  VAL A 637      87.063 103.681  87.196  1.00  7.71           C  
ATOM   4483  C   VAL A 637      85.735 103.625  87.945  1.00  7.71           C  
ATOM   4484  O   VAL A 637      84.669 103.514  87.330  1.00  7.71           O  
ATOM   4485  CB  VAL A 637      87.715 102.291  87.080  1.00  7.71           C  
ATOM   4486  CG1 VAL A 637      86.804 101.343  86.332  1.00  7.71           C  
ATOM   4487  CG2 VAL A 637      89.016 102.396  86.324  1.00  7.71           C  
ATOM   4488  N   LEU A 638      85.771 103.693  89.276  1.00  6.14           N  
ATOM   4489  CA  LEU A 638      84.527 103.729  90.038  1.00  6.14           C  
ATOM   4490  C   LEU A 638      83.748 105.017  89.794  1.00  6.14           C  
ATOM   4491  O   LEU A 638      82.514 105.003  89.805  1.00  6.14           O  
ATOM   4492  CB  LEU A 638      84.810 103.567  91.532  1.00  6.14           C  
ATOM   4493  CG  LEU A 638      85.317 102.215  92.031  1.00  6.14           C  
ATOM   4494  CD1 LEU A 638      85.232 102.149  93.545  1.00  6.14           C  
ATOM   4495  CD2 LEU A 638      84.550 101.069  91.395  1.00  6.14           C  
ATOM   4496  N   ALA A 639      84.417 106.131  89.482  1.00  7.16           N  
ATOM   4497  CA  ALA A 639      83.727 107.435  89.326  1.00  7.16           C  
ATOM   4498  C   ALA A 639      83.219 107.675  87.898  1.00  7.16           C  
ATOM   4499  O   ALA A 639      82.722 108.782  87.641  1.00  7.16           O  
ATOM   4500  CB  ALA A 639      84.634 108.548  89.768  1.00  7.16           C  
ATOM   4501  N   ARG A 640      83.333 106.688  87.007  1.00  7.46           N  
ATOM   4502  CA  ARG A 640      82.914 106.858  85.588  1.00  7.46           C  
ATOM   4503  C   ARG A 640      81.385 106.860  85.462  1.00  7.46           C  
ATOM   4504  O   ARG A 640      80.891 107.253  84.394  1.00  7.46           O  
ATOM   4505  CB  ARG A 640      83.625 105.863  84.665  1.00  7.46           C  
ATOM   4506  CG  ARG A 640      84.987 106.344  84.187  1.00  7.46           C  
ATOM   4507  CD  ARG A 640      85.518 105.552  83.009  1.00  7.46           C  
ATOM   4508  NE  ARG A 640      86.696 106.166  82.414  1.00  7.46           N  
ATOM   4509  CZ  ARG A 640      87.411 105.633  81.432  1.00  7.46           C  
ATOM   4510  NH1 ARG A 640      87.074 104.459  80.926  1.00  7.46           N  
ATOM   4511  NH2 ARG A 640      88.465 106.274  80.961  1.00  7.46           N  
ATOM   4512  N   LYS A 641      80.671 106.440  86.509  1.00  9.93           N  
ATOM   4513  CA  LYS A 641      79.184 106.368  86.491  1.00  9.93           C  
ATOM   4514  C   LYS A 641      78.604 107.720  86.913  1.00  9.93           C  
ATOM   4515  O   LYS A 641      77.372 107.825  86.994  1.00  9.93           O  
ATOM   4516  CB  LYS A 641      78.730 105.279  87.466  1.00  9.93           C  
ATOM   4517  CG  LYS A 641      79.330 103.901  87.232  1.00  9.93           C  
ATOM   4518  CD  LYS A 641      78.868 103.266  85.942  1.00  9.93           C  
ATOM   4519  CE  LYS A 641      79.437 101.880  85.733  1.00  9.93           C  
ATOM   4520  NZ  LYS A 641      80.918 101.889  85.714  1.00  9.93           N  
ATOM   4521  N   HIS A 642      79.460 108.708  87.171  1.00  7.47           N  
ATOM   4522  CA  HIS A 642      79.015 110.033  87.670  1.00  7.47           C  
ATOM   4523  C   HIS A 642      79.008 111.071  86.548  1.00  7.47           C  
ATOM   4524  O   HIS A 642      79.251 112.249  86.846  1.00  7.47           O  
ATOM   4525  CB  HIS A 642      79.965 110.430  88.793  1.00  7.47           C  
ATOM   4526  CG  HIS A 642      79.863 109.518  89.964  1.00  7.47           C  
ATOM   4527  ND1 HIS A 642      79.047 109.825  91.004  1.00  7.47           N  
ATOM   4528  CD2 HIS A 642      80.420 108.324  90.249  1.00  7.47           C  
ATOM   4529  CE1 HIS A 642      79.104 108.881  91.916  1.00  7.47           C  
ATOM   4530  NE2 HIS A 642      79.946 107.942  91.473  1.00  7.47           N  
ATOM   4531  N   THR A 643      78.715 110.654  85.315  1.00 12.00           N  
ATOM   4532  CA  THR A 643      78.669 111.576  84.150  1.00 12.00           C  
ATOM   4533  C   THR A 643      77.487 112.550  84.205  1.00 12.00           C  
ATOM   4534  O   THR A 643      77.668 113.692  83.749  1.00 12.00           O  
ATOM   4535  CB  THR A 643      78.706 110.783  82.837  1.00 12.00           C  
ATOM   4536  OG1 THR A 643      77.650 109.824  82.880  1.00 12.00           O  
ATOM   4537  CG2 THR A 643      80.022 110.070  82.620  1.00 12.00           C  
ATOM   4538  N   THR A 644      76.315 112.117  84.675  1.00 13.39           N  
ATOM   4539  CA  THR A 644      75.108 112.988  84.610  1.00 13.39           C  
ATOM   4540  C   THR A 644      74.903 113.845  85.864  1.00 13.39           C  
ATOM   4541  O   THR A 644      74.190 114.859  85.749  1.00 13.39           O  
ATOM   4542  CB  THR A 644      73.853 112.176  84.273  1.00 13.39           C  
ATOM   4543  OG1 THR A 644      73.493 111.417  85.428  1.00 13.39           O  
ATOM   4544  CG2 THR A 644      74.048 111.255  83.089  1.00 13.39           C  
ATOM   4545  N   CYS A 645      75.461 113.459  87.016  1.00 12.29           N  
ATOM   4546  CA  CYS A 645      75.208 114.206  88.242  1.00 12.29           C  
ATOM   4547  C   CYS A 645      76.349 115.143  88.604  1.00 12.29           C  
ATOM   4548  O   CYS A 645      76.102 116.220  89.154  1.00 12.29           O  
ATOM   4549  CB  CYS A 645      74.972 113.263  89.424  1.00 12.29           C  
ATOM   4550  SG  CYS A 645      76.284 112.069  89.705  1.00 12.29           S  
ATOM   4551  N   CYS A 646      77.587 114.768  88.301  1.00 10.15           N  
ATOM   4552  CA  CYS A 646      78.761 115.517  88.719  1.00 10.15           C  
ATOM   4553  C   CYS A 646      79.383 116.202  87.510  1.00 10.15           C  
ATOM   4554  O   CYS A 646      79.431 115.628  86.419  1.00 10.15           O  
ATOM   4555  CB  CYS A 646      79.805 114.600  89.376  1.00 10.15           C  
ATOM   4556  SG  CYS A 646      79.282 113.589  90.789  1.00 10.15           S  
ATOM   4557  N   SER A 647      79.839 117.437  87.701  1.00 10.23           N  
ATOM   4558  CA  SER A 647      80.694 118.082  86.720  1.00 10.23           C  
ATOM   4559  C   SER A 647      82.134 117.614  86.909  1.00 10.23           C  
ATOM   4560  O   SER A 647      82.460 116.886  87.850  1.00 10.23           O  
ATOM   4561  CB  SER A 647      80.597 119.602  86.834  1.00 10.23           C  
ATOM   4562  OG  SER A 647      81.122 120.050  88.068  1.00 10.23           O  
ATOM   4563  N   LEU A 648      83.008 118.035  85.994  1.00  9.01           N  
ATOM   4564  CA  LEU A 648      84.396 117.592  86.051  1.00  9.01           C  
ATOM   4565  C   LEU A 648      85.172 118.211  87.205  1.00  9.01           C  
ATOM   4566  O   LEU A 648      86.078 117.565  87.735  1.00  9.01           O  
ATOM   4567  CB  LEU A 648      85.094 117.883  84.726  1.00  9.01           C  
ATOM   4568  CG  LEU A 648      84.602 117.033  83.554  1.00  9.01           C  
ATOM   4569  CD1 LEU A 648      85.657 116.960  82.479  1.00  9.01           C  
ATOM   4570  CD2 LEU A 648      84.229 115.634  84.014  1.00  9.01           C  
ATOM   4571  N   SER A 649      84.834 119.431  87.623  1.00  7.64           N  
ATOM   4572  CA  SER A 649      85.459 119.988  88.819  1.00  7.64           C  
ATOM   4573  C   SER A 649      84.950 119.297  90.077  1.00  7.64           C  
ATOM   4574  O   SER A 649      85.724 119.038  91.008  1.00  7.64           O  
ATOM   4575  CB  SER A 649      85.207 121.492  88.890  1.00  7.64           C  
ATOM   4576  OG  SER A 649      83.852 121.786  88.614  1.00  7.64           O  
ATOM   4577  N   HIS A 650      83.655 118.980  90.109  1.00  7.87           N  
ATOM   4578  CA  HIS A 650      83.102 118.190  91.202  1.00  7.87           C  
ATOM   4579  C   HIS A 650      83.799 116.843  91.299  1.00  7.87           C  
ATOM   4580  O   HIS A 650      84.164 116.395  92.391  1.00  7.87           O  
ATOM   4581  CB  HIS A 650      81.599 118.004  90.997  1.00  7.87           C  
ATOM   4582  CG  HIS A 650      80.807 119.266  91.129  1.00  7.87           C  
ATOM   4583  ND1 HIS A 650      79.430 119.286  91.109  1.00  7.87           N  
ATOM   4584  CD2 HIS A 650      81.199 120.551  91.302  1.00  7.87           C  
ATOM   4585  CE1 HIS A 650      79.008 120.529  91.252  1.00  7.87           C  
ATOM   4586  NE2 HIS A 650      80.061 121.316  91.374  1.00  7.87           N  
ATOM   4587  N   ARG A 651      84.001 116.187  90.154  1.00  7.42           N  
ATOM   4588  CA  ARG A 651      84.667 114.892  90.148  1.00  7.42           C  
ATOM   4589  C   ARG A 651      86.130 115.018  90.553  1.00  7.42           C  
ATOM   4590  O   ARG A 651      86.663 114.147  91.251  1.00  7.42           O  
ATOM   4591  CB  ARG A 651      84.527 114.242  88.773  1.00  7.42           C  
ATOM   4592  CG  ARG A 651      83.233 113.454  88.614  1.00  7.42           C  
ATOM   4593  CD  ARG A 651      82.873 113.200  87.163  1.00  7.42           C  
ATOM   4594  NE  ARG A 651      83.774 112.236  86.542  1.00  7.42           N  
ATOM   4595  CZ  ARG A 651      83.496 111.555  85.436  1.00  7.42           C  
ATOM   4596  NH1 ARG A 651      82.337 111.728  84.822  1.00  7.42           N  
ATOM   4597  NH2 ARG A 651      84.379 110.700  84.945  1.00  7.42           N  
ATOM   4598  N   PHE A 652      86.798 116.101  90.142  1.00  5.55           N  
ATOM   4599  CA  PHE A 652      88.186 116.274  90.556  1.00  5.55           C  
ATOM   4600  C   PHE A 652      88.300 116.471  92.060  1.00  5.55           C  
ATOM   4601  O   PHE A 652      89.208 115.922  92.688  1.00  5.55           O  
ATOM   4602  CB  PHE A 652      88.857 117.443  89.843  1.00  5.55           C  
ATOM   4603  CG  PHE A 652      90.310 117.578  90.199  1.00  5.55           C  
ATOM   4604  CD1 PHE A 652      91.230 116.649  89.752  1.00  5.55           C  
ATOM   4605  CD2 PHE A 652      90.740 118.577  91.054  1.00  5.55           C  
ATOM   4606  CE1 PHE A 652      92.555 116.743  90.105  1.00  5.55           C  
ATOM   4607  CE2 PHE A 652      92.064 118.670  91.412  1.00  5.55           C  
ATOM   4608  CZ  PHE A 652      92.972 117.754  90.936  1.00  5.55           C  
ATOM   4609  N   TYR A 653      87.419 117.276  92.656  1.00  6.64           N  
ATOM   4610  CA  TYR A 653      87.488 117.431  94.106  1.00  6.64           C  
ATOM   4611  C   TYR A 653      87.071 116.166  94.839  1.00  6.64           C  
ATOM   4612  O   TYR A 653      87.594 115.889  95.922  1.00  6.64           O  
ATOM   4613  CB  TYR A 653      86.671 118.631  94.576  1.00  6.64           C  
ATOM   4614  CG  TYR A 653      87.368 119.942  94.324  1.00  6.64           C  
ATOM   4615  CD1 TYR A 653      88.218 120.479  95.277  1.00  6.64           C  
ATOM   4616  CD2 TYR A 653      87.185 120.638  93.146  1.00  6.64           C  
ATOM   4617  CE1 TYR A 653      88.866 121.671  95.062  1.00  6.64           C  
ATOM   4618  CE2 TYR A 653      87.828 121.832  92.921  1.00  6.64           C  
ATOM   4619  CZ  TYR A 653      88.667 122.346  93.882  1.00  6.64           C  
ATOM   4620  OH  TYR A 653      89.311 123.538  93.661  1.00  6.64           O  
ATOM   4621  N   ARG A 654      86.167 115.370  94.266  1.00  5.79           N  
ATOM   4622  CA  ARG A 654      85.875 114.070  94.859  1.00  5.79           C  
ATOM   4623  C   ARG A 654      87.101 113.164  94.847  1.00  5.79           C  
ATOM   4624  O   ARG A 654      87.387 112.494  95.847  1.00  5.79           O  
ATOM   4625  CB  ARG A 654      84.715 113.414  94.117  1.00  5.79           C  
ATOM   4626  CG  ARG A 654      83.354 113.991  94.454  1.00  5.79           C  
ATOM   4627  CD  ARG A 654      83.146 114.087  95.945  1.00  5.79           C  
ATOM   4628  NE  ARG A 654      83.245 112.781  96.584  1.00  5.79           N  
ATOM   4629  CZ  ARG A 654      83.283 112.597  97.897  1.00  5.79           C  
ATOM   4630  NH1 ARG A 654      83.232 113.637  98.710  1.00  5.79           N  
ATOM   4631  NH2 ARG A 654      83.379 111.377  98.395  1.00  5.79           N  
ATOM   4632  N   LEU A 655      87.860 113.166  93.748  1.00  5.49           N  
ATOM   4633  CA  LEU A 655      89.092 112.383  93.694  1.00  5.49           C  
ATOM   4634  C   LEU A 655      90.148 112.920  94.652  1.00  5.49           C  
ATOM   4635  O   LEU A 655      90.858 112.144  95.301  1.00  5.49           O  
ATOM   4636  CB  LEU A 655      89.639 112.358  92.270  1.00  5.49           C  
ATOM   4637  CG  LEU A 655      90.919 111.539  92.097  1.00  5.49           C  
ATOM   4638  CD1 LEU A 655      90.618 110.063  91.924  1.00  5.49           C  
ATOM   4639  CD2 LEU A 655      91.723 112.073  90.929  1.00  5.49           C  
ATOM   4640  N   ALA A 656      90.286 114.243  94.733  1.00  6.30           N  
ATOM   4641  CA  ALA A 656      91.269 114.833  95.632  1.00  6.30           C  
ATOM   4642  C   ALA A 656      90.937 114.520  97.083  1.00  6.30           C  
ATOM   4643  O   ALA A 656      91.832 114.244  97.890  1.00  6.30           O  
ATOM   4644  CB  ALA A 656      91.344 116.342  95.407  1.00  6.30           C  
ATOM   4645  N   ASN A 657      89.649 114.546  97.429  1.00  6.99           N  
ATOM   4646  CA  ASN A 657      89.229 114.154  98.766  1.00  6.99           C  
ATOM   4647  C   ASN A 657      89.514 112.683  99.026  1.00  6.99           C  
ATOM   4648  O   ASN A 657      89.991 112.321 100.109  1.00  6.99           O  
ATOM   4649  CB  ASN A 657      87.746 114.460  98.951  1.00  6.99           C  
ATOM   4650  CG  ASN A 657      87.513 115.783  99.631  1.00  6.99           C  
ATOM   4651  OD1 ASN A 657      87.731 115.918 100.828  1.00  6.99           O  
ATOM   4652  ND2 ASN A 657      87.074 116.772  98.870  1.00  6.99           N  
ATOM   4653  N   GLU A 658      89.248 111.820  98.042  1.00  9.96           N  
ATOM   4654  CA  GLU A 658      89.543 110.402  98.219  1.00  9.96           C  
ATOM   4655  C   GLU A 658      91.030 110.177  98.460  1.00  9.96           C  
ATOM   4656  O   GLU A 658      91.416 109.405  99.342  1.00  9.96           O  
ATOM   4657  CB  GLU A 658      89.061 109.606  97.006  1.00  9.96           C  
ATOM   4658  CG  GLU A 658      87.714 108.930  97.218  1.00  9.96           C  
ATOM   4659  CD  GLU A 658      87.307 108.035  96.060  1.00  9.96           C  
ATOM   4660  OE1 GLU A 658      87.307 106.799  96.238  1.00  9.96           O  
ATOM   4661  OE2 GLU A 658      86.974 108.566  94.981  1.00  9.96           O  
ATOM   4662  N   CYS A 659      91.883 110.848  97.686  1.00 10.29           N  
ATOM   4663  CA  CYS A 659      93.322 110.706  97.892  1.00 10.29           C  
ATOM   4664  C   CYS A 659      93.741 111.214  99.265  1.00 10.29           C  
ATOM   4665  O   CYS A 659      94.426 110.504 100.009  1.00 10.29           O  
ATOM   4666  CB  CYS A 659      94.095 111.433  96.793  1.00 10.29           C  
ATOM   4667  SG  CYS A 659      94.113 110.572  95.210  1.00 10.29           S  
ATOM   4668  N   ALA A 660      93.297 112.418  99.641  1.00  8.41           N  
ATOM   4669  CA  ALA A 660      93.698 112.997 100.917  1.00  8.41           C  
ATOM   4670  C   ALA A 660      93.111 112.259 102.111  1.00  8.41           C  
ATOM   4671  O   ALA A 660      93.553 112.489 103.240  1.00  8.41           O  
ATOM   4672  CB  ALA A 660      93.295 114.469 100.980  1.00  8.41           C  
ATOM   4673  N   GLN A 661      92.121 111.397 101.898  1.00  9.93           N  
ATOM   4674  CA  GLN A 661      91.503 110.666 102.994  1.00  9.93           C  
ATOM   4675  C   GLN A 661      91.923 109.209 103.101  1.00  9.93           C  
ATOM   4676  O   GLN A 661      92.007 108.696 104.217  1.00  9.93           O  
ATOM   4677  CB  GLN A 661      89.977 110.740 102.876  1.00  9.93           C  
ATOM   4678  CG  GLN A 661      89.392 112.065 103.328  1.00  9.93           C  
ATOM   4679  CD  GLN A 661      88.075 112.391 102.657  1.00  9.93           C  
ATOM   4680  OE1 GLN A 661      87.239 111.515 102.452  1.00  9.93           O  
ATOM   4681  NE2 GLN A 661      87.861 113.664 102.360  1.00  9.93           N  
ATOM   4682  N   VAL A 662      92.196 108.523 101.992  1.00 11.53           N  
ATOM   4683  CA  VAL A 662      92.544 107.106 102.070  1.00 11.53           C  
ATOM   4684  C   VAL A 662      93.862 106.761 101.399  1.00 11.53           C  
ATOM   4685  O   VAL A 662      94.358 105.636 101.582  1.00 11.53           O  
ATOM   4686  CB  VAL A 662      91.412 106.218 101.497  1.00 11.53           C  
ATOM   4687  CG1 VAL A 662      90.090 106.509 102.190  1.00 11.53           C  
ATOM   4688  CG2 VAL A 662      91.293 106.378  99.995  1.00 11.53           C  
ATOM   4689  N   LEU A 663      94.483 107.637 100.612  1.00 11.90           N  
ATOM   4690  CA  LEU A 663      95.730 107.259  99.955  1.00 11.90           C  
ATOM   4691  C   LEU A 663      96.949 107.722 100.749  1.00 11.90           C  
ATOM   4692  O   LEU A 663      97.785 106.907 101.148  1.00 11.90           O  
ATOM   4693  CB  LEU A 663      95.760 107.817  98.528  1.00 11.90           C  
ATOM   4694  CG  LEU A 663      96.861 107.298  97.605  1.00 11.90           C  
ATOM   4695  CD1 LEU A 663      97.021 105.797  97.755  1.00 11.90           C  
ATOM   4696  CD2 LEU A 663      96.559 107.655  96.164  1.00 11.90           C  
ATOM   4697  N   SER A 664      97.054 109.023 101.000  1.00 13.11           N  
ATOM   4698  CA  SER A 664      98.216 109.612 101.650  1.00 13.11           C  
ATOM   4699  C   SER A 664      97.804 110.441 102.855  1.00 13.11           C  
ATOM   4700  O   SER A 664      98.367 111.505 103.123  1.00 13.11           O  
ATOM   4701  CB  SER A 664      99.014 110.457 100.663  1.00 13.11           C  
ATOM   4702  OG  SER A 664      98.367 111.693 100.419  1.00 13.11           O  
ATOM   4703  N   GLU A 665      96.816 109.964 103.606  1.00 13.75           N  
ATOM   4704  CA  GLU A 665      96.346 110.679 104.781  1.00 13.75           C  
ATOM   4705  C   GLU A 665      97.339 110.526 105.932  1.00 13.75           C  
ATOM   4706  O   GLU A 665      98.359 109.840 105.831  1.00 13.75           O  
ATOM   4707  CB  GLU A 665      94.959 110.180 105.180  1.00 13.75           C  
ATOM   4708  CG  GLU A 665      94.945 108.892 105.991  1.00 13.75           C  
ATOM   4709  CD  GLU A 665      95.237 107.651 105.166  1.00 13.75           C  
ATOM   4710  OE1 GLU A 665      96.111 107.702 104.280  1.00 13.75           O  
ATOM   4711  OE2 GLU A 665      94.586 106.613 105.407  1.00 13.75           O  
ATOM   4712  N   MET A 666      97.040 111.195 107.040  1.00 15.94           N  
ATOM   4713  CA  MET A 666      97.824 111.065 108.257  1.00 15.94           C  
ATOM   4714  C   MET A 666      97.264 109.944 109.119  1.00 15.94           C  
ATOM   4715  O   MET A 666      96.048 109.779 109.234  1.00 15.94           O  
ATOM   4716  CB  MET A 666      97.844 112.381 109.033  1.00 15.94           C  
ATOM   4717  CG  MET A 666      98.820 113.387 108.460  1.00 15.94           C  
ATOM   4718  SD  MET A 666      99.202 114.755 109.559  1.00 15.94           S  
ATOM   4719  CE  MET A 666      99.303 116.090 108.372  1.00 15.94           C  
ATOM   4720  N   VAL A 667      98.162 109.172 109.720  1.00 14.40           N  
ATOM   4721  CA  VAL A 667      97.803 107.966 110.454  1.00 14.40           C  
ATOM   4722  C   VAL A 667      98.068 108.200 111.931  1.00 14.40           C  
ATOM   4723  O   VAL A 667      99.189 108.540 112.325  1.00 14.40           O  
ATOM   4724  CB  VAL A 667      98.577 106.742 109.942  1.00 14.40           C  
ATOM   4725  CG1 VAL A 667      98.279 105.532 110.804  1.00 14.40           C  
ATOM   4726  CG2 VAL A 667      98.220 106.464 108.497  1.00 14.40           C  
ATOM   4727  N   MET A 668      97.036 108.014 112.745  1.00 19.94           N  
ATOM   4728  CA  MET A 668      97.155 108.051 114.196  1.00 19.94           C  
ATOM   4729  C   MET A 668      97.550 106.655 114.665  1.00 19.94           C  
ATOM   4730  O   MET A 668      96.749 105.719 114.590  1.00 19.94           O  
ATOM   4731  CB  MET A 668      95.840 108.503 114.824  1.00 19.94           C  
ATOM   4732  CG  MET A 668      95.777 108.384 116.331  1.00 19.94           C  
ATOM   4733  SD  MET A 668      96.712 109.661 117.182  1.00 19.94           S  
ATOM   4734  CE  MET A 668      96.383 111.065 116.126  1.00 19.94           C  
ATOM   4735  N   CYS A 669      98.788 106.509 115.137  1.00 17.69           N  
ATOM   4736  CA  CYS A 669      99.335 105.198 115.499  1.00 17.69           C  
ATOM   4737  C   CYS A 669     100.039 105.330 116.848  1.00 17.69           C  
ATOM   4738  O   CYS A 669     101.212 105.701 116.917  1.00 17.69           O  
ATOM   4739  CB  CYS A 669     100.276 104.683 114.416  1.00 17.69           C  
ATOM   4740  SG  CYS A 669     100.914 103.017 114.690  1.00 17.69           S  
ATOM   4741  N   GLY A 670      99.317 105.010 117.918  1.00 19.15           N  
ATOM   4742  CA  GLY A 670      99.889 105.068 119.248  1.00 19.15           C  
ATOM   4743  C   GLY A 670      99.995 106.453 119.840  1.00 19.15           C  
ATOM   4744  O   GLY A 670     100.906 106.710 120.634  1.00 19.15           O  
ATOM   4745  N   GLY A 671      99.085 107.355 119.485  1.00 19.82           N  
ATOM   4746  CA  GLY A 671      99.128 108.716 119.970  1.00 19.82           C  
ATOM   4747  C   GLY A 671     100.010 109.650 119.176  1.00 19.82           C  
ATOM   4748  O   GLY A 671     100.164 110.812 119.571  1.00 19.82           O  
ATOM   4749  N   SER A 672     100.592 109.187 118.075  1.00 16.16           N  
ATOM   4750  CA  SER A 672     101.489 109.985 117.256  1.00 16.16           C  
ATOM   4751  C   SER A 672     100.985 110.015 115.821  1.00 16.16           C  
ATOM   4752  O   SER A 672     100.348 109.070 115.352  1.00 16.16           O  
ATOM   4753  CB  SER A 672     102.910 109.428 117.300  1.00 16.16           C  
ATOM   4754  OG  SER A 672     103.448 109.513 118.606  1.00 16.16           O  
ATOM   4755  N   LEU A 673     101.274 111.111 115.126  1.00 13.66           N  
ATOM   4756  CA  LEU A 673     100.813 111.323 113.761  1.00 13.66           C  
ATOM   4757  C   LEU A 673     101.931 111.009 112.776  1.00 13.66           C  
ATOM   4758  O   LEU A 673     103.038 111.540 112.896  1.00 13.66           O  
ATOM   4759  CB  LEU A 673     100.331 112.760 113.567  1.00 13.66           C  
ATOM   4760  CG  LEU A 673      98.859 113.020 113.885  1.00 13.66           C  
ATOM   4761  CD1 LEU A 673      98.546 114.505 113.817  1.00 13.66           C  
ATOM   4762  CD2 LEU A 673      97.963 112.236 112.940  1.00 13.66           C  
ATOM   4763  N   TYR A 674     101.632 110.152 111.804  1.00 11.98           N  
ATOM   4764  CA  TYR A 674     102.569 109.758 110.764  1.00 11.98           C  
ATOM   4765  C   TYR A 674     101.936 109.986 109.401  1.00 11.98           C  
ATOM   4766  O   TYR A 674     100.716 110.083 109.271  1.00 11.98           O  
ATOM   4767  CB  TYR A 674     102.978 108.287 110.895  1.00 11.98           C  
ATOM   4768  CG  TYR A 674     103.576 107.921 112.228  1.00 11.98           C  
ATOM   4769  CD1 TYR A 674     102.777 107.483 113.270  1.00 11.98           C  
ATOM   4770  CD2 TYR A 674     104.945 107.985 112.437  1.00 11.98           C  
ATOM   4771  CE1 TYR A 674     103.320 107.146 114.485  1.00 11.98           C  
ATOM   4772  CE2 TYR A 674     105.495 107.644 113.649  1.00 11.98           C  
ATOM   4773  CZ  TYR A 674     104.678 107.226 114.669  1.00 11.98           C  
ATOM   4774  OH  TYR A 674     105.222 106.882 115.881  1.00 11.98           O  
ATOM   4775  N   VAL A 675     102.781 110.080 108.383  1.00 11.88           N  
ATOM   4776  CA  VAL A 675     102.324 110.172 107.003  1.00 11.88           C  
ATOM   4777  C   VAL A 675     102.356 108.782 106.390  1.00 11.88           C  
ATOM   4778  O   VAL A 675     103.392 108.110 106.406  1.00 11.88           O  
ATOM   4779  CB  VAL A 675     103.191 111.149 106.192  1.00 11.88           C  
ATOM   4780  CG1 VAL A 675     102.621 111.315 104.795  1.00 11.88           C  
ATOM   4781  CG2 VAL A 675     103.268 112.486 106.881  1.00 11.88           C  
ATOM   4782  N   LYS A 676     101.207 108.331 105.891  1.00 11.75           N  
ATOM   4783  CA  LYS A 676     101.142 107.019 105.200  1.00 11.75           C  
ATOM   4784  C   LYS A 676     101.728 107.211 103.797  1.00 11.75           C  
ATOM   4785  O   LYS A 676     101.203 108.063 103.063  1.00 11.75           O  
ATOM   4786  CB  LYS A 676      99.676 106.589 105.117  1.00 11.75           C  
ATOM   4787  CG  LYS A 676      99.393 105.261 104.434  1.00 11.75           C  
ATOM   4788  CD  LYS A 676      97.967 104.816 104.657  1.00 11.75           C  
ATOM   4789  CE  LYS A 676      97.329 104.218 103.424  1.00 11.75           C  
ATOM   4790  NZ  LYS A 676      95.853 104.190 103.530  1.00 11.75           N  
ATOM   4791  N   PRO A 677     102.786 106.472 103.388  1.00 10.69           N  
ATOM   4792  CA  PRO A 677     103.343 106.599 102.032  1.00 10.69           C  
ATOM   4793  C   PRO A 677     102.342 106.296 100.931  1.00 10.69           C  
ATOM   4794  O   PRO A 677     102.416 106.900  99.855  1.00 10.69           O  
ATOM   4795  CB  PRO A 677     104.497 105.587 102.034  1.00 10.69           C  
ATOM   4796  CG  PRO A 677     104.862 105.433 103.466  1.00 10.69           C  
ATOM   4797  CD  PRO A 677     103.566 105.539 104.214  1.00 10.69           C  
ATOM   4798  N   GLY A 678     101.412 105.381 101.168  1.00 10.04           N  
ATOM   4799  CA  GLY A 678     100.475 104.963 100.145  1.00 10.04           C  
ATOM   4800  C   GLY A 678      99.866 103.622 100.515  1.00 10.04           C  
ATOM   4801  O   GLY A 678      99.924 103.199 101.666  1.00 10.04           O  
ATOM   4802  N   GLY A 679      99.301 102.964  99.510  1.00 13.41           N  
ATOM   4803  CA  GLY A 679      98.595 101.719  99.717  1.00 13.41           C  
ATOM   4804  C   GLY A 679      97.152 101.934 100.136  1.00 13.41           C  
ATOM   4805  O   GLY A 679      96.695 103.049 100.385  1.00 13.41           O  
ATOM   4806  N   THR A 680      96.419 100.828 100.215  1.00 17.29           N  
ATOM   4807  CA  THR A 680      94.997 100.881 100.513  1.00 17.29           C  
ATOM   4808  C   THR A 680      94.762 101.115 102.002  1.00 17.29           C  
ATOM   4809  O   THR A 680      95.687 101.133 102.818  1.00 17.29           O  
ATOM   4810  CB  THR A 680      94.300  99.596 100.071  1.00 17.29           C  
ATOM   4811  OG1 THR A 680      94.850  98.481 100.783  1.00 17.29           O  
ATOM   4812  CG2 THR A 680      94.466  99.379  98.585  1.00 17.29           C  
ATOM   4813  N   SER A 681      93.492 101.297 102.354  1.00 19.84           N  
ATOM   4814  CA  SER A 681      93.054 101.392 103.737  1.00 19.84           C  
ATOM   4815  C   SER A 681      91.943 100.380 103.962  1.00 19.84           C  
ATOM   4816  O   SER A 681      90.990 100.312 103.182  1.00 19.84           O  
ATOM   4817  CB  SER A 681      92.564 102.807 104.073  1.00 19.84           C  
ATOM   4818  OG  SER A 681      92.266 102.931 105.452  1.00 19.84           O  
ATOM   4819  N   SER A 682      92.068  99.598 105.035  1.00 21.52           N  
ATOM   4820  CA  SER A 682      91.086  98.552 105.301  1.00 21.52           C  
ATOM   4821  C   SER A 682      89.706  99.139 105.569  1.00 21.52           C  
ATOM   4822  O   SER A 682      88.691  98.563 105.162  1.00 21.52           O  
ATOM   4823  CB  SER A 682      91.538  97.694 106.481  1.00 21.52           C  
ATOM   4824  OG  SER A 682      91.339  98.369 107.710  1.00 21.52           O  
ATOM   4825  N   GLY A 683      89.647 100.280 106.253  1.00 19.61           N  
ATOM   4826  CA  GLY A 683      88.379 100.872 106.623  1.00 19.61           C  
ATOM   4827  C   GLY A 683      87.707 101.701 105.563  1.00 19.61           C  
ATOM   4828  O   GLY A 683      86.588 102.171 105.778  1.00 19.61           O  
ATOM   4829  N   ASP A 684      88.369 101.908 104.429  1.00 16.83           N  
ATOM   4830  CA  ASP A 684      87.765 102.624 103.316  1.00 16.83           C  
ATOM   4831  C   ASP A 684      86.519 101.879 102.847  1.00 16.83           C  
ATOM   4832  O   ASP A 684      86.479 100.647 102.839  1.00 16.83           O  
ATOM   4833  CB  ASP A 684      88.794 102.766 102.186  1.00 16.83           C  
ATOM   4834  CG  ASP A 684      88.178 103.129 100.844  1.00 16.83           C  
ATOM   4835  OD1 ASP A 684      87.055 103.676 100.802  1.00 16.83           O  
ATOM   4836  OD2 ASP A 684      88.865 102.927  99.821  1.00 16.83           O  
ATOM   4837  N   ALA A 685      85.489 102.643 102.475  1.00 17.65           N  
ATOM   4838  CA  ALA A 685      84.218 102.043 102.076  1.00 17.65           C  
ATOM   4839  C   ALA A 685      84.354 101.176 100.831  1.00 17.65           C  
ATOM   4840  O   ALA A 685      83.620 100.195 100.678  1.00 17.65           O  
ATOM   4841  CB  ALA A 685      83.174 103.135 101.841  1.00 17.65           C  
ATOM   4842  N   THR A 686      85.280 101.515  99.939  1.00 12.13           N  
ATOM   4843  CA  THR A 686      85.385 100.891  98.628  1.00 12.13           C  
ATOM   4844  C   THR A 686      86.490  99.849  98.536  1.00 12.13           C  
ATOM   4845  O   THR A 686      86.779  99.379  97.432  1.00 12.13           O  
ATOM   4846  CB  THR A 686      85.614 101.961  97.555  1.00 12.13           C  
ATOM   4847  OG1 THR A 686      86.710 102.797  97.941  1.00 12.13           O  
ATOM   4848  CG2 THR A 686      84.375 102.814  97.379  1.00 12.13           C  
ATOM   4849  N   THR A 687      87.109  99.480  99.662  1.00 11.13           N  
ATOM   4850  CA  THR A 687      88.373  98.746  99.638  1.00 11.13           C  
ATOM   4851  C   THR A 687      88.291  97.472  98.803  1.00 11.13           C  
ATOM   4852  O   THR A 687      89.136  97.235  97.935  1.00 11.13           O  
ATOM   4853  CB  THR A 687      88.804  98.409 101.064  1.00 11.13           C  
ATOM   4854  OG1 THR A 687      88.716  99.580 101.880  1.00 11.13           O  
ATOM   4855  CG2 THR A 687      90.235  97.903 101.076  1.00 11.13           C  
ATOM   4856  N   ALA A 688      87.280  96.637  99.057  1.00  7.78           N  
ATOM   4857  CA  ALA A 688      87.171  95.373  98.334  1.00  7.78           C  
ATOM   4858  C   ALA A 688      86.921  95.593  96.849  1.00  7.78           C  
ATOM   4859  O   ALA A 688      87.488  94.887  96.007  1.00  7.78           O  
ATOM   4860  CB  ALA A 688      86.061  94.517  98.942  1.00  7.78           C  
ATOM   4861  N   TYR A 689      86.114  96.592  96.506  1.00  7.02           N  
ATOM   4862  CA  TYR A 689      85.791  96.856  95.110  1.00  7.02           C  
ATOM   4863  C   TYR A 689      86.987  97.449  94.376  1.00  7.02           C  
ATOM   4864  O   TYR A 689      87.268  97.080  93.230  1.00  7.02           O  
ATOM   4865  CB  TYR A 689      84.589  97.795  95.041  1.00  7.02           C  
ATOM   4866  CG  TYR A 689      83.378  97.271  95.781  1.00  7.02           C  
ATOM   4867  CD1 TYR A 689      83.179  97.573  97.119  1.00  7.02           C  
ATOM   4868  CD2 TYR A 689      82.431  96.484  95.145  1.00  7.02           C  
ATOM   4869  CE1 TYR A 689      82.085  97.099  97.802  1.00  7.02           C  
ATOM   4870  CE2 TYR A 689      81.327  96.010  95.823  1.00  7.02           C  
ATOM   4871  CZ  TYR A 689      81.160  96.321  97.150  1.00  7.02           C  
ATOM   4872  OH  TYR A 689      80.067  95.851  97.831  1.00  7.02           O  
ATOM   4873  N   ALA A 690      87.709  98.359  95.031  1.00  7.24           N  
ATOM   4874  CA  ALA A 690      88.932  98.900  94.450  1.00  7.24           C  
ATOM   4875  C   ALA A 690      89.985  97.814  94.270  1.00  7.24           C  
ATOM   4876  O   ALA A 690      90.713  97.807  93.273  1.00  7.24           O  
ATOM   4877  CB  ALA A 690      89.466 100.035  95.323  1.00  7.24           C  
ATOM   4878  N   ASN A 691      90.091  96.893  95.230  1.00  4.58           N  
ATOM   4879  CA  ASN A 691      91.025  95.782  95.083  1.00  4.58           C  
ATOM   4880  C   ASN A 691      90.628  94.877  93.927  1.00  4.58           C  
ATOM   4881  O   ASN A 691      91.491  94.330  93.235  1.00  4.58           O  
ATOM   4882  CB  ASN A 691      91.109  94.985  96.379  1.00  4.58           C  
ATOM   4883  CG  ASN A 691      91.930  95.675  97.442  1.00  4.58           C  
ATOM   4884  OD1 ASN A 691      92.350  96.817  97.270  1.00  4.58           O  
ATOM   4885  ND2 ASN A 691      92.168  94.986  98.546  1.00  4.58           N  
ATOM   4886  N   SER A 692      89.324  94.691  93.712  1.00  7.44           N  
ATOM   4887  CA  SER A 692      88.873  93.936  92.547  1.00  7.44           C  
ATOM   4888  C   SER A 692      89.259  94.634  91.248  1.00  7.44           C  
ATOM   4889  O   SER A 692      89.696  93.982  90.288  1.00  7.44           O  
ATOM   4890  CB  SER A 692      87.364  93.727  92.621  1.00  7.44           C  
ATOM   4891  OG  SER A 692      87.000  93.131  93.847  1.00  7.44           O  
ATOM   4892  N   VAL A 693      89.118  95.961  91.204  1.00  7.07           N  
ATOM   4893  CA  VAL A 693      89.547  96.711  90.025  1.00  7.07           C  
ATOM   4894  C   VAL A 693      91.043  96.540  89.802  1.00  7.07           C  
ATOM   4895  O   VAL A 693      91.497  96.339  88.672  1.00  7.07           O  
ATOM   4896  CB  VAL A 693      89.168  98.198  90.151  1.00  7.07           C  
ATOM   4897  CG1 VAL A 693      89.514  98.937  88.874  1.00  7.07           C  
ATOM   4898  CG2 VAL A 693      87.698  98.354  90.444  1.00  7.07           C  
ATOM   4899  N   PHE A 694      91.827  96.622  90.876  1.00  2.81           N  
ATOM   4900  CA  PHE A 694      93.272  96.439  90.786  1.00  2.81           C  
ATOM   4901  C   PHE A 694      93.642  95.052  90.276  1.00  2.81           C  
ATOM   4902  O   PHE A 694      94.553  94.905  89.452  1.00  2.81           O  
ATOM   4903  CB  PHE A 694      93.888  96.701  92.158  1.00  2.81           C  
ATOM   4904  CG  PHE A 694      95.278  96.173  92.315  1.00  2.81           C  
ATOM   4905  CD1 PHE A 694      96.363  96.865  91.813  1.00  2.81           C  
ATOM   4906  CD2 PHE A 694      95.501  94.998  93.008  1.00  2.81           C  
ATOM   4907  CE1 PHE A 694      97.634  96.379  91.976  1.00  2.81           C  
ATOM   4908  CE2 PHE A 694      96.769  94.510  93.172  1.00  2.81           C  
ATOM   4909  CZ  PHE A 694      97.838  95.201  92.655  1.00  2.81           C  
ATOM   4910  N   ASN A 695      92.960  94.022  90.773  1.00  5.02           N  
ATOM   4911  CA  ASN A 695      93.245  92.656  90.352  1.00  5.02           C  
ATOM   4912  C   ASN A 695      92.944  92.470  88.869  1.00  5.02           C  
ATOM   4913  O   ASN A 695      93.742  91.873  88.129  1.00  5.02           O  
ATOM   4914  CB  ASN A 695      92.428  91.695  91.217  1.00  5.02           C  
ATOM   4915  CG  ASN A 695      92.889  90.263  91.108  1.00  5.02           C  
ATOM   4916  OD1 ASN A 695      93.791  89.940  90.340  1.00  5.02           O  
ATOM   4917  ND2 ASN A 695      92.273  89.393  91.889  1.00  5.02           N  
ATOM   4918  N   ILE A 696      91.811  93.009  88.407  1.00  8.10           N  
ATOM   4919  CA  ILE A 696      91.494  92.947  86.982  1.00  8.10           C  
ATOM   4920  C   ILE A 696      92.529  93.715  86.166  1.00  8.10           C  
ATOM   4921  O   ILE A 696      92.950  93.266  85.094  1.00  8.10           O  
ATOM   4922  CB  ILE A 696      90.063  93.455  86.723  1.00  8.10           C  
ATOM   4923  CG1 ILE A 696      89.040  92.438  87.223  1.00  8.10           C  
ATOM   4924  CG2 ILE A 696      89.836  93.725  85.245  1.00  8.10           C  
ATOM   4925  CD1 ILE A 696      87.649  92.995  87.356  1.00  8.10           C  
ATOM   4926  N   CYS A 697      92.948  94.883  86.652  1.00  4.78           N  
ATOM   4927  CA  CYS A 697      93.960  95.670  85.953  1.00  4.78           C  
ATOM   4928  C   CYS A 697      95.257  94.888  85.783  1.00  4.78           C  
ATOM   4929  O   CYS A 697      95.850  94.870  84.698  1.00  4.78           O  
ATOM   4930  CB  CYS A 697      94.214  96.975  86.711  1.00  4.78           C  
ATOM   4931  SG  CYS A 697      95.559  97.984  86.055  1.00  4.78           S  
ATOM   4932  N   GLN A 698      95.713  94.235  86.853  1.00  7.52           N  
ATOM   4933  CA  GLN A 698      96.952  93.468  86.776  1.00  7.52           C  
ATOM   4934  C   GLN A 698      96.817  92.282  85.830  1.00  7.52           C  
ATOM   4935  O   GLN A 698      97.760  91.958  85.097  1.00  7.52           O  
ATOM   4936  CB  GLN A 698      97.378  93.003  88.170  1.00  7.52           C  
ATOM   4937  CG  GLN A 698      97.810  94.097  89.168  1.00  7.52           C  
ATOM   4938  CD  GLN A 698      98.953  94.999  88.695  1.00  7.52           C  
ATOM   4939  OE1 GLN A 698      99.026  95.400  87.536  1.00  7.52           O  
ATOM   4940  NE2 GLN A 698      99.861  95.310  89.609  1.00  7.52           N  
ATOM   4941  N   ALA A 699      95.649  91.628  85.815  1.00  6.03           N  
ATOM   4942  CA  ALA A 699      95.456  90.512  84.893  1.00  6.03           C  
ATOM   4943  C   ALA A 699      95.435  90.965  83.434  1.00  6.03           C  
ATOM   4944  O   ALA A 699      96.013  90.293  82.567  1.00  6.03           O  
ATOM   4945  CB  ALA A 699      94.170  89.768  85.235  1.00  6.03           C  
ATOM   4946  N   VAL A 700      94.798  92.100  83.142  1.00  5.01           N  
ATOM   4947  CA  VAL A 700      94.804  92.609  81.772  1.00  5.01           C  
ATOM   4948  C   VAL A 700      96.205  93.045  81.362  1.00  5.01           C  
ATOM   4949  O   VAL A 700      96.604  92.861  80.206  1.00  5.01           O  
ATOM   4950  CB  VAL A 700      93.779  93.748  81.608  1.00  5.01           C  
ATOM   4951  CG1 VAL A 700      93.709  94.196  80.168  1.00  5.01           C  
ATOM   4952  CG2 VAL A 700      92.407  93.286  82.051  1.00  5.01           C  
ATOM   4953  N   THR A 701      96.977  93.615  82.289  1.00  7.58           N  
ATOM   4954  CA  THR A 701      98.360  93.962  81.979  1.00  7.58           C  
ATOM   4955  C   THR A 701      99.178  92.716  81.663  1.00  7.58           C  
ATOM   4956  O   THR A 701      99.981  92.708  80.723  1.00  7.58           O  
ATOM   4957  CB  THR A 701      98.987  94.732  83.140  1.00  7.58           C  
ATOM   4958  OG1 THR A 701      98.109  95.785  83.543  1.00  7.58           O  
ATOM   4959  CG2 THR A 701     100.321  95.316  82.726  1.00  7.58           C  
ATOM   4960  N   ALA A 702      98.990  91.653  82.448  1.00 16.74           N  
ATOM   4961  CA  ALA A 702      99.696  90.406  82.185  1.00 16.74           C  
ATOM   4962  C   ALA A 702      99.349  89.855  80.809  1.00 16.74           C  
ATOM   4963  O   ALA A 702     100.234  89.400  80.075  1.00 16.74           O  
ATOM   4964  CB  ALA A 702      99.375  89.382  83.272  1.00 16.74           C  
ATOM   4965  N   ASN A 703      98.070  89.905  80.433  1.00  7.83           N  
ATOM   4966  CA  ASN A 703      97.681  89.399  79.119  1.00  7.83           C  
ATOM   4967  C   ASN A 703      98.264  90.247  77.993  1.00  7.83           C  
ATOM   4968  O   ASN A 703      98.749  89.708  76.990  1.00  7.83           O  
ATOM   4969  CB  ASN A 703      96.161  89.331  79.007  1.00  7.83           C  
ATOM   4970  CG  ASN A 703      95.577  88.154  79.753  1.00  7.83           C  
ATOM   4971  OD1 ASN A 703      95.368  87.090  79.179  1.00  7.83           O  
ATOM   4972  ND2 ASN A 703      95.312  88.336  81.037  1.00  7.83           N  
ATOM   4973  N   VAL A 704      98.231  91.573  78.140  1.00  8.08           N  
ATOM   4974  CA  VAL A 704      98.780  92.453  77.111  1.00  8.08           C  
ATOM   4975  C   VAL A 704     100.279  92.222  76.948  1.00  8.08           C  
ATOM   4976  O   VAL A 704     100.792  92.160  75.824  1.00  8.08           O  
ATOM   4977  CB  VAL A 704      98.460  93.923  77.441  1.00  8.08           C  
ATOM   4978  CG1 VAL A 704      99.320  94.855  76.614  1.00  8.08           C  
ATOM   4979  CG2 VAL A 704      96.997  94.209  77.189  1.00  8.08           C  
ATOM   4980  N   ASN A 705     101.006  92.090  78.062  1.00 10.41           N  
ATOM   4981  CA  ASN A 705     102.448  91.874  77.979  1.00 10.41           C  
ATOM   4982  C   ASN A 705     102.778  90.510  77.386  1.00 10.41           C  
ATOM   4983  O   ASN A 705     103.735  90.380  76.612  1.00 10.41           O  
ATOM   4984  CB  ASN A 705     103.089  92.023  79.357  1.00 10.41           C  
ATOM   4985  CG  ASN A 705     103.220  93.466  79.784  1.00 10.41           C  
ATOM   4986  OD1 ASN A 705     103.246  94.368  78.952  1.00 10.41           O  
ATOM   4987  ND2 ASN A 705     103.311  93.692  81.084  1.00 10.41           N  
ATOM   4988  N   ALA A 706     102.005  89.481  77.738  1.00 11.13           N  
ATOM   4989  CA  ALA A 706     102.210  88.169  77.139  1.00 11.13           C  
ATOM   4990  C   ALA A 706     101.991  88.219  75.635  1.00 11.13           C  
ATOM   4991  O   ALA A 706     102.757  87.631  74.864  1.00 11.13           O  
ATOM   4992  CB  ALA A 706     101.278  87.146  77.785  1.00 11.13           C  
ATOM   4993  N   LEU A 707     100.947  88.924  75.197  1.00 12.20           N  
ATOM   4994  CA  LEU A 707     100.658  88.979  73.769  1.00 12.20           C  
ATOM   4995  C   LEU A 707     101.701  89.795  73.013  1.00 12.20           C  
ATOM   4996  O   LEU A 707     102.079  89.435  71.894  1.00 12.20           O  
ATOM   4997  CB  LEU A 707      99.256  89.538  73.538  1.00 12.20           C  
ATOM   4998  CG  LEU A 707      98.608  89.204  72.195  1.00 12.20           C  
ATOM   4999  CD1 LEU A 707      98.632  87.710  71.951  1.00 12.20           C  
ATOM   5000  CD2 LEU A 707      97.183  89.713  72.165  1.00 12.20           C  
ATOM   5001  N   LEU A 708     102.184  90.892  73.597  1.00 12.62           N  
ATOM   5002  CA  LEU A 708     103.155  91.721  72.890  1.00 12.62           C  
ATOM   5003  C   LEU A 708     104.587  91.211  72.995  1.00 12.62           C  
ATOM   5004  O   LEU A 708     105.440  91.659  72.224  1.00 12.62           O  
ATOM   5005  CB  LEU A 708     103.090  93.166  73.384  1.00 12.62           C  
ATOM   5006  CG  LEU A 708     101.823  93.942  73.022  1.00 12.62           C  
ATOM   5007  CD1 LEU A 708     102.013  95.421  73.282  1.00 12.62           C  
ATOM   5008  CD2 LEU A 708     101.468  93.702  71.572  1.00 12.62           C  
ATOM   5009  N   SER A 709     104.877  90.292  73.913  1.00 17.18           N  
ATOM   5010  CA  SER A 709     106.227  89.756  74.027  1.00 17.18           C  
ATOM   5011  C   SER A 709     106.462  88.517  73.171  1.00 17.18           C  
ATOM   5012  O   SER A 709     107.581  87.995  73.165  1.00 17.18           O  
ATOM   5013  CB  SER A 709     106.544  89.429  75.487  1.00 17.18           C  
ATOM   5014  OG  SER A 709     106.098  88.133  75.837  1.00 17.18           O  
ATOM   5015  N   THR A 710     105.447  88.023  72.467  1.00 24.78           N  
ATOM   5016  CA  THR A 710     105.602  86.817  71.669  1.00 24.78           C  
ATOM   5017  C   THR A 710     106.063  87.155  70.254  1.00 24.78           C  
ATOM   5018  O   THR A 710     105.815  88.249  69.739  1.00 24.78           O  
ATOM   5019  CB  THR A 710     104.293  86.024  71.622  1.00 24.78           C  
ATOM   5020  OG1 THR A 710     104.534  84.727  71.066  1.00 24.78           O  
ATOM   5021  CG2 THR A 710     103.264  86.732  70.770  1.00 24.78           C  
ATOM   5022  N   ASP A 711     106.761  86.203  69.636  1.00 36.14           N  
ATOM   5023  CA  ASP A 711     107.259  86.367  68.272  1.00 36.14           C  
ATOM   5024  C   ASP A 711     106.090  86.323  67.297  1.00 36.14           C  
ATOM   5025  O   ASP A 711     105.464  85.275  67.112  1.00 36.14           O  
ATOM   5026  CB  ASP A 711     108.281  85.280  67.951  1.00 36.14           C  
ATOM   5027  CG  ASP A 711     109.222  85.676  66.830  1.00 36.14           C  
ATOM   5028  OD1 ASP A 711     108.861  86.562  66.029  1.00 36.14           O  
ATOM   5029  OD2 ASP A 711     110.326  85.099  66.748  1.00 36.14           O  
ATOM   5030  N   GLY A 712     105.794  87.464  66.672  1.00 34.98           N  
ATOM   5031  CA  GLY A 712     104.650  87.539  65.780  1.00 34.98           C  
ATOM   5032  C   GLY A 712     104.752  86.625  64.577  1.00 34.98           C  
ATOM   5033  O   GLY A 712     103.735  86.140  64.076  1.00 34.98           O  
ATOM   5034  N   ASN A 713     105.970  86.382  64.091  1.00 39.19           N  
ATOM   5035  CA  ASN A 713     106.135  85.515  62.930  1.00 39.19           C  
ATOM   5036  C   ASN A 713     105.793  84.068  63.257  1.00 39.19           C  
ATOM   5037  O   ASN A 713     105.390  83.313  62.366  1.00 39.19           O  
ATOM   5038  CB  ASN A 713     107.562  85.619  62.395  1.00 39.19           C  
ATOM   5039  CG  ASN A 713     107.873  86.990  61.829  1.00 39.19           C  
ATOM   5040  OD1 ASN A 713     107.267  87.423  60.850  1.00 39.19           O  
ATOM   5041  ND2 ASN A 713     108.819  87.684  62.449  1.00 39.19           N  
ATOM   5042  N   LYS A 714     105.939  83.667  64.518  1.00 38.66           N  
ATOM   5043  CA  LYS A 714     105.655  82.297  64.921  1.00 38.66           C  
ATOM   5044  C   LYS A 714     104.191  82.058  65.264  1.00 38.66           C  
ATOM   5045  O   LYS A 714     103.789  80.899  65.407  1.00 38.66           O  
ATOM   5046  CB  LYS A 714     106.527  81.909  66.118  1.00 38.66           C  
ATOM   5047  CG  LYS A 714     108.014  82.085  65.874  1.00 38.66           C  
ATOM   5048  CD  LYS A 714     108.826  81.046  66.629  1.00 38.66           C  
ATOM   5049  CE  LYS A 714     110.315  81.241  66.402  1.00 38.66           C  
ATOM   5050  NZ  LYS A 714     110.592  81.892  65.093  1.00 38.66           N  
ATOM   5051  N   ILE A 715     103.389  83.113  65.405  1.00 34.53           N  
ATOM   5052  CA  ILE A 715     101.958  82.957  65.641  1.00 34.53           C  
ATOM   5053  C   ILE A 715     101.330  82.334  64.403  1.00 34.53           C  
ATOM   5054  O   ILE A 715     101.321  82.940  63.326  1.00 34.53           O  
ATOM   5055  CB  ILE A 715     101.285  84.298  65.981  1.00 34.53           C  
ATOM   5056  CG1 ILE A 715     101.676  84.760  67.383  1.00 34.53           C  
ATOM   5057  CG2 ILE A 715      99.775  84.174  65.875  1.00 34.53           C  
ATOM   5058  CD1 ILE A 715     101.592  86.255  67.561  1.00 34.53           C  
ATOM   5059  N   ALA A 716     100.802  81.118  64.546  1.00 37.25           N  
ATOM   5060  CA  ALA A 716     100.248  80.416  63.394  1.00 37.25           C  
ATOM   5061  C   ALA A 716      98.904  80.989  62.967  1.00 37.25           C  
ATOM   5062  O   ALA A 716      98.571  80.957  61.777  1.00 37.25           O  
ATOM   5063  CB  ALA A 716     100.113  78.926  63.704  1.00 37.25           C  
ATOM   5064  N   ASP A 717      98.125  81.514  63.908  1.00 36.86           N  
ATOM   5065  CA  ASP A 717      96.764  81.951  63.621  1.00 36.86           C  
ATOM   5066  C   ASP A 717      96.785  83.356  63.031  1.00 36.86           C  
ATOM   5067  O   ASP A 717      97.355  84.277  63.625  1.00 36.86           O  
ATOM   5068  CB  ASP A 717      95.918  81.904  64.892  1.00 36.86           C  
ATOM   5069  CG  ASP A 717      94.429  82.035  64.614  1.00 36.86           C  
ATOM   5070  OD1 ASP A 717      94.034  82.870  63.774  1.00 36.86           O  
ATOM   5071  OD2 ASP A 717      93.647  81.290  65.241  1.00 36.86           O  
ATOM   5072  N   LYS A 718      96.170  83.514  61.857  1.00 35.66           N  
ATOM   5073  CA  LYS A 718      96.048  84.829  61.234  1.00 35.66           C  
ATOM   5074  C   LYS A 718      95.338  85.821  62.148  1.00 35.66           C  
ATOM   5075  O   LYS A 718      95.755  86.982  62.269  1.00 35.66           O  
ATOM   5076  CB  LYS A 718      95.301  84.692  59.907  1.00 35.66           C  
ATOM   5077  CG  LYS A 718      94.972  85.997  59.205  1.00 35.66           C  
ATOM   5078  CD  LYS A 718      96.216  86.768  58.816  1.00 35.66           C  
ATOM   5079  CE  LYS A 718      95.855  88.174  58.367  1.00 35.66           C  
ATOM   5080  NZ  LYS A 718      94.830  88.794  59.253  1.00 35.66           N  
ATOM   5081  N   TYR A 719      94.269  85.375  62.812  1.00 28.89           N  
ATOM   5082  CA  TYR A 719      93.465  86.278  63.628  1.00 28.89           C  
ATOM   5083  C   TYR A 719      94.261  86.819  64.809  1.00 28.89           C  
ATOM   5084  O   TYR A 719      94.218  88.018  65.100  1.00 28.89           O  
ATOM   5085  CB  TYR A 719      92.205  85.563  64.114  1.00 28.89           C  
ATOM   5086  CG  TYR A 719      91.393  86.376  65.091  1.00 28.89           C  
ATOM   5087  CD1 TYR A 719      90.867  87.608  64.729  1.00 28.89           C  
ATOM   5088  CD2 TYR A 719      91.169  85.923  66.382  1.00 28.89           C  
ATOM   5089  CE1 TYR A 719      90.130  88.358  65.621  1.00 28.89           C  
ATOM   5090  CE2 TYR A 719      90.434  86.668  67.280  1.00 28.89           C  
ATOM   5091  CZ  TYR A 719      89.918  87.885  66.895  1.00 28.89           C  
ATOM   5092  OH  TYR A 719      89.186  88.629  67.787  1.00 28.89           O  
ATOM   5093  N   VAL A 720      95.004  85.952  65.496  1.00 26.27           N  
ATOM   5094  CA  VAL A 720      95.752  86.403  66.664  1.00 26.27           C  
ATOM   5095  C   VAL A 720      96.935  87.276  66.257  1.00 26.27           C  
ATOM   5096  O   VAL A 720      97.292  88.214  66.976  1.00 26.27           O  
ATOM   5097  CB  VAL A 720      96.198  85.198  67.508  1.00 26.27           C  
ATOM   5098  CG1 VAL A 720      96.870  85.662  68.784  1.00 26.27           C  
ATOM   5099  CG2 VAL A 720      95.005  84.321  67.834  1.00 26.27           C  
ATOM   5100  N   ARG A 721      97.555  87.002  65.108  1.00 31.98           N  
ATOM   5101  CA  ARG A 721      98.625  87.870  64.622  1.00 31.98           C  
ATOM   5102  C   ARG A 721      98.099  89.264  64.294  1.00 31.98           C  
ATOM   5103  O   ARG A 721      98.720  90.278  64.652  1.00 31.98           O  
ATOM   5104  CB  ARG A 721      99.288  87.228  63.405  1.00 31.98           C  
ATOM   5105  CG  ARG A 721     100.709  87.683  63.151  1.00 31.98           C  
ATOM   5106  CD  ARG A 721     101.207  87.213  61.793  1.00 31.98           C  
ATOM   5107  NE  ARG A 721     101.183  85.757  61.682  1.00 31.98           N  
ATOM   5108  CZ  ARG A 721     100.353  85.075  60.899  1.00 31.98           C  
ATOM   5109  NH1 ARG A 721      99.470  85.713  60.145  1.00 31.98           N  
ATOM   5110  NH2 ARG A 721     100.408  83.752  60.868  1.00 31.98           N  
ATOM   5111  N   ASN A 722      96.939  89.336  63.638  1.00 27.38           N  
ATOM   5112  CA  ASN A 722      96.335  90.636  63.369  1.00 27.38           C  
ATOM   5113  C   ASN A 722      95.935  91.333  64.666  1.00 27.38           C  
ATOM   5114  O   ASN A 722      96.058  92.560  64.786  1.00 27.38           O  
ATOM   5115  CB  ASN A 722      95.129  90.468  62.447  1.00 27.38           C  
ATOM   5116  CG  ASN A 722      94.509  91.789  62.053  1.00 27.38           C  
ATOM   5117  OD1 ASN A 722      95.208  92.780  61.847  1.00 27.38           O  
ATOM   5118  ND2 ASN A 722      93.186  91.812  61.946  1.00 27.38           N  
ATOM   5119  N   LEU A 723      95.468  90.562  65.652  1.00 22.56           N  
ATOM   5120  CA  LEU A 723      95.125  91.130  66.950  1.00 22.56           C  
ATOM   5121  C   LEU A 723      96.348  91.710  67.644  1.00 22.56           C  
ATOM   5122  O   LEU A 723      96.264  92.773  68.263  1.00 22.56           O  
ATOM   5123  CB  LEU A 723      94.473  90.068  67.831  1.00 22.56           C  
ATOM   5124  CG  LEU A 723      93.613  90.575  68.991  1.00 22.56           C  
ATOM   5125  CD1 LEU A 723      92.298  91.144  68.488  1.00 22.56           C  
ATOM   5126  CD2 LEU A 723      93.377  89.466  69.996  1.00 22.56           C  
ATOM   5127  N   GLN A 724      97.488  91.024  67.564  1.00 21.53           N  
ATOM   5128  CA  GLN A 724      98.710  91.552  68.164  1.00 21.53           C  
ATOM   5129  C   GLN A 724      99.141  92.844  67.484  1.00 21.53           C  
ATOM   5130  O   GLN A 724      99.523  93.815  68.156  1.00 21.53           O  
ATOM   5131  CB  GLN A 724      99.830  90.520  68.080  1.00 21.53           C  
ATOM   5132  CG  GLN A 724     101.208  91.148  68.057  1.00 21.53           C  
ATOM   5133  CD  GLN A 724     102.317  90.135  68.120  1.00 21.53           C  
ATOM   5134  OE1 GLN A 724     102.916  89.782  67.109  1.00 21.53           O  
ATOM   5135  NE2 GLN A 724     102.592  89.650  69.315  1.00 21.53           N  
ATOM   5136  N   HIS A 725      99.078  92.875  66.151  1.00 25.48           N  
ATOM   5137  CA  HIS A 725      99.434  94.094  65.431  1.00 25.48           C  
ATOM   5138  C   HIS A 725      98.540  95.258  65.837  1.00 25.48           C  
ATOM   5139  O   HIS A 725      99.028  96.365  66.111  1.00 25.48           O  
ATOM   5140  CB  HIS A 725      99.339  93.850  63.927  1.00 25.48           C  
ATOM   5141  CG  HIS A 725      99.954  94.932  63.098  1.00 25.48           C  
ATOM   5142  ND1 HIS A 725      99.207  95.880  62.436  1.00 25.48           N  
ATOM   5143  CD2 HIS A 725     101.250  95.215  62.826  1.00 25.48           C  
ATOM   5144  CE1 HIS A 725     100.016  96.700  61.789  1.00 25.48           C  
ATOM   5145  NE2 HIS A 725     101.261  96.318  62.010  1.00 25.48           N  
ATOM   5146  N   ARG A 726      97.234  95.053  65.895  1.00 21.28           N  
ATOM   5147  CA  ARG A 726      96.281  96.130  66.266  1.00 21.28           C  
ATOM   5148  C   ARG A 726      96.408  96.505  67.736  1.00 21.28           C  
ATOM   5149  O   ARG A 726      96.175  97.647  68.058  1.00 21.28           O  
ATOM   5150  CB  ARG A 726      94.867  95.736  65.854  1.00 21.28           C  
ATOM   5151  CG  ARG A 726      94.427  96.301  64.513  1.00 21.28           C  
ATOM   5152  CD  ARG A 726      93.030  95.814  64.194  1.00 21.28           C  
ATOM   5153  NE  ARG A 726      92.943  94.386  64.457  1.00 21.28           N  
ATOM   5154  CZ  ARG A 726      91.833  93.750  64.796  1.00 21.28           C  
ATOM   5155  NH1 ARG A 726      90.701  94.418  64.917  1.00 21.28           N  
ATOM   5156  NH2 ARG A 726      91.860  92.449  65.018  1.00 21.28           N  
ATOM   5157  N   LEU A 727      96.767  95.559  68.592  1.00 15.94           N  
ATOM   5158  CA  LEU A 727      97.024  95.897  69.990  1.00 15.94           C  
ATOM   5159  C   LEU A 727      98.225  96.821  70.124  1.00 15.94           C  
ATOM   5160  O   LEU A 727      98.173  97.829  70.842  1.00 15.94           O  
ATOM   5161  CB  LEU A 727      97.237  94.619  70.802  1.00 15.94           C  
ATOM   5162  CG  LEU A 727      97.491  94.768  72.302  1.00 15.94           C  
ATOM   5163  CD1 LEU A 727      96.224  95.155  73.027  1.00 15.94           C  
ATOM   5164  CD2 LEU A 727      98.059  93.486  72.876  1.00 15.94           C  
ATOM   5165  N   TYR A 728      99.325  96.494  69.444  1.00 17.69           N  
ATOM   5166  CA  TYR A 728     100.495  97.364  69.509  1.00 17.69           C  
ATOM   5167  C   TYR A 728     100.168  98.745  68.954  1.00 17.69           C  
ATOM   5168  O   TYR A 728     100.525  99.772  69.549  1.00 17.69           O  
ATOM   5169  CB  TYR A 728     101.666  96.746  68.747  1.00 17.69           C  
ATOM   5170  CG  TYR A 728     102.937  97.556  68.852  1.00 17.69           C  
ATOM   5171  CD1 TYR A 728     103.222  98.557  67.937  1.00 17.69           C  
ATOM   5172  CD2 TYR A 728     103.855  97.313  69.861  1.00 17.69           C  
ATOM   5173  CE1 TYR A 728     104.375  99.299  68.029  1.00 17.69           C  
ATOM   5174  CE2 TYR A 728     105.016  98.047  69.959  1.00 17.69           C  
ATOM   5175  CZ  TYR A 728     105.272  99.038  69.039  1.00 17.69           C  
ATOM   5176  OH  TYR A 728     106.428  99.772  69.132  1.00 17.69           O  
ATOM   5177  N   GLU A 729      99.484  98.785  67.806  1.00 21.74           N  
ATOM   5178  CA  GLU A 729      99.108 100.061  67.209  1.00 21.74           C  
ATOM   5179  C   GLU A 729      98.218 100.872  68.142  1.00 21.74           C  
ATOM   5180  O   GLU A 729      98.358 102.096  68.235  1.00 21.74           O  
ATOM   5181  CB  GLU A 729      98.406  99.820  65.874  1.00 21.74           C  
ATOM   5182  CG  GLU A 729      97.586 100.995  65.380  1.00 21.74           C  
ATOM   5183  CD  GLU A 729      96.801 100.666  64.128  1.00 21.74           C  
ATOM   5184  OE1 GLU A 729      96.232 101.595  63.518  1.00 21.74           O  
ATOM   5185  OE2 GLU A 729      96.754  99.475  63.756  1.00 21.74           O  
ATOM   5186  N   CYS A 730      97.298 100.209  68.843  1.00 20.25           N  
ATOM   5187  CA  CYS A 730      96.359 100.916  69.703  1.00 20.25           C  
ATOM   5188  C   CYS A 730      97.009 101.405  70.988  1.00 20.25           C  
ATOM   5189  O   CYS A 730      96.553 102.398  71.563  1.00 20.25           O  
ATOM   5190  CB  CYS A 730      95.168 100.015  70.027  1.00 20.25           C  
ATOM   5191  SG  CYS A 730      93.658 100.895  70.458  1.00 20.25           S  
ATOM   5192  N   LEU A 731      98.057 100.731  71.460  1.00 12.95           N  
ATOM   5193  CA  LEU A 731      98.779 101.261  72.614  1.00 12.95           C  
ATOM   5194  C   LEU A 731      99.699 102.414  72.228  1.00 12.95           C  
ATOM   5195  O   LEU A 731      99.569 103.523  72.755  1.00 12.95           O  
ATOM   5196  CB  LEU A 731      99.571 100.162  73.323  1.00 12.95           C  
ATOM   5197  CG  LEU A 731      98.859  99.381  74.429  1.00 12.95           C  
ATOM   5198  CD1 LEU A 731      97.828  98.415  73.886  1.00 12.95           C  
ATOM   5199  CD2 LEU A 731      99.875  98.654  75.288  1.00 12.95           C  
ATOM   5200  N   TYR A 732     100.642 102.179  71.313  1.00 12.85           N  
ATOM   5201  CA  TYR A 732     101.714 103.154  71.138  1.00 12.85           C  
ATOM   5202  C   TYR A 732     101.586 104.049  69.912  1.00 12.85           C  
ATOM   5203  O   TYR A 732     102.332 105.027  69.816  1.00 12.85           O  
ATOM   5204  CB  TYR A 732     103.076 102.452  71.115  1.00 12.85           C  
ATOM   5205  CG  TYR A 732     103.337 101.631  72.353  1.00 12.85           C  
ATOM   5206  CD1 TYR A 732     103.554 102.246  73.574  1.00 12.85           C  
ATOM   5207  CD2 TYR A 732     103.366 100.248  72.304  1.00 12.85           C  
ATOM   5208  CE1 TYR A 732     103.791 101.509  74.711  1.00 12.85           C  
ATOM   5209  CE2 TYR A 732     103.601  99.501  73.438  1.00 12.85           C  
ATOM   5210  CZ  TYR A 732     103.814 100.137  74.639  1.00 12.85           C  
ATOM   5211  OH  TYR A 732     104.051  99.399  75.774  1.00 12.85           O  
ATOM   5212  N   ARG A 733     100.680 103.768  68.983  1.00 22.87           N  
ATOM   5213  CA  ARG A 733     100.531 104.624  67.809  1.00 22.87           C  
ATOM   5214  C   ARG A 733      99.279 105.485  67.825  1.00 22.87           C  
ATOM   5215  O   ARG A 733      99.316 106.616  67.340  1.00 22.87           O  
ATOM   5216  CB  ARG A 733     100.556 103.786  66.525  1.00 22.87           C  
ATOM   5217  CG  ARG A 733     101.894 103.116  66.245  1.00 22.87           C  
ATOM   5218  CD  ARG A 733     102.941 104.163  65.885  1.00 22.87           C  
ATOM   5219  NE  ARG A 733     104.079 103.611  65.154  1.00 22.87           N  
ATOM   5220  CZ  ARG A 733     105.249 103.301  65.702  1.00 22.87           C  
ATOM   5221  NH1 ARG A 733     105.449 103.483  66.999  1.00 22.87           N  
ATOM   5222  NH2 ARG A 733     106.222 102.807  64.950  1.00 22.87           N  
ATOM   5223  N   ASN A 734      98.168 104.993  68.362  1.00 25.73           N  
ATOM   5224  CA  ASN A 734      96.959 105.796  68.475  1.00 25.73           C  
ATOM   5225  C   ASN A 734      96.878 106.441  69.852  1.00 25.73           C  
ATOM   5226  O   ASN A 734      97.418 105.927  70.834  1.00 25.73           O  
ATOM   5227  CB  ASN A 734      95.703 104.954  68.232  1.00 25.73           C  
ATOM   5228  CG  ASN A 734      95.713 104.248  66.889  1.00 25.73           C  
ATOM   5229  OD1 ASN A 734      96.527 104.563  66.021  1.00 25.73           O  
ATOM   5230  ND2 ASN A 734      94.830 103.272  66.720  1.00 25.73           N  
ATOM   5231  N   ARG A 735      96.192 107.579  69.915  1.00 24.99           N  
ATOM   5232  CA  ARG A 735      95.916 108.237  71.185  1.00 24.99           C  
ATOM   5233  C   ARG A 735      94.439 108.488  71.437  1.00 24.99           C  
ATOM   5234  O   ARG A 735      94.054 108.649  72.602  1.00 24.99           O  
ATOM   5235  CB  ARG A 735      96.684 109.564  71.284  1.00 24.99           C  
ATOM   5236  CG  ARG A 735      97.997 109.417  72.038  1.00 24.99           C  
ATOM   5237  CD  ARG A 735      98.972 110.543  71.768  1.00 24.99           C  
ATOM   5238  NE  ARG A 735      98.380 111.863  71.937  1.00 24.99           N  
ATOM   5239  CZ  ARG A 735      99.041 112.997  71.742  1.00 24.99           C  
ATOM   5240  NH1 ARG A 735     100.313 112.965  71.371  1.00 24.99           N  
ATOM   5241  NH2 ARG A 735      98.435 114.162  71.918  1.00 24.99           N  
ATOM   5242  N   ASP A 736      93.601 108.520  70.405  1.00 31.02           N  
ATOM   5243  CA  ASP A 736      92.169 108.386  70.607  1.00 31.02           C  
ATOM   5244  C   ASP A 736      91.841 106.953  71.009  1.00 31.02           C  
ATOM   5245  O   ASP A 736      92.529 106.004  70.623  1.00 31.02           O  
ATOM   5246  CB  ASP A 736      91.406 108.758  69.335  1.00 31.02           C  
ATOM   5247  CG  ASP A 736      91.527 110.230  68.990  1.00 31.02           C  
ATOM   5248  OD1 ASP A 736      92.550 110.847  69.351  1.00 31.02           O  
ATOM   5249  OD2 ASP A 736      90.599 110.769  68.352  1.00 31.02           O  
ATOM   5250  N   VAL A 737      90.781 106.796  71.796  1.00 23.21           N  
ATOM   5251  CA  VAL A 737      90.365 105.463  72.217  1.00 23.21           C  
ATOM   5252  C   VAL A 737      89.676 104.769  71.049  1.00 23.21           C  
ATOM   5253  O   VAL A 737      88.711 105.291  70.478  1.00 23.21           O  
ATOM   5254  CB  VAL A 737      89.448 105.536  73.442  1.00 23.21           C  
ATOM   5255  CG1 VAL A 737      89.122 104.139  73.943  1.00 23.21           C  
ATOM   5256  CG2 VAL A 737      90.099 106.362  74.530  1.00 23.21           C  
ATOM   5257  N   ASP A 738      90.179 103.592  70.680  1.00 24.11           N  
ATOM   5258  CA  ASP A 738      89.568 102.772  69.634  1.00 24.11           C  
ATOM   5259  C   ASP A 738      88.576 101.833  70.305  1.00 24.11           C  
ATOM   5260  O   ASP A 738      88.924 100.738  70.744  1.00 24.11           O  
ATOM   5261  CB  ASP A 738      90.630 102.014  68.850  1.00 24.11           C  
ATOM   5262  CG  ASP A 738      90.087 101.402  67.573  1.00 24.11           C  
ATOM   5263  OD1 ASP A 738      89.004 101.828  67.122  1.00 24.11           O  
ATOM   5264  OD2 ASP A 738      90.740 100.494  67.022  1.00 24.11           O  
ATOM   5265  N   THR A 739      87.317 102.271  70.385  1.00 21.26           N  
ATOM   5266  CA  THR A 739      86.313 101.508  71.118  1.00 21.26           C  
ATOM   5267  C   THR A 739      86.071 100.138  70.498  1.00 21.26           C  
ATOM   5268  O   THR A 739      85.782  99.177  71.219  1.00 21.26           O  
ATOM   5269  CB  THR A 739      85.004 102.294  71.189  1.00 21.26           C  
ATOM   5270  OG1 THR A 739      84.631 102.721  69.874  1.00 21.26           O  
ATOM   5271  CG2 THR A 739      85.165 103.510  72.087  1.00 21.26           C  
ATOM   5272  N   ASP A 740      86.195 100.022  69.175  1.00 20.10           N  
ATOM   5273  CA  ASP A 740      85.976  98.731  68.535  1.00 20.10           C  
ATOM   5274  C   ASP A 740      87.056  97.728  68.916  1.00 20.10           C  
ATOM   5275  O   ASP A 740      86.756  96.549  69.146  1.00 20.10           O  
ATOM   5276  CB  ASP A 740      85.918  98.903  67.021  1.00 20.10           C  
ATOM   5277  CG  ASP A 740      84.703  99.686  66.574  1.00 20.10           C  
ATOM   5278  OD1 ASP A 740      83.581  99.325  66.981  1.00 20.10           O  
ATOM   5279  OD2 ASP A 740      84.871 100.669  65.823  1.00 20.10           O  
ATOM   5280  N   PHE A 741      88.305  98.178  69.045  1.00 16.06           N  
ATOM   5281  CA  PHE A 741      89.339  97.253  69.483  1.00 16.06           C  
ATOM   5282  C   PHE A 741      89.230  96.935  70.968  1.00 16.06           C  
ATOM   5283  O   PHE A 741      89.567  95.825  71.384  1.00 16.06           O  
ATOM   5284  CB  PHE A 741      90.735  97.780  69.174  1.00 16.06           C  
ATOM   5285  CG  PHE A 741      91.789  96.733  69.318  1.00 16.06           C  
ATOM   5286  CD1 PHE A 741      91.874  95.693  68.415  1.00 16.06           C  
ATOM   5287  CD2 PHE A 741      92.645  96.744  70.401  1.00 16.06           C  
ATOM   5288  CE1 PHE A 741      92.823  94.710  68.564  1.00 16.06           C  
ATOM   5289  CE2 PHE A 741      93.592  95.763  70.555  1.00 16.06           C  
ATOM   5290  CZ  PHE A 741      93.683  94.745  69.635  1.00 16.06           C  
ATOM   5291  N   VAL A 742      88.778  97.884  71.786  1.00 14.20           N  
ATOM   5292  CA  VAL A 742      88.532  97.561  73.188  1.00 14.20           C  
ATOM   5293  C   VAL A 742      87.446  96.498  73.296  1.00 14.20           C  
ATOM   5294  O   VAL A 742      87.570  95.540  74.069  1.00 14.20           O  
ATOM   5295  CB  VAL A 742      88.173  98.827  73.986  1.00 14.20           C  
ATOM   5296  CG1 VAL A 742      88.037  98.492  75.457  1.00 14.20           C  
ATOM   5297  CG2 VAL A 742      89.232  99.891  73.793  1.00 14.20           C  
ATOM   5298  N   ASN A 743      86.381  96.632  72.498  1.00 15.26           N  
ATOM   5299  CA  ASN A 743      85.332  95.617  72.483  1.00 15.26           C  
ATOM   5300  C   ASN A 743      85.878  94.263  72.049  1.00 15.26           C  
ATOM   5301  O   ASN A 743      85.582  93.235  72.672  1.00 15.26           O  
ATOM   5302  CB  ASN A 743      84.199  96.047  71.551  1.00 15.26           C  
ATOM   5303  CG  ASN A 743      83.311  97.111  72.156  1.00 15.26           C  
ATOM   5304  OD1 ASN A 743      83.233  97.249  73.371  1.00 15.26           O  
ATOM   5305  ND2 ASN A 743      82.632  97.868  71.306  1.00 15.26           N  
ATOM   5306  N   GLU A 744      86.704  94.247  71.001  1.00 15.24           N  
ATOM   5307  CA  GLU A 744      87.200  92.978  70.482  1.00 15.24           C  
ATOM   5308  C   GLU A 744      88.186  92.314  71.437  1.00 15.24           C  
ATOM   5309  O   GLU A 744      88.151  91.092  71.619  1.00 15.24           O  
ATOM   5310  CB  GLU A 744      87.841  93.195  69.117  1.00 15.24           C  
ATOM   5311  CG  GLU A 744      88.140  91.915  68.378  1.00 15.24           C  
ATOM   5312  CD  GLU A 744      88.890  92.158  67.095  1.00 15.24           C  
ATOM   5313  OE1 GLU A 744      89.334  93.302  66.876  1.00 15.24           O  
ATOM   5314  OE2 GLU A 744      89.034  91.207  66.302  1.00 15.24           O  
ATOM   5315  N   PHE A 745      89.054  93.099  72.075  1.00  7.03           N  
ATOM   5316  CA  PHE A 745      90.020  92.534  73.007  1.00  7.03           C  
ATOM   5317  C   PHE A 745      89.332  92.066  74.284  1.00  7.03           C  
ATOM   5318  O   PHE A 745      89.719  91.048  74.871  1.00  7.03           O  
ATOM   5319  CB  PHE A 745      91.110  93.569  73.292  1.00  7.03           C  
ATOM   5320  CG  PHE A 745      92.225  93.072  74.169  1.00  7.03           C  
ATOM   5321  CD1 PHE A 745      93.255  92.317  73.633  1.00  7.03           C  
ATOM   5322  CD2 PHE A 745      92.258  93.372  75.517  1.00  7.03           C  
ATOM   5323  CE1 PHE A 745      94.286  91.864  74.427  1.00  7.03           C  
ATOM   5324  CE2 PHE A 745      93.289  92.924  76.310  1.00  7.03           C  
ATOM   5325  CZ  PHE A 745      94.303  92.167  75.767  1.00  7.03           C  
ATOM   5326  N   TYR A 746      88.292  92.781  74.721  1.00  7.43           N  
ATOM   5327  CA  TYR A 746      87.520  92.324  75.869  1.00  7.43           C  
ATOM   5328  C   TYR A 746      86.802  91.017  75.558  1.00  7.43           C  
ATOM   5329  O   TYR A 746      86.760  90.109  76.397  1.00  7.43           O  
ATOM   5330  CB  TYR A 746      86.532  93.411  76.289  1.00  7.43           C  
ATOM   5331  CG  TYR A 746      85.573  92.999  77.376  1.00  7.43           C  
ATOM   5332  CD1 TYR A 746      86.013  92.799  78.674  1.00  7.43           C  
ATOM   5333  CD2 TYR A 746      84.225  92.823  77.109  1.00  7.43           C  
ATOM   5334  CE1 TYR A 746      85.142  92.425  79.668  1.00  7.43           C  
ATOM   5335  CE2 TYR A 746      83.348  92.450  78.099  1.00  7.43           C  
ATOM   5336  CZ  TYR A 746      83.811  92.255  79.376  1.00  7.43           C  
ATOM   5337  OH  TYR A 746      82.939  91.882  80.367  1.00  7.43           O  
ATOM   5338  N   ALA A 747      86.243  90.897  74.350  1.00  9.07           N  
ATOM   5339  CA  ALA A 747      85.629  89.637  73.945  1.00  9.07           C  
ATOM   5340  C   ALA A 747      86.657  88.513  73.890  1.00  9.07           C  
ATOM   5341  O   ALA A 747      86.366  87.374  74.271  1.00  9.07           O  
ATOM   5342  CB  ALA A 747      84.942  89.803  72.592  1.00  9.07           C  
ATOM   5343  N   TYR A 748      87.867  88.821  73.423  1.00  7.73           N  
ATOM   5344  CA  TYR A 748      88.934  87.826  73.371  1.00  7.73           C  
ATOM   5345  C   TYR A 748      89.294  87.326  74.766  1.00  7.73           C  
ATOM   5346  O   TYR A 748      89.450  86.119  74.985  1.00  7.73           O  
ATOM   5347  CB  TYR A 748      90.151  88.438  72.677  1.00  7.73           C  
ATOM   5348  CG  TYR A 748      91.402  87.596  72.669  1.00  7.73           C  
ATOM   5349  CD1 TYR A 748      91.568  86.570  71.754  1.00  7.73           C  
ATOM   5350  CD2 TYR A 748      92.430  87.847  73.563  1.00  7.73           C  
ATOM   5351  CE1 TYR A 748      92.716  85.812  71.738  1.00  7.73           C  
ATOM   5352  CE2 TYR A 748      93.579  87.092  73.557  1.00  7.73           C  
ATOM   5353  CZ  TYR A 748      93.718  86.075  72.642  1.00  7.73           C  
ATOM   5354  OH  TYR A 748      94.864  85.318  72.629  1.00  7.73           O  
ATOM   5355  N   LEU A 749      89.433  88.243  75.725  1.00  7.38           N  
ATOM   5356  CA  LEU A 749      89.736  87.825  77.091  1.00  7.38           C  
ATOM   5357  C   LEU A 749      88.592  87.025  77.698  1.00  7.38           C  
ATOM   5358  O   LEU A 749      88.827  86.027  78.384  1.00  7.38           O  
ATOM   5359  CB  LEU A 749      90.060  89.031  77.971  1.00  7.38           C  
ATOM   5360  CG  LEU A 749      91.224  89.931  77.571  1.00  7.38           C  
ATOM   5361  CD1 LEU A 749      91.258  91.142  78.480  1.00  7.38           C  
ATOM   5362  CD2 LEU A 749      92.526  89.163  77.639  1.00  7.38           C  
ATOM   5363  N   ARG A 750      87.347  87.449  77.466  1.00  7.80           N  
ATOM   5364  CA  ARG A 750      86.210  86.696  77.985  1.00  7.80           C  
ATOM   5365  C   ARG A 750      86.161  85.294  77.399  1.00  7.80           C  
ATOM   5366  O   ARG A 750      85.754  84.347  78.081  1.00  7.80           O  
ATOM   5367  CB  ARG A 750      84.905  87.439  77.694  1.00  7.80           C  
ATOM   5368  CG  ARG A 750      84.757  88.763  78.425  1.00  7.80           C  
ATOM   5369  CD  ARG A 750      84.567  88.590  79.927  1.00  7.80           C  
ATOM   5370  NE  ARG A 750      83.390  87.808  80.320  1.00  7.80           N  
ATOM   5371  CZ  ARG A 750      82.141  87.991  79.886  1.00  7.80           C  
ATOM   5372  NH1 ARG A 750      81.834  88.971  79.046  1.00  7.80           N  
ATOM   5373  NH2 ARG A 750      81.177  87.198  80.327  1.00  7.80           N  
ATOM   5374  N   LYS A 751      86.580  85.141  76.144  1.00  8.18           N  
ATOM   5375  CA  LYS A 751      86.573  83.838  75.493  1.00  8.18           C  
ATOM   5376  C   LYS A 751      87.714  82.947  75.975  1.00  8.18           C  
ATOM   5377  O   LYS A 751      87.528  81.735  76.128  1.00  8.18           O  
ATOM   5378  CB  LYS A 751      86.640  84.028  73.978  1.00  8.18           C  
ATOM   5379  CG  LYS A 751      86.780  82.758  73.161  1.00  8.18           C  
ATOM   5380  CD  LYS A 751      85.509  81.941  73.130  1.00  8.18           C  
ATOM   5381  CE  LYS A 751      85.831  80.464  73.015  1.00  8.18           C  
ATOM   5382  NZ  LYS A 751      84.769  79.613  73.605  1.00  8.18           N  
ATOM   5383  N   HIS A 752      88.898  83.513  76.220  1.00  8.50           N  
ATOM   5384  CA  HIS A 752      90.079  82.695  76.466  1.00  8.50           C  
ATOM   5385  C   HIS A 752      90.680  82.828  77.860  1.00  8.50           C  
ATOM   5386  O   HIS A 752      91.496  81.982  78.235  1.00  8.50           O  
ATOM   5387  CB  HIS A 752      91.162  83.017  75.425  1.00  8.50           C  
ATOM   5388  CG  HIS A 752      90.800  82.598  74.034  1.00  8.50           C  
ATOM   5389  ND1 HIS A 752      90.987  81.314  73.573  1.00  8.50           N  
ATOM   5390  CD2 HIS A 752      90.280  83.297  72.998  1.00  8.50           C  
ATOM   5391  CE1 HIS A 752      90.589  81.237  72.317  1.00  8.50           C  
ATOM   5392  NE2 HIS A 752      90.157  82.427  71.943  1.00  8.50           N  
ATOM   5393  N   PHE A 753      90.332  83.866  78.628  1.00  7.17           N  
ATOM   5394  CA  PHE A 753      90.974  84.095  79.926  1.00  7.17           C  
ATOM   5395  C   PHE A 753      89.904  84.510  80.943  1.00  7.17           C  
ATOM   5396  O   PHE A 753      89.982  85.538  81.605  1.00  7.17           O  
ATOM   5397  CB  PHE A 753      92.105  85.121  79.807  1.00  7.17           C  
ATOM   5398  CG  PHE A 753      93.028  85.170  81.001  1.00  7.17           C  
ATOM   5399  CD1 PHE A 753      94.152  84.363  81.047  1.00  7.17           C  
ATOM   5400  CD2 PHE A 753      92.811  86.059  82.041  1.00  7.17           C  
ATOM   5401  CE1 PHE A 753      95.010  84.405  82.120  1.00  7.17           C  
ATOM   5402  CE2 PHE A 753      93.671  86.107  83.117  1.00  7.17           C  
ATOM   5403  CZ  PHE A 753      94.772  85.280  83.155  1.00  7.17           C  
ATOM   5404  N   SER A 754      88.836  83.722  81.047  1.00 16.74           N  
ATOM   5405  CA  SER A 754      87.718  84.079  81.913  1.00 16.74           C  
ATOM   5406  C   SER A 754      88.120  84.024  83.382  1.00 16.74           C  
ATOM   5407  O   SER A 754      88.818  83.108  83.820  1.00 16.74           O  
ATOM   5408  CB  SER A 754      86.525  83.156  81.665  1.00 16.74           C  
ATOM   5409  OG  SER A 754      86.811  81.827  82.050  1.00 16.74           O  
ATOM   5410  N   MET A 755      87.665  85.015  84.143  1.00  7.37           N  
ATOM   5411  CA  MET A 755      88.125  85.247  85.501  1.00  7.37           C  
ATOM   5412  C   MET A 755      86.967  85.233  86.488  1.00  7.37           C  
ATOM   5413  O   MET A 755      85.831  85.574  86.152  1.00  7.37           O  
ATOM   5414  CB  MET A 755      88.854  86.589  85.608  1.00  7.37           C  
ATOM   5415  CG  MET A 755      90.276  86.572  85.099  1.00  7.37           C  
ATOM   5416  SD  MET A 755      91.041  88.198  85.123  1.00  7.37           S  
ATOM   5417  CE  MET A 755      89.829  89.163  84.234  1.00  7.37           C  
ATOM   5418  N   MET A 756      87.275  84.830  87.715  1.00  7.63           N  
ATOM   5419  CA  MET A 756      86.393  84.993  88.862  1.00  7.63           C  
ATOM   5420  C   MET A 756      87.153  85.823  89.882  1.00  7.63           C  
ATOM   5421  O   MET A 756      88.226  85.415  90.334  1.00  7.63           O  
ATOM   5422  CB  MET A 756      85.987  83.639  89.445  1.00  7.63           C  
ATOM   5423  CG  MET A 756      84.720  83.673  90.273  1.00  7.63           C  
ATOM   5424  SD  MET A 756      84.620  82.363  91.503  1.00  7.63           S  
ATOM   5425  CE  MET A 756      85.220  80.971  90.565  1.00  7.63           C  
ATOM   5426  N   ILE A 757      86.640  87.008  90.215  1.00  5.32           N  
ATOM   5427  CA  ILE A 757      87.441  87.933  91.070  1.00  5.32           C  
ATOM   5428  C   ILE A 757      86.708  88.356  92.338  1.00  5.32           C  
ATOM   5429  O   ILE A 757      85.596  88.885  92.222  1.00  5.32           O  
ATOM   5430  CB  ILE A 757      87.844  89.185  90.258  1.00  5.32           C  
ATOM   5431  CG1 ILE A 757      88.579  88.843  88.959  1.00  5.32           C  
ATOM   5432  CG2 ILE A 757      88.628  90.168  91.113  1.00  5.32           C  
ATOM   5433  CD1 ILE A 757      90.072  88.712  89.110  1.00  5.32           C  
ATOM   5434  N   LEU A 758      87.303  88.111  93.504  1.00  6.64           N  
ATOM   5435  CA  LEU A 758      86.741  88.673  94.756  1.00  6.64           C  
ATOM   5436  C   LEU A 758      87.907  89.383  95.439  1.00  6.64           C  
ATOM   5437  O   LEU A 758      88.793  88.675  95.935  1.00  6.64           O  
ATOM   5438  CB  LEU A 758      86.169  87.558  95.634  1.00  6.64           C  
ATOM   5439  CG  LEU A 758      85.290  88.031  96.790  1.00  6.64           C  
ATOM   5440  CD1 LEU A 758      84.253  86.982  97.152  1.00  6.64           C  
ATOM   5441  CD2 LEU A 758      86.130  88.399  98.003  1.00  6.64           C  
ATOM   5442  N   SER A 759      87.913  90.719  95.435  1.00  8.12           N  
ATOM   5443  CA  SER A 759      89.032  91.496  96.029  1.00  8.12           C  
ATOM   5444  C   SER A 759      90.361  91.097  95.377  1.00  8.12           C  
ATOM   5445  O   SER A 759      90.463  91.191  94.146  1.00  8.12           O  
ATOM   5446  CB  SER A 759      89.062  91.382  97.523  1.00  8.12           C  
ATOM   5447  OG  SER A 759      89.977  92.306  98.089  1.00  8.12           O  
ATOM   5448  N   ASP A 760      91.339  90.679  96.182  1.00 10.22           N  
ATOM   5449  CA  ASP A 760      92.669  90.269  95.657  1.00 10.22           C  
ATOM   5450  C   ASP A 760      92.735  88.762  95.347  1.00 10.22           C  
ATOM   5451  O   ASP A 760      93.808  88.308  94.917  1.00 10.22           O  
ATOM   5452  CB  ASP A 760      93.785  90.743  96.587  1.00 10.22           C  
ATOM   5453  CG  ASP A 760      93.696  90.160  97.984  1.00 10.22           C  
ATOM   5454  OD1 ASP A 760      92.565  90.018  98.488  1.00 10.22           O  
ATOM   5455  OD2 ASP A 760      94.760  89.856  98.556  1.00 10.22           O  
ATOM   5456  N   ASP A 761      91.643  88.017  95.546  1.00  8.47           N  
ATOM   5457  CA  ASP A 761      91.615  86.566  95.218  1.00  8.47           C  
ATOM   5458  C   ASP A 761      91.101  86.360  93.788  1.00  8.47           C  
ATOM   5459  O   ASP A 761      90.255  87.165  93.360  1.00  8.47           O  
ATOM   5460  CB  ASP A 761      90.863  85.764  96.281  1.00  8.47           C  
ATOM   5461  CG  ASP A 761      91.329  84.324  96.400  1.00  8.47           C  
ATOM   5462  OD1 ASP A 761      91.849  83.792  95.402  1.00  8.47           O  
ATOM   5463  OD2 ASP A 761      91.176  83.750  97.494  1.00  8.47           O  
ATOM   5464  N   ALA A 762      91.611  85.350  93.069  1.00  7.02           N  
ATOM   5465  CA  ALA A 762      91.208  85.180  91.683  1.00  7.02           C  
ATOM   5466  C   ALA A 762      91.339  83.722  91.269  1.00  7.02           C  
ATOM   5467  O   ALA A 762      92.257  83.019  91.694  1.00  7.02           O  
ATOM   5468  CB  ALA A 762      92.034  86.074  90.753  1.00  7.02           C  
ATOM   5469  N   VAL A 763      90.403  83.281  90.434  1.00  7.41           N  
ATOM   5470  CA  VAL A 763      90.467  81.992  89.760  1.00  7.41           C  
ATOM   5471  C   VAL A 763      90.275  82.248  88.274  1.00  7.41           C  
ATOM   5472  O   VAL A 763      89.333  82.943  87.880  1.00  7.41           O  
ATOM   5473  CB  VAL A 763      89.401  81.010  90.287  1.00  7.41           C  
ATOM   5474  CG1 VAL A 763      89.240  79.833  89.339  1.00  7.41           C  
ATOM   5475  CG2 VAL A 763      89.769  80.523  91.672  1.00  7.41           C  
ATOM   5476  N   VAL A 764      91.170  81.707  87.453  1.00  7.03           N  
ATOM   5477  CA  VAL A 764      91.120  81.898  86.010  1.00  7.03           C  
ATOM   5478  C   VAL A 764      90.988  80.547  85.326  1.00  7.03           C  
ATOM   5479  O   VAL A 764      91.717  79.603  85.643  1.00  7.03           O  
ATOM   5480  CB  VAL A 764      92.359  82.653  85.487  1.00  7.03           C  
ATOM   5481  CG1 VAL A 764      92.218  82.932  84.010  1.00  7.03           C  
ATOM   5482  CG2 VAL A 764      92.524  83.949  86.233  1.00  7.03           C  
ATOM   5483  N   CYS A 765      90.048  80.461  84.393  1.00  8.42           N  
ATOM   5484  CA  CYS A 765      89.956  79.347  83.464  1.00  8.42           C  
ATOM   5485  C   CYS A 765      90.491  79.829  82.122  1.00  8.42           C  
ATOM   5486  O   CYS A 765      89.894  80.706  81.491  1.00  8.42           O  
ATOM   5487  CB  CYS A 765      88.514  78.856  83.339  1.00  8.42           C  
ATOM   5488  SG  CYS A 765      88.323  77.249  82.554  1.00  8.42           S  
ATOM   5489  N   PHE A 766      91.614  79.266  81.692  1.00  8.63           N  
ATOM   5490  CA  PHE A 766      92.322  79.767  80.527  1.00  8.63           C  
ATOM   5491  C   PHE A 766      92.565  78.645  79.530  1.00  8.63           C  
ATOM   5492  O   PHE A 766      92.637  77.469  79.894  1.00  8.63           O  
ATOM   5493  CB  PHE A 766      93.656  80.426  80.915  1.00  8.63           C  
ATOM   5494  CG  PHE A 766      94.641  79.485  81.536  1.00  8.63           C  
ATOM   5495  CD1 PHE A 766      94.539  79.132  82.867  1.00  8.63           C  
ATOM   5496  CD2 PHE A 766      95.666  78.945  80.785  1.00  8.63           C  
ATOM   5497  CE1 PHE A 766      95.443  78.265  83.435  1.00  8.63           C  
ATOM   5498  CE2 PHE A 766      96.568  78.079  81.349  1.00  8.63           C  
ATOM   5499  CZ  PHE A 766      96.458  77.738  82.675  1.00  8.63           C  
ATOM   5500  N   ASN A 767      92.673  79.031  78.261  1.00 10.09           N  
ATOM   5501  CA  ASN A 767      92.941  78.100  77.171  1.00 10.09           C  
ATOM   5502  C   ASN A 767      94.400  77.664  77.244  1.00 10.09           C  
ATOM   5503  O   ASN A 767      95.310  78.484  77.093  1.00 10.09           O  
ATOM   5504  CB  ASN A 767      92.614  78.771  75.839  1.00 10.09           C  
ATOM   5505  CG  ASN A 767      92.769  77.846  74.648  1.00 10.09           C  
ATOM   5506  OD1 ASN A 767      93.497  76.860  74.692  1.00 10.09           O  
ATOM   5507  ND2 ASN A 767      92.073  78.167  73.568  1.00 10.09           N  
ATOM   5508  N   SER A 768      94.622  76.368  77.478  1.00 10.58           N  
ATOM   5509  CA  SER A 768      95.970  75.869  77.736  1.00 10.58           C  
ATOM   5510  C   SER A 768      96.865  76.000  76.514  1.00 10.58           C  
ATOM   5511  O   SER A 768      98.056  76.303  76.640  1.00 10.58           O  
ATOM   5512  CB  SER A 768      95.907  74.411  78.176  1.00 10.58           C  
ATOM   5513  OG  SER A 768      95.033  74.268  79.272  1.00 10.58           O  
ATOM   5514  N   THR A 769      96.318  75.743  75.327  1.00 11.14           N  
ATOM   5515  CA  THR A 769      97.116  75.814  74.109  1.00 11.14           C  
ATOM   5516  C   THR A 769      97.611  77.234  73.861  1.00 11.14           C  
ATOM   5517  O   THR A 769      98.773  77.442  73.494  1.00 11.14           O  
ATOM   5518  CB  THR A 769      96.297  75.299  72.927  1.00 11.14           C  
ATOM   5519  OG1 THR A 769      96.088  73.891  73.073  1.00 11.14           O  
ATOM   5520  CG2 THR A 769      97.018  75.554  71.621  1.00 11.14           C  
ATOM   5521  N   TYR A 770      96.743  78.225  74.065  1.00  9.54           N  
ATOM   5522  CA  TYR A 770      97.151  79.618  73.910  1.00  9.54           C  
ATOM   5523  C   TYR A 770      98.194  80.016  74.948  1.00  9.54           C  
ATOM   5524  O   TYR A 770      99.138  80.748  74.633  1.00  9.54           O  
ATOM   5525  CB  TYR A 770      95.931  80.536  73.990  1.00  9.54           C  
ATOM   5526  CG  TYR A 770      95.084  80.562  72.738  1.00  9.54           C  
ATOM   5527  CD1 TYR A 770      95.006  79.462  71.898  1.00  9.54           C  
ATOM   5528  CD2 TYR A 770      94.375  81.700  72.386  1.00  9.54           C  
ATOM   5529  CE1 TYR A 770      94.240  79.491  70.756  1.00  9.54           C  
ATOM   5530  CE2 TYR A 770      93.606  81.737  71.244  1.00  9.54           C  
ATOM   5531  CZ  TYR A 770      93.541  80.630  70.433  1.00  9.54           C  
ATOM   5532  OH  TYR A 770      92.775  80.665  69.293  1.00  9.54           O  
ATOM   5533  N   ALA A 771      98.037  79.555  76.191  1.00  9.20           N  
ATOM   5534  CA  ALA A 771      99.022  79.868  77.220  1.00  9.20           C  
ATOM   5535  C   ALA A 771     100.370  79.226  76.924  1.00  9.20           C  
ATOM   5536  O   ALA A 771     101.415  79.818  77.214  1.00  9.20           O  
ATOM   5537  CB  ALA A 771      98.515  79.425  78.591  1.00  9.20           C  
ATOM   5538  N   SER A 772     100.372  78.022  76.352  1.00 11.61           N  
ATOM   5539  CA  SER A 772     101.633  77.376  76.007  1.00 11.61           C  
ATOM   5540  C   SER A 772     102.321  78.073  74.841  1.00 11.61           C  
ATOM   5541  O   SER A 772     103.554  78.081  74.766  1.00 11.61           O  
ATOM   5542  CB  SER A 772     101.399  75.903  75.681  1.00 11.61           C  
ATOM   5543  OG  SER A 772     101.041  75.735  74.322  1.00 11.61           O  
ATOM   5544  N   GLN A 773     101.549  78.653  73.926  1.00 11.94           N  
ATOM   5545  CA  GLN A 773     102.090  79.390  72.794  1.00 11.94           C  
ATOM   5546  C   GLN A 773     102.376  80.849  73.116  1.00 11.94           C  
ATOM   5547  O   GLN A 773     102.858  81.576  72.244  1.00 11.94           O  
ATOM   5548  CB  GLN A 773     101.128  79.315  71.608  1.00 11.94           C  
ATOM   5549  CG  GLN A 773     101.160  78.001  70.865  1.00 11.94           C  
ATOM   5550  CD  GLN A 773      99.955  77.814  69.972  1.00 11.94           C  
ATOM   5551  OE1 GLN A 773      99.406  76.720  69.872  1.00 11.94           O  
ATOM   5552  NE2 GLN A 773      99.532  78.888  69.319  1.00 11.94           N  
ATOM   5553  N   GLY A 774     102.086  81.295  74.335  1.00 10.35           N  
ATOM   5554  CA  GLY A 774     102.259  82.688  74.682  1.00 10.35           C  
ATOM   5555  C   GLY A 774     101.167  83.605  74.191  1.00 10.35           C  
ATOM   5556  O   GLY A 774     101.396  84.811  74.072  1.00 10.35           O  
ATOM   5557  N   LEU A 775      99.983  83.072  73.894  1.00  9.71           N  
ATOM   5558  CA  LEU A 775      98.873  83.890  73.424  1.00  9.71           C  
ATOM   5559  C   LEU A 775      98.028  84.456  74.557  1.00  9.71           C  
ATOM   5560  O   LEU A 775      97.337  85.459  74.351  1.00  9.71           O  
ATOM   5561  CB  LEU A 775      97.983  83.079  72.479  1.00  9.71           C  
ATOM   5562  CG  LEU A 775      98.317  83.074  70.986  1.00  9.71           C  
ATOM   5563  CD1 LEU A 775      99.757  82.683  70.725  1.00  9.71           C  
ATOM   5564  CD2 LEU A 775      97.377  82.146  70.240  1.00  9.71           C  
ATOM   5565  N   VAL A 776      98.061  83.842  75.741  1.00  7.41           N  
ATOM   5566  CA  VAL A 776      97.420  84.384  76.932  1.00  7.41           C  
ATOM   5567  C   VAL A 776      98.399  84.259  78.091  1.00  7.41           C  
ATOM   5568  O   VAL A 776      99.372  83.505  78.035  1.00  7.41           O  
ATOM   5569  CB  VAL A 776      96.076  83.696  77.284  1.00  7.41           C  
ATOM   5570  CG1 VAL A 776      95.114  83.740  76.110  1.00  7.41           C  
ATOM   5571  CG2 VAL A 776      96.299  82.270  77.748  1.00  7.41           C  
ATOM   5572  N   ALA A 777      98.133  85.024  79.144  1.00  7.59           N  
ATOM   5573  CA  ALA A 777      99.052  85.113  80.269  1.00  7.59           C  
ATOM   5574  C   ALA A 777      99.142  83.795  81.029  1.00  7.59           C  
ATOM   5575  O   ALA A 777      98.185  83.020  81.101  1.00  7.59           O  
ATOM   5576  CB  ALA A 777      98.616  86.222  81.221  1.00  7.59           C  
ATOM   5577  N   SER A 778     100.311  83.553  81.602  1.00  9.62           N  
ATOM   5578  CA  SER A 778     100.562  82.463  82.531  1.00  9.62           C  
ATOM   5579  C   SER A 778     101.176  83.030  83.808  1.00  9.62           C  
ATOM   5580  O   SER A 778     101.288  84.243  83.982  1.00  9.62           O  
ATOM   5581  CB  SER A 778     101.464  81.401  81.898  1.00  9.62           C  
ATOM   5582  OG  SER A 778     102.567  81.992  81.238  1.00  9.62           O  
ATOM   5583  N   ILE A 779     101.566  82.132  84.715  1.00 11.39           N  
ATOM   5584  CA  ILE A 779     102.158  82.548  85.984  1.00 11.39           C  
ATOM   5585  C   ILE A 779     103.438  83.343  85.757  1.00 11.39           C  
ATOM   5586  O   ILE A 779     103.746  84.273  86.511  1.00 11.39           O  
ATOM   5587  CB  ILE A 779     102.393  81.311  86.876  1.00 11.39           C  
ATOM   5588  CG1 ILE A 779     101.056  80.781  87.393  1.00 11.39           C  
ATOM   5589  CG2 ILE A 779     103.310  81.632  88.040  1.00 11.39           C  
ATOM   5590  CD1 ILE A 779     100.458  81.611  88.504  1.00 11.39           C  
ATOM   5591  N   LYS A 780     104.191  83.002  84.709  1.00 13.39           N  
ATOM   5592  CA  LYS A 780     105.398  83.742  84.350  1.00 13.39           C  
ATOM   5593  C   LYS A 780     105.101  85.217  84.091  1.00 13.39           C  
ATOM   5594  O   LYS A 780     105.820  86.108  84.564  1.00 13.39           O  
ATOM   5595  CB  LYS A 780     106.023  83.092  83.115  1.00 13.39           C  
ATOM   5596  CG  LYS A 780     107.328  83.698  82.651  1.00 13.39           C  
ATOM   5597  CD  LYS A 780     107.861  82.931  81.454  1.00 13.39           C  
ATOM   5598  CE  LYS A 780     109.163  83.543  80.957  1.00 13.39           C  
ATOM   5599  NZ  LYS A 780     109.722  82.822  79.783  1.00 13.39           N  
ATOM   5600  N   ASN A 781     104.039  85.491  83.330  1.00 10.06           N  
ATOM   5601  CA  ASN A 781     103.702  86.869  82.996  1.00 10.06           C  
ATOM   5602  C   ASN A 781     103.232  87.652  84.215  1.00 10.06           C  
ATOM   5603  O   ASN A 781     103.561  88.836  84.351  1.00 10.06           O  
ATOM   5604  CB  ASN A 781     102.645  86.890  81.896  1.00 10.06           C  
ATOM   5605  CG  ASN A 781     103.081  86.133  80.661  1.00 10.06           C  
ATOM   5606  OD1 ASN A 781     102.379  85.249  80.182  1.00 10.06           O  
ATOM   5607  ND2 ASN A 781     104.243  86.485  80.132  1.00 10.06           N  
ATOM   5608  N   PHE A 782     102.479  87.015  85.114  1.00  9.72           N  
ATOM   5609  CA  PHE A 782     102.125  87.676  86.365  1.00  9.72           C  
ATOM   5610  C   PHE A 782     103.356  87.958  87.209  1.00  9.72           C  
ATOM   5611  O   PHE A 782     103.441  89.007  87.854  1.00  9.72           O  
ATOM   5612  CB  PHE A 782     101.121  86.837  87.152  1.00  9.72           C  
ATOM   5613  CG  PHE A 782      99.730  86.914  86.620  1.00  9.72           C  
ATOM   5614  CD1 PHE A 782      98.862  87.886  87.078  1.00  9.72           C  
ATOM   5615  CD2 PHE A 782      99.289  86.024  85.663  1.00  9.72           C  
ATOM   5616  CE1 PHE A 782      97.582  87.967  86.588  1.00  9.72           C  
ATOM   5617  CE2 PHE A 782      98.008  86.099  85.170  1.00  9.72           C  
ATOM   5618  CZ  PHE A 782      97.155  87.072  85.630  1.00  9.72           C  
ATOM   5619  N   LYS A 783     104.317  87.035  87.219  1.00 10.68           N  
ATOM   5620  CA  LYS A 783     105.558  87.269  87.950  1.00 10.68           C  
ATOM   5621  C   LYS A 783     106.265  88.512  87.427  1.00 10.68           C  
ATOM   5622  O   LYS A 783     106.666  89.390  88.201  1.00 10.68           O  
ATOM   5623  CB  LYS A 783     106.465  86.043  87.835  1.00 10.68           C  
ATOM   5624  CG  LYS A 783     107.910  86.296  88.221  1.00 10.68           C  
ATOM   5625  CD  LYS A 783     108.719  85.014  88.263  1.00 10.68           C  
ATOM   5626  CE  LYS A 783     108.147  84.014  89.249  1.00 10.68           C  
ATOM   5627  NZ  LYS A 783     109.100  82.904  89.513  1.00 10.68           N  
ATOM   5628  N   SER A 784     106.389  88.619  86.105  1.00  8.27           N  
ATOM   5629  CA  SER A 784     107.080  89.764  85.518  1.00  8.27           C  
ATOM   5630  C   SER A 784     106.330  91.069  85.779  1.00  8.27           C  
ATOM   5631  O   SER A 784     106.940  92.093  86.128  1.00  8.27           O  
ATOM   5632  CB  SER A 784     107.274  89.536  84.022  1.00  8.27           C  
ATOM   5633  OG  SER A 784     107.925  88.304  83.787  1.00  8.27           O  
ATOM   5634  N   VAL A 785     105.005  91.055  85.605  1.00  5.01           N  
ATOM   5635  CA  VAL A 785     104.214  92.268  85.798  1.00  5.01           C  
ATOM   5636  C   VAL A 785     104.286  92.731  87.247  1.00  5.01           C  
ATOM   5637  O   VAL A 785     104.442  93.924  87.522  1.00  5.01           O  
ATOM   5638  CB  VAL A 785     102.761  92.040  85.341  1.00  5.01           C  
ATOM   5639  CG1 VAL A 785     101.850  93.137  85.865  1.00  5.01           C  
ATOM   5640  CG2 VAL A 785     102.690  91.981  83.834  1.00  5.01           C  
ATOM   5641  N   LEU A 786     104.166  91.802  88.196  1.00  7.07           N  
ATOM   5642  CA  LEU A 786     104.271  92.171  89.599  1.00  7.07           C  
ATOM   5643  C   LEU A 786     105.674  92.616  89.976  1.00  7.07           C  
ATOM   5644  O   LEU A 786     105.827  93.386  90.927  1.00  7.07           O  
ATOM   5645  CB  LEU A 786     103.836  91.003  90.480  1.00  7.07           C  
ATOM   5646  CG  LEU A 786     102.405  91.057  91.014  1.00  7.07           C  
ATOM   5647  CD1 LEU A 786     101.399  91.016  89.880  1.00  7.07           C  
ATOM   5648  CD2 LEU A 786     102.168  89.911  91.969  1.00  7.07           C  
ATOM   5649  N   TYR A 787     106.701  92.154  89.261  1.00  6.01           N  
ATOM   5650  CA  TYR A 787     108.042  92.661  89.521  1.00  6.01           C  
ATOM   5651  C   TYR A 787     108.191  94.107  89.073  1.00  6.01           C  
ATOM   5652  O   TYR A 787     108.702  94.947  89.822  1.00  6.01           O  
ATOM   5653  CB  TYR A 787     109.089  91.785  88.837  1.00  6.01           C  
ATOM   5654  CG  TYR A 787     110.454  91.880  89.475  1.00  6.01           C  
ATOM   5655  CD1 TYR A 787     110.754  91.173  90.626  1.00  6.01           C  
ATOM   5656  CD2 TYR A 787     111.442  92.680  88.924  1.00  6.01           C  
ATOM   5657  CE1 TYR A 787     111.998  91.259  91.210  1.00  6.01           C  
ATOM   5658  CE2 TYR A 787     112.686  92.772  89.498  1.00  6.01           C  
ATOM   5659  CZ  TYR A 787     112.961  92.060  90.641  1.00  6.01           C  
ATOM   5660  OH  TYR A 787     114.202  92.149  91.221  1.00  6.01           O  
ATOM   5661  N   TYR A 788     107.749  94.427  87.857  1.00  5.16           N  
ATOM   5662  CA  TYR A 788     108.091  95.749  87.339  1.00  5.16           C  
ATOM   5663  C   TYR A 788     107.042  96.809  87.649  1.00  5.16           C  
ATOM   5664  O   TYR A 788     107.362  98.002  87.624  1.00  5.16           O  
ATOM   5665  CB  TYR A 788     108.377  95.690  85.830  1.00  5.16           C  
ATOM   5666  CG  TYR A 788     107.202  95.755  84.875  1.00  5.16           C  
ATOM   5667  CD1 TYR A 788     106.609  96.968  84.546  1.00  5.16           C  
ATOM   5668  CD2 TYR A 788     106.723  94.609  84.257  1.00  5.16           C  
ATOM   5669  CE1 TYR A 788     105.559  97.029  83.666  1.00  5.16           C  
ATOM   5670  CE2 TYR A 788     105.674  94.665  83.374  1.00  5.16           C  
ATOM   5671  CZ  TYR A 788     105.096  95.876  83.082  1.00  5.16           C  
ATOM   5672  OH  TYR A 788     104.049  95.934  82.200  1.00  5.16           O  
ATOM   5673  N   GLN A 789     105.830  96.405  88.054  1.00  6.82           N  
ATOM   5674  CA  GLN A 789     104.724  97.381  88.266  1.00  6.82           C  
ATOM   5675  C   GLN A 789     104.258  97.428  89.728  1.00  6.82           C  
ATOM   5676  O   GLN A 789     103.721  98.468  90.114  1.00  6.82           O  
ATOM   5677  CB  GLN A 789     103.574  97.111  87.292  1.00  6.82           C  
ATOM   5678  CG  GLN A 789     102.362  98.013  87.461  1.00  6.82           C  
ATOM   5679  CD  GLN A 789     101.484  97.983  86.234  1.00  6.82           C  
ATOM   5680  OE1 GLN A 789     101.902  98.353  85.140  1.00  6.82           O  
ATOM   5681  NE2 GLN A 789     100.251  97.539  86.404  1.00  6.82           N  
ATOM   5682  N   ASN A 790     104.392  96.378  90.518  1.00  7.50           N  
ATOM   5683  CA  ASN A 790     103.867  96.358  91.900  1.00  7.50           C  
ATOM   5684  C   ASN A 790     105.027  96.330  92.891  1.00  7.50           C  
ATOM   5685  O   ASN A 790     104.732  96.462  94.073  1.00  7.50           O  
ATOM   5686  CB  ASN A 790     102.799  95.277  92.109  1.00  7.50           C  
ATOM   5687  CG  ASN A 790     102.147  95.330  93.467  1.00  7.50           C  
ATOM   5688  OD1 ASN A 790     102.696  95.904  94.393  1.00  7.50           O  
ATOM   5689  ND2 ASN A 790     100.979  94.731  93.592  1.00  7.50           N  
ATOM   5690  N   ASN A 791     106.279  96.148  92.432  1.00  8.55           N  
ATOM   5691  CA  ASN A 791     107.480  96.161  93.318  1.00  8.55           C  
ATOM   5692  C   ASN A 791     107.492  94.988  94.304  1.00  8.55           C  
ATOM   5693  O   ASN A 791     107.878  95.217  95.461  1.00  8.55           O  
ATOM   5694  CB  ASN A 791     107.714  97.518  93.987  1.00  8.55           C  
ATOM   5695  CG  ASN A 791     107.958  98.633  92.993  1.00  8.55           C  
ATOM   5696  OD1 ASN A 791     107.544  99.768  93.216  1.00  8.55           O  
ATOM   5697  ND2 ASN A 791     108.623  98.318  91.894  1.00  8.55           N  
ATOM   5698  N   VAL A 792     107.104  93.785  93.872  1.00  9.70           N  
ATOM   5699  CA  VAL A 792     107.115  92.586  94.701  1.00  9.70           C  
ATOM   5700  C   VAL A 792     107.585  91.409  93.864  1.00  9.70           C  
ATOM   5701  O   VAL A 792     107.484  91.417  92.634  1.00  9.70           O  
ATOM   5702  CB  VAL A 792     105.735  92.276  95.323  1.00  9.70           C  
ATOM   5703  CG1 VAL A 792     105.443  93.225  96.466  1.00  9.70           C  
ATOM   5704  CG2 VAL A 792     104.646  92.322  94.272  1.00  9.70           C  
ATOM   5705  N   PHE A 793     108.110  90.393  94.538  1.00 13.34           N  
ATOM   5706  CA  PHE A 793     108.420  89.120  93.903  1.00 13.34           C  
ATOM   5707  C   PHE A 793     107.348  88.102  94.270  1.00 13.34           C  
ATOM   5708  O   PHE A 793     107.164  87.784  95.449  1.00 13.34           O  
ATOM   5709  CB  PHE A 793     109.800  88.608  94.309  1.00 13.34           C  
ATOM   5710  CG  PHE A 793     110.189  87.340  93.616  1.00 13.34           C  
ATOM   5711  CD1 PHE A 793     110.488  87.336  92.269  1.00 13.34           C  
ATOM   5712  CD2 PHE A 793     110.219  86.143  94.306  1.00 13.34           C  
ATOM   5713  CE1 PHE A 793     110.828  86.170  91.629  1.00 13.34           C  
ATOM   5714  CE2 PHE A 793     110.556  84.974  93.669  1.00 13.34           C  
ATOM   5715  CZ  PHE A 793     110.862  84.988  92.329  1.00 13.34           C  
ATOM   5716  N   MET A 794     106.644  87.599  93.262  1.00 16.85           N  
ATOM   5717  CA  MET A 794     105.654  86.543  93.442  1.00 16.85           C  
ATOM   5718  C   MET A 794     106.330  85.198  93.209  1.00 16.85           C  
ATOM   5719  O   MET A 794     106.634  84.839  92.068  1.00 16.85           O  
ATOM   5720  CB  MET A 794     104.480  86.741  92.487  1.00 16.85           C  
ATOM   5721  CG  MET A 794     103.206  86.041  92.908  1.00 16.85           C  
ATOM   5722  SD  MET A 794     101.910  86.191  91.666  1.00 16.85           S  
ATOM   5723  CE  MET A 794     102.592  85.212  90.334  1.00 16.85           C  
ATOM   5724  N   SER A 795     106.570  84.459  94.287  1.00 24.43           N  
ATOM   5725  CA  SER A 795     107.184  83.144  94.177  1.00 24.43           C  
ATOM   5726  C   SER A 795     106.142  82.102  93.794  1.00 24.43           C  
ATOM   5727  O   SER A 795     105.007  82.128  94.278  1.00 24.43           O  
ATOM   5728  CB  SER A 795     107.861  82.755  95.489  1.00 24.43           C  
ATOM   5729  OG  SER A 795     106.908  82.365  96.456  1.00 24.43           O  
ATOM   5730  N   GLU A 796     106.541  81.177  92.918  1.00 30.04           N  
ATOM   5731  CA  GLU A 796     105.625  80.159  92.417  1.00 30.04           C  
ATOM   5732  C   GLU A 796     105.163  79.193  93.500  1.00 30.04           C  
ATOM   5733  O   GLU A 796     104.222  78.429  93.266  1.00 30.04           O  
ATOM   5734  CB  GLU A 796     106.281  79.380  91.277  1.00 30.04           C  
ATOM   5735  CG  GLU A 796     105.867  79.846  89.893  1.00 30.04           C  
ATOM   5736  CD  GLU A 796     106.427  78.971  88.790  1.00 30.04           C  
ATOM   5737  OE1 GLU A 796     107.654  79.013  88.559  1.00 30.04           O  
ATOM   5738  OE2 GLU A 796     105.640  78.238  88.154  1.00 30.04           O  
ATOM   5739  N   ALA A 797     105.808  79.194  94.668  1.00 27.99           N  
ATOM   5740  CA  ALA A 797     105.389  78.305  95.747  1.00 27.99           C  
ATOM   5741  C   ALA A 797     103.973  78.612  96.215  1.00 27.99           C  
ATOM   5742  O   ALA A 797     103.235  77.698  96.596  1.00 27.99           O  
ATOM   5743  CB  ALA A 797     106.364  78.403  96.919  1.00 27.99           C  
ATOM   5744  N   LYS A 798     103.578  79.883  96.200  1.00 28.15           N  
ATOM   5745  CA  LYS A 798     102.244  80.280  96.628  1.00 28.15           C  
ATOM   5746  C   LYS A 798     101.220  80.257  95.502  1.00 28.15           C  
ATOM   5747  O   LYS A 798     100.032  80.464  95.763  1.00 28.15           O  
ATOM   5748  CB  LYS A 798     102.284  81.676  97.258  1.00 28.15           C  
ATOM   5749  CG  LYS A 798     102.390  81.670  98.776  1.00 28.15           C  
ATOM   5750  CD  LYS A 798     103.676  81.017  99.254  1.00 28.15           C  
ATOM   5751  CE  LYS A 798     104.894  81.764  98.744  1.00 28.15           C  
ATOM   5752  NZ  LYS A 798     106.169  81.107  99.140  1.00 28.15           N  
ATOM   5753  N   CYS A 799     101.643  80.008  94.270  1.00 20.82           N  
ATOM   5754  CA  CYS A 799     100.741  79.906  93.135  1.00 20.82           C  
ATOM   5755  C   CYS A 799     100.383  78.445  92.890  1.00 20.82           C  
ATOM   5756  O   CYS A 799     101.022  77.528  93.406  1.00 20.82           O  
ATOM   5757  CB  CYS A 799     101.387  80.521  91.894  1.00 20.82           C  
ATOM   5758  SG  CYS A 799     101.400  82.315  91.906  1.00 20.82           S  
ATOM   5759  N   TRP A 800      99.347  78.231  92.084  1.00 10.17           N  
ATOM   5760  CA  TRP A 800      98.911  76.872  91.804  1.00 10.17           C  
ATOM   5761  C   TRP A 800      98.315  76.790  90.407  1.00 10.17           C  
ATOM   5762  O   TRP A 800      97.928  77.796  89.810  1.00 10.17           O  
ATOM   5763  CB  TRP A 800      97.904  76.371  92.848  1.00 10.17           C  
ATOM   5764  CG  TRP A 800      96.650  77.176  92.944  1.00 10.17           C  
ATOM   5765  CD1 TRP A 800      96.414  78.222  93.780  1.00 10.17           C  
ATOM   5766  CD2 TRP A 800      95.461  77.008  92.166  1.00 10.17           C  
ATOM   5767  NE1 TRP A 800      95.150  78.712  93.580  1.00 10.17           N  
ATOM   5768  CE2 TRP A 800      94.544  77.985  92.592  1.00 10.17           C  
ATOM   5769  CE3 TRP A 800      95.084  76.124  91.153  1.00 10.17           C  
ATOM   5770  CZ2 TRP A 800      93.275  78.102  92.042  1.00 10.17           C  
ATOM   5771  CZ3 TRP A 800      93.827  76.244  90.607  1.00 10.17           C  
ATOM   5772  CH2 TRP A 800      92.936  77.225  91.051  1.00 10.17           C  
ATOM   5773  N   THR A 801      98.271  75.565  89.889  1.00 14.14           N  
ATOM   5774  CA  THR A 801      97.643  75.258  88.613  1.00 14.14           C  
ATOM   5775  C   THR A 801      97.000  73.883  88.705  1.00 14.14           C  
ATOM   5776  O   THR A 801      97.597  72.947  89.242  1.00 14.14           O  
ATOM   5777  CB  THR A 801      98.657  75.290  87.462  1.00 14.14           C  
ATOM   5778  OG1 THR A 801      99.265  76.585  87.395  1.00 14.14           O  
ATOM   5779  CG2 THR A 801      97.976  74.993  86.135  1.00 14.14           C  
ATOM   5780  N   GLU A 802      95.784  73.764  88.181  1.00 16.76           N  
ATOM   5781  CA  GLU A 802      95.050  72.507  88.174  1.00 16.76           C  
ATOM   5782  C   GLU A 802      94.657  72.179  86.742  1.00 16.76           C  
ATOM   5783  O   GLU A 802      94.043  73.004  86.061  1.00 16.76           O  
ATOM   5784  CB  GLU A 802      93.810  72.588  89.070  1.00 16.76           C  
ATOM   5785  CG  GLU A 802      92.872  71.396  88.960  1.00 16.76           C  
ATOM   5786  CD  GLU A 802      93.495  70.105  89.459  1.00 16.76           C  
ATOM   5787  OE1 GLU A 802      94.210  70.138  90.481  1.00 16.76           O  
ATOM   5788  OE2 GLU A 802      93.265  69.052  88.827  1.00 16.76           O  
ATOM   5789  N   THR A 803      95.009  70.977  86.290  1.00 17.75           N  
ATOM   5790  CA  THR A 803      94.802  70.589  84.902  1.00 17.75           C  
ATOM   5791  C   THR A 803      93.482  69.868  84.661  1.00 17.75           C  
ATOM   5792  O   THR A 803      93.075  69.730  83.503  1.00 17.75           O  
ATOM   5793  CB  THR A 803      95.953  69.697  84.423  1.00 17.75           C  
ATOM   5794  OG1 THR A 803      96.142  68.621  85.348  1.00 17.75           O  
ATOM   5795  CG2 THR A 803      97.237  70.499  84.331  1.00 17.75           C  
ATOM   5796  N   ASP A 804      92.805  69.409  85.709  1.00 21.19           N  
ATOM   5797  CA  ASP A 804      91.571  68.645  85.577  1.00 21.19           C  
ATOM   5798  C   ASP A 804      90.418  69.458  86.151  1.00 21.19           C  
ATOM   5799  O   ASP A 804      90.409  69.769  87.347  1.00 21.19           O  
ATOM   5800  CB  ASP A 804      91.693  67.298  86.288  1.00 21.19           C  
ATOM   5801  CG  ASP A 804      90.576  66.344  85.926  1.00 21.19           C  
ATOM   5802  OD1 ASP A 804      89.791  66.664  85.010  1.00 21.19           O  
ATOM   5803  OD2 ASP A 804      90.484  65.269  86.555  1.00 21.19           O  
ATOM   5804  N   LEU A 805      89.448  69.801  85.300  1.00 16.25           N  
ATOM   5805  CA  LEU A 805      88.312  70.600  85.743  1.00 16.25           C  
ATOM   5806  C   LEU A 805      87.313  69.824  86.588  1.00 16.25           C  
ATOM   5807  O   LEU A 805      86.455  70.450  87.216  1.00 16.25           O  
ATOM   5808  CB  LEU A 805      87.586  71.218  84.548  1.00 16.25           C  
ATOM   5809  CG  LEU A 805      87.941  72.675  84.250  1.00 16.25           C  
ATOM   5810  CD1 LEU A 805      89.403  72.819  83.876  1.00 16.25           C  
ATOM   5811  CD2 LEU A 805      87.033  73.234  83.172  1.00 16.25           C  
ATOM   5812  N   THR A 806      87.384  68.493  86.622  1.00 17.49           N  
ATOM   5813  CA  THR A 806      86.539  67.763  87.557  1.00 17.49           C  
ATOM   5814  C   THR A 806      86.999  67.962  88.989  1.00 17.49           C  
ATOM   5815  O   THR A 806      86.184  67.876  89.912  1.00 17.49           O  
ATOM   5816  CB  THR A 806      86.516  66.273  87.219  1.00 17.49           C  
ATOM   5817  OG1 THR A 806      87.857  65.787  87.093  1.00 17.49           O  
ATOM   5818  CG2 THR A 806      85.771  66.042  85.917  1.00 17.49           C  
ATOM   5819  N   LYS A 807      88.285  68.224  89.188  1.00 18.80           N  
ATOM   5820  CA  LYS A 807      88.742  68.861  90.406  1.00 18.80           C  
ATOM   5821  C   LYS A 807      88.366  70.339  90.363  1.00 18.80           C  
ATOM   5822  O   LYS A 807      88.214  70.935  89.294  1.00 18.80           O  
ATOM   5823  CB  LYS A 807      90.254  68.710  90.549  1.00 18.80           C  
ATOM   5824  CG  LYS A 807      90.762  67.313  90.258  1.00 18.80           C  
ATOM   5825  CD  LYS A 807      90.515  66.367  91.411  1.00 18.80           C  
ATOM   5826  CE  LYS A 807      91.450  65.176  91.332  1.00 18.80           C  
ATOM   5827  NZ  LYS A 807      92.833  65.591  90.974  1.00 18.80           N  
ATOM   5828  N   GLY A 808      88.211  70.936  91.533  1.00 13.12           N  
ATOM   5829  CA  GLY A 808      87.880  72.336  91.589  1.00 13.12           C  
ATOM   5830  C   GLY A 808      89.115  73.202  91.499  1.00 13.12           C  
ATOM   5831  O   GLY A 808      90.215  72.725  91.208  1.00 13.12           O  
ATOM   5832  N   PRO A 809      88.955  74.501  91.730  1.00 10.55           N  
ATOM   5833  CA  PRO A 809      90.126  75.332  92.011  1.00 10.55           C  
ATOM   5834  C   PRO A 809      90.784  74.870  93.300  1.00 10.55           C  
ATOM   5835  O   PRO A 809      90.113  74.442  94.240  1.00 10.55           O  
ATOM   5836  CB  PRO A 809      89.543  76.743  92.132  1.00 10.55           C  
ATOM   5837  CG  PRO A 809      88.140  76.537  92.550  1.00 10.55           C  
ATOM   5838  CD  PRO A 809      87.695  75.232  91.935  1.00 10.55           C  
ATOM   5839  N   HIS A 810      92.113  74.934  93.331  1.00 12.82           N  
ATOM   5840  CA  HIS A 810      92.832  74.420  94.490  1.00 12.82           C  
ATOM   5841  C   HIS A 810      92.512  75.225  95.741  1.00 12.82           C  
ATOM   5842  O   HIS A 810      92.380  74.662  96.834  1.00 12.82           O  
ATOM   5843  CB  HIS A 810      94.334  74.415  94.222  1.00 12.82           C  
ATOM   5844  CG  HIS A 810      95.157  74.071  95.423  1.00 12.82           C  
ATOM   5845  ND1 HIS A 810      95.680  75.027  96.265  1.00 12.82           N  
ATOM   5846  CD2 HIS A 810      95.529  72.875  95.936  1.00 12.82           C  
ATOM   5847  CE1 HIS A 810      96.349  74.436  97.239  1.00 12.82           C  
ATOM   5848  NE2 HIS A 810      96.272  73.130  97.063  1.00 12.82           N  
ATOM   5849  N   GLU A 811      92.367  76.537  95.601  1.00 12.05           N  
ATOM   5850  CA  GLU A 811      92.260  77.412  96.763  1.00 12.05           C  
ATOM   5851  C   GLU A 811      91.591  78.705  96.330  1.00 12.05           C  
ATOM   5852  O   GLU A 811      92.123  79.421  95.477  1.00 12.05           O  
ATOM   5853  CB  GLU A 811      93.652  77.668  97.352  1.00 12.05           C  
ATOM   5854  CG  GLU A 811      93.802  78.874  98.268  1.00 12.05           C  
ATOM   5855  CD  GLU A 811      92.702  79.003  99.292  1.00 12.05           C  
ATOM   5856  OE1 GLU A 811      92.273  77.971  99.849  1.00 12.05           O  
ATOM   5857  OE2 GLU A 811      92.274  80.148  99.544  1.00 12.05           O  
ATOM   5858  N   PHE A 812      90.426  78.997  96.902  1.00  8.04           N  
ATOM   5859  CA  PHE A 812      89.733  80.246  96.629  1.00  8.04           C  
ATOM   5860  C   PHE A 812      88.969  80.653  97.876  1.00  8.04           C  
ATOM   5861  O   PHE A 812      88.129  79.892  98.360  1.00  8.04           O  
ATOM   5862  CB  PHE A 812      88.783  80.106  95.434  1.00  8.04           C  
ATOM   5863  CG  PHE A 812      88.101  81.385  95.044  1.00  8.04           C  
ATOM   5864  CD1 PHE A 812      88.817  82.416  94.459  1.00  8.04           C  
ATOM   5865  CD2 PHE A 812      86.744  81.553  95.243  1.00  8.04           C  
ATOM   5866  CE1 PHE A 812      88.197  83.590  94.094  1.00  8.04           C  
ATOM   5867  CE2 PHE A 812      86.119  82.726  94.877  1.00  8.04           C  
ATOM   5868  CZ  PHE A 812      86.847  83.744  94.300  1.00  8.04           C  
ATOM   5869  N   CYS A 813      89.261  81.849  98.384  1.00 10.32           N  
ATOM   5870  CA  CYS A 813      88.633  82.370  99.599  1.00 10.32           C  
ATOM   5871  C   CYS A 813      88.752  81.380 100.754  1.00 10.32           C  
ATOM   5872  O   CYS A 813      87.816  81.179 101.527  1.00 10.32           O  
ATOM   5873  CB  CYS A 813      87.173  82.743  99.344  1.00 10.32           C  
ATOM   5874  SG  CYS A 813      86.942  84.112  98.196  1.00 10.32           S  
ATOM   5875  N   SER A 814      89.920  80.746 100.857  1.00 11.60           N  
ATOM   5876  CA  SER A 814      90.257  79.801 101.920  1.00 11.60           C  
ATOM   5877  C   SER A 814      89.372  78.559 101.917  1.00 11.60           C  
ATOM   5878  O   SER A 814      89.245  77.889 102.945  1.00 11.60           O  
ATOM   5879  CB  SER A 814      90.216  80.471 103.298  1.00 11.60           C  
ATOM   5880  OG  SER A 814      91.202  81.481 103.402  1.00 11.60           O  
ATOM   5881  N   GLN A 815      88.751  78.232 100.789  1.00 10.92           N  
ATOM   5882  CA  GLN A 815      87.946  77.026 100.660  1.00 10.92           C  
ATOM   5883  C   GLN A 815      88.521  76.120  99.580  1.00 10.92           C  
ATOM   5884  O   GLN A 815      88.886  76.584  98.496  1.00 10.92           O  
ATOM   5885  CB  GLN A 815      86.490  77.356 100.320  1.00 10.92           C  
ATOM   5886  CG  GLN A 815      85.847  78.451 101.158  1.00 10.92           C  
ATOM   5887  CD  GLN A 815      85.897  78.166 102.641  1.00 10.92           C  
ATOM   5888  OE1 GLN A 815      85.361  77.164 103.108  1.00 10.92           O  
ATOM   5889  NE2 GLN A 815      86.524  79.060 103.395  1.00 10.92           N  
ATOM   5890  N   HIS A 816      88.607  74.829  99.882  1.00 11.91           N  
ATOM   5891  CA  HIS A 816      88.869  73.833  98.859  1.00 11.91           C  
ATOM   5892  C   HIS A 816      87.555  73.383  98.228  1.00 11.91           C  
ATOM   5893  O   HIS A 816      86.465  73.745  98.674  1.00 11.91           O  
ATOM   5894  CB  HIS A 816      89.623  72.645  99.442  1.00 11.91           C  
ATOM   5895  CG  HIS A 816      90.922  73.010 100.087  1.00 11.91           C  
ATOM   5896  ND1 HIS A 816      92.038  73.364  99.361  1.00 11.91           N  
ATOM   5897  CD2 HIS A 816      91.279  73.088 101.390  1.00 11.91           C  
ATOM   5898  CE1 HIS A 816      93.030  73.634 100.190  1.00 11.91           C  
ATOM   5899  NE2 HIS A 816      92.595  73.476 101.427  1.00 11.91           N  
ATOM   5900  N   THR A 817      87.663  72.588  97.169  1.00 11.44           N  
ATOM   5901  CA  THR A 817      86.502  72.176  96.396  1.00 11.44           C  
ATOM   5902  C   THR A 817      86.540  70.671  96.180  1.00 11.44           C  
ATOM   5903  O   THR A 817      87.607  70.094  95.953  1.00 11.44           O  
ATOM   5904  CB  THR A 817      86.458  72.907  95.043  1.00 11.44           C  
ATOM   5905  OG1 THR A 817      86.187  74.296  95.261  1.00 11.44           O  
ATOM   5906  CG2 THR A 817      85.372  72.338  94.155  1.00 11.44           C  
ATOM   5907  N   MET A 818      85.372  70.037  96.260  1.00 15.19           N  
ATOM   5908  CA  MET A 818      85.213  68.631  95.925  1.00 15.19           C  
ATOM   5909  C   MET A 818      83.972  68.450  95.066  1.00 15.19           C  
ATOM   5910  O   MET A 818      82.967  69.138  95.263  1.00 15.19           O  
ATOM   5911  CB  MET A 818      85.101  67.760  97.178  1.00 15.19           C  
ATOM   5912  CG  MET A 818      84.061  68.239  98.171  1.00 15.19           C  
ATOM   5913  SD  MET A 818      83.853  67.120  99.566  1.00 15.19           S  
ATOM   5914  CE  MET A 818      85.516  67.071 100.214  1.00 15.19           C  
ATOM   5915  N   LEU A 819      84.045  67.521  94.117  1.00 17.22           N  
ATOM   5916  CA  LEU A 819      82.891  67.140  93.312  1.00 17.22           C  
ATOM   5917  C   LEU A 819      82.126  66.041  94.039  1.00 17.22           C  
ATOM   5918  O   LEU A 819      82.663  64.955  94.279  1.00 17.22           O  
ATOM   5919  CB  LEU A 819      83.316  66.681  91.920  1.00 17.22           C  
ATOM   5920  CG  LEU A 819      82.188  66.510  90.901  1.00 17.22           C  
ATOM   5921  CD1 LEU A 819      81.813  67.823  90.254  1.00 17.22           C  
ATOM   5922  CD2 LEU A 819      82.598  65.502  89.845  1.00 17.22           C  
ATOM   5923  N   VAL A 820      80.875  66.327  94.381  1.00 22.15           N  
ATOM   5924  CA  VAL A 820      80.078  65.500  95.275  1.00 22.15           C  
ATOM   5925  C   VAL A 820      78.797  65.091  94.565  1.00 22.15           C  
ATOM   5926  O   VAL A 820      78.140  65.919  93.926  1.00 22.15           O  
ATOM   5927  CB  VAL A 820      79.761  66.256  96.581  1.00 22.15           C  
ATOM   5928  CG1 VAL A 820      78.648  65.575  97.345  1.00 22.15           C  
ATOM   5929  CG2 VAL A 820      81.003  66.367  97.432  1.00 22.15           C  
ATOM   5930  N   LYS A 821      78.445  63.814  94.674  1.00 31.54           N  
ATOM   5931  CA  LYS A 821      77.152  63.347  94.194  1.00 31.54           C  
ATOM   5932  C   LYS A 821      76.077  63.762  95.189  1.00 31.54           C  
ATOM   5933  O   LYS A 821      76.118  63.365  96.358  1.00 31.54           O  
ATOM   5934  CB  LYS A 821      77.160  61.833  94.007  1.00 31.54           C  
ATOM   5935  CG  LYS A 821      75.989  61.312  93.198  1.00 31.54           C  
ATOM   5936  CD  LYS A 821      76.253  59.910  92.677  1.00 31.54           C  
ATOM   5937  CE  LYS A 821      75.086  59.404  91.846  1.00 31.54           C  
ATOM   5938  NZ  LYS A 821      74.271  60.525  91.298  1.00 31.54           N  
ATOM   5939  N   GLN A 822      75.116  64.555  94.724  1.00 34.77           N  
ATOM   5940  CA  GLN A 822      74.059  65.093  95.579  1.00 34.77           C  
ATOM   5941  C   GLN A 822      72.752  64.949  94.807  1.00 34.77           C  
ATOM   5942  O   GLN A 822      72.480  65.720  93.883  1.00 34.77           O  
ATOM   5943  CB  GLN A 822      74.339  66.541  95.960  1.00 34.77           C  
ATOM   5944  CG  GLN A 822      73.145  67.307  96.492  1.00 34.77           C  
ATOM   5945  CD  GLN A 822      73.393  68.799  96.536  1.00 34.77           C  
ATOM   5946  OE1 GLN A 822      74.034  69.305  97.455  1.00 34.77           O  
ATOM   5947  NE2 GLN A 822      72.887  69.512  95.538  1.00 34.77           N  
ATOM   5948  N   GLY A 823      71.960  63.951  95.177  1.00 44.14           N  
ATOM   5949  CA  GLY A 823      70.763  63.655  94.411  1.00 44.14           C  
ATOM   5950  C   GLY A 823      71.125  62.892  93.153  1.00 44.14           C  
ATOM   5951  O   GLY A 823      71.895  61.926  93.185  1.00 44.14           O  
ATOM   5952  N   ASP A 824      70.565  63.325  92.026  1.00 48.03           N  
ATOM   5953  CA  ASP A 824      70.797  62.667  90.747  1.00 48.03           C  
ATOM   5954  C   ASP A 824      71.965  63.256  89.966  1.00 48.03           C  
ATOM   5955  O   ASP A 824      72.233  62.791  88.853  1.00 48.03           O  
ATOM   5956  CB  ASP A 824      69.528  62.726  89.893  1.00 48.03           C  
ATOM   5957  N   ASP A 825      72.665  64.253  90.504  1.00 40.82           N  
ATOM   5958  CA  ASP A 825      73.726  64.910  89.755  1.00 40.82           C  
ATOM   5959  C   ASP A 825      74.827  65.362  90.702  1.00 40.82           C  
ATOM   5960  O   ASP A 825      74.635  65.453  91.917  1.00 40.82           O  
ATOM   5961  CB  ASP A 825      73.184  66.095  88.948  1.00 40.82           C  
ATOM   5962  CG  ASP A 825      72.198  66.934  89.734  1.00 40.82           C  
ATOM   5963  OD1 ASP A 825      72.175  66.823  90.978  1.00 40.82           O  
ATOM   5964  OD2 ASP A 825      71.442  67.704  89.107  1.00 40.82           O  
ATOM   5965  N   TYR A 826      75.989  65.649  90.121  1.00 31.15           N  
ATOM   5966  CA  TYR A 826      77.186  66.018  90.864  1.00 31.15           C  
ATOM   5967  C   TYR A 826      77.293  67.531  90.980  1.00 31.15           C  
ATOM   5968  O   TYR A 826      77.013  68.259  90.024  1.00 31.15           O  
ATOM   5969  CB  TYR A 826      78.438  65.463  90.184  1.00 31.15           C  
ATOM   5970  CG  TYR A 826      78.530  63.956  90.200  1.00 31.15           C  
ATOM   5971  CD1 TYR A 826      77.824  63.190  89.286  1.00 31.15           C  
ATOM   5972  CD2 TYR A 826      79.330  63.301  91.123  1.00 31.15           C  
ATOM   5973  CE1 TYR A 826      77.904  61.815  89.296  1.00 31.15           C  
ATOM   5974  CE2 TYR A 826      79.417  61.925  91.140  1.00 31.15           C  
ATOM   5975  CZ  TYR A 826      78.703  61.187  90.225  1.00 31.15           C  
ATOM   5976  OH  TYR A 826      78.788  59.814  90.239  1.00 31.15           O  
ATOM   5977  N   VAL A 827      77.706  68.001  92.159  1.00 18.93           N  
ATOM   5978  CA  VAL A 827      77.842  69.425  92.434  1.00 18.93           C  
ATOM   5979  C   VAL A 827      79.176  69.686  93.118  1.00 18.93           C  
ATOM   5980  O   VAL A 827      79.782  68.795  93.715  1.00 18.93           O  
ATOM   5981  CB  VAL A 827      76.687  69.968  93.304  1.00 18.93           C  
ATOM   5982  CG1 VAL A 827      75.371  69.884  92.557  1.00 18.93           C  
ATOM   5983  CG2 VAL A 827      76.608  69.204  94.608  1.00 18.93           C  
ATOM   5984  N   TYR A 828      79.634  70.930  93.012  1.00 13.17           N  
ATOM   5985  CA  TYR A 828      80.851  71.382  93.671  1.00 13.17           C  
ATOM   5986  C   TYR A 828      80.514  71.949  95.044  1.00 13.17           C  
ATOM   5987  O   TYR A 828      79.716  72.884  95.157  1.00 13.17           O  
ATOM   5988  CB  TYR A 828      81.568  72.430  92.824  1.00 13.17           C  
ATOM   5989  CG  TYR A 828      82.129  71.911  91.524  1.00 13.17           C  
ATOM   5990  CD1 TYR A 828      83.240  71.081  91.513  1.00 13.17           C  
ATOM   5991  CD2 TYR A 828      81.576  72.280  90.308  1.00 13.17           C  
ATOM   5992  CE1 TYR A 828      83.770  70.617  90.333  1.00 13.17           C  
ATOM   5993  CE2 TYR A 828      82.095  71.812  89.120  1.00 13.17           C  
ATOM   5994  CZ  TYR A 828      83.192  70.981  89.140  1.00 13.17           C  
ATOM   5995  OH  TYR A 828      83.718  70.515  87.961  1.00 13.17           O  
ATOM   5996  N   LEU A 829      81.120  71.385  96.078  1.00 12.73           N  
ATOM   5997  CA  LEU A 829      80.926  71.869  97.429  1.00 12.73           C  
ATOM   5998  C   LEU A 829      82.214  72.469  97.974  1.00 12.73           C  
ATOM   5999  O   LEU A 829      83.289  71.885  97.804  1.00 12.73           O  
ATOM   6000  CB  LEU A 829      80.465  70.744  98.361  1.00 12.73           C  
ATOM   6001  CG  LEU A 829      79.063  70.181  98.137  1.00 12.73           C  
ATOM   6002  CD1 LEU A 829      78.740  69.135  99.188  1.00 12.73           C  
ATOM   6003  CD2 LEU A 829      78.036  71.288  98.144  1.00 12.73           C  
ATOM   6004  N   PRO A 830      82.145  73.630  98.615  1.00 10.32           N  
ATOM   6005  CA  PRO A 830      83.326  74.178  99.279  1.00 10.32           C  
ATOM   6006  C   PRO A 830      83.509  73.575 100.659  1.00 10.32           C  
ATOM   6007  O   PRO A 830      82.546  73.255 101.357  1.00 10.32           O  
ATOM   6008  CB  PRO A 830      83.007  75.673  99.371  1.00 10.32           C  
ATOM   6009  CG  PRO A 830      81.524  75.718  99.474  1.00 10.32           C  
ATOM   6010  CD  PRO A 830      80.976  74.512  98.750  1.00 10.32           C  
ATOM   6011  N   TYR A 831      84.769  73.420 101.059  1.00 12.96           N  
ATOM   6012  CA  TYR A 831      85.039  72.929 102.398  1.00 12.96           C  
ATOM   6013  C   TYR A 831      86.295  73.559 102.981  1.00 12.96           C  
ATOM   6014  O   TYR A 831      87.279  73.779 102.261  1.00 12.96           O  
ATOM   6015  CB  TYR A 831      85.145  71.395 102.423  1.00 12.96           C  
ATOM   6016  CG  TYR A 831      86.395  70.799 101.826  1.00 12.96           C  
ATOM   6017  CD1 TYR A 831      86.451  70.469 100.483  1.00 12.96           C  
ATOM   6018  CD2 TYR A 831      87.504  70.527 102.610  1.00 12.96           C  
ATOM   6019  CE1 TYR A 831      87.579  69.906  99.935  1.00 12.96           C  
ATOM   6020  CE2 TYR A 831      88.637  69.966 102.069  1.00 12.96           C  
ATOM   6021  CZ  TYR A 831      88.669  69.657 100.731  1.00 12.96           C  
ATOM   6022  OH  TYR A 831      89.800  69.097 100.187  1.00 12.96           O  
ATOM   6023  N   PRO A 832      86.278  73.877 104.270  1.00 15.06           N  
ATOM   6024  CA  PRO A 832      87.425  74.532 104.895  1.00 15.06           C  
ATOM   6025  C   PRO A 832      88.498  73.544 105.325  1.00 15.06           C  
ATOM   6026  O   PRO A 832      88.311  72.327 105.322  1.00 15.06           O  
ATOM   6027  CB  PRO A 832      86.801  75.218 106.113  1.00 15.06           C  
ATOM   6028  CG  PRO A 832      85.703  74.298 106.494  1.00 15.06           C  
ATOM   6029  CD  PRO A 832      85.143  73.767 105.200  1.00 15.06           C  
ATOM   6030  N   ASP A 833      89.639  74.103 105.694  1.00 17.72           N  
ATOM   6031  CA  ASP A 833      90.691  73.345 106.349  1.00 17.72           C  
ATOM   6032  C   ASP A 833      90.205  72.881 107.718  1.00 17.72           C  
ATOM   6033  O   ASP A 833      89.797  73.720 108.534  1.00 17.72           O  
ATOM   6034  CB  ASP A 833      91.937  74.214 106.482  1.00 17.72           C  
ATOM   6035  CG  ASP A 833      93.165  73.423 106.865  1.00 17.72           C  
ATOM   6036  OD1 ASP A 833      93.320  72.286 106.376  1.00 17.72           O  
ATOM   6037  OD2 ASP A 833      93.978  73.942 107.657  1.00 17.72           O  
ATOM   6038  N   PRO A 834      90.214  71.576 108.008  1.00 18.48           N  
ATOM   6039  CA  PRO A 834      89.698  71.101 109.303  1.00 18.48           C  
ATOM   6040  C   PRO A 834      90.379  71.731 110.505  1.00 18.48           C  
ATOM   6041  O   PRO A 834      89.735  71.939 111.547  1.00 18.48           O  
ATOM   6042  CB  PRO A 834      89.961  69.592 109.242  1.00 18.48           C  
ATOM   6043  CG  PRO A 834      89.938  69.269 107.795  1.00 18.48           C  
ATOM   6044  CD  PRO A 834      90.526  70.463 107.097  1.00 18.48           C  
ATOM   6045  N   SER A 835      91.673  72.040 110.387  1.00 19.36           N  
ATOM   6046  CA  SER A 835      92.384  72.711 111.467  1.00 19.36           C  
ATOM   6047  C   SER A 835      91.769  74.063 111.785  1.00 19.36           C  
ATOM   6048  O   SER A 835      91.737  74.469 112.948  1.00 19.36           O  
ATOM   6049  CB  SER A 835      93.857  72.876 111.098  1.00 19.36           C  
ATOM   6050  OG  SER A 835      94.498  73.797 111.963  1.00 19.36           O  
ATOM   6051  N   ARG A 836      91.256  74.761 110.770  1.00 17.58           N  
ATOM   6052  CA  ARG A 836      90.671  76.080 110.987  1.00 17.58           C  
ATOM   6053  C   ARG A 836      89.400  75.985 111.826  1.00 17.58           C  
ATOM   6054  O   ARG A 836      89.201  76.771 112.762  1.00 17.58           O  
ATOM   6055  CB  ARG A 836      90.398  76.730 109.629  1.00 17.58           C  
ATOM   6056  CG  ARG A 836      89.667  78.056 109.642  1.00 17.58           C  
ATOM   6057  CD  ARG A 836      90.327  79.031 110.592  1.00 17.58           C  
ATOM   6058  NE  ARG A 836      89.639  80.313 110.631  1.00 17.58           N  
ATOM   6059  CZ  ARG A 836      88.795  80.679 111.586  1.00 17.58           C  
ATOM   6060  NH1 ARG A 836      88.219  81.869 111.544  1.00 17.58           N  
ATOM   6061  NH2 ARG A 836      88.523  79.851 112.580  1.00 17.58           N  
ATOM   6062  N   ILE A 837      88.557  74.990 111.544  1.00 20.41           N  
ATOM   6063  CA  ILE A 837      87.323  74.811 112.302  1.00 20.41           C  
ATOM   6064  C   ILE A 837      87.617  74.313 113.712  1.00 20.41           C  
ATOM   6065  O   ILE A 837      86.998  74.765 114.684  1.00 20.41           O  
ATOM   6066  CB  ILE A 837      86.379  73.859 111.547  1.00 20.41           C  
ATOM   6067  CG1 ILE A 837      86.193  74.332 110.107  1.00 20.41           C  
ATOM   6068  CG2 ILE A 837      85.034  73.770 112.246  1.00 20.41           C  
ATOM   6069  CD1 ILE A 837      85.278  75.524 109.974  1.00 20.41           C  
ATOM   6070  N   LEU A 838      88.568  73.386 113.857  1.00 20.79           N  
ATOM   6071  CA  LEU A 838      88.927  72.937 115.199  1.00 20.79           C  
ATOM   6072  C   LEU A 838      89.526  74.069 116.023  1.00 20.79           C  
ATOM   6073  O   LEU A 838      89.289  74.152 117.231  1.00 20.79           O  
ATOM   6074  CB  LEU A 838      89.884  71.752 115.137  1.00 20.79           C  
ATOM   6075  CG  LEU A 838      89.278  70.455 114.612  1.00 20.79           C  
ATOM   6076  CD1 LEU A 838      90.365  69.436 114.453  1.00 20.79           C  
ATOM   6077  CD2 LEU A 838      88.219  69.952 115.571  1.00 20.79           C  
ATOM   6078  N   GLY A 839      90.320  74.937 115.397  1.00 20.60           N  
ATOM   6079  CA  GLY A 839      90.819  76.104 116.103  1.00 20.60           C  
ATOM   6080  C   GLY A 839      89.711  77.051 116.514  1.00 20.60           C  
ATOM   6081  O   GLY A 839      89.723  77.592 117.622  1.00 20.60           O  
ATOM   6082  N   ALA A 840      88.733  77.264 115.629  1.00 21.89           N  
ATOM   6083  CA  ALA A 840      87.597  78.101 115.996  1.00 21.89           C  
ATOM   6084  C   ALA A 840      86.782  77.492 117.125  1.00 21.89           C  
ATOM   6085  O   ALA A 840      86.110  78.226 117.857  1.00 21.89           O  
ATOM   6086  CB  ALA A 840      86.699  78.338 114.784  1.00 21.89           C  
ATOM   6087  N   GLY A 841      86.831  76.175 117.282  1.00 23.26           N  
ATOM   6088  CA  GLY A 841      86.178  75.535 118.407  1.00 23.26           C  
ATOM   6089  C   GLY A 841      86.962  75.614 119.704  1.00 23.26           C  
ATOM   6090  O   GLY A 841      86.400  75.916 120.761  1.00 23.26           O  
ATOM   6091  N   CYS A 842      88.268  75.347 119.631  1.00 28.98           N  
ATOM   6092  CA  CYS A 842      89.077  75.211 120.840  1.00 28.98           C  
ATOM   6093  C   CYS A 842      89.371  76.559 121.490  1.00 28.98           C  
ATOM   6094  O   CYS A 842      89.391  76.663 122.720  1.00 28.98           O  
ATOM   6095  CB  CYS A 842      90.383  74.485 120.518  1.00 28.98           C  
ATOM   6096  SG  CYS A 842      90.217  72.703 120.276  1.00 28.98           S  
ATOM   6097  N   PHE A 843      89.607  77.599 120.694  1.00 27.53           N  
ATOM   6098  CA  PHE A 843      90.051  78.879 121.227  1.00 27.53           C  
ATOM   6099  C   PHE A 843      89.045  79.969 120.893  1.00 27.53           C  
ATOM   6100  O   PHE A 843      88.506  80.011 119.784  1.00 27.53           O  
ATOM   6101  CB  PHE A 843      91.431  79.282 120.686  1.00 27.53           C  
ATOM   6102  CG  PHE A 843      92.450  78.181 120.722  1.00 27.53           C  
ATOM   6103  CD1 PHE A 843      93.236  77.988 121.843  1.00 27.53           C  
ATOM   6104  CD2 PHE A 843      92.611  77.330 119.644  1.00 27.53           C  
ATOM   6105  CE1 PHE A 843      94.170  76.973 121.883  1.00 27.53           C  
ATOM   6106  CE2 PHE A 843      93.545  76.319 119.677  1.00 27.53           C  
ATOM   6107  CZ  PHE A 843      94.325  76.138 120.799  1.00 27.53           C  
ATOM   6108  N   VAL A 844      88.805  80.854 121.863  1.00 31.92           N  
ATOM   6109  CA  VAL A 844      87.884  81.973 121.713  1.00 31.92           C  
ATOM   6110  C   VAL A 844      88.562  83.239 122.219  1.00 31.92           C  
ATOM   6111  O   VAL A 844      89.545  83.193 122.961  1.00 31.92           O  
ATOM   6112  CB  VAL A 844      86.549  81.753 122.463  1.00 31.92           C  
ATOM   6113  CG1 VAL A 844      85.897  80.455 122.028  1.00 31.92           C  
ATOM   6114  CG2 VAL A 844      86.775  81.761 123.961  1.00 31.92           C  
ATOM   6115  N   ASP A 845      88.056  84.394 121.816  1.00 38.00           N  
ATOM   6116  CA  ASP A 845      88.655  85.687 122.214  1.00 38.00           C  
ATOM   6117  C   ASP A 845      87.842  86.354 123.326  1.00 38.00           C  
ATOM   6118  O   ASP A 845      88.122  87.521 123.595  1.00 38.00           O  
ATOM   6119  CB  ASP A 845      88.812  86.571 120.986  1.00 38.00           C  
ATOM   6120  CG  ASP A 845      87.507  87.119 120.433  1.00 38.00           C  
ATOM   6121  OD1 ASP A 845      86.522  87.170 121.191  1.00 38.00           O  
ATOM   6122  OD2 ASP A 845      87.489  87.496 119.244  1.00 38.00           O  
ATOM   6123  N   ASP A 846      86.885  85.659 123.959  1.00 47.12           N  
ATOM   6124  CA  ASP A 846      86.184  86.209 125.113  1.00 47.12           C  
ATOM   6125  C   ASP A 846      85.630  85.054 125.934  1.00 47.12           C  
ATOM   6126  O   ASP A 846      85.034  84.129 125.376  1.00 47.12           O  
ATOM   6127  CB  ASP A 846      85.057  87.153 124.679  1.00 47.12           C  
ATOM   6128  CG  ASP A 846      84.192  87.620 125.843  1.00 47.12           C  
ATOM   6129  OD1 ASP A 846      84.630  87.513 127.010  1.00 47.12           O  
ATOM   6130  OD2 ASP A 846      83.065  88.094 125.588  1.00 47.12           O  
ATOM   6131  N   ILE A 847      85.834  85.111 127.253  1.00 48.50           N  
ATOM   6132  CA  ILE A 847      85.360  84.055 128.141  1.00 48.50           C  
ATOM   6133  C   ILE A 847      83.842  83.936 128.134  1.00 48.50           C  
ATOM   6134  O   ILE A 847      83.309  82.862 128.433  1.00 48.50           O  
ATOM   6135  CB  ILE A 847      85.877  84.285 129.577  1.00 48.50           C  
ATOM   6136  CG1 ILE A 847      85.232  85.528 130.188  1.00 48.50           C  
ATOM   6137  CG2 ILE A 847      87.392  84.402 129.588  1.00 48.50           C  
ATOM   6138  CD1 ILE A 847      85.583  85.744 131.640  1.00 48.50           C  
ATOM   6139  N   VAL A 848      83.127  85.016 127.809  1.00 49.02           N  
ATOM   6140  CA  VAL A 848      81.669  84.971 127.807  1.00 49.02           C  
ATOM   6141  C   VAL A 848      81.144  84.029 126.733  1.00 49.02           C  
ATOM   6142  O   VAL A 848      80.034  83.498 126.862  1.00 49.02           O  
ATOM   6143  CB  VAL A 848      81.099  86.393 127.632  1.00 49.02           C  
ATOM   6144  CG1 VAL A 848      79.579  86.392 127.749  1.00 49.02           C  
ATOM   6145  CG2 VAL A 848      81.712  87.336 128.654  1.00 49.02           C  
ATOM   6146  N   LYS A 849      81.927  83.778 125.684  1.00 45.10           N  
ATOM   6147  CA  LYS A 849      81.544  82.819 124.654  1.00 45.10           C  
ATOM   6148  C   LYS A 849      81.658  81.370 125.113  1.00 45.10           C  
ATOM   6149  O   LYS A 849      81.502  80.465 124.286  1.00 45.10           O  
ATOM   6150  CB  LYS A 849      82.377  83.054 123.394  1.00 45.10           C  
ATOM   6151  CG  LYS A 849      82.087  84.396 122.737  1.00 45.10           C  
ATOM   6152  CD  LYS A 849      83.330  85.047 122.168  1.00 45.10           C  
ATOM   6153  CE  LYS A 849      82.979  85.926 120.981  1.00 45.10           C  
ATOM   6154  NZ  LYS A 849      84.063  86.886 120.648  1.00 45.10           N  
ATOM   6155  N   THR A 850      81.937  81.128 126.393  1.00 49.23           N  
ATOM   6156  CA  THR A 850      81.814  79.802 126.984  1.00 49.23           C  
ATOM   6157  C   THR A 850      80.406  79.549 127.522  1.00 49.23           C  
ATOM   6158  O   THR A 850      80.033  78.391 127.744  1.00 49.23           O  
ATOM   6159  CB  THR A 850      82.877  79.641 128.091  1.00 49.23           C  
ATOM   6160  OG1 THR A 850      84.179  79.600 127.492  1.00 49.23           O  
ATOM   6161  CG2 THR A 850      82.690  78.363 128.898  1.00 49.23           C  
ATOM   6162  N   ASP A 851      79.597  80.598 127.662  1.00 53.56           N  
ATOM   6163  CA  ASP A 851      78.208  80.453 128.082  1.00 53.56           C  
ATOM   6164  C   ASP A 851      77.460  79.615 127.052  1.00 53.56           C  
ATOM   6165  O   ASP A 851      77.599  79.831 125.845  1.00 53.56           O  
ATOM   6166  CB  ASP A 851      77.572  81.839 128.239  1.00 53.56           C  
ATOM   6167  CG  ASP A 851      76.041  81.815 128.281  1.00 53.56           C  
ATOM   6168  OD1 ASP A 851      75.422  80.738 128.420  1.00 53.56           O  
ATOM   6169  OD2 ASP A 851      75.448  82.914 128.247  1.00 53.56           O  
ATOM   6170  N   GLY A 852      76.667  78.658 127.539  1.00 50.00           N  
ATOM   6171  CA  GLY A 852      76.002  77.720 126.647  1.00 50.00           C  
ATOM   6172  C   GLY A 852      75.138  78.386 125.594  1.00 50.00           C  
ATOM   6173  O   GLY A 852      75.059  77.915 124.459  1.00 50.00           O  
ATOM   6174  N   THR A 853      74.482  79.494 125.949  1.00 49.41           N  
ATOM   6175  CA  THR A 853      73.541  80.117 125.022  1.00 49.41           C  
ATOM   6176  C   THR A 853      74.237  80.674 123.785  1.00 49.41           C  
ATOM   6177  O   THR A 853      73.692  80.586 122.680  1.00 49.41           O  
ATOM   6178  CB  THR A 853      72.758  81.224 125.728  1.00 49.41           C  
ATOM   6179  OG1 THR A 853      73.665  82.236 126.182  1.00 49.41           O  
ATOM   6180  CG2 THR A 853      71.996  80.658 126.918  1.00 49.41           C  
ATOM   6181  N   LEU A 854      75.426  81.256 123.945  1.00 44.89           N  
ATOM   6182  CA  LEU A 854      76.182  81.729 122.790  1.00 44.89           C  
ATOM   6183  C   LEU A 854      77.016  80.609 122.182  1.00 44.89           C  
ATOM   6184  O   LEU A 854      77.231  80.573 120.963  1.00 44.89           O  
ATOM   6185  CB  LEU A 854      77.075  82.901 123.195  1.00 44.89           C  
ATOM   6186  CG  LEU A 854      76.467  84.301 123.110  1.00 44.89           C  
ATOM   6187  CD1 LEU A 854      77.552  85.357 123.230  1.00 44.89           C  
ATOM   6188  CD2 LEU A 854      75.688  84.476 121.816  1.00 44.89           C  
ATOM   6189  N   MET A 855      77.487  79.692 123.026  1.00 43.02           N  
ATOM   6190  CA  MET A 855      78.320  78.592 122.559  1.00 43.02           C  
ATOM   6191  C   MET A 855      77.553  77.687 121.601  1.00 43.02           C  
ATOM   6192  O   MET A 855      78.109  77.220 120.599  1.00 43.02           O  
ATOM   6193  CB  MET A 855      78.848  77.810 123.762  1.00 43.02           C  
ATOM   6194  CG  MET A 855      79.934  76.811 123.447  1.00 43.02           C  
ATOM   6195  SD  MET A 855      80.628  76.009 124.907  1.00 43.02           S  
ATOM   6196  CE  MET A 855      79.172  75.808 125.927  1.00 43.02           C  
ATOM   6197  N   ILE A 856      76.273  77.436 121.887  1.00 40.27           N  
ATOM   6198  CA  ILE A 856      75.479  76.582 121.010  1.00 40.27           C  
ATOM   6199  C   ILE A 856      75.323  77.222 119.636  1.00 40.27           C  
ATOM   6200  O   ILE A 856      75.474  76.552 118.610  1.00 40.27           O  
ATOM   6201  CB  ILE A 856      74.119  76.250 121.658  1.00 40.27           C  
ATOM   6202  CG1 ILE A 856      73.373  75.204 120.828  1.00 40.27           C  
ATOM   6203  CG2 ILE A 856      73.267  77.496 121.863  1.00 40.27           C  
ATOM   6204  CD1 ILE A 856      72.391  74.383 121.630  1.00 40.27           C  
ATOM   6205  N   GLU A 857      75.063  78.532 119.587  1.00 36.69           N  
ATOM   6206  CA  GLU A 857      74.943  79.212 118.300  1.00 36.69           C  
ATOM   6207  C   GLU A 857      76.261  79.207 117.543  1.00 36.69           C  
ATOM   6208  O   GLU A 857      76.278  79.039 116.314  1.00 36.69           O  
ATOM   6209  CB  GLU A 857      74.474  80.652 118.505  1.00 36.69           C  
ATOM   6210  CG  GLU A 857      73.047  80.798 118.994  1.00 36.69           C  
ATOM   6211  CD  GLU A 857      72.879  81.982 119.928  1.00 36.69           C  
ATOM   6212  OE1 GLU A 857      71.999  81.929 120.812  1.00 36.69           O  
ATOM   6213  OE2 GLU A 857      73.640  82.961 119.784  1.00 36.69           O  
ATOM   6214  N   ARG A 858      77.373  79.346 118.266  1.00 26.73           N  
ATOM   6215  CA  ARG A 858      78.707  79.389 117.633  1.00 26.73           C  
ATOM   6216  C   ARG A 858      79.011  78.030 117.018  1.00 26.73           C  
ATOM   6217  O   ARG A 858      79.474  78.005 115.895  1.00 26.73           O  
ATOM   6218  CB  ARG A 858      79.749  79.820 118.661  1.00 26.73           C  
ATOM   6219  CG  ARG A 858      81.178  79.543 118.226  1.00 26.73           C  
ATOM   6220  CD  ARG A 858      82.189  79.585 119.349  1.00 26.73           C  
ATOM   6221  NE  ARG A 858      83.507  79.828 118.790  1.00 26.73           N  
ATOM   6222  CZ  ARG A 858      84.093  81.013 118.764  1.00 26.73           C  
ATOM   6223  NH1 ARG A 858      85.294  81.149 118.235  1.00 26.73           N  
ATOM   6224  NH2 ARG A 858      83.483  82.057 119.287  1.00 26.73           N  
ATOM   6225  N   PHE A 859      78.679  76.945 117.713  1.00 26.30           N  
ATOM   6226  CA  PHE A 859      78.900  75.614 117.158  1.00 26.30           C  
ATOM   6227  C   PHE A 859      77.917  75.283 116.040  1.00 26.30           C  
ATOM   6228  O   PHE A 859      78.260  74.525 115.131  1.00 26.30           O  
ATOM   6229  CB  PHE A 859      78.876  74.571 118.271  1.00 26.30           C  
ATOM   6230  CG  PHE A 859      80.140  74.541 119.072  1.00 26.30           C  
ATOM   6231  CD1 PHE A 859      81.304  74.065 118.504  1.00 26.30           C  
ATOM   6232  CD2 PHE A 859      80.190  75.039 120.355  1.00 26.30           C  
ATOM   6233  CE1 PHE A 859      82.481  74.041 119.210  1.00 26.30           C  
ATOM   6234  CE2 PHE A 859      81.372  75.029 121.061  1.00 26.30           C  
ATOM   6235  CZ  PHE A 859      82.515  74.525 120.491  1.00 26.30           C  
ATOM   6236  N   VAL A 860      76.701  75.835 116.067  1.00 22.94           N  
ATOM   6237  CA  VAL A 860      75.827  75.690 114.900  1.00 22.94           C  
ATOM   6238  C   VAL A 860      76.455  76.342 113.674  1.00 22.94           C  
ATOM   6239  O   VAL A 860      76.429  75.779 112.573  1.00 22.94           O  
ATOM   6240  CB  VAL A 860      74.420  76.252 115.175  1.00 22.94           C  
ATOM   6241  CG1 VAL A 860      73.522  75.988 113.987  1.00 22.94           C  
ATOM   6242  CG2 VAL A 860      73.810  75.576 116.372  1.00 22.94           C  
ATOM   6243  N   SER A 861      77.035  77.532 113.843  1.00 20.66           N  
ATOM   6244  CA  SER A 861      77.688  78.182 112.708  1.00 20.66           C  
ATOM   6245  C   SER A 861      78.881  77.368 112.213  1.00 20.66           C  
ATOM   6246  O   SER A 861      79.062  77.178 111.001  1.00 20.66           O  
ATOM   6247  CB  SER A 861      78.129  79.591 113.098  1.00 20.66           C  
ATOM   6248  OG  SER A 861      77.019  80.413 113.400  1.00 20.66           O  
ATOM   6249  N   LEU A 862      79.687  76.849 113.138  1.00 19.92           N  
ATOM   6250  CA  LEU A 862      80.854  76.075 112.734  1.00 19.92           C  
ATOM   6251  C   LEU A 862      80.473  74.723 112.146  1.00 19.92           C  
ATOM   6252  O   LEU A 862      81.234  74.166 111.353  1.00 19.92           O  
ATOM   6253  CB  LEU A 862      81.804  75.891 113.915  1.00 19.92           C  
ATOM   6254  CG  LEU A 862      82.329  77.178 114.548  1.00 19.92           C  
ATOM   6255  CD1 LEU A 862      83.119  76.876 115.802  1.00 19.92           C  
ATOM   6256  CD2 LEU A 862      83.176  77.944 113.552  1.00 19.92           C  
ATOM   6257  N   ALA A 863      79.312  74.179 112.516  1.00 19.79           N  
ATOM   6258  CA  ALA A 863      78.829  72.956 111.888  1.00 19.79           C  
ATOM   6259  C   ALA A 863      78.264  73.220 110.501  1.00 19.79           C  
ATOM   6260  O   ALA A 863      78.390  72.372 109.613  1.00 19.79           O  
ATOM   6261  CB  ALA A 863      77.776  72.290 112.771  1.00 19.79           C  
ATOM   6262  N   ILE A 864      77.629  74.376 110.293  1.00 19.84           N  
ATOM   6263  CA  ILE A 864      77.229  74.752 108.940  1.00 19.84           C  
ATOM   6264  C   ILE A 864      78.457  74.891 108.056  1.00 19.84           C  
ATOM   6265  O   ILE A 864      78.439  74.522 106.876  1.00 19.84           O  
ATOM   6266  CB  ILE A 864      76.394  76.047 108.949  1.00 19.84           C  
ATOM   6267  CG1 ILE A 864      75.098  75.861 109.733  1.00 19.84           C  
ATOM   6268  CG2 ILE A 864      76.074  76.480 107.532  1.00 19.84           C  
ATOM   6269  CD1 ILE A 864      74.192  77.064 109.690  1.00 19.84           C  
ATOM   6270  N   ASP A 865      79.548  75.419 108.613  1.00 19.33           N  
ATOM   6271  CA  ASP A 865      80.779  75.523 107.834  1.00 19.33           C  
ATOM   6272  C   ASP A 865      81.461  74.172 107.624  1.00 19.33           C  
ATOM   6273  O   ASP A 865      82.028  73.931 106.554  1.00 19.33           O  
ATOM   6274  CB  ASP A 865      81.749  76.492 108.508  1.00 19.33           C  
ATOM   6275  CG  ASP A 865      81.376  77.941 108.280  1.00 19.33           C  
ATOM   6276  OD1 ASP A 865      81.001  78.285 107.141  1.00 19.33           O  
ATOM   6277  OD2 ASP A 865      81.455  78.738 109.239  1.00 19.33           O  
ATOM   6278  N   ALA A 866      81.422  73.289 108.624  1.00 19.45           N  
ATOM   6279  CA  ALA A 866      82.163  72.034 108.571  1.00 19.45           C  
ATOM   6280  C   ALA A 866      81.432  70.925 107.826  1.00 19.45           C  
ATOM   6281  O   ALA A 866      82.049  69.898 107.528  1.00 19.45           O  
ATOM   6282  CB  ALA A 866      82.489  71.560 109.986  1.00 19.45           C  
ATOM   6283  N   TYR A 867      80.141  71.091 107.540  1.00 20.82           N  
ATOM   6284  CA  TYR A 867      79.328  69.995 107.013  1.00 20.82           C  
ATOM   6285  C   TYR A 867      79.907  69.306 105.781  1.00 20.82           C  
ATOM   6286  O   TYR A 867      79.882  68.067 105.736  1.00 20.82           O  
ATOM   6287  CB  TYR A 867      77.907  70.494 106.721  1.00 20.82           C  
ATOM   6288  CG  TYR A 867      77.134  69.557 105.824  1.00 20.82           C  
ATOM   6289  CD1 TYR A 867      76.536  68.417 106.336  1.00 20.82           C  
ATOM   6290  CD2 TYR A 867      77.007  69.809 104.466  1.00 20.82           C  
ATOM   6291  CE1 TYR A 867      75.839  67.554 105.524  1.00 20.82           C  
ATOM   6292  CE2 TYR A 867      76.310  68.951 103.646  1.00 20.82           C  
ATOM   6293  CZ  TYR A 867      75.728  67.826 104.181  1.00 20.82           C  
ATOM   6294  OH  TYR A 867      75.031  66.965 103.371  1.00 20.82           O  
ATOM   6295  N   PRO A 868      80.413  70.010 104.761  1.00 17.93           N  
ATOM   6296  CA  PRO A 868      80.896  69.300 103.562  1.00 17.93           C  
ATOM   6297  C   PRO A 868      82.030  68.322 103.824  1.00 17.93           C  
ATOM   6298  O   PRO A 868      82.325  67.500 102.949  1.00 17.93           O  
ATOM   6299  CB  PRO A 868      81.342  70.440 102.637  1.00 17.93           C  
ATOM   6300  CG  PRO A 868      80.524  71.592 103.070  1.00 17.93           C  
ATOM   6301  CD  PRO A 868      80.459  71.466 104.556  1.00 17.93           C  
ATOM   6302  N   LEU A 869      82.681  68.389 104.988  1.00 19.43           N  
ATOM   6303  CA  LEU A 869      83.772  67.468 105.294  1.00 19.43           C  
ATOM   6304  C   LEU A 869      83.313  66.014 105.311  1.00 19.43           C  
ATOM   6305  O   LEU A 869      84.128  65.109 105.103  1.00 19.43           O  
ATOM   6306  CB  LEU A 869      84.403  67.838 106.634  1.00 19.43           C  
ATOM   6307  CG  LEU A 869      85.182  69.151 106.677  1.00 19.43           C  
ATOM   6308  CD1 LEU A 869      85.812  69.357 108.039  1.00 19.43           C  
ATOM   6309  CD2 LEU A 869      86.240  69.145 105.600  1.00 19.43           C  
ATOM   6310  N   THR A 870      82.028  65.764 105.571  1.00 21.21           N  
ATOM   6311  CA  THR A 870      81.527  64.393 105.579  1.00 21.21           C  
ATOM   6312  C   THR A 870      81.633  63.719 104.220  1.00 21.21           C  
ATOM   6313  O   THR A 870      81.700  62.488 104.156  1.00 21.21           O  
ATOM   6314  CB  THR A 870      80.076  64.352 106.051  1.00 21.21           C  
ATOM   6315  OG1 THR A 870      79.296  65.291 105.303  1.00 21.21           O  
ATOM   6316  CG2 THR A 870      79.997  64.675 107.516  1.00 21.21           C  
ATOM   6317  N   LYS A 871      81.643  64.489 103.137  1.00 23.22           N  
ATOM   6318  CA  LYS A 871      81.761  63.930 101.799  1.00 23.22           C  
ATOM   6319  C   LYS A 871      83.202  63.617 101.423  1.00 23.22           C  
ATOM   6320  O   LYS A 871      83.435  62.986 100.387  1.00 23.22           O  
ATOM   6321  CB  LYS A 871      81.164  64.901 100.779  1.00 23.22           C  
ATOM   6322  CG  LYS A 871      79.648  64.928 100.759  1.00 23.22           C  
ATOM   6323  CD  LYS A 871      79.067  63.557 100.481  1.00 23.22           C  
ATOM   6324  CE  LYS A 871      77.550  63.609 100.437  1.00 23.22           C  
ATOM   6325  NZ  LYS A 871      77.017  64.721 101.270  1.00 23.22           N  
ATOM   6326  N   HIS A 872      84.161  64.038 102.240  1.00 25.91           N  
ATOM   6327  CA  HIS A 872      85.566  63.850 101.923  1.00 25.91           C  
ATOM   6328  C   HIS A 872      85.955  62.382 102.086  1.00 25.91           C  
ATOM   6329  O   HIS A 872      85.550  61.737 103.058  1.00 25.91           O  
ATOM   6330  CB  HIS A 872      86.415  64.741 102.830  1.00 25.91           C  
ATOM   6331  CG  HIS A 872      87.774  65.055 102.289  1.00 25.91           C  
ATOM   6332  ND1 HIS A 872      88.585  64.109 101.703  1.00 25.91           N  
ATOM   6333  CD2 HIS A 872      88.447  66.226 102.210  1.00 25.91           C  
ATOM   6334  CE1 HIS A 872      89.711  64.677 101.312  1.00 25.91           C  
ATOM   6335  NE2 HIS A 872      89.652  65.963 101.607  1.00 25.91           N  
ATOM   6336  N   PRO A 873      86.719  61.822 101.145  1.00 32.98           N  
ATOM   6337  CA  PRO A 873      87.190  60.438 101.306  1.00 32.98           C  
ATOM   6338  C   PRO A 873      87.993  60.203 102.571  1.00 32.98           C  
ATOM   6339  O   PRO A 873      87.967  59.090 103.111  1.00 32.98           O  
ATOM   6340  CB  PRO A 873      88.045  60.223 100.051  1.00 32.98           C  
ATOM   6341  CG  PRO A 873      87.404  61.090  99.034  1.00 32.98           C  
ATOM   6342  CD  PRO A 873      86.972  62.324  99.783  1.00 32.98           C  
ATOM   6343  N   ASN A 874      88.706  61.210 103.064  1.00 35.24           N  
ATOM   6344  CA  ASN A 874      89.519  61.059 104.266  1.00 35.24           C  
ATOM   6345  C   ASN A 874      88.599  61.026 105.479  1.00 35.24           C  
ATOM   6346  O   ASN A 874      88.025  62.051 105.859  1.00 35.24           O  
ATOM   6347  CB  ASN A 874      90.530  62.196 104.368  1.00 35.24           C  
ATOM   6348  CG  ASN A 874      91.734  61.831 105.207  1.00 35.24           C  
ATOM   6349  OD1 ASN A 874      91.987  60.656 105.470  1.00 35.24           O  
ATOM   6350  ND2 ASN A 874      92.487  62.837 105.630  1.00 35.24           N  
ATOM   6351  N   GLN A 875      88.463  59.849 106.094  1.00 38.07           N  
ATOM   6352  CA  GLN A 875      87.574  59.701 107.239  1.00 38.07           C  
ATOM   6353  C   GLN A 875      88.008  60.563 108.415  1.00 38.07           C  
ATOM   6354  O   GLN A 875      87.166  60.953 109.229  1.00 38.07           O  
ATOM   6355  CB  GLN A 875      87.501  58.231 107.658  1.00 38.07           C  
ATOM   6356  CG  GLN A 875      86.540  57.941 108.803  1.00 38.07           C  
ATOM   6357  CD  GLN A 875      85.093  58.236 108.452  1.00 38.07           C  
ATOM   6358  OE1 GLN A 875      84.691  58.130 107.293  1.00 38.07           O  
ATOM   6359  NE2 GLN A 875      84.306  58.624 109.450  1.00 38.07           N  
ATOM   6360  N   GLU A 876      89.300  60.881 108.516  1.00 41.06           N  
ATOM   6361  CA  GLU A 876      89.746  61.804 109.551  1.00 41.06           C  
ATOM   6362  C   GLU A 876      89.146  63.189 109.354  1.00 41.06           C  
ATOM   6363  O   GLU A 876      88.933  63.917 110.328  1.00 41.06           O  
ATOM   6364  CB  GLU A 876      91.271  61.880 109.567  1.00 41.06           C  
ATOM   6365  CG  GLU A 876      91.929  60.845 110.463  1.00 41.06           C  
ATOM   6366  CD  GLU A 876      93.351  60.531 110.044  1.00 41.06           C  
ATOM   6367  OE1 GLU A 876      93.823  61.118 109.048  1.00 41.06           O  
ATOM   6368  OE2 GLU A 876      93.997  59.695 110.710  1.00 41.06           O  
ATOM   6369  N   TYR A 877      88.871  63.570 108.105  1.00 33.30           N  
ATOM   6370  CA  TYR A 877      88.194  64.834 107.838  1.00 33.30           C  
ATOM   6371  C   TYR A 877      86.701  64.731 108.127  1.00 33.30           C  
ATOM   6372  O   TYR A 877      86.100  65.666 108.663  1.00 33.30           O  
ATOM   6373  CB  TYR A 877      88.425  65.266 106.389  1.00 33.30           C  
ATOM   6374  CG  TYR A 877      89.794  65.849 106.108  1.00 33.30           C  
ATOM   6375  CD1 TYR A 877      90.812  65.776 107.045  1.00 33.30           C  
ATOM   6376  CD2 TYR A 877      90.062  66.482 104.905  1.00 33.30           C  
ATOM   6377  CE1 TYR A 877      92.061  66.310 106.787  1.00 33.30           C  
ATOM   6378  CE2 TYR A 877      91.305  67.018 104.637  1.00 33.30           C  
ATOM   6379  CZ  TYR A 877      92.301  66.930 105.580  1.00 33.30           C  
ATOM   6380  OH  TYR A 877      93.538  67.465 105.315  1.00 33.30           O  
ATOM   6381  N   ALA A 878      86.088  63.601 107.765  1.00 30.38           N  
ATOM   6382  CA  ALA A 878      84.646  63.443 107.934  1.00 30.38           C  
ATOM   6383  C   ALA A 878      84.239  63.512 109.399  1.00 30.38           C  
ATOM   6384  O   ALA A 878      83.182  64.059 109.730  1.00 30.38           O  
ATOM   6385  CB  ALA A 878      84.188  62.123 107.317  1.00 30.38           C  
ATOM   6386  N   ASP A 879      85.060  62.953 110.291  1.00 35.05           N  
ATOM   6387  CA  ASP A 879      84.711  62.907 111.707  1.00 35.05           C  
ATOM   6388  C   ASP A 879      84.676  64.283 112.357  1.00 35.05           C  
ATOM   6389  O   ASP A 879      84.167  64.407 113.475  1.00 35.05           O  
ATOM   6390  CB  ASP A 879      85.683  62.005 112.466  1.00 35.05           C  
ATOM   6391  CG  ASP A 879      85.394  60.533 112.257  1.00 35.05           C  
ATOM   6392  OD1 ASP A 879      84.380  60.043 112.797  1.00 35.05           O  
ATOM   6393  OD2 ASP A 879      86.175  59.864 111.552  1.00 35.05           O  
ATOM   6394  N   VAL A 880      85.208  65.313 111.696  1.00 28.16           N  
ATOM   6395  CA  VAL A 880      85.177  66.652 112.276  1.00 28.16           C  
ATOM   6396  C   VAL A 880      83.748  67.170 112.377  1.00 28.16           C  
ATOM   6397  O   VAL A 880      83.396  67.849 113.348  1.00 28.16           O  
ATOM   6398  CB  VAL A 880      86.069  67.606 111.462  1.00 28.16           C  
ATOM   6399  CG1 VAL A 880      86.133  68.969 112.129  1.00 28.16           C  
ATOM   6400  CG2 VAL A 880      87.462  67.023 111.316  1.00 28.16           C  
ATOM   6401  N   PHE A 881      82.901  66.858 111.394  1.00 26.02           N  
ATOM   6402  CA  PHE A 881      81.508  67.290 111.457  1.00 26.02           C  
ATOM   6403  C   PHE A 881      80.745  66.547 112.544  1.00 26.02           C  
ATOM   6404  O   PHE A 881      80.003  67.159 113.324  1.00 26.02           O  
ATOM   6405  CB  PHE A 881      80.832  67.070 110.109  1.00 26.02           C  
ATOM   6406  CG  PHE A 881      79.422  67.565 110.055  1.00 26.02           C  
ATOM   6407  CD1 PHE A 881      79.117  68.854 110.440  1.00 26.02           C  
ATOM   6408  CD2 PHE A 881      78.405  66.752 109.597  1.00 26.02           C  
ATOM   6409  CE1 PHE A 881      77.827  69.316 110.379  1.00 26.02           C  
ATOM   6410  CE2 PHE A 881      77.111  67.205 109.542  1.00 26.02           C  
ATOM   6411  CZ  PHE A 881      76.822  68.490 109.931  1.00 26.02           C  
ATOM   6412  N   HIS A 882      80.909  65.224 112.604  1.00 33.99           N  
ATOM   6413  CA  HIS A 882      80.186  64.429 113.588  1.00 33.99           C  
ATOM   6414  C   HIS A 882      80.568  64.818 115.006  1.00 33.99           C  
ATOM   6415  O   HIS A 882      79.730  64.758 115.910  1.00 33.99           O  
ATOM   6416  CB  HIS A 882      80.446  62.944 113.349  1.00 33.99           C  
ATOM   6417  CG  HIS A 882      79.856  62.430 112.074  1.00 33.99           C  
ATOM   6418  ND1 HIS A 882      78.526  62.594 111.751  1.00 33.99           N  
ATOM   6419  CD2 HIS A 882      80.417  61.767 111.036  1.00 33.99           C  
ATOM   6420  CE1 HIS A 882      78.291  62.047 110.572  1.00 33.99           C  
ATOM   6421  NE2 HIS A 882      79.422  61.539 110.116  1.00 33.99           N  
ATOM   6422  N   LEU A 883      81.821  65.225 115.219  1.00 29.18           N  
ATOM   6423  CA  LEU A 883      82.222  65.760 116.515  1.00 29.18           C  
ATOM   6424  C   LEU A 883      81.387  66.978 116.884  1.00 29.18           C  
ATOM   6425  O   LEU A 883      80.892  67.093 118.012  1.00 29.18           O  
ATOM   6426  CB  LEU A 883      83.707  66.117 116.486  1.00 29.18           C  
ATOM   6427  CG  LEU A 883      84.302  66.666 117.780  1.00 29.18           C  
ATOM   6428  CD1 LEU A 883      84.674  65.523 118.700  1.00 29.18           C  
ATOM   6429  CD2 LEU A 883      85.507  67.533 117.477  1.00 29.18           C  
ATOM   6430  N   TYR A 884      81.218  67.899 115.935  1.00 25.76           N  
ATOM   6431  CA  TYR A 884      80.455  69.112 116.201  1.00 25.76           C  
ATOM   6432  C   TYR A 884      78.989  68.798 116.466  1.00 25.76           C  
ATOM   6433  O   TYR A 884      78.377  69.388 117.362  1.00 25.76           O  
ATOM   6434  CB  TYR A 884      80.604  70.084 115.033  1.00 25.76           C  
ATOM   6435  CG  TYR A 884      81.822  70.966 115.152  1.00 25.76           C  
ATOM   6436  CD1 TYR A 884      83.077  70.499 114.802  1.00 25.76           C  
ATOM   6437  CD2 TYR A 884      81.719  72.261 115.625  1.00 25.76           C  
ATOM   6438  CE1 TYR A 884      84.192  71.297 114.915  1.00 25.76           C  
ATOM   6439  CE2 TYR A 884      82.830  73.065 115.741  1.00 25.76           C  
ATOM   6440  CZ  TYR A 884      84.063  72.579 115.386  1.00 25.76           C  
ATOM   6441  OH  TYR A 884      85.170  73.381 115.502  1.00 25.76           O  
ATOM   6442  N   LEU A 885      78.410  67.863 115.712  1.00 28.62           N  
ATOM   6443  CA  LEU A 885      77.021  67.490 115.970  1.00 28.62           C  
ATOM   6444  C   LEU A 885      76.861  66.803 117.319  1.00 28.62           C  
ATOM   6445  O   LEU A 885      75.887  67.058 118.032  1.00 28.62           O  
ATOM   6446  CB  LEU A 885      76.477  66.612 114.848  1.00 28.62           C  
ATOM   6447  CG  LEU A 885      75.642  67.410 113.851  1.00 28.62           C  
ATOM   6448  CD1 LEU A 885      76.425  68.596 113.356  1.00 28.62           C  
ATOM   6449  CD2 LEU A 885      75.197  66.534 112.696  1.00 28.62           C  
ATOM   6450  N   GLN A 886      77.795  65.925 117.686  1.00 34.14           N  
ATOM   6451  CA  GLN A 886      77.725  65.279 118.991  1.00 34.14           C  
ATOM   6452  C   GLN A 886      77.827  66.306 120.110  1.00 34.14           C  
ATOM   6453  O   GLN A 886      77.115  66.218 121.120  1.00 34.14           O  
ATOM   6454  CB  GLN A 886      78.836  64.240 119.110  1.00 34.14           C  
ATOM   6455  CG  GLN A 886      78.465  62.878 118.567  1.00 34.14           C  
ATOM   6456  CD  GLN A 886      79.637  61.924 118.566  1.00 34.14           C  
ATOM   6457  OE1 GLN A 886      79.871  61.210 119.539  1.00 34.14           O  
ATOM   6458  NE2 GLN A 886      80.386  61.911 117.473  1.00 34.14           N  
ATOM   6459  N   TYR A 887      78.703  67.297 119.943  1.00 33.72           N  
ATOM   6460  CA  TYR A 887      78.834  68.336 120.955  1.00 33.72           C  
ATOM   6461  C   TYR A 887      77.575  69.192 121.023  1.00 33.72           C  
ATOM   6462  O   TYR A 887      77.186  69.647 122.103  1.00 33.72           O  
ATOM   6463  CB  TYR A 887      80.065  69.190 120.665  1.00 33.72           C  
ATOM   6464  CG  TYR A 887      80.485  70.070 121.812  1.00 33.72           C  
ATOM   6465  CD1 TYR A 887      80.842  69.518 123.033  1.00 33.72           C  
ATOM   6466  CD2 TYR A 887      80.548  71.445 121.675  1.00 33.72           C  
ATOM   6467  CE1 TYR A 887      81.235  70.309 124.086  1.00 33.72           C  
ATOM   6468  CE2 TYR A 887      80.942  72.244 122.724  1.00 33.72           C  
ATOM   6469  CZ  TYR A 887      81.285  71.673 123.927  1.00 33.72           C  
ATOM   6470  OH  TYR A 887      81.676  72.469 124.977  1.00 33.72           O  
ATOM   6471  N   ILE A 888      76.928  69.426 119.878  1.00 31.98           N  
ATOM   6472  CA  ILE A 888      75.659  70.153 119.877  1.00 31.98           C  
ATOM   6473  C   ILE A 888      74.580  69.352 120.598  1.00 31.98           C  
ATOM   6474  O   ILE A 888      73.762  69.916 121.331  1.00 31.98           O  
ATOM   6475  CB  ILE A 888      75.241  70.516 118.441  1.00 31.98           C  
ATOM   6476  CG1 ILE A 888      76.133  71.629 117.893  1.00 31.98           C  
ATOM   6477  CG2 ILE A 888      73.787  70.953 118.396  1.00 31.98           C  
ATOM   6478  CD1 ILE A 888      76.052  71.793 116.397  1.00 31.98           C  
ATOM   6479  N   ARG A 889      74.556  68.031 120.403  1.00 40.45           N  
ATOM   6480  CA  ARG A 889      73.655  67.187 121.190  1.00 40.45           C  
ATOM   6481  C   ARG A 889      73.922  67.342 122.680  1.00 40.45           C  
ATOM   6482  O   ARG A 889      72.990  67.490 123.476  1.00 40.45           O  
ATOM   6483  CB  ARG A 889      73.782  65.710 120.792  1.00 40.45           C  
ATOM   6484  CG  ARG A 889      73.773  65.366 119.308  1.00 40.45           C  
ATOM   6485  CD  ARG A 889      72.777  66.190 118.509  1.00 40.45           C  
ATOM   6486  NE  ARG A 889      71.461  66.176 119.143  1.00 40.45           N  
ATOM   6487  CZ  ARG A 889      70.401  65.540 118.655  1.00 40.45           C  
ATOM   6488  NH1 ARG A 889      70.496  64.859 117.521  1.00 40.45           N  
ATOM   6489  NH2 ARG A 889      69.246  65.583 119.304  1.00 40.45           N  
ATOM   6490  N   LYS A 890      75.195  67.300 123.075  1.00 39.59           N  
ATOM   6491  CA  LYS A 890      75.534  67.431 124.490  1.00 39.59           C  
ATOM   6492  C   LYS A 890      75.073  68.774 125.047  1.00 39.59           C  
ATOM   6493  O   LYS A 890      74.478  68.842 126.130  1.00 39.59           O  
ATOM   6494  CB  LYS A 890      77.040  67.253 124.685  1.00 39.59           C  
ATOM   6495  CG  LYS A 890      77.478  67.271 126.136  1.00 39.59           C  
ATOM   6496  CD  LYS A 890      78.985  67.395 126.257  1.00 39.59           C  
ATOM   6497  CE  LYS A 890      79.651  66.032 126.254  1.00 39.59           C  
ATOM   6498  NZ  LYS A 890      79.944  65.550 127.632  1.00 39.59           N  
ATOM   6499  N   LEU A 891      75.333  69.857 124.312  1.00 40.27           N  
ATOM   6500  CA  LEU A 891      74.946  71.188 124.771  1.00 40.27           C  
ATOM   6501  C   LEU A 891      73.432  71.343 124.837  1.00 40.27           C  
ATOM   6502  O   LEU A 891      72.904  71.930 125.788  1.00 40.27           O  
ATOM   6503  CB  LEU A 891      75.551  72.253 123.858  1.00 40.27           C  
ATOM   6504  CG  LEU A 891      76.831  72.930 124.346  1.00 40.27           C  
ATOM   6505  CD1 LEU A 891      77.944  71.920 124.471  1.00 40.27           C  
ATOM   6506  CD2 LEU A 891      77.224  74.039 123.392  1.00 40.27           C  
ATOM   6507  N   HIS A 892      72.719  70.834 123.832  1.00 48.26           N  
ATOM   6508  CA  HIS A 892      71.264  70.914 123.831  1.00 48.26           C  
ATOM   6509  C   HIS A 892      70.665  70.095 124.963  1.00 48.26           C  
ATOM   6510  O   HIS A 892      69.645  70.489 125.540  1.00 48.26           O  
ATOM   6511  CB  HIS A 892      70.725  70.443 122.480  1.00 48.26           C  
ATOM   6512  CG  HIS A 892      69.281  70.759 122.259  1.00 48.26           C  
ATOM   6513  ND1 HIS A 892      68.838  72.023 121.931  1.00 48.26           N  
ATOM   6514  CD2 HIS A 892      68.178  69.975 122.310  1.00 48.26           C  
ATOM   6515  CE1 HIS A 892      67.524  72.004 121.794  1.00 48.26           C  
ATOM   6516  NE2 HIS A 892      67.099  70.774 122.019  1.00 48.26           N  
ATOM   6517  N   ASP A 893      71.277  68.955 125.289  1.00 51.92           N  
ATOM   6518  CA  ASP A 893      70.827  68.174 126.435  1.00 51.92           C  
ATOM   6519  C   ASP A 893      71.080  68.919 127.738  1.00 51.92           C  
ATOM   6520  O   ASP A 893      70.239  68.897 128.644  1.00 51.92           O  
ATOM   6521  CB  ASP A 893      71.527  66.816 126.447  1.00 51.92           C  
ATOM   6522  CG  ASP A 893      70.652  65.715 127.009  1.00 51.92           C  
ATOM   6523  OD1 ASP A 893      69.514  66.013 127.428  1.00 51.92           O  
ATOM   6524  OD2 ASP A 893      71.102  64.551 127.031  1.00 51.92           O  
ATOM   6525  N   GLU A 894      72.234  69.582 127.852  1.00 52.73           N  
ATOM   6526  CA  GLU A 894      72.516  70.360 129.053  1.00 52.73           C  
ATOM   6527  C   GLU A 894      71.509  71.490 129.218  1.00 52.73           C  
ATOM   6528  O   GLU A 894      71.088  71.785 130.342  1.00 52.73           O  
ATOM   6529  CB  GLU A 894      73.969  70.865 129.002  1.00 52.73           C  
ATOM   6530  CG  GLU A 894      74.516  71.692 130.197  1.00 52.73           C  
ATOM   6531  CD  GLU A 894      73.863  73.051 130.425  1.00 52.73           C  
ATOM   6532  OE1 GLU A 894      73.249  73.601 129.489  1.00 52.73           O  
ATOM   6533  OE2 GLU A 894      73.969  73.574 131.555  1.00 52.73           O  
ATOM   6534  N   LEU A 895      71.109  72.127 128.122  1.00 52.52           N  
ATOM   6535  CA  LEU A 895      70.079  73.159 128.168  1.00 52.52           C  
ATOM   6536  C   LEU A 895      68.689  72.542 128.047  1.00 52.52           C  
ATOM   6537  O   LEU A 895      67.696  73.140 128.459  1.00 52.52           O  
ATOM   6538  CB  LEU A 895      70.292  74.194 127.060  1.00 52.52           C  
ATOM   6539  CG  LEU A 895      71.510  75.112 127.176  1.00 52.52           C  
ATOM   6540  CD1 LEU A 895      71.669  75.954 125.922  1.00 52.52           C  
ATOM   6541  CD2 LEU A 895      71.383  76.002 128.400  1.00 52.52           C  
ATOM   6542  N   ASN A 911      61.144  69.279 110.596  1.00 63.68           N  
ATOM   6543  CA  ASN A 911      62.410  68.857 111.184  1.00 63.68           C  
ATOM   6544  C   ASN A 911      63.593  69.514 110.480  1.00 63.68           C  
ATOM   6545  O   ASN A 911      64.732  69.417 110.938  1.00 63.68           O  
ATOM   6546  CB  ASN A 911      62.537  67.330 111.137  1.00 63.68           C  
ATOM   6547  CG  ASN A 911      62.580  66.786 109.719  1.00 63.68           C  
ATOM   6548  OD1 ASN A 911      63.530  67.024 108.973  1.00 63.68           O  
ATOM   6549  ND2 ASN A 911      61.542  66.049 109.340  1.00 63.68           N  
ATOM   6550  N   THR A 912      63.314  70.181 109.359  1.00 60.10           N  
ATOM   6551  CA  THR A 912      64.364  70.842 108.594  1.00 60.10           C  
ATOM   6552  C   THR A 912      64.937  72.054 109.321  1.00 60.10           C  
ATOM   6553  O   THR A 912      66.012  72.535 108.946  1.00 60.10           O  
ATOM   6554  CB  THR A 912      63.815  71.246 107.219  1.00 60.10           C  
ATOM   6555  OG1 THR A 912      63.133  70.129 106.635  1.00 60.10           O  
ATOM   6556  CG2 THR A 912      64.940  71.660 106.274  1.00 60.10           C  
ATOM   6557  N   SER A 913      64.267  72.538 110.365  1.00 52.40           N  
ATOM   6558  CA  SER A 913      64.753  73.652 111.165  1.00 52.40           C  
ATOM   6559  C   SER A 913      65.365  73.208 112.486  1.00 52.40           C  
ATOM   6560  O   SER A 913      65.784  74.059 113.277  1.00 52.40           O  
ATOM   6561  CB  SER A 913      63.619  74.647 111.429  1.00 52.40           C  
ATOM   6562  OG  SER A 913      63.013  75.060 110.216  1.00 52.40           O  
ATOM   6563  N   ARG A 914      65.421  71.903 112.745  1.00 49.76           N  
ATOM   6564  CA  ARG A 914      65.971  71.366 113.989  1.00 49.76           C  
ATOM   6565  C   ARG A 914      67.448  71.075 113.769  1.00 49.76           C  
ATOM   6566  O   ARG A 914      67.831  70.026 113.252  1.00 49.76           O  
ATOM   6567  CB  ARG A 914      65.202  70.127 114.428  1.00 49.76           C  
ATOM   6568  CG  ARG A 914      63.764  70.421 114.817  1.00 49.76           C  
ATOM   6569  CD  ARG A 914      62.902  69.164 114.800  1.00 49.76           C  
ATOM   6570  NE  ARG A 914      61.786  69.188 115.751  1.00 49.76           N  
ATOM   6571  CZ  ARG A 914      60.886  70.164 115.883  1.00 49.76           C  
ATOM   6572  NH1 ARG A 914      60.900  71.234 115.097  1.00 49.76           N  
ATOM   6573  NH2 ARG A 914      59.933  70.048 116.798  1.00 49.76           N  
ATOM   6574  N   TYR A 915      68.287  72.020 114.179  1.00 41.76           N  
ATOM   6575  CA  TYR A 915      69.728  72.051 113.944  1.00 41.76           C  
ATOM   6576  C   TYR A 915      70.511  70.991 114.710  1.00 41.76           C  
ATOM   6577  O   TYR A 915      71.744  71.008 114.602  1.00 41.76           O  
ATOM   6578  CB  TYR A 915      70.256  73.450 114.272  1.00 41.76           C  
ATOM   6579  CG  TYR A 915      69.890  73.957 115.649  1.00 41.76           C  
ATOM   6580  CD1 TYR A 915      70.451  73.411 116.794  1.00 41.76           C  
ATOM   6581  CD2 TYR A 915      68.976  74.991 115.798  1.00 41.76           C  
ATOM   6582  CE1 TYR A 915      70.113  73.880 118.046  1.00 41.76           C  
ATOM   6583  CE2 TYR A 915      68.633  75.466 117.044  1.00 41.76           C  
ATOM   6584  CZ  TYR A 915      69.202  74.908 118.165  1.00 41.76           C  
ATOM   6585  OH  TYR A 915      68.859  75.381 119.409  1.00 41.76           O  
ATOM   6586  N   TRP A 916      69.911  70.080 115.470  1.00 46.05           N  
ATOM   6587  CA  TRP A 916      70.671  69.002 116.083  1.00 46.05           C  
ATOM   6588  C   TRP A 916      70.765  67.761 115.204  1.00 46.05           C  
ATOM   6589  O   TRP A 916      71.493  66.827 115.556  1.00 46.05           O  
ATOM   6590  CB  TRP A 916      70.077  68.623 117.446  1.00 46.05           C  
ATOM   6591  CG  TRP A 916      68.580  68.601 117.511  1.00 46.05           C  
ATOM   6592  CD1 TRP A 916      67.770  67.509 117.397  1.00 46.05           C  
ATOM   6593  CD2 TRP A 916      67.715  69.714 117.768  1.00 46.05           C  
ATOM   6594  NE1 TRP A 916      66.455  67.877 117.537  1.00 46.05           N  
ATOM   6595  CE2 TRP A 916      66.394  69.225 117.767  1.00 46.05           C  
ATOM   6596  CE3 TRP A 916      67.928  71.078 117.985  1.00 46.05           C  
ATOM   6597  CZ2 TRP A 916      65.293  70.051 117.976  1.00 46.05           C  
ATOM   6598  CZ3 TRP A 916      66.833  71.896 118.191  1.00 46.05           C  
ATOM   6599  CH2 TRP A 916      65.533  71.380 118.185  1.00 46.05           C  
ATOM   6600  N   GLU A 917      70.058  67.730 114.076  1.00 45.20           N  
ATOM   6601  CA  GLU A 917      70.059  66.602 113.159  1.00 45.20           C  
ATOM   6602  C   GLU A 917      70.722  66.990 111.840  1.00 45.20           C  
ATOM   6603  O   GLU A 917      70.687  68.160 111.448  1.00 45.20           O  
ATOM   6604  CB  GLU A 917      68.630  66.111 112.897  1.00 45.20           C  
ATOM   6605  CG  GLU A 917      67.981  65.457 114.106  1.00 45.20           C  
ATOM   6606  CD  GLU A 917      66.493  65.722 114.184  1.00 45.20           C  
ATOM   6607  OE1 GLU A 917      66.092  66.900 114.080  1.00 45.20           O  
ATOM   6608  OE2 GLU A 917      65.724  64.753 114.354  1.00 45.20           O  
ATOM   6609  N   PRO A 918      71.338  66.032 111.138  1.00 38.13           N  
ATOM   6610  CA  PRO A 918      72.137  66.395 109.955  1.00 38.13           C  
ATOM   6611  C   PRO A 918      71.334  66.974 108.801  1.00 38.13           C  
ATOM   6612  O   PRO A 918      71.912  67.673 107.961  1.00 38.13           O  
ATOM   6613  CB  PRO A 918      72.806  65.069 109.562  1.00 38.13           C  
ATOM   6614  CG  PRO A 918      71.924  64.018 110.127  1.00 38.13           C  
ATOM   6615  CD  PRO A 918      71.382  64.587 111.406  1.00 38.13           C  
ATOM   6616  N   GLU A 919      70.030  66.704 108.715  1.00 37.64           N  
ATOM   6617  CA  GLU A 919      69.249  67.215 107.594  1.00 37.64           C  
ATOM   6618  C   GLU A 919      69.152  68.736 107.593  1.00 37.64           C  
ATOM   6619  O   GLU A 919      68.951  69.330 106.529  1.00 37.64           O  
ATOM   6620  CB  GLU A 919      67.848  66.599 107.594  1.00 37.64           C  
ATOM   6621  CG  GLU A 919      67.833  65.080 107.502  1.00 37.64           C  
ATOM   6622  CD  GLU A 919      67.970  64.408 108.852  1.00 37.64           C  
ATOM   6623  OE1 GLU A 919      67.367  64.904 109.826  1.00 37.64           O  
ATOM   6624  OE2 GLU A 919      68.684  63.386 108.938  1.00 37.64           O  
ATOM   6625  N   PHE A 920      69.286  69.376 108.757  1.00 31.80           N  
ATOM   6626  CA  PHE A 920      69.298  70.835 108.812  1.00 31.80           C  
ATOM   6627  C   PHE A 920      70.479  71.403 108.036  1.00 31.80           C  
ATOM   6628  O   PHE A 920      70.343  72.403 107.323  1.00 31.80           O  
ATOM   6629  CB  PHE A 920      69.319  71.285 110.278  1.00 31.80           C  
ATOM   6630  CG  PHE A 920      69.489  72.771 110.479  1.00 31.80           C  
ATOM   6631  CD1 PHE A 920      70.738  73.367 110.396  1.00 31.80           C  
ATOM   6632  CD2 PHE A 920      68.398  73.570 110.758  1.00 31.80           C  
ATOM   6633  CE1 PHE A 920      70.891  74.725 110.584  1.00 31.80           C  
ATOM   6634  CE2 PHE A 920      68.547  74.931 110.945  1.00 31.80           C  
ATOM   6635  CZ  PHE A 920      69.795  75.506 110.858  1.00 31.80           C  
ATOM   6636  N   TYR A 921      71.646  70.776 108.165  1.00 25.98           N  
ATOM   6637  CA  TYR A 921      72.856  71.254 107.507  1.00 25.98           C  
ATOM   6638  C   TYR A 921      72.895  70.875 106.032  1.00 25.98           C  
ATOM   6639  O   TYR A 921      73.394  71.647 105.207  1.00 25.98           O  
ATOM   6640  CB  TYR A 921      74.071  70.714 108.254  1.00 25.98           C  
ATOM   6641  CG  TYR A 921      74.053  71.101 109.711  1.00 25.98           C  
ATOM   6642  CD1 TYR A 921      74.054  72.435 110.088  1.00 25.98           C  
ATOM   6643  CD2 TYR A 921      73.957  70.144 110.706  1.00 25.98           C  
ATOM   6644  CE1 TYR A 921      74.021  72.803 111.414  1.00 25.98           C  
ATOM   6645  CE2 TYR A 921      73.912  70.505 112.035  1.00 25.98           C  
ATOM   6646  CZ  TYR A 921      73.947  71.835 112.385  1.00 25.98           C  
ATOM   6647  OH  TYR A 921      73.904  72.200 113.709  1.00 25.98           O  
ATOM   6648  N   GLU A 922      72.387  69.690 105.685  1.00 28.83           N  
ATOM   6649  CA  GLU A 922      72.364  69.271 104.287  1.00 28.83           C  
ATOM   6650  C   GLU A 922      71.565  70.244 103.429  1.00 28.83           C  
ATOM   6651  O   GLU A 922      71.920  70.500 102.273  1.00 28.83           O  
ATOM   6652  CB  GLU A 922      71.790  67.858 104.179  1.00 28.83           C  
ATOM   6653  CG  GLU A 922      71.961  67.204 102.817  1.00 28.83           C  
ATOM   6654  CD  GLU A 922      70.677  67.176 102.010  1.00 28.83           C  
ATOM   6655  OE1 GLU A 922      70.754  67.221 100.764  1.00 28.83           O  
ATOM   6656  OE2 GLU A 922      69.591  67.106 102.623  1.00 28.83           O  
ATOM   6657  N   ALA A 923      70.484  70.798 103.981  1.00 25.30           N  
ATOM   6658  CA  ALA A 923      69.636  71.719 103.234  1.00 25.30           C  
ATOM   6659  C   ALA A 923      70.341  73.023 102.884  1.00 25.30           C  
ATOM   6660  O   ALA A 923      69.886  73.732 101.980  1.00 25.30           O  
ATOM   6661  CB  ALA A 923      68.366  72.017 104.028  1.00 25.30           C  
ATOM   6662  N   MET A 924      71.430  73.361 103.575  1.00 19.15           N  
ATOM   6663  CA  MET A 924      72.137  74.608 103.309  1.00 19.15           C  
ATOM   6664  C   MET A 924      72.907  74.592 101.998  1.00 19.15           C  
ATOM   6665  O   MET A 924      73.276  75.660 101.503  1.00 19.15           O  
ATOM   6666  CB  MET A 924      73.103  74.927 104.450  1.00 19.15           C  
ATOM   6667  CG  MET A 924      72.440  75.301 105.756  1.00 19.15           C  
ATOM   6668  SD  MET A 924      71.521  76.837 105.606  1.00 19.15           S  
ATOM   6669  CE  MET A 924      72.864  78.012 105.508  1.00 19.15           C  
ATOM   6670  N   TYR A 925      73.163  73.417 101.428  1.00 18.63           N  
ATOM   6671  CA  TYR A 925      73.975  73.302 100.223  1.00 18.63           C  
ATOM   6672  C   TYR A 925      73.198  72.765  99.029  1.00 18.63           C  
ATOM   6673  O   TYR A 925      73.812  72.269  98.079  1.00 18.63           O  
ATOM   6674  CB  TYR A 925      75.201  72.430 100.504  1.00 18.63           C  
ATOM   6675  CG  TYR A 925      76.157  73.070 101.482  1.00 18.63           C  
ATOM   6676  CD1 TYR A 925      77.041  74.056 101.073  1.00 18.63           C  
ATOM   6677  CD2 TYR A 925      76.168  72.696 102.815  1.00 18.63           C  
ATOM   6678  CE1 TYR A 925      77.908  74.647 101.961  1.00 18.63           C  
ATOM   6679  CE2 TYR A 925      77.033  73.283 103.711  1.00 18.63           C  
ATOM   6680  CZ  TYR A 925      77.901  74.257 103.279  1.00 18.63           C  
ATOM   6681  OH  TYR A 925      78.766  74.844 104.171  1.00 18.63           O  
ATOM   6682  N   THR A 926      71.869  72.852  99.046  1.00 24.52           N  
ATOM   6683  CA  THR A 926      71.053  72.418  97.927  1.00 24.52           C  
ATOM   6684  C   THR A 926      70.372  73.617  97.277  1.00 24.52           C  
ATOM   6685  O   THR A 926      70.000  74.569  97.972  1.00 24.52           O  
ATOM   6686  CB  THR A 926      69.990  71.396  98.363  1.00 24.52           C  
ATOM   6687  OG1 THR A 926      68.867  72.080  98.933  1.00 24.52           O  
ATOM   6688  CG2 THR A 926      70.563  70.425  99.376  1.00 24.52           C  
ATOM   6689  N   PRO A 927      70.191  73.594  95.954  1.00 25.73           N  
ATOM   6690  CA  PRO A 927      69.806  74.817  95.231  1.00 25.73           C  
ATOM   6691  C   PRO A 927      68.546  75.506  95.731  1.00 25.73           C  
ATOM   6692  O   PRO A 927      68.482  76.741  95.706  1.00 25.73           O  
ATOM   6693  CB  PRO A 927      69.628  74.306  93.798  1.00 25.73           C  
ATOM   6694  CG  PRO A 927      70.651  73.244  93.682  1.00 25.73           C  
ATOM   6695  CD  PRO A 927      70.630  72.541  95.025  1.00 25.73           C  
ATOM   6696  N   HIS A 928      67.541  74.759  96.178  1.00 36.48           N  
ATOM   6697  CA  HIS A 928      66.265  75.364  96.556  1.00 36.48           C  
ATOM   6698  C   HIS A 928      66.446  76.096  97.879  1.00 36.48           C  
ATOM   6699  O   HIS A 928      66.436  75.486  98.950  1.00 36.48           O  
ATOM   6700  CB  HIS A 928      65.175  74.304  96.649  1.00 36.48           C  
ATOM   6701  CG  HIS A 928      63.816  74.802  96.266  1.00 36.48           C  
ATOM   6702  ND1 HIS A 928      63.246  75.920  96.836  1.00 36.48           N  
ATOM   6703  CD2 HIS A 928      62.915  74.334  95.371  1.00 36.48           C  
ATOM   6704  CE1 HIS A 928      62.052  76.120  96.308  1.00 36.48           C  
ATOM   6705  NE2 HIS A 928      61.826  75.171  95.416  1.00 36.48           N  
ATOM   6706  N   THR A 929      66.608  77.413  97.805  1.00 30.87           N  
ATOM   6707  CA  THR A 929      66.830  78.235  98.990  1.00 30.87           C  
ATOM   6708  C   THR A 929      65.521  78.586  99.683  1.00 30.87           C  
ATOM   6709  O   THR A 929      65.521  79.197 100.751  1.00 30.87           O  
ATOM   6710  CB  THR A 929      67.573  79.537  98.639  1.00 30.87           C  
ATOM   6711  OG1 THR A 929      67.797  80.299  99.832  1.00 30.87           O  
ATOM   6712  CG2 THR A 929      66.765  80.366  97.659  1.00 30.87           C  
TER    6713      THR A 929                                                      
ATOM   6714  N   ASP B  78      70.070 117.186 124.872  1.00 48.15           N  
ATOM   6715  CA  ASP B  78      70.192 116.709 123.500  1.00 48.15           C  
ATOM   6716  C   ASP B  78      71.636 116.358 123.163  1.00 48.15           C  
ATOM   6717  O   ASP B  78      72.558 117.109 123.478  1.00 48.15           O  
ATOM   6718  CB  ASP B  78      69.667 117.759 122.518  1.00 48.15           C  
ATOM   6719  N   LYS B  79      71.820 115.200 122.525  1.00 45.17           N  
ATOM   6720  CA  LYS B  79      73.150 114.798 122.078  1.00 45.17           C  
ATOM   6721  C   LYS B  79      73.724 115.799 121.082  1.00 45.17           C  
ATOM   6722  O   LYS B  79      74.941 116.001 121.024  1.00 45.17           O  
ATOM   6723  CB  LYS B  79      73.092 113.399 121.467  1.00 45.17           C  
ATOM   6724  N   ARG B  80      72.859 116.418 120.276  1.00 45.01           N  
ATOM   6725  CA  ARG B  80      73.291 117.428 119.314  1.00 45.01           C  
ATOM   6726  C   ARG B  80      74.050 118.559 120.000  1.00 45.01           C  
ATOM   6727  O   ARG B  80      75.191 118.876 119.638  1.00 45.01           O  
ATOM   6728  CB  ARG B  80      72.055 117.957 118.582  1.00 45.01           C  
ATOM   6729  CG  ARG B  80      72.206 119.256 117.814  1.00 45.01           C  
ATOM   6730  CD  ARG B  80      73.040 119.109 116.563  1.00 45.01           C  
ATOM   6731  NE  ARG B  80      73.159 120.387 115.868  1.00 45.01           N  
ATOM   6732  CZ  ARG B  80      73.095 120.527 114.548  1.00 45.01           C  
ATOM   6733  NH1 ARG B  80      72.915 119.466 113.776  1.00 45.01           N  
ATOM   6734  NH2 ARG B  80      73.208 121.728 114.000  1.00 45.01           N  
ATOM   6735  N   ALA B  81      73.444 119.150 121.033  1.00 48.15           N  
ATOM   6736  CA  ALA B  81      74.089 120.251 121.738  1.00 48.15           C  
ATOM   6737  C   ALA B  81      75.284 119.774 122.551  1.00 48.15           C  
ATOM   6738  O   ALA B  81      76.275 120.501 122.677  1.00 48.15           O  
ATOM   6739  CB  ALA B  81      73.081 120.960 122.640  1.00 48.15           C  
ATOM   6740  N   LYS B  82      75.212 118.562 123.104  1.00 48.61           N  
ATOM   6741  CA  LYS B  82      76.328 118.031 123.880  1.00 48.61           C  
ATOM   6742  C   LYS B  82      77.569 117.858 123.010  1.00 48.61           C  
ATOM   6743  O   LYS B  82      78.678 118.242 123.402  1.00 48.61           O  
ATOM   6744  CB  LYS B  82      75.924 116.703 124.521  1.00 48.61           C  
ATOM   6745  CG  LYS B  82      76.970 116.102 125.440  1.00 48.61           C  
ATOM   6746  CD  LYS B  82      76.415 114.892 126.173  1.00 48.61           C  
ATOM   6747  CE  LYS B  82      77.345 114.443 127.288  1.00 48.61           C  
ATOM   6748  NZ  LYS B  82      78.237 115.541 127.751  1.00 48.61           N  
ATOM   6749  N   VAL B  83      77.397 117.298 121.812  1.00 45.58           N  
ATOM   6750  CA  VAL B  83      78.538 117.120 120.923  1.00 45.58           C  
ATOM   6751  C   VAL B  83      78.996 118.456 120.344  1.00 45.58           C  
ATOM   6752  O   VAL B  83      80.197 118.654 120.124  1.00 45.58           O  
ATOM   6753  CB  VAL B  83      78.216 116.088 119.824  1.00 45.58           C  
ATOM   6754  CG1 VAL B  83      77.296 116.668 118.770  1.00 45.58           C  
ATOM   6755  CG2 VAL B  83      79.498 115.579 119.189  1.00 45.58           C  
ATOM   6756  N   THR B  84      78.076 119.400 120.111  1.00 46.57           N  
ATOM   6757  CA  THR B  84      78.499 120.738 119.710  1.00 46.57           C  
ATOM   6758  C   THR B  84      79.397 121.365 120.769  1.00 46.57           C  
ATOM   6759  O   THR B  84      80.462 121.917 120.453  1.00 46.57           O  
ATOM   6760  CB  THR B  84      77.274 121.618 119.461  1.00 46.57           C  
ATOM   6761  OG1 THR B  84      76.460 121.028 118.440  1.00 46.57           O  
ATOM   6762  CG2 THR B  84      77.688 123.017 119.042  1.00 46.57           C  
ATOM   6763  N   SER B  85      78.999 121.251 122.037  1.00 46.38           N  
ATOM   6764  CA  SER B  85      79.795 121.804 123.124  1.00 46.38           C  
ATOM   6765  C   SER B  85      81.138 121.099 123.236  1.00 46.38           C  
ATOM   6766  O   SER B  85      82.165 121.750 123.444  1.00 46.38           O  
ATOM   6767  CB  SER B  85      79.026 121.706 124.439  1.00 46.38           C  
ATOM   6768  OG  SER B  85      79.034 120.379 124.934  1.00 46.38           O  
ATOM   6769  N   ALA B  86      81.154 119.772 123.099  1.00 46.62           N  
ATOM   6770  CA  ALA B  86      82.413 119.038 123.199  1.00 46.62           C  
ATOM   6771  C   ALA B  86      83.380 119.439 122.088  1.00 46.62           C  
ATOM   6772  O   ALA B  86      84.563 119.700 122.346  1.00 46.62           O  
ATOM   6773  CB  ALA B  86      82.148 117.534 123.165  1.00 46.62           C  
ATOM   6774  N   MET B  87      82.895 119.496 120.845  1.00 47.61           N  
ATOM   6775  CA  MET B  87      83.761 119.867 119.731  1.00 47.61           C  
ATOM   6776  C   MET B  87      84.292 121.285 119.892  1.00 47.61           C  
ATOM   6777  O   MET B  87      85.484 121.540 119.678  1.00 47.61           O  
ATOM   6778  CB  MET B  87      83.020 119.718 118.403  1.00 47.61           C  
ATOM   6779  CG  MET B  87      83.138 118.336 117.785  1.00 47.61           C  
ATOM   6780  SD  MET B  87      82.159 118.121 116.289  1.00 47.61           S  
ATOM   6781  CE  MET B  87      80.554 118.658 116.858  1.00 47.61           C  
ATOM   6782  N   GLN B  88      83.424 122.230 120.271  1.00 51.40           N  
ATOM   6783  CA  GLN B  88      83.885 123.609 120.396  1.00 51.40           C  
ATOM   6784  C   GLN B  88      84.839 123.771 121.575  1.00 51.40           C  
ATOM   6785  O   GLN B  88      85.811 124.533 121.494  1.00 51.40           O  
ATOM   6786  CB  GLN B  88      82.693 124.556 120.518  1.00 51.40           C  
ATOM   6787  CG  GLN B  88      83.083 126.021 120.576  1.00 51.40           C  
ATOM   6788  CD  GLN B  88      81.917 126.943 120.300  1.00 51.40           C  
ATOM   6789  OE1 GLN B  88      80.915 126.536 119.713  1.00 51.40           O  
ATOM   6790  NE2 GLN B  88      82.043 128.198 120.715  1.00 51.40           N  
ATOM   6791  N   THR B  89      84.588 123.058 122.676  1.00 50.03           N  
ATOM   6792  CA  THR B  89      85.500 123.090 123.812  1.00 50.03           C  
ATOM   6793  C   THR B  89      86.873 122.564 123.421  1.00 50.03           C  
ATOM   6794  O   THR B  89      87.899 123.161 123.766  1.00 50.03           O  
ATOM   6795  CB  THR B  89      84.922 122.277 124.972  1.00 50.03           C  
ATOM   6796  OG1 THR B  89      83.769 122.944 125.498  1.00 50.03           O  
ATOM   6797  CG2 THR B  89      85.954 122.112 126.080  1.00 50.03           C  
ATOM   6798  N   MET B  90      86.915 121.443 122.695  1.00 48.89           N  
ATOM   6799  CA  MET B  90      88.201 120.902 122.265  1.00 48.89           C  
ATOM   6800  C   MET B  90      88.916 121.872 121.333  1.00 48.89           C  
ATOM   6801  O   MET B  90      90.122 122.102 121.466  1.00 48.89           O  
ATOM   6802  CB  MET B  90      88.011 119.549 121.581  1.00 48.89           C  
ATOM   6803  CG  MET B  90      89.320 118.907 121.134  1.00 48.89           C  
ATOM   6804  SD  MET B  90      89.148 117.757 119.758  1.00 48.89           S  
ATOM   6805  CE  MET B  90      88.145 118.725 118.636  1.00 48.89           C  
ATOM   6806  N   LEU B  91      88.184 122.451 120.377  1.00 48.40           N  
ATOM   6807  CA  LEU B  91      88.810 123.363 119.424  1.00 48.40           C  
ATOM   6808  C   LEU B  91      89.365 124.603 120.113  1.00 48.40           C  
ATOM   6809  O   LEU B  91      90.443 125.090 119.752  1.00 48.40           O  
ATOM   6810  CB  LEU B  91      87.815 123.751 118.331  1.00 48.40           C  
ATOM   6811  CG  LEU B  91      87.608 122.702 117.236  1.00 48.40           C  
ATOM   6812  CD1 LEU B  91      86.234 122.826 116.612  1.00 48.40           C  
ATOM   6813  CD2 LEU B  91      88.683 122.829 116.178  1.00 48.40           C  
ATOM   6814  N   PHE B  92      88.646 125.138 121.103  1.00 56.36           N  
ATOM   6815  CA  PHE B  92      89.148 126.314 121.807  1.00 56.36           C  
ATOM   6816  C   PHE B  92      90.227 125.967 122.826  1.00 56.36           C  
ATOM   6817  O   PHE B  92      91.090 126.805 123.112  1.00 56.36           O  
ATOM   6818  CB  PHE B  92      87.998 127.056 122.490  1.00 56.36           C  
ATOM   6819  CG  PHE B  92      87.305 128.051 121.600  1.00 56.36           C  
ATOM   6820  CD1 PHE B  92      86.693 127.645 120.426  1.00 56.36           C  
ATOM   6821  CD2 PHE B  92      87.273 129.393 121.935  1.00 56.36           C  
ATOM   6822  CE1 PHE B  92      86.058 128.559 119.606  1.00 56.36           C  
ATOM   6823  CE2 PHE B  92      86.640 130.311 121.119  1.00 56.36           C  
ATOM   6824  CZ  PHE B  92      86.032 129.893 119.953  1.00 56.36           C  
ATOM   6825  N   THR B  93      90.199 124.755 123.383  1.00 56.24           N  
ATOM   6826  CA  THR B  93      91.219 124.362 124.352  1.00 56.24           C  
ATOM   6827  C   THR B  93      92.581 124.200 123.687  1.00 56.24           C  
ATOM   6828  O   THR B  93      93.613 124.527 124.282  1.00 56.24           O  
ATOM   6829  CB  THR B  93      90.804 123.067 125.052  1.00 56.24           C  
ATOM   6830  OG1 THR B  93      89.672 123.322 125.893  1.00 56.24           O  
ATOM   6831  CG2 THR B  93      91.938 122.519 125.904  1.00 56.24           C  
ATOM   6832  N   MET B  94      92.602 123.703 122.450  1.00 52.77           N  
ATOM   6833  CA  MET B  94      93.861 123.487 121.745  1.00 52.77           C  
ATOM   6834  C   MET B  94      94.577 124.786 121.395  1.00 52.77           C  
ATOM   6835  O   MET B  94      95.740 124.742 120.982  1.00 52.77           O  
ATOM   6836  CB  MET B  94      93.606 122.651 120.491  1.00 52.77           C  
ATOM   6837  CG  MET B  94      93.214 121.214 120.810  1.00 52.77           C  
ATOM   6838  SD  MET B  94      93.044 120.157 119.363  1.00 52.77           S  
ATOM   6839  CE  MET B  94      92.179 121.266 118.267  1.00 52.77           C  
ATOM   6840  N   LEU B  95      93.919 125.935 121.538  1.00 56.44           N  
ATOM   6841  CA  LEU B  95      94.538 127.215 121.207  1.00 56.44           C  
ATOM   6842  C   LEU B  95      95.436 127.770 122.306  1.00 56.44           C  
ATOM   6843  O   LEU B  95      96.047 128.824 122.097  1.00 56.44           O  
ATOM   6844  CB  LEU B  95      93.471 128.257 120.863  1.00 56.44           C  
ATOM   6845  CG  LEU B  95      93.014 128.365 119.408  1.00 56.44           C  
ATOM   6846  CD1 LEU B  95      92.802 127.013 118.767  1.00 56.44           C  
ATOM   6847  CD2 LEU B  95      91.748 129.168 119.356  1.00 56.44           C  
ATOM   6848  N   ARG B  96      95.527 127.113 123.466  1.00 60.18           N  
ATOM   6849  CA  ARG B  96      96.474 127.568 124.480  1.00 60.18           C  
ATOM   6850  C   ARG B  96      97.904 127.523 123.961  1.00 60.18           C  
ATOM   6851  O   ARG B  96      98.749 128.312 124.398  1.00 60.18           O  
ATOM   6852  CB  ARG B  96      96.347 126.730 125.753  1.00 60.18           C  
ATOM   6853  CG  ARG B  96      94.922 126.501 126.227  1.00 60.18           C  
ATOM   6854  CD  ARG B  96      94.460 127.610 127.167  1.00 60.18           C  
ATOM   6855  NE  ARG B  96      93.005 127.699 127.294  1.00 60.18           N  
ATOM   6856  CZ  ARG B  96      92.210 126.734 127.753  1.00 60.18           C  
ATOM   6857  NH1 ARG B  96      90.902 126.936 127.816  1.00 60.18           N  
ATOM   6858  NH2 ARG B  96      92.711 125.579 128.170  1.00 60.18           N  
ATOM   6859  N   LYS B  97      98.193 126.610 123.035  1.00 56.46           N  
ATOM   6860  CA  LYS B  97      99.512 126.517 122.423  1.00 56.46           C  
ATOM   6861  C   LYS B  97      99.631 127.376 121.169  1.00 56.46           C  
ATOM   6862  O   LYS B  97     100.672 128.003 120.947  1.00 56.46           O  
ATOM   6863  CB  LYS B  97      99.833 125.058 122.087  1.00 56.46           C  
ATOM   6864  N   LEU B  98      98.586 127.421 120.346  1.00 54.42           N  
ATOM   6865  CA  LEU B  98      98.642 128.153 119.090  1.00 54.42           C  
ATOM   6866  C   LEU B  98      98.608 129.662 119.329  1.00 54.42           C  
ATOM   6867  O   LEU B  98      98.502 130.147 120.460  1.00 54.42           O  
ATOM   6868  CB  LEU B  98      97.496 127.743 118.165  1.00 54.42           C  
ATOM   6869  CG  LEU B  98      97.738 126.560 117.223  1.00 54.42           C  
ATOM   6870  CD1 LEU B  98      98.452 125.413 117.914  1.00 54.42           C  
ATOM   6871  CD2 LEU B  98      96.437 126.090 116.620  1.00 54.42           C  
ATOM   6872  N   ASP B  99      98.716 130.404 118.226  1.00 60.03           N  
ATOM   6873  CA  ASP B  99      98.824 131.862 118.210  1.00 60.03           C  
ATOM   6874  C   ASP B  99     100.064 132.357 118.948  1.00 60.03           C  
ATOM   6875  O   ASP B  99     100.171 133.546 119.263  1.00 60.03           O  
ATOM   6876  CB  ASP B  99      97.563 132.527 118.776  1.00 60.03           C  
ATOM   6877  CG  ASP B  99      97.386 133.955 118.288  1.00 60.03           C  
ATOM   6878  OD1 ASP B  99      97.518 134.189 117.068  1.00 60.03           O  
ATOM   6879  OD2 ASP B  99      97.124 134.846 119.123  1.00 60.03           O  
ATOM   6880  N   ASN B 100     101.007 131.461 119.227  1.00 59.50           N  
ATOM   6881  CA  ASN B 100     102.328 131.877 119.669  1.00 59.50           C  
ATOM   6882  C   ASN B 100     102.993 132.673 118.553  1.00 59.50           C  
ATOM   6883  O   ASN B 100     102.775 132.405 117.369  1.00 59.50           O  
ATOM   6884  CB  ASN B 100     103.164 130.651 120.046  1.00 59.50           C  
ATOM   6885  CG  ASN B 100     104.528 131.010 120.611  1.00 59.50           C  
ATOM   6886  OD1 ASN B 100     104.907 132.179 120.681  1.00 59.50           O  
ATOM   6887  ND2 ASN B 100     105.274 129.992 121.023  1.00 59.50           N  
ATOM   6888  N   ASP B 101     103.799 133.667 118.930  1.00 60.38           N  
ATOM   6889  CA  ASP B 101     104.373 134.558 117.927  1.00 60.38           C  
ATOM   6890  C   ASP B 101     105.307 133.849 116.952  1.00 60.38           C  
ATOM   6891  O   ASP B 101     105.593 134.405 115.887  1.00 60.38           O  
ATOM   6892  CB  ASP B 101     105.092 135.732 118.609  1.00 60.38           C  
ATOM   6893  CG  ASP B 101     106.406 135.334 119.277  1.00 60.38           C  
ATOM   6894  OD1 ASP B 101     106.780 134.141 119.275  1.00 60.38           O  
ATOM   6895  OD2 ASP B 101     107.083 136.242 119.804  1.00 60.38           O  
ATOM   6896  N   ALA B 102     105.786 132.649 117.287  1.00 55.45           N  
ATOM   6897  CA  ALA B 102     106.520 131.843 116.317  1.00 55.45           C  
ATOM   6898  C   ALA B 102     105.640 131.502 115.121  1.00 55.45           C  
ATOM   6899  O   ALA B 102     106.078 131.571 113.966  1.00 55.45           O  
ATOM   6900  CB  ALA B 102     107.044 130.571 116.984  1.00 55.45           C  
ATOM   6901  N   LEU B 103     104.385 131.129 115.388  1.00 52.73           N  
ATOM   6902  CA  LEU B 103     103.451 130.826 114.311  1.00 52.73           C  
ATOM   6903  C   LEU B 103     103.231 132.038 113.419  1.00 52.73           C  
ATOM   6904  O   LEU B 103     103.183 131.913 112.189  1.00 52.73           O  
ATOM   6905  CB  LEU B 103     102.122 130.345 114.891  1.00 52.73           C  
ATOM   6906  CG  LEU B 103     101.894 128.837 114.932  1.00 52.73           C  
ATOM   6907  CD1 LEU B 103     100.618 128.508 115.683  1.00 52.73           C  
ATOM   6908  CD2 LEU B 103     101.830 128.294 113.521  1.00 52.73           C  
ATOM   6909  N   ASN B 104     103.108 133.223 114.020  1.00 55.76           N  
ATOM   6910  CA  ASN B 104     102.928 134.428 113.222  1.00 55.76           C  
ATOM   6911  C   ASN B 104     104.177 134.754 112.417  1.00 55.76           C  
ATOM   6912  O   ASN B 104     104.069 135.160 111.256  1.00 55.76           O  
ATOM   6913  CB  ASN B 104     102.553 135.606 114.121  1.00 55.76           C  
ATOM   6914  CG  ASN B 104     101.109 135.555 114.574  1.00 55.76           C  
ATOM   6915  OD1 ASN B 104     100.189 135.630 113.760  1.00 55.76           O  
ATOM   6916  ND2 ASN B 104     100.901 135.432 115.880  1.00 55.76           N  
ATOM   6917  N   ASN B 105     105.362 134.557 113.000  1.00 57.36           N  
ATOM   6918  CA  ASN B 105     106.600 134.803 112.266  1.00 57.36           C  
ATOM   6919  C   ASN B 105     106.732 133.863 111.076  1.00 57.36           C  
ATOM   6920  O   ASN B 105     107.249 134.253 110.022  1.00 57.36           O  
ATOM   6921  CB  ASN B 105     107.804 134.657 113.196  1.00 57.36           C  
ATOM   6922  CG  ASN B 105     107.845 135.725 114.269  1.00 57.36           C  
ATOM   6923  OD1 ASN B 105     107.128 136.722 114.196  1.00 57.36           O  
ATOM   6924  ND2 ASN B 105     108.684 135.518 115.278  1.00 57.36           N  
ATOM   6925  N   ILE B 106     106.287 132.616 111.230  1.00 50.28           N  
ATOM   6926  CA  ILE B 106     106.323 131.679 110.110  1.00 50.28           C  
ATOM   6927  C   ILE B 106     105.306 132.073 109.046  1.00 50.28           C  
ATOM   6928  O   ILE B 106     105.619 132.115 107.851  1.00 50.28           O  
ATOM   6929  CB  ILE B 106     106.098 130.239 110.603  1.00 50.28           C  
ATOM   6930  CG1 ILE B 106     107.218 129.825 111.557  1.00 50.28           C  
ATOM   6931  CG2 ILE B 106     105.996 129.278 109.430  1.00 50.28           C  
ATOM   6932  CD1 ILE B 106     108.573 129.734 110.895  1.00 50.28           C  
ATOM   6933  N   ILE B 107     104.073 132.370 109.460  1.00 51.90           N  
ATOM   6934  CA  ILE B 107     102.994 132.534 108.491  1.00 51.90           C  
ATOM   6935  C   ILE B 107     103.085 133.869 107.755  1.00 51.90           C  
ATOM   6936  O   ILE B 107     102.740 133.949 106.569  1.00 51.90           O  
ATOM   6937  CB  ILE B 107     101.634 132.354 109.194  1.00 51.90           C  
ATOM   6938  CG1 ILE B 107     101.415 130.881 109.548  1.00 51.90           C  
ATOM   6939  CG2 ILE B 107     100.492 132.842 108.317  1.00 51.90           C  
ATOM   6940  CD1 ILE B 107     100.061 130.588 110.150  1.00 51.90           C  
ATOM   6941  N   ASN B 108     103.578 134.928 108.407  1.00 57.06           N  
ATOM   6942  CA  ASN B 108     103.428 136.260 107.828  1.00 57.06           C  
ATOM   6943  C   ASN B 108     104.396 136.501 106.675  1.00 57.06           C  
ATOM   6944  O   ASN B 108     104.044 137.180 105.703  1.00 57.06           O  
ATOM   6945  CB  ASN B 108     103.614 137.330 108.907  1.00 57.06           C  
ATOM   6946  CG  ASN B 108     105.061 137.502 109.319  1.00 57.06           C  
ATOM   6947  OD1 ASN B 108     105.736 136.542 109.679  1.00 57.06           O  
ATOM   6948  ND2 ASN B 108     105.543 138.739 109.277  1.00 57.06           N  
ATOM   6949  N   ASN B 109     105.611 135.960 106.752  1.00 58.50           N  
ATOM   6950  CA  ASN B 109     106.594 136.214 105.706  1.00 58.50           C  
ATOM   6951  C   ASN B 109     106.396 135.341 104.474  1.00 58.50           C  
ATOM   6952  O   ASN B 109     107.054 135.580 103.456  1.00 58.50           O  
ATOM   6953  CB  ASN B 109     108.016 136.074 106.278  1.00 58.50           C  
ATOM   6954  CG  ASN B 109     108.432 134.627 106.548  1.00 58.50           C  
ATOM   6955  OD1 ASN B 109     108.096 133.703 105.812  1.00 58.50           O  
ATOM   6956  ND2 ASN B 109     109.181 134.437 107.627  1.00 58.50           N  
ATOM   6957  N   ALA B 110     105.520 134.340 104.543  1.00 55.70           N  
ATOM   6958  CA  ALA B 110     105.162 133.573 103.358  1.00 55.70           C  
ATOM   6959  C   ALA B 110     104.530 134.488 102.316  1.00 55.70           C  
ATOM   6960  O   ALA B 110     103.754 135.388 102.649  1.00 55.70           O  
ATOM   6961  CB  ALA B 110     104.205 132.442 103.729  1.00 55.70           C  
ATOM   6962  N   ARG B 111     104.900 134.250 101.061  1.00 59.23           N  
ATOM   6963  CA  ARG B 111     104.424 135.078  99.924  1.00 59.23           C  
ATOM   6964  C   ARG B 111     102.908 135.221  99.931  1.00 59.23           C  
ATOM   6965  O   ARG B 111     102.415 136.305  99.571  1.00 59.23           O  
ATOM   6966  CB  ARG B 111     104.776 134.328  98.633  1.00 59.23           C  
ATOM   6967  CG  ARG B 111     106.268 134.266  98.344  1.00 59.23           C  
ATOM   6968  CD  ARG B 111     106.588 133.808  96.935  1.00 59.23           C  
ATOM   6969  NE  ARG B 111     106.131 132.450  96.683  1.00 59.23           N  
ATOM   6970  CZ  ARG B 111     106.829 131.357  96.969  1.00 59.23           C  
ATOM   6971  NH1 ARG B 111     106.329 130.164  96.702  1.00 59.23           N  
ATOM   6972  NH2 ARG B 111     108.022 131.460  97.528  1.00 59.23           N  
ATOM   6973  N   ASP B 112     102.203 134.176 100.333  1.00 45.85           N  
ATOM   6974  CA  ASP B 112     100.748 134.189 100.254  1.00 45.85           C  
ATOM   6975  C   ASP B 112     100.087 133.821 101.577  1.00 45.85           C  
ATOM   6976  O   ASP B 112      98.864 133.634 101.609  1.00 45.85           O  
ATOM   6977  CB  ASP B 112     100.259 133.249  99.145  1.00 45.85           C  
ATOM   6978  CG  ASP B 112     100.624 131.804  99.405  1.00 45.85           C  
ATOM   6979  OD1 ASP B 112     101.582 131.561 100.167  1.00 45.85           O  
ATOM   6980  OD2 ASP B 112      99.959 130.910  98.842  1.00 45.85           O  
ATOM   6981  N   GLY B 113     100.848 133.711 102.664  1.00 39.76           N  
ATOM   6982  CA  GLY B 113     100.279 133.378 103.952  1.00 39.76           C  
ATOM   6983  C   GLY B 113      99.878 131.934 104.122  1.00 39.76           C  
ATOM   6984  O   GLY B 113      99.282 131.589 105.145  1.00 39.76           O  
ATOM   6985  N   CYS B 114     100.196 131.076 103.158  1.00 30.64           N  
ATOM   6986  CA  CYS B 114      99.839 129.666 103.191  1.00 30.64           C  
ATOM   6987  C   CYS B 114     101.109 128.830 103.264  1.00 30.64           C  
ATOM   6988  O   CYS B 114     102.012 128.999 102.439  1.00 30.64           O  
ATOM   6989  CB  CYS B 114      99.018 129.296 101.956  1.00 30.64           C  
ATOM   6990  SG  CYS B 114      98.403 127.614 101.932  1.00 30.64           S  
ATOM   6991  N   VAL B 115     101.177 127.933 104.243  1.00 19.08           N  
ATOM   6992  CA  VAL B 115     102.385 127.144 104.477  1.00 19.08           C  
ATOM   6993  C   VAL B 115     102.030 125.664 104.580  1.00 19.08           C  
ATOM   6994  O   VAL B 115     100.885 125.324 104.906  1.00 19.08           O  
ATOM   6995  CB  VAL B 115     103.124 127.616 105.741  1.00 19.08           C  
ATOM   6996  CG1 VAL B 115     103.432 129.101 105.661  1.00 19.08           C  
ATOM   6997  CG2 VAL B 115     102.311 127.305 106.981  1.00 19.08           C  
ATOM   6998  N   PRO B 116     102.960 124.758 104.277  1.00 13.86           N  
ATOM   6999  CA  PRO B 116     102.703 123.331 104.504  1.00 13.86           C  
ATOM   7000  C   PRO B 116     102.507 123.021 105.982  1.00 13.86           C  
ATOM   7001  O   PRO B 116     103.135 123.624 106.852  1.00 13.86           O  
ATOM   7002  CB  PRO B 116     103.958 122.649 103.946  1.00 13.86           C  
ATOM   7003  CG  PRO B 116     104.571 123.644 103.035  1.00 13.86           C  
ATOM   7004  CD  PRO B 116     104.246 124.985 103.603  1.00 13.86           C  
ATOM   7005  N   LEU B 117     101.618 122.066 106.258  1.00 12.26           N  
ATOM   7006  CA  LEU B 117     101.343 121.681 107.638  1.00 12.26           C  
ATOM   7007  C   LEU B 117     102.536 120.979 108.277  1.00 12.26           C  
ATOM   7008  O   LEU B 117     102.763 121.104 109.484  1.00 12.26           O  
ATOM   7009  CB  LEU B 117     100.106 120.786 107.690  1.00 12.26           C  
ATOM   7010  CG  LEU B 117      99.629 120.298 109.059  1.00 12.26           C  
ATOM   7011  CD1 LEU B 117      99.439 121.457 110.015  1.00 12.26           C  
ATOM   7012  CD2 LEU B 117      98.345 119.520 108.912  1.00 12.26           C  
ATOM   7013  N   ASN B 118     103.304 120.226 107.484  1.00 14.35           N  
ATOM   7014  CA  ASN B 118     104.372 119.400 108.040  1.00 14.35           C  
ATOM   7015  C   ASN B 118     105.472 120.233 108.683  1.00 14.35           C  
ATOM   7016  O   ASN B 118     106.197 119.732 109.551  1.00 14.35           O  
ATOM   7017  CB  ASN B 118     104.970 118.503 106.956  1.00 14.35           C  
ATOM   7018  CG  ASN B 118     104.086 117.320 106.621  1.00 14.35           C  
ATOM   7019  OD1 ASN B 118     103.259 116.897 107.428  1.00 14.35           O  
ATOM   7020  ND2 ASN B 118     104.266 116.769 105.428  1.00 14.35           N  
ATOM   7021  N   ILE B 119     105.626 121.494 108.272  1.00 15.65           N  
ATOM   7022  CA  ILE B 119     106.701 122.325 108.804  1.00 15.65           C  
ATOM   7023  C   ILE B 119     106.306 123.096 110.054  1.00 15.65           C  
ATOM   7024  O   ILE B 119     107.177 123.715 110.683  1.00 15.65           O  
ATOM   7025  CB  ILE B 119     107.206 123.344 107.765  1.00 15.65           C  
ATOM   7026  CG1 ILE B 119     106.128 124.389 107.484  1.00 15.65           C  
ATOM   7027  CG2 ILE B 119     107.616 122.643 106.485  1.00 15.65           C  
ATOM   7028  CD1 ILE B 119     106.665 125.709 107.006  1.00 15.65           C  
ATOM   7029  N   ILE B 120     105.031 123.093 110.431  1.00 16.48           N  
ATOM   7030  CA  ILE B 120     104.567 123.917 111.545  1.00 16.48           C  
ATOM   7031  C   ILE B 120     105.141 123.388 112.859  1.00 16.48           C  
ATOM   7032  O   ILE B 120     105.812 124.152 113.569  1.00 16.48           O  
ATOM   7033  CB  ILE B 120     103.032 124.005 111.579  1.00 16.48           C  
ATOM   7034  CG1 ILE B 120     102.523 124.878 110.433  1.00 16.48           C  
ATOM   7035  CG2 ILE B 120     102.564 124.562 112.906  1.00 16.48           C  
ATOM   7036  CD1 ILE B 120     102.718 126.348 110.654  1.00 16.48           C  
ATOM   7037  N   PRO B 121     104.924 122.120 113.243  1.00 16.11           N  
ATOM   7038  CA  PRO B 121     105.607 121.635 114.453  1.00 16.11           C  
ATOM   7039  C   PRO B 121     107.113 121.643 114.305  1.00 16.11           C  
ATOM   7040  O   PRO B 121     107.835 121.836 115.289  1.00 16.11           O  
ATOM   7041  CB  PRO B 121     105.060 120.211 114.631  1.00 16.11           C  
ATOM   7042  CG  PRO B 121     104.582 119.812 113.302  1.00 16.11           C  
ATOM   7043  CD  PRO B 121     104.120 121.052 112.618  1.00 16.11           C  
ATOM   7044  N   LEU B 122     107.606 121.427 113.088  1.00 16.88           N  
ATOM   7045  CA  LEU B 122     109.042 121.330 112.858  1.00 16.88           C  
ATOM   7046  C   LEU B 122     109.745 122.641 113.191  1.00 16.88           C  
ATOM   7047  O   LEU B 122     110.834 122.644 113.773  1.00 16.88           O  
ATOM   7048  CB  LEU B 122     109.288 120.916 111.408  1.00 16.88           C  
ATOM   7049  CG  LEU B 122     110.708 120.702 110.901  1.00 16.88           C  
ATOM   7050  CD1 LEU B 122     111.246 119.415 111.474  1.00 16.88           C  
ATOM   7051  CD2 LEU B 122     110.699 120.639 109.392  1.00 16.88           C  
ATOM   7052  N   THR B 123     109.141 123.769 112.820  1.00 20.13           N  
ATOM   7053  CA  THR B 123     109.751 125.072 113.043  1.00 20.13           C  
ATOM   7054  C   THR B 123     109.235 125.802 114.277  1.00 20.13           C  
ATOM   7055  O   THR B 123     109.848 126.796 114.678  1.00 20.13           O  
ATOM   7056  CB  THR B 123     109.544 125.978 111.824  1.00 20.13           C  
ATOM   7057  OG1 THR B 123     108.159 125.996 111.466  1.00 20.13           O  
ATOM   7058  CG2 THR B 123     110.366 125.489 110.649  1.00 20.13           C  
ATOM   7059  N   THR B 124     108.132 125.361 114.890  1.00 20.10           N  
ATOM   7060  CA  THR B 124     107.535 126.134 115.974  1.00 20.10           C  
ATOM   7061  C   THR B 124     107.302 125.376 117.275  1.00 20.10           C  
ATOM   7062  O   THR B 124     106.992 126.023 118.280  1.00 20.10           O  
ATOM   7063  CB  THR B 124     106.192 126.741 115.532  1.00 20.10           C  
ATOM   7064  OG1 THR B 124     105.159 125.754 115.635  1.00 20.10           O  
ATOM   7065  CG2 THR B 124     106.261 127.263 114.106  1.00 20.10           C  
ATOM   7066  N   ALA B 125     107.429 124.052 117.301  1.00 18.13           N  
ATOM   7067  CA  ALA B 125     107.173 123.316 118.533  1.00 18.13           C  
ATOM   7068  C   ALA B 125     108.231 123.626 119.582  1.00 18.13           C  
ATOM   7069  O   ALA B 125     109.424 123.706 119.283  1.00 18.13           O  
ATOM   7070  CB  ALA B 125     107.130 121.814 118.268  1.00 18.13           C  
ATOM   7071  N   ALA B 126     107.782 123.806 120.824  1.00 20.67           N  
ATOM   7072  CA  ALA B 126     108.692 124.049 121.933  1.00 20.67           C  
ATOM   7073  C   ALA B 126     109.299 122.772 122.494  1.00 20.67           C  
ATOM   7074  O   ALA B 126     110.341 122.837 123.153  1.00 20.67           O  
ATOM   7075  CB  ALA B 126     107.969 124.803 123.050  1.00 20.67           C  
ATOM   7076  N   LYS B 127     108.660 121.616 122.279  1.00 20.64           N  
ATOM   7077  CA  LYS B 127     109.154 120.343 122.871  1.00 20.64           C  
ATOM   7078  C   LYS B 127     109.391 119.302 121.772  1.00 20.64           C  
ATOM   7079  O   LYS B 127     108.586 119.258 120.826  1.00 20.64           O  
ATOM   7080  CB  LYS B 127     108.138 119.830 123.893  1.00 20.64           C  
ATOM   7081  CG  LYS B 127     108.485 118.510 124.566  1.00 20.64           C  
ATOM   7082  CD  LYS B 127     107.405 118.026 125.506  1.00 20.64           C  
ATOM   7083  CE  LYS B 127     107.075 119.032 126.587  1.00 20.64           C  
ATOM   7084  NZ  LYS B 127     105.986 118.550 127.468  1.00 20.64           N  
ATOM   7085  N   LEU B 128     110.439 118.482 121.911  1.00 19.72           N  
ATOM   7086  CA  LEU B 128     110.712 117.393 120.936  1.00 19.72           C  
ATOM   7087  C   LEU B 128     110.741 116.047 121.661  1.00 19.72           C  
ATOM   7088  O   LEU B 128     111.426 115.954 122.690  1.00 19.72           O  
ATOM   7089  CB  LEU B 128     112.048 117.656 120.238  1.00 19.72           C  
ATOM   7090  CG  LEU B 128     112.671 116.469 119.504  1.00 19.72           C  
ATOM   7091  CD1 LEU B 128     111.848 116.084 118.288  1.00 19.72           C  
ATOM   7092  CD2 LEU B 128     114.097 116.781 119.091  1.00 19.72           C  
ATOM   7093  N   MET B 129     110.038 115.046 121.135  1.00 23.82           N  
ATOM   7094  CA  MET B 129     110.041 113.697 121.683  1.00 23.82           C  
ATOM   7095  C   MET B 129     110.785 112.766 120.737  1.00 23.82           C  
ATOM   7096  O   MET B 129     110.429 112.659 119.560  1.00 23.82           O  
ATOM   7097  CB  MET B 129     108.616 113.191 121.909  1.00 23.82           C  
ATOM   7098  CG  MET B 129     107.957 113.730 123.165  1.00 23.82           C  
ATOM   7099  SD  MET B 129     106.340 112.999 123.479  1.00 23.82           S  
ATOM   7100  CE  MET B 129     106.523 111.399 122.694  1.00 23.82           C  
ATOM   7101  N   VAL B 130     111.807 112.091 121.253  1.00 22.80           N  
ATOM   7102  CA  VAL B 130     112.609 111.151 120.480  1.00 22.80           C  
ATOM   7103  C   VAL B 130     112.339 109.750 121.007  1.00 22.80           C  
ATOM   7104  O   VAL B 130     112.363 109.525 122.221  1.00 22.80           O  
ATOM   7105  CB  VAL B 130     114.108 111.487 120.557  1.00 22.80           C  
ATOM   7106  CG1 VAL B 130     114.900 110.571 119.647  1.00 22.80           C  
ATOM   7107  CG2 VAL B 130     114.350 112.939 120.200  1.00 22.80           C  
ATOM   7108  N   VAL B 131     112.079 108.813 120.100  1.00 22.77           N  
ATOM   7109  CA  VAL B 131     111.869 107.412 120.447  1.00 22.77           C  
ATOM   7110  C   VAL B 131     112.996 106.607 119.818  1.00 22.77           C  
ATOM   7111  O   VAL B 131     113.134 106.581 118.589  1.00 22.77           O  
ATOM   7112  CB  VAL B 131     110.498 106.905 119.976  1.00 22.77           C  
ATOM   7113  CG1 VAL B 131     110.370 105.423 120.245  1.00 22.77           C  
ATOM   7114  CG2 VAL B 131     109.388 107.673 120.665  1.00 22.77           C  
ATOM   7115  N   ILE B 132     113.790 105.946 120.652  1.00 29.55           N  
ATOM   7116  CA  ILE B 132     115.043 105.331 120.237  1.00 29.55           C  
ATOM   7117  C   ILE B 132     114.957 103.828 120.481  1.00 29.55           C  
ATOM   7118  O   ILE B 132     114.704 103.400 121.609  1.00 29.55           O  
ATOM   7119  CB  ILE B 132     116.243 105.941 120.980  1.00 29.55           C  
ATOM   7120  CG1 ILE B 132     116.661 107.243 120.301  1.00 29.55           C  
ATOM   7121  CG2 ILE B 132     117.404 104.971 121.016  1.00 29.55           C  
ATOM   7122  CD1 ILE B 132     117.354 108.202 121.213  1.00 29.55           C  
ATOM   7123  N   PRO B 133     115.153 102.985 119.456  1.00 32.47           N  
ATOM   7124  CA  PRO B 133     114.967 101.539 119.638  1.00 32.47           C  
ATOM   7125  C   PRO B 133     116.141 100.821 120.289  1.00 32.47           C  
ATOM   7126  O   PRO B 133     115.933  99.840 121.008  1.00 32.47           O  
ATOM   7127  CB  PRO B 133     114.747 101.042 118.203  1.00 32.47           C  
ATOM   7128  CG  PRO B 133     115.507 101.998 117.375  1.00 32.47           C  
ATOM   7129  CD  PRO B 133     115.312 103.335 118.038  1.00 32.47           C  
ATOM   7130  N   ASP B 134     117.368 101.280 120.053  1.00 42.57           N  
ATOM   7131  CA  ASP B 134     118.545 100.596 120.575  1.00 42.57           C  
ATOM   7132  C   ASP B 134     119.677 101.600 120.738  1.00 42.57           C  
ATOM   7133  O   ASP B 134     119.593 102.741 120.280  1.00 42.57           O  
ATOM   7134  CB  ASP B 134     118.949  99.419 119.677  1.00 42.57           C  
ATOM   7135  CG  ASP B 134     119.112  99.813 118.219  1.00 42.57           C  
ATOM   7136  OD1 ASP B 134     119.617 100.918 117.935  1.00 42.57           O  
ATOM   7137  OD2 ASP B 134     118.731  99.005 117.346  1.00 42.57           O  
ATOM   7138  N   TYR B 135     120.742 101.155 121.409  1.00 46.55           N  
ATOM   7139  CA  TYR B 135     121.804 102.070 121.816  1.00 46.55           C  
ATOM   7140  C   TYR B 135     122.585 102.612 120.625  1.00 46.55           C  
ATOM   7141  O   TYR B 135     123.129 103.722 120.696  1.00 46.55           O  
ATOM   7142  CB  TYR B 135     122.748 101.374 122.791  1.00 46.55           C  
ATOM   7143  CG  TYR B 135     123.670 102.326 123.514  1.00 46.55           C  
ATOM   7144  CD1 TYR B 135     124.896 102.679 122.978  1.00 46.55           C  
ATOM   7145  CD2 TYR B 135     123.303 102.889 124.723  1.00 46.55           C  
ATOM   7146  CE1 TYR B 135     125.738 103.542 123.631  1.00 46.55           C  
ATOM   7147  CE2 TYR B 135     124.142 103.759 125.379  1.00 46.55           C  
ATOM   7148  CZ  TYR B 135     125.355 104.085 124.832  1.00 46.55           C  
ATOM   7149  OH  TYR B 135     126.188 104.957 125.490  1.00 46.55           O  
ATOM   7150  N   ASN B 136     122.670 101.847 119.538  1.00 46.16           N  
ATOM   7151  CA  ASN B 136     123.371 102.337 118.359  1.00 46.16           C  
ATOM   7152  C   ASN B 136     122.682 103.572 117.794  1.00 46.16           C  
ATOM   7153  O   ASN B 136     123.348 104.525 117.374  1.00 46.16           O  
ATOM   7154  CB  ASN B 136     123.462 101.233 117.307  1.00 46.16           C  
ATOM   7155  CG  ASN B 136     124.517 100.194 117.645  1.00 46.16           C  
ATOM   7156  OD1 ASN B 136     125.676 100.526 117.890  1.00 46.16           O  
ATOM   7157  ND2 ASN B 136     124.117  98.929 117.664  1.00 46.16           N  
ATOM   7158  N   THR B 137     121.349 103.573 117.776  1.00 41.44           N  
ATOM   7159  CA  THR B 137     120.619 104.778 117.402  1.00 41.44           C  
ATOM   7160  C   THR B 137     120.752 105.871 118.457  1.00 41.44           C  
ATOM   7161  O   THR B 137     120.663 107.058 118.128  1.00 41.44           O  
ATOM   7162  CB  THR B 137     119.148 104.449 117.158  1.00 41.44           C  
ATOM   7163  OG1 THR B 137     118.629 103.724 118.277  1.00 41.44           O  
ATOM   7164  CG2 THR B 137     118.993 103.608 115.905  1.00 41.44           C  
ATOM   7165  N   TYR B 138     120.953 105.499 119.724  1.00 45.03           N  
ATOM   7166  CA  TYR B 138     121.098 106.508 120.769  1.00 45.03           C  
ATOM   7167  C   TYR B 138     122.390 107.300 120.602  1.00 45.03           C  
ATOM   7168  O   TYR B 138     122.381 108.535 120.663  1.00 45.03           O  
ATOM   7169  CB  TYR B 138     121.039 105.865 122.153  1.00 45.03           C  
ATOM   7170  CG  TYR B 138     120.854 106.875 123.265  1.00 45.03           C  
ATOM   7171  CD1 TYR B 138     121.947 107.464 123.885  1.00 45.03           C  
ATOM   7172  CD2 TYR B 138     119.588 107.247 123.686  1.00 45.03           C  
ATOM   7173  CE1 TYR B 138     121.780 108.387 124.894  1.00 45.03           C  
ATOM   7174  CE2 TYR B 138     119.412 108.170 124.693  1.00 45.03           C  
ATOM   7175  CZ  TYR B 138     120.510 108.736 125.294  1.00 45.03           C  
ATOM   7176  OH  TYR B 138     120.336 109.656 126.298  1.00 45.03           O  
ATOM   7177  N   LYS B 139     123.518 106.609 120.405  1.00 47.57           N  
ATOM   7178  CA  LYS B 139     124.780 107.324 120.227  1.00 47.57           C  
ATOM   7179  C   LYS B 139     124.764 108.203 118.986  1.00 47.57           C  
ATOM   7180  O   LYS B 139     125.415 109.253 118.962  1.00 47.57           O  
ATOM   7181  CB  LYS B 139     125.961 106.358 120.144  1.00 47.57           C  
ATOM   7182  CG  LYS B 139     127.282 107.019 120.541  1.00 47.57           C  
ATOM   7183  CD  LYS B 139     128.514 106.192 120.182  1.00 47.57           C  
ATOM   7184  CE  LYS B 139     128.319 104.709 120.410  1.00 47.57           C  
ATOM   7185  NZ  LYS B 139     127.951 104.434 121.819  1.00 47.57           N  
ATOM   7186  N   ASN B 140     124.039 107.796 117.948  1.00 47.83           N  
ATOM   7187  CA  ASN B 140     123.984 108.571 116.718  1.00 47.83           C  
ATOM   7188  C   ASN B 140     123.022 109.750 116.793  1.00 47.83           C  
ATOM   7189  O   ASN B 140     123.061 110.609 115.905  1.00 47.83           O  
ATOM   7190  CB  ASN B 140     123.589 107.670 115.547  1.00 47.83           C  
ATOM   7191  CG  ASN B 140     124.729 106.792 115.077  1.00 47.83           C  
ATOM   7192  OD1 ASN B 140     125.899 107.108 115.291  1.00 47.83           O  
ATOM   7193  ND2 ASN B 140     124.394 105.682 114.431  1.00 47.83           N  
ATOM   7194  N   THR B 141     122.170 109.822 117.811  1.00 43.59           N  
ATOM   7195  CA  THR B 141     121.144 110.861 117.794  1.00 43.59           C  
ATOM   7196  C   THR B 141     121.146 111.756 119.027  1.00 43.59           C  
ATOM   7197  O   THR B 141     120.970 112.969 118.893  1.00 43.59           O  
ATOM   7198  CB  THR B 141     119.761 110.202 117.619  1.00 43.59           C  
ATOM   7199  OG1 THR B 141     119.663 109.644 116.304  1.00 43.59           O  
ATOM   7200  CG2 THR B 141     118.650 111.218 117.792  1.00 43.59           C  
ATOM   7201  N   CYS B 142     121.367 111.202 120.222  1.00 44.48           N  
ATOM   7202  CA  CYS B 142     121.200 111.966 121.455  1.00 44.48           C  
ATOM   7203  C   CYS B 142     122.413 111.861 122.370  1.00 44.48           C  
ATOM   7204  O   CYS B 142     122.265 111.795 123.592  1.00 44.48           O  
ATOM   7205  CB  CYS B 142     119.945 111.526 122.209  1.00 44.48           C  
ATOM   7206  SG  CYS B 142     118.420 111.604 121.263  1.00 44.48           S  
ATOM   7207  N   ASP B 143     123.616 111.836 121.805  1.00 50.20           N  
ATOM   7208  CA  ASP B 143     124.815 111.856 122.630  1.00 50.20           C  
ATOM   7209  C   ASP B 143     124.904 113.170 123.399  1.00 50.20           C  
ATOM   7210  O   ASP B 143     124.714 114.250 122.832  1.00 50.20           O  
ATOM   7211  CB  ASP B 143     126.058 111.659 121.762  1.00 50.20           C  
ATOM   7212  CG  ASP B 143     127.347 111.841 122.540  1.00 50.20           C  
ATOM   7213  OD1 ASP B 143     127.401 111.421 123.714  1.00 50.20           O  
ATOM   7214  OD2 ASP B 143     128.308 112.403 121.974  1.00 50.20           O  
ATOM   7215  N   GLY B 144     125.192 113.074 124.695  1.00 44.58           N  
ATOM   7216  CA  GLY B 144     125.324 114.248 125.532  1.00 44.58           C  
ATOM   7217  C   GLY B 144     123.990 114.803 125.996  1.00 44.58           C  
ATOM   7218  O   GLY B 144     122.912 114.329 125.638  1.00 44.58           O  
ATOM   7219  N   THR B 145     124.080 115.843 126.828  1.00 40.58           N  
ATOM   7220  CA  THR B 145     122.889 116.475 127.384  1.00 40.58           C  
ATOM   7221  C   THR B 145     122.218 117.442 126.416  1.00 40.58           C  
ATOM   7222  O   THR B 145     121.086 117.861 126.677  1.00 40.58           O  
ATOM   7223  CB  THR B 145     123.239 117.201 128.686  1.00 40.58           C  
ATOM   7224  OG1 THR B 145     122.034 117.590 129.357  1.00 40.58           O  
ATOM   7225  CG2 THR B 145     124.083 118.434 128.409  1.00 40.58           C  
ATOM   7226  N   THR B 146     122.879 117.812 125.320  1.00 36.93           N  
ATOM   7227  CA  THR B 146     122.274 118.655 124.298  1.00 36.93           C  
ATOM   7228  C   THR B 146     122.640 118.100 122.932  1.00 36.93           C  
ATOM   7229  O   THR B 146     123.756 117.618 122.728  1.00 36.93           O  
ATOM   7230  CB  THR B 146     122.726 120.123 124.383  1.00 36.93           C  
ATOM   7231  OG1 THR B 146     124.002 120.272 123.748  1.00 36.93           O  
ATOM   7232  CG2 THR B 146     122.812 120.609 125.823  1.00 36.93           C  
ATOM   7233  N   PHE B 147     121.694 118.176 122.001  1.00 28.58           N  
ATOM   7234  CA  PHE B 147     121.895 117.660 120.657  1.00 28.58           C  
ATOM   7235  C   PHE B 147     121.144 118.543 119.674  1.00 28.58           C  
ATOM   7236  O   PHE B 147     120.281 119.337 120.057  1.00 28.58           O  
ATOM   7237  CB  PHE B 147     121.460 116.190 120.559  1.00 28.58           C  
ATOM   7238  CG  PHE B 147     119.970 115.984 120.572  1.00 28.58           C  
ATOM   7239  CD1 PHE B 147     119.299 115.804 121.768  1.00 28.58           C  
ATOM   7240  CD2 PHE B 147     119.242 115.964 119.397  1.00 28.58           C  
ATOM   7241  CE1 PHE B 147     117.937 115.613 121.792  1.00 28.58           C  
ATOM   7242  CE2 PHE B 147     117.879 115.772 119.419  1.00 28.58           C  
ATOM   7243  CZ  PHE B 147     117.227 115.599 120.618  1.00 28.58           C  
ATOM   7244  N   THR B 148     121.493 118.408 118.399  1.00 26.89           N  
ATOM   7245  CA  THR B 148     120.908 119.211 117.336  1.00 26.89           C  
ATOM   7246  C   THR B 148     120.002 118.358 116.459  1.00 26.89           C  
ATOM   7247  O   THR B 148     120.321 117.207 116.149  1.00 26.89           O  
ATOM   7248  CB  THR B 148     121.991 119.879 116.479  1.00 26.89           C  
ATOM   7249  OG1 THR B 148     121.375 120.682 115.466  1.00 26.89           O  
ATOM   7250  CG2 THR B 148     122.897 118.846 115.823  1.00 26.89           C  
ATOM   7251  N   TYR B 149     118.855 118.922 116.092  1.00 24.69           N  
ATOM   7252  CA  TYR B 149     117.939 118.283 115.164  1.00 24.69           C  
ATOM   7253  C   TYR B 149     117.073 119.356 114.522  1.00 24.69           C  
ATOM   7254  O   TYR B 149     116.643 120.302 115.186  1.00 24.69           O  
ATOM   7255  CB  TYR B 149     117.061 117.241 115.864  1.00 24.69           C  
ATOM   7256  CG  TYR B 149     115.988 116.656 114.982  1.00 24.69           C  
ATOM   7257  CD1 TYR B 149     116.314 115.966 113.824  1.00 24.69           C  
ATOM   7258  CD2 TYR B 149     114.648 116.812 115.295  1.00 24.69           C  
ATOM   7259  CE1 TYR B 149     115.334 115.434 113.013  1.00 24.69           C  
ATOM   7260  CE2 TYR B 149     113.663 116.288 114.490  1.00 24.69           C  
ATOM   7261  CZ  TYR B 149     114.010 115.600 113.350  1.00 24.69           C  
ATOM   7262  OH  TYR B 149     113.028 115.074 112.545  1.00 24.69           O  
ATOM   7263  N   ALA B 150     116.812 119.188 113.224  1.00 24.42           N  
ATOM   7264  CA  ALA B 150     115.945 120.091 112.464  1.00 24.42           C  
ATOM   7265  C   ALA B 150     116.382 121.548 112.599  1.00 24.42           C  
ATOM   7266  O   ALA B 150     115.565 122.444 112.823  1.00 24.42           O  
ATOM   7267  CB  ALA B 150     114.485 119.922 112.878  1.00 24.42           C  
ATOM   7268  N   SER B 151     117.690 121.782 112.465  1.00 24.16           N  
ATOM   7269  CA  SER B 151     118.278 123.125 112.482  1.00 24.16           C  
ATOM   7270  C   SER B 151     118.020 123.854 113.797  1.00 24.16           C  
ATOM   7271  O   SER B 151     117.876 125.078 113.822  1.00 24.16           O  
ATOM   7272  CB  SER B 151     117.780 123.968 111.305  1.00 24.16           C  
ATOM   7273  OG  SER B 151     118.381 123.558 110.090  1.00 24.16           O  
ATOM   7274  N   ALA B 152     117.954 123.115 114.900  1.00 24.85           N  
ATOM   7275  CA  ALA B 152     117.802 123.708 116.219  1.00 24.85           C  
ATOM   7276  C   ALA B 152     118.638 122.921 117.216  1.00 24.85           C  
ATOM   7277  O   ALA B 152     119.071 121.799 116.947  1.00 24.85           O  
ATOM   7278  CB  ALA B 152     116.333 123.745 116.655  1.00 24.85           C  
ATOM   7279  N   LEU B 153     118.868 123.525 118.376  1.00 26.30           N  
ATOM   7280  CA  LEU B 153     119.543 122.864 119.483  1.00 26.30           C  
ATOM   7281  C   LEU B 153     118.524 122.501 120.551  1.00 26.30           C  
ATOM   7282  O   LEU B 153     117.693 123.326 120.938  1.00 26.30           O  
ATOM   7283  CB  LEU B 153     120.637 123.749 120.085  1.00 26.30           C  
ATOM   7284  CG  LEU B 153     122.014 123.772 119.415  1.00 26.30           C  
ATOM   7285  CD1 LEU B 153     122.663 122.400 119.495  1.00 26.30           C  
ATOM   7286  CD2 LEU B 153     121.947 124.253 117.973  1.00 26.30           C  
ATOM   7287  N   TRP B 154     118.592 121.262 121.023  1.00 22.08           N  
ATOM   7288  CA  TRP B 154     117.624 120.731 121.968  1.00 22.08           C  
ATOM   7289  C   TRP B 154     118.356 120.256 123.214  1.00 22.08           C  
ATOM   7290  O   TRP B 154     119.431 119.658 123.120  1.00 22.08           O  
ATOM   7291  CB  TRP B 154     116.838 119.577 121.347  1.00 22.08           C  
ATOM   7292  CG  TRP B 154     116.086 119.962 120.114  1.00 22.08           C  
ATOM   7293  CD1 TRP B 154     116.557 119.947 118.836  1.00 22.08           C  
ATOM   7294  CD2 TRP B 154     114.736 120.431 120.037  1.00 22.08           C  
ATOM   7295  NE1 TRP B 154     115.585 120.370 117.967  1.00 22.08           N  
ATOM   7296  CE2 TRP B 154     114.456 120.673 118.680  1.00 22.08           C  
ATOM   7297  CE3 TRP B 154     113.736 120.666 120.982  1.00 22.08           C  
ATOM   7298  CZ2 TRP B 154     113.220 121.138 118.246  1.00 22.08           C  
ATOM   7299  CZ3 TRP B 154     112.511 121.129 120.550  1.00 22.08           C  
ATOM   7300  CH2 TRP B 154     112.263 121.360 119.195  1.00 22.08           C  
ATOM   7301  N   GLU B 155     117.776 120.526 124.379  1.00 30.17           N  
ATOM   7302  CA  GLU B 155     118.357 120.130 125.655  1.00 30.17           C  
ATOM   7303  C   GLU B 155     117.443 119.115 126.330  1.00 30.17           C  
ATOM   7304  O   GLU B 155     116.230 119.326 126.424  1.00 30.17           O  
ATOM   7305  CB  GLU B 155     118.615 121.357 126.544  1.00 30.17           C  
ATOM   7306  CG  GLU B 155     117.421 121.900 127.307  1.00 30.17           C  
ATOM   7307  CD  GLU B 155     117.563 123.373 127.632  1.00 30.17           C  
ATOM   7308  OE1 GLU B 155     116.740 123.895 128.413  1.00 30.17           O  
ATOM   7309  OE2 GLU B 155     118.497 124.012 127.104  1.00 30.17           O  
ATOM   7310  N   ILE B 156     118.027 117.999 126.767  1.00 29.65           N  
ATOM   7311  CA  ILE B 156     117.241 116.870 127.251  1.00 29.65           C  
ATOM   7312  C   ILE B 156     116.684 117.169 128.635  1.00 29.65           C  
ATOM   7313  O   ILE B 156     117.416 117.577 129.545  1.00 29.65           O  
ATOM   7314  CB  ILE B 156     118.086 115.589 127.256  1.00 29.65           C  
ATOM   7315  CG1 ILE B 156     118.731 115.373 125.886  1.00 29.65           C  
ATOM   7316  CG2 ILE B 156     117.244 114.395 127.659  1.00 29.65           C  
ATOM   7317  CD1 ILE B 156     119.499 114.080 125.771  1.00 29.65           C  
ATOM   7318  N   GLN B 157     115.376 116.966 128.795  1.00 33.64           N  
ATOM   7319  CA  GLN B 157     114.702 117.123 130.077  1.00 33.64           C  
ATOM   7320  C   GLN B 157     114.552 115.795 130.815  1.00 33.64           C  
ATOM   7321  O   GLN B 157     114.890 115.699 131.998  1.00 33.64           O  
ATOM   7322  CB  GLN B 157     113.330 117.768 129.868  1.00 33.64           C  
ATOM   7323  CG  GLN B 157     112.887 118.667 131.006  1.00 33.64           C  
ATOM   7324  CD  GLN B 157     111.414 119.018 130.932  1.00 33.64           C  
ATOM   7325  OE1 GLN B 157     110.552 118.139 130.960  1.00 33.64           O  
ATOM   7326  NE2 GLN B 157     111.117 120.308 130.842  1.00 33.64           N  
ATOM   7327  N   GLN B 158     114.053 114.765 130.134  1.00 34.10           N  
ATOM   7328  CA  GLN B 158     113.848 113.462 130.751  1.00 34.10           C  
ATOM   7329  C   GLN B 158     114.088 112.367 129.724  1.00 34.10           C  
ATOM   7330  O   GLN B 158     113.934 112.574 128.518  1.00 34.10           O  
ATOM   7331  CB  GLN B 158     112.434 113.314 131.322  1.00 34.10           C  
ATOM   7332  CG  GLN B 158     112.255 113.815 132.738  1.00 34.10           C  
ATOM   7333  CD  GLN B 158     110.806 113.771 133.178  1.00 34.10           C  
ATOM   7334  OE1 GLN B 158     109.925 113.368 132.420  1.00 34.10           O  
ATOM   7335  NE2 GLN B 158     110.551 114.194 134.411  1.00 34.10           N  
ATOM   7336  N   VAL B 159     114.471 111.193 130.220  1.00 32.42           N  
ATOM   7337  CA  VAL B 159     114.507 109.968 129.433  1.00 32.42           C  
ATOM   7338  C   VAL B 159     113.719 108.903 130.181  1.00 32.42           C  
ATOM   7339  O   VAL B 159     113.931 108.692 131.379  1.00 32.42           O  
ATOM   7340  CB  VAL B 159     115.949 109.488 129.168  1.00 32.42           C  
ATOM   7341  CG1 VAL B 159     115.943 108.282 128.246  1.00 32.42           C  
ATOM   7342  CG2 VAL B 159     116.786 110.607 128.578  1.00 32.42           C  
ATOM   7343  N   VAL B 160     112.807 108.233 129.475  1.00 32.82           N  
ATOM   7344  CA  VAL B 160     112.025 107.145 130.045  1.00 32.82           C  
ATOM   7345  C   VAL B 160     112.072 105.959 129.092  1.00 32.82           C  
ATOM   7346  O   VAL B 160     112.314 106.102 127.893  1.00 32.82           O  
ATOM   7347  CB  VAL B 160     110.562 107.549 130.334  1.00 32.82           C  
ATOM   7348  CG1 VAL B 160     110.510 108.778 131.226  1.00 32.82           C  
ATOM   7349  CG2 VAL B 160     109.811 107.793 129.042  1.00 32.82           C  
ATOM   7350  N   ASP B 161     111.848 104.771 129.650  1.00 38.48           N  
ATOM   7351  CA  ASP B 161     111.845 103.545 128.870  1.00 38.48           C  
ATOM   7352  C   ASP B 161     110.416 103.163 128.492  1.00 38.48           C  
ATOM   7353  O   ASP B 161     109.460 103.899 128.742  1.00 38.48           O  
ATOM   7354  CB  ASP B 161     112.533 102.417 129.638  1.00 38.48           C  
ATOM   7355  CG  ASP B 161     111.964 102.226 131.026  1.00 38.48           C  
ATOM   7356  OD1 ASP B 161     111.204 103.104 131.480  1.00 38.48           O  
ATOM   7357  OD2 ASP B 161     112.277 101.200 131.663  1.00 38.48           O  
ATOM   7358  N   ALA B 162     110.268 101.988 127.878  1.00 37.80           N  
ATOM   7359  CA  ALA B 162     108.954 101.528 127.443  1.00 37.80           C  
ATOM   7360  C   ALA B 162     107.999 101.313 128.609  1.00 37.80           C  
ATOM   7361  O   ALA B 162     106.786 101.217 128.392  1.00 37.80           O  
ATOM   7362  CB  ALA B 162     109.090 100.237 126.639  1.00 37.80           C  
ATOM   7363  N   ASP B 163     108.513 101.227 129.832  1.00 44.97           N  
ATOM   7364  CA  ASP B 163     107.691 101.107 131.027  1.00 44.97           C  
ATOM   7365  C   ASP B 163     107.368 102.455 131.658  1.00 44.97           C  
ATOM   7366  O   ASP B 163     106.755 102.487 132.730  1.00 44.97           O  
ATOM   7367  CB  ASP B 163     108.387 100.213 132.055  1.00 44.97           C  
ATOM   7368  CG  ASP B 163     108.486  98.774 131.600  1.00 44.97           C  
ATOM   7369  OD1 ASP B 163     107.577  98.318 130.877  1.00 44.97           O  
ATOM   7370  OD2 ASP B 163     109.472  98.101 131.962  1.00 44.97           O  
ATOM   7371  N   SER B 164     107.781 103.557 131.027  1.00 44.60           N  
ATOM   7372  CA  SER B 164     107.529 104.913 131.516  1.00 44.60           C  
ATOM   7373  C   SER B 164     108.200 105.173 132.861  1.00 44.60           C  
ATOM   7374  O   SER B 164     107.725 105.987 133.657  1.00 44.60           O  
ATOM   7375  CB  SER B 164     106.029 105.211 131.598  1.00 44.60           C  
ATOM   7376  OG  SER B 164     105.482 105.410 130.307  1.00 44.60           O  
ATOM   7377  N   LYS B 165     109.303 104.483 133.130  1.00 43.83           N  
ATOM   7378  CA  LYS B 165     110.118 104.759 134.304  1.00 43.83           C  
ATOM   7379  C   LYS B 165     111.309 105.628 133.920  1.00 43.83           C  
ATOM   7380  O   LYS B 165     111.880 105.476 132.837  1.00 43.83           O  
ATOM   7381  CB  LYS B 165     110.591 103.459 134.954  1.00 43.83           C  
ATOM   7382  CG  LYS B 165     109.588 102.875 135.935  1.00 43.83           C  
ATOM   7383  CD  LYS B 165     110.007 101.500 136.418  1.00 43.83           C  
ATOM   7384  CE  LYS B 165     109.277 100.407 135.655  1.00 43.83           C  
ATOM   7385  NZ  LYS B 165     107.799 100.547 135.764  1.00 43.83           N  
ATOM   7386  N   ILE B 166     111.678 106.543 134.817  1.00 41.68           N  
ATOM   7387  CA  ILE B 166     112.729 107.507 134.520  1.00 41.68           C  
ATOM   7388  C   ILE B 166     114.077 106.805 134.440  1.00 41.68           C  
ATOM   7389  O   ILE B 166     114.445 106.016 135.322  1.00 41.68           O  
ATOM   7390  CB  ILE B 166     112.744 108.621 135.580  1.00 41.68           C  
ATOM   7391  CG1 ILE B 166     111.533 109.538 135.402  1.00 41.68           C  
ATOM   7392  CG2 ILE B 166     114.030 109.423 135.497  1.00 41.68           C  
ATOM   7393  CD1 ILE B 166     111.394 110.580 136.484  1.00 41.68           C  
ATOM   7394  N   VAL B 167     114.825 107.094 133.377  1.00 41.92           N  
ATOM   7395  CA  VAL B 167     116.154 106.534 133.155  1.00 41.92           C  
ATOM   7396  C   VAL B 167     117.159 107.677 133.175  1.00 41.92           C  
ATOM   7397  O   VAL B 167     117.029 108.641 132.411  1.00 41.92           O  
ATOM   7398  CB  VAL B 167     116.228 105.761 131.831  1.00 41.92           C  
ATOM   7399  CG1 VAL B 167     117.648 105.301 131.564  1.00 41.92           C  
ATOM   7400  CG2 VAL B 167     115.285 104.574 131.860  1.00 41.92           C  
ATOM   7401  N   GLN B 168     118.160 107.571 134.044  1.00 50.52           N  
ATOM   7402  CA  GLN B 168     119.193 108.591 134.144  1.00 50.52           C  
ATOM   7403  C   GLN B 168     120.182 108.470 132.992  1.00 50.52           C  
ATOM   7404  O   GLN B 168     120.395 107.388 132.438  1.00 50.52           O  
ATOM   7405  CB  GLN B 168     119.929 108.484 135.482  1.00 50.52           C  
ATOM   7406  CG  GLN B 168     119.028 108.343 136.710  1.00 50.52           C  
ATOM   7407  CD  GLN B 168     118.011 109.467 136.870  1.00 50.52           C  
ATOM   7408  OE1 GLN B 168     118.183 110.548 136.310  1.00 50.52           O  
ATOM   7409  NE2 GLN B 168     116.922 109.196 137.582  1.00 50.52           N  
ATOM   7410  N   LEU B 169     120.785 109.605 132.627  1.00 51.10           N  
ATOM   7411  CA  LEU B 169     121.719 109.623 131.504  1.00 51.10           C  
ATOM   7412  C   LEU B 169     122.936 108.746 131.763  1.00 51.10           C  
ATOM   7413  O   LEU B 169     123.522 108.205 130.819  1.00 51.10           O  
ATOM   7414  CB  LEU B 169     122.157 111.058 131.205  1.00 51.10           C  
ATOM   7415  CG  LEU B 169     121.323 111.895 130.230  1.00 51.10           C  
ATOM   7416  CD1 LEU B 169     121.416 111.325 128.828  1.00 51.10           C  
ATOM   7417  CD2 LEU B 169     119.870 111.999 130.670  1.00 51.10           C  
ATOM   7418  N   SER B 170     123.337 108.597 133.028  1.00 55.38           N  
ATOM   7419  CA  SER B 170     124.482 107.757 133.355  1.00 55.38           C  
ATOM   7420  C   SER B 170     124.203 106.276 133.139  1.00 55.38           C  
ATOM   7421  O   SER B 170     125.145 105.504 132.935  1.00 55.38           O  
ATOM   7422  CB  SER B 170     124.911 107.999 134.802  1.00 55.38           C  
ATOM   7423  OG  SER B 170     123.790 108.009 135.669  1.00 55.38           O  
ATOM   7424  N   GLU B 171     122.935 105.864 133.176  1.00 53.91           N  
ATOM   7425  CA  GLU B 171     122.597 104.454 133.018  1.00 53.91           C  
ATOM   7426  C   GLU B 171     122.725 103.990 131.575  1.00 53.91           C  
ATOM   7427  O   GLU B 171     122.927 102.797 131.327  1.00 53.91           O  
ATOM   7428  CB  GLU B 171     121.173 104.200 133.514  1.00 53.91           C  
ATOM   7429  CG  GLU B 171     120.872 104.784 134.881  1.00 53.91           C  
ATOM   7430  CD  GLU B 171     119.612 104.206 135.491  1.00 53.91           C  
ATOM   7431  OE1 GLU B 171     119.477 102.966 135.514  1.00 53.91           O  
ATOM   7432  OE2 GLU B 171     118.754 104.991 135.947  1.00 53.91           O  
ATOM   7433  N   ILE B 172     122.616 104.907 130.619  1.00 49.76           N  
ATOM   7434  CA  ILE B 172     122.529 104.547 129.210  1.00 49.76           C  
ATOM   7435  C   ILE B 172     123.934 104.348 128.655  1.00 49.76           C  
ATOM   7436  O   ILE B 172     124.584 105.306 128.222  1.00 49.76           O  
ATOM   7437  CB  ILE B 172     121.747 105.623 128.434  1.00 49.76           C  
ATOM   7438  CG1 ILE B 172     120.319 105.717 128.970  1.00 49.76           C  
ATOM   7439  CG2 ILE B 172     121.669 105.285 126.971  1.00 49.76           C  
ATOM   7440  CD1 ILE B 172     119.756 107.118 128.974  1.00 49.76           C  
ATOM   7441  N   SER B 173     124.419 103.104 128.677  1.00 53.91           N  
ATOM   7442  CA  SER B 173     125.766 102.770 128.230  1.00 53.91           C  
ATOM   7443  C   SER B 173     125.760 101.415 127.534  1.00 53.91           C  
ATOM   7444  O   SER B 173     124.818 100.634 127.683  1.00 53.91           O  
ATOM   7445  CB  SER B 173     126.761 102.752 129.396  1.00 53.91           C  
ATOM   7446  OG  SER B 173     126.234 102.047 130.504  1.00 53.91           O  
ATOM   7447  N   MET B 174     126.825 101.148 126.764  1.00 58.75           N  
ATOM   7448  CA  MET B 174     126.985  99.853 126.099  1.00 58.75           C  
ATOM   7449  C   MET B 174     126.868  98.678 127.059  1.00 58.75           C  
ATOM   7450  O   MET B 174     126.191  97.693 126.746  1.00 58.75           O  
ATOM   7451  CB  MET B 174     128.343  99.788 125.390  1.00 58.75           C  
ATOM   7452  CG  MET B 174     128.501  98.742 124.267  1.00 58.75           C  
ATOM   7453  SD  MET B 174     127.153  98.301 123.150  1.00 58.75           S  
ATOM   7454  CE  MET B 174     126.542  99.888 122.631  1.00 58.75           C  
ATOM   7455  N   ASP B 175     127.531  98.754 128.210  1.00 58.84           N  
ATOM   7456  CA  ASP B 175     127.542  97.597 129.143  1.00 58.84           C  
ATOM   7457  C   ASP B 175     126.206  97.463 129.874  1.00 58.84           C  
ATOM   7458  O   ASP B 175     125.826  96.324 130.182  1.00 58.84           O  
ATOM   7459  CB  ASP B 175     128.723  97.673 130.110  1.00 58.84           C  
ATOM   7460  CG  ASP B 175     128.928  99.053 130.707  1.00 58.84           C  
ATOM   7461  OD1 ASP B 175     127.919  99.740 130.956  1.00 58.84           O  
ATOM   7462  OD2 ASP B 175     130.097  99.432 130.912  1.00 58.84           O  
ATOM   7463  N   ASN B 176     125.553  98.578 130.191  1.00 54.00           N  
ATOM   7464  CA  ASN B 176     124.300  98.541 130.933  1.00 54.00           C  
ATOM   7465  C   ASN B 176     123.109  98.324 130.003  1.00 54.00           C  
ATOM   7466  O   ASN B 176     122.095  97.771 130.436  1.00 54.00           O  
ATOM   7467  CB  ASN B 176     124.198  99.844 131.756  1.00 54.00           C  
ATOM   7468  CG  ASN B 176     122.866 100.031 132.504  1.00 54.00           C  
ATOM   7469  OD1 ASN B 176     121.826  99.484 132.164  1.00 54.00           O  
ATOM   7470  ND2 ASN B 176     122.923 100.836 133.556  1.00 54.00           N  
ATOM   7471  N   SER B 177     123.256  98.641 128.713  1.00 50.95           N  
ATOM   7472  CA  SER B 177     122.140  98.667 127.758  1.00 50.95           C  
ATOM   7473  C   SER B 177     121.210  97.457 127.799  1.00 50.95           C  
ATOM   7474  O   SER B 177     119.989  97.662 127.769  1.00 50.95           O  
ATOM   7475  CB  SER B 177     122.695  98.837 126.336  1.00 50.95           C  
ATOM   7476  OG  SER B 177     121.704  98.546 125.367  1.00 50.95           O  
ATOM   7477  N   PRO B 178     121.682  96.204 127.846  1.00 51.52           N  
ATOM   7478  CA  PRO B 178     120.732  95.081 127.886  1.00 51.52           C  
ATOM   7479  C   PRO B 178     119.893  95.031 129.151  1.00 51.52           C  
ATOM   7480  O   PRO B 178     118.874  94.328 129.164  1.00 51.52           O  
ATOM   7481  CB  PRO B 178     121.637  93.847 127.766  1.00 51.52           C  
ATOM   7482  CG  PRO B 178     122.937  94.290 128.308  1.00 51.52           C  
ATOM   7483  CD  PRO B 178     123.073  95.721 127.866  1.00 51.52           C  
ATOM   7484  N   ASN B 179     120.279  95.745 130.209  1.00 49.84           N  
ATOM   7485  CA  ASN B 179     119.449  95.802 131.405  1.00 49.84           C  
ATOM   7486  C   ASN B 179     118.262  96.743 131.239  1.00 49.84           C  
ATOM   7487  O   ASN B 179     117.222  96.533 131.870  1.00 49.84           O  
ATOM   7488  CB  ASN B 179     120.286  96.231 132.610  1.00 49.84           C  
ATOM   7489  CG  ASN B 179     121.483  95.329 132.839  1.00 49.84           C  
ATOM   7490  OD1 ASN B 179     121.577  94.245 132.266  1.00 49.84           O  
ATOM   7491  ND2 ASN B 179     122.403  95.773 133.687  1.00 49.84           N  
ATOM   7492  N   LEU B 180     118.394  97.779 130.415  1.00 45.53           N  
ATOM   7493  CA  LEU B 180     117.306  98.731 130.231  1.00 45.53           C  
ATOM   7494  C   LEU B 180     116.204  98.152 129.352  1.00 45.53           C  
ATOM   7495  O   LEU B 180     116.457  97.383 128.422  1.00 45.53           O  
ATOM   7496  CB  LEU B 180     117.821 100.027 129.605  1.00 45.53           C  
ATOM   7497  CG  LEU B 180     119.058 100.690 130.205  1.00 45.53           C  
ATOM   7498  CD1 LEU B 180     119.639 101.687 129.224  1.00 45.53           C  
ATOM   7499  CD2 LEU B 180     118.694 101.377 131.506  1.00 45.53           C  
ATOM   7500  N   ALA B 181     114.968  98.534 129.659  1.00 39.45           N  
ATOM   7501  CA  ALA B 181     113.857  98.256 128.762  1.00 39.45           C  
ATOM   7502  C   ALA B 181     113.888  99.225 127.587  1.00 39.45           C  
ATOM   7503  O   ALA B 181     114.223 100.400 127.743  1.00 39.45           O  
ATOM   7504  CB  ALA B 181     112.528  98.365 129.505  1.00 39.45           C  
ATOM   7505  N   TRP B 182     113.532  98.731 126.409  1.00 34.71           N  
ATOM   7506  CA  TRP B 182     113.576  99.526 125.194  1.00 34.71           C  
ATOM   7507  C   TRP B 182     112.222  99.477 124.504  1.00 34.71           C  
ATOM   7508  O   TRP B 182     111.471  98.514 124.684  1.00 34.71           O  
ATOM   7509  CB  TRP B 182     114.661  99.010 124.237  1.00 34.71           C  
ATOM   7510  CG  TRP B 182     116.057  99.254 124.718  1.00 34.71           C  
ATOM   7511  CD1 TRP B 182     116.797  98.444 125.525  1.00 34.71           C  
ATOM   7512  CD2 TRP B 182     116.884 100.384 124.418  1.00 34.71           C  
ATOM   7513  NE1 TRP B 182     118.032  98.999 125.749  1.00 34.71           N  
ATOM   7514  CE2 TRP B 182     118.110 100.191 125.080  1.00 34.71           C  
ATOM   7515  CE3 TRP B 182     116.706 101.541 123.655  1.00 34.71           C  
ATOM   7516  CZ2 TRP B 182     119.151 101.111 125.003  1.00 34.71           C  
ATOM   7517  CZ3 TRP B 182     117.740 102.451 123.581  1.00 34.71           C  
ATOM   7518  CH2 TRP B 182     118.946 102.232 124.251  1.00 34.71           C  
ATOM   7519  N   PRO B 183     111.878 100.498 123.702  1.00 31.54           N  
ATOM   7520  CA  PRO B 183     112.586 101.738 123.362  1.00 31.54           C  
ATOM   7521  C   PRO B 183     112.690 102.755 124.495  1.00 31.54           C  
ATOM   7522  O   PRO B 183     111.986 102.649 125.495  1.00 31.54           O  
ATOM   7523  CB  PRO B 183     111.738 102.322 122.225  1.00 31.54           C  
ATOM   7524  CG  PRO B 183     111.031 101.163 121.646  1.00 31.54           C  
ATOM   7525  CD  PRO B 183     110.712 100.303 122.829  1.00 31.54           C  
ATOM   7526  N   LEU B 184     113.567 103.738 124.322  1.00 29.73           N  
ATOM   7527  CA  LEU B 184     113.681 104.871 125.228  1.00 29.73           C  
ATOM   7528  C   LEU B 184     113.030 106.095 124.599  1.00 29.73           C  
ATOM   7529  O   LEU B 184     113.189 106.347 123.401  1.00 29.73           O  
ATOM   7530  CB  LEU B 184     115.144 105.179 125.557  1.00 29.73           C  
ATOM   7531  CG  LEU B 184     115.834 104.494 126.741  1.00 29.73           C  
ATOM   7532  CD1 LEU B 184     115.503 103.027 126.809  1.00 29.73           C  
ATOM   7533  CD2 LEU B 184     117.335 104.691 126.662  1.00 29.73           C  
ATOM   7534  N   ILE B 185     112.300 106.854 125.412  1.00 27.27           N  
ATOM   7535  CA  ILE B 185     111.620 108.065 124.965  1.00 27.27           C  
ATOM   7536  C   ILE B 185     112.321 109.262 125.592  1.00 27.27           C  
ATOM   7537  O   ILE B 185     112.330 109.416 126.819  1.00 27.27           O  
ATOM   7538  CB  ILE B 185     110.122 108.058 125.313  1.00 27.27           C  
ATOM   7539  CG1 ILE B 185     109.428 106.779 124.823  1.00 27.27           C  
ATOM   7540  CG2 ILE B 185     109.442 109.280 124.728  1.00 27.27           C  
ATOM   7541  CD1 ILE B 185     109.524 105.585 125.760  1.00 27.27           C  
ATOM   7542  N   VAL B 186     112.894 110.114 124.748  1.00 26.15           N  
ATOM   7543  CA  VAL B 186     113.655 111.281 125.176  1.00 26.15           C  
ATOM   7544  C   VAL B 186     112.844 112.528 124.863  1.00 26.15           C  
ATOM   7545  O   VAL B 186     112.415 112.724 123.720  1.00 26.15           O  
ATOM   7546  CB  VAL B 186     115.028 111.335 124.487  1.00 26.15           C  
ATOM   7547  CG1 VAL B 186     115.752 112.614 124.844  1.00 26.15           C  
ATOM   7548  CG2 VAL B 186     115.857 110.124 124.865  1.00 26.15           C  
ATOM   7549  N   THR B 187     112.633 113.367 125.873  1.00 25.83           N  
ATOM   7550  CA  THR B 187     111.943 114.640 125.715  1.00 25.83           C  
ATOM   7551  C   THR B 187     112.946 115.778 125.857  1.00 25.83           C  
ATOM   7552  O   THR B 187     113.775 115.773 126.772  1.00 25.83           O  
ATOM   7553  CB  THR B 187     110.800 114.780 126.728  1.00 25.83           C  
ATOM   7554  OG1 THR B 187     110.125 116.028 126.529  1.00 25.83           O  
ATOM   7555  CG2 THR B 187     111.302 114.692 128.155  1.00 25.83           C  
ATOM   7556  N   ALA B 188     112.890 116.732 124.930  1.00 23.06           N  
ATOM   7557  CA  ALA B 188     113.838 117.834 124.892  1.00 23.06           C  
ATOM   7558  C   ALA B 188     113.098 119.139 124.647  1.00 23.06           C  
ATOM   7559  O   ALA B 188     112.030 119.159 124.031  1.00 23.06           O  
ATOM   7560  CB  ALA B 188     114.900 117.624 123.809  1.00 23.06           C  
ATOM   7561  N   LEU B 189     113.676 120.231 125.139  1.00 22.82           N  
ATOM   7562  CA  LEU B 189     113.130 121.568 124.954  1.00 22.82           C  
ATOM   7563  C   LEU B 189     114.009 122.358 123.995  1.00 22.82           C  
ATOM   7564  O   LEU B 189     115.237 122.236 124.022  1.00 22.82           O  
ATOM   7565  CB  LEU B 189     113.021 122.310 126.286  1.00 22.82           C  
ATOM   7566  CG  LEU B 189     111.982 121.788 127.277  1.00 22.82           C  
ATOM   7567  CD1 LEU B 189     111.944 122.671 128.510  1.00 22.82           C  
ATOM   7568  CD2 LEU B 189     110.614 121.706 126.631  1.00 22.82           C  
ATOM   7569  N   ARG B 190     113.375 123.167 123.149  1.00 21.52           N  
ATOM   7570  CA  ARG B 190     114.116 123.984 122.197  1.00 21.52           C  
ATOM   7571  C   ARG B 190     114.940 125.035 122.930  1.00 21.52           C  
ATOM   7572  O   ARG B 190     114.433 125.738 123.808  1.00 21.52           O  
ATOM   7573  CB  ARG B 190     113.157 124.654 121.213  1.00 21.52           C  
ATOM   7574  CG  ARG B 190     113.839 125.246 119.993  1.00 21.52           C  
ATOM   7575  CD  ARG B 190     112.847 125.921 119.062  1.00 21.52           C  
ATOM   7576  NE  ARG B 190     111.824 125.002 118.577  1.00 21.52           N  
ATOM   7577  CZ  ARG B 190     111.748 124.565 117.326  1.00 21.52           C  
ATOM   7578  NH1 ARG B 190     112.639 124.959 116.429  1.00 21.52           N  
ATOM   7579  NH2 ARG B 190     110.785 123.730 116.972  1.00 21.52           N  
ATOM   7580  N   ALA B 191     116.214 125.136 122.570  1.00 26.66           N  
ATOM   7581  CA  ALA B 191     117.105 126.108 123.189  1.00 26.66           C  
ATOM   7582  C   ALA B 191     116.773 127.520 122.722  1.00 26.66           C  
ATOM   7583  O   ALA B 191     117.065 127.892 121.586  1.00 26.66           O  
ATOM   7584  CB  ALA B 191     118.553 125.775 122.879  1.00 26.66           C  
TER    7585      ALA B 191                                                      
ATOM   7586  N   LYS C   2     100.748  64.396 122.605  1.00 57.95           N  
ATOM   7587  CA  LYS C   2     101.720  65.090 123.441  1.00 57.95           C  
ATOM   7588  C   LYS C   2     101.853  66.556 123.048  1.00 57.95           C  
ATOM   7589  O   LYS C   2     101.717  67.446 123.888  1.00 57.95           O  
ATOM   7590  CB  LYS C   2     103.086  64.407 123.356  1.00 57.95           C  
ATOM   7591  CG  LYS C   2     103.978  64.654 124.564  1.00 57.95           C  
ATOM   7592  CD  LYS C   2     105.350  64.005 124.409  1.00 57.95           C  
ATOM   7593  CE  LYS C   2     105.275  62.636 123.747  1.00 57.95           C  
ATOM   7594  NZ  LYS C   2     104.389  61.695 124.487  1.00 57.95           N  
ATOM   7595  N   MET C   3     102.123  66.797 121.763  1.00 55.61           N  
ATOM   7596  CA  MET C   3     102.383  68.157 121.302  1.00 55.61           C  
ATOM   7597  C   MET C   3     101.161  69.051 121.472  1.00 55.61           C  
ATOM   7598  O   MET C   3     101.283  70.201 121.915  1.00 55.61           O  
ATOM   7599  CB  MET C   3     102.834  68.136 119.843  1.00 55.61           C  
ATOM   7600  CG  MET C   3     103.798  69.251 119.481  1.00 55.61           C  
ATOM   7601  SD  MET C   3     104.409  69.109 117.792  1.00 55.61           S  
ATOM   7602  CE  MET C   3     102.871  69.132 116.873  1.00 55.61           C  
ATOM   7603  N   SER C   4      99.974  68.540 121.134  1.00 47.39           N  
ATOM   7604  CA  SER C   4      98.761  69.344 121.252  1.00 47.39           C  
ATOM   7605  C   SER C   4      98.502  69.737 122.698  1.00 47.39           C  
ATOM   7606  O   SER C   4      98.066  70.862 122.978  1.00 47.39           O  
ATOM   7607  CB  SER C   4      97.568  68.580 120.682  1.00 47.39           C  
ATOM   7608  OG  SER C   4      96.367  69.304 120.873  1.00 47.39           O  
ATOM   7609  N   ASP C   5      98.770  68.824 123.632  1.00 49.65           N  
ATOM   7610  CA  ASP C   5      98.657  69.162 125.045  1.00 49.65           C  
ATOM   7611  C   ASP C   5      99.636  70.264 125.420  1.00 49.65           C  
ATOM   7612  O   ASP C   5      99.293  71.169 126.186  1.00 49.65           O  
ATOM   7613  CB  ASP C   5      98.892  67.923 125.907  1.00 49.65           C  
ATOM   7614  CG  ASP C   5      98.112  66.719 125.423  1.00 49.65           C  
ATOM   7615  OD1 ASP C   5      96.913  66.613 125.756  1.00 49.65           O  
ATOM   7616  OD2 ASP C   5      98.698  65.877 124.712  1.00 49.65           O  
ATOM   7617  N   VAL C   6     100.857  70.208 124.883  1.00 47.08           N  
ATOM   7618  CA  VAL C   6     101.846  71.242 125.177  1.00 47.08           C  
ATOM   7619  C   VAL C   6     101.366  72.600 124.681  1.00 47.08           C  
ATOM   7620  O   VAL C   6     101.473  73.607 125.391  1.00 47.08           O  
ATOM   7621  CB  VAL C   6     103.209  70.864 124.570  1.00 47.08           C  
ATOM   7622  CG1 VAL C   6     104.128  72.069 124.543  1.00 47.08           C  
ATOM   7623  CG2 VAL C   6     103.841  69.735 125.360  1.00 47.08           C  
ATOM   7624  N   LYS C   7     100.817  72.650 123.465  1.00 40.89           N  
ATOM   7625  CA  LYS C   7     100.329  73.918 122.923  1.00 40.89           C  
ATOM   7626  C   LYS C   7      99.162  74.457 123.745  1.00 40.89           C  
ATOM   7627  O   LYS C   7      99.124  75.646 124.098  1.00 40.89           O  
ATOM   7628  CB  LYS C   7      99.920  73.741 121.461  1.00 40.89           C  
ATOM   7629  CG  LYS C   7     100.922  72.967 120.633  1.00 40.89           C  
ATOM   7630  CD  LYS C   7     100.962  73.424 119.193  1.00 40.89           C  
ATOM   7631  CE  LYS C   7     102.341  73.194 118.604  1.00 40.89           C  
ATOM   7632  NZ  LYS C   7     102.336  73.236 117.118  1.00 40.89           N  
ATOM   7633  N   CYS C   8      98.192  73.592 124.052  1.00 42.40           N  
ATOM   7634  CA  CYS C   8      97.029  74.026 124.815  1.00 42.40           C  
ATOM   7635  C   CYS C   8      97.414  74.480 126.216  1.00 42.40           C  
ATOM   7636  O   CYS C   8      96.809  75.414 126.753  1.00 42.40           O  
ATOM   7637  CB  CYS C   8      96.002  72.897 124.882  1.00 42.40           C  
ATOM   7638  SG  CYS C   8      95.282  72.454 123.285  1.00 42.40           S  
ATOM   7639  N   THR C   9      98.408  73.832 126.828  1.00 41.72           N  
ATOM   7640  CA  THR C   9      98.879  74.272 128.136  1.00 41.72           C  
ATOM   7641  C   THR C   9      99.629  75.593 128.041  1.00 41.72           C  
ATOM   7642  O   THR C   9      99.505  76.443 128.927  1.00 41.72           O  
ATOM   7643  CB  THR C   9      99.756  73.196 128.774  1.00 41.72           C  
ATOM   7644  OG1 THR C   9     100.770  72.790 127.848  1.00 41.72           O  
ATOM   7645  CG2 THR C   9      98.917  71.996 129.186  1.00 41.72           C  
ATOM   7646  N   SER C  10     100.427  75.779 126.987  1.00 40.81           N  
ATOM   7647  CA  SER C  10     101.141  77.040 126.828  1.00 40.81           C  
ATOM   7648  C   SER C  10     100.180  78.207 126.657  1.00 40.81           C  
ATOM   7649  O   SER C  10     100.442  79.305 127.164  1.00 40.81           O  
ATOM   7650  CB  SER C  10     102.093  76.960 125.637  1.00 40.81           C  
ATOM   7651  OG  SER C  10     101.382  77.059 124.418  1.00 40.81           O  
ATOM   7652  N   VAL C  11      99.062  77.993 125.958  1.00 37.62           N  
ATOM   7653  CA  VAL C  11      98.095  79.076 125.770  1.00 37.62           C  
ATOM   7654  C   VAL C  11      97.521  79.525 127.111  1.00 37.62           C  
ATOM   7655  O   VAL C  11      97.508  80.720 127.437  1.00 37.62           O  
ATOM   7656  CB  VAL C  11      96.983  78.646 124.799  1.00 37.62           C  
ATOM   7657  CG1 VAL C  11      95.918  79.725 124.714  1.00 37.62           C  
ATOM   7658  CG2 VAL C  11      97.565  78.369 123.426  1.00 37.62           C  
ATOM   7659  N   VAL C  12      97.047  78.572 127.916  1.00 40.25           N  
ATOM   7660  CA  VAL C  12      96.460  78.933 129.202  1.00 40.25           C  
ATOM   7661  C   VAL C  12      97.529  79.463 130.152  1.00 40.25           C  
ATOM   7662  O   VAL C  12      97.241  80.300 131.015  1.00 40.25           O  
ATOM   7663  CB  VAL C  12      95.687  77.737 129.795  1.00 40.25           C  
ATOM   7664  CG1 VAL C  12      96.570  76.512 129.896  1.00 40.25           C  
ATOM   7665  CG2 VAL C  12      95.089  78.088 131.149  1.00 40.25           C  
ATOM   7666  N   LEU C  13      98.778  79.013 130.003  1.00 40.60           N  
ATOM   7667  CA  LEU C  13      99.851  79.538 130.840  1.00 40.60           C  
ATOM   7668  C   LEU C  13     100.152  80.996 130.507  1.00 40.60           C  
ATOM   7669  O   LEU C  13     100.349  81.821 131.410  1.00 40.60           O  
ATOM   7670  CB  LEU C  13     101.098  78.668 130.689  1.00 40.60           C  
ATOM   7671  CG  LEU C  13     102.322  79.044 131.521  1.00 40.60           C  
ATOM   7672  CD1 LEU C  13     102.000  78.920 132.990  1.00 40.60           C  
ATOM   7673  CD2 LEU C  13     103.473  78.131 131.170  1.00 40.60           C  
ATOM   7674  N   LEU C  14     100.173  81.344 129.219  1.00 36.95           N  
ATOM   7675  CA  LEU C  14     100.323  82.753 128.878  1.00 36.95           C  
ATOM   7676  C   LEU C  14      99.124  83.560 129.349  1.00 36.95           C  
ATOM   7677  O   LEU C  14      99.284  84.711 129.763  1.00 36.95           O  
ATOM   7678  CB  LEU C  14     100.520  82.946 127.378  1.00 36.95           C  
ATOM   7679  CG  LEU C  14     101.189  84.295 127.083  1.00 36.95           C  
ATOM   7680  CD1 LEU C  14     102.659  84.257 127.468  1.00 36.95           C  
ATOM   7681  CD2 LEU C  14     101.022  84.737 125.644  1.00 36.95           C  
ATOM   7682  N   SER C  15      97.924  82.977 129.308  1.00 38.25           N  
ATOM   7683  CA  SER C  15      96.749  83.690 129.803  1.00 38.25           C  
ATOM   7684  C   SER C  15      96.850  83.971 131.299  1.00 38.25           C  
ATOM   7685  O   SER C  15      96.533  85.079 131.751  1.00 38.25           O  
ATOM   7686  CB  SER C  15      95.485  82.893 129.494  1.00 38.25           C  
ATOM   7687  OG  SER C  15      95.160  82.970 128.119  1.00 38.25           O  
ATOM   7688  N   VAL C  16      97.293  82.985 132.085  1.00 41.71           N  
ATOM   7689  CA  VAL C  16      97.372  83.187 133.530  1.00 41.71           C  
ATOM   7690  C   VAL C  16      98.483  84.175 133.866  1.00 41.71           C  
ATOM   7691  O   VAL C  16      98.351  84.979 134.797  1.00 41.71           O  
ATOM   7692  CB  VAL C  16      97.536  81.849 134.282  1.00 41.71           C  
ATOM   7693  CG1 VAL C  16      98.718  81.069 133.785  1.00 41.71           C  
ATOM   7694  CG2 VAL C  16      97.650  82.081 135.780  1.00 41.71           C  
ATOM   7695  N   LEU C  17      99.593  84.141 133.121  1.00 40.72           N  
ATOM   7696  CA  LEU C  17     100.598  85.188 133.288  1.00 40.72           C  
ATOM   7697  C   LEU C  17     100.030  86.561 132.949  1.00 40.72           C  
ATOM   7698  O   LEU C  17     100.301  87.542 133.650  1.00 40.72           O  
ATOM   7699  CB  LEU C  17     101.827  84.898 132.429  1.00 40.72           C  
ATOM   7700  CG  LEU C  17     102.680  83.705 132.844  1.00 40.72           C  
ATOM   7701  CD1 LEU C  17     103.754  83.447 131.812  1.00 40.72           C  
ATOM   7702  CD2 LEU C  17     103.293  83.954 134.208  1.00 40.72           C  
ATOM   7703  N   GLN C  18      99.244  86.649 131.873  1.00 41.60           N  
ATOM   7704  CA  GLN C  18      98.683  87.929 131.454  1.00 41.60           C  
ATOM   7705  C   GLN C  18      97.762  88.499 132.524  1.00 41.60           C  
ATOM   7706  O   GLN C  18      97.814  89.696 132.827  1.00 41.60           O  
ATOM   7707  CB  GLN C  18      97.958  87.756 130.113  1.00 41.60           C  
ATOM   7708  CG  GLN C  18      97.357  89.017 129.458  1.00 41.60           C  
ATOM   7709  CD  GLN C  18      96.200  89.638 130.225  1.00 41.60           C  
ATOM   7710  OE1 GLN C  18      95.171  89.000 130.444  1.00 41.60           O  
ATOM   7711  NE2 GLN C  18      96.363  90.889 130.632  1.00 41.60           N  
ATOM   7712  N   GLN C  19      96.911  87.660 133.116  1.00 46.43           N  
ATOM   7713  CA  GLN C  19      95.977  88.193 134.101  1.00 46.43           C  
ATOM   7714  C   GLN C  19      96.651  88.535 135.423  1.00 46.43           C  
ATOM   7715  O   GLN C  19      96.024  89.183 136.268  1.00 46.43           O  
ATOM   7716  CB  GLN C  19      94.824  87.215 134.356  1.00 46.43           C  
ATOM   7717  CG  GLN C  19      95.245  85.812 134.728  1.00 46.43           C  
ATOM   7718  CD  GLN C  19      95.076  85.539 136.211  1.00 46.43           C  
ATOM   7719  OE1 GLN C  19      94.330  86.233 136.899  1.00 46.43           O  
ATOM   7720  NE2 GLN C  19      95.772  84.527 136.710  1.00 46.43           N  
ATOM   7721  N   LEU C  20      97.901  88.120 135.621  1.00 47.89           N  
ATOM   7722  CA  LEU C  20      98.693  88.527 136.776  1.00 47.89           C  
ATOM   7723  C   LEU C  20      99.511  89.788 136.513  1.00 47.89           C  
ATOM   7724  O   LEU C  20     100.419  90.092 137.295  1.00 47.89           O  
ATOM   7725  CB  LEU C  20      99.607  87.382 137.220  1.00 47.89           C  
ATOM   7726  CG  LEU C  20      98.873  86.180 137.824  1.00 47.89           C  
ATOM   7727  CD1 LEU C  20      99.829  85.229 138.527  1.00 47.89           C  
ATOM   7728  CD2 LEU C  20      97.788  86.647 138.780  1.00 47.89           C  
ATOM   7729  N   ARG C  21      99.218  90.504 135.422  1.00 49.27           N  
ATOM   7730  CA  ARG C  21      99.832  91.793 135.091  1.00 49.27           C  
ATOM   7731  C   ARG C  21     101.317  91.671 134.761  1.00 49.27           C  
ATOM   7732  O   ARG C  21     102.093  92.590 135.027  1.00 49.27           O  
ATOM   7733  CB  ARG C  21      99.620  92.824 136.206  1.00 49.27           C  
ATOM   7734  CG  ARG C  21      98.198  92.880 136.732  1.00 49.27           C  
ATOM   7735  CD  ARG C  21      98.047  93.933 137.811  1.00 49.27           C  
ATOM   7736  NE  ARG C  21      96.695  94.483 137.839  1.00 49.27           N  
ATOM   7737  CZ  ARG C  21      96.378  95.654 138.381  1.00 49.27           C  
ATOM   7738  NH1 ARG C  21      97.318  96.402 138.941  1.00 49.27           N  
ATOM   7739  NH2 ARG C  21      95.122  96.077 138.363  1.00 49.27           N  
ATOM   7740  N   VAL C  22     101.726  90.541 134.181  1.00 45.25           N  
ATOM   7741  CA  VAL C  22     103.101  90.402 133.708  1.00 45.25           C  
ATOM   7742  C   VAL C  22     103.372  91.346 132.543  1.00 45.25           C  
ATOM   7743  O   VAL C  22     104.489  91.856 132.392  1.00 45.25           O  
ATOM   7744  CB  VAL C  22     103.379  88.932 133.332  1.00 45.25           C  
ATOM   7745  CG1 VAL C  22     104.643  88.809 132.503  1.00 45.25           C  
ATOM   7746  CG2 VAL C  22     103.482  88.081 134.585  1.00 45.25           C  
ATOM   7747  N   GLU C  23     102.357  91.618 131.719  1.00 45.79           N  
ATOM   7748  CA  GLU C  23     102.534  92.458 130.539  1.00 45.79           C  
ATOM   7749  C   GLU C  23     102.834  93.913 130.877  1.00 45.79           C  
ATOM   7750  O   GLU C  23     103.202  94.672 129.975  1.00 45.79           O  
ATOM   7751  CB  GLU C  23     101.297  92.380 129.641  1.00 45.79           C  
ATOM   7752  CG  GLU C  23     100.147  93.267 130.073  1.00 45.79           C  
ATOM   7753  CD  GLU C  23      98.903  93.053 129.232  1.00 45.79           C  
ATOM   7754  OE1 GLU C  23      97.801  93.410 129.698  1.00 45.79           O  
ATOM   7755  OE2 GLU C  23      99.026  92.536 128.103  1.00 45.79           O  
ATOM   7756  N   SER C  24     102.684  94.321 132.135  1.00 45.98           N  
ATOM   7757  CA  SER C  24     103.091  95.654 132.562  1.00 45.98           C  
ATOM   7758  C   SER C  24     104.595  95.758 132.791  1.00 45.98           C  
ATOM   7759  O   SER C  24     105.068  96.797 133.262  1.00 45.98           O  
ATOM   7760  CB  SER C  24     102.341  96.056 133.834  1.00 45.98           C  
ATOM   7761  OG  SER C  24     103.005  95.579 134.991  1.00 45.98           O  
ATOM   7762  N   SER C  25     105.346  94.700 132.478  1.00 43.25           N  
ATOM   7763  CA  SER C  25     106.810  94.698 132.492  1.00 43.25           C  
ATOM   7764  C   SER C  25     107.244  94.202 131.116  1.00 43.25           C  
ATOM   7765  O   SER C  25     107.415  93.000 130.904  1.00 43.25           O  
ATOM   7766  CB  SER C  25     107.359  93.829 133.614  1.00 43.25           C  
ATOM   7767  OG  SER C  25     108.739  93.576 133.422  1.00 43.25           O  
ATOM   7768  N   SER C  26     107.418  95.143 130.184  1.00 39.13           N  
ATOM   7769  CA  SER C  26     107.575  94.789 128.776  1.00 39.13           C  
ATOM   7770  C   SER C  26     108.782  93.892 128.534  1.00 39.13           C  
ATOM   7771  O   SER C  26     108.752  93.047 127.632  1.00 39.13           O  
ATOM   7772  CB  SER C  26     107.683  96.057 127.931  1.00 39.13           C  
ATOM   7773  OG  SER C  26     109.019  96.523 127.875  1.00 39.13           O  
ATOM   7774  N   LYS C  27     109.844  94.051 129.327  1.00 40.82           N  
ATOM   7775  CA  LYS C  27     111.056  93.271 129.100  1.00 40.82           C  
ATOM   7776  C   LYS C  27     110.817  91.780 129.303  1.00 40.82           C  
ATOM   7777  O   LYS C  27     111.419  90.955 128.607  1.00 40.82           O  
ATOM   7778  CB  LYS C  27     112.173  93.766 130.018  1.00 40.82           C  
ATOM   7779  CG  LYS C  27     113.513  93.090 129.792  1.00 40.82           C  
ATOM   7780  CD  LYS C  27     114.652  94.079 129.946  1.00 40.82           C  
ATOM   7781  CE  LYS C  27     114.677  94.663 131.347  1.00 40.82           C  
ATOM   7782  NZ  LYS C  27     115.374  93.771 132.313  1.00 40.82           N  
ATOM   7783  N   LEU C  28     109.947  91.415 130.244  1.00 38.55           N  
ATOM   7784  CA  LEU C  28     109.608  90.015 130.474  1.00 38.55           C  
ATOM   7785  C   LEU C  28     108.460  89.558 129.584  1.00 38.55           C  
ATOM   7786  O   LEU C  28     108.451  88.410 129.123  1.00 38.55           O  
ATOM   7787  CB  LEU C  28     109.249  89.796 131.947  1.00 38.55           C  
ATOM   7788  CG  LEU C  28     108.898  88.377 132.403  1.00 38.55           C  
ATOM   7789  CD1 LEU C  28     109.855  87.353 131.808  1.00 38.55           C  
ATOM   7790  CD2 LEU C  28     108.884  88.286 133.918  1.00 38.55           C  
ATOM   7791  N   TRP C  29     107.483  90.436 129.350  1.00 35.96           N  
ATOM   7792  CA  TRP C  29     106.366  90.091 128.479  1.00 35.96           C  
ATOM   7793  C   TRP C  29     106.841  89.772 127.069  1.00 35.96           C  
ATOM   7794  O   TRP C  29     106.285  88.889 126.410  1.00 35.96           O  
ATOM   7795  CB  TRP C  29     105.341  91.224 128.457  1.00 35.96           C  
ATOM   7796  CG  TRP C  29     104.157  90.940 127.582  1.00 35.96           C  
ATOM   7797  CD1 TRP C  29     103.829  91.571 126.418  1.00 35.96           C  
ATOM   7798  CD2 TRP C  29     103.150  89.942 127.791  1.00 35.96           C  
ATOM   7799  NE1 TRP C  29     102.681  91.036 125.894  1.00 35.96           N  
ATOM   7800  CE2 TRP C  29     102.244  90.033 126.717  1.00 35.96           C  
ATOM   7801  CE3 TRP C  29     102.926  88.982 128.782  1.00 35.96           C  
ATOM   7802  CZ2 TRP C  29     101.134  89.203 126.606  1.00 35.96           C  
ATOM   7803  CZ3 TRP C  29     101.824  88.159 128.670  1.00 35.96           C  
ATOM   7804  CH2 TRP C  29     100.941  88.274 127.590  1.00 35.96           C  
ATOM   7805  N   ALA C  30     107.871  90.472 126.589  1.00 32.44           N  
ATOM   7806  CA  ALA C  30     108.394  90.172 125.260  1.00 32.44           C  
ATOM   7807  C   ALA C  30     108.910  88.740 125.170  1.00 32.44           C  
ATOM   7808  O   ALA C  30     108.647  88.045 124.181  1.00 32.44           O  
ATOM   7809  CB  ALA C  30     109.500  91.163 124.897  1.00 32.44           C  
ATOM   7810  N   GLN C  31     109.590  88.262 126.210  1.00 37.35           N  
ATOM   7811  CA  GLN C  31     110.097  86.895 126.223  1.00 37.35           C  
ATOM   7812  C   GLN C  31     108.995  85.870 126.437  1.00 37.35           C  
ATOM   7813  O   GLN C  31     109.059  84.774 125.868  1.00 37.35           O  
ATOM   7814  CB  GLN C  31     111.156  86.735 127.316  1.00 37.35           C  
ATOM   7815  CG  GLN C  31     112.427  87.519 127.061  1.00 37.35           C  
ATOM   7816  CD  GLN C  31     113.483  87.264 128.115  1.00 37.35           C  
ATOM   7817  OE1 GLN C  31     113.436  86.262 128.827  1.00 37.35           O  
ATOM   7818  NE2 GLN C  31     114.442  88.175 128.222  1.00 37.35           N  
ATOM   7819  N   CYS C  32     107.981  86.205 127.237  1.00 38.46           N  
ATOM   7820  CA  CYS C  32     106.825  85.322 127.363  1.00 38.46           C  
ATOM   7821  C   CYS C  32     106.135  85.134 126.017  1.00 38.46           C  
ATOM   7822  O   CYS C  32     105.793  84.010 125.632  1.00 38.46           O  
ATOM   7823  CB  CYS C  32     105.845  85.874 128.399  1.00 38.46           C  
ATOM   7824  SG  CYS C  32     106.554  86.173 130.030  1.00 38.46           S  
ATOM   7825  N   VAL C  33     105.925  86.231 125.285  1.00 32.29           N  
ATOM   7826  CA  VAL C  33     105.334  86.146 123.952  1.00 32.29           C  
ATOM   7827  C   VAL C  33     106.225  85.346 123.012  1.00 32.29           C  
ATOM   7828  O   VAL C  33     105.736  84.536 122.215  1.00 32.29           O  
ATOM   7829  CB  VAL C  33     105.045  87.552 123.400  1.00 32.29           C  
ATOM   7830  CG1 VAL C  33     104.342  87.452 122.080  1.00 32.29           C  
ATOM   7831  CG2 VAL C  33     104.156  88.305 124.354  1.00 32.29           C  
ATOM   7832  N   GLN C  34     107.540  85.570 123.072  1.00 36.21           N  
ATOM   7833  CA  GLN C  34     108.447  84.818 122.210  1.00 36.21           C  
ATOM   7834  C   GLN C  34     108.333  83.322 122.466  1.00 36.21           C  
ATOM   7835  O   GLN C  34     108.218  82.530 121.523  1.00 36.21           O  
ATOM   7836  CB  GLN C  34     109.885  85.290 122.425  1.00 36.21           C  
ATOM   7837  CG  GLN C  34     110.903  84.619 121.521  1.00 36.21           C  
ATOM   7838  CD  GLN C  34     111.000  85.278 120.161  1.00 36.21           C  
ATOM   7839  OE1 GLN C  34     110.599  86.428 119.985  1.00 36.21           O  
ATOM   7840  NE2 GLN C  34     111.534  84.550 119.189  1.00 36.21           N  
ATOM   7841  N   LEU C  35     108.326  82.919 123.739  1.00 38.08           N  
ATOM   7842  CA  LEU C  35     108.228  81.501 124.069  1.00 38.08           C  
ATOM   7843  C   LEU C  35     106.882  80.923 123.656  1.00 38.08           C  
ATOM   7844  O   LEU C  35     106.821  79.818 123.112  1.00 38.08           O  
ATOM   7845  CB  LEU C  35     108.456  81.297 125.565  1.00 38.08           C  
ATOM   7846  CG  LEU C  35     109.903  81.327 126.060  1.00 38.08           C  
ATOM   7847  CD1 LEU C  35     109.945  81.529 127.562  1.00 38.08           C  
ATOM   7848  CD2 LEU C  35     110.613  80.047 125.678  1.00 38.08           C  
ATOM   7849  N   HIS C  36     105.793  81.651 123.908  1.00 35.51           N  
ATOM   7850  CA  HIS C  36     104.463  81.187 123.520  1.00 35.51           C  
ATOM   7851  C   HIS C  36     104.363  80.963 122.014  1.00 35.51           C  
ATOM   7852  O   HIS C  36     103.914  79.900 121.558  1.00 35.51           O  
ATOM   7853  CB  HIS C  36     103.428  82.197 124.026  1.00 35.51           C  
ATOM   7854  CG  HIS C  36     102.030  81.963 123.543  1.00 35.51           C  
ATOM   7855  ND1 HIS C  36     100.963  81.846 124.405  1.00 35.51           N  
ATOM   7856  CD2 HIS C  36     101.502  81.967 122.296  1.00 35.51           C  
ATOM   7857  CE1 HIS C  36      99.849  81.703 123.710  1.00 35.51           C  
ATOM   7858  NE2 HIS C  36     100.148  81.779 122.427  1.00 35.51           N  
ATOM   7859  N   ASN C  37     104.782  81.952 121.224  1.00 35.14           N  
ATOM   7860  CA  ASN C  37     104.712  81.809 119.775  1.00 35.14           C  
ATOM   7861  C   ASN C  37     105.637  80.704 119.277  1.00 35.14           C  
ATOM   7862  O   ASN C  37     105.287  79.968 118.347  1.00 35.14           O  
ATOM   7863  CB  ASN C  37     105.034  83.137 119.099  1.00 35.14           C  
ATOM   7864  CG  ASN C  37     104.127  84.256 119.562  1.00 35.14           C  
ATOM   7865  OD1 ASN C  37     104.536  85.411 119.645  1.00 35.14           O  
ATOM   7866  ND2 ASN C  37     102.885  83.916 119.873  1.00 35.14           N  
ATOM   7867  N   ASP C  38     106.821  80.568 119.881  1.00 41.41           N  
ATOM   7868  CA  ASP C  38     107.720  79.488 119.489  1.00 41.41           C  
ATOM   7869  C   ASP C  38     107.113  78.123 119.782  1.00 41.41           C  
ATOM   7870  O   ASP C  38     107.227  77.203 118.964  1.00 41.41           O  
ATOM   7871  CB  ASP C  38     109.064  79.642 120.197  1.00 41.41           C  
ATOM   7872  CG  ASP C  38     109.932  80.714 119.571  1.00 41.41           C  
ATOM   7873  OD1 ASP C  38     109.709  81.040 118.386  1.00 41.41           O  
ATOM   7874  OD2 ASP C  38     110.843  81.223 120.258  1.00 41.41           O  
ATOM   7875  N   ILE C  39     106.475  77.966 120.944  1.00 38.23           N  
ATOM   7876  CA  ILE C  39     105.822  76.700 121.263  1.00 38.23           C  
ATOM   7877  C   ILE C  39     104.733  76.394 120.249  1.00 38.23           C  
ATOM   7878  O   ILE C  39     104.625  75.263 119.760  1.00 38.23           O  
ATOM   7879  CB  ILE C  39     105.258  76.718 122.697  1.00 38.23           C  
ATOM   7880  CG1 ILE C  39     106.377  76.886 123.724  1.00 38.23           C  
ATOM   7881  CG2 ILE C  39     104.465  75.452 122.972  1.00 38.23           C  
ATOM   7882  CD1 ILE C  39     105.876  77.287 125.096  1.00 38.23           C  
ATOM   7883  N   LEU C  40     103.913  77.391 119.908  1.00 31.79           N  
ATOM   7884  CA  LEU C  40     102.831  77.114 118.968  1.00 31.79           C  
ATOM   7885  C   LEU C  40     103.352  76.823 117.567  1.00 31.79           C  
ATOM   7886  O   LEU C  40     102.727  76.058 116.826  1.00 31.79           O  
ATOM   7887  CB  LEU C  40     101.835  78.267 118.919  1.00 31.79           C  
ATOM   7888  CG  LEU C  40     101.130  78.680 120.205  1.00 31.79           C  
ATOM   7889  CD1 LEU C  40     100.339  79.923 119.916  1.00 31.79           C  
ATOM   7890  CD2 LEU C  40     100.235  77.580 120.726  1.00 31.79           C  
ATOM   7891  N   LEU C  41     104.480  77.413 117.183  1.00 37.08           N  
ATOM   7892  CA  LEU C  41     105.033  77.176 115.857  1.00 37.08           C  
ATOM   7893  C   LEU C  41     105.903  75.928 115.780  1.00 37.08           C  
ATOM   7894  O   LEU C  41     106.244  75.497 114.672  1.00 37.08           O  
ATOM   7895  CB  LEU C  41     105.841  78.392 115.404  1.00 37.08           C  
ATOM   7896  CG  LEU C  41     104.996  79.556 114.891  1.00 37.08           C  
ATOM   7897  CD1 LEU C  41     105.812  80.831 114.860  1.00 37.08           C  
ATOM   7898  CD2 LEU C  41     104.434  79.240 113.518  1.00 37.08           C  
ATOM   7899  N   ALA C  42     106.267  75.344 116.918  1.00 44.24           N  
ATOM   7900  CA  ALA C  42     107.108  74.157 116.929  1.00 44.24           C  
ATOM   7901  C   ALA C  42     106.396  72.973 116.285  1.00 44.24           C  
ATOM   7902  O   ALA C  42     105.169  72.852 116.336  1.00 44.24           O  
ATOM   7903  CB  ALA C  42     107.512  73.805 118.360  1.00 44.24           C  
ATOM   7904  N   LYS C  43     107.188  72.093 115.674  1.00 50.32           N  
ATOM   7905  CA  LYS C  43     106.692  70.848 115.104  1.00 50.32           C  
ATOM   7906  C   LYS C  43     107.309  69.619 115.755  1.00 50.32           C  
ATOM   7907  O   LYS C  43     107.011  68.497 115.332  1.00 50.32           O  
ATOM   7908  CB  LYS C  43     106.955  70.812 113.593  1.00 50.32           C  
ATOM   7909  CG  LYS C  43     105.779  71.264 112.747  1.00 50.32           C  
ATOM   7910  CD  LYS C  43     105.994  70.924 111.286  1.00 50.32           C  
ATOM   7911  CE  LYS C  43     107.259  71.582 110.757  1.00 50.32           C  
ATOM   7912  NZ  LYS C  43     107.068  73.031 110.483  1.00 50.32           N  
ATOM   7913  N   ASP C  44     108.156  69.798 116.767  1.00 58.14           N  
ATOM   7914  CA  ASP C  44     108.755  68.703 117.514  1.00 58.14           C  
ATOM   7915  C   ASP C  44     108.495  68.945 118.993  1.00 58.14           C  
ATOM   7916  O   ASP C  44     108.603  70.078 119.471  1.00 58.14           O  
ATOM   7917  CB  ASP C  44     110.265  68.594 117.237  1.00 58.14           C  
ATOM   7918  CG  ASP C  44     111.001  67.758 118.272  1.00 58.14           C  
ATOM   7919  OD1 ASP C  44     110.400  66.822 118.841  1.00 58.14           O  
ATOM   7920  OD2 ASP C  44     112.205  68.012 118.486  1.00 58.14           O  
ATOM   7921  N   THR C  45     108.144  67.880 119.713  1.00 57.05           N  
ATOM   7922  CA  THR C  45     107.740  68.025 121.106  1.00 57.05           C  
ATOM   7923  C   THR C  45     108.908  68.275 122.054  1.00 57.05           C  
ATOM   7924  O   THR C  45     108.672  68.726 123.177  1.00 57.05           O  
ATOM   7925  CB  THR C  45     106.965  66.788 121.562  1.00 57.05           C  
ATOM   7926  OG1 THR C  45     106.546  66.959 122.920  1.00 57.05           O  
ATOM   7927  CG2 THR C  45     107.834  65.546 121.459  1.00 57.05           C  
ATOM   7928  N   THR C  46     110.150  68.012 121.642  1.00 59.05           N  
ATOM   7929  CA  THR C  46     111.282  68.230 122.541  1.00 59.05           C  
ATOM   7930  C   THR C  46     111.568  69.717 122.730  1.00 59.05           C  
ATOM   7931  O   THR C  46     111.695  70.196 123.866  1.00 59.05           O  
ATOM   7932  CB  THR C  46     112.523  67.511 122.010  1.00 59.05           C  
ATOM   7933  OG1 THR C  46     112.337  66.093 122.109  1.00 59.05           O  
ATOM   7934  CG2 THR C  46     113.755  67.910 122.807  1.00 59.05           C  
ATOM   7935  N   GLU C  47     111.665  70.463 121.628  1.00 57.94           N  
ATOM   7936  CA  GLU C  47     111.821  71.908 121.738  1.00 57.94           C  
ATOM   7937  C   GLU C  47     110.601  72.539 122.390  1.00 57.94           C  
ATOM   7938  O   GLU C  47     110.731  73.506 123.152  1.00 57.94           O  
ATOM   7939  CB  GLU C  47     112.084  72.519 120.359  1.00 57.94           C  
ATOM   7940  CG  GLU C  47     110.970  72.311 119.344  1.00 57.94           C  
ATOM   7941  CD  GLU C  47     111.233  73.024 118.030  1.00 57.94           C  
ATOM   7942  OE1 GLU C  47     110.943  72.438 116.966  1.00 57.94           O  
ATOM   7943  OE2 GLU C  47     111.730  74.169 118.062  1.00 57.94           O  
ATOM   7944  N   ALA C  48     109.413  71.991 122.124  1.00 54.38           N  
ATOM   7945  CA  ALA C  48     108.203  72.496 122.759  1.00 54.38           C  
ATOM   7946  C   ALA C  48     108.260  72.310 124.269  1.00 54.38           C  
ATOM   7947  O   ALA C  48     107.909  73.219 125.023  1.00 54.38           O  
ATOM   7948  CB  ALA C  48     106.972  71.804 122.173  1.00 54.38           C  
ATOM   7949  N   PHE C  49     108.710  71.140 124.730  1.00 57.84           N  
ATOM   7950  CA  PHE C  49     108.846  70.912 126.165  1.00 57.84           C  
ATOM   7951  C   PHE C  49     109.894  71.825 126.784  1.00 57.84           C  
ATOM   7952  O   PHE C  49     109.682  72.375 127.872  1.00 57.84           O  
ATOM   7953  CB  PHE C  49     109.187  69.449 126.442  1.00 57.84           C  
ATOM   7954  CG  PHE C  49     107.998  68.605 126.790  1.00 57.84           C  
ATOM   7955  CD1 PHE C  49     107.597  68.472 128.107  1.00 57.84           C  
ATOM   7956  CD2 PHE C  49     107.281  67.945 125.808  1.00 57.84           C  
ATOM   7957  CE1 PHE C  49     106.507  67.696 128.440  1.00 57.84           C  
ATOM   7958  CE2 PHE C  49     106.188  67.166 126.135  1.00 57.84           C  
ATOM   7959  CZ  PHE C  49     105.800  67.042 127.452  1.00 57.84           C  
ATOM   7960  N   GLU C  50     111.043  71.984 126.121  1.00 52.90           N  
ATOM   7961  CA  GLU C  50     112.081  72.850 126.672  1.00 52.90           C  
ATOM   7962  C   GLU C  50     111.581  74.284 126.815  1.00 52.90           C  
ATOM   7963  O   GLU C  50     111.748  74.913 127.870  1.00 52.90           O  
ATOM   7964  CB  GLU C  50     113.328  72.800 125.791  1.00 52.90           C  
ATOM   7965  N   LYS C  51     110.919  74.802 125.781  1.00 51.17           N  
ATOM   7966  CA  LYS C  51     110.431  76.173 125.844  1.00 51.17           C  
ATOM   7967  C   LYS C  51     109.248  76.296 126.799  1.00 51.17           C  
ATOM   7968  O   LYS C  51     109.080  77.331 127.451  1.00 51.17           O  
ATOM   7969  CB  LYS C  51     110.077  76.655 124.437  1.00 51.17           C  
ATOM   7970  CG  LYS C  51     111.319  76.986 123.614  1.00 51.17           C  
ATOM   7971  CD  LYS C  51     111.042  77.049 122.124  1.00 51.17           C  
ATOM   7972  CE  LYS C  51     112.000  78.010 121.439  1.00 51.17           C  
ATOM   7973  NZ  LYS C  51     111.871  77.968 119.956  1.00 51.17           N  
ATOM   7974  N   MET C  52     108.442  75.239 126.922  1.00 51.38           N  
ATOM   7975  CA  MET C  52     107.322  75.247 127.856  1.00 51.38           C  
ATOM   7976  C   MET C  52     107.807  75.311 129.299  1.00 51.38           C  
ATOM   7977  O   MET C  52     107.255  76.055 130.115  1.00 51.38           O  
ATOM   7978  CB  MET C  52     106.454  74.008 127.627  1.00 51.38           C  
ATOM   7979  CG  MET C  52     105.365  73.779 128.664  1.00 51.38           C  
ATOM   7980  SD  MET C  52     104.439  75.270 129.074  1.00 51.38           S  
ATOM   7981  CE  MET C  52     103.067  74.569 129.983  1.00 51.38           C  
ATOM   7982  N   VAL C  53     108.828  74.521 129.642  1.00 52.26           N  
ATOM   7983  CA  VAL C  53     109.360  74.576 131.004  1.00 52.26           C  
ATOM   7984  C   VAL C  53     110.065  75.906 131.248  1.00 52.26           C  
ATOM   7985  O   VAL C  53     109.986  76.471 132.348  1.00 52.26           O  
ATOM   7986  CB  VAL C  53     110.269  73.365 131.298  1.00 52.26           C  
ATOM   7987  CG1 VAL C  53     109.523  72.065 131.033  1.00 52.26           C  
ATOM   7988  CG2 VAL C  53     111.558  73.415 130.501  1.00 52.26           C  
ATOM   7989  N   SER C  54     110.747  76.441 130.229  1.00 49.14           N  
ATOM   7990  CA  SER C  54     111.332  77.773 130.367  1.00 49.14           C  
ATOM   7991  C   SER C  54     110.256  78.820 130.639  1.00 49.14           C  
ATOM   7992  O   SER C  54     110.466  79.751 131.425  1.00 49.14           O  
ATOM   7993  CB  SER C  54     112.122  78.131 129.109  1.00 49.14           C  
ATOM   7994  OG  SER C  54     113.082  77.134 128.809  1.00 49.14           O  
ATOM   7995  N   LEU C  55     109.096  78.681 129.994  1.00 47.68           N  
ATOM   7996  CA  LEU C  55     108.001  79.624 130.196  1.00 47.68           C  
ATOM   7997  C   LEU C  55     107.361  79.437 131.569  1.00 47.68           C  
ATOM   7998  O   LEU C  55     106.999  80.415 132.233  1.00 47.68           O  
ATOM   7999  CB  LEU C  55     106.970  79.442 129.080  1.00 47.68           C  
ATOM   8000  CG  LEU C  55     105.612  80.150 129.105  1.00 47.68           C  
ATOM   8001  CD1 LEU C  55     105.741  81.602 129.529  1.00 47.68           C  
ATOM   8002  CD2 LEU C  55     104.928  80.037 127.754  1.00 47.68           C  
ATOM   8003  N   LEU C  56     107.211  78.185 132.005  1.00 50.61           N  
ATOM   8004  CA  LEU C  56     106.608  77.897 133.302  1.00 50.61           C  
ATOM   8005  C   LEU C  56     107.494  78.373 134.446  1.00 50.61           C  
ATOM   8006  O   LEU C  56     106.990  78.703 135.527  1.00 50.61           O  
ATOM   8007  CB  LEU C  56     106.331  76.397 133.422  1.00 50.61           C  
ATOM   8008  CG  LEU C  56     105.663  75.859 134.690  1.00 50.61           C  
ATOM   8009  CD1 LEU C  56     104.511  76.752 135.126  1.00 50.61           C  
ATOM   8010  CD2 LEU C  56     105.186  74.431 134.477  1.00 50.61           C  
ATOM   8011  N   SER C  57     108.814  78.387 134.237  1.00 51.76           N  
ATOM   8012  CA  SER C  57     109.717  78.940 135.241  1.00 51.76           C  
ATOM   8013  C   SER C  57     109.374  80.387 135.569  1.00 51.76           C  
ATOM   8014  O   SER C  57     109.592  80.834 136.701  1.00 51.76           O  
ATOM   8015  CB  SER C  57     111.164  78.833 134.759  1.00 51.76           C  
ATOM   8016  OG  SER C  57     112.025  79.638 135.545  1.00 51.76           O  
ATOM   8017  N   VAL C  58     108.834  81.131 134.600  1.00 52.91           N  
ATOM   8018  CA  VAL C  58     108.455  82.518 134.848  1.00 52.91           C  
ATOM   8019  C   VAL C  58     107.323  82.592 135.866  1.00 52.91           C  
ATOM   8020  O   VAL C  58     107.350  83.420 136.784  1.00 52.91           O  
ATOM   8021  CB  VAL C  58     108.075  83.209 133.526  1.00 52.91           C  
ATOM   8022  CG1 VAL C  58     107.558  84.615 133.788  1.00 52.91           C  
ATOM   8023  CG2 VAL C  58     109.266  83.238 132.580  1.00 52.91           C  
ATOM   8024  N   LEU C  59     106.309  81.736 135.720  1.00 53.96           N  
ATOM   8025  CA  LEU C  59     105.236  81.695 136.708  1.00 53.96           C  
ATOM   8026  C   LEU C  59     105.747  81.184 138.048  1.00 53.96           C  
ATOM   8027  O   LEU C  59     105.352  81.689 139.105  1.00 53.96           O  
ATOM   8028  CB  LEU C  59     104.087  80.820 136.205  1.00 53.96           C  
ATOM   8029  CG  LEU C  59     102.859  80.701 137.115  1.00 53.96           C  
ATOM   8030  CD1 LEU C  59     102.471  82.053 137.701  1.00 53.96           C  
ATOM   8031  CD2 LEU C  59     101.687  80.080 136.377  1.00 53.96           C  
ATOM   8032  N   LEU C  60     106.628  80.182 138.022  1.00 56.86           N  
ATOM   8033  CA  LEU C  60     107.148  79.625 139.266  1.00 56.86           C  
ATOM   8034  C   LEU C  60     107.989  80.637 140.033  1.00 56.86           C  
ATOM   8035  O   LEU C  60     108.073  80.562 141.264  1.00 56.86           O  
ATOM   8036  CB  LEU C  60     107.965  78.366 138.979  1.00 56.86           C  
ATOM   8037  CG  LEU C  60     107.164  77.089 138.717  1.00 56.86           C  
ATOM   8038  CD1 LEU C  60     108.067  75.866 138.765  1.00 56.86           C  
ATOM   8039  CD2 LEU C  60     106.022  76.957 139.714  1.00 56.86           C  
ATOM   8040  N   SER C  61     108.623  81.579 139.332  1.00 59.05           N  
ATOM   8041  CA  SER C  61     109.479  82.550 140.004  1.00 59.05           C  
ATOM   8042  C   SER C  61     108.670  83.467 140.914  1.00 59.05           C  
ATOM   8043  O   SER C  61     109.010  83.649 142.088  1.00 59.05           O  
ATOM   8044  CB  SER C  61     110.255  83.364 138.970  1.00 59.05           C  
ATOM   8045  OG  SER C  61     110.965  82.515 138.084  1.00 59.05           O  
ATOM   8046  N   MET C  62     107.597  84.056 140.392  1.00 60.96           N  
ATOM   8047  CA  MET C  62     106.740  84.896 141.214  1.00 60.96           C  
ATOM   8048  C   MET C  62     105.771  84.024 142.014  1.00 60.96           C  
ATOM   8049  O   MET C  62     105.729  82.798 141.873  1.00 60.96           O  
ATOM   8050  CB  MET C  62     106.014  85.925 140.350  1.00 60.96           C  
ATOM   8051  CG  MET C  62     105.492  85.399 139.029  1.00 60.96           C  
ATOM   8052  SD  MET C  62     104.801  86.729 138.027  1.00 60.96           S  
ATOM   8053  CE  MET C  62     103.085  86.671 138.514  1.00 60.96           C  
ATOM   8054  N   GLN C  63     104.973  84.673 142.867  1.00 62.39           N  
ATOM   8055  CA  GLN C  63     104.178  83.944 143.850  1.00 62.39           C  
ATOM   8056  C   GLN C  63     103.126  83.045 143.212  1.00 62.39           C  
ATOM   8057  O   GLN C  63     102.748  82.036 143.816  1.00 62.39           O  
ATOM   8058  CB  GLN C  63     103.492  84.910 144.825  1.00 62.39           C  
ATOM   8059  CG  GLN C  63     104.403  85.700 145.782  1.00 62.39           C  
ATOM   8060  CD  GLN C  63     105.642  86.281 145.129  1.00 62.39           C  
ATOM   8061  OE1 GLN C  63     105.548  87.080 144.198  1.00 62.39           O  
ATOM   8062  NE2 GLN C  63     106.810  85.883 145.616  1.00 62.39           N  
ATOM   8063  N   GLY C  64     102.660  83.372 142.011  1.00 56.93           N  
ATOM   8064  CA  GLY C  64     101.663  82.559 141.339  1.00 56.93           C  
ATOM   8065  C   GLY C  64     100.346  82.464 142.086  1.00 56.93           C  
ATOM   8066  O   GLY C  64     100.027  83.311 142.921  1.00 56.93           O  
TER    8067      GLY C  64                                                      
ATOM   8068  P     G P  10      57.869  85.578 101.156  1.00143.84           P  
ATOM   8069  OP1   G P  10      58.763  85.788  99.989  1.00143.84           O  
ATOM   8070  OP2   G P  10      57.821  84.250 101.818  1.00143.84           O  
ATOM   8071  O5'   G P  10      58.250  86.667 102.253  1.00143.84           O  
ATOM   8072  C5'   G P  10      57.303  87.093 103.228  1.00143.84           C  
ATOM   8073  C4'   G P  10      57.405  88.576 103.485  1.00143.84           C  
ATOM   8074  O4'   G P  10      56.875  88.866 104.807  1.00143.84           O  
ATOM   8075  C3'   G P  10      58.824  89.133 103.469  1.00143.84           C  
ATOM   8076  O3'   G P  10      58.789  90.483 103.012  1.00143.84           O  
ATOM   8077  C2'   G P  10      59.207  89.099 104.943  1.00143.84           C  
ATOM   8078  O2'   G P  10      60.238  89.992 105.304  1.00143.84           O  
ATOM   8079  C1'   G P  10      57.882  89.455 105.611  1.00143.84           C  
ATOM   8080  N9    G P  10      57.740  88.915 106.964  1.00143.84           N  
ATOM   8081  C8    G P  10      58.119  87.661 107.377  1.00143.84           C  
ATOM   8082  N7    G P  10      57.868  87.438 108.636  1.00143.84           N  
ATOM   8083  C5    G P  10      57.287  88.616 109.080  1.00143.84           C  
ATOM   8084  C6    G P  10      56.806  88.962 110.365  1.00143.84           C  
ATOM   8085  O6    G P  10      56.801  88.272 111.389  1.00143.84           O  
ATOM   8086  N1    G P  10      56.293  90.253 110.390  1.00143.84           N  
ATOM   8087  C2    G P  10      56.247  91.107 109.315  1.00143.84           C  
ATOM   8088  N2    G P  10      55.712  92.316 109.544  1.00143.84           N  
ATOM   8089  N3    G P  10      56.693  90.795 108.107  1.00143.84           N  
ATOM   8090  C4    G P  10      57.197  89.542 108.062  1.00143.84           C  
ATOM   8091  P     A P  11      60.116  91.177 102.435  1.00136.84           P  
ATOM   8092  OP1   A P  11      59.714  92.196 101.432  1.00136.84           O  
ATOM   8093  OP2   A P  11      61.066  90.101 102.053  1.00136.84           O  
ATOM   8094  O5'   A P  11      60.714  91.941 103.698  1.00136.84           O  
ATOM   8095  C5'   A P  11      61.656  92.989 103.540  1.00136.84           C  
ATOM   8096  C4'   A P  11      61.330  94.154 104.439  1.00136.84           C  
ATOM   8097  O4'   A P  11      60.168  93.843 105.248  1.00136.84           O  
ATOM   8098  C3'   A P  11      62.399  94.532 105.451  1.00136.84           C  
ATOM   8099  O3'   A P  11      63.416  95.340 104.882  1.00136.84           O  
ATOM   8100  C2'   A P  11      61.599  95.236 106.541  1.00136.84           C  
ATOM   8101  O2'   A P  11      61.333  96.582 106.177  1.00136.84           O  
ATOM   8102  C1'   A P  11      60.281  94.459 106.513  1.00136.84           C  
ATOM   8103  N9    A P  11      60.201  93.418 107.557  1.00136.84           N  
ATOM   8104  C8    A P  11      60.196  92.058 107.377  1.00136.84           C  
ATOM   8105  N7    A P  11      60.098  91.370 108.487  1.00136.84           N  
ATOM   8106  C5    A P  11      60.025  92.343 109.471  1.00136.84           C  
ATOM   8107  C6    A P  11      59.909  92.263 110.869  1.00136.84           C  
ATOM   8108  N6    A P  11      59.844  91.111 111.541  1.00136.84           N  
ATOM   8109  N1    A P  11      59.863  93.421 111.564  1.00136.84           N  
ATOM   8110  C2    A P  11      59.928  94.575 110.888  1.00136.84           C  
ATOM   8111  N3    A P  11      60.038  94.780 109.576  1.00136.84           N  
ATOM   8112  C4    A P  11      60.082  93.610 108.914  1.00136.84           C  
ATOM   8113  P     U P  12      64.816  95.541 105.642  1.00123.44           P  
ATOM   8114  OP1   U P  12      65.776  96.158 104.691  1.00123.44           O  
ATOM   8115  OP2   U P  12      65.163  94.262 106.311  1.00123.44           O  
ATOM   8116  O5'   U P  12      64.489  96.618 106.768  1.00123.44           O  
ATOM   8117  C5'   U P  12      65.427  96.900 107.793  1.00123.44           C  
ATOM   8118  C4'   U P  12      64.774  97.572 108.974  1.00123.44           C  
ATOM   8119  O4'   U P  12      63.500  96.938 109.263  1.00123.44           O  
ATOM   8120  C3'   U P  12      65.543  97.482 110.282  1.00123.44           C  
ATOM   8121  O3'   U P  12      66.566  98.456 110.387  1.00123.44           O  
ATOM   8122  C2'   U P  12      64.449  97.632 111.327  1.00123.44           C  
ATOM   8123  O2'   U P  12      64.082  98.996 111.475  1.00123.44           O  
ATOM   8124  C1'   U P  12      63.289  96.892 110.659  1.00123.44           C  
ATOM   8125  N1    U P  12      63.200  95.467 111.064  1.00123.44           N  
ATOM   8126  C2    U P  12      63.077  95.110 112.402  1.00123.44           C  
ATOM   8127  O2    U P  12      63.054  95.898 113.334  1.00123.44           O  
ATOM   8128  N3    U P  12      62.996  93.759 112.632  1.00123.44           N  
ATOM   8129  C4    U P  12      63.011  92.746 111.697  1.00123.44           C  
ATOM   8130  O4    U P  12      62.926  91.576 112.071  1.00123.44           O  
ATOM   8131  C5    U P  12      63.128  93.192 110.345  1.00123.44           C  
ATOM   8132  C6    U P  12      63.212  94.500 110.086  1.00123.44           C  
ATOM   8133  P     U P  13      68.045  98.025 110.838  1.00101.07           P  
ATOM   8134  OP1   U P  13      68.916  99.226 110.783  1.00101.07           O  
ATOM   8135  OP2   U P  13      68.421  96.814 110.068  1.00101.07           O  
ATOM   8136  O5'   U P  13      67.872  97.605 112.365  1.00101.07           O  
ATOM   8137  C5'   U P  13      67.471  98.553 113.342  1.00101.07           C  
ATOM   8138  C4'   U P  13      67.322  97.913 114.699  1.00101.07           C  
ATOM   8139  O4'   U P  13      66.160  97.046 114.705  1.00101.07           O  
ATOM   8140  C3'   U P  13      68.467  97.009 115.132  1.00101.07           C  
ATOM   8141  O3'   U P  13      69.554  97.729 115.685  1.00101.07           O  
ATOM   8142  C2'   U P  13      67.797  96.067 116.122  1.00101.07           C  
ATOM   8143  O2'   U P  13      67.654  96.690 117.390  1.00101.07           O  
ATOM   8144  C1'   U P  13      66.409  95.909 115.503  1.00101.07           C  
ATOM   8145  N1    U P  13      66.297  94.705 114.648  1.00101.07           N  
ATOM   8146  C2    U P  13      66.193  93.476 115.264  1.00101.07           C  
ATOM   8147  O2    U P  13      66.202  93.327 116.473  1.00101.07           O  
ATOM   8148  N3    U P  13      66.082  92.417 114.404  1.00101.07           N  
ATOM   8149  C4    U P  13      66.060  92.448 113.028  1.00101.07           C  
ATOM   8150  O4    U P  13      65.953  91.393 112.400  1.00101.07           O  
ATOM   8151  C5    U P  13      66.167  93.757 112.466  1.00101.07           C  
ATOM   8152  C6    U P  13      66.276  94.812 113.278  1.00101.07           C  
ATOM   8153  P     A P  14      71.058  97.206 115.482  1.00 68.16           P  
ATOM   8154  OP1   A P  14      71.981  98.274 115.942  1.00 68.16           O  
ATOM   8155  OP2   A P  14      71.174  96.679 114.098  1.00 68.16           O  
ATOM   8156  O5'   A P  14      71.181  95.980 116.493  1.00 68.16           O  
ATOM   8157  C5'   A P  14      70.979  96.159 117.887  1.00 68.16           C  
ATOM   8158  C4'   A P  14      70.955  94.839 118.616  1.00 68.16           C  
ATOM   8159  O4'   A P  14      69.835  94.041 118.159  1.00 68.16           O  
ATOM   8160  C3'   A P  14      72.162  93.941 118.404  1.00 68.16           C  
ATOM   8161  O3'   A P  14      73.257  94.303 119.225  1.00 68.16           O  
ATOM   8162  C2'   A P  14      71.608  92.553 118.706  1.00 68.16           C  
ATOM   8163  O2'   A P  14      71.558  92.328 120.108  1.00 68.16           O  
ATOM   8164  C1'   A P  14      70.174  92.670 118.189  1.00 68.16           C  
ATOM   8165  N9    A P  14      69.992  92.107 116.837  1.00 68.16           N  
ATOM   8166  C8    A P  14      69.964  92.795 115.650  1.00 68.16           C  
ATOM   8167  N7    A P  14      69.762  92.035 114.602  1.00 68.16           N  
ATOM   8168  C5    A P  14      69.645  90.759 115.131  1.00 68.16           C  
ATOM   8169  C6    A P  14      69.422  89.510 114.528  1.00 68.16           C  
ATOM   8170  N6    A P  14      69.276  89.358 113.212  1.00 68.16           N  
ATOM   8171  N1    A P  14      69.357  88.414 115.321  1.00 68.16           N  
ATOM   8172  C2    A P  14      69.505  88.600 116.642  1.00 68.16           C  
ATOM   8173  N3    A P  14      69.718  89.724 117.327  1.00 68.16           N  
ATOM   8174  C4    A P  14      69.781  90.786 116.505  1.00 68.16           C  
ATOM   8175  P     A P  15      74.762  94.008 118.751  1.00 44.26           P  
ATOM   8176  OP1   A P  15      75.677  94.695 119.696  1.00 44.26           O  
ATOM   8177  OP2   A P  15      74.857  94.288 117.296  1.00 44.26           O  
ATOM   8178  O5'   A P  15      74.932  92.440 118.967  1.00 44.26           O  
ATOM   8179  C5'   A P  15      74.837  91.868 120.263  1.00 44.26           C  
ATOM   8180  C4'   A P  15      74.703  90.369 120.189  1.00 44.26           C  
ATOM   8181  O4'   A P  15      73.486  90.024 119.483  1.00 44.26           O  
ATOM   8182  C3'   A P  15      75.795  89.644 119.420  1.00 44.26           C  
ATOM   8183  O3'   A P  15      76.959  89.427 120.197  1.00 44.26           O  
ATOM   8184  C2'   A P  15      75.104  88.358 118.988  1.00 44.26           C  
ATOM   8185  O2'   A P  15      75.064  87.430 120.060  1.00 44.26           O  
ATOM   8186  C1'   A P  15      73.682  88.847 118.730  1.00 44.26           C  
ATOM   8187  N9    A P  15      73.431  89.145 117.309  1.00 44.26           N  
ATOM   8188  C8    A P  15      73.326  90.371 116.704  1.00 44.26           C  
ATOM   8189  N7    A P  15      73.080  90.306 115.419  1.00 44.26           N  
ATOM   8190  C5    A P  15      73.013  88.945 115.166  1.00 44.26           C  
ATOM   8191  C6    A P  15      72.787  88.215 113.993  1.00 44.26           C  
ATOM   8192  N6    A P  15      72.567  88.781 112.807  1.00 44.26           N  
ATOM   8193  N1    A P  15      72.788  86.868 114.083  1.00 44.26           N  
ATOM   8194  C2    A P  15      73.008  86.305 115.276  1.00 44.26           C  
ATOM   8195  N3    A P  15      73.235  86.884 116.449  1.00 44.26           N  
ATOM   8196  C4    A P  15      73.226  88.219 116.321  1.00 44.26           C  
ATOM   8197  P     G P  16      78.409  89.458 119.509  1.00 21.42           P  
ATOM   8198  OP1   G P  16      79.428  89.447 120.586  1.00 21.42           O  
ATOM   8199  OP2   G P  16      78.414  90.549 118.503  1.00 21.42           O  
ATOM   8200  O5'   G P  16      78.499  88.068 118.740  1.00 21.42           O  
ATOM   8201  C5'   G P  16      78.375  86.842 119.444  1.00 21.42           C  
ATOM   8202  C4'   G P  16      78.101  85.690 118.511  1.00 21.42           C  
ATOM   8203  O4'   G P  16      76.870  85.922 117.787  1.00 21.42           O  
ATOM   8204  C3'   G P  16      79.128  85.452 117.418  1.00 21.42           C  
ATOM   8205  O3'   G P  16      80.265  84.747 117.883  1.00 21.42           O  
ATOM   8206  C2'   G P  16      78.328  84.686 116.370  1.00 21.42           C  
ATOM   8207  O2'   G P  16      78.232  83.315 116.720  1.00 21.42           O  
ATOM   8208  C1'   G P  16      76.941  85.312 116.518  1.00 21.42           C  
ATOM   8209  N9    G P  16      76.625  86.307 115.473  1.00 21.42           N  
ATOM   8210  C8    G P  16      76.504  87.666 115.610  1.00 21.42           C  
ATOM   8211  N7    G P  16      76.185  88.266 114.495  1.00 21.42           N  
ATOM   8212  C5    G P  16      76.079  87.243 113.566  1.00 21.42           C  
ATOM   8213  C6    G P  16      75.764  87.273 112.184  1.00 21.42           C  
ATOM   8214  O6    G P  16      75.496  88.244 111.467  1.00 21.42           O  
ATOM   8215  N1    G P  16      75.772  86.000 111.632  1.00 21.42           N  
ATOM   8216  C2    G P  16      76.047  84.847 112.317  1.00 21.42           C  
ATOM   8217  N2    G P  16      76.013  83.703 111.625  1.00 21.42           N  
ATOM   8218  N3    G P  16      76.344  84.807 113.600  1.00 21.42           N  
ATOM   8219  C4    G P  16      76.342  86.031 114.158  1.00 21.42           C  
ATOM   8220  P     U P  17      81.688  84.935 117.166  1.00 16.74           P  
ATOM   8221  OP1   U P  17      82.717  84.304 118.027  1.00 16.74           O  
ATOM   8222  OP2   U P  17      81.826  86.362 116.783  1.00 16.74           O  
ATOM   8223  O5'   U P  17      81.570  84.066 115.837  1.00 16.74           O  
ATOM   8224  C5'   U P  17      81.384  82.660 115.898  1.00 16.74           C  
ATOM   8225  C4'   U P  17      81.164  82.071 114.529  1.00 16.74           C  
ATOM   8226  O4'   U P  17      79.911  82.552 113.981  1.00 16.74           O  
ATOM   8227  C3'   U P  17      82.190  82.441 113.473  1.00 16.74           C  
ATOM   8228  O3'   U P  17      83.377  81.674 113.557  1.00 16.74           O  
ATOM   8229  C2'   U P  17      81.419  82.237 112.177  1.00 16.74           C  
ATOM   8230  O2'   U P  17      81.348  80.859 111.847  1.00 16.74           O  
ATOM   8231  C1'   U P  17      80.022  82.697 112.581  1.00 16.74           C  
ATOM   8232  N1    U P  17      79.749  84.109 112.225  1.00 16.74           N  
ATOM   8233  C2    U P  17      79.344  84.395 110.935  1.00 16.74           C  
ATOM   8234  O2    U P  17      79.225  83.547 110.073  1.00 16.74           O  
ATOM   8235  N3    U P  17      79.094  85.719 110.686  1.00 16.74           N  
ATOM   8236  C4    U P  17      79.191  86.762 111.582  1.00 16.74           C  
ATOM   8237  O4    U P  17      78.934  87.909 111.223  1.00 16.74           O  
ATOM   8238  C5    U P  17      79.607  86.384 112.895  1.00 16.74           C  
ATOM   8239  C6    U P  17      79.862  85.104 113.164  1.00 16.74           C  
ATOM   8240  P     U P  18      84.767  82.285 113.039  1.00 16.74           P  
ATOM   8241  OP1   U P  18      85.856  81.359 113.426  1.00 16.74           O  
ATOM   8242  OP2   U P  18      84.833  83.701 113.467  1.00 16.74           O  
ATOM   8243  O5'   U P  18      84.632  82.252 111.455  1.00 16.74           O  
ATOM   8244  C5'   U P  18      84.430  81.027 110.768  1.00 16.74           C  
ATOM   8245  C4'   U P  18      84.036  81.258 109.332  1.00 16.74           C  
ATOM   8246  O4'   U P  18      82.783  81.983 109.268  1.00 16.74           O  
ATOM   8247  C3'   U P  18      84.926  82.101 108.506  1.00 16.74           C  
ATOM   8248  O3'   U P  18      86.053  81.371 108.067  1.00 16.74           O  
ATOM   8249  C2'   U P  18      84.047  82.617 107.377  1.00 16.74           C  
ATOM   8250  O2'   U P  18      83.854  81.611 106.398  1.00 16.74           O  
ATOM   8251  C1'   U P  18      82.723  82.830 108.103  1.00 16.74           C  
ATOM   8252  N1    U P  18      82.523  84.230 108.537  1.00 16.74           N  
ATOM   8253  C2    U P  18      82.076  85.148 107.609  1.00 16.74           C  
ATOM   8254  O2    U P  18      81.842  84.873 106.448  1.00 16.74           O  
ATOM   8255  N3    U P  18      81.905  86.419 108.076  1.00 16.74           N  
ATOM   8256  C4    U P  18      82.126  86.859 109.356  1.00 16.74           C  
ATOM   8257  O4    U P  18      81.928  88.040 109.629  1.00 16.74           O  
ATOM   8258  C5    U P  18      82.587  85.854 110.257  1.00 16.74           C  
ATOM   8259  C6    U P  18      82.763  84.606 109.828  1.00 16.74           C  
ATOM   8260  P     A P  19      87.449  82.116 107.828  1.00 10.55           P  
ATOM   8261  OP1   A P  19      88.435  81.075 107.484  1.00 10.55           O  
ATOM   8262  OP2   A P  19      87.700  83.049 108.945  1.00 10.55           O  
ATOM   8263  O5'   A P  19      87.205  82.973 106.517  1.00 10.55           O  
ATOM   8264  C5'   A P  19      87.075  82.337 105.260  1.00 10.55           C  
ATOM   8265  C4'   A P  19      86.583  83.292 104.212  1.00 10.55           C  
ATOM   8266  O4'   A P  19      85.351  83.909 104.650  1.00 10.55           O  
ATOM   8267  C3'   A P  19      87.490  84.467 103.917  1.00 10.55           C  
ATOM   8268  O3'   A P  19      88.554  84.122 103.053  1.00 10.55           O  
ATOM   8269  C2'   A P  19      86.529  85.488 103.327  1.00 10.55           C  
ATOM   8270  O2'   A P  19      86.246  85.176 101.973  1.00 10.55           O  
ATOM   8271  C1'   A P  19      85.266  85.222 104.142  1.00 10.55           C  
ATOM   8272  N9    A P  19      85.068  86.165 105.262  1.00 10.55           N  
ATOM   8273  C8    A P  19      85.198  85.923 106.600  1.00 10.55           C  
ATOM   8274  N7    A P  19      84.931  86.947 107.361  1.00 10.55           N  
ATOM   8275  C5    A P  19      84.567  87.929 106.462  1.00 10.55           C  
ATOM   8276  C6    A P  19      84.162  89.259 106.630  1.00 10.55           C  
ATOM   8277  N6    A P  19      84.049  89.848 107.817  1.00 10.55           N  
ATOM   8278  N1    A P  19      83.884  89.982 105.529  1.00 10.55           N  
ATOM   8279  C2    A P  19      84.004  89.393 104.340  1.00 10.55           C  
ATOM   8280  N3    A P  19      84.367  88.151 104.056  1.00 10.55           N  
ATOM   8281  C4    A P  19      84.642  87.463 105.171  1.00 10.55           C  
ATOM   8282  P     U P  20      90.046  84.533 103.231  1.00 13.96           P  
ATOM   8283  OP1   U P  20      90.927  83.719 102.373  1.00 13.96           O  
ATOM   8284  OP2   U P  20      90.326  84.650 104.677  1.00 13.96           O  
ATOM   8285  O5'   U P  20      89.958  86.076 102.582  1.00 13.96           O  
ATOM   8286  C5'   U P  20      89.636  86.288 101.229  1.00 13.96           C  
ATOM   8287  C4'   U P  20      89.247  87.753 101.058  1.00 13.96           C  
ATOM   8288  O4'   U P  20      88.004  88.055 101.691  1.00 13.96           O  
ATOM   8289  C3'   U P  20      90.201  88.728 101.730  1.00 13.96           C  
ATOM   8290  O3'   U P  20      91.484  88.827 101.139  1.00 13.96           O  
ATOM   8291  C2'   U P  20      89.386  89.994 101.771  1.00 13.96           C  
ATOM   8292  O2'   U P  20      89.412  90.668 100.538  1.00 13.96           O  
ATOM   8293  C1'   U P  20      87.994  89.409 102.065  1.00 13.96           C  
ATOM   8294  N1    U P  20      87.750  89.526 103.553  1.00 13.96           N  
ATOM   8295  C2    U P  20      87.247  90.744 104.045  1.00 13.96           C  
ATOM   8296  O2    U P  20      86.922  91.671 103.308  1.00 13.96           O  
ATOM   8297  N3    U P  20      87.150  90.877 105.427  1.00 13.96           N  
ATOM   8298  C4    U P  20      87.524  89.920 106.369  1.00 13.96           C  
ATOM   8299  O4    U P  20      87.395  90.152 107.569  1.00 13.96           O  
ATOM   8300  C5    U P  20      88.053  88.688 105.796  1.00 13.96           C  
ATOM   8301  C6    U P  20      88.151  88.547 104.454  1.00 13.96           C  
TER    8302        U P  20                                                      
ATOM   8303  P     U T   8      89.733 105.297 124.520  1.00 94.23           P  
ATOM   8304  OP1   U T   8      90.796 106.271 124.161  1.00 94.23           O  
ATOM   8305  OP2   U T   8      88.428 105.793 125.019  1.00 94.23           O  
ATOM   8306  O5'   U T   8      89.458 104.368 123.255  1.00 94.23           O  
ATOM   8307  C5'   U T   8      90.324 104.400 122.130  1.00 94.23           C  
ATOM   8308  C4'   U T   8      90.559 103.021 121.565  1.00 94.23           C  
ATOM   8309  O4'   U T   8      90.786 102.077 122.645  1.00 94.23           O  
ATOM   8310  C3'   U T   8      89.409 102.405 120.784  1.00 94.23           C  
ATOM   8311  O3'   U T   8      89.306 102.886 119.457  1.00 94.23           O  
ATOM   8312  C2'   U T   8      89.718 100.919 120.870  1.00 94.23           C  
ATOM   8313  O2'   U T   8      90.760 100.575 119.969  1.00 94.23           O  
ATOM   8314  C1'   U T   8      90.260 100.812 122.295  1.00 94.23           C  
ATOM   8315  N1    U T   8      89.193 100.452 123.257  1.00 94.23           N  
ATOM   8316  C2    U T   8      88.813  99.124 123.326  1.00 94.23           C  
ATOM   8317  O2    U T   8      89.321  98.252 122.642  1.00 94.23           O  
ATOM   8318  N3    U T   8      87.814  98.853 124.228  1.00 94.23           N  
ATOM   8319  C4    U T   8      87.171  99.758 125.049  1.00 94.23           C  
ATOM   8320  O4    U T   8      86.291  99.360 125.812  1.00 94.23           O  
ATOM   8321  C5    U T   8      87.618 101.110 124.916  1.00 94.23           C  
ATOM   8322  C6    U T   8      88.588 101.402 124.045  1.00 94.23           C  
ATOM   8323  P     U T   9      87.895 102.823 118.694  1.00 68.87           P  
ATOM   8324  OP1   U T   9      87.995 103.701 117.504  1.00 68.87           O  
ATOM   8325  OP2   U T   9      86.816 103.047 119.686  1.00 68.87           O  
ATOM   8326  O5'   U T   9      87.796 101.319 118.175  1.00 68.87           O  
ATOM   8327  C5'   U T   9      88.360 100.955 116.926  1.00 68.87           C  
ATOM   8328  C4'   U T   9      88.562  99.465 116.789  1.00 68.87           C  
ATOM   8329  O4'   U T   9      89.087  98.900 118.017  1.00 68.87           O  
ATOM   8330  C3'   U T   9      87.330  98.625 116.515  1.00 68.87           C  
ATOM   8331  O3'   U T   9      86.892  98.705 115.173  1.00 68.87           O  
ATOM   8332  C2'   U T   9      87.796  97.232 116.917  1.00 68.87           C  
ATOM   8333  O2'   U T   9      88.608  96.664 115.901  1.00 68.87           O  
ATOM   8334  C1'   U T   9      88.684  97.548 118.123  1.00 68.87           C  
ATOM   8335  N1    U T   9      87.970  97.338 119.403  1.00 68.87           N  
ATOM   8336  C2    U T   9      88.158  96.116 120.014  1.00 68.87           C  
ATOM   8337  O2    U T   9      88.884  95.252 119.554  1.00 68.87           O  
ATOM   8338  N3    U T   9      87.476  95.944 121.192  1.00 68.87           N  
ATOM   8339  C4    U T   9      86.635  96.849 121.804  1.00 68.87           C  
ATOM   8340  O4    U T   9      86.092  96.545 122.867  1.00 68.87           O  
ATOM   8341  C5    U T   9      86.484  98.087 121.103  1.00 68.87           C  
ATOM   8342  C6    U T   9      87.138  98.284 119.954  1.00 68.87           C  
ATOM   8343  P     U T  10      85.331  98.567 114.832  1.00 30.58           P  
ATOM   8344  OP1   U T  10      84.578  99.317 115.867  1.00 30.58           O  
ATOM   8345  OP2   U T  10      85.031  97.134 114.587  1.00 30.58           O  
ATOM   8346  O5'   U T  10      85.176  99.342 113.454  1.00 30.58           O  
ATOM   8347  C5'   U T  10      85.628 100.679 113.326  1.00 30.58           C  
ATOM   8348  C4'   U T  10      86.207 100.933 111.960  1.00 30.58           C  
ATOM   8349  O4'   U T  10      87.467 100.227 111.816  1.00 30.58           O  
ATOM   8350  C3'   U T  10      85.379 100.434 110.791  1.00 30.58           C  
ATOM   8351  O3'   U T  10      84.304 101.289 110.459  1.00 30.58           O  
ATOM   8352  C2'   U T  10      86.419 100.298 109.693  1.00 30.58           C  
ATOM   8353  O2'   U T  10      86.754 101.576 109.175  1.00 30.58           O  
ATOM   8354  C1'   U T  10      87.613  99.775 110.486  1.00 30.58           C  
ATOM   8355  N1    U T  10      87.672  98.295 110.495  1.00 30.58           N  
ATOM   8356  C2    U T  10      88.191  97.659 109.385  1.00 30.58           C  
ATOM   8357  O2    U T  10      88.593  98.256 108.407  1.00 30.58           O  
ATOM   8358  N3    U T  10      88.218  96.291 109.459  1.00 30.58           N  
ATOM   8359  C4    U T  10      87.792  95.508 110.510  1.00 30.58           C  
ATOM   8360  O4    U T  10      87.885  94.285 110.425  1.00 30.58           O  
ATOM   8361  C5    U T  10      87.269  96.236 111.621  1.00 30.58           C  
ATOM   8362  C6    U T  10      87.230  97.569 111.576  1.00 30.58           C  
ATOM   8363  P     A T  11      82.891 100.652 110.049  1.00 22.72           P  
ATOM   8364  OP1   A T  11      81.862 101.721 110.055  1.00 22.72           O  
ATOM   8365  OP2   A T  11      82.709  99.430 110.866  1.00 22.72           O  
ATOM   8366  O5'   A T  11      83.110 100.177 108.550  1.00 22.72           O  
ATOM   8367  C5'   A T  11      83.517 101.092 107.549  1.00 22.72           C  
ATOM   8368  C4'   A T  11      83.846 100.374 106.269  1.00 22.72           C  
ATOM   8369  O4'   A T  11      85.074  99.616 106.430  1.00 22.72           O  
ATOM   8370  C3'   A T  11      82.840  99.329 105.825  1.00 22.72           C  
ATOM   8371  O3'   A T  11      81.689  99.874 105.206  1.00 22.72           O  
ATOM   8372  C2'   A T  11      83.678  98.442 104.920  1.00 22.72           C  
ATOM   8373  O2'   A T  11      83.906  99.079 103.673  1.00 22.72           O  
ATOM   8374  C1'   A T  11      84.997  98.417 105.687  1.00 22.72           C  
ATOM   8375  N9    A T  11      85.060  97.280 106.624  1.00 22.72           N  
ATOM   8376  C8    A T  11      84.723  97.267 107.951  1.00 22.72           C  
ATOM   8377  N7    A T  11      84.880  96.103 108.527  1.00 22.72           N  
ATOM   8378  C5    A T  11      85.347  95.291 107.506  1.00 22.72           C  
ATOM   8379  C6    A T  11      85.711  93.937 107.468  1.00 22.72           C  
ATOM   8380  N6    A T  11      85.654  93.131 108.525  1.00 22.72           N  
ATOM   8381  N1    A T  11      86.140  93.431 106.293  1.00 22.72           N  
ATOM   8382  C2    A T  11      86.192  94.242 105.232  1.00 22.72           C  
ATOM   8383  N3    A T  11      85.882  95.531 105.143  1.00 22.72           N  
ATOM   8384  C4    A T  11      85.458  96.000 106.328  1.00 22.72           C  
ATOM   8385  P     U T  12      80.244  99.252 105.528  1.00 16.53           P  
ATOM   8386  OP1   U T  12      79.224 100.271 105.191  1.00 16.53           O  
ATOM   8387  OP2   U T  12      80.285  98.669 106.891  1.00 16.53           O  
ATOM   8388  O5'   U T  12      80.105  98.053 104.491  1.00 16.53           O  
ATOM   8389  C5'   U T  12      80.262  98.282 103.100  1.00 16.53           C  
ATOM   8390  C4'   U T  12      80.783  97.063 102.379  1.00 16.53           C  
ATOM   8391  O4'   U T  12      82.004  96.591 103.001  1.00 16.53           O  
ATOM   8392  C3'   U T  12      79.889  95.838 102.376  1.00 16.53           C  
ATOM   8393  O3'   U T  12      78.822  95.930 101.449  1.00 16.53           O  
ATOM   8394  C2'   U T  12      80.876  94.723 102.065  1.00 16.53           C  
ATOM   8395  O2'   U T  12      81.193  94.709 100.683  1.00 16.53           O  
ATOM   8396  C1'   U T  12      82.111  95.191 102.835  1.00 16.53           C  
ATOM   8397  N1    U T  12      82.222  94.543 104.163  1.00 16.53           N  
ATOM   8398  C2    U T  12      82.766  93.275 104.205  1.00 16.53           C  
ATOM   8399  O2    U T  12      83.148  92.685 103.214  1.00 16.53           O  
ATOM   8400  N3    U T  12      82.850  92.711 105.447  1.00 16.53           N  
ATOM   8401  C4    U T  12      82.452  93.276 106.635  1.00 16.53           C  
ATOM   8402  O4    U T  12      82.594  92.639 107.677  1.00 16.53           O  
ATOM   8403  C5    U T  12      81.903  94.588 106.515  1.00 16.53           C  
ATOM   8404  C6    U T  12      81.808  95.163 105.315  1.00 16.53           C  
ATOM   8405  P     A T  13      77.383  95.322 101.815  1.00 16.74           P  
ATOM   8406  OP1   A T  13      76.400  95.841 100.837  1.00 16.74           O  
ATOM   8407  OP2   A T  13      77.151  95.522 103.263  1.00 16.74           O  
ATOM   8408  O5'   A T  13      77.552  93.761 101.567  1.00 16.74           O  
ATOM   8409  C5'   A T  13      78.018  93.268 100.322  1.00 16.74           C  
ATOM   8410  C4'   A T  13      78.395  91.813 100.409  1.00 16.74           C  
ATOM   8411  O4'   A T  13      79.602  91.654 101.195  1.00 16.74           O  
ATOM   8412  C3'   A T  13      77.400  90.904 101.100  1.00 16.74           C  
ATOM   8413  O3'   A T  13      76.298  90.558 100.283  1.00 16.74           O  
ATOM   8414  C2'   A T  13      78.266  89.717 101.498  1.00 16.74           C  
ATOM   8415  O2'   A T  13      78.508  88.871 100.386  1.00 16.74           O  
ATOM   8416  C1'   A T  13      79.574  90.412 101.866  1.00 16.74           C  
ATOM   8417  N9    A T  13      79.676  90.642 103.317  1.00 16.74           N  
ATOM   8418  C8    A T  13      79.343  91.763 104.029  1.00 16.74           C  
ATOM   8419  N7    A T  13      79.545  91.646 105.316  1.00 16.74           N  
ATOM   8420  C5    A T  13      80.040  90.361 105.455  1.00 16.74           C  
ATOM   8421  C6    A T  13      80.446  89.627 106.575  1.00 16.74           C  
ATOM   8422  N6    A T  13      80.418  90.118 107.812  1.00 16.74           N  
ATOM   8423  N1    A T  13      80.889  88.367 106.380  1.00 16.74           N  
ATOM   8424  C2    A T  13      80.910  87.885 105.133  1.00 16.74           C  
ATOM   8425  N3    A T  13      80.550  88.480 104.000  1.00 16.74           N  
ATOM   8426  C4    A T  13      80.117  89.728 104.236  1.00 16.74           C  
ATOM   8427  P     A T  14      74.874  90.250 100.953  1.00  9.47           P  
ATOM   8428  OP1   A T  14      73.844  90.289  99.892  1.00  9.47           O  
ATOM   8429  OP2   A T  14      74.730  91.122 102.141  1.00  9.47           O  
ATOM   8430  O5'   A T  14      75.008  88.749 101.460  1.00  9.47           O  
ATOM   8431  C5'   A T  14      75.266  87.695 100.548  1.00  9.47           C  
ATOM   8432  C4'   A T  14      75.806  86.476 101.249  1.00  9.47           C  
ATOM   8433  O4'   A T  14      77.017  86.811 101.973  1.00  9.47           O  
ATOM   8434  C3'   A T  14      74.912  85.861 102.309  1.00  9.47           C  
ATOM   8435  O3'   A T  14      73.881  85.062 101.760  1.00  9.47           O  
ATOM   8436  C2'   A T  14      75.906  85.084 103.162  1.00  9.47           C  
ATOM   8437  O2'   A T  14      76.269  83.871 102.524  1.00  9.47           O  
ATOM   8438  C1'   A T  14      77.116  86.015 103.134  1.00  9.47           C  
ATOM   8439  N9    A T  14      77.176  86.891 104.320  1.00  9.47           N  
ATOM   8440  C8    A T  14      76.822  88.210 104.433  1.00  9.47           C  
ATOM   8441  N7    A T  14      76.998  88.704 105.631  1.00  9.47           N  
ATOM   8442  C5    A T  14      77.503  87.639 106.357  1.00  9.47           C  
ATOM   8443  C6    A T  14      77.903  87.510 107.696  1.00  9.47           C  
ATOM   8444  N6    A T  14      77.850  88.500 108.583  1.00  9.47           N  
ATOM   8445  N1    A T  14      78.358  86.310 108.106  1.00  9.47           N  
ATOM   8446  C2    A T  14      78.413  85.313 107.219  1.00  9.47           C  
ATOM   8447  N3    A T  14      78.074  85.313 105.936  1.00  9.47           N  
ATOM   8448  C4    A T  14      77.620  86.519 105.562  1.00  9.47           C  
ATOM   8449  P     C T  15      72.418  85.059 102.420  1.00 16.74           P  
ATOM   8450  OP1   C T  15      71.483  84.435 101.459  1.00 16.74           O  
ATOM   8451  OP2   C T  15      72.137  86.418 102.942  1.00 16.74           O  
ATOM   8452  O5'   C T  15      72.560  84.078 103.664  1.00 16.74           O  
ATOM   8453  C5'   C T  15      73.007  82.744 103.488  1.00 16.74           C  
ATOM   8454  C4'   C T  15      73.541  82.162 104.773  1.00 16.74           C  
ATOM   8455  O4'   C T  15      74.671  82.940 105.239  1.00 16.74           O  
ATOM   8456  C3'   C T  15      72.593  82.162 105.957  1.00 16.74           C  
ATOM   8457  O3'   C T  15      71.636  81.120 105.901  1.00 16.74           O  
ATOM   8458  C2'   C T  15      73.549  82.063 107.137  1.00 16.74           C  
ATOM   8459  O2'   C T  15      74.023  80.734 107.289  1.00 16.74           O  
ATOM   8460  C1'   C T  15      74.712  82.927 106.651  1.00 16.74           C  
ATOM   8461  N1    C T  15      74.627  84.317 107.153  1.00 16.74           N  
ATOM   8462  C2    C T  15      75.097  84.593 108.438  1.00 16.74           C  
ATOM   8463  O2    C T  15      75.572  83.675 109.117  1.00 16.74           O  
ATOM   8464  N3    C T  15      75.032  85.853 108.913  1.00 16.74           N  
ATOM   8465  C4    C T  15      74.515  86.818 108.159  1.00 16.74           C  
ATOM   8466  N4    C T  15      74.471  88.045 108.678  1.00 16.74           N  
ATOM   8467  C5    C T  15      74.029  86.572 106.847  1.00 16.74           C  
ATOM   8468  C6    C T  15      74.099  85.319 106.390  1.00 16.74           C  
ATOM   8469  P     U T  16      70.180  81.326 106.543  1.00 23.55           P  
ATOM   8470  OP1   U T  16      69.271  80.296 105.991  1.00 23.55           O  
ATOM   8471  OP2   U T  16      69.826  82.756 106.412  1.00 23.55           O  
ATOM   8472  O5'   U T  16      70.399  81.013 108.087  1.00 23.55           O  
ATOM   8473  C5'   U T  16      70.980  79.788 108.503  1.00 23.55           C  
ATOM   8474  C4'   U T  16      71.480  79.862 109.923  1.00 23.55           C  
ATOM   8475  O4'   U T  16      72.534  80.851 110.030  1.00 23.55           O  
ATOM   8476  C3'   U T  16      70.467  80.299 110.964  1.00 23.55           C  
ATOM   8477  O3'   U T  16      69.596  79.253 111.356  1.00 23.55           O  
ATOM   8478  C2'   U T  16      71.352  80.817 112.090  1.00 23.55           C  
ATOM   8479  O2'   U T  16      71.883  79.740 112.845  1.00 23.55           O  
ATOM   8480  C1'   U T  16      72.496  81.458 111.305  1.00 23.55           C  
ATOM   8481  N1    U T  16      72.320  82.918 111.132  1.00 23.55           N  
ATOM   8482  C2    U T  16      72.620  83.739 112.199  1.00 23.55           C  
ATOM   8483  O2    U T  16      73.007  83.319 113.273  1.00 23.55           O  
ATOM   8484  N3    U T  16      72.440  85.076 111.966  1.00 23.55           N  
ATOM   8485  C4    U T  16      72.003  85.665 110.800  1.00 23.55           C  
ATOM   8486  O4    U T  16      71.895  86.889 110.746  1.00 23.55           O  
ATOM   8487  C5    U T  16      71.721  84.751 109.741  1.00 23.55           C  
ATOM   8488  C6    U T  16      71.888  83.444 109.941  1.00 23.55           C  
ATOM   8489  P     U T  17      68.045  79.558 111.638  1.00 44.05           P  
ATOM   8490  OP1   U T  17      67.319  78.267 111.669  1.00 44.05           O  
ATOM   8491  OP2   U T  17      67.601  80.614 110.696  1.00 44.05           O  
ATOM   8492  O5'   U T  17      68.044  80.156 113.113  1.00 44.05           O  
ATOM   8493  C5'   U T  17      68.623  79.430 114.186  1.00 44.05           C  
ATOM   8494  C4'   U T  17      68.915  80.318 115.369  1.00 44.05           C  
ATOM   8495  O4'   U T  17      69.932  81.291 115.021  1.00 44.05           O  
ATOM   8496  C3'   U T  17      67.759  81.165 115.873  1.00 44.05           C  
ATOM   8497  O3'   U T  17      66.853  80.442 116.687  1.00 44.05           O  
ATOM   8498  C2'   U T  17      68.474  82.293 116.603  1.00 44.05           C  
ATOM   8499  O2'   U T  17      68.924  81.858 117.877  1.00 44.05           O  
ATOM   8500  C1'   U T  17      69.695  82.502 115.709  1.00 44.05           C  
ATOM   8501  N1    U T  17      69.484  83.580 114.718  1.00 44.05           N  
ATOM   8502  C2    U T  17      69.716  84.873 115.133  1.00 44.05           C  
ATOM   8503  O2    U T  17      70.080  85.145 116.262  1.00 44.05           O  
ATOM   8504  N3    U T  17      69.506  85.835 114.179  1.00 44.05           N  
ATOM   8505  C4    U T  17      69.094  85.635 112.880  1.00 44.05           C  
ATOM   8506  O4    U T  17      68.951  86.605 112.137  1.00 44.05           O  
ATOM   8507  C5    U T  17      68.876  84.268 112.525  1.00 44.05           C  
ATOM   8508  C6    U T  17      69.072  83.313 113.435  1.00 44.05           C  
ATOM   8509  P     A T  18      65.278  80.741 116.597  1.00 77.34           P  
ATOM   8510  OP1   A T  18      64.558  79.593 117.198  1.00 77.34           O  
ATOM   8511  OP2   A T  18      64.968  81.154 115.206  1.00 77.34           O  
ATOM   8512  O5'   A T  18      65.075  82.002 117.548  1.00 77.34           O  
ATOM   8513  C5'   A T  18      65.475  81.955 118.909  1.00 77.34           C  
ATOM   8514  C4'   A T  18      65.548  83.334 119.516  1.00 77.34           C  
ATOM   8515  O4'   A T  18      66.591  84.107 118.866  1.00 77.34           O  
ATOM   8516  C3'   A T  18      64.307  84.198 119.367  1.00 77.34           C  
ATOM   8517  O3'   A T  18      63.292  83.886 120.305  1.00 77.34           O  
ATOM   8518  C2'   A T  18      64.868  85.604 119.516  1.00 77.34           C  
ATOM   8519  O2'   A T  18      65.118  85.900 120.882  1.00 77.34           O  
ATOM   8520  C1'   A T  18      66.210  85.466 118.798  1.00 77.34           C  
ATOM   8521  N9    A T  18      66.113  85.859 117.379  1.00 77.34           N  
ATOM   8522  C8    A T  18      65.944  85.045 116.288  1.00 77.34           C  
ATOM   8523  N7    A T  18      65.891  85.691 115.150  1.00 77.34           N  
ATOM   8524  C5    A T  18      66.026  87.021 115.517  1.00 77.34           C  
ATOM   8525  C6    A T  18      66.049  88.211 114.771  1.00 77.34           C  
ATOM   8526  N6    A T  18      65.928  88.253 113.443  1.00 77.34           N  
ATOM   8527  N1    A T  18      66.202  89.372 115.441  1.00 77.34           N  
ATOM   8528  C2    A T  18      66.323  89.330 116.772  1.00 77.34           C  
ATOM   8529  N3    A T  18      66.317  88.276 117.583  1.00 77.34           N  
ATOM   8530  C4    A T  18      66.163  87.139 116.886  1.00 77.34           C  
ATOM   8531  P     A T  19      61.817  84.499 120.128  1.00106.03           P  
ATOM   8532  OP1   A T  19      60.866  83.643 120.879  1.00106.03           O  
ATOM   8533  OP2   A T  19      61.592  84.751 118.682  1.00106.03           O  
ATOM   8534  O5'   A T  19      61.901  85.913 120.857  1.00106.03           O  
ATOM   8535  C5'   A T  19      60.970  86.944 120.562  1.00106.03           C  
ATOM   8536  C4'   A T  19      61.655  88.280 120.423  1.00106.03           C  
ATOM   8537  O4'   A T  19      62.766  88.165 119.500  1.00106.03           O  
ATOM   8538  C3'   A T  19      60.806  89.407 119.852  1.00106.03           C  
ATOM   8539  O3'   A T  19      59.997  90.029 120.835  1.00106.03           O  
ATOM   8540  C2'   A T  19      61.845  90.346 119.250  1.00106.03           C  
ATOM   8541  O2'   A T  19      62.410  91.177 120.253  1.00106.03           O  
ATOM   8542  C1'   A T  19      62.919  89.365 118.774  1.00106.03           C  
ATOM   8543  N9    A T  19      62.833  89.067 117.331  1.00106.03           N  
ATOM   8544  C8    A T  19      62.719  87.835 116.735  1.00106.03           C  
ATOM   8545  N7    A T  19      62.681  87.880 115.426  1.00106.03           N  
ATOM   8546  C5    A T  19      62.786  89.232 115.142  1.00106.03           C  
ATOM   8547  C6    A T  19      62.806  89.945 113.934  1.00106.03           C  
ATOM   8548  N6    A T  19      62.723  89.364 112.740  1.00106.03           N  
ATOM   8549  N1    A T  19      62.919  91.287 113.991  1.00106.03           N  
ATOM   8550  C2    A T  19      63.005  91.869 115.191  1.00106.03           C  
ATOM   8551  N3    A T  19      62.999  91.310 116.396  1.00106.03           N  
ATOM   8552  C4    A T  19      62.884  89.975 116.303  1.00106.03           C  
ATOM   8553  P     U T  20      58.412  89.769 120.875  1.00129.51           P  
ATOM   8554  OP1   U T  20      57.952  90.011 122.265  1.00129.51           O  
ATOM   8555  OP2   U T  20      58.135  88.458 120.238  1.00129.51           O  
ATOM   8556  O5'   U T  20      57.809  90.911 119.944  1.00129.51           O  
ATOM   8557  C5'   U T  20      57.981  92.284 120.266  1.00129.51           C  
ATOM   8558  C4'   U T  20      57.950  93.146 119.031  1.00129.51           C  
ATOM   8559  O4'   U T  20      59.009  92.738 118.128  1.00129.51           O  
ATOM   8560  C3'   U T  20      56.686  93.057 118.188  1.00129.51           C  
ATOM   8561  O3'   U T  20      55.638  93.876 118.683  1.00129.51           O  
ATOM   8562  C2'   U T  20      57.172  93.463 116.802  1.00129.51           C  
ATOM   8563  O2'   U T  20      57.258  94.876 116.694  1.00129.51           O  
ATOM   8564  C1'   U T  20      58.591  92.890 116.789  1.00129.51           C  
ATOM   8565  N1    U T  20      58.668  91.575 116.110  1.00129.51           N  
ATOM   8566  C2    U T  20      58.972  91.590 114.765  1.00129.51           C  
ATOM   8567  O2    U T  20      59.167  92.624 114.154  1.00129.51           O  
ATOM   8568  N3    U T  20      59.042  90.358 114.167  1.00129.51           N  
ATOM   8569  C4    U T  20      58.840  89.133 114.769  1.00129.51           C  
ATOM   8570  O4    U T  20      58.936  88.107 114.095  1.00129.51           O  
ATOM   8571  C5    U T  20      58.529  89.199 116.165  1.00129.51           C  
ATOM   8572  C6    U T  20      58.458  90.388 116.773  1.00129.51           C  
ATOM   8573  P     C T  21      54.100  93.463 118.460  1.00142.11           P  
ATOM   8574  OP1   C T  21      53.293  94.086 119.539  1.00142.11           O  
ATOM   8575  OP2   C T  21      54.044  91.995 118.261  1.00142.11           O  
ATOM   8576  O5'   C T  21      53.701  94.158 117.083  1.00142.11           O  
ATOM   8577  C5'   C T  21      53.418  95.549 117.008  1.00142.11           C  
ATOM   8578  C4'   C T  21      53.329  96.004 115.574  1.00142.11           C  
ATOM   8579  O4'   C T  21      54.549  95.614 114.890  1.00142.11           O  
ATOM   8580  C3'   C T  21      52.213  95.370 114.753  1.00142.11           C  
ATOM   8581  O3'   C T  21      50.970  96.035 114.897  1.00142.11           O  
ATOM   8582  C2'   C T  21      52.769  95.399 113.334  1.00142.11           C  
ATOM   8583  O2'   C T  21      52.600  96.685 112.757  1.00142.11           O  
ATOM   8584  C1'   C T  21      54.261  95.171 113.584  1.00142.11           C  
ATOM   8585  N1    C T  21      54.649  93.743 113.491  1.00142.11           N  
ATOM   8586  C2    C T  21      55.473  93.329 112.441  1.00142.11           C  
ATOM   8587  O2    C T  21      55.858  94.167 111.612  1.00142.11           O  
ATOM   8588  N3    C T  21      55.832  92.025 112.364  1.00142.11           N  
ATOM   8589  C4    C T  21      55.402  91.152 113.278  1.00142.11           C  
ATOM   8590  N4    C T  21      55.774  89.876 113.170  1.00142.11           N  
ATOM   8591  C5    C T  21      54.565  91.541 114.355  1.00142.11           C  
ATOM   8592  C6    C T  21      54.226  92.828 114.417  1.00142.11           C  
TER    8593        C T  21                                                      
HETATM 8594 ZN    ZN A1001      96.331 117.049  82.559  1.00 39.81          ZN  
HETATM 8595 ZN    ZN A1002      78.230 111.511  90.977  1.00 39.19          ZN  
HETATM 8596  P1  POP A1003      98.704  88.743 103.451  0.50 19.48           P  
HETATM 8597  O1  POP A1003     100.113  88.777 102.922  0.50 19.48           O  
HETATM 8598  O2  POP A1003      97.985  87.427 103.304  0.50 19.48           O  
HETATM 8599  O3  POP A1003      98.549  89.378 104.805  0.50 19.48           O  
HETATM 8600  O   POP A1003      97.928  89.726 102.450  0.50 19.48           O  
HETATM 8601  P2  POP A1003      96.972  90.885 103.010  0.50 19.48           P  
HETATM 8602  O4  POP A1003      96.725  91.745 101.796  0.50 19.48           O  
HETATM 8603  O5  POP A1003      95.757  90.149 103.511  0.50 19.48           O  
HETATM 8604  O6  POP A1003      97.772  91.527 104.104  0.50 19.48           O  
HETATM 8605 MG    MG A1004      97.212  88.488 100.157  0.50 14.12          MG  
HETATM 8606 MG    MG A1005      92.442  84.162 100.658  0.50 11.84          MG  
HETATM 8607  C8  F86 P 101      90.089  93.714 102.212  0.50 17.13           C  
HETATM 8608  C5  F86 P 101      91.043  92.580 104.194  0.50 17.13           C  
HETATM 8609  C6  F86 P 101      93.646  90.983 101.106  0.50 17.13           C  
HETATM 8610  N1  F86 P 101      90.372  93.279 105.194  0.50 17.13           N  
HETATM 8611  C2  F86 P 101      92.527  94.119 102.804  0.50 17.13           C  
HETATM 8612  N3  F86 P 101      89.132  94.151 101.727  0.50 17.13           N  
HETATM 8613  C4  F86 P 101      92.877  92.286 101.308  0.50 17.13           C  
HETATM 8614  O2  F86 P 101      92.236  95.336 102.134  0.50 17.13           O  
HETATM 8615  N2  F86 P 101      89.857  94.508 105.120  0.50 17.13           N  
HETATM 8616  O4  F86 P 101      93.558  90.117 102.223  0.50 17.13           O  
HETATM 8617  N4  F86 P 101      89.204  94.166 107.454  0.50 17.13           N  
HETATM 8618  C7  F86 P 101      91.404  91.340 104.711  0.50 17.13           C  
HETATM 8619  O6  F86 P 101      92.596  88.024 103.361  0.50 17.13           O  
HETATM 8620  C1  F86 P 101      91.312  93.155 102.826  0.50 17.13           C  
HETATM 8621  C10 F86 P 101      90.974  91.189 106.069  0.50 17.13           C  
HETATM 8622  C11 F86 P 101      89.741  92.925 107.450  0.50 17.13           C  
HETATM 8623  C12 F86 P 101      89.278  94.874 106.294  0.50 17.13           C  
HETATM 8624  C3  F86 P 101      93.634  93.333 102.101  0.50 17.13           C  
HETATM 8625  C9  F86 P 101      90.358  92.437 106.276  0.50 17.13           C  
HETATM 8626  N5  F86 P 101      89.647  92.176 108.620  0.50 17.13           N  
HETATM 8627  O1  F86 P 101      91.691  92.036 102.032  0.50 17.13           O  
HETATM 8628  O3  F86 P 101      94.420  94.107 101.216  0.50 17.13           O  
HETATM 8629  O5  F86 P 101      93.876  87.784 101.166  0.50 17.13           O  
HETATM 8630  P1  F86 P 101      92.931  88.546 102.018  0.50 17.13           P  
HETATM 8631  O   HOH A1101      96.300  85.200 115.600  1.00 15.86           O  
HETATM 8632  O   HOH A1102      96.522  87.195  96.424  1.00 10.59           O  
HETATM 8633  O   HOH A1103      94.321  81.227  95.507  1.00 11.16           O  
HETATM 8634  O   HOH A1104      95.247  84.970  98.340  1.00 16.72           O  
HETATM 8635  O   HOH A1105      99.955  86.280 100.814  1.00 23.74           O  
CONECT 1771 8594                                                                
CONECT 1816 8594                                                                
CONECT 1857 8594                                                                
CONECT 1889 8594                                                                
CONECT 3297 8595                                                                
CONECT 4527 8595                                                                
CONECT 4550 8595                                                                
CONECT 4556 8595                                                                
CONECT 8283 8606                                                                
CONECT 8290 8630                                                                
CONECT 8594 1771 1816 1857 1889                                                 
CONECT 8595 3297 4527 4550 4556                                                 
CONECT 8596 8597 8598 8599 8600                                                 
CONECT 8597 8596                                                                
CONECT 8598 8596                                                                
CONECT 8599 8596                                                                
CONECT 8600 8596 8601 8605                                                      
CONECT 8601 8600 8602 8603 8604                                                 
CONECT 8602 8601                                                                
CONECT 8603 8601                                                                
CONECT 8604 8601                                                                
CONECT 8605 8600                                                                
CONECT 8606 8283                                                                
CONECT 8607 8612 8620                                                           
CONECT 8608 8610 8618 8620                                                      
CONECT 8609 8613 8616                                                           
CONECT 8610 8608 8615 8625                                                      
CONECT 8611 8614 8620 8624                                                      
CONECT 8612 8607                                                                
CONECT 8613 8609 8624 8627                                                      
CONECT 8614 8611                                                                
CONECT 8615 8610 8623                                                           
CONECT 8616 8609 8630                                                           
CONECT 8617 8622 8623                                                           
CONECT 8618 8608 8621                                                           
CONECT 8619 8630                                                                
CONECT 8620 8607 8608 8611 8627                                                 
CONECT 8621 8618 8625                                                           
CONECT 8622 8617 8625 8626                                                      
CONECT 8623 8615 8617                                                           
CONECT 8624 8611 8613 8628                                                      
CONECT 8625 8610 8621 8622                                                      
CONECT 8626 8622                                                                
CONECT 8627 8613 8620                                                           
CONECT 8628 8624                                                                
CONECT 8629 8630                                                                
CONECT 8630 8290 8616 8619 8629                                                 
MASTER      498    0    6   55   31    0    8    6 8630    5   47  103          
END